>d101m__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrvkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d102l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaaakseldkaigrntngvit
kdeaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslr
mlqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d102m__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkagvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d103l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnsldaakseldkaigrntngv
itkdeaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftns
lrmlqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d103m__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkagvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d104la_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaaksaaeldkaigrntngvi
tkdeaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnsl
rmlqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d104lb_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaaksaaeldkaigrntngvi
tkdeaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnsl
rmlqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d104m__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgyqg
>d105m__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgyqg
>d106m__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtfltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d107l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakgeldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d107m__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtfltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d108l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakieldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d108m__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtfltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d109l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakkeldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d109m__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d10gsa1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d10gsa2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d10gsb1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d10gsb2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d10mha_ 3.56.1.5.1 DNA methylase HhaI, coenzyme-binding domain {Haemophilus haemolyticus}
mieikdkqltglrfidlfaglggfrlalescgaecvysnewdkyaqevyemnfgekpegd
itqvnektipdhdilcagfpcqafsisgkqkgfedsrgtlffdiarivrekkpkvvfmen
vknfashdngntlevvkntmneldysfhakvlnaldygipqkreriymicfrndlniqnf
qfpkpfelntfvkdlllpdsevehlvidrkdlvmtnqeieqttpktvrlgivgkggqger
iystrgiaitlsaygggifaktggylvngktrklhprecarvmgypdsykvhpstsqayk
qfgnsvvinvlqyiaynigsslnfkpy
>d110l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakleldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d110m__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d111l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakneldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d111m__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d112l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakpeldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d112m__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d113l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakreldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d114l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakteldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d115l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakveldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d117ea_ 2.35.5.1.1 Inorganic pyrophosphatase {Baker's yeast (Saccharomyces cerevisiae)}
tyttrqigakntleykvyiekdgapvsafhdiplyadkennifnmvveiprwtnakleit
keetlnpiiqdtkkgalrfvrncfphhgyihnygafpqtwedpnvshpetkavgdnepid
vleigetiaytgqvkqvkalgimalldegetdwkviaidindplapklndiedvekyfpg
llaatnewfriykipdgkpenafafsgeaknkkyaldiikethdswkqliagkssdskgi
dltnvtlpdtptysaaasdaippaslkadapidksidkwffi
>d117eb_ 2.35.5.1.1 Inorganic pyrophosphatase {Baker's yeast (Saccharomyces cerevisiae)}
tyttrqigakntleykvyiekdgapvsafhdiplyadkannifnmvveiprwtnakleit
keetlnpiiqdtkkgalrfvrncfphhgyihnygafpqtwedpnvshpetkavgdnepid
vleigetiaytgqvkqvkalgimalldegetdwkviaidindplapklndiedvekyfpg
llratnewfriykipdgkpenafafsgeaknkkyaldiikathdswkqliagkssdskgi
dltnvtlpdtptyskaasdaippaslkadapidksidkwffi
>d118l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeasvnlaksrwynqtpnrakrvittfrtgtwdayk
>d119l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlsksrwynqtpnrakrvittfrtgtwdayk
>d11asa_ 4.82.1.1.12 Asparagine synthetase {Escherichia coli}
ayiakqrqisfvkshfsrqleerlglievqapilsrvgdgtqdnlsgaekavqvkvkalp
daqfevvhslakwkrqtlgqhdfsageglythmkalrpdedrlsplhsvyvdqwdwervm
gdgerqfstlkstveaiwagikateaavseefglapflpdqihfvhsqellsrypdldak
greraiakdlgavflvgiggklsdghrhdvrapdyddwstpselghaglngdilvwnpvl
edafelssmgirvdadtlkhqlaltgdedrlelewhqallrgempqtigggigqsrltml
llqlphigqvqagvwpaavresvpsll
>d11asb_ 4.82.1.1.12 Asparagine synthetase {Escherichia coli}
ayiakqrqisfvkshfsrqleerlglievqapilsrvgdgtqdnlsgaekavqvkvkalp
daqfevvhslakwkrqtlgqhdfsageglythmkalrpdedrlsplhsvyvdqwdwervm
gdgerqfstlkstveaiwagikateaavseefglapflpdqihfvhsqellsrypdldak
greraiakdlgavflvgiggklsdghrhdvrapdyddwstpselghaglngdilvwnpvl
edafelssmgirvdadtlkhqlaltgdedrlelewhqallrgempqtigggigqsrltml
llqlphigqvqagvwpaavresvpsll
>d11baa_ 4.5.1.1.5 Seminal ribonucleasease {Bovine (Bos taurus)}
kesaaakferqhmdsgnspssssnycnlmmccrkmtqgkckpvntfvhesladvkavcsq
kkvtckngqtncyqskstmritdcretgsskypncaykttqvekhiivacggkpsvpvhf
dasv
>d11bab_ 4.5.1.1.5 Seminal ribonucleasease {Bovine (Bos taurus)}
kesaaakferqhmdsgnspssssnycnlmmccrkmtqgkckpvntfvhesladvkavcsq
kkvtckngqtncyqskstmritdcretgsskypncaykttqvekhiivacggkpsvpvhf
dasv
>d11gsa1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d11gsa2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d11gsb1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d11gsb2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d120l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnsakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d121p__ 3.30.1.6.1 cH-p21 Ras protein {Human (Homo sapiens)}
mteyklvvvgaggvgksaltiqliqnhfvdeydptiedsyrkqvvidgetclldildtag
qeeysamrdqymrtgegflcvfainntksfedihqyreqikrvkdsddvpmvlvgnkcdl
aartvesrqaqdlarsygipyietsaktrqgvedafytlvreirqh
>d122l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdsavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d123l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnsklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d125l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraslinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d126l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrtittfrtgtwdayk
>d127l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaatrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d128l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkptydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d129l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldtvrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d12asa_ 4.82.1.1.12 Asparagine synthetase {Escherichia coli}
ayiakqrqisfvkshfsrqleerlglievqapilsrvgdgtqdnlsgaekavqvkvkalp
daqfevvhslakwkrqtlgqhdfsageglythmkalrpdedrlsplhsvyvdqwdwervm
gdgerqfstlkstveaiwagikateaavseefglapflpdqihfvhsqellsrypdldak
greraiakdlgavflvgiggklsdghrhdvrapdyddwstpselghaglngdilvwnpvl
edafelssmgirvdadtlkhqlaltgdedrlelewhqallrgempqtigggigqsrltml
llqlphigqvqagvwpaavresvpsll
>d12asb_ 4.82.1.1.12 Asparagine synthetase {Escherichia coli}
ayiakqrqisfvkshfsrqleerlglievqapilsrvgdgtqdnlsgaekavqvkvkalp
daqfevvhslakwkrqtlgqhdfsageglythmkalrpdedrlsplhsvyvdqwdwervm
gdgerqfstlkstveaiwagikateaavseefglapflpdqihfvhsqellsrypdldak
greraiakdlgavflvgiggklsdghrhdvrapdyddwstpselghaglngdilvwnpvl
edafelssmgirvdadtlkhqlaltgdedrlelewhqallrgempqtigggigqsrltml
llqlphigqvqagvwpaavresvpsll
>d12ca__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlahwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d12e8h1 2.1.1.1.110 (1-114) Immunoglobulin (variable domains of L and H chains) {Fab 2E8 (mouse), kappa L chain}
evqlqqsgaevvrsgasvklsctasgfnikdyyihwvkqrpekglewigwidpeigdtey
vpkfqgkatmtadtssntaylqlssltsedtavyycnaghdydrgrfpywgqgtlvtvsa
a
>d12e8h2 2.1.1.2.109 (115-214) Immunoglobulin (constant domains of L and H chains) {Fab 2E8 (mouse), kappa L chain}
kttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsdl
ytlsssvtvpsstwpsetvtcnvahpasstkvdkkivprd
>d12e8l1 2.1.1.1.110 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab 2E8 (mouse), kappa L chain}
divmtqsqkfmstsvgdrvsitckasqnvgtavawyqqkpgqspklmiysasnrytgvpd
rftgsgsgtdftltisnmqsedladyfcqqyssypltfgagtklelk
>d12e8l2 2.1.1.2.109 (108-214) Immunoglobulin (constant domains of L and H chains) {Fab 2E8 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnsatdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d12e8m1 2.1.1.1.110 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab 2E8 (mouse), kappa L chain}
divmtqsqkfmstsvgdrvsitckasqnvgtavawyqqkpgqspklmiysasnrytgvpd
rftgsgsgtdftltisnmqsedladyfcqqyssypltfgagtklelk
>d12e8m2 2.1.1.2.109 (108-214) Immunoglobulin (constant domains of L and H chains) {Fab 2E8 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnsatdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d12e8p1 2.1.1.1.110 (1-114) Immunoglobulin (variable domains of L and H chains) {Fab 2E8 (mouse), kappa L chain}
evqlqqsgaevvrsgasvklsctasgfnikdyyihwvkqrpekglewigwidpeigdtey
vpkfqgkatmtadtssntaylqlssltsedtavyycnaghdydrgrfpywgqgtlvtvsa
a
>d12e8p2 2.1.1.2.109 (115-214) Immunoglobulin (constant domains of L and H chains) {Fab 2E8 (mouse), kappa L chain}
kttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsdl
ytlsssvtvpsstwpsetvtcnvahpasstkvdkkivprd
>d12gsa1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d12gsa2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d12gsb1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d12gsb2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d130l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvistfrtgtwdayk
>d131l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyysigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d132l__ 4.2.1.2.1 Lysozyme {Chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d133l__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawvawrnhcqnrd
vrqyvqgcgv
>d134l__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawvawrnecqnrd
vrqyvqgcgv
>d135l__ 4.2.1.2.2 Lysozyme {Turkey (Meleagris gallopavo)}
kvygrcelaaamkrlgldnyrgyslgnwvcaakfesnfnthatnrntdgstdygilqins
rwwcndgrtpgsknlcnipcsallssditasvncakkiasggngmnawvawrnrckgtdv
hawirgcrl
>d137la_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakfeldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d137lb_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakfeldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d138l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldcvrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d139l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfcqdvdaavrgilrnaklkpvydsldcvrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d13gsa1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d13gsa2 3.38.1.5.4 (0-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
mppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgd
ltlyqsntilrhlgrtl
>d13gsb1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d13gsb2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d13pka_ 3.75.1.1.4 Phosphoglycerate kinase {Trypanosoma brucei}
ekksinecdlkgkkvlirvdfnvpvkngkitndyrirsalptlkkvlteggscvlmshlg
rpkgipmaqagkirstggvpgfqqkatlkpvakrlselllrpvtfapdclnaadvvskms
pgdvvllenvrfykeegskkakdreamakilasygdvyisdafgtahrdsatmtgipkil
gngaagylmekeisyfakvlgnpprplvaivggakvsdkiqlldnmlqridylliggama
ytflkaqgysigkskceesklefarsllkkaedrkvqvilpidhvchtefkavdsplite
dqnipeghmaldigpktiekyvqtigkcksaiwngpmgvfemvpyskgtfaiakamgrgt
hehglmsiigggdsasaaelsgeakrmshvstgggaslellegktlpgvtvlddk
>d13pkb_ 3.75.1.1.4 Phosphoglycerate kinase {Trypanosoma brucei}
ekksinecdlkgkkvlirvdfnvpvkngkitndyrirsalptlkkvlteggscvlmshlg
rpkgipmaqagkirstggvpgfqqkatlkpvakrlselllrpvtfapdclnaadvvskms
pgdvvllenvrfykeegskkakdreamakilasygdvyisdafgtahrdsatmtgipkil
gngaagylmekeisyfakvlgnpprplvaivggakvsdkiqlldnmlqridylliggama
ytflkaqgysigkskceesklefarsllkkaedrkvqvilpidhvchtefkavdsplite
dqnipeghmaldigpktiekyvqtigkcksaiwngpmgvfemvpyskgtfaiakamgrgt
hehglmsiigggdsasaaelsgeakrmshvstgggaslellegktlpgvtvlddk
>d13pkc_ 3.75.1.1.4 Phosphoglycerate kinase {Trypanosoma brucei}
ekksinecdlkgkkvlirvdfnvpvkngkitndyrirsalptlkkvlteggscvlmshlg
rpkgipmaqagkirstggvpgfqqkatlkpvakrlselllrpvtfapdclnaadvvskms
pgdvvllenvrfykeegskkakdreamakilasygdvyisdafgtahrdsatmtgipkil
gngaagylmekeisyfakvlgnpprplvaivggakvsdkiqlldnmlqridylliggama
ytflkaqgysigkskceesklefarsllkkaedrkvqvilpidhvchtefkavdsplite
dqnipeghmaldigpktiekyvqtigkcksaiwngpmgvfemvpyskgtfaiakamgrgt
hehglmsiigggdsasaaelsgeakrmshvstgggaslellegktlpgvtvlddk
>d13pkd_ 3.75.1.1.4 Phosphoglycerate kinase {Trypanosoma brucei}
ekksinecdlkgkkvlirvdfnvpvkngkitndyrirsalptlkkvlteggscvlmshlg
rpkgipmaqagkirstggvpgfqqkatlkpvakrlselllrpvtfapdclnaadvvskms
pgdvvllenvrfykeegskkakdreamakilasygdvyisdafgtahrdsatmtgipkil
gngaagylmekeisyfakvlgnpprplvaivggakvsdkiqlldnmlqridylliggama
ytflkaqgysigkskceesklefarsllkkaedrkvqvilpidhvchtefkavdsplite
dqnipeghmaldigpktiekyvqtigkcksaiwngpmgvfemvpyskgtfaiakamgrgt
hehglmsiigggdsasaaelsgeakrmshvstgggaslellegktlpgvtvlddk
>d140l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
aqqkrwdemavnlaksrwynqtpnrakrvittlrtgtwdayk
>d141l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
aqqkrwdemavnlaksrwynqtpnrakriittfrtgtwdayk
>d142l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
aqqkrwdevavnaaksrwynqtpnrakrvittlrtgtwdayk
>d143l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
aqqkrwdevavnmaksrwynqtpnrakrvittlrtgtwdayk
>d144l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
iqqkrwdelavnmaksrwynqtpnrakrvittwrtgtwdayk
>d145l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
iqqkrwdewavnmaksrwynqtpnrakrvittfrtgtwdayk
>d146l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
mqqkrwdelavnmaksrwynqtpnrakriittwrtgtwdayk
>d147l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
mqqkrwdeaavnvaksrwynqtpnrakrvittlrtgtwdayk
>d148le_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyyeigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdaykn
>d149l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnlfemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d14gsa1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d14gsa2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d14gsb1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d14gsb2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d150la_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifeilrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d150lb_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifeilrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d150lc_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifeilrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d150ld_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifeilrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d151l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighllaaaaslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d152l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mncfemlrcdeglrlkiykdcegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqcpnrakrvittfrtgtwdayknc
>d153l__ 4.2.1.5.1 Lysozyme {Goose (Anser anser anser)}
rtdcygnvnridttgascktakpeglsycgvsaskkiaerdlqamdryktiikkvgeklc
vepaviagiisreshagkvlkngwgdrgngfglmqvdkrshkpqgtwngevhitqgttil
infiktiqkkfpswtkdqqlkggisaynagagnvrsyarmdigtthddyandvvaraqyy
kqhgy
>d154l__ 4.2.1.5.1 Lysozyme {Goose (Anser anser anser)}
rtdcygnvnridttgascktakpeglsycgvsaskkiaerdlqamdryktiikkvgeklc
vepaviagiisreshagkvlkngwgdrgngfglmqvdkrshkpqgtwngevhitqgttil
infiktiqkkfpswtkdqqlkggisaynagagnvrsyarmdigtthddyandvvaraqyy
kqhgy
>d155c__ 1.3.1.1.17 Cytochrome c2 {Paracoccus denitrificans}
xnegdaakgekefnkckachmiqapdgtdikggktgpnlygvvgrkiaseegfkygegil
evaeknpdltwteanlieyvtdpkplvkkmtddkgaktkmtfkmgknqadvvaflaqddp
daxxxxxxxxxxxxx
>d155l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagfanalrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d156l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagfanslam
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d157l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagfaaalaa
laakrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d158l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnalam
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d159l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslam
lqakrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d15c8h1 2.1.1.1.117 (1-113) Immunoglobulin (variable domains of L and H chains) {Catalytic Fab 5C8 (mouse), kappa L chain}
evqlqqsgaelvkpgasvklsctasgfnikdtymhwvkqkpeqglewiaqidpangntky
dpkfqgkatitadtssntaylhlssltsedsavyycaadppyyghgdywgqgttltvss
>d15c8h2 2.1.1.2.115 (114-226) Immunoglobulin (constant domains of L and H chains) {Catalytic Fab 5C8 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpsstwpsetvtcnvahpasstkvdkkiv
>d15c8l1 2.1.1.1.117 (1-107) Immunoglobulin (variable domains of L and H chains) {Catalytic Fab 5C8 (mouse), kappa L chain}
divltqspaimsaslgervtmtctasssvsssnlhwyqqkpgsspklwiystsnlasgvp
arfsgsgsgtsysltissmeaedaatyychqyhrspytfgggtkleik
>d15c8l2 2.1.1.2.115 (108-212) Immunoglobulin (constant domains of L and H chains) {Catalytic Fab 5C8 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrn
>d160l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslra
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d161l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftaslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d162l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
laqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d163l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqakrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d164l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslam
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d165l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnalrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d166l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagfanslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d167la_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mncfemlrcdeglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknc
>d167lb_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mncfemlrcdeglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknc
>d168la_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdaaaaalaaaawynqtpnrakrvittfrtgtwdayknl
>d168lb_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdaaaaalaaaawynqtpnrakrvittfrtgtwdayknl
>d168lc_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdaaaaalaaaawynqtpnrakrvittfrtgtwdayknl
>d168ld_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdaaaaalaaaawynqtpnrakrvittfrtgtwdayknl
>d168le_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdaaaaalaaaawynqtpnrakrvittfrtgtwdayknl
>d169la_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdaaaaalaaaawaaatpnrakrvittfrtgtwdayk
>d169lb_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdaaaaalaaaawaaatpnrakrvittfrtgtwdayk
>d169lc_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdaaaaalaaaawaaatpnrakrvittfrtgtwdayk
>d169ld_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdaaaaalaaaawaaatpnrakrvittfrtgtwdayk
>d169le_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdaaaaalaaaawaaatpnrakrvittfrtgtwdayk
>d16gsa1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d16gsa2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d16gsb1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d16gsb2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d16pk__ 3.75.1.1.4 Phosphoglycerate kinase {Trypanosoma brucei}
ekksinecdlkgkkvlirvdfnvpvkngkitndyrirsalptlkkvlteggscvlmshlg
rpkgipmaqagkirstggvpgfqqkatlkpvakrlselllrpvtfapdclnaadvvskms
pgdvvllenvrfykeegskkakdreamakilasygdvyisdafgtahrdsatmtgipkil
gngaagylmekeisyfakvlgnpprplvaivggakvsdkiqlldnmlqridylliggama
ytflkaqgysigkskceesklefarsllkkaedrkvqvilpidhvchtefkavdsplite
dqnipeghmaldigpktiekyvqtigkcksaiwngpmgvfemvpyskgtfaiakamgrgt
hehglmsiigggdsasaaelsgeakrmshvstgggaslellegktlpgvtvlddk
>d16vpa_ 4.149.1.1.1 Conserved core of transcriptional regulatory protein vp16 {Herpes simplex virus, type 1, HSV-1}
srmpsppmpvppaalfnrllddlgfsagpalctmldtwnedlfsalptnadlyreckfls
tlpsdvvewgdayvpertqidirahgdvafptlpatrdglglyyealsrffhaelraree
syrtvlanfcsalyrylrasvrqlhrqahmrgrdrdlgemlratiadryyretarlarvl
flhlylfltreilwaayaeqmmrpdlfdclccdleswrqlaglfqpfmfvngaltvrgvp
iearrlrelnhirehlnlplvrsaateepgaplttpptlhgnqarasgyfmvliraklds
yssfttspseavmrehaysraptknnygstieglldlpdddapeeaglaaprlsfl
>d170l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrnsngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrsalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrckrvittfrtgtwdayknl
>d171l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaaksaldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d172l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mncfemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d173l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrleiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslem
lqqkrwdeaavnlaesrwynqtpnraervittfrtgtwdayk
>d174la_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighllaaaadlaaakaalaaaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d174lb_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighllaaaadlaaakaalaaaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d175la_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavraaalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d175lb_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavraaalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d176la_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigightlkvdgnsnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d176lb_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigightlkvdgnsnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d177l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwceaavnlaksrwynqtpnrakrvittfctgtwdayk
>d178l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwceaavnlaksrwynqtpnrakrvittfctgtwdayk
>d179l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwceaavnlaksrwynqtpnrakrvittfctgtwdayk
>d17gsa1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d17gsa2 3.38.1.5.4 (0-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
mppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpafqdgd
ltlyqsntilrhlgrtl
>d17gsb1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d17gsb2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpafqdgdlt
lyqsntilrhlgrtl
>d180la_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyyeigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d180lb_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyyeigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d181l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraaainmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d182l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraaainmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d183l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraaainmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d184l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraaainmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d185l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraaainmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d186l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraaainmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d187l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraaainmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d188l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraaainmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d189l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnlfemlrideglrlkiykdtegyytigighlltkspdlnvakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnpklkpvydsldavrrcalinmvfqmgetgvagftdslrm
lqqkrwdeaaanlaksrwynqtpdrakrvittfrtgtwdayknl
>d18gsa1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d18gsa2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d18gsb1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d18gsb2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d190l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigracagaitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1914__ 4.40.1.1.1 Signal recognition particle alu RNA binding heterodimer, SRP9/14 {Mouse (Mus musculus)}
mvlleseqflteltrlfqkcrssgsvfitlkkydgrtkpiprkssveglepaenkcllra
tdgkrkistvvsskevnkfqmaysnllranmdglkkrdkknkskkskpaqggeqklisee
ddsagspmpqfqtweefsraaeklyladpmkvrvvlkyrhvdgnlcikvtddlvclvyrt
dqaqdvkkiekfhsqlmrlmvakesrnv
>d191l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigracagaitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdaaaaalaksrwynqtpnrakrvittfrtgtwdayk
>d192l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslaaakaalaaaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwaaaaaalaksrwynqtpnrakrvittfrtgtwdayk
>d193l__ 4.2.1.2.1 Lysozyme {Chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d194l__ 4.2.1.2.1 Lysozyme {Chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d195l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdelavnlaksrwynqtpnrakrvittfrtgtwdayk
>d196l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdemavnlaksrwynqtpnrakrvittfrtgtwdayk
>d197l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdemavnlaksrwynqtpnrakrvittartgtwdayk
>d198l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
aqqkrwdelavnlaksrwynqtpnrakrvittfrtgtwdayk
>d199l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
aqqkrwdemavnlaksrwynqtpnrakrvittfrtgtwdayk
>d19gsa1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d19gsa2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d19gsb1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d19gsb2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d1a00a_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a00b_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypytqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a00c_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a00d_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypytqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a01a_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a01b_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypatqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a01c_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a01d_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypatqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a02n1 2.1.1.5.20 (577-678) Transcription factor NFATC, C-terminal domain {Human (Homo sapiens)}
lpmverqdtdsclvyggqqmiltgqnftseskvvftekttdgqqiwemeatvdkdksqpn
mlfveipeyrnkhirtpvkvnfyvingkrkrsqpqhftyhpv
>d1a02n2 2.2.5.1.2 (399-576) Transcription factor NFATC, DNA-binding domain {Human (Homo sapiens)}
wplssqsgsyelrievqpkphhrahyetegsrgavkaptgghpvvqlhgymenkplglqi
figtaderilkphafyqvhritgktvtttsyekivgntkvleiplepknnmratidcagi
lklrnadielrkgetdigrkntrvrlvfrvhipessgrivslqtasnpiecsqrsahe
>d1a03a_ 1.42.1.2.1 Calcyclin (S100) {Rabbit (Oryctolagus cuniculus)}
maspldqaiglligifhkysgkegdkhtlskkelkeliqkeltigsklqdaeivklmddl
drnkdqevnfqeyitflgalamiynealkg
>d1a03b_ 1.42.1.2.1 Calcyclin (S100) {Rabbit (Oryctolagus cuniculus)}
maspldqaiglligifhkysgkegdkhtlskkelkeliqkeltigsklqdaeivklmddl
drnkdqevnfqeyitflgalamiynealkg
>d1a04a1 1.37.1.2.1 (150-216) Nitrate/nitrite response regulator (NARL), receiver domain {Escherichia coli}
erdvnqltprerdilkliaqglpnkmiarrlditestvkvhvkhmlkkmklksrveaavw
vhqerif
>d1a04a2 3.16.2.1.4 (5-142) Nitrate/nitrite response regulator (NARL), receiver domain {Escherichia coli}
epatilliddhpmlrtgvkqlismapditvvgeasngeqgielaesldpdlilldlnmpg
mngletldklrekslsgrivvfsvsnheedvvtalkrgadgyllkdmepedllkalhqaa
agemvlsealtpvlaasl
>d1a04b1 1.37.1.2.1 (150-216) Nitrate/nitrite response regulator (NARL), receiver domain {Escherichia coli}
erdvnqltprerdilkliaqglpnkmiarrlditestvkvhvkhmlkkmklksrveaavw
vhqerif
>d1a04b2 3.16.2.1.4 (5-142) Nitrate/nitrite response regulator (NARL), receiver domain {Escherichia coli}
epatilliddhpmlrtgvkqlismapditvvgeasngeqgielaesldpdlilldlnmpg
mngletldklrekslsgrivvfsvsnheedvvtalkrgadgyllkdmepedllkalhqaa
agemvlsealtpvlaasl
>d1a05a_ 3.65.1.1.4 3-isopropylmalate dehydrogenase, IPMDH {Thiobacillus ferrooxidans}
mkkiaifagdgigpeivaaarqvldavdqaahlglrcteglvggaaldasddplpaaslq
lamaadavilgavggprwdayppakrpeqgllrlrkgldlyanlrpaqifpqlldasplr
pelvrdvdilvvreltgdiyfgqprglevidgkrrgfntmvydedeirriahvafraaqg
rrkqlcsvdkanvlettrlwrevvtevardypdvrlshmyvdnaamqlirapaqfdvllt
gnmfgdilsdeasqltgsigmlpsaslgegramyepihgsapdiagqdkanplatilsva
mmlrhslnaepwaqrveaavqrvldqglrtadiaapgtpvigtkamgaavvnalnlk
>d1a05b_ 3.65.1.1.4 3-isopropylmalate dehydrogenase, IPMDH {Thiobacillus ferrooxidans}
mkkiaifagdgigpeivaaarqvldavdqaahlglrcteglvggaaldasddplpaaslq
lamaadavilgavggprwdayppakrpeqgllrlrkgldlyanlrpaqifpqlldasplr
pelvrdvdilvvreltgdiyfgqprglevidgkrrgfntmvydedeirriahvafraaqg
rrkqlcsvdkanvlettrlwrevvtevardypdvrlshmyvdnaamqlirapaqfdvllt
gnmfgdilsdeasqltgsigmlpsaslgegramyepihgsapdiagqdkanplatilsva
mmlrhslnaepwaqrveaavqrvldqglrtadiaapgtpvigtkamgaavvnalnlk
>d1a06__ 4.117.1.1.6 Calmodulin-dependent protein kinase {Rat (Rattus norvegicus)}
wkqaedirdiydfrdvlgtgafsevilaedkrtqklvaikciakkalegkegsmeneiav
lhkikhpnivalddiyesgghlylimqlvsggelfdrivekgfyterdasrlifqvldav
kylhdlgivhrdlkpenllyysldedskimisdfglskmedpgsvlstacgtpgyvapev
laqkpyskavdcwsigviayillcgyppfydendaklfeqilkaeyefdspywddisdsa
kdfirhlmekdpekrftceqalqhpwiagdtaldknihqsvseqikknfakskwkqafna
tavvrhm
>d1a07a_ 4.72.1.1.3 c-src tyrosine kinase {Human (Homo sapiens)}
siqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkh
ykirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a07b_ 4.72.1.1.3 c-src tyrosine kinase {Human (Homo sapiens)}
iqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkhy
kirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a08a_ 4.72.1.1.3 c-src tyrosine kinase {Human (Homo sapiens)}
siqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkh
ykirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a08b_ 4.72.1.1.3 c-src tyrosine kinase {Human (Homo sapiens)}
iqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkhy
kirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a09a_ 4.72.1.1.3 c-src tyrosine kinase {Human (Homo sapiens)}
dsiqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvk
hykirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a09b_ 4.72.1.1.3 c-src tyrosine kinase {Human (Homo sapiens)}
aeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkhyki
rkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a0aa_ 1.41.1.1.5 Pho4 B/HLH domain {Baker's yeast (Saccharomyces cerevisiae)}
mkreshkhaeqarrnrlavalhelaslipaewkqqnvsaapskattveaacryirhlqqn
gst
>d1a0ab_ 1.41.1.1.5 Pho4 B/HLH domain {Baker's yeast (Saccharomyces cerevisiae)}
mkreshkhaeqarrnrlavalhelaslipaewkqqnvsaapskattveaacryirhlqqn
gst
>d1a0b__ 1.25.9.1.1 Aerobic respiration control sensor protein, ArcB {Escherichia coli}
ksealldipmleqylelvgpklitdglavfekmmpgyvsvlesnltaqdkkgiveeghki
kgaagsvglrhlqqlgqqiqspdlpawednvgewieemkeewrhdvevlkawvakat
>d1a0ca_ 3.1.13.2.7 D-xylose isomerase {Clostridium Thermosulfurogenes, also known as Thermoanaerobacter thermosulfurigenes}
nkyfenvskikyegpksnnpysfkfynpeevidgktmeehlrfsiaywhtftadgtdqfg
katmqrpwnhytdpmdiakarveaafeffdkinapyfcfhdrdiapegdtlretnknldt
ivamikdylktsktkvlwgtanlfsnprfvhgastscnadvfaysaaqvkkaleitkelg
genyvfwggregyetllntdmefeldnfarflhmavdyakeigfegqfliepkpkeptkh
qydfdvanvlaflrkydldkyfkvnieanhatlafhdfqhelryaringvlgsidantgd
mllgwdtdqfptdirmttlamyevikmggfdkgglnfdakvrrasfepedlflghiagmd
afakgfkvayklvkdrvfdkfieeryasykdgigadivsgkadfrslekyalersqivnk
sgrqellesilnqylfa
>d1a0cb_ 3.1.13.2.7 D-xylose isomerase {Clostridium Thermosulfurogenes, also known as Thermoanaerobacter thermosulfurigenes}
nkyfenvskikyegpksnnpysfkfynpeevidgktmeehlrfsiaywhtftadgtdqfg
katmqrpwnhytdpmdiakarveaafeffdkinapyfcfhdrdiapegdtlretnknldt
ivamikdylktsktkvlwgtanlfsnprfvhgastscnadvfaysaaqvkkaleitkelg
genyvfwggregyetllntdmefeldnfarflhmavdyakeigfegqfliepkpkeptkh
qydfdvanvlaflrkydldkyfkvnieanhatlafhdfqhelryaringvlgsidantgd
mllgwdtdqfptdirmttlamyevikmggfdkgglnfdakvrrasfepedlflghiagmd
afakgfkvayklvkdrvfdkfieeryasykdgigadivsgkadfrslekyalersqivnk
sgrqellesilnqylfa
>d1a0cc_ 3.1.13.2.7 D-xylose isomerase {Clostridium Thermosulfurogenes, also known as Thermoanaerobacter thermosulfurigenes}
nkyfenvskikyegpksnnpysfkfynpeevidgktmeehlrfsiaywhtftadgtdqfg
katmqrpwnhytdpmdiakarveaafeffdkinapyfcfhdrdiapegdtlretnknldt
ivamikdylktsktkvlwgtanlfsnprfvhgastscnadvfaysaaqvkkaleitkelg
genyvfwggregyetllntdmefeldnfarflhmavdyakeigfegqfliepkpkeptkh
qydfdvanvlaflrkydldkyfkvnieanhatlafhdfqhelryaringvlgsidantgd
mllgwdtdqfptdirmttlamyevikmggfdkgglnfdakvrrasfepedlflghiagmd
afakgfkvayklvkdrvfdkfieeryasykdgigadivsgkadfrslekyalersqivnk
sgrqellesilnqylfa
>d1a0cd_ 3.1.13.2.7 D-xylose isomerase {Clostridium Thermosulfurogenes, also known as Thermoanaerobacter thermosulfurigenes}
nkyfenvskikyegpksnnpysfkfynpeevidgktmeehlrfsiaywhtftadgtdqfg
katmqrpwnhytdpmdiakarveaafeffdkinapyfcfhdrdiapegdtlretnknldt
ivamikdylktsktkvlwgtanlfsnprfvhgastscnadvfaysaaqvkkaleitkelg
genyvfwggregyetllntdmefeldnfarflhmavdyakeigfegqfliepkpkeptkh
qydfdvanvlaflrkydldkyfkvnieanhatlafhdfqhelryaringvlgsidantgd
mllgwdtdqfptdirmttlamyevikmggfdkgglnfdakvrrasfepedlflghiagmd
afakgfkvayklvkdrvfdkfieeryasykdgigadivsgkadfrslekyalersqivnk
sgrqellesilnqylfa
>d1a0da_ 3.1.13.2.8 D-xylose isomerase {Bacillus stearothermophilus}
pyfdnistiayegpasknplafkfynpeekvgdktmeehlrfsvaywhtftgdgsdpfga
gnmirpwnkysgmdlakarveaafeffeklnipffcfhdvdiapegetlketyknldiiv
dmieeymktsktkllwntanlfthprfvhgaatscnadvfayaaakvkkgleiakrlgae
nyvfwggregyetllntdmkleldnlarflhmavdyakeigfdgqfliepkpkeptkhqy
dfdvatalaflqtyglkdyfkfnieanhatlaghtfehelrvarihgmlgsvdanqgdml
lgwdtdefptdlysttlamyeilkngglgrgglnfdakvrrgsfepedlfyahiagmdsf
avglkvahrliedrvfdefieeryksytegigreivegtadfhkleahalqlgeiqnqsg
rqerlktllnqyllevc
>d1a0db_ 3.1.13.2.8 D-xylose isomerase {Bacillus stearothermophilus}
pyfdnistiayegpasknplafkfynpeekvgdktmeehlrfsvaywhtftgdgsdpfga
gnmirpwnkysgmdlakarveaafeffeklnipffcfhdvdiapegetlketyknldiiv
dmieeymktsktkllwntanlfthprfvhgaatscnadvfayaaakvkkgleiakrlgae
nyvfwggregyetllntdmkleldnlarflhmavdyakeigfdgqfliepkpkeptkhqy
dfdvatalaflqtyglkdyfkfnieanhatlaghtfehelrvarihgmlgsvdanqgdml
lgwdtdefptdlysttlamyeilkngglgrgglnfdakvrrgsfepedlfyahiagmdsf
avglkvahrliedrvfdefieeryksytegigreivegtadfhkleahalqlgeiqnqsg
rqerlktllnqyllevc
>d1a0dc_ 3.1.13.2.8 D-xylose isomerase {Bacillus stearothermophilus}
pyfdnistiayegpasknplafkfynpeekvgdktmeehlrfsvaywhtftgdgsdpfga
gnmirpwnkysgmdlakarveaafeffeklnipffcfhdvdiapegetlketyknldiiv
dmieeymktsktkllwntanlfthprfvhgaatscnadvfayaaakvkkgleiakrlgae
nyvfwggregyetllntdmkleldnlarflhmavdyakeigfdgqfliepkpkeptkhqy
dfdvatalaflqtyglkdyfkfnieanhatlaghtfehelrvarihgmlgsvdanqgdml
lgwdtdefptdlysttlamyeilkngglgrgglnfdakvrrgsfepedlfyahiagmdsf
avglkvahrliedrvfdefieeryksytegigreivegtadfhkleahalqlgeiqnqsg
rqerlktllnqyllevc
>d1a0dd_ 3.1.13.2.8 D-xylose isomerase {Bacillus stearothermophilus}
pyfdnistiayegpasknplafkfynpeekvgdktmeehlrfsvaywhtftgdgsdpfga
gnmirpwnkysgmdlakarveaafeffeklnipffcfhdvdiapegetlketyknldiiv
dmieeymktsktkllwntanlfthprfvhgaatscnadvfayaaakvkkgleiakrlgae
nyvfwggregyetllntdmkleldnlarflhmavdyakeigfdgqfliepkpkeptkhqy
dfdvatalaflqtyglkdyfkfnieanhatlaghtfehelrvarihgmlgsvdanqgdml
lgwdtdefptdlysttlamyeilkngglgrgglnfdakvrrgsfepedlfyahiagmdsf
avglkvahrliedrvfdefieeryksytegigreivegtadfhkleahalqlgeiqnqsg
rqerlktllnqyllevc
>d1a0ea_ 3.1.13.2.9 D-xylose isomerase {Thermotoga neapolitana}
aeffpeipkvqfegkestnplafkfydpeeiidgkplkdhlkfsvafwhtfvnegrdpfg
dptadrpwnrytdpmdkafarvdalfefceklnieyfcfhdrdiapegktlretnkildk
vverikermkdsnvkllwgtanlfshprymhgaattcsadvfayaaaqvkkaleitkelg
gegyvfwggregyetllntdlgfelenlarflrmavdyakrigftgqfliepkpkeptkh
qydfdvatayaflkshgldeyfkfnieanhatlaghtfqhelrmarilgklgsidanqgd
lllgwdtdqfptnvydttlamyevikaggftkgglnfdakvrrasykvedlfighiagmd
tfalgfkvayklvkdgvldkfieekyrsfregigrdivegkvdfekleeyiidketielp
sgkqeyleslinsyivktilelr
>d1a0ed_ 3.1.13.2.9 D-xylose isomerase {Thermotoga neapolitana}
aeffpeipkvqfegkestnplafkfydpeeiidgkplkdhlkfsvafwhtfvnegrdpfg
dptadrpwnrytdpmdkafarvdalfefceklnieyfcfhdrdiapegktlretnkildk
vverikermkdsnvkllwgtanlfshprymhgaattcsadvfayaaaqvkkaleitkelg
gegyvfwggregyetllntdlgfelenlarflrmavdyakrigftgqfliepkpkeptkh
qydfdvatayaflkshgldeyfkfnieanhatlaghtfqhelrmarilgklgsidanqgd
lllgwdtdqfptnvydttlamyevikaggftkgglnfdakvrrasykvedlfighiagmd
tfalgfkvayklvkdgvldkfieekyrsfregigrdivegkvdfekleeyiidketielp
sgkqeyleslinsyivktilelr
>d1a0fa1 1.48.1.1.19 (81-201) Glutathione S-transferase {Escherichia coli}
qllapvnsisryktiewlnyiatelhkgftplfrpdtpeeykptvraqlekklqyvneal
kdehwicgqrftiadaylftvlrwayavklnleglehiaafmqrmaerpevqdalsaegl
k
>d1a0fa2 3.38.1.5.19 (1-80) Glutathione S-transferase {Escherichia coli}
mklfykpgacslashitlresgkdftlvsvdlmkkrlengddyfavnpkgqvpalllddg
tlltegvaimqyladsvpdr
>d1a0fb1 1.48.1.1.19 (81-201) Glutathione S-transferase {Escherichia coli}
qllapvnsisryktiewlnyiatelhkgftplfrpdtpeeykptvraqlekklqyvneal
kdehwicgqrftiadaylftvlrwayavklnleglehiaafmqrmaerpevqdalsaegl
k
>d1a0fb2 3.38.1.5.19 (1-80) Glutathione S-transferase {Escherichia coli}
mklfykpgacslashitlresgkdftlvsvdlmkkrlengddyfavnpkgqvpalllddg
tlltegvaimqyladsvpdr
>d1a0ga_ 5.13.1.1.1 D-amino acid aminotransferase {Bacillus strain YM-1}
gytlwndqivkdeevkidkedrgyqfgdgvyevvkvyngemftvnehidrlyasaekiri
tipytkdkfhqllhelveknelntghiyfqvtrgtsprahqfpentvkpviigytkenpr
plenlekgvkatfvedirwlrcdikslnllgavlakqeahekgcyeailhrnntvtegss
snvfgikdgilythpannmiakgitrdvviacaneinmpvkeipftthealkmdelfvts
ttseitpvieidgklirdgkvgewtrklqkqfetkipkpl
>d1a0gb_ 5.13.1.1.1 D-amino acid aminotransferase {Bacillus strain YM-1}
gytlwndqivkdeevkidkedrgyqfgdgvyevvkvyngemftvnehidrlyasaekiri
tipytkdkfhqllhelveknelntghiyfqvtrgtsprahqfpentvkpviigytkenpr
plenlekgvkatfvedirwlrcdikslnllgavlakqeahekgcyeailhrnntvtegss
snvfgikdgilythpannmiakgitrdvviacaneinmpvkeipftthealkmdelfvts
ttseitpvieidgklirdgkvgewtrklqkqfetkipkplhi
>e1a0h.1a 2.41.1.2.12 (271-320) Thrombin {Bovine (Bos taurus)}
rtsedhfqpffnektfgageadcglrplfekkqvqdqtekelfesyiegr
>e1a0h.1b 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
ivegqdaevglspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftvddll
vrigkhsrtryerkvekismldkiyihprynwkenldrdiallklkrpielsdyihpvcl
pdkqtaakllhagfkgrvtgwgnrretwttsvaevqpsvlqvvnlplverpvckastrir
itdnmfcagykpgegkrgdacegdsggpfvmkspynnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidrlgs
>e1a0h.2d 2.41.1.2.12 (271-320) Thrombin {Bovine (Bos taurus)}
rtsedhfqpffnektfgageadcglrplfekkqvqdqtekelfesyiegr
>e1a0h.2e 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
ivegqdaevglspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftvddll
vrigkhsrtryerkvekismldkiyihprynwkenldrdiallklkrpielsdyihpvcl
pdkqtaakllhagfkgrvtgwgnrretwttsvaevqpsvlqvvnlplverpvckastrir
itdnmfcagykpgegkrgdacegdsggpfvmkspynnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidrlgs
>d1a0ha1 7.14.1.1.5 (164-270) Meizothrombin domain {Bovine (Bos taurus)}
splletcvpdrgreyrgrlavtthgsrclawsseqakalskdqdfnpavplaenfcrnpd
gdeegawcyvadqpgdfeycdlnyceepvdgdlgdrlgedpdpdaaieg
>d1a0hd1 7.14.1.1.5 (164-270) Meizothrombin domain {Bovine (Bos taurus)}
splletcvpdrgreyrgrlavtthgsrclawsseqakalskdqdfnpavplaenfcrnpd
gdeegawcyvadqpgdfeycdlnyceepvdgdlgdrlgedpdpdaaieg
>d1a0i_1 2.35.4.6.2 (241-349) ATP-dependent DNA ligase {Bacteriophage T7}
peneadgiiqglvwgtkglanegkvigfevllesgrlvnatnisralmdeftetvkeatl
sqwgffspygigdndactinpydgwacqisymeetpdgslrhpsfvmfr
>d1a0i_2 4.115.2.1.1 (2-240) ATP-dependent DNA ligase, N-terminal domain {Bacteriophage T7}
vniktnpfkavsfvesaikkaldnagyliaeikydgvrgnicvdntansywlsrvsktip
alehlngfdvrwkrllnddrcfykdgfmldgelmvkgvdfntgsgllrtkwtdtknqefh
eelfvepirkkdkvpfklhtghlhiklyailplhivesgedcdvmtllmqehvknmlpll
qeyfpeiewqaaesyevydmvelqqlyeqkraegheglivkdpmciykrgkksgwwkmk
>d1a0ja_ 2.41.1.2.5 Trypsin(ogen) {North atlantic salmon (Salmo salar)}
ivggyecrknsasyqaslqsgyhfcggslisstwvvsaahcyksriqvrlgehniavneg
teqfidsvkvimhpsynsrnldndimliklskpaslnsyvstvalpsscassgtrclvsg
wgnlsgsssnypdtlrcldlpilsssscnsaypgqitsnmfcagfmeggkdscqgdsggp
vvcngqlqgvvswgygcaqrnkpgvytkvcnyrswisstmssn
>d1a0jb_ 2.41.1.2.5 Trypsin(ogen) {North atlantic salmon (Salmo salar)}
ivggyecrknsasyqaslqsgyhfcggslisstwvvsaahcyksriqvrlgehniavneg
teqfidsvkvimhpsynsrnldndimliklskpaslnsyvstvalpsscassgtrclvsg
wgnlsgsssnypdtlrcldlpilsssscnsaypgqitsnmfcagfmeggkdscqgdsggp
vvcngqlqgvvswgygcaqrnkpgvytkvcnyrswisstmssn
>d1a0jc_ 2.41.1.2.5 Trypsin(ogen) {North atlantic salmon (Salmo salar)}
ivggyecrknsasyqaslqsgyhfcggslisstwvvsaahcyksriqvrlgehniavneg
teqfidsvkvimhpsynsrnldndimliklskpaslnsyvstvalpsscassgtrclvsg
wgnlsgsssnypdtlrcldlpilsssscnsaypgqitsnmfcagfmeggkdscqgdsggp
vvcngqlqgvvswgygcaqrnkpgvytkvcnyrswisstmssn
>d1a0jd_ 2.41.1.2.5 Trypsin(ogen) {North atlantic salmon (Salmo salar)}
ivggyecrknsasyqaslqsgyhfcggslisstwvvsaahcyksriqvrlgehniavneg
teqfidsvkvimhpsynsrnldndimliklskpaslnsyvstvalpsscassgtrclvsg
wgnlsgsssnypdtlrcldlpilsssscnsaypgqitsnmfcagfmeggkdscqgdsggp
vvcngqlqgvvswgygcaqrnkpgvytkvcnyrswisstmssn
>d1a0k__ 4.86.1.1.6 Profilin (actin-binding protein) {Mouse-ear cress (Arabidopsis thaliana)}
swqsyvddhlmcdvegnhltaaailgqdgsvwaqsakfpqlkpqeidgikkdfeepgfla
ptglflggekymviqgeqgavirgkkgpggvtikktnqalvfgfydepmtggqcnlvver
lgdyliesel
>d1a0la_ 2.41.1.2.19 beta-Tryptase {Human (Homo sapiens)}
ivggqeaprskwpwqvslrvhgpywmhfcggslihpqwvltaahcvgpdvkdlaalrvql
reqhlyyqdqllpvsriivhpqfytaqigadialleleepvkvsshvhtvtlppasetfp
pgmpcwvtgwgdvdnderlpppfplkqvkvpimenhicdakyhlgaytgddvrivrddml
cagntrrdscqgdsggplvckvngtwlqagvvswgegcaqpnrpgiytrvtyyldwihhy
vpkk
>d1a0lb_ 2.41.1.2.19 beta-Tryptase {Human (Homo sapiens)}
ivggqeaprskwpwqvslrvhgpywmhfcggslihpqwvltaahcvgpdvkdlaalrvql
reqhlyyqdqllpvsriivhpqfytaqigadialleleepvkvsshvhtvtlppasetfp
pgmpcwvtgwgdvdnderlpppfplkqvkvpimenhicdakyhlgaytgddvrivrddml
cagntrrdscqgdsggplvckvngtwlqagvvswgegcaqpnrpgiytrvtyyldwihhy
vpkk
>d1a0lc_ 2.41.1.2.19 beta-Tryptase {Human (Homo sapiens)}
ivggqeaprskwpwqvslrvhgpywmhfcggslihpqwvltaahcvgpdvkdlaalrvql
reqhlyyqdqllpvsriivhpqfytaqigadialleleepvkvsshvhtvtlppasetfp
pgmpcwvtgwgdvdnderlpppfplkqvkvpimenhicdakyhlgaytgddvrivrddml
cagntrrdscqgdsggplvckvngtwlqagvvswgegcaqpnrpgiytrvtyyldwihhy
vpkk
>d1a0ld_ 2.41.1.2.19 beta-Tryptase {Human (Homo sapiens)}
ivggqeaprskwpwqvslrvhgpywmhfcggslihpqwvltaahcvgpdvkdlaalrvql
reqhlyyqdqllpvsriivhpqfytaqigadialleleepvkvsshvhtvtlppasetfp
pgmpcwvtgwgdvdnderlpppfplkqvkvpimenhicdakyhlgaytgddvrivrddml
cagntrrdscqgdsggplvckvngtwlqagvvswgegcaqpnrpgiytrvtyyldwihhy
vpkk
>d1a0nb_ 2.30.2.1.2 Fyn proto-oncogene tyrosine kinase, SH3 domain {Human (Homo sapiens)}
vtlfvalydyearteddlsfhkgekfqilnssegdwwearslttgetgyipsnyvapv
>d1a0oa_ 3.16.2.1.1 CheY protein {Escherichia coli}
adkelkflvvddfstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmp
nmdglellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleekln
kifeklgm
>d1a0ob_ 4.47.21.1.1 CheY-binding domain of CheA {Escherichia coli}
prriilsrlkagevdlleeelghlttltdvvkgadslsailpgdiaedditavlcfviea
dqitfetvev
>d1a0oc_ 3.16.2.1.1 CheY protein {Escherichia coli}
adkelkflvvddfstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmp
nmdglellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleekln
kifeklgm
>d1a0od_ 4.47.21.1.1 CheY-binding domain of CheA {Escherichia coli}
rriilsrlkagevdlleeelghlttltdvvkgadslsailpgdiaedditavlcfviead
qitfetv
>d1a0oe_ 3.16.2.1.1 CheY protein {Escherichia coli}
adkelkflvvddfstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmp
nmdglellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleekln
kifeklgm
>d1a0of_ 4.47.21.1.1 CheY-binding domain of CheA {Escherichia coli}
prriilsrlkagevdlleeelghlttltdvvkgadslsailpgdiaedditavlcfviea
dqitfetve
>d1a0og_ 3.16.2.1.1 CheY protein {Escherichia coli}
adkelkflvvddfstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmp
nmdglellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleekln
kifeklgm
>d1a0oh_ 4.47.21.1.1 CheY-binding domain of CheA {Escherichia coli}
rriilsrlkagevdlleeelghlttltdvvkgadslsailpgdiaedditavlcfviead
qitfetv
>d1a0p_1 1.61.2.1.2 (3-100) Recombinase XerD {Escherichia coli}
qdlarieqfldalwleknlaentlnayrrdlsmmvewlhhrgltlataqsddlqallaer
leggykatssarllsavrrlfqylyrekfreddpsahl
>d1a0p_2 4.133.1.1.4 (111-292) Recombinase XerD {Escherichia coli}
kdlseaqverllqaplidqplelrdkamlevlyatglrvselvgltmsdislrqgvvrvi
gkgnkerlvplgeeavywletylehgrpwllngvsidvlfpsqraqqmtrqtfwhrikhy
avlagidseklsphvlrhafathllnhgadlrvvqmllghsdlsttqiythvaterlrql
hq
>d1a0qh1 2.1.1.1.114 (2-114) Immunoglobulin (variable domains of L and H chains) {Fab 29G11 (mouse), kappa L chain}
vqlqesdaelvkpgasvkisckasgytftdhvihwvkqkpeqglewigyispgngdikyn
ekfkgkatltadkssstaymqlnsltsedsavylckrgyygrsnvdywgqgttltvssa
>d1a0qh2 2.1.1.2.112 (115-211) Immunoglobulin (constant domains of L and H chains) {Fab 29G11 (mouse), kappa L chain}
kttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsdl
ytlsssvtvpsstwpsetvtcnvahpasstkvdkkie
>d1a0ql1 2.1.1.1.114 (2-108) Immunoglobulin (variable domains of L and H chains) {Fab 29G11 (mouse), kappa L chain}
ieltqspsslsaslggkvtitckasqdikkyigwyqhkpgkqprllihytstllpgipsr
frgsgsgrdysfsisnlepediatyyclqyynlrtfgggtkleikr
>d1a0ql2 2.1.1.2.112 (109-213) Immunoglobulin (constant domains of L and H chains) {Fab 29G11 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfyskdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrne
>d1a0rb_ 2.60.3.1.1 beta1-subunit of the signal-transducing G protein heterotrimer {Bovine (Bos taurus)}
seldqlrqeaeqlknqirdarkacadatlsqitnnidpvgriqmrtrrtlrghlakiyam
hwgtdsrlllsasqdgkliiwdsyttnkvhaiplrsswvmtcayapsgnyvacggldnic
siynlktregnvrvsrelaghtgylsccrflddnqivtssgdttcalwdietgqqtttft
ghtgdvmslslapdtrlfvsgacdasaklwdvregmcrqtftghesdinaicffpngnaf
atgsddatcrlfdlradqelmtyshdniicgitsvsfsksgrlllagyddfncnvwdalk
adragvlaghdnrvsclgvtddgmavatgswdsflkiwn
>d1a0rg_ 1.125.2.1.1 Transducin (heterotrimeric G protein), gamma chain {Bovine (Bos taurus)}
pviniedltekdklkmevdqlkkevtlermlvskcceefrdyveersgedplvkgipedk
npfke
>d1a0rp_ 3.38.1.6.1 Phosducin {Rat (Rattus norvegicus)}
fegqashtgpkgvindwrkfklesedsdsvahskkeilrqmsspqsrddkdskerfsrkm
svqeyelihkdkedenclrkyrrqcmqdmhqklsfgprygfvyelesgeqfletiekeqk
ittivvhiyedgikgcdalnssliclaaeypmvkfckikasntgagdrfssdvlptllvy
kggellsnfisvteqlaeefftgdvesflneygllpek
>d1a0sp_ 6.4.3.2.3 Sucrose-specific porin {Enterobacterium (Salmonella typhimurium)}
sgfefhgyarsgvimndsgastksgayitpagetggaigrlgnqadtyvemnlehkqtld
ngattrfkvmvadgqtsyndwtastsdlnvrqafvelgnlptfagpfkgstlwagkrfdr
dnfdihwidsdvvflagtgggiydvkwndglrsnfslygrnfgdiddssnsvqnyiltmn
hfagplqmmvsglrakdnderkdsngnlakgdaantgvhallglhndsfyglrdgsskta
llyghglgaevkgigsdgalrpgadtwriasygttplsenwsvapamlaqrskdryadgd
syqwatfnlrliqainqnfalayegsyqymdlkpegyndrqavngsfykltfaptfkvgs
igdffsrpeirfytswmdwskklnnyasddalgsdgfnsggewsfgvqmetwf
>d1a0sq_ 6.4.3.2.3 Sucrose-specific porin {Enterobacterium (Salmonella typhimurium)}
sgfefhgyarsgvimndsgastksgayitpagetggaigrlgnqadtyvemnlehkqtld
ngattrfkvmvadgqtsyndwtastsdlnvrqafvelgnlptfagpfkgstlwagkrfdr
dnfdihwidsdvvflagtgggiydvkwndglrsnfslygrnfgdiddssnsvqnyiltmn
hfagplqmmvsglrakdnderkdsngnlakgdaantgvhallglhndsfyglrdgsskta
llyghglgaevkgigsdgalrpgadtwriasygttplsenwsvapamlaqrskdryadgd
syqwatfnlrliqainqnfalayegsyqymdlkpegyndrqavngsfykltfaptfkvgs
igdffsrpeirfytswmdwskklnnyasddalgsdgfnsggewsfgvqmetwf
>d1a0sr_ 6.4.3.2.3 Sucrose-specific porin {Enterobacterium (Salmonella typhimurium)}
sgfefhgyarsgvimndsgastksgayitpagetggaigrlgnqadtyvemnlehkqtld
ngattrfkvmvadgqtsyndwtastsdlnvrqafvelgnlptfagpfkgstlwagkrfdr
dnfdihwidsdvvflagtgggiydvkwndglrsnfslygrnfgdiddssnsvqnyiltmn
hfagplqmmvsglrakdnderkdsngnlakgdaantgvhallglhndsfyglrdgsskta
llyghglgaevkgigsdgalrpgadtwriasygttplsenwsvapamlaqrskdryadgd
syqwatfnlrliqainqnfalayegsyqymdlkpegyndrqavngsfykltfaptfkvgs
igdffsrpeirfytswmdwskklnnyasddalgsdgfnsggewsfgvqmetwf
>d1a0tp_ 6.4.3.2.3 Sucrose-specific porin {Enterobacterium (Salmonella typhimurium)}
sgfefhgyarsgvimndsgastksgayitpagetggaigrlgnqadtyvemnlehkqtld
ngattrfkvmvadgqtsyndwtastsdlnvrqafvelgnlptfagpfkgstlwagkrfdr
dnfdihwidsdvvflagtgggiydvkwndglrsnfslygrnfgdiddssnsvqnyiltmn
hfagplqmmvsglrakdnderkdsngnlakgdaantgvhallglhndsfyglrdgsskta
llyghglgaevkgigsdgalrpgadtwriasygttplsenwsvapamlaqrskdryadgd
syqwatfnlrliqainqnfalayegsyqymdlkpegyndrqavngsfykltfaptfkvgs
igdffsrpeirfytswmdwskklnnyasddalgsdgfnsggewsfgvqmetwf
>d1a0tq_ 6.4.3.2.3 Sucrose-specific porin {Enterobacterium (Salmonella typhimurium)}
sgfefhgyarsgvimndsgastksgayitpagetggaigrlgnqadtyvemnlehkqtld
ngattrfkvmvadgqtsyndwtastsdlnvrqafvelgnlptfagpfkgstlwagkrfdr
dnfdihwidsdvvflagtgggiydvkwndglrsnfslygrnfgdiddssnsvqnyiltmn
hfagplqmmvsglrakdnderkdsngnlakgdaantgvhallglhndsfyglrdgsskta
llyghglgaevkgigsdgalrpgadtwriasygttplsenwsvapamlaqrskdryadgd
syqwatfnlrliqainqnfalayegsyqymdlkpegyndrqavngsfykltfaptfkvgs
igdffsrpeirfytswmdwskklnnyasddalgsdgfnsggewsfgvqmetwf
>d1a0tr_ 6.4.3.2.3 Sucrose-specific porin {Enterobacterium (Salmonella typhimurium)}
sgfefhgyarsgvimndsgastksgayitpagetggaigrlgnqadtyvemnlehkqtld
ngattrfkvmvadgqtsyndwtastsdlnvrqafvelgnlptfagpfkgstlwagkrfdr
dnfdihwidsdvvflagtgggiydvkwndglrsnfslygrnfgdiddssnsvqnyiltmn
hfagplqmmvsglrakdnderkdsngnlakgdaantgvhallglhndsfyglrdgsskta
llyghglgaevkgigsdgalrpgadtwriasygttplsenwsvapamlaqrskdryadgd
syqwatfnlrliqainqnfalayegsyqymdlkpegyndrqavngsfykltfaptfkvgs
igdffsrpeirfytswmdwskklnnyasddalgsdgfnsggewsfgvqmetwf
>d1a0ua_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a0ub_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a0uc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a0ud_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a0va_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a0vb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypytqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a0vc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a0vd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypytqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a0wa_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a0wb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypatqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a0wc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a0wd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypatqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a0xa_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a0xb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypgtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a0xc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a0xd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypgtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a0ya_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a0yb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypetqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a0yc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a0yd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypetqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a0za_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a0zb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a0zc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a0zd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a10e_ 3.33.1.1.3 Subtilisin Carlsberg {Bacillus licheniformis, alcalase}
aqtvpygiplikadkvqaqgfkganvkvavldtgiqashpdlnvvggasfvageayntdg
nghgthvagtvaaldnttgvlgvapsvslyavkvlnssgsgsysgivsgiewattngmdv
inmslggasgstamkqavdnayargvvvvaaagnsgssgntntigypakydsviavgavd
snsnrasfssvgaelevmapgagvystyptntyatlngtsmasphvagaaalilskhpnl
sasqvrnrlsstatylgssfyygkglinveaaaq
>d1a10i_ 4.33.1.1.2 Chymotrypsin inhibitor CI-2 {Barley (Hordeum vulgare)}
ktewpelvgksveeakkvilqdkpeaqiivlpvgtivtpeyridrvrlfvdkldniaevp
rvg
>d1a12a_ 2.60.4.1.1 Regulator of chromosome condensation RCC1 {Human (Homo sapiens)}
kkvkvshrshstepglvltlgqgdvgqlglgenvmerkkpalvsipedvvqaeaggmhtv
clsksgqvysfgcndegalgrdtsvegsemvpgkvelqekvvqvsagdshtaaltddgrv
flwgsfrdnngvigllepmkksmvpvqvqldvpvvkvasgndhlvmltadgdlytlgcge
qgqlgrvpelfanrggrqglerllvpkcvmlksrgsrghvrfqdafcgayftfaishegh
vygfglsnyhqlgtpgtescfipqnltsfknstkswvgfsggqhhtvcmdsegkayslgr
aeygrlglgegaeeksiptlisrlpavssvacgasvgyavtkdgrvfawgmgtnyqlgtg
qdedawspvemmgkqlenrvvlsvssggqhtvllvkdkeqs
>d1a12b_ 2.60.4.1.1 Regulator of chromosome condensation RCC1 {Human (Homo sapiens)}
kkvkvshrshstepglvltlgqgdvgqlglgenvmerkkpalvsipedvvqaeaggmhtv
clsksgqvysfgcndegalgrdtsvegsemvpgkvelqekvvqvsagdshtaaltddgrv
flwgsfrdnngvigllepmkksmvpvqvqldvpvvkvasgndhlvmltadgdlytlgcge
qgqlgrvpelfanrggrqglerllvpkcvmlksrgsrghvrfqdafcgayftfaishegh
vygfglsnyhqlgtpgtescfipqnltsfknstkswvgfsggqhhtvcmdsegkayslgr
aeygrlglgegaeeksiptlisrlpavssvacgasvgyavtkdgrvfawgmgtnyqlgtg
qdedawspvemmgkqlenrvvlsvssggqhtvllvkdkeqs
>d1a12c_ 2.60.4.1.1 Regulator of chromosome condensation RCC1 {Human (Homo sapiens)}
kkvkvshrshstepglvltlgqgdvgqlglgenvmerkkpalvsipedvvqaeaggmhtv
clsksgqvysfgcndegalgrdtsvegsemvpgkvelqekvvqvsagdshtaaltddgrv
flwgsfrdnngvigllepmkksmvpvqvqldvpvvkvasgndhlvmltadgdlytlgcge
qgqlgrvpelfanrggrqglerllvpkcvmlksrgsrghvrfqdafcgayftfaishegh
vygfglsnyhqlgtpgtescfipqnltsfknstkswvgfsggqhhtvcmdsegkayslgr
aeygrlglgegaeeksiptlisrlpavssvacgasvgyavtkdgrvfawgmgtnyqlgtg
qdedawspvemmgkqlenrvvlsvssggqhtvllvkdkeqs
>d1a14h_ 2.1.1.1.62 Immunoglobulin (variable domains of L and H chains) {Fab NC10 (mouse), kappa L chain}
qvqlqqsgaelvkpgasvrmsckasgytftnynmywvkqspgqglewigifypgngdtsy
nqkfkdkatltadkssntaymqlssltsedsavyycarsggsyrydggfdywgqgttvtv
>d1a14l_ 2.1.1.1.62 Immunoglobulin (variable domains of L and H chains) {Fab NC10 (mouse), kappa L chain}
dieltqttsslsaslgdrvtiscrasqdisnylnwyqqnpdgtvklliyytsnlhsevps
rfsgsgsgtdysltisnleqediatyfcqqdftlpftfgggtaa
>d1a14n_ 2.59.1.1.2 Influenza neuraminidase {Influenza virus A, different strains}
rdfnnltkglctinswhiygkdnavrigedsdvlvtrepyvscdpdecrfyalsqgttir
gkhsngtihdrsqyraliswplsspptvynsrvecigwsstschdgktrmsicisgpnnn
asaviwynrrpvteintwarnilrtqesecvchngvcpvvftdgsatgpaetriyyfkeg
kilkweplagtakhieecscygeraeitctcrdnwqgsnrpviridpvamthtsqyicsp
vltdnprpndptvgkcndpypgnnnngvkgfsyldgvntwlgrtisiasrsgyemlkvpn
altddkskptqgqtivlntdwsgysgsfmdywaegecyracfyvelirgrpkedkvwwts
nsivsmcssteflgqwdwpdgakieyfl
>d1a15a_ 4.8.1.1.15 Stromal cell-derived factor-1 (SDF-1) {Human (Homo sapiens)}
kpvslsyrcpcrffeshvaranvkhlkilntpacalqivarlknnnrqvcidpklkwiqe
ylekaln
>d1a15b_ 4.8.1.1.15 Stromal cell-derived factor-1 (SDF-1) {Human (Homo sapiens)}
rcpcrffeshvaranvkhlkilntpacalqivarlknnnrqvcidpklkwiqeylek
>d1a16__ 4.101.1.1.5 Aminopeptidase P {Escherichia coli}
seisrqefqrrrqalveqmqpgsaalifaapevtrsadseypyrqnsdfwyftgfnepea
vlvliksddthnhsvlfnrvrdltaeiwfgrrlgqdaapeklgvdralafseinqqlyql
lngldvvyhaqgeyayadvivnsaleklrkgsrqnltapatmidwrpvvhemrlfkspee
iavlrrageitamahtramekcrpgmfeyhlegeihhefnrhgarypsyntivgsgengc
ilhytenecemrdgdlvlidagceykgyagditrtfpvngkftqaqreiydivleslets
lrlyrpgtsilevtgevvrimvsglvklgilkgdvdeliaqnahrpffmhglshwlgldv
hdvgvygqdrsrilepgmvltvepglyiapdaevpeqyrgigirieddivitetgnenlt
asvvkkpeeiealmvaarkq
>d1a17__ 1.110.8.1.1 Protein phosphatase 5 {Human (Homo sapiens)}
ppadgalkraeelktqandyfkakdyenaikfysqaielnpsnaiyygnrslaylrtecy
gyalgdatraieldkkyikgyyrraasnmalgkfraalrdyetvvkvkphdkdakmkyqe
cnkivkqkaferaiagdehkrsvvdsldiesmtiedeys
>d1a18__ 2.53.1.2.6 Adipocyte lipid-binding protein, ALBP {Mouse (Mus musculus)}
cdafvgtwklvssenfddymkevgvgfatrkvagmakpnmiisvngdlvtirsestfknt
eisfklgvefdeitaddrkvksiitldggalvqvqkwdgksttikrkrdgdklvvexvmk
gvtstrvyera
>d1a19a_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdcltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegaditiils
>d1a19b_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdcltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegaditiils
>d1a1aa_ 4.72.1.1.3 c-src tyrosine kinase {Human (Homo sapiens)}
dsiqaeewyfgkitrreserlllnaenprgtflvresettkgayslsvsdfdnakglnvk
hykirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a1ab_ 4.72.1.1.3 c-src tyrosine kinase {Human (Homo sapiens)}
aeewyfgkitrreserlllnaenprgtflvresettkgayslsvsdfdnakglnvkhyki
rkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a1ba_ 4.72.1.1.3 c-src tyrosine kinase {Human (Homo sapiens)}
siqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkh
ykirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a1bb_ 4.72.1.1.3 c-src tyrosine kinase {Human (Homo sapiens)}
iqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkhy
kirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a1ca_ 4.72.1.1.3 c-src tyrosine kinase {Human (Homo sapiens)}
siqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkh
ykirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a1cb_ 4.72.1.1.3 c-src tyrosine kinase {Human (Homo sapiens)}
iqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkhy
kirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a1d__ 2.35.4.9.1 RNA polymerase subunit RBP8 {Baker's yeast (Saccharomyces cerevisiae)}
msntlfddifqvsevdpgrynkvcrieaasttqdqckltldinvelfpvaaqdsltvtia
sslnledtpandssatrswrppqagdrsladdydyvmygtaykfeevskdliavyysfgg
llmrlegnyrnlnnlkqenayllirr
>d1a1ea_ 4.72.1.1.3 c-src tyrosine kinase {Human (Homo sapiens)}
iqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkhy
kirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a1eb_ 4.72.1.1.3 c-src tyrosine kinase {Human (Homo sapiens)}
iqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkhy
kirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a1fa1 7.31.1.1.1 (103-131) ZIF268 {Mouse (Mus musculus)}
rpyacpvescdrrfsdssnltrhirihtg
>d1a1fa2 7.31.1.1.1 (132-159) ZIF268 {Mouse (Mus musculus)}
qkpfqcricmrnfsrsdhltthirthtg
>d1a1fa3 7.31.1.1.1 (160-186) ZIF268 {Mouse (Mus musculus)}
ekpfacdicgrkfarsderkrhtkihl
>d1a1ga1 7.31.1.1.1 (103-131) ZIF268 {Mouse (Mus musculus)}
rpyacpvescdrrfsdssnltrhirihtg
>d1a1ga2 7.31.1.1.1 (132-159) ZIF268 {Mouse (Mus musculus)}
qkpfqcricmrnfsrsdhltthirthtg
>d1a1ga3 7.31.1.1.1 (160-186) ZIF268 {Mouse (Mus musculus)}
ekpfacdicgrkfarsderkrhtkihl
>d1a1ha1 7.31.1.1.1 (103-131) ZIF268 {Mouse (Mus musculus)}
rpyacpvescdrrfsqsgsltrhirihtg
>d1a1ha2 7.31.1.1.1 (132-159) ZIF268 {Mouse (Mus musculus)}
qkpfqcricmrnfsrsdhltthirthtg
>d1a1ha3 7.31.1.1.1 (160-187) ZIF268 {Mouse (Mus musculus)}
ekpfacdicgrkfarsderkrhtkihlr
>d1a1ia1 7.31.1.1.1 (103-131) ZIF268 {Mouse (Mus musculus)}
rpyacpvescdrrfsrsadltrhirihtg
>d1a1ia2 7.31.1.1.1 (132-159) ZIF268 {Mouse (Mus musculus)}
qkpfqcricmrnfsrsdhltthirthtg
>d1a1ia3 7.31.1.1.1 (160-187) ZIF268 {Mouse (Mus musculus)}
ekpfacdicgrkfarsderkrhtkihlr
>d1a1ja1 7.31.1.1.1 (103-131) ZIF268 {Mouse (Mus musculus)}
rpyacpvescdrrfsrsadltrhirihtg
>d1a1ja2 7.31.1.1.1 (132-159) ZIF268 {Mouse (Mus musculus)}
qkpfqcricmrnfsrsdhltthirthtg
>d1a1ja3 7.31.1.1.1 (160-186) ZIF268 {Mouse (Mus musculus)}
ekpfacdicgrkfarsderkrhtkihl
>d1a1ka1 7.31.1.1.1 (103-131) ZIF268 {Mouse (Mus musculus)}
rpyacpvescdrrfsrsadltrhirihtg
>d1a1ka2 7.31.1.1.1 (132-159) ZIF268 {Mouse (Mus musculus)}
qkpfqcricmrnfsrsdhltthirthtg
>d1a1ka3 7.31.1.1.1 (160-187) ZIF268 {Mouse (Mus musculus)}
ekpfacdicgrkfarsderkrhtkihlr
>d1a1la1 7.31.1.1.1 (103-131) ZIF268 {Mouse (Mus musculus)}
rpyacpvescdrrfsrsdeltrhirihtg
>d1a1la2 7.31.1.1.1 (132-159) ZIF268 {Mouse (Mus musculus)}
qkpfqcricmrnfsrsdhltthirthtg
>d1a1la3 7.31.1.1.1 (160-187) ZIF268 {Mouse (Mus musculus)}
ekpfacdicgrkfarsderkrhtkihlr
>d1a1ma1 2.1.1.2.9 (182-278) Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-B53}
adppkthvthhpvsdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrwephh
>d1a1ma2 4.17.1.1.16 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-B53}
gshsmryfytamsrpgrgeprfiavgyvddtqfvrfdsdaasprteprppwieqegpeyw
drntqifktntqtyrenlrialryynqseagshiiqrmygcdlgpdgrllrghdqsaydg
kdyialnedlsswtaadtaaqitqrkweaarvaeqlrayleglcvewlrrylengketlq
r
>d1a1mb1 2.1.1.2.9 Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-B53}
iqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskdw
sfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1a1na1 2.1.1.2.10 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-B*3501}
adppkthvthhpvsdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrwep
>d1a1na2 4.17.1.1.17 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-B*3501}
gshsmryfytamsrpgrgeprfiavgyvddtqfvrfdsdaasprteprppwieqegpeyw
drntqifktntqtyreslrnlrgyynqseagshiiqrmygcdlgpdgrllrghdqsaydg
kdyialnedlsswtaadtaaqitqrkweaarvaeqlrayleglcvewlrrylengketlq
r
>d1a1nb1 2.1.1.2.10 Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-B*3501}
iqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskdw
sfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1a1oa1 2.1.1.2.9 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-B53}
adppkthvthhpvsdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrwep
>d1a1oa2 4.17.1.1.16 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-B53}
gshsmryfytamsrpgrgeprfiavgyvddtqfvrfdsdaasprteprppwieqegpeyw
drntqifktntqtyrenlrialryynqseagshiiqrmygcdlgpdgrllrghdqsaydg
kdyialnedlsswtaadtaaqitqrkweaarvaeqlrayleglcvewlrrylengketlq
r
>d1a1ob1 2.1.1.2.9 Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-B53}
iqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskdw
sfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1a1qa_ 2.41.1.3.3 NS3 protease {Human hepatitis C virus, Bk strain}
pitaysqqtrgllgciitsltgrdknqvegevqvvstatqsflatcvngvcwtvyhgags
ktlagpkgpitqmytnvdqdlvgwqappgarsltpctcgssdlylvtrhadvipvrrrgd
srgsllsprpvsylkgssggpllcpsghavgifraavctrgvakavdfvpvesmettmrs
pvf
>d1a1qb_ 2.41.1.3.3 NS3 protease {Human hepatitis C virus, Bk strain}
pitaysqqtrgllgciitsltgrdknqvegevqvvstatqsflatcvngvcwtvyhgags
ktlagpkgpitqmytnvdqdlvgwqappgarsltpctcgssdlylvtrhadvipvrrrgd
srgsllsprpvsylkgssggpllcpsghavgifraavctrgvakavdfvpvesmettm
>d1a1qc_ 2.41.1.3.3 NS3 protease {Human hepatitis C virus, Bk strain}
pitaysqqtrgllgciitsltgrdknqvegevqvvstatqsflatcvngvcwtvyhgags
ktlagpkgpitqmytnvdqdlvgwqappgarsltpctcgssdlylvtrhadvipvrrrgd
srgsllsprpvsylkgssggpllcpsghavgifraavctrgvakavdfvpvesmettm
>e1a1r.1a 2.41.1.3.3 NS3 protease {Human hepatitis C virus, Bk strain}
vegevqivstatqtflatcingvcwtvyhgagtrtiaspkgpviqmytnvdqdlvgwpap
qgsrsltpctcgssdlylvtrhadvipvrrrgdsrgsllsprpisylkgssggpllcptg
havglfraavctrgvakavdfipvenlettmr
>e1a1r.2b 2.41.1.3.3 NS3 protease {Human hepatitis C virus, Bk strain}
pitayaqqtrgllgciitsltgrdknqvegevqivstatqtflatcingvcwtvyhgagt
rtiaspkgpviqmytnvdqdlvgwpapqgsrsltpctcgssdlylvtrhadvipvrrrgd
srgsllsprpisylkgssggpllcptghavglfraavctrgvakavdfipvenlettmr
>e1a1r.2d 2.41.1.3.3 NS3 protease {Human hepatitis C virus, Bk strain}
kgsvvivgrivlsgkpaiipk
>d1a1s_1 3.66.1.1.5 (1-150) Ornithine transcarbamoylase {Pyrococcus furiosus}
vvslagrdllclqdytaeeiwtiletakmfkiwqkigkphrllegktlamifqkpstrtr
vsfevamahlgghalylnaqdlqlrrgetiadtarvlsryvdaimarvydhkdvedlaky
atvpvinglsdfshpcqaladymtiwekkg
>d1a1s_2 3.66.1.1.5 (151-313) Ornithine transcarbamoylase {Pyrococcus furiosus}
tikgvkvvyvgdgnnvahslmiagtklgadvvvatpegyepdekvikwaeqnaaesggsf
ellhdpvkavkdadviytdvwasmgqeaeaeerrkifrpfqvnkdlvkhakpdymfmhcl
pahrgeevtddvidspnsvvwdqaenrlhaqkavlalvmggik
>d1a1ta_ 7.34.1.1.2 HIV nucleocapsid {Human immunodeficiency virus, type 1, Mn isolate}
mqkgnfrnqrktvkcfncgkeghiakncraprkkgcwkcgkeghqmkdcterqan
>d1a1ua_ 1.55.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
eyftlqirgrerfekireynealelkdaq
>d1a1uc_ 1.55.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
eyftlqirgrerfekireynealelkdaq
>d1a1va1 3.30.1.11.1 (190-325) HCV helicase domain {Hepatitis C virus, HCV}
ppavpqsfqvahlhaptgsgkstkvpaayaaqgykvlvlnpsvaatlgfgaymskahgvd
pnirtgvrtittgspitystygkfladggxsggaydiiicdechstdatsilgigtvldq
aetagarlvvlatatp
>d1a1va2 3.30.1.11.1 (326-624) HCV helicase domain {Hepatitis C virus, HCV}
pgsvtvphpnieevalsttgeipfygkaiplevikggrhlifchskkkcdelaaklvalg
inavayyrgldvsviptsgdvvvvatdalmtgftgdfdsvidcntxvtqtvdfsldptft
ietttlpqdavsrtqrrgrtgrgkpgiyrfvapgerpsgmfdssvlcecydagxawyelt
paettvrlraymntpglpvcqdhlefwegvftglthidahflsqtkqsgenfpylvayqa
tvcaraqapppswdqmwkclirlkptlhgptpllyrlgavqnevtlthpitkyimtcms
>d1a1w__ 1.76.1.1.3 FADD (Mort1) {Human (Homo sapiens)}
mdpflvllhsvssslssseltelkylclgrvgkrklervqsgldlfsmlleqndlepght
ellrellaslrrhdllrrvddfe
>d1a1x__ 2.56.1.1.2 MTCP-1 {Human (Homo sapiens)}
agedvgappdhlwvhqegiyrdeyqrtwvavveeetsflrarvqqiqvplgdaarpshll
tsqlplmwqlypeerymdnnsrlwqiqhhlmvrgvqelllkllpdd
>d1a1ye_ 3.33.1.1.3 Subtilisin Carlsberg {Bacillus licheniformis, alcalase}
aqtvpygiplikadkvqaqgfkganvkvavldtgiqashpdlnvvggasfvageayntdg
nghgthvagtvaaldnttgvlgvapsvslyavkvlnssgsgsysgivsgiewattngmdv
inmslggasgstamkqavdnayargvvvvaaagnsgssgntntigypakydsviavgavd
snsnrasfssvgaelevmapgagvystyptntyatlngtsmasphvagaaalilskhpnl
sasqvrnrlsstatylgssfyygkglinveaaaq
>d1a1yi_ 4.33.1.1.2 Chymotrypsin inhibitor CI-2 {Barley (Hordeum vulgare)}
ktewpelvgksveeakkvilqdkpeaqiivlpvgtivtmeyridrvrlfvdkldniaevp
rvg
>d1a1z__ 1.76.1.1.3 FADD (Mort1) {Human (Homo sapiens)}
mdpflvllhsvssslssseltelkglclgrvgkrklervqsgldlfsmlleqndlepght
ellrellaslrrhdllrrvddfe
>d1a21a1 2.1.2.1.2 (4-106) Extracellular region of human tissue factor {Rabbit (Oryctolagus cuniculus)}
tgraynltwkstnfktilewepksidhvytvqistrlenwkskcfltaetecdltdevvk
dvgqtymarvlsyparngnttgfpeeppfrnspeftpyldtnl
>d1a21a2 2.1.2.1.2 (107-208) Extracellular region of human tissue factor {Rabbit (Oryctolagus cuniculus)}
gqptiqsfeqvgtklnvtvqdartlvrrngtflslravfgkdlnytlyywrasstgkkta
ttntneflidvdkgenycfsvqavipsrkrkqrspesltect
>d1a21b1 2.1.2.1.2 (4-106) Extracellular region of human tissue factor {Rabbit (Oryctolagus cuniculus)}
tgraynltwkstnfktilewepksidhvytvqistrlenwkskcfltaetecdltdevvk
dvgqtymarvlsyparngnttgfpeeppfrnspeftpyldtnl
>d1a21b2 2.1.2.1.2 (107-208) Extracellular region of human tissue factor {Rabbit (Oryctolagus cuniculus)}
gqptiqsfeqvgtklnvtvqdartlvrrngtflslravfgkdlnytlyywrasstgkkta
ttntneflidvdkgenycfsvqavipsrkrkqrspesltect
>d1a22a_ 1.27.1.1.6 Growth hormone, somatotropin {Human (Homo sapiens)}
fptiplsrlfdnamlrahrlhqlafdtyqefeeayipkeqkysflqnpqtslcfsesipt
psnreetqqksnlellrisllliqswlepvqflrsvfanslvygasdsnvydllkdleer
iqtlmgrlegqifkqtyskfdtdallknygllycfrkdmdkvetflrivqcrsvegscgf
>d1a22b1 2.1.2.1.8 (233-328) Growth hormone receptor {Human (Homo sapiens)}
pkftkcrsperetfschwtdevhhgtknlgpiqlfytrrntqewtqewkecpdyvsagen
scyfnssftsiwipycikltsnggtvdekcfsvdei
>d1a22b2 2.1.2.1.8 (329-437) Growth hormone receptor {Human (Homo sapiens)}
vqpdppialnwtllnvsltgihadiqvrweaprnadiqkgwmvleyelqykevnetkwkm
mdpilttsvpvyslkvdkeyevrvrskqrnsgnygefsevlyvtlpqms
>d1a23_1 1.47.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1a23_2 3.38.1.4.1 (1-64,129-189) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
aqyedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsekk
>d1a24_1 1.47.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1a24_2 3.38.1.4.1 (1-64,129-189) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
aqyedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsekk
>d1a25a_ 2.6.1.2.2 C2 domain from protein kinase c (beta) {Rat (Rattus norvegicus)}
errgriyiqahidrevlivvvrdaknlvpmdpnglsdpyvklklipdpkseskqktktik
cslnpewnetfrfqlkesdkdrrlsveiwdwdltsrndfmgslsfgiselqkagvdgwfk
llsqeegeyfnv
>d1a25b_ 2.6.1.2.2 C2 domain from protein kinase c (beta) {Rat (Rattus norvegicus)}
errgriyiqahidrevlivvvrdaknlvpmdpnglsdpyvklklipdpkseskqktktik
cslnpewnetfrfqlkesdkdrrlsveiwdwdltsrndfmgslsfgiselqkagvdgwfk
llsqeegeyfnv
>d1a26_1 1.44.1.1.1 (662-796) Domain of poly(ADP-ribose) polymerase {Chicken (Gallus gallus)}
ksklakpiqdlikmifdvesmkkamvefeidlqkmplgklskrqiqsaysilnevqqavs
dggsesqildlsnrfytliphdfgmkkppllsnleyiqakvqmldnlldievaysllrgg
nedgdkdpidinyek
>d1a26_2 4.136.1.2.1 (797-1012) Poly(ADP-ribose) polymerase, C-terminal domain {Chicken (Gallus gallus)}
lrtdikvvdkdseeakiikqyvknthaathnaydlkvveifrieregesqrykpfkqlhn
rqllwhgsrttnfagilsqglriappeapvtgymfgkgiyfadmvsksanychtsqadpi
glillgevalgnmyelknashitklpkgkhsvkglgktapdptatttldgvevplgngis
tgindtcllyneyivydvaqvnlkyllklkfnykts
>d1a27__ 3.2.1.2.8 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylahskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevfg
>d1a28a_ 1.114.1.1.3 Progesterone receptor {Human (Homo sapiens)}
qlipplinllmsiepdviyaghdntkpdtssslltslnqlgerqllsvvkwskslpgfrn
lhiddqitliqyswmslmvfglgwrsykhvsgqmlyfapdlilneqrmkessfyslcltm
wqipqefvklqvsqeeflcmkvllllntipleglrsqtqfeemrssyirelikaiglrqk
gvvsssqrfyqltklldnlhdlvkqlhlyclntfiqsralsvefpemmseviaaqlpkil
agmvkpllfhk
>d1a28b_ 1.114.1.1.3 Progesterone receptor {Human (Homo sapiens)}
lipplinllmsiepdviyaghdntkpdtssslltslnqlgerqllsvvkwskslpgfrnl
hiddqitliqyswmslmvfglgwrsykhvsgqmlyfapdlilneqrmkessfyslcltmw
qipqefvklqvsqeeflcmkvllllntipleglrsqtqfeemrssyirelikaiglrqkg
vvsssqrfyqltklldnlhdlvkqlhlyclntfiqsralsvefpemmseviaaqlpkila
gmvkpllfh
>d1a29__ 1.42.1.5.8 Calmodulin {Bovine (Bos taurus)}
qlteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngt
idfpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevd
emireadidgdgqvnyeefvqmmt
>d1a2aa_ 1.123.1.2.4 Snake phospholipase A2 {Chinese water moccasin (Agkistrodon halys pallas), different isoforms}
nllqfnkmikeetgknaipfyafygcycggggngkpkdgtdrccfvhdccygrlvncntk
sdiysyslkegyitcgkgtnceeqicecdrvaaecfrrnldtynngymfyrdskctetse
ec
>d1a2ab_ 1.123.1.2.4 Snake phospholipase A2 {Chinese water moccasin (Agkistrodon halys pallas), different isoforms}
nllqfnkmikeetgknaipfyafygcycggggngkpkdgtdrccfvhdccygrlvncntk
sdiysyslkegyitcgkgtnceeqicecdrvaaecfrrnldtynngymfyrdskctetse
ec
>d1a2ac_ 1.123.1.2.4 Snake phospholipase A2 {Chinese water moccasin (Agkistrodon halys pallas), different isoforms}
nllqfnkmikeetgknaipfyafygcycggggngkpkdgtdrccfvhdccygrlvncntk
sdiysyslkegyitcgkgtnceeqicecdrvaaecfrrnldtynngymfyrdskctetse
ec
>d1a2ad_ 1.123.1.2.4 Snake phospholipase A2 {Chinese water moccasin (Agkistrodon halys pallas), different isoforms}
nllqfnkmikeetgknaipfyafygcycggggngkpkdgtdrccfvhdccygrlvncntk
sdiysyslkegyitcgkgtnceeqicecdrvaaecfrrnldtynngymfyrdskctetse
ec
>d1a2ae_ 1.123.1.2.4 Snake phospholipase A2 {Chinese water moccasin (Agkistrodon halys pallas), different isoforms}
nllqfnkmikeetgknaipfyafygcycggggngkpkdgtdrccfvhdccygrlvncntk
sdiysyslkegyitcgkgtnceeqicecdrvaaecfrrnldtynngymfyrdskctetse
ec
>d1a2af_ 1.123.1.2.4 Snake phospholipase A2 {Chinese water moccasin (Agkistrodon halys pallas), different isoforms}
nllqfnkmikeetgknaipfyafygcycggggngkpkdgtdrccfvhdccygrlvncntk
sdiysyslkegyitcgkgtnceeqicecdrvaaecfrrnldtynngymfyrdskctetse
ec
>d1a2ag_ 1.123.1.2.4 Snake phospholipase A2 {Chinese water moccasin (Agkistrodon halys pallas), different isoforms}
nllqfnkmikeetgknaipfyafygcycggggngkpkdgtdrccfvhdccygrlvncntk
sdiysyslkegyitcgkgtnceeqicecdrvaaecfrrnldtynngymfyrdskctetse
ec
>d1a2ah_ 1.123.1.2.4 Snake phospholipase A2 {Chinese water moccasin (Agkistrodon halys pallas), different isoforms}
nllqfnkmikeetgknaipfyafygcycggggngkpkdgtdrccfvhdccygrlvncntk
sdiysyslkegyitcgkgtnceeqicecdrvaaecfrrnldtynngymfyrdskctetse
ec
>d1a2b__ 3.30.1.6.8 RhoA {Human (Homo sapiens)}
irkklvivgdvacgktcllivfskdqfpevyvptvfenyvadievdgkqvelalwdtagq
edydrlrplsypdtdvilmcfsidspdslenipekwtpevkhfcpnvpiilvgnkkdlrn
dehtrrelakmkqepvkpeegrdmanrigafgymecsaktkdgvrevfematraalqa
>e1a2c.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>e1a2c.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>d1a2da_ 2.53.1.2.6 Adipocyte lipid-binding protein, ALBP {Mouse (Mus musculus)}
cdafvgtwklvssenfddymkevgvgfatrkvagmakpnmiisvngdlvtirsestfknt
eisfklgvefdeitaddrkvksiitldggalvqvqkwdgksttikrkrdgdklvvexvmk
gvtstrvyera
>d1a2db_ 2.53.1.2.6 Adipocyte lipid-binding protein, ALBP {Mouse (Mus musculus)}
cdafvgtwklvssenfddymkevgvgfatrkvagmakpnmiisvngdlvtirsestfknt
eisfklgvefdeitaddrkvksiitldggalvqvqkwdgksttikrkrdgdklvvexvmk
gvtstrvyera
>d1a2f__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalkgahalgkthlk
nsgyegpwgaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1a2g__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpwgaannvftnefylnllnedwklekndanneqwdsksgymhlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1a2i__ 1.126.1.1.2 Cytochrome c3 {Desulfovibrio vulgaris}
apkapadglkmeatkqpvvfnhsthksvkcgdchhpvngkedyrkcgtagchdsmdkkdk
sakgyyhvmhdkntkfkscvgchvevagadaakkkdltgckkskche
>d1a2j_1 1.47.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1a2j_2 3.38.1.4.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
aqyedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsek
>d1a2ka_ 4.15.3.2.1 Nuclear transport factor-2 (NTF2) {Rat (Rattus norvegicus)}
kpiweqigssfiqhyyqlfdndrtqlgaiyidascltwegqqfqgkaaiveklsslpfqk
iqhsitaqdhqptpdsciismvvgqlkadedpimgfhqmfllknindawvctndmfrlal
hnfg
>d1a2kb_ 4.15.3.2.1 Nuclear transport factor-2 (NTF2) {Rat (Rattus norvegicus)}
kpiweqigssfiqhyyqlfdndrtqlgaiyidascltwegqqfqgkaaiveklsslpfqk
iqhsitaqdhqptpdsciismvvgqlkadedpimgfhqmfllknindawvctndmfrlal
hnfg
>d1a2kc_ 3.30.1.6.6 Ran {Dog (Canis familiaris)}
qvqfklvlvgdggtgkttfvkrhltgefekkyvatlgvevhplvfhtnrgpikfnvwdta
gqekfgglrdgyyiqaqcaiimfdvtsrvtyknvpnwhrdlvrvcenipivlcgnkvdik
drkvkaksivfhrkknlqyydisaksnynfekpflwlarkligdpnlefvampalappev
vmdpalaaqyehdlev
>d1a2kd_ 3.30.1.6.6 Ran {Dog (Canis familiaris)}
qvqfklvlvgdggtgkttfvkrhltgefekkyvatlgvevhplvfhtnrgpikfnvwdta
gqekfgglrdgyyiqaqcaiimfdvtsrvtyknvpnwhrdlvrvcenipivlcgnkvdik
drkvkaksivfhrkknlqyydisaksnynfekpflwlarkligdpnlefvampalappev
vmdpalaaqyehdlevaqt
>d1a2ke_ 3.30.1.6.6 Ran {Dog (Canis familiaris)}
qvqfklvlvgdggtgkttfvkrhltgefekkyvatlgvevhplvfhtnrgpikfnvwdta
gqekfgglrdgyyiqaqcaiimfdvtsrvtyknvpnwhrdlvrvcenipivlcgnkvdik
drkvkaksivfhrkknlqyydisaksnynfekpflwlarkligdpnlefvampalappev
vmdpalaaqyehdlevaqttalpde
>d1a2la1 1.47.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1a2la2 3.38.1.4.1 (3-64,129-188) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
yedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyhvn
fmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvkyl
sek
>d1a2lb1 1.47.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1a2lb2 3.38.1.4.1 (3-64,129-188) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
yedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyhvn
fmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvkyl
sek
>d1a2ma1 1.47.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1a2ma2 3.38.1.4.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
aqyedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsek
>d1a2mb1 1.47.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1a2mb2 3.38.1.4.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
aqyedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsek
>d1a2n__ 4.52.2.1.1 UDP-N-acetylglucosamine enolpyruvyl transferase (EPT, MurA, MurZ) {Escherichia coli}
mdkfrvqgptklqgevtisgaknaalpilfaallaeepveiqnvpklkdvdtsmkllsql
gakverngsvhidardvnvfcapydlvktmrasiwalgplvarfgqgqvslpggatigar
pvdlhisgleqlgatikleegyvkasvdgrlkgahivmdkvsvgatvtimcaatlaegtt
iienaarepeivdtanflitlgakisgqgtdriviegverlgggvyrvlpdrietgtflv
aaaisrgkiicrnaqpdtldavlaklrdagadievgedwisldmhgkrpkavnvrtaphp
afptdmqaqftllnlvaegtgfitetvfenrfmhvpelsrmgahaeiesntvichgvekl
sgaqvmatdlrasaslvlagciaegttvvdriyhidrgyeriedklralganiervkg
>d1a2oa1 3.16.2.1.7 (1-140) Methylesterase CheB, N-terminal domain {Salmonella typhimurium}
mskirvlsvddsalmrqimteiinshsdmemvatapdplvardlikkfnpdvltldvemp
rmdgldfleklmrlrpmpvvmvssltgkgsevtlralelgaidfvtkpqlgiregmlays
emiaekvrtaarariaahkp
>d1a2oa2 3.32.1.1.1 (141-347) Methylesterase CheB, C-terminal domain {Salmonella typhimurium}
maapttlkagpllssekliaigastggteairhvlqplplsspaviitqhmppgftrsfa
erlnklcqisvkeaedgervlpghayiapgdkhmelarsganyqikihdgppvnrhrpsv
dvlfhsvakhagrnavgviltgmgndgaagmlamyqagawtiaqneascvvfgmpreain
mggvsevvdlsqvsqqmlakisagqai
>d1a2ob1 3.16.2.1.7 (1-140) Methylesterase CheB, N-terminal domain {Salmonella typhimurium}
mskirvlsvddsalmrqimteiinshsdmemvatapdplvardlikkfnpdvltldvemp
rmdgldfleklmrlrpmpvvmvssltgkgsevtlralelgaidfvtkpqlgiregmlays
emiaekvrtaarariaahkp
>d1a2ob2 3.32.1.1.1 (141-347) Methylesterase CheB, C-terminal domain {Salmonella typhimurium}
maapttlkagpllssekliaigastggteairhvlqplplsspaviitqhmppgftrsfa
erlnklcqisvkeaedgervlpghayiapgdkhmelarsganyqikihdgppvnrhrpsv
dvlfhsvakhagrnavgviltgmgndgaagmlamyqagawtiaqneascvvfgmpreain
mggvsevvdlsqvsqqmlakisagqai
>d1a2pa_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1a2pb_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1a2pc_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1a2q__ 3.33.1.1.7 Subtilisin Novo/BPN' {Bacillus amyloliquefaciens}
aqsvpygvsqikapalhsqgycgsnvkvavidsgidsshpdlkvaggasmvpsetnpfqd
nnshgthvagtvaalnnsigvlgvapcaslyavkvlgadgsgqyswiingiewaiannmd
vinmslggpsgsaalkaavdkavasgvvvvaaagnegtsgssstvgypakypsviavgav
dssnqrasfssvgpeldvmapgvsiqstlpgnkygaysgtxmasphvagaaalilskhpn
wtntqvrsslentttklgdsfyygkglinvqaaaq
>d1a2s__ 1.3.1.1.1 Cytochrome c6 (synonym: cytochrome c553) {Monoraphidium braunii}
eadlalgkavfdgncaachagggnnvipdhtlqkaaieqfldggfnieaivyqiengkga
mpawdgrldedeiagvaayvydqaagnkw
>d1a2t__ 2.35.1.1.1 Staphylococcal nuclease {Staphylococcus aureus}
lhkepatlikaidgdtxklmykgqpmtfrlllvdtpetkhpkkgvekygpeasaftkkmv
enakkievefdkgqrtdkygrglayiyadgkmvnealvrqglakvayvykpnntheqhlr
kseaqakkeklniws
>d1a2u__ 2.35.1.1.1 Staphylococcal nuclease {Staphylococcus aureus}
lhkepatlikaidgdtxklmykgqpmtfrlllvdtpetkhpkkgvekygpeasaftkkmv
enakkievefdkgqrtdkygrglayiyadgkmvnealvrqglakvayvykpnntheqhlr
kseaqakkeklniws
>d1a2va1 2.27.2.1.4 (237-672) Copper amine oxidase, domain 3 (catalytic) {Yeast (Hansenula polymorpha)}
peappinvtqpegvsfkmtgnvmewsnfkfhigfnyregivlsdvsyndhgnvrpifhri
slsemivpygspefphqrkhaldigeygagymtnplslgcdckgvihyldahfsdragdp
itvknavciheeddgllfkhsdfrdnfatslvtratklvvsqiftaanxeyclywvfmqd
gairldirltgilntyilgddeeagpwgtrvypnvnahnhqhlfslridpridgdgnsaa
acdaksspyplgspenmygnafysekttfktvkdsltnyesatgrswdifnpnkvnpysg
kppsyklvstqcppllakegslvakrapwashsvnvvpykdnrlypsgdhvpqwsgdgvr
gmrewigdgsenidntdilffhtfgithfpapedfplmpaepitlmlrprhfftenpgld
iqpsyamttseakrav
>d1a2va2 4.15.2.1.4 (18-115) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
parpahpldplstaeikaatntvksyfagkkisfntvtlreparkayiqwkeqggplppr
layyvileagkpgvkeglvdlaslsvietraletvqpi
>d1a2va3 4.15.2.1.4 (116-236) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
ltvedlcsteevirndpavieqcvlsgipanemhkvycdpwtigyderwgtgkrlqqalv
yyrsdeddsqyshpldfcpivdteekkvifidipnrrrkvskhkhanfypkhmiekvgam
r
>d1a2vb1 2.27.2.1.4 (237-672) Copper amine oxidase, domain 3 (catalytic) {Yeast (Hansenula polymorpha)}
peappinvtqpegvsfkmtgnvmewsnfkfhigfnyregivlsdvsyndhgnvrpifhri
slsemivpygspefphqrkhaldigeygagymtnplslgcdckgvihyldahfsdragdp
itvknavciheeddgllfkhsdfrdnfatslvtratklvvsqiftaanxeyclywvfmqd
gairldirltgilntyilgddeeagpwgtrvypnvnahnhqhlfslridpridgdgnsaa
acdaksspyplgspenmygnafysekttfktvkdsltnyesatgrswdifnpnkvnpysg
kppsyklvstqcppllakegslvakrapwashsvnvvpykdnrlypsgdhvpqwsgdgvr
gmrewigdgsenidntdilffhtfgithfpapedfplmpaepitlmlrprhfftenpgld
iqpsyamttseakrav
>d1a2vb2 4.15.2.1.4 (18-115) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
parpahpldplstaeikaatntvksyfagkkisfntvtlreparkayiqwkeqggplppr
layyvileagkpgvkeglvdlaslsvietraletvqpi
>d1a2vb3 4.15.2.1.4 (116-236) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
ltvedlcsteevirndpavieqcvlsgipanemhkvycdpwtigyderwgtgkrlqqalv
yyrsdeddsqyshpldfcpivdteekkvifidipnrrrkvskhkhanfypkhmiekvgam
r
>d1a2vc1 2.27.2.1.4 (237-672) Copper amine oxidase, domain 3 (catalytic) {Yeast (Hansenula polymorpha)}
peappinvtqpegvsfkmtgnvmewsnfkfhigfnyregivlsdvsyndhgnvrpifhri
slsemivpygspefphqrkhaldigeygagymtnplslgcdckgvihyldahfsdragdp
itvknavciheeddgllfkhsdfrdnfatslvtratklvvsqiftaanxeyclywvfmqd
gairldirltgilntyilgddeeagpwgtrvypnvnahnhqhlfslridpridgdgnsaa
acdaksspyplgspenmygnafysekttfktvkdsltnyesatgrswdifnpnkvnpysg
kppsyklvstqcppllakegslvakrapwashsvnvvpykdnrlypsgdhvpqwsgdgvr
gmrewigdgsenidntdilffhtfgithfpapedfplmpaepitlmlrprhfftenpgld
iqpsyamttseakrav
>d1a2vc2 4.15.2.1.4 (18-115) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
parpahpldplstaeikaatntvksyfagkkisfntvtlreparkayiqwkeqggplppr
layyvileagkpgvkeglvdlaslsvietraletvqpi
>d1a2vc3 4.15.2.1.4 (116-236) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
ltvedlcsteevirndpavieqcvlsgipanemhkvycdpwtigyderwgtgkrlqqalv
yyrsdeddsqyshpldfcpivdteekkvifidipnrrrkvskhkhanfypkhmiekvgam
r
>d1a2vd1 2.27.2.1.4 (237-672) Copper amine oxidase, domain 3 (catalytic) {Yeast (Hansenula polymorpha)}
peappinvtqpegvsfkmtgnvmewsnfkfhigfnyregivlsdvsyndhgnvrpifhri
slsemivpygspefphqrkhaldigeygagymtnplslgcdckgvihyldahfsdragdp
itvknavciheeddgllfkhsdfrdnfatslvtratklvvsqiftaanxeyclywvfmqd
gairldirltgilntyilgddeeagpwgtrvypnvnahnhqhlfslridpridgdgnsaa
acdaksspyplgspenmygnafysekttfktvkdsltnyesatgrswdifnpnkvnpysg
kppsyklvstqcppllakegslvakrapwashsvnvvpykdnrlypsgdhvpqwsgdgvr
gmrewigdgsenidntdilffhtfgithfpapedfplmpaepitlmlrprhfftenpgld
iqpsyamttseakrav
>d1a2vd2 4.15.2.1.4 (18-115) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
parpahpldplstaeikaatntvksyfagkkisfntvtlreparkayiqwkeqggplppr
layyvileagkpgvkeglvdlaslsvietraletvqpi
>d1a2vd3 4.15.2.1.4 (116-236) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
ltvedlcsteevirndpavieqcvlsgipanemhkvycdpwtigyderwgtgkrlqqalv
yyrsdeddsqyshpldfcpivdteekkvifidipnrrrkvskhkhanfypkhmiekvgam
r
>d1a2ve1 2.27.2.1.4 (237-672) Copper amine oxidase, domain 3 (catalytic) {Yeast (Hansenula polymorpha)}
peappinvtqpegvsfkmtgnvmewsnfkfhigfnyregivlsdvsyndhgnvrpifhri
slsemivpygspefphqrkhaldigeygagymtnplslgcdckgvihyldahfsdragdp
itvknavciheeddgllfkhsdfrdnfatslvtratklvvsqiftaanxeyclywvfmqd
gairldirltgilntyilgddeeagpwgtrvypnvnahnhqhlfslridpridgdgnsaa
acdaksspyplgspenmygnafysekttfktvkdsltnyesatgrswdifnpnkvnpysg
kppsyklvstqcppllakegslvakrapwashsvnvvpykdnrlypsgdhvpqwsgdgvr
gmrewigdgsenidntdilffhtfgithfpapedfplmpaepitlmlrprhfftenpgld
iqpsyamttseakrav
>d1a2ve2 4.15.2.1.4 (18-115) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
parpahpldplstaeikaatntvksyfagkkisfntvtlreparkayiqwkeqggplppr
layyvileagkpgvkeglvdlaslsvietraletvqpi
>d1a2ve3 4.15.2.1.4 (116-236) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
ltvedlcsteevirndpavieqcvlsgipanemhkvycdpwtigyderwgtgkrlqqalv
yyrsdeddsqyshpldfcpivdteekkvifidipnrrrkvskhkhanfypkhmiekvgam
r
>d1a2vf1 2.27.2.1.4 (237-672) Copper amine oxidase, domain 3 (catalytic) {Yeast (Hansenula polymorpha)}
peappinvtqpegvsfkmtgnvmewsnfkfhigfnyregivlsdvsyndhgnvrpifhri
slsemivpygspefphqrkhaldigeygagymtnplslgcdckgvihyldahfsdragdp
itvknavciheeddgllfkhsdfrdnfatslvtratklvvsqiftaanxeyclywvfmqd
gairldirltgilntyilgddeeagpwgtrvypnvnahnhqhlfslridpridgdgnsaa
acdaksspyplgspenmygnafysekttfktvkdsltnyesatgrswdifnpnkvnpysg
kppsyklvstqcppllakegslvakrapwashsvnvvpykdnrlypsgdhvpqwsgdgvr
gmrewigdgsenidntdilffhtfgithfpapedfplmpaepitlmlrprhfftenpgld
iqpsyamttseakrav
>d1a2vf2 4.15.2.1.4 (18-115) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
parpahpldplstaeikaatntvksyfagkkisfntvtlreparkayiqwkeqggplppr
layyvileagkpgvkeglvdlaslsvietraletvqpi
>d1a2vf3 4.15.2.1.4 (116-236) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
ltvedlcsteevirndpavieqcvlsgipanemhkvycdpwtigyderwgtgkrlqqalv
yyrsdeddsqyshpldfcpivdteekkvifidipnrrrkvskhkhanfypkhmiekvgam
r
>d1a2wa_ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1a2wb_ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1a2xa_ 1.42.1.5.3 Troponin C {Rabbit (Oryctolagus cuniculus)}
dqqaearsylseemiaefkaafdmfdadgggdisvkelgtvmrmlgqtptkeeldaiiee
vdedgsgtidfeeflvmmvrqmkedakgkseeelaecfrifdrnadgyidaeelaeifra
sgehvtdeeieslmkdgdknndgridfdeflkmmegvq
>d1a2ya_ 2.1.1.1.42 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
divltqspaslsasvgetvtitcrasgnihnylawyqqkqgkspqllvyytttladgvps
rfsgsgsgtqyslkinslqpedfgsyycqhfwstprtfgggtkleik
>d1a2yb_ 2.1.1.1.42 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
qvqlqesgpglvapsqslsitctvsgfsltgygvnwvrqppgkglewlgmiwgdgntdyn
salksrlsiskdnsksqvflkmnslhtddtaryycarerdyrldywgqgttltvss
>d1a2yc_ 4.2.1.2.1 Lysozyme {Chicken (Gallus gallus)}
kvfgrcelaaamkrhglanyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1a2za_ 3.47.3.1.1 Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase) {Thermococcus litoralis}
mkkvlitgfepfggdsknpteqiakyfdrkqignamvygrvlpvsvkratielkryleei
kpeivinlglaptysnitveriavniidaripdndgyqpidekieedaplaymatlpvra
itktlrdngipatisysagtylcnyvmfktlhfskiegyplkagfihvpytpdqvvnkff
llgkntpsmcleaeikaielavkvsldylekdrddikipl
>d1a2zb_ 3.47.3.1.1 Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase) {Thermococcus litoralis}
mkkvlitgfepfggdsknpteqiakyfdrkqignamvygrvlpvsvkratielkryleei
kpeivinlglaptysnitveriavniidaripdndgyqpidekieedaplaymatlpvra
itktlrdngipatisysagtylcnyvmfktlhfskiegyplkagfihvpytpdqvvnkff
llgkntpsmcleaeikaielavkvsldylekdrddikipl
>d1a2zc_ 3.47.3.1.1 Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase) {Thermococcus litoralis}
mkkvlitgfepfggdsknpteqiakyfdrkqignamvygrvlpvsvkratielkryleei
kpeivinlglaptysnitveriavniidaripdndgyqpidekieedaplaymatlpvra
itktlrdngipatisysagtylcnyvmfktlhfskiegyplkagfihvpytpdqvvnkff
llgkntpsmcleaeikaielavkvsldylekdrddikipl
>d1a2zd_ 3.47.3.1.1 Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase) {Thermococcus litoralis}
mkkvlitgfepfggdsknpteqiakyfdrkqignamvygrvlpvsvkratielkryleei
kpeivinlglaptysnitveriavniidaripdndgyqpidekieedaplaymatlpvra
itktlrdngipatisysagtylcnyvmfktlhfskiegyplkagfihvpytpdqvvnkff
llgkntpsmcleaeikaielavkvsldylekdrddikipl
>d1a30a_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwkrplvtikiggqlkealldtgaddtvieemslpgrwkpkmiggiggfikvrqyd
qiiieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1a30b_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwkrplvtikiggqlkealldtgaddtvieemslpgrwkpkmiggiggfikvrqyd
qiiieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1a31a1 4.133.1.2.1 (431-626,720-765) Eukaryotic DNA topoisomerase I, catalytic core {Human (Homo sapiens)}
pssrikgekdwqkyetarrlkkcvdkirnqyredwkskemkvrqravalyfidklalrag
nekeegetadtvgccslrvehinlhpeldgqeyvvefdflgkdsiryynkvpvekrvfkn
lqlfmenkqpeddlfdrlntgilnkhlqdlmegltakvfrtynasitlqqqlkeltapde
nipakilsynranravXklnxldpritvawckkwgvpiekiynktqrekfawaidmaded
yef
>d1a31a2 5.12.1.1.1 (215-430) Eukaryotic DNA topoisomerase I, N-terminal DNA-binding fragment {Human (Homo sapiens)}
ikwkflehkgpvfappyeplpenvkfyydgkvmklspkaeevatffakmldheyttkeif
rknffkdwrkemtneekniitnlskcdftqmsqyfkaqtearkqmskeeklkikeenekl
lkeygfcimdnhkerianfkieppglfrgrgnhpkmgmlkrrimpediiincskdakvps
pppghkwkevrhdnkvtwlvswteniqgsikyimln
>d1a32__ 1.16.1.2.1 Ribosomal protein S15 {Bacillus stearothermophilus}
ltqerkreiieqfkvhendtgspevqiailteqinnlnehlrvhkkdhhsrrgllkmvgk
rrrllaylrnkdvaryreiveklgl
>d1a33__ 2.55.1.1.4 Cyclophilin (eukaryotic) {Nematode (Brugia malayi)}
kdrrrvfldvtidgnlagrivmelyndiaprtcnnflmlctgmagtgkisgkplhykgst
fhrviknfmiqggdftkgdgtggesiyggmfddeefvmkhdepfvvsmankgpntngsqf
fitttpaphlnnihvvfgkvvsgqevvtkieylktnsknrpladvvilncgelv
>d1a34a_ 2.9.1.2.2 STMV coat protein {Satellite tobacco mosaic virus}
tgdnsnvvtmiragsypkvnptptwvraipfevsvqsgiafkvpvgslfsanfrtdsfts
vtvmsvrawtqltppvneysfvrlkplfktgdsteefegrasnintrasvgyriptnlrq
ntvaadnvcevrsncrqvalvisccfn
>d1a35a1 4.133.1.2.1 (431-635,713-765) Eukaryotic DNA topoisomerase I, catalytic core {Human (Homo sapiens)}
pssrikgekdwqkyetarrlkkcvdkirnqyredwkskemkvrqravalyfidklalrag
nekeegetadtvgccslrvehinlhpeldgqeyvvefdflgkdsiryynkvpvekrvfkn
lqlfmenkqpeddlfdrlntgilnkhlqdlmegltakvfrtynasitlqqqlkeltapde
nipakilsynranravailcnhqrappktfeksmmnlqtkidakkeqlaXqialgtskln
fldpritvawckkwgvpiekiynktqrekfawaidmadedyef
>d1a35a2 5.12.1.1.1 (215-430) Eukaryotic DNA topoisomerase I, N-terminal DNA-binding fragment {Human (Homo sapiens)}
ikwkflehkgpvfappyeplpenvkfyydgkvmklspkaeevatffakmldheyttkeif
rknffkdwrkemtneekniitnlskcdftqmsqyfkaqtearkqmskeeklkikeenekl
lkeygfcimdnhkerianfkieppglfrgrgnhpkmgmlkrrimpediiincskdakvps
pppghkwkevrhdnkvtwlvswteniqgsikyimln
>d1a36a1 1.2.5.1.1 (641-712) Eukaryotic DNA topoisomerase I, dispensable insert domain {Human (Homo sapiens)}
eksmmnlqtkidakkeqladarrdlksakadakvmkdaktkkvveskkkavqrleeqlmk
levqatdreenk
>d1a36a2 4.133.1.2.1 (431-633,713-765) Eukaryotic DNA topoisomerase I, catalytic core {Human (Homo sapiens)}
pssrikgekdwqkyetarrlkkcvdkirnqyredwkskemkvrqravalyfidklalrag
nekeegetadtvgccslrvehinlhpeldgqeyvvefdflgkdsiryynkvpvekrvfkn
lqlfmenkqpeddlfdrlntgilnkhlqdlmegltakvfrtynasitlqqqlkeltapde
nipakilsynranravailcnhqXqialgtsklnfldpritvawckkwgvpiekiynktq
rekfawaidmadedyef
>d1a36a3 5.12.1.1.1 (215-430) Eukaryotic DNA topoisomerase I, N-terminal DNA-binding fragment {Human (Homo sapiens)}
ikwkflehkgpvfappyeplpenvkfyydgkvmklspkaeevatffakmldheyttkeif
rknffkdwrkemtneekniitnlskcdftqmsqyfkaqtearkqmskeeklkikeenekl
lkeygfcimdnhkerianfkieppglfrgrgnhpkmgmlkrrimpediiincskdakvps
pppghkwkevrhdnkvtwlvswteniqgsikyimln
>d1a37a_ 1.110.7.1.2 zeta isoform {Bovine (Bos taurus)}
mdknelvqkaklaeqaeryddmaacmksvteqgaelsneernllsvayknvvgarrsswr
vvssieqktegaekkqqmareyrekietelrdicndvlsllekflipnasqaeskvfylk
mkgdyyrylaevaagddkkgivdqsqqayqeafeiskkemqpthpirlglalnfsvfyye
ilnspekacslaktafdeaiaeldtlseesykdstlimqllrdnltlw
>d1a37b_ 1.110.7.1.2 zeta isoform {Bovine (Bos taurus)}
mdknelvqkaklaeqaeryddmaacmksvteqgaelsneernllsvayknvvgarrsswr
vvssieqktegaekkqqmareyrekietelrdicndvlsllekflipnasqaeskvfylk
mkgdyyrylaevaagddkkgivdqsqqayqeafeiskkemqpthpirlglalnfsvfyye
ilnspekacslaktafdeaiaeldtlseesykdstlimqllrdnltlw
>d1a38a_ 1.110.7.1.2 zeta isoform {Bovine (Bos taurus)}
mdknelvqkaklaeqaeryddmaacmksvteqgaelsneernllsvayknvvgarrsswr
vvssieqktegaekkqqmareyrekietelrdicndvlsllekflipnasqaeskvfylk
mkgdyyrylaevaagddkkgivdqsqqayqeafeiskkemqpthpirlglalnfsvfyye
ilnspekacslaktafdeaiaeldtlseesykdstlimqllrdnltlw
>d1a38b_ 1.110.7.1.2 zeta isoform {Bovine (Bos taurus)}
mdknelvqkaklaeqaeryddmaacmksvteqgaelsneernllsvayknvvgarrsswr
vvssieqktegaekkqqmareyrekietelrdicndvlsllekflipnasqaeskvfylk
mkgdyyrylaevaagddkkgivdqsqqayqeafeiskkemqpthpirlglalnfsvfyye
ilnspekacslaktafdeaiaeldtlseesykdstlimqllrdnltlw
>d1a39__ 2.26.1.9.4 Endoglucanase I {Humicola insolens}
kpgetkevhpqlttfrctkrggckpatnfivldslwhwihraeglgpggcgdwgnpppkd
vcpdvescakncimegipdysqygvttngtslrlqhilpdgrvpsprvylldktkrryem
lhltgfeftfdvdatklpcgmnsalylsemhptgakskynpggayygtgycdaqcfvtpf
inglgniegkgsccnemdiweansrashvaphtcnkkglylcegeecafegvcdkngcgw
nnyrvnvtdyygrgeefkvntlkpftvvtqflanrrgklekihrfyvqdgkviesfytnk
egvpytnmiddefceatgsrkymelgatqgmgealtrgmvlamsiwwdqggnmewldhge
agpcakgegapsnivqvepfpevtytnlrwgeigstyqelq
>d1a3aa_ 4.88.1.1.2 Phosphotransferase IIa-mannitol {Escherichia coli}
lfklgaeniflgrkaatkeeairfageqlvkggyvepeyvqamldrekltptylgesiav
phgtveakdrvlktgvvfcqypegvrfgeeeddiarlvigiaarnnehiqvitsltnald
desvierlahttsvdevlellagrk
>d1a3ab_ 4.88.1.1.2 Phosphotransferase IIa-mannitol {Escherichia coli}
fklgaeniflgrkaatkeeairfageqlvkggyvepeyvqamldrekltptylgesiavp
hgtveakdrvlktgvvfcqypegvrfgeeeddiarlvigiaarnnehiqvitsltnaldd
esvierlahttsvdevlella
>d1a3ac_ 4.88.1.1.2 Phosphotransferase IIa-mannitol {Escherichia coli}
nlfklgaeniflgrkaatkeeairfageqlvkggyvepeyvqamldrekltptylgesia
vphgtveakdrvlktgvvfcqypegvrfgeeeddiarlvigiaarnnehiqvitsltnal
ddesvierlahttsvdevlellagrk
>d1a3ad_ 4.88.1.1.2 Phosphotransferase IIa-mannitol {Escherichia coli}
lfklgaeniflgrkaatkeeairfageqlvkggyvepeyvqamldrekltptylgesiav
phgtveakdrvlktgvvfcqypegvrfgeeeddiarlvigiaarnnehiqvitsltnald
desvierlahttsvdevlellagr
>e1a3b.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqf
>e1a3b.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>d1a3c__ 3.51.1.1.12 Uracil PRTase {Bacillus subtilis}
qkavildeqairraltriahemiernkgmnncilvgiktrgiylakrlaerieqiegnpv
tvgeiditlyrddlskktsndeplvkgadipvditdqkvilvddvlytgrtvragmdalv
dvgrpssiqlavlvdrghrelpiradyigkniptsksekvmvqldevdqndlvaiyen
>d1a3d__ 1.123.1.2.2 Snake phospholipase A2 {Indian cobra (Naja naja naja)}
nlyqfknmikctvpsrswwdfadygcycgrggsgtpvddldrccqvhdncyneaekisgc
wpyfktysyecsqgtltckgdnnacaasvcdcdrlaaicfagapyndnnynidlkarcq
>e1a3e.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqf
>e1a3e.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>d1a3fa_ 1.123.1.2.2 Snake phospholipase A2 {Indian cobra (Naja naja naja)}
nlyqfknmikctvpsrswwdfadygcycgrggsgtpvddldrccqvhdncyneaekisgc
wpyfktysyecsqgtltckgdnnacaasvcdcdrlaaicfagapyndnnynidlkarcq
>d1a3fb_ 1.123.1.2.2 Snake phospholipase A2 {Indian cobra (Naja naja naja)}
nlyqfknmikctvpsrswwdfadygcycgrggsgtpvddldrccqvhdncyneaekisgc
wpyfktysyecsqgtltckgdnnacaasvcdcdrlaaicfagapyndnnynidlkarcq
>d1a3fc_ 1.123.1.2.2 Snake phospholipase A2 {Indian cobra (Naja naja naja)}
nlyqfknmikctvpsrswwdfadygcycgrggsgtpvddldrccqvhdncyneaekisgc
wpyfktysyecsqgtltckgdnnacaasvcdcdrlaaicfagapyndnnynidlkarcq
>d1a3ga_ 5.13.1.1.2 Branched-chain amino acid aminotransferase {Escherichia coli}
kadyiwfngemvrwedakvhvmshalhygtsvfegircydshkgpvvfrhrehmqrlhds
akiyrfpvsqsidelmeacrdvirknnltsayirplifvgdvgmgvnppagystdviiaa
fpwgaylgaealeqgidamvsswnraapntiptaakaggnylssllvgsearrhgyqegi
aldvngyisegagenlfevkdgvlftppftssalpgitrdaiiklakelgievreqvlsr
eslyladevfmsgtaaeitpvrsvdgiqvgegrcgpvtkriqqaffglftgetedkwgwl
dqvnq
>d1a3gb_ 5.13.1.1.2 Branched-chain amino acid aminotransferase {Escherichia coli}
kadyiwfngemvrwedakvhvmshalhygtsvfegircydshkgpvvfrhrehmqrlhds
akiyrfpvsqsidelmeacrdvirknnltsayirplifvgdvgmgvnppagystdviiaa
fpwgaylgaealeqgidamvsswnraapntiptaakaggnylssllvgsearrhgyqegi
aldvngyisegagenlfevkdgvlftppftssalpgitrdaiiklakelgievreqvlsr
eslyladevfmsgtaaeitpvrsvdgiqvgegrcgpvtkriqqaffglftgetedkwgwl
dqvnq
>d1a3gc_ 5.13.1.1.2 Branched-chain amino acid aminotransferase {Escherichia coli}
kadyiwfngemvrwedakvhvmshalhygtsvfegircydshkgpvvfrhrehmqrlhds
akiyrfpvsqsidelmeacrdvirknnltsayirplifvgdvgmgvnppagystdviiaa
fpwgaylgaealeqgidamvsswnraapntiptaakaggnylssllvgsearrhgyqegi
aldvngyisegagenlfevkdgvlftppftssalpgitrdaiiklakelgievreqvlsr
eslyladevfmsgtaaeitpvrsvdgiqvgegrcgpvtkriqqaffglftgetedkwgwl
dqvnq
>d1a3h__ 3.1.7.3.7 Endoglucanase Cel5a {Bacillus agaradherans}
svveehgqlsisngelvnergeqvqlkgmsshglqwygqfvnyesmkwlrddwginvfra
amytssggyiddpsvkekvkeaveaaidldiyviidwhilsdndpniykeeakdffdems
elygdypnviyeianepngsdvtwgnqikpyaeevipiirnndpnniiivgtgtwsqdvh
haadnqladpnvmyafhfyagthgqnlrdqvdyaldqgaaifvsewgtsaatgdggvfld
eaqvwidfmdernlswanwslthkdessaalmpganptggwteaelspsgtfvrekires
>d1a3k__ 2.26.1.3.5 Galectin-3 CRD {Human (Homo sapiens)}
livpynlplpggvvprmlitilgtvkpnanrialdfqrgndvafhfnprfnennrrvivc
ntkldnnwgreerqsvfpfesgkpfkiqvlvepdhfkvavndahllqynhrvkklneisk
lgisgdidltsasytmi
>d1a3lh1 2.1.1.1.104 (1-113) Immunoglobulin (variable domains of L and H chains) {Diels alder catalytic Fab 13G5 (mouse), kappa L chain}
evqleesgpelvrpgtsvkisckasgytftnywlgwvkqrpghgfewigdiypggvyttn
nekfrgkailtadtssstaymqlssltsedsavyfcaraggyytggdywgqgtsvtvss
>d1a3lh2 2.1.1.2.105 (114-227) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab 13G5 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpsstwpsetvtcnvahpasstkvdkkivp
>d1a3ll1 2.1.1.1.104 (1-107) Immunoglobulin (variable domains of L and H chains) {Diels alder catalytic Fab 13G5 (mouse), kappa L chain}
divltqaafsnpvtlgasasiscrssksllnsngiihmywylqkpgqspqlliyqmskla
sgapdrfsgsgsgtdftlrisrveaedvgvyycaqnlelpytfgggtkleik
>d1a3ll2 2.1.1.2.105 (108-212) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab 13G5 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
tkdstysmsstltltkdeyerhnsytceathktstspivksfnrn
>d1a3na_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a3nb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
hltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkvk
ahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgke
ftppvqaayqkvvagvanalahkyh
>d1a3nc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a3nd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
hltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkvk
ahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgke
ftppvqaayqkvvagvanalahkyh
>d1a3oa_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttkthfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a3ob_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
hltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkvk
ahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgke
ftppvqaayqkvvagvanalahkyh
>d1a3oc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttkthfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a3od_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
hltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkvk
ahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgke
ftppvqaayqkvvagvanalahkyh
>d1a3p__ 7.3.11.1.12 Epidermal growth factor, EGF {Mouse (Mus musculus)}
pgxpssydgyclnggvxmhiesldsytcncvigysgdrcqtrdlr
>d1a3qa1 2.1.1.5.22 (227-327) p50 subunit of NF-kappa B transcription factor, C-terminal domain {Mouse (Mus musculus)}
nlkisrmdktagsvrggdevyllcdkvqkddievrfyeddengwqafgdfsptdvhkqya
ivfrtppyhkmkierpvtvflqlkrkrggdvsdskqftyyp
>d1a3qa2 2.2.5.1.4 (37-226) p50 subunit of NF-kappa B (NFKB), N-terminal domain {Mouse (Mus musculus)}
gpylviveqpkqrgfrfrygcegpshgglpgassekgrktyptvkicnyegpakievdlv
thsdpprahahslvgkqcselgicavsvgpkdmtaqfnnlgvlhvtkknmmgtmiqklqr
qrlrsrpqglteaeqreleqeakelkkvmdlsivrlrfsaflrslplkpvisqpihdsks
pgas
>d1a3qb1 2.1.1.5.22 (227-327) p50 subunit of NF-kappa B transcription factor, C-terminal domain {Mouse (Mus musculus)}
nlkisrmdktagsvrggdevyllcdkvqkddievrfyeddengwqafgdfsptdvhkqya
ivfrtppyhkmkierpvtvflqlkrkrggdvsdskqftyyp
>d1a3qb2 2.2.5.1.4 (37-226) p50 subunit of NF-kappa B (NFKB), N-terminal domain {Mouse (Mus musculus)}
gpylviveqpkqrgfrfrygcegpshgglpgassekgrktyptvkicnyegpakievdlv
thsdpprahahslvgkqcselgicavsvgpkdmtaqfnnlgvlhvtkknmmgtmiqklqr
qrlrsrpqglteaeqreleqeakelkkvmdlsivrlrfsaflrslplkpvisqpihdsks
pgas
>d1a3rh1 2.1.1.1.15 (2-119) Immunoglobulin (variable domains of L and H chains) {Fab 8F5 (mouse), kappa L chain}
vqlqqsgaelvrpgasvklscttsgfnikdiyihwvkqrpeqglewigrldpangytkyd
pkfqgkatitvdtssntaylhlssltsedtavyycdgyysyydmdywgpgtsvtvssakt
tap
>d1a3rh2 2.1.1.2.25 (120-228) Immunoglobulin (constant domains of L and H chains) {Fab 8F5 (mouse), kappa L chain}
svyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsdlytlss
svtvtsstwpsqsitcnvahpasstkvdkkiepr
>d1a3rl1 2.1.1.1.15 (1-114) Immunoglobulin (variable domains of L and H chains) {Fab 8F5 (mouse), kappa L chain}
divmtqspssltvttgekvtmtckssqsllnsrtqknyltwyqqkpgqspklliywastr
esgvpdrftgsgsgtdftlsisgvqaedlavyycqnnynypltfgagtklelkradaapt
>d1a3rl2 2.1.1.2.25 (115-214) Immunoglobulin (constant domains of L and H chains) {Fab 8F5 (mouse), kappa L chain}
vsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqdskdstys
msstltltkdeyerhnsytceathktstspivksfnrnec
>d1a3s__ 4.18.1.1.5 Ubiquitin conjugating enzyme {Human/mouse (Homo sapiens/Mus musculus), ubc9}
msgialsrlaqerkawrkdhpfgfvavptknpdgtmnlmnwecaipgkkgtpwegglfkl
rmlfkddypssppkckfepplfhpnvypsgtvclsileedkdwrpaitikqillgiqell
nepniqdpaqaeaytiycqnrveyekrvraqakkfaps
>d1a3t__ 2.35.1.1.1 Staphylococcal nuclease {Staphylococcus aureus}
lhkepatlikaidgdtxklmykgqpmtfrlllvdtpetkhpkkgvekygpeasaftkkmv
enakkievefdkgqrtdkygrglayiyadgkmvnealvrqglakvayvykpnntheqhlr
kseaqakkeklniws
>d1a3u__ 2.35.1.1.1 Staphylococcal nuclease {Staphylococcus aureus}
lhkepatlikaidgdtxklmykgqpmtfrlllvdtpetkhpkkgvekygpeasaftkkmv
enakkievefdkgqrtdkygrglayiyadgkmvnealvrqglakvayvykpnntheqhlr
kseaqakkeklniws
>d1a3v__ 2.35.1.1.1 Staphylococcal nuclease {Staphylococcus aureus}
lhkepatlikaidgdtxklmykgqpmtfrlllvdtpetkhpkkgvekygpeasaftkkmv
enakkievefdkgqrtdkygrglayiyadgkmvnealvrqglakvayvykpnntheqhlr
kseaqakkeklniws
>d1a3wa1 2.52.1.1.4 (88-188) Pyruvate kinase {Baker's yeast (Saccharomyces cerevisiae)}
peirtgtttndvdypippnhemifttddkyakacddkimyvdyknitkvisagriiyvdd
gvlsfqvlevvddktlkvkalnagkicshkgvnlpgtdvdl
>d1a3wa2 3.1.11.1.4 (2-87,189-366) Pyruvate kinase, N-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
srlerltslnvvagsdlrrtsiigtigpktnnpetlvalrkaglnivrmnfshgsyeyhk
svidnarkseelypgrplaialdtkgXpalsekdkedlrfgvkngvhmvfasfirtandv
ltirevlgeqgkdvkiivkienqqgvnnfdeilkvtdgvmvargdlgieipapevlavqk
kliaksnlagkpvicatqmlesmtynprptraevsdvgnaildgadcvmlsgetakgnyp
inavttmaetaviaeqaiaylpnyd
>d1a3wa3 3.40.1.1.4 (367-500) Pyruvate kinase, C-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
dmrnctpkptsttetvaasavaavfeqkakaiivlstsgttprlvskyrpncpiilvtrc
praarfshlyrgvfpfvfekepvsdwtddvearinfgiekakefgilkkgdtyvsiqgfk
agaghsntlqvstv
>d1a3wb1 2.52.1.1.4 (88-188) Pyruvate kinase {Baker's yeast (Saccharomyces cerevisiae)}
peirtgtttndvdypippnhemifttddkyakacddkimyvdyknitkvisagriiyvdd
gvlsfqvlevvddktlkvkalnagkicshkgvnlpgtdvdl
>d1a3wb2 3.1.11.1.4 (2-87,189-366) Pyruvate kinase, N-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
srlerltslnvvagsdlrrtsiigtigpktnnpetlvalrkaglnivrmnfshgsyeyhk
svidnarkseelypgrplaialdtkgXpalsekdkedlrfgvkngvhmvfasfirtandv
ltirevlgeqgkdvkiivkienqqgvnnfdeilkvtdgvmvargdlgieipapevlavqk
kliaksnlagkpvicatqmlesmtynprptraevsdvgnaildgadcvmlsgetakgnyp
inavttmaetaviaeqaiaylpnyd
>d1a3wb3 3.40.1.1.4 (367-500) Pyruvate kinase, C-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
dmrnctpkptsttetvaasavaavfeqkakaiivlstsgttprlvskyrpncpiilvtrc
praarfshlyrgvfpfvfekepvsdwtddvearinfgiekakefgilkkgdtyvsiqgfk
agaghsntlqvstv
>d1a3xa1 2.52.1.1.4 (88-188) Pyruvate kinase {Baker's yeast (Saccharomyces cerevisiae)}
peirtgtttndvdypippnhemifttddkyakacddkimyvdyknitkvisagriiyvdd
gvlsfqvlevvddktlkvkalnagkicshkgvnlpgtdvdl
>d1a3xa2 3.1.11.1.4 (1-87,189-366) Pyruvate kinase, N-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
msrlerltslnvvagsdlrrtsiigtigpktnnpetlvalrkaglnivrmnfshgsyeyh
ksvidnarkseelypgrplaialdtkgXpalsekdkedlrfgvkngvhmvfasfirtand
vltirevlgeqgkdvkiivkienqqgvnnfdeilkvtdgvmvargdlgieipapevlavq
kkliaksnlagkpvicatqmlesmtynprptraevsdvgnaildgadcvmlsgetakgny
pinavttmaetaviaeqaiaylpnyd
>d1a3xa3 3.40.1.1.4 (367-500) Pyruvate kinase, C-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
dmrnctpkptsttetvaasavaavfeqkakaiivlstsgttprlvskyrpncpiilvtrc
praarfshlyrgvfpfvfekepvsdwtddvearinfgiekakefgilkkgdtyvsiqgfk
agaghsntlqvstv
>d1a3xb1 2.52.1.1.4 (88-188) Pyruvate kinase {Baker's yeast (Saccharomyces cerevisiae)}
peirtgtttndvdypippnhemifttddkyakacddkimyvdyknitkvisagriiyvdd
gvlsfqvlevvddktlkvkalnagkicshkgvnlpgtdvdl
>d1a3xb2 3.1.11.1.4 (1-87,189-366) Pyruvate kinase, N-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
msrlerltslnvvagsdlrrtsiigtigpktnnpetlvalrkaglnivrmnfshgsyeyh
ksvidnarkseelypgrplaialdtkgXpalsekdkedlrfgvkngvhmvfasfirtand
vltirevlgeqgkdvkiivkienqqgvnnfdeilkvtdgvmvargdlgieipapevlavq
kkliaksnlagkpvicatqmlesmtynprptraevsdvgnaildgadcvmlsgetakgny
pinavttmaetaviaeqaiaylpnyd
>d1a3xb3 3.40.1.1.4 (367-500) Pyruvate kinase, C-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
dmrnctpkptsttetvaasavaavfeqkakaiivlstsgttprlvskyrpncpiilvtrc
praarfshlyrgvfpfvfekepvsdwtddvearinfgiekakefgilkkgdtyvsiqgfk
agaghsntlqvstv
>d1a3ya_ 2.53.1.1.6 Odorant-binding protein {Pig (Sus scrofa)}
pfelsgkwitsyigssdlekigenapfqvfmrsiefddkeskvylnffskengiceefsl
igtkqegntydvnyagnnkfvvsyasetaliisninvdeegdktimtgllgkgtdiedqd
lekfkevtrengipeenivniierddcpa
>d1a3yb_ 2.53.1.1.6 Odorant-binding protein {Pig (Sus scrofa)}
elsgkwitsyigssdlekigenapfqvfmrsiefddkeskvylnffskengiceefslig
tkqegntydvnyagnnkfvvsyasetaliisninvdeegdktimtgllgkgtdiedqdle
kfkevtrengipeenivniierddcpa
>d1a3z__ 2.5.1.1.26 Rusticyanin {Thiobacillus ferrooxidans}
twkeatlpqvkamlekddgkvsgdtvtysgktvhvvaaavlpgfpfpsfevhdkknptle
ipagatvdvtfintnkgfghsfditkkgppyavmpvidpivagtgfspvpkdgkfgytdf
twhptagtyyyvcqipghaatgmfgkivvk
>d1a40__ 3.84.1.1.5 Phosphate-binding protein {Escherichia coli}
easltgagatfpapvyakwadtyqketgnkvnyqgigssggvkqiiantvdfgasdapls
deklaqeglfqfptviggvvlavnipglksgelvldgktlgdiylgkikkwddeaiakln
pglklpsqniavvrradgsgtsfvftsylakvneewknnvgtgstvkwpiglggkgndgi
aafvqrlpgaigyveywyakqnnlaytklisadgkpvspteenfanaakgadwsktfaqd
ltnqkgedawpitsttfilihkdqkkpeqgtevlkffdwayktgakqandldyaslpdsv
veqvraawktnikdssgkply
>d1a41__ 4.133.1.2.2 Eukaryotic DNA topoisomerase I, catalytic core {Vaccinia virus}
nakrdrifvrvynvmkrincfinknikksstdsnyqlavfmlmetmffirfgkmkylken
etvglltlknkhieispdeivikfvgkdkvshefvvhksnrlykpllkltddsspeeflf
nklserkvyecikqfgirikdlrtygvnytflynfwtnvksisplpspkklialtikqta
evvghtpsiskraymattilemvkdknfldvvskttfdeflsivvdhvks
>d1a42__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasf
>d1a43__ 1.29.3.1.3 HIV capsid protein, dimerisation domain {Human immunodeficiency virus, type 1, HIV-1}
tsildirqgpkepfrdyvdrfyktlraeqasqevknwmtetllvqnanpdcktilkalgp
gatleemmtacq
>d1a44__ 2.15.1.1.2 Phosphatidylethanolamine binding protein {Bovine (Bos taurus)}
pvdlskwsgplslqevderpqhplqvkyggaevdelgkvltptqvknrptsitwdgldpg
klytlvltdpdapsrkdpkyrewhhflvvnmkgnnissgtvlsdyvgsgppkgtglhryv
wlvyeqegplkcdepilsnrsgdhrgkfkvasfrkkyelgapvagtcyqaewddyvpkly
eqlsg
>d1a45_1 2.10.1.1.4 (1-84) gamma-Crystallin {Bovine (Bos taurus), isoform F}
gkitfyedrgfqgrhyecssdhsnlqpyfsrcnsirvdsgcwmlyeqpnfqgpqyflrrg
dypdyqqwmglndsirscrlipht
>d1a45_2 2.10.1.1.4 (86-174) gamma-Crystallin {Bovine (Bos taurus), isoform F}
gshrlriyeredyrgqmveitedcsslhdrfhfseihsfnvlegwwvlyemtnyrgrqyl
lrpgdyrryhdwgatnarvgslrravdfy
>e1a46.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1a46.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
dcglrplfekksledkterellesyi
>d1a47_1 2.1.1.5.7 (496-578) Cyclodextrin glycosyltransferase, domain E {Thermoanaerobacterium thermosulfurigenes, EM1}
snsplighvgptmtkagqtitidgrgfgttsgqvlfgstagtivswddtevkvkvpsvtp
gkynislktssgatsntynnini
>d1a47_2 2.3.1.1.4 (579-683) Cyclodextrin glycosyltransferase, C-terminal domain {Thermoanaerobacterium thermosulfurigenes, EM1}
ltgnqicvrfvvnnastvygenvyltgnvaelgnwdtskaigpmfnqvvyqyptwyydvs
vpagttiqfkfikkngntitweggsnhtytvpssstgtvivnwqq
>d1a47_3 2.62.1.1.7 (407-495) Cyclodextrin glycosyltransferase {Thermoanaerobacterium thermosulfurigenes, EM1}
gttqqrwinndvyiyerkfgnnvalvainrnlstsynitglytalpagtytdvlggllng
nsisvasdgsvtpftlsagevavwqyvss
>d1a47_4 3.1.7.1.7 (1-406) Cyclodextrin glycosyltransferase {Thermoanaerobacterium thermosulfurigenes, EM1}
asdtavsnvvnystdviyqivtdrfvdgntsnnptgdlydpthtslkkyfggdwqgiink
indgyltgmgvtaiwisqpveniyavlpdstfggstsyhgywardfkrtnpyfgsftdfq
nlintahahnikviidfapnhtspasetdptyaengrlydngtllggytndtngyfhhyg
gtdfssyedgiyrnlfdladlnqqnstidsylksaikvwldmgidgirldavkhmpfgwq
knfmdsilsyrpvftfgewflgtneidvnntyfanesgmslldfrfsqkvrqvfrdntdt
mygldsmiqstasdynfindmvtfidnhdmdrfynggstrpveqalaftltsrgvpaiyy
gteqymtgngdpynrammtsfntsttaynvikklaplrksnpaiay
>d1a48__ 4.116.1.1.1 SAICAR synthase {Baker's yeast (Saccharomyces cerevisiae)}
sitkteldgilplvargkvrdiyevdagtllfvatdrisaydvimensipekgilltkls
efwfkflsndvrnhlvdiapgktifdylpaklsepkyktqledrsllvhkhklipleviv
rgyitgsawkeyvktgtvhglkqpqglkesqefpepiftpstkaeqgehdenispaqaae
lvgedlsrrvaelavklyskckdyakekgiiiadtkfefgidektneiilvdevltpdss
rfwngasykvgesqdsydkqflrdwltanklngvngvkmpqdivdrtrakyieayetltg
skwsh
>d1a49a1 2.52.1.1.1 (116-217) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a49a2 3.1.11.1.2 (12-115,218-395) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a49a3 3.40.1.1.2 (396-530) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a49b1 2.52.1.1.1 (716-817) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a49b2 3.1.11.1.2 (612-715,818-995) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a49b3 3.40.1.1.2 (996-1130) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a49c1 2.52.1.1.1 (1316-1417) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a49c2 3.1.11.1.2 (1212-1315,1418-1595) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a49c3 3.40.1.1.2 (1596-1730) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a49d1 2.52.1.1.1 (1916-2017) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a49d2 3.1.11.1.2 (1812-1915,2018-2195) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a49d3 3.40.1.1.2 (2196-2330) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a49e1 2.52.1.1.1 (3116-3217) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a49e2 3.1.11.1.2 (3012-3115,3218-3395) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a49e3 3.40.1.1.2 (3396-3530) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a49f1 2.52.1.1.1 (3716-3817) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a49f2 3.1.11.1.2 (3612-3715,3818-3995) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a49f3 3.40.1.1.2 (3996-4130) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a49g1 2.52.1.1.1 (4316-4417) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a49g2 3.1.11.1.2 (4212-4315,4418-4595) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a49g3 3.40.1.1.2 (4596-4730) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a49h1 2.52.1.1.1 (4916-5017) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a49h2 3.1.11.1.2 (4812-4915,5018-5195) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a49h3 3.40.1.1.2 (5196-5330) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a4aa_ 2.5.1.1.21 Azurin {Alcaligenes denitrificans}
aqceatiesndamqydlkemvvdksckqftvhlkhvgkmaksamghnwvltkeadkegva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
hkgtlklsn
>d1a4ab_ 2.5.1.1.21 Azurin {Alcaligenes denitrificans}
aqceatiesndamqydlkemvvdksckqftvhlkhvgkmaksamghnwvltkeadkegva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
hkgtlklsn
>d1a4ba_ 2.5.1.1.21 Azurin {Alcaligenes denitrificans}
aqceatiesndamqydlkemvvdksckqftvhlkhvgkmaksamghnwvltkeadkegva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
hkgtlklsn
>d1a4bb_ 2.5.1.1.21 Azurin {Alcaligenes denitrificans}
aqceatiesndamqydlkemvvdksckqftvhlkhvgkmaksamghnwvltkeadkegva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
hkgtlklsn
>d1a4ca_ 2.5.1.1.21 Azurin {Alcaligenes denitrificans}
aqceatiesndamqydlkemvvdksckqftvhlkhvgkmaksamghnwvltkeadkegva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
hkgtlklsn
>d1a4cb_ 2.5.1.1.21 Azurin {Alcaligenes denitrificans}
aqceatiesndamqydlkemvvdksckqftvhlkhvgkmaksamghnwvltkeadkegva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
hkgtlklsn
>d1a4cc_ 2.5.1.1.21 Azurin {Alcaligenes denitrificans}
aqceatiesndamqydlkemvvdksckqftvhlkhvgkmaksamghnwvltkeadkegva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
hkgtlklsn
>d1a4cd_ 2.5.1.1.21 Azurin {Alcaligenes denitrificans}
aqceatiesndamqydlkemvvdksckqftvhlkhvgkmaksamghnwvltkeadkegva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
hkgtlklsn
>d1a4ea_ 5.5.1.1.3 Catalase I {Baker's yeast (Saccharomyces cerevisiae)}
dvredrvvtnstgnpinepfvtqrigehgplllqdynlidslahfnrenipqrnphahgs
gafgyfevtdditdicgsamfskigkrtkcltrfstvggdkgsadtvrdprgfatkfyte
egnldwvynntpvffirdpskfphfihtqkrnpqtnlrdadmfwdflttpenqvaihqvm
ilfsdrgtpanyrsmhgysghtykwsnkngdwhyvqvhiktdqgiknltieeatkiagsn
pdycqqdlfeaiqngnypswtvyiqtmterdakklpfsvfdltkvwpqgqfplrrvgkiv
lnenplnffaqveqaafapsttvpyqeasadpvlqarlfsyadahryrlgpnfhqipvnc
pyaskffnpairdgpmnvngnfgseptylandksytyiqqdrpiqqhqevwngpaipyhw
atspgdvdfvqarnlyrvlgkqpgqqknlaynigihvegacpqiqqrvydmfarvdkgls
eaikkvae
>d1a4eb_ 5.5.1.1.3 Catalase I {Baker's yeast (Saccharomyces cerevisiae)}
dvredrvvtnstgnpinepfvtqrigehgplllqdynlidslahfnrenipqrnphahgs
gafgyfevtdditdicgsamfskigkrtkcltrfstvggdkgsadtvrdprgfatkfyte
egnldwvynntpvffirdpskfphfihtqkrnpqtnlrdadmfwdflttpenqvaihqvm
ilfsdrgtpanyrsmhgysghtykwsnkngdwhyvqvhiktdqgiknltieeatkiagsn
pdycqqdlfeaiqngnypswtvyiqtmterdakklpfsvfdltkvwpqgqfplrrvgkiv
lnenplnffaqveqaafapsttvpyqeasadpvlqarlfsyadahryrlgpnfhqipvnc
pyaskffnpairdgpmnvngnfgseptylandksytyiqqdrpiqqhqevwngpaipyhw
atspgdvdfvqarnlyrvlgkqpgqqknlaynigihvegacpqiqqrvydmfarvdkgls
eaikkvae
>d1a4ec_ 5.5.1.1.3 Catalase I {Baker's yeast (Saccharomyces cerevisiae)}
dvredrvvtnstgnpinepfvtqrigehgplllqdynlidslahfnrenipqrnphahgs
gafgyfevtdditdicgsamfskigkrtkcltrfstvggdkgsadtvrdprgfatkfyte
egnldwvynntpvffirdpskfphfihtqkrnpqtnlrdadmfwdflttpenqvaihqvm
ilfsdrgtpanyrsmhgysghtykwsnkngdwhyvqvhiktdqgiknltieeatkiagsn
pdycqqdlfeaiqngnypswtvyiqtmterdakklpfsvfdltkvwpqgqfplrrvgkiv
lnenplnffaqveqaafapsttvpyqeasadpvlqarlfsyadahryrlgpnfhqipvnc
pyaskffnpairdgpmnvngnfgseptylandksytyiqqdrpiqqhqevwngpaipyhw
atspgdvdfvqarnlyrvlgkqpgqqknlaynigihvegacpqiqqrvydmfarvdkgls
eaikkvae
>d1a4ed_ 5.5.1.1.3 Catalase I {Baker's yeast (Saccharomyces cerevisiae)}
dvredrvvtnstgnpinepfvtqrigehgplllqdynlidslahfnrenipqrnphahgs
gafgyfevtdditdicgsamfskigkrtkcltrfstvggdkgsadtvrdprgfatkfyte
egnldwvynntpvffirdpskfphfihtqkrnpqtnlrdadmfwdflttpenqvaihqvm
ilfsdrgtpanyrsmhgysghtykwsnkngdwhyvqvhiktdqgiknltieeatkiagsn
pdycqqdlfeaiqngnypswtvyiqtmterdakklpfsvfdltkvwpqgqfplrrvgkiv
lnenplnffaqveqaafapsttvpyqeasadpvlqarlfsyadahryrlgpnfhqipvnc
pyaskffnpairdgpmnvngnfgseptylandksytyiqqdrpiqqhqevwngpaipyhw
atspgdvdfvqarnlyrvlgkqpgqqknlaynigihvegacpqiqqrvydmfarvdkgls
eaikkvae
>d1a4fa_ 1.1.1.1.22 Hemoglobin D {Bar-headed goose (Anser indicus)}
vlsaadktnvkgvfskisghaeeygaetlermftaypqtktyfphfdlqhgsaqikahgk
kvvaalveavnhiddiagalsklsdlhaqklrvdpvnfkflghcflvvvaihhpsaltae
vhasldkflcavgtvltakyr
>d1a4fb_ 1.1.1.1.37 Hemoglobin D {Bar-headed goose (Anser indicus)}
vhwsaeekqlitglwgkvnvadcgaealarllivypwtqrffssfgnlssptailgnpmv
rahgkkvltsfgdavknldnikntfaqlselhcdklhvdpenfrllgdiliivlaahfak
eftpdcqaawqklvrvvahalarkyh
>d1a4ga_ 2.59.1.1.3 Influenza neuraminidase {Influenza virus B, different strains}
epewtyprlscqgstfqkallisphrfgeargnsapliirepfiacgpkeckhfalthya
aqpggyyngtredrnklrhlisvklgkiptvensifhmaawsgsachdgrewtyigvdgp
dsnalikikygeaytdtyhsyannilrtqesacnciggdcylmitdgsasgiskcrflki
regriikeifptgrvehteectcgfasnktiecacrdnsytakrpfvklnvetdtaeirl
mctetyldtprpddgsitgpcesngdkgrggikggfvhqrmaskigrwysrtmsktermg
melyvrydgdpwtdsdalahsgvmvsmkepgwysfgfeikdkkcdvpcigiemvhdggkk
twhsaataiyclmgsgqllwdtvtgvdmal
>d1a4gb_ 2.59.1.1.3 Influenza neuraminidase {Influenza virus B, different strains}
epewtyprlscqgstfqkallisphrfgeargnsapliirepfiacgpkeckhfalthya
aqpggyyngtredrnklrhlisvklgkiptvensifhmaawsgsachdgrewtyigvdgp
dsnalikikygeaytdtyhsyannilrtqesacnciggdcylmitdgsasgiskcrflki
regriikeifptgrvehteectcgfasnktiecacrdnsytakrpfvklnvetdtaeirl
mctetyldtprpddgsitgpcesngdkgrggikggfvhqrmaskigrwysrtmsktermg
melyvrydgdpwtdsdalahsgvmvsmkepgwysfgfeikdkkcdvpcigiemvhdggkk
twhsaataiyclmgsgqllwdtvtgvdmal
>d1a4h__ 4.96.1.1.1 HSP90 {Baker's yeast (Saccharomyces cerevisiae)}
masetfefqaeitqlmsliintvysnkeiflrelisnasdaldkirykslsdpkqletep
dlfiritpkpeqkvleirdsgigmtkaelinnlgtiaksgtkafmealsagadvsmigqf
gvgfyslflvadrvqvisksnddeqyiwesnaggsftvtldevnerigrgtilrlflkdd
qleyleekrikevikrhsefvaypiqlvvtkeve
>d1a4ia1 3.2.1.7.7 (127-296) Tetrahydrofolate dehydrogenase/cyclohydrolase {Human (Homo sapiens)}
ltsinagrlargdlndcfipctpkgcleliketgvpiagrhavvvgrskivgapmhdlll
wnnatvttchsktahldeevnkgdilvvatgqpemvkgewikpgaividcginyvpddkk
pngrkvvgdvaydeakerasfitpvpggvgpmtvamlmqstvesakrfle
>d1a4ia2 3.48.1.2.1 (2-126) Tetrahydrofolate dehydrogenase/cyclohydrolase {Human (Homo sapiens)}
apaeilngkeisaqirarlknqvtqlkeqvpgftprlailqvgnrddsnlyinvklkaae
eigikathiklprtttesevmkyitslnedstvhgflvqlpldsensinteevinaiape
kdvdg
>d1a4ib1 3.2.1.7.7 (127-296) Tetrahydrofolate dehydrogenase/cyclohydrolase {Human (Homo sapiens)}
ltsinagrlargdlndcfipctpkgcleliketgvpiagrhavvvgrskivgapmhdlll
wnnatvttchsktahldeevnkgdilvvatgqpemvkgewikpgaividcginyvpddkk
pngrkvvgdvaydeakerasfitpvpggvgpmtvamlmqstvesakrfle
>d1a4ib2 3.48.1.2.1 (2-126) Tetrahydrofolate dehydrogenase/cyclohydrolase {Human (Homo sapiens)}
apaeilngkeisaqirarlknqvtqlkeqvpgftprlailqvgnrddsnlyinvklkaae
eigikathiklprtttesevmkyitslnedstvhgflvqlpldsensinteevinaiape
kdvdg
>d1a4ja1 2.1.1.1.103 (1-112) Immunoglobulin (variable domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
elvmtqtplslpvslgdqasiscrssqslvhsngntylhwylqkpgqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyfcsqsthvpptfgggtkleik
>d1a4ja2 2.1.1.2.104 (113-217) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
rtvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqd
skdstyslsstltlskadyekhkvyacevthqglsspvtksfnrg
>d1a4jb1 2.1.1.1.103 (1-119) Immunoglobulin (variable domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
qvqllesgpelkkpgetvkisckasgytftnygmnwvkqapgkglkwmgwintytgepty
addfkgrfafsletsastaylqinnlknedtatyfcvqaerlrrtfdywgagttvtvss
>d1a4jb2 2.1.1.2.104 (120-217) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
astkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkv
>d1a4jh1 2.1.1.1.103 (1-119) Immunoglobulin (variable domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
qvqllesgpelkkpgetvkisckasgytftnygmnwvkqapgkglkwmgwintytgepty
addfkgrfafsletsastaylqinnlknedtatyfcvqaerlrrtfdywgagttvtvss
>d1a4jh2 2.1.1.2.104 (120-217) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
astkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkv
>d1a4jl1 2.1.1.1.103 (1-112) Immunoglobulin (variable domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
elvmtqtplslpvslgdqasiscrssqslvhsngntylhwylqkpgqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyfcsqsthvpptfgggtkleik
>d1a4jl2 2.1.1.2.104 (113-217) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
rtvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqd
skdstyslsstltlskadyekhkvyacevthqglsspvtksfnrg
>d1a4ka1 2.1.1.1.103 (1-112) Immunoglobulin (variable domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
elvmtqtplslpvslgdqasiscrssqsllhsngntylhwylqkpgqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyfcsqvthvpptfgggtkleikrtvaa
>d1a4ka2 2.1.1.2.104 (113-211) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
psvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqdskdst
yslsstltlskadyekhkvyacevthqglsspvtksfnr
>d1a4kb1 2.1.1.1.103 (1-119) Immunoglobulin (variable domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
qvqllesgpelkkpgetvkisckasgytftnygmnwvkqapgkglkwmgwintytgepty
addfkgrfafsletsastaylqinnlknedtatyfcvqaerlrrtfdywgagttvtvssa
stkgp
>d1a4kb2 2.1.1.2.104 (120-213) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
svfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqssglysls
svvtvpssslgtqtyicnvnhkpsntkvdkkvep
>d1a4kh1 2.1.1.1.103 (1-119) Immunoglobulin (variable domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
qvqllesgpelkkpgetvkisckasgytftnygmnwvkqapgkglkwmgwintytgepty
addfkgrfafsletsastaylqinnlknedtatyfcvqaerlrrtfdywgagttvtvssa
stkgp
>d1a4kh2 2.1.1.2.104 (120-211) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
svfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqssglysls
svvtvpssslgtqtyicnvnhkpsntkvdkkv
>d1a4kl1 2.1.1.1.103 (1-112) Immunoglobulin (variable domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
elvmtqtplslpvslgdqasiscrssqsllhsngntylhwylqkpgqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyfcsqvthvpptfgggtkleikrtvaa
>d1a4kl2 2.1.1.2.104 (113-212) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
psvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqdskdst
yslsstltlskadyekhkvyacevthqglsspvtksfnrg
>d1a4la_ 3.1.8.1.1 Adenosine deaminase (ADA) {Mouse (Mus musculus)}
tpafnkpkvelhvhldgaikpetilyfgkkrgialpadtveelrniigmdkplslpgfla
kfdyympviagcreaikriayefvemkakegvvyvevrysphllanskvdpmpwnqtegd
vtpddvvdlvnqglqegeqafgikvrsilccmrhqpswslevlelckkynqktvvamdla
gdetiegsslfpghveayegavkngihrtvhagevgspevvreavdilktervghgyhti
edealynrllkenmhfevcpwssyltgawdpktthavvrfkndkanyslntddplifkst
ldtdyqmtkkdmgfteeefkrlninaakssflpeeekkellerlyreyq
>d1a4lb_ 3.1.8.1.1 Adenosine deaminase (ADA) {Mouse (Mus musculus)}
tpafnkpkvelhvhldgaikpetilyfgkkrgialpadtveelrniigmdkplslpgfla
kfdyympviagcreaikriayefvemkakegvvyvevrysphllanskvdpmpwnqtegd
vtpddvvdlvnqglqegeqafgikvrsilccmrhqpswslevlelckkynqktvvamdla
gdetiegsslfpghveayegavkngihrtvhagevgspevvreavdilktervghgyhti
edealynrllkenmhfevcpwssyltgawdpktthavvrfkndkanyslntddplifkst
ldtdyqmtkkdmgfteeefkrlninaakssflpeeekkellerlyreyq
>d1a4lc_ 3.1.8.1.1 Adenosine deaminase (ADA) {Mouse (Mus musculus)}
tpafnkpkvelhvhldgaikpetilyfgkkrgialpadtveelrniigmdkplslpgfla
kfdyympviagcreaikriayefvemkakegvvyvevrysphllanskvdpmpwnqtegd
vtpddvvdlvnqglqegeqafgikvrsilccmrhqpswslevlelckkynqktvvamdla
gdetiegsslfpghveayegavkngihrtvhagevgspevvreavdilktervghgyhti
edealynrllkenmhfevcpwssyltgawdpktthavvrfkndkanyslntddplifkst
ldtdyqmtkkdmgfteeefkrlninaakssflpeeekkellerlyreyq
>d1a4ld_ 3.1.8.1.1 Adenosine deaminase (ADA) {Mouse (Mus musculus)}
tpafnkpkvelhvhldgaikpetilyfgkkrgialpadtveelrniigmdkplslpgfla
kfdyympviagcreaikriayefvemkakegvvyvevrysphllanskvdpmpwnqtegd
vtpddvvdlvnqglqegeqafgikvrsilccmrhqpswslevlelckkynqktvvamdla
gdetiegsslfpghveayegavkngihrtvhagevgspevvreavdilktervghgyhti
edealynrllkenmhfevcpwssyltgawdpktthavvrfkndkanyslntddplifkst
ldtdyqmtkkdmgfteeefkrlninaakssflpeeekkellerlyreyq
>d1a4ma_ 3.1.8.1.1 Adenosine deaminase (ADA) {Mouse (Mus musculus)}
tpafnkpkvelhvhldgaikpetilyfgkkrgialpadtveelrniigmdkplslpgfla
kfdyympviagcreaikriayefvemkakegvvyvevrysphllanskvdpmpwnqtegd
vtpddvvdlvnqglqegeqafgikvrsilccmrhqpswslevlelckkynqktvvamdla
gdetiegsslfpghveayegavkngihrtvhagevgspevvreavdilktervghgyhti
edealynrllkenmhfevcpwssyltgawdpktthavvrfkndkanyslntddplifkst
ldtdyqmtkkdmgfteeefkrlninaakssflpeeekkellerlyreyq
>d1a4mb_ 3.1.8.1.1 Adenosine deaminase (ADA) {Mouse (Mus musculus)}
tpafnkpkvelhvhldgaikpetilyfgkkrgialpadtveelrniigmdkplslpgfla
kfdyympviagcreaikriayefvemkakegvvyvevrysphllanskvdpmpwnqtegd
vtpddvvdlvnqglqegeqafgikvrsilccmrhqpswslevlelckkynqktvvamdla
gdetiegsslfpghveayegavkngihrtvhagevgspevvreavdilktervghgyhti
edealynrllkenmhfevcpwssyltgawdpktthavvrfkndkanyslntddplifkst
ldtdyqmtkkdmgfteeefkrlninaakssflpeeekkellerlyreyq
>d1a4mc_ 3.1.8.1.1 Adenosine deaminase (ADA) {Mouse (Mus musculus)}
tpafnkpkvelhvhldgaikpetilyfgkkrgialpadtveelrniigmdkplslpgfla
kfdyympviagcreaikriayefvemkakegvvyvevrysphllanskvdpmpwnqtegd
vtpddvvdlvnqglqegeqafgikvrsilccmrhqpswslevlelckkynqktvvamdla
gdetiegsslfpghveayegavkngihrtvhagevgspevvreavdilktervghgyhti
edealynrllkenmhfevcpwssyltgawdpktthavvrfkndkanyslntddplifkst
ldtdyqmtkkdmgfteeefkrlninaakssflpeeekkellerlyreyq
>d1a4md_ 3.1.8.1.1 Adenosine deaminase (ADA) {Mouse (Mus musculus)}
tpafnkpkvelhvhldgaikpetilyfgkkrgialpadtveelrniigmdkplslpgfla
kfdyympviagcreaikriayefvemkakegvvyvevrysphllanskvdpmpwnqtegd
vtpddvvdlvnqglqegeqafgikvrsilccmrhqpswslevlelckkynqktvvamdla
gdetiegsslfpghveayegavkngihrtvhagevgspevvreavdilktervghgyhti
edealynrllkenmhfevcpwssyltgawdpktthavvrfkndkanyslntddplifkst
ldtdyqmtkkdmgfteeefkrlninaakssflpeeekkellerlyreyq
>d1a4oa_ 1.110.7.1.2 zeta isoform {Bovine (Bos taurus)}
mdknelvqkaklaeqaeryddmaacmksvteqgaelsneernllsvayknvvgarrsswr
vvssieqktegaekkqqmareyrekietelrdicndvlsllekflipnasqaeskvfylk
mkgdyyrylaevaagddkkgivdqsqqayqeafeiskkemqpthpirlglalnfsvfyye
ilnspekacslaktafdeaiaeldtlseesykdstlimqllrdnltlw
>d1a4ob_ 1.110.7.1.2 zeta isoform {Bovine (Bos taurus)}
mdknelvqkaklaeqaeryddmaacmksvteqgaelsneernllsvayknvvgarrsswr
vvssieqktegaekkqqmareyrekietelrdicndvlsllekflipnasqaeskvfylk
mkgdyyrylaevaagddkkgivdqsqqayqeafeiskkemqpthpirlglalnfsvfyye
ilnspekacslaktafdeaiaeldtlseesykdstlimqllrdnltlw
>d1a4oc_ 1.110.7.1.2 zeta isoform {Bovine (Bos taurus)}
mdknelvqkaklaeqaeryddmaacmksvteqgaelsneernllsvayknvvgarrsswr
vvssieqktegaekkqqmareyrekietelrdicndvlsllekflipnasqaeskvfylk
mkgdyyrylaevaagddkkgivdqsqqayqeafeiskkemqpthpirlglalnfsvfyye
ilnspekacslaktafdeaiaeldtlseesykdstlimqllrdnltlw
>d1a4od_ 1.110.7.1.2 zeta isoform {Bovine (Bos taurus)}
mdknelvqkaklaeqaeryddmaacmksvteqgaelsneernllsvayknvvgarrsswr
vvssieqktegaekkqqmareyrekietelrdicndvlsllekflipnasqaeskvfylk
mkgdyyrylaevaagddkkgivdqsqqayqeafeiskkemqpthpirlglalnfsvfyye
ilnspekacslaktafdeaiaeldtlseesykdstlimqllrdnltlw
>d1a4pa_ 1.42.1.2.5 Calcyclin (S100) {Human (Homo sapiens), P11 s100a10, calpactin}
psqmehametmmftfhkfagdkgyltkedlrvlmekefpgflenqkdplavdkimkdldq
crdgkvgfqsffsliagltiacndyfvvhmkq
>d1a4pb_ 1.42.1.2.5 Calcyclin (S100) {Human (Homo sapiens), P11 s100a10, calpactin}
psqmehametmmftfhkfagdkgyltkedlrvlmekefpgflenqkdplavdkimkdldq
crdgkvgfqsffsliagltiacndyfvvhmk
>d1a4qa_ 2.59.1.1.3 Influenza neuraminidase {Influenza virus B, different strains}
epewtyprlscqgstfqkallisphrfgeargnsapliirepfiacgpkeckhfalthya
aqpggyyngtredrnklrhlisvklgkiptvensifhmaawsgsachdgrewtyigvdgp
dsnalikikygeaytdtyhsyannilrtqesacnciggdcylmitdgsasgiskcrflki
regriikeifptgrvehteectcgfasnktiecacrdnsytakrpfvklnvetdtaeirl
mctetyldtprpddgsitgpcesngdkgrggikggfvhqrmaskigrwysrtmsktermg
melyvrydgdpwtdsdalahsgvmvsmkepgwysfgfeikdkkcdvpcigiemvhdggkk
twhsaataiyclmgsgqllwdtvtgvdmal
>d1a4qb_ 2.59.1.1.3 Influenza neuraminidase {Influenza virus B, different strains}
epewtyprlscqgstfqkallisphrfgeargnsapliirepfiacgpkeckhfalthya
aqpggyyngtredrnklrhlisvklgkiptvensifhmaawsgsachdgrewtyigvdgp
dsnalikikygeaytdtyhsyannilrtqesacnciggdcylmitdgsasgiskcrflki
regriikeifptgrvehteectcgfasnktiecacrdnsytakrpfvklnvetdtaeirl
mctetyldtprpddgsitgpcesngdkgrggikggfvhqrmaskigrwysrtmsktermg
melyvrydgdpwtdsdalahsgvmvsmkepgwysfgfeikdkkcdvpcigiemvhdggkk
twhsaataiyclmgsgqllwdtvtgvdmal
>d1a4ra_ 3.30.1.6.11 CDC42 {Human (Homo sapiens)}
mqtikcvvvgdvavgktcllisyttnkfpseyvptvfdnyavtvmiggepytlglfdtag
qedydrlrplsypqtdvflvcfsvvspssfenvkekwvpeithhcpktpfllvgtqidlr
ddpstieklaknkqkpitpetaeklardlkavkyvecsaltqkglknvfdeailaalepp
epkksrrcvl
>d1a4rb_ 3.30.1.6.11 CDC42 {Human (Homo sapiens)}
mqtikcvvvgdvavgktcllisyttnkfpseyvptvfdnyavtvmiggepytlglfdtag
qedydrlrplsypqtdvflvcfsvvspssfenvkekwvpeithhcpktpfllvgtqidlr
ddpstieklaknkqkpitpetaeklardlkavkyvecsaltqkglknvfdeailaalepp
epkksrrcvl
>d1a4sa_ 3.71.1.1.6 Aldehyde reductase (dehydrogenase), ALDH {Baltic cod (Gadus callarias)}
aqlvdsmpsastgsvvvtddlnywggrrikskdgattepvfepatgrvlcqmvpcgaeev
dqavqsaqaaylkwskmagiersrvmleaariirerrdniaklevinngktiteaeydid
aawqcieyyaglaptlsgqhiqlpggafaytrreplgvcagilawnypfmiaawkcapal
acgnavvfkpspmtpvtgvilaeifheagvpvglvnvvqggaetgsllchhpnvakvsft
gsvptgkkvmemsaktvkhvtlelggkspllifkdcelenavrgalmanfltqgqvctng
trvfvqreimpqfleevvkrtkaivvgdplltetrmggliskpqldkvlgfvaqakkega
rvlcggepltpsdpklkngyfmspcvldncrddmtcvkeeifgpvmsvlpfdteeevlqr
annttfglasgvftrdisrahrvaanleagtcyintysispvevpfggykmsgfgrengq
atvdyysqlktvivemgdvdslf
>d1a4sb_ 3.71.1.1.6 Aldehyde reductase (dehydrogenase), ALDH {Baltic cod (Gadus callarias)}
aqlvdsmpsastgsvvvtddlnywggrrikskdgattepvfepatgrvlcqmvpcgaeev
dqavqsaqaaylkwskmagiersrvmleaariirerrdniaklevinngktiteaeydid
aawqcieyyaglaptlsgqhiqlpggafaytrreplgvcagilawnypfmiaawkcapal
acgnavvfkpspmtpvtgvilaeifheagvpvglvnvvqggaetgsllchhpnvakvsft
gsvptgkkvmemsaktvkhvtlelggkspllifkdcelenavrgalmanfltqgqvctng
trvfvqreimpqfleevvkrtkaivvgdplltetrmggliskpqldkvlgfvaqakkega
rvlcggepltpsdpklkngyfmspcvldncrddmtcvkeeifgpvmsvlpfdteeevlqr
annttfglasgvftrdisrahrvaanleagtcyintysispvevpfggykmsgfgrengq
atvdyysqlktvivemgdvdslf
>d1a4sc_ 3.71.1.1.6 Aldehyde reductase (dehydrogenase), ALDH {Baltic cod (Gadus callarias)}
aqlvdsmpsastgsvvvtddlnywggrrikskdgattepvfepatgrvlcqmvpcgaeev
dqavqsaqaaylkwskmagiersrvmleaariirerrdniaklevinngktiteaeydid
aawqcieyyaglaptlsgqhiqlpggafaytrreplgvcagilawnypfmiaawkcapal
acgnavvfkpspmtpvtgvilaeifheagvpvglvnvvqggaetgsllchhpnvakvsft
gsvptgkkvmemsaktvkhvtlelggkspllifkdcelenavrgalmanfltqgqvctng
trvfvqreimpqfleevvkrtkaivvgdplltetrmggliskpqldkvlgfvaqakkega
rvlcggepltpsdpklkngyfmspcvldncrddmtcvkeeifgpvmsvlpfdteeevlqr
annttfglasgvftrdisrahrvaanleagtcyintysispvevpfggykmsgfgrengq
atvdyysqlktvivemgdvdslf
>d1a4sd_ 3.71.1.1.6 Aldehyde reductase (dehydrogenase), ALDH {Baltic cod (Gadus callarias)}
aqlvdsmpsastgsvvvtddlnywggrrikskdgattepvfepatgrvlcqmvpcgaeev
dqavqsaqaaylkwskmagiersrvmleaariirerrdniaklevinngktiteaeydid
aawqcieyyaglaptlsgqhiqlpggafaytrreplgvcagilawnypfmiaawkcapal
acgnavvfkpspmtpvtgvilaeifheagvpvglvnvvqggaetgsllchhpnvakvsft
gsvptgkkvmemsaktvkhvtlelggkspllifkdcelenavrgalmanfltqgqvctng
trvfvqreimpqfleevvkrtkaivvgdplltetrmggliskpqldkvlgfvaqakkega
rvlcggepltpsdpklkngyfmspcvldncrddmtcvkeeifgpvmsvlpfdteeevlqr
annttfglasgvftrdisrahrvaanleagtcyintysispvevpfggykmsgfgrengq
atvdyysqlktvivemgdvdslf
>d1a4ua_ 3.2.1.2.12 Drosophila alcohol dehydrogenase {Fruit fly (Drosophila lebanonensis)}
mdltnknvifvaalggigldtsrelvkrnlknfvildrvenptalaelkainpkvnitfh
tydvtvpvaeskkllkkifdqlktvdilingagilddhqiertiainftglvntttaild
fwdkrkggpggiianicsvtgfnaihqvpvysaskaavvsftnslaklapitgvtaysin
pgitrtplvhtfnswldveprvaelllshptqtseqcgqnfvkaieankngaiwkldlgt
leaiewtkhwdshi
>d1a4ub_ 3.2.1.2.12 Drosophila alcohol dehydrogenase {Fruit fly (Drosophila lebanonensis)}
mdltnknvifvaalggigldtsrelvkrnlknfvildrvenptalaelkainpkvnitfh
tydvtvpvaeskkllkkifdqlktvdilingagilddhqiertiainftglvntttaild
fwdkrkggpggiianicsvtgfnaihqvpvysaskaavvsftnslaklapitgvtaysin
pgitrtplvhtfnswldveprvaelllshptqtseqcgqnfvkaieankngaiwkldlgt
leaiewtkhwdshi
>d1a4v__ 4.2.1.2.14 alpha-Lactalbumin {Human (Homo sapiens)}
kqftkcelsqllkdidgyggialpelictmfhtsgydtqaivennesteyglfqisnklw
ckssqvpqsrnicdiscdkflddditddimcakkildikgidywlahkalctekleqwlc
ekl
>e1a4w.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidq
>e1a4w.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
dcglrplfekksledkterellesyi
>d1a4xa_ 3.51.1.1.12 Uracil PRTase {Bacillus subtilis}
kavildeqairraltriahemiernkgmnncilvgiktrgiylakrlaerieqiegnpvt
vgeiditlyrddlskktsndeplvkgadipvditdqkvilvddvlytgrtvragmdalvd
vgrpssiqlavlvdrghrelpiradyigkniptsksekvmvqldevdqndlvaiyen
>d1a4xb_ 3.51.1.1.12 Uracil PRTase {Bacillus subtilis}
kavildeqairraltriahemiernkgmnncilvgiktrgiylakrlaerieqiegnpvt
vgeiditlyrddlskktsndeplvkgadipvditdqkvilvddvlytgrtvragmdalvd
vgrpssiqlavlvdrghrelpiradyigkniptsksekvmvqldevdqndlvaiyen
>d1a4ya_ 3.9.1.1.1 Ribonuclease inhibitor {Pig (Sus scrofa)}
sldiqsldiqceelsdarwaellpllqqcqvvrlddcgltearckdissalrvnpalael
nlrsnelgdvgvhcvlqglqtpsckiqklslqnccltgagcgvlsstlrtlptlqelhls
dnllgdaglqllceglldpqcrleklqleycslsaasceplasvlrakpdfkeltvsnnd
ineagvrvlcqglkdspcqlealklescgvtsdncrdlcgivaskaslrelalgsnklgd
vgmaelcpgllhpssrlrtlwiwecgitakgcgdlcrvlrakeslkelslagnelgdega
rllcetllepgcqleslwvkscsftaaccshfssvlaqnrfllelqisnnrledagvrel
cqglgqpgsvlrvlwladcdvsdsscsslaatllanhslreldlsnnclgdagilqlves
vrqpgclleqlvlydiywseemedrlqalekdkpslrvis
>d1a4yb_ 4.5.1.1.7 Angiogenin {Human (Homo sapiens)}
qdnsrythfltqhydakpqgrddrycesimrrrgltspckdintfihgnkrsikaicenk
ngnphrenlriskssfqvttcklhggspwppcqyratagfrnvvvacenglpvhldqsif
rrp
>d1a4yd_ 3.9.1.1.1 Ribonuclease inhibitor {Pig (Sus scrofa)}
sldiqsldiqceelsdarwaellpllqqcqvvrlddcgltearckdissalrvnpalael
nlrsnelgdvgvhcvlqglqtpsckiqklslqnccltgagcgvlsstlrtlptlqelhls
dnllgdaglqllceglldpqcrleklqleycslsaasceplasvlrakpdfkeltvsnnd
ineagvrvlcqglkdspcqlealklescgvtsdncrdlcgivaskaslrelalgsnklgd
vgmaelcpgllhpssrlrtlwiwecgitakgcgdlcrvlrakeslkelslagnelgdega
rllcetllepgcqleslwvkscsftaaccshfssvlaqnrfllelqisnnrledagvrel
cqglgqpgsvlrvlwladcdvsdsscsslaatllanhslreldlsnnclgdagilqlves
vrqpgclleqlvlydiywseemedrlqalekdkpslrvis
>d1a4ye_ 4.5.1.1.7 Angiogenin {Human (Homo sapiens)}
qdnsrythfltqhydakpqgrddrycesimrrrgltspckdintfihgnkrsikaicenk
ngnphrenlriskssfqvttcklhggspwppcqyratagfrnvvvacenglpvhldqsif
rrp
>d1a4za_ 3.71.1.1.3 Aldehyde reductase (dehydrogenase), ALDH {Bovine (Bos taurus), mitochondrial}
vptpnqqpevlynqifinnewhdavskktfptvnpstgdvichvaegdkadvdravkaar
aafqlgspwrrmdasergrllnrladlierdrtylaaletldngkpyiisylvdldmvlk
clryyagwadkyhgktipidgdyfsytrhepvgvcgqiipwnfpllmqawklgpalatgn
vvvmkvaeqtpltalyvanlikeagfppgvvnvipgfgptagaaiashedvdkvaftgst
evghliqvaagksnlkrvtleiggkspniimsdadmdwaveqahfalffnqgqcccagsr
tfvqediyaefversvaraksrvvgnpfdsrteqgpqvdetqfkkvlgyiksgkeeglkl
lcgggaaadrgyfiqptvfgdlqdgmtiakeeifgpvmqilkfksmeevvgrannskygl
aaavftkdldkanylsqalqagtvwvncydvfgaqspfggyklsgsgrelgeyglqayte
vktvtvrvpqkns
>d1a4zb_ 3.71.1.1.3 Aldehyde reductase (dehydrogenase), ALDH {Bovine (Bos taurus), mitochondrial}
vptpnqqpevlynqifinnewhdavskktfptvnpstgdvichvaegdkadvdravkaar
aafqlgspwrrmdasergrllnrladlierdrtylaaletldngkpyiisylvdldmvlk
clryyagwadkyhgktipidgdyfsytrhepvgvcgqiipwnfpllmqawklgpalatgn
vvvmkvaeqtpltalyvanlikeagfppgvvnvipgfgptagaaiashedvdkvaftgst
evghliqvaagksnlkrvtleiggkspniimsdadmdwaveqahfalffnqgqcccagsr
tfvqediyaefversvaraksrvvgnpfdsrteqgpqvdetqfkkvlgyiksgkeeglkl
lcgggaaadrgyfiqptvfgdlqdgmtiakeeifgpvmqilkfksmeevvgrannskygl
aaavftkdldkanylsqalqagtvwvncydvfgaqspfggyklsgsgrelgeyglqayte
vktvtvrvpqkns
>d1a4zc_ 3.71.1.1.3 Aldehyde reductase (dehydrogenase), ALDH {Bovine (Bos taurus), mitochondrial}
vptpnqqpevlynqifinnewhdavskktfptvnpstgdvichvaegdkadvdravkaar
aafqlgspwrrmdasergrllnrladlierdrtylaaletldngkpyiisylvdldmvlk
clryyagwadkyhgktipidgdyfsytrhepvgvcgqiipwnfpllmqawklgpalatgn
vvvmkvaeqtpltalyvanlikeagfppgvvnvipgfgptagaaiashedvdkvaftgst
evghliqvaagksnlkrvtleiggkspniimsdadmdwaveqahfalffnqgqcccagsr
tfvqediyaefversvaraksrvvgnpfdsrteqgpqvdetqfkkvlgyiksgkeeglkl
lcgggaaadrgyfiqptvfgdlqdgmtiakeeifgpvmqilkfksmeevvgrannskygl
aaavftkdldkanylsqalqagtvwvncydvfgaqspfggyklsgsgrelgeyglqayte
vktvtvrvpqkns
>d1a4zd_ 3.71.1.1.3 Aldehyde reductase (dehydrogenase), ALDH {Bovine (Bos taurus), mitochondrial}
vptpnqqpevlynqifinnewhdavskktfptvnpstgdvichvaegdkadvdravkaar
aafqlgspwrrmdasergrllnrladlierdrtylaaletldngkpyiisylvdldmvlk
clryyagwadkyhgktipidgdyfsytrhepvgvcgqiipwnfpllmqawklgpalatgn
vvvmkvaeqtpltalyvanlikeagfppgvvnvipgfgptagaaiashedvdkvaftgst
evghliqvaagksnlkrvtleiggkspniimsdadmdwaveqahfalffnqgqcccagsr
tfvqediyaefversvaraksrvvgnpfdsrteqgpqvdetqfkkvlgyiksgkeeglkl
lcgggaaadrgyfiqptvfgdlqdgmtiakeeifgpvmqilkfksmeevvgrannskygl
aaavftkdldkanylsqalqagtvwvncydvfgaqspfggyklsgsgrelgeyglqayte
vktvtvrvpqkns
>d1a50a_ 3.1.2.2.5 Trp synthase alpha-subunit {Salmonella typhimurium}
eryenlfaqlndrregafvpfvtlgdpgieqslkiidtlidagadalelgvpfsdpladg
ptiqnanlrafaagvtpaqcfemlalirekhptipigllmyanlvfnngidafyarceqv
gvdsvlvadvpveesapfrqaalrhniapificppnadddllrqvasygrgytyllsrsg
vtgaenrgalplhhlieklkeyhaapalqgfgisspeqvsaavragaagaisgsaivkii
eknlaspkqmlaelrsfvsamkaasr
>d1a50b_ 3.67.1.1.1 Tryptophan synthase, beta-subunit {Salmonella typhimurium}
ttllnpyfgefggmyvpqilmpalnqleeafvraqkdpefqaqfadllknyagrptaltk
cqnitagtrttlylkredllhggahktnqvlgqallakrmgkseiiaetgagqhgvasal
asallglkcriymgakdverqspnvfrmrlmgaevipvhsgsatlkdacnealrdwsgsy
etahymlgtaagphpyptivrefqrmigeetkaqildkegrlpdaviacvgggsnaigmf
adfindtsvgligvepgghgietgehgaplkhgrvgiyfgmkapmmqtadgqieesysis
agldfpsvgpqhaylnsigradyvsitddealeafktlcrhegiipalesshalahalkm
mreqpekeqllvvnlsgrgdkdiftvhdil
>d1a52a_ 1.114.1.1.4 Estrogen receptor alpha {Human (Homo sapiens)}
lalsltadqmvsalldaeppilyseydptrpfseasmmglltnladrelvhminwakrvp
gfvdltlhdqvhllecawleilmiglvwrsmehpgkllfapnllldrnqgkcvegmveif
dmllatssrfrmmnlqgeefvclksiillnsgvytflsstlksleekdhihrvldkitdt
lihlmakagltlqqqherlaqlllilshirhmsnkgmehlysmkcknvvplydllleml
>d1a52b_ 1.114.1.1.4 Estrogen receptor alpha {Human (Homo sapiens)}
slalsltadqmvsalldaeppilyseydptrpfseasmmglltnladrelvhminwakrv
pgfvdltlhdqvhllecawleilmiglvwrsmehpgkllfapnllldrnqgkcvegmvei
fdmllatssrfrmmnlqgeefvclksiillnsgvytflsstlksleekdhihrvldkitd
tlihlmakagltlqqqherlaqlllilshirhmsnkgmehlysmkcknvvplydllleml
>d1a53__ 3.1.2.2.4 Indole-3-glycerophosphate (IGP) synthase {Sulfolobus solfataricus}
prylkgwlkdvvqlslrrpsfrasrqrpiislnerilefnkrnitaiiaeykrkspsgld
verdpieyskfmeryavglsilteekyfngsyetlrkiassvsipilmkdfivkesqidd
aynlgadtvllivkiltereleslleyarsygmeplieindendldialrigarfigins
rdletleinkenqrklismipsnvvkvaesgiserneieelrklgvnafligsslmrnpe
kikefil
>d1a54a_ 3.84.1.1.5 Phosphate-binding protein {Escherichia coli}
easltgagatfpapvyakwadtyqketgnkvnyqgigssggvkqiiantvdfgasdapls
deklaqeglfqfptviggvvlavnipglksgelvldgktlgdiylgkikkwddeaiakln
pglklpsqniavvrradgsgtsfvftsylakvneewknnvgtgstvkwpiglggkgndgi
aafvqrlpgaigyveycyakqnnlaytklisadgkpvspteenfanaakgadwsktfaqd
ltnqkgedawpitsttfilihkdqkkpeqgtevlkffdwayktgakqandldyaslpdsv
veqvraawktnikdssgkply
>d1a55a_ 3.84.1.1.5 Phosphate-binding protein {Escherichia coli}
easltgagatfpapvyakwadtyqketgnkvnyqgigssggvkqiiantvdfgasdapls
deklaqeglfqfptviggvvlavnipglksgelvldgktlgdiylgkikkwddeaiakln
pglklpsqniavvrradgsgtsfvftsylakvneewknnvgtgstvkwpiglggkgndgi
aafvqrlpgaigyveycyakqnnlaytklisadgkpvspteenfanaakgadwsktfaqd
ltnqkgedawpitsttfilihkdqkkpeqgtevlkffdwayktgakqandldyaslpdsv
veqvraawktnikdssgkply
>d1a56__ 1.3.1.1.24 Cytochrome c552 {Nitrosomonas europaea}
dadlakknnciachqvetkvvgpalkdiaakyadkddaatylagkikggssgvwgqipmp
pnvnvsdadakaladwiltlk
>d1a57__ 2.53.1.2.3 Intestinal fatty acid binding protein {Rat (Rattus rattus)}
afdgtwkvdrnenysgahdnlkltitqegnkftvkessnfrnidvvfelgvdfaysladg
teltgtwtmegnklvgkfkrvdngkeliavreisgneliqtytyegveakrifkke
>d1a58__ 2.55.1.1.4 Cyclophilin (eukaryotic) {Nematode (Brugia malayi)}
mskkdrrrvfldvtidgnlagrivmelyndiaprtcnnflmlctgmagtgkisgkplhyk
gstfhrviknfmiqggdftkgdgtggesiyggmfddeefvmkhdepfvvsmankgpntng
sqffitttpaphlnnihvvfgkvvsgqevvtkieylktnsknrpladvvilncgelv
>d1a59__ 1.99.1.1.4 Citrate synthase {Antarctic bacterium, ds2-3r}
eptihkglagvtadvtaiskvnsdtnsllyrgypvqelaakcsfeqvayllwnselpnds
elkafvnfershrkldenvkgaidllstachpmdvartavsvlganharaqdsspeanle
kamsllatfpsvvaydqrrrrgeeliepredldysanflwmtfgeeaapevveafnvsmi
lyaehsfnastftarvitstladlhsavtgaigalkgplhgganeavmhtfeeigirkde
sldeaatrskawmvdalaqkkkvmgfghrvykngdsrvptmksaldamikhydrpemlgl
yngleaameeakqikpnldypagptynlmgfdtemftplfiaaritgwtahimeqvadna
lirplseyngpeqrqvp
>d1a5aa_ 3.1.2.2.5 Trp synthase alpha-subunit {Salmonella typhimurium}
meryenlfaqlndrregafvpfvtlgdpgieqslkiidtlidagadalelgvpfsdplan
gptiqnanlrafaagvtpaqcfemlalirekhptipigllmyanlvfnngidafyarceq
vgvdsvlvadvpveesapfrqaalrhniapificppnadddllrqvasygrgytyllsrs
gvtgaenrgalplhhlieklkeyhaapalqgfgisspeqvsaavragaagaisgsaivki
ieknlaspkqmlaelrsfvsamkaasra
>d1a5ab_ 3.67.1.1.1 Tryptophan synthase, beta-subunit {Salmonella typhimurium}
tllnpyfgefggmyvpqilmpalnqleeafvraqkdpefqaqfadllknyagrptaltkc
qnitagtrttlylkredllhggahktnqvlgqallakrmgkseiiaetgagqhgvasala
sallglkcriymgakdverqspnvfrmrlmgaevipvhsgsatlkdacnealrdwsgsye
tahymlgtaagphpyptivrefqrmigeetkaqildkegrlpdaviacvgggsnaigmfa
dfindtsvgligvepgghgietgehgaplkhgrvgiyfgmkapmmqtadgqieesysisa
gldfpsvgpqhaylnsigradyvsitddealeafktlcrhegiipalesshalahalkmm
reqpekeqllvvnlsgrgdkdiftvhdil
>d1a5ba_ 3.1.2.2.5 Trp synthase alpha-subunit {Salmonella typhimurium}
meryenlfaqlndrregafvpfvtlgdpgieqslkiidtlidagadalelgvpfsdplan
gptiqnanlrafaagvtpaqcfemlalirekhptipigllmyanlvfnngidafyarceq
vgvdsvlvadvpveesapfrqaalrhniapificppnadddllrqvasygrgytyllsrs
gvtgaenrgalplhhlieklkeyhaapalqgfgisspeqvsaavragaagaisgsaivki
ieknlaspkqmlaelrsfvsamkaasra
>d1a5bb_ 3.67.1.1.1 Tryptophan synthase, beta-subunit {Salmonella typhimurium}
tllnpyfgefggmyvpqilmpalnqleeafvraqkdpefqaqfadllknyagrptaltkc
qnitagtrttlylkredllhggahktnqvlgqallakrmgkseiiaetgagqhgvasala
sallglkcriymgakdverqspnvfrmrlmgaevipvhsgsatlkdacnealrdwsgsye
tahymlgtaagphpyptivrefqrmigeetkaqildkegrlpdaviacvgggsnaigmfa
dfindtsvgligvepgghgietgehgaplkhgrvgiyfgmkapmmqtadgqieesysisa
gldfpsvgpqhaylnsigradyvsitddealeafktlcrhegiipalesshalahalkmm
reqpekeqllvvnlsgrgdkdiftvhdil
>d1a5ca_ 3.1.9.1.6 Fructose-1,6-bisphosphate aldolase {Plasmodium falciparum}
lpadvaeelattaqklvqagkgilaadestqtikkrfdniklentienrasyrdllfgtk
glgkfisgailfeetlfqkneagvpmvnllhneniipgikvdkglvnipctdeekstqgl
dglaerckeyykagarfakwrtvlvidtakgkptdlsihetawglaryasicqqnrlvpi
vepeiladgphsievcavvtqkvlscvfkalqengvllegallkpnmvtagyectakttt
qdvgfltvrtlrrtvppalpgvvflsggqseeeasvnlnsinalgphpwaltfsygralq
asvlntwqgkkenvakarevllqraeanslatygkykggagg
>d1a5cb_ 3.1.9.1.6 Fructose-1,6-bisphosphate aldolase {Plasmodium falciparum}
lpadvaeelattaqklvqagkgilaadestqtikkrfdniklentienrasyrdllfgtk
glgkfisgailfeetlfqkneagvpmvnllhneniipgikvdkglvnipctdeekstqgl
dglaerckeyykagarfakwrtvlvidtakgkptdlsihetawglaryasicqqnrlvpi
vepeiladgphsievcavvtqkvlscvfkalqengvllegallkpnmvtagyectakttt
qdvgfltvrtlrrtvppalpgvvflsggqseeeasvnlnsinalgphpwaltfsygralq
asvlntwqgkkenvakarevllqraeanslatygkykggagg
>d1a5da1 2.10.1.1.6 (1-84) beta-Crystallin {Rat (Rattus norvegicus), isoform E}
gkitfyedrgfqgrhyecstdhsnlqpyfsrcnsvrvdsgcwmlyeqpnftgcqyflrrg
dypdyqqwmgfsdsvrscrliphs
>d1a5da2 2.10.1.1.6 (85-174) beta-Crystallin {Rat (Rattus norvegicus), isoform E}
sshririyeredyrgqmveitddcphlqdrfhfsdfhsfhvmegywvlyempnyrgrqyl
lrpgeyrryhdwgamnarvgslrrimdfy
>d1a5db1 2.10.1.1.6 (1-84) beta-Crystallin {Rat (Rattus norvegicus), isoform E}
gkitfyedrgfqgrhyecstdhsnlqpyfsrcnsvrvdsgcwmlyeqpnftgcqyflrrg
dypdyqqwmgfsdsvrscrliphs
>d1a5db2 2.10.1.1.6 (85-174) beta-Crystallin {Rat (Rattus norvegicus), isoform E}
sshririyeredyrgqmveitddcphlqdrfhfsdfhsfhvmegywvlyempnyrgrqyl
lrpgeyrryhdwgamnarvgslrrimdfy
>d1a5e__ 1.110.2.1.5 Cell cycle inhibitor p16ink4A {Human (Homo sapiens)}
mepaagssmepsadwlataaargrveevralleagalpnapnsygrrpiqvmmmgsarva
ellllhgaepncadpatltrpvhdaaregfldtlvvlhragarldvrdawgrlpvdlaee
lghrdvarylraaaggtrgsnharidaaegpsdipd
>d1a5fh1 2.1.1.1.118 (1-120) Immunoglobulin (variable domains of L and H chains) {Anti-E-selectin Fab (mouse), kappa L chain}
evalqqsgaelvkpgasvklscaasgftikdaymhwvkqkpeqglewigridsgssntny
dptfkgkatitaddssntaylqmssltsedtavyycarvglsywyamdywgqgtsvtvss
>d1a5fh2 2.1.1.2.116 (121-217) Immunoglobulin (constant domains of L and H chains) {Anti-E-selectin Fab (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvsvptstetvtcnvahapsstkvdkkivpr
>d1a5fl1 2.1.1.1.118 (1-113) Immunoglobulin (variable domains of L and H chains) {Anti-E-selectin Fab (mouse), kappa L chain}
divmtqspssltvttgekvtmtckssqsllnsgaqknyltwyqqkpgqspklliywastr
esgvpdrftgsgsgtdftlsisgvqaedlavyycqnnynypltfgagtklelk
>d1a5fl2 2.1.1.2.116 (114-220) Immunoglobulin (constant domains of L and H chains) {Anti-E-selectin Fab (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>e1a5g.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1a5g.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1a5h.1a 2.41.1.2.28 Two-chain tissue plasminogen activator (TC)-T-PA {Human (Homo sapiens)}
ikgglfadiashpwqaaifakhrrspgerflcggilisscwilsaahcfqerfpphhltv
ilgrtyrvvpgeeeqkfevekyivhkefdddtydndiallqlksdssrcaqessvvrtvc
lppadlqlpdwtecelsgygkhealspfyserlkeahvrlypssrctsqhllnrtvtdnm
lcagdtrsggpqanlhdacqgdsggplvclndgrmtlvgiiswglgcgqkdvpgvytkvt
nyldwirdnmrp
>e1a5h.2b 2.41.1.2.28 Two-chain tissue plasminogen activator (TC)-T-PA {Human (Homo sapiens)}
ikgglfadiashpwqaaifakhrrspgerflcggilisscwilsaahcfqerfpphhltv
ilgrtyrvvpgeeeqkfevekyivhkefdddtydndiallqlksdssrcaqessvvrtvc
lppadlqlpdwtecelsgygkhealspfyserlkeahvrlypssrctsqhllnrtvtdnm
lcagdtrsggpqanlhdacqgdsggplvclndgrmtlvgiiswglgcgqkdvpgvytkvt
nyldwirdnmrp
>d1a5ia_ 2.41.1.2.30 Single chain tissue plasminogen activator {Vampire bat (Desmodus rotundus)}
tcglrkykepqlhstgglftditshpwqaaifaqnrrssgerflcggilisscwvltaah
cfqesylpdqlkvvlgrtyrvkpgeeeqtfkvkkyivhkefdddtynndiallqlksdsp
qcaqesdsvraiclpeanlqlpdwtecelsgygkhkssspfyseqlkeghvrlypssrca
pkflfnktvtnnmlcagdtrsgeiypnvhdacqgdsggplvcmndnhmtllgiiswgvgc
gekdvpgvytkvtnylgwirdnmhl
>d1a5j_1 1.4.1.3.3 (1-55) b-Myb DNA binding domain {Chicken (Gallus gallus)}
gipdlvkgpwtkeedqkvielvkkygtkqwtliakhlkgrlgkqcrerwhnhlnp
>d1a5j_2 1.4.1.3.3 (56-110) b-Myb DNA binding domain {Chicken (Gallus gallus)}
evkksswteeedriifeahkvlgnrwaeiakllpgrtdnavknhwnstikrkvdt
>d1a5ka_ 4.7.1.1.1 Urease, gamma-subunit {Klebsiella aerogenes}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1a5kb_ 2.75.2.1.1 Urease, beta-subunit {Klebsiella aerogenes}
mipgeyhvkpgqialntgratcrvvvenhgdrpiqvgshyhfaevnpalkfdrqqaagyr
lnipagtavrfepgqkrevelvafaghravfgfrgevmgpl
>d1a5kc1 2.80.1.1.1 (2-129,423-475) alpha-Subunit of urease, composite domain {Klebsiella aerogenes}
snisrqayadmfgptvgdkvrladtelwieveddlttygeevkfgggkvirdgmgqgqml
aadcvdlvltnalivdhwgivkadigvkdgrifaigkagnpdiqpnvtipigaateviaa
egkivtagXsievgkladlvvwspaffgvkpatvikggmiaiapmgdinasiptpqpvhy
rp
>d1a5kc2 3.1.8.2.1 (130-422,476-567) alpha-subunit of urease, catalytic domain {Klebsiella aerogenes}
gidthihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagvigleihedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvchhldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf
>d1a5la_ 4.7.1.1.1 Urease, gamma-subunit {Klebsiella aerogenes}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1a5lb_ 2.75.2.1.1 Urease, beta-subunit {Klebsiella aerogenes}
mipgeyhvkpgqialntgratcrvvvenhgdrpiqvgshyhfaevnpalkfdrqqaagyr
lnipagtavrfepgqkrevelvafaghravfgfrgevmgpl
>d1a5lc1 2.80.1.1.1 (2-129,423-475) alpha-Subunit of urease, composite domain {Klebsiella aerogenes}
snisrqayadmfgptvgdkvrladtelwieveddlttygeevkfgggkvirdgmgqgqml
aadcvdlvltnalivdhwgivkadigvkdgrifaigkagnpdiqpnvtipigaateviaa
egkivtagXsievgkladlvvwspaffgvkpatvikggmiaiapmgdinasiptpqpvhy
rp
>d1a5lc2 3.1.8.2.1 (130-422,476-567) alpha-subunit of urease, catalytic domain {Klebsiella aerogenes}
gidthihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagviglcihedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvahhldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf
>d1a5ma_ 4.7.1.1.1 Urease, gamma-subunit {Klebsiella aerogenes}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1a5mb_ 2.75.2.1.1 Urease, beta-subunit {Klebsiella aerogenes}
mipgeyhvkpgqialntgratcrvvvenhgdrpiqvgshyhfaevnpalkfdrqqaagyr
lnipagtavrfepgqkrevelvafaghravfgfrgevmgpl
>d1a5mc1 2.80.1.1.1 (2-129,423-475) alpha-Subunit of urease, composite domain {Klebsiella aerogenes}
snisrqayadmfgptvgdkvrladtelwieveddlttygeevkfgggkvirdgmgqgqml
aadcvdlvltnalivdhwgivkadigvkdgrifaigkagnpdiqpnvtipigaateviaa
egkivtagXsievgkladlvvwspaffgvkpatvikggmiaiapmgdinasiptpqpvhy
rp
>d1a5mc2 3.1.8.2.1 (130-422,476-567) alpha-subunit of urease, catalytic domain {Klebsiella aerogenes}
gidthihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagviglaihedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvchhldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf
>d1a5na_ 4.7.1.1.1 Urease, gamma-subunit {Klebsiella aerogenes}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1a5nb_ 2.75.2.1.1 Urease, beta-subunit {Klebsiella aerogenes}
mipgeyhvkpgqialntgratcrvvvenhgdrpiqvgshyhfaevnpalkfdrqqaagyr
lnipagtavrfepgqkrevelvafaghravfgfrgevmgpl
>d1a5nc1 2.80.1.1.1 (2-129,423-475) alpha-Subunit of urease, composite domain {Klebsiella aerogenes}
snisrqayadmfgptvgdkvrladtelwieveddlttygeevkfgggkvirdgmgqgqml
aadcvdlvltnalivdhwgivkadigvkdgrifaigkagnpdiqpnvtipigaateviaa
egkivtagXsievgkladlvvwspaffgvkpatvikggmiaiapmgdinasiptpqpvhy
rp
>d1a5nc2 3.1.8.2.1 (130-422,476-567) alpha-subunit of urease, catalytic domain {Klebsiella aerogenes}
gidthihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagviglaihedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvchhldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf
>d1a5oa_ 4.7.1.1.1 Urease, gamma-subunit {Klebsiella aerogenes}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1a5ob_ 2.75.2.1.1 Urease, beta-subunit {Klebsiella aerogenes}
mipgeyhvkpgqialntgratcrvvvenhgdrpiqvgshyhfaevnpalkfdrqqaagyr
lnipagtavrfepgqkrevelvafaghravfgfrgevmgpl
>d1a5oc1 2.80.1.1.1 (2-129,423-475) alpha-Subunit of urease, composite domain {Klebsiella aerogenes}
snisrqayadmfgptvgdkvrladtelwieveddlttygeevkfgggkvirdgmgqgqml
aadcvdlvltnalivdhwgivkadigvkdgrifaigkagnpdiqpnvtipigaateviaa
egkivtagXsievgkladlvvwspaffgvkpatvikggmiaiapmgdinasiptpqpvhy
rp
>d1a5oc2 3.1.8.2.1 (130-422,476-567) alpha-subunit of urease, catalytic domain {Klebsiella aerogenes}
gidthihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagviglcihedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvchhldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf
>d1a5p__ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrakpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypnaaykttqankhiivacegnpyvpvhf
dasv
>d1a5q__ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskyancaykttqankhiivacegnpyvpvhf
dasv
>d1a5r__ 4.13.2.1.3 SUMO-1 {Human (Homo sapiens)}
gsmsdqeakpstedlgdkkegeyiklkvigqdsseihfkvkmtthlkklkesycqrqgvp
mnslrflfegqriadnhtpkelgmeeedvievyqeqtgghstv
>d1a5sa_ 3.1.2.2.5 Trp synthase alpha-subunit {Salmonella typhimurium}
eryenlfaqlndrregafvpfvtlgdpgieqslkiidtlidagadalelgvpfsdpladg
ptiqnanlrafaagvtpaqcfemlalirekhptipigllmyanlvfnngidafyarceqv
gvdsvlvadvpveesapfrqaalrhniapificppnadddllrqvasygrgytyllsrsg
vtgaenrgalplhhlieklkeyhaapalqgfgisspeqvsaavragaagaisgsaivkii
eknlaspkqmlaelrsfvsamkaasr
>d1a5sb_ 3.67.1.1.1 Tryptophan synthase, beta-subunit {Salmonella typhimurium}
tllnpyfgefggmyvpqilmpalnqleeafvraqkdpefqaqfadllknyagrptaltkc
qnitagtrttlylkredllhggahktnqvlgqallakrmgkseiiaetgagqhgvasala
sallglkcriymgakdverqspnvfrmrlmgaevipvhsgsatlkdacnealrdwsgsye
tahymlgtaagphpyptivrefqrmigeetkaqildkegrlpdaviacvgggsnaigmfa
dfindtsvgligvepgghgietgehgaplkhgrvgiyfgmkapmmqtadgqieesysisa
gldfpsvgpqhaylnsigradyvsitddealeafktlcrhegiipalesshalahalkmm
reqpekeqllvvnlsgrgdkdiftvhd
>d1a5t_1 1.112.1.1.1 (167-330) delta prime subunit of DNA polymerase III, C-terminal domain {Escherichia coli}
ppeqyavtwlsrevtmsqdallaalrlsagspgaalalfqgdnwqaretlcqalaysvps
gdwysllaalnheqaparlhwlatllmdalkrhhgaaqvtnvdvpglvaelanhlspsrl
qailgdvchireqlmsvtginrellitdlllriehylqpgvvlp
>d1a5t_2 3.30.1.10.3 (1-166) delta prime subunit of DNA polymerase III, N-terminal domain {Escherichia coli}
mrwypwlrpdfeklvasyqagrghhalliqalpgmgddaliyalsryllcqqpqghkscg
hcrgcqlmqagthpdyytlapekgkntlgvdavrevteklneharlggakvvwvtdaall
tdaaanallktleeppaetwfflatreperllatlrsrcrlhylap
>d1a5ua1 2.52.1.1.1 (116-217) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a5ua2 3.1.11.1.2 (12-115,218-395) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a5ua3 3.40.1.1.2 (396-530) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a5ub1 2.52.1.1.1 (716-817) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a5ub2 3.1.11.1.2 (612-715,818-995) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a5ub3 3.40.1.1.2 (996-1130) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a5uc1 2.52.1.1.1 (1316-1417) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a5uc2 3.1.11.1.2 (1212-1315,1418-1595) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a5uc3 3.40.1.1.2 (1596-1730) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a5ud1 2.52.1.1.1 (1916-2017) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a5ud2 3.1.11.1.2 (1812-1915,2018-2195) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a5ud3 3.40.1.1.2 (2196-2330) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a5ue1 2.52.1.1.1 (3116-3217) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a5ue2 3.1.11.1.2 (3012-3115,3218-3395) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a5ue3 3.40.1.1.2 (3396-3530) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a5uf1 2.52.1.1.1 (3716-3817) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a5uf2 3.1.11.1.2 (3612-3715,3818-3995) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a5uf3 3.40.1.1.2 (3996-4130) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a5ug1 2.52.1.1.1 (4316-4417) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a5ug2 3.1.11.1.2 (4212-4315,4418-4595) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a5ug3 3.40.1.1.2 (4596-4730) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a5uh1 2.52.1.1.1 (4916-5017) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a5uh2 3.1.11.1.2 (4812-4915,5018-5195) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a5uh3 3.40.1.1.2 (5196-5330) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a5v__ 3.46.3.2.1 ASV integrase, catalytic domain {Avian sarcoma virus, Rous sarcoma virus, Schmidt-Ruppin strain B}
glgplqiwqtdftleprmaprswlavtvdtassaivvtqhgrvtsvaaqhhwataiavlg
rpkaiktdngscftskstrewlarwgiahttgipgnsqgqamveranrllkdkirvlaeg
dgfmkriptskqgellakamyalnhf
>d1a5w__ 3.46.3.2.1 ASV integrase, catalytic domain {Avian sarcoma virus, Rous sarcoma virus, Schmidt-Ruppin strain B}
glgplqiwqtdftleprmaprswlavtvdtassaivvtqhgrvtsvaaqhhwataiavlg
rpkaiktdngscftskstrewlarwgiahttgipgnsqgqamveranrllkdkirvlaeg
dgfmkriptskqgellakamyalnhf
>d1a5x__ 3.46.3.2.1 ASV integrase, catalytic domain {Avian sarcoma virus, Rous sarcoma virus, Schmidt-Ruppin strain B}
glgplqiwqtdftleprmaprswlavtvdtassaivvtqhgrvtsvaaqhhwataiavlg
rpkaiktdngscftskstrewlarwgiahttgipgnsqgqamveranrllkdkirvlaeg
dgfmkriptskqgellakamyalnhf
>d1a5y__ 3.37.1.3.1 Tyrosine phosphatase {Human (Homo sapiens), 1B}
emekefeqidksgswaaiyqdirheasdfpcrvaklpknknrnryrdvspfdhsriklhq
edndyinaslikmeeaqrsyiltqgplpntcghfwemvweqksrgvvmlnrvmekgslkc
aqywpqkeekemifedtnlkltlisediksyytvrqlelenlttqetreilhfhyttwpd
fgvpespasflnflfkvresgslspehgpvvvhxsagigrsgtfcladtclllmdkrkdp
ssvdikkvlldmrkfrmgliataeqlrfsylaviegakfimgds
>d1a5z_1 3.2.1.5.15 (22-163) Lactate dehydrogenase {Thermotoga maritima}
mkigivglgrvgsstafallmkgfaremvlidvdkkraegdaldlihgtpftrraniyag
dyadlkgsdvvivaagvpqkpgetrlqllgrnarvmkeiarnvskyapdsivivvtnpvd
vltyfflkesgmdprkvfgs
>d1a5z_2 4.132.1.1.15 (164-333) Lactate dehydrogenase {Thermotoga maritima}
gtvldtarlrtliaqhcgfsprsvhvyvigehgdsevpvwsgamiggiplqnmcqvcqkc
dskilenfaektkraayeiierkgathyaialavadivesiffdekrvltlsvyledylg
vkdlcisvpvtlgkhgverilelnlneeeleafrksasilknaineitaeen
>e1a61.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1a61.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>d1a62__ 2.35.4.5.5 Rho termination factor, N-terminal, RNA-binding domain {Escherichia coli}
nltelkntpvselitlgenxglenlarxrkqdiifailkqhaksgedifgdgvleilqdg
fgflrsadssylagpddiyvspsqirrfnlrtgdtisgkirppkegeryfallkvnevnf
dkpe
>d1a63__ 2.35.4.5.5 Rho termination factor, N-terminal, RNA-binding domain {Escherichia coli}
mnltelkntpvselitlgenmglenlarmrkqdiifailkqhaksgedifgdgvleilqd
gfgflrsadssylagpddiyvspsqirrfnlrtgdtisgkirppkegeryfallkvnevn
fdkpenarnk
>d1a64a_ 2.1.1.1.8 CD2, first domain {Rat (Rattus rattus)}
gtvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlki
knltrddsgtynvtvystngtrildkaldlrile
>d1a64b_ 2.1.1.1.8 CD2, first domain {Rat (Rattus rattus)}
gtvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlki
knltrddsgtynvtvystngtrildkaldlrile
>d1a65a1 2.5.1.3.5 (1-131) Laccase {Inky cap fungus (Coprinus cinereus)}
qivnsvdtmtltnanvspdgftragilvngvhgplirggkndnfelnvvndldnptmlrp
tsihwhglfqrgtnwadgadgvnqcpispghaflykftpaghagtfwyhshfgtqycdgl
rgpmviyddnd
>d1a65a2 2.5.1.3.5 (132-303) Laccase {Inky cap fungus (Coprinus cinereus)}
phaalydeddentiitladwyhipapsiqgaaqpdatlingkgryvggpaaelsivnveq
gkkyrmrlislscdpnwqfsidgheltiievdgeltephtvdrlqiftgqrysfvldanq
pvdnywiraqpnkgrnglagtfangvnsailryagaanadpttsanpnpaql
>d1a65a3 2.5.1.3.5 (304-504) Laccase {Inky cap fungus (Coprinus cinereus)}
neadlhalidpaapgiptpgaadvnlrfqlgfsggrftingtayespsvptllqimsgaq
sandllpagsvyelprnqvvelvvpagvlggphpfhlhghafsvvrsagsstynfvnpvk
rdvvslgvtgdevtirfvtdnpgpwffhchiefhlmnglaivfaedmantvdannppvew
aqlceiyddlppeatsiqtvv
>d1a66a_ 2.2.5.1.2 Transcription factor NFATC, DNA-binding domain {Human (Homo sapiens)}
mkdwqlpshsgpyelrievqpkshhraryetegsrgavkasagghpivqlhgyleneplm
lqlfigtaddrllrphafyqvhritgktvsttsheailsntkvleipllpensmravidc
agilklrnsdielrkgetdigrkntrvrlvfrvhvpqpsgrtlslqvasnpiecsqrs
>d1a67__ 4.15.1.2.1 Cystatin {Chicken (Gallus gallus)}
gapvpvdendeglqralqfamaeynrasndkyssrvvrvisakrqlvsgikyilqveigr
ttcpkssgdlqscefhdepemakyttctfvvysipwlnqiklleskcq
>d1a68__ 4.35.1.2.1 Shaker potassium channel {California sea hare (Aplysia californica)}
ervvinvsglrfetqlktlnqfpdtllgnpqkrnryydplrneyffdrnrpsfdailyfy
qsggrlrrpvnvpldvfseeikfyelg
>d1a69a_ 3.47.1.1.3 Purine nucleoside phosphorylase, PNP {Escherichia coli}
atphinaemgdfadvvlmpgdplrakyiaetfledarevnnvrgmlgftgtykgrkisvm
ghgmgipscsiytkelitdfgvkkiirvgscgavlphvklrdvvigmgactdskvnrirf
kdhdfaaiadfdmvrnavdaakalgidarvgnlfsadlfyspdgemfdvmekygilgvem
eaagiygvaaefgakaltictvsdhirtheqttaaerqttfndmikialesvllgdk
>d1a69b_ 3.47.1.1.3 Purine nucleoside phosphorylase, PNP {Escherichia coli}
atphinaemgdfadvvlmpgdplrakyiaetfledarevnnvrgmlgftgtykgrkisvm
ghgmgipscsiytkelitdfgvkkiirvgscgavlphvklrdvvigmgactdskvnrirf
kdhdfaaiadfdmvrnavdaakalgidarvgnlfsadlfyspdgemfdvmekygilgvem
eaagiygvaaefgakaltictvsdhirtheqttaaerqttfndmikialesvllgdk
>d1a69c_ 3.47.1.1.3 Purine nucleoside phosphorylase, PNP {Escherichia coli}
atphinaemgdfadvvlmpgdplrakyiaetfledarevnnvrgmlgftgtykgrkisvm
ghgmgipscsiytkelitdfgvkkiirvgscgavlphvklrdvvigmgactdskvnrirf
kdhdfaaiadfdmvrnavdaakalgidarvgnlfsadlfyspdgemfdvmekygilgvem
eaagiygvaaefgakaltictvsdhirtheqttaaerqttfndmikialesvllgdk
>d1a6aa1 2.1.1.2.151 (82-180) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dr3}
itnvppevtvltnspvelrepnvlicfidkftppvvnvtwlrngkpvttgvsetvflpre
dhlfrkfhylpflpstedvydcrvehwgldepllkhwef
>d1a6aa2 4.17.1.1.6 (5-81) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr3}
hviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgalania
vdkanleimtkrsnytp
>d1a6ab1 2.1.1.2.151 (93-191) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dr3}
rrvhpkvtvypsktqplqhhnllvcsvsgfypgsievrwfrngqeektgvvstglihngd
wtfqtlvmletvprsgevytcqvehpsvtspltvewrar
>d1a6ab2 4.17.1.1.6 (5-92) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr3}
prfleystsechffngtervryldryfhnqeenvrfdsdvgefravtelgrpdaeywnsq
kdlleqkrgrvdnycrhnygvvesftvq
>d1a6bb_ 7.34.1.1.5 Zinc finger protein ncp10 {Moloney murine leukemia virus, MMLV}
gerrrsqldrdqcayckekghwakdcpkkprgprgprpqt
>d1a6ca1 2.9.1.2.6 (1-176) TRSV capsid protein {Tobacco ringspot virus}
avtvvpdptccgtlsfkvpkdakkgkhlgtfdirqaimdygglhsqewcakgivnptftv
rmhaprnafaglsiactfddykridlpalgnecppsemfelptkvfmlkdadvhewqfny
geltghglcnwanvatqptlyffvastnqvtmaadwqcivtmhvdmgpvidrfeln
>d1a6ca2 2.9.1.2.6 (177-348) TRSV capsid protein {Tobacco ringspot virus}
ptmtwpiqlgdtfaidryyeakeikldgstsmlsisynfggpvkhskkhaisysravmsr
nlgwsgtisgsvksvsslfctasfvifpweceapptlrqvlwgphqimhgdgqfeiaikt
rlhsaatteegfgrlgilplsgpiapdahvgsyefivhintwrpdsqvhppm
>d1a6ca3 2.9.1.2.6 (349-513) TRSV capsid protein {Tobacco ringspot virus}
fssselynwftltnlkpdantgvvnfdipgyihdfaskdatvtlasnplswlvaatgwhy
gevdlciswsrskqaqaqegsvsittnyrdwgaywqgqariydlrrteaeipiflgsyag
atpsgalgkqnyvrisivnakdivalrvclrpksikfwgrsatlf
>d1a6da1 1.119.1.2.1 (17-145,404-519) Thermosome {Thermoplasma acidophilum}
reqgknaqrnnieaakaiadavrttlgpkgmdkmlvdsigdiiisndgatilkemdvehp
takmivevskaqdtavgdgtttavvlsgellkqaetlldqgvhptvisngyrlavneark
iideiaeksXflwgggaveaelamrlakyansvggreqlaieafakaleiiprtlaenag
idpintliklkaddekgrisvgvdldnngvgdmkakgvvdplrvkthalesavevatmil
riddvi
>d1a6da2 3.7.5.2.1 (215-367) Thermosome {Thermoplasma acidophilum}
gividkekvhskmpdvvknakialidsaleikkteieakvqisdpskiqdflnqetntfk
qmvekikksganvvlcqkgiddvaqhylakegiyavrrvkksdmeklakatgakivtdld
dltpsvlgeaetveerkigddrmtfvmgcknpk
>d1a6da3 4.46.1.2.1 (146-214,368-403) Thermosome {Thermoplasma acidophilum}
tddatlrkialtalsgkntglsndfladlvvkavnavaevrdgktivdtanikvdkkngg
svndtqfisXavsilirggtdhvvseveralndairvvaitkedgk
>d1a6db1 1.119.1.2.1 (20-144,404-521) Thermosome {Thermoplasma acidophilum}
kdamkenieaaiaisnsvrsslgprgmdkmlvdslgdivitndgvtilkemdvehpaakm
mvevsktqdsfvgdgtttaviiaggllqqaqglinqnvhptvisegyrmaseeakrvide
istkiXayaagggataaeiafrlrsyaqkiggrqqlaiekfadaieeipralaenagldp
idillklraehakgnktyginvftgeiedmvkngviepirvgkqaiesateaaimilrid
dvia
>d1a6db2 3.7.5.2.1 (216-367) Thermosome {Thermoplasma acidophilum}
giivdkekvhpgmpdvvkdakialldapleikkpefdtnlriedpsmiqkflaqeenmlr
emvdkiksvganvvitqkgiddmaqhylsragiyavrrvkksdmdklakatgasivstid
eisssdlgtaerveqvkvgedymtfvtgcknp
>d1a6db3 4.46.1.2.1 (145-215,368-403) Thermosome {Thermoplasma acidophilum}
gadekalllkmaqtslnsksasvakdklaeisyeavksvaelrdgkyyvdfdniqvvkkq
ggaiddtqlinXkavsilvrgetehvvdemersitdslhvvasaledg
>d1a6ea1 1.119.1.2.1 (17-145,404-519) Thermosome {Thermoplasma acidophilum}
reqgknaqrnnieaakaiadavrttlgpkgmdkmlvdsigdiiisndgatilkemdvehp
takmivevskaqdtavgdgtttavvlsgellkqaetlldqgvhptvisngyrlavneark
iideiaeksXflwgggaveaelamrlakyansvggreqlaieafakaleiiprtlaenag
idpintliklkaddekgrisvgvdldnngvgdmkakgvvdplrvkthalesavevatmil
riddvi
>d1a6ea2 3.7.5.2.1 (215-367) Thermosome {Thermoplasma acidophilum}
gividkekvhskmpdvvknakialidsaleikkteieakvqisdpskiqdflnqetntfk
qmvekikksganvvlcqkgiddvaqhylakegiyavrrvkksdmeklakatgakivtdld
dltpsvlgeaetveerkigddrmtfvmgcknpk
>d1a6ea3 4.46.1.2.1 (146-214,368-403) Thermosome {Thermoplasma acidophilum}
tddatlrkialtalsgkntglsndfladlvvkavnavaevrdgktivdtanikvdkkngg
svndtqfisXavsilirggtdhvvseveralndairvvaitkedgk
>d1a6eb1 1.119.1.2.1 (20-144,404-521) Thermosome {Thermoplasma acidophilum}
kdamkenieaaiaisnsvrsslgprgmdkmlvdslgdivitndgvtilkemdvehpaakm
mvevsktqdsfvgdgtttaviiaggllqqaqglinqnvhptvisegyrmaseeakrvide
istkiXayaagggataaeiafrlrsyaqkiggrqqlaiekfadaieeipralaenagldp
idillklraehakgnktyginvftgeiedmvkngviepirvgkqaiesateaaimilrid
dvia
>d1a6eb2 3.7.5.2.1 (216-367) Thermosome {Thermoplasma acidophilum}
giivdkekvhpgmpdvvkdakialldapleikkpefdtnlriedpsmiqkflaqeenmlr
emvdkiksvganvvitqkgiddmaqhylsragiyavrrvkksdmdklakatgasivstid
eisssdlgtaerveqvkvgedymtfvtgcknp
>d1a6eb3 4.46.1.2.1 (145-215,368-403) Thermosome {Thermoplasma acidophilum}
gadekalllkmaqtslnsksasvakdklaeisyeavksvaelrdgkyyvdfdniqvvkkq
ggaiddtqlinXkavsilvrgetehvvdemersitdslhvvasaledg
>d1a6f__ 4.12.1.2.1 RNase P protein {Bacillus subtilis}
ahlkkrnrlkknedfqkvfkhgtsvanrqfvlytldqpendelrvglsvskkignavmrn
rikrlirqafleekerlkekdyiiiarkpasqltyeetkkslqhlfrksslyk
>d1a6g__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gnfgadaqgamnkalelfrkdiaakykelgy
>d1a6i_1 1.37.1.1.1 (2-67) Tetracyclin repressor (Tet-repressor, TetR), N-terminal domain {Escherichia coli}
srldkskvinsalellnevgieglttrklaqklgveqptlywhvknkralldalaveila
rhhdys
>d1a6i_2 1.113.1.1.1 (68-208) Tetracyclin repressor (Tet-repressor, TetR), C-terminal domain {Escherichia coli}
lpaageswqsflrnnamsfrrallryrdgakvhlgtrpdekqydtvetqlrfmtengfsl
rdglyaisavshftlgavleqqehtaaltdrpaapdenlppllrealqimdsddgeqafl
hgleslirgfevqltallqiv
>d1a6ja_ 4.88.1.1.1 Nitrogen regulatory bacterial protein IIa-ntr {Escherichia coli}
lqlssvlnrectrsrvhcqskkraleiiselaakqlslppqvvfeailtrekmgstgign
giaiphgkleedtlravgvfvqletpiafdaidnqpvdllfallvpadqtkthlhtlslv
akrladkticrrlraaqsdeelyqiitdte
>d1a6jb_ 4.88.1.1.1 Nitrogen regulatory bacterial protein IIa-ntr {Escherichia coli}
mtnndttlqlssvlnrectrsrvhcqskkraleiiselaakqlslppqvvfeailtrekm
gstgigngiaiphgkleedtlravgvfvqletpiafdaidnqpvdllfallvpadqtkth
lhtlslvakrladkticrrlraaqsdeelyqiitdte
>d1a6k__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgy
>d1a6l__ 4.47.1.2.1 Ferredoxin {Azotobacter vinelandii}
afvvtdncikckycdcvevcpvdcfyegpnflvihpdecidcalcepecpaqaifsedev
pedmqefiqlnaelaevwpnitekkdplpdaedwdgvkgklqhler
>d1a6m__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgy
>d1a6n__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgy
>d1a6o__ 4.117.1.1.18 Protein kiase CK2, alpha subunit {Maize (Zea mays)}
skarvyadvnvlrpkeywdyealtvqwgeqddyevvrkvgrgkysevfeginvnnnekci
ikilkpvkkkkikreikilqnlcggpnivklldivrdqhsktpslifeyvnntdfkvlyp
tltdydiryyiyellkaldychsqgimhrdvkphnvmidhelrklrlidwglaefyhpgk
eynvrvasryfkgpellvdlqdydysldmwslgcmfagmifrkepffyghdnhdqlvkia
kvlgtdglnvylnkyrieldpqlealvgrhsrkpwlkfmnadnqhlvspeaidfldkllr
ydhqerltaleamthpyfqqvraaens
>d1a6pa_ 2.1.1.1.8 CD2, first domain {Rat (Rattus rattus)}
gtvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlki
knltrddsgtynvtvystngtrildkaldlrile
>d1a6pb_ 2.1.1.1.8 CD2, first domain {Rat (Rattus rattus)}
gtvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlki
knltrddsgtynvtvystngtrildkaldlrile
>d1a6q__ 4.129.1.1.1 Protein serine/threonine phosphatase 2C {Human (Homo sapiens)}
gafldkpkmekhnaqgqgnglryglssmqgwrvemedahtaviglpsgleswsffavydg
hagsqvakyccehlldhitnnqdfkgsagapsvenvkngirtgfleidehmrvmsekkhg
adrsgstavgvlispqhtyfincgdsrgllcrnrkvhfftqdhkpsnplekeriqnaggs
vmiqrvngslavsralgdfdykcvhgkgpteqlvspepevhdierseeddqfiilacdgi
wdvmgneelcdfvrsrlevtddlekvcnevvdtclykgsrdnmsvilicfpnapkvspea
vkkeaeldkylecrveeiikkqgegvpdlvhvmrtlasenipslppggelaskrnvieav
ynrlnpy
>d1a6r__ 4.3.1.1.8 Bleomycin hydrolase, Gal6 {Baker's yeast (Saccharomyces cerevisiae)}
afqgamassidiskinswnkefqsdlthqlattvlknynaddallnktrlqkqdnrvfnt
vvstdstpvtnqkssgrawlfaatnqlrlnvlselnlkefelsqaylffydklekanyfl
dqivssadqdidsrlvqyllaaptedggqysmflnlvkkyglipkdlygdlpysttasrk
wnsllttklrefaetlrtalkersaddsiivtlreqmqreifrlmslfmdippvqpneqf
tweyvdkdkkihtikstplefaskyakldpstpvslindprhpygklikidrlgnvlggd
aviylnvdnetlsklvvkrlqnnkavffgshtpkfmdkktgvmdielwnypaigynlpqq
kasriryheslmthamlitgchvdetsklplryrvenswgkdsgkdglyvmtqkyfeeyc
fqivvdinelpkelaskftsgkeepivlpiwdpmgalak
>d1a6s__ 1.62.1.4.1 GAG polyprotein M-domain {Rous sarcoma virus, RSV}
geavikvissacktycgktspskkeigamlsllqkegllmspsdlyspgswdpitaalsq
ramilgksgelktwglvlgalkaaree
>d1a6ta1 2.1.1.1.107 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab Mab1-IA (mouse), kappa L chain}
qsvlsqspailsaspgekvimtcspsssvsymqwyqqkpgsspkpwiystsnlasgvpgr
fsgggsgtsfsltisgveaedaatyycqqysshpltfgggtklelk
>d1a6ta2 2.1.1.2.107 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab Mab1-IA (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1a6tb1 2.1.1.1.107 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab Mab1-IA (mouse), kappa L chain}
evqlqqsgpdlvkpgasvkisckasgysfstyymhwvkqshgkslewigrvdpdnggtsf
nqkfkgkailtvdkssstaymelgsltsedsavyycarrddyyfdfwgqgtsltvss
>d1a6tb2 2.1.1.2.107 (114-213) Immunoglobulin (constant domains of L and H chains) {Fab Mab1-IA (mouse), kappa L chain}
akttppsvyplapvcggttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsg
lytlsssvtvtsstwpsqtitcnvahpasstkvdkkiepr
>d1a6tc1 2.1.1.1.107 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab Mab1-IA (mouse), kappa L chain}
qsvlsqspailsaspgekvimtcspsssvsymqwyqqkpgsspkpwiystsnlasgvpgr
fsgggsgtsfsltisgveaedaatyycqqysshpltfgggtklelk
>d1a6tc2 2.1.1.2.107 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab Mab1-IA (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1a6td1 2.1.1.1.107 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab Mab1-IA (mouse), kappa L chain}
evqlqqsgpdlvkpgasvkisckasgysfstyymhwvkqshgkslewigrvdpdnggtsf
nqkfkgkailtvdkssstaymelgsltsedsavyycarrddyyfdfwgqgtsltvss
>d1a6td2 2.1.1.2.107 (114-213) Immunoglobulin (constant domains of L and H chains) {Fab Mab1-IA (mouse), kappa L chain}
akttppsvyplapvcggttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsg
lytlsssvtvtsstwpsqtitcnvahpasstkvdkkiepr
>d1a6uh_ 2.1.1.1.108 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
qvqlqqpgaelvkpgasvklsckasgytftsywmhwvkqrpgrglewigridpnsggtky
nekfkskatltvdkpsstaymqlssltsedsavyycarydyygssyfdywgqgttvtvss
>d1a6ul_ 2.1.1.1.108 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
avvtqesalttspgetvtltcrsstgavttsnyanwvqekpdhlftgliggtnnrapgvp
arfsgslignkaaltitgaqtedeaiyfcalwysnhwvfgggtkltvl
>d1a6vh_ 2.1.1.1.108 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
qvqlqqpgaelvkpgasvklsckasgytftsywmhwvkqrpgrglewigridpnsggtky
nekfkskatltvdkpsstaymqlssltsedsavyycarydyygssyfdywgqgttvtv
>d1a6vi_ 2.1.1.1.108 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
qvqlqqpgaelvkpgasvklsckasgytftsywmhwvkqrpgrglewigridpnsggtky
nekfkskatltvdkpsstaymqlssltsedsavyycarydyygssyfdywgqgttvtvs
>d1a6vj_ 2.1.1.1.108 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
qvqlqqpgaelvkpgasvklsckasgytftsywmhwvkqrpgrglewigridpnsggtky
nekfkskatltvdkpsstaymqlssltsedsavyycarydyygssyfdywgqgttvtvss
>d1a6vl_ 2.1.1.1.108 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
qavvtqesalttspgetvtltcrsstgavttsnyanwvqekpdhlftgliggtnnrapgv
parfsgslignkaaltitgaqtedeaiyfcalwysnhwvfgggtkltvle
>d1a6vm_ 2.1.1.1.108 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
qavvtqesalttspgetvtltcrsstgavttsnyanwvqekpdhlftgliggtnnrapgv
parfsgslignkaaltitgaqtedeaiyfcalwysnhwvfgggtkltvl
>d1a6vn_ 2.1.1.1.108 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
qavvtqesalttspgetvtltcrsstgavttsnyanwvqekpdhlftgliggtnnrapgv
parfsgslignkaaltitgaqtedeaiyfcalwysnhwvfgggtkltvl
>d1a6wh_ 2.1.1.1.108 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
qvqlqqpgaelvkpgasvklsckasgytftsywmhwvkqrpgrglewigridpnsggtky
nekfkskatltvdkpsstaymqlssltsedsavyycarydyygssyfdywgqgttvtvss
>d1a6wl_ 2.1.1.1.108 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
avvtqesalttspgetvtltcrsstgavttsnyanwvqekpdhlftgliggtnnrapgvp
arfsgslignkaaltitgaqtedeaiyfcalwysnhwvfgggtkltvle
>d1a6x__ 2.74.1.1.1 Biotinyl domain of acetyl-CoA carboxylase {Escherichia coli}
meapaaaeisghivrspmvgtfyrtpspdakafievgqkvnvgdtlciveamkmmnqiea
dksgtvkailvesgqpvefdeplvvie
>d1a6ya_ 7.33.1.2.7 Orphan nuclear receptor reverb {Human (Homo sapiens)}
llckvcgdvasgfhygvhacegckgffrrsiqqniqykrclknencsivrinrnrcqqcr
fkkclsvgmsrdavrfgr
>d1a6yb_ 7.33.1.2.7 Orphan nuclear receptor reverb {Human (Homo sapiens)}
gmvllckvcgdvasgfhygvhacegckgffrrsiqqniqykrclknencsivrinrnrcq
qcrfkkclsvgmsrdavrfgripk
>d1a6za1 2.1.1.2.12 (182-275) Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), hemochromatosis protein Hfe}
qqvpplvkvthhvtssvttlrcralnyypqnitmkwlkdkqpmdakefepkdvlpngdgt
yqgwitlavppgeeqrytcqvehpgldqpliviw
>d1a6za2 4.17.1.1.19 (4-181) MHC class I, alpha-1 and alpha-2 domains {Human (Homo sapiens), hemochromatosis protein Hfe}
rshslhylfmgaseqdlglslfealgyvddqlfvfydhesrrveprtpwvssrissqmwl
qlsqslkgwdhmftvdfwtimenhnhskeshtlqvilgcemqednstegywkygydgqdh
lefcpdtldwraaeprawptklewerhkirarqnraylerdcpaqlqqllelgrgvld
>d1a6zb1 2.1.1.2.12 Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), hemochromatosis protein Hfe}
iqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskdw
sfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1a6zc1 2.1.1.2.12 (182-275) Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), hemochromatosis protein Hfe}
qqvpplvkvthhvtssvttlrcralnyypqnitmkwlkdkqpmdakefepkdvlpngdgt
yqgwitlavppgeeqrytcqvehpgldqpliviw
>d1a6zc2 4.17.1.1.19 (4-181) MHC class I, alpha-1 and alpha-2 domains {Human (Homo sapiens), hemochromatosis protein Hfe}
rshslhylfmgaseqdlglslfealgyvddqlfvfydhesrrveprtpwvssrissqmwl
qlsqslkgwdhmftvdfwtimenhnhskeshtlqvilgcemqednstegywkygydgqdh
lefcpdtldwraaeprawptklewerhkirarqnraylerdcpaqlqqllelgrgvld
>d1a6zd1 2.1.1.2.12 Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), hemochromatosis protein Hfe}
iqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskdw
sfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1a70__ 4.13.6.1.10 2Fe-2S ferredoxin {Spinach (Spinacia oleracea)}
aaykvtlvtptgnvefqcpddvyildaaeeegidlpyscragscsscagklktgslnqdd
qsfldddqidegwvltcaaypvsdvtiethkkeelta
>d1a71a1 2.31.1.2.1 (1-174,325-374) Alcohol dehydrogenase {Horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplwtpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1a71a2 3.2.1.1.1 (175-324) Alcohol dehydrogenase {Horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggaglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1a71b1 2.31.1.2.1 (1-174,325-374) Alcohol dehydrogenase {Horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplwtpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1a71b2 3.2.1.1.1 (175-324) Alcohol dehydrogenase {Horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggaglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1a72_1 2.31.1.2.1 (1-174,325-374) Alcohol dehydrogenase {Horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplwtpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1a72_2 3.2.1.1.1 (175-324) Alcohol dehydrogenase {Horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggaglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1a73a_ 4.4.1.3.1 Intron-encoded homing endonuclease I-PpoI {Slime mold (Physarum polycephalum)}
altnaqilavidsweetvgqfpvithhvplggglqgtlhcyeiplaapygvgfakngptr
wqykrtinqvvhrwgshtvpfllepdningktctashlchntrchnplhlcweslddnkg
rnwcpgpnggcvhavvclrqgplygpgatvagpqqrgshfvv
>d1a73b_ 4.4.1.3.1 Intron-encoded homing endonuclease I-PpoI {Slime mold (Physarum polycephalum)}
altnaqilavidsweetvgqfpvithhvplggglqgtlhcyeiplaapygvgfakngptr
wqykrtinqvvhrwgshtvpfllepdningktctashlchntrchnplhlcweslddnkg
rnwcpgpnggcvhavvclrqgplygpgatvagpqqrgshfvv
>d1a74a_ 4.4.1.3.1 Intron-encoded homing endonuclease I-PpoI {Slime mold (Physarum polycephalum)}
altnaqilavidsweetvgqfpvithhvplggglqgtlhcyeiplaapygvgfakngptr
wqykrtinqvvhrwgshtvpfllepdningktctashlchntrchnplhlcweslddnkg
rnwcpgpnggcvhavvclrqgplygpgatvagpqqrgshfvv
>d1a74b_ 4.4.1.3.1 Intron-encoded homing endonuclease I-PpoI {Slime mold (Physarum polycephalum)}
altnaqilavidsweetvgqfpvithhvplggglqgtlhcyeiplaapygvgfakngptr
wqykrtinqvvhrwgshtvpfllepdningktctashlchntrchnplhlcweslddnkg
rnwcpgpnggcvhavvclrqgplygpgatvagpqqrgshfvv
>d1a75a_ 1.42.1.4.5 Parvalbumin {Whiting (Merlangius merlangus)}
agiladadcaaavkaceaadsfsykaffakcglsgksaddikkafvfidqdksgfieede
lklflqvfkagaraltdaetkaflkagdsdgdgaigveewvalvka
>d1a75b_ 1.42.1.4.5 Parvalbumin {Whiting (Merlangius merlangus)}
afagiladadcaaavkaceaadsfsykaffakcglsgksaddikkafvfidqdksgfiee
delklflqvfkagaraltdaetkaflkagdsdgdgaigveewvalvka
>d1a76_1 1.61.3.1.4 (209-316) Flap endonuclease-1 from methanococcus jannaschii {Methanococcus jannaschii}
islddlidiaifmgtdynpggvkgigfkrayelvrsgvakdvlkkeveyydeikrifkep
kvtdnyslslklpdkegiikflvdendfnydrvkkhvdklynliankt
>d1a76_2 3.44.1.2.4 (2-208) Flap endonuclease-1 from methanococcus jannaschii {Methanococcus jannaschii}
gvqfgdfipkniisfedlkgkkvaidgmnalyqfltsirlrdgsplrnrkgeitsayngv
fyktihllenditpiwvfdgeppklkektrkvrremkekaelkmkeaikkedfeeaakya
krvsyltpkmvenckyllslmgipyveapsegeaqasymakkgdvwavvsqdydallyga
prvvrnltttkempelielnevledlr
>d1a77_1 1.61.3.1.4 (209-316) Flap endonuclease-1 from methanococcus jannaschii {Methanococcus jannaschii}
islddlidiaifmgtdynpggvkgigfkrayelvrsgvakdvlkkeveyydeikrifkep
kvtdnyslslklpdkegiikflvdendfnydrvkkhvdklynliankt
>d1a77_2 3.44.1.2.4 (2-208) Flap endonuclease-1 from methanococcus jannaschii {Methanococcus jannaschii}
gvqfgdfipkniisfedlkgkkvaidgmnalyqfltsirlrdgsplrnrkgeitsayngv
fyktihllenditpiwvfdgeppklkektrkvrremkekaelkmkeaikkedfeeaakya
krvsyltpkmvenckyllslmgipyveapsegeaqasymakkgdvwavvsqdydallyga
prvvrnltttkempelielnevledlr
>d1a78a_ 2.26.1.3.3 S-lectin, different isoforms {Toad (Bufo arenarum)}
asagvavtnlnlkpghcveikgsippdckgfavnlgedasnfllhfnarfdlhgdvnkiv
cnskeadawgseqreevfpfqqgaevmvcfeyqtqkiiikfssgdqfsfpvrkvlpsipf
lsleglafksitte
>d1a78b_ 2.26.1.3.3 S-lectin, different isoforms {Toad (Bufo arenarum)}
asagvavtnlnlkpghcveikgsippdckgfavnlgedasnfllhfnarfdlhgdvnkiv
cnskeadawgseqreevfpfqqgaevmvcfeyqtqkiiikfssgdqfsfpvrkvlpsipf
lsleglafksitte
>d1a79a1 3.43.2.1.1 (83-179) tRNA splicing endonuclease, C-terminal domain {Methanococcus jannaschii}
erlclkylvykdlrtrgyivktglkygadfrlyerganidkehsvylvkvfpedssflls
eltgfvrvahsvrkklliaivdadgdivyynmtyvkp
>d1a79a2 4.57.1.1.1 (9-82) tRNA splicing endonuclease, N-terminal domain {Methanococcus jannaschii}
kitglldgdrvivfdkngisklsarhygnvegnflslslvealylinlgwlevkykdnkp
lsfeelyeyarnve
>d1a79b1 3.43.2.1.1 (83-179) tRNA splicing endonuclease, C-terminal domain {Methanococcus jannaschii}
erlclkylvykdlrtrgyivktglkygadfrlyerganidkehsvylvkvfpedssflls
eltgfvrvahsvrkklliaivdadgdivyynmtyvkp
>d1a79b2 4.57.1.1.1 (9-82) tRNA splicing endonuclease, N-terminal domain {Methanococcus jannaschii}
kitglldgdrvivfdkngisklsarhygnvegnflslslvealylinlgwlevkykdnkp
lsfeelyeyarnve
>d1a79c1 3.43.2.1.1 (83-179) tRNA splicing endonuclease, C-terminal domain {Methanococcus jannaschii}
erlclkylvykdlrtrgyivktglkygadfrlyerganidkehsvylvkvfpedssflls
eltgfvrvahsvrkklliaivdadgdivyynmtyvkp
>d1a79c2 4.57.1.1.1 (9-82) tRNA splicing endonuclease, N-terminal domain {Methanococcus jannaschii}
kitglldgdrvivfdkngisklsarhygnvegnflslslvealylinlgwlevkykdnkp
lsfeelyeyarnve
>d1a79d1 3.43.2.1.1 (83-179) tRNA splicing endonuclease, C-terminal domain {Methanococcus jannaschii}
erlclkylvykdlrtrgyivktglkygadfrlyerganidkehsvylvkvfpedssflls
eltgfvrvahsvrkklliaivdadgdivyynmtyvkp
>d1a79d2 4.57.1.1.1 (9-82) tRNA splicing endonuclease, N-terminal domain {Methanococcus jannaschii}
kitglldgdrvivfdkngisklsarhygnvegnflslslvealylinlgwlevkykdnkp
lsfeelyeyarnve
>d1a7aa1 3.2.1.4.8 (190-352) S-adenosylhomocystein hydrolase {Human (Homo sapiens)}
dnlygcreslidgikratdvxiagkvavvagygdvgkgcaqalrgfgarviiteidpina
lqaaxegyevttxdeacqegnifvtttgcidiilgrhfeqxkddaivcnighfdveidvk
wlnenavekvnikpqvdryrlkngrriillaegrlvnlgcaxg
>d1a7aa2 3.16.9.3.1 (2-189,353-432) S-adenosylhomocystein hydrolase {Human (Homo sapiens)}
sdklpykvadiglaawgrkaldiaenexpglxrxrerysaskplkgariagclhxtveta
vlietlvtlgaevqwsscnifstqnhaaaaiakagipvyawkgetdeeylwcieqtlyfk
dgplnxilddggdltnlihtkypqllpgirgiseetttgvhnlykxxangilkvpainvn
dsvtkskfXhpsfvxsnsftnqvxaqielwthpdkypvgvhflpkkldeavaeahlgkln
vkltkltekqaqylgxscdgpfkpdhyry
>d1a7ab1 3.2.1.4.8 (190-352) S-adenosylhomocystein hydrolase {Human (Homo sapiens)}
dnlygcreslidgikratdvxiagkvavvagygdvgkgcaqalrgfgarviiteidpina
lqaaxegyevttxdeacqegnifvtttgcidiilgrhfeqxkddaivcnighfdveidvk
wlnenavekvnikpqvdryrlkngrriillaegrlvnlgcaxg
>d1a7ab2 3.16.9.3.1 (3-189,353-432) S-adenosylhomocystein hydrolase {Human (Homo sapiens)}
dklpykvadiglaawgrkaldiaenexpglxrxrerysaskplkgariagclhxtvetav
lietlvtlgaevqwsscnifstqnhaaaaiakagipvyawkgetdeeylwcieqtlyfkd
gplnxilddggdltnlihtkypqllpgirgiseetttgvhnlykxxangilkvpainvnd
svtkskfXhpsfvxsnsftnqvxaqielwthpdkypvgvhflpkkldeavaeahlgklnv
kltkltekqaqylgxscdgpfkpdhyry
>d1a7ba_ 2.1.1.1.8 CD2, first domain {Rat (Rattus rattus)}
tvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlkik
nltrddsgtynvtvystngtrildkaldlrile
>d1a7bb_ 2.1.1.1.8 CD2, first domain {Rat (Rattus rattus)}
tvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlkik
nltrddsgtynvtvystngtrildkaldlrile
>d1a7bc_ 2.1.1.1.8 CD2, first domain {Rat (Rattus rattus)}
tvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlkik
nltrddsgtynvtvystngtrildkaldlrile
>d1a7bd_ 2.1.1.1.8 CD2, first domain {Rat (Rattus rattus)}
tvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlkik
nltrddsgtynvtvystngtrildkaldlrile
>d1a7ca_ 5.1.1.1.7 Plasminogen activator inhibitor-1 {Human (Homo sapiens)}
hhppsyvahlasdfgvrvfqqvaqaskdrnvvfspygvasvlamlqlttggetqqqiqaa
mgfkiddkgmapalrhlykelmgpwnkdeisttdaifvqrdlklvqgfmphffrlfrstv
kqvdfseverarfiindwvkthtkgmisnllgkgavdqltrlvlvnalyfngqwktpfpd
ssthrrlfhksdgstvsvpmmaqtnkfnytefttpdghyydilelpyhgdtlsmfiaapy
ekevplsaltnilsaqlishwkgnmtrlprllvlpkfsletevdlrkplenlgmtdmfrq
fqadftslsdqeplhvaqalqkvkievnesgtvessstavivsarmapeeiimdrpflfv
vrhnptgtvlfmgqvmep
>d1a7d__ 1.25.4.1.3 Myohemerythin {Sipunculan worm (Themiste zostericola)}
gweipepyvwdesfrvfyeqldeehkkifkgifdcirdnsapnlatlvkvttnhftheea
mmdaakysevvphkkmhkdflekigglsapvdaknvdyckewlvnhikgtdfkykgkl
>d1a7e__ 1.25.4.1.3 Myohemerythin {Sipunculan worm (Themiste zostericola)}
gweipepyvwdesfrvfyeqldeehkkifkgifdcirdnsapnlatlvkvttnhftheea
mmdaakysevvphkkmhkdflekigglsapvdaknvdyckewnvnhikgtdfkykgkl
>e1a7f.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1a7f.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealelvcgerggfytpk
>d1a7ge_ 4.47.8.1.2 Papillomavirus-1 E2 protein {Human papillomavirus-31}
attpiihlkgdanilkclryrlskykqlyeqvsstwhwtctdgkhknaivtltyistsqr
ddflntvvipntvsvstgymti
>d1a7ha_ 2.10.1.1.3 gamma-Crystallin {Bovine (Bos taurus), isoform S}
mykiqifekgdfngqmhettedcpsimeqfhmrevhsckvlegawifyelpnyrgrqyll
dkkeyrkpvdwgaaspavqsfrrive
>d1a7hb_ 2.10.1.1.3 gamma-Crystallin {Bovine (Bos taurus), isoform S}
mykiqifekgdfngqmhettedcpsimeqfhmrevhsckvlegawifyelpnyrgrqyll
dkkeyrkpvdwgaaspavqsfrrive
>d1a7i_1 7.33.1.3.2 (8-35) Cysteine-rich (intestinal) protein, CRP, CRIP {Japanese quail (Coturnix coturnix japonica), CRP2}
nkcgacgrtvyhaeevqcdgrsfhrccf
>d1a7i_2 7.33.1.3.2 (36-67) Cysteine-rich (intestinal) protein, CRP, CRIP {Japanese quail (Coturnix coturnix japonica), CRP2}
lcmvcrknldsttvaihdaevyckscygkkyg
>d1a7j__ 3.30.1.4.1 Phosphoribulokinase {Rhodobacter sphaeroides}
skkhpiisvtgssgagtstvkhtfdqifrregvkavsiegdafhrfnradmkaeldrrya
agdatfshfsyeanelkelervfreygetgqgrtrtyvhddaeaartgvapgnftdwrdf
dsdshllfyeglhgavvnsevniagladlkigvvpvinlewiqkihrdratrgytteavt
dvilrrmhayvhcivpqfsqtdinfqrvpvvdtsnpfiarwiptadesvvvirfrnprgi
dfpyltsmihgswmsransivvpgnkldlamqliltplidrvvreskv
>d1a7ka1 3.2.1.3.7 (1-165,335-358) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Leishmania mexicana}
apikvgingfgrigrmvfqaicdqgligteidvvavvdmstnaeyfayqmkhdtvhgrpk
ytveavksspsvetadvlvvnghrikcvkaqrnpadlpwgklgvdyviestglftdklka
eghikggakkvvisapasggaktivmgvnqheyspashhvvsnasXnewayshrvvdlvr
ymaakdaass
>d1a7ka2 4.61.1.1.7 (166-334) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Leishmania mexicana}
cttnclapivhvltkenfgietglmttihsytatqktvdgvslkdwrggraaavniipst
tgaakavgmvipstkgkltgmsfrvptpdvsvvdltfratrdtsiqeidkaikkaaqtym
kgilgftdeelvsadfindnrssvydskatlqnnlpgekrffkvvswyd
>d1a7kb1 3.2.1.3.7 (1-165,335-358) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Leishmania mexicana}
apikvgingfgrigrmvfqaicdqgligteidvvavvdmstnaeyfayqmkhdtvhgrpk
ytveavksspsvetadvlvvnghrikcvkaqrnpadlpwgklgvdyviestglftdklka
eghikggakkvvisapasggaktivmgvnqheyspashhvvsnasXnewayshrvvdlvr
ymaakdaass
>d1a7kb2 4.61.1.1.7 (166-334) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Leishmania mexicana}
cttnclapivhvltkenfgietglmttihsytatqktvdgvslkdwrggraaavniipst
tgaakavgmvipstkgkltgmsfrvptpdvsvvdltfratrdtsiqeidkaikkaaqtym
kgilgftdeelvsadfindnrssvydskatlqnnlpgekrffkvvswyd
>d1a7kc1 3.2.1.3.7 (1-165,335-358) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Leishmania mexicana}
apikvgingfgrigrmvfqaicdqgligteidvvavvdmstnaeyfayqmkhdtvhgrpk
ytveavksspsvetadvlvvnghrikcvkaqrnpadlpwgklgvdyviestglftdklka
eghikggakkvvisapasggaktivmgvnqheyspashhvvsnasXnewayshrvvdlvr
ymaakdaass
>d1a7kc2 4.61.1.1.7 (166-334) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Leishmania mexicana}
cttnclapivhvltkenfgietglmttihsytatqktvdgvslkdwrggraaavniipst
tgaakavgmvipstkgkltgmsfrvptpdvsvvdltfratrdtsiqeidkaikkaaqtym
kgilgftdeelvsadfindnrssvydskatlqnnlpgekrffkvvswyd
>d1a7kd1 3.2.1.3.7 (1-165,335-358) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Leishmania mexicana}
apikvgingfgrigrmvfqaicdqgligteidvvavvdmstnaeyfayqmkhdtvhgrpk
ytveavksspsvetadvlvvnghrikcvkaqrnpadlpwgklgvdyviestglftdklka
eghikggakkvvisapasggaktivmgvnqheyspashhvvsnasXnewayshrvvdlvr
ymaakdaass
>d1a7kd2 4.61.1.1.7 (166-334) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Leishmania mexicana}
cttnclapivhvltkenfgietglmttihsytatqktvdgvslkdwrggraaavniipst
tgaakavgmvipstkgkltgmsfrvptpdvsvvdltfratrdtsiqeidkaikkaaqtym
kgilgftdeelvsadfindnrssvydskatlqnnlpgekrffkvvswyd
>d1a7la_ 3.84.1.1.6 D-maltodextrin-binding protein, MBP {Escherichia coli}
egklviwingdkgynglaevgkkfekdtgikvtvehpdkleekfpqvaatgdgpdiifwa
hdrfggyaqsgllaeitpdkafqdklypftwdavryngkliaypiavealsliynkdllp
nppktweeipaldkelkakgksalmfnlqepyftwpliaadggyafkyengkydikdvgv
dnagakagltflvdliknkhmnadtdysiaeaafnkgetamtingpwawsnidtskvnyg
vtvlptfkgqpskpfvgvlsaginaaspnkelakeflenylltdegleavnkdkplgava
lksyeeelakdpriaatmenaqkgeimpnipqmsafwyavrtavinaasgrqtvdealkd
gsqdprvrglyfpaggsecc
>d1a7lb_ 3.84.1.1.6 D-maltodextrin-binding protein, MBP {Escherichia coli}
egklviwingdkgynglaevgkkfekdtgikvtvehpdkleekfpqvaatgdgpdiifwa
hdrfggyaqsgllaeitpdkafqdklypftwdavryngkliaypiavealsliynkdllp
nppktweeipaldkelkakgksalmfnlqepyftwpliaadggyafkyengkydikdvgv
dnagakagltflvdliknkhmnadtdysiaeaafnkgetamtingpwawsnidtskvnyg
vtvlptfkgqpskpfvgvlsaginaaspnkelakeflenylltdegleavnkdkplgava
lksyeeelakdpriaatmenaqkgeimpnipqmsafwyavrtavinaasgrqtvdealkd
gsqdprvrglyf
>d1a7lc_ 3.84.1.1.6 D-maltodextrin-binding protein, MBP {Escherichia coli}
egklviwingdkgynglaevgkkfekdtgikvtvehpdkleekfpqvaatgdgpdiifwa
hdrfggyaqsgllaeitpdkafqdklypftwdavryngkliaypiavealsliynkdllp
nppktweeipaldkelkakgksalmfnlqepyftwpliaadggyafkyengkydikdvgv
dnagakagltflvdliknkhmnadtdysiaeaafnkgetamtingpwawsnidtskvnyg
vtvlptfkgqpskpfvgvlsaginaaspnkelakeflenylltdegleavnkdkplgava
lksyeeelakdpriaatmenaqkgeimpnipqmsafwyavrtavinaasgrqtvdealkd
gs
>d1a7m__ 1.27.1.1.5 Leukemia inhibitory factor (LIF) {Mouse (Mus musculus)}
splpitpvnatcairhpchgnlmnqiknqlaqlngsanalfisyytaqgepfpnnldklc
gpnvtdfppfhangtekaklvelyrmvaylsasltnitrdqkvlnpsavslhsklnatid
vmrgllsnvlcrlcnkyrvghvdvppvpdhsdkevfqkkklgcqllgtykqvisvvvqaf
>d1a7nh_ 2.1.1.1.42 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
qvqlqesgpglvapsqslsitctvsgfsltgygvnwvrqppgkglewlgmiwgdgntdyn
salksrlsiskdnsksqvflkmnslhtddtaryycarerdyrldywgqgttvtvss
>d1a7nl_ 2.1.1.1.42 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
divltqspaslsasvgetvtitcrasgnihnylawyqqkqgkspqllvyytttladgvps
rfsgsgsgtqyslkinslqpddfgsyycqhfwstprtfgggtkleik
>d1a7oh_ 2.1.1.1.42 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
qvqlqesgpglvapsqslsitctvsgfsltgygvnwvrqppgkglewlgmiwgdgntdyn
salksrlsiskdnsksqvflkmnslhtddtaryycarerdyrldywgqgttvtvss
>d1a7ol_ 2.1.1.1.42 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
divltqspaslsasvgetvtitcrasgnihnylawyqqkqgkspqllvyytttladgvps
rfsgsgsgtqyslkinslqpddfgsyycqhfwstptfgggtkleik
>d1a7ph_ 2.1.1.1.42 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
qvqlqesgpglvapsqslsitctvsgfsltgygvnwvrqppgkglewlgmiwgdgntdyn
salksrlsiskdnsksqvflkmnslhtddtaryycarerdyrldywgqgttvtvss
>d1a7pl_ 2.1.1.1.42 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
divltqspaslsasvgetvtitcrasgnihnylawyqqkqgkspqllvyytttladgvps
rfsgsgsgtqyslkinslqpddfgsyycqhfwstsrtfgggtkleik
>d1a7qh_ 2.1.1.1.42 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
qvqlqesgpglvapsqslsitctvsgfsltgygvnwvrqlpgkglewlgmiwgdgntayn
salksrlsiskdnsksqvflemdslhtddtaryycarerdyrldywgqgttvtvss
>d1a7ql_ 2.1.1.1.42 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
divltqspaslsasvgetvtitcraggnthnylawyqqkqgkspqllvyytttlaagvps
rfsgsgsgtqyslkinslqpddfgsyycqhfwstprsfgggtklei
>d1a7rh_ 2.1.1.1.42 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
qvqlqesgpglvapsqslsitctvsgfsltgygvnwvrqppgkglewlgmiwgdgntdyn
salksrlsiskdnsksqvflkmnslhtddtaryycarerdyrldywgqgttltvss
>d1a7rl_ 2.1.1.1.42 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
divltqspaslsasvgetvtitcrasgnihnylawyqqkqgkspqllvyytttladgvps
rfsgsgsgtqyslkinslqpddfgsyycqhfwstprtfgggtkleik
>d1a7s__ 2.41.1.2.18 Heparin binding protein, HBP {Human (Homo sapiens)}
ivggrkarprqfpflasiqnqgrhfcggaliharfvmtaascfpgvstvvlgaydlrrre
rqsrqtfsissmsengydpqqnlndlmllqldreanltssvtilplplqnatveagtrcq
vagwgsqrsggrlsrfprfvnvtvtpedqcrpnnvctgvltrrggicngdggtplvcegl
ahgvasfslgpcgrgpdfftrvalfrdwidgvlnnpgpgpa
>d1a7ta_ 4.128.1.1.2 Zn metallo-beta-lactamase {Bacteroides fragilis}
svkisddisitqlsdkvytyvslaeiegwgmvpsngmivinnhqaalldtpindaqteml
vnwvtdslhakvttfipnhwhgdcigglgylqrkgvqsyanqmtidlakekglpvpehgf
tdsltvsldgmplqcyylggghatdnivvwlptenilfggcmlkdnqttsignisdadvt
awpktldkvkakfpsaryvvpghgnyggteliehtkqivnqyiests
>d1a7tb_ 4.128.1.1.2 Zn metallo-beta-lactamase {Bacteroides fragilis}
svkisddisitqlsdkvytyvslaeiegwgmvpsngmivinnhqaalldtpindaqteml
vnwvtdslhakvttfipnhwhgdcigglgylqrkgvqsyanqmtidlakekglpvpehgf
tdsltvsldgmplqcyylggghatdnivvwlptenilfggcmlkdnqttsignisdadvt
awpktldkvkakfpsaryvvpghgnyggteliehtkqivnqyiests
>d1a7ua_ 3.59.1.10.3 Chloroperoxidase T {Streptomyces aureofaciens}
pfitvgqenstsidlyyedhgagqpvvlihgfplsghswerqsaalldagyrvitydrrg
fgqssqpttgydydtfaadlntvletldlqdavlvgfsmgtgevaryvssygtariakva
flaslepfllktddnpdgaapkeffdgivaavkadryafytgffndfynldenlgtrise
eavrnswntaasggffaaaaapttwytdfradipridvpalilhgtgdrtlpientarvf
hkalpsaeyvevegaphgllwthaeevntallaflak
>d1a7ub_ 3.59.1.10.3 Chloroperoxidase T {Streptomyces aureofaciens}
pfitvgqenstsidlyyedhgagqpvvlihgfplsghswerqsaalldagyrvitydrrg
fgqssqpttgydydtfaadlntvletldlqdavlvgfsmgtgevaryvssygtariakva
flaslepfllktddnpdgaapkeffdgivaavkadryafytgffndfynldenlgtrise
eavrnswntaasggffaaaaapttwytdfradipridvpalilhgtgdrtlpientarvf
hkalpsaeyvevegaphgllwthaeevntallaflak
>d1a7va_ 1.25.3.2.7 Cytochrome c' {Rhodopseudomonas palustris}
qtdviaqrkailkqmgeatkpiaamlkgeakfdqavvqkslaaiaddskklpalfpadsk
tggdtaalpkiwedkakfddlfaklaaaataaqgtikdeaslkaniggvlgnckschddf
rakks
>d1a7vb_ 1.25.3.2.7 Cytochrome c' {Rhodopseudomonas palustris}
qtdviaqrkailkqmgeatkpiaamlkgeakfdqavvqkslaaiaddskklpalfpadsk
tggdtaalpkiwedkakfddlfaklaaaataaqgtikdeaslkaniggvlgnckschddf
rakks
>d1a7w__ 1.23.1.2.2 Histone B {Methanothermus fervidus}
melpiapigriikdagaervsddaritlakileemgrdiaseaiklarhagrktikaedi
elavrrfk
>d1a7xa_ 4.23.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1a7xb_ 4.23.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1a80__ 3.1.6.1.6 2,5-diketo-D-gluconic acid reductase A {Corynebacterium}
tvpsivlndgnsipqlgygvfkvppadtqraveealevgyrhidtaaiygneegvgaaia
asgiarddlfittklwndrhdgdepaaaiaeslaklaldqvdlylvhwptpaadnyvhaw
ekmielraagltrsigvsnhlvphlerivaatgvvpavnqielhpayqqreitdwaaahd
vkieswgplgqgkydlfgaepvtaaaaahgktpaqavlrwhlqkgfvvfpksvrrerlee
nldvfdfdltdteiaaidamdpgdgsgrvsahpdevd
>d1a81a_ 4.72.1.1.13 Syk tyrosine kinase {Human (Homo sapiens)}
sanhlpfffgnitreeaedylvqggmsdglyllrqsrnylggfalsvahgrkahhytier
elngtyaiaggrthaspadlchyhsqesdglvcllkkpfnrpqgvqpktgpfedlkenli
reyvkqtwnlqgqaleqaiisqkpqlekliattahekmpwfhgkisreeseqivligskt
ngkflirardnngsyalcllhegkvlhyridkdktgklsipegkkfdtlwqlvehysyka
dgllrvltvpcqki
>d1a81c_ 4.72.1.1.13 Syk tyrosine kinase {Human (Homo sapiens)}
sanhlpfffgnitreeaedylvqggmsdglyllrqsrnylggfalsvahgrkahhytier
elngtyaiaggrthaspadlchyhsqesdglvcllkkpfnrpqgvqpktgpfedlkenli
reyvkqtwnlqgqaleqaiisqkpqlekliattahekmpwfhgkisreeseqivligskt
ngkflirardnngsyalcllhegkvlhyridkdktgklsipegkkfdtlwqlvehysyka
dgllrvltvpcqki
>d1a81e_ 4.72.1.1.13 Syk tyrosine kinase {Human (Homo sapiens)}
sanhlpfffgnitreeaedylvqggmsdglyllrqsrnylggfalsvahgrkahhytier
elngtyaiaggrthaspadlchyhsqesdglvcllkkpfnrpqgvqpktgpfedlkenli
reyvkqtwnlqgqaleqaiisqkpqlekliattahekmpwfhgkisreeseqivligskt
ngkflirardnngsyalcllhegkvlhyridkdktgklsipegkkfdtlwqlvehysyka
dgllrvltvpcqki
>d1a81g_ 4.72.1.1.13 Syk tyrosine kinase {Human (Homo sapiens)}
sanhlpfffgnitreeaedylvqggmsdglyllrqsrnylggfalsvahgrkahhytier
elngtyaiaggrthaspadlchyhsqesdglvcllkkpfnrpqgvqpktgpfedlkenli
reyvkqtwnlqgqaleqaiisqkpqlekliattahekmpwfhgkisreeseqivligskt
ngkflirardnngsyalcllhegkvlhyridkdktgklsipegkkfdtlwqlvehysyka
dgllrvltvpcqki
>d1a81i_ 4.72.1.1.13 Syk tyrosine kinase {Human (Homo sapiens)}
sanhlpfffgnitreeaedylvqggmsdglyllrqsrnylggfalsvahgrkahhytier
elngtyaiaggrthaspadlchyhsqesdglvcllkkpfnrpqgvqpktgpfedlkenli
reyvkqtwnlqgqaleqaiisqkpqlekliattahekmpwfhgkisreeseqivligskt
ngkflirardnngsyalcllhegkvlhyridkdktgklsipegkkfdtlwqlvehysyka
dgllrvltvpcqki
>d1a81k_ 4.72.1.1.13 Syk tyrosine kinase {Human (Homo sapiens)}
sanhlpfffgnitreeaedylvqggmsdglyllrqsrnylggfalsvahgrkahhytier
elngtyaiaggrthaspadlchyhsqesdglvcllkkpfnrpqgvqpktgpfedlkenli
reyvkqtwnlqgqaleqaiisqkpqlekliattahekmpwfhgkisreeseqivligskt
ngkflirardnngsyalcllhegkvlhyridkdktgklsipegkkfdtlwqlvehysyka
dgllrvltvpcqki
>d1a82__ 3.30.1.8.1 Dethiobiotin synthetase {Escherichia coli}
skryfvtgtdtevgktvascallqaakaagyrtagykpvasgsektpeglrnsdalalqr
nsslqldyatvnpytfaeptsphiisaqegrpieslvmsaglraleqqadwvlvegaggw
ftplsdtftfadwvtqeqlpvilvvgvklgcinhamltaqviqhagltlagwvandvtpp
gkrhaeymttltrmipapllgeipwlaenpenaatgkyinlall
>d1a85a_ 4.71.1.9.2 Neutrophil collagenase (MMP-8) {Human (Homo sapiens)}
npkwertnltyrirnytpqlseaeveraikdafelwsvaspliftrisqgeadiniafyq
rdhgdnspfdgpngilahafqpgqgiggdahfdaeetwtntsanynlflvaahefghslg
lahssdpgalmypnyafretsnyslpqddidgiqaiyg
>d1a86a_ 4.71.1.9.2 Neutrophil collagenase (MMP-8) {Human (Homo sapiens)}
npkwertnltyrirnytpqlseaeveraikdafelwsvaspliftrisqgeadiniafyq
rdhgdnspfdgpngilahafqpgqgiggdahfdaeetwtntsanynlflvaahefghslg
lahssdpgalmypnyafretsnyslpqddidgiqaiyg
>d1a87__ 6.1.1.1.2 Colicin N {Escherichia coli}
sakvgeititpdnskpgryissnpeysllaklidaesikgtevytfhtrkgqyvkvtvpd
snidkmrvdyvnwkgpkynnklvkrfvsqfllfrkeekeknekeallkaselvsgmgdkl
geylgvkyknvakevandiknfhgrnirsyneamaslnkvlanpkmkvnksdkdaivnaw
kqvnakdmankignlgkafkvadlaikvekireksiegyntgnwgpllleveswiiggvv
agvaislfgavlsflpisglavtalgvigimtisylssfidanrvsninniissvir
>d1a88a_ 3.59.1.10.4 Chloroperoxidase L {Streptomyces lividans}
gtvttsdgtnifykdwgprdglpvvfhhgwplsaddwdnqmlfflshgyrviahdrrghg
rsdqpstghdmdtyaadvaaltealdlrgavhighstgggevaryvaraepgrvakavlv
savppvmvksdtnpdglplevfdefraalaanraqfyidvpsgpfygfnregatvsqgli
dhwwlqgmmgaanahyeciaafsetdftddlkridvpvlvahgtddqvvpyadaapksae
llanatlksyeglphgmlsthpevlnpdllafvks
>d1a88b_ 3.59.1.10.4 Chloroperoxidase L {Streptomyces lividans}
gtvttsdgtnifykdwgprdglpvvfhhgwplsaddwdnqmlfflshgyrviahdrrghg
rsdqpstghdmdtyaadvaaltealdlrgavhighstgggevaryvaraepgrvakavlv
savppvmvksdtnpdglplevfdefraalaanraqfyidvpsgpfygfnregatvsqgli
dhwwlqgmmgaanahyeciaafsetdftddlkridvpvlvahgtddqvvpyadaapksae
llanatlksyeglphgmlsthpevlnpdllafvks
>d1a88c_ 3.59.1.10.4 Chloroperoxidase L {Streptomyces lividans}
gtvttsdgtnifykdwgprdglpvvfhhgwplsaddwdnqmlfflshgyrviahdrrghg
rsdqpstghdmdtyaadvaaltealdlrgavhighstgggevaryvaraepgrvakavlv
savppvmvksdtnpdglplevfdefraalaanraqfyidvpsgpfygfnregatvsqgli
dhwwlqgmmgaanahyeciaafsetdftddlkridvpvlvahgtddqvvpyadaapksae
llanatlksyeglphgmlsthpevlnpdllafvks
>d1a8a__ 1.66.1.1.6 Annexin V {Rat (Rattus norvegicus)}
alrgtvtdfsgfdgradaevlrkamkglgtdedsilnlltarsnaqrqqiaeefktlfgr
dlvndmkseltgkfeklivalmkpsrlydayelkhalkgagtdekvlteiiasrtpeelr
aikqayeeeygsnleddvvgdtsgyyqrmlvvllqanrdpdtaiddaqveldaqalfqag
elkwgtdeekfitilgtrsvshlrrvfdkymtisgfqieetidretsgnlenlllavvks
irsipaylaetlyyamkgagtddhtlirvivsrseidlfnirkefrknfatslysmikgd
tsgdykkallllcggedd
>d1a8b__ 1.66.1.1.6 Annexin V {Rat (Rattus norvegicus)}
alrgtvtdfsgfdgradaevlrkamkglgtdedsilnlltarsnaqrqqiaeefktlfgr
dlvndmkseltgkfeklivalmkpsrlydayelkhalkgagtdekvlteiiasrtpeelr
aikqayeeeygsnleddvvgdtsgyyqrmlvvllqanrdpdtaiddaqveldaqalfqag
elkwgtdeekfitilgtrsvshlrrvfdkymtisgfqieetidretsgnlenlllavvks
irsipaylaetlyyamkgagtddhtlirvivsrseidlfnirkefrknfatslysmikgd
tsgdykkallllcggedd
>d1a8c__ 1.3.1.1.24 Cytochrome c552 {Nitrosomonas europaea}
dadlakknnciachqvetkvvgpalkdiaakyadkddaatylagkikggssgvwgqipmp
pnvnvsdadakaladwiltlk
>d1a8d_1 2.26.1.5.1 (1-247) Tetanus neurotoxin {Clostridium tetani}
mknldcwvdneedidvilkkstilnldinndiisdisgfnssvitypdaqlvpgingkai
hlvnnessevivhkamdieyndmfnnftvsfwlrvpkvsashleqygtneysiissmkkh
slsigsgwsvslkgnnliwtlkdsagevrqitfrdlpdkfnaylankwvfititndrlss
anlyingvlmgsaeitglgairednnitlkldrcnnnnqyvsidkfrifckalnpkeiek
lytsyls
>d1a8d_2 2.37.4.2.1 (248-452) Tetanus neurotoxin {Clostridium tetani}
itflrdfwgnplrydteyylipvassskdvqlknitdymyltnapsytngklniyyrrly
nglkfiikrytpnneidsfvksgdfiklyvsynnnehivgypkdgnafnnldrilrvgyn
apgiplykkmeavklrdlktysvqlklyddknaslglvgthngqigndpnrdiliasnwy
fnhlkdkilgcdwyfvptdegwtnd
>d1a8e__ 3.84.1.2.8 Transferrin {Human (Homo sapiens)}
dktvrwcavseheatkcqsfrdhmksvipsdgpsvacvkkasyldciraiaaneadavtl
daglvydaylapnnlkpvvaefygskedpqtfyyavavvkkdsgfqmnqlrgkkschtgl
grsagwnipigllycdlpeprkplekavanffsgscapcadgtdfpqlcqlcpgcgcstl
nqyfgysgafkclkdgagdvafvkhstifenlankadrdqyellcldntrkpvdeykdch
laqvpshtvvarsmggkedliwellnqaqehfgkdkskefqlfssphgkdllfkdsahgf
lkvpprmdakmylgyeyvtairnlregtc
>d1a8f__ 3.84.1.2.8 Transferrin {Human (Homo sapiens)}
dktvrwcavseheatkcqsfrdhmksvipsdgpsvacvkkasyldciraiaaneadavtl
daglvydaylapnnlkpvvaefygskedpqtfyyavavvkkdsgfqmnqlrgkkschtgl
grsagwnipigllycdlpeprkplekavanffsgscapcadgtdfpqlcqlcpgcgcstl
nqyfgysgafkclkdgagdvafvkhstifenlankadrdqyellcldntrkpvdeykdch
laqvpshtvvarsmggkedliwellnqaqehfgkdkskefqlfssphgkdllfkdsahgf
lkvpprmdakmylgyeyvtairnlregtc
>d1a8ga_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddtvleemnlpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1a8gb_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddtvleemnlpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1a8h_1 1.28.1.1.1 (349-500) Methionyl-tRNA synthetase (MetRS) {Thermus thermophilus}
laddlgnlvqrtramlfrfaegripepvageelaegtglagrlrplvrelkfhvaleeam
ayvkalnryinekkpwelfkkepeearavlyrvveglriasilltpampdkmaelrralg
lkeevrleeaerwglaeprpipeeapvlfpkk
>d1a8h_2 3.19.1.1.5 (1-348) Methionyl-tRNA synthetase (MetRS) {Thermus thermophilus}
mekvfyvttpiyyvnaephlghayttvvadflarwhrldgyrtffltgtdehgetvyraa
qaagedpkafvdrvsgrfkrawdllgiayddfirtteerhkkvvqlvlkkvyeagdiyyg
eyeglycvscerfytekelveglcpihgrpverrkegnyffrmekyrpwlqeyiqenpdl
irpegyrnevlamlaepigdlsisrpksrvpwgiplpwdenhvtyvwfdallnyvsaldy
pegeayrtfwphawhligkdilkphavfwptmlkaagipmyrhlnvggfllgpdgrkmsk
tlgnvvdpfallekygrdalryyllreipygqdtpvseealrtryead
>d1a8i__ 3.77.1.2.1 Glycogen phosphorylase {Rabbit (Oryctolagus cuniculus)}
qekrkqisvrglagvenvtelkknfnrhlhftlvkdrnvatprdyyfalahtvrdhlvgr
wirtqqhyyekdpkriyylslefymgrtlqntmvnlalenacdeatyqlgldmeeleeie
edaglgngglgrlaacfldsmatlglaaygygiryefgifnqkicggwqmeeaddwlryg
npwekarpeftlpvhfygrvehtsqgakwvdtqvvlampydtpvpgyrnnvvntmrlwsa
kapndfnlkdfnvggyiqavldrnlaenisrvlypndnffegkelrlkqeyfvvaatlqd
iirrfksskfgcrdpvrtnfdafpdkvaiqlndthpslaipelmrvlvdlerldwdkawe
vtvktcaytnhtvipealerwpvhlletllprhlqiiyeinqrflnrvaaafpgdvdrlr
rmslveegavkrinmahlciagshavngvarihseilkktifkdfyelephkfqnktngi
tprrwlvlcnpglaeiiaerigeeyisdldqlrkllsyvddeafirdvakvkqenklkfa
aylereykvhinpnslfdvqvkriheykrqllnclhvitlynrikkepnkfvvprtvmig
gkaapgyhmakmiiklitaigdvvnhdpvvgdrlrviflenyrvslaekvipaadlseqi
stagteasgtgnmxfmlngaltigtmdganvemaeeageenffifgmrvedvdrldqrgy
naqeyydripelrqiieqlssgffspkqpdlfkdivnmlmhhdrfkvfadyeeyvkcqer
vsalyknprewtrmvirniatsgkfssdrtiaqyareiwgvepsrqrlp
>d1a8jh1 2.1.1.1.151 (2-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
saltqppsasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvp
drfsgsksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1a8jh2 2.1.1.2.136 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1a8jl1 2.1.1.1.151 (2-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
saltqppsasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvp
drfsgsksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1a8jl2 2.1.1.2.136 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1a8ka_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwkrplvtikiggqlkealldtgaddtvieemslpgrwkpkmiggiggfikvrqyd
qiiieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1a8kb_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwkrplvtikiggqlkealldtgaddtvieemslpgrwkpkmiggiggfikvrqyd
qiiieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1a8kd_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwkrplvtikiggqlkealldtgaddtvieemslpgrwkpkmiggiggfikvrqyd
qiiieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1a8ke_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwkrplvtikiggqlkealldtgaddtvieemslpgrwkpkmiggiggfikvrqyd
qiiieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1a8l_1 3.38.1.2.2 (1-119) Protein disulfide isomerase {Pyrococcus furiosus}
mglisdadkkvikeeffskmvnpvklivfvrkdhcqycdqlkqlvqelseltdklsyeiv
dfdtpegkelakryridrapattitqdgkdfgvryfglpaghefaafledivdvsreet
>d1a8l_2 3.38.1.2.2 (120-226) Protein disulfide isomerase {Pyrococcus furiosus}
nlmdetkqairnidqdvrilvfvtptcpycplavrmahkfaientkagkgkilgdmveai
eypewadqynvmavpkiviqvngedrvefegaypekmflekllsals
>d1a8ma_ 2.20.1.1.3 Tumor necrosis factor (TNF) {Human (Homo sapiens)}
rtpsdkpvahvvanpqaegqlqwlndranallangvelrdnqlvvpseglyliysqvlfk
gqgcpsthvllthtisriavsyqtkvnllsaikspcqretpegaeakpwyepiylggvfq
lekgdrlsaeinrpdyldfaesgqvyfgiial
>d1a8mb_ 2.20.1.1.3 Tumor necrosis factor (TNF) {Human (Homo sapiens)}
rtpsdkpvahvvanpqaegqlqwlndranallangvelrdnqlvvpseglyliysqvlfk
gqgcpsthvllthtisriavsyqtkvnllsaikspcqretpegaeakpwyepiylggvfq
lekgdrlsaeinrpdyldfaesgqvyfgiial
>d1a8mc_ 2.20.1.1.3 Tumor necrosis factor (TNF) {Human (Homo sapiens)}
rtpsdkpvahvvanpqaegqlqwlndranallangvelrdnqlvvpseglyliysqvlfk
gqgcpsthvllthtisriavsyqtkvnllsaikspcqretpegaeakpwyepiylggvfq
lekgdrlsaeinrpdyldfaesgqvyfgiial
>d1a8o__ 1.29.3.1.3 HIV capsid protein, dimerisation domain {Human immunodeficiency virus, type 1, HIV-1}
dirqgpkepfrdyvdrfyktlraeqasqevknwxtetllvqnanpdcktilkalgpgatl
eexxtacqg
>d1a8p_1 2.38.1.1.5 (2-100) Ferredoxin reductase (flavodoxin reductase) {Azotobacter vinelandii}
snlnvervlsvhhwndtlfsfkttrnpslrfengqfvmiglevdgrplmraysiaspnye
ehleffsikvqngpltsrlqhlkegdelmvsrkptgtlv
>d1a8p_2 3.18.1.1.5 (101-258) Ferredoxin reductase (flavodoxin reductase) {Azotobacter vinelandii}
tsdllpgkhlymlstgtglapfmsliqdpevyerfekvvlihgvrqvnelayqqfitehl
pqseyfgeavkekliyyptvtresfhnqgrltdlmrsgklfediglppinpqddramicg
spsmldescevldgfglkisprmgepgdylierafvek
>d1a8q__ 3.59.1.10.2 Bromoperoxidase A1 {Streptomyces aureofaciens}
picttrdgveifykdwgqgrpvvfihgwplngdawqdqlkavvdagyrgiahdrrghghs
tpvwdgydfdtfaddlndlltdldlrdvtlvahsmgggelaryvgrhgtgrlrsavllsa
ippvmiksdknpdgvpdevfdalkngvltersqfwkdtaegffsanrpgnkvtqgnkdaf
wymamaqtieggvrcvdafgytdftedlkkfdiptlvvhgdddqvvpidatgrksaqiip
naelkvyegsshgiamvpgdkekfnrdlleflnk
>d1a8ra_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a8rb_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a8rc_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a8rd_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a8re_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a8rf_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a8rg_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a8rh_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a8ri_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a8rj_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a8rk_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a8rl_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a8rm_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a8rn_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a8ro_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a8s__ 3.59.1.10.5 Chloroperoxidase F {Pseudomonas fluorescens}
ttfttrdgtqiyykdwgsgqpivfshgwplnadswesqmiflaaqgyrviahdrrghgrs
sqpwsgndmdtyaddlaqliehldlrdavlfgfstgggevaryigrhgtarvakaglisa
vpplmlkteanpgglpmevfdgirqasladrsqlykdlasgpffgfnqpgakssagmvdw
fwlqgmaaghknaydcikafsetdftedlkkidvptlvvhgdadqvvpieasgiasaalv
kgstlkiysgaphgltdthkdqlnadllafikg
>d1a8ta_ 4.128.1.1.2 Zn metallo-beta-lactamase {Bacteroides fragilis}
aqksvkisddisitqlsdkvytyvslaeiegwgmvpsngmivinnhqaalldtpindaqt
emlvnwvtdslhakvttfipnhwhgdcigglgylqrkgvqsyanqmtidlakekglpvpe
hgftdsltvsldgmplqcyylggghatdnivvwlptenilfggcmlkdnqttsignisda
dvtawpktldkvkakfpsaryvvpghgnyggteliehtkqivnqyiests
>d1a8tb_ 4.128.1.1.2 Zn metallo-beta-lactamase {Bacteroides fragilis}
ksvkisddisitqlsdkvytyvslaeiegwgmvpsngmivinnhqaalldtpindaqtem
lvnwvtdslhakvttfipnhwhgdcigglgylqrkgvqsyanqmtidlakekglpvpehg
ftdsltvsldgmplqcyylggghatdnivvwlptenilfggcmlkdnqttsignisdadv
tawpktldkvkakfpsaryvvpghgnyggteliehtkqivnqyiests
>d1a8ua_ 3.59.1.10.3 Chloroperoxidase T {Streptomyces aureofaciens}
pfitvgqenstsidlyyedhgagqpvvlihgfplsghswerqsaalldagyrvitydrrg
fgqssqpttgydydtfaadlntvletldlqdavlvgfsmgtgevaryvssygtariakva
flaslepfllktddnpdgaapkeffdgivaavkadryafytgffndfynldenlgtrise
eavrnswntaasggffaaaaapttwytdfradipridvpalilhgtgdrtlpientarvf
hkalpsaeyvevegaphgllwthaeevntallaflak
>d1a8ub_ 3.59.1.10.3 Chloroperoxidase T {Streptomyces aureofaciens}
pfitvgqenstsidlyyedhgagqpvvlihgfplsghswerqsaalldagyrvitydrrg
fgqssqpttgydydtfaadlntvletldlqdavlvgfsmgtgevaryvssygtariakva
flaslepfllktddnpdgaapkeffdgivaavkadryafytgffndfynldenlgtrise
eavrnswntaasggffaaaaapttwytdfradipridvpalilhgtgdrtlpientarvf
hkalpsaeyvevegaphgllwthaeevntallaflak
>d1a8va_ 2.35.4.5.5 Rho termination factor, N-terminal, RNA-binding domain {Escherichia coli}
ghmnltelkntpvselitlgenmglenlarmrkqdiifailkqhaksgedifgdgvleil
qdgfgflrsadssylagpddiyvspsqirrfnlrtgdtisgkirppkegeryfallkvne
>d1a8vb_ 2.35.4.5.5 Rho termination factor, N-terminal, RNA-binding domain {Escherichia coli}
ghmnltelkntpvselitlgenmglenlarmrkqdiifailkqhaksgedifgdgvleil
qdgfgflrsadssylagpddiyvspsqirrfnlrtgdtisgkirppkegeryfallkvne
>d1a8y_1 3.38.1.3.1 (3-126) Calsequestrin {Rabbit (Oryctolagus cuniculus)}
gldfpeydgvdrvinvnaknyknvfkkyevlallyheppeddkasqrqfemeelilelaa
qvledkgvgfglvdsekdaavakklglteedsiyvfkedevieydgefsadtlveflldv
ledp
>d1a8y_2 3.38.1.3.1 (127-228) Calsequestrin {Rabbit (Oryctolagus cuniculus)}
veliegerelqafeniedeikligyfknkdsehykafkeaaeefhpyipffatfdskvak
kltlklneidfyeafmeepvtipdkpnseeeivnfveehrrs
>d1a8y_3 3.38.1.3.1 (229-347) Calsequestrin {Rabbit (Oryctolagus cuniculus)}
tlrklkpesmyetweddmdgihivafaeeadpdgyefleilksvaqdntdnpdlsiiwid
pddfpllvpywektfdidlsapqigvvnvtdadsvwmemddeedlpsaeeledwledvl
>d1a8z__ 2.5.1.1.26 Rusticyanin {Thiobacillus ferrooxidans}
ldtswkeatlpqvkamlqkdtgkvsgdtvtysgktvhvvaaavlpgfpfpsfevhdkknp
tldipagatvdvtfintnkgfghsfditqktppfavmpvidpivagtgfspvpkdgkfgy
tnftwhptagtyyyvcqipghaatgmfgkivvk
>d1a90__ 4.15.1.2.1 Cystatin {Chicken (Gallus gallus)}
gapvpvdendeglqralqfaiaeynrasndkyssrvvrvisakrqlvsgikyilqveigr
ttcpkssgdlqscefhdepelakyttctfvvysipwlnqiklleskcq
>d1a91__ 6.2.1.1.7 Subunit C of the F1F0 ATP synthase {Escherichia coli}
menlnmdllymaaavmmglaaigaaigigilggkflegaarqpdlipllrtqffivmglv
daipmiavglglyvmfava
>d1a94a_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwkrplvtikiggqlkealldtgaddtvieemslpgrwepkmiggiggfikvrqyd
qiiieiaghkaigtvlvgptpvniigrnlltqigatlnf
>d1a94b_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwkrplvtikiggqlkealldtgaddtvieemslpgrwepkmiggiggfikvrqyd
qiiieiaghkaigtvlvgptpvniigrnlltqigatlnf
>d1a94d_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwkrplvtikiggqlkealldtgaddtvieemslpgrwepkmiggiggfikvrqyd
qiiieiaghkaigtvlvgptpvniigrnlltqigatlnf
>d1a94e_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwkrplvtikiggqlkealldtgaddtvieemslpgrwepkmiggiggfikvrqyd
qiiieiaghkaigtvlvgptpvniigrnlltqigatlnf
>d1a95a_ 3.51.1.1.1 Xantine-guanine PRTase (XPRTase) {Escherichia coli}
ekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvciss
ydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrplv
ddyvvdipqdtwieqpwdmgvvfvppis
>d1a95b_ 3.51.1.1.1 Xantine-guanine PRTase (XPRTase) {Escherichia coli}
ekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvciss
ydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrplv
ddyvvdipqdtwieqpwdmgvvfvppisgr
>d1a95c_ 3.51.1.1.1 Xantine-guanine PRTase (XPRTase) {Escherichia coli}
ekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvciss
ydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrplv
ddyvvdipqdtwieqpwdmgvvfvppisgr
>d1a95d_ 3.51.1.1.1 Xantine-guanine PRTase (XPRTase) {Escherichia coli}
sekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvcis
sydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrpl
vddyvvdipqdtwieqpwdmgvvfvppisg
>d1a96a_ 3.51.1.1.1 Xantine-guanine PRTase (XPRTase) {Escherichia coli}
ekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvciss
ydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrplv
ddyvvdipqdtwieqpwdmgvvfvppis
>d1a96b_ 3.51.1.1.1 Xantine-guanine PRTase (XPRTase) {Escherichia coli}
ekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvciss
ydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrplv
ddyvvdipqdtwieqpwdmgvvfvppisgr
>d1a96c_ 3.51.1.1.1 Xantine-guanine PRTase (XPRTase) {Escherichia coli}
ekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvciss
ydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrplv
ddyvvdipqdtwieqpwdmgvvfvppisgr
>d1a96d_ 3.51.1.1.1 Xantine-guanine PRTase (XPRTase) {Escherichia coli}
ekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvciss
ydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrplv
ddyvvdipqdtwieqpwdmgvvfvppisgr
>d1a97a_ 3.51.1.1.1 Xantine-guanine PRTase (XPRTase) {Escherichia coli}
ekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvaiss
ydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrplv
ddyvvdipqdtwieqpwdmgvvfvppis
>d1a97b_ 3.51.1.1.1 Xantine-guanine PRTase (XPRTase) {Escherichia coli}
ekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvaiss
ydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrplv
ddyvvdipqdtwieqpwdmgvvfvppis
>d1a97c_ 3.51.1.1.1 Xantine-guanine PRTase (XPRTase) {Escherichia coli}
ekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvaiss
ydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrplv
ddyvvdipqdtwieqpwdmgvvfvppis
>d1a97d_ 3.51.1.1.1 Xantine-guanine PRTase (XPRTase) {Escherichia coli}
ekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvaiss
ydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrplv
ddyvvdipqdtwieqpwdmgvvfvppis
>d1a98a_ 3.51.1.1.1 Xantine-guanine PRTase (XPRTase) {Escherichia coli}
ekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvaiss
ydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrplv
ddyvvdipqdtwieqpwdmgvvfvppisgr
>d1a98b_ 3.51.1.1.1 Xantine-guanine PRTase (XPRTase) {Escherichia coli}
ekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvaiss
ydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrplv
ddyvvdipqdtwieqpwdmgvvfvppis
>d1a99a_ 3.84.1.1.13 Putrescine receptor (PotF) {Escherichia coli}
qktlhiynwsdyiapdtvanfeketgikvvydvfdsnevlegklmagstgfdlvvpsasf
lerqltagvfqpldksklpewknldpellklvakhdpdnkfampymwattgigynvdkvk
avlgenapvdswdlilkpenleklkscgvsfldapeevfatvlnylgkdpnstkaddytg
patdlllklrpniryfhssqyindlangdicvaigwagdvwqasnrakeakngvnvsfsi
pkegamaffdvfampadaknkdeayqflnyllrpdvvahisdhvfyanankaatplvsae
vrenpgiyppadvraklftlkvqdpkidrvrtrawtkvksg
>d1a99b_ 3.84.1.1.13 Putrescine receptor (PotF) {Escherichia coli}
qktlhiynwsdyiapdtvanfeketgikvvydvfdsnevlegklmagstgfdlvvpsasf
lerqltagvfqpldksklpewknldpellklvakhdpdnkfampymwattgigynvdkvk
avlgenapvdswdlilkpenleklkscgvsfldapeevfatvlnylgkdpnstkaddytg
patdlllklrpniryfhssqyindlangdicvaigwagdvwqasnrakeakngvnvsfsi
pkegamaffdvfampadaknkdeayqflnyllrpdvvahisdhvfyanankaatplvsae
vrenpgiyppadvraklftlkvqdpkidrvrtrawtkvksg
>d1a99c_ 3.84.1.1.13 Putrescine receptor (PotF) {Escherichia coli}
qktlhiynwsdyiapdtvanfeketgikvvydvfdsnevlegklmagstgfdlvvpsasf
lerqltagvfqpldksklpewknldpellklvakhdpdnkfampymwattgigynvdkvk
avlgenapvdswdlilkpenleklkscgvsfldapeevfatvlnylgkdpnstkaddytg
patdlllklrpniryfhssqyindlangdicvaigwagdvwqasnrakeakngvnvsfsi
pkegamaffdvfampadaknkdeayqflnyllrpdvvahisdhvfyanankaatplvsae
vrenpgiyppadvraklftlkvqdpkidrvrtrawtkvksg
>d1a99d_ 3.84.1.1.13 Putrescine receptor (PotF) {Escherichia coli}
qktlhiynwsdyiapdtvanfeketgikvvydvfdsnevlegklmagstgfdlvvpsasf
lerqltagvfqpldksklpewknldpellklvakhdpdnkfampymwattgigynvdkvk
avlgenapvdswdlilkpenleklkscgvsfldapeevfatvlnylgkdpnstkaddytg
patdlllklrpniryfhssqyindlangdicvaigwagdvwqasnrakeakngvnvsfsi
pkegamaffdvfampadaknkdeayqflnyllrpdvvahisdhvfyanankaatplvsae
vrenpgiyppadvraklftlkvqdpkidrvrtrawtkvksg
>d1a9ba1 2.1.1.2.10 (182-277) Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-B*3501}
adppkthvthhpvsdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrweps
>d1a9ba2 4.17.1.1.17 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-B*3501}
gshsmryfytamsrpgrgeprfiavgyvddtqfvrfdsdaasprteprapwieqegpeyw
drntqifktntqtyreslrnlrgyynqseagshiiqrmygcdlgpdgrllrghdqsaydg
kdyialnedlsswtaadtaaqitqrkweaarvaeqlrayleglcvewlrrylengketlq
r
>d1a9bb1 2.1.1.2.10 Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-B*3501}
miqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskd
wsfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1a9bd1 2.1.1.2.10 (182-277) Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-B*3501}
adppkthvthhpvsdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrweps
>d1a9bd2 4.17.1.1.17 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-B*3501}
gshsmryfytamsrpgrgeprfiavgyvddtqfvrfdsdaasprteprapwieqegpeyw
drntqifktntqtyreslrnlrgyynqseagshiiqrmygcdlgpdgrllrghdqsaydg
kdyialnedlsswtaadtaaqitqrkweaarvaeqlrayleglcvewlrrylengketlq
r
>d1a9be1 2.1.1.2.10 Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-B*3501}
miqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskd
wsfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1a9ca_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstsehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a9cb_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstsehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a9cc_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstsehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a9cd_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstsehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a9ce_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstsehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a9cf_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstsehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a9cg_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstsehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a9ch_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstsehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a9ci_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstsehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a9cj_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstsehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a9ck_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstsehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a9cl_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstsehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a9cm_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstsehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a9cn_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstsehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a9co_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstsehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a9ea1 2.1.1.2.10 (182-277) Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-B*3501}
adppkthvthhpvsdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrweps
>d1a9ea2 4.17.1.1.17 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-B*3501}
gshsmryfytamsrpgrgeprfiavgyvddtqfvrfdsdaasprteprapwieqegpeyw
drntqifktntqtyreslrnlrgyynqseagshiiqrmygcdlgpdgrllrghdqsaydg
kdyialnedlsswtaadtaaqitqrkweaarvaeqlrayleglcvewlrrylengketlq
r
>d1a9eb1 2.1.1.2.10 Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-B*3501}
miqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskd
wsfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1a9ma_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmihgiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1a9mb_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmihgiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1a9na_ 3.9.2.1.1 Splicesomal U2A' protein {Human (Homo sapiens)}
vkltaelieqaaqytnavrdreldlrgykipvienlgatldqfdaidfsdneirkldgfp
llrrlktllvnnnricrigegldqalpdlteliltnnslvelgdldplaslksltylcil
rnpvtnkkhyrlyviykvpqvrvldfqkvklkerqeaekmfk
>d1a9nb_ 4.47.7.1.3 Splicing factor U2B'' {Human (Homo sapiens)}
irpnhtiyinnmndkikkeelkrslyalfsqfghvvdivalktmkmrgqafvifkelgss
tnalrqlqgfpfygkpmriqyaktdsdiiskmrg
>d1a9nc_ 3.9.2.1.1 Splicesomal U2A' protein {Human (Homo sapiens)}
vkltaelieqaaqytnavrdreldlrgykipvienlgatldqfdaidfsdneirkldgfp
llrrlktllvnnnricrigegldqalpdlteliltnnslvelgdldplaslksltylcil
rnpvtnkkhyrlyviykvpqvrvldfqkvklkerqeaekmfkgkrgaqlakdia
>d1a9nd_ 4.47.7.1.3 Splicing factor U2B'' {Human (Homo sapiens)}
irpnhtiyinnmndkikkeelkrslyalfsqfghvvdivalktmkmrgqafvifkelgss
tnalrqlqgfpfygkpmriqyaktdsdiiskmr
>d1a9o__ 3.47.1.1.2 Purine nucleoside phosphorylase, PNP {Bovine (Bos taurus)}
mqngytyedyqdtakwllshteqrpqvavicgsglgglvnkltqaqtfdyseipnfpest
vpghagrlvfgilngracvmmqgrfhmyegypfwkvtfpvrvfrllgvetlvvtnaaggl
npnfevgdimlirdhinlpgfsgenplrgpneerfgvrfpamsdaydrdmrqkahstwkq
mgeqrelqegtyvmlggpnfetvaecrllrnlgadavgmstvpevivarhcglrvfgfsl
itnkvimdtesqgkanheevleagkqaaqkleqfvsllmasipvsghtg
>d1a9p__ 3.47.1.1.2 Purine nucleoside phosphorylase, PNP {Bovine (Bos taurus)}
mqngytyedyqdtakwllshteqrpqvavicgsglgglvnkltqaqtfdyseipnfpest
vpghagrlvfgilngracvmmqgrfhmyegypfwkvtfpvrvfrllgvetlvvtnaaggl
npnfevgdimlirdhinlpgfsgenplrgpneerfgvrfpamsdaydrdmrqkahstwkq
mgeqrelqegtyvmlggpnfetvaecrllrnlgadavgmstvpevivarhcglrvfgfsl
itnkvimdtesqgkanheevleagkqaaqkleqfvsllmasipvsghtg
>d1a9q__ 3.47.1.1.2 Purine nucleoside phosphorylase, PNP {Bovine (Bos taurus)}
mqngytyedyqdtakwllshteqrpqvavicgsglgglvnkltqaqtfdyseipnfpest
vpghagrlvfgilngracvmmqgrfhmyegypfwkvtfpvrvfrllgvetlvvtnaaggl
npnfevgdimlirdhinlpgfsgenplrgpneerfgvrfpamsdaydrdmrqkahstwkq
mgeqrelqegtyvmlggpnfetvaecrllrnlgadavgmstvpevivarhcglrvfgfsl
itnkvimdtesqgkanheevleagkqaaqkleqfvsllmasi
>d1a9r__ 3.47.1.1.2 Purine nucleoside phosphorylase, PNP {Bovine (Bos taurus)}
mqngytyedyqdtakwllshteqrpqvavicgsglgglvnkltqaqtfdyseipnfpest
vpghagrlvfgilngracvmmqgrfhmyegypfwkvtfpvrvfrllgvetlvvtnaaggl
npnfevgdimlirdhinlpgfsgenplrgpneerfgvrfpamsdaydrdmrqkahstwkq
mgeqrelqegtyvmlggpnfetvaecrllrnlgadavgmstvpevivarhcglrvfgfsl
itnkvimdtesqgkanheevleagkqaaqkleqfvsllmasi
>d1a9s__ 3.47.1.1.2 Purine nucleoside phosphorylase, PNP {Bovine (Bos taurus)}
mqngytyedyqdtakwllshteqrpqvavicgsglgglvnkltqaqtfdyseipnfpest
vpghagrlvfgilngracvmmqgrfhmyegypfwkvtfpvrvfrllgvetlvvtnaaggl
npnfevgdimlirdhinlpgfsgenplrgpneerfgvrfpamsdaydrdmrqkahstwkq
mgeqrelqegtyvmlggpnfetvaecrllrnlgadavgmstvpevivarhcglrvfgfsl
itnkvimdtesqgkanheevleagkqaaqkleqfvsllmasi
>d1a9t__ 3.47.1.1.2 Purine nucleoside phosphorylase, PNP {Bovine (Bos taurus)}
mangytyedyqdtakwllshteqrpqvavicgsglgglvnkltqaqtfdyseipnfpest
vpghagrlvfgilngracvmmqgrfhmyegypfwkvtfpvrvfrllgvetlvvtnaaggl
npnfevgdimlirdhinlpgfsgenplrgpneerfgvrfpamsdaydrdmrqkahstwkq
mgeqrelqegtyvmlggpnfetvaecrllrnlgadavgmstvpevivarhcglrvfgfsl
itnkvimdtesqgkanheevleagkqaaqkleqfvsllmasipv
>d1a9u__ 4.117.1.1.11 MAP kinase p38 {Human (Homo sapiens)}
erptfyrqelnktiwevperyqnlspvgsgaygsvcaafdtktglrvavkklsrpfqsii
hakrtyrelrllkhmkhenviglldvftparsleefndvylvthlmgadlnnivkcqklt
ddhvqfliyqilrglkyihsadiihrdlkpsnlavnedcelkildfglarhtddemtgyv
atrwyrapeimlnwmhynqtvdiwsvgcimaelltgrtlfpgtdhidqlklilrlvgtpg
aellkkissesarnyiqsltqmpkmnfanvfiganplavdllekmlvldsdkritaaqal
ahayfaqyhdpddepvadpydqsfesrdllidewksltydevisfvpppld
>d1a9v__ 2.1.1.5.26 Major mite allergen {House-dust mite (Dermatophagoides pteronyssinus), Der p 2}
sqvdvkdcanheikkvlvpgchgsepciihrgkpfqleavfeanqntktakieikasidg
levdvpgidpnachymkcplvkgqqydikytwnvpkiapksenvvvtvkvmgddgvlaca
iathakird
>d1a9wa_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a9wc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a9we_ 1.1.1.1.30 Hemoglobin, beta-chain {Human (Homo sapiens), embryonic gower II}
vhftaeekaavtslwskmnveeaggealgrllvvypwtqrffdsfgnlsspsailgnpkv
kahgkkvltsfgdaiknmdnlkpafaklselhcdklhvdpenfkllgnvmviilathfgk
eftpevqaawqklvsavaialahky
>d1a9wf_ 1.1.1.1.30 Hemoglobin, beta-chain {Human (Homo sapiens), embryonic gower II}
vhftaeekaavtslwskmnveeaggealgrllvvypwtqrffdsfgnlsspsailgnpkv
kahgkkvltsfgdaiknmdnlkpafaklselhcdklhvdpenfkllgnvmviilathfgk
eftpevqaawqklvsavaialahky
>d1a9xa1 1.89.1.1.1 (403-555) Carbamoyl phosphate synthetase, large subunit connection domain {Escherichia coli}
evgatgfdpkvslddpealtkirrelkdagadriwyiadafraglsvdgvfnltnidrwf
lvqieelvrleekvaevgitglnadflrqlkrkgfadarlaklagvreaeirklrdqydl
hpvykrvdtcaaefatdtaymystyeeeceanp
>d1a9xa2 3.17.1.1.1 (936-1073) Carbamoyl phosphate synthetase, large subunit allosteric, C-terminal domain {Escherichia coli}
nstmkkhgrallsvregdkervvdlaakllkqgfeldathgtaivlgeaginprlvnkvh
egrphiqdrikngeytyiinttsgrraiedsrvirrsalqykvhydttlnggfatamaln
adatekvisvqemhaqik
>d1a9xa3 3.24.1.1.3 (1-127) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
mpkrtdiksililgagpivigqacefdysgaqackalreegyrvinvnsnpatimtdpem
adatyiepihwevvrkiiekerpdavlptmggqtalncalelerqgvleefgvtmigata
daidkae
>d1a9xa4 3.24.1.1.3 (556-676) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
stdrekimvlgggpnrigqgiefdyccvhaslalredgyetimvncnpetvstdydtsdr
lyfepvtledvleivriekpkgvivqyggqtplklaraleaagvpvigtspdaidraedr
e
>d1a9xa5 4.115.1.2.3 (128-402) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
drrrfdvamkkigletarsgiahtmeealavaadvgfpciirpsftmggsgggiaynree
feeicargldlsptkellidesligwkeyemevvrdkndnciivcsienfdamgihtgds
itvapaqtltdkeyqimrnasmavlreigvetggsnvqfavnpkngrliviemnprvsrs
salaskatgfpiakvaaklavgytldelmnditggrtpasfepsidyvvtkiprfnfekf
agandrlttqmksvgevmaigrtqqeslqkalrgl
>d1a9xa6 4.115.1.2.3 (677-935) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
rfqhaverlklkqpanatvtaiemavekakeigyplvvraameivydeadlrryfqtavl
ldhflddavevdvdaicdgemvliggimehieqagvhsgdsacslpaytlsqeiqdvmrq
qvqklafelqvrglmnvqfavknnevylievnpraartvpfvskatgvplakvaarvmag
kslaeqgvtkevippyysvkevvlpfnkfpgvdpllgpemrstgevmgvgrtfaeafaka
qlgs
>d1a9xb1 3.7.3.1.1 (1502-1652) Carbamoyl phosphate synthetase, small subunit N-terminal domain {Escherichia coli}
iksallvledgtqfhgraigatgsavgevvfntsmtgyqeiltdpsysrqivtltyphig
nvgtndadeessqvhaqglvirdlpliasnfrntedlssylkrhnivaiadidtrkltrl
lrekgaqngciiagdnpdaalalekarafpg
>d1a9xb2 3.58.1.1.2 (1653-1880) Carbamoyl phosphate synthetase, small subunit C-terminal domain {Escherichia coli}
lngmdlakevttaeayswtqgswtltgglpqakkedelpfhvvaydfgakrnilrmlvdr
gcrltivpaqtsaedvlkmnpdgiflsngpgdpapcdyaitaiqkfletdipvfgixlgh
qllalasgaktvkmkfghhggnhpvkdveknvvmitaqnhgfavdeatlpanlrvthksl
fdgtlqgihrtdkpafsfqgnpeaspgphdaaplfdhfielieqyrkt
>d1a9xc1 1.89.1.1.1 (2403-2555) Carbamoyl phosphate synthetase, large subunit connection domain {Escherichia coli}
evgatgfdpkvslddpealtkirrelkdagadriwyiadafraglsvdgvfnltnidrwf
lvqieelvrleekvaevgitglnadflrqlkrkgfadarlaklagvreaeirklrdqydl
hpvykrvdtcaaefatdtaymystyeeeceanp
>d1a9xc2 3.17.1.1.1 (2936-3073) Carbamoyl phosphate synthetase, large subunit allosteric, C-terminal domain {Escherichia coli}
nstmkkhgrallsvregdkervvdlaakllkqgfeldathgtaivlgeaginprlvnkvh
egrphiqdrikngeytyiinttsgrraiedsrvirrsalqykvhydttlnggfatamaln
adatekvisvqemhaqik
>d1a9xc3 3.24.1.1.3 (2001-2127) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
mpkrtdiksililgagpivigqacefdysgaqackalreegyrvinvnsnpatimtdpem
adatyiepihwevvrkiiekerpdavlptmggqtalncalelerqgvleefgvtmigata
daidkae
>d1a9xc4 3.24.1.1.3 (2556-2676) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
stdrekimvlgggpnrigqgiefdyccvhaslalredgyetimvncnpetvstdydtsdr
lyfepvtledvleivriekpkgvivqyggqtplklaraleaagvpvigtspdaidraedr
e
>d1a9xc5 4.115.1.2.3 (2128-2402) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
drrrfdvamkkigletarsgiahtmeealavaadvgfpciirpsftmggsgggiaynree
feeicargldlsptkellidesligwkeyemevvrdkndnciivcsienfdamgihtgds
itvapaqtltdkeyqimrnasmavlreigvetggsnvqfavnpkngrliviemnprvsrs
salaskatgfpiakvaaklavgytldelmnditggrtpasfepsidyvvtkiprfnfekf
agandrlttqmksvgevmaigrtqqeslqkalrgl
>d1a9xc6 4.115.1.2.3 (2677-2935) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
rfqhaverlklkqpanatvtaiemavekakeigyplvvraameivydeadlrryfqtavl
ldhflddavevdvdaicdgemvliggimehieqagvhsgdsacslpaytlsqeiqdvmrq
qvqklafelqvrglmnvqfavknnevylievnpraartvpfvskatgvplakvaarvmag
kslaeqgvtkevippyysvkevvlpfnkfpgvdpllgpemrstgevmgvgrtfaeafaka
qlgs
>d1a9xd1 3.7.3.1.1 (3502-3652) Carbamoyl phosphate synthetase, small subunit N-terminal domain {Escherichia coli}
iksallvledgtqfhgraigatgsavgevvfntsmtgyqeiltdpsysrqivtltyphig
nvgtndadeessqvhaqglvirdlpliasnfrntedlssylkrhnivaiadidtrkltrl
lrekgaqngciiagdnpdaalalekarafpg
>d1a9xd2 3.58.1.1.2 (3653-3880) Carbamoyl phosphate synthetase, small subunit C-terminal domain {Escherichia coli}
lngmdlakevttaeayswtqgswtltgglpqakkedelpfhvvaydfgakrnilrmlvdr
gcrltivpaqtsaedvlkmnpdgiflsngpgdpapcdyaitaiqkfletdipvfgixlgh
qllalasgaktvkmkfghhggnhpvkdveknvvmitaqnhgfavdeatlpanlrvthksl
fdgtlqgihrtdkpafsfqgnpeaspgphdaaplfdhfielieqyrkt
>d1a9xe1 1.89.1.1.1 (4403-4555) Carbamoyl phosphate synthetase, large subunit connection domain {Escherichia coli}
evgatgfdpkvslddpealtkirrelkdagadriwyiadafraglsvdgvfnltnidrwf
lvqieelvrleekvaevgitglnadflrqlkrkgfadarlaklagvreaeirklrdqydl
hpvykrvdtcaaefatdtaymystyeeeceanp
>d1a9xe2 3.17.1.1.1 (4936-5073) Carbamoyl phosphate synthetase, large subunit allosteric, C-terminal domain {Escherichia coli}
nstmkkhgrallsvregdkervvdlaakllkqgfeldathgtaivlgeaginprlvnkvh
egrphiqdrikngeytyiinttsgrraiedsrvirrsalqykvhydttlnggfatamaln
adatekvisvqemhaqik
>d1a9xe3 3.24.1.1.3 (4001-4127) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
mpkrtdiksililgagpivigqacefdysgaqackalreegyrvinvnsnpatimtdpem
adatyiepihwevvrkiiekerpdavlptmggqtalncalelerqgvleefgvtmigata
daidkae
>d1a9xe4 3.24.1.1.3 (4556-4676) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
stdrekimvlgggpnrigqgiefdyccvhaslalredgyetimvncnpetvstdydtsdr
lyfepvtledvleivriekpkgvivqyggqtplklaraleaagvpvigtspdaidraedr
e
>d1a9xe5 4.115.1.2.3 (4128-4402) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
drrrfdvamkkigletarsgiahtmeealavaadvgfpciirpsftmggsgggiaynree
feeicargldlsptkellidesligwkeyemevvrdkndnciivcsienfdamgihtgds
itvapaqtltdkeyqimrnasmavlreigvetggsnvqfavnpkngrliviemnprvsrs
salaskatgfpiakvaaklavgytldelmnditggrtpasfepsidyvvtkiprfnfekf
agandrlttqmksvgevmaigrtqqeslqkalrgl
>d1a9xe6 4.115.1.2.3 (4677-4935) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
rfqhaverlklkqpanatvtaiemavekakeigyplvvraameivydeadlrryfqtavl
ldhflddavevdvdaicdgemvliggimehieqagvhsgdsacslpaytlsqeiqdvmrq
qvqklafelqvrglmnvqfavknnevylievnpraartvpfvskatgvplakvaarvmag
kslaeqgvtkevippyysvkevvlpfnkfpgvdpllgpemrstgevmgvgrtfaeafaka
qlgs
>d1a9xf1 3.7.3.1.1 (5502-5652) Carbamoyl phosphate synthetase, small subunit N-terminal domain {Escherichia coli}
iksallvledgtqfhgraigatgsavgevvfntsmtgyqeiltdpsysrqivtltyphig
nvgtndadeessqvhaqglvirdlpliasnfrntedlssylkrhnivaiadidtrkltrl
lrekgaqngciiagdnpdaalalekarafpg
>d1a9xf2 3.58.1.1.2 (5653-5880) Carbamoyl phosphate synthetase, small subunit C-terminal domain {Escherichia coli}
lngmdlakevttaeayswtqgswtltgglpqakkedelpfhvvaydfgakrnilrmlvdr
gcrltivpaqtsaedvlkmnpdgiflsngpgdpapcdyaitaiqkfletdipvfgixlgh
qllalasgaktvkmkfghhggnhpvkdveknvvmitaqnhgfavdeatlpanlrvthksl
fdgtlqgihrtdkpafsfqgnpeaspgphdaaplfdhfielieqyrkt
>d1a9xg1 1.89.1.1.1 (6403-6555) Carbamoyl phosphate synthetase, large subunit connection domain {Escherichia coli}
evgatgfdpkvslddpealtkirrelkdagadriwyiadafraglsvdgvfnltnidrwf
lvqieelvrleekvaevgitglnadflrqlkrkgfadarlaklagvreaeirklrdqydl
hpvykrvdtcaaefatdtaymystyeeeceanp
>d1a9xg2 3.17.1.1.1 (6936-7073) Carbamoyl phosphate synthetase, large subunit allosteric, C-terminal domain {Escherichia coli}
nstmkkhgrallsvregdkervvdlaakllkqgfeldathgtaivlgeaginprlvnkvh
egrphiqdrikngeytyiinttsgrraiedsrvirrsalqykvhydttlnggfatamaln
adatekvisvqemhaqik
>d1a9xg3 3.24.1.1.3 (6001-6127) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
mpkrtdiksililgagpivigqacefdysgaqackalreegyrvinvnsnpatimtdpem
adatyiepihwevvrkiiekerpdavlptmggqtalncalelerqgvleefgvtmigata
daidkae
>d1a9xg4 3.24.1.1.3 (6556-6676) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
stdrekimvlgggpnrigqgiefdyccvhaslalredgyetimvncnpetvstdydtsdr
lyfepvtledvleivriekpkgvivqyggqtplklaraleaagvpvigtspdaidraedr
e
>d1a9xg5 4.115.1.2.3 (6128-6402) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
drrrfdvamkkigletarsgiahtmeealavaadvgfpciirpsftmggsgggiaynree
feeicargldlsptkellidesligwkeyemevvrdkndnciivcsienfdamgihtgds
itvapaqtltdkeyqimrnasmavlreigvetggsnvqfavnpkngrliviemnprvsrs
salaskatgfpiakvaaklavgytldelmnditggrtpasfepsidyvvtkiprfnfekf
agandrlttqmksvgevmaigrtqqeslqkalrgl
>d1a9xg6 4.115.1.2.3 (6677-6935) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
rfqhaverlklkqpanatvtaiemavekakeigyplvvraameivydeadlrryfqtavl
ldhflddavevdvdaicdgemvliggimehieqagvhsgdsacslpaytlsqeiqdvmrq
qvqklafelqvrglmnvqfavknnevylievnpraartvpfvskatgvplakvaarvmag
kslaeqgvtkevippyysvkevvlpfnkfpgvdpllgpemrstgevmgvgrtfaeafaka
qlgs
>d1a9xh1 3.7.3.1.1 (7502-7652) Carbamoyl phosphate synthetase, small subunit N-terminal domain {Escherichia coli}
iksallvledgtqfhgraigatgsavgevvfntsmtgyqeiltdpsysrqivtltyphig
nvgtndadeessqvhaqglvirdlpliasnfrntedlssylkrhnivaiadidtrkltrl
lrekgaqngciiagdnpdaalalekarafpg
>d1a9xh2 3.58.1.1.2 (7653-7880) Carbamoyl phosphate synthetase, small subunit C-terminal domain {Escherichia coli}
lngmdlakevttaeayswtqgswtltgglpqakkedelpfhvvaydfgakrnilrmlvdr
gcrltivpaqtsaedvlkmnpdgiflsngpgdpapcdyaitaiqkfletdipvfgixlgh
qllalasgaktvkmkfghhggnhpvkdveknvvmitaqnhgfavdeatlpanlrvthksl
fdgtlqgihrtdkpafsfqgnpeaspgphdaaplfdhfielieqyrkt
>d1a9y__ 3.2.1.2.1 Uridine diphosphogalactose-4-epimerase (UDP-galactose 4-epimerase) {Escherichia coli}
mrvlvtggsgyigshtcvqllqnghdviildnlcnskrsvlpvierlggkhptfvegdir
nealmteilhdhaidtvihfaglkavgesvqkpleyydnnvngtlrlisamraanvknfi
fssaatvygdqpkipyvesfptgtpqspfgksklmveqiltdlqkaqpdwsiallryfnp
vgahpsgdmgedpqgipnnlmpyiaqvavgrrdslaifgndyptedgtgvrdyihvmdla
dghvvameklankpgvhiynlgagvgnsvldvvnafskacgkpvnyhfaprregdlpayw
adaskadrelnwrvtrtldemaqdtwhwqsrhpqgypd
>d1a9z__ 3.2.1.2.1 Uridine diphosphogalactose-4-epimerase (UDP-galactose 4-epimerase) {Escherichia coli}
mrvlvtggsgyigshtcvqllqnghdviildnlcnskrsvlpvierlggkhptfvegdir
nealmteilhdhaidtvihfaglkavgesvqkpleyydnnvngtlrlisamraanvknfi
fssaatvygdnpkipyvesfptgtpqspfgksklmveqiltdlqkaqpdwsiallryfnp
vgahpsgdmgedpqgipnnlmpyiaqvavgrrdslaifgndyptedgtgvrdyihvmdla
dghvvameklankpgvhiynlgagvgnsvldvvnafskacgkpvnyhfaprregdlpayw
adaskadrelnwrvtrtldemaqdtwhwqsrhpqgypd
>d1aa1b1 3.1.12.1.2 (148-463) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
fqgpphgiqverdklnkygrpllgctikpklglsaknygravyeclrggldftxddenvn
sqpfmrwrdrflfcaealykaqaetgeikghylnatagtcedmmkravfarelgvpivmh
dyltggftanttlshycrdnglllhihramhavidrqknhgmhfrvlakalrlsggdhih
sgtvvgklegerditlgfvdllrddytekdrsrgiyftqswvstpgvlpvasggihvwhm
palteifgddsvlqfgggtlghpwgnapgavanrvaleacvqarnegrdlaregntiire
atkwspelaaacevwk
>d1aa1b2 4.47.9.1.2 (21-147) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
kltyytpeyetldtdilaafrvspqpgvppeeagaavaaesstgtwttvwtdgltnldry
kgrcyhiepvageenqyicyvaypldlfeegsvtnmftsivgnvfgfkalralrledlri
pvayvkt
>d1aa1c_ 4.55.1.1.2 Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
mqvwpilnlkkyetlsylpplttdqlarqvdyllnnkwvpclefetdhgfvyrehhnspg
yydgrywtmwklpmfgctdpaqvlneleeckkeypnafiriigfdsnrevqcisfiaykp
agy
>d1aa1e1 3.1.12.1.2 (148-463) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
fqgpphgiqverdklnkygrpllgctikpklglsaknygravyeclrggldftxddenvn
sqpfmrwrdrflfcaealykaqaetgeikghylnatagtcedmmkravfarelgvpivmh
dyltggftanttlshycrdnglllhihramhavidrqknhgmhfrvlakalrlsggdhih
sgtvvgklegerditlgfvdllrddytekdrsrgiyftqswvstpgvlpvasggihvwhm
palteifgddsvlqfgggtlghpwgnapgavanrvaleacvqarnegrdlaregntiire
atkwspelaaacevwk
>d1aa1e2 4.47.9.1.2 (21-147) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
kltyytpeyetldtdilaafrvspqpgvppeeagaavaaesstgtwttvwtdgltnldry
kgrcyhiepvageenqyicyvaypldlfeegsvtnmftsivgnvfgfkalralrledlri
pvayvkt
>d1aa1f_ 4.55.1.1.2 Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
mqvwpilnlkkyetlsylpplttdqlarqvdyllnnkwvpclefetdhgfvyrehhnspg
yydgrywtmwklpmfgctdpaqvlneleeckkeypnafiriigfdsnrevqcisfiaykp
agy
>d1aa1h1 3.1.12.1.2 (148-463) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
fqgpphgiqverdklnkygrpllgctikpklglsaknygravyeclrggldftxddenvn
sqpfmrwrdrflfcaealykaqaetgeikghylnatagtcedmmkravfarelgvpivmh
dyltggftanttlshycrdnglllhihramhavidrqknhgmhfrvlakalrlsggdhih
sgtvvgklegerditlgfvdllrddytekdrsrgiyftqswvstpgvlpvasggihvwhm
palteifgddsvlqfgggtlghpwgnapgavanrvaleacvqarnegrdlaregntiire
atkwspelaaacevwk
>d1aa1h2 4.47.9.1.2 (21-147) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
kltyytpeyetldtdilaafrvspqpgvppeeagaavaaesstgtwttvwtdgltnldry
kgrcyhiepvageenqyicyvaypldlfeegsvtnmftsivgnvfgfkalralrledlri
pvayvkt
>d1aa1i_ 4.55.1.1.2 Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
mqvwpilnlkkyetlsylpplttdqlarqvdyllnnkwvpclefetdhgfvyrehhnspg
yydgrywtmwklpmfgctdpaqvlneleeckkeypnafiriigfdsnrevqcisfiaykp
agy
>d1aa1l1 3.1.12.1.2 (148-463) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
fqgpphgiqverdklnkygrpllgctikpklglsaknygravyeclrggldftxddenvn
sqpfmrwrdrflfcaealykaqaetgeikghylnatagtcedmmkravfarelgvpivmh
dyltggftanttlshycrdnglllhihramhavidrqknhgmhfrvlakalrlsggdhih
sgtvvgklegerditlgfvdllrddytekdrsrgiyftqswvstpgvlpvasggihvwhm
palteifgddsvlqfgggtlghpwgnapgavanrvaleacvqarnegrdlaregntiire
atkwspelaaacevwk
>d1aa1l2 4.47.9.1.2 (21-147) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
kltyytpeyetldtdilaafrvspqpgvppeeagaavaaesstgtwttvwtdgltnldry
kgrcyhiepvageenqyicyvaypldlfeegsvtnmftsivgnvfgfkalralrledlri
pvayvkt
>d1aa1s_ 4.55.1.1.2 Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
mqvwpilnlkkyetlsylpplttdqlarqvdyllnnkwvpclefetdhgfvyrehhnspg
yydgrywtmwklpmfgctdpaqvlneleeckkeypnafiriigfdsnrevqcisfiaykp
agy
>d1aa2__ 1.43.1.1.1 beta-spectrin {Human (Homo sapiens)}
ksakdalllwcqmktagypnvnihnfttswrdgmafnalihkhrpdlidfdklkksnahy
nlqnafnlaeqhlgltklldpedisvdhpdeksiityvvtyyhyfskm
>d1aa3__ 4.39.1.1.1 RecA protein, C-terminal domain {Escherichia coli}
infygelvdlgvkekliekagawysykgekigqgkanatawlkdnpetakeiekkvrell
lsn
>d1aa4__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1aa6_1 2.46.2.2.3 (565-715) Formate dehydrogenase H {Escherichia coli}
pidkltdeypmvlstvrevghyscrsmtgncaalaaladepgyaqintedakrlgiedea
lvwvhsrkgkiitraqvsdrpnkgaiymtyqwwigacnelvtenlspitktpeykycavr
vepiadqraaeqyvideynklktrlreaala
>d1aa6_2 3.70.1.1.3 (1-564) Formate dehydrogenase H {Escherichia coli}
mkkvvtvcpycasgckinlvvdngkivraeaaqgktnqgtlclkgyygwdfindtqiltp
rlktpmirrqrggklepvswdealnyvaerlsaikekygpdaiqttgssrgtgnetnyvm
qkfaravigtnnvdccarvxhgpsvaglhqsvgngamsnaineidntdlvfvfgynpads
hpivanhvinakrngakiivcdprkietariadmhialkngsniallnamghviieenly
dkafvasrtegfeeyrkivegytpesveditgvsaseirqaarmyaqaksaailwgmgvt
qfyqgvetvrsltslamltgnlgkphagvnpvrgqnnvqgacdmgalpdtypgyqyvkdp
anrekfakawgveslpahtgyriselphraahgevraayimgedplqtdaelsavrkafe
dlelvivqdifmtktasaadvilpstswgehegvftaadrgfqrffkavepkwdlktdwq
iiseiatrmgypmhynntqeiwdelrhlcpdfygatyekmgelgfiqwpcrdtsdadqgt
sylfkekfdtpnglaqfftcdwva
>d1aa7a_ 1.91.1.1.1 Influenza virus matrix protein M1 {Influenza virus}
mslltevetyvlsiipsgplkaeiaqrledvfagkntdlevlmewlktrpilspltkgil
gfvftltvpserglqrrrfvqnalngngdpnnmdkavklyrklkreitfhgakeislsys
agalascmgliynrmgavttevafglvcatceqiadsq
>d1aa7b_ 1.91.1.1.1 Influenza virus matrix protein M1 {Influenza virus}
slltevetyvlsiipsgplkaeiaqrledvfagkntdlevlmewlktrpilspltkgilg
fvftltvpserglqrrrfvqnalngngdpnnmdkavklyrklkreitfhgakeislsysa
galascmgliynrmgavttevafglvcatceqiadsq
>d1aa8a1 3.4.1.2.1 (1-194,288-340) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernll
>d1aa8a2 4.14.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1aa8b1 3.4.1.2.1 (1-194,288-340) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernll
>d1aa8b2 4.14.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1aa9__ 3.30.1.6.1 cH-p21 Ras protein {Human (Homo sapiens)}
mteyklvvvgaggvgksaltiqliqnhfvdeydptiedsyrkqvvidgetclldildtag
qeeysamrdqymrtgegflcvfainntksfedihqyreqikrvkdsddvpmvlvgnkcdl
aartvesrqaqdlarsygipyietsaktrqgvedafytlvreirqhklrkl
>d1aab__ 1.22.1.1.1 HMG1, domains A and B {Rat/Hamster (Rattus norvegicus/Cricetulus griseus)}
gkgdpkkprgkmssyaffvqtsreehkkkhpdasvnfsefskkcserwktmsakekgkfe
dmakadkaryeremktyippkge
>d1aac__ 2.5.1.1.1 Amicyanin {Paracoccus denitrificans}
dkatipsespfaaaevadgaivvdiakmkyetpelhvkvgdtvtwinreamphnvhfvag
vlgeaalkgpmmkkeqaysltfteagtydyhctphpfmrgkvvve
>d1aaf__ 7.34.1.1.2 HIV nucleocapsid {Human immunodeficiency virus, type 1, Mn isolate}
mqrgnfrnqrkiikcfncgkeghiakncraprkrgcwkcgkeghqmkdcterqan
>d1aaj__ 2.5.1.1.1 Amicyanin {Paracoccus denitrificans}
dkatipsespfaaaevadgaivvdiakmkyetpelhvkvgdtvtwinreamphnvhfvag
vlgeaalkgpmmkkeqaysltfteagtydyhctphpfmrgkvvve
>d1aala_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglvqtfvyggcrakrnnfksaedamrtcgga
>d1aalb_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglvqtfvyggcrakrnnfksaedamrtcgg
>d1aam__ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaaidanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aan__ 2.5.1.1.1 Amicyanin {Paracoccus denitrificans}
dkatipsespfaaaevadgaivvdiakmkyetpelhvkvgdtvtwinreamphnvhfvag
vlgeaalkgpmmkkeqaysltfteagtydyhctphpfmrgkvvve
>d1aapa_ 7.8.1.1.4 Alzheimer's amyloid B-protein precursor, APPI {Human (Homo sapiens)}
vrevcseqaetgpcramisrwyfdvtegkcapffyggcggnrnnfdteeycmavcg
>d1aapb_ 7.8.1.1.4 Alzheimer's amyloid B-protein precursor, APPI {Human (Homo sapiens)}
vrevcseqaetgpcramisrwyfdvtegkcapffyggcggnrnnfdteeycmavcg
>d1aaqa_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qiiieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1aaqb_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qiiieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1aara_ 4.13.2.1.1 Ubiquitin {Human (Homo sapiens)}
mqifvktltgktitlevepsdtienvkakiqdkegippdqqrlifagkqledgrtlsdyn
iqkestlhlvlrlrgg
>d1aarb_ 4.13.2.1.1 Ubiquitin {Human (Homo sapiens)}
mqifvktltgktitlevepsdtienvkakiqdkegippdqqrlifagkqledgrtlsdyn
iqkestlhlvlrlrgg
>d1aat__ 3.57.1.1.2 Aspartate aminotransferase, AAT {Chicken (Gallus gallus), cytosolic form}
aasifaavprappvavfkltadfredgdsrkvnlgvgayrtdegqpwvlpvvrkveqlia
gngslnheylpilglpefranasrialgddspaiaqkrvgsvqglggtgalrigaeflrr
wyngnnntatpvyvssptwenhnsvfmdagfkdirtyrywdaakrgldlqgllsdmekap
efsifilhacahnptgtdptpdewkqiaavmkrrclfpffdsayqgfasgnlekdawavr
yfvsegfelfcaqsfsknfglynervgnlsvvgkdednvqrvlsqmekivrttwsnppsq
garivattltspqlfaewkdnvktmadrvllmrselrsrleslgtpgtwnhitdqigmfs
ftglnpkqveymikekhiylmasgrinmcglttknldyvaksiheavtkiq
>d1aaw__ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aax__ 3.37.1.3.1 Tyrosine phosphatase {Human (Homo sapiens), 1B}
emekefeqidksgswaaiyqdirheasdfpcrvaklpknknrnryrdvspfdhsriklhq
edndyinaslikmeeaqrsyiltqgplpntcghfwemvweqksrgvvmlnrvmekgslkc
aqywpqkeekemifedtnlkltlisediksyytvrqlelenlttqetreilhfhyttwpd
fgvpespasflnflfkvresgslspehgpvvvhssagigrsgtfcladtclllmdkrkdp
ssvdikkvllemrkfrmgliqtadqlrfsylaviegakfimgdssvqdqwkelshed
>d1aaya1 7.31.1.1.1 (103-131) ZIF268 {Mouse (Mus musculus)}
rpyacpvescdrrfsrsdeltrhirihtg
>d1aaya2 7.31.1.1.1 (132-159) ZIF268 {Mouse (Mus musculus)}
qkpfqcricmrnfsrsdhltthirthtg
>d1aaya3 7.31.1.1.1 (160-187) ZIF268 {Mouse (Mus musculus)}
ekpfacdicgrkfarsderkrhtkihlr
>d1aaza_ 3.38.1.1.6 Glutaredoxin {Bacteriophage T4}
mfkvygydsnihkcvycdnakrlltvkkqpfefinimpekgvfddekiaelltklgrdtq
igltmpqvfapdgshiggfdqlreyfk
>d1aazb_ 3.38.1.1.6 Glutaredoxin {Bacteriophage T4}
mfkvygydsnihkcvycdnakrlltvkkqpfefinimpekgvfddekiaelltklgrdtq
igltmpqvfapdgshiggfdqlreyfk
>d1ab0__ 2.53.1.2.6 Adipocyte lipid-binding protein, ALBP {Mouse (Mus musculus)}
gdafvgtwklvssenfddymkevgvgfatrkdagmakpnmiisvngdlvtirsesthknt
eisfklgvefdeitaddrkvksiitldggalvqvqkwdgksttikrkrdgdklvvecvmk
gvtstrvyera
>d1ab1__ 7.13.1.1.1 Crambin {Abyssinian cabbage (Crambe abyssinica)}
ttccpsivarsnfnvcrlpgtseaicatytgciiipgatcpgdyan
>d1ab2__ 4.72.1.1.12 Proto-oncogen tyrosine kinase {Human (Homo sapiens)}
gsgnslekhswyhgpvsrnaaeyllssgingsflvresesspgqrsislryegrvyhyri
ntasdgklyvssesrfntlaelvhhhstvadglittlhypapkrgihrd
>d1ab3__ 1.16.1.2.2 Ribosomal protein S15 {Thermus thermophilus}
pitkeekqkviqefarfpgdtgstevqvalltlrinrlsehlkvhkkdhhshrgllmmvg
qrrrllrylqredperyralieklgirg
>d1ab4__ 5.11.1.1.2 DNA Gyrase A {Escherichia coli}
vgralpdvrdglkpvhrrvlyamnvlgndwnkaykksarvvgdvigkyhphgdsavydti
vrmaqpfslrymlvdgqgnfgsidgdsaaamryteirlakiahelmadleketvdfvdny
dgtekipdvmptkipnllvngssgiavgmatnipphnltevingclayiddedisieglm
ehipgpdfptaaiingrrgieeayrtgrgkvyiraraevevetiivheipyqvnkarlie
kiaelvkekrvegisalrdesdkdgmriviegevvlnnlysqtqlqvsfginmvalhhgq
pkimnlkdiiaafvrhrrevvtrrtifelrkardrahilealavalanidpiielirhap
tpaeaktalvanpwqlgnvaamledaarpewlepefgvrdglyylteqqaqaildlrlqk
ltgleheklldeykelldqiaellrilgsadrlmevireelelvreqfgdkrrteit
>d1ab5a_ 3.16.2.1.1 CheY protein {Escherichia coli}
elkflvvddnstmrritrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmpnmd
glellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleeklnkif
eklgm
>d1ab5b_ 3.16.2.1.1 CheY protein {Escherichia coli}
elkflvvddnstmrritrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmpnmd
glellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleeklnkif
eklgm
>d1ab6a_ 3.16.2.1.1 CheY protein {Escherichia coli}
elkflvvddnstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmpnmd
glellktiradgamsalpvlmttaeakkeniiaaaqagasgyvvkpftaatleeklnkif
eklgm
>d1ab6b_ 3.16.2.1.1 CheY protein {Escherichia coli}
elkflvvddnstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmpnmd
glellktiradgamsalpvlmttaeakkeniiaaaqagasgyvvkpftaatleeklnkif
eklgm
>d1ab7__ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdaltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegaditiils
>d1ab8a_ 4.47.24.1.1 Type II adenylyl cyclase C2 domain {Rat (Rattus norvegicus)}
lyhqsydcvcvmfasipdfkefytesdvnkegleclrllneiiadfddllskpkfsgvek
iktigstymaatglsaipsqehaqeperqymhigtmvefayalvgkldainkhsfndfkl
rvginhgpviagvigaqkpqydiwgntvnvasrmdstgvldkiqvteetslilqtlgytc
tc
>d1ab8b_ 4.47.24.1.1 Type II adenylyl cyclase C2 domain {Rat (Rattus norvegicus)}
eelyhqsydcvcvmfasipdfkefytesdvnkegleclrllneiiadfddllskpkfsgv
ekiktigstymaatglsaipsqehaqeperqymhigtmvefayalvgkldainkhsfndf
klrvginhgpviagvigaqkpqydiwgntvnvasrmdstgvldkiqvteetslilqtlgy
tctc
>e1ab9.1b 2.41.1.2.7 (alpha,gamma)-chymotrypsin(ogen) {Bovine (Bos taurus)}
ivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgvttsdvvvagefdqgs
ssekiqklkiakvfknskynsltinnditllklstaasfsqtvsavclpsasddfaagtt
cvttgwgltry
>e1ab9.1c 2.41.1.2.7 (alpha,gamma)-chymotrypsin(ogen) {Bovine (Bos taurus)}
ntpdrlqqaslpllsntnckkywgtkikdamicagasgvsscmgdsggplvckkngawtl
vgivswgsstcststpgvyarvtalvnwvqqtlaan
>d1aba__ 3.38.1.1.6 Glutaredoxin {Bacteriophage T4}
mfkvygydsnihkcgpcdnakrlltvkkqpfefinimpekgvfddekiaelltklgrdtq
igltmpqvfapdgshiggfdqlreyfk
>d1abba_ 3.77.1.2.1 Glycogen phosphorylase {Rabbit (Oryctolagus cuniculus)}
rkqisvrglagvenvtelkknfnrhlhftlvkdrnvatprdyyfalahtvrdhlvgrwir
tqqhyyekdpkriyylslefymgrtlqntmvnlalenacdeatyqlgldmeeleeieeda
glgngglgrlaacfldsmatlglaaygygiryefgifnqkicggwqmeeaddwlrygnpw
ekarpeftlpvhfygrvehtsqgakwvdtqvvlampydtpvpgyrnnvvntmrlwsakap
ndfnlkdfnvggyiqavldrnlaenisrvlypndnffegkelrlkqeyfvvaatlqdiir
rfksskfgcrdpvrtnfdafpdkvaiqlndthpslaipelmrvlvdlerldwdkawevtv
ktcaytnhtvipealerwpvhlletllprhlqiiyeinqrflnrvaaafpgdvdrlrrms
lveegavkrinmahlciagshavngvarihseilkktifkdfyelephkfqnktngitpr
rwlvlcnpglaeiiaerigeeyisdldqlrkllsyvddeafirdvakvkqenklkfaayl
ereykvhinpnslfdvqvkriheykrqllnclhvitlynrikkepnkfvvprtvmiggka
apgyhmakmiiklitaigdvvnhdpvvgdrlrviflenyrvslaekvipaadlseqista
gteasgtgnmkfmlngaltigtmdganvemaeeageenffifgmrvedvdrldqrgynaq
eyydripelrqiieqlssgffspkqpdlfkdivnmlmhhdrfkvfadyeeyvkcqervsa
lyknprewtrmvirniatsgkfssdrtiaqyareiwgvepsrqrlpap
>d1abbb_ 3.77.1.2.1 Glycogen phosphorylase {Rabbit (Oryctolagus cuniculus)}
rkqisvrglagvenvtelkknfnrhlhftlvkdrnvatprdyyfalahtvrdhlvgrwir
tqqhyyekdpkriyylslefymgrtlqntmvnlalenacdeatyqlgldmeeleeieeda
glgngglgrlaacfldsmatlglaaygygiryefgifnqkicggwqmeeaddwlrygnpw
ekarpeftlpvhfygrvehtsqgakwvdtqvvlampydtpvpgyrnnvvntmrlwsakap
ndfnlkdfnvggyiqavldrnlaenisrvlypndnffegkelrlkqeyfvvaatlqdiir
rfksskfgcrdpvrtnfdafpdkvaiqlndthpslaipelmrvlvdlerldwdkawevtv
ktcaytnhtvipealerwpvhlletllprhlqiiyeinqrflnrvaaafpgdvdrlrrms
lveegavkrinmahlciagshavngvarihseilkktifkdfyelephkfqnktngitpr
rwlvlcnpglaeiiaerigeeyisdldqlrkllsyvddeafirdvakvkqenklkfaayl
ereykvhinpnslfdvqvkriheykrqllnclhvitlynrikkepnkfvvprtvmiggka
apgyhmakmiiklitaigdvvnhdpvvgdrlrviflenyrvslaekvipaadlseqista
gteasgtgnmkfmlngaltigtmdganvemaeeageenffifgmrvedvdrldqrgynaq
eyydripelrqiieqlssgffspkqpdlfkdivnmlmhhdrfkvfadyeeyvkcqervsa
lyknprewtrmvirniatsgkfssdrtiaqyareiwgvepsrqrlpap
>d1abbc_ 3.77.1.2.1 Glycogen phosphorylase {Rabbit (Oryctolagus cuniculus)}
rkqisvrglagvenvtelkknfnrhlhftlvkdrnvatprdyyfalahtvrdhlvgrwir
tqqhyyekdpkriyylslefymgrtlqntmvnlalenacdeatyqlgldmeeleeieeda
glgngglgrlaacfldsmatlglaaygygiryefgifnqkicggwqmeeaddwlrygnpw
ekarpeftlpvhfygrvehtsqgakwvdtqvvlampydtpvpgyrnnvvntmrlwsakap
ndfnlkdfnvggyiqavldrnlaenisrvlypndnffegkelrlkqeyfvvaatlqdiir
rfksskfgcrdpvrtnfdafpdkvaiqlndthpslaipelmrvlvdlerldwdkawevtv
ktcaytnhtvipealerwpvhlletllprhlqiiyeinqrflnrvaaafpgdvdrlrrms
lveegavkrinmahlciagshavngvarihseilkktifkdfyelephkfqnktngitpr
rwlvlcnpglaeiiaerigeeyisdldqlrkllsyvddeafirdvakvkqenklkfaayl
ereykvhinpnslfdvqvkriheykrqllnclhvitlynrikkepnkfvvprtvmiggka
apgyhmakmiiklitaigdvvnhdpvvgdrlrviflenyrvslaekvipaadlseqista
gteasgtgnmkfmlngaltigtmdganvemaeeageenffifgmrvedvdrldqrgynaq
eyydripelrqiieqlssgffspkqpdlfkdivnmlmhhdrfkvfadyeeyvkcqervsa
lyknprewtrmvirniatsgkfssdrtiaqyareiwgvepsrqrlpap
>d1abbd_ 3.77.1.2.1 Glycogen phosphorylase {Rabbit (Oryctolagus cuniculus)}
rkqisvrglagvenvtelkknfnrhlhftlvkdrnvatprdyyfalahtvrdhlvgrwir
tqqhyyekdpkriyylslefymgrtlqntmvnlalenacdeatyqlgldmeeleeieeda
glgngglgrlaacfldsmatlglaaygygiryefgifnqkicggwqmeeaddwlrygnpw
ekarpeftlpvhfygrvehtsqgakwvdtqvvlampydtpvpgyrnnvvntmrlwsakap
ndfnlkdfnvggyiqavldrnlaenisrvlypndnffegkelrlkqeyfvvaatlqdiir
rfksskfgcrdpvrtnfdafpdkvaiqlndthpslaipelmrvlvdlerldwdkawevtv
ktcaytnhtvipealerwpvhlletllprhlqiiyeinqrflnrvaaafpgdvdrlrrms
lveegavkrinmahlciagshavngvarihseilkktifkdfyelephkfqnktngitpr
rwlvlcnpglaeiiaerigeeyisdldqlrkllsyvddeafirdvakvkqenklkfaayl
ereykvhinpnslfdvqvkriheykrqllnclhvitlynrikkepnkfvvprtvmiggka
apgyhmakmiiklitaigdvvnhdpvvgdrlrviflenyrvslaekvipaadlseqista
gteasgtgnmkfmlngaltigtmdganvemaeeageenffifgmrvedvdrldqrgynaq
eyydripelrqiieqlssgffspkqpdlfkdivnmlmhhdrfkvfadyeeyvkcqervsa
lyknprewtrmvirniatsgkfssdrtiaqyareiwgvepsrqrlpap
>d1abe__ 3.83.1.1.2 L-arabinose-binding protein {Escherichia coli}
nlklgflvkqpeepwfqtewkfadkagkdlgfevikiavpdgektlnaidslaasgakgf
victpdpklgsaivakargydmkviavddqfvnakgkpmdtvplvmmaatkigerqgqel
ykemqkrgwdvkesavmaitaneldtarrrttgsmdalkaagfpekqiyqvptksndipg
afdaansmlvqhpevkhwlivgmndstvlggvrategqgfkaadiigigingvdavsels
kaqatgfygsllpspdvhgykssemlynwvakdveppkftevtdvvlitrdnfkeelekk
glggk
>d1abf__ 3.83.1.1.2 L-arabinose-binding protein {Escherichia coli}
nlklgflvkqpeepwfqtewkfadkagkdlgfevikiavpdgektlnaidslaasgakgf
victpdpklgsaivakargydmkviavddqfvnakgkpmdtvplvmmaatkigerqgqel
ykemqkrgwdvkesavmaitaneldtarrrttgsmdalkaagfpekqiyqvptksndipg
afdaansmlvqhpevkhwlivgmndstvlggvrategqgfkaadiigigingvdavsels
kaqatgfygsllpspdvhgykssemlynwvakdveppkftevtdvvlitrdnfkeelekk
glggk
>e1abi.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>e1abi.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
sgeadcglrplfekksledkterellesyidgr
>e1abj.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1abj.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>d1abma1 1.2.7.1.6 (1-83) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaayvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1abma2 4.37.1.1.3 (84-198) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
ngggepkgelleaikrdfgsfdkfkekltaasvgvqgsgwgwlgfnkerghlqiaacpnq
dplqgttglipllgidvwehayylqyknvrpdylkaiwnvinwenvterymackk
>d1abmb1 1.2.7.1.6 (1-83) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaayvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1abmb2 4.37.1.1.3 (84-198) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
ngggepkgelleaikrdfgsfdkfkekltaasvgvqgsgwgwlgfnkerghlqiaacpnq
dplqgttglipllgidvwehayylqyknvrpdylkaiwnvinwenvterymackk
>d1abn__ 3.1.6.1.3 Aldose reductase (aldehyde reductase) {Human (Homo sapiens)}
srlllnngakmpilglgtwksppgqvteavkvaidvgyrhidcahvyqnenevgvaiqek
lreqvvkreelfivsklwctyhekglvkgacqktlsdlkldyldlylihwptgfkpgkef
fpldesgnvvpsdtnildtwaameelvdeglvkaigisnfnhlqvemilnkpglkykpav
nqiechpyltqekliqycqskgivvtaysplgspdrpwakpedpslledprikaiaakhn
kttaqvlirfpmqrnlvvipksvtperiaenfkvfdfelssqdmttllsynrnwrvsall
sctshkdypfheef
>d1aboa_ 2.30.2.1.4 Abl tyrosine kinase, SH3 domain {Mouse (Mus musculus)}
nlfvalydfvasgdntlsitkgeklrvlgynhngewceaqtkngqgwvpsnyitpvns
>d1abob_ 2.30.2.1.4 Abl tyrosine kinase, SH3 domain {Mouse (Mus musculus)}
nlfvalydfvasgdntlsitkgeklrvlgynhngewceaqtkngqgwvpsnyitpvns
>d1abq__ 2.30.2.1.4 Abl tyrosine kinase, SH3 domain {Mouse (Mus musculus)}
lfvalydfvasgdntlsitkgeklrvlgynhngewceaqtkngqgwvpsnyitpvn
>d1abra_ 4.135.1.1.5 Abrin A-chain {Abrus precatorius}
edrpikfstegatsqsykqfiealrerlrgglihdipvlpdpttlqernryitvelsnsd
tesievgidvtnayvvayragtqsyflrdapssasdylftgtdqhslpfygtygdlerwa
hqsrqqiplglqalthgisffrsggndneekartliviiqmvaeaarfryisnrvrvsiq
tgtafqpdaamislennwdnlsrgvqesvqdtfpnqvtltnirnepvivdslshptvavl
almlfvcnppn
>d1abrb1 2.37.2.1.2 (1-140) Plant cytotoxin B-chain (lectin) {Abrus precatorius}
ivekskicssryeptvriggrdgmcvdvydngyhngnriimwkckdrleenqlwtlksdk
tirsngkclttygyapgsyvmiydctsavaeatyweiwdngtiinpksalvlsaesssmg
gtltvqtneylmrqgwrtgn
>d1abrb2 2.37.2.1.2 (141-267) Plant cytotoxin B-chain (lectin) {Abrus precatorius}
ntspfvtsisgysdlcmqaqgsnvwmadcdsnkkeqqwalytdgsirsvqntnncltskd
hkqgstillmgcsngwasqrwvfkndgsiyslyddmvmdvkgsdpslkqiilwpytgkpn
qiwltlf
>d1abs__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1abta_ 7.7.1.1.10 Bungarotoxin {Alpha-bungarotoxin (Bungarus multicinctus)}
ivchttatspisavtcppgenlcyrkmwcdafcssrgkvvelgcaatcpskkpyeevtcc
stdkcnphpkqrpg
>d1abv__ 1.71.1.1.1 N-terminal domain of the delta subunit of the F1F0-ATP synthase {Escherichia coli}
sefitvarpyakaafdfavehqsverwqdmlafaaevtkneqmaellsgalapetlaesf
iavcgeqldengqnlirvmaengrlnalpdvleqfihlravseat
>d1abwa1 1.1.1.1.16 (1-142) Hemoglobin, alpha-chain {Human (Homo sapiens)}
mlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyrg
>d1abwa2 1.1.1.1.16 (143-283) Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1abwb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgkvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1abwd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgkvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1abya1 1.1.1.1.16 (1-142) Hemoglobin, alpha-chain {Human (Homo sapiens)}
mlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyrg
>d1abya2 1.1.1.1.16 (143-283) Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1abyb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgkvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1abyd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgkvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1ac0__ 2.3.1.1.5 Glucoamilase, granular starch-binding domain {Aspergillus niger}
cttptavavtfdltatttygeniylvgsisqlgdwetsdgialsadkytssdplwyvtvt
lpagesfeykfiriesddsvewesdpnreytvpqacgtstatvtdtwr
>d1ac1a1 1.47.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1ac1a2 3.38.1.4.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
aqyedgkqyttlekpvagapqvleffsffcplcyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsek
>d1ac1b1 1.47.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1ac1b2 3.38.1.4.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
aqyedgkqyttlekpvagapqvleffsffcplcyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsek
>d1ac4__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1ac5__ 3.59.1.4.3 Serine carboxypeptidase II {Baker's yeast (Saccharomyces cerevisiae), kex1(delta)p}
lpsseeykvayellpglsevpdpsnipqmhaghiplrsedadeqdssdleyffwkftnnd
sngnvdrpliiwlnggpgcssmdgalvesgpfrvnsdgklylnegswiskgdllfidqpt
gtgfsveqnkdegkidknkfdedledvtkhfmdflenyfkifpedltrkiilsgesyagq
yipffanailnhnkfskidgdtydlkalligngwidpntqslsylpfamekklidesnpn
fkhltnahencqnlinsastdeaahfsyqecenilnlllsytressqkgtadclnmynfn
lkdsypscgmnwpkdisfvskffstpgvidslhldsdkidhwkectnsvgtklsnpiskp
sihllpgllesgieivlfngdkdlicnnkgvldtidnlkwggikgfsddavsfdwihksk
stddseefsgyvkydrnltfvsvynashmvpfdkslvsrgivdiysndvmiidnngknvm
itt
>d1ac6a_ 2.1.1.1.155 T-cell antigen receptor {Human (Homo sapiens), alpha-chain}
dsvtqtegqvalseedfltihcnysasgypalfwyvqypgegpqflfrasrdkekgssrg
featynkeatsfhlqkasvqesdsavyycalsggnnkltfgagtkltikp
>d1ac6b_ 2.1.1.1.155 T-cell antigen receptor {Human (Homo sapiens), alpha-chain}
dsvtqtegqvalseedfltihcnysasgypalfwyvqypgegpqflfrasrdkekgssrg
featynkeatsfhlqkasvqesdsavyycalsggnnkltfgagtkltikp
>d1ac8__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aca__ 1.11.1.1.1 Acyl-CoA binding protein {Bovine (Bos taurus)}
sqaefdkaaeevkhlktkpadeemlfiyshykqatvgdinterpgmldfkgkakwdawne
lkgtskedamkayidkveelkkkygi
>d1acbe_ 2.41.1.2.7 (alpha,gamma)-chymotrypsin(ogen) {Bovine (Bos taurus)}
cgvpaiqpvlsglsrivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgv
ttsdvvvagefdqgsssekiqklkiakvfknskynsltinnditllklstaasfsqtvsa
vclpsasddfaagttcvttgwgltrytnantpdrlqqaslpllsntnckkywgtkikdam
icagasgvsscmgdsggplvckkngawtlvgivswgsstcststpgvyarvtalvnwvqq
tlaan
>d1acbi_ 4.33.1.1.1 Eglin C {Leech (Hirudo medicinalis)}
ksfpevvgktvdqareyftlhypqydvyflpegspvtldlrynrvrvfynpgtnvvnhvp
hvg
>d1acc__ 6.10.1.1.1 Anthrax protective antigen {Anthrax bacillus (Bacillus anthracis)}
sssqgllgyyfsdlnfqapmvvtssttgdlsipsselenipsenqyfqsaiwsgfikvkk
sdeytfatsadnhvtmwvddqevinkasnsnkirlekgrlyqikiqyqrenptekgldfk
lywtdsqnkkevissdnlqlpelkqkssnsrkkrstsagptvpdrdndgipdslevegyt
vdvknkrtflspwisnihekkgltkyksspekwstasdpysdfekvtgridknvspearh
plvaaypivhvdmeniilsknedqstqntdsetrtiskntstsrthtsevhgnaevhasf
fdiggsvsagfsnsnsstvaidhslslagertwaetmglntadtarlnaniryvntgtap
iynvlpttslvlgknqtlatikakenqlsqilapnnyypsknlapialnaqddfsstpit
mnynqflelektkqlrldtdqvygniatynfengrvrvdtgsnwsevlpqiqettariif
ngkdlnlverriaavnpsdplettkpdmtlkealkiafgfnepngnlqyqgkditefdfn
fdqqtsqniknqlaelnatniytvldkiklnakmnilirdkrfhydrnniavgadesvvk
eahrevinssteglllnidkdirkilsgyiveiedteglkevindrydmlnisslrqdgk
tfidfkkyndklplyisnpnykvnvyavtkentiinpsengdtstngikkilifskkgye
ig
>d1acd__ 2.53.1.2.6 Adipocyte lipid-binding protein, ALBP {Mouse (Mus musculus)}
gdafvgtwklvssenfddymkevgvgfatrkdagmakpnmiisvngdlvtirsesthknt
eisfklgvefdeitaddrkvksiitldggalvqvqkwdgksttikrkrdgdklvvexvmk
gvtstrvyera
>d1acf__ 4.86.1.1.3 Profilin (actin-binding protein) {Acanthamoeba castellanii}
swqtyvdtnlvgtgavtqaailgldgntwatsagfavtpaqgttlagafnnadairaggf
dlagvhyvtlraddrsiygkkgssgvitvktskailvgvynekiqpgtaanvvekladyl
igqgf
>d1aci__ 1.4.4.1.1 Ribosomal protein L11, C-terminal domain {Bacillus stearothermophilus}
mtfitktppaavllkkaagiesgsgepnrnkvatikrdkvreiaelkmpdlnaasieaam
rmiegtarsmgivved
>d1acj__ 3.59.1.1.1 Acetylcholinesterase {Electric ray (Torpedo californica)}
sellvntksgkvmgtrvpvlsshisaflgipfaeppvgnmrfrrpepkkpwsgvwnasty
pnncqqyvdeqfpgfsgsemwnpnremsedclylniwvpsprpksttvmvwiygggfysg
sstldvyngkylayteevvlvslsyrvgafgflalhgsqeapgnvglldqrmalqwvhdn
iqffggdpktvtifgesaggasvgmhilspgsrdlfrrailqsgspncpwasvsvaegrr
ravelgrnlncnlnsdeelihclrekkpqelidvewnvlpfdsifrfsfvpvidgeffpt
slesmlnsgnfkktqillgvnkdegsffllygapgfskdseskisredfmsgvklsvpha
ndlgldavtlqytdwmddnngiknrdglddivgdhnvicplmhfvnkytkfgngtylyff
nhrasnlvwpewmgvihgyeiefvfglplvkelnytaeeealsrrimhywatfaktgnpn
ephsqeskwplfttkeqkfidlntepmkvhqrlrvqmcvfwnqflpkllnat
>d1acl__ 3.59.1.1.1 Acetylcholinesterase {Electric ray (Torpedo californica)}
sellvntksgkvmgtrvpvlsshisaflgipfaeppvgnmrfrrpepkkpwsgvwnasty
pnncqqyvdeqfpgfsgsemwnpnremsedclylniwvpsprpksttvmvwiygggfysg
sstldvyngkylayteevvlvslsyrvgafgflalhgsqeapgnvglldqrmalqwvhdn
iqffggdpktvtifgesaggasvgmhilspgsrdlfrrailqsgspncpwasvsvaegrr
ravelgrnlncnlnsdeelihclrekkpqelidvewnvlpfdsifrfsfvpvidgeffpt
slesmlnsgnfkktqillgvnkdegsffllygapgfskdseskisredfmsgvklsvpha
ndlgldavtlqytdwmddnngiknrdglddivgdhnvicplmhfvnkytkfgngtylyff
nhrasnlvwpewmgvihgyeiefvfglplvkelnytaeeealsrrimhywatfaktgnpn
ephsqeskwplfttkeqkfidlntepmkvhqrlrvqmcvfwnqflpkllnat
>d1acma1 3.66.1.1.1 (1-150) Aspartate carbamoyltransferase catalytic subunit {Escherichia coli}
anplyqkhiisindlsrddlnlvlataaklkanpqpellkhkviascffeastatrlsfq
tsmhrlgasvvgfsdsantslgkkgetladtisvistyvdaivmrhpqegaarlatefsg
nvpvlnagdgsnqhptqtlldlftiqqteg
>d1acma2 3.66.1.1.1 (151-310) Aspartate carbamoyltransferase catalytic subunit {Escherichia coli}
rldnlhvamvgdlkygrtvhsltqalakfdgnrfyfiapdalampeyildmldekgiaws
lhssieevmaevdilymtrvqkerldpseyanvkaqfvlrasdlhnakanmkvlhplprv
deiatdvdktphawyfqqagngifarqallalvlnrdlvl
>d1acmb1 4.47.2.1.1 (8-100) Aspartate carbamoyltransferase {Escherichia coli}
gveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlikientfls
edqvdqlalyapqatvnridnyevvgksrpslp
>d1acmb2 7.35.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1acmc1 3.66.1.1.1 (1-150) Aspartate carbamoyltransferase catalytic subunit {Escherichia coli}
anplyqkhiisindlsrddlnlvlataaklkanpqpellkhkviascffeastatrlsfq
tsmhrlgasvvgfsdsantslgkkgetladtisvistyvdaivmrhpqegaarlatefsg
nvpvlnagdgsnqhptqtlldlftiqqteg
>d1acmc2 3.66.1.1.1 (151-310) Aspartate carbamoyltransferase catalytic subunit {Escherichia coli}
rldnlhvamvgdlkygrtvhsltqalakfdgnrfyfiapdalampeyildmldekgiaws
lhssieevmaevdilymtrvqkerldpseyanvkaqfvlrasdlhnakanmkvlhplprv
deiatdvdktphawyfqqagngifarqallalvlnrdlvl
>d1acmd1 4.47.2.1.1 (8-100) Aspartate carbamoyltransferase {Escherichia coli}
gveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlikientfls
edqvdqlalyapqatvnridnyevvgksrpslp
>d1acmd2 7.35.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1aco_1 3.7.2.1.2 (529-754) Aconitase, C-terminal domain {Bovine (Bos taurus)}
vdvsptsqrlqllepfdkwdgkdledlqilikvkgkcttdhisaagpwlkfrghldnisn
nlligainsenrkansvrnavtqefgpvpdtaryykqhgirwvvigdenygegssrehsa
leprflggraiitksfarihetnlkkqgllpltfadpadynkihpvdkltiqglkdfapg
kpltciikhpngtqetillnhtfnetqiewfragsalnrmkelqqk
>d1aco_2 3.72.1.1.2 (2-528) Aconitase, first 3 domains {Bovine (Bos taurus)}
rakvamshfepheyirydlleknidivrkrlnrpltlsekivyghlddpanqeiergkty
lrlrpdrvamqdataqmamlqfissglpkvavpstihcdhlieaqlggekdlrrakdinq
evynflatagakygvgfwrpgsgiihqiilenyaypgvlligtdshtpnggglggicigv
ggadavdvmagipwelkcpkvigvkltgslsgwtspkdvilkvagiltvkggtgaiveyh
gpgvdsisctgmaticnmgaeigattsvfpynhrmkkylsktgradianladefkdhlvp
dsgchydqlieinlselkphingpftpdlahpvaevgsvaekegwpldirvgligsctns
syedmgrsaavakqalahglkcksqftitpgseqiratierdgyaqvlrdvggivlanac
gpcigqwdrkdikkgekntivtsynrnftgrndanpethafvtspeivtalaiagtlkfn
petdfltgkdgkkfkleapdadelpraefdpgqdtyqhppkdssgqr
>d1acp__ 1.29.1.1.1 Acyl carrier protein {Escherichia coli}
stieervkkiigeqlgvkqeevtnnasfvedlgadsldtvelvmaleeefdteipdeeae
kittvqaaidyinghqa
>d1acva1 1.47.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1acva2 3.38.1.4.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
aqyedgkqyttlekpvagapqvleffsffcpscyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsek
>d1acvb1 1.47.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1acvb2 3.38.1.4.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
aqyedgkqyttlekpvagapqvleffsffcpscyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsek
>d1acw__ 7.3.7.2.14 Toxin analog P01 {Androctonus mauretanicus}
vscedcpehcstqkaqakcdndkcvcepi
>d1acx__ 2.1.7.1.3 Actinoxanthin {Actinomyces globisporus, number 1131}
apafsvspasgasdgqsvsvsvaaagetyyiaqcapvggqdacnpatatsfttdasgaas
fsftvrksyagqtpsgtpvgsvdcatdacnlgagnsglnlghvaltfg
>d1acyh1 2.1.1.1.31 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab 59.1 (mouse), kappa L chain}
qvklqesgpavikpsqslsltcivsgfsitrtnycwhwirqapgkglewmgricyegsiy
yspsiksrstisrdtslnkffiqlisvtnedtamyycsrenhmyetyfdvwgqgttvtvs
>d1acyh2 2.1.1.2.40 (113-226) Immunoglobulin (constant domains of L and H chains) {Fab 59.1 (mouse), kappa L chain}
sakttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqs
dlytlsssvtvpssprpsetvtcnvahpasstkvdkkivpr
>d1acyl1 2.1.1.1.31 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab 59.1 (mouse), kappa L chain}
divmtqspaslvvslgqratiscrasesvdsygksfmhwyqqkpgqppkvliyiasnles
gvparfsgsgsrtdftltidpveaddaatyycqqnnedpptfgagtklemrr
>d1acyl2 2.1.1.2.40 (109-211) Immunoglobulin (constant domains of L and H chains) {Fab 59.1 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1acz__ 2.3.1.1.5 Glucoamilase, granular starch-binding domain {Aspergillus niger}
cttptavavtfdltatttygeniylvgsisqlgdwetsdgialsadkytssdplwyvtvt
lpagesfeykfiriesddsvewesdpnreytvpqacgtstatvtdtwr
>d1ad0a1 2.1.1.1.80 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab A5B7 (engineered human construct), kappa L chain}
qtvltqspsslsvsvgdrvtitcrasssvtyihwyqqkpglapksliyatsnlasgvpsr
fsgsgsgtdytftisslqpediatyycqhwsskpptfgqgtkvevkr
>d1ad0a2 2.1.1.2.84 (108-213) Immunoglobulin (constant domains of L and H chains) {Fab A5B7 (engineered human construct), kappa L chain}
tvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqds
kdstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1ad0b1 2.1.1.1.80 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab A5B7 (engineered human construct), kappa L chain}
evqllesggglvqpggslrlscatsgftftdyymnwvrqapgkglewlgfignkangytt
eysasvkgrftisrdkskstlylqmntlqaedsaiyyctrdrglrfyfdywgqgtlvtvs
s
>d1ad0b2 2.1.1.2.84 (114-211) Immunoglobulin (constant domains of L and H chains) {Fab A5B7 (engineered human construct), kappa L chain}
astkgpsvfplapcsrstsestaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtktytcnvdhkpsntkvdkrve
>d1ad0c1 2.1.1.1.80 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab A5B7 (engineered human construct), kappa L chain}
qtvltqspsslsvsvgdrvtitcrasssvtyihwyqqkpglapksliyatsnlasgvpsr
fsgsgsgtdytftisslqpediatyycqhwsskpptfgqgtkvevkr
>d1ad0c2 2.1.1.2.84 (108-213) Immunoglobulin (constant domains of L and H chains) {Fab A5B7 (engineered human construct), kappa L chain}
tvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqds
kdstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1ad0d1 2.1.1.1.80 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab A5B7 (engineered human construct), kappa L chain}
evqllesggglvqpggslrlscatsgftftdyymnwvrqapgkglewlgfignkangytt
eysasvkgrftisrdkskstlylqmntlqaedsaiyyctrdrglrfyfdywgqgtlvtvs
s
>d1ad0d2 2.1.1.2.84 (114-211) Immunoglobulin (constant domains of L and H chains) {Fab A5B7 (engineered human construct), kappa L chain}
astkgpsvfplapcsrstsestaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtktytcnvdhkpsntkvdkrve
>d1ad1a_ 3.1.19.1.2 Dihydropteroate synthetase {Staphylococcus aureus}
tktkimgilnvtpdsfsdggkfnnvesavtrvkammdegadiidvggvstrpghemitve
eelnrvlpvveaivgfdvkisvdtfrsevaeaclklgvdiindqwaglydhrmfqvvaky
daeivlmhngngnrdepvveemltsllaqahqakiagipsnkiwldpgigfaktrneeae
vmarldelvateypvllatsrkrftkemmgydttpverdevtaattaygimkgvravrvh
nvelnaklakgidflkenenarhn
>d1ad1b_ 3.1.19.1.2 Dihydropteroate synthetase {Staphylococcus aureus}
tktkimgilnvtpdsfsdggkfnnvesavtrvkammdegadiidvggvstrpghemitve
eelnrvlpvveaivgfdvkisvdtfrsevaeaclklgvdiindqwaglydhrmfqvvaky
daeivlmhngngnrdepvveemltsllaqahqakiagipsnkiwldpgigfaktrneeae
vmarldelvateypvllatsrkrftkemmgydttpverdevtaattaygimkgvravrvh
nvelnaklakgidflkenenarhnfs
>d1ad2__ 5.20.1.1.1 Ribosomal protein L1 {Thermus thermophilus}
kryrallekvdpnkiytideaahlvkelatakfdetvevhaklgidprrsdqnvrgtvsl
phglgkqvrvlaiakgekikeaeeagadyvggeeiiqkildgwmdfdavvatpdvmgavg
sklgrilgprgllpnpkagtvgfnigeiireikagriefrndktgaihapvgkacfppek
ladnirafiraleahkpegakgtflrsvyvtttmgpsvrinphs
>d1ad3a_ 3.71.1.1.1 Aldehyde reductase (dehydrogenase), ALDH {Rat (Rattus norvegicus)}
sisdtvkrareafnsgktrslqfriqqlealqrminenlksisgalasdlgknewtsyye
evahvleeldttikelpdwaedepvaktrqtqqddlyihseplgvvlvigawnypfnlti
qpmvgavaagnavilkpsevsghmadllatlipqymdqnlylvvkggvpettellkerfd
himytgstavgkivmaaaakhltpvtlelggkspcyvdkdcdldvacrriawgkfmnsgq
tcvapdyilcdpsiqnqiveklkkslkdfygedakqsrdygriindrhfqrvkglidnqk
vahggtwdqssryiaptilvdvdpqspvmqeeifgpvmpivcvrsleeaiqfinqrekpl
alyvfsnnekvikkmiaetssggvtandvivhitvptlpfggvgnsgmgayhgkksfetf
shrrsclvksllneeahkaryppspa
>d1ad3b_ 3.71.1.1.1 Aldehyde reductase (dehydrogenase), ALDH {Rat (Rattus norvegicus)}
sisdtvkrareafnsgktrslqfriqqlealqrminenlksisgalasdlgknewtsyye
evahvleeldttikelpdwaedepvaktrqtqqddlyihseplgvvlvigawnypfnlti
qpmvgavaagnavilkpsevsghmadllatlipqymdqnlylvvkggvpettellkerfd
himytgstavgkivmaaaakhltpvtlelggkspcyvdkdcdldvacrriawgkfmnsgq
tcvapdyilcdpsiqnqiveklkkslkdfygedakqsrdygriindrhfqrvkglidnqk
vahggtwdqssryiaptilvdvdpqspvmqeeifgpvmpivcvrsleeaiqfinqrekpl
alyvfsnnekvikkmiaetssggvtandvivhitvptlpfggvgnsgmgayhgkksfetf
shrrsclvksllneeahkaryppspa
>d1ad4a_ 3.1.19.1.2 Dihydropteroate synthetase {Staphylococcus aureus}
tktkimgilnvtpdsfsdggkfnnvesavtrvkammdegadiidvggvstrpghemitve
eelnrvlpvveaivgfdvkisvdtfrsevaeaclklgvdiindqwaglydhrmfqvvaky
daeivlmhngngnrdepvveemltsllaqahqakiagipsnkiwldpgigfaktrneeae
vmarldelvateypvllatsrkrftkemmgydttpverdevtaattaygimkgvravrvh
nvelnaklakgidflkenenarh
>d1ad4b_ 3.1.19.1.2 Dihydropteroate synthetase {Staphylococcus aureus}
tktkimgilnvtpdsfsdggkfnnvesavtrvkammdegadiidvggvstrpghemitve
eelnrvlpvveaivgfdvkisvdtfrsevaeaclklgvdiindqwaglydhrmfqvvaky
daeivlmhngngnrdepvveemltsllaqahqakiagipsnkiwldpgigfaktrneeae
vmarldelvateypvllatsrkrftkemmgydttpverdevtaattaygimkgvravrvh
nvelnaklakgidflkenenarhnfs
>d1ad5a1 2.30.2.1.10 (82-145) Hemapoetic cell kinase Hck {Human (Homo sapiens)}
ediivvalydyeaihhedlsfqkgdqmvvleesgewwkarslatrkegyipsnyvarvds
let
>d1ad5a2 4.72.1.1.8 (146-248) Hemopoetic cell kinase Hck {Human (Homo sapiens)}
eewffkgisrkdaerqllapgnmlgsfmirdsettkgsyslsvrdydprqgdtvkhykir
tldnggfyisprstfstlqelvdhykkgndglcqklsvpcmss
>d1ad5a3 4.117.1.2.1 (249-531) Haemopoetic cell kinase Hck {Human (Homo sapiens)}
kpqkpwekdaweipreslklekklgagqfgevwmatynkhtkvavktmkpgsmsveafla
eanvmktlqhdklvklhavvtkepiyiitefmakgslldflksdegskqplpklidfsaq
iaegmafieqrnyihrdlraanilvsaslvckiadfglarvgakfpikwtapeainfgsf
tiksdvwsfgillmeivtygripypgmsnpeviralergyrmprpencpeelynimmrcw
knrpeerptfeyiqsvlddfytatesqxqqqp
>d1ad5b1 2.30.2.1.10 (82-145) Hemapoetic cell kinase Hck {Human (Homo sapiens)}
ediivvalydyeaihhedlsfqkgdqmvvleesgewwkarslatrkegyipsnyvarvds
let
>d1ad5b2 4.72.1.1.8 (146-248) Hemopoetic cell kinase Hck {Human (Homo sapiens)}
eewffkgisrkdaerqllapgnmlgsfmirdsettkgsyslsvrdydprqgdtvkhykir
tldnggfyisprstfstlqelvdhykkgndglcqklsvpcmss
>d1ad5b3 4.117.1.2.1 (249-531) Haemopoetic cell kinase Hck {Human (Homo sapiens)}
kpqkpwekdaweipreslklekklgagqfgevwmatynkhtkvavktmkpgsmsveafla
eanvmktlqhdklvklhavvtkepiyiitefmakgslldflksdegskqplpklidfsaq
iaegmafieqrnyihrdlraanilvsaslvckiadfglarvgakfpikwtapeainfgsf
tiksdvwsfgillmeivtygripypgmsnpeviralergyrmprpencpeelynimmrcw
knrpeerptfeyiqsvlddfytatesqxqqqp
>d1ad6__ 1.73.1.3.1 Retinoblastoma tumor suppressor domains {Human (Homo sapiens)}
vmntiqqlmmilnsasdqpsenlisyfnnctvnpkesilkrvkdigyifkekfakavgqg
cveigsqryklgvrlyyrvmesmlkseeerlsiqnfskllndnifhmsllacalevvmat
ysrstsqnldsgtdlsfpwilnvlnlkafdfykviesfikaegnltremikhlercehri
mesla
>e1ad8.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqf
>e1ad8.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
eadcglrplfekksledkterellesyi
>d1ad9a1 2.1.1.1.98 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab CTM01 (human consruct), kappa L chain}
diqmtqspstlsasvgdrvtitcrssksllhsngdtflywfqqkpgkapkllmyrmsnla
sgvpsrfsgsgsgteftltisslqpddfatyycmqhleypftfgqgtkvevkr
>d1ad9a2 2.1.1.2.99 (108-213) Immunoglobulin (constant domains of L and H chains) {Fab CTM01 (human construct), kappa L chain}
tvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqds
kdstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1ad9b1 2.1.1.1.98 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab CTM01 (human consruct), kappa L chain}
eiqlvqsgaevkkpgssvkvsckasgytftdyyinwmrqapgqglewigwidpgsgntky
nekfkgratltvdtstntaymelsslrsedtafyfcarekttyyyamdywgqgtlvtvss
>d1ad9b2 2.1.1.2.99 (114-212) Immunoglobulin (constant domains of L and H chains) {Fab CTM01 (human construct), kappa L chain}
astkgpsvfplapcsrstsestaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtktytcnvdhkpsntkvdkrve
>d1ad9h1 2.1.1.1.98 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab CTM01 (human consruct), kappa L chain}
eiqlvqsgaevkkpgssvkvsckasgytftdyyinwmrqapgqglewigwidpgsgntky
nekfkgratltvdtstntaymelsslrsedtafyfcarekttyyyamdywgqgtlvtvss
>d1ad9h2 2.1.1.2.99 (114-212) Immunoglobulin (constant domains of L and H chains) {Fab CTM01 (human construct), kappa L chain}
astkgpsvfplapcsrstsestaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtktytcnvdhkpsntkvdkrve
>d1ad9l1 2.1.1.1.98 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab CTM01 (human consruct), kappa L chain}
diqmtqspstlsasvgdrvtitcrssksllhsngdtflywfqqkpgkapkllmyrmsnla
sgvpsrfsgsgsgteftltisslqpddfatyycmqhleypftfgqgtkvevkr
>d1ad9l2 2.1.1.2.99 (108-213) Immunoglobulin (constant domains of L and H chains) {Fab CTM01 (human construct), kappa L chain}
tvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqds
kdstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1adba1 2.31.1.2.1 (1-174,325-374) Alcohol dehydrogenase {Horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1adba2 3.2.1.1.1 (175-324) Alcohol dehydrogenase {Horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1adbb1 2.31.1.2.1 (1-174,325-374) Alcohol dehydrogenase {Horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1adbb2 3.2.1.1.1 (175-324) Alcohol dehydrogenase {Horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1adca1 2.31.1.2.1 (1-174,325-374) Alcohol dehydrogenase {Horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1adca2 3.2.1.1.1 (175-324) Alcohol dehydrogenase {Horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1adcb1 2.31.1.2.1 (1-174,325-374) Alcohol dehydrogenase {Horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1adcb2 3.2.1.1.1 (175-324) Alcohol dehydrogenase {Horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1add__ 3.1.8.1.1 Adenosine deaminase (ADA) {Mouse (Mus musculus)}
tpafnkpkvelhvhldgaikpetilyfgkkrgialpadtveelrniigmdkplslpgfla
kfdyympviagcreaikriayefvemkakegvvyvevrysphllanskvdpmpwnqtegd
vtpddvvdlvnqglqegeqafgikvrsilccmrhqpswslevlelckkynqktvvamdla
gdetiegsslfpghveayegavkngihrtvhagevgspevvreavdilktervghgyhti
edealynrllkenmhfevcpwssyltgawdpktthavvrfkndkanyslntddplifkst
ldtdyqmtkkdmgfteeefkrlninaakssflpeeekkellerlyreyq
>d1adea_ 3.30.1.8.2 Adenylosuccinate synthetase (gene purA product) {Escherichia coli}
gnnvvvlgtqwgdegkgkivdllterakyvvryqgghnaghtlvingektvlhlipsgil
renvtsiigngvvlspaalmkemkeledrgipvrerlllseacplildyhvaldnareka
rgakaigttgrgigpayedkvarrglrvgdlfdketfaeklkevmeyhnfqlvnyykaea
vdyqkvlddtmavadiltsmvvdvsdlldqarqrgdfvmfegaqgtlldidhgtypyvts
snttaggvatgsglgpryvdyvlgilkaystrvgagpfptelfdetgeflckqgnefgat
tgrrrrtgwldtvavrravqlnslsgfcltkldvldglkevklcvayrmpdgrevtttpl
aaddwkgvepiyetmpgwsestfgvkdrsglpqaalnyikrieeltgvpidiistgpdrt
etmilrdpfda
>d1adeb_ 3.30.1.8.2 Adenylosuccinate synthetase (gene purA product) {Escherichia coli}
gnnvvvlgtqwgdegkgkivdllterakyvvryqgghnaghtlvingektvlhlipsgil
renvtsiigngvvlspaalmkemkeledrgipvrerlllseacplildyhvaldnareka
rgakaigttgrgigpayedkvarrglrvgdlfdketfaeklkevmeyhnfqlvnyykaea
vdyqkvlddtmavadiltsmvvdvsdlldqarqrgdfvmfegaqgtlldidhgtypyvts
snttaggvatgsglgpryvdyvlgilkaystrvgagpfptelfdetgeflckqgnefgat
tgrrrrtgwldtvavrravqlnslsgfcltkldvldglkevklcvayrmpdgrevtttpl
aaddwkgvepiyetmpgwsestfgvkdrsglpqaalnyikrieeltgvpidiistgpdrt
etmilrdpfda
>d1adf_1 2.31.1.2.1 (1-174,325-374) Alcohol dehydrogenase {Horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1adf_2 3.2.1.1.1 (175-324) Alcohol dehydrogenase {Horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1adg_1 2.31.1.2.1 (1-174,325-374) Alcohol dehydrogenase {Horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1adg_2 3.2.1.1.1 (175-324) Alcohol dehydrogenase {Horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1adia_ 3.30.1.8.2 Adenylosuccinate synthetase (gene purA product) {Escherichia coli}
gnnvvvlgtqwgdegkgkivdllterakyvvryqgghnaghtlvingektvlhlipsgil
renvtsiigngvvlspaalmkemkeledrgipvrerlllseacplildyhvaldnareka
rgakaigttgrgigpayedkvarrglrvgdlfdketfaeklkevmeyhnfqlvnyykaea
vdyqkvlddtmavadiltsmvvdvsdlldqarqrgdfvmfegaqgtlldidhgtypyvts
snttaggvatgsglgpryvdyvlgilkaystrvgagpfptelfdetgeflckqgnefgat
tgrrrrtgwldtvavrravqlnslsgfcltkldvldglkevklcvayrmpdgrevtttpl
aaddwkgvepiyetmpgwsestfgvkdrsglpqaalnyikrieeltgvpidiistgpdrt
etmilrdpfda
>d1adib_ 3.30.1.8.2 Adenylosuccinate synthetase (gene purA product) {Escherichia coli}
gnnvvvlgtqwgdegkgkivdllterakyvvryqgghnaghtlvingektvlhlipsgil
renvtsiigngvvlspaalmkemkeledrgipvrerlllseacplildyhvaldnareka
rgakaigttgrgigpayedkvarrglrvgdlfdketfaeklkevmeyhnfqlvnyykaea
vdyqkvlddtmavadiltsmvvdvsdlldqarqrgdfvmfegaqgtlldidhgtypyvts
snttaggvatgsglgpryvdyvlgilkaystrvgagpfptelfdetgeflckqgnefgat
tgrrrrtgwldtvavrravqlnslsgfcltkldvldglkevklcvayrmpdgrevtttpl
aaddwkgvepiyetmpgwsestfgvkdrsglpqaalnyikrieeltgvpidiistgpdrt
etmilrdpfda
>d1adja1 3.42.1.1.2 (326-421) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Thermus thermophilus}
ekgpdlyliplteeavaeafylaealrprlraeyalaprkpakgleealkrgaafagflg
edelragevtlkrlatgeqvrlsreevpgyllqalg
>d1adja2 4.82.1.1.4 (2-325) Histidyl-tRNA synthetase (HisRS) {Thermus thermophilus}
taravrgtkdlfgkelrmhqrivatarkvleaagalelvtpifeetqvfekgvgaatdiv
rkemftfqdrggrsltlrpegtaamvraylehgmkvwpqpvrlwmagpmfraerpqkgry
rqfhqvnyealgsenpildaeavvllyeclkelglrrlkvklssvgdpedrarynaylre
vlsphrealsedskerleenpmrildskserdqallkelgvrpmldflgeearahlkeve
rhlerlsvpyelepalvrgldyyvrtafevhheeigaqsalggggrydglsellggprvp
gvgfafgvervalaleaegfglpe
>d1adjb1 3.42.1.1.2 (326-421) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Thermus thermophilus}
ekgpdlyliplteeavaeafylaealrprlraeyalaprkpakgleealkrgaafagflg
edelragevtlkrlatgeqvrlsreevpgyllqalg
>d1adjb2 4.82.1.1.4 (2-325) Histidyl-tRNA synthetase (HisRS) {Thermus thermophilus}
taravrgtkdlfgkelrmhqrivatarkvleaagalelvtpifeetqvfekgvgaatdiv
rkemftfqdrggrsltlrpegtaamvraylehgmkvwpqpvrlwmagpmfraerpqkgry
rqfhqvnyealgsenpildaeavvllyeclkelglrrlkvklssvgdpedrarynaylre
vlsphrealsedskerleenpmrildskserdqallkelgvrpmldflgeearahlkeve
rhlerlsvpyelepalvrgldyyvrtafevhheeigaqsalggggrydglsellggprvp
gvgfafgvervalaleaegfglpe
>d1adjc1 3.42.1.1.2 (326-421) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Thermus thermophilus}
ekgpdlyliplteeavaeafylaealrprlraeyalaprkpakgleealkrgaafagflg
edelragevtlkrlatgeqvrlsreevpgyllqalg
>d1adjc2 4.82.1.1.4 (2-325) Histidyl-tRNA synthetase (HisRS) {Thermus thermophilus}
taravrgtkdlfgkelrmhqrivatarkvleaagalelvtpifeetqvfekgvgaatdiv
rkemftfqdrggrsltlrpegtaamvraylehgmkvwpqpvrlwmagpmfraerpqkgry
rqfhqvnyealgsenpildaeavvllyeclkelglrrlkvklssvgdpedrarynaylre
vlsphrealsedskerleenpmrildskserdqallkelgvrpmldflgeearahlkeve
rhlerlsvpyelepalvrgldyyvrtafevhheeigaqsalggggrydglsellggprvp
gvgfafgvervalaleaegfglpe
>d1adjd1 3.42.1.1.2 (326-421) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Thermus thermophilus}
ekgpdlyliplteeavaeafylaealrprlraeyalaprkpakgleealkrgaafagflg
edelragevtlkrlatgeqvrlsreevpgyllqalg
>d1adjd2 4.82.1.1.4 (2-325) Histidyl-tRNA synthetase (HisRS) {Thermus thermophilus}
taravrgtkdlfgkelrmhqrivatarkvleaagalelvtpifeetqvfekgvgaatdiv
rkemftfqdrggrsltlrpegtaamvraylehgmkvwpqpvrlwmagpmfraerpqkgry
rqfhqvnyealgsenpildaeavvllyeclkelglrrlkvklssvgdpedrarynaylre
vlsphrealsedskerleenpmrildskserdqallkelgvrpmldflgeearahlkeve
rhlerlsvpyelepalvrgldyyvrtafevhheeigaqsalggggrydglsellggprvp
gvgfafgvervalaleaegfglpe
>d1adl__ 2.53.1.2.6 Adipocyte lipid-binding protein, ALBP {Mouse (Mus musculus)}
cdafvgtwklvssenfddymkevgvgfatrkvagmakpnmiisvngdlvtirsestfknt
eisfklgvefdeitaddrkvksiitldggalvqvqkwdgksttikrkrdgdklvvecvmk
gvtstrvyera
>d1adn__ 7.40.1.1.1 Ada DNA repair protein, N-terminal domain (N-Ada 10) {Escherichia coli}
mkkatcltddqrwqsvlardpnadgefvfavrttgifcrpscrarhalrenvsfyanase
alaagfrpckrcqpdkanprqhrldkithacr
>d1adoa_ 3.1.9.1.5 Fructose-1,6-bisphosphate aldolase {Rabbit (Oryctolagus cuniculus)}
phshpaltpeqkkelsdiahrivapgkgilaadestgsiakrlqsigtenteenrrfyrq
llltaddrvnpciggvilfhetlyqkaddgrpfpqvikskggvvgikvdkgvvplagtng
etttqgldglsercaqykkdgadfakwrcvlkigehtpsalaimenanvlaryasicqqn
givpivepeilpdgdhdlkrcqyvtekvlaavykalsdhhiylegtllkpnmvtpghact
qkysheeiamatvtalrrtvppavtgvtflsggqseeeasinlnainkcpllkpwaltfs
ygralqasalkawggkkenlkaaqeeyvkralanslacqgkytssgqagaaaseslfisn
hay
>d1adob_ 3.1.9.1.5 Fructose-1,6-bisphosphate aldolase {Rabbit (Oryctolagus cuniculus)}
phshpaltpeqkkelsdiahrivapgkgilaadestgsiakrlqsigtenteenrrfyrq
llltaddrvnpciggvilfhetlyqkaddgrpfpqvikskggvvgikvdkgvvplagtng
etttqgldglsercaqykkdgadfakwrcvlkigehtpsalaimenanvlaryasicqqn
givpivepeilpdgdhdlkrcqyvtekvlaavykalsdhhiylegtllkpnmvtpghact
qkysheeiamatvtalrrtvppavtgvtflsggqseeeasinlnainkcpllkpwaltfs
ygralqasalkawggkkenlkaaqeeyvkralanslacqgkytssgqagaaaseslfisn
hay
>d1adoc_ 3.1.9.1.5 Fructose-1,6-bisphosphate aldolase {Rabbit (Oryctolagus cuniculus)}
phshpaltpeqkkelsdiahrivapgkgilaadestgsiakrlqsigtenteenrrfyrq
llltaddrvnpciggvilfhetlyqkaddgrpfpqvikskggvvgikvdkgvvplagtng
etttqgldglsercaqykkdgadfakwrcvlkigehtpsalaimenanvlaryasicqqn
givpivepeilpdgdhdlkrcqyvtekvlaavykalsdhhiylegtllkpnmvtpghact
qkysheeiamatvtalrrtvppavtgvtflsggqseeeasinlnainkcpllkpwaltfs
ygralqasalkawggkkenlkaaqeeyvkralanslacqgkytssgqagaaaseslfisn
hay
>d1adod_ 3.1.9.1.5 Fructose-1,6-bisphosphate aldolase {Rabbit (Oryctolagus cuniculus)}
phshpaltpeqkkelsdiahrivapgkgilaadestgsiakrlqsigtenteenrrfyrq
llltaddrvnpciggvilfhetlyqkaddgrpfpqvikskggvvgikvdkgvvplagtng
etttqgldglsercaqykkdgadfakwrcvlkigehtpsalaimenanvlaryasicqqn
givpivepeilpdgdhdlkrcqyvtekvlaavykalsdhhiylegtllkpnmvtpghact
qkysheeiamatvtalrrtvppavtgvtflsggqseeeasinlnainkcpllkpwaltfs
ygralqasalkawggkkenlkaaqeeyvkralanslacqgkytssgqagaaaseslfisn
hay
>d1adqa1 2.1.1.2.139 (238-341) Immunoglobulin (constant domains of L and H chains) {Fc (human) IgG1 class}
psvflfppkpkdtlmisrtpevtcvvvdvsqedpqvqfnwyvdgvqvhnaktkpreqqfn
styrvvsvltvlhqnwldgkeykckvsnkglpssiektiskakg
>d1adqa2 2.1.1.2.139 (342-443) Immunoglobulin (constant domains of L and H chains) {Fc (human) IgG1 class}
qprepqvytlppsqeemtknqvsltclvkgfypsdiavewesngqpennykttppvldsd
gsfflysrltvdksrwqegnvfscsvmhealhnhytqkslsl
>d1adqh1 2.1.1.1.111 (1-113) Immunoglobulin (variable domains of L and H chains) {IgM rheumatoid factor Fab (human), lambda L chain}
evqlvesggglvqpgrslrlscvtsgftfddyamhwvrqspgkglewvsgiswntgtiiy
adsvkgrfiisrdnaknslylqmnslrvedtalyycaktrsyvvaaeyyfhywgqgilvt
vss
>d1adqh2 2.1.1.2.110 (114-223b) Immunoglobulin (constant domains of L and H chains) {IgM rheumatoid factor Fab (human), lambda L chain}
gsasaptlfplvscensnpsstvavgclaqdflpdsitfswkyknnsdisstrgfpsvlr
ggkyaatsqvllpskdvmqgtnehvvckvqhpngnkekdvpl
>d1adql1 2.1.1.1.111 (2-107) Immunoglobulin (variable domains of L and H chains) {IgM rheumatoid factor Fab (human), lambda L chain}
yvltqppsvsvapgqtaritcggnnigsksvhwyqqkpgqapvlvvyddsdrppgiperf
sgsnsgntatltisrveagdeadyycqvwdsssdhavfgggtkltvlg
>d1adql2 2.1.1.2.110 (108-215) Immunoglobulin (constant domains of L and H chains) {IgM rheumatoid factor Fab (human), lambda L chain}
qpkaapsvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvetttpskq
snnkyaassylsltpeqwkshksyscqvthegstvektvaptecs
>d1adr__ 1.36.1.2.4 p22 C2 repressor, DNA-binding domain {Bacteriophage p22 (Salmonella)}
mntqlmgerirarrkklkirqaalgkmvgvsnvaisqwersetepngenllalskalqcs
pdyllkgdlsqtnvay
>d1ads__ 3.1.6.1.3 Aldose reductase (aldehyde reductase) {Human (Homo sapiens)}
asrlllnngakmpilglgtwksppgqvteavkvaidvgyrhidcahvyqnenevgvaiqe
klreqvvkreelfivsklwctyhekglvkgacqktlsdlkldyldlylihwptgfkpgke
ffpldesgnvvpsdtnildtwaameelvdeglvkaigisnfnhlqvemilnkpglkykpa
vnqiechpyltqekliqycqskgivvtaysplgspdrpwakpedpslledprikaiaakh
nkttaqvlirfpmqrnlvvipksvtperiaenfkvfdfelssqdmttllsynrnwrvcal
lsctshkdypfheef
>d1adt_1 1.56.1.1.1 (176-265) Domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
pivsawekgmeaaralmdkyhvdndlkanfkllpdqvealaavcktwlneehrglqltft
snktfvtmmgrflqaylqsfaevtykhhep
>d1adt_2 7.43.1.1.1 (266-385) First Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
tgcalwlhrcaeiegelkclhgsiminkehviemdvtsengqralkeqsskakivknrwg
rnvvqisntdarccvhdaacpanqfsgkscgmffsegakaqvafkqikafmqalypnaqt
>d1adt_3 7.43.1.1.2 (386-529) Second Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
ghghllmplrcecnskpghapflgrqlpkltpfalsnaedldadlisdksvlasvhhpal
ivfqccnpvyrnsraqgggpncdfkisapdllnalvmvrslwsenftelprmvvpqfkws
tkhqyrnvslpvahsdarqnpfdf
>d1adua1 1.56.1.1.1 (180-265) Domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
awekgmeaaralmdkyhvdndlkanfkllpdqvealaavcktwlneehrglqltftsnkt
fvtmmgrflqaylqsfaevtykhhep
>d1adua2 7.43.1.1.1 (266-385) First Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
tgcalwlhrcaeiegelkclhgsiminkehviemdvtsengqralkeqsskakivknrwg
rnvvqisntdarccvhdaacpanqfsgkscgmffsegakaqvafkqikafmqalypnaqt
>d1adua3 7.43.1.1.2 (386-529) Second Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
ghghllmplrcecnskpghapflgrqlpkltpfalsnaedldadlisdksvlasvhhpal
ivfqccnpvyrnsraqgggpncdfkisapdllnalvmvrslwsenftelprmvvpefkws
tkhqyrnvslpvahsdarqnpfdf
>d1adub1 1.56.1.1.1 (180-265) Domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
awekgmeaaralmdkyhvdndlkanfkllpdqvealaavcktwlneehrglqltftsnkt
fvtmmgrflqaylqsfaevtykhhep
>d1adub2 7.43.1.1.1 (266-385) First Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
tgcalwlhrcaeiegelkclhgsiminkehviemdvtsengqralkeqsskakivknrwg
rnvvqisntdarccvhdaacpanqfsgkscgmffsegakaqvafkqikafmqalypnaqt
>d1adub3 7.43.1.1.2 (386-529) Second Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
ghghllmplrcecnskpghapflgrqlpkltpfalsnaedldadlisdksvlasvhhpal
ivfqccnpvyrnsraqgggpncdfkisapdllnalvmvrslwsenftelprmvvpefkws
tkhqyrnvslpvahsdarqnpfdf
>d1adva1 1.56.1.1.1 (180-265) Domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
awekgmeaaralmdkyhvdndlkanfkllpdqvealaavcktwlneehrglqltftsnkt
fvtmmgrflqaylqsfaevtykhhep
>d1adva2 7.43.1.1.1 (266-385) First Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
tgcalwlhrcaeiegelkclhgsiminkehviemdvtsengqralkeqsskakivknrwg
rnvvqisntdarccvhdaacpanqfsgkscgmffsegakaqvafkqikafmqalypnaqt
>d1adva3 7.43.1.1.2 (386-529) Second Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
ghghllmplrcecnskpghapflgrqlpkltpfalsnaedldadlisdksvlasvhhpal
ivfqccnpvyrnsraqgggpncdfkisapdllnalvmvrslwsenftelprmvvpefkws
tkhqyrnvslpvahsdarqnpfdf
>d1advb1 1.56.1.1.1 (180-265) Domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
awekgmeaaralmdkyhvdndlkanfkllpdqvealaavcktwlneehrglqltftsnkt
fvtmmgrflqaylqsfaevtykhhep
>d1advb2 7.43.1.1.1 (266-385) First Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
tgcalwlhrcaeiegelkclhgsiminkehviemdvtsengqralkeqsskakivknrwg
rnvvqisntdarccvhdaacpanqfsgkscgmffsegakaqvafkqikafmqalypnaqt
>d1advb3 7.43.1.1.2 (386-529) Second Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
ghghllmplrcecnskpghapflgrqlpkltpfalsnaedldadlisdksvlasvhhpal
ivfqccnpvyrnsraqgggpncdfkisapdllnalvmvrslwsenftelprmvvpefkws
tkhqyrnvslpvahsdarqnpfdf
>d1adwa_ 2.5.1.1.19 Pseudoazurin {Thiosphaera pantotropha}
athevhmlnkgesgamvfepafvraepgdvinfvptdkshnveaikeilpegvesfkski
nesytltvtepglygvkctphfgmgmvglvqvgdapenldaaktakmpkkarermdaela
qvn
>d1adwb_ 2.5.1.1.19 Pseudoazurin {Thiosphaera pantotropha}
athevhmlnkgesgamvfepafvraepgdvinfvptdkshnveaikeilpegvesfkski
nesytltvtepglygvkctphfgmgmvglvqvgdapenldaaktakmpkkarermdaela
qvn
>d1adx__ 7.3.11.1.17 Thrombomodulin, different EGF-like domains {Human (Homo sapiens)}
qmfcnqtacpadcdpntqascecpegyilddgfictdide
>d1adya1 3.42.1.1.2 (326-421) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Thermus thermophilus}
ekgpdlyliplteeavaeafylaealrprlraeyalaprkpakgleealkrgaafagflg
edelragevtlkrlatgeqvrlsreevpgyllqalg
>d1adya2 4.82.1.1.4 (2-325) Histidyl-tRNA synthetase (HisRS) {Thermus thermophilus}
taravrgtkdlfgkelrmhqrivatarkvleaagalelvtpifeetqvfekgvgaatdiv
rkemftfqdrggrsltlrpegtaamvraylehgmkvwpqpvrlwmagpmfraerpqkgry
rqfhqvnyealgsenpildaeavvllyeclkelglrrlkvklssvgdpedrarynaylre
vlsphrealsedskerleenpmrildskserdqallkelgvrpmldflgeearahlkeve
rhlerlsvpyelepalvrgldyyvrtafevhheeigaqsalggggrydglsellggprvp
gvgfafgvervalaleaegfglpe
>d1adyb1 3.42.1.1.2 (326-421) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Thermus thermophilus}
ekgpdlyliplteeavaeafylaealrprlraeyalaprkpakgleealkrgaafagflg
edelragevtlkrlatgeqvrlsreevpgyllqalg
>d1adyb2 4.82.1.1.4 (2-325) Histidyl-tRNA synthetase (HisRS) {Thermus thermophilus}
taravrgtkdlfgkelrmhqrivatarkvleaagalelvtpifeetqvfekgvgaatdiv
rkemftfqdrggrsltlrpegtaamvraylehgmkvwpqpvrlwmagpmfraerpqkgry
rqfhqvnyealgsenpildaeavvllyeclkelglrrlkvklssvgdpedrarynaylre
vlsphrealsedskerleenpmrildskserdqallkelgvrpmldflgeearahlkeve
rhlerlsvpyelepalvrgldyyvrtafevhheeigaqsalggggrydglsellggprvp
gvgfafgvervalaleaegfglpe
>d1adyc1 3.42.1.1.2 (326-421) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Thermus thermophilus}
ekgpdlyliplteeavaeafylaealrprlraeyalaprkpakgleealkrgaafagflg
edelragevtlkrlatgeqvrlsreevpgyllqalg
>d1adyc2 4.82.1.1.4 (2-325) Histidyl-tRNA synthetase (HisRS) {Thermus thermophilus}
taravrgtkdlfgkelrmhqrivatarkvleaagalelvtpifeetqvfekgvgaatdiv
rkemftfqdrggrsltlrpegtaamvraylehgmkvwpqpvrlwmagpmfraerpqkgry
rqfhqvnyealgsenpildaeavvllyeclkelglrrlkvklssvgdpedrarynaylre
vlsphrealsedskerleenpmrildskserdqallkelgvrpmldflgeearahlkeve
rhlerlsvpyelepalvrgldyyvrtafevhheeigaqsalggggrydglsellggprvp
gvgfafgvervalaleaegfglpe
>d1adyd1 3.42.1.1.2 (326-421) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Thermus thermophilus}
ekgpdlyliplteeavaeafylaealrprlraeyalaprkpakgleealkrgaafagflg
edelragevtlkrlatgeqvrlsreevpgyllqalg
>d1adyd2 4.82.1.1.4 (2-325) Histidyl-tRNA synthetase (HisRS) {Thermus thermophilus}
taravrgtkdlfgkelrmhqrivatarkvleaagalelvtpifeetqvfekgvgaatdiv
rkemftfqdrggrsltlrpegtaamvraylehgmkvwpqpvrlwmagpmfraerpqkgry
rqfhqvnyealgsenpildaeavvllyeclkelglrrlkvklssvgdpedrarynaylre
vlsphrealsedskerleenpmrildskserdqallkelgvrpmldflgeearahlkeve
rhlerlsvpyelepalvrgldyyvrtafevhheeigaqsalggggrydglsellggprvp
gvgfafgvervalaleaegfglpe
>d1adz__ 7.8.1.1.3 Tissue factor pathway inhibitor {Human (Homo sapiens)}
dykddddklkpdfcfleedpgicrgyitryfynnqtkqcerfkyggclgnmnnfetleec
knicedgpngf
>d1ae1a_ 3.2.1.2.16 Tropinone reductase {Jimsonweed (Datura stramonium), I}
rwslkgttalvtggskgigyaiveelaglgarvytcsrnekeldecleiwrekglnvegs
vcdllsrterdklmqtvahvfdgklnilvnnagvvihkeakdftekdyniimgtnfeaay
hlsqiaypllkasqngnviflssiagfsalpsvslysaskgainqmtkslacewakdnir
vnsvapgviltplvetaikknphqkeeidnfivktpmgragkpqevsaliaflcfpaasy
itgqiiwadggftanggf
>d1ae1b_ 3.2.1.2.16 Tropinone reductase {Jimsonweed (Datura stramonium), I}
rwslkgttalvtggskgigyaiveelaglgarvytcsrnekeldecleiwrekglnvegs
vcdllsrterdklmqtvahvfdgklnilvnnagvvihkeakdftekdyniimgtnfeaay
hlsqiaypllkasqngnviflssiagfsalpsvslysaskgainqmtkslacewakdnir
vnsvapgviltplvetaikknphqkeeidnfivktpmgragkpqevsaliaflcfpaasy
itgqiiwadggftanggf
>d1ae2__ 2.35.4.8.1 Gene V protein {Bacteriophage f1}
mikveikpsqaqfttrsgvsrqgkpyslneqrcyvdlgneypvlvkitldegqpayapgl
ytvhlssfkvgqfgslmidrlrlvpa
>d1ae3__ 2.35.4.8.1 Gene V protein {Bacteriophage f1}
mikveikpsqaqfttrsgvsrqgkpyslneqlcyvdlgneypvlvkitldegqpayapgl
ytvhlssfkvgqfgslmidrlclvpa
>d1ae4__ 3.1.6.1.5 Aldose reductase (aldehyde reductase) {Porcine (Sus scrofa)}
aascvllhtgqkmpliglgtwksepgqvkaaikyaltvgyrhidcaaiygneleigealt
etvgpgkavpreelfvtsklwntkhhpedvepalrktladlqleyldlylmhwpyaferg
dnpfpknadgtirydathykdtwkalealvakglvralglsnfssrqiddvlsvasvrpa
vlqvechpylaqneliahcqarglevtaysplgssdrawrdpnepvlleepvvqalaeky
nrspaqillrwqvqrkvicipksvtpsripqniqvfdftfspeemkqldalnknlrfivp
mltvdgkrvprdaghplypfndpy
>d1ae5__ 2.41.1.2.18 Heparin binding protein, HBP {Human (Homo sapiens)}
ivggrkarprqfpflasiqnqgrhfcggaliharfvmtaascfqsqnpgvstvvlgaydl
rrrerqsrqtfsissmsengydpqqnlndlmllqldreanltssvtilplplqnatveag
trcqvagwgsqrsggrlsrfprfvnvtvtpedqcrpnnvctgvltrrggicngdggtplv
ceglahgvasfslgpcgrgpdfftrvalfrdwidgvlnnpgpgpa
>d1ae6h1 2.1.1.1.97 (1-114) Immunoglobulin (variable domains of L and H chains) {Fab CTM01 (mouse), kappa L chain}
qiqlqqsgpelvkpgasvkisckasgytftdyyinwmkqkpgqglewigwidpgsgntky
nekfkgkatltvdtssstaymqlssltsedtavyfcarekttyyyamdywgqgtsvtvsa
a
>d1ae6h2 2.1.1.2.98 (115-211) Immunoglobulin (constant domains of L and H chains) {Fab CTM01 (mouse), kappa L chain}
kttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsdl
ytlsssvtvpssprpsetvtcnvahpasstkvdkkiv
>d1ae6l1 2.1.1.1.97 (1-106a) Immunoglobulin (variable domains of L and H chains) {Fab CTM01 (mouse), kappa L chain}
divmtqaapsvpvtpgeslsiscrssksllhsngdtflywflqrpgqspqlliyrmsnla
sgvpdrfsgsgsgtaftlrvsrveaedvgvyycmqhleypftfgagtklelk
>d1ae6l2 2.1.1.2.98 (107-213) Immunoglobulin (constant domains of L and H chains) {Fab CTM01 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1ae7__ 1.123.1.2.7 Snake phospholipase A2 {Mainland tiger snake (Notechis scutatus scutatus), notexin}
nlvqfsyliqcanhgkrptwhymdygcycgaggsgtpvdeldrcckihddcydeagkkgc
fpkmsaydyycgengpycrnikkkclrfvcdcdveaafcfakapynnanwnidtkkrcq
>e1ae8.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>e1ae8.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>d1ae9a_ 4.133.1.1.2 Integrase (Int) {Bacteriophage lambda}
rsrltadeylkiyqaaesspcwlrlamelavvtgqrvgdlcemkwsdivdgylyveqskt
gvkiaiptalhidalgismketldkckeilggetiiastrreplssgtvsryfmrarkas
glsfegdpptfhelrslsarlyekqisdkfaqhllghksdtmasqfrddrgrewdkiei
>d1ae9b_ 4.133.1.1.2 Integrase (Int) {Bacteriophage lambda}
rsrltadeylkiyqaaesspcwlrlamelavvtgqrvgdlcemkwsdivdgylyveqskt
gvkiaiptalhidalgismketldkckeilggetiiastrreplssgtvsryfmrarkas
glsfegdpptfhelrslsarlyekqisdkfaqhllghksdtmasqfrddrgrewdkiei
>d1aeb__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aec__ 4.3.1.1.1 Actinidin {Chinese gooseberry or kiwifruit (Actinidia chinensis)}
lpsyvdwrsagavvdiksqgecggcwafsaiatveginkivtgvlislseqelidcgrtq
ntrgcnggyitdgfqfiinngginteenypytaqdgecnvdlqnekyvtidtyenvpynn
ewalqtavtyqpvsvaldaagdafkqyssgiftgpcgtaidhavtivgygteggidywiv
knswdttwgeegymrilrnvggagtcgiatmpsypvky
>d1aed__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aee__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aef__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aeg__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aeh__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aeia_ 1.66.1.1.8 Annexin XII {Hydra (Hydra attenuata)}
vvqgtvkphasfnsredaetlrkamkgigtdeksithilatrsnaqrqqiktdyttlfgk
hledelkselsgnyeaaalallrkpdeflaeqlhaamkglgtdenalidilctqsnaqih
aikaafkllykedlekeiisetsgnfqrllvsmlqggrkedepvnaahaaedaaaiyqag
egqigtdesrfnavlatrsypqlhqifheyskisnktilqaienefsgdikngllaivks
venrfayfaerlhhamkglgtsdktlirilvsrseidlaniketfqamygkslyefiadd
csgdykdlllqitgh
>d1aeib_ 1.66.1.1.8 Annexin XII {Hydra (Hydra attenuata)}
vvqgtvkphasfnsredaetlrkamkgigtdeksithilatrsnaqrqqiktdyttlfgk
hledelkselsgnyeaaalallrkpdeflaeqlhaamkglgtdenalidilctqsnaqih
aikaafkllykedlekeiisetsgnfqrllvsmlqggrkedepvnaahaaedaaaiyqag
egqigtdesrfnavlatrsypqlhqifheyskisnktilqaienefsgdikngllaivks
venrfayfaerlhhamkglgtsdktlirilvsrseidlaniketfqamygkslyefiadd
csgdykdlllqitgh
>d1aeic_ 1.66.1.1.8 Annexin XII {Hydra (Hydra attenuata)}
vvqgtvkphasfnsredaetlrkamkgigtdeksithilatrsnaqrqqiktdyttlfgk
hledelkselsgnyeaaalallrkpdeflaeqlhaamkglgtdenalidilctqsnaqih
aikaafkllykedlekeiisetsgnfqrllvsmlqggrkedepvnaahaaedaaaiyqag
egqigtdesrfnavlatrsypqlhqifheyskisnktilqaienefsgdikngllaivks
venrfayfaerlhhamkglgtsdktlirilvsrseidlaniketfqamygkslyefiadd
csgdykdlllqitgh
>d1aeid_ 1.66.1.1.8 Annexin XII {Hydra (Hydra attenuata)}
vvqgtvkphasfnsredaetlrkamkgigtdeksithilatrsnaqrqqiktdyttlfgk
hledelkselsgnyeaaalallrkpdeflaeqlhaamkglgtdenalidilctqsnaqih
aikaafkllykedlekeiisetsgnfqrllvsmlqggrkedepvnaahaaedaaaiyqag
egqigtdesrfnavlatrsypqlhqifheyskisnktilqaienefsgdikngllaivks
venrfayfaerlhhamkglgtsdktlirilvsrseidlaniketfqamygkslyefiadd
csgdykdlllqitgh
>d1aeie_ 1.66.1.1.8 Annexin XII {Hydra (Hydra attenuata)}
vvqgtvkphasfnsredaetlrkamkgigtdeksithilatrsnaqrqqiktdyttlfgk
hledelkselsgnyeaaalallrkpdeflaeqlhaamkglgtdenalidilctqsnaqih
aikaafkllykedlekeiisetsgnfqrllvsmlqggrkedepvnaahaaedaaaiyqag
egqigtdesrfnavlatrsypqlhqifheyskisnktilqaienefsgdikngllaivks
venrfayfaerlhhamkglgtsdktlirilvsrseidlaniketfqamygkslyefiadd
csgdykdlllqitgh
>d1aeif_ 1.66.1.1.8 Annexin XII {Hydra (Hydra attenuata)}
vvqgtvkphasfnsredaetlrkamkgigtdeksithilatrsnaqrqqiktdyttlfgk
hledelkselsgnyeaaalallrkpdeflaeqlhaamkglgtdenalidilctqsnaqih
aikaafkllykedlekeiisetsgnfqrllvsmlqggrkedepvnaahaaedaaaiyqag
egqigtdesrfnavlatrsypqlhqifheyskisnktilqaienefsgdikngllaivks
venrfayfaerlhhamkglgtsdktlirilvsrseidlaniketfqamygkslyefiadd
csgdykdlllqitgh
>d1aej__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aek__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1ael__ 2.53.1.2.3 Intestinal fatty acid binding protein {Rat (Rattus rattus)}
afdgtwkvdrnenyekfmekmginvvkrklgahdnlkltitqegnkftvkessnfrnidv
vfelgvdfaysladgteltgtwtmegnklvgkfkrvdngkeliavreisgneliqtytye
gveakrifkke
>d1aem__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aen__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aeo__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aep__ 1.64.1.1.1 Apolipophorin-III {African locust (Locusta migratoria)}
niaeavqqlnhtivnaahelhetlglptpdealnllteqanafktkiaevttslkqeaek
hqgsvaeqlnafarnlnnsihdaatslnlqdqlnslqsaltnvghqwqdiatktqasaqe
awapvqsalqeaaektkeaaanlqnsiqsavqk
>d1aeq__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aera_ 4.136.1.1.4 Exotoxin A, C-terminal domain {Pseudomonas aeruginosa}
aflgdggdvsfstrgtqnwtverllqahrqleergyvfvgyhgtfleaaqsivfggvraa
iwrgfyiagdpalaygyaqdqepdargrirngallrvyvprsslpgfyrtsltlaapeaa
geverlighplplrldaitgpeeeggrletilgwplaertvvipsaiptdprnvggdldp
ssipdkeqaisalpdyasqpgkppr
>d1aerb_ 4.136.1.1.4 Exotoxin A, C-terminal domain {Pseudomonas aeruginosa}
flgdggdvsfstrgtqnwtverllqahrqleergyvfvgyhgtfleaaqsivfggvrars
qdldaiwrgfyiagdpalaygyaqdqepdrgrirngallrvyvprsslpgfyrtsltlaa
peaageverlighplplrldaitgprletilgwplaertvvipsaiptdprnvggdldps
sipdkeqaisalpdy
>d1aes__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aet__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aeu__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aev__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aew__ 1.26.1.1.5 (Apo)ferritin {Horse (Equus caballus), L chain}
sqirqnysteveaavnrlvnlylrasytylslgfyfdrddvalegvchffrelaeekreg
aerllkmqnqrggralfqdlqkpsqdewgttpdamkaaivlekslnqalldlhalgsaqa
dphlcdfleshfldeevklikkmgdhltniqrlvgsqaglgeylferltl
>d1aex__ 2.35.1.1.1 Staphylococcal nuclease {Staphylococcus aureus}
lhkepatlikaidgdtxklmykgqpmtfrlllvdtpetkhpkkgvekygpeasaftkkmv
enakkievefdkgqrtdkygrglayiyadgkmvnealvrqglakvayvykpnntheqhlr
kseaqakkeklniws
>d1aey__ 2.30.2.1.8 alpha-Spectrin, SH3 domain {Chicken (Gallus gallus)}
gkelvlalydyqeksprevtmkkgdiltllnstnkdwwkvevndrqgfvpaayvkkld
>d1af0a1 2.70.1.1.2 (247-471) Metalloprotease, C-terminal domain {Serratia marcescens}
ganlstrtgdtvygfnsntgrdflsttsnsqkvifaawdaggndtfdfsgytanqrinln
eksfsdvgglkgnvsiaagvtienaiggsgndvivgnaannvlkggagndvlfggggade
lwggagkdifvfsaasdsapgasdwirdfqkgidkidlsffdkeansssfihfvdhfsgt
ageallsynassnvtdlsvnigghqapdflvkivgqvdvatdfiv
>d1af0a2 4.71.1.4.2 (2-246) Metallo protease, catalytic (N-terminal) domain {Serratia marcescens}
attgydavddllhyhergngiqingkdsfsneqaglfitrenqtwngykvfgqpvkltfs
fpdykfsstnvagdtglskfsaeqqqqaklslqswadvanitftevaagqkanitfgnys
qdrpghydygtqayaflpntiwqgqdlggqtwynvnqsnvkhpatedygrqtftheigha
lglshpgdynagegdptyndvtyaedtrqfslmsywsetntggdngghyaaapllddiaa
iqhly
>d1af2a1 3.87.1.1.1 (1-150) Cytidine deaminase {Escherichia coli}
mhprfqtafaqladnlqsalepiladkyfpalltgeqvsslksatgldedalafallpla
aacartplsnfnvgaiargvsgtwyfganmefigatmqqtvhaeqsaishawlsgekala
aitvnytpcghcrqfmnelnsgldlrihlp
>d1af2a2 3.87.1.1.1 (151-294) Cytidine deaminase {Escherichia coli}
greahalrdylpdafgpkdleiktllmdeqdhgyaltgdalsqaaiaaanrshmpysksp
sgvaleckdgrifsgsyaenaafnptlpplqgalillnlkgydypdiqravlaekadapl
iqwdatsatlkalgchsidrvlla
>d1af3__ 6.1.4.1.2 Apoptosis regulator Bcl-xL {Rat (Rattus norvegicus)}
sqsnrelvvdflsyklsqkgyswsqfsdveenrteapeeteperetpsaingnpswhlad
spavngatghsssldarevipmaavkqalreagdefelryrrafsdltsqlhitpgtayq
sfeqvvnelfrdgvnwgrivaffsfggalcvesvdkemqvlvsriaswmatylndhlepw
iqenggwdtfvdlyg
>d1af4__ 3.33.1.1.2 Subtilisin Carlsberg {Bacillus licheniformis}
aqtvpygiplikadkvqaqgfkganvkvavldtgiqashpdlnvvggasfvageayntdg
nghgthvagtvaaldnttgvlgvapsvslyavkvlnssgsgsysgivsgiewattngmdv
inmslggasgstamkqavdnayargvvvvaaagnsgnsgstntigypakydsviavgavd
snsnrasfssvgaelevmapgagvystyptntyatlngtsmasphvagaaalilskhpnl
sasqvrnrlsstatylgssfyygkglinveaaaq
>d1af5__ 4.74.2.1.1 DNA endonuclease I-CreI {Chlamydomonas reinhardtii}
kynkefllylagfvdgdgsiiaqikpnqsykfkhqlsltfqvtqktqrrwflgklvdeig
vgyvrdrgsvsdyilseikplhnfltqlqpflklkqkqanlvlkiieqlplevctwvdqi
aalnds
>d1af6a_ 6.4.3.2.1 Maltoporin (also LamB protein) {Escherichia coli}
vdfhgyarsgigwtgsggeqqcfqttgaqskyrlgnecetyaelklgqevwkegdksfyf
dtnvaysvaqqndweatdpafreanvqgknliewlpgstiwagkrfyqrhdvhmidfyyw
disgpgaglenidvgfgklslaatrsseaggsssfasnniydytnetandvfdvrlaqme
inpggtlelgvdygranlrdnyrlvdgaskdgwlftaehtqsvlkgfnkfvvqyatdsmt
sqgkglsqgsgvafdnekfayninnnghmlrildhgaismgdnwdmmyvgmyqdinwdnd
ngtkwwtvgirpmykwtpimstvmeigydnvesqrtgdknnqykitlaqqwqagdsiwsr
pairvfatyakwdekwgydytgnadnnanfgkavpadfnggsfgrgdsdewtfgaqmeiw
w
>d1af6b_ 6.4.3.2.1 Maltoporin (also LamB protein) {Escherichia coli}
vdfhgyarsgigwtgsggeqqcfqttgaqskyrlgnecetyaelklgqevwkegdksfyf
dtnvaysvaqqndweatdpafreanvqgknliewlpgstiwagkrfyqrhdvhmidfyyw
disgpgaglenidvgfgklslaatrsseaggsssfasnniydytnetandvfdvrlaqme
inpggtlelgvdygranlrdnyrlvdgaskdgwlftaehtqsvlkgfnkfvvqyatdsmt
sqgkglsqgsgvafdnekfayninnnghmlrildhgaismgdnwdmmyvgmyqdinwdnd
ngtkwwtvgirpmykwtpimstvmeigydnvesqrtgdknnqykitlaqqwqagdsiwsr
pairvfatyakwdekwgydytgnadnnanfgkavpadfnggsfgrgdsdewtfgaqmeiw
w
>d1af6c_ 6.4.3.2.1 Maltoporin (also LamB protein) {Escherichia coli}
vdfhgyarsgigwtgsggeqqcfqttgaqskyrlgnecetyaelklgqevwkegdksfyf
dtnvaysvaqqndweatdpafreanvqgknliewlpgstiwagkrfyqrhdvhmidfyyw
disgpgaglenidvgfgklslaatrsseaggsssfasnniydytnetandvfdvrlaqme
inpggtlelgvdygranlrdnyrlvdgaskdgwlftaehtqsvlkgfnkfvvqyatdsmt
sqgkglsqgsgvafdnekfayninnnghmlrildhgaismgdnwdmmyvgmyqdinwdnd
ngtkwwtvgirpmykwtpimstvmeigydnvesqrtgdknnqykitlaqqwqagdsiwsr
pairvfatyakwdekwgydytgnadnnanfgkavpadfnggsfgrgdsdewtfgaqmeiw
w
>d1af7_1 1.60.1.1.1 (11-91) Chemotaxis receptor methyltransferase CheR, N-terminal domain {Salmonella typhimurium}
svllqmtqrlalsdahfrricqliyqragivladhkrdmvynrlvrrlralglddfgryl
smleanqnsaewqafinaltt
>d1af7_2 3.56.1.3.1 (92-284) Chemotaxis receptor methyltransferase CheR, C-terminal domain {Salmonella typhimurium}
nltaffreahhfpilaeharrrhgeyrvwsaaastgeepysiaitladalgmapgrwkvf
asdidtevlekarsgiyrlselktlspqqlqryfmrgtgpheglvrvrqelanyvefssv
nllekqynvpgpfdaifcrnvmiyfdkttqedilrrfvpllkpdgllfaghsenfsnlvr
efslrgqtvyals
>d1af8__ 1.29.1.1.2 Actinorhodin polyketide synthase acyl carrier protein, ACT ACP {Streptomyces coelicolor, A3(2)}
matllttddlrralvecagetdgtdlsgdfldlrfedigydslalmetaarlesrygvsi
pddvagrvdtprelldlingalaeaa
>d1af9_1 2.26.1.5.1 (875-1110) Tetanus neurotoxin {Clostridium tetani}
edidvilkkstilnldinndiisdisgfnssvitypdaqlvpgingkaihlvnnessevi
vhkamdieyndmfnnftvsfwlrvpkvsashleqygtneysiissmkkhslsigsgwsvs
lkgnnliwtlkdsagevrqitfrdlpdkfnaylankwvfititndrlssanlyingvlmg
saeitglgairednnitlkldrcnnnnqyvsidkfrifckalnpkeieklytsyls
>d1af9_2 2.37.4.2.1 (1111-1315) Tetanus neurotoxin {Clostridium tetani}
itflrdfwgnplrydteyylipvassskdvqlknitdymyltnapsytngklniyyrrly
nglkfiikrytpnneidsfvksgdfiklyvsynnnehivgypkdgnafnnldrilrvgyn
apgiplykkmeavklrdlktysvqlklyddknaslglvgthngqigndpnrdiliasnwy
fnhlkdkilgcdwyfvptdegwtnd
>d1afa11 4.139.1.1.7 (105-226) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvtivdnglwndiscqashtavcef
pa
>d1afa21 4.139.1.1.7 (105-226) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvtivdnglwndiscqashtavcef
pa
>d1afa31 4.139.1.1.7 (105-226) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvtivdnglwndiscqashtavcef
pa
>d1afb11 4.139.1.1.7 (105-226) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvtivdnglwndiscqashtavcef
pa
>d1afb21 4.139.1.1.7 (105-226) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvtivdnglwndiscqashtavcef
pa
>d1afb31 4.139.1.1.7 (105-226) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvtivdnglwndiscqashtavcef
pa
>d1afca_ 2.37.1.1.2 Acidic FGF {Bovine (Bos taurus)}
kpkllycsnggyflrilpdgtvdgtkdrsdqhiqlqlaaesigevyikstetgqflamdt
dgllygsqtpneeclflerleenhyntyiskkhaekhwfvglkkngrsklgprthfgqka
ilflplp
>d1afcb_ 2.37.1.1.2 Acidic FGF {Bovine (Bos taurus)}
kpkllycsnggyflrilpdgtvdgtkdrsdqhiqlqlaaesigevyikstetgqflamdt
dgllygsqtpneeclflerleenhyntyiskkhaekhwfvglkkngrsklgprthfgqka
ilflplp
>d1afcc_ 2.37.1.1.2 Acidic FGF {Bovine (Bos taurus)}
kpkllycsnggyflrilpdgtvdgtkdrsdqhiqlqlaaesigevyikstetgqflamdt
dgllygsqtpneeclflerleenhyntyiskkhaekhwfvglkkngrsklgprthfgqka
ilflplp
>d1afcd_ 2.37.1.1.2 Acidic FGF {Bovine (Bos taurus)}
kpkllycsnggyflrilpdgtvdgtkdrsdqhiqlqlaaesigevyikstetgqflamdt
dgllygsqtpneeclflerleenhyntyiskkhaekhwfvglkkngrsklgprthfgqka
ilflplp
>d1afce_ 2.37.1.1.2 Acidic FGF {Bovine (Bos taurus)}
kpkllycsnggyflrilpdgtvdgtkdrsdqhiqlqlaaesigevyikstetgqflamdt
dgllygsqtpneeclflerleenhyntyiskkhaekhwfvglkkngrsklgprthfgqka
ilflplp
>d1afcf_ 2.37.1.1.2 Acidic FGF {Bovine (Bos taurus)}
kpkllycsnggyflrilpdgtvdgtkdrsdqhiqlqlaaesigevyikstetgqflamdt
dgllygsqtpneeclflerleenhyntyiskkhaekhwfvglkkngrsklgprthfgqka
ilflplp
>d1afcg_ 2.37.1.1.2 Acidic FGF {Bovine (Bos taurus)}
kpkllycsnggyflrilpdgtvdgtkdrsdqhiqlqlaaesigevyikstetgqflamdt
dgllygsqtpneeclflerleenhyntyiskkhaekhwfvglkkngrsklgprthfgqka
ilflplp
>d1afch_ 2.37.1.1.2 Acidic FGF {Bovine (Bos taurus)}
kpkllycsnggyflrilpdgtvdgtkdrsdqhiqlqlaaesigevyikstetgqflamdt
dgllygsqtpneeclflerleenhyntyiskkhaekhwfvglkkngrsklgprthfgqka
ilflplp
>d1afd11 4.139.1.1.7 (105-226) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvtivdnglwndiscqashtavcef
pa
>d1afd21 4.139.1.1.7 (105-226) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvtivdnglwndiscqashtavcef
pa
>d1afd31 4.139.1.1.7 (105-226) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvtivdnglwndiscqashtavcef
pa
>e1afe.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>e1afe.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>d1afh__ 1.54.1.1.4 Plant non-specific lipid-transfer protein (ns-LTP) {Maize (Zea mays)}
aiscgqvasaiapcisyargqgsgpsagccsgvrslnnaarttadrraacnclknaaagv
sglnagnaasipskcgvsipytiststdcsrvn
>d1afi__ 4.47.16.1.1 Mercuric ion binding protein MerP {Shigella flexneri}
atqtvtlavpgmtcaacpitvkkalskvegvskvdvgfekreavvtfddtkasvqkltka
tadagypssvkq
>d1afj__ 4.47.16.1.1 Mercuric ion binding protein MerP {Shigella flexneri}
atqtvtlavpgmtcaacpitvkkalskvegvskvdvgfekreavvtfddtkasvqkltka
tadagypssvkq
>d1afka_ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1afkb_ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1afla_ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1aflb_ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1afp__ 7.26.1.1.1 Antifungal protein (AGAFP) {Mold (Aspergillus giganteus)}
atyngkcykkdnickykaqsgktaickcyvkkcprdgakcefdsykgkcyc
>e1afq.1b 2.41.1.2.7 (alpha,gamma)-chymotrypsin(ogen) {Bovine (Bos taurus)}
ivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgvttsdvvvagefdqgs
ssekiqklkiakvfknskynsltinnditllklstaasfsqtvsavclpsasddfaagtt
cvttgwgltry
>e1afq.1c 2.41.1.2.7 (alpha,gamma)-chymotrypsin(ogen) {Bovine (Bos taurus)}
ntpdrlqqaslpllsntnckkywgtkikdamicagasgvsscmgdsggplvckkngawtl
vgivswgsstcststpgvyarvtalvnwvqqtlaan
>d1afra_ 1.26.1.2.6 delta 9-stearoyl-acyl carrier protein desaturase {Castor bean (Ricinus communis)}
mpprevhvqvthsmppqkieifksldnwaeenilvhlkpvekcwqpqdflpdpasdgfde
qvrelrerakeipddyfvvlvgdmiteealptyqtmlntldgvrdetgasptswaiwtra
wtaeenrhgdllnkylylsgrvdmrqiektiqyligsgmdprtenspylgfiytsfqera
tfishgntarqakehgdiklaqicgtiaadekrhetaytkiveklfeidpdgtvlafadm
mrkkismpahlmydgrddnlfdhfsavaqrlgvytakdyadileflvgrwkvdkltglsa
egqkaqdyvcrlpprirrleeraqgrakeaptmpfswifdrqvkl
>d1afrb_ 1.26.1.2.6 delta 9-stearoyl-acyl carrier protein desaturase {Castor bean (Ricinus communis)}
mpprevhvqvthsmppqkieifksldnwaeenilvhlkpvekcwqpqdflpdpasdgfde
qvrelrerakeipddyfvvlvgdmiteealptyqtmlntldgvrdetgasptswaiwtra
wtaeenrhgdllnkylylsgrvdmrqiektiqyligsgmdprtenspylgfiytsfqera
tfishgntarqakehgdiklaqicgtiaadekrhetaytkiveklfeidpdgtvlafadm
mrkkismpahlmydgrddnlfdhfsavaqrlgvytakdyadileflvgrwkvdkltglsa
egqkaqdyvcrlpprirrleeraqgrakeaptmpfswifdrqvkl
>d1afrc_ 1.26.1.2.6 delta 9-stearoyl-acyl carrier protein desaturase {Castor bean (Ricinus communis)}
mpprevhvqvthsmppqkieifksldnwaeenilvhlkpvekcwqpqdflpdpasdgfde
qvrelrerakeipddyfvvlvgdmiteealptyqtmlntldgvrdetgasptswaiwtra
wtaeenrhgdllnkylylsgrvdmrqiektiqyligsgmdprtenspylgfiytsfqera
tfishgntarqakehgdiklaqicgtiaadekrhetaytkiveklfeidpdgtvlafadm
mrkkismpahlmydgrddnlfdhfsavaqrlgvytakdyadileflvgrwkvdkltglsa
egqkaqdyvcrlpprirrleeraqgrakeaptmpfswifdrqvkl
>d1afrd_ 1.26.1.2.6 delta 9-stearoyl-acyl carrier protein desaturase {Castor bean (Ricinus communis)}
mpprevhvqvthsmppqkieifksldnwaeenilvhlkpvekcwqpqdflpdpasdgfde
qvrelrerakeipddyfvvlvgdmiteealptyqtmlntldgvrdetgasptswaiwtra
wtaeenrhgdllnkylylsgrvdmrqiektiqyligsgmdprtenspylgfiytsfqera
tfishgntarqakehgdiklaqicgtiaadekrhetaytkiveklfeidpdgtvlafadm
mrkkismpahlmydgrddnlfdhfsavaqrlgvytakdyadileflvgrwkvdkltglsa
egqkaqdyvcrlpprirrleeraqgrakeaptmpfswifdrqvkl
>d1afre_ 1.26.1.2.6 delta 9-stearoyl-acyl carrier protein desaturase {Castor bean (Ricinus communis)}
mpprevhvqvthsmppqkieifksldnwaeenilvhlkpvekcwqpqdflpdpasdgfde
qvrelrerakeipddyfvvlvgdmiteealptyqtmlntldgvrdetgasptswaiwtra
wtaeenrhgdllnkylylsgrvdmrqiektiqyligsgmdprtenspylgfiytsfqera
tfishgntarqakehgdiklaqicgtiaadekrhetaytkiveklfeidpdgtvlafadm
mrkkismpahlmydgrddnlfdhfsavaqrlgvytakdyadileflvgrwkvdkltglsa
egqkaqdyvcrlpprirrleeraqgrakeaptmpfswifdrqvkl
>d1afrf_ 1.26.1.2.6 delta 9-stearoyl-acyl carrier protein desaturase {Castor bean (Ricinus communis)}
mpprevhvqvthsmppqkieifksldnwaeenilvhlkpvekcwqpqdflpdpasdgfde
qvrelrerakeipddyfvvlvgdmiteealptyqtmlntldgvrdetgasptswaiwtra
wtaeenrhgdllnkylylsgrvdmrqiektiqyligsgmdprtenspylgfiytsfqera
tfishgntarqakehgdiklaqicgtiaadekrhetaytkiveklfeidpdgtvlafadm
mrkkismpahlmydgrddnlfdhfsavaqrlgvytakdyadileflvgrwkvdkltglsa
egqkaqdyvcrlpprirrleeraqgrakeaptmpfswifdrqvkl
>d1afsa_ 3.1.6.1.7 3-alpha-hydroxysteroid dehydrogenase {Rat (Rattus norvegicus), sprague-dawley strain}
mdsislrvalndgnfipvlgfgttvpekvakdevikatkiaidngfrhfdsaylyeveee
vgqairskiedgtvkredifytsklwstfhrpelvrtclektlkstqldyvdlyiihfpm
alqpgdiffprdehgkllfetvdicdtweamekckdaglaksigvsnfncrqlerilnkp
glkykpvcnqvechlylnqskmldyckskdiilvsyctlgssrdktwvdqkspvllddpv
lcaiakkykqtpalvalryqlqrgvvplirsfnakrikeltqvfefqlasedmkaldgln
rnfrynnakyfddhpnhpf
>d1afsb_ 3.1.6.1.7 3-alpha-hydroxysteroid dehydrogenase {Rat (Rattus norvegicus), sprague-dawley strain}
mdsislrvalndgnfipvlgfgttvpekvakdevikatkiaidngfrhfdsaylyeveee
vgqairskiedgtvkredifytsklwstfhrpelvrtclektlkstqldyvdlyiihfpm
alqpgdiffprdehgkllfetvdicdtweamekckdaglaksigvsnfncrqlerilnkp
glkykpvcnqvechlylnqskmldyckskdiilvsyctlgssrdktwvdqkspvllddpv
lcaiakkykqtpalvalryqlqrgvvplirsfnakrikeltqvfefqlasedmkaldgln
rnfrynnakyfddhpnhpf
>d1afua_ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1afub_ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1afva_ 1.72.1.1.1 HIV-1 capsid protein {Human immunodeficiency virus, type 1, HIV-1}
pivqnlqgqmvhqaisprtlnawvkvveekafspevipmfsalsegatpqdlntmlntvg
ghqaamqmlketineeaaewdrlhpvhagpiapgqmreprgsdiagttstlqeqigwmth
nppipvgeiykrwiilglnkivrmysptsil
>d1afvb_ 1.72.1.1.1 HIV-1 capsid protein {Human immunodeficiency virus, type 1, HIV-1}
pivqnlqgqmvhqaisprtlnawvkvveekafspevipmfsalsegatpqdlntmlntvg
ghqaamqmlketineeaaewdrlhpvhagpiapgqmreprgsdiagttstlqeqigwmth
nppipvgeiykrwiilglnkivrmysptsil
>d1afvh1 2.1.1.1.82 (1-120) Immunoglobulin (variable domains of L and H chains) {Fab 25.3 (mouse), kappa L chain}
qvqlqqpgsvlvrpgasvklsckasgytftsswihwakqrpgqglewigeihpnsgntny
nekfkgkatltvdtssstayvdlssltsedsavyycarwrygspyyfdywgqgttltvss
>d1afvh2 2.1.1.2.86 (121-220) Immunoglobulin (constant domains of L and H chains) {Fab 25.3 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpsstwpsetvtcnvahpasstkvdkkivpk
>d1afvk1 2.1.1.1.82 (1-120) Immunoglobulin (variable domains of L and H chains) {Fab 25.3 (mouse), kappa L chain}
qvqlqqpgsvlvrpgasvklsckasgytftsswihwakqrpgqglewigeihpnsgntny
nekfkgkatltvdtssstayvdlssltsedsavyycarwrygspyyfdywgqgttltvss
>d1afvk2 2.1.1.2.86 (121-220) Immunoglobulin (constant domains of L and H chains) {Fab 25.3 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpsstwpsetvtcnvahpasstkvdkkivpk
>d1afvl1 2.1.1.1.82 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab 25.3 (mouse), kappa L chain}
divltqspaslavslgqratiscrasesvdnygisfmnwfqqkpgqppklliyaasnlgs
gvparfsgsgsgtdfslnihpmeeedtamyfcqqskevpltfgagtkvelkr
>d1afvl2 2.1.1.2.86 (113-217) Immunoglobulin (constant domains of L and H chains) {Fab 25.3 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrne
>d1afvm1 2.1.1.1.82 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab 25.3 (mouse), kappa L chain}
divltqspaslavslgqratiscrasesvdnygisfmnwfqqkpgqppklliyaasnlgs
gvparfsgsgsgtdfslnihpmeeedtamyfcqqskevpltfgagtkvelkr
>d1afvm2 2.1.1.2.86 (113-217) Immunoglobulin (constant domains of L and H chains) {Fab 25.3 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrne
>d1afwa1 3.85.1.1.1 (25-293) Thiolase {Baker's yeast (Saccharomyces cerevisiae)}
knsllekrpedvvivaanrsaigkgfkgafkdvntdyllynflnefigrfpeplradlnl
ieevacgnvlnvgagatehraaclasgipystpfvalnrqcssgltavndiankikvgqi
diglalgvesmtnnyknvnplgmisseelqknreakkclipmgitnenvaanfkisrkdq
defaansyqkaykakneglfedeilpiklpdgsicqsdegprpnvtaeslssirpafikd
rgtttagnasqvsdgvagvllarrsvanq
>d1afwa2 3.85.1.1.1 (294-417) Thiolase {Baker's yeast (Saccharomyces cerevisiae)}
lnlpvlgryidfqtvgvppeimgvgpayaipkvleatglqvqdidifeineafaaqalyc
ihklgidlnkvnprggaialghplgctgarqvatilrelkkdqigvvsmcigtgmgaaai
fike
>d1afwb1 3.85.1.1.1 (25-293) Thiolase {Baker's yeast (Saccharomyces cerevisiae)}
knsllekrpedvvivaanrsaigkgfkgafkdvntdyllynflnefigrfpeplradlnl
ieevacgnvlnvgagatehraaclasgipystpfvalnrqcssgltavndiankikvgqi
diglalgvesmtnnyknvnplgmisseelqknreakkclipmgitnenvaanfkisrkdq
defaansyqkaykakneglfedeilpiklpdgsicqsdegprpnvtaeslssirpafikd
rgtttagnasqvsdgvagvllarrsvanq
>d1afwb2 3.85.1.1.1 (294-417) Thiolase {Baker's yeast (Saccharomyces cerevisiae)}
lnlpvlgryidfqtvgvppeimgvgpayaipkvleatglqvqdidifeineafaaqalyc
ihklgidlnkvnprggaialghplgctgarqvatilrelkkdqigvvsmcigtgmgaaai
fike
>d1ag0a_ 2.5.1.1.23 Azurin {Pseudomonas aeruginosa}
aaecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgv
vtdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffdtfpghsa
lmkgtltlk
>d1ag0b_ 2.5.1.1.23 Azurin {Pseudomonas aeruginosa}
aaecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgv
vtdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffdtfpghsa
lmkgtltlk
>d1ag1o_ 3.1.1.1.4 Triosephosphate isomerase {Trypanosoma brucei brucei}
skpqpiaaanwkcngsqqslselidlfnstsinhdvqcvvastfvhlamtkerlshpkfv
iaaqnaiaksgaftgevslpilkdfgvnwivlghserrayygetneivadkvaaavasgf
mviacigetlqeresgrtavvvltqiaaiakklkkadwakvviayepvwaigtgkvatpq
qaqeahalirswvsskigadvagelrilyggsvngknartlyqqrdvngflvggaslkpe
fvdiikatq
>d1ag1t_ 3.1.1.1.4 Triosephosphate isomerase {Trypanosoma brucei brucei}
skpqpiaaanwkcngsqqslselidlfnstsinhdvqcvvastfvhlamtkerlshpkfv
iaaqnaiaksgaftgevslpilkdfgvnwivlghserrayygetneivadkvaaavasgf
mviacigetlqeresgrtavvvltqiaaiakklkkadwakvviayepvwaigtgkvatpq
qaqeahalirswvsskigadvagelrilyggsvngknartlyqqrdvngflvggaslkpe
fvdiikatq
>d1ag2__ 4.6.1.1.1 Prion protein domain {Mouse (Mus musculus)}
glggymlgsamsrpmihfgndwedryyrenmyrypnqvyyrpvdqysnqnnfvhdcvnit
ikqhtvttttkgenftetdvkmmervveqmcvtqyqkesqayy
>d1ag4__ 2.10.1.2.2 Spherulin 3a (S3a) {Slime mold (Physarum polycephalum)}
msvckgvsgnpakgevflykhvnfqgdswkvtgnvydfrsvsglndvvssvkvgpntkaf
ifkddrfngnfirleessqvtdlttrnlndaissiivatfesa
>d1ag6__ 2.5.1.1.5 Plastocyanin {Spinach (Spinacia oleracea)}
vevllggddgslaflpgdfsvasgeeivfknnagfphnvvfdedeipsgvdaakismsee
dllnapgetykvtltekgtykfycsphqgagmvgkvtvn
>d1ag7__ 7.3.6.1.2 Conotoxin {Synthetic (Conus geographus), GS}
acsgrgsrcxxqccmglrcgrgnpqkcigahxdv
>d1ag8a_ 3.71.1.1.3 Aldehyde reductase (dehydrogenase), ALDH {Bovine (Bos taurus), mitochondrial}
vptpnqqpevlynqifinnewhdavskktfptvnpstgdvichvaegdkadvdravkaar
aafqlgspwrrmdasergrllnrladlierdrtylaaletldngkpyiisylvdldmvlk
clryyagwadkyhgktipidgdyfsytrhepvgvcgqiipwnfpllmqawklgpalatgn
vvvmkvaeqtpltalyvanlikeagfppgvvnvipgfgptagaaiashedvdkvaftgst
evghliqvaagksnlkrvtleiggkspniimsdadmdwaveqahfalffnqgqcccagsr
tfvqediyaefversvaraksrvvgnpfdsrteqgpqvdetqfkkvlgyiksgkeeglkl
lcgggaaadrgyfiqptvfgdlqdgmtiakeeifgpvmqilkfksmeevvgrannskygl
aaavftkdldkanylsqalqagtvwvncydvfgaqspfggyklsgsgrelgeyglqayte
vktvtvrvpqkns
>d1ag8b_ 3.71.1.1.3 Aldehyde reductase (dehydrogenase), ALDH {Bovine (Bos taurus), mitochondrial}
vptpnqqpevlynqifinnewhdavskktfptvnpstgdvichvaegdkadvdravkaar
aafqlgspwrrmdasergrllnrladlierdrtylaaletldngkpyiisylvdldmvlk
clryyagwadkyhgktipidgdyfsytrhepvgvcgqiipwnfpllmqawklgpalatgn
vvvmkvaeqtpltalyvanlikeagfppgvvnvipgfgptagaaiashedvdkvaftgst
evghliqvaagksnlkrvtleiggkspniimsdadmdwaveqahfalffnqgqcccagsr
tfvqediyaefversvaraksrvvgnpfdsrteqgpqvdetqfkkvlgyiksgkeeglkl
lcgggaaadrgyfiqptvfgdlqdgmtiakeeifgpvmqilkfksmeevvgrannskygl
aaavftkdldkanylsqalqagtvwvncydvfgaqspfggyklsgsgrelgeyglqayte
vktvtvrvpqkns
>d1ag8c_ 3.71.1.1.3 Aldehyde reductase (dehydrogenase), ALDH {Bovine (Bos taurus), mitochondrial}
vptpnqqpevlynqifinnewhdavskktfptvnpstgdvichvaegdkadvdravkaar
aafqlgspwrrmdasergrllnrladlierdrtylaaletldngkpyiisylvdldmvlk
clryyagwadkyhgktipidgdyfsytrhepvgvcgqiipwnfpllmqawklgpalatgn
vvvmkvaeqtpltalyvanlikeagfppgvvnvipgfgptagaaiashedvdkvaftgst
evghliqvaagksnlkrvtleiggkspniimsdadmdwaveqahfalffnqgqcccagsr
tfvqediyaefversvaraksrvvgnpfdsrteqgpqvdetqfkkvlgyiksgkeeglkl
lcgggaaadrgyfiqptvfgdlqdgmtiakeeifgpvmqilkfksmeevvgrannskygl
aaavftkdldkanylsqalqagtvwvncydvfgaqspfggyklsgsgrelgeyglqayte
vktvtvrvpqkns
>d1ag8d_ 3.71.1.1.3 Aldehyde reductase (dehydrogenase), ALDH {Bovine (Bos taurus), mitochondrial}
vptpnqqpevlynqifinnewhdavskktfptvnpstgdvichvaegdkadvdravkaar
aafqlgspwrrmdasergrllnrladlierdrtylaaletldngkpyiisylvdldmvlk
clryyagwadkyhgktipidgdyfsytrhepvgvcgqiipwnfpllmqawklgpalatgn
vvvmkvaeqtpltalyvanlikeagfppgvvnvipgfgptagaaiashedvdkvaftgst
evghliqvaagksnlkrvtleiggkspniimsdadmdwaveqahfalffnqgqcccagsr
tfvqediyaefversvaraksrvvgnpfdsrteqgpqvdetqfkkvlgyiksgkeeglkl
lcgggaaadrgyfiqptvfgdlqdgmtiakeeifgpvmqilkfksmeevvgrannskygl
aaavftkdldkanylsqalqagtvwvncydvfgaqspfggyklsgsgrelgeyglqayte
vktvtvrvpqkns
>d1ag9a_ 3.16.4.1.4 Flavodoxin {Escherichia coli}
aitgiffgsdtgnteniakmiqkqlgkdvadvhdiaksskedleaydilllgiptwyyge
aqcdwddffptleeidfngklvalfgcgdqedyaeyfcdalgtirdiieprgativghwp
tagyhfeaskgladddhfvglaidedrqpeltaervekwvkqiseelhldeilna
>d1ag9b_ 3.16.4.1.4 Flavodoxin {Escherichia coli}
aitgiffgsdtgnteniakmiqkqlgkdvadvhdiaksskedleaydilllgiptwyyge
aqcdwddffptleeidfngklvalfgcgdqedyaeyfcdalgtirdiieprgativghwp
tagyhfeaskgladddhfvglaidedrqpeltaervekwvkqiseelhldeilna
>d1agba1 2.1.1.2.8 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-b0801}
adppkthvthhpisdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrwep
>d1agba2 4.17.1.1.15 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-b0801}
gshsmryfdtamsrpgrgeprfisvgyvddtqfvrfdsdaaspreeprapwieqegpeyw
drntqifktntqtdreslrnlrgyynqseagshtlqsmygcdvgpdgrllrghnqyaydg
kdyialnedlrswtaadtaaqitqrkweaarvaeqdraylegtcvewlrrylengkdtle
r
>d1agbb1 2.1.1.2.8 Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-b0801}
iqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskdw
sfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1agca1 2.1.1.2.8 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-b0801}
adppkthvthhpisdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrwep
>d1agca2 4.17.1.1.15 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-b0801}
gshsmryfdtamsrpgrgeprfisvgyvddtqfvrfdsdaaspreeprapwieqegpeyw
drntqifktntqtdreslrnlrgyynqseagshtlqsmygcdvgpdgrllrghnqyaydg
kdyialnedlrswtaadtaaqitqrkweaarvaeqdraylegtcvewlrrylengkdtle
r
>d1agcb1 2.1.1.2.8 Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-b0801}
iqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskdw
sfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1agda1 2.1.1.2.8 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-b0801}
adppkthvthhpisdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrwep
>d1agda2 4.17.1.1.15 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-b0801}
gshsmryfdtamsrpgrgeprfisvgyvddtqfvrfdsdaaspreeprapwieqegpeyw
drntqifktntqtdreslrnlrgyynqseagshtlqsmygcdvgpdgrllrghnqyaydg
kdyialnedlrswtaadtaaqitqrkweaarvaeqdraylegtcvewlrrylengkdtle
r
>d1agdb1 2.1.1.2.8 Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-b0801}
iqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskdw
sfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1agea1 2.1.1.2.8 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-b0801}
adppkthvthhpisdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrwep
>d1agea2 4.17.1.1.15 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-b0801}
gshsmryfdtamsrpgrgeprfisvgyvddtqfvrfdsdaaspreeprapwieqegpeyw
drntqifktntqtdreslrnlrgyynqseagshtlqsmygcdvgpdgrllrghnqyaydg
kdyialnedlrswtaadtaaqitqrkweaarvaeqdraylegtcvewlrrylengkdtle
r
>d1ageb1 2.1.1.2.8 Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-b0801}
iqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskdw
sfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1agfa1 2.1.1.2.8 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-b0801}
adppkthvthhpisdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrwep
>d1agfa2 4.17.1.1.15 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-b0801}
gshsmryfdtamsrpgrgeprfisvgyvddtqfvrfdsdaaspreeprapwieqegpeyw
drntqifktntqtdreslrnlrgyynqseagshtlqsmygcdvgpdgrllrghnqyaydg
kdyialnedlrswtaadtaaqitqrkweaarvaeqdraylegtcvewlrrylengkdtle
r
>d1agfb1 2.1.1.2.8 Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-b0801}
iqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskdw
sfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1agg__ 7.3.6.2.1 omega-Agatoxin IV, IVa, IVb {Funnel web spider (Agelenopsis aperta)}
ednciaedygkctwggtkccrgrpcrcsmigtncectprlimeglsfa
>d1agi__ 4.5.1.1.8 Angiogenin {Bovine (Bos taurus)}
aqddyryihfltqhydakpkgrndeycfnmmknrrltrpckdrntfihgnkndikaiced
rngqpyrgdlrisksefqitickhkggssrppcrygatedsrvivvgcenglpvhfdesf
itprh
>d1agja_ 2.41.1.1.8 Epidermolytic (exfoliative) toxin A {Staphylococcus aureus}
evsaeeikkheekwnkyygvnafnlpkelfskvdekdrqkypyntignvfvkgqtsatgv
ligkntvltnrhiakfangdpskvsfrpsintddngntetpygeyevkeilqepfgagvd
lalirlkpdqngvslgdkispakigtsndlkdgdkleligypfdhkvnqmhrseielttl
srglryygftvpgnsgsgifnsngelvgihsskvshldrehqinygvgignyvkriinek
ne
>d1agjb_ 2.41.1.1.8 Epidermolytic (exfoliative) toxin A {Staphylococcus aureus}
evsaeeikkheekwnkyygvnafnlpkelfskvdekdrqkypyntignvfvkgqtsatgv
ligkntvltnrhiakfangdpskvsfrpsintddngntetpygeyevkeilqepfgagvd
lalirlkpdqngvslgdkispakigtsndlkdgdkleligypfdhkvnqmhrseielttl
srglryygftvpgnsgsgifnsngelvgihsskvshldrehqinygvgignyvkriinek
ne
>d1agm__ 1.98.1.1.1 Glucoamylase {Aspergillus awamori, variant x100}
atldswlsneatvartailnnigadgawvsgadsgivvaspstdnpdyfytwtrdsglvi
ktlvdlfrngdtdllstiehyissqaiiqgvsnpsgdlssgglgepkfnvdetaytgswg
rpqrdgpalratamigfgqwlldngytsaateivwplvrndlsyvaqywnqtgydlweev
ngssfftiavqhralvegsafatavgsscswcdsqapqilcylqsfwtgsyilanfdssr
sgkdtntllgsihtfdpeagcddstfqpcspralanhkevvdsfrsiytlndglsdseav
avgrypedsyyngnpwflctlaaaeqlydalyqwdkqgsleitdvsldffkalysgaatg
tyssssstyssivsavktfadgfvsivethaasngslseqfdksdgdelsardltwsyaa
lltannrrnsvvppswgetsassvpgtcaatsasgtyssvtvtswpsiva
>d1agna1 2.31.1.2.2 (1-174,325-374) Alcohol dehydrogenase {Human (Homo sapiens)}
gtagkvikckaavlweqkqpfsieeievappktkevrikilatgicrtddhvikgtmvsk
fpvivgheatgivesigegvttvkpgdkviplflpqcrecnacrnpdgnlcirsditgrg
vladgttrftckgkpvhhfmntstfteytvvdessvakiddaappekvcligcXrddvpk
lvteflakkfdldqlithvlpfkkisegfellnsgqsirtvltf
>d1agna2 3.2.1.1.2 (175-324) Alcohol dehydrogenase {Human (Homo sapiens), different isozymes}
gfstgygaavktgkvkpgstcvvfglggvglsvimgcksagasriigidlnkdkfekama
vgatecispkdstkpisevlsemtgnnvgytfevighletmidalaschmnygtsvvvgv
ppsakmltydpmllftgrtwkgcvfgglks
>d1agnb1 2.31.1.2.2 (1-174,325-374) Alcohol dehydrogenase {Human (Homo sapiens)}
gtagkvikckaavlweqkqpfsieeievappktkevrikilatgicrtddhvikgtmvsk
fpvivgheatgivesigegvttvkpgdkviplflpqcrecnacrnpdgnlcirsditgrg
vladgttrftckgkpvhhfmntstfteytvvdessvakiddaappekvcligcXrddvpk
lvteflakkfdldqlithvlpfkkisegfellnsgqsirtvltf
>d1agnb2 3.2.1.1.2 (175-324) Alcohol dehydrogenase {Human (Homo sapiens), different isozymes}
gfstgygaavktgkvkpgstcvvfglggvglsvimgcksagasriigidlnkdkfekama
vgatecispkdstkpisevlsemtgnnvgytfevighletmidalaschmnygtsvvvgv
ppsakmltydpmllftgrtwkgcvfgglks
>d1agnc1 2.31.1.2.2 (1-174,325-374) Alcohol dehydrogenase {Human (Homo sapiens)}
gtagkvikckaavlweqkqpfsieeievappktkevrikilatgicrtddhvikgtmvsk
fpvivgheatgivesigegvttvkpgdkviplflpqcrecnacrnpdgnlcirsditgrg
vladgttrftckgkpvhhfmntstfteytvvdessvakiddaappekvcligcXrddvpk
lvteflakkfdldqlithvlpfkkisegfellnsgqsirtvltf
>d1agnc2 3.2.1.1.2 (175-324) Alcohol dehydrogenase {Human (Homo sapiens), different isozymes}
gfstgygaavktgkvkpgstcvvfglggvglsvimgcksagasriigidlnkdkfekama
vgatecispkdstkpisevlsemtgnnvgytfevighletmidalaschmnygtsvvvgv
ppsakmltydpmllftgrtwkgcvfgglks
>d1agnd1 2.31.1.2.2 (1-174,325-374) Alcohol dehydrogenase {Human (Homo sapiens)}
gtagkvikckaavlweqkqpfsieeievappktkevrikilatgicrtddhvikgtmvsk
fpvivgheatgivesigegvttvkpgdkviplflpqcrecnacrnpdgnlcirsditgrg
vladgttrftckgkpvhhfmntstfteytvvdessvakiddaappekvcligcXrddvpk
lvteflakkfdldqlithvlpfkkisegfellnsgqsirtvltf
>d1agnd2 3.2.1.1.2 (175-324) Alcohol dehydrogenase {Human (Homo sapiens), different isozymes}
gfstgygaavktgkvkpgstcvvfglggvglsvimgcksagasriigidlnkdkfekama
vgatecispkdstkpisevlsemtgnnvgytfevighletmidalaschmnygtsvvvgv
ppsakmltydpmllftgrtwkgcvfgglks
>d1agp__ 3.30.1.6.1 cH-p21 Ras protein {Human (Homo sapiens)}
mteyklvvvgadgvgksaltiqliqnhfvdeydptiedsyrkqvvidgetclldildtag
qeeysamrdqymrtgegflcvfainntksfedihqyreqikrvkdsddvpmvlvgnkcdl
aartvesrqaqdlarsygipyietsaktrqgvedafytlvreirqh
>d1agqa_ 7.17.1.2.6 Glial cell-derived neurotrophic factor, GDNF {Rat (Rattus norvegicus)}
nrgcvltaihlnvtdlglgyetkeelifrycsgsceaaetmydkilknlsrsrrltsdkv
gqaccrpvafdddlsflddslvyhilrkhsakrcgci
>d1agqb_ 7.17.1.2.6 Glial cell-derived neurotrophic factor, GDNF {Rat (Rattus norvegicus)}
knrgcvltaihlnvtdlglgyetkeelifrycsgsceaaetmydkilknlsrsrrltsdk
vgqaccrpvafdddlsflddslvyhilrkhsakrcgci
>d1agqc_ 7.17.1.2.6 Glial cell-derived neurotrophic factor, GDNF {Rat (Rattus norvegicus)}
gcvltaihlnvtdlglgyetkeelifrycsgsceaaetmydkilknlsrsrrltsdkvgq
accrpvafdddlsflddslvyhilrkhsakrcgci
>d1agqd_ 7.17.1.2.6 Glial cell-derived neurotrophic factor, GDNF {Rat (Rattus norvegicus)}
gcvltaihlnvtdlglgyetkeelifrycsgsceaaetmydkilknlsrsrrltsdkvgq
accrpvafdddlsflddslvyhilrkhsakrcgci
>d1agra1 1.67.1.1.2 (61-181) Transducin (alpha subunit), insertion domain {Rat (Rattus rattus)}
yseeeckqykavvysntiqsiiaiiramgrlkidfgdaaraddarqlfvlagaaeegfmt
aelagvikrlwkdsgvqacfnrsreyqlndsaayylndldriaqpnyiptqqdvlrtrvk
t
>d1agra2 3.30.1.6.13 (5-60,182-354) Transducin (alpha subunit) {Rat (Rattus rattus)}
lsaedkaaverskmidrnlredgekaarevkllllgagesgkstivkqmkiiheagXtgi
vethftfkdlhfkmfdvggqrserkkwihcfegvtaiifcvalsdydlvlaedeemnrmh
esmklfdsicnnkwftdtsiilflnkkdlfeekikksplticypeyagsntyeeaaayiq
cqfedlnkrkdtkeiythftcatdtknvqfvfdavtdviiknnlkdcglf
>d1agrd1 1.67.1.1.2 (61-181) Transducin (alpha subunit), insertion domain {Rat (Rattus rattus)}
yseeeckqykavvysntiqsiiaiiramgrlkidfgdaaraddarqlfvlagaaeegfmt
aelagvikrlwkdsgvqacfnrsreyqlndsaayylndldriaqpnyiptqqdvlrtrvk
t
>d1agrd2 3.30.1.6.13 (11-60,182-354) Transducin (alpha subunit) {Rat (Rattus rattus)}
aaverskmidrnlredgekaarevkllllgagesgkstivkqmkiiheagXtgivethft
fkdlhfkmfdvggqrserkkwihcfegvtaiifcvalsdydlvlaedeemnrmhesmklf
dsicnnkwftdtsiilflnkkdlfeekikksplticypeyagsntyeeaaayiqcqfedl
nkrkdtkeiythftcatdtknvqfvfdavtdviiknnlkdcglf
>d1agre_ 1.88.1.1.1 Regulator of G-protein signalling 4, RGS4 {Rat (Rattus norvegicus)}
vsqeevkkwaeslenlinhecglaafkaflkseyseenidfwisceeykkikspsklspk
akkiynefisvqatkevnldsctreetsrnmleptitcfdeaqkkifnlmekdsyrrflk
srfyldlt
>d1agrh_ 1.88.1.1.1 Regulator of G-protein signalling 4, RGS4 {Rat (Rattus norvegicus)}
aeslenlinhecglaafkaflkseyseenidfwisceeykkikspsklspkakkiynefi
svqatkevnldsctreetsrnmleptitcfdeaqkkifnlmekdsyrrflksrfyl
>d1agsa1 1.48.1.1.9 (80-221) Glutathione S-transferase {Human (Homo sapiens), class alpha}
lyrkdikekalidmyiegiadlgemilllpftqpeeqdaklalikekiknryfpafekvl
kshgqdylvgnklsradihlvellyyveeldsslissfpllkalktrisnlptvkkflqp
gsprkppmdeksleearkifrf
>d1agsa2 3.38.1.5.9 (1-79) Glutathione S-transferase {Human (Homo sapiens), class alpha}
aekpklhyfnargrmestrwllaaagvefeekfiksaedldklrndgylmfqqvpmveid
gmklvqtrailnyiaskyn
>d1agsb1 1.48.1.1.9 (80-221) Glutathione S-transferase {Human (Homo sapiens), class alpha}
lyrkdikekalidmyiegiadlgemilllpftqpeeqdaklalikekiknryfpafekvl
kshgqdylvgnklsradihlvellyyveeldsslissfpllkalktrisnlptvkkflqp
gsprkppmdeksleearkifrf
>d1agsb2 3.38.1.5.9 (1-79) Glutathione S-transferase {Human (Homo sapiens), class alpha}
aekpklhyfnargrmestrwllaaagvefeekfiksaedldklrndgylmfqqvpmveid
gmklvqtrailnyiaskyn
>d1agt__ 7.3.7.2.9 Agitoxin {Scorpion (Leiurus quinquestriatus hebraeus)}
gvpinvsctgspqcikpckdagmrfgkcmnrkchctpk
>d1agwa_ 4.117.1.2.5 Fibroblast growth factor receptor 1 {Human (Homo sapiens)}
elpedprwelprdrlvlgkplgegafgqvvlaeaigldkdkpnrvtkvavkmlksdatek
dlsdlisememmkmigkhkniinllgactqdgplyviveyaskgnlreylqarrppgley
synpshnpeeqlsskdlvscayqvargmeylaskkcihrdlaarnvlvtednvmkiadfg
lardihhidyykkttngrlpvkwmapealfdriythqsdvwsfgvllweiftlggspypg
vpveelfkllkeghrmdkpsnctnelymmmrdcwhavpsqrptfkqlvedldrivalts
>d1agwb_ 4.117.1.2.5 Fibroblast growth factor receptor 1 {Human (Homo sapiens)}
seyelpedprwelprdrlvlgkplgegafgqvvlaeaigldkdkpnrvtkvavkmlksda
tekdlsdlisememmkmigkhkniinllgactqdgplyviveyaskgnlreylqarrppg
leysynpshnpeeqlsskdlvscayqvargmeylaskkcihrdlaarnvlvtednvmkia
dfglardihhidyykkttngrlpvkwmapealfdriythqsdvwsfgvllweiftlggsp
ypgvpveelfkllkeghrmdkpsnctnelymmmrdcwhavpsqrptfkqlvedldrival
t
>d1agx__ 3.78.1.1.3 Glutaminase-asparaginase {Acinetobacter glutaminasificans}
knnvvivatggtiagagasstnsatysaakvpvdalikavpqvndlanitgiqalqvase
sitdkellslarqvndlvkkpsvngvvithgtdtmeetafflnlvvhtdkpivlvgsmrp
stalsadgplnlysavalassneaknkgvmvlmndsifaardvtkginihthafvsqwga
lgtlvegkpywfrssvkkhtnnsefniekiqgdalpgvqivygsdnmmpdayqafakagv
kaiihagtgngsmanylvpevrklhdeqglqivrssrvaqgfvlrnaeqpddkygwiaah
dlnpqkarllmalaltktndakeiqnmfwny
>d1agy__ 3.16.7.1.1 Cutinase {Fungus (Fusarium solani), subsp. Pisi}
rttrddlingnsascrdvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1ah0__ 3.1.6.1.5 Aldose reductase (aldehyde reductase) {Porcine (Sus scrofa)}
ashlvlytgakmpilglgtwksppgkvteavkvaidlgyrhidcahvyqnenevglglqe
klqgqvvkredlfivsklwctdheknlvkgacqttlrdlkldyldlylihwptgfkpgkd
pfpldgdgnvvpdesdfvetweameelvdeglvkaigvsnfnhlqvekilnkpglkykpa
vnqievhpyltqeklieyckskgivvtaysplgspdrpwakpedpslledprikaiaaky
nkttaqvlirfpmqrnlivipksvtperiaenfqvfdfelspedmntllsynrnwrvcal
mscashkdypfheey
>d1ah1__ 2.1.1.1.159 Immunoreceptor CTLA-4 (CD152), N-terminal fragment {Human (Homo sapiens)}
amhvaqpavvlassrgiasfvceyaspgkatevrvtvlrqadsqvtevcaatymmgnelt
flddsictgtssgnqvnltiqglramdtglyickvelmypppyylgigngtqiyvidpep
cpdsdqepk
>d1ah2__ 3.33.1.1.11 Serine protease PB92 {Bacillus alcalophylus}
aqsvpwgisrvqapaahnrgltgsgvkvavldtgisthpdlnirggasfvpgepstqdgn
ghgthvagtiaalnnsigvlgvapnaelyavkvlgasgsgsvssiaqglewagnngmhva
nlslgspspsatleqavnsatsrgvlvvaasgnsgagsisyparyanamavgatdqnnnr
asfsqygagldivapgvnvqstypgstyaslngtsmatphvagaaalvkqknpswsnvqi
rnhlkntatslgstnlygsglvnaeaatr
>d1ah3__ 3.1.6.1.5 Aldose reductase (aldehyde reductase) {Porcine (Sus scrofa)}
shlvlytgakmpilglgtwksppgkvteavkvaidlgyrhidcahvyqnenevglglqek
lqgqvvkredlfivsklwctdheknlvkgacqttlrdlkldyldlylihwptgfkpgkdp
fpldgdgnvvpdesdfvetweameelvdeglvkaigvsnfnhlqvekilnkpglkykpav
nqievhpyltqeklieyckskgivvtaysplgspdrpwakpedpslledprikaiaakyn
kttaqvlirfpmqrnlivipksvtperiaenfqvfdfelspedmntllsynrnwrvcalm
scashkdypfheey
>d1ah4__ 3.1.6.1.5 Aldose reductase (aldehyde reductase) {Porcine (Sus scrofa)}
shlvlytgakmpilglgtwksppgkvteavkvaidlgyrhidcahvyqnenevglglqek
lqgqvvkredlfivsklwctdheknlvkgacqttlrdlkldyldlylihwptgfkpgkdp
fpldgdgnvvpdesdfvetweameelvdeglvkaigvsnfnhlqvekilnkpglkykpav
nqievhpyltqeklieyckskgivvtaysplgspdrpwakpedpslledprikaiaakyn
kttaqvlirfpmqrnlivipksvtperiaenfqvfdfelspedmntllsynrnwrvcalm
scashkdypfheey
>d1ah5_1 3.84.1.1.2 (3-219) Porphobilinogen deaminase (hydroxymethylbilane synthase), N-terminal domain {Escherichia coli}
dnvlriatrqsplalwqahyvkdklxashpglvvelvpxvtrgdvildtplakvggkglf
vkelevallenradiavhsxkdvpvefpqglglvticeredprdafvsnnydsldalpag
sivgtsslrrqcqlaerrpdliirslrgnvgtrlskldngeydaiilavaglkrlglesr
iraalppeislpavgqgavgiecrlddsrtrellaal
>d1ah5_2 4.41.2.1.1 (220-313) Porphobilinogen deaminase (hydroxymethylbilane synthase), C-terminal domain {Escherichia coli}
nhhetalrvtaeraxntrleggcqvpigsyaelidgeiwlralvgapdgsqiirgerrga
pqdaeqxgislaeellnngareilaevyngdapa
>d1ah6__ 4.96.1.1.1 HSP90 {Baker's yeast (Saccharomyces cerevisiae)}
asetfefqaeitqlmsliintvysnkeiflrelisnasdaldkirykslsdpkqletepd
lfiritpkpeqkvleirdsgigmtkaelinnlgtiaksgtkafmealsagadvsmigqfg
vgfyslflvadrvqvisksnddeqyiwesnaggsftvtldevnerigrgtilrlflkddq
leyleekrikevikrhsefvaypiqlvvtkeve
>d1ah7__ 1.115.1.1.1 Bacterial phosholipase C {Bacillus cereus}
wsaedkhkegvnshlwivnraidimsrnttlvkqdrvaqlnewrtelengiyaadyenpy
ydnstfashfydpdngktyipfakqaketgakyfklagesyknkdmkqaffylglslhyl
gdvnqpmhaanftnlsypqgfhskyenfvdtikdnykvtdgngywnwkgtnpeewihgaa
vvakqdysgivndntkdwfvkaavsqeyadkwraevtpmtgkrlmdaqrvtagyiqlwfd
tygdr
>d1ah8a_ 4.96.1.1.1 HSP90 {Baker's yeast (Saccharomyces cerevisiae)}
asetfefqaeitqlmsliintvysnkeiflrelisnasdaldkirykslsdpkqletepd
lfiritpkpeqkvleirdsgigmtkaelinnlgtiaksgtkafmealsagadvsmigqfg
vgfyslflvadrvqvisksnddeqyiwesnaggsftvtldevnerigrgtilrlflkddq
leyleekrikevikrhsefvaypiqlvvtkeveke
>d1ah8b_ 4.96.1.1.1 HSP90 {Baker's yeast (Saccharomyces cerevisiae)}
asetfefqaeitqlmsliintvysnkeiflrelisnasdaldkirykslsdpkqletepd
lfiritpkpeqkvleirdsgigmtkaelinnlgtiaksgtkafmealsagadvsmigqfg
vgfyslflvadrvqvisksnddeqyiwesnaggsftvtldevnerigrgtilrlflkddq
leyleekrikevikrhsefvaypiqlvvtkevekevpi
>d1ah9__ 2.35.4.5.4 Translational initiation factor 1, IF1 {Escherichia coli}
akedniemqgtvletlpntmfrvelenghvvtahisgkmrknyiriltgdkvtveltpyd
lskgrivfrsr
>d1aha__ 4.135.1.1.3 alpha-Momorcharin (momordin) {Bitter gourd (Momordica charantia)}
dvsfrlsgadprsygmfikdlrnalpfrekvyniplllpsvsgagryllmhlfnydgkti
tvavdvtnvyimgyladttsyffnepaaelasqyvfrdarrkitlpysgnyerlqiaagk
prekipiglpaldsaistllhydstaaagallvliqttaeaarfkyieqqiqerayrdev
pslatislenswsglskqiqlaqgnngifrtpivlvdnkgnrvqitnvtskvvtsniqll
lntrni
>d1ahb__ 4.135.1.1.3 alpha-Momorcharin (momordin) {Bitter gourd (Momordica charantia)}
dvsfrlsgadprsygmfikdlrnalpfrekvyniplllpsvsgagryllmhlfnydgkti
tvavdvtnvyimgyladttsyffnepaaelasqyvfrdarrkitlpysgnyerlqiaagk
prekipiglpaldsaistllhydstaaagallvliqttaeaarfkyieqqiqerayrdev
pslatislenswsglskqiqlaqgnngifrtpivlvdnkgnrvqitnvtskvvtsniqll
lntrni
>d1ahc__ 4.135.1.1.3 alpha-Momorcharin (momordin) {Bitter gourd (Momordica charantia)}
dvsfrlsgadprsygmfikdlrnalpfrekvyniplllpsvsgagryllmhlfnydgkti
tvavdvtnvyimgyladttsyffnepaaelasqyvfrdarrkitlpysgnyerlqiaagk
prekipiglpaldsaistllhydstaaagallvliqttaeaarfkyieqqiqerayrdev
pslatislenswsglskqiqlaqgnngifrtpivlvdnkgnrvqitnvtskvvtsniqll
lntrni
>d1ahdp_ 1.4.1.1.13 Antennapedia Homeodomain {Drosophila melanogaster}
mrkrgrqtytryqtlelekefhfnryltrrrrieiahalslterqikiwfqnrrmkwkke
nktkgepg
>d1ahea_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgiglyydetgkipvltsvkkaeqyllene
ttklylgidgipefgrctqellfgkgsalindkrartaqtpggsgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanyssppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aheb_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgiglyydetgkipvltsvkkaeqyllene
ttklylgidgipefgrctqellfgkgsalindkrartaqtpggsgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanyssppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ahfa_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgiglyydetgkipvltsvkkaeqyllene
ttklylgidgipefgrctqellfgkgsalindkrartaqtpggsgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanyssppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ahfb_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgiglyydetgkipvltsvkkaeqyllene
ttklylgidgipefgrctqellfgkgsalindkrartaqtpggsgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanyssppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ahga_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgiglyydetgkipvltsvkkaeqyllene
ttklylgidgipefgrctqellfgkgsalindkrartaqtpggsgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanyssppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ahgb_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgiglyydetgkipvltsvkkaeqyllene
ttklylgidgipefgrctqellfgkgsalindkrartaqtpggsgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanyssppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ahha_ 3.2.1.2.9 7-alpha-hydroxysteroid dehydrogenase {Escherichia coli}
mfnsdnlrldgkcaiitgagagigkeiaitfatagasvvvsdinadaanhvvdeiqqlgg
qafacrcditseqelsaladfaisklgkvdilvnnaggggpkpfdmpmadfrrayelnvf
sffhlsqlvapemekngggviltitsmaaenkninmtsyasskaaashlvrnmafdlgek
nirvngiapgailtdalksvitpeieqkmlqhtpirrlgqpqdianaalflcspaaswvs
gqiltvsgggvqe
>d1ahhb_ 3.2.1.2.9 7-alpha-hydroxysteroid dehydrogenase {Escherichia coli}
mfnsdnlrldgkcaiitgagagigkeiaitfatagasvvvsdinadaanhvvdeiqqlgg
qafacrcditseqelsaladfaisklgkvdilvnnaggggpkpfdmpmadfrrayelnvf
sffhlsqlvapemekngggviltitsmaaenkninmtsyasskaaashlvrnmafdlgek
nirvngiapgailtdalksvitpeieqkmlqhtpirrlgqpqdianaalflcspaaswvs
gqiltvsgggvqe
>d1ahia_ 3.2.1.2.9 7-alpha-hydroxysteroid dehydrogenase {Escherichia coli}
mfnsdnlrldgkcaiitgagagigkeiaitfatagasvvvsdinadaanhvvdeiqqlgg
qafacrcditseqelsaladfaisklgkvdilvnnaggggpkpfdmpmadfrrayelnvf
sffhlsqlvapemekngggviltitsmaaenkninmtsyasskaaashlvrnmafdlgek
nirvngiapgailtdalksvitpeieqkmlqhtpirrlgqpqdianaalflcspaaswvs
gqiltvsgggvqeln
>d1ahib_ 3.2.1.2.9 7-alpha-hydroxysteroid dehydrogenase {Escherichia coli}
mfnsdnlrldgkcaiitgagagigkeiaitfatagasvvvsdinadaanhvvdeiqqlgg
qafacrcditseqelsaladfaisklgkvdilvnnaggggpkpfdmpmadfrrayelnvf
sffhlsqlvapemekngggviltitsmaaenkninmtsyasskaaashlvrnmafdlgek
nirvngiapgailtdalksvitpeieqkmlqhtpirrlgqpqdianaalflcspaaswvs
gqiltvsgggvqeln
>d1ahja_ 4.121.1.1.1 Nitrile hydratase alpha chain {Rhodococcus sp. r312}
enaapaqaavsdrawalfraldgkglvpdgyvegwkktfeedfsprrgaelvarawtdpe
frqllltdgtaavaqygylgpqgeyivavedtptlknvivcslcsctawpilglpptwyk
sfeyrarvvreprkvlsemgteiasdieirvydttaetrymvlpqrpagtegwsqeqlqe
ivtkdcligvaipqvptv
>d1ahjb_ 2.30.6.1.1 Nitrile hydratase beta chain {Rhodococcus sp. r312}
mdgvhdlagvqgfgkvphtvdadigptfhaewehlpyslmfagvaelgafsvdevryvve
rmeprhymmtpyyeryvigvatlmvekgiltqdeleslaggpfplsrpsesegrpapvet
ttfevgqrvrvrdeyvpghirmpaycrgrvgtishrttekwpfpdaighgrndageepty
hvkfaaeelfgsdtdggsvvvdlfegylepaa
>d1ahjc_ 4.121.1.1.1 Nitrile hydratase alpha chain {Rhodococcus sp. r312}
enaapaqaavsdrawalfraldgkglvpdgyvegwkktfeedfsprrgaelvarawtdpe
frqllltdgtaavaqygylgpqgeyivavedtptlknvivcslcsctawpilglpptwyk
sfeyrarvvreprkvlsemgteiasdieirvydttaetrymvlpqrpagtegwsqeqlqe
ivtkdcligvaipqvptv
>d1ahjd_ 2.30.6.1.1 Nitrile hydratase beta chain {Rhodococcus sp. r312}
mdgvhdlagvqgfgkvphtvdadigptfhaewehlpyslmfagvaelgafsvdevryvve
rmeprhymmtpyyeryvigvatlmvekgiltqdeleslaggpfplsrpsesegrpapvet
ttfevgqrvrvrdeyvpghirmpaycrgrvgtishrttekwpfpdaighgrndageepty
hvkfaaeelfgsdtdggsvvvdlfegylepaa
>d1ahje_ 4.121.1.1.1 Nitrile hydratase alpha chain {Rhodococcus sp. r312}
enaapaqaavsdrawalfraldgkglvpdgyvegwkktfeedfsprrgaelvarawtdpe
frqllltdgtaavaqygylgpqgeyivavedtptlknvivcslcsctawpilglpptwyk
sfeyrarvvreprkvlsemgteiasdieirvydttaetrymvlpqrpagtegwsqeqlqe
ivtkdcligvaipqvptv
>d1ahjf_ 2.30.6.1.1 Nitrile hydratase beta chain {Rhodococcus sp. r312}
mdgvhdlagvqgfgkvphtvdadigptfhaewehlpyslmfagvaelgafsvdevryvve
rmeprhymmtpyyeryvigvatlmvekgiltqdeleslaggpfplsrpsesegrpapvet
ttfevgqrvrvrdeyvpghirmpaycrgrvgtishrttekwpfpdaighgrndageepty
hvkfaaeelfgsdtdggsvvvdlfegylepaa
>d1ahjg_ 4.121.1.1.1 Nitrile hydratase alpha chain {Rhodococcus sp. r312}
enaapaqaavsdrawalfraldgkglvpdgyvegwkktfeedfsprrgaelvarawtdpe
frqllltdgtaavaqygylgpqgeyivavedtptlknvivcslcsctawpilglpptwyk
sfeyrarvvreprkvlsemgteiasdieirvydttaetrymvlpqrpagtegwsqeqlqe
ivtkdcligvaipqvptv
>d1ahjh_ 2.30.6.1.1 Nitrile hydratase beta chain {Rhodococcus sp. r312}
mdgvhdlagvqgfgkvphtvdadigptfhaewehlpyslmfagvaelgafsvdevryvve
rmeprhymmtpyyeryvigvatlmvekgiltqdeleslaggpfplsrpsesegrpapvet
ttfevgqrvrvrdeyvpghirmpaycrgrvgtishrttekwpfpdaighgrndageepty
hvkfaaeelfgsdtdggsvvvdlfegylepaa
>d1ahk__ 2.1.1.5.25 Major mite allergen {House-dust mite (Dermatophagoides farinae), Der f 2}
dqvdvkdcanneikkvmvdgchgsdpciihrgkpftlealfdanqntktakieikasldg
leidvpgidtnachfvkcplvkgqqydikytwnvpkiapksenvvvtvkligdngvlaca
iathgkird
>d1ahl__ 7.9.1.1.7 Anthopleurin-A {Giant green sea anemone (Anthopleura xanthogrammica)}
gvsclcdsdgpsvrgntlsgtlwlypsgcpsgwhnckahgptigwcckq
>d1ahm__ 2.1.1.5.25 Major mite allergen {House-dust mite (Dermatophagoides farinae), Der f 2}
dqvdvkdcanneikkvmvdgchgsdpciihrgkpftlealfdanqntktakieikasldg
leidvpgidtnachfvkcplvkgqqydikytwnvpkiapksenvvvtvkligdngvlaca
iathgkird
>d1ahn__ 3.16.4.1.4 Flavodoxin {Escherichia coli}
aitgiffgsdtgnteniakmiqkqlgkdvadvhdiaksskedleaydilllgiptwyyge
aqcdwddffptleeidfngklvalfgcgdqedyaeyfcdalgtirdiieprgativghwp
tagyhfeaskgladddhfvglaidedrqpeltaervekwvkqiseelhl
>d1aho__ 7.3.7.1.5 Scorpion toxin {Androctonus australius hector, Toxin II}
vkdgyivddvnctyfcgrnaycneectklkgesgycqwaspygnacycyklpdhvrtkgp
grch
>d1ahpa_ 3.77.1.2.3 Maltodextrin phosphorylase (MALP) {Escherichia coli}
sqpifndkqfqealsrqwqryglnsaaemtprqwwlavsealaemlraqpfakpvanqrh
vnyismefligrltgnnllnlgwyqdvqdslkaydinltdlleeeidpalgagglgrlaa
cfldsmatvgqsatgyglnyqyglfrqsfvdgkqveapddwhrsnypwfrhnealdvqvg
iggavtkdgrwepeftitgqawdlpvvgyrngvaqplrlwqathahpfdltkfndgdflr
aeqqginaekltkvlypndnhtagkklrlmqqyfqcacsvadilrrhhlagrelhelady
eviqlndthptiaipellrvlidehqmswddawaitsktfaytnhtlmpealerwdvklv
kgllprhmqiineintrfktlvektwpgdekvwaklavvhdkqvhmanlcvvggfavngv
aalhsdlvvkdlfpeyhqlwpnkfhnvtngitprrwikqcnpalaalldkslqkewandl
dqlinlvkladdakfrdlyrvikqankvrlaefvkvrtgidinpqaifdiqikrlheykr
qhlnllrilalykeirenpqadrvprvflfgakaapgyylakniifainkvadvinndpl
vgdklkvvflpdycvsaaeklipaadiseqistagkeasgtgnmklalngaltvgtldga
nveiaekvgeenififghtvkqvkailakgydpvkwrkkdkvldavlkelesgkysdgdk
hafdqmlhsigkqggdpylvmadfaayveaqkqvdvlyrdqeawtraailntarcgmfss
drsirdyqariwqaar
>d1ahpb_ 3.77.1.2.3 Maltodextrin phosphorylase (MALP) {Escherichia coli}
sqpifndkqfqealsrqwqryglnsaaemtprqwwlavsealaemlraqpfakpvanqrh
vnyismefligrltgnnllnlgwyqdvqdslkaydinltdlleeeidpalgagglgrlaa
cfldsmatvgqsatgyglnyqyglfrqsfvdgkqveapddwhrsnypwfrhnealdvqvg
iggavtkdgrwepeftitgqawdlpvvgyrngvaqplrlwqathahpfdltkfndgdflr
aeqqginaekltkvlypndnhtagkklrlmqqyfqcacsvadilrrhhlagrelhelady
eviqlndthptiaipellrvlidehqmswddawaitsktfaytnhtlmpealerwdvklv
kgllprhmqiineintrfktlvektwpgdekvwaklavvhdkqvhmanlcvvggfavngv
aalhsdlvvkdlfpeyhqlwpnkfhnvtngitprrwikqcnpalaalldkslqkewandl
dqlinlvkladdakfrdlyrvikqankvrlaefvkvrtgidinpqaifdiqikrlheykr
qhlnllrilalykeirenpqadrvprvflfgakaapgyylakniifainkvadvinndpl
vgdklkvvflpdycvsaaeklipaadiseqistagkeasgtgnmklalngaltvgtldga
nveiaekvgeenififghtvkqvkailakgydpvkwrkkdkvldavlkelesgkysdgdk
hafdqmlhsigkqggdpylvmadfaayveaqkqvdvlyrdqeawtraailntarcgmfss
drsirdyqariwqaar
>d1ahq__ 4.85.1.2.2 Actophorin {Amoeba (Acanthamoeba castellanii)}
giavsddcvqkfnelklghqhryvtfkmnasntevvvehvggpnatyedfksqlperdcr
yaifdyefqvdggqrnkitfilwapdsapikskmmytstkdsikkklvgiqvevqatdaa
eisedavserakk
>d1ahr__ 1.42.1.5.10 Calmodulin {Chicken (Gallus gallus)}
adqlteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgn
gtidfpefltmmarkmkdseeeireafrvfdkdgngfisaaelrhvmtnlgekltdeevd
emireadidgdgqvnyeefvtmmtsk
>d1ahsa_ 2.17.1.1.2 Virus coat protein vp7 (BTV-10 vp7), central (top) domain {African horse sickness virus}
tgpyagavevqqsgryyvpqgrtrggyinsniaevcmdagaagqvnallaprrgdavmiy
fvwrplrifcdpqgaslesapgtfvtvdgvnvaagdvvawntiapvnvgnpgarrsilqf
evlwyt
>d1ahsb_ 2.17.1.1.2 Virus coat protein vp7 (BTV-10 vp7), central (top) domain {African horse sickness virus}
tgpyagavevqqsgryyvpqgrtrggyinsniaevcmdagaagqvnallaprrgdavmiy
fvwrplrifcdpqgaslesapgtfvtvdgvnvaagdvvawntiapvnvgnpgarrsilqf
evlwyt
>d1ahsc_ 2.17.1.1.2 Virus coat protein vp7 (BTV-10 vp7), central (top) domain {African horse sickness virus}
tgpyagavevqqsgryyvpqgrtrggyinsniaevcmdagaagqvnallaprrgdavmiy
fvwrplrifcdpqgaslesapgtfvtvdgvnvaagdvvawntiapvnvgnpgarrsilqf
evlwyt
>e1aht.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1aht.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
eadcglrplfekksledkterellesyi
>d1ahua1 4.47.27.1.1 (274-560) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
rgyqsylitlpkdgdlkqavdiirplrlgmalqnvptirhilldaavlgdkrsyssrtep
lsdeeldkiakqlnlgrwnfygalygpepirrvlwetikdafsaipgvkfyfpedtpens
vlrvrdktmqgiptydelkwidwlpngahlffspiakvsgedammqyavtkkrcqeagld
figtftvgmremhhivcivfnkkdliqkrkvqwlmrtliddcaangwgeyrthlafmdqi
metynwnnssflrfnevlknavdpngiiapgksgvwpsqyshvtwkl
>d1ahua2 4.118.1.1.1 (6-273) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
efrpltlppklslsdfnefiqdiirivgsenvevisskdqivdgsymkpththdphhvmd
qdyflasaivaprnvadvqsivglankfsfplwpisigrnsgyggaaprvsgsvvldmgk
nmnrvlevnvegaycvvepgvtyhdlhnyleannlrdklwldvpdlgggsvlgnavergv
gytpygdhwmmhsgmevvlangellrtgmgalpdpkrpetmglkpedqpwskiahlfpyg
fgpyidglfsqsnmgivtkigiwlmpnp
>d1ahub1 4.47.27.1.1 (274-560) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
rgyqsylitlpkdgdlkqavdiirplrlgmalqnvptirhilldaavlgdkrsyssrtep
lsdeeldkiakqlnlgrwnfygalygpepirrvlwetikdafsaipgvkfyfpedtpens
vlrvrdktmqgiptydelkwidwlpngahlffspiakvsgedammqyavtkkrcqeagld
figtftvgmremhhivcivfnkkdliqkrkvqwlmrtliddcaangwgeyrthlafmdqi
metynwnnssflrfnevlknavdpngiiapgksgvwpsqyshvtwkl
>d1ahub2 4.118.1.1.1 (6-273) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
efrpltlppklslsdfnefiqdiirivgsenvevisskdqivdgsymkpththdphhvmd
qdyflasaivaprnvadvqsivglankfsfplwpisigrnsgyggaaprvsgsvvldmgk
nmnrvlevnvegaycvvepgvtyhdlhnyleannlrdklwldvpdlgggsvlgnavergv
gytpygdhwmmhsgmevvlangellrtgmgalpdpkrpetmglkpedqpwskiahlfpyg
fgpyidglfsqsnmgivtkigiwlmpnp
>d1ahva1 4.47.27.1.1 (274-560) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
rgyqsylitlpkdgdlkqavdiirplrlgmalqnvptirhilldaavlgdkrsyssrtep
lsdeeldkiakqlnlgrwnfygalygpepirrvlwetikdafsaipgvkfyfpedtpens
vlrvrdktmqgiptydelkwidwlpngahlffspiakvsgedammqyavtkkrcqeagld
figtftvgmremhhivcivfnkkdliqkrkvqwlmrtliddcaangwgeyrthlafmdqi
metynwnnssflrfnevlknavdpngiiapgksgvwpsqyshvtwkl
>d1ahva2 4.118.1.1.1 (6-273) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
efrpltlppklslsdfnefiqdiirivgsenvevisskdqivdgsymkpththdphhvmd
qdyflasaivaprnvadvqsivglankfsfplwpisigrnsgyggaaprvsgsvvldmgk
nmnrvlevnvegaycvvepgvtyhdlhnyleannlrdklwldvpdlgggsvlgnavergv
gytpygdhwmmhsgmevvlangellrtgmgalpdpkrpetmglkpedqpwskiahlfpyg
fgpyidglfsqsnmgivtkigiwlmpnp
>d1ahvb1 4.47.27.1.1 (274-560) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
rgyqsylitlpkdgdlkqavdiirplrlgmalqnvptirhilldaavlgdkrsyssrtep
lsdeeldkiakqlnlgrwnfygalygpepirrvlwetikdafsaipgvkfyfpedtpens
vlrvrdktmqgiptydelkwidwlpngahlffspiakvsgedammqyavtkkrcqeagld
figtftvgmremhhivcivfnkkdliqkrkvqwlmrtliddcaangwgeyrthlafmdqi
metynwnnssflrfnevlknavdpngiiapgksgvwpsqyshvtwkl
>d1ahvb2 4.118.1.1.1 (6-273) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
efrpltlppklslsdfnefiqdiirivgsenvevisskdqivdgsymkpththdphhvmd
qdyflasaivaprnvadvqsivglankfsfplwpisigrnsgyggaaprvsgsvvldmgk
nmnrvlevnvegaycvvepgvtyhdlhnyleannlrdklwldvpdlgggsvlgnavergv
gytpygdhwmmhsgmevvlangellrtgmgalpdpkrpetmglkpedqpwskiahlfpyg
fgpyidglfsqsnmgivtkigiwlmpnp
>d1ahwa1 2.1.1.1.99 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
dikmtqspssmyaslgervtitckasqdirkylnwyqqkpwkspktliyyatsladgvps
rfsgsgsgqdysltisslesddtatyyclqhgespytfgggtkleinr
>d1ahwa2 2.1.1.2.100 (109-214) Immunoglobulin (constant domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1ahwb1 2.1.1.1.99 (1-117) Immunoglobulin (variable domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
eiqlqqsgaelvrpgalvklsckasgfnikdyymhwvkqrpeqglewiglidpengntiy
dpkfqgkasitadtssntaylqlssltsedtavyycardnsyyfdywgqgttltvss
>d1ahwb2 2.1.1.2.100 (118-214) Immunoglobulin (constant domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpsstwpsetvtcnvahpasstkvdkki
>d1ahwc1 2.1.2.1.1 (4-106) Extracellular region of human tissue factor {Human (Homo sapiens)}
tntvaaynltwkstnfktilewepkpvnqvytvqistksgdwkskcfyttdtecdltdei
vkdvkqtylarvfsypagnvestgsageplyenspeftpylet
>d1ahwc2 2.1.2.1.1 (107-211) Extracellular region of human tissue factor {Human (Homo sapiens)}
nlgqptiqsfeqvgtkvnvtvedertlvrrnntflslrdvfgkdliytlyywkssssgkk
taktntneflidvdkgenycfsvqavipsrtvnrkstdspvecmg
>d1ahwd1 2.1.1.1.99 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
dikmtqspssmyaslgervtitckasqdirkylnwyqqkpwkspktliyyatsladgvps
rfsgsgsgqdysltisslesddtatyyclqhgespytfgggtkleinr
>d1ahwd2 2.1.1.2.100 (109-214) Immunoglobulin (constant domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1ahwe1 2.1.1.1.99 (1-117) Immunoglobulin (variable domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
eiqlqqsgaelvrpgalvklsckasgfnikdyymhwvkqrpeqglewiglidpengntiy
dpkfqgkasitadtssntaylqlssltsedtavyycardnsyyfdywgqgttltvss
>d1ahwe2 2.1.1.2.100 (118-214) Immunoglobulin (constant domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpsstwpsetvtcnvahpasstkvdkki
>d1ahwf1 2.1.2.1.1 (4-106) Extracellular region of human tissue factor {Human (Homo sapiens)}
tntvaaynltwkstnfktilewepkpvnqvytvqistksgdwkskcfyttdtecdltdei
vkdvkqtylarvfsypagnvestgsageplyenspeftpylet
>d1ahwf2 2.1.2.1.1 (107-211) Extracellular region of human tissue factor {Human (Homo sapiens)}
nlgqptiqsfeqvgtkvnvtvedertlvrrnntflslrdvfgkdliytlyywkssssgkk
taktntneflidvdkgenycfsvqavipsrtvnrkstdspvecmg
>d1ahxa_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgiglyydetgkipvltsvkkaeqyllene
ttklylgidgipefgrctqellfgkgsalindkrartaqtpggsgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanyssppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ahxb_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgiglyydetgkipvltsvkkaeqyllene
ttklylgidgipefgrctqellfgkgsalindkrartaqtpggsgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanyssppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ahya_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgiglyydetgkipvltsvkkaeqyllene
ttklylgidgipefgrctqellfgkgsalindkrartaqtpggsgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanyssppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ahyb_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgiglyydetgkipvltsvkkaeqyllene
ttklylgidgipefgrctqellfgkgsalindkrartaqtpggsgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanyssppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ahza1 4.47.27.1.1 (274-560) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
rgyqsylitlpkdgdlkqavdiirplrlgmalqnvptirhilldaavlgdkrsyssrtep
lsdeeldkiakqlnlgrwnfygalygpepirrvlwetikdafsaipgvkfyfpedtpens
vlrvrdktmqgiptydelkwidwlpngahlffspiakvsgedammqyavtkkrcqeagld
figtftvgmremhhivcivfnkkdliqkrkvqwlmrtliddcaangwgeyrthlafmdqi
metynwnnssflrfnevlknavdpngiiapgksgvwpsqyshvtwkl
>d1ahza2 4.118.1.1.1 (6-273) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
efrpltlppklslsdfnefiqdiirivgsenvevisskdqivdgsymkpththdphhvmd
qdyflasaivaprnvadvqsivglankfsfplwpisigrnsgyggaaprvsgsvvldmgk
nmnrvlevnvegaycvvepgvtyhdlhnyleannlrdklwldvpdlgggsvlgnavergv
gytpygdhwmmhsgmevvlangellrtgmgalpdpkrpetmglkpedqpwskiahlfpyg
fgpyidglfsqsnmgivtkigiwlmpnp
>d1ahzb1 4.47.27.1.1 (274-560) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
rgyqsylitlpkdgdlkqavdiirplrlgmalqnvptirhilldaavlgdkrsyssrtep
lsdeeldkiakqlnlgrwnfygalygpepirrvlwetikdafsaipgvkfyfpedtpens
vlrvrdktmqgiptydelkwidwlpngahlffspiakvsgedammqyavtkkrcqeagld
figtftvgmremhhivcivfnkkdliqkrkvqwlmrtliddcaangwgeyrthlafmdqi
metynwnnssflrfnevlknavdpngiiapgksgvwpsqyshvtwkl
>d1ahzb2 4.118.1.1.1 (6-273) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
efrpltlppklslsdfnefiqdiirivgsenvevisskdqivdgsymkpththdphhvmd
qdyflasaivaprnvadvqsivglankfsfplwpisigrnsgyggaaprvsgsvvldmgk
nmnrvlevnvegaycvvepgvtyhdlhnyleannlrdklwldvpdlgggsvlgnavergv
gytpygdhwmmhsgmevvlangellrtgmgalpdpkrpetmglkpedqpwskiahlfpyg
fgpyidglfsqsnmgivtkigiwlmpnp
>e1ai0.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1ai0.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1ai0.2c 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1ai0.2d 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1ai0.3e 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1ai0.3f 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1ai0.4g 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1ai0.4h 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1ai0.5i 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1ai0.5j 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1ai0.6k 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1ai0.6l 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>d1ai1h1 2.1.1.1.31 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab 59.1 (mouse), kappa L chain}
qvklqesgpavikpsqslsltcivsgfsitrtnycwhwirqapgkglewmgricyegsiy
yspsiksrstisrdtslnkffiqlisvtnedtamyycsrenhmyetyfdvwgqgttvtvs
>d1ai1h2 2.1.1.2.40 (113-226) Immunoglobulin (constant domains of L and H chains) {Fab 59.1 (mouse), kappa L chain}
sakttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqs
dlytlsssvtvpssprpsetvtcnvahpasstkvdkkivpr
>d1ai1l1 2.1.1.1.31 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab 59.1 (mouse), kappa L chain}
divmtqspaslvvslgqratiscrasesvdsygksfmhwyqqkpgqppkvliyiasnles
gvparfsgsgsrtdftltidpveaddaatyycqqnnedpptfgagtklemrr
>d1ai1l2 2.1.1.2.40 (109-211) Immunoglobulin (constant domains of L and H chains) {Fab 59.1 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1ai2__ 3.65.1.1.7 Isocitrate dehydrogenase, ICDH {Escherichia coli}
skvvvpaqgkkitlqngklnvpenpiipyiegdgigvdvtpamlkvvdaavekaykgerk
iswmeiytgekstqvygqdvwlpaetldlireyrvaikgplttpvgggirslnvalrqel
dlyiclrpvryyqgtpspvkhpeltdmvifrensediyagiewkadsadaekvikflree
mgvkkirfpehcgigikpcseegtkrlvraaieyaiandrdsvtlvhkgnimkftegafk
dwgyqlareefggelidggpwlkvknpntgkeivikdviadaflqqillrpaeydviacm
nlngdyisdalaaqvggigiapganigdecalfeathgtapkyagqdkvnpgsiilsaem
mlrhmgwteaadlivkgmegainaktvtydferlmdgakllkcsefgdaiienm
>d1ai3__ 3.65.1.1.7 Isocitrate dehydrogenase, ICDH {Escherichia coli}
skvvvpaqgkkitlqngklnvpenpiipyiegdgigvdvtpamlkvvdaavekaykgerk
iswmeiytgekstqvygqdvwlpaetldlireyrvaikgplttpvgggirslnvalrqel
dlyiclrpvryyqgtpspvkhpeltdmvifrensediyagiewkadsadaekvikflree
mgvkkirfpehcgigikpcseegtkrlvraaieyaiandrdsvtlvhkgnimkftegafk
dwgyqlareefggelidggpwlkvknpntgkeivikdviadaflqqillrpaeydviacm
nlngdyisdalaaqvggigiapganigdecalfeathgtapkyagqdkvnpgsiilsaem
mlrhmgwteaadlivkgmegainaktvtydferlmdgakllkcsefgdaiienm
>e1ai4.1a 4.124.1.2.1 Penicillin acylase, catalytic domain {Escherichia coli}
ssseikivrdeygmphiyandtwhlfygygyvvaqdrlfqmemarrstqgtvaevlgkdf
vkfdkdirrnywpdairaqiaalspedmsilqgyadgmnawidkvntnpetllpkqfntf
gftpkrwepfdvamifvgtmanrfsdstseidnlalltalkdkygvsqgmavfnqlkwlv
npsapttiavqesnyplkfnqqnsqt
>e1ai4.1b 4.124.1.2.1 Penicillin acylase, catalytic domain {Escherichia coli}
snmwvigkskaqdakaimvngpqfgwyapaytygiglhgagydvtgntpfaypglvfghn
gviswgstagfgddvdifaerlsaekpgyylhngkwvkmlsreetitvkngqaetftvwr
tvhgnilqtdqttqtayaksrawdgkevasllawthqmkaknwqqwtqqaakqaltinwy
yadvngnigyvhtgaypdrqsghdprlpvpgtgkwdwkgllpfemnpkvynpqsgyianw
nnspqkdypasdlfaflwggadrvteidrlleqkprltadqawdvirqtsrqdlnlrlfl
ptlqaatsgltqsdprrqlvetltrwdginllnddgktwqqpgsailnvwltsmlkrtvv
aavpmpfdkwysasgyettqdgptgslnisvgakilyeavqgdkspipqavdlfagkpqq
evvlaaledtwetlskrygnnvsnwktpamaltfrannffgvpqaaaeetrhqaeyqnrg
tendmivfspttsdrpvlawdvvapgqsgfiapdgtvdkhyedqlkmyenfgrkslwltk
qdveahkesqevlhvqr
>e1ai5.1a 4.124.1.2.1 Penicillin acylase, catalytic domain {Escherichia coli}
ssseikivrdeygmphiyandtwhlfygygyvvaqdrlfqmemarrstqgtvaevlgkdf
vkfdkdirrnywpdairaqiaalspedmsilqgyadgmnawidkvntnpetllpkqfntf
gftpkrwepfdvamifvgtmanrfsdstseidnlalltalkdkygvsqgmavfnqlkwlv
npsapttiavqesnyplkfnqqnsqt
>e1ai5.1b 4.124.1.2.1 Penicillin acylase, catalytic domain {Escherichia coli}
snmwvigkskaqdakaimvngpqfgwyapaytygiglhgagydvtgntpfaypglvfghn
gviswgstagfgddvdifaerlsaekpgyylhngkwvkmlsreetitvkngqaetftvwr
tvhgnilqtdqttqtayaksrawdgkevasllawthqmkaknwqqwtqqaakqaltinwy
yadvngnigyvhtgaypdrqsghdprlpvpgtgkwdwkgllpfemnpkvynpqsgyianw
nnspqkdypasdlfaflwggadrvteidrlleqkprltadqawdvirqtsrqdlnlrlfl
ptlqaatsgltqsdprrqlvetltrwdginllnddgktwqqpgsailnvwltsmlkrtvv
aavpmpfdkwysasgyettqdgptgslnisvgakilyeavqgdkspipqavdlfagkpqq
evvlaaledtwetlskrygnnvsnwktpamaltfrannffgvpqaaaeetrhqaeyqnrg
tendmivfspttsdrpvlawdvvapgqsgfiapdgtvdkhyedqlkmyenfgrkslwltk
qdveahkesqevlhvqr
>e1ai6.1a 4.124.1.2.1 Penicillin acylase, catalytic domain {Escherichia coli}
ssseikivrdeygmphiyandtwhlfygygyvvaqdrlfqmemarrstqgtvaevlgkdf
vkfdkdirrnywpdairaqiaalspedmsilqgyadgmnawidkvntnpetllpkqfntf
gftpkrwepfdvamifvgtmanrfsdstseidnlalltalkdkygvsqgmavfnqlkwlv
npsapttiavqesny
>e1ai6.1b 4.124.1.2.1 Penicillin acylase, catalytic domain {Escherichia coli}
snmwvigkskaqdakaimvngpqfgwyapaytygiglhgagydvtgntpfaypglvfghn
gviswgstagfgddvdifaerlsaekpgyylhngkwvkmlsreetitvkngqaetftvwr
tvhgnilqtdqttqtayaksrawdgkevasllawthqmkaknwqqwtqqaakqaltinwy
yadvngnigyvhtgaypdrqsghdprlpvpgtgkwdwkgllpfemnpkvynpqsgyianw
nnspqkdypasdlfaflwggadrvteidrlleqkprltadqawdvirqtsrqdlnlrlfl
ptlqaatsgltqsdprrqlvetltrwdginllnddgktwqqpgsailnvwltsmlkrtvv
aavpmpfdkwysasgyettqdgptgslnisvgakilyeavqgdkspipqavdlfagkpqq
evvlaaledtwetlskrygnnvsnwktpamaltfrannffgvpqaaaeetrhqaeyqnrg
tendmivfspttsdrpvlawdvvapgqsgfiapdgtvdkhyedqlkmyenfgrkslwltk
qdveahkesqevlhvqr
>e1ai7.1a 4.124.1.2.1 Penicillin acylase, catalytic domain {Escherichia coli}
ssseikivrdeygmphiyandtwhlfygygyvvaqdrlfqmemarrstqgtvaevlgkdf
vkfdkdirrnywpdairaqiaalspedmsilqgyadgmnawidkvntnpetllpkqfntf
gftpkrwepfdvamifvgtmanrfsdstseidnlalltalkdkygvsqgmavfnqlkwlv
npsapttiavqesnyplkfnqqnsqt
>e1ai7.1b 4.124.1.2.1 Penicillin acylase, catalytic domain {Escherichia coli}
snmwvigkskaqdakaimvngpqfgwyapaytygiglhgagydvtgntpfaypglvfghn
gviswgstagfgddvdifaerlsaekpgyylhngkwvkmlsreetitvkngqaetftvwr
tvhgnilqtdqttqtayaksrawdgkevasllawthqmkaknwqqwtqqaakqaltinwy
yadvngnigyvhtgaypdrqsghdprlpvpgtgkwdwkgllpfemnpkvynpqsgyianw
nnspqkdypasdlfaflwggadrvteidrlleqkprltadqawdvirqtsrqdlnlrlfl
ptlqaatsgltqsdprrqlvetltrwdginllnddgktwqqpgsailnvwltsmlkrtvv
aavpmpfdkwysasgyettqdgptgslnisvgakilyeavqgdkspipqavdlfagkpqq
evvlaaledtwetlskrygnnvsnwktpamaltfrannffgvpqaaaeetrhqaeyqnrg
tendmivfspttsdrpvlawdvvapgqsgfiapdgtvdkhyedqlkmyenfgrkslwltk
qdveahkesqevlhvqr
>e1ai8.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqf
>e1ai8.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>d1ai9a_ 3.61.1.1.7 Dihydrofolate reductases, eukaryotic type {Yeast (Candida albicans)}
mlkpnvaiivaalkpalgigykgkmpwrlrkeiryfkdvttrttkpntrnavimgrktwe
sipqkfrplpdrlniilsrsyeneiiddniihassiesslnlvsdvervfiiggaeiyne
linnslvshlliteiehpspesiemdtflkfpleswtkqpkselqkfvgdtvleddikeg
dftynytlwtrk
>d1ai9b_ 3.61.1.1.7 Dihydrofolate reductases, eukaryotic type {Yeast (Candida albicans)}
mlkpnvaiivaalkpalgigykgkmpwrlrkeiryfkdvttrttkpntrnavimgrktwe
sipqkfrplpdrlniilsrsyeneiiddniihassiesslnlvsdvervfiiggaeiyne
linnslvshlliteiehpspesiemdtflkfpleswtkqpkselqkfvgdtvleddikeg
dftynytlwtrk
>d1aiaa_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assyshnfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aiab_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assyshnfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aiba_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assyshnfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aibb_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assyshnfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aica_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assyshnfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aicb_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assyshnfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aida_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtiriggqlkealldtgaddtvleemnlpgkwkpkmiggiggfikvrqyd
qipveicghkaigtvlvgptpvniigrnlltqigctlnf
>d1aidb_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtiriggqlkealldtgaddtvleemnlpgkwkpkmiggiggfikvrqyd
qipveicghkaigtvlvgptpvniigrnlltqigctlnf
>d1aie__ 1.55.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
eyftlqirgrerfemfrelnealelkdaqag
>d1aifa1 2.1.1.1.66 (1-109) Immunoglobulin (variable domains of L and H chains) {Fab 409.5.3 (mouse), kappa L chain}
diqltqspafmaaspgekvtitcsvsssisssnlhwyqqksetspkpwiygtsnlasgvp
vrfsgsgsgtsysltissmeaedaatyycqqwnsypytfgggtkleikr
>d1aifa2 2.1.1.2.71 (110-215) Immunoglobulin (constant domains of L and H chains) {Fab 409.5.3 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1aifb1 2.1.1.1.66 (1-121) Immunoglobulin (variable domains of L and H chains) {Fab 409.5.3 (mouse), kappa L chain}
evklqesggglvqpggsmklscvasgftfnnywmswvrqspekglewvaeirlnsdnfat
hyaesvkgkfiisrddsksrlylqmnslraedtgiyycvlrplfyyavdywgqgtsvtvs
s
>d1aifb2 2.1.1.2.71 (122-218) Immunoglobulin (constant domains of L and H chains) {Fab 409.5.3 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpstwrpsetvtcnvahpasstkvdkki
>d1aifh1 2.1.1.1.66 (1-121) Immunoglobulin (variable domains of L and H chains) {Fab 409.5.3 (mouse), kappa L chain}
evklqesggglvqpggsmklscvasgftfnnywmswvrqspekglewvaeirlnsdnfat
hyaesvkgkfiisrddsksrlylqmnslraedtgiyycvlrplfyyavdywgqgtsvtvs
s
>d1aifh2 2.1.1.2.71 (122-218) Immunoglobulin (constant domains of L and H chains) {Fab 409.5.3 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpstwrpsetvtcnvahpasstkvdkki
>d1aifl1 2.1.1.1.66 (1-109) Immunoglobulin (variable domains of L and H chains) {Fab 409.5.3 (mouse), kappa L chain}
diqltqspafmaaspgekvtitcsvsssisssnlhwyqqksetspkpwiygtsnlasgvp
vrfsgsgsgtsysltissmeaedaatyycqqwnsypytfgggtkleikr
>d1aifl2 2.1.1.2.71 (110-215) Immunoglobulin (constant domains of L and H chains) {Fab 409.5.3 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1aigh1 2.36.1.1.2 (36-258) Photosynthetic reaction centre {Rhodobacter sphaeroides}
mregyplenedgtpaanqgpfplpkpktfilphgrgtltvpgpesedrpialartavseg
fphaptgdpmkdgvgpaswvarrdlpeldghghnkikpmkaaagfhvsagknpiglpvrg
cdleiagkvvdiwvdipeqmarflevelkdgstrllpmqmvkvqsnrvhvnalssdlfag
iptiksptevtlleedkicgyvagglmyaapkrksvvaamlae
>d1aigh2 6.2.1.1.4 (11-35) Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
dlaslaiysfwiflagliyylqten
>d1aigl1 6.2.1.1.4 Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
allsferkyrvpggtlvggnlfdfwvgpfyvgffgvatfffaalgiiliawsavlqgtwn
pqlisvyppaleyglggaplakgglwqiiticatgafvswalreveicrklgigyhipfa
fafailayltlvlfrpvmmgawgyafpygiwthldwvsntgytygnfhynpahmiaisff
ftnalalalhgalvlsaanpekgkemrtpdhedtffrdlvgysigtlgihrlglllslsa
vffsalcmiitgtiwfdqwvdwwqwwvklpwwanipgging
>d1aigm1 6.2.1.1.4 Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
yqnifsqvqvrgpadlgmtedvnlanrsgvgpfstllgwfgnaqlgpiylgslgvlslfs
glmwfftigiwfwyqagwnpavflrdlfffsleppapeyglsfaaplkegglwliasffm
fvavwswwgrtylraqalgmgkhtawaflsaiwlwmvlgfirpilmgswseavpygifsh
ldwtnnfslvhgnlfynpfhglsiaflygsallfamhgatilavsrfggereleqiadrg
taaeraalfwrwtmgfnatmegihrwaiwmavlvtltggigillsgtvvdnwyvwgqnh
>d1aign1 6.2.1.1.4 Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
allsferkyrvpggtlvggnlfdfwvgpfyvgffgvatfffaalgiiliawsavlqgtwn
pqlisvyppaleyglggaplakgglwqiiticatgafvswalreveicrklgigyhipfa
fafailayltlvlfrpvmmgawgyafpygiwthldwvsntgytygnfhynpahmiaisff
ftnalalalhgalvlsaanpekgkemrtpdhedtffrdlvgysigtlgihrlglllslsa
vffsalcmiitgtiwfdqwvdwwqwwvklpwwanipgging
>d1aigo1 6.2.1.1.4 Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
yqnifsqvqvrgpadlgmtedvnlanrsgvgpfstllgwfgnaqlgpiylgslgvlslfs
glmwfftigiwfwyqagwnpavflrdlfffsleppapeyglsfaaplkegglwliasffm
fvavwswwgrtylraqalgmgkhtawaflsaiwlwmvlgfirpilmgswseavpygifsh
ldwtnnfslvhgnlfynpfhglsiaflygsallfamhgatilavsrfggereleqiadrg
taaeraalfwrwtmgfnatmegihrwaiwmavlvtltggigillsgtvvdnwyvwgqnh
>d1aigp1 2.36.1.1.2 (36-258) Photosynthetic reaction centre {Rhodobacter sphaeroides}
mregyplenedgtpaanqgpfplpkpktfilphgrgtltvpgpesedrpialartavseg
fphaptgdpmkdgvgpaswvarrdlpeldghghnkikpmkaaagfhvsagknpiglpvrg
cdleiagkvvdiwvdipeqmarflevelkdgstrllpmqmvkvqsnrvhvnalssdlfag
iptiksptevtlleedkicgyvagglmyaapkrksvvaamlae
>d1aigp2 6.2.1.1.4 (11-35) Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
dlaslaiysfwiflagliyylqten
>d1aiha_ 4.133.1.1.1 Integrase {Bacteriophage HP1}
etelaflyerdiyrllaecdnsrnpdlglivriclatgarwseaetltqsqvmpykitft
ntkskknrtvpisdelfdmlpkkrgrlfndayesfenavlraeielpkgqlthvlrhtfa
shfmmnggnilvlkeilghstiemtmryahfapshlesavkfnplsnpaq
>d1aihb_ 4.133.1.1.1 Integrase {Bacteriophage HP1}
elaflyerdiyrllaecdnsrnpdlglivriclatgarwseaetltqsqvmpykitftnt
kskknrtvpisdelfdmlpkkrgrlfndayesfenavlraeielpkgqlthvlrhtfash
fmmnggnilvlkeilghstiemtmryahfapshlesavkfnplsnpaq
>d1aihc_ 4.133.1.1.1 Integrase {Bacteriophage HP1}
elaflyerdiyrllaecdnsrnpdlglivriclatgarwseaetltqsqvmpykitftnt
kskknrtvpisdelfdmlpkkrgrlfndayesfenavlraeielpkgqlthvlrhtfash
fmmnggnilvlkeilghstiemtmryahfapshlesavkfnplsnpaq
>d1aihd_ 4.133.1.1.1 Integrase {Bacteriophage HP1}
etelaflyerdiyrllaecdnsrnpdlglivriclatgarwseaetltqsqvmpykitft
ntkskknrtvpisdelfdmlpkkrgrlfndayesfenavlraeielpkgqlthvlrhtfa
shfmmnggnilvlkeilghstiemtmryahfapshlesavkfnplsnpaq
>d1aii__ 1.66.1.1.2 Annexin III {Human (Homo sapiens)}
asiwvghrgtvrdypdfspsvdaeaiqkairgigtdekmlisiltersnaqrqlivkeyq
aaygkelkddlkgdlsghfehlmvalvtppavfdakqlkksmkgagtnedalieilttrt
srqmkdisqayytvykkslgddissetsgdfrkalltladgrrdeslkvdehlakqdaqi
lykagenrwgtdedkfteilclrsfpqlkltfdeyrnisqkdivdsikgelsghfedlll
aivncvrntpaflaerlhralkgigtdeftlnrimvsrseidlldirtefkkhygyslys
aiksdtsgdyeitllkicggdd
>d1aijh1 2.36.1.1.2 (36-256) Photosynthetic reaction centre {Rhodobacter sphaeroides}
mregyplenedgtpaanqgpfplpkpktfilphgrgtltvpgpesedrpialartavseg
fphaptgdpmkdgvgpaswvarrdlpeldghghnkikpmkaaagfhvsagknpiglpvrg
cdleiagkvvdiwvdipeqmarflevelkdgstrllpmqmvkvqsnrvhvnalssdlfag
iptiksptevtlleedkicgyvagglmyaapkrksvvaaml
>d1aijh2 6.2.1.1.4 (11-35) Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
dlaslaiysfwiflagliyylqten
>d1aijl1 6.2.1.1.4 Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
allsferkyrvpggtlvggnlfdfwvgpfyvgffgvatfffaalgiiliawsavlqgtwn
pqlisvyppaleyglggaplakgglwqiiticatgafvswalreveicrklgigyhipfa
fafailayltlvlfrpvmmgawgyafpygiwthldwvsntgytygnfhynpahmiaisff
ftnalalalhgalvlsaanpekgkemrtpdhedtffrdlvgysigtlgihrlglllslsa
vffsalcmiitgtiwfdqwvdwwqwwvklpwwanipgging
>d1aijm1 6.2.1.1.4 Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
aeyqnifsqvqvrgpadlgmtedvnlanrsgvgpfstllgwfgnaqlgpiylgslgvlsl
fsglmwfftigiwfwyqagwnpavflrdlfffsleppapeyglsfaaplkegglwliasf
fmfvavwswwgrtylraqalgmgkhtawaflsaiwlwmvlgfirpilmgswseavpygif
shldwtnnfslvhgnlfynpfhglsiaflygsallfamhgatilavsrfggereleqiad
rgtaaeraalfwrwtmgfnatmegihrwaiwmavlvtltggigillsgtvvdnwyvwgqn
h
>d1aijr1 6.2.1.1.4 Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
allsferkyrvpggtlvggnlfdfwvgpfyvgffgvatfffaalgiiliawsavlqgtwn
pqlisvyppaleyglggaplakgglwqiiticatgafvswalreveicrklgigyhipfa
fafailayltlvlfrpvmmgawgyafpygiwthldwvsntgytygnfhynpahmiaisff
ftnalalalhgalvlsaanpekgkemrtpdhedtffrdlvgysigtlgihrlglllslsa
vffsalcmiitgtiwfdqwvdwwqwwvklpwwanipgging
>d1aijs1 6.2.1.1.4 Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
yqnifsqvqvrgpadlgmtedvnlanrsgvgpfstllgwfgnaqlgpiylgslgvlslfs
glmwfftigiwfwyqagwnpavflrdlfffsleppapeyglsfaaplkegglwliasffm
fvavwswwgrtylraqalgmgkhtawaflsaiwlwmvlgfirpilmgswseavpygifsh
ldwtnnfslvhgnlfynpfhglsiaflygsallfamhgatilavsrfggereleqiadrg
taaeraalfwrwtmgfnatmegihrwaiwmavlvtltggigillsgtvvdnwyvwgqnh
>d1aijt1 2.36.1.1.2 (36-256) Photosynthetic reaction centre {Rhodobacter sphaeroides}
mregyplenedgtpaanqgpfplpkpktfilphgrgtltvpgpesedrpialartavseg
fphaptgdpmkdgvgpaswvarrdlpeldghghnkikpmkaaagfhvsagknpiglpvrg
cdleiagkvvdiwvdipeqmarflevelkdgstrllpmqmvkvqsnrvhvnalssdlfag
iptiksptevtlleedkicgyvagglmyaapkrksvvaaml
>d1aijt2 6.2.1.1.4 (11-35) Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
dlaslaiysfwiflagliyylqten
>d1ail__ 1.16.1.1.1 N-terminal, RNA-binding domain of nonstructural protein NS1 {Influenza virus A}
mdsntvssfqvdcflwhvrkqvvdqelgdapfldrlrrdqkslrgrgstlglnieaathv
gkqivekilk
>d1aim__ 4.3.1.1.9 Cruzain {Trypanosoma cruzi}
apaavdwrargavtavkdqgqcgscwafsaignvecqwflaghpltnlseqmlvscdktd
sgcsgglmnnafewivqenngavytedsypyasgegisppcttsghtvgatitghvelpq
deaqiaawlavngpvavavdasswmtytggvmtscvsealdhgvllvgyndsaavpywii
knswttqwgeegyiriakgsnqclvkeeassavvg
>d1ain__ 1.66.1.1.1 Annexin I {Human (Homo sapiens)}
gsavspyptfnpssdvaalhkaimvkgvdeatiidiltkrnnaqrqqikaaylqetgkpl
detlkkaltghleevvlallktpaqfdadelraamkglgtdedtlieilasrtnkeirdi
nrvyreelkrdlakditsdtsgdfrnallslakgdrsedfgvnedladsdaralyeager
rkgtdvnvfntilttrsypqlrrvfqkytkyskhdmnkvldlelkgdiekcltaivkcat
skpaffaeklhqamkgvgtrhkalirimvsrseidmndikafyqkmygislcqaildetk
gdyekilvalcggn
>d1aipa1 2.38.3.1.3 (213-312) Elongation factor Tu (EF-Tu), domain 2 {Thermus thermophilus}
pvrdvdkpflmpvedvftitgrgtvatgriergkvkvgdeveivglapetrrtvvtgvem
hrktlqegiagdnvgvllrgvsreevergqvlakpgsitp
>d1aipa2 2.39.1.1.3 (313-405) Elongation factor Tu (EF-Tu), C-terminal domain {Thermus thermophilus}
htkfeasvyvlkkeeggrhtgffsgyrpqfyfrttdvtgvvqlppgvemvmpgdnvtftv
elikpvaleeglrfaireggrtvgagvvtk
>d1aipa3 3.30.1.6.16 (9-212) Elongation factor Tu (EF-Tu), N-terminal (G) domain {Thermus thermophilus}
kphvnvgtighvdhgkttltaaltyvtaaenpnvevkdygdidkapeerargitintahv
eyetakrhyshvdcpghadyiknmitgaaqmdgailvvsaadgpmpqtrehillarqvgv
pyivvfmnkvdmvddpelldlvemevrdllnqyefpgdevpvirgsallaleqmhrnpkt
rrgenewvdkiwelldaideyipt
>d1aipb1 2.38.3.1.3 (213-312) Elongation factor Tu (EF-Tu), domain 2 {Thermus thermophilus}
pvrdvdkpflmpvedvftitgrgtvatgriergkvkvgdeveivglapetrrtvvtgvem
hrktlqegiagdnvgvllrgvsreevergqvlakpgsitp
>d1aipb2 2.39.1.1.3 (313-405) Elongation factor Tu (EF-Tu), C-terminal domain {Thermus thermophilus}
htkfeasvyvlkkeeggrhtgffsgyrpqfyfrttdvtgvvqlppgvemvmpgdnvtftv
elikpvaleeglrfaireggrtvgagvvtk
>d1aipb3 3.30.1.6.16 (9-212) Elongation factor Tu (EF-Tu), N-terminal (G) domain {Thermus thermophilus}
kphvnvgtighvdhgkttltaaltyvtaaenpnvevkdygdidkapeerargitintahv
eyetakrhyshvdcpghadyiknmitgaaqmdgailvvsaadgpmpqtrehillarqvgv
pyivvfmnkvdmvddpelldlvemevrdllnqyefpgdevpvirgsallaleqmhrnpkt
rrgenewvdkiwelldaideyipt
>d1aipc_ 4.36.1.1.2 Elongation factor Ts (EF-Ts), dimerisation domain {Thermus thermophilus}
sqmelikklreatgagmmdvkraledagwdeekavqllrergamkaakkadrearegiig
hyihhnqrvgvlvelncetdfvarnelfqnlakdlamhiammnpryvsaeeipaeeleke
rqiyiqaalnegkpqqiaekiaegrlkkyleevvlleqpfvkddkvkvkeliqqaiakig
enivvrrfcrfelga
>d1aipd_ 4.36.1.1.2 Elongation factor Ts (EF-Ts), dimerisation domain {Thermus thermophilus}
sqmelikklreatgagmmdvkraledagwdeekavqllrergamkaakkadrearegiig
hyihhnqrvgvlvelncetdfvarnelfqnlakdlamhiammnpryvsaeeipaeeleke
rqiyiqaalnegkpqqiaekiaegrlkkyleevvlleqpfvkddkvkvkeliqqaiakig
enivvrrfcrfelga
>d1aipe1 2.38.3.1.3 (213-312) Elongation factor Tu (EF-Tu), domain 2 {Thermus thermophilus}
pvrdvdkpflmpvedvftitgrgtvatgriergkvkvgdeveivglapetrrtvvtgvem
hrktlqegiagdnvgvllrgvsreevergqvlakpgsitp
>d1aipe2 2.39.1.1.3 (313-405) Elongation factor Tu (EF-Tu), C-terminal domain {Thermus thermophilus}
htkfeasvyvlkkeeggrhtgffsgyrpqfyfrttdvtgvvqlppgvemvmpgdnvtftv
elikpvaleeglrfaireggrtvgagvvtkile
>d1aipe3 3.30.1.6.16 (9-212) Elongation factor Tu (EF-Tu), N-terminal (G) domain {Thermus thermophilus}
kphvnvgtighvdhgkttltaaltyvtaaenpnvevkdygdidkapeerargitintahv
eyetakrhyshvdcpghadyiknmitgaaqmdgailvvsaadgpmpqtrehillarqvgv
pyivvfmnkvdmvddpelldlvemevrdllnqyefpgdevpvirgsallaleqmhrnpkt
rrgenewvdkiwelldaideyipt
>d1aipf1 2.38.3.1.3 (213-312) Elongation factor Tu (EF-Tu), domain 2 {Thermus thermophilus}
pvrdvdkpflmpvedvftitgrgtvatgriergkvkvgdeveivglapetrrtvvtgvem
hrktlqegiagdnvgvllrgvsreevergqvlakpgsitp
>d1aipf2 2.39.1.1.3 (313-405) Elongation factor Tu (EF-Tu), C-terminal domain {Thermus thermophilus}
htkfeasvyvlkkeeggrhtgffsgyrpqfyfrttdvtgvvqlppgvemvmpgdnvtftv
elikpvaleeglrfaireggrtvgagvvtkile
>d1aipf3 3.30.1.6.16 (9-212) Elongation factor Tu (EF-Tu), N-terminal (G) domain {Thermus thermophilus}
kphvnvgtighvdhgkttltaaltyvtaaenpnvevkdygdidkapeerargitintahv
eyetakrhyshvdcpghadyiknmitgaaqmdgailvvsaadgpmpqtrehillarqvgv
pyivvfmnkvdmvddpelldlvemevrdllnqyefpgdevpvirgsallaleqmhrnpkt
rrgenewvdkiwelldaideyipt
>d1aipg_ 4.36.1.1.2 Elongation factor Ts (EF-Ts), dimerisation domain {Thermus thermophilus}
sqmelikklreatgagmmdvkraledagwdeekavqllrergamkaakkadrearegiig
hyihhnqrvgvlvelncetdfvarnelfqnlakdlamhiammnpryvsaeeipaeeleke
rqiyiqaalnegkpqqiaekiaegrlkkyleevvlleqpfvkddkvkvkeliqqaiakig
enivvrrfcrfelga
>d1aiph_ 4.36.1.1.2 Elongation factor Ts (EF-Ts), dimerisation domain {Thermus thermophilus}
qmelikklreatgagmmdvkraledagwdeekavqllrergamkaakkadrearegiigh
yihhnqrvgvlvelncetdfvarnelfqnlakdlamhiammnpryvsaeeipaeeleker
qiyiqaalnegkpqqiaekiaegrlkkyleevvlleqpfvkddkvkvkeliqqaiakige
nivvrrfcrfelga
>d1aiqa_ 4.91.1.1.1 Thymidylate synthase {Escherichia coli}
kqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihellw
flqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlkn
dpdseriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfniasy
allvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesifd
yrfedfeiegydphpgikapvai
>d1aiqb_ 4.91.1.1.1 Thymidylate synthase {Escherichia coli}
kqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihellw
flqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlkn
dpdseriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfniasy
allvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesifd
yrfedfeiegydphpgikapvai
>d1air__ 2.71.1.1.1 Pectate lyase {Erwinia chrysanthemi, type C}
atdtggyaataggnvtgavsktatsmqdivniidaarldangkkvkggayplvitytgne
dslinaaaanicgqwskdprgveikeftkgitiigangssanfgiwikkssdvvvqnmri
gylpggakdgdmirvddspnvwvdhnelfaanhecdgtpdndttfesavdikgasntvtv
synyihgvkkvgldgssssdtgrnityhhnyyndvnarlplqrgglvhaynnlytnitgs
glnvrqngqaliennwfekainpvtsrydgknfgtwvlkgnnitkpadfstysitwtadt
kpyvnadswtstgtfptvaynyspvsaqcvkdklpgyagvgknlatltstac
>d1aisa1 4.103.1.1.4 (1-92) TATA-box binding protein (TBP), C-terminal domain {Pyrococcus woesei}
mvdmskvklrienivasvdlfaqldlekvldlcpnskynpeefpgiichlddpkvallif
ssgklvvtgaksvqdieravaklaqklksigv
>d1aisa2 4.103.1.1.4 (93-181) TATA-box binding protein (TBP), C-terminal domain {Pyrococcus woesei}
kfkrapqidvqnmvfsgdigrefnldvvaltlpnceyepeqfpgviyrvkepksvillfs
sgkivcsgakseadaweavrkllreldky
>d1aisb1 1.73.1.2.2 (1108-1205) Transcription factor IIB (TFIIB), core domain {Pyrococcus woesei}
nlafalseldritaqlklprhveeeaarlyreavrkglirgrsiesvmaacvyaacrllk
vprtldeiadiarvdkkeigrsyrfiarnlnltpkklf
>d1aisb2 1.73.1.2.2 (1206-1300) Transcription factor IIB (TFIIB), core domain {Pyrococcus woesei}
vkptdyvnkfadelglsekvrrraieildeaykrgltsgkspaglvaaalyiasllegek
rtqrevaevarvtevtvrnrykelveklkikvpia
>d1aiu__ 3.38.1.1.4 Thioredoxin {Human (Homo sapiens)}
mvkqiesktafqealdaagdklvvvdfsatwcgpckmikpffhslsekysnviflevdvn
dcqdvasecevkcmptfqffkkgqkvgefsgankekleatinelv
>d1aiv_1 3.84.1.2.6 (1-334) Ovotransferrin {Chicken (Gallus gallus)}
appksvirwctisspeekkcnnlrdltqqerisltcvqkatyldcikaianneadaisld
ggqafeaglapyklkpiaaevyehtegsttsyyavavvkkgteftvndlqgktschtglg
rsagwnipigtllhrgaiewegiesgsveqavakffsascvpgatieqklcrqckgdpkt
kcarnapysgysgafhclkdgkgdvafvkhttvnenapdqkdeyellcldgsrqpvdnyk
tcnwarvaahavvarddnkvediwsflskaqsdfgvdtksdfhlfgppgkkdpvlkdllf
kdsaimlkrvpslmdsqlylgfeyysaiqsmrkd
>d1aiv_2 3.84.1.2.6 (335-686) Ovotransferrin {Chicken (Gallus gallus)}
qltpsprenriqwcavgkdekskcdrwsvvsngdvectvvdetkdciikimkgeadaval
dgglvytagvcglvpvmaeryddesqcsktderpasyfavavarkdsnvnwnnlkgkksc
htavgrtagwvipmglihnrtgtcnfdeyfsegcapgsppnsrlcqlcqgsggippekcv
asshekyfgytgalrclvekgdvafiqhstveentggknkadwaknlqmddfellctdgr
ranvmdyrecnlaevpthavvvrpekankirdllerqekrfgvngsekskfmmfesqnkd
llfkdltkclfkvregttykeflgdkfytvisslktcnpsdilqmcsflegk
>d1aiw__ 2.63.1.1.1 Cellulose-binding domain of endoglucanase Z {Erwinia chrysanthemi}
mgdcananvypnwvskdwaggqpthneagqsivykgnlytanwytasvpgsdsswtqvgs
cn
>e1aix.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqf
>e1aix.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1aiy.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1aiy.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1aiy.2c 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1aiy.2d 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1aiy.3e 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1aiy.3f 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1aiy.4g 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1aiy.4h 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1aiy.5i 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1aiy.5j 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1aiy.6k 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1aiy.6l 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>d1aiza_ 2.5.1.1.21 Azurin {Alcaligenes denitrificans}
aqceatiesndamqynlkemvvdksckqftvhlkhvgkmakvamghnwvltkeadkqgva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
mkgtlklsn
>d1aizb_ 2.5.1.1.21 Azurin {Alcaligenes denitrificans}
aqceatiesndamqynlkemvvdksckqftvhlkhvgkmakvamghnwvltkeadkqgva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
mkgtlklsn
>d1aj0__ 3.1.19.1.1 Dihydropteroate synthetase {Escherichia coli}
mklfaqgtsldlshphvmgilnvtpdsfsdggthnslidavkhanlminagatiidvgge
strpgaaevsveeelqrvipvveaiaqrfevwisvdtskpeviresakvgahiindirsl
sepgaleaaaetglpvclmhmqgnpktmqeapkyddvfaevnryfieqiarceqagiake
kllldpgfgfgknlshnysllarlaefhhfnlpllvgmsrksmigqllnvgpserlsgsl
acaviaamqgahiirvhdvketveamrvveatlsakenkrye
>d1aj2__ 3.1.19.1.1 Dihydropteroate synthetase {Escherichia coli}
mklfaqgtsldlshphvmgilnvtpdsfsdggthnslidavkhanlminagatiidvgge
strpgaaevsveeelqrvipvveaiaqrfevwisvdtskpeviresakvgahiindirsl
sepgaleaaaetglpvclmhmqgnpktmqeapkyddvfaevnryfieqiarceqagiake
kllldpgfgfgknlshnysllarlaefhhfnlpllvgmsrksmigqllnvgpserlsgsl
acaviaamqgahiirvhdvketveamrvveatlsakenkrye
>d1aj3__ 1.7.1.1.2 Spectrin {Chicken (Gallus gallus)}
hqffrdmddeeswikekkllvssedygrdltgvqnlrkkhkrleaelaahepaiqgvldt
gkklsddntigkeeiqqrlaqfvdhwkelkqlaaargq
>d1aj4__ 1.42.1.5.1 Troponin C {Chicken (Gallus gallus)}
adiykaaveqlteeqknefkaafdifvlgaedgsistkelgkvmrmlgqnptpeelqemi
devdedgsgtvdfdeflvmmvrsmkddskgkteeelsdlfrmfdknadgyidleelkiml
qatgetiteddieelmkdgdknndgridydeflefmkgve
>d1aj5a_ 1.42.1.7.2 Calpain domain VI {Rat (Rattus norvegicus)}
eeerqfrklfvqlagddmevsatelmnilnkvvtrhpdlktdgfgidtcrsmvavmdsdt
tgklgfeefkylwnnikkwqgiykrfdtdrsgtigsnelpgafeaagfhlnqhiysmiir
rysdetgnmdfdnfisclvrldamfrafrsldkngtgqiqvniqewlqltmys
>d1aj5b_ 1.42.1.7.2 Calpain domain VI {Rat (Rattus norvegicus)}
eeerqfrklfvqlagddmevsatelmnilnkvvtrhpdlktdgfgidtcrsmvavmdsdt
tgklgfeefkylwnnikkwqgiykrfdtdrsgtigsnelpgafeaagfhlnqhiysmiir
rysdetgnmdfdnfisclvrldamfrafrsldkngtgqiqvniqewlqltmys
>d1aj6__ 4.96.1.2.1 DNA gyrase B {Escherichia coli}
vlkgldavrkrpgmyigdtddgtglhhmvfevvdnaidealaghckeiivtihadnsvsv
qddgrgiptgihpeegvsaaevimtvlhaggkfddnsykvsgglhgvgvsvvnalsqkle
lviqhegkihrqiyehgvpqaplavtgetektgtmvrfwpsletftnvtefeyeilakrl
relsflnsgvsirlrdkrdgkedhfh
>d1aj7h1 2.1.1.1.68 (1-114) Immunoglobulin (variable domains of L and H chains) {Fab 48G7 (mouse/human), kappa L chain}
qvqlqqsgaelvkpgasvklsctasgfnikdtymhwvkqrpeqglewigridpangntky
dpkfqgkatitadtssntaylqlssltsedtavyycasyygiywgqgttltvssa
>d1aj7h2 2.1.1.2.73 (115-216) Immunoglobulin (constant domains of L and H chains) {Fab 48G7 (mouse/human), kappa L chain}
stkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqssg
lyslssvvtvpssslgtqtyicnvnhkpsntkvdkkvepksc
>d1aj7l1 2.1.1.1.68 (1-109) Immunoglobulin (variable domains of L and H chains) {Fab 48G7 (mouse/human), kappa L chain}
diqmtqspsslsaslgervsltcrasqeisgylswlqqkpdgtikrliyaastldsgvpk
rfsgsrsgsdysltisslesedfadyyclqyasyprtfgggtkveikrt
>d1aj7l2 2.1.1.2.73 (110-214) Immunoglobulin (constant domains of L and H chains) {Fab 48G7 (mouse/human), kappa L chain}
vaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqdsk
dstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1aj8a_ 1.99.1.1.3 Citrate synthase {Pyrococcus furiosus}
lakgledvyidqtnicyidgkegklyyrgysveelaelstfeevvyllwwgklpslsele
nfkkelaksrglpkevieimealpknthpmgalrtiisylgniddsgdipvtpeevyrig
isvtakiptivanwyrikngleyvppkeklshaanflymlhgeeppkewekamdvalily
aeheinastlavmtvgstlsdyysailagigalkgpihggaveeaikqfmeigspekvee
wffkalqqkrkimgaghrvyktydprarifkkyasklgdkklfeiaerlerlveeylskk
gisinvdywsglvfygmkipielyttifamgriagwtahlaeyvshnriirprlqyvgei
gkkylpielrr
>d1aj8b_ 1.99.1.1.3 Citrate synthase {Pyrococcus furiosus}
lakgledvyidqtnicyidgkegklyyrgysveelaelstfeevvyllwwgklpslsele
nfkkelaksrglpkevieimealpknthpmgalrtiisylgniddsgdipvtpeevyrig
isvtakiptivanwyrikngleyvppkeklshaanflymlhgeeppkewekamdvalily
aeheinastlavmtvgstlsdyysailagigalkgpihggaveeaikqfmeigspekvee
wffkalqqkrkimgaghrvyktydprarifkkyasklgdkklfeiaerlerlveeylskk
gisinvdywsglvfygmkipielyttifamgriagwtahlaeyvshnriirprlqyvgei
gkkylpielr
>d1aj9a_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgssqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1aj9b_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1ajaa_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqgatpaalvahvtsrkcygpsatsekcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaeargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1ajab_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqgatpaalvahvtsrkcygpsatsekcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaeargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1ajba_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqgatpaalvahvtsrkcygpsatsekcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaeargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1ajbb_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqgatpaalvahvtsrkcygpsatsekcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaeargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1ajca_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqgatpaalvahvtsrkcygpsatsekcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaeargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1ajcb_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqgatpaalvahvtsrkcygpsatsekcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaeargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1ajda_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqgatpaalvahvtsrkcygpsatsekcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaeargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1ajdb_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqgatpaalvahvtsrkcygpsatsekcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaeargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1aje__ 3.30.1.6.11 CDC42 {Human (Homo sapiens)}
gskiisamqtikcvvvgdgavgktcllisyttnkfpseyvptvfdnyavtvmiggepytl
glfdtagqedydrlrplsypqtdvflvcfsvvspssfenvkekwvpeithhcpktpfllv
gtqidlrddpstieklaknkqkpitpetaeklardlkavkyvecsaltqkglknvfdeai
laaleppepkksrr
>d1ajg__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgyqg
>d1ajh__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgyqg
>d1ajj__ 7.12.1.1.1 Ligand-binding domain of low-density lipoprotein receptor {Human (Homo sapiens)}
pcsafefhclsgecihsswrcdggpdckdksdeenca
>d1ajka_ 2.26.1.2.3 Bacillus 1-3,1-4-beta-glucanase {Bacillus macerans}
ntgivssfftytgpahgtqwdeidieflgkdttkvqfnyytngvgghekvislgfdaskg
fhtyafdwqpgyikwyvdgvlkhtatanipstpgkimmnlwngtgvddwlgsynganply
aeydwvkytsnqtggsffepfnsynsgtwekadgysnggvfnctwrannvnftndgklkl
gltssaynkfdcaeyrstniygyglyevsmkpak
>d1ajkb_ 2.26.1.2.3 Bacillus 1-3,1-4-beta-glucanase {Bacillus macerans}
ntgivssfftytgpahgtqwdeidieflgkdttkvqfnyytngvgghekvislgfdaskg
fhtyafdwqpgyikwyvdgvlkhtatanipstpgkimmnlwngtgvddwlgsynganply
aeydwvkytsnqtggsffepfnsynsgtwekadgysnggvfnctwrannvnftndgklkl
gltssaynkfdcaeyrstniygyglyevsmkpak
>d1ajm__ 4.91.1.1.1 Thymidylate synthase {Escherichia coli}
kqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihellw
flqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlkn
dpdseriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfniasy
allvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesifd
yrfedfeiegydphpgikapvai
>e1ajn.1a 4.124.1.2.1 Penicillin acylase, catalytic domain {Escherichia coli}
ssseikivrdeygmphiyandtwhlfygygyvvaqdrlfqmemarrstqgtvaevlgkdf
vkfdkdirrnywpdairaqiaalspedmsilqgyadgmnawidkvntnpetllpkqfntf
gftpkrwepfdvamifvgtmanrfsdstseidnlalltalkdkygvsqgmavfnqlkwlv
npsapttiavqesnyplkfnqqnsqt
>e1ajn.1b 4.124.1.2.1 Penicillin acylase, catalytic domain {Escherichia coli}
snmwvigkskaqdakaimvngpqfgwyapaytygiglhgagydvtgntpfaypglvfghn
gviswgstagfgddvdifaerlsaekpgyylhngkwvkmlsreetitvkngqaetftvwr
tvhgnilqtdqttqtayaksrawdgkevasllawthqmkaknwqqwtqqaakqaltinwy
yadvngnigyvhtgaypdrqsghdprlpvpgtgkwdwkgllpfemnpkvynpqsgyianw
nnspqkdypasdlfaflwggadrvteidrlleqkprltadqawdvirqtsrqdlnlrlfl
ptlqaatsgltqsdprrqlvetltrwdginllnddgktwqqpgsailnvwltsmlkrtvv
aavpmpfdkwysasgyettqdgptgslnisvgakilyeavqgdkspipqavdlfagkpqq
evvlaaledtwetlskrygnnvsnwktpamaltfrannffgvpqaaaeetrhqaeyqnrg
tendmivfspttsdrpvlawdvvapgqsgfiapdgtvdkhyedqlkmyenfgrkslwltk
qdveahkesqevlhvqr
>d1ajoa_ 2.26.1.2.3 Bacillus 1-3,1-4-beta-glucanase {Bacillus macerans}
ghekvislgfdaskgfhtyafdwqpgyikwyvdgvlkhtatanipstpgkimmnlwngtg
vddwlgsynganplyaeydwvkytsnqtggsffepfnsynsgtwekadgysnggvfnctw
rannvnftndgklklgltssaynkfdcaeyrstniygyglyevsmkpakntgivssffty
tgpahgtqwdeidieflgkdttkvqfnyytng
>d1ajob_ 2.26.1.2.3 Bacillus 1-3,1-4-beta-glucanase {Bacillus macerans}
vgghekvislgfdaskgfhtyafdwqpgyikwyvdgvlkhtatanipstpgkimmnlwng
tgvddwlgsynganplyaeydwvkytsnqtggsffepfnsynsgtwekadgysnggvfnc
twrannvnftndgklklgltssaynkfdcaeyrstniygyglyevsmkpakntgivssff
tytgpahgtqwdeidieflgkdttkvqfnyytng
>e1ajp.1a 4.124.1.2.1 Penicillin acylase, catalytic domain {Escherichia coli}
ssseikivrdeygmphiyandtwhlfygygyvvaqdrlfqmemarrstqgtvaevlgkdf
vkfdkdirrnywpdairaqiaalspedmsilqgyadgmnawidkvntnpetllpkqfntf
gftpkrwepfdvamifvgtmanrfsdstseidnlalltalkdkygvsqgmavfnqlkwlv
npsapttiavqesnyplkfnqqnsqt
>e1ajp.1b 4.124.1.2.1 Penicillin acylase, catalytic domain {Escherichia coli}
snmwvigkskaqdakaimvngpqfgwyapaytygiglhgagydvtgntpfaypglvfghn
gviswgstagfgddvdifaerlsaekpgyylhngkwvkmlsreetitvkngqaetftvwr
tvhgnilqtdqttqtayaksrawdgkevasllawthqmkaknwqqwtqqaakqaltinwy
yadvngnigyvhtgaypdrqsghdprlpvpgtgkwdwkgllpfemnpkvynpqsgyianw
nnspqkdypasdlfaflwggadrvteidrlleqkprltadqawdvirqtsrqdlnlrlfl
ptlqaatsgltqsdprrqlvetltrwdginllnddgktwqqpgsailnvwltsmlkrtvv
aavpmpfdkwysasgyettqdgptgslnisvgakilyeavqgdkspipqavdlfagkpqq
evvlaaledtwetlskrygnnvsnwktpamaltfrannffgvpqaaaeetrhqaeyqnrg
tendmivfspttsdrpvlawdvvapgqsgfiapdgtvdkhyedqlkmyenfgrkslwltk
qdveahkesqevlhvqr
>e1ajq.1a 4.124.1.2.1 Penicillin acylase, catalytic domain {Escherichia coli}
ssseikivrdeygmphiyandtwhlfygygyvvaqdrlfqmemarrstqgtvaevlgkdf
vkfdkdirrnywpdairaqiaalspedmsilqgyadgmnawidkvntnpetllpkqfntf
gftpkrwepfdvamifvgtmanrfsdstseidnlalltalkdkygvsqgmavfnqlkwlv
npsapttiavqesnyplkfnqqnsqt
>e1ajq.1b 4.124.1.2.1 Penicillin acylase, catalytic domain {Escherichia coli}
snmwvigkskaqdakaimvngpqfgwyapaytygiglhgagydvtgntpfaypglvfghn
gviswgstagfgddvdifaerlsaekpgyylhngkwvkmlsreetitvkngqaetftvwr
tvhgnilqtdqttqtayaksrawdgkevasllawthqmkaknwqqwtqqaakqaltinwy
yadvngnigyvhtgaypdrqsghdprlpvpgtgkwdwkgllpfemnpkvynpqsgyianw
nnspqkdypasdlfaflwggadrvteidrlleqkprltadqawdvirqtsrqdlnlrlfl
ptlqaatsgltqsdprrqlvetltrwdginllnddgktwqqpgsailnvwltsmlkrtvv
aavpmpfdkwysasgyettqdgptgslnisvgakilyeavqgdkspipqavdlfagkpqq
evvlaaledtwetlskrygnnvsnwktpamaltfrannffgvpqaaaeetrhqaeyqnrg
tendmivfspttsdrpvlawdvvapgqsgfiapdgtvdkhyedqlkmyenfgrkslwltk
qdveahkesqevlhvqr
>d1ajra_ 3.57.1.1.3 Aspartate aminotransferase, AAT {Pig (Sus scrofa), cytosolic form}
appsvfaevpqaqpvlvfkliadfredpdprkvnlgvgayrtddcqpwvlpvvrkveqri
annsslnheylpilglaefrtcasrlalgddspalqekrvggvqslggtgalrigaefla
rwyngtnnkdtpvyvssptwenhngvfttagfkdirsyrywdtekrgldlqgflsdlena
pefsifvlhacahnptgtdptpeqwkqiasvmkrrflfpffdsayqgfasgnlekdawai
ryfvsegfelfcaqsfsxnfglynervgnltvvakepdsilrvlsqmqkivrvtwsnppa
qgarivartlsdpelfhewtgnvktmadrilsmrselrarlealktpgtwnhitdqigmf
sftglnpkqveylinqkhiyllpsgrinmcglttknldyvatsiheavtkiq
>d1ajrb_ 3.57.1.1.3 Aspartate aminotransferase, AAT {Pig (Sus scrofa), cytosolic form}
appsvfaevpqaqpvlvfkliadfredpdprkvnlgvgayrtddcqpwvlpvvrkveqri
annsslnheylpilglaefrtcasrlalgddspalqekrvggvqslggtgalrigaefla
rwyngtnnkdtpvyvssptwenhngvfttagfkdirsyrywdtekrgldlqgflsdlena
pefsifvlhacahnptgtdptpeqwkqiasvmkrrflfpffdsayqgfasgnlekdawai
ryfvsegfelfcaqsfsxnfglynervgnltvvakepdsilrvlsqmqkivrvtwsnppa
qgarivartlsdpelfhewtgnvktmadrilsmrselrarlealktpgtwnhitdqigmf
sftglnpkqveylinqkhiyllpsgrinmcglttknldyvatsiheavtkiq
>d1ajsa_ 3.57.1.1.3 Aspartate aminotransferase, AAT {Pig (Sus scrofa), cytosolic form}
appsvfaevpqaqpvlvfkliadfredpdprkvnlgvgayrtddcqpwvlpvvrkveqri
annsslnheylpilglaefrtcasrlalgddspalqekrvggvqslggtgalrigaefla
rwyngtnnkdtpvyvssptwenhngvfttagfkdirsyrywdtekrgldlqgflsdlena
pefsifvlhacahnptgtdptpeqwkqiasvmkrrflfpffdsayqgfasgnlekdawai
ryfvsegfelfcaqsfsknfglynervgnltvvakepdsilrvlsqmqkivrvtwsnppa
qgarivartlsdpelfhewtgnvktmadrilsmrselrarlealktpgtwnhitdqigmf
sftglnpkqveylinqkhiyllpsgrinmcglttknldyvatsiheavtkiq
>d1ajsb_ 3.57.1.1.3 Aspartate aminotransferase, AAT {Pig (Sus scrofa), cytosolic form}
appsvfaevpqaqpvlvfkliadfredpdprkvnlgvgayrtddcqpwvlpvvrkveqri
annsslnheylpilglaefrtcasrlalgddspalqekrvggvqslggtgalrigaefla
rwyngtnnkdtpvyvssptwenhngvfttagfkdirsyrywdtekrgldlqgflsdlena
pefsifvlhacahnptgtdptpeqwkqiasvmkrrflfpffdsayqgfasgnlekdawai
ryfvsegfelfcaqsfsxnfglynervgnltvvakepdsilrvlsqmqkivrvtwsnppa
qgarivartlsdpelfhewtgnvktmadrilsmrselrarlealktpgtwnhitdqigmf
sftglnpkqveylinqkhiyllpsgrinmcglttknldyvatsiheavtkiq
>d1ajva_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1ajvb_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1ajw__ 2.1.1.5.18 Rho GDP-dissociation inhibitor 1, RhoGDI {Bovine (Bos taurus)}
avsadpnvpnvvvtrltlvcstapgpleldltgdlesfkkqsfvlkegveyrikisfrvn
reivsgmkyiqhtyrkgvkidktdymvgsygpraeeyefltpmeeapkgmlargsyniks
rftdddrtdhlswewnltikkewkd
>d1ajxa_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1ajxb_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1ajya1 7.32.1.1.3 (30-66) PUT3 {Baker's yeast (Saccharomyces cerevisiae)}
msvaclscrkrhikcpggnpcqkcvtsnaiceyleps
>d1ajyb1 7.32.1.1.3 (30-66) PUT3 {Baker's yeast (Saccharomyces cerevisiae)}
msvaclscrkrhikcpggnpcqkcvtsnaiceyleps
>d1ajz__ 3.1.19.1.1 Dihydropteroate synthetase {Escherichia coli}
mklfaqgtsldlshphvmgilnvtpdsfsdggthnslidavkhanlminagatiidvgge
strpgaaevsveeelqrvipvveaiaqrfevwisvdtskpeviresakvgahiindirsl
sepgaleaaaetglpvclmhmqgnpktmqeapkyddvfaevnryfieqiarceqagiake
kllldpgfgfgknlshnysllarlaefhhfnlpllvgmsrksmigqllnvgpserlsgsl
acaviaamqgahiirvhdvketveamrvveatlsakenkrye
>d1ak0__ 1.115.1.2.1 P1 nuclease {Penicillium citrinum}
wgalghatvayvaqhyvspeaaswaqgilgsssssylasiaswadeyrltsagkwsaslh
fidaednpptncnvdyerdcgssgcsisaianytqrvsdsslssenhaealrflvhfigd
mtqplhdeayavggnkinvtfdgyhdnlhsdwdtympqkligghalsdaeswaktlvqni
esgnytaqaigwikgdnisepittatrwasdanalvctvvmphgaaalqtgdlyptyyds
vidtielqiakggyrlanwineih
>d1ak1__ 3.82.1.1.1 Ferrochelatase {Bacillus subtilis}
rkkmgllvmaygtpykeedieryythirrgrkpepemlqdlkdryeaiggisplaqiteq
qahnleqhlneiqdeitfkayiglkhiepfiedavaemhkdgiteavsivlaphfstfsv
qsynkrakeeaeklggltitsveswydepkfvtywvdrvketyasmpederenamlivsa
hslpekikefgdpypdqlhesakliaegagvseyavgwqsegntpdpwlgpdvqdltrdl
feqkgyqafvyvpvgfvadhlevlydndyeckvvtddigasyyrpempnakpefidalat
vvlkklgr
>d1ak2_1 3.30.1.1.10 (14-146,177-233) Adenylate kinase {Bovine (Bos taurus), mitochondrial izozyme-2}
pkgvravllgppgagkgtqapklaknfcvchlatgdmlramvasgselgkklkatmdagk
lvsdemvlelieknletppckngflldgfprtvrqaemlddlmekrkekldsviefsipd
sllirritgrlihXsddnkkalkirleayhtqttplveyyskrgihsaidasqtpdvvfa
silaafskats
>d1ak2_2 7.35.2.1.4 (147-176) Microbial and mitochondrial ADK, insert "zinc finger" domain {Bovine (Bos taurus), mitochondrial izozyme-2}
pqsgrsyheefnppkepmkdditgeplirr
>d1ak4a_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
mvnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgf
mcqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictakte
wldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1ak4b_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
nptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfmc
qggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktewl
dgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1ak4c_ 1.72.1.1.1 HIV-1 capsid protein {Human immunodeficiency virus, type 1, HIV-1}
pivqnlqgqmvhqaisprtlnawvkvveekafspevipmfsalsegatpqdlntmlntvg
ghqaamqmlketineeaaewdrlhpvhagpiapgqmreprgsdiagttstlqeqigwmth
nppipvgeiykrwiilglnkivrmy
>d1ak4d_ 1.72.1.1.1 HIV-1 capsid protein {Human immunodeficiency virus, type 1, HIV-1}
pivqnlqgqmvhqaisprtlnawvkvveekafspevipmfsalsegatpqdlntmlntvg
ghqaamqmlketineeaaewdrlhpvhagpiapgqmreprgsdiagttstlqeqigwmth
nppipvgeiykrwiilglnkivrmy
>d1ak5_1 3.1.6.2.1 (2-101,222-483) Inosine monophosphate dehydrogenase (IMPDH) {Tritrichomonas foetus}
akyynepchtfneyllipglstvdcipsnvnlstplvkfqkgqqseinlkiplvsaimqs
vsgekmaialareggisfifgsqsiesqaamvhavknfkaXhnelvdsqkrylvgagint
rdfrervpalveagadvlcidssdgfsewqkitigwirekygdkvkvgagnivdgegfry
ladagadfikigigggsicitreqkgigrgqatavidvvaernkyfeetgiyipvcsdgg
ivydyhmtlalamgadfimlgryfarfeesptrkvtingsvmkeywgegssrarnwqryd
lggkqklsfeegvdsyvpyagklkdnveaslnkvkstmcncgaltipqlqskakitlvss
vsi
>d1ak6__ 4.85.1.2.3 Destrin {Human (Homo sapiens)/pig (Sus scrofa)}
tmitpssgnsasgvqvadevcrifydmkvrkcstpeeikkrkkavifclsadkkciivee
gkeilvgdvgvtitdpfkhfvgmlpekdcryalydasfetkesrkeelmfflwapelapl
kskmiyasskdaikkkfqgikhecqangpedlnraciaeklggslivafegcpv
>d1ak7__ 4.85.1.2.3 Destrin {Human (Homo sapiens)/pig (Sus scrofa)}
tmitpssgnsasgvqvadevcrifydmkvrkcstpeeikkrkkavifclsadkkciivee
gkeilvgdvgvtitdpfkhfvgmlpekdcryalydasfetkesrkeelmfflwapelapl
kskmiyasskdaikkkfqgikhecqangpedlnraciaeklggslivafegcpv
>d1ak8__ 1.42.1.5.8 Calmodulin {Bovine (Bos taurus)}
madqlteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadg
ngtidfpefltmmark
>d1ak9__ 3.33.1.1.7 Subtilisin Novo/BPN' {Bacillus amyloliquefaciens}
aqsvpygvsqikapalhsqgycgsnvkvavidsgidsshpdlkvaggasfvpsetnpfqd
nnshgthvagtvaalnnsigvlgvapcaslyavkvlgadgsgqyswiingiewaiannmd
vinmslggpsgsaalkaavdkavasgvvvvaaagnegtsgssstvgypakypsviavgav
dssnqrasfssvgpeldvmapgvsiqstlpgnkygaksgtsmasphvagaaalilskhpn
wtntqvrsslentttklgdsfyygkglinvqaaaq
>d1akaa_ 3.57.1.1.1 Aspartate aminotransferase, AAT {Chicken (Gallus gallus), mitochondria}
sswwshvemgppdpilgvteafkrdtnskkmnlgvgayrddngkpyvlncvrkaeamiaa
kkmdkeylpiagladftrasaelalgenseafksgryvtvqgisgtgslrvganflqrff
kfsrdvylpkpswgnhtpifrdaglqlqayryydpktcsldftgamediskipeksiill
hacahnptgvdprqeqwkelasvvkkrnllayfdmayqgfasgdinrdawalrhfieqgi
dvvlsqsyahnmglygeragaftvicrdaeeakrvesqlkilirpmysnppmngariasl
ilntpelrkewlvevkgmadriismrtqlvsnlkkegsshnwqhitdqigmfcftglkpe
qverltkefsiymtkdgrisvagvassnvgylahaihqvtk
>d1akab_ 3.57.1.1.1 Aspartate aminotransferase, AAT {Chicken (Gallus gallus), mitochondria}
sswwshvemgppdpilgvteafkrdtnskkmnlgvgayrddngkpyvlncvrkaeamiaa
kkmdkeylpiagladftrasaelalgenseafksgryvtvqgisgtgslrvganflqrff
kfsrdvylpkpswgnhtpifrdaglqlqayryydpktcsldftgamediskipeksiill
hacahnptgvdprqeqwkelasvvkkrnllayfdmayqgfasgdinrdawalrhfieqgi
dvvlsqsyahnmglygeragaftvicrdaeeakrvesqlkilirpmysnppmngariasl
ilntpelrkewlvevkgmadriismrtqlvsnlkkegsshnwqhitdqigmfcftglkpe
qverltkefsiymtkdgrisvagvassnvgylahaihqvtk
>d1akba_ 3.57.1.1.1 Aspartate aminotransferase, AAT {Chicken (Gallus gallus), mitochondria}
sswwshvemgppdpilgvteafkrdtnskkmnlgvgayrddngkpyvlncvrkaeamiaa
kkmdkeylpiagladftrasaelalgenseafksgryvtvqgisgtgslrvganflqrff
kfsrdvylpkpswgnhtpifrdaglqlqayryydpktcsldftgamediskipeksiill
hacahnptgvdprqeqwkelasvvkkrnllayfdmayqgfasgdinrdawalrhfieqgi
dvvlsqsyahnmglygeragaftvicrdaeeakrvesqlkilirpmysnppmngariasl
ilntpelrkewlvevkgmadriismrtqlvsnlkkegsshnwqhitdqigmfcftglkpe
qverltkefsiymtkdgrisvagvassnvgylahaihqvtk
>d1akca_ 3.57.1.1.1 Aspartate aminotransferase, AAT {Chicken (Gallus gallus), mitochondria}
sswwshvemgppdpilgvteafkrdtnskkmnlgvgayrddngkpyvlncvrkaeamiaa
kkmdkeylpiagladftrasaelalgenseafksgryvtvqgisgtgslrvganflqrff
kfsrdvylpkpswgnhtpifrdaglqlqayryydpktcsldftgamediskipeksiill
hacahnptgvdprqeqwkelasvvkkrnllayfdmayqgfasgdinrdawalrhfieqgi
dvvlsqsyahnmglygeragaftvicrdaeeakrvesqlkilirpmysnppmngariasl
ilntpelrkewlvevkgmadriismrtqlvsnlkkegsshnwqhitdqigmfcftglkpe
qverltkefsiymtkdgrisvagvassnvgylahaihqvtk
>d1akd__ 1.100.1.1.1 Cytochrome P450 {Pseudomonas putida}
nlaplpphvpehlvfdfdmynpsnlsagvqeawavlqesnvpdlvwtrcngghwiatrgq
lireayedyrhfssecpfipreageaydfiptsmdppeqrqfralanqvvgmpvvdklen
riqelacslieslrpqgqcnftedyaepfpirifmllaglpeediphlkyltdqmtrpdg
smtfaeakealydylipiieqrrqkpgtdaisivangqvngrpitsdeakrmcglllvgg
ldtvvnflsfsmeflakspehrqeliqrperipaaceellrrfslvadgriltsdyefhg
vqlkkgdqillpqmlsglderenacpmhvdfsrqkvshttfghgshlclgqhlarreiiv
tlkewltripdfsiapgaqiqhksgivsgvqalplvwdpattkav
>d1akea1 3.30.1.1.12 (1-121,157-214) Adenylate kinase {Escherichia coli}
mriillgapgagkgtqaqfimekygipqistgdmlraavksgselgkqakdimdagklvt
delvialvkeriaqedcrngflldgfprtipqadamkeaginvdyvlefdvpdelivdri
vXkddqeetvrkrlveyhqmtapligyyskeaeagntkyakvdgtkpvaevradlekilg
>d1akea2 7.35.2.1.2 (122-156) Microbial and mitochondrial ADK, insert "zinc finger" domain {Escherichia coli}
grrvhapsgrvyhvkfnppkvegkddvtgeelttr
>d1akeb1 3.30.1.1.12 (1-121,157-214) Adenylate kinase {Escherichia coli}
mriillgapgagkgtqaqfimekygipqistgdmlraavksgselgkqakdimdagklvt
delvialvkeriaqedcrngflldgfprtipqadamkeaginvdyvlefdvpdelivdri
vXkddqeetvrkrlveyhqmtapligyyskeaeagntkyakvdgtkpvaevradlekilg
>d1akeb2 7.35.2.1.2 (122-156) Microbial and mitochondrial ADK, insert "zinc finger" domain {Escherichia coli}
grrvhapsgrvyhvkfnppkvegkddvtgeelttr
>d1akha_ 1.4.1.1.2 Mating type protein A1 Homeodomain {Baker's yeast (Saccharomyces cerevisiae)}
ispqarafleevfrrkqslnskekeevakkcgitplqvrvwfinkrmrs
>d1akhb_ 1.4.1.1.3 mat alpha2 Homeodomain {Baker's yeast (Saccharomyces cerevisiae)}
tkpyrghrftkenvrileswfaknienpyldtkglenlmkntslsriqiknwvsnrrrke
ktitiapeladllsgepl
>d1aki__ 4.2.1.2.1 Lysozyme {Chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1akja1 2.1.1.2.4 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-a0201}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrdgedqtqdtelvetrpagdgtf
qkwaavvvpsgqeqrytchvqheglpkpltlrwep
>d1akja2 4.17.1.1.11 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-a0201}
gshsmryfftsvsrpgrgeprfiavgyvddtqfvrfdsdaasqrmeprapwieqegpeyw
dgetrkvkahsqthrvdlgtlrgyynqseagshtvqrmygcdvgsdwrflrgyhqyaydg
kdyialkedlrswtaadmaaqttkhkweaahvaeqlraylegtcvewlrrylengketlq
r
>d1akjb1 2.1.1.2.4 Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-a0201}
qrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskdws
fyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1akjd_ 2.1.1.1.3 CD8 {Human (Homo sapiens)}
sqfrvspldrtwnlgetvelkcqvllsnptsgcswlfqprgaaasptfllylsqnkpkaa
egldtqrfsgkrlgdtfvltlsdfrrenegyyfcsalsnsimyfshfvpvflpa
>d1akje_ 2.1.1.1.3 CD8 {Human (Homo sapiens)}
sqfrvspldrtwnlgetvelkcqvllsnptsgcswlfqprgaaasptfllylsqnkpkaa
egldtqrfsgkrlgdtfvltlsdfrrenegyyfcsalsnsimyfshfvpvflpa
>d1akk__ 1.3.1.1.8 Mitochondrial cytochrome c {Horse (Equus caballus)}
gdvekgkkifvqkcaqchtvekggkhktgpnlhglfgrktgqapgftytdanknkgitwk
eetlmeylenpkkyipgtkmifagikkkteredliaylkkatne
>d1akl_1 2.70.1.1.1 (247-470) Metalloprotease, C-terminal domain {Pseudomonas aeruginosa, alkaline protease}
ganlttrtgdtvygfnsnterdfysatssssklvfsvwdaggndtldfsgfsqnqkinln
ekalsdvgglkgnvsiaagvtvenaiggsgsdlligndvanvlkggagndilygglgadq
lwggagadtfvygdiaessaaapdtlrdfvsgqdkidlsgldafvngglvlqyvdafagk
agqailsydaaskagslaidfsgdahadfainligqatqadivv
>d1akl_2 4.71.1.4.1 (1-246) Metallo protease, catalytic (N-terminal) domain {Pseudomonas aeruginosa, alkaline protease}
grsdaytqvdnflhayarggdelvnghpsytvdqaaeqilreqaswqkapgdsvltlsys
fltkpndffntpwkyvsdiyslgkfsafsaqqqaqaklslqswsdvtnihfvdagqgdqg
dltfgnfsssvggaafaflpdvpdalkgqswylinssysanvnpangnygrqtltheigh
tlglshpgdynagegdptyadatyaedtraysvmsyweeqntgqdfkgayssapllddia
aiqkly
>d1akma1 3.66.1.1.4 (1-150) Ornithine transcarbamoylase {Escherichia coli}
sgfyhkhflklldftpaelnsllqlaaklkadkksgkeeakltgknialifekdstrtrc
sfevaaydqgarvtylgpsgsqighkesikdtarvlgrmydgiqyrgygqeivetlaeya
svpvwngltnefhptqlladlltmqehlpg
>d1akma2 3.66.1.1.4 (151-333) Ornithine transcarbamoylase {Escherichia coli}
kafnemtlvyagdarnnmgnsmleaaaltgldlrlvapqacwpeaalvtecralaqqngg
nitltedvakgvegadfiytdvwvsmgeakekwaeriallreyqvnskmmqltgnpevkf
lhclpafhddqttlgkkmaeefglhggmevtdevfesaasivfdqaenrmhtikavmvat
lsk
>d1akmb1 3.66.1.1.4 (1-150) Ornithine transcarbamoylase {Escherichia coli}
sgfyhkhflklldftpaelnsllqlaaklkadkksgkeeakltgknialifekdstrtrc
sfevaaydqgarvtylgpsgsqighkesikdtarvlgrmydgiqyrgygqeivetlaeya
svpvwngltnefhptqlladlltmqehlpg
>d1akmb2 3.66.1.1.4 (151-333) Ornithine transcarbamoylase {Escherichia coli}
kafnemtlvyagdarnnmgnsmleaaaltgldlrlvapqacwpeaalvtecralaqqngg
nitltedvakgvegadfiytdvwvsmgeakekwaeriallreyqvnskmmqltgnpevkf
lhclpafhddqttlgkkmaeefglhggmevtdevfesaasivfdqaenrmhtikavmvat
lsk
>d1akmc1 3.66.1.1.4 (1-150) Ornithine transcarbamoylase {Escherichia coli}
sgfyhkhflklldftpaelnsllqlaaklkadkksgkeeakltgknialifekdstrtrc
sfevaaydqgarvtylgpsgsqighkesikdtarvlgrmydgiqyrgygqeivetlaeya
svpvwngltnefhptqlladlltmqehlpg
>d1akmc2 3.66.1.1.4 (151-333) Ornithine transcarbamoylase {Escherichia coli}
kafnemtlvyagdarnnmgnsmleaaaltgldlrlvapqacwpeaalvtecralaqqngg
nitltedvakgvegadfiytdvwvsmgeakekwaeriallreyqvnskmmqltgnpevkf
lhclpafhddqttlgkkmaeefglhggmevtdevfesaasivfdqaenrmhtikavmvat
lsk
>d1akn__ 3.59.1.1.4 Bile-salt activated lipase (cholesterol esterase) {Bovine (Bos taurus)}
aklgsvyteggfvegvnkklslfgdsidifkgipfaaapkalekperhpgwqgtlkaksf
kkrclqatltqdstygnedclylniwvpqgrkevshdlpvmiwiyggaflmgasqganfl
snylydgeeiatrgnvivvtfnyrvgplgflstgdsnlpgnyglwdqhmaiawvkrniea
fggdpdnitlfgesaggasvslqtlspynkglikraisqsgvglcpwaiqqdplfwakri
aekvgcpvddtskmagclkitdpraltlayklplgsteypklhylsfvpvidgdfipddp
vnlyanaadvdyiagtndmdghlfvgmdvpainsnkqdvteedfyklvsgltvtkglrga
natyevytepwaqdssqetrkktmvdletdilfliptkiavaqhkshaksantytylfsq
psrmpiypkwmgadhaddlqyvfgkpfatplgyraqdrtvskamiaywtnfartgdpntg
hstvpanwdpytleddnyleinkqmdsnsmklhlrtnylqfwtqtyqalptvtsagasll
ppednsq
>d1ako__ 4.122.1.1.1 DNA-repair enzyme exonuclease III {Escherichia coli}
mkfvsfninglrarphqleaivekhqpdviglqetkvhddmfpleevaklgynvfyhgqk
ghygvalltketpiavrrgfpgddeeaqrriimaeipsllgnvtvingyfpqgesrdhpi
kfpakaqfyqnlqnyletelkrdnpvlimgdmnisptdldigigeenrkrwlrtgkcsfl
peerewmdrlmswglvdtfrhanpqtadrfswfdyrskgfddnrglridlllasqplaec
cvetgidyeirsmekpsdhapvwatfrr
>d1akp__ 2.1.7.1.4 Kedarcidin (apo form) {Actimomycete strain L585-6}
asaavsvspatgladgatvtvsasgfatstsatalqcailadgrgacnvaefhdfslsgg
egttsvvvrrsftgyvmpdgpevgavdcdtapggceivvggntgeygnaaisfg
>d1akq__ 3.16.4.1.2 Flavodoxin {Desulfovibrio vulgaris}
pkalivygsttgnteytaetiareladagyevdsrdaasveagglfegfdlvllgcstwg
ddsielqddfiplfdsleetgaqgrkvacfgcgassyeyfcgavdaieeklknlgaeivq
dglridgdpraarddivgwahdvrgai
>d1akr__ 3.16.4.1.2 Flavodoxin {Desulfovibrio vulgaris}
pkalivygsttgnteytaetiareladagyevdsrdaasveagglfegfdlvllgcstwa
ddsielqddfiplfdsleetgaqgrkvacfgcgdssyeyfcgavdaieeklknlgaeivq
dglridgdpraarddivgwahdvrgai
>e1aks.1a 2.41.1.2.2 Trypsin(ogen) {Porcine (Sus scrofa)}
ivggytcaansipyqvslnsgshfcggslinsqwvvsaahcyksriqvrlgehnidvleg
neqfinaakiithpnfngntldndimliklsspatlnsrvatvslprscaaagteclisg
wgntk
>e1aks.1b 2.41.1.2.2 Trypsin(ogen) {Porcine (Sus scrofa)}
ssgssypsllqclkapvlsnssckssypgqitgnmicvgflqggkdscqgdsggpvvcng
qlqgivswgygcaqknkpgvytkvcnyvnwiqqtiaan
>d1akt__ 3.16.4.1.2 Flavodoxin {Desulfovibrio vulgaris}
pkalivygsttgnteytaetiareladagyevdsrdaasveagglfegfdlvllgcstwn
ddsielqddfiplfdsleetgaqgrkvacfgcgdssyeyfcgavdaieeklknlgaeivq
dglridgdpraarddivgwahdvrgai
>d1aku__ 3.16.4.1.2 Flavodoxin {Desulfovibrio vulgaris}
pkalivygsttgnteytaetiareladagyevdsrdaasveagglfegfdlvllgcstwg
ddsielqddfiplfdsleetgaqgrkvacfgcgassyeyfcgavdaieeklknlgaeivq
dglridgdpraarddivgwahdvrgai
>d1akv__ 3.16.4.1.2 Flavodoxin {Desulfovibrio vulgaris}
pkalivygsttgnteytaetiareladagyevdsrdaasveagglfegfdlvllgcstwg
ddsielqddfiplfdsleetgaqgrkvacfgcgassyeyfcgavdaieeklknlgaeivq
dglridgdpraarddivgwahdvrgai
>d1akw__ 3.16.4.1.2 Flavodoxin {Desulfovibrio vulgaris}
pkalivygsttgnteytaetiareladagyevdsrdaasveagglfegfdlvllgcstwl
ddsielqddfiplfdsleetgaqgrkvacfgcgdssyeyfcgavdaieeklknlgaeivq
dglridgdpraarddivgwahdvrgai
>d1aky_1 3.30.1.1.11 (3-130,169-220) Adenylate kinase {Baker's yeast (Saccharomyces cerevisiae)}
esirmvligppgagkgtqapnlqerfhaahlatgdmlrsqiakgtqlgleakkimdqggl
vsddimvnmikdeltnnpackngfildgfprtipqaekldqmlkeqgtplekaielkvdd
ellvaritXnadalkkrlaayhaqtepivdfykktgiwagvdasqppatvwadilnklgk
n
>d1aky_2 7.35.2.1.5 (131-168) Microbial and mitochondrial ADK, insert "zinc finger" domain {Baker's yeast (Saccharomyces cerevisiae)}
grlihpasgrsyhkifnppkedmkddvtgealvqrsdd
>d1akz__ 3.14.1.1.1 Uracil-DNA glycosylase {Human (Homo sapiens)}
meffgeswkkhlsgefgkpyfiklmgfvaeerkhytvyppphqvftwtqmcdikdvkvvi
lgqdpyhgpnqahglcfsvqrpvppppsleniykelstdiedfvhpghgdlsgwakqgvl
llnavltvrahqanshkergweqftdavvswlnqnsnglvfllwgsyaqkkgsaidrkrh
hvlqtahpsplsvyrgffgcrhfsktnellqksgkkpidwkel
>d1al01_ 1.81.1.1.1 Scaffolding protein gpD of bacteriophage procapsid {Bacteriophage phi-x174}
eqsvrfqtalasikliqasavldlteddfdfltsnkvwiatdrsrarrcveacvygtldf
vgyprfpapvefiaaviayyvhpvniqtaclimegaefteniingverpvkaaelfaftl
rvragntdvltdaeenvrqklra
>d1al02_ 1.81.1.1.1 Scaffolding protein gpD of bacteriophage procapsid {Bacteriophage phi-x174}
eqsvrfqtalasikliqasavldlteddfdfltsnkvwiatdrsrarrcveacvygtldf
vgyprfpapvefiaaviayyvhpvniqtaclimegaefteniingverpvkaaelfaftl
rvragntdvltda
>d1al03_ 1.81.1.1.1 Scaffolding protein gpD of bacteriophage procapsid {Bacteriophage phi-x174}
teqsvrfqtalasikliqasavldlteddfdfltsnkvwiatdrsrarrcveacvygtld
fvgyprfpapvefiaaviayyvhpvniqtaclimegaefteniingverpvkaaelfaft
lrvragntdvltdaeenvrq
>d1al04_ 1.81.1.1.1 Scaffolding protein gpD of bacteriophage procapsid {Bacteriophage phi-x174}
qsvrfqtalasikliqasavldlteddfdfltsnkvwiatdrsrarrcveacvygtldfv
gyprfpapvefiaaviayyvhpvniqtaclimegaefteniingverpvkaaelfaftlr
vragntdvltdaeenvrqklraegvm
>d1al0f_ 2.9.1.1.1 Bacteriophage capsid proteins {Bacteriophage phiX174}
qtgaermphdlshlgflagqigrlitisttpviagdsfemdavgalrlsplrrglaidst
vdiftfyvphrhvygeqwikfmkdgvnatplptvnttgyidhaaflgtinpdtnkipkhl
fqgylniynnyfkapwmpdrteanpnelnqddarygfrcchlkniwtaplppetelsrqm
ttsttsidimglqaayanlhtdqerdyfmqryrdvissfggktsydadnrpllvmrsnlw
asgydvdgtdqtslgqfsgrvqqtykhsvprffvpehgtmftlalvrfpptatkeiqyln
akgaltytdiagdpvlygnlppreismkdvfrsgdsskkfkiaegqwyryapsyvspayh
llegfpfiqeppsgdlqervlirhhdydqcfqsvqllqwnsqvkfnvtvyrnlpttrd
>d1al0g_ 2.9.1.1.1 Bacteriophage capsid proteins {Bacteriophage phiX174}
mfqtfisrhnsnffsdklvltsvtpassapvlqtpkatsstlyfdsltvnagnggflhci
qmdtsvnaanqvvsvgadiafdadpkffaclvrfesssvpttlptaydvyplngrhdggy
ytvkdcvtidvlprtpgnnvyvgfmvwsnftatkcrglvslnqvikeiiclqplk
>d1al21_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
aatsrdalpnteasgpthskeipaltavetgatnplvpsdtvqtrhvvqhrsrsessies
ffargacvtimtvdnpasttnkdklfavwkitykdtvqlrrklefftysrfdmeltfvvt
anftetnnghalnqvyqimyippgapvpekwddytwqtssnpsifytygtaparisvpyv
gisnayshfydgfskvplkdqsaalgdslygaaslndfgilavrvvndhnptkvtskirv
ylkpkhirvwcprppravayygpgvdykdgtltplstkdltty
>d1al22_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
eacgysdrvlqltlgnstittqeaansvvaygrwpeylrdseanpvdqptepdvaacrfy
tldtvswtkesrgwwwklpdalrdmglfgqnmyyhylgrsgytvhvqcnaskfhqgalgv
favpemclagdsntttmhtsyqnanpgekggtftgtftpdnnqtsparrfcpvdyllgng
tllgnafvfphqiinlrtnncatlvlpyvnslsidsmvkhnnwgiailplaplnfasess
peipitltiapmccefnglrnitlprlq
>d1al23_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
glpvmntpgsnqyltadnfqspcalpefdvtppidipgevknmmelaeidtmipfdlsat
kkntmemyrvrlsdkphtddpilclslspasdprlshtmlgeilnyythwagslkftflf
cgsmmatgkllvsyappgadppkkrkeamlgthviwdiglqssctmvvpwisnttyrqti
ddsfteggyisvfyqtrivvplstpremdilgfvsacndfsvrllrdtthieqka
>d1al3__ 3.84.1.1.18 Cofactor-binding fragment of CysB {Klebsiella aerogenes}
twpdkgslyvatthtqaryalpgvikgfieryprvslhmhqgsptqiaeavskgnadfai
atealhlyddlvmlpcyhwnrsivvtpehplatkgsvsieelaqyplvtytfgftgrsel
dtafnragltprivftatdadviktyvrlglgvgviasmavdpvsdpdlvkldangifsh
sttkigfrrstflrsymydfiqrfaphltrdvvdtavalrsnedieamfkdiklpek
>d1al6__ 1.99.1.1.1 Citrate synthase {Chicken (Gallus gallus)}
stnlkdvlaslipkeqariktfrqqhgntavgqitvdmsyggmrgmkgliyetsvldpde
girfrgfsipecqkllpkagggeeplpeglfwllvtgqiptpeqvswvskewakraalps
hvvtmldnfptnlhpmsqlsaaitalnsesnfarayaeginrtkywefvyedamdliakl
pcvaakiyrnlyragssigaidskldwshnftnmlgytdpqftelmrlyltihsdheggn
vsahtshlvgsalsdpylsfaaamnglagplhglanqevllwlsqlqkdlgadasdeklr
dyiwntlnsgrvvpgyghavlrktdprytcqrefalkhlpsdpmfklvaqlykivpnvll
eqgkaknpwpnvdahsgvllqyygmtemnyytvlfgvsralgvlaqliwsralgfplerp
ksmstagleklsagg
>d1al7__ 3.1.4.1.4 Glycolate oxidase {Spinach (Spinacia oleracea)}
meitnvneyeaiakqklpkmvydyyasgaedqwtlaenrnafsrilfrprilidvtnidm
tttilgfkismpimiaptamqkmahpegeyataraasaagtimtlsswatssveevastg
pgirffqlyvykdrnvvaqlvrraeragfkaialtvdtprlgrreadiknrfvlppfltl
knfegidlgkmdkandsglssyvagqidrslswkdvawlqtitslpilvkgvitaedarl
avqhgaagiivsnhgarqldyvpatimaleevvkaaqgripvfldggvrrgtdvfkalal
gaagvfigrpvvfslaaegeagvkkvlqmmrdefeltmalsgcrslkeisrshiaadwd
>d1al8__ 3.1.4.1.4 Glycolate oxidase {Spinach (Spinacia oleracea)}
meitnvneyeaiakqklpkmvydyyasgaedqwtlaenrnafsrilfrprilidvtnidm
tttilgfkismpimiaptamqkmahpegeyataraasaagtimtlsswatssveevastg
pgirffqlyvykdrnvvaqlvrraeragfkaialtvdtprlgrreadiknrfvlppfltl
knfegidlgkmdkandsglssyvagqidrslswkdvawlqtitslpilvkgvitaedarl
avqhgaagiivsnhgarqldyvpatimaleevvkaaqgripvfldggvrrgtdvfkalal
gaagvfigrpvvfslaaegeagvkkvlqmmrdefeltmalsgcrslkeisrshiaadwd
>d1ala__ 1.66.1.1.4 Annexin V {Chicken (Gallus gallus)}
kytrgtvtafspfdaradaealrkamkgmgtdeetilkiltsrnnaqrqeiasafktlfg
rdlvddlkseltgkfetlmvslmrparifdahalkhaikgagtnekvlteilasrtpaev
qnikqvymqeyeanledkitgetsghfqrllvvllqanrdpdgrveealvekdaqvlfra
gelkwgtdeetfitilgtrsvshlrrvfdkymtisgfqieetidretsgdleklllavvk
cirsvpayfaetlyysmkgagtdddtlirvmvsrseidlldirhefrknfakslyqmiqk
dtsgdyrkallllcgg
>d1alb__ 2.53.1.2.6 Adipocyte lipid-binding protein, ALBP {Mouse (Mus musculus)}
cdafvgtwklvssenfddymkevgvgfatrkvagmakpnmiisvngdlvtirsestfknt
eisfklgvefdeitaddrkvksiitldggalvqvqkwdgksttikrkrdgdklvvecvmk
gvtstrvyera
>d1alc__ 4.2.1.2.13 alpha-Lactalbumin {Baboon (Papio cynocephalus)}
kqftkcelsqnlydidgygrialpelictmfhtsgydtqaivendesteyglfqisnalw
ckssqspqsrnicditcdkflddditddimcakkildikgidywiahkalctekleqwlc
ek
>d1ald__ 3.1.9.1.3 Fructose-1,6-bisphosphate aldolase {Human (Homo sapiens)}
pyqypaltpeqkkelsdiahrivapgkgilaadestgsiakrlqsigtenteenrrfyrq
llltaddrvnpciggvilfhetlyqkaddgrpfpqvikskggvvgikvdkgvvplagtng
etttqgldglsercaqykkdgadfakwrcvlkigehtpsalaimenanvlaryasicqqn
givpivepeilpdgdhdlkrcqyvtekvlaavykalsdhhiylegtllkpnmvtpghact
qkfsheeiamatvtalrrtvppavtgitflsggqseeeasinlnainkcpllkpwaltfs
ygralqasalkawggkkenlkaaqeeyvkralanslacqgkytpsgqagaaaseslfvsn
hay
>d1alha_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
mpvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseitaarn
yaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngalgvd
ihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpgnal
ekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaeargyqlvsdaasl
nsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptlaqmt
dkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkegntl
vivtanhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlriaayg
phaanvvgltdqtdlfytmkaalglk
>d1alhb_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
mpvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseitaarn
yaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngalgvd
ihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpgnal
ekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaeargyqlvsdaasl
nsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptlaqmt
dkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkegntl
vivtanhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlriaayg
phaanvvgltdqtdlfytmkaalglk
>d1alia_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
mpvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseitaarn
yaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngalgvd
ihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpgnal
ekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsdaasl
nsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptlaqmt
dkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkegntl
vivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqentgsqlriaayg
phaanvvgltdqtdlfytmkaalglk
>d1alib_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
mpvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseitaarn
yaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngalgvd
ihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpgnal
ekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsdaasl
nsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptlaqmt
dkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkegntl
vivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqentgsqlriaayg
phaanvvgltdqtdlfytmkaalglk
>d1alja_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
mpvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseitaarn
yaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngalgvd
ihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpgnal
ekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsdaasl
nsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptlaqmt
dkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkegntl
vivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqentgsqlriaayg
phaanvvgltdqtdlfytmkaalglk
>d1aljb_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
mpvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseitaarn
yaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngalgvd
ihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpgnal
ekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsdaasl
nsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptlaqmt
dkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkegntl
vivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqentgsqlriaayg
phaanvvgltdqtdlfytmkaalglk
>d1alka_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgnitapggarrltgdqtaalrnslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsqkcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreeaeargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1alkb_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgnitapggarrltgdqtaalrnslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsqkcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreeaeargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1alla_ 1.1.1.2.3 Allophycocyanin {Spirulina platensis}
sivtksivnadaearylspgeldriksfvtsgerrvriaetmtgareriikqagdqlfgk
rpdvvspggnaygadmtatclrdldyylrlitygivagdvtpieeigvvgvremykslgt
pieaiaegvramksvatsllsgadaaeagsyfdyligams
>d1allb_ 1.1.1.2.3 Allophycocyanin {Spirulina platensis}
mqdaitsvinssdvqgkyldasaiqklkayfatgelrvraattisanaanivkeavaksl
lysdvtrpggnmyttrryaacirdldyylryatyamlagdpsildervlnglketynslg
vpigatvqaiqamkevtaglvgggagkemgiyfdyicsgls
>d1aln_1 3.87.1.1.1 (1-150) Cytidine deaminase {Escherichia coli}
mhprfqtafaqladnlqsalepiladkyfpalltgeqvsslksatgldedalafallpla
aacartplsnfnvgaiargvsgtwyfganmefigatmqqtvhaeqsaishawlsgekala
aitvnytpcghcrqfmnelnsgldlrihlp
>d1aln_2 3.87.1.1.1 (151-294) Cytidine deaminase {Escherichia coli}
greahalrdylpdafgpkdleiktllmdeqdhgyaltgdalsqaaiaaanrshmpysksp
sgvaleckdgrifsgsyaenaafnptlpplqgalillnlkgydypdiqravlaekadapl
iqwdatsatlkalgchsidrvlla
>d1alo_1 1.58.1.1.1 (81-193) Aldehyde oxidoreductase, domain 2 {Desulfovibrio gigas}
qpenlhplqkawvlhggaqcgfcspgfivsakglldtnadpsredvrdwfqkhrnacrct
gykplvdavmdaaavingkkpetdlefkmpadgriwgskyprptavakvtgtl
>d1alo_2 4.13.6.2.2 (1-80) Aldehyde oxidoreductase, N-terminal domain {Desulfovibrio gigas}
miqkvitvngieqnlfvdaeallsdvlrqqlgltgvkvgceqgqcgacsvildgkvvrac
vtkmkrvadgaqittiegvg
>d1alo_3 4.34.1.1.1 (194-310) Aldehyde oxidoreductase, domain 3 {Desulfovibrio gigas}
dygadlglkmpagtlhlamvqakvshanikgidtsealtmpgvhsvithkdvkgknritg
litfptnkgdgwdrpilcdekvfqygdcialvcadseanaraaaekvkvdleelpay
>d1alo_4 4.107.1.1.1 (311-907) Aldehyde oxidoreductase {Desulfovibrio gigas}
msgpaaaaedaieihpgtpnvyfeqpivkgedtgpifasadvtvegdfyvgrqphmpiep
dvafaymgddgkcyihsksigvhlhlymiapgvglepdqlvlvanpmggtfgykfsptse
alvavaamatgrpvhlrynyqqqqqytgkrspwemnvkfaakkdgtllamesdwlvdhgp
ysefgdlltlrgaqfigagynipnirglgrtvatnhvwgsafrgygapqsmfaseclmdm
laeklgmdplelryknayrpgdtnptgqepevfslpdmidqlrpkyqaalekaqkestat
hkkgvgisigvygsgldgpdaseawaelnadgtitvhtawedhgqgadigcvgtahealr
pmgvapekikftwpntattpnsgpsggsreqvmtgnairvacenllkacekpgggyytyd
elkaadkptkitgnwtasgathcdavtglgkpfvvymygvfmaevtvdvatgqttvdgmt
lmadlgslcnqlatdgqiygglaqgiglalsedfedikkhatlvgagfpfikqipdkldi
vyvnhprpdgpfgasgvgelpltsphaaiinaiksatgvriyrlpaypekvlealka
>d1alq__ 5.3.1.1.6 beta-Lactamase, class A {Staphylococcus aureus}
sepivlviftnkdnksdkpndklisetaksvmkefaagsknaakelndlekkynahigvy
aldtksgkevkfnsdkrfayastskainsailleqvpynklnkkvhinkddivayspile
kyvgkditlkalieasmtysdntannkiikeiggikkvkqrlkelgdkvtnpvryeieln
yyspkskkdtstpaafgktlnkliangklskenkkflldlmlnnksgdtlikdgvpkdyk
vadksgqaityasrndvafvypk
>d1alu__ 1.27.1.1.4 Interleukin-6 {Human (Homo sapiens)}
ltsseridkqiryildgisalrketcnksnmcesskealaennlnlpkmaekdgcfqsgf
neetclvkiitgllefevyleylqnrfesseeqaravqmstkvliqflqkkaknldaitt
pdpttnaslltklqaqnqwlqdmtthlilrsfkeflqsslralrqm
>d1alva_ 1.42.1.7.3 Calpain domain VI {Pig (Sus scrofa)}
eevrqfrrlfaqlagddmevsatelmnilnkvvtrhpdlktdgfgidtcrsmvavmdsdt
tgklgfeefkylwnnikkwqaiykqfdvdrsgtigsselpgafeaagfhlnehlysmiir
rysdeggnmdfdnfisclvrldamfrafksldkdgtgqiqvniqewlqltmys
>d1alvb_ 1.42.1.7.3 Calpain domain VI {Pig (Sus scrofa)}
eevrqfrrlfaqlagddmevsatelmnilnkvvtrhpdlktdgfgidtcrsmvavmdsdt
tgklgfeefkylwnnikkwqaiykqfdvdrsgtigsselpgafeaagfhlnehlysmiir
rysdeggnmdfdnfisclvrldamfrafksldkdgtgqiqvniqewlqltmys
>d1alwa_ 1.42.1.7.3 Calpain domain VI {Pig (Sus scrofa)}
eevrqfrrlfaqlagddmevsatelmnilnkvvtrhpdlktdgfgidtcrsmvavmdsdt
tgklgfeefkylwnnikkwqaiykqfdvdrsgtigsselpgafeaagfhlnehlysmiir
rysdeggnmdfdnfisclvrldamfrafksldkdgtgqiqvniqewlqltmys
>d1alwb_ 1.42.1.7.3 Calpain domain VI {Pig (Sus scrofa)}
eevrqfrrlfaqlagddmevsatelmnilnkvvtrhpdlktdgfgidtcrsmvavmdsdt
tgklgfeefkylwnnikkwqaiykqfdvdrsgtigsselpgafeaagfhlnehlysmiir
rysdeggnmdfdnfisclvrldamfrafksldkdgtgqiqvniqewlqltmys
>d1aly__ 2.20.1.1.1 Extracellular domain of CD40 ligand {Human (Homo sapiens)}
gdqnpqiaahviseasskttsvlqwaekgyytmsnnlvtlengkqltvkrqglyyiyaqv
tfcsnreassqapfiaslclkspgrferillraanthssakpcgqqsihlggvfelqpga
svfvnvtdpsqvshgtgftsfgllkl
>d1am1__ 4.96.1.1.1 HSP90 {Baker's yeast (Saccharomyces cerevisiae)}
asetfefqaeitqlmsliintvysnkeiflrelisnasdaldkirykslsdpkqletepd
lfiritpkpeqkvleirdsgigmtkaelinnlgtiaksgtkafmealsagadvsmigqfg
vgfyslflvadrvqvisksnddeqyiwesnaggsftvtldevnerigrgtilrlflkddq
leyleekrikevikrhsefvaypiqlvvtkeve
>d1am2__ 2.76.1.2.2 GyrA intein {Mycobacterium xenopi}
asitgdalvalpegesvriadivpgarpnsdnaidlkvldrhgnpvladrlfhsgehpvy
avrtveglrvtgtanhpllclvdvagvptllwklideikpgdyaviqrsafsvdcagfar
gkpefapttytvgvpglvrfleahhrdpdakaiadeltdgrfyyakvasvtdagvqpvys
lrvdtadhafitngfvshn
>d1am4a_ 1.108.1.1.1 p50 RhoGAP domain {Human (Homo sapiens)}
prpplpnqqfgvslqhlqeknpeqepipivlretvaylqahalttegifrrsantqvvre
vqqkynmglpvdfdqynelhlpavilktflrelpeplltfdlyphvvgflnidesqrvpa
tlqvlqtlpeenyqvlrfltaflvqisahsdqnkmtntnlavvfgpnllwakdaaitlka
inpintftkflldhqgelf
>d1am4b_ 1.108.1.1.1 p50 RhoGAP domain {Human (Homo sapiens)}
prpplpnqqfgvslqhlqeknpeqepipivlretvaylqahalttegifrrsantqvvre
vqqkynmglpvdfdqynelhlpavilktflrelpeplltfdlyphvvgflnidesqrvpa
tlqvlqtlpeenyqvlrfltaflvqisahsdqnkmtntnlavvfgpnllwakdaaitlka
inpintftkflldhqgelf
>d1am4c_ 1.108.1.1.1 p50 RhoGAP domain {Human (Homo sapiens)}
prpplpnqqfgvslqhlqeknpeqepipivlretvaylqahalttegifrrsantqvvre
vqqkynmglpvdfdqynelhlpavilktflrelpeplltfdlyphvvgflnidesqrvpa
tlqvlqtlpeenyqvlrfltaflvqisahsdqnkmtntnlavvfgpnllwakdaaitlka
inpintftkflldhqgelf
>d1am4d_ 3.30.1.6.11 CDC42 {Human (Homo sapiens)}
pqtikcvvvgdgavgktcllisyttnkfpseyvptvfdnyavtvmiggepytlglfdtag
qedydrlrplsypqtdvflvcfsvvspssfenvkekwvpeithhcpktpfllvgtqidlr
ddpstieklaknkqkpitpetaeklardlkavkyvecsaltqrglknvfdeailaal
>d1am4e_ 3.30.1.6.11 CDC42 {Human (Homo sapiens)}
pqtikcvvvgdgavgktcllisyttnkfpseyvptvfdnyavtvmiggepytlglfdtag
qedydrlrplsypqtdvflvcfsvvspssfenvkekwvpeithhcpktpfllvgtqidlr
ddpstieklaknkqkpitpetaeklardlkavkyvecsaltqrglknvfdeailaal
>d1am4f_ 3.30.1.6.11 CDC42 {Human (Homo sapiens)}
pqtikcvvvgdgavgktcllisyttnkfpseyvptvfdnyavtvmiggepytlglfdtag
qedydrlrplsypqtdvflvcfsvvspssfenvkekwvpeithhcpktpfllvgtqidlr
ddpstieklaknkqkpitpetaeklardlkavkyvecsaltqrglknvfdeailaal
>d1am5__ 2.44.1.2.12 Pepsin(ogen) {Atlantic cod (Gadus morhua)}
rvteqmkneadteyygvisigtppesfkvifdtgssnlwvssshcsaqacsnhnkfkprq
sstyvetgktvdltygtggmrgilgqdtvsvgggsdpnqelgesqtepgpfqaaapfdgi
lglaypsiaaagavpvfdnmgsqslvekdlfsfylsgggangsevmlggvdnshytgsih
wipvtaekywqvaldgitvngqtaacegcqaivdtgtskivapvsalanimkdigasenq
gemmgncasvqslpditftingvkqplppsayiegdqafctsglgssgvpsntselwifg
dvflrnyytiydrtnnkvgfapaa
>d1am6__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnn
ghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvh
wntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprg
llpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvd
nwrpaqplknrqikasfk
>d1am7a_ 4.2.1.4.1 Lambda lysozyme {Bacteriophage lambda}
mveinnqrkafldmlaxsegtdngrqktrnhgydvivggelftdysdhprklvtlnpklk
stgagryqllsrxxdayrkqlglkdfspksqdavalqqikergalpmidrgdirqaidrc
snixaslpgagygqfehkadsliakfkeaggtvr
>d1am7b_ 4.2.1.4.1 Lambda lysozyme {Bacteriophage lambda}
mveinnqrkafldmlaxsegtdngrqktrnhgydvivggelftdysdhprklvtlnpklk
stgagryqllsrxxdayrkqlglkdfspksqdavalqqikergalpmidrgdirqaidrc
snixaslpgagygqfehkadsliakfkeaggtvr
>d1am7c_ 4.2.1.4.1 Lambda lysozyme {Bacteriophage lambda}
mveinnqrkafldmlaxsegtdngrqktrnhgydvivggelftdysdhprklvtlnpklk
stgagryqllsrxxdayrkqlglkdfspksqdavalqqikergalpmidrgdirqaidrc
snixaslpgagygqfehkadsliakfkeaggtvr
>d1am9a_ 1.41.1.1.6 SREBP-1a {Human (Homo sapiens)}
qsrgekrtahnaiekryrssindkiielkdlvvgteaklnksavlrkaidyirflqhsnq
klkqenlslrtavhkskslk
>d1am9b_ 1.41.1.1.6 SREBP-1a {Human (Homo sapiens)}
srgekrtahnaiekryrssindkiielkdlvvgteaklnksavlrkaidyirflqhsnqk
lkqenlslrtavhks
>d1am9c_ 1.41.1.1.6 SREBP-1a {Human (Homo sapiens)}
qsrgekrtahnaiekryrssindkiielkdlvvgteaklnksavlrkaidyirflqhsnq
klkqenlslrtavhkskslkdl
>d1am9d_ 1.41.1.1.6 SREBP-1a {Human (Homo sapiens)}
qsrgekrtahnaiekryrssindkiielkdlvvgteaklnksavlrkaidyirflqhsnq
klkqenlslrtavhks
>d1ama__ 3.57.1.1.1 Aspartate aminotransferase, AAT {Chicken (Gallus gallus), mitochondria}
sswwshvemgppdpilgvteafkrdtnskkmnlgvgayrddngkpyvlncvrkaeamiaa
kkmdkeylpiagladftrasaelalgenseafksgryvtvqgisgtgslrvganflqrff
kfsrdvylpkpswgnhtpifrdaglqlqayryydpktcsldftgamediskipeksiill
hacahnptgvdprqeqwkelasvvkkrnllayfdmayqgfasgdinrdawalrhfieqgi
dvvlsqsyaknmglygeragaftvicrdaeeakrvesqlkilirpmysnppmngariasl
ilntpelrkewlvevkgmadriismrtqlvsnlkkegsshnwqhitdqigmfcftglkpe
qverltkefsiymtkdgrisvagvassnvgylahaihqvtk
>d1ame__ 2.75.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
anqasvvanqlipintaltlvmmrsevvtpvgipaediprlvsmqvnravplgttlmpdm
vkgyaa
>d1amf__ 3.84.1.1.16 Molybdate-binding protein, ModA {Escherichia coli}
gkitvfaaasltnamqdiatqfkkekgvdvvssfassstlarqieagapadlfisadqkw
mdyavdkkaidtatrqtllgnslvvvapkasvqkdftidsktnwtsllnggrlavgdpeh
vpagiyakealqklgawdtlspklapaedvrgalalverneaplgivygsdavaskgvkv
vatfpedshkkveypvavveghnnatvkafydylkgpqaaeifkrygftik
>d1amha_ 2.41.1.2.3 Trypsin(ogen) {Rat (Rattus rattus)}
ivggytcqensvpyqvslnsgyhfcggslindqwvvsaahcyksriqvrlgehninvleg
neqfvnaakiikhpnfdrktlnndimliklsspvklnarvatvalpsscapagtqclisg
wgntlssgvnepdllqcldapllpqadceasypgkitdnmvcvgfleggksscqgdsggp
vvcngelqgivswgygcalpdnpgvytkvcnyvdwiqdtiaan
>d1amhb_ 2.41.1.2.3 Trypsin(ogen) {Rat (Rattus rattus)}
ivggytcqensvpyqvslnsgyhfcggslindqwvvsaahcyksriqvrlgehninvleg
neqfvnaakiikhpnfdrktlnndimliklsspvklnarvatvalpsscapagtqclisg
wgntlssgvnepdllqcldapllpqadceasypgkitdnmvcvgfleggksscqgdsggp
vvcngelqgivswgygcalpdnpgvytkvcnyvdwiqdtiaan
>d1ami_1 3.7.2.1.2 (529-754) Aconitase, C-terminal domain {Bovine (Bos taurus)}
vdvsptsqrlqllepfdkwdgkdledlqilikvkgkcttdhisaagpwlkfrghldnisn
nlligainsenrkansvrnavtqefgpvpdtaryykqhgirwvvigdenygegssrehsa
leprflggraiitksfarihetnlkkqgllpltfadpadynkihpvdkltiqglkdfapg
kpltciikhpngtqetillnhtfnetqiewfragsalnrmkelqqk
>d1ami_2 3.72.1.1.2 (2-528) Aconitase, first 3 domains {Bovine (Bos taurus)}
rakvamshfepheyirydlleknidivrkrlnrpltlsekivyghlddpanqeiergkty
lrlrpdrvamqdataqmamlqfissglpkvavpstihcdhlieaqlggekdlrrakdinq
evynflatagakygvgfwrpgsgiihqiilenyaypgvlligtdshtpnggglggicigv
ggadavdvmagipwelkcpkvigvkltgslsgwtspkdvilkvagiltvkggtgaiveyh
gpgvdsisctgmaticnmgaeigattsvfpynhrmkkylsktgradianladefkdhlvp
dsgchydqlieinlselkphingpftpdlahpvaevgsvaekegwpldirvgligsctns
syedmgrsaavakqalahglkcksqftitpgseqiratierdgyaqvlrdvggivlanac
gpcigqwdrkdikkgekntivtsynrnftgrndanpethafvtspeivtalaiagtlkfn
petdfltgkdgkkfkleapdadelpraefdpgqdtyqhppkdssgqr
>d1amj_1 3.7.2.1.2 (529-754) Aconitase, C-terminal domain {Bovine (Bos taurus)}
vdvsptsqrlqllepfdkwdgkdledlqilikvkgkcttdhisaagpwlkfrghldnisn
nlligainsenrkansvrnavtqefgpvpdtaryykqhgirwvvigdenygegssrehsa
leprflggraiitksfarihetnlkkqgllpltfadpadynkihpvdkltiqglkdfapg
kpltciikhpngtqetillnhtfnetqiewfragsalnrmkelqqk
>d1amj_2 3.72.1.1.2 (2-528) Aconitase, first 3 domains {Bovine (Bos taurus)}
rakvamshfepheyirydlleknidivrkrlnrpltlsekivyghlddpanqeiergkty
lrlrpdrvamqdataqmamlqfissglpkvavpstihcdhlieaqlggekdlrrakdinq
evynflatagakygvgfwrpgsgiihqiilenyaypgvlligtdshtpnggglggicigv
ggadavdvmagipwelkcpkvigvkltgslsgwtspkdvilkvagiltvkggtgaiveyh
gpgvdsisctgmaticnmgaeigattsvfpynhrmkkylsktgradianladefkdhlvp
dsgchydqlieinlselkphingpftpdlahpvaevgsvaekegwpldirvgligsctns
syedmgrsaavakqalahglkcksqftitpgseqiratierdgyaqvlrdvggivlanac
gpcigqwdrkdikkgekntivtsynrnftgrndanpethafvtspeivtalaiagtlkfn
petdfltgkdgkkfkleapdadelpraefdpgqdtyqhppkdssgqr
>d1amk__ 3.1.1.1.7 Triosephosphate isomerase {Leishmania mexicana}
sakpqpiaaanwkcngttasieklvqvfnehtishdvqcvvaptfvhiplvqaklrnpky
visaenaiaksgaftgevsmpilkdigvhwvilghserrtyygetdeivaqkvseackqg
fmviacigetlqqreanqtakvvlsqtsaiaakltkdawnqvvlayepvwaigtgkvatp
eqaqevhlllrkwvsenigtdvaaklrilyggsvnaanaatlyakpdingflvggaslkp
efrdiidatr
>d1amm_1 2.10.1.1.1 (1-85) gamma-Crystallin {Bovine (Bos taurus), isoform II (B)}
gkitfyedrgfqghcyecssdcpnlqpyfsrcnsirvdsgcwmlyerpnyqghqyflrrg
dypdyqqwmgfndsirscrlipqht
>d1amm_2 2.10.1.1.1 (86-174) gamma-Crystallin {Bovine (Bos taurus), isoform II (B)}
gtfrmriyerddfrgqmseitddcpslqdrfhltevhslnvlegswvlyempsyrgrqyl
lrpgeyrryldwgamnakvgslrrvmdfy
>d1amn__ 3.59.1.1.1 Acetylcholinesterase {Electric ray (Torpedo californica)}
sellvntksgkvmgtrvpvlsshisaflgipfaeppvgnmrfrrpepkkpwsgvwnasty
pnncqqyvdeqfpgfsgsemwnpnremsedclylniwvpsprpksttvmvwiygggfysg
sstldvyngkylayteevvlvslsyrvgafgflalhgsqeapgnvglldqrmalqwvhdn
iqffggdpktvtifgesaggasvgmhilspgsrdlfrrailqsgspncpwasvsvaegrr
ravelgrnlncnlnsdeelihclrekkpqelidvewnvlpfdsifrfsfvpvidgeffpt
slesmlnsgnfkktqillgvnkdegsffllygapgfskdseskisredfmsgvklsvpha
ndlgldavtlqytdwmddnngiknrdglddivgdhnvicplmhfvnkytkfgngtylyff
nhrasnlvwpewmgvihgyeiefvfglplvkelnytaeeealsrrimhywatfaktgnpn
eskwplfttkeqkfidlntepmkvhqrlrvqmcvfwnqflpkllna
>d1amoa1 2.38.1.4.1 (243-518) NADPH-cytochrome p450 reductase {Rat (Rattus norvegicus)}
rqyelvvhedmdvakvytgemgrlksyenqkppfdaknpflaavtanrklnqgterhlmh
leldisdskiryesgdhvavypandsalvnqigeilgadldvimslnnldeesnkkhpfp
cpttyrtaltyylditnpprtnvlyelaqyasepseqehlhkmasssgegkelylswvve
arrhilailqdypslrppidhlcellprlqaryysiassskvhpnsvhicavaveyeaks
grvnkgvatswlrakepagenggralvpmfvrksqf
>d1amoa2 3.16.4.2.1 (64-235) NADPH-cytochrome p450 reductase, N-terminal domain {Rat (Rattus norvegicus)}
vkessfvekmkktgrniivfygsqtgtaeefanrlskdahrygmrgmsadpeeydladls
slpeidkslvvfcmatygegdptdnaqdfydwlqetdvdltgvkfavfglgnktyehfna
mgkyvdqrleqlgaqrifelglgdddgnleedfitwreqfwpavceffgvea
>d1amoa3 3.18.1.3.1 (519-678) NADPH-cytochrome p450 reductase {Rat (Rattus norvegicus)}
rlpfksttpvimvgpgtgiapfmgfiqerawlreqgkevgetllyygcrrsdedylyree
larfhkdgaltqlnvafsreqahkvyvqhllkrdrehlwkliheggahiyvcgdarnmak
dvqntfydivaefgpmehtqavdyvkklmtkgrysldvws
>d1amob1 2.38.1.4.1 (243-518) NADPH-cytochrome p450 reductase {Rat (Rattus norvegicus)}
rqyelvvhedmdvakvytgemgrlksyenqkppfdaknpflaavtanrklnqgterhlmh
leldisdskiryesgdhvavypandsalvnqigeilgadldvimslnnldeesnkkhpfp
cpttyrtaltyylditnpprtnvlyelaqyasepseqehlhkmasssgegkelylswvve
arrhilailqdypslrppidhlcellprlqaryysiassskvhpnsvhicavaveyeaks
grvnkgvatswlrakepagenggralvpmfvrksqf
>d1amob2 3.16.4.2.1 (64-235) NADPH-cytochrome p450 reductase, N-terminal domain {Rat (Rattus norvegicus)}
vkessfvekmkktgrniivfygsqtgtaeefanrlskdahrygmrgmsadpeeydladls
slpeidkslvvfcmatygegdptdnaqdfydwlqetdvdltgvkfavfglgnktyehfna
mgkyvdqrleqlgaqrifelglgdddgnleedfitwreqfwpavceffgvea
>d1amob3 3.18.1.3.1 (519-678) NADPH-cytochrome p450 reductase {Rat (Rattus norvegicus)}
rlpfksttpvimvgpgtgiapfmgfiqerawlreqgkevgetllyygcrrsdedylyree
larfhkdgaltqlnvafsreqahkvyvqhllkrdrehlwkliheggahiyvcgdarnmak
dvqntfydivaefgpmehtqavdyvkklmtkgrysldvws
>d1amp__ 3.47.4.4.1 Aminopeptidase {Aeromonas proteolytica}
mppitqqatvtawlpqvdasqitgtisslesftnrfytttsgaqasdwiasewqalsasl
pnasvkqvshsgynqksvvmtitgseapdewivigghldstigshtneqsvapgadddas
giaavtevirvlsennfqpkrsiafmayaaeevglrgsqdlanqyksegknvvsalqldm
tnykgsaqdvvfitdytdsnftqyltqlmdeylpsltygfdtcgyacsdhaswhnagypa
ampfeskfndynprihttqdtlansdptgshakkftqlglayaiemgsatg
>d1amq__ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1amr__ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ams__ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1amua_ 5.19.1.1.2 Phenylalanine activating domain of gramicidin synthetase 1 {Bacillus brevis}
gtheeeqylfavnntkaeyprdktihqlfeeqvskrpnnvaivceneqltyhelnvkanq
larifiekgigkdtlvgimmeksidlfigilavlkaggayvpidieypkeriqyilddsq
armlltqkhlvhlihniqfngqveifeedtikiregtnlhvpskstdlayviytsgttgn
pkgtmlehkgisnlkvffenslnvtekdrigqfasisfdasvwemfmalltgaslyiilk
dtindfvkfeqyinqkeitvitlpptyvvhldperilsiqtlitagsatspslvnkwkek
vtyinaygptetticattwvatketighsvpigapiqntqiyivdenlqlksvgeagelc
iggeglargywkrpeltsqkfvdnpfvpgeklyktgdqarwlsdgnieylgridnqvkir
ghrveleevesillkhmyisetavsvhkdhqeqpylcayfvsekhipleqlrqfsseelp
tymipsyfiqldkmpltsngkidrkqlpepdltf
>d1amub_ 5.19.1.1.2 Phenylalanine activating domain of gramicidin synthetase 1 {Bacillus brevis}
gtheeeqylfavnntkaeyprdktihqlfeeqvskrpnnvaivceneqltyhelnvkanq
larifiekgigkdtlvgimmeksidlfigilavlkaggayvpidieypkeriqyilddsq
armlltqkhlvhlihniqfngqveifeedtikiregtnlhvpskstdlayviytsgttgn
pkgtmlehkgisnlkvffenslnvtekdrigqfasisfdasvwemfmalltgaslyiilk
dtindfvkfeqyinqkeitvitlpptyvvhldperilsiqtlitagsatspslvnkwkek
vtyinaygptetticattwvatketighsvpigapiqntqiyivdenlqlksvgeagelc
iggeglargywkrpeltsqkfvdnpfvpgeklyktgdqarwlsdgnieylgridnqvkir
ghrveleevesillkhmyisetavsvhkdhqeqpylcayfvsekhipleqlrqfsseelp
tymipsyfiqldkmpltsngkidrkqlpepdltf
>d1amw__ 4.96.1.1.1 HSP90 {Baker's yeast (Saccharomyces cerevisiae)}
asetfefqaeitqlmsliintvysnkeiflrelisnasdaldkirykslsdpkqletepd
lfiritpkpeqkvleirdsgigmtkaelinnlgtiaksgtkafmealsagadvsmigqfg
vgfyslflvadrvqvisksnddeqyiwesnaggsftvtldevnerigrgtilrlflkddq
leyleekrikevikrhsefvaypiqlvvtkeve
>d1amx__ 2.2.3.1.1 Collagen-binding domain of adhesin {Staphylococcus aureus}
tssvfyyktgdmlpedtthvrwflninneksyvskditikdqiqggqqldlstlninvtg
thsnyysgqsaitdfekafpgskitvdntkntidvtipqgygsynsfsinyktkitneqq
kefvnnsqawyqehgkeevngksfnhtvhn
>d1amy_1 2.62.1.1.16 (347-403) Plant alpha-amylase {Barley (Hordeum vulgare), seeds, AMY2 isozyme}
hnesklqiieadadlylaeidgkvivklgprydvgnlipggfkvaahgndyavweki
>d1amy_2 3.1.7.1.16 (1-346) Plant alpha-amylase {Barley (Hordeum vulgare), seeds, AMY2 isozyme}
qvlfqgfnweswkhnggwynflmgkvddiaaagithvwlppasqsvaeqgympgrlydld
askygnkaqlksligalhgkgvkaiadivinhrtaehkdgrgiycifeggtpdarldwgp
hmicrddrpyadgtgnpdtgadfgaapdidhlnlrvqkelvewlnwlkadigfdgwrfdf
akgysadvakiyidrsepsfavaeiwtslayggdgkpnlnqdqhrqelvnwvdkvggkgp
attfdfttkgilnvavegelwrlrgtdgkapgmigwwpakavtfvdnhdtgstqhmwpfp
sdrvmqgyayilthpgtpcifydhffdwglkeeidrlvsvrtrhgi
>d1amz__ 1.99.1.1.1 Citrate synthase {Chicken (Gallus gallus)}
stnlkdvlaslipkeqariktfrqqhgntavgqitvdmsyggmrgmkgliyetsvldpde
girfrgfsipecqkllpkagggeeplpeglfwllvtgqiptpeqvswvskewakraalps
hvvtmldnfptnlhpmsqlsaaitalnsesnfarayaeginrtkywefvyedamdliakl
pcvaakiyrnlyragssigaidskldwshnftnmlgytdpqftelmrlyltihsdheggn
vsahtshlvgsalsdpylsfaaamnglagplhglanqevllwlsqlqkdlgadasdeklr
dyiwntlnsgrvvpgyghavlrktdprytcqrefalkhlpsdpmfklvaqlykivpnvll
eqgkaknpwpnvdahsgvllqyygmtemnyytvlfgvsralgvlaqliwsralgfplerp
ksmstagleklsagg
>d1an0a_ 3.30.1.6.11 CDC42 {Human (Homo sapiens)}
qtikcvvvgdgavgktcllisyttnkfpseyvptvfdnyavtvxiggepytlglfdtagq
edydrlrplsypqtdvflvcfsvvspssfenvkekwvpeithhcpktpfllvgtqidlrd
dpstieklaknkqkpitpetaeklardlkavkyvecsaltqkglknvfdeailaaleppe
pkksrrcv
>d1an0b_ 3.30.1.6.11 CDC42 {Human (Homo sapiens)}
qtikcvvvgdgavgktcllisyttnkfpseyvptvfdnyavtvxiggepytlglfdtagq
edydrlrplsypqtdvflvcfsvvspssfenvkekwvpeithhcpktpfllvgtqidlrd
dpstieklaknkqkpitpetaeklardlkavkyvecsaltqkglknvfdeailaaleppe
pkksrrcv
>d1an1e_ 2.41.1.2.3 Trypsin(ogen) {Rat (Rattus rattus)}
ivggytcaansipyqvslnsgshfcggslinsqwvvsaahcyksriqvrlgehnidvleg
neqfinaakiithpnfngntldndimliklsspatlxsrvatvslprscaaagteclisg
wgntkssgssypsllqclkapvlsdssckssypgqitgnmicvgfleggkdscqgdsggp
vvcngqlqgivswgygcaqknkpgvytkvcnyvnwiqqtiaan
>d1an1i_ 7.15.1.1.10 Leech derived tryptase inhibitor (LDTI-C) {Medicinal leech (Hirudo medicinalis)}
kvcacpkilkpvcgsdgrtyansciarcngvsiksegscp
>d1an2a_ 1.41.1.1.2 Max protein {Mouse (Mus musculus)}
adkrahhnalerkrrdhikdsfhslrdsvpslqgekasraqildkateyiqymrrknhth
qqdiddlkrqnalleqqvralekars
>d1an2c_ 1.41.1.1.2 Max protein {Mouse (Mus musculus)}
adkrahhnalerkrrdhikdsfhslrdsvpslqgekasraqildkateyiqymrrknhth
qqdiddlkrqnalleqqvralekars
>d1an4a_ 1.41.1.1.4 Usf B/HLH domain {Human (Homo sapiens)}
mdekrraqhneverrrrdkinnwivqlskiipdssmestksgqskggilskasdyiqelr
qsnhr
>d1an4b_ 1.41.1.1.4 Usf B/HLH domain {Human (Homo sapiens)}
mdekrraqhneverrrrdkinnwivqlskiipdssmestksgqskggilskasdyiqelr
qsnhr
>d1an5a_ 4.91.1.1.1 Thymidylate synthase {Escherichia coli}
mkqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihell
wflqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlk
ndpdsrriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfnias
yallvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesif
dyrfedfeiegydphpgikapvai
>d1an5b_ 4.91.1.1.1 Thymidylate synthase {Escherichia coli}
mkqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihell
wflqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlk
ndpdsrriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfnias
yallvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesif
dyrfedfeiegydphpgikapvai
>d1an7a_ 4.113.1.1.2 Ribosomal protein S8 {Thermus thermophilus}
tdpiadmltrirnatrvykestdvpasrfkeeilrilaregfikgyervdvdgkpylrvy
lkygprrqgpdprpeqvihhirriskpgrrvyvgvkeiprvrrglgiailstskgvltdr
earklgvggelicevw
>d1an7b_ 4.113.1.1.2 Ribosomal protein S8 {Thermus thermophilus}
tdpiadmltrirnatrvykestdvpasrfkeeilrilaregfikgyervdvdgkpylrvy
lkygprrqgpdprpeqvihhirriskpgrrvyvgvkeiprvrrglgiailstskgvltdr
earklgvggelicevw
>d1an8_1 2.35.2.2.6 (3-95) Streptococcal superantigen Spe-C {Streptococcus pyogenes}
kkdisnvksdllyaytitpydykdcrvnfstthtlnidtqkyrgkdyyissemsyeasqk
fkrddhvdvfglfyilnshtgeyiyggitpaqn
>d1an8_2 4.13.7.1.6 (96-208) Streptococcal superantigen Spe-C {Streptococcus pyogenes}
nkvnhkllgnlfisgesqqnlnnkiilekdivtfqeidfkirkylmdnykiydatspyvs
grieigtkdgkheqidlfdspnegtrsdifakykdnriinmknfshfdiylek
>d1an9a1 3.4.1.2.1 (1-194,288-340) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernll
>d1an9a2 4.14.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1an9b1 3.4.1.2.1 (1-194,288-340) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernll
>d1an9b2 4.14.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1anb__ 2.41.1.2.3 Trypsin(ogen) {Rat (Rattus rattus)}
ivggytcqensvpyqvslnsgyhfcggslindqwvvsaahcyksriqvrlgehninvleg
neqfvnaakiikhpnfdrktlnndimliklsspvklnarvatvalpsscapagtqclisg
wgntlssgvnepdllqcldapllpqadceasypgkitdnmvcvgfleggkdscqgdsggp
vvcngelqgivewgygcalpdnpgvytkvcnyvdwiqdtiaan
>d1anc__ 2.41.1.2.3 Trypsin(ogen) {Rat (Rattus rattus)}
ivggytcqensvpyqvslnsgyhfcggslindqwvvsaahcyksriqvrlgehninvleg
neqfvnaakiikhpnfdrktlnndimliklsspvklnarvatvalpsscapagtqclisg
wgntlssgvnepdllqcldapllpqadceasypgkitdnmvcvgfleggkdscqgdsggp
vvcngelqgivkwgygcalpdnpgvytkvcnyvdwiqdtiaan
>d1and__ 2.41.1.2.3 Trypsin(ogen) {Rat (Rattus rattus)}
ivggytcqensvpyqvslnsgyhfcggslindqwvvsaahcyksriqvrlgehninvleg
neqfvnaakiikhpnfdhktlnndimliklsspvklnarvatvalpsscapagtqclisg
wgntlssgvnepdllqcldapllpqadceasypgkitdnmvcvgfleggkdscqgdsggp
vvcngelqgivswgygcalpdnpgvytkvcnyvdwiqdtiaan
>d1ane__ 2.41.1.2.3 Trypsin(ogen) {Rat (Rattus rattus)}
ivggytcqensvpyqvslnsgyhfcggslindqwvvsaahcyksriqvrlgehninvleg
neqfvnaakiikhpnfdrktlnndimliklsspvklnarvatvalpsscapagtqclisg
wgntlssgvnepdllqcldapllpqadceasypgkitdnmvcvgfleggkdscqgdsggp
vvcngelqgivswgygcalpdnpgvytkvcnyvdwiqdtiaan
>d1anf__ 3.84.1.1.6 D-maltodextrin-binding protein, MBP {Escherichia coli}
kieegklviwingdkgynglaevgkkfekdtgikvtvehpdkleekfpqvaatgdgpdii
fwahdrfggyaqsgllaeitpdkafqdklypftwdavryngkliaypiavealsliynkd
llpnppktweeipaldkelkakgksalmfnlqepyftwpliaadggyafkyengkydikd
vgvdnagakagltflvdliknkhmnadtdysiaeaafnkgetamtingpwawsnidtskv
nygvtvlptfkgqpskpfvgvlsaginaaspnkelakeflenylltdegleavnkdkplg
avalksyeeelakdpriaatmenaqkgeimpnipqmsafwyavrtavinaasgrqtvdea
lkdaqtritk
>d1ang__ 4.5.1.1.7 Angiogenin {Human (Homo sapiens)}
qdnsrythfltqhydakpqgrddrycesimrrrgltspckdintfihgnkrsikaicenk
ngnphrenlriskssfqvttcklhggspwppcqyratagfrnvvvacenglpvhldqsif
rrp
>d1ania_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
mpvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseitaarn
yaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngalgvd
ihekdhptilemakaaglatgnvstaelqhatpaalvahvtsrkcygpsatsekcpgnal
ekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsdaasl
nsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptlaqmt
dkaiellsknekgfflqvegasidhqdhaanpcgqigetvdldeavqralefakkegntl
vivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlriaayg
phaanvvgltdqtdlfytmkaalglk
>d1anib_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
mpvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseitaarn
yaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngalgvd
ihekdhptilemakaaglatgnvstaelqhatpaalvahvtsrkcygpsatsekcpgnal
ekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsdaasl
nsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptlaqmt
dkaiellsknekgfflqvegasidhqdhaanpcgqigetvdldeavqralefakkegntl
vivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlriaayg
phaanvvgltdqtdlfytmkaalglk
>d1anja_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
mpvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseitaarn
yaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngalgvd
ihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpgnal
ekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsdaasl
nsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptlaqmt
dkaiellsknekgfflqvegasidhqdhaanpcgqigetvdldeavqralefakkegntl
vivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlriaayg
phaanvvgltdqtdlfytmkaalglk
>d1anjb_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
mpvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseitaarn
yaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngalgvd
ihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpgnal
ekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsdaasl
nsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptlaqmt
dkaiellsknekgfflqvegasidhqdhaanpcgqigetvdldeavqralefakkegntl
vivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlriaayg
phaanvvgltdqtdlfytmkaalglk
>d1anka1 3.30.1.1.12 (1-121,157-214) Adenylate kinase {Escherichia coli}
mriillgapgagkgtqaqfimekygipqistgdmlraavksgselgkqakdimdagklvt
delvialvkeriaqedcrngflldgfprtipqadamkeaginvdyvlefdvpdelivdri
vXkddqeetvrkrlveyhqmtapligyyskeaeagntkyakvdgtkpvaevradlekilg
>d1anka2 7.35.2.1.2 (122-156) Microbial and mitochondrial ADK, insert "zinc finger" domain {Escherichia coli}
grrvhapsgrvyhvkfnppkvegkddvtgeelttr
>d1ankb1 3.30.1.1.12 (1-121,157-214) Adenylate kinase {Escherichia coli}
mriillgapgagkgtqaqfimekygipqistgdmlraavksgselgkqakdimdagklvt
delvialvkeriaqedcrngflldgfprtipqadamkeaginvdyvlefdvpdelivdri
vXkddqeetvrkrlveyhqmtapligyyskeaeagntkyakvdgtkpvaevradlekilg
>d1ankb2 7.35.2.1.2 (122-156) Microbial and mitochondrial ADK, insert "zinc finger" domain {Escherichia coli}
grrvhapsgrvyhvkfnppkvegkddvtgeelttr
>d1ann__ 1.66.1.1.3 Annexin IV {Bovine (Bos taurus)}
ggtvkaasgfnaaedaqtlrkamkglgtdedaiinvlayrstaqrqeirtaykttigrdl
mddlkselsgnfeqvilgmmtptvlydvqelrkamkgagtdegclieilasrtpeeirri
nqtyqlqygrsleddirsdtsfmfqrvlvslsaggrdesnylddalmrqdaqdlyeagek
kwgtdevkfltvlcsrnrnhllhvfdeykriaqkdieqsiksetsgsfedallaivkcmr
nksayfaerlyksmkglgtdddtlirvmvsraeidmldiranfkrlygkslysfikgdts
gdyrkvllilcggdd
>d1ans__ 7.11.1.1.1 Neurotoxin III (ATX III) {Sea anemone (Anemonia sulcata)}
rsccpcywggcpwgqncypegcsgpkv
>d1anti_ 5.1.1.1.6 Antithrombin {Human (Homo sapiens)}
rdipmnpmciyrspekkatedegseqkipeatnrrvwelskansrfattfyqhladsknd
ndniflsplsistafamtklgacndtlqqlmevfkfdtisektsdqihfffaklncrlyr
kankssklvsanrlfgdksltfnetyqdiselvygaklqpldfkenaeqsraainkwvsn
ktegritdvipseaineltvlvlvntiyfkglwkskfspentrkelfykadgescsasmm
yqegkfryrrvaegtqvlelpfkgdditmvlilpkpekslakvekeltpevlqewldele
emmlvvhmprfriedgfslkeqlqdmglvdlfspeksklpgivaegrddlyvsdafhkaf
levneegseaaastavviagrslnpnrvtfkanrpflvfirevplntiifmgrvanpcvk
>d1antl_ 5.1.1.1.6 Antithrombin {Human (Homo sapiens)}
dipmnpmciyrspekkatedegseqkipeatnrrvwelskansrfattfyqhladskndn
dniflsplsistafamtklgacndtlqqlmevfkfdtisektsdqihfffaklncrlyrk
ankssklvsanrlfgdksltfnetyqdiselvygaklqpldfkenaeqsraainkwvsnk
tegritdvipseaineltvlvlvntiyfkglwkskfspentrkelfykadgescsasmmy
qegkfryrrvaegtqvlelpfkgdditmvlilpkpekslakvekeltpevlqewldelee
mmlvvhmprfriedgfslkeqlqdmglvdlfspeksklpgivaegrddlyvsdafhkafl
evneegseaaastavviagrslnpnrvtfkanrpflvfirevplntiifmgrvanpcvk
>d1anu__ 2.2.2.2.3 Cohesin-2 domain of cellulosome {Clostridium thermocellum}
vvveigkvtgsvgttveipvyfrgvpskgiancdfvfrydpnvleiigidpgdiivdpnp
tksfdtaiypdrkiivflfaedsgtgayaitkdgvfakiratvkssapgyitfdevggfa
dndlveqkvsfidggvnv
>d1anv_1 1.56.1.1.1 (179-265) Domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
sawekgmeaaralmdkyhvdndlkanfkllpdqvealaavcktwlneehrglqltftsnk
tfvtmmgrflqaylqsfaevtykhhep
>d1anv_2 7.43.1.1.1 (266-385) First Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
tgcalwlhrcaeiegelkclhgsiminkehviemdvtsengqralkeqsskakivknrwg
rnvvqisntdarccvhdaacpanqfsgkscgmffsegakaqvafkqikafmqalypnaqt
>d1anv_3 7.43.1.1.2 (386-529) Second Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
ghghllmplrcecnskpghapflgrqlpkltpfalsnaedldadlisdksvlasvhhpal
ivfqccnpvyrnsraqgggpncdfkisapdllnalvmvrslwsenftelprmvvpefkws
tkhqyrnvslpvahsdarqnpfdf
>d1anwa_ 1.66.1.1.5 Annexin V {Human (Homo sapiens)}
aqvlrgtvtdfpgfderadaetlrkamkglgtdeesiltlltsrsnaqrqeisaafktlf
grdllddlkseltgkfeklivalmkpsrlydayelkhalkgagtnekvlteiiasrtpee
lraikqvyeeeygssleddvvgdtsgyyqrmlvvllqanrdpdagideaqveqdaqalfq
agelkwgtdeekfitifgtrsvshlrkvfdkymtisgfqieetidretsgnleqlllavv
ksirsipaylaetlyyamkgagtddhtlirvmvsrseidlfnirkefrknfatslysmik
gdtsgdykkallllcgedd
>d1anwb_ 1.66.1.1.5 Annexin V {Human (Homo sapiens)}
aqvlrgtvtdfpgfderadaetlrkamkglgtdeesiltlltsrsnaqrqeisaafktlf
grdllddlkseltgkfeklivalmkpsrlydayelkhalkgagtnekvlteiiasrtpee
lraikqvyeeeygssleddvvgdtsgyyqrmlvvllqanrdpdagideaqveqdaqalfq
agelkwgtdeekfitifgtrsvshlrkvfdkymtisgfqieetidretsgnleqlllavv
ksirsipaylaetlyyamkgagtddhtlirvmvsrseidlfnirkefrknfatslysmik
gdtsgdykkallllcgedd
>d1anxa_ 1.66.1.1.5 Annexin V {Human (Homo sapiens)}
qvlrgtvtdfpgfderadaetlrkamkglgtdeesiltlltsrsnaqrqeisaafktlfg
rdllddlkseltgkfeklivalmkpsrlydayelkhalkgagtnekvlteiiasrtpeel
raikqvyeeeygssleddvvgdtsgyyqrmlvvllqanrdpdagideaqveqdaqalfqa
gelkwgtdeekfitifgtrsvshlrkvfdkymtisgfqieetidretsgnleqlllavvk
sirsipaylaetlyyamkgagtddhtlirvmvsrseidlfnirkefrknfatslysmikg
dtsgdykkallllcge
>d1anxb_ 1.66.1.1.5 Annexin V {Human (Homo sapiens)}
qvlrgtvtdfpgfderadaetlrkamkglgtdeesiltlltsrsnaqrqeisaafktlfg
rdllddlkseltgkfeklivalmkpsrlydayelkhalkgagtnekvlteiiasrtpeel
raikqvyeeeygssleddvvgdtsgyyqrmlvvllqanrdpdagideaqveqdaqalfqa
gelkwgtdeekfitifgtrsvshlrkvfdkymtisgfqieetidretsgnleqlllavvk
sirsipaylaetlyyamkgagtddhtlirvmvsrseidlfnirkefrknfatslysmikg
dtsgdykkallllcge
>d1anxc_ 1.66.1.1.5 Annexin V {Human (Homo sapiens)}
qvlrgtvtdfpgfderadaetlrkamkglgtdeesiltlltsrsnaqrqeisaafktlfg
rdllddlkseltgkfeklivalmkpsrlydayelkhalkgagtnekvlteiiasrtpeel
raikqvyeeeygssleddvvgdtsgyyqrmlvvllqanrdpdagideaqveqdaqalfqa
gelkwgtdeekfitifgtrsvshlrkvfdkymtisgfqieetidretsgnleqlllavvk
sirsipaylaetlyyamkgagtddhtlirvmvsrseidlfnirkefrknfatslysmikg
dtsgdykkallllcge
>d1ao0a1 3.51.1.1.4 (235-459) Glutamine PRPP amidotransferase, C-terminal domain {Bacillus subtilis}
icsmeyiyfsrpdsnidginvhsarknlgkmlaqesaveadvvtgvpdssisaaigyaea
tgipyelgliknryvgrtfiqpsqalreqgvrmklsavrgvvegkrvvmvddsivrgtts
rrivtmlreagatevhvkissppiahpcfygidtstheeliasshsveeirqeigadtls
flsvegllkgigrkyddsncgqclacftgkypteiyqdtvlphvk
>d1ao0a2 4.124.1.1.2 (1-234) Glutamine PRPP amidotransferase, N-terminal domain {Bacillus subtilis}
cgvfgiwgheeapqityyglhslqhrgqegagivatdgekltahkgqglitevfqngels
kvkgkgaighvryataggggyenvqpllfrsqnngslalahngnlvnatqlkqqlenqgs
ifqtssdtevlahlikrsghftlkdqiknslsmlkgayaflimtetemivaldpnglrpl
sigmmgdayvvasetcafdvvgatylrevepgemliindegmkserfsmninrs
>d1ao0b1 3.51.1.1.4 (235-459) Glutamine PRPP amidotransferase, C-terminal domain {Bacillus subtilis}
icsmeyiyfsrpdsnidginvhsarknlgkmlaqesaveadvvtgvpdssisaaigyaea
tgipyelgliknryvgrtfiqpsqalreqgvrmklsavrgvvegkrvvmvddsivrgtts
rrivtmlreagatevhvkissppiahpcfygidtstheeliasshsveeirqeigadtls
flsvegllkgigrkyddsncgqclacftgkypteiyqdtvlphvk
>d1ao0b2 4.124.1.1.2 (1-234) Glutamine PRPP amidotransferase, N-terminal domain {Bacillus subtilis}
cgvfgiwgheeapqityyglhslqhrgqegagivatdgekltahkgqglitevfqngels
kvkgkgaighvryataggggyenvqpllfrsqnngslalahngnlvnatqlkqqlenqgs
ifqtssdtevlahlikrsghftlkdqiknslsmlkgayaflimtetemivaldpnglrpl
sigmmgdayvvasetcafdvvgatylrevepgemliindegmkserfsmninrs
>d1ao0c1 3.51.1.1.4 (235-459) Glutamine PRPP amidotransferase, C-terminal domain {Bacillus subtilis}
icsmeyiyfsrpdsnidginvhsarknlgkmlaqesaveadvvtgvpdssisaaigyaea
tgipyelgliknryvgrtfiqpsqalreqgvrmklsavrgvvegkrvvmvddsivrgtts
rrivtmlreagatevhvkissppiahpcfygidtstheeliasshsveeirqeigadtls
flsvegllkgigrkyddsncgqclacftgkypteiyqdtvlphvk
>d1ao0c2 4.124.1.1.2 (1-234) Glutamine PRPP amidotransferase, N-terminal domain {Bacillus subtilis}
cgvfgiwgheeapqityyglhslqhrgqegagivatdgekltahkgqglitevfqngels
kvkgkgaighvryataggggyenvqpllfrsqnngslalahngnlvnatqlkqqlenqgs
ifqtssdtevlahlikrsghftlkdqiknslsmlkgayaflimtetemivaldpnglrpl
sigmmgdayvvasetcafdvvgatylrevepgemliindegmkserfsmninrs
>d1ao0d1 3.51.1.1.4 (235-459) Glutamine PRPP amidotransferase, C-terminal domain {Bacillus subtilis}
icsmeyiyfsrpdsnidginvhsarknlgkmlaqesaveadvvtgvpdssisaaigyaea
tgipyelgliknryvgrtfiqpsqalreqgvrmklsavrgvvegkrvvmvddsivrgtts
rrivtmlreagatevhvkissppiahpcfygidtstheeliasshsveeirqeigadtls
flsvegllkgigrkyddsncgqclacftgkypteiyqdtvlphvk
>d1ao0d2 4.124.1.1.2 (1-234) Glutamine PRPP amidotransferase, N-terminal domain {Bacillus subtilis}
cgvfgiwgheeapqityyglhslqhrgqegagivatdgekltahkgqglitevfqngels
kvkgkgaighvryataggggyenvqpllfrsqnngslalahngnlvnatqlkqqlenqgs
ifqtssdtevlahlikrsghftlkdqiknslsmlkgayaflimtetemivaldpnglrpl
sigmmgdayvvasetcafdvvgatylrevepgemliindegmkserfsmninrs
>d1ao3a_ 3.52.1.1.2 von Willebrand factor A3 domain {Human (Homo sapiens)}
csqpldvillldgsssfpasyfdemksfakafiskanigprltqvsvlqygsittidvpw
nvvpekahllslvdvmqreggpsqigdalgfavryltsemhgarpgaskavvilvtdvsv
dsvdaaadaarsnrvtvfpigigdrydaaqlrilagpagdsnvvklqriedlptmvtlgn
sflhklc
>d1ao3b_ 3.52.1.1.2 von Willebrand factor A3 domain {Human (Homo sapiens)}
csqpldvillldgsssfpasyfdemksfakafiskanigprltqvsvlqygsittidvpw
nvvpekahllslvdvmqreggpsqigdalgfavryltsemhgarpgaskavvilvtdvsv
dsvdaaadaarsnrvtvfpigigdrydaaqlrilagpagdsnvvklqriedlptmvtlgn
sflhklc
>d1ao5a_ 2.41.1.2.32 Kallikrein-13 {Mouse (Mus musculus)}
vvggfnceknsqpwqvavyyqkehicggvlldrnwvltaahcyvdqyevwlgknklfqee
psaqhrlvsksfphpgfnmsllmlqtippgadfsddlmllrlskpaditdvvkpialptk
epkpgskclasgwgsitptrwqkpddlqcvfitllpnencakvylqkvtdvmlcagemgg
gkdtcrddsggplicdgilqgttsygpvpcgkpgvpaiytnlikfnswikdtmmkna
>d1ao5b_ 2.41.1.2.32 Kallikrein-13 {Mouse (Mus musculus)}
vvggfnceknsqpwqvavyyqkehicggvlldrnwvltaahcyvdqyevwlgknklfqee
psaqhrlvsksfphpgfnmsllmlqtippgadfsddlmllrlskpaditdvvkpialptk
epkpgskclasgwgsitptrwqkpddlqcvfitllpnencakvylqkvtdvmlcagemgg
gkdtcrddsggplicdgilqgttsygpvpcgkpgvpaiytnlikfnswikdtmmkna
>d1ao6a1 1.116.1.1.1 (5-196) Serum albumin {Human (Homo sapiens)}
sevahrfkdlgeenfkalvliafaqylqqcpfedhvklvnevtefaktcvadesaencdk
slhtlfgdklctvatlretygemadccakqepernecflqhkddnpnlprlvrpevdvmc
tafhdneetflkkylyeiarrhpyfyapellffakrykaafteccqaadkaacllpklde
lrdegkassakq
>d1ao6a2 1.116.1.1.1 (197-388) Serum albumin {Human (Homo sapiens)}
rlkcaslqkfgerafkawavarlsqrfpkaefaevsklvtdltkvhtecchgdllecadd
radlakyicenqdsissklkeccekpllekshciaevendempadlpslaadfveskdvc
knyaeakdvflgmflyeyarrhpdysvvlllrlaktyettlekccaaadphecyakvfde
fkplveepqnli
>d1ao6a3 1.116.1.1.1 (389-582) Serum albumin {Human (Homo sapiens)}
kqncelfeqlgeykfqnallvrytkkvpqvstptlvevsrnlgkvgskcckhpeakrmpc
aedylsvvlnqlcvlhektpvsdrvtkccteslvnrrpcfsalevdetyvpkefnaetft
fhadictlsekerqikkqtalvelvkhkpkatkeqlkavmddfaafvekcckaddketcf
aeegkklvaasqaa
>d1ao6b1 1.116.1.1.1 (5-196) Serum albumin {Human (Homo sapiens)}
sevahrfkdlgeenfkalvliafaqylqqcpfedhvklvnevtefaktcvadesaencdk
slhtlfgdklctvatlretygemadccakqepernecflqhkddnpnlprlvrpevdvmc
tafhdneetflkkylyeiarrhpyfyapellffakrykaafteccqaadkaacllpklde
lrdegkassakq
>d1ao6b2 1.116.1.1.1 (197-388) Serum albumin {Human (Homo sapiens)}
rlkcaslqkfgerafkawavarlsqrfpkaefaevsklvtdltkvhtecchgdllecadd
radlakyicenqdsissklkeccekpllekshciaevendempadlpslaadfveskdvc
knyaeakdvflgmflyeyarrhpdysvvlllrlaktyettlekccaaadphecyakvfde
fkplveepqnli
>d1ao6b3 1.116.1.1.1 (389-582) Serum albumin {Human (Homo sapiens)}
kqncelfeqlgeykfqnallvrytkkvpqvstptlvevsrnlgkvgskcckhpeakrmpc
aedylsvvlnqlcvlhektpvsdrvtkccteslvnrrpcfsalevdetyvpkefnaetft
fhadictlsekerqikkqtalvelvkhkpkatkeqlkavmddfaafvekcckaddketcf
aeegkklvaasqaa
>d1ao7a1 2.1.1.2.4 (182-274) Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-a0201}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrdgedqtqdtelvetrpagdgtf
qkwaavvvpsgqeqrytchvqheglpkpltlrw
>d1ao7a2 4.17.1.1.11 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-a0201}
gshsmryfftsvsrpgrgeprfiavgyvddtqfvrfdsdaasqrmeprapwieqegpeyw
dgetrkvkahsqthrvdlgtlrgyynqseagshtvqrmygcdvgsdwrflrgyhqyaydg
kdyialkedlrswtaadmaaqttkhkweaahvaeqlraylegtcvewlrrylengketlq
r
>d1ao7b1 2.1.1.2.4 Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-a0201}
miqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskd
wsfyllycteftptekdeyacrvnhvtlsqpcivkwdrdm
>d1ao7d_ 2.1.1.1.155 T-cell antigen receptor {Human (Homo sapiens), alpha-chain}
keveqnsgplsvpegaiaslnctysdrgsqsffwyrqysgkspelimsiysngdkedgrf
taqlnkasqyvsllirdsqpsdsatylcavttdswgklqfgagtqvvvtpdiqnp
>d1ao7e1 2.1.1.1.157 (3-118) T-cell antigen receptor {Human (Homo sapiens), beta-chain}
gvtqtpkfqvlktgqsmtlqcaqdmnheymswyrqdpgmglrlihysvgagitdqgevpn
gynvsrsttedfplrllsaapsqtsvyfcasrpglaggrpeqyfgpgtrltvted
>d1ao7e2 2.1.1.2.146 (119-246) T-cell antigen receptor {Human (Homo sapiens), beta-chain}
lknvfppevavfepseaeishtqkatlvclatgfypdhvelswwvngkevhsgvstdpqp
lkeqpalndsryalssrlrvsatfwqnprnhfrcqvqfyglsendewtqdrakpvtqivs
aeawgrad
>d1ao8__ 3.61.1.1.2 Dihydrofolate reductase, prokaryotic type {Lactobacillus casei}
taflwaqdrdgligkdghlpwhlpddlhyfraqtvgkimvvgrrtyesfpkrplpertnv
vlthqedyqaqgavvvhdvaavfayakqhpdqelviaggaqiftafkddvdtllvtrlag
sfegdtkmiplnwddftkvssrtvedtnpalthtyevwqkka
>d1aoa_1 1.43.1.1.2 (121-251) N-terminal actin-crosslinking domain from fimbrin {Human (Homo sapiens)}
yseeekyafvnwinkalendpdcrhvipmnpntddlfkavgdgivlckminlsvpdtide
rainkkkltpfiiqenlnlalnsasaigchvvnigaedlragkphlvlgllwqiikiglf
adielsrneal
>d1aoa_2 1.43.1.1.2 (260-375) N-terminal actin-crosslinking domain from fimbrin {Human (Homo sapiens)}
tleelmklspeelllrwanfhlensgwqkinnfsadikdskayfhllnqiapkgqkegep
ridinmsgfnetddlkraesmlqqadklgcrqfvtpadvvsgnpklnlafvanlfn
>d1aob__ 4.91.1.1.1 Thymidylate synthase {Escherichia coli}
mkqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihell
wflqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlk
ndpdsrriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfnias
yallvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesif
dyrfedfeiegydphpgikapvai
>d1aoca_ 7.17.1.5.1 Coagulogen {Japanese horseshoe crab (Tachypleus tridentatus)}
adtnapiclcdepgvlgrtqivtteikdkiekaveavaqesgvsgrgfsifshhpvfrec
gkyecrtvrpehsrcynfppfthfksecpvstrdcepvfgytvagefrvivqapragfrq
cvwqhkcrfgsnscgyngrctqqrsvvrlvtynlekdgflcesfrtccgcpcrsf
>d1aocb_ 7.17.1.5.1 Coagulogen {Japanese horseshoe crab (Tachypleus tridentatus)}
adtnapiclcdepgvlgrtqivtteikdkiekaveavaqesgvsgrgfsifshhpvfrec
gkyecrtvrpehsrcynfppfthfksecpvstrdcepvfgytvagefrvivqapragfrq
cvwqhkcrfgsnscgyngrctqqrsvvrlvtynlekdgflcesfrtccgcpcrsf
>d1aod__ 3.1.16.2.2 Phosphatidylinositol-specific phospholipase C {Listeria monocytogenes}
vttkqwmsalpdttnlaalsipgthdtmsyngditwtltkplaqtqtmslyqqleagiry
idirakdnlniyhgpiflnaslsgvletitqflkknpketiimrlkdeqnsndsfdyriq
pliniykdyfyttprtdtsnkiptlkdvrgkilllsenhtkkplvinsrkfgmqfgapnq
viqddyngpsvktkfkeivqtayqaskadnklflnhisatsltftprqyaaalnnkveqf
vlnltsekvrglgilimdfpekqtikniiknnkf
>d1aoea_ 3.61.1.1.7 Dihydrofolate reductases, eukaryotic type {Yeast (Candida albicans)}
mlkpnvaiivaalkpalgigykgkmpwrlrkeiryfkdvttrttkpntrnavimgrktwe
sipqkfrplpdrlniilsrsyeneiiddniihassiesslnlvsdvervfiiggaeiyne
linnslvshlliteiehpspesiemdtflkfpleswtkqpkselqkfvgdtvleddikeg
dftynytlwtrk
>d1aoeb_ 3.61.1.1.7 Dihydrofolate reductases, eukaryotic type {Yeast (Candida albicans)}
mlkpnvaiivaalkpalgigykgkmpwrlrkeiryfkdvttrttkpntrnavimgrktwe
sipqkfrplpdrlniilsrsyeneiiddniihassiesslnlvsdvervfiiggaeiyne
linnslvshlliteiehpspesiemdtflkfpleswtkqpkselqkfvgdtvleddikeg
dftynytlwtrk
>d1aofa1 1.3.1.2.1 (36-133) N-terminal (heme c) domain of cytochrome cd1-nitrite reductase {Thiosphaera pantotropha}
dvaapgapegvtalsdaqyneankiyfercagchgvlrkgatgkaltpdltrdlgfdylq
sfityaspagmpnwgtsgelsaeqvdlmanyllldpaa
>d1aofa2 2.61.2.1.1 (134-567) C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase {Thiosphaera pantotropha}
ppefgmkemreswkvhvapedrptqqmndwdlenlfsvtlrdagqialidgstyeiktvl
dtgyavhisrlsasgrylfvigrdgkvnmidlwmkepttvaeikigsearsietskmegw
edkyaiagaywppqyvimdgetlepkkiqstrgmtydeqeyhpeprvaailashyrpefi
vnvketgkillvdytdlnnlktteisaerflhdggldgshryfitaanarnklvvidtke
gklvaiedtggqtphpgrganfvhptfgpvwatshmgddsvaligtdpeghpdnawkild
sfpalgggslfikthpnsqylyvdatlnpeaeisgsvavfdikamtgdgsdpefktlpia
ewagitegqprvvqgefnkdgtevwfsvwngkdqesalvvvddktlelkhvikderlvtp
tgkfnvyntmtdty
>d1aofb1 1.3.1.2.1 (26-133) N-terminal (heme c) domain of cytochrome cd1-nitrite reductase {Thiosphaera pantotropha}
epsldnlaqqdvaapgapegvtalsdaqyneankiyfercagchgvlrkgatgkaltpdl
trdlgfdylqsfityaspagmpnwgtsgelsaeqvdlmanyllldpaa
>d1aofb2 2.61.2.1.1 (134-567) C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase {Thiosphaera pantotropha}
ppefgmkemreswkvhvapedrptqqmndwdlenlfsvtlrdagqialidgstyeiktvl
dtgyavhisrlsasgrylfvigrdgkvnmidlwmkepttvaeikigsearsietskmegw
edkyaiagaywppqyvimdgetlepkkiqstrgmtydeqeyhpeprvaailashyrpefi
vnvketgkillvdytdlnnlktteisaerflhdggldgshryfitaanarnklvvidtke
gklvaiedtggqtphpgrganfvhptfgpvwatshmgddsvaligtdpeghpdnawkild
sfpalgggslfikthpnsqylyvdatlnpeaeisgsvavfdikamtgdgsdpefktlpia
ewagitegqprvvqgefnkdgtevwfsvwngkdqesalvvvddktlelkhvikderlvtp
tgkfnvyntmtdty
>d1aoga1 3.3.1.5.4 (3-169,287-357) Trypanothione reductase {Trypanosoma cruzi}
skifdlvvigagsggleaawnaatlykkrvavidvqmvhgppffsalggtcvnvgcvpkk
lmvtgaqymehlresagfgwefdrttlraewknliavkdeavlninksydemfrdtegle
fflgwgslesknvvnvresadpasavkerletehillasgswphmpnXgrsprtkdlqlq
nagvmiknggvqvdeysrtnvsniyaigdvtnrvmltpvaineaaalvdtvfgttprkt
>d1aoga2 3.3.1.5.4 (170-286) Trypanothione reductase {Trypanosoma cruzi}
ipgiehcissneafylpepprrvltvgggfisvefagifnaykpkdgqvtlcyrgemilr
gfdhtlreeltkqltangiqiltkenpakvelnadgsksvtfesgkkmdfdlvmmai
>d1aoga3 4.67.1.1.4 (358-487) Trypanothione reductase {Trypanosoma cruzi}
dhtrvasavfsippigtcglieevaskryevvavylssftplmhkvsgskyktfvakiit
nhsdgtvlgvhllgdnapeiiqgigiclklnakisdfyntigvhptsaeelcsmrtpsyy
yvkgekmekp
>d1aogb1 3.3.1.5.4 (5-169,287-357) Trypanothione reductase {Trypanosoma cruzi}
ifdlvvigagsggleaawnaatlykkrvavidvqmvhgppffsalggtcvnvgcvpkklm
vtgaqymehlresagfgwefdrttlraewknliavkdeavlninksydemfrdtegleff
lgwgslesknvvnvresadpasavkerletehillasgswphmpnXgrsprtkdlqlqna
gvmiknggvqvdeysrtnvsniyaigdvtnrvmltpvaineaaalvdtvfgttprkt
>d1aogb2 3.3.1.5.4 (170-286) Trypanothione reductase {Trypanosoma cruzi}
ipgiehcissneafylpepprrvltvgggfisvefagifnaykpkdgqvtlcyrgemilr
gfdhtlreeltkqltangiqiltkenpakvelnadgsksvtfesgkkmdfdlvmmai
>d1aogb3 4.67.1.1.4 (358-487) Trypanothione reductase {Trypanosoma cruzi}
dhtrvasavfsippigtcglieevaskryevvavylssftplmhkvsgskyktfvakiit
nhsdgtvlgvhllgdnapeiiqgigiclklnakisdfyntigvhptsaeelcsmrtpsyy
yvkgekmekp
>d1aoha_ 2.2.2.2.4 Cohesin domain from scaffolding protein CipA {Clostridium thermocellum}
avrikvdtvnakpgdtvripvrfsgipskgiancdfvysydpnvleiieiepgelivdpn
ptksfdtavypdrkmivflfaedsgtgayaitedgvfativakvksgapnglsvikfvev
ggfanndlveqktqffdggvnvg
>d1aohb_ 2.2.2.2.4 Cohesin domain from scaffolding protein CipA {Clostridium thermocellum}
tdldavrikvdtvnakpgdtvripvrfsgipskgiancdfvysydpnvleiieiepgeli
vdpnptksfdtavypdrkmivflfaedsgtgayaitedgvfativakvksgapnglsvik
fvevggfanndlveqktqffdggvnvg
>d1aoia_ 1.23.1.1.6 Histone H3 {African clawed frog (Xenopus laevis)}
phryrpgtvalreirryqkstellirklpfqrlvreiaqdfktdlrfqssavmalqease
aylvalfedtnlcaihakrvtimpkdiqlarrirgera
>d1aoib_ 1.23.1.1.8 Histone H4 {African clawed frog (Xenopus laevis)}
kvlrdniqgitkpairrlarrggvkrisgliyeetrgvlkvflenvirdavtytehakrk
tvtamdvvyalkrqgrtlygfgg
>d1aoic_ 1.23.1.1.2 Histone H2A {African clawed frog (Xenopus laevis)}
gkqggktrakaktrssraglqfpvgrvhrllrkgnyaervgagapvylaavleyltaeil
elagnaardnkktriiprhlqlavrndeelnkllgrvtiaqggvlpniqsvllpk
>d1aoid_ 1.23.1.1.4 Histone H2B {African clawed frog (Xenopus laevis)}
kkrrktrkesyaiyvykvlkqvhpdtgisskamsimnsfvndvferiageasrlahynkr
stitsreiqtavrlllpgelakhavsegtkavtkytsak
>d1aoie_ 1.23.1.1.6 Histone H3 {African clawed frog (Xenopus laevis)}
latkaarksapatggvkkphryrpgtvalreirryqkstellirklpfqrlvreiaqdfk
tdlrfqssavmalqeaseaylvalfedtnlcaihakrvtimpkdiqlarrirgera
>d1aoif_ 1.23.1.1.8 Histone H4 {African clawed frog (Xenopus laevis)}
krhrkvlrdniqgitkpairrlarrggvkrisgliyeetrgvlkvflenvirdavtyteh
akrktvtamdvvyalkrqgrtlygfgg
>d1aoig_ 1.23.1.1.2 Histone H2A {African clawed frog (Xenopus laevis)}
akaktrssraglqfpvgrvhrllrkgnyaervgagapvylaavleyltaeilelagnaar
dnkktriiprhlqlavrndeelnkllgrvtiaqggvlpniqsvllpkk
>d1aoih_ 1.23.1.1.4 Histone H2B {African clawed frog (Xenopus laevis)}
kkrrktrkesyaiyvykvlkqvhpdtgisskamsimnsfvndvferiageasrlahynkr
stitsreiqtavrlllpgelakhavsegtkavtkytsak
>d1aoja_ 2.30.2.1.24 EPS8 SH3 domain {Mouse (Mus musculus)}
kkyakskydfvarnsselsvmkddvleilddrrqwwkvrnasgdsgfvpnnildimrtpe
>d1aojb_ 2.30.2.1.24 EPS8 SH3 domain {Mouse (Mus musculus)}
kkyakskydfvarnsselsvmkddvleilddrrqwwkvrnasgdsgfvpnnildimrtpe
>d1aoka_ 1.123.1.2.10 Snake phospholipase A2 {Sand viper (Vipera ammodytes), vipoxin}
nlfqfgdmilqktgkeavhsyaiygcycgwggqgraqdatdrccfaqdccygrvndcnpk
tatytysrengdivcgdddlclravcecdraaaiclgenvntydknyeyysishcteese
qc
>d1aokb_ 1.123.1.2.10 Snake phospholipase A2 {Sand viper (Vipera ammodytes), vipoxin}
nlfqfakmingklgafsvwnyisygcycgwggqgtpkdatdrccfvhdccygrvrgcnpk
laiyyysfkkgnivcgknngclrdicecdrvaancfhqnkntynanykflsssrcrqtge
kc
>d1aol__ 2.18.1.1.1 F-MuLV receptor-binding domain {Friend murine leukemia virus, F-MuLV}
qvynitwevtngdretvwaisgnhplwtwwpvltpdlcmlalsgpphwgleyqapysspp
gppccsgssgssagcsrdcdepltsltprcntawnrlkldqvthkssegfyvcpgshrpr
eakscggpdsfycaswgcettgrvywkpssswdyitvdnnlttsqavqvckdnkwcnpla
iqftnagkqvtswttghywglrlyvsgrdpgltfgirlryqnlgprvp
>d1aoma1 2.61.2.1.1 (129-567) C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase {Thiosphaera pantotropha}
ldpaappefgmkemreswkvhvapedrptqqmndwdlenlfsvtlrdagqialidgstye
iktvldtgyavhisrlsasgrylfvigrdgkvnmidlwmkepttvaeikigsearsiets
kmegwedkyaiagaywppqyvimdgetlepkkiqstrgmtydeqeyhpeprvaailashy
rpefivnvketgkillvdytdlnnlktteisaerflhdggldgshryfitaanarnklvv
idtkegklvaiedtggqtphpgrganfvhptfgpvwatshmgddsvaligtdpeghpdna
wkildsfpalgggslfikthpnsqylyvdatlnpeaeisgsvavfdikamtgdgsdpefk
tlpiaewagitegqprvvqgefnkdgtevwfsvwngkdqesalvvvddktlelkhvikde
rlvtptgkfnvyntmtdty
>d1aomb1 1.3.1.2.1 (9-133) N-terminal (heme c) domain of cytochrome cd1-nitrite reductase {Thiosphaera pantotropha}
dpaaaledhktrtdnryepsldnlaqqdvaapgapegvtalsdaqyneankiyfercagc
hgvlrkgatgkaltpdltrdlgfdylqsfityaspagmpnwgtsgelsaeqvdlmanyll
ldpaa
>d1aomb2 2.61.2.1.1 (134-567) C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase {Thiosphaera pantotropha}
ppefgmkemreswkvhvapedrptqqmndwdlenlfsvtlrdagqialidgstyeiktvl
dtgyavhisrlsasgrylfvigrdgkvnmidlwmkepttvaeikigsearsietskmegw
edkyaiagaywppqyvimdgetlepkkiqstrgmtydeqeyhpeprvaailashyrpefi
vnvketgkillvdytdlnnlktteisaerflhdggldgshryfitaanarnklvvidtke
gklvaiedtggqtphpgrganfvhptfgpvwatshmgddsvaligtdpeghpdnawkild
sfpalgggslfikthpnsqylyvdatlnpeaeisgsvavfdikamtgdgsdpefktlpia
ewagitegqprvvqgefnkdgtevwfsvwngkdqesalvvvddktlelkhvikderlvtp
tgkfnvyntmtdty
>d1aona1 1.119.1.1.1 (2-136,410-525) GroEL {Escherichia coli}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aona2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aona3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonb1 1.119.1.1.1 (2-136,410-525) GroEL {Escherichia coli}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aonb2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aonb3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonc1 1.119.1.1.1 (2-136,410-525) GroEL {Escherichia coli}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aonc2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aonc3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aond1 1.119.1.1.1 (2-136,410-525) GroEL {Escherichia coli}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aond2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aond3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aone1 1.119.1.1.1 (2-136,410-525) GroEL {Escherichia coli}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aone2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aone3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonf1 1.119.1.1.1 (2-136,410-525) GroEL {Escherichia coli}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aonf2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aonf3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aong1 1.119.1.1.1 (2-136,410-525) GroEL {Escherichia coli}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aong2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aong3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonh1 1.119.1.1.1 (2-136,410-525) GroEL {Escherichia coli}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aonh2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aonh3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aoni1 1.119.1.1.1 (2-136,410-525) GroEL {Escherichia coli}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aoni2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aoni3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonj1 1.119.1.1.1 (2-136,410-525) GroEL {Escherichia coli}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aonj2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aonj3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonk1 1.119.1.1.1 (2-136,410-525) GroEL {Escherichia coli}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aonk2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aonk3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonl1 1.119.1.1.1 (2-136,410-525) GroEL {Escherichia coli}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aonl2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aonl3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonm1 1.119.1.1.1 (2-136,410-525) GroEL {Escherichia coli}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aonm2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aonm3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonn1 1.119.1.1.1 (2-136,410-525) GroEL {Escherichia coli}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aonn2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aonn3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aono_ 2.31.1.1.1 Chaperonin-10 (GroES) {Escherichia coli}
mnirplhdrvivkrkevetksaggivltgsaaakstrgevlavgngrilengevkpldvk
vgdivifndgygvksekidneevlimsesdilaivea
>d1aonp_ 2.31.1.1.1 Chaperonin-10 (GroES) {Escherichia coli}
mnirplhdrvivkrkevetksaggivltgsaaakstrgevlavgngrilengevkpldvk
vgdivifndgygvksekidneevlimsesdilaivea
>d1aonq_ 2.31.1.1.1 Chaperonin-10 (GroES) {Escherichia coli}
mnirplhdrvivkrkevetksaggivltgsaaakstrgevlavgngrilengevkpldvk
vgdivifndgygvksekidneevlimsesdilaivea
>d1aonr_ 2.31.1.1.1 Chaperonin-10 (GroES) {Escherichia coli}
mnirplhdrvivkrkevetksaggivltgsaaakstrgevlavgngrilengevkpldvk
vgdivifndgygvksekidneevlimsesdilaivea
>d1aons_ 2.31.1.1.1 Chaperonin-10 (GroES) {Escherichia coli}
mnirplhdrvivkrkevetksaggivltgsaaakstrgevlavgngrilengevkpldvk
vgdivifndgygvksekidneevlimsesdilaivea
>d1aont_ 2.31.1.1.1 Chaperonin-10 (GroES) {Escherichia coli}
mnirplhdrvivkrkevetksaggivltgsaaakstrgevlavgngrilengevkpldvk
vgdivifndgygvksekidneevlimsesdilaivea
>d1aonu_ 2.31.1.1.1 Chaperonin-10 (GroES) {Escherichia coli}
mnirplhdrvivkrkevetksaggivltgsaaakstrgevlavgngrilengevkpldvk
vgdivifndgygvksekidneevlimsesdilaivea
>d1aoo__ 7.38.1.1.5 Metallothionein {Baker's yeast (Saccharomyces cerevisiae)}
qneghecqcqcgscknneqcqkscscptgcnsddkcpcgn
>d1aop_1 4.47.29.1.1 (81-145) Sulfite reductase, domains 1 and 3 {Escherichia coli}
llrcrlpggvittkqwqaidkfagentiygsirltnrqtfqfhgilkknvkpvhqmlhsv
gldal
>d1aop_2 4.47.29.1.1 (346-425) Sulfite reductase, domains 1 and 3 {Escherichia coli}
igwvkgiddnwhltlfiengrildyparplktglleiakihkgdfritanqnliiagvpe
sekakiekiakesglmnavt
>d1aop_3 4.108.1.1.1 (149-345) Sulfite reductase hemoprotein (SiRHP), domains 2 and 4 {Escherichia coli}
ndmnrnvlctsnpyesqlhaeayewakkisehllprtrayaeiwldqekvattdeepilg
qtylprkfkttvvippqndidlhandmnfvaiaengklvgfnllvggglsiehgnkktya
rtasefgylplehtlavaeavvttqrdwgnrtdrknaktkytlervgvetfkaeverrag
ikfepirpyeftgrgdr
>d1aop_4 4.108.1.1.1 (426-570) Sulfite reductase hemoprotein (SiRHP), domains 2 and 4 {Escherichia coli}
pqrensmacvsfptcplamaeaerflpsfidnidnlmakhgvsdehivmrvtgcpngcgr
amlaevglvgkapgrynlhlggnrigtriprmykenitepeilasldeligrwakereag
egfgdftvragiirpvldpardlwd
>d1aoqa1 1.3.1.2.1 (17-133) N-terminal (heme c) domain of cytochrome cd1-nitrite reductase {Thiosphaera pantotropha}
hktrtdnryepsldnlaqqdvaapgapegvtalsdaqyneankiyfercagchgvlrkga
tgkaltpdltrdlgfdylqsfityaspagmpnwgtsgelsaeqvdlmanyllldpaa
>d1aoqa2 2.61.2.1.1 (134-567) C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase {Thiosphaera pantotropha}
ppefgmkemreswkvhvapedrptqqmndwdlenlfsvtlrdagqialidgstyeiktvl
dtgyavhisrlsasgrylfvigrdgkvnmidlwmkepttvaeikigsearsietskmegw
edkyaiagaywppqyvimdgetlepkkiqstrgmtydeqeyhpeprvaailashyrpefi
vnvketgkillvdytdlnnlktteisaerflhdggldgshryfitaanarnklvvidtke
gklvaiedtggqtphpgrganfvhptfgpvwatshmgddsvaligtdpeghpdnawkild
sfpalgggslfikthpnsqylyvdatlnpeaeisgsvavfdikamtgdgsdpefktlpia
ewagitegqprvvqgefnkdgtevwfsvwngkdqesalvvvddktlelkhvikderlvtp
tgkfnvyntmtdty
>d1aoqb1 1.3.1.2.1 (9-133) N-terminal (heme c) domain of cytochrome cd1-nitrite reductase {Thiosphaera pantotropha}
dpaaaledhktrtdnryepsldnlaqqdvaapgapegvtalsdaqyneankiyfercagc
hgvlrkgatgkaltpdltrdlgfdylqsfityaspagmpnwgtsgelsaeqvdlmanyll
ldpaa
>d1aoqb2 2.61.2.1.1 (134-567) C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase {Thiosphaera pantotropha}
ppefgmkemreswkvhvapedrptqqmndwdlenlfsvtlrdagqialidgstyeiktvl
dtgyavhisrlsasgrylfvigrdgkvnmidlwmkepttvaeikigsearsietskmegw
edkyaiagaywppqyvimdgetlepkkiqstrgmtydeqeyhpeprvaailashyrpefi
vnvketgkillvdytdlnnlktteisaerflhdggldgshryfitaanarnklvvidtke
gklvaiedtggqtphpgrganfvhptfgpvwatshmgddsvaligtdpeghpdnawkild
sfpalgggslfikthpnsqylyvdatlnpeaeisgsvavfdikamtgdgsdpefktlpia
ewagitegqprvvqgefnkdgtevwfsvwngkdqesalvvvddktlelkhvikderlvtp
tgkfnvyntmtdty
>d1aora1 1.104.1.1.1 (211-605) Aldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
iadkqkfmlvvrekvnklrndpvaggglpkygtavlvniinenglypvknfqtgvypyay
eqsgeamaakylvrnkpcyacpigcgrvnrlptvgetegpeyesvwalganlgindlasi
ieanhmcdelgldtistggtlatamelyekghikdeelgdappfrwgntevlhyyiekia
kregfgdklaegsyrlaesyghpelsmtvkklelpaydprgaeghglgyatnnrggchik
nymispeilgypykmdphdvsddkikmlilfqdltalidsaglclfttfglgaddyrdll
naalgwdfttedylkigeriwnaerlfnlkagldparddtlpkrfleepmpegpnkghtv
rlkemlpryyklrgwtedgkipkekleelgiaefy
>d1aora2 4.123.1.1.1 (1-210) Aldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
mygnwgrfirvnlstgdikveeydeelakkwlgsrglaiylllkemdptvdplspenkli
iaagpltgtsaptggrynvvtkspltgfitmansggyfgaelkfagydaivvegkaekpv
yiyikdehieirdashiwgkkvseteatirkevgsekvkiasigpagenlvkfaaimndg
hraagrggvgavmgsknlkaiavegsktvp
>d1aorb1 1.104.1.1.1 (211-605) Aldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
iadkqkfmlvvrekvnklrndpvaggglpkygtavlvniinenglypvknfqtgvypyay
eqsgeamaakylvrnkpcyacpigcgrvnrlptvgetegpeyesvwalganlgindlasi
ieanhmcdelgldtistggtlatamelyekghikdeelgdappfrwgntevlhyyiekia
kregfgdklaegsyrlaesyghpelsmtvkklelpaydprgaeghglgyatnnrggchik
nymispeilgypykmdphdvsddkikmlilfqdltalidsaglclfttfglgaddyrdll
naalgwdfttedylkigeriwnaerlfnlkagldparddtlpkrfleepmpegpnkghtv
rlkemlpryyklrgwtedgkipkekleelgiaefy
>d1aorb2 4.123.1.1.1 (1-210) Aldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
mygnwgrfirvnlstgdikveeydeelakkwlgsrglaiylllkemdptvdplspenkli
iaagpltgtsaptggrynvvtkspltgfitmansggyfgaelkfagydaivvegkaekpv
yiyikdehieirdashiwgkkvseteatirkevgsekvkiasigpagenlvkfaaimndg
hraagrggvgavmgsknlkaiavegsktvp
>d1aosa_ 1.117.1.1.4 Argininosuccinate lyase/delta-crystallin {Human (Homo sapiens)}
imekfnasiaydrhlwevdvqgskaysrglekaglltkaemdqilhgldkvaeewaqgtf
klnsndedihtanerrlkeligatagklhtgrsrndqvvtdlrlwmrqtcstlsgllwel
irtmvdraeaerdvlfpgythlqraqpirwshwilshavaltrdserllevrkrinvlpl
gsgaiagnplgvdrellraelnfgaitlnsmdatserdfvaeflfwrslcmthlsrmaed
lilyctkefsfvqlsdaystgsslmpqkknpdslelirskagrvfgrcagllmtlkglps
tynkdlqedkeavfevsdtmsavlqvatgvistlqihqenmgqalspdmlatdlayylvr
kgmpfrqaheasgkavfmaetkgvalnqlslqelqtisplfsgdvicvwdyrhsveqyga
lggtarssvdwqirqvrallqaq
>d1aosb_ 1.117.1.1.4 Argininosuccinate lyase/delta-crystallin {Human (Homo sapiens)}
imekfnasiaydrhlwevdvqgskaysrglekaglltkaemdqilhgldkvaeewaqgtf
klnsndedihtanerrlkeligatagklhtgrsrndqvvtdlrlwmrqtcstlsgllwel
irtmvdraeaerdvlfpgythlqraqpirwshwilshavaltrdserllevrkrinvlpl
gsgaiagnplgvdrellraelnfgaitlnsmdatserdfvaeflfwrslcmthlsrmaed
lilyctkefsfvqlsdaystgsslmpqkknpdslelirskagrvfgrcagllmtlkglps
tynkdlqedkeavfevsdtmsavlqvatgvistlqihqenmgqalspdmlatdlayylvr
kgmpfrqaheasgkavfmaetkgvalnqlslqelqtisplfsgdvicvwdyrhsveqyga
lggtarssvdwqirqvrallqaq
>d1aotf_ 4.72.1.1.5 Tyrosine kinase Fyn {Human (Homo sapiens)}
siqaeewyfgklgrkdaerqllsfgnprgtfliresettkgayslsirdwddmkgdhvkh
ykirkldnggyyittraqfetlqqlvqhyseraaglssrlvvpshk
>d1aouf_ 4.72.1.1.5 Tyrosine kinase Fyn {Human (Homo sapiens)}
siqaeewyfgklgrkdaerqllsfgnprgtfliresettkgayslsirdwddmkgdhvkh
ykirkldnggyyittraqfetlqqlvqhyseraaglssrlvvpshk
>d1aov_1 3.84.1.2.5 (1-334) Ovotransferrin {Duck (Anas platyrhynchos)}
appkttvrwctissaeekkcnslkdhmqqervtlscvqkatyldcikaisnneadaisld
ggqvfeaglapyklkpiaaevyersggsttsyyavavvkkgtdfmikdlrgktschtglg
rsagwnipigtlihrediewegiesgiseqavakffsascvpgatieqklcrqckgdakt
kclrngpysgysgafqclkdgkgdvafvkhttvqenapeekdeyellcldgsrqpvdsyk
tcnwarvaahavvarddskiddiwsflgmqayslgvdttsdfhlfgppgkkdpvlkdllf
kdsaimlkrvpelmdsqlylgfeyysaiqslrkd
>d1aov_2 3.84.1.2.5 (335-686) Ovotransferrin {Duck (Anas platyrhynchos)}
qltvgprenkiqwcavgkdekskcdrwsvvsngevectilddnkdcivkitkgeadaisl
dggfvytagvcglvpvvgesyedetqcskdeeqpayyfavavvkkssaitwnnlqgkksc
htavgrtagwnipmglihnktgscdfddyfsegcapgsppnsrlcklcqgsgenllekcv
asshekyygytgalrclveqgdvafikhstvgenvsgsnkddwakgltrddfellctngk
raktmdyktchlakvpthavvarpekankirellegqeklfglhgtekerfmmfqsqtkd
llfkaltkclvklrqgitykeflgdeyyasvaslntcnpsdllqvctfledk
>d1aow__ 1.66.1.1.3 Annexin IV {Bovine (Bos taurus)}
asgfnaaedaqtlrkamkglgtdedaiinvlayrstaqrqeirtaykttigrdlmddlks
elsgnfeqvilgmmtptvlydvqevrkamkgagtdegclieilasrtpeeirrinqtyql
qygrsleddirsdtsfmfqrvlvslsaggrdesnylddalmrqdaqdlyeagekkwgtde
vkfltvlcsrnrnhllhvfdeykriaqkdieqsiksetsgsfedallaivkcmrnksayf
aerlyksmkglgtdddtlirvmvsraeidmldiranfkrlygkslysfikgdtsgdyrkv
llilcggdd
>d1aoxa_ 3.52.1.1.5 Integrin alpha2-beta1 {Human (Homo sapiens)}
scpslidvvvvcdesnsiypwdavknflekfvqgldigptktqvgliqyannprvvfnln
tyktkeemivatsqtsqyggdltntfgaiqyarkyaysaasggrrsatkvmvvvtdgesh
dgsmlkavidqcnhdnilrfgiavlgylnrnaldtknlikeikaiasipteryffnvsde
aallekagtlgeqifsieggt
>d1aoxb_ 3.52.1.1.5 Integrin alpha2-beta1 {Human (Homo sapiens)}
rsscpslidvvvvcdesnsiypwdavknflekfvqgldigptktqvgliqyannprvvfn
lntyktkeemivatsqtsqyggdltntfgaiqyarkyaysaasggrrsatkvmvvvtdge
shdgsmlkavidqcnhdnilrfgiavlgylnrnaldtknlikeikaiasipteryffnvs
deaallekagtlgeqifsieg
>d1aoy__ 1.4.3.3.1 Arginine repressor (ArgR), N-terminal DNA-binding domain {Escherichia coli}
mrssakqeelvkafkallkeekfssqgeivaalqeqgfdninqskvsrmltkfgavrtrn
akmemvyclpaelgvptt
>d1aoza1 2.5.1.3.4 (1-129) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
sqirhykweveymfwapncnenivmgingqfpgptiranagdsvvveltnklhtegvvih
whgilqrgtpwadgtasisqcainpgetffynftvdnpgtffyhghlgmqrsaglygsli
vdppqgkke
>d1aoza2 2.5.1.3.4 (130-338) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
pfhydgeinlllsdwwhqsihkqevglsskpirwigepqtillngrgqfdcsiaakydsn
lepcklkgsescapyifhvspkktyririasttalaalnfaignhqllvveadgnyvqpf
ytsdidiysgesysvlittdqnpsenywvsvgtrarhpntppgltllnylpnsvsklpts
pppqtpawddfdrsknftyritaamgspk
>d1aoza3 2.5.1.3.4 (339-552) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
ppvkfnrrifllntqnvingyvkwaindvslalpptpylgamkynllhafdqnpppevfp
edydidtpptnektrigngvyqfkigevvdvilqnanmmkenlsethpwhlhghdfwvlg
ygdgkfsaeeesslnlknpplrntvvifpygwtairfvadnpgvwafhchiephlhmgmg
vvfaegvekvgriptkalacggtakslinnpknp
>d1aozb1 2.5.1.3.4 (1-129) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
sqirhykweveymfwapncnenivmgingqfpgptiranagdsvvveltnklhtegvvih
whgilqrgtpwadgtasisqcainpgetffynftvdnpgtffyhghlgmqrsaglygsli
vdppqgkke
>d1aozb2 2.5.1.3.4 (130-338) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
pfhydgeinlllsdwwhqsihkqevglsskpirwigepqtillngrgqfdcsiaakydsn
lepcklkgsescapyifhvspkktyririasttalaalnfaignhqllvveadgnyvqpf
ytsdidiysgesysvlittdqnpsenywvsvgtrarhpntppgltllnylpnsvsklpts
pppqtpawddfdrsknftyritaamgspk
>d1aozb3 2.5.1.3.4 (339-552) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
ppvkfnrrifllntqnvingyvkwaindvslalpptpylgamkynllhafdqnpppevfp
edydidtpptnektrigngvyqfkigevvdvilqnanmmkenlsethpwhlhghdfwvlg
ygdgkfsaeeesslnlknpplrntvvifpygwtairfvadnpgvwafhchiephlhmgmg
vvfaegvekvgriptkalacggtakslinnpknp
>d1ap0__ 4.8.2.2.1 Modifier protein 1 (HP1 beta) {Mouse (Mus musculus)}
hmveevleeeeeeyvvekvldrrvvkgkveyllkwkgfsdedntwepeenldcpdliaef
lqsqktahetdks
>d1ap2a_ 2.1.1.1.91 Immunoglobulin (variable domains of L and H chains) {scFv c219}
divmtqspssltvtagekvtmsckssqsllnsgnqknyltwyqqkpgqppklliywastr
esgvpdrftgsgsgtdftltissvqaedlavyycqndysypltfgagtklep
>d1ap2b_ 2.1.1.1.91 Immunoglobulin (variable domains of L and H chains) {scFv c219}
evqlqqsgaelvrpgasvklsctasgfnikddfmhwvkqrpeqglewigridpandntky
apkfqdkatiiadtssntaylqlssltsedtavyycarrevysyyspldvwgagttvtvp
>d1ap2c_ 2.1.1.1.91 Immunoglobulin (variable domains of L and H chains) {scFv c219}
divmtqspssltvtagekvtmsckssqsllnsgnqknyltwyqqkpgqppklliywastr
esgvpdrftgsgsgtdftltissvqaedlavyycqndysypltfgagtklepg
>d1ap2d_ 2.1.1.1.91 Immunoglobulin (variable domains of L and H chains) {scFv c219}
evqlqqsgaelvrpgasvklsctasgfnikddfmhwvkqrpeqglewigridpandntky
apkfqdkatiiadtssntaylqlssltsedtavyycarrevysyyspldvwgagttvtvp
sgs
>d1ap4__ 1.42.1.5.4 Troponin C {Human (Homo sapiens), cardiac isoform}
mddiykaaveqlteeqknefkaafdifvlgaedgcistkelgkvmrmlgqnptpeelqem
idevdedgsgtvdfdeflvmmvrcmkdds
>d1ap5a1 1.2.7.1.6 (1-83) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaafvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1ap5a2 4.37.1.1.3 (84-198) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
ngggepkgelleaikrdfgsfdkfkekltaasvgvqgsgwgwlgfnkerghlqiaacpnq
dplqgttglipllgidvwehayylqyknvrpdylkaiwnvinwenvterymackk
>d1ap5b1 1.2.7.1.6 (1-83) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaafvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1ap5b2 4.37.1.1.3 (84-198) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
ngggepkgelleaikrdfgsfdkfkekltaasvgvqgsgwgwlgfnkerghlqiaacpnq
dplqgttglipllgidvwehayylqyknvrpdylkaiwnvinwenvterymackk
>d1ap6a1 1.2.7.1.6 (1-83) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaafvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1ap6a2 4.37.1.1.3 (84-198) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
ngggepkgelleaikrdfgsfdkfkekltaasvgvqgsgwgwlgfnkerghlqiaacpnq
dplqgttglipllgidvwehayylqyknvrpdylkaiwnvinwenvterymackk
>d1ap6b1 1.2.7.1.6 (1-83) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaafvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1ap6b2 4.37.1.1.3 (84-198) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
ngggepkgelleaikrdfgsfdkfkekltaasvgvqgsgwgwlgfnkerghlqiaacpnq
dplqgttglipllgidvwehayylqyknvrpdylkaiwnvinwenvterymackk
>d1ap7__ 1.110.2.1.6 Cell cycle inhibitor p16ink4A {Mouse (Mus musculus)}
gsmlleevcvgdrlsgaaargdvqevrrllhrelvhpdalnrfgktalqvmmfgspaval
ellkqgaspnvqdasgtspvhdaartgfldtlkvlvehgadvnaldstgslpihlaireg
hssvvsflapesdlhhrdasgltplelarqrgaqnlmdilqghmmipm
>d1ap8__ 4.66.1.1.1 Translation initiation factor eIF4e {Baker's yeast (Saccharomyces cerevisiae)}
msveevskkfeenvsvddttatpktvlsdsahfdvkhplntkwtlwytkpavdkseswsd
llrpvtsfqtveefwaiiqnipephelplksdyhvfrndvrpewedeanakggkwsfqlr
gkgadidelwlrtllavigetideddsqingvvlsirkggnkfalwtksedkepllrigg
kfkqvlkltddghleffphssangrhpqpsitl
>d1ap9__ 6.2.1.1.2 Bacteriorhodopsin {Halobacterium salinarium}
rpewiwlalgtalmglgtlyflvkgmgvsdpdakkfyaittlvpaiaftmylsmllgygl
tmvpfggeqnpiywaryadwlfttplllldlallvdadqgtilalvgadgimigtglvga
ltkvysyrfvwwaistaamlyilyvlffgftskaesmrpevastfkvlrnvtvvlwsayp
vvwligsegagivplnietllfmvldvsakvgfglillr
>d1apa__ 4.135.1.1.6 Pokeweed antiviral protein alpha {Pokeweed (Phytolacca americana)}
intitfdvgnatinkyatfmksihnqakdptlkcygipmlpntnltpkyllvtlqdsslk
titlmlkrnnlyvmgyadtyngkcryhifkdisntterndvmttlcpnpssrvgkninyd
ssypalekkvgrprsqvqlgiqilnsgigkiygvdsftekteaefllvaiqmvseaarfk
yienqvktnfnrafypnakvlnleeswgkistaihnakngaltsplelknangskwivlr
vddiepdvgllkyvngtcqat
>d1apb__ 3.83.1.1.2 L-arabinose-binding protein {Escherichia coli}
nlklgflvkqpeepwfqtewkfadkagkdlgfevikiavpdgektlnaidslaasgakgf
victpdpklgsaivakargydmkviavddqfvnakgkpmdtvplvmmaatkigerqgqel
ykemqkrgwdvkesavmaitaneldtarrrttgsmdalkaagfpekqiyqvptksndipg
afdaansmlvqhpevkhwlivgmndstvlggvrategqgfkaadiigigingvdavsels
kaqatgfygsllgspdvhgykssemlynwvakdveppkftevtdvvlitrdnfkeelekk
glggk
>d1apc__ 1.25.3.1.1 Cytochrome b562 {Escherichia coli}
adlednmetlndnlkviekadnaaqvkdaltkmraaaldaqkatppkledkspdspemkd
frhgfdilvgqiddalklanegkvkeaqaaaeqlkttrnayhqkyr
>d1apf__ 7.9.1.1.8 Anthopleurin-B {Giant green sea anemone (Anthopleura xanthogrammica)}
gvpclcdsdgprprgntlsgilwfypsgcpsgwhnckahgpnigwcckk
>d1apga_ 4.135.1.1.7 Ricin A-chain {Castor bean (Ricinus communis)}
ifpkqypiinfttagatvqsytnfiravrgrlttgadvrheipvlpnrvglpinqrfilv
elsnhaelsvtlaldvtnayvvgyragnsayffhpdnqedaeaithlftdvqnrytfafg
gnydrleqlagnlrenielgngpleeaisalyyystggtqlptlarsfiiciqmiseaar
fqyiegemrtrirynrrsapdpsvitlenswgrlstaiqesnqgafaspiqlqrrngskf
svydvsilipiialmvyrcapppssqf
>e1aph.1a 7.1.1.1.1 Insulin {Bovine (Bos taurus)}
giveqccasvcslyqlenycn
>e1aph.1b 7.1.1.1.1 Insulin {Bovine (Bos taurus)}
fvnqhlcgshlvealylvcgergffytpka
>d1apj__ 7.23.1.1.1 Fibrillin {Human (Homo sapiens)}
saqdlrmsycyakfeggkcsspksrnhskqecccalkgegwgdpcelcptepdeafrqic
pygsgiivgpddsa
>d1aplc_ 1.4.1.1.3 mat alpha2 Homeodomain {Baker's yeast (Saccharomyces cerevisiae)}
yrghrftkenvrileswfaknienpyldtkglenlmkntslsriqiknwvsnrrrkekt
>d1apld_ 1.4.1.1.3 mat alpha2 Homeodomain {Baker's yeast (Saccharomyces cerevisiae)}
rghrftkenvrileswfaknienpyldtkglenlmkntslsriqiknwvsnrrrkekt
>d1apme_ 4.117.1.1.5 cAMP-dependent PK, catalytic subunit {Mouse (Mus musculus)}
seqesvkeflakakedflkkwetpsqntaqldqfdriktlgtgsfgrvmlvkhkesgnhy
amkildkqkvvklkqiehtlnekrilqavnfpflvklefsfkdnsnlymvmeyvaggemf
shlrrigrfaepharfyaaqivltfeylhsldliyrdlkpenllidqqgyiqvtdfgfak
rvkgrtwtlcgtpeylapeiilskgynkavdwwalgvliyemaagyppffadqpiqiyek
ivsgkvrfpshfssdlkdllrnllqvdltkrfgnlkngvndiknhkwfattdwiaiyqrk
veapfipkfkgpgdtsnfddyeeeeirvsinekcgkeftef
>d1apna_ 2.26.1.1.1 Concanavalin A {Jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1apnb_ 2.26.1.1.1 Concanavalin A {Jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1apo__ 7.3.11.1.6 Factor X, N-terminal module {Bovine (Bos taurus)}
kdgdqceghpclnqghckdgigdytctcaegfegkncefstr
>d1apq__ 7.3.11.1.19 Complement protease C1R {Human (Homo sapiens)}
avdldecasrsksgeedpqpqcqhlchnyvggyfcscrpgyelqedrhscqae
>d1aps__ 4.47.10.1.2 Acylphosphatase {Horse (Equus caballus)}
starplksvdyevfgrvqgvcfrmyaedearkigvvgwvkntskgtvtgqvqgpeekvns
mkswlskvgspssridrtnfsnektiskleysnfsvry
>d1apte_ 2.44.1.2.2 Acid protease {Fungus (Penicillium janthinellum), penicillopepsin}
aasgvatntptandeeyitpvtiggttlnlnfdtgsadlwvfstelpasqqsghsvynps
atgkelsgytwsisygdgssasgnvftdsvtvggvtahgqavqaaqqisaqfqqdtnndg
llglafssintvqpqsqttffdtvksslaqplfavalkhqqpgvydfgfidsskytgslt
ytgvdnsqgfwsfnvdsytagsqsgdgfsgiadtgttllllddsvvsqyysqvsgaqqds
naggyvfdcstnlpdfsvsisgytatvpgslinygpsgdgstclggiqsnsgigfsifgd
iflksqyvvfdsdgpqlgfapqa
>d1apue_ 2.44.1.2.2 Acid protease {Fungus (Penicillium janthinellum), penicillopepsin}
aasgvatntptandeeyitpvtiggttlnlnfdtgsadlwvfstelpasqqsghsvynps
atgkelsgytwsisygdgssasgnvftdsvtvggvtahgqavqaaqqisaqfqqdtnndg
llglafssintvqpqsqttffdtvksslaqplfavalkhqqpgvydfgfidsskytgslt
ytgvdnsqgfwsfnvdsytagsqsgdgfsgiadtgttllllddsvvsqyysqvsgaqqds
naggyvfdcstnlpdfsvsisgytatvpgslinygpsgdgstclggiqsnsgigfsifgd
iflksqyvvfdsdgpqlgfapqa
>d1apve_ 2.44.1.2.2 Acid protease {Fungus (Penicillium janthinellum), penicillopepsin}
aasgvatntptandeeyitpvtiggttlnlnfdtgsadlwvfstelpasqqsghsvynps
atgkelsgytwsisygdgssasgnvftdsvtvggvtahgqavqaaqqisaqfqqdtnndg
llglafssintvqpqsqttffdtvksslaqplfavalkhqqpgvydfgfidsskytgslt
ytgvdnsqgfwsfnvdsytagsqsgdgfsgiadtgttllllddsvvsqyysqvsgaqqds
naggyvfdcstnlpdfsvsisgytatvpgslinygpsgdgstclggiqsnsgigfsifgd
iflksqyvvfdsdgpqlgfapqa
>d1apwe_ 2.44.1.2.2 Acid protease {Fungus (Penicillium janthinellum), penicillopepsin}
aasgvatntptandeeyitpvtiggttlnlnfdtgsadlwvfstelpasqqsghsvynps
atgkelsgytwsisygdgssasgnvftdsvtvggvtahgqavqaaqqisaqfqqdtnndg
llglafssintvqpqsqttffdtvksslaqplfavalkhqqpgvydfgfidsskytgslt
ytgvdnsqgfwsfnvdsytagsqsgdgfsgiadtgttllllddsvvsqyysqvsgaqqds
naggyvfdcstnlpdfsvsisgytatvpgslinygpsgdgstclggiqsnsgigfsifgd
iflksqyvvfdsdgpqlgfapqa
>d1apxa_ 1.90.1.1.5 Ascorbate peroxidase {Pea (Pisum sativum)}
gksyptvspdyqkaiekakrklrgfiaekkcaplilrlawhsagtfdsktktggpfgtik
hqaelahganngldiavrllepikeqfpivsyadfyqlagvvaveitggpevpfhpgred
kpepppegrlpdatkgsdhlrdvfgkamglsdqdivalsgghtigaahkersgfegpwts
nplifdnsyftelltgekdgllqlpsdkalltdsvfrplvekyaadedvffadyaeahlk
lselgfaea
>d1apxb_ 1.90.1.1.5 Ascorbate peroxidase {Pea (Pisum sativum)}
gksyptvspdyqkaiekakrklrgfiaekkcaplilrlawhsagtfdsktktggpfgtik
hqaelahganngldiavrllepikeqfpivsyadfyqlagvvaveitggpevpfhpgred
kpepppegrlpdatkgsdhlrdvfgkamglsdqdivalsgghtigaahkersgfegpwts
nplifdnsyftelltgekdgllqlpsdkalltdsvfrplvekyaadedvffadyaeahlk
lselgfaea
>d1apxc_ 1.90.1.1.5 Ascorbate peroxidase {Pea (Pisum sativum)}
gksyptvspdyqkaiekakrklrgfiaekkcaplilrlawhsagtfdsktktggpfgtik
hqaelahganngldiavrllepikeqfpivsyadfyqlagvvaveitggpevpfhpgred
kpepppegrlpdatkgsdhlrdvfgkamglsdqdivalsgghtigaahkersgfegpwts
nplifdnsyftelltgekdgllqlpsdkalltdsvfrplvekyaadedvffadyaeahlk
lselgfaea
>d1apxd_ 1.90.1.1.5 Ascorbate peroxidase {Pea (Pisum sativum)}
gksyptvspdyqkaiekakrklrgfiaekkcaplilrlawhsagtfdsktktggpfgtik
hqaelahganngldiavrllepikeqfpivsyadfyqlagvvaveitggpevpfhpgred
kpepppegrlpdatkgsdhlrdvfgkamglsdqdivalsgghtigaahkersgfegpwts
nplifdnsyftelltgekdgllqlpsdkalltdsvfrplvekyaadedvffadyaeahlk
lselgfaea
>e1apy.1a 4.124.1.4.1 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Human (Homo sapiens)}
splplvvntwpfknateaawralasggsaldavesgcamcereqcdgsvgfggspdelge
ttldamimdgttmdvgavgdlrriknaigvarkvlehtthtllvgesattfaqsmgfine
dlstsasqalhsdwlarncqpnywrnvipdpskycgpykpp
>e1apy.1b 4.124.1.4.1 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Human (Homo sapiens)}
tigmvvihktghiaagtstngikfkihgrvgdspipgagayaddtagaaaatgngdilmr
flpsyqaveymrrgedptiacqkvisriqkhfpeffgavicanvtgsygaacnklstftq
fsfmvynseknqpteekvdci
>e1apy.2c 4.124.1.4.1 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Human (Homo sapiens)}
splplvvntwpfknateaawralasggsaldavesgcamcereqcdgsvgfggspdelge
ttldamimdgttmdvgavgdlrriknaigvarkvlehtthtllvgesattfaqsmgfine
dlstsasqalhsdwlarncqpnywrnvipdpskycgpykpp
>e1apy.2d 4.124.1.4.1 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Human (Homo sapiens)}
tigmvvihktghiaagtstngikfkihgrvgdspipgagayaddtagaaaatgngdilmr
flpsyqaveymrrgedptiacqkvisriqkhfpeffgavicanvtgsygaacnklstftq
fsfmvynseknqpteekvdci
>e1apz.1a 4.124.1.4.1 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Human (Homo sapiens)}
splplvvntwpfknateaawralasggsaldavesgcamcereqcdgsvgfggspdelge
ttldamimdgttmdvgavgdlrriknaigvarkvlehtthtllvgesattfaqsmgfine
dlstsasqalhsdwlarncqpnywrnvipdpskycgpykpp
>e1apz.1b 4.124.1.4.1 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Human (Homo sapiens)}
tigmvvihktghiaagtstngikfkihgrvgdspipgagayaddtagaaaatgngdilmr
flpsyqaveymrrgedptiacqkvisriqkhfpeffgavicanvtgsygaacnklstftq
fsfmvynseknqpteekvdci
>e1apz.2c 4.124.1.4.1 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Human (Homo sapiens)}
splplvvntwpfknateaawralasggsaldavesgcamcereqcdgsvgfggspdelge
ttldamimdgttmdvgavgdlrriknaigvarkvlehtthtllvgesattfaqsmgfine
dlstsasqalhsdwlarncqpnywrnvipdpskycgpykpp
>e1apz.2d 4.124.1.4.1 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Human (Homo sapiens)}
tigmvvihktghiaagtstngikfkihgrvgdspipgagayaddtagaaaatgngdilmr
flpsyqaveymrrgedptiacqkvisriqkhfpeffgavicanvtgsygaacnklstftq
fsfmvynseknqpteekvdci
>d1aq0a_ 3.1.7.3.11 Plant beta-glucanases {Barley (Hordeum vulgare), 1,3-1,4-beta-glucanase}
igvcygmsannlpaastvvsmfksngiksmrlyapnqaalqavggtginvvvgapndvls
nlaaspaaaaswvksniqaypkvsfryvcvgnevaggatrnlvpamknvhgalvaaglgh
ikvttsvsqailgvfsppsagsftgeaaafmgpvvqflartnaplmaniypylawaynps
amdmgyalfnasgtvvrdgaygyqnlfdttvdafytamgkhggssvklvvsesgwpsggg
taatpanarfynqhlinhvgrgtprhpgaietyifamfnenqkdsgveqnwglfypnmqh
vypinf
>d1aq0b_ 3.1.7.3.11 Plant beta-glucanases {Barley (Hordeum vulgare), 1,3-1,4-beta-glucanase}
igvcygmsannlpaastvvsmfksngiksmrlyapnqaalqavggtginvvvgapndvls
nlaaspaaaaswvksniqaypkvsfryvcvgnevaggatrnlvpamknvhgalvaaglgh
ikvttsvsqailgvfsppsagsftgeaaafmgpvvqflartnaplmaniypylawaynps
amdmgyalfnasgtvvrdgaygyqnlfdttvdafytamgkhggssvklvvsesgwpsggg
taatpanarfynqhlinhvgrgtprhpgaietyifamfnenqkdsgveqnwglfypnmqh
vypinf
>d1aq1__ 4.117.1.1.1 Cyclin-dependent PK (different isozymes) {Human (Homo sapiens)}
menfqkvekigegtygvvykarnkltgevvalkkirldtetegvpstaireisllkelnh
pnivklldvihtenklylvfeflhqdlkkfmdasaltgiplpliksylfqllqglafchs
hrvlhrdlkpqnllintegaikladfglarafgvpvrtythevvtlwyrapeillgckyy
stavdiwslgcifaemvtrralfpgdseidqlfrifrtlgtpdevvwpgvtsmpdykpsf
pkwarqdfskvvppldedgrsllsqmlhydpnkrisakaalahpffqdvtkpvphlrl
>d1aq2__ 3.81.1.1.1 Phosphoenolpyruvate carboxykinase (ATP-oxaloacetate carboxy-liase) {Escherichia coli}
nngltpqeleaygisdvhdivynpsydllyqeeldpsltgyergvltnlgavavdtgift
grspkdkyivrddttrdtfwwadkgkgkndnkplspetwqhlkglvtrqlsgkrlfvvda
fcganpdtrlsvrfitevawqahfvknmfirpsdeelagfkpdfivmngakctnpqwkeq
glnsenfvafnltermqliggtwyggemkkgmfsmmnyllplkgiasmhcsanvgekgdv
avffglsgtgkttlstdpkrrligddehgwdddgvfnfeggcyaktiklskeaepeiyna
irrdallenvtvredgtidfddgsktentrvsypiyhidnivkpvskaghatkvifltad
afgvlppvsrltadqtqyhflsgftaklagtergiteptptfsacfgaaflslhptqyae
vlvkrmqaagaqaylvntgwngtgkrisikdtraiidailngsldnaetftlpmfnlaip
telpgvdtkildprntyaspeqwqekaetlaklfidnfdkytdtpagaalvaagpkl
>d1aq3a_ 4.65.1.1.1 MS2 virus coat protein {Bacteriophage MS2}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvtcsvrqssaqnrkysi
kvevpkvatqtvggvelpvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1aq3b_ 4.65.1.1.1 MS2 virus coat protein {Bacteriophage MS2}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvtcsvrqssaqnrkysi
kvevpkvatqtvggvelpvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1aq3c_ 4.65.1.1.1 MS2 virus coat protein {Bacteriophage MS2}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvtcsvrqssaqnrkysi
kvevpkvatqtvggvelpvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1aq4a_ 4.65.1.1.1 MS2 virus coat protein {Bacteriophage MS2}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvacsvrqssaqnrkyti
kvevpkvatqtvggvelpvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1aq4b_ 4.65.1.1.1 MS2 virus coat protein {Bacteriophage MS2}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvacsvrqssaqnrkyti
kvevpkvatqtvggvelpvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1aq4c_ 4.65.1.1.1 MS2 virus coat protein {Bacteriophage MS2}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvacsvrqssaqnrkyti
kvevpkvatqtvggvelpvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1aq6a_ 5.17.1.1.2 L-2-Haloacid dehalogenase {Xanthobacter autotrophicus}
mikavvfdaygtlfdvqsvadateraypgrgeyitqvwrqkqleyswlralmgryadfwg
vtrealaytlgtlglepdesfladmaqaynrltpypdaaqclaelaplkrailsngapdm
lqalvanagltdsfdavisvdakrvfkphpdsyalveevlgvtpaevlfvssngfdvgga
knfgfsvarvarlsqealarelvsgtiapltmfkalrmreetyaeapdfvvpalgdlprl
vrgma
>d1aq6b_ 5.17.1.1.2 L-2-Haloacid dehalogenase {Xanthobacter autotrophicus}
mikavvfdaygtlfdvqsvadateraypgrgeyitqvwrqkqleyswlralmgryadfwg
vtrealaytlgtlglepdesfladmaqaynrltpypdaaqclaelaplkrailsngapdm
lqalvanagltdsfdavisvdakrvfkphpdsyalveevlgvtpaevlfvssngfdvgga
knfgfsvarvarlsqealarelvsgtiapltmfkalrmreetyaeapdfvvpalgdlprl
vrgma
>d1aq7__ 2.41.1.2.1 Trypsin(ogen) {Bovine (Bos taurus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1aq8a1 2.5.1.3.2 (9-166) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
iaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhamafngtv
pgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilrfkatk
pgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>d1aq8a2 2.5.1.3.2 (167-339) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
gkaltydkiyyvgeqdfyvprdengkykkyeapgdayedtvkvmrtltpthvvfngavga
ltgdkamtaavgekvlivhsqanrdtrphligghgdyvwatgkfntppdvdqetwfipgg
aagaafytfqqpgiyayvnhnlieafelgaaahfkvtgewnddlmtsvlapsg
>d1aq8b1 2.5.1.3.2 (9-166) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
iaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhamafngtv
pgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilrfkatk
pgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>d1aq8b2 2.5.1.3.2 (167-339) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
gkaltydkiyyvgeqdfyvprdengkykkyeapgdayedtvkvmrtltpthvvfngavga
ltgdkamtaavgekvlivhsqanrdtrphligghgdyvwatgkfntppdvdqetwfipgg
aagaafytfqqpgiyayvnhnlieafelgaaahfkvtgewnddlmtsvlapsg
>d1aq8c1 2.5.1.3.2 (9-166) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
iaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhamafngtv
pgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilrfkatk
pgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>d1aq8c2 2.5.1.3.2 (167-339) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
gkaltydkiyyvgeqdfyvprdengkykkyeapgdayedtvkvmrtltpthvvfngavga
ltgdkamtaavgekvlivhsqanrdtrphligghgdyvwatgkfntppdvdqetwfipgg
aagaafytfqqpgiyayvnhnlieafelgaaahfkvtgewnddlmtsvlapsg
>d1aqa__ 4.94.1.1.2 Cytochrome b5 {Rat (Rattus norvegicus)}
kyytleeiqkhkdskstwvilhhkvydltkfleehpggeevlreqaggdatenfedvghs
tdarelsktyiigelhpddrskia
>d1aqb__ 2.53.1.1.2 Retinol binding protein {Pig (Sus scrofa domestica)}
erdcrvssfrvkenfdkarfsgtwyamakkdpeglflqdnivaefsvdenghmsatakgr
vrllnnwdvcadmvgtftdtedpakfkmkywgvasflqkgnddhwiidtdydtyavqysc
rlqnldgtcadsysfvfardphgfspevqkivrqrqeelclarqyriithngycd
>d1aqca_ 2.49.1.2.1 X11 {Human (Homo sapiens)}
edlidgiifaanylgstqllsdktpsknvrxxqaqeavsrikxaqklaksrkkapegesq
pxtevdlfiltqrikvlnadtqetxxdhplrtisyiadignivvlxarrriprsnsqenv
eashpsqdgkrqykxichvfesedaqliaqsigqafsvayqeflr
>d1aqcb_ 2.49.1.2.1 X11 {Human (Homo sapiens)}
iifaanylgstqllsdktpsknvrxxqaqeavsrikxaqklaksrkkapegesqpxtevd
lfiltqrikvlnadtqetxxdhplrtisyiadignivvlxarrriprsnsqenveashps
qdgkrqykxichvfesedaqliaqsigqafsvayqeflranginp
>d1aqda1 2.1.1.2.149 (82-181) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dr1}
itnvppevtvltnspvelrepnvlicfidkftppvvnvtwlrngkpvttgvsetvflpre
dhlfrkfhylpflpstedvydcrvehwgldepllkhwefd
>d1aqda2 4.17.1.1.4 (3-81) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
eehviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgalan
iavdkanleimtkrsnytp
>d1aqdb1 2.1.1.2.149 (93-190) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dr1}
rrvepkvtvypsktqplqhhnllvcsvsgfypgsievrwfrngqeekagvvstgliqngd
wtfqtlvmletvprsgevytcqvehpsvtspltvewra
>d1aqdb2 4.17.1.1.4 (4-92) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
rprflwqlkfechffngtervrllerciynqeesvrfdsdvgeyravtelgrpdaeywns
qkdlleqrraavdtycrhnygvgesftvq
>d1aqdd1 2.1.1.2.149 (82-179) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dr1}
itnvppevtvltnspvelrepnvlicfidkftppvvnvtwlrngkpvttgvsetvflpre
dhlfrkfhylpflpstedvydcrvehwgldepllkhwe
>d1aqdd2 4.17.1.1.4 (3-81) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
eehviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgalan
iavdkanleimtkrsnytp
>d1aqde1 2.1.1.2.149 (93-190) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dr1}
rrvepkvtvypsktqplqhhnllvcsvsgfypgsievrwfrngqeekagvvstgliqngd
wtfqtlvmletvprsgevytcqvehpsvtspltvewra
>d1aqde2 4.17.1.1.4 (4-92) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
rprflwqlkfechffngtervrllerciynqeesvrfdsdvgeyravtelgrpdaeywns
qkdlleqrraavdtycrhnygvgesftvq
>d1aqdg1 2.1.1.2.149 (82-179) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dr1}
itnvppevtvltnspvelrepnvlicfidkftppvvnvtwlrngkpvttgvsetvflpre
dhlfrkfhylpflpstedvydcrvehwgldepllkhwe
>d1aqdg2 4.17.1.1.4 (3-81) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
eehviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgalan
iavdkanleimtkrsnytp
>d1aqdh1 2.1.1.2.149 (93-190) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dr1}
rrvepkvtvypsktqplqhhnllvcsvsgfypgsievrwfrngqeekagvvstgliqngd
wtfqtlvmletvprsgevytcqvehpsvtspltvewra
>d1aqdh2 4.17.1.1.4 (4-92) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
rprflwqlkfechffngtervrllerciynqeesvrfdsdvgeyravtelgrpdaeywns
qkdlleqrraavdtycrhnygvgesftvq
>d1aqdj1 2.1.1.2.149 (82-179) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dr1}
itnvppevtvltnspvelrepnvlicfidkftppvvnvtwlrngkpvttgvsetvflpre
dhlfrkfhylpflpstedvydcrvehwgldepllkhwe
>d1aqdj2 4.17.1.1.4 (3-81) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
eehviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgalan
iavdkanleimtkrsnytp
>d1aqdk1 2.1.1.2.149 (93-191) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dr1}
rrvepkvtvypsktqplqhhnllvcsvsgfypgsievrwfrngqeekagvvstgliqngd
wtfqtlvmletvprsgevytcqvehpsvtspltvewrar
>d1aqdk2 4.17.1.1.4 (4-92) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
rprflwqlkfechffngtervrllerciynqeesvrfdsdvgeyravtelgrpdaeywns
qkdlleqrraavdtycrhnygvgesftvq
>d1aqe__ 1.126.1.1.1 Cytochrome c3 {Desulfovibrio desulfuricans, different strains}
tfeipesvtmspkqfegytpkkgdvtfnhashmdiacqqchhtvpdtytiescmtegchd
nikerteissvertfhttkdsekscvgchrelkrqgpsdaplacnschvq
>d1aqfa1 2.52.1.1.1 (116-217) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1aqfa2 3.1.11.1.2 (12-115,218-395) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1aqfa3 3.40.1.1.2 (396-530) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1aqfb1 2.52.1.1.1 (116-217) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1aqfb2 3.1.11.1.2 (12-115,218-395) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1aqfb3 3.40.1.1.2 (396-530) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1aqfc1 2.52.1.1.1 (116-217) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1aqfc2 3.1.11.1.2 (12-115,218-395) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1aqfc3 3.40.1.1.2 (396-530) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1aqfd1 2.52.1.1.1 (116-217) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1aqfd2 3.1.11.1.2 (12-115,218-395) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1aqfd3 3.40.1.1.2 (396-530) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1aqfe1 2.52.1.1.1 (116-217) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1aqfe2 3.1.11.1.2 (12-115,218-395) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1aqfe3 3.40.1.1.2 (396-530) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1aqff1 2.52.1.1.1 (116-217) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1aqff2 3.1.11.1.2 (12-115,218-395) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1aqff3 3.40.1.1.2 (396-530) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1aqfg1 2.52.1.1.1 (116-217) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1aqfg2 3.1.11.1.2 (12-115,218-395) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1aqfg3 3.40.1.1.2 (396-530) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1aqfh1 2.52.1.1.1 (116-217) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1aqfh2 3.1.11.1.2 (12-115,218-395) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1aqfh3 3.40.1.1.2 (396-530) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1aqh_1 2.62.1.1.2 (355-448) Bacterial alpha-Amylase (BLA) {Alteromonas haloplanctis}
nwavtnwwdntnnqisfgrgssghmainkedstltatvqtdmasgqycnvlkgelsadak
scsgevitvnsdgtinlnigawdamaihknakln
>d1aqh_2 3.1.7.1.2 (1-354) Bacterial alpha-amylase (BLA) {Alteromonas haloplanctis}
tpttfvhlfewnwqdvaqeceqylgpkgyaavqvsppnehitgsqwwtryqpvsyelqsr
ggnraqfidmvnrcsaagvdiyvdtlinhmaagsgtgtagnsfgnksfpiyspqdfhesc
tinnsdygndryrvqncelvgladldtasnyvqntiaayindlqaigvkgfrfdaskhva
asdiqslmakvngspvvfqevidqggeavgaseylstglvtefkystelgntfrngslaw
lsnfgegwgfmpsssavvfvdnhdnqrghggagnvitfedgrlydlanvfmlaypygypk
vmssydfhgdtdaggpnvpvhnngnlecfasnwkcehrwsyiaggvdfrnntad
>d1aqia_ 3.56.1.5.2 DNA methylase TaqI, coenzyme-binding domain {Thermus aquaticus}
vetppevvdfmvslaeaprggrvlepacahgpflrafreahgtgyrfvgveidpkaldlp
pwaegiladfllwepgeafdlilgnppygivgeaskypihvfkavkdlykkafstwkgky
nlygaflekavrllkpggvlvfvvpatwlvledfallreflaregktsvyylgevfpqkk
vsavvirfqksgkglslwdtqesesgftpilwaeyphwegeiirfeteetrkleisgmpl
gdlfhirfaarspefkkhpavrkepgpglvpvltgrnlkpgwvdyeknhsglwmpkerak
elrdfyatphlvvahtkgtrvvaawderaypwreefhllpkegvrldpstlvqwlnseam
qkhvrtlyrdfvphltlrmlerlpvrreygfht
>d1aqib_ 3.56.1.5.2 DNA methylase TaqI, coenzyme-binding domain {Thermus aquaticus}
vetppevvdfmvslaeaprggrvlepacahgpflrafreahgtgyrfvgveidpkaldlp
pwaegiladfllwepgeafdlilgnppygivgeaskypihvfkavkdlykkafstwkgky
nlygaflekavrllkpggvlvfvvpatwlvledfallreflaregktsvyylgevfpqkk
vsavvirfqksgkglslwdtqesesgftpilwaeyphwegeiirfeteetrkleisgmpl
gdlfhirfaarspefkkhpavrkepgpglvpvltgrnlkpgwvdyeknhsglwmpkerak
elrdfyatphlvvahtkgtrvvaawderaypwreefhllpkegvrldpstlvqwlnseam
qkhvrtlyrdfvphltlrmlerlpvrreygfht
>d1aqja_ 3.56.1.5.2 DNA methylase TaqI, coenzyme-binding domain {Thermus aquaticus}
vetppevvdfmvslaeaprggrvlepacahgpflrafreahgtgyrfvgveidpkaldlp
pwaegiladfllwepgeafdlilgnppygivgeaskypihvfkavkdlykkafstwkgky
nlygaflekavrllkpggvlvfvvpatwlvledfallreflaregktsvyylgevfpqkk
vsavvirfqksgkglslwdtqesesgftpilwaeyphwegeiirfeteetrkleisgmpl
gdlfhirfaarspefkkhpavrkepgpglvpvltgrnlkpgwvdyeknhsglwmpkerak
elrdfyatphlvvahtkgtrvvaawderaypwreefhllpkegvrldpsslvqwlnseam
qkhvrtlyrdfvphltlrmlerlpvrreygfht
>d1aqjb_ 3.56.1.5.2 DNA methylase TaqI, coenzyme-binding domain {Thermus aquaticus}
vetppevvdfmvslaeaprggrvlepacahgpflrafreahgtgyrfvgveidpkaldlp
pwaegiladfllwepgeafdlilgnppygivgeaskypihvfkavkdlykkafstwkgky
nlygaflekavrllkpggvlvfvvpatwlvledfallreflaregktsvyylgevfpqkk
vsavvirfqksgkglslwdtqesesgftpilwaeyphwegeiirfeteetrkleisgmpl
gdlfhirfaarspefkkhpavrkepgpglvpvltgrnlkpgwvdyeknhsglwmpkerak
elrdfyatphlvvahtkgtrvvaawderaypwreefhllpkegvrldpsslvqwlnseam
qkhvrtlyrdfvphltlrmlerlpvrreygfht
>d1aqkh1 2.1.1.1.94 (2-123) Immunoglobulin (variable domains of L and H chains) {Fab B7-15A2 (human), lambda L chain}
vqlvesgggvvqpgrslrlscaasgftfnnyaihwvrqapgkglewvafisydgsknyya
dsvkgrftisrdnskntlflqmnslrpedtaiyycarvlfqqlvlyapfdiwgqgtmvtv
ss
>d1aqkh2 2.1.1.2.96 (124-226) Immunoglobulin (constant domains of L and H chains) {Fab B7-15A2 (human), lambda L chain}
astkgpsvfplapsskstsggtaalgclvkdyfpqpvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkvepksc
>d1aqkl1 2.1.1.1.94 (2-111) Immunoglobulin (variable domains of L and H chains) {Fab B7-15A2 (human), lambda L chain}
nvltqppsvsgapgqrvtisctgsnsnigagftvhwyqhlpgtapkllifantnrpsgvp
drfsgsksgtsaslaitglqaedeadyycqsydsslsarfgggtrltvlg
>d1aqkl2 2.1.1.2.96 (112-216) Immunoglobulin (constant domains of L and H chains) {Fab B7-15A2 (human), lambda L chain}
qpkaapsvtlfppsseelqankatlvclisdfypgavtvawkadsspvnagvettkpskq
snnkyaassylsltpeqwkshksyscqvthegstvektvapaecs
>d1aqla_ 3.59.1.1.4 Bile-salt activated lipase (cholesterol esterase) {Bovine (Bos taurus)}
aklgsvyteggfvegvnkklslfgdsidifkgipfaaapkalekperhpgwqgtlkaksf
kkrclqatltqdstygnedclylniwvpqgrkevshdlpvmiwiyggaflmgasqganfl
snylydgeeiatrgnvivvtfnyrvgplgflstgdsnlpgnyglwdqhmaiawvkrniea
fggdpdnitlfgesaggasvslqtlspynkglikraisqsgvglcpwaiqqdplfwakri
aekvgcpvddtskmagclkitdpraltlayklplgsteypklhylsfvpvidgdfipddp
vnlyanaadvdyiagtndmdghlfvgmdvpainsnkqdvteedfyklvsgltvtkglrga
natyevytepwaqdssqetrkktmvdletdilfliptkiavaqhkshaksantytylfsq
psrmpiypkwmgadhaddlqyvfgkpfatplgyraqdrtvskamiaywtnfartgdpntg
hstvpanwdpytleddnyleinkqmdsnsmklhlrtnylqfwtqtyqalptv
>d1aqlb_ 3.59.1.1.4 Bile-salt activated lipase (cholesterol esterase) {Bovine (Bos taurus)}
aklgsvyteggfvegvnkklslfgdsidifkgipfaaapkalekperhpgwqgtlkaksf
kkrclqatltqdstygnedclylniwvpqgrkevshdlpvmiwiyggaflmgasqganfl
snylydgeeiatrgnvivvtfnyrvgplgflstgdsnlpgnyglwdqhmaiawvkrniea
fggdpdnitlfgesaggasvslqtlspynkglikraisqsgvglcpwaiqqdplfwakri
aekvgcpvddtskmagclkitdpraltlayklplgsteypklhylsfvpvidgdfipddp
vnlyanaadvdyiagtndmdghlfvgmdvpainsnkqdvteedfyklvsgltvtkglrga
natyevytepwaqdssqetrkktmvdletdilfliptkiavaqhkshaksantytylfsq
psrmpiypkwmgadhaddlqyvfgkpfatplgyraqdrtvskamiaywtnfartgdpntg
hstvpanwdpytleddnyleinkqmdsnsmklhlrtnylqfwtqtyqalptv
>d1aqm_1 2.62.1.1.2 (355-448) Bacterial alpha-Amylase (BLA) {Alteromonas haloplanctis}
nwavtnwwdntnnqisfgrgssghmainkedstltatvqtdmasgqycnvlkgelsadak
scsgevitvnsdgtinlnigawdamaihknakln
>d1aqm_2 3.1.7.1.2 (1-354) Bacterial alpha-amylase (BLA) {Alteromonas haloplanctis}
tpttfvhlfewnwqdvaqeceqylgpkgyaavqvsppnehitgsqwwtryqpvsyelqsr
ggnraqfidmvnrcsaagvdiyvdtlinhmaagsgtgtagnsfgnksfpiyspqdfhesc
tinnsdygndryrvqncelvgladldtasnyvqntiaayindlqaigvkgfrfdaskhva
asdiqslmakvngspvvfqevidqggeavgaseylstglvtefkystelgntfrngslaw
lsnfgegwgfmpsssavvfvdnhdnqrghggagnvitfedgrlydlanvfmlaypygypk
vmssydfhgdtdaggpnvpvhnngnlecfasnwkcehrwsyiaggvdfrnntad
>d1aqn__ 3.33.1.1.7 Subtilisin Novo/BPN' {Bacillus amyloliquefaciens}
aqsvpygvsqikapalhsqgycgsnvkvavidsgidsshpdlkvaggasfvpsetnpfqd
nnshgthvagtvaalnnsigvlgvapcaslyavkvlgadgsgqyswiingiewaiannmd
vinmslggpsgsaalkaavdkavasgvvvvaaagnegtsgssstvgypakypsviavgav
dssnqrasfssvgpeldvmapgvsicstlpgnkygaksgtsmasphvagaaalilskhpn
wtntqvrsslentttklgdsfyygkglinvqaaaq
>d1aqp__ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1aqq__ 7.38.1.1.5 Metallothionein {Baker's yeast (Saccharomyces cerevisiae)}
qneghecqcqcgscknneqcqkscscptgcnsddkcpcgn
>d1aqr__ 7.38.1.1.5 Metallothionein {Baker's yeast (Saccharomyces cerevisiae)}
qneghecqcqcgscknneqcqkscscptgcnsddkcpcgn
>d1aqs__ 7.38.1.1.5 Metallothionein {Baker's yeast (Saccharomyces cerevisiae)}
qneghecqcqcgscknneqcqkscscptgcnsddkcpcgn
>d1aqt_1 1.2.6.1.1 (87-136) Epsilon subunit of F1F0-ATP synthase C-terminal domain {Escherichia coli}
qdldearameakrkaeehissshgdvdyaqasaelakaiaqlrvieltkk
>d1aqt_2 2.81.1.1.1 (2-86) Epsilon subunit of F1F0-ATP synthase N-terminal domain {Escherichia coli}
styhldvvsaeqqmfsglvekiqvtgsegelgiypghaplltaikpgmirivkqhgheef
iylsggilevqpgnvtvladtairg
>d1aqua_ 3.30.1.3.1 Estrogen sulfotransferase {Mouse (Mus musculus)}
eyyevfgefrgvlmdkrftkywedvemflarpddlviatypksgttwisevvymiykegd
vekckedaifnripylecrnedlingikqlkekesprivkthlppkllpasfweknckmi
ylcrnakdvavsyyyfllmitsypnpksfsefvekfmqgqvpygswydhvkawwekskns
rvlfmfyedmkedirrevvklieflerkpsaelvdriiqhtsfqemknnpstnytmmpee
mmnqkvspfmrkgiigdwknhfpealrerfdehykqqmkdctvkfrme
>d1aqub_ 3.30.1.3.1 Estrogen sulfotransferase {Mouse (Mus musculus)}
eyyevfgefrgvlmdkrftkywedvemflarpddlviatypksgttwisevvymiykegd
vekckedaifnripylecrnedlingikqlkekesprivkthlppkllpasfweknckmi
ylcrnakdvavsyyyfllmitsypnpksfsefvekfmqgqvpygswydhvkawwekskns
rvlfmfyedmkedirrevvklieflerkpsaelvdriiqhtsfqemknnpstnytmmpee
mmnqkvspfmrkgiigdwknhfpealrerfdehykqqmkdctvkfrm
>d1aqva1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d1aqva2 3.38.1.5.4 (1-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d1aqvb1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d1aqvb2 3.38.1.5.4 (1-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d1aqwa1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d1aqwa2 3.38.1.5.4 (1-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d1aqwb1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d1aqwb2 3.38.1.5.4 (1-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d1aqwc1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d1aqwc2 3.38.1.5.4 (1-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d1aqwd1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d1aqwd2 3.38.1.5.4 (1-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d1aqxa1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d1aqxa2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d1aqxb1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d1aqxb2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d1aqxc1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d1aqxc2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d1aqxd1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d1aqxd2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d1aqya_ 3.30.1.3.1 Estrogen sulfotransferase {Mouse (Mus musculus)}
eyyevfgefrgvlmdkrftkywedvemflarpddlviatypksgttwisevvymiykegd
vekckedaifnripylecrnedlingikqlkekesprivkthlppkllpasfweknckmi
ylcrnakdvavsyyyfllmitsypnpksfsefvekfmqgqvpygswydhvkawwekskns
rvlfmfyedmkedirrevvklieflerkpsaelvdriiqhtsfqemknnpstnytmmpee
mmnqkvspfmrkgiigdwknhfpealrerfdehykqqmkdctvkfrme
>d1aqyb_ 3.30.1.3.1 Estrogen sulfotransferase {Mouse (Mus musculus)}
eyyevfgefrgvlmdkrftkywedvemflarpddlviatypksgttwisevvymiykegd
vekckedaifnripylecrnedlingikqlkekesprivkthlppkllpasfweknckmi
ylcrnakdvavsyyyfllmitsypnpksfsefvekfmqgqvpygswydhvkawwekskns
rvlfmfyedmkedirrevvklieflerkpsaelvdriiqhtsfqemknnpstnytmmpee
mmnqkvspfmrkgiigdwknhfpealrerfdehykqqmkdctvkfrm
>d1aqza_ 4.1.1.1.9 Ribotoxin restrictocin {Fungus (Aspergillus restrictus)}
atwtcinqqlnpktnkwedkrllysqakaesnshhaplsdgktgssyphwftngydgngk
likgrtpikfgkadcdrppkhsqngmgkddhyllefptfpdghdykfdskkpkenpgpar
viytypnkvfcgivahqrgnqgdlrlcsh
>d1aqzb_ 4.1.1.1.9 Ribotoxin restrictocin {Fungus (Aspergillus restrictus)}
atwtcinqqlnpktnkwedkrllysqakaesnshhaplsdgktgssyphwftngydgngk
likgrtpikfgkadcdrppkhsqngmgkddhyllefptfpdghdykfdskkpkenpgpar
viytypnkvfcgivahqrgnqgdlrlcsh
>d1ar0a_ 4.15.3.2.1 Nuclear transport factor-2 (NTF2) {Rat (Rattus norvegicus)}
gdkpiweqigssfiqhyyqlfdndrtqlgaiyidascltwkgqqfqgkaaiveklsslpf
qkiqhsitaqdhqptpdsciismvvgqlkadedpimgfhqmfllknindawvctndmfrl
alhnf
>d1ar0b_ 4.15.3.2.1 Nuclear transport factor-2 (NTF2) {Rat (Rattus norvegicus)}
kpiweqigssfiqhyyqlfdndrtqlgaiyidascltwkgqqfqgkaaiveklsslpfqk
iqhsitaqdhqptpdsciismvvgqlkadedpimgfhqmfllknindawvctndmfrlal
h
>d1ar1a1 6.2.1.1.6 Cytochrome c oxidase {Paracoccus denitrificans}
gfftrwfmstnhkdigilylftagivglisvcftvymrmelqhpgvqymclegarliada
saectpnghlwnvmityhgvlmmffvvipalfggfgnyfmplhigapdmafprlnnlsyw
myvcgvalgvasllapggndqmgsgvgwvlypplstteagysmdlaifavhvsgassilg
ainiittflnmrapgmtlfkvplfawsvfitawlillslpvlagaitmllmdrnfgtqff
dpagggdpvlyqhilwffghpevyiiilpgfgiishvistfakkpifgylpmvlamaaig
ilgfvvwahhmytagmsltqqayfmlatmtiavptgikvfswiatmwggsiefktpmlwa
fgflflftvggvtgvvlsqapldrvyhdtyyvvahfhyvmslgavfgifagvyywigkms
grqypewagqlhfwmmfigsnliffpqhflgrqgmprryidypvefaywnnissigayis
fasflffigivfytlfagkrvnvpnywnehadtlewtlpspppehtfet
>d1ar1b1 2.5.1.2.3 (108-252) Cytochrome c oxidase {Paracoccus denitrificans}
ndpdlvikaighqwywsyeypndgvafdalmlekealadagysedeyllatdnpvvvpvg
kkvlvqvtatdvihawtipafavkqdavpgriaqlwfsvdqegvyfgqcselcginhaym
pivvkavsqekyeawlagakeefaa
>d1ar1b2 6.2.1.1.6 (1-107) Cytochrome c oxidase {Paracoccus denitrificans}
qdvlgdlpvigkpvnggmnfqpassplahdqqwldhfvlyiitavtifvcllllicivrf
nrranpvparfthntpieviwtlvpvlilvaigafslpilfrsqemp
>d1ar1c_ 2.1.1.1.96 Immunoglobulin (variable domains of L and H chains) {Fv against Paracoccus denitrificans cytochrome c oxidase (mouse), kappa L chain}
evklqesggdlvqpggslklscaasgftfssytmswvrqtpekrlewvasinngggrtyy
pdtvkgrftisrdnakntlylqmsslksedtamyycvrheyyyamdywgqgttvtvss
>d1ar1d_ 2.1.1.1.96 Immunoglobulin (variable domains of L and H chains) {Fv against Paracoccus denitrificans cytochrome c oxidase (mouse), kappa L chain}
dieltqtpvslsasvgetvtitcraseniysylawyqqkqgkspqflvynaktlgegvps
rfsgsgsgtqfslkinsllpedfgsyycqhhygtppltfgggtkleik
>d1ar2__ 2.1.1.1.143 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (kappa) dimer REI (human)}
tpdiqmtqspsslsasvgdrvtitvqasqdiikhlnwyqqtpgkapklliyeasnlqagv
psrfsgsgsgtdytftisslqpediatyycqqyqslpytfgqgtklqit
>d1ar4a1 1.2.7.1.9 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1ar4a2 4.37.1.1.9 (87-201) Cambialistic superoxide dismutase {Propionibacterium freudenreichii, shermani}
saperptdelgaaideffgsfdnmkaqftaaatgiqgsgwaslvwdplgkrintlqfydh
qnnlpagsipllqldmwehafylqyknvkgdyvkswwnvvnwddvalrfsearva
>d1ar4b1 1.2.7.1.9 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1ar4b2 4.37.1.1.9 (87-201) Cambialistic superoxide dismutase {Propionibacterium freudenreichii, shermani}
saperptdelgaaideffgsfdnmkaqftaaatgiqgsgwaslvwdplgkrintlqfydh
qnnlpagsipllqldmwehafylqyknvkgdyvkswwnvvnwddvalrfsearva
>d1ar5a1 1.2.7.1.9 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1ar5a2 4.37.1.1.9 (87-201) Cambialistic superoxide dismutase {Propionibacterium freudenreichii, shermani}
saperptdelgaaideffgsfdnmkaqftaaatgiqgsgwaslvwdplgkrintlqfydh
qnnlpagsipllqldmwehafylqyknvkgdyvkswwnvvnwddvalrfsearva
>d1ar5b1 1.2.7.1.9 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1ar5b2 4.37.1.1.9 (87-201) Cambialistic superoxide dismutase {Propionibacterium freudenreichii, shermani}
saperptdelgaaideffgsfdnmkaqftaaatgiqgsgwaslvwdplgkrintlqfydh
qnnlpagsipllqldmwehafylqyknvkgdyvkswwnvvnwddvalrfsearva
>d1ar61_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
aatsrdalpnteasgpthskeipaltavetgatnplvpsdtvqtrhvvqhrsrsessies
ffargacvtimtvdnsasttnkdklfavwkitykdtvqlrrklefftysrfdmeltfvvt
anftetnnghalnqvyqimyippgapvpekwddytwqtssnpsifytygtaparisvpyv
gisnayshfydgfskvplkdqsaalgdslygaaslndfgilavrvvndhnptkvtskirv
ylkpkhirvwcprppravayygpgvdykdgtltplstkdltty
>d1ar62_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
eacgysdrvlqltlgnstittqeaansvvaygrwpeylrdseanpvdqptepdvaacrfy
tldtvswtkesrgwwwklpdalrdmglfgqnmyyhylgrsgytvhvqcnaskfhqgalgv
favpemclagdsntttmhtsyqnanpgekggtftgtftpdnnqtsparrfcpvdyllgng
tllgnafvfphqiinlrtnncatlvlpyvnslsidsmvkhnnwgiailplaplnfasess
peipitltiapmccefnglrnitlprlq
>d1ar63_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
glpvmntpgsnqyltadnfqspcalpefdvtppidipgevknmmelaeidtmipfdlsat
kkntmemyrvrlsdkphtddpilclslspasdprlshtmlgeilnyythwagslkftflf
cgsmmatgkllvsyappgadppkkrkeamlgthviwdiglqssctmvvpwisnttyrqti
ddsfteggyisvfyqtrivvplstpremdilgfvsacndfsvrllrdtthieqka
>d1ar71_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
aatsrdalpnteasgpthskeipaltavetgatnplvpsdtvqtrhvvqhrsrsessies
ffargacvtimtvdnsasttnkdklfavwkitykdtvqlrrklefftysrfdmeltfvvt
anftetnnghalnqvyqimyvppgapvpekwddytwqtssnpsifytygtaparisvpyv
gisnayshfydgfskvplkdqsaalgdslygaaslndfgilavrvvndhnptkvtskirv
ylkpkhirvwcprppravayygpgvdykdgtltplstkdltty
>d1ar72_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
eacgysdrvlqltlgnstittqeaansvvaygrwpeylrdseanpvdqptepdvaacrfy
tldtvswtkesrgwwwklpdalrdmglfgqnmyyhylgrsgytvhvqcnaskfhqgalgv
favpemclagdsntttmytsyqnanpgekggtftgtftpdnnqtsparrfcpvdyllgng
tllgnafvfphqiinlrtnncatlvlpyvnslsidsmvkhnnwgiailplaplnfasess
peipitltiapmccefnglrnitlprlq
>d1ar73_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
glpvmntpgsnqyltadnfqspcalpefdvtppidipgevknmmelaeidtmipfdlsat
kkntmemyrvrlsdkphtddpilclslspasdprlshtmlgeilnyythwagslkftflf
cgsmmatgkllvsyappgadppkkrkeamlgthviwdiglqssctmvvpwisnttyrqti
ddsfteggyisvfyqtrivvplstpremdilgfvsacndfsvrllrdtthieqka
>d1ar81_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
aatsrdalpnteasgpthskeipaltavetgatnplvpsdtvqtrhvvqhrsrsessies
ffargacvtimtvdnsasttnkdklfavwkitykdtvqlrrklefftysrfdmeltfvvt
anftetnnghalnqvyqimyvppgapvpekwddytwqtssnpsifytygtaparisvpyv
gisnayshfydgfskvplkdqsaalgdslygaaslndfgilavrvvndhnptkvtskirv
ylkpkhirvwcprppravayygpgvdykdgtltplstkdltty
>d1ar82_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
eacgysdrvlqltlgnstittqeaansvvaygrwpeylrdseanpvdqptepdvaacrfy
tldtvswtkesrgwwwklpdalrdmglfgqnmyyhylgrsgytvhvqcnaskfhqgalgv
favpemclagdsntttmhtsyqnanpgekggtftgtftpdnnqtsparrfcpvdyllgng
tllgnafvfphqiinlrtnncatlvlpyvnslsidsmvkhnnwgiailplaplnfasess
peipitltiapmccefnglrnitlprlq
>d1ar83_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
glpvmntpgsnqyltadnfqspcalpefdvtppidipgevknmmelaeidtmipfdlsat
kkntmemyrvrlsdkphtddpilclslspasdprlshtmlgeilnyythwagslkftflf
cgsmmatgkllvsyappgadppkkrkeamlgthviwdiglqssctmvvpwisnttyrqti
ddsfteggyisvfyqtrivvplstpremdilgfvsacndfsvrllrdtthieqka
>d1ar91_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
aatsrdalpnteasgpthskeipaltavetgatnplvpsdtvqtrhvvqhrsrsessies
ffargacvtimtvdnpasttnkdklfavwkitykdtvqlrrklefftysrfdmeltfvvt
anftetnnghalnqvyqimyvppgapvpekwddytwqtssnpsifytygtaparisvpyv
gisnayshfydgfskvplkdqsaalgdslygaaslndfgilavrvvndhnptkvtskirv
ylkpkhirvwcprppravayygpgvdykdgtltplstkdltty
>d1ar92_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
eacgysdrvlqltlgnstittqeaansvvaygrwpeylrdseanpvdqptepdvaacrfy
tldtvswtkesrgwwwklpdalrdmglfgqnmyyhylgrsgytvhvqcnaskfhqgalgv
favpemclagdsntttmytsyqnanpgekggtftgtftpdnnqtsparrfcpvdyllgng
tllgnafvfphqiinlrtnncatlvlpyvnslsidsmvkhnnwgiailplaplnfasess
peipitltiapmccefnglrnitlprlq
>d1ar93_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
glpvmntpgsnqyltadnfqspcalpefdvtppidipgevknmmelaeidtmipfdlsat
kkntmemyrvrlsdkphtddpilclslspasdprlshtmlgeilnyythwagslkftflf
cgsmmatgkllvsyappgadppkkrkeamlgthviwdiglqssctmvvpwisnttyrqti
ddsfteggyisvfyqtrivvplstpremdilgfvsacndfsvrllrdtthieqka
>d1arb__ 2.41.1.1.1 Achromobacter protease {Achromobacter lyticus, strain m497-1}
gvsgscnidvvcpegdgrrdiiravgaysksgtlactgslvnntandrkmyfltahhcgm
gtastaasivvywnyqnstcrapntpasgangdgsmsqtqsgstvkatyatsdftlleln
naanpafnlfwagwdrrdqnypgaiaihhpnvaekrisnstsptsfvawgggagtthlnv
qwqpsggvtepgssgspiyspekrvlgqlhggpsscsatgtnrsdqygrvftswtgggaa
asrlsdwldpastgaqfidglds
>d1arc__ 2.41.1.1.1 Achromobacter protease {Achromobacter lyticus, strain m497-1}
gvsgscnidvvcpegdgrrdiiravgaysksgtlactgslvnntandrkmyfltahhcgm
gtastaasivvywnyqnstcrapntpasgangdgsmsqtqsgstvkatyatsdftlleln
naanpafnlfwagwdrrdqnypgaiaihhpnvaekrisnstsptsfvawgggagtthlnv
qwqpsggvtepgssgspiyspekrvlgqlhggpsscsatgtnrsdqygrvftswtgggaa
asrlsdwldpastgaqfidglds
>d1ard__ 7.31.1.1.4 ADR1 {Synthetic, based on Saccharomyces cerevisiae sequence}
rsfvcevctrafarqehlkrhyrshtnek
>d1are__ 7.31.1.1.4 ADR1 {Synthetic, based on Saccharomyces cerevisiae sequence}
rsfvcevctrafarqealkrhyrshtnek
>d1arf__ 7.31.1.1.4 ADR1 {Synthetic, based on Saccharomyces cerevisiae sequence}
rsfvcevctrafarqeylkrhyrshtnek
>d1arga_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1argb_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1arha_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfarqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgavnvagmtpdnmaplceaivavl
>d1arhb_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfarqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgavnvagmtpdnmaplceaivavl
>d1aria_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpshpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1arib_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpshpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ark__ 2.30.2.1.3 SH3 domain from nebulin {Human (Homo sapiens)}
tagkiframydymaadadevsfkdgdaiinvqaidegwmygtvqrtgrtgmlpanyveai
>d1arl__ 3.47.4.1.1 Carboxypeptidase A {Bovine (Bos taurus)}
arstntfnyatyhtldeiydfmdllvaehpqlvsklqigrsyegrpiyvlkfstggsnrp
aiwidlgihsrewitqatgvwfakkftedygqdpsftaildsmdifleivtnpdgfafth
sqnrlwrktrsvtssslcvgvdanrnwdagfgkagassspcsetyhgkyansevevksiv
dfvkdhgnfkaflsihsysqlllypygyttqsipdktelnqvaksavaalkslygtsyky
gsiittiyqasggsidwsynqgikysftfelrdtgrygfllpasqiiptaqetwlgvlti
mehtvnn
>d1arm__ 3.47.4.1.1 Carboxypeptidase A {Bovine (Bos taurus)}
arstntfnyatyhtldeiydfmdllvaehpqlvsklqigrsyegrpiyvlkfstggsnrp
aiwidlgihsrewitqatgvwfakkftedygqdpsftaildsmdifleivtnpdgfafth
sqnrlwrktrsvtssslcvgvdanrnwdagfgkagassspcsetyhgkyansevevksiv
dfvkdhgnfkaflsihsysqlllypygyttqsipdktelnqvaksavaalkslygtsyky
gsiittiyqasggsidwsynqgikysftfelrdtgrygfllpasqiiptaqetwlgvlti
mehtvnn
>d1arn__ 2.5.1.1.22 Azurin {Alcaligenes xylosoxidans, NCIMB (11015), different isoforms}
aqceatvesndamqynvkeivvdksckqftmhlkhvgkmakvamghnlvltkdadkqava
tdgmgaglaqdyvkagdtrviahtkvigggesdsvtfdvskiaagenyayfcsfpghwam
mkgtlklgs
>d1arol_ 4.92.1.1.1 Bacteriophage T7 lysozyme (Zn amidase) {Bacteriophage T7}
rvqfkqrestdaifvhcsatkpsqnvgvreirqwhkeqgwldvgyhfiikrdgtveagrd
emavgshakgynhnsigvclvggiddkgkfdanftpaqmqslrsllvtllakyegavlra
hhevapkacpsfdlkrwweknelvtsdrg
>d1arop_ 5.8.1.3.1 T7 RNA polymerase {Bacteriophage T7}
kndfsdielaaipfntladhygerlareqlalehesyemgearfrkmferqlkagevadn
aaakplittllpkmiarindwfeevkakrgkrptafqflqeikpeavayitikttlaclt
sadnttvqavasaigraiedearfgrirdleakhfkknveeqlnkrvghvykkafmqvve
admlskgllggeawsswhkedsihvgvrciemliestgmvslhrqnagvvgqdsetiela
peyaeaiatragalagispmfqpcvvppkpwtgitgggywangrrplalvrthskkalmr
yedvympevykainiaqntawkinkkvlavanvitkwkhspvedipaiereelpmkpedi
dmnpealtawkraaaavyrkdkarksrrislefmleqankfanhkaiwfpynmdwrgrvy
avsmfnpqgndmtkglltlakgkpigkegyywlkihgancagvdkvpfperikfieenhe
nimacaksplentwwaeqdspfcflafcfeyagvqhhglsyncslplafdgscsgiqhfs
amlrdevggravnllpsetvqdiygivakkvneilqadaingtdnevvtvtdentgeise
kvklgtkalagqwlaygvtrsvtkrsvmtlaygskefgfrqqvledtiqpaidsgkglmf
tqpnqaagymakliwesvsvtvvaaveamnwlksaakllaaevkdkktgeilrkrsavhw
vtpdgfpvwqeykkpiqtrlnlmflgqfrlqptintnkdseidahkqesgiapnfvhsqd
gshlrktvvwahekygiesfalihdsfgtipadaanlfkavretmvdtyessdvladfyd
qfadqlhesqldkmpalpakgnlnlrdilesd
>d1arp__ 1.90.1.1.2 Peroxidase {Arthromyces ramous}
svtcpggqstsnsqccvwfdvlddlqtnfyqgskcespvrkilrivfhdaigfspaltaa
gqfggggadgsiiahsnielafpanggltdtiealravginhgvsfgdliqfatavgmsn
cpgsprlefltgrsnssqpsppslipgpgntvtaildrmgdagfspdevvdllaahslas
qeglnsaifrspldstpqvfdtqfyietllkgttqpgpslgfaeelspfpgefrmrsdal
lardsrtacrwqsmtssnevmgqryraamakmsvlgfdrnaltdcsdvipsavsnnaapv
ipggltvddievscpsepfpeiatasgplpslapap
>d1arqa_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1arqb_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1arra_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1arrb_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1ars__ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1art__ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aru__ 1.90.1.1.2 Peroxidase {Arthromyces ramous}
svtcpggqstsnsqccvwfdvlddlqtnfyqgskcespvrkilrivfhdaigfspaltaa
gqfggggadgsiiahsnielafpanggltdtiealravginhgvsfgdliqfatavgmsn
cpgsprlefltgrsnssqpsppslipgpgntvtaildrmgdagfspdevvdllaahslas
qeglnsaifrspldstpqvfdtqfyietllkgttqpgpslgfaeelspfpgefrmrsdal
lardsrtacrwqsmtssnevmgqryraamakmsvlgfdrnaltdcsdvipsavsnnaapv
ipggltvddievscpsepfpeiatasgplpslapap
>d1arv__ 1.90.1.1.2 Peroxidase {Arthromyces ramous}
svtcpggqstsnsqccvwfdvlddlqtnfyqgskcespvrkilrivfhdaigfspaltaa
gqfggggadgsiiahsnielafpanggltdtiealravginhgvsfgdliqfatavgmsn
cpgsprlefltgrsnssqpsppslipgpgntvtaildrmgdagfspdevvdllaahslas
qeglnsaifrspldstpqvfdtqfyietllkgttqpgpslgfaeelspfpgefrmrsdal
lardsrtacrwqsmtssnevmgqryraamakmsvlgfdrnaltdcsdvipsavsnnaapv
ipggltvddievscpsepfpeiatasgplpslapap
>d1arw__ 1.90.1.1.2 Peroxidase {Arthromyces ramous}
svtcpggqstsnsqccvwfdvlddlqtnfyqgskcespvrkilrivfhdaigfspaltaa
gqfggggadgsiiahsnielafpanggltdtiealravginhgvsfgdliqfatavgmsn
cpgsprlefltgrsnssqpsppslipgpgntvtaildrmgdagfspdevvdllaahslas
qeglnsaifrspldstpqvfdtqfyietllkgttqpgpslgfaeelspfpgefrmrsdal
lardsrtacrwqsmtssnevmgqryraamakmsvlgfdrnaltdcsdvipsavsnnaapv
ipggltvddievscpsepfpeiatasgplpslapap
>d1arx__ 1.90.1.1.2 Peroxidase {Arthromyces ramous}
svtcpggqstsnsqccvwfdvlddlqtnfyqgskcespvrkilrivfhdaigfspaltaa
gqfggggadgsiiahsnielafpanggltdtiealravginhgvsfgdliqfatavgmsn
cpgsprlefltgrsnssqpsppslipgpgntvtaildrmgdagfspdevvdllaahslas
qeglnsaifrspldstpqvfdtqfyietllkgttqpgpslgfaeelspfpgefrmrsdal
lardsrtacrwqsmtssnevmgqryraamakmsvlgfdrnaltdcsdvipsavsnnaapv
ipggltvddievscpsepfpeiatasgplpslapap
>d1ary__ 1.90.1.1.2 Peroxidase {Arthromyces ramous}
svtcpggqstsnsqccvwfdvlddlqtnfyqgskcespvrkilrivfhdaigfspaltaa
gqfggggadgsiiahsnielafpanggltdtiealravginhgvsfgdliqfatavgmsn
cpgsprlefltgrsnssqpsppslipgpgntvtaildrmgdagfspdevvdllaahslas
qeglnsaifrspldstpqvfdtqfyietllkgttqpgpslgfaeelspfpgefrmrsdal
lardsrtacrwqsmtssnevmgqryraamakmsvlgfdrnaltdcsdvipsavsnnaapv
ipggltvddievscpsepfpeiatasgplpslapap
>d1arza1 3.2.1.3.13 (4-130,241-273) Dihydrodipicolinate reductase {Escherichia coli}
anirvaiagaggrmgrqliqaalalegvqlgaaleregssllgsdagelagagktgvtvq
ssldavkddfdvfidftrpegtlnhlafcrqhgkgmvigttgfdeagkqairdaaadiai
vfaanfsXmtfangavrsalwlsgkesglfdmrdvldlnnl
>d1arza2 4.61.1.2.2 (131-240) Dihydrodipicolinate reductase {Escherichia coli}
vgvnvmlkllekaakvmgdytdieiieahhrhkvdapsgtalamgeaiahaldkdlkdca
vysreghtgervpgtigfatvragdivgehtamfadigerleithkassr
>d1arzb1 3.2.1.3.13 (5-130,241-273) Dihydrodipicolinate reductase {Escherichia coli}
nirvaiagaggrmgrqliqaalalegvqlgaaleregssllgsdagelagagktgvtvqs
sldavkddfdvfidftrpegtlnhlafcrqhgkgmvigttgfdeagkqairdaaadiaiv
faanfsXmtfangavrsalwlsgkesglfdmrdvldlnnl
>d1arzb2 4.61.1.2.2 (131-240) Dihydrodipicolinate reductase {Escherichia coli}
vgvnvmlkllekaakvmgdytdieiieahhrhkvdapsgtalamgeaiahaldkdlkdca
vysreghtgervpgtigfatvragdivgehtamfadigerleithkassr
>d1arzc1 3.2.1.3.13 (3-130,241-273) Dihydrodipicolinate reductase {Escherichia coli}
danirvaiagaggrmgrqliqaalalegvqlgaaleregssllgsdagelagagktgvtv
qssldavkddfdvfidftrpegtlnhlafcrqhgkgmvigttgfdeagkqairdaaadia
ivfaanfsXmtfangavrsalwlsgkesglfdmrdvldlnnl
>d1arzc2 4.61.1.2.2 (131-240) Dihydrodipicolinate reductase {Escherichia coli}
vgvnvmlkllekaakvmgdytdieiieahhrhkvdapsgtalamgeaiahaldkdlkdca
vysreghtgervpgtigfatvragdivgehtamfadigerleithkassr
>d1arzd1 3.2.1.3.13 (3-130,241-273) Dihydrodipicolinate reductase {Escherichia coli}
danirvaiagaggrmgrqliqaalalegvqlgaaleregssllgsdagelagagktgvtv
qssldavkddfdvfidftrpegtlnhlafcrqhgkgmvigttgfdeagkqairdaaadia
ivfaanfsXmtfangavrsalwlsgkesglfdmrdvldlnnl
>d1arzd2 4.61.1.2.2 (131-240) Dihydrodipicolinate reductase {Escherichia coli}
vgvnvmlkllekaakvmgdytdieiieahhrhkvdapsgtalamgeaiahaldkdlkdca
vysreghtgervpgtigfatvragdivgehtamfadigerleithkassr
>d1as0_1 1.67.1.1.2 (61-181) Transducin (alpha subunit), insertion domain {Rat (Rattus rattus)}
yseeeckqykavvysntiqsiiaiiramgrlkidfgdaaraddarqlfvlagaaeegfmt
aelagvikrlwkdsgvqacfnrsreyqlndsaayylndldriaqpnyiptqqdvlrtrvk
t
>d1as0_2 3.30.1.6.13 (32-60,182-344) Transducin (alpha subunit) {Rat (Rattus rattus)}
revkllllgavesgkstivkqmkiiheagXtgivethftfkdlhfkmfdvggqrserkkw
ihcfegvtaiifcvalsdydlvlaedeemnrmhesmklfdsicnnkwftdtsiilflnkk
dlfeekikksplticypeyagsntyeeaaayiqcqfedlnkrkdtkeiythftcatdtkn
vqfvfdavtdvii
>d1as2_1 1.67.1.1.2 (61-181) Transducin (alpha subunit), insertion domain {Rat (Rattus rattus)}
yseeeckqykavvysntiqsiiaiiramgrlkidfgdaaraddarqlfvlagaaeegfmt
aelagvikrlwkdsgvqacfnrsreyqlndsaayylndldriaqpnyiptqqdvlrtrvk
t
>d1as2_2 3.30.1.6.13 (32-60,182-346) Transducin (alpha subunit) {Rat (Rattus rattus)}
revkllllgavesgkstivkqmkiiheagXtgivethftfkdlhfkmfdvggqrserkkw
ihcfegvtaiifcvalsdydlvlaedeemnrmhesmklfdsicnnkwftdtsiilflnkk
dlfeekikksplticypeyagsntyeeaaayiqcqfedlnkrkdtkeiythftcatdtkn
vqfvfdavtdviikn
>d1as3_1 1.67.1.1.2 (61-181) Transducin (alpha subunit), insertion domain {Rat (Rattus rattus)}
yseeeckqykavvysntiqsiiaiiramgrlkidfgdaaraddarqlfvlagaaeegfmt
aelagvikrlwkdsgvqacfnrsreyqlndsaayylndldriaqpnyiptqqdvlrtrvk
t
>d1as3_2 3.30.1.6.13 (9-60,182-354) Transducin (alpha subunit) {Rat (Rattus rattus)}
dkaaverskmidrnlredgekaarevkllllgavesgkstivkqmkiiheagXtgiveth
ftfkdlhfkmfdvggqrserkkwihcfegvtaiifcvalsdydlvlaedeemnrmhesmk
lfdsicnnkwftdtsiilflnkkdlfeekikksplticypeyagsntyeeaaayiqcqfe
dlnkrkdtkeiythftcatdtknvqfvfdavtdviiknnlkdcglf
>e1as4.1a 5.1.1.1.3 Antichymotrypsin, alpha-1 {Human (Homo sapiens)}
glasanvdfafslykqlvlkapdknvifsplsistalaflslgahnttlteilkglkfnl
tetseaeihqsfqhllrtlnqssdelqlsmgnamfvkeqlslldrftedakrlygseafa
tdfqdsaaakklindyvkngtrgkitdlikdldsqtmmvlvnyiffkakwempfdpqdth
qsrfylskkkwvmvpmmslhhltipyfrdeelsctvvelkytgnasalfilpdqdkmeev
eamllpetlkrwrdslefreigelylpkfsisrdynlndillqlgieeaftskadlsgit
garnlavsqvvhkavldvfeegteasratavkitll
>e1as4.1b 5.1.1.1.3 Antichymotrypsin, alpha-1 {Human (Homo sapiens)}
gtivrfnrpflmiivptdtqniffmskvtnpkq
>d1as6a1 2.5.1.3.2 (5-166) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
taaeiaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhamaf
ngtvpgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilrf
katkpgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>d1as6a2 2.5.1.3.2 (167-339) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
gkaltydkiyyvgeqdfyvprdengkykkyeapgdayedtvkvmrtltpthvvfngavga
ltgdkamtaavgekvlivhsqanrdtrphligghgdyvwatgkfntppdvdqetwfipgg
aagaafytfqqpgiyayvnhnlieafelgaaahfkvtgewnddlmtsvlapsg
>d1as6b1 2.5.1.3.2 (4-166) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
ataaeiaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhama
fngtvpgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilr
fkatkpgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>d1as6b2 2.5.1.3.2 (167-339) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
gkaltydkiyyvgeqdfyvprdengkykkyeapgdayedtvkvmrtltpthvvfngavga
ltgdkamtaavgekvlivhsqanrdtrphligghgdyvwatgkfntppdvdqetwfipgg
aagaafytfqqpgiyayvnhnlieafelgaaahfkvtgewnddlmtsvlapsg
>d1as6c1 2.5.1.3.2 (5-166) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
taaeiaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhamaf
ngtvpgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilrf
katkpgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>d1as6c2 2.5.1.3.2 (167-339) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
gkaltydkiyyvgeqdfyvprdengkykkyeapgdayedtvkvmrtltpthvvfngavga
ltgdkamtaavgekvlivhsqanrdtrphligghgdyvwatgkfntppdvdqetwfipgg
aagaafytfqqpgiyayvnhnlieafelgaaahfkvtgewnddlmtsvlapsg
>d1as7a1 2.5.1.3.2 (4-166) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
ataaeiaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhama
fngtvpgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilr
fkatkpgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>d1as7a2 2.5.1.3.2 (167-340) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
gkaltydkiyyvgeqdfyvprdengkykkyeapgdayedtvkvmrtltpthvvfngavga
ltgdkamtaavgekvlivhsqanrdtrphligghgdyvwatgkfntppdvdqetwfipgg
aagaafytfqqpgiyayvnhnlieafelgaaahfkvtgewnddlmtsvlapsgt
>d1as7b1 2.5.1.3.2 (4-166) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
ataaeiaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhama
fngtvpgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilr
fkatkpgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>d1as7b2 2.5.1.3.2 (167-340) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
gkaltydkiyyvgeqdfyvprdengkykkyeapgdayedtvkvmrtltpthvvfngavga
ltgdkamtaavgekvlivhsqanrdtrphligghgdyvwatgkfntppdvdqetwfipgg
aagaafytfqqpgiyayvnhnlieafelgaaahfkvtgewnddlmtsvlapsgt
>d1as7c1 2.5.1.3.2 (4-166) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
ataaeiaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhama
fngtvpgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilr
fkatkpgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>d1as7c2 2.5.1.3.2 (167-340) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
gkaltydkiyyvgeqdfyvprdengkykkyeapgdayedtvkvmrtltpthvvfngavga
ltgdkamtaavgekvlivhsqanrdtrphligghgdyvwatgkfntppdvdqetwfipgg
aagaafytfqqpgiyayvnhnlieafelgaaahfkvtgewnddlmtsvlapsgt
>d1as8a1 2.5.1.3.2 (4-166) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
ataaeiaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhama
fngtvpgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilr
fkatkpgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>d1as8a2 2.5.1.3.2 (167-339) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
gkaltydkiyyvgeqdfyvprdengkykkyeapgdayedtvkvmrtltpthvvfngavga
ltgdkamtaavgekvlivhsqanrdtrphligghgdyvwatgkfntppdvdqetwfipgg
aagaafytfqqpgiyayvnhnlieafelgaaahfkvtgewnddlmtsvlapsg
>d1as8b1 2.5.1.3.2 (4-166) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
ataaeiaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhama
fngtvpgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilr
fkatkpgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>d1as8b2 2.5.1.3.2 (167-339) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
gkaltydkiyyvgeqdfyvprdengkykkyeapgdayedtvkvmrtltpthvvfngavga
ltgdkamtaavgekvlivhsqanrdtrphligghgdyvwatgkfntppdvdqetwfipgg
aagaafytfqqpgiyayvnhnlieafelgaaahfkvtgewnddlmtsvlapsg
>d1as8c1 2.5.1.3.2 (4-166) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
ataaeiaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhama
fngtvpgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilr
fkatkpgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>d1as8c2 2.5.1.3.2 (167-339) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
gkaltydkiyyvgeqdfyvprdengkykkyeapgdayedtvkvmrtltpthvvfngavga
ltgdkamtaavgekvlivhsqanrdtrphligghgdyvwatgkfntppdvdqetwfipgg
aagaafytfqqpgiyayvnhnlieafelgaaahfkvtgewnddlmtsvlapsg
>d1asa__ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1asb__ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfafayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1asc__ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfafayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1asd__ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ase__ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1asf__ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfafqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1asg__ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfafqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ash__ 1.1.1.1.44 Ascaris hemoglobin, domain 1 {Pig roundworm (Ascaris suum)}
anktrelcmkslehakvdtsnearqdgidlykhmfenypplrkyfksreeytaedvqndp
ffakqgqkillachvlcatyddretfnaytrelldrhardhvhmppevwtdfwklfeeyl
gkkttldeptkqawheigrefakeink
>d1asj1_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
aatsrdalpnteasgpthskeipaltavetgatnplvpsdtvqtrhvvqhrsrsessies
ffargacvtimtvdnpasttnkdklfavwkitykdtvqlrrklefftysrfdmeltfvvt
anftetnnghalnqvyqimyvppgapvpekwddytwqtssnpsifytygtaparisvpyv
gisnayshfydgfskvplkdqsaalgdslygaaslndfgilavrvvndhnptkvtskirv
ylkpkhirvwcprppravayygpgvdykdgtltplstkdltty
>d1asj2_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
eacgysdrvlqltlgnstittqeaansvvaygrwpeylrdseanpvdqptepdvaacrfy
tldtvswtkesrgwwwklpdalrdmglfgqnmyyhylgrsgytvhvqcnaskfhqgalgv
favpemclagdsntttmhtsyqnanpgekggtftgtftpdnnqtsparrfcpvdyllgng
tllgnafvfphqiinlrtnncatlvlpyvnslsidsmvkhnnwgiailplaplnfasess
peipitltiapmccefnglrnitlprlq
>d1asj3_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
glpvmntpgsnqyltadnfqspcalpefdvtppidipgevknmmelaeidtmipfdlsat
kkntmemyrvrlsdkphtddpilclslspasdprlshtmlgeilnyythwagslkftflf
cgsmmatgkllvsyappgadppkkrkeamlgthviwdiglqssctmvvpwisnttyrqti
ddsfteggyisvfyqtrivvplstpremdilgfvsacndfsvrllrdtthieqka
>d1aska_ 4.15.3.2.1 Nuclear transport factor-2 (NTF2) {Rat (Rattus norvegicus)}
gdkpiweqigssfiqhyyqlfdndrtqlgaiyidascltwegqqfqgkaaiveklsslpf
qkiqasitaqdhqptpdsciismvvgqlkadedpimgfhqmfllknindawvctndmfrl
alhnf
>d1askb_ 4.15.3.2.1 Nuclear transport factor-2 (NTF2) {Rat (Rattus norvegicus)}
kpiweqigssfiqhyyqlfdndrtqlgaiyidascltwegqqfqgkaaiveklsslpfqk
iqasitaqdhqptpdsciismvvgqlkadedpimgfhqmfllknindawvctndmfrlal
>d1asla_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aslb_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1asma_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1asmb_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1asna_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1asnb_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1asoa1 2.5.1.3.4 (1-129) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
sqirhykweveymfwapncnenivmgingqfpgptiranagdsvvveltnklhtegvvih
whgilqrgtpwadgtasisqcainpgetffynftvdnpgtffyhghlgmqrsaglygsli
vdppqgkke
>d1asoa2 2.5.1.3.4 (130-338) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
pfhydgeinlllsdwwhqsihkqevglsskpirwigepqtillngrgqfdcsiaakydsn
lepcklkgsescapyifhvspkktyririasttalaalnfaignhqllvveadgnyvqpf
ytsdidiysgesysvlittdqnpsenywvsvgtrarhpntppgltllnylpnsvsklpts
pppqtpawddfdrsknftyritaamgspk
>d1asoa3 2.5.1.3.4 (339-552) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
ppvkfnrrifllntqnvingyvkwaindvslalpptpylgamkynllhafdqnpppevfp
edydidtpptnektrigngvyqfkigevvdvilqnanmmkenlsethpwhlhghdfwvlg
ygdgkfsaeeesslnlknpplrntvvifpygwtairfvadnpgvwafhchiephlhmgmg
vvfaegvekvgriptkalacggtakslinnpknp
>d1asob1 2.5.1.3.4 (1-129) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
sqirhykweveymfwapncnenivmgingqfpgptiranagdsvvveltnklhtegvvih
whgilqrgtpwadgtasisqcainpgetffynftvdnpgtffyhghlgmqrsaglygsli
vdppqgkke
>d1asob2 2.5.1.3.4 (130-338) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
pfhydgeinlllsdwwhqsihkqevglsskpirwigepqtillngrgqfdcsiaakydsn
lepcklkgsescapyifhvspkktyririasttalaalnfaignhqllvveadgnyvqpf
ytsdidiysgesysvlittdqnpsenywvsvgtrarhpntppgltllnylpnsvsklpts
pppqtpawddfdrsknftyritaamgspk
>d1asob3 2.5.1.3.4 (339-552) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
ppvkfnrrifllntqnvingyvkwaindvslalpptpylgamkynllhafdqnpppevfp
edydidtpptnektrigngvyqfkigevvdvilqnanmmkenlsethpwhlhghdfwvlg
ygdgkfsaeeesslnlknpplrntvvifpygwtairfvadnpgvwafhchiephlhmgmg
vvfaegvekvgriptkalacggtakslinnpknp
>d1aspa1 2.5.1.3.4 (1-129) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
sqirhykweveymfwapncnenivmgingqfpgptiranagdsvvveltnklhtegvvih
whgilqrgtpwadgtasisqcainpgetffynftvdnpgtffyhghlgmqrsaglygsli
vdppqgkke
>d1aspa2 2.5.1.3.4 (130-338) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
pfhydgeinlllsdwwhqsihkqevglsskpirwigepqtillngrgqfdcsiaakydsn
lepcklkgsescapyifhvspkktyririasttalaalnfaignhqllvveadgnyvqpf
ytsdidiysgesysvlittdqnpsenywvsvgtrarhpntppgltllnylpnsvsklpts
pppqtpawddfdrsknftyritaamgspk
>d1aspa3 2.5.1.3.4 (339-552) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
ppvkfnrrifllntqnvingyvkwaindvslalpptpylgamkynllhafdqnpppevfp
edydidtpptnektrigngvyqfkigevvdvilqnanmmkenlsethpwhlhghdfwvlg
ygdgkfsaeeesslnlknpplrntvvifpygwtairfvadnpgvwafhchiephlhmgmg
vvfaegvekvgriptkalacggtakslinnpknp
>d1aspb1 2.5.1.3.4 (1-129) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
sqirhykweveymfwapncnenivmgingqfpgptiranagdsvvveltnklhtegvvih
whgilqrgtpwadgtasisqcainpgetffynftvdnpgtffyhghlgmqrsaglygsli
vdppqgkke
>d1aspb2 2.5.1.3.4 (130-338) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
pfhydgeinlllsdwwhqsihkqevglsskpirwigepqtillngrgqfdcsiaakydsn
lepcklkgsescapyifhvspkktyririasttalaalnfaignhqllvveadgnyvqpf
ytsdidiysgesysvlittdqnpsenywvsvgtrarhpntppgltllnylpnsvsklpts
pppqtpawddfdrsknftyritaamgspk
>d1aspb3 2.5.1.3.4 (339-552) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
ppvkfnrrifllntqnvingyvkwaindvslalpptpylgamkynllhafdqnpppevfp
edydidtpptnektrigngvyqfkigevvdvilqnanmmkenlsethpwhlhghdfwvlg
ygdgkfsaeeesslnlknpplrntvvifpygwtairfvadnpgvwafhchiephlhmgmg
vvfaegvekvgriptkalacggtakslinnpknp
>d1asqa1 2.5.1.3.4 (1-129) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
sqirhykweveymfwapncnenivmgingqfpgptiranagdsvvveltnklhtegvvih
whgilqrgtpwadgtasisqcainpgetffynftvdnpgtffyhghlgmqrsaglygsli
vdppqgkke
>d1asqa2 2.5.1.3.4 (130-338) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
pfhydgeinlllsdwwhqsihkqevglsskpirwigepqtillngrgqfdcsiaakydsn
lepcklkgsescapyifhvspkktyririasttalaalnfaignhqllvveadgnyvqpf
ytsdidiysgesysvlittdqnpsenywvsvgtrarhpntppgltllnylpnsvsklpts
pppqtpawddfdrsknftyritaamgspk
>d1asqa3 2.5.1.3.4 (339-552) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
ppvkfnrrifllntqnvingyvkwaindvslalpptpylgamkynllhafdqnpppevfp
edydidtpptnektrigngvyqfkigevvdvilqnanmmkenlsethpwhlhghdfwvlg
ygdgkfsaeeesslnlknpplrntvvifpygwtairfvadnpgvwafhchiephlhmgmg
vvfaegvekvgriptkalacggtakslinnpknp
>d1asqb1 2.5.1.3.4 (1-129) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
sqirhykweveymfwapncnenivmgingqfpgptiranagdsvvveltnklhtegvvih
whgilqrgtpwadgtasisqcainpgetffynftvdnpgtffyhghlgmqrsaglygsli
vdppqgkke
>d1asqb2 2.5.1.3.4 (130-338) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
pfhydgeinlllsdwwhqsihkqevglsskpirwigepqtillngrgqfdcsiaakydsn
lepcklkgsescapyifhvspkktyririasttalaalnfaignhqllvveadgnyvqpf
ytsdidiysgesysvlittdqnpsenywvsvgtrarhpntppgltllnylpnsvsklpts
pppqtpawddfdrsknftyritaamgspk
>d1asqb3 2.5.1.3.4 (339-552) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
ppvkfnrrifllntqnvingyvkwaindvslalpptpylgamkynllhafdqnpppevfp
edydidtpptnektrigngvyqfkigevvdvilqnanmmkenlsethpwhlhghdfwvlg
ygdgkfsaeeesslnlknpplrntvvifpygwtairfvadnpgvwafhchiephlhmgmg
vvfaegvekvgriptkalacggtakslinnpknp
>d1ass__ 3.7.5.2.1 Thermosome {Thermoplasma acidophilum}
msgividkekvhskmpdvvknakialidsaleikkteieakvqisdpskiqdflnqetnt
fkqmvekikksganvvlcqkgiddvaqhylakegiyavrrvkksdmeklakatgakivtd
lddltpsvlgeaetveerkigddrmtfvmgck
>d1ast__ 4.71.1.6.1 Astacin {European fresh water crayfish (Astacus astacus)}
aailgdeylwsggvipytfagvsgadqsailsgmqeleektcirfvprttesdyveifts
gsgcwsyvgrisgaqqvslqangcvyhgtiihelmhaigfyhehtrmdrdnyvtinyqnv
dpsmtsnfdidtysryvgedyqyysimhygkysfsiqwgvletivplqngidltdpydka
hmlqtdanqinnlytnecsl
>d1asu__ 3.46.3.2.1 ASV integrase, catalytic domain {Avian sarcoma virus, Rous sarcoma virus, Schmidt-Ruppin strain B}
plreprglgplqiwqtdftleprmaprswlavtvdtassaivvtqhgrvtsvaaqhhwat
aiavlgrpkaiktdngscftskstrewlarwgiahttgipgnsqgqamveranrllkdki
rvlaegdgfmkriptskqgellakamyalnhfergentktnl
>d1asv__ 3.46.3.2.1 ASV integrase, catalytic domain {Avian sarcoma virus, Rous sarcoma virus, Schmidt-Ruppin strain B}
glgplqiwqtdftleprmaprswlavtvdtassaivvtqhgrvtsvaaqhhwataiavlg
rpkaiktdngscftskstrewlarwgiahttgipgnsqgqamveranrllkdkirvlaeg
dgfmkriptskqgellakamyalnhf
>d1asw__ 3.46.3.2.1 ASV integrase, catalytic domain {Avian sarcoma virus, Rous sarcoma virus, Schmidt-Ruppin strain B}
reprglgplqiwqtdftleprxaprswlavtvdtassaivvtqhgrvtsvaaqhhwatai
avlgrpkaiktdngscftskstrewlarwgiahttgipgnsqgqaxveranrllkdkirv
laegdgfxkriptskqgellakaxyalnhfer
>d1asx__ 3.7.5.2.1 Thermosome {Thermoplasma acidophilum}
msgividkekvhskmpdvvknakialidsaleikkteieakvqisdpskiqdflnqetnt
fkqmvekikksganvvlcqkgiddvaqhylakegiyavrrvkksdmeklakatgakivtd
lddltpsvlgeaetveerkigddrmtfvmgck
>d1asya1 2.35.4.1.1 (68-204) Aspartyl-tRNA synthetase (AspRS) {Baker's yeast (Saccharomyces cerevisiae)}
edtakdnygklpliqsrdsdrtgqkrvkfvdldeakdsdkevlfrarvhntrqqgatlaf
ltlrqqasliqglvkankegtisknmvkwagslnlesivlvrgivkkvdepiksatvqnl
eihitkiytisetpeal
>d1asya2 4.82.1.1.7 (205-557) Aspartyl-tRNA synthetase (AspRS) {Baker's yeast (Saccharomyces cerevisiae)}
pilledasrseaeaeaaglpvvnldtrldyrvidlrtvtnqaifriqagvcelfreylat
kkftevhtpkllgapseggssvfevtyfkgkaylaqspqfnkqqlivadfervyeigpvf
raensnthrhmteftgldmemafeehyhevldtlselfvfifselpkrfaheielvrkqy
pveefklpkdgkmvrltykegiemlraagkeigdfedlstenekflgklvrdkydtdfyi
ldkfpleirpfytmpdpanpkysnsydffmrgeeilsgaqrihdhallqermkahglspe
dpglkdycdgfsygcpphagggiglervvmfyldlknirraslfprdpkrlrp
>d1asyb1 2.35.4.1.1 (68-204) Aspartyl-tRNA synthetase (AspRS) {Baker's yeast (Saccharomyces cerevisiae)}
edtakdnygklpliqsrdsdrtgqkrvkfvdldeakdsdkevlfrarvhntrqqgatlaf
ltlrqqasliqglvkankegtisknmvkwagslnlesivlvrgivkkvdepiksatvqnl
eihitkiytisetpeal
>d1asyb2 4.82.1.1.7 (205-557) Aspartyl-tRNA synthetase (AspRS) {Baker's yeast (Saccharomyces cerevisiae)}
pilledasrseaeaeaaglpvvnldtrldyrvidlrtvtnqaifriqagvcelfreylat
kkftevhtpkllgapseggssvfevtyfkgkaylaqspqfnkqqlivadfervyeigpvf
raensnthrhmteftgldmemafeehyhevldtlselfvfifselpkrfaheielvrkqy
pveefklpkdgkmvrltykegiemlraagkeigdfedlstenekflgklvrdkydtdfyi
ldkfpleirpfytmpdpanpkysnsydffmrgeeilsgaqrihdhallqermkahglspe
dpglkdycdgfsygcpphagggiglervvmfyldlknirraslfprdpkrlrp
>d1asza1 2.35.4.1.1 (68-204) Aspartyl-tRNA synthetase (AspRS) {Baker's yeast (Saccharomyces cerevisiae)}
edtakdnygklpliqsrdsdrtgqkrvkfvdldeakdsdkevlfrarvhntrqqgatlaf
ltlrqqasliqglvkankegtisknmvkwagslnlesivlvrgivkkvdepiksatvqnl
eihitkiytisetpeal
>d1asza2 4.82.1.1.7 (205-557) Aspartyl-tRNA synthetase (AspRS) {Baker's yeast (Saccharomyces cerevisiae)}
pilledasrseaeaeaaglpvvnldtrldyrvidlrtvtnqaifriqagvcelfreylat
kkftevhtpkllgapseggssvfevtyfkgkaylaqspqfnkqqlivadfervyeigpvf
raensnthrhmteftgldmemafeehyhevldtlselfvfifselpkrfaheielvrkqy
pveefklpkdgkmvrltykegiemlraagkeigdfedlstenekflgklvrdkydtdfyi
ldkfpleirpfytmpdpanpkysnsydffmrgeeilsgaqrihdhallqermkahglspe
dpglkdycdgfsygcpphagggiglervvmfyldlknirraslfprdpkrlrp
>d1aszb1 2.35.4.1.1 (68-204) Aspartyl-tRNA synthetase (AspRS) {Baker's yeast (Saccharomyces cerevisiae)}
edtakdnygklpliqsrdsdrtgqkrvkfvdldeakdsdkevlfrarvhntrqqgatlaf
ltlrqqasliqglvkankegtisknmvkwagslnlesivlvrgivkkvdepiksatvqnl
eihitkiytisetpeal
>d1aszb2 4.82.1.1.7 (205-557) Aspartyl-tRNA synthetase (AspRS) {Baker's yeast (Saccharomyces cerevisiae)}
pilledasrseaeaeaaglpvvnldtrldyrvidlrtvtnqaifriqagvcelfreylat
kkftevhtpkllgapseggssvfevtyfkgkaylaqspqfnkqqlivadfervyeigpvf
raensnthrhmteftgldmemafeehyhevldtlselfvfifselpkrfaheielvrkqy
pveefklpkdgkmvrltykegiemlraagkeigdfedlstenekflgklvrdkydtdfyi
ldkfpleirpfytmpdpanpkysnsydffmrgeeilsgaqrihdhallqermkahglspe
dpglkdycdgfsygcpphagggiglervvmfyldlknirraslfprdpkrlrp
>d1at0__ 2.76.1.1.1 Hedgehog {Fruit fly (Drosophila melanogaster)}
cftpestallesgvrkplgelsigdrvlsxtangqavysevilfxdrnleqxqnfvqlht
dggavltvtpahlvsvwqpesqkltfvfadrieeknqvlvrdvetgelrpqrvvkvgsvr
skgvvapltregtivvnsvaascya
>d1at1a1 3.66.1.1.1 (1-150) Aspartate carbamoyltransferase catalytic subunit {Escherichia coli}
anplyqkhiisindlsrddlnlvlataaklkanpqpellkhkviascffeastrtrlsfq
tsmhrlgasvvgfsdsantslgkkgetladtisvistyvdaivmrhpqegaarlatefsg
nvpvlnagdgsnqhptqtlldlftiqqteg
>d1at1a2 3.66.1.1.1 (151-310) Aspartate carbamoyltransferase catalytic subunit {Escherichia coli}
rldnlhvamvgdlkygrtvhsltqalakfdgnrfyfiapdalampeyildmldekgiaws
lhssieevmaevdilymtrvqkerldpseyanvkaqfvlrasdlhnakanmkvlhplprv
deiatdvdktphawyfqqagngifarqallalvlnrdlvl
>d1at1b1 4.47.2.1.1 (8-100) Aspartate carbamoyltransferase {Escherichia coli}
gveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlikientfls
edqvdqlalyapqatvnridnyevvgksrpslp
>d1at1b2 7.35.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1at1c1 3.66.1.1.1 (1-150) Aspartate carbamoyltransferase catalytic subunit {Escherichia coli}
anplyqkhiisindlsrddlnlvlataaklkanpqpellkhkviascffeastrtrlsfq
tsmhrlgasvvgfsdsantslgkkgetladtisvistyvdaivmrhpqegaarlatefsg
nvpvlnagdgsnqhptqtlldlftiqqteg
>d1at1c2 3.66.1.1.1 (151-310) Aspartate carbamoyltransferase catalytic subunit {Escherichia coli}
rldnlhvamvgdlkygrtvhsltqalakfdgnrfyfiapdalampeyildmldekgiaws
lhssieevmaevdilymtrvqkerldpseyanvkaqfvlrasdlhnakanmkvlhplprv
deiatdvdktphawyfqqagngifarqallalvlnrdlvl
>d1at1d1 4.47.2.1.1 (8-100) Aspartate carbamoyltransferase {Escherichia coli}
gveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlikientfls
edqvdqlalyapqatvnridnyevvgksrpslp
>d1at1d2 7.35.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1at3a_ 2.51.1.1.2 HSV-2 protease {Herpes simplex virus type II, HSV-2}
ravpiyvagflalydsgdpgelaldpdtvraalppenplpinvdhrarcevgrvlavvnd
prgpffvgliacvqlervletaasaaiferrgpalsreerllylitnylpsvslstkrrg
devppdrtlfahvalcaigrrlgtivtydtsldaaiapfrhldpatregvrreaaeaela
lagrtwapgvealthtllstavnnmmlrdrwslvaerrrqagiaghtylqa
>d1at3b_ 2.51.1.1.2 HSV-2 protease {Herpes simplex virus type II, HSV-2}
ravpiyvagflalydsgdpgelaldpdtvraalppenplpinvdhrarcevgrvlavvnd
prgpffvgliacvqlervletaasaaiferrgpalsreerllylitnylpsvslstkrrg
devppdrtlfahvalcaigrrlgtivtydtsldaaiapfrhldpatregvrreaaeaela
lagrtwapgvealthtllstavnnmmlrdrwslvaerrrqagiaghtylqa
>d1at5__ 4.2.1.2.1 Lysozyme {Chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsxxngmnawvawrnrckgtdv
qawirgcrl
>d1at6__ 4.2.1.2.1 Lysozyme {Chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsxgngmnawvawrnrckgtdv
qawirgcrl
>d1at9__ 6.2.1.1.2 Bacteriorhodopsin {Halobacterium salinarium}
aqitgrpewiwlalgtalmglgtlyflvkgmgvsdpdakkfyaittlvpaiaftmylsml
lgygltmvpfggeqnpiywaryadwlfttplllldlallvdadqgtilalvgadgimigt
glvgaltkvysyrfvwwaistaamlyilyvlffgftskaesmrpevastfkvlrnvtvvl
wsaypvvwligsegagivplnietllfmvldvsakvgfglillrsraifg
>d1ata__ 7.22.1.1.1 Ascaris trypsin inhibitor {Pig roundworm (Ascaris Lumbricoides), var. Suum}
eaekctkpneqwtkcggcegtcaqkivpctreckpprceciasagfvrdaqgncikfedc
pk
>d1atb__ 7.22.1.1.1 Ascaris trypsin inhibitor {Pig roundworm (Ascaris Lumbricoides), var. Suum}
eaekctkpneqwtkcggcegtcaqkivpctreckpprceciasagfvrdaqgncikfedc
pk
>d1atd__ 7.22.1.1.1 Ascaris trypsin inhibitor {Pig roundworm (Ascaris Lumbricoides), var. Suum}
eaekctkpneqwtkcggcegtcaqkivpctreckpprceciasagfvrdaqgncikfedc
pk
>d1ate__ 7.22.1.1.1 Ascaris trypsin inhibitor {Pig roundworm (Ascaris Lumbricoides), var. Suum}
eaekctkpneqwtkcggcegtcaqkivpctreckpprceciasagfvrdaqgncikfedc
pk
>d1atg__ 3.84.1.1.17 Molybdate-binding protein, ModA {Azotobacter vinelandii}
elkvvtatnflgtleqlagqfakqtghavvissgssgpvyaqivngapynvffsadeksp
ekldnqgfalpgsrftyaigklvlwsakpglvdnqgkvlagngwrhiaisnpqiapygla
gtqvlthlglldkltaqeriveansvgqahsqtasgaadlgfvalaqiiqaaakipgshw
fppanyyepivqqavitkstaekanaeqfmswmkgpkavaiikaagyvlpq
>d1atha_ 5.1.1.1.6 Antithrombin {Human (Homo sapiens)}
rrvwelskansrfattfyqhladskndndniflsplsistafamtklgacndtlqqlmev
fkfdtisektsdqihfffaklncrlyrkankssklvsanrlfgdksltfnetyqdiselv
ygaklqpldfkenaeqsraainkwvsnktegritdvipseaineltvlvlvntiyfkglw
kskfspentrkelfykadgescsasmmyqegkfryrrvaegtqvlelpfkgdditmvlil
pkpekslakvekeltpevlqewldeleemmlvvhmprfriedgfslkeqlqdmglvdlfs
peksklpgivaegrddlyvsdafhkaflevneegseaaastavviagrslnpnrvtfkan
rpflvfirevplntiifmgrvanpcv
>d1athb_ 5.1.1.1.6 Antithrombin {Human (Homo sapiens)}
vwelskansrfattfyqhladskndndniflsplsistafamtklgacndtlqqlmevfk
fdtisektsdqihfffaklncrlyrkankssklvsanrlfgdksltfnetyqdiselvyg
aklqpldfkenaeqsraainkwvsnktegritdvipseaineltvlvlvntiyfkglwks
kfspentrkelfykadgescsasmmyqegkfryrrvaegtqvlelpfkgdditmvlilpk
pekslakvekeltpevlqewldeleemmlvvhmprfriedgfslkeqlqdmglvdlfspe
ksklpgivaegrddlyvsdafhkaflevneegseaaastavviagrslnpnrvtfkanrp
flvfirevplntiifmgrvanpc
>d1atia1 3.42.1.1.3 (395-505) Glycyl-tRNA synthetase (GlyRS), C-terminal domain {Thermus thermophilus}
qlapikvaviplvknrpeiteyakrlkarllalglgrvlyedtgnigkayrrhdevgtpf
avtvdydtigqskdgttrlkdtvtvrdrdtmeqirlhvdelegflrerlrw
>d1atia2 4.82.1.1.5 (1-394) Glycyl-tRNA synthetase (GlyRS) {Thermus thermophilus}
aassldelvalckrrgfifqsseiygglqgvydygplgvelknnlkqawwrrnvyerddm
egldasvlthrlvlhysgheatfadpmvdnritkkryrldhllkeqpeevlkrlyramev
eeenlhalvqammqaperaggamtaagvldpasgepgdwtppryfnmmfqdlrgprggrg
llaylrpetaqgifvnfknvldatsrklgfgiaqigkafrneitprnfifrvrefeqmei
eyfvrpgedeywhrywveerlkwwqemglsrenlvpyqqppessahyakatvdilyrfph
gslelegiaqrtdfdlgshtkdqealgitarvlrnehstqrlayrdpetgkwfvpyviep
sagvdrgvlallaeaftreelpngeerivlklkp
>d1atib1 3.42.1.1.3 (395-505) Glycyl-tRNA synthetase (GlyRS), C-terminal domain {Thermus thermophilus}
qlapikvaviplvknrpeiteyakrlkarllalglgrvlyedtgnigkayrrhdevgtpf
avtvdydtigqskdgttrlkdtvtvrdrdtmeqirlhvdelegflrerlrw
>d1atib2 4.82.1.1.5 (1-394) Glycyl-tRNA synthetase (GlyRS) {Thermus thermophilus}
aassldelvalckrrgfifqsseiygglqgvydygplgvelknnlkqawwrrnvyerddm
egldasvlthrlvlhysgheatfadpmvdnritkkryrldhllkeqpeevlkrlyramev
eeenlhalvqammqaperaggamtaagvldpasgepgdwtppryfnmmfqdlrgprggrg
llaylrpetaqgifvnfknvldatsrklgfgiaqigkafrneitprnfifrvrefeqmei
eyfvrpgedeywhrywveerlkwwqemglsrenlvpyqqppessahyakatvdilyrfph
gslelegiaqrtdfdlgshtkdqealgitarvlrnehstqrlayrdpetgkwfvpyviep
sagvdrgvlallaeaftreelpngeerivlklkp
>d1atja_ 1.90.1.1.6 Peroxidase {Horseradish (Armoracia rusticana)}
qltptfydnscpnvsnivrdtivnelrsdpriaasilrlhfhdcfvngcdasilldntts
frtekdafgnansargfpvidrmkaavesacprtvscadlltiaaqqsvtlaggpswrvp
lgrrdslqafldlananlpapfftlpqlkdsfrnvglnrssdlvalsgghtfgknqcrfi
mdrlynfsntglpdptlnttylqtlrglcplngnlsalvdfdlrtptifdnkyyvnleeq
kgliqsdqelfsspnatdtiplvrsfanstqtffnafveamdrmgnitpltgtqgqirln
crvvns
>d1atjb_ 1.90.1.1.6 Peroxidase {Horseradish (Armoracia rusticana)}
qltptfydnscpnvsnivrdtivnelrsdpriaasilrlhfhdcfvngcdasilldntts
frtekdafgnansargfpvidrmkaavesacprtvscadlltiaaqqsvtlaggpswrvp
lgrrdslqafldlananlpapfftlpqlkdsfrnvglnrssdlvalsgghtfgknqcrfi
mdrlynfsntglpdptlnttylqtlrglcplngnlsalvdfdlrtptifdnkyyvnleeq
kgliqsdqelfsspnatdtiplvrsfanstqtffnafveamdrmgnitpltgtqgqirln
crvvns
>d1atjc_ 1.90.1.1.6 Peroxidase {Horseradish (Armoracia rusticana)}
qltptfydnscpnvsnivrdtivnelrsdpriaasilrlhfhdcfvngcdasilldntts
frtekdafgnansargfpvidrmkaavesacprtvscadlltiaaqqsvtlaggpswrvp
lgrrdslqafldlananlpapfftlpqlkdsfrnvglnrssdlvalsgghtfgknqcrfi
mdrlynfsntglpdptlnttylqtlrglcplngnlsalvdfdlrtptifdnkyyvnleeq
kgliqsdqelfsspnatdtiplvrsfanstqtffnafveamdrmgnitpltgtqgqirln
crvvns
>d1atjd_ 1.90.1.1.6 Peroxidase {Horseradish (Armoracia rusticana)}
qltptfydnscpnvsnivrdtivnelrsdpriaasilrlhfhdcfvngcdasilldntts
frtekdafgnansargfpvidrmkaavesacprtvscadlltiaaqqsvtlaggpswrvp
lgrrdslqafldlananlpapfftlpqlkdsfrnvglnrssdlvalsgghtfgknqcrfi
mdrlynfsntglpdptlnttylqtlrglcplngnlsalvdfdlrtptifdnkyyvnleeq
kgliqsdqelfsspnatdtiplvrsfanstqtffnafveamdrmgnitpltgtqgqirln
crvvns
>d1atje_ 1.90.1.1.6 Peroxidase {Horseradish (Armoracia rusticana)}
qltptfydnscpnvsnivrdtivnelrsdpriaasilrlhfhdcfvngcdasilldntts
frtekdafgnansargfpvidrmkaavesacprtvscadlltiaaqqsvtlaggpswrvp
lgrrdslqafldlananlpapfftlpqlkdsfrnvglnrssdlvalsgghtfgknqcrfi
mdrlynfsntglpdptlnttylqtlrglcplngnlsalvdfdlrtptifdnkyyvnleeq
kgliqsdqelfsspnatdtiplvrsfanstqtffnafveamdrmgnitpltgtqgqirln
crvvns
>d1atjf_ 1.90.1.1.6 Peroxidase {Horseradish (Armoracia rusticana)}
qltptfydnscpnvsnivrdtivnelrsdpriaasilrlhfhdcfvngcdasilldntts
frtekdafgnansargfpvidrmkaavesacprtvscadlltiaaqqsvtlaggpswrvp
lgrrdslqafldlananlpapfftlpqlkdsfrnvglnrssdlvalsgghtfgknqcrfi
mdrlynfsntglpdptlnttylqtlrglcplngnlsalvdfdlrtptifdnkyyvnleeq
kgliqsdqelfsspnatdtiplvrsfanstqtffnafveamdrmgnitpltgtqgqirln
crvvns
>d1atk__ 4.3.1.1.13 (Pro)cathepsin K {Human (Homo sapiens)}
apdsvdyrkkgyvtpvknqgqcgscwafssvgalegqlkkktgkllnlspqnlvdcvsen
dgcgggymtnafqyvqknrgidsedaypyvgqeescmynptgkaakcrgyreipegneka
lkravarvgpvsvaidasltsfqfyskgvyydescnsdnlnhavlavgygiqkgnkhwii
knswgenwgnkgyilmarnknnacgianlasfpkm
>d1atla_ 4.71.1.7.2 Snake venom metalloprotease {Western diamonback rattlesnake (Crotalus atrox), atrolysin C}
lpqryielvvvadhrvfmkynsdlntirtrvheivnfingfyrslnihvsltdleiwsne
dqiniqsassdtlnafaewretdllnrkshdnaqlltaieldeetlglaplgtmcdpkls
igivqdhspinllmgvtmahelghnlgmehdgkdclrgaslcimrpgltkgrsyefsdds
mhyyerflkqykpqcilnkp
>d1atlb_ 4.71.1.7.2 Snake venom metalloprotease {Western diamonback rattlesnake (Crotalus atrox), atrolysin C}
lpqryielvvvadhrvfmkynsdlntirtrvheivnfingfyrslnihvsltdleiwsne
dqiniqsassdtlnafaewretdllnrkshdnaqlltaieldeetlglaplgtmcdpkls
igivqdhspinllmgvtmahelghnlgmehdgkdclrgaslcimrpgltkgrsyefsdds
mhyyerflkqykpqcilnkp
>d1atna1 3.46.1.1.4 (1-146) Actin {Bovine (Bos taurus), pancreas}
dedettalvcdngsglvkagfagddapravfpsivgrprhqgvmvgmgqkdsyvgdeaqs
krgiltlkypiehgiitnwddmekiwhhtfynelrvapeehptllteaplnpkanrekmt
qimfetfnvpamyvaiqavlslyasg
>d1atna2 3.46.1.1.4 (147-372) Actin {Bovine (Bos taurus), pancreas}
rttgivldsgdgvthnvpiyegyalphaimrldlagrdltdylmkiltergysfvttaer
eivrdikeklcyvaldfenemataassssleksyelpdgqvitignerfrcpetlfqpsf
igmesagihettynsimkcdidirkdlyannvmsggttmypgiadrmqkeitalapstmk
ikiiapperkysvwiggsilaslstfqqmwitkqeydeagpsivhr
>d1atnd_ 4.122.1.1.3 Deoxyribonuclease I {Bovine (Bos taurus)}
lkiaafnirtfgetkmsnatlasyivrivrrydivliqevrdshlvavgklldylnqddp
ntyhyvvseplgrnsykerylflfrpnkvsvldtyqyddgcgncgndsfsrepavvkfss
hstkvkefaivalhsapsdavaeinslydvyldvqqkwhlndvmlmgdfnadcsyvtssq
wssirlrtsstfqwlipdsadttatstncaydrivvagsllqssvvpgsaapfdfqaayg
lsnemalaisdhypvevtlt
>d1atpe_ 4.117.1.1.5 cAMP-dependent PK, catalytic subunit {Mouse (Mus musculus)}
vkeflakakedflkkwetpsqntaqldqfdriktlgtgsfgrvmlvkhkesgnhyamkil
dkqkvvklkqiehtlnekrilqavnfpflvklefsfkdnsnlymvmeyvaggemfshlrr
igrfsepharfyaaqivltfeylhsldliyrdlkpenllidqqgyiqvtdfgfakrvkgr
twtlcgtpeylapeiilskgynkavdwwalgvliyemaagyppffadqpiqiyekivsgk
vrfpshfssdlkdllrnllqvdltkrfgnlkngvndiknhkwfattdwiaiyqrkveapf
ipkfkgpgdtsnfddyeeeeirvsinekcgkeftef
>d1atr_1 3.46.1.1.1 (2-188) Heat shock protein 70kDa, ATPase fragment {Bovine (Bos taurus)}
skgpavgidlgttyscvgvfqhgkveiiandqgnrttpsyvaftdterligdaaknqvam
nptntvfdakrligrrfddavvqsdmkhwpfmvvndagrpkvqveykgetksfypeevss
mvltkmkeiaeaylgktvtnavvtvpayfndsqrqatkdagtiaglnvlriineptaaai
aygldkk
>d1atr_2 3.46.1.1.1 (189-384) Heat shock protein 70kDa, ATPase fragment {Bovine (Bos taurus)}
vgaernvlifdlgggvfdvsiltiedgifevkstagdthlggedfdnrmvnhfiaefkrk
hkkdisenkravrrlrtacerakrtlssstqasieidslyegidfytsitrarfeelnad
lfrgtldpvekalrdakldksqihdivlvggstripkiqkllqdffngkelnksinpdea
vaygaavqaailsgdk
>d1ats_1 3.46.1.1.1 (2-188) Heat shock protein 70kDa, ATPase fragment {Bovine (Bos taurus)}
skgpavgidlgttyscvgvfqhgkveiiandqgnrttpsyvaftdterligdaaknqvam
nptntvfdakrligrrfddavvqsdmkhwpfmvvndagrpkvqveykgetksfypeevss
mvltkmkeiaeaylgktvtnavvtvpayfndsqrqatkdagtiaglnvlriineptaaai
aygldkk
>d1ats_2 3.46.1.1.1 (189-383) Heat shock protein 70kDa, ATPase fragment {Bovine (Bos taurus)}
vgaernvlifdlgggefdvsiltiedgifevkstagdthlggedfdnrmvnhfiaefkrk
hkkdisenkravrrlrtacerakrtlssstqasieidslyegidfytsitrarfeelnad
lfrgtldpvekalrdakldksqihdivlvggstripkiqkllqdffngkelnksinpdea
vaygaavqaailsgd
>d1atta_ 5.1.1.1.5 Antithrombin {Bovine (Bos taurus)}
vedvctakprdipvnpmciyrategqgseqkipgatnrrvwelskanshfatafyqhlad
sknnndniflsplsistafamtklgacnntltqlmevfkfdtisektsdqihfffaklnc
rlyrkanksselvsanrlfgdksitfnetyqdisevvygaklqpldfkgnaeqsrltinq
wisnktegritdvippqaineftvlvlvntiyfkglwkskfspentrkelfykadgescs
vlmmyqeskfryrrvaestqvlelpfkgdditmvlilpklektlakveqeltpdmlqewl
deltetllvvhmprfriedsfsvkeqlqdmgledlfspeksrlpgivaegrsdlyvsdaf
hkaflevneegseaaastvisiagrslrvtfkanrpflvlirevalntiifmgrvanpcv
d
>d1attb_ 5.1.1.1.5 Antithrombin {Bovine (Bos taurus)}
kprdipvnpmciyrssqkipgatnrrvwelskanshfatafyqhladsknnndniflspl
sistafamtklgacnntltqlmevfkfdtisektsdqihfffaklncrlyrkanksselv
sanrlfgdksitfnetyqdisevvygaklqpldfkgnaeqsrltinqwisnktegritdv
ippqaineftvlvlvntiyfkglwkskfspentrkelfykadgescsvlmmyqeskfryr
rvaestqvlelpfkgdditmvlilpklektlakveqeltpdmlqewldeltetllvvhmp
rfriedsfsvkeqlqdmgledlfspeksrlpgivaegrsdlyvsdafhkaflevneegse
aaastvisiagrslnsdrvtfkanrpflvlirevalntiifmgrvanpcvd
>d1atu__ 5.1.1.1.4 Antitrypsin, alpha-1 {Human (Homo sapiens)}
ptfnkitpnlaefafslyrqlahqsnstnilfspvsiaaafamlslgakgdthdeilegl
nfnlteipeaqihegfqellrtlnqpdsqlqlttgnglflseglklvdkfledvkklyhs
eaftvnfgdteeakkqindyvekgtqgkivdlvkeldrdtvfalvnyiffkgkwerpfev
kdteeedfhvdqvttvkvpmmkrlgmfniqhckklsswvllmkylgnataifflpdegkl
qhlenelthdiitkflenedrrsaslhlpklsitgtydlksvlgqlgitkvfsngadlsg
vteeaplklskavhkavltidekgteaagamfleaipmsippevkfnkpfvfliieqntk
aplfmgrvvnptqk
>d1atx__ 7.9.1.1.6 Sea anemone toxin IA {Sea anemone (Anemonia sulcata)}
gaaclcksdgpntrgnsmsgtiwvfgcpsgwnncegraiigycckq
>d1atza_ 3.52.1.1.2 von Willebrand factor A3 domain {Human (Homo sapiens)}
qpldvillldgsssfpasyfdemksfakafiskanigprltqvsvlqygsittidvpwnv
vpekahllslvdvmqreggpsqigdalgfavryltsemhgarpgaskavvilvtdvsvds
vdaaadaarsnrvtvfpigigdrydaaqlrilagpagdsnvvklqriedlptmvtlgnsf
lhkl
>d1atzb_ 3.52.1.1.2 von Willebrand factor A3 domain {Human (Homo sapiens)}
dcsqpldvillldgsssfpasyfdemksfakafiskanigprltqvsvlqygsittidvp
wnvvpekahllslvdvmqreggpsqigdalgfavryltsemhgarpgaskavvilvtdvs
vdsvdaaadaarsnrvtvfpigigdrydaaqlrilagpagdsnvvklqriedlptmvtlg
nsflhklcs
>d1au0__ 4.3.1.1.13 (Pro)cathepsin K {Human (Homo sapiens)}
apdsvdyrkkgyvtpvknqgqcgscwafssvgalegqlkkktgkllnlspqnlvdcvsen
dgcgggymtnafqyvqknrgidsedaypyvgqeescmynptgkaakcrgyreipegneka
lkravarvgpvsvaidasltsfqfyskgvyydescnsdnlnhavlavgygiqkgnkhwii
knswgenwgnkgyilmarnknnacgianlasfpkm
>d1au1a_ 1.27.1.3.3 Interferon-beta {Human (Homo sapiens)}
msynllgflqrssnfqcqkllwqlngrleyclkdrmnfdipeeikqlqqfqkedaaltiy
emlqnifaifrqdssstgwnetivenllanvyhqinhlktvleeklekedftrgklmssl
hlkryygrilhylkakeyshcawtivrveilrnfyfinrltgylrn
>d1au1b_ 1.27.1.3.3 Interferon-beta {Human (Homo sapiens)}
msynllgflqrssnfqcqkllwqlngrleyclkdrmnfdipeeikqlqqfqkedaaltiy
emlqnifaifrqdssstgwnetivenllanvyhqinhlktvleeklekedftrgklmssl
hlkryygrilhylkakeyshcawtivrveilrnfyfinrltgylrn
>d1au2__ 4.3.1.1.13 (Pro)cathepsin K {Human (Homo sapiens)}
apdsvdyrkkgyvtpvknqgqcgscwafssvgalegqlkkktgkllnlspqnlvdcvsen
dgcgggymtnafqyvqknrgidsedaypyvgqeescmynptgkaakcrgyreipegneka
lkravarvgpvsvaidasltsfqfyskgvyydescnsdnlnhavlavgygiqkgnkhwii
knswgenwgnkgyilmarnknnacgianlasfpkm
>d1au3__ 4.3.1.1.13 (Pro)cathepsin K {Human (Homo sapiens)}
apdsvdyrkkgyvtpvknqgqcgscwafssvgalegqlkkktgkllnlspqnlvdcvsen
dgcgggymtnafqyvqknrgidsedaypyvgqeescmynptgkaakcrgyreipegneka
lkravarvgpvsvaidasltsfqfyskgvyydescnsdnlnhavlavgygiqkgnkhwii
knswgenwgnkgyilmarnknnacgianlasfpkm
>d1au4__ 4.3.1.1.13 (Pro)cathepsin K {Human (Homo sapiens)}
apdsvdyrkkgyvtpvknqgqcgscwafssvgalegqlkkktgkllnlspqnlvdcvsen
dgcgggymtnafqyvqknrgidsedaypyvgqeescmynptgkaakcrgyreipegneka
lkravarvgpvsvaidasltsfqfyskgvyydescnsdnlnhavlavgygiqkgnkhwii
knswgenwgnkgyilmarnknnacgianlasfpkm
>d1au7a1 1.4.1.1.6 (103-160) Pit-1 POU homeodomain {Rat (Rattus norvegicus)}
krrttisiaakdalerhfgehskpssqeimrmaeelnlekevvrvwfcnrrqrekrvk
>d1au7a2 1.36.1.1.2 (5-76) Pit-1 {Rat (Rattus norvegicus)}
gmraleqfanefkvrriklgytqtnvgealaavhgsefsqtticrfenlqlsfknacklk
ailskwleeaeq
>d1au7b1 1.4.1.1.6 (103-160) Pit-1 POU homeodomain {Rat (Rattus norvegicus)}
krrttisiaakdalerhfgehskpssqeimrmaeelnlekevvrvwfcnrrqrekrvk
>d1au7b2 1.36.1.1.2 (5-74) Pit-1 {Rat (Rattus norvegicus)}
gmraleqfanefkvrriklgytqtnvgealaavhgsefsqtticrfenlqlsfknacklk
ailskwleea
>d1au8a_ 2.41.1.2.20 Cathepsin G {Human (Homo sapiens)}
iiggresrphsrpymaylqiqspagqsrcggflvredfvltaahcwgsninvtlgahniq
rrentqqhitarrairhpqynqrtiqndimllqlsrrvrrnrnvnpvalpraqeglrpgt
lctvagwgrvsmrrgtdtlrevqlrvqrdrqclrifgsydprrqicvgdrrerkaafkgd
sggpllcnnvahgivsygkssgvppevftrvssflpwirttmrs
>d1au9__ 3.33.1.1.7 Subtilisin Novo/BPN' {Bacillus amyloliquefaciens}
aqsvpygvsqikapalhsqgycgsnvkvavidsgidsshpdlkvaggasfvpsetnpfqd
nnshgthvagtvaalnnsigvlgvapcaslyavkvlgadgsgqyswiingiewaiannmd
vinmslggpsgsaalkaavdkavasgvvvvaaagnegtsgssstvgypakypsviavgav
dssnqrasfssvgpeldvmapgvsicstlpgnkygaksgtsmasphvagaaalilskhpn
wtntqvrsslentttklgdsfyygkglinvqaaaq
>d1aua_1 1.5.3.1.1 (4-96) N-terminal domain of phosphatidylinositol transfer protein sec14p {Baker's yeast (Saccharomyces cerevisiae)}
qqekeflesypqncppdalpgtpgnldsaqekalaelrklledagfierlddstllrflr
arkfdvqlakemfencekwrkdygtdtilqdfh
>d1aua_2 3.10.1.1.1 (97-299) C-terminal domain of phosphatidylinositol transfer protein sec14p {Baker's yeast (Saccharomyces cerevisiae)}
ydekpliakfypqyyhktdkdgrpvyfeelgavnlhemnkvtseermlknlvweyesvvq
yrlpacsraaghlvetsctimdlkgisissaysvmsyvreasyisqnyypermgkfyiin
apfgfstafrlfkpfldpvtvskifilgssyqkellkqipaenlpvkfggksevdeskgg
lylsdigpwrdpkyigpegeape
>d1aub__ 1.4.5.1.2 N-terminal Zn binding domain of HIV integrase {Human immunodeficiency virus, type 2, HIV-2}
flekiepaqeehekyhsnvkelshkfgipnlvarqivnscaqcqqk
>d1auc__ 3.38.1.1.4 Thioredoxin {Human (Homo sapiens)}
mvkqiesktafqealdaagdklvvvdfsatwcgpckmikpffhslsekysnviflevdvd
dcqdvasecevkcmptfqffkkgqkvgefsgankekleatinelv
>d1auda_ 4.47.7.1.2 Splicesomal U1A protein {Human (Homo sapiens)}
avpetrpnhtiyinnlnekikkdelkkslhaifsrfgqildilvsrslkmrgqafvifke
vssatnalrsmqgfpfydkpmriqyaktdsdiiakmkgtfv
>d1auea_ 1.25.7.1.1 FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP) {Human (Homo sapiens)}
lwhemwhegleeasrlyfgernvkgmfevleplhammergpqtlketsfnqaygrdlmea
qewcrkymksgnvkdltqawdlyyhvfrrisk
>d1aueb_ 1.25.7.1.1 FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP) {Human (Homo sapiens)}
ilwhemwhegleeasrlyfgernvkgmfevleplhammergpqtlketsfnqaygrdlme
aqewcrkymksgnvkdltqawdlyyhvfrriskq
>d1auga_ 3.47.3.1.2 Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase) {Bacillus amyloliquefaciens}
mekkvlltgfdpfggetvnpsweavkrlngaaegpasivseqvptvfykslavlreaikk
hqpdiiicvgqaggrmqitpervainlnearipdnegnqpvgedisqggpaaywtglpik
riveeikkegipaavsytagtfvcnhlfyglmdeisrhhphirggfihipyipeqtlqks
apslsldhitkalkiaavtaavheddietg
>d1augb_ 3.47.3.1.2 Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase) {Bacillus amyloliquefaciens}
mekkvlltgfdpfggetvnpsweavkrlngaaegpasivseqvptvfykslavlreaikk
hqpdiiicvgqaggrmqitpervainlnearipdnegnqpvgedisqggpaaywtglpik
riveeikkegipaavsytagtfvcnhlfyglmdeisrhhphirggfihipyipeqtlqks
apslsldhitkalkiaavtaavheddietg
>d1augc_ 3.47.3.1.2 Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase) {Bacillus amyloliquefaciens}
mekkvlltgfdpfggetvnpsweavkrlngaaegpasivseqvptvfykslavlreaikk
hqpdiiicvgqaggrmqitpervainlnearipdnegnqpvgedisqggpaaywtglpik
riveeikkegipaavsytagtfvcnhlfyglmdeisrhhphirggfihipyipeqtlqks
apslsldhitkalkiaavtaavheddietg
>d1augd_ 3.47.3.1.2 Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase) {Bacillus amyloliquefaciens}
mekkvlltgfdpfggetvnpsweavkrlngaaegpasivseqvptvfykslavlreaikk
hqpdiiicvgqaggrmqitpervainlnearipdnegnqpvgedisqggpaaywtglpik
riveeikkegipaavsytagtfvcnhlfyglmdeisrhhphirggfihipyipeqtlqks
apslsldhitkalkiaavtaavheddietg
>d1auia_ 4.130.1.3.3 Protein phosphatase-2B (PP-2B, calcineurin A subunit) {Human (Homo sapiens)}
tdrvvkavpfppshrltakevfdndgkprvdilkahlmkegrleesvalriitegasilr
qeknlldidapvtvcgdihgqffdlmklfevggspantrylflgdyvdrgyfsiecvlyl
walkilypktlfllrgnhecrhlteyftfkqeckikyservydacmdafdclplaalmnq
qflcvhgglspeintlddirkldrfkeppaygpmcdilwsdpledfgnektqehfthntv
rgcsyfysypavceflqhnnllsilraheaqdagyrmyrksqttgfpslitifsapnyld
vynnkaavlkyennvmnirqfncsphpywlpnfmdvftwslpfvgekvtemlvnvlnics
ddelgseedgfdgataaarkevirnkiraigkmarvfsvlreesesvltlkgltptgmlp
sgvlsggkqtlqsatveaieadeaikgfspqhkitsfeeakgldrinermppr
>d1auib_ 1.42.1.5.20 Calcineurin regulatory subunit (B-chain) {Human (Homo sapiens)}
syplemcshfdadeikrlgkrfkkldldnsgslsveefmslpelqqnplvqrvidifdtd
gngevdfkefiegvsqfsvkgdkeqklrfafriydmdkdgyisngelfqvlkmmvgnnlk
dtqlqqivdktiinadkdgdgrisfeefcavvggldihkkmvvdv
>d1auj__ 2.41.1.2.1 Trypsin(ogen) {Bovine (Bos taurus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1auk__ 3.64.1.2.1 Arylsulfatase A {Human (Homo sapiens)}
rppnivlifaddlgygdlgcyghpssttpnldqlaagglrftdfyvpvslxtpsraallt
grlpvrmgmypgvlvpssrgglpleevtvaevlaargyltgmagkwhlgvgpegaflpph
qgfhrflgipyshdqgpcqnltcfppatpcdggcdqglvpipllanlsveaqppwlpgle
arymafahdlmadaqrqdrpfflyyashhthypqfsgqsfaersgrgpfgdslmeldaav
gtlmtaigdlglleetlviftadngpetmrmsrggcsgllrcgkgttyeggvrepalafw
pghiapgvthelassldllptlaalagaplpnvtldgfdlsplllgtgksprqslffyps
ypdevrgvfavrtgkykahfftqgsahsdttadpachasssltaheppllydlskdpgen
ynllggvagatpevlqalkqlqllkaqldaavtfgpsqvargedpalqicchpgctprpa
cchcp
>d1aum__ 1.29.3.1.3 HIV capsid protein, dimerisation domain {Human immunodeficiency virus, type 1, HIV-1}
ldirqgpkepfrdyvdrfyktlraeqasqevknwmtetllvqnanpdcktilkalgpgat
leemmtacqg
>d1aun__ 2.23.1.1.1 Pathogenesis-related protein 5d {Common tobacco (Nicotiana tabacum)}
sgvfevhnncpytvwaaatpvgggrrlergqswwfwappgtkmariwgrtncnfdgagrg
wcqtgdcggvleckgwgkppntlaeyalnqfsnldfwdisvidgfnipmsfgptkpgpgk
chgiqctaningecpgslrvpggcnnpcttfggqqycctqgpcgptelsrwfkqrcpday
sypqddptstftctswttdykvmfcpyg
>d1auoa_ 3.59.1.12.1 Carboxylesterase {Pseudomonas fluorescens}
mteplilqpakpadacviwlhglgadrydfmpvaealqesllttrfvlpqaptrpvting
gyempswydikamsparsisleelevsakmvtdlieaqkrtgidasriflagfsqggavv
fhtafinwqgplggvialstyaptfgdelelsasqqripalclhgqyddvvqnamgrsaf
ehlksrgvtvtwqeypmghevlpqeihdigawlaarlg
>d1auob_ 3.59.1.12.1 Carboxylesterase {Pseudomonas fluorescens}
mteplilqpakpadacviwlhglgadrydfmpvaealqesllttrfvlpqaptrpvting
gyempswydikamsparsisleelevsakmvtdlieaqkrtgidasriflagfsqggavv
fhtafinwqgplggvialstyaptfgdelelsasqqripalclhgqyddvvqnamgrsaf
ehlksrgvtvtwqeypmghevlpqeihdigawlaarlg
>d1aup_1 3.2.1.7.1 (205-449) Glutamate dehydrogenase {Clostridium symbiosum}
rpeatgygsvyyveavmkhendtlvgktvalagfgnvawgaakklaelgakavtlsgpdg
yiydpegitteekinymlemrasgrnkvqdyadkfgvqffpgekpwgqkvdiimpcatqn
dvdleqakkivannvkyyievanmpttnealrflmqqpnmvvapskavnaggvlvvgfem
sqnserlswtaeevdsklhqvmtdihdgsaaaaeryglgynlvaganivgfqkiadamma
qgiaw
>d1aup_2 3.48.1.1.1 (1-192) Glutamate dehydrogenase {Clostridium symbiosum}
skyvdrviaevekkyadepefvqtveevlsslgpvvdahpeyeevallermvipervief
rvpweddngkvhvntgyrvqfngaigpylgglrfapsvnlsimkflgfeqafkdslttlp
mggakggsdfdpngksdrevmrfcqafmtelyrhigpdidvpagdlgvgareigymygqy
rkivggfyngvl
>d1auq__ 3.52.1.1.3 von Willebrand factor A1 domain {Human (Homo sapiens)}
disepplhdfycsrlldlvflldgssrlseaefevlkafvvdmmerlrisqkwvrvavve
yhdgshayiglkdrkrpselrriasqvkyagsqvastsevlkytlfqifskidrpeasri
alllmasqepqrmsrnfvryvqglkkkkvivipvgigphanlkqirliekqapenkafvl
ssvdeleqqrdeivsylcdlapeapppt
>d1aura_ 3.59.1.12.1 Carboxylesterase {Pseudomonas fluorescens}
mteplilqpakpadacviwlhglgadrydfmpvaealqesllttrfvlpqaptrpvting
gyempswydikamsparsisleelevsakmvtdlieaqkrtgidasriflagfsqggavv
fhtafinwqgplggvialstyaptfgdelelsasqqripalclhgqyddvvqnamgrsaf
ehlksrgvtvtwqeypmghevlpqeihdigawlaarlg
>d1aurb_ 3.59.1.12.1 Carboxylesterase {Pseudomonas fluorescens}
mteplilqpakpadacviwlhglgadrydfmpvaealqesllttrfvlpqaptrpvting
gyempswydikamsparsisleelevsakmvtdlieaqkrtgidasriflagfsqggavv
fhtafinwqgplggvialstyaptfgdelelsasqqripalclhgqyddvvqnamgrsaf
ehlksrgvtvtwqeypmghevlpqeihdigawlaarlg
>d1ausl1 3.1.12.1.2 (148-463) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
fqgpphgiqverdklnkygrpllgctikpklglsaknygravyeclrggldftkddenvn
sqpfmrwrdrflfcaealykaqaetgeikghylnatagtcedmmkravfarelgvpivmh
dyltggftanttlshycrdnglllhihramhavidrqknhgmhfrvlakalrlsggdhih
sgtvvgklegerditlgfvdllrddytekdrsrgiyftqswvstpgvlpvasggihvwhm
palteifgddsvlqfgggtlghpwgnapgavanrvaleacvqarnegrdlaregntiire
atkwspelaaacevwk
>d1ausl2 4.47.9.1.2 (20-147) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
ykltyytpeyetldtdilaafrvspqpgvppeeagaavaaesstgtwttvwtdgltnldr
ykgrcyhiepvageenqyicyvaypldlfeegsvtnmftsivgnvfgfkalralrledlr
ipvayvkt
>d1auss_ 4.55.1.1.2 Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
mqvwpilnlkkyetlsylpplttdqlarqvdyllnnkwvpclefetdhgfvyrehhnspg
yydgrywtmwklpmfgctdpaqvlneleeckkeypnafiriigfdsnrevqcisfiaykp
agy
>d1autc_ 2.41.1.2.36 Activated protein c (autoprothrombin IIa) {Human (Homo sapiens)}
lidgkmtrrgdspwqvvlldskkklacgavlihpswvltaahcmdeskkllvrlgeydlr
rwekweldldikevfvhpnysksttdndiallhlaqpatlsqtivpiclpdsglaereln
qagqetlvtgwgyhssrekeakrnrtfvlnfikipvvphnecsevmsnmvsenmlcagil
gdrqdacegdsggpmvasfhgtwflvglvswgegcgllhnygvytkvsryldwihghird
>d1autl1 7.3.11.1.7 (49-96) Activated protein c (autoprothrombin IIa) {Human (Homo sapiens)}
qclvlplehpcaslccghgtcixgigsfscdcrsgwegrfcqrevsfl
>d1autl2 7.3.11.1.7 (97-146) Activated protein c (autoprothrombin IIa) {Human (Homo sapiens)}
ncsldnggcthycleevgwrrcscapgyklgddllqchpavkfpcgrpwk
>d1auua_ 2.31.2.1.1 SacY {Bacillus subtilis}
mkikrilnhnaivvkdqneekillgagiafnkkkndivdpskiektfirkdtpdy
>d1auub_ 2.31.2.1.1 SacY {Bacillus subtilis}
mkikrilnhnaivvkdqneekillgagiafnkkkndivdpskiektfirkdtpdy
>d1auva1 3.24.1.5.1 (112-213) Synapsin Ia domain {Bovine (Bos taurus)}
aarvllvidephtdwakyfkgkkihgeidikveqaefsdlnlvahanggfsvdxevlrng
vkvvrslkpdfvlirqhafsxarngdyrslviglqyagipsi
>d1auva2 4.115.1.3.1 (214-417) Synapsin Ia, C-terminal domain {Bovine (Bos taurus)}
nslhsvynfcdkpwvfaqxvrlhkklgteefplinqtfypnhkexlssttypvvvkxgha
hsgxgkvkvdnqhdfqdiasvvaltktyattepfidakydvriqkigqnykayxrtsvsg
nwktntgsaxleqiaxsdryklwvdtcseifggldicavealhgkdgrdhiievvgssxp
ligdhqdedkqlivelvvnkxaqa
>d1auvb1 3.24.1.5.1 (110-213) Synapsin Ia domain {Bovine (Bos taurus)}
gaaarvllvidephtdwakyfkgkkihgeidikveqaefsdlnlvahanggfsvdxevlr
ngvkvvrslkpdfvlirqhafsxarngdyrslviglqyagipsi
>d1auvb2 4.115.1.3.1 (214-417) Synapsin Ia, C-terminal domain {Bovine (Bos taurus)}
nslhsvynfcdkpwvfaqxvrlhkklgteefplinqtfypnhkexlssttypvvvkxgha
hsgxgkvkvdnqhdfqdiasvvaltktyattepfidakydvriqkigqnykayxrtsvsg
nwktntgsaxleqiaxsdryklwvdtcseifggldicavealhgkdgrdhiievvgssxp
ligdhqdedkqlivelvvnkxaqa
>d1auwa_ 1.117.1.1.5 Argininosuccinate lyase/delta-crystallin {Domestic duck (Anas platyrhynchos), delta-crystallin}
tdpimeklnssiaydqrlsevdiqgsmayakalekagiltktelekilsglekiseewsk
gvfvvkqsdedintanerrlkeligdiagklhtgrsrndqvvtdlklfmknslsiisthl
lqliktlveraaieidvilpgythlqkaqpirwsqfllshavaltrdserlgevkkrinv
lplgsgalagnpldidremlrselefasislnsmdaiserdfvveflsfatllmihlskm
aedliiystsefgfltdsdafstgsslmpqkknpdslelirskagrvfgrlasilmvlkg
lpstynkdlqedkeavfdvvdtltavlqvatgvistlqiskenmekaltpemlatdlaly
lvrkgvpfrqahtasgkavhlaetkgitinklsledlksispqfssdvsqvfnfvnsveq
ytalggtakssvttqieqlrelmkkqk
>d1auwb_ 1.117.1.1.5 Argininosuccinate lyase/delta-crystallin {Domestic duck (Anas platyrhynchos), delta-crystallin}
tdpimeklnssiaydqrlsevdiqgsmayakalekagiltktelekilsglekiseewsk
gvfvvkqsdedintanerrlkeligdiagklhtgrsrndqvvtdlklfmknslsiisthl
lqliktlveraaieidvilpgythlqkaqpirwsqfllshavaltrdserlgevkkrinv
lplgsgalagnpldidremlrselefasislnsmdaiserdfvveflsfatllmihlskm
aedliiystsefgfltdsdafstgsslmpqkknpdslelirskagrvfgrlasilmvlkg
lpstynkdlqedkeavfdvvdtltavlqvatgvistlqiskenmekaltpemlatdlaly
lvrkgvpfrqahtasgkavhlaetkgitinklsledlksispqfssdvsqvfnfvnsveq
ytalggtakssvttqieqlrelmkkqk
>d1auwc_ 1.117.1.1.5 Argininosuccinate lyase/delta-crystallin {Domestic duck (Anas platyrhynchos), delta-crystallin}
tdpimeklnssiaydqrlsevdiqgsmayakalekagiltktelekilsglekiseewsk
gvfvvkqsdedintanerrlkeligdiagklhtgrsrndqvvtdlklfmknslsiisthl
lqliktlveraaieidvilpgythlqkaqpirwsqfllshavaltrdserlgevkkrinv
lplgsgalagnpldidremlrselefasislnsmdaiserdfvveflsfatllmihlskm
aedliiystsefgfltdsdafstgsslmpqkknpdslelirskagrvfgrlasilmvlkg
lpstynkdlqedkeavfdvvdtltavlqvatgvistlqiskenmekaltpemlatdlaly
lvrkgvpfrqahtasgkavhlaetkgitinklsledlksispqfssdvsqvfnfvnsveq
ytalggtakssvttqieqlrelmkkqk
>d1auwd_ 1.117.1.1.5 Argininosuccinate lyase/delta-crystallin {Domestic duck (Anas platyrhynchos), delta-crystallin}
tdpimeklnssiaydqrlsevdiqgsmayakalekagiltktelekilsglekiseewsk
gvfvvkqsdedintanerrlkeligdiagklhtgrsrndqvvtdlklfmknslsiisthl
lqliktlveraaieidvilpgythlqkaqpirwsqfllshavaltrdserlgevkkrinv
lplgsgalagnpldidremlrselefasislnsmdaiserdfvveflsfatllmihlskm
aedliiystsefgfltdsdafstgsslmpqkknpdslelirskagrvfgrlasilmvlkg
lpstynkdlqedkeavfdvvdtltavlqvatgvistlqiskenmekaltpemlatdlaly
lvrkgvpfrqahtasgkavhlaetkgitinklsledlksispqfssdvsqvfnfvnsveq
ytalggtakssvttqieqlrelmkkqk
>d1auxa1 3.24.1.5.1 (112-213) Synapsin Ia domain {Bovine (Bos taurus)}
aarvllvidephtdwakyfkgkkihgeidikveqaefsdlnlvahanggfsvdmevlrng
vkvvrslkpdfvlirqhafsmarngdyrslviglqyagipsi
>d1auxa2 4.115.1.3.1 (214-417) Synapsin Ia, C-terminal domain {Bovine (Bos taurus)}
nslhsvynfcdkpwvfaqmvrlhkklgteefplinqtfypnhkemlssttypvvvkmgha
hsgmgkvkvdnqhdfqdiasvvaltktyattepfidakydvriqkigqnykaymrtsvsg
nwktntgsamleqiamsdryklwvdtcseifggldicavealhgkdgrdhiievvgssmp
ligdhqdedkqlivelvvnkmaqa
>d1auxb1 3.24.1.5.1 (112-213) Synapsin Ia domain {Bovine (Bos taurus)}
aarvllvidephtdwakyfkgkkihgeidikveqaefsdlnlvahanggfsvdmevlrng
vkvvrslkpdfvlirqhafsmarngdyrslviglqyagipsi
>d1auxb2 4.115.1.3.1 (214-417) Synapsin Ia, C-terminal domain {Bovine (Bos taurus)}
nslhsvynfcdkpwvfaqmvrlhkklgteefplinqtfypnhkemlssttypvvvkmgha
hsgmgkvkvdnqhdfqdiasvvaltktyattepfidakydvriqkigqnykaymrtsvsg
nwktntgsamleqiamsdryklwvdtcseifggldicavealhgkdgrdhiievvgssmp
ligdhqdedkqlivelvvnkmaqa
>d1auya_ 2.9.1.2.11 TYMV coat protein {Turnip yellow mosaic virus}
spltikqpfqsevlfagtkdaeasltianidsvstlttfyrhasleslwvtihptlqapt
fpttvgvcwvpaqspvtpaqitktyggqifciggaiqtlsplivkcplemmqprvkdsiq
yldspkllisitaqptappastciitvsgtlsmhsplitdtst
>d1auyb_ 2.9.1.2.11 TYMV coat protein {Turnip yellow mosaic virus}
meidkelapqdrtvtvatvlpavpgpspltikqpfqsevlfagtkdaeasltianidsvs
tlttfyrhasleslwvtihptlqaptfpttvgvcwvpaqspvtpaqitktyggqifcigg
aiqtlsplivkcplemmqprvkdsiqyldspkllisitaqptappastciitvsgtlsmh
splitdtst
>d1auyc_ 2.9.1.2.11 TYMV coat protein {Turnip yellow mosaic virus}
meidkelapqdrtvtvatvlpavpgpspltikqpfqsevlfagtkdaeasltianidsvs
tlttfyrhasleslwvtihptlqaptfpttvgvcwvpaqspvtpaqitktyggqifcigg
aiqtlsplivkcplemmqprvkdsiqyldspkllisitaqptappastciitvsgtlsmh
splitdtst
>d1auz__ 3.10.2.1.1 SpoIIaa {Bacillus subtilis}
slgidmnvkesvlcirltgeldhhtaetlkqkvtqslekddirhivlnledlsfmdssgl
gvilgrykqikqiggemvvcaispavkrlfdmsglfkiirfeqseqqalltlgvas
>d1av3__ 7.3.6.1.6 Conotoxin {Conus purpurascens, kappa-pVIIa}
crixnqkcfqhlddccsrkcnrfnkcv
>d1av4_1 2.27.2.1.3 (212-628) Copper amine oxidase, domain 3 (catalytic) {Arthrobacter globiformis}
plrttqkpisitqpegpsftvtggnhiewekwsldvgfdvregvvlhniafrdgdrlrpi
inrasiaemvvpygdpspirswqnyfdtgeylvgqyanslelgcdclgditylspvisda
fgnpreirngicmheedwgilakhsdlwsginytrrnrrmvisffttignxdygfywyly
ldgtiefeakatgvvftsafpeggsdnisqlapglgapfhqhifsarldmaidgftnrve
eedvvrqtmgpgnergnafsrkrtvltreseavreadartgrtwiisnpesknrlnepvg
yklhahnqptlladpgssiarraafatkdlwvtryadderyptgdfvnqhsggaglpsyi
aqdrdidgqdivvwhtfglthfprvedwpimpvdtvgfklrpegffdrspvldvpan
>d1av4_2 4.15.2.1.3 (9-96) Copper amine oxidase, domains 1 and 2 {Arthrobacter globiformis}
aspfrlasageisevqgilrtagllgpekriaylgvldpargagseaedrrfrvfihdvs
garpqevtvsvtngtvisaveldtaatg
>d1av4_3 4.15.2.1.3 (97-211) Copper amine oxidase, domains 1 and 2 {Arthrobacter globiformis}
elpvleeefevveqllatderwlkalaarnldvskvrvaplsagvfeyaeergrrilrgl
afvqdfpedsawahpvdglvayvdvvskevtrvidtgvfpvpaehgnytdpeltg
>d1av5a_ 4.11.1.1.3 Protein kinase C inhibitor-1, PKCI-1 {Human (Homo sapiens)}
ggdtifgkiirkeipakiifeddrclafhdispqapthflvipkkhisqisvaedddesl
lghlmivgkkcaadlglnkgyrmvvnegsdggqsvyhvhlhvlggrqmhwppg
>d1av5b_ 4.11.1.1.3 Protein kinase C inhibitor-1, PKCI-1 {Human (Homo sapiens)}
ggdtifgkiirkeipakiifeddrclafhdispqapthflvipkkhisqisvaedddesl
lghlmivgkkcaadlglnkgyrmvvnegsdggqsvyhvhlhvlggrqmhwppg
>d1av6a_ 3.56.1.4.1 Polymerase regulatory subunit VP39 {Vaccinia virus}
vvsldkpfmyfeeidneldyepesanevakklpyqgqlklllgelfflsklqrhgildga
tvvyigsapgthirylrdhfynlgviikwmlidgrhhdpilnglrdvtlvtrfvdeeylr
sikkqlhpskiilisdvrspstadllsnyalqnvmisilnpvasslkwrcpfpdqwikdf
yiphgnkmlqpfapsysaemrllsiytgenmrltrvtksdavnyekkmyylnkivrnkvv
vnfdypnqeydyfhmyfmlrtvycnktfpttkakvlflqqsifrflnip
>d1av7__ 3.33.1.1.2 Subtilisin Carlsberg {Bacillus licheniformis}
aqtvpygiplikadkvqaqgfkganvkvavldtgiqashpdlnvvggasfvageayntdg
nghgthvagtvaaldnttgvlgvapsvslyavkvlnssgsgsysgivsgiewattngmdv
inmslggasgstamkqavdnayargvvvvaaagnsgnsgstntigypakydsviavgavd
snsnrasfssvgaelevmapgagvystyptntyatlngtxmasphvagaaalilskhpnl
sasqvrnrlsstatylgssfyygkglinveaaaq
>d1av8a_ 1.26.1.2.3 Ribonucleotide reductase R2 {Escherichia coli}
ayttfsqtkndqlkepmffgqpvnvarydqqkydifekliekqlsffwrpeevdvsrdri
dyqalpehekhifisnlkyqtlldsiqgrspnvallplisipeletwvetwafsetihsr
sythiirnivndpsvvfddivtneqiqkraegissyydeliemtsywhllgegthtvngk
tvtvslrelkkklylclmsvnaleairfyvsfacsfafaerelmegnakiirliardeal
hltgtqhmlnllrsgaddpemaeiaeeckqecydlfvqaaqqekdwadylfrdgsmigln
kdilcqyveyitnirmqavgldlpfqtrsnpipwintwlv
>d1av8b_ 1.26.1.2.3 Ribonucleotide reductase R2 {Escherichia coli}
ayttfsqtkndqlkepmffgqpvnvarydqqkydifekliekqlsffwrpeevdvsrdri
dyqalpehekhifisnlkyqtlldsiqgrspnvallplisipeletwvetwafsetihsr
sythiirnivndpsvvfddivtneqiqkraegissyydeliemtsywhllgegthtvngk
tvtvslrelkkklylclmsvnaleairfyvsfacsfafaerelmegnakiirliardeal
hltgtqhmlnllrsgaddpemaeiaeeckqecydlfvqaaqqekdwadylfrdgsmigln
kdilcqyveyitnirmqavgldlpfqtrsnpipwintwlv
>d1avaa1 2.62.1.1.16 (347-403) Plant alpha-amylase {Barley (Hordeum vulgare), seeds, AMY2 isozyme}
hnesklqiieadadlylaeidgkvivklgprydvgnlipggfkvaahgndyavweki
>d1avaa2 3.1.7.1.16 (1-346) Plant alpha-amylase {Barley (Hordeum vulgare), seeds, AMY2 isozyme}
qvlfqgfnweswkhnggwynflmgkvddiaaagithvwlppasqsvaeqgympgrlydld
askygnkaqlksligalhgkgvkaiadivinhrtaehkdgrgiycifeggtpdarldwgp
hmicrddrpyadgtgnpdtgadfgaapdidhlnlrvqkelvewlnwlkadigfdgwrfdf
akgysadvakiyidrsepsfavaeiwtslayggdgkpnlnqdqhrqelvnwvdkvggkgp
attfdfttkgilnvavegelwrlrgtdgkapgmigwwpakavtfvdnhdtgstqhmwpfp
sdrvmqgyayilthpgtpcifydhffdwglkeeidrlvsvrtrhgi
>d1avab1 2.62.1.1.16 (347-403) Plant alpha-amylase {Barley (Hordeum vulgare), seeds, AMY2 isozyme}
hnesklqiieadadlylaeidgkvivklgprydvgnlipggfkvaahgndyavweki
>d1avab2 3.1.7.1.16 (1-346) Plant alpha-amylase {Barley (Hordeum vulgare), seeds, AMY2 isozyme}
qvlfqgfnweswkhnggwynflmgkvddiaaagithvwlppasqsvaeqgympgrlydld
askygnkaqlksligalhgkgvkaiadivinhrtaehkdgrgiycifeggtpdarldwgp
hmicrddrpyadgtgnpdtgadfgaapdidhlnlrvqkelvewlnwlkadigfdgwrfdf
akgysadvakiyidrsepsfavaeiwtslayggdgkpnlnqdqhrqelvnwvdkvggkgp
attfdfttkgilnvavegelwrlrgtdgkapgmigwwpakavtfvdnhdtgstqhmwpfp
sdrvmqgyayilthpgtpcifydhffdwglkeeidrlvsvrtrhgi
>d1avac_ 2.37.4.1.5 Amylase/subtilisin inhibitor {Barley (Hordeum vulgare), seed}
adpppvhdtdghelradanyyvlsanrahgggltmapghgrhcplfvsqdpngqhdgfpv
ritpygvapsdkiirlstdvrisfrayttclqstewhidselaagrrhvitgpvkdpsps
grenafriekysgaevheyklmscgdwcqdlgvfrdlkggawflgatepyhvvvfkkapp
a
>d1avad_ 2.37.4.1.5 Amylase/subtilisin inhibitor {Barley (Hordeum vulgare), seed}
adpppvhdtdghelradanyyvlsanrahgggltmapghgrhcplfvsqdpngqhdgfpv
ritpygvapsdkiirlstdvrisfrayttclqstewhidselaagrrhvitgpvkdpsps
grenafriekysgaevheyklmscgdwcqdlgvfrdlkggawflgatepyhvvvfkkapp
a
>d1avba_ 2.26.1.1.15 Phytohemagglutinin-L, PHA-L, also arcelin {Kidney bean (Phaseolus vulgaris)}
sndasfnvetfnktnlilqgdatvsseghllltnvkgneedsmgrafysapiqindrtid
nlasfstnftfrinakniensayglafalvpvgsrpklkgrylglfnttnydrdahtvav
vfdtvsnrieidvnsirpiatescnfghnngekaevritydspkndlrvsllypsseekc
hvsatvplekevedwvsvgfsatsgskkettethnvlswsfssnfi
>d1avbb_ 2.26.1.1.15 Phytohemagglutinin-L, PHA-L, also arcelin {Kidney bean (Phaseolus vulgaris)}
sndasfnvetfnktnlilqgdatvsseghllltnvkgneedsmgrafysapiqindrtid
nlasfstnftfrinakniensayglafalvpvgsrpklkgrylglfnttnydrdahtvav
vfdtvsnrieidvnsirpiatescnfghnngekaevritydspkndlrvsllypsseekc
hvsatvplekevedwvsvgfsatsgskkettethnvlswsfssnfi
>d1avc__ 1.66.1.1.7 Annexin VI {Bovine (Bos taurus)}
yrgsirdfpdfnpsqdaetlynamkgfgsdkeaiinlitsrsnkqrqeicqnykslygkd
liadlkyeltgkferlivglmrppayadakeikdaisgigtdekclieilasrtneqihq
lvaaykdayerdleaditgdtsghfrkmlvvllqgtreeddvvsedlvqqdvqdlyeage
lkwgtdeaqfiyilgnrskqhlrlvfdeylkttgkpieasirgelsgdfeklmlavvkci
rstaeyfaerlfkamkglgtrdntlirimvsrseldmldireifrtkyekslysmikndt
sgeykktllklcggdddaagqffpeaaqvayqmwelsavarvelkgtvrpagdfnpdada
kalrkamkglgtdedtiidiithrsnaqrqqirqtfkshfgrdlmadlkselsgdlarli
lglmmppahydakqlkkamegagtdekalieilatrtnaeiqainkaykedyhktledal
ssdtsghfkrilislatgnreeggedreraredaqvaaeileiadttsgdkssletrfmm
ilctrsypdlrrvfqefvkmtnydvehtikkemsgdvrdvfvaivqsvknkplffadkly
ksmkgagteektltrimvsrseidllnirrefiekydkslhqaiegdtsghflkallaic
gg
>d1avda_ 2.54.1.1.2 Avidin {Chicken (Gallus gallus)}
kcsltgkwtndlgsnmtigavnsrgeftgtyttavtatsneikesplhgtentinkrtqp
tfgftvnwkfsesttvftgqcfidrngkevlktmwllrssvndigddwkatrvginiftr
lrt
>d1avdb_ 2.54.1.1.2 Avidin {Chicken (Gallus gallus)}
rkcsltgkwtndlgsnmtigavnsrgeftgtyttavtatsneikesplhgtentinkrtq
ptfgftvnwkfsesttvftgqcfidrngkevlktmwllrssvndigddwkatrvginift
rlrt
>d1avea_ 2.54.1.1.2 Avidin {Chicken (Gallus gallus)}
kcsltgkwtndlgsnmtigavnsrgeftgtyttavtatsneikesplhgtentinkrtqp
tfgftvnwkfsesttvftgqcfidrngkevlktmwllrssvndigddwkatrvginiftr
lrt
>d1aveb_ 2.54.1.1.2 Avidin {Chicken (Gallus gallus)}
kcsltgkwtndlgsnmtigavnsrgeftgtyttavtatsneikesplhgtentinkrtqp
tfgftvnwkfsesttvftgqcfidrngkevlktmwllrssvndigddwkatrvginiftr
lrt
>e1avf.1a 2.44.1.2.11 Pepsin(ogen) {Human (Homo sapiens), progastricsin (pepsinogen C)}
vtyepmaymdaayfgeisigtppqnflvlfdtgssnlwvpsvycqsqactshsrfnpses
stystngqtfslqygsgsltgffgydtltvqsiqvpnqefglsenepgtnfvyaqfdgim
glaypalsvdeattamqgmvqegaltspvfsvylsnqqgssggavvfggvdsslytgqiy
wapvtqelywqigieefliggqasgwcsegcqaivdtgtslltvpqqymsallqatgaqe
deygqflvncnsiqnlpsltfiingvefplppssyilsnngyctvgveptylssqngqpl
wilgdvflrsyysvydlgnnrvgfataa
>e1avf.1p 2.44.1.2.11 Pepsin(ogen) {Human (Homo sapiens), progastricsin (pepsinogen C)}
avvkvplkkfksiretmkekg
>e1avf.2j 2.44.1.2.11 Pepsin(ogen) {Human (Homo sapiens), progastricsin (pepsinogen C)}
vtyepmaymdaayfgeisigtppqnflvlfdtgssnlwvpsvycqsqactshsrfnpses
stystngqtfslqygsgsltgffgydtltvqsiqvpnqefglsenepgtnfvyaqfdgim
glaypalsvdeattamqgmvqegaltspvfsvylsnqqgssggavvfggvdsslytgqiy
wapvtqelywqigieefliggqasgwcsegcqaivdtgtslltvpqqymsallqatgaqe
deygqflvncnsiqnlpsltfiingvefplppssyilsnngyctvgveptylssqngqpl
wilgdvflrsyysvydlgnnrvgfataa
>e1avf.2q 2.44.1.2.11 Pepsin(ogen) {Human (Homo sapiens), progastricsin (pepsinogen C)}
avvkvplkkfksiretmkekgl
>e1avg.1h 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
ivegqdaevglspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftvddll
vrigkhsrtryerkvekismldkiyihprynwkenldrdiallklkrpielsdyihpvcl
pdkqtaakllhagfkgrvtgwgnrretwttsvaevqpsvlqvvnlplverpvckastrir
itdnmfcagykpgegkrgdacegdsggpfvmkspynnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidrlgs
>e1avg.1l 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
ffnektfgageadcglrplfekkqvqdqtekelfesyiegr
>d1avgi_ 2.53.1.3.1 Thrombin inhibitor {Triatomine bug (Triatoma pallidipennis)}
aegddcsiekamgdfkpeeffngtwylahgpgvtspavcqkfttsgskgftqiveigynk
fesnvkfqcnqvdnkngeqysfkckssdntefeadftfisvsydnfalvcrsitftsqpk
edrylvfertksdtdpdakeic
>d1avha_ 1.66.1.1.5 Annexin V {Human (Homo sapiens)}
qvlrgtvtdfpgfderadaetlrkamkglgtdeesiltlltsrsnaqrqeisaafktlfg
rdllddlkseltgkfeklivalmkpsrlydayelkhalkgagtnekvlteiiasrtpeel
raikqvyeeeygssleddvvgdtsgyyqrmlvvllqanrdpdagideaqveqdaqalfqa
gelkwgtdeekfitifgtrsvshlrkvfdkymtisgfqieetidretsgnleqlllavvk
sirsipaylaetlyyamkgagtddhtlirvmvsrseidlfnirkefrknfatslysmikg
dtsgdykkallllcgedd
>d1avhb_ 1.66.1.1.5 Annexin V {Human (Homo sapiens)}
qvlrgtvtdfpgfderadaetlrkamkglgtdeesiltlltsrsnaqrqeisaafktlfg
rdllddlkseltgkfeklivalmkpsrlydayelkhalkgagtnekvlteiiasrtpeel
raikqvyeeeygssleddvvgdtsgyyqrmlvvllqanrdpdagideaqveqdaqalfqa
gelkwgtdeekfitifgtrsvshlrkvfdkymtisgfqieetidretsgnleqlllavvk
sirsipaylaetlyyamkgagtddhtlirvmvsrseidlfnirkefrknfatslysmikg
dtsgdykkallllcgedd
>d1avk_1 2.27.2.1.3 (212-628) Copper amine oxidase, domain 3 (catalytic) {Arthrobacter globiformis}
plrttqkpisitqpegpsftvtggnhiewekwsldvgfdvregvvlhniafrdgdrlrpi
inrasiaemvvpygdpspirswqnyfdtgeylvgqyanslelgcdclgditylspvisda
fgnpreirngicmheedwgilakhsdlwsginytrrnrrmvisffttignydygfywyly
ldgtiefeakatgvvftsafpeggsdnisqlapglgapfhqhifsarldmaidgftnrve
eedvvrqtmgpgnergnafsrkrtvltreseavreadartgrtwiisnpesknrlnepvg
yklhahnqptlladpgssiarraafatkdlwvtryadderyptgdfvnqhsggaglpsyi
aqdrdidgqdivvwhtfglthfprvedwpimpvdtvgfklrpegffdrspvldvpan
>d1avk_2 4.15.2.1.3 (9-96) Copper amine oxidase, domains 1 and 2 {Arthrobacter globiformis}
aspfrlasageisevqgilrtagllgpekriaylgvldpargagseaedrrfrvfihdvs
garpqevtvsvtngtvisaveldtaatg
>d1avk_3 4.15.2.1.3 (97-211) Copper amine oxidase, domains 1 and 2 {Arthrobacter globiformis}
elpvleeefevveqllatderwlkalaarnldvskvrvaplsagvfeyaeergrrilrgl
afvqdfpedsawahpvdglvayvdvvskevtrvidtgvfpvpaehgnytdpeltg
>d1avl_1 2.27.2.1.3 (212-628) Copper amine oxidase, domain 3 (catalytic) {Arthrobacter globiformis}
plrttqkpisitqpegpsftvtggnhiewekwsldvgfdvregvvlhniafrdgdrlrpi
inrasiaemvvpygdpspirswqnyfdtgeylvgqyanslelgcdclgditylspvisda
fgnpreirngicmheedwgilakhsdlwsginytrrnrrmvisffttignxdygfywyly
ldgtiefeakatgvvftsafpeggsdnisqlapglgapfhqhifsarldmaidgftnrve
eedvvrqtmgpgnergnafsrkrtvltreseavreadartgrtwiisnpesknrlnepvg
yklhahnqptlladpgssiarraafatkdlwvtryadderyptgdfvnqhsggaglpsyi
aqdrdidgqdivvwhtfglthfprvedwpimpvdtvgfklrpegffdrspvldvpan
>d1avl_2 4.15.2.1.3 (9-96) Copper amine oxidase, domains 1 and 2 {Arthrobacter globiformis}
aspfrlasageisevqgilrtagllgpekriaylgvldpargagseaedrrfrvfihdvs
garpqevtvsvtngtvisaveldtaatg
>d1avl_3 4.15.2.1.3 (97-211) Copper amine oxidase, domains 1 and 2 {Arthrobacter globiformis}
elpvleeefevveqllatderwlkalaarnldvskvrvaplsagvfeyaeergrrilrgl
afvqdfpedsawahpvdglvayvdvvskevtrvidtgvfpvpaehgnytdpeltg
>d1avma1 1.2.7.1.9 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1avma2 4.37.1.1.9 (87-201) Cambialistic superoxide dismutase {Propionibacterium freudenreichii, shermani}
saperptdelgaaideffgsfdnmkaqftaaatgiqgsgwaslvwdplgkrintlqfydh
qnnlpagsipllqldmwehafylqyknvkgdyvkswwnvvnwddvalrfsearva
>d1avmb1 1.2.7.1.9 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1avmb2 4.37.1.1.9 (87-201) Cambialistic superoxide dismutase {Propionibacterium freudenreichii, shermani}
saperptdelgaaideffgsfdnmkaqftaaatgiqgsgwaslvwdplgkrintlqfydh
qnnlpagsipllqldmwehafylqyknvkgdyvkswwnvvnwddvalrfsearva
>d1avn__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasfk
>e1avo.1a 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
lrvqpeaqakvdvfredlctktenllgsyfpkkiseldaflkepalneanlsnlkapldi
>e1avo.1b 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
avncnekivvllqrlkpeikdvieqlnlvttwlqlqipriedgnnfgvavqekvfelmts
lhtklegfhtqiskyfsergdavtkaakqphvgdyrqlvheldeaeyrdirlmvmeirna
yavlydiilknfeklkkprg
>e1avo.2c 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
lrvqpeaqakvdvfredlctktenllgsyfpkkiseldaflkepalneanlsnlkapldi
>e1avo.2d 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
avncnekivvllqrlkpeikdvieqlnlvttwlqlqipriedgnnfgvavqekvfelmts
lhtklegfhtqiskyfsergdavtkaakqphvgdyrqlvheldeaeyrdirlmvmeirna
yavlydiilknfeklkkprg
>e1avo.3e 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
lrvqpeaqakvdvfredlctktenllgsyfpkkiseldaflkepalneanlsnlkapldi
>e1avo.3f 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
avncnekivvllqrlkpeikdvieqlnlvttwlqlqipriedgnnfgvavqekvfelmts
lhtklegfhtqiskyfsergdavtkaakqphvgdyrqlvheldeaeyrdirlmvmeirna
yavlydiilknfeklkkprg
>e1avo.4g 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
lrvqpeaqakvdvfredlctktenllgsyfpkkiseldaflkepalneanlsnlkapldi
>e1avo.4h 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
avncnekivvllqrlkpeikdvieqlnlvttwlqlqipriedgnnfgvavqekvfelmts
lhtklegfhtqiskyfsergdavtkaakqphvgdyrqlvheldeaeyrdirlmvmeirna
yavlydiilknfeklkkprg
>e1avo.5i 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
lrvqpeaqakvdvfredlctktenllgsyfpkkiseldaflkepalneanlsnlkapldi
>e1avo.5j 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
avncnekivvllqrlkpeikdvieqlnlvttwlqlqipriedgnnfgvavqekvfelmts
lhtklegfhtqiskyfsergdavtkaakqphvgdyrqlvheldeaeyrdirlmvmeirna
yavlydiilknfeklkkprg
>e1avo.6k 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
lrvqpeaqakvdvfredlctktenllgsyfpkkiseldaflkepalneanlsnlkapldi
>e1avo.6l 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
avncnekivvllqrlkpeikdvieqlnlvttwlqlqipriedgnnfgvavqekvfelmts
lhtklegfhtqiskyfsergdavtkaakqphvgdyrqlvheldeaeyrdirlmvmeirna
yavlydiilknfeklkkprg
>e1avo.7m 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
lrvqpeaqakvdvfredlctktenllgsyfpkkiseldaflkepalneanlsnlkapldi
>e1avo.7n 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
avncnekivvllqrlkpeikdvieqlnlvttwlqlqipriedgnnfgvavqekvfelmts
lhtklegfhtqiskyfsergdavtkaakqphvgdyrqlvheldeaeyrdirlmvmeirna
yavlydiilknfeklkkprg
>d1avpa_ 4.3.1.4.1 Human adenovirus 2 proteinase {Mastadenovirus h2}
mgsseqelkaivkdlgcgpyflgtydkrfpgfvsphklacaivntagretggvhwmafaw
nprsktcylfepfgfsdqrlkqvyqfeyesllrrsaiasspdrcitlekstqsvqgpnsa
acglfccmflhafanwpqtpmdhnptmnlitgvpnsmlnspqvqptlrrnqeqlysfler
hspyfrshsaqirsatsfchlknm
>d1avqa_ 3.43.1.7.1 lambda exonuclease {Bacteriophage lambda}
shmtpdiilqrtgidvraveqgddawhklrlgvitasevhnviakprsgkkwpdmkmsyf
htllaevctgvapevnakalawgkqyendartlfeftsgvnvtespiiyrdesmrtacsp
dglcsdgnglelkcpftsrdfmkfrlggfeaiksaymaqvqysmwvtrknawyfanydpr
mkreglhyvvierdekymasfdeivpefiekmdealaeigfvfgeqwr
>d1avqb_ 3.43.1.7.1 lambda exonuclease {Bacteriophage lambda}
shmtpdiilqrtgidvraveqgddawhklrlgvitasevhnviakprsgkkwpdmkmsyf
htllaevctgvapevnakalawgkqyendartlfeftsgvnvtespiiyrdesmrtacsp
dglcsdgnglelkcpftsrdfmkfrlggfeaiksaymaqvqysmwvtrknawyfanydpr
mkreglhyvvierdekymasfdeivpefiekmdealaeigfvfgeqwr
>d1avqc_ 3.43.1.7.1 lambda exonuclease {Bacteriophage lambda}
tpdiilqrtgidvraveqgddawhklrlgvitasevhnviakprsgkkwpdmkmsyfhtl
laevctgvapevnakalawgkqyendartlfeftsgvnvtespiiyrdesmrtacspdgl
csdgnglelkcpftsrdfmkfrlggfeaiksaymaqvqysmwvtrknawyfanydprmkr
eglhyvvierdekymasfdeivpefiekmdealaeigfvfgeqwr
>d1avr__ 1.66.1.1.5 Annexin V {Human (Homo sapiens)}
qvlrgtvtdfpgfderadaetlrkamkglgtdeesiltlltsrsnaqrqeisaafktlfg
rdllddlkseltgkfeklivalmkpsrlydayelkhalkgagtnekvlteiiasrtpeel
raikqvyeeeygssleddvvgdtsgyyqrmlvvllqanrdpdagideaqveqdaqalfqa
gelkwgtdeekfitifgtrsvshlrkvfdkymtisgfqieetidretsgnleqlllavvk
sirsipaylaetlyyamkgagtddhtlirvmvsrseidlfnirkefrknfatslysmikg
dtsgdykkallllcged
>d1avsa_ 1.42.1.5.1 Troponin C {Chicken (Gallus gallus)}
qaearaflseemiaefkaafdmfdadgggdistkelgtvmrmlgqnptkeeldaiieevd
edgsgtidfeeflvmmvrqmk
>d1avsb_ 1.42.1.5.1 Troponin C {Chicken (Gallus gallus)}
qqaearaflseemiaefkaafdmfdadgggdistkelgtvmrmlgqnptkeeldaiieev
dedgsgtidfeeflvmmvrqmk
>d1avt__ 3.33.1.1.2 Subtilisin Carlsberg {Bacillus licheniformis}
aqtvpygiplikadkvqaqgfkganvkvavldtgiqashpdlnvvggasfvageayntdg
nghgthvagtvaaldnttgvlgvapsvslyavkvlnssgsgsysgivsgiewattngmdv
inmslggasgstamkqavdnayargvvvvaaagnsgnsgstntigypakydsviavgavd
snsnrasfssvgaelevmapgagvystyptntyatlngtxmasphvagaaalilskhpnl
sasqvrnrlsstatylgssfyygkglinveaaaq
>d1avu__ 2.37.4.1.4 Soybean trypsin inhibitor {Soybean (Glycine max)}
dfvldnegnplenggtyyilsditafggiraaptgnercpltvvqsrneldkgigtiiss
pyrirfiaeghplslkfdsfavimlcvgiptewsvvedlpegpavkigenkdamdgwfrl
ervsddefnnyklvfcpqqaeddkcgdigisidhddgtrrlvvsknkplvvqfqkld
>d1avv__ 4.80.1.1.1 Regulatory factor Nef {Human immunodeficiency virus, type 1, HIV-1}
vplrpmtykaavdlshflkekggleglihsqrrqdildlwiyhtqgyfpdwqnytpgpgv
rypltfgwcyklvpvepdkveeankgentsllhpvslhgmddperevlewrfdsrlafhh
varelhpeyf
>d1avwa_ 2.41.1.2.2 Trypsin(ogen) {Porcine (Sus scrofa)}
ivggytcaansipyqvslnsgshfcggslinsqwvvsaahcyksriqvrlgehnidvleg
neqfinaakiithpnfngntldndimliklsspatlnsrvatvslprscaaagteclisg
wgntkssgssypsllqclkapvlsdssckssypgqitgnmicvgfleggkdscqgdsggp
vvcngqlqgivswgygcaqknkpgvytkvcnyvnwiqqtiaan
>d1avwb_ 2.37.4.1.4 Soybean trypsin inhibitor {Soybean (Glycine max)}
dfvldnegnplenggtyyilsditafggiraaptgnercpltvvqsrneldkgigtiiss
pyrirfiaeghplslkfdsfavimlcvgiptewsvvedlpegpavkigenkdamdgwfrl
ervsefnnyklvfcpqdkcgdigisidhddgtrrlvvsknkplvvqfqkld
>d1avxa_ 2.41.1.2.2 Trypsin(ogen) {Porcine (Sus scrofa)}
ivggytcaansipyqvslnsgshfcggslinsqwvvsaahcyksriqvrlgehnidvleg
neqfinaakiithpnfngntldndimliklsspatlnsrvatvslprscaaagteclisg
wgntkssgssypsllqclkapvlsdssckssypgqitgnmicvgfleggkdscqgdsggp
vvcngqlqgivswgygcaqknkpgvytkvcnyvnwiqqtiaan
>d1avxb_ 2.37.4.1.4 Soybean trypsin inhibitor {Soybean (Glycine max)}
dfvldnegnplenggtyyilsditafggiraaptgnercpltvvqsrneldkgigtiiss
pyrirfiaeghplslkfdsfavimlcvgiptewsvvedlpegpavkigenkdamdgwfrl
ervsddefnnyklvfcpqkcgdigisidhddgtrrlvvsknkplvvqfqkld
>d1avza_ 4.80.1.1.1 Regulatory factor Nef {Human immunodeficiency virus, type 1, HIV-1}
vplrpmtykaavdlshflkekggleglihsqrrqdildlwiyhtqgyfpdwqnytpgpgv
rypltfgwcyklvpvepdkveeankgentsllhpvslhgmddperevlewrfdsrlafhh
varelhpeyf
>d1avzb_ 4.80.1.1.1 Regulatory factor Nef {Human immunodeficiency virus, type 1, HIV-1}
tpqvplrpmtykaavdlshflkekggleglihsqrrqdildlwiyhtqgyfpdwqnytpg
pgvrypltfgwcyklvpvepdkveeankgentsllhpvslhgmddperevlewrfdsrla
fhhvarelhpeyf
>d1avzc_ 2.30.2.1.2 Fyn proto-oncogene tyrosine kinase, SH3 domain {Human (Homo sapiens)}
tlfvalydyearteddlsfhkgekfqilnssegdwwearslttgetgyipsnyvapv
>d1aw0__ 4.47.16.1.2 Menkes copper-transporting ATPase {Human (Homo sapiens)}
ltqetvinidgmtcnscvqsiegviskkpgvksirvslansngtveydplltspetlrga
iedmgfdatlsd
>d1aw1a_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeaka
>d1aw1b_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeak
>d1aw1d_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeaka
>d1aw1e_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeak
>d1aw1g_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeaka
>d1aw1h_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeak
>d1aw1j_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeaka
>d1aw1k_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeak
>d1aw2a_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeaka
>d1aw2b_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeak
>d1aw2d_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeaka
>d1aw2e_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeak
>d1aw2g_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeaka
>d1aw2h_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeak
>d1aw2j_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeaka
>d1aw2k_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeak
>d1aw3__ 4.94.1.1.2 Cytochrome b5 {Rat (Rattus norvegicus)}
dkdvkyytleeiqkhkdskstwvilhhkvydltkfleehpggeevlreqaggdatenfed
vghstdarelsktyiigelhpddrskiakpsetl
>d1aw5__ 3.1.9.3.1 5-aminolevulinate dehydratase (porphobilinogen synthase) {Baker's yeast (Saccharomyces cerevisiae)}
htaefletepteissvlaggynhpllrqwqserqltknxlifplfisdnpddfteidsap
ninrigvnrlkdylkplvakglrsvilfgvplipgtkdpvgtaaddpagpviqgirfire
kfpelyiicdvclceytshghcgvlyddgtinrersvsrlaavavnyakagahcvapsdx
idgrirdikrglinanlahktfvlsyaakfsgnlygpacyqlppagrglarralerdxse
gadgiivkpstfyldivrdaseickdlpicayhvsgeyaxlhaaaekgvvdlktiafesh
qgflragarliitylapefldwlde
>d1aw6__ 7.32.1.1.1 Gal4 {Baker's yeast (Saccharomyces cerevisiae)}
mkllssieqacdicrlkklkcskekpkcakclknnwecryspk
>d1aw7a1 2.35.2.2.3 (1-93) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d1aw7a2 4.13.7.1.3 (94-194) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
lptpielplkvkvhgkdsplkywpkfdkkqlaistldfeirhaltqihglyrssdktggy
wkitmndgstyqsdlskkfeyntekppinideiktieaein
>d1aw7b1 2.35.2.2.3 (201-293) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d1aw7b2 4.13.7.1.3 (294-394) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
lptpielplkvkvhgkdsplkywpkfdkkqlaistldfeirhaltqihglyrssdktggy
wkitmndgstyqsdlskkfeyntekppinideiktieaein
>d1aw7c1 2.35.2.2.3 (401-493) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d1aw7c2 4.13.7.1.3 (494-594) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
lptpielplkvkvhgkdsplkywpkfdkkqlaistldfeirhaltqihglyrssdktggy
wkitmndgstyqsdlskkfeyntekppinideiktieaein
>d1aw7d1 2.35.2.2.3 (601-693) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d1aw7d2 4.13.7.1.3 (694-794) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
lptpielplkvkvhgkdsplkywpkfdkkqlaistldfeirhaltqihglyrssdktggy
wkitmndgstyqsdlskkfeyntekppinideiktieaein
>e1aw8.1a 2.46.2.1.1 Pyruvoyl dependent aspartate decarboxylase, ADC {Escherichia coli}
mirtmlqgklhrvkvthadlhyeg
>e1aw8.1b 2.46.2.1.1 Pyruvoyl dependent aspartate decarboxylase, ADC {Escherichia coli}
caidqdfldaagileneaidiwnvtngkrfstyaiaaergsriisvngaaahcasvgdiv
iiasfvtmpdeeartwrpnvayfegdnemk
>e1aw8.2d 2.46.2.1.1 Pyruvoyl dependent aspartate decarboxylase, ADC {Escherichia coli}
mirtmlqgklhrvkvthadlhyeg
>e1aw8.2e 2.46.2.1.1 Pyruvoyl dependent aspartate decarboxylase, ADC {Escherichia coli}
caidqdfldaagileneaidiwnvtngkrfstyaiaaergsriisvngaaahcasvgdiv
iiasfvtmpdeeartwrpnvayfegdnemk
>d1aw9_1 1.48.1.1.18 (83-217) Glutathione S-transferase {Maize (Zea mays), type III}
gtdllpatasaaklevwleveshhfypnasplvfqllvrpllggapdaavvdkhaeqlak
vldvyeahlarnkylagdeftladanhasyllylsktpkaglvaarphvkawweaivarp
afqktvaaiplpppp
>d1aw9_2 3.38.1.5.18 (2-82) Glutathione S-transferase {Maize (Zea mays), type III}
aplklygmplspnvvrvatvlnekgldfeivpvdlttgahkqpdflalnpfgqipalvdg
devlfesrainryiaskyase
>d1awba_ 5.7.1.2.1 Inositol monophosphatase {Human (Homo sapiens)}
wqecmdyavtlarqagevvceaiknemnvmlksspvdlvtatdqkvekmlissikekyps
hsfigeesvaageksiltdnptwiidpidgttnfvhrfpfvavsigfavnkkiefgvvys
cvegkmytarkgkgafcngqklqvsqqeditksllvtelgssrtpetvrmvlsnmeklfc
ipvhgirsvgtaavnmclvatggadayyemgihcwdvagagiivteaggvlmdvtggpfd
lmsrrviaannrilaeriakeiqviplqrdde
>d1awbb_ 5.7.1.2.1 Inositol monophosphatase {Human (Homo sapiens)}
wqecmdyavtlarqagevvceaiknemnvmlksspvdlvtatdqkvekmlissikekyps
hsfigeesvaageksiltdnptwiidpidgttnfvhrfpfvavsigfavnkkiefgvvys
cvegkmytarkgkgafcngqklqvsqqeditksllvtelgssrtpetvrmvlsnmeklfc
ipvhgirsvgtaavnmclvatggadayyemgihcwdvagagiivteaggvlmdvtggpfd
lmsrrviaannrilaeriakeiqviplqrdde
>d1awca_ 1.4.3.16.5 GA binding protein (GABP) alpha {Mouse (Mus musculus)}
iqlwqfllelltdkdardciswvgdegefklnqpelvaqkwgqrknkptmnyeklsralr
yyydgdmickvqgkrfvykfvcdlktligysaaelnrlvieceqkklarm
>d1awcb_ 1.110.2.1.2 GA bindinig protein (GABP) beta 1 {Mouse (Mus musculus)}
dlgkklleaaragqddevrilmangapfttdwlgtsplhlaaqyghfsttevllragvsr
dartkvdrtplhmaaseghanivevllkhgadvnakdmlkmtalhwatehnhqevvelli
kygadvhtqskfcktafdisidngnedlaeilq
>d1awd__ 4.13.6.1.6 2Fe-2S ferredoxin {Chlorella fusca}
ykvtlktpsgeetiecpedtyildaaeeagldlpyscragacsscagkvesgevdqsdqs
flddaqmgkgfvltcvayptsdvtilthqeaaly
>d1awe__ 2.49.1.1.8 Son of sevenless-1 (sos-1) {Human (Homo sapiens)}
mneiqknidgwegkdigqccnefimegtltrvgakherhiflfdglmiccksnhgqprlp
gasnaeyrlkekffmrkvqindkddtneykhafeiilkdensvifsaksaeeknnwmaal
islqyrstle
>e1awf.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1awf.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1awh.1a 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1awh.1b 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>e1awh.2c 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1awh.2d 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>d1awia_ 4.86.1.1.2 Profilin (actin-binding protein) {Human (Homo sapiens)}
gwnayidnlmadgtcqdaaivgykdspsvwaavpgktfvnitpaevgvlvgkdrssfyvn
gltlggqkcsvirdsllqdgefsmdlrtkstggaptfnvtvtktdktlvllmgkegvhgg
linkkcyemashlrrsqy
>d1awib_ 4.86.1.1.2 Profilin (actin-binding protein) {Human (Homo sapiens)}
gwnayidnlmadgtcqdaaivgykdspsvwaavpgktfvnitpaevgvlvgkdrssfyvn
gltlggqkcsvirdsllqdgefsmdlrtkstggaptfnvtvtktdktlvllmgkegvhgg
linkkcyemashlrrsqy
>d1awj__ 2.30.2.1.9 IL-2 inducible T-cell (Itc) kinase {Mouse (Mus musculus)}
kkplpptpednrrsfqepeetlvialydyqtndpqelalrcdeeyylldsseihwwrvqd
knghegyapssylveks
>d1awo__ 2.30.2.1.5 Abl tyrosine kinase, SH3 domain {Human (Homo sapiens)}
slfvalydfvasgdntlsitkgeklrvlgynhngewceaqtkngqgwvpsnyitpvs
>d1awpa_ 4.94.1.1.2 Cytochrome b5 {Rat (Rattus norvegicus)}
dpavtyyrleevakrntaeetwmvihgrvyditrflsehpggeellleqagadatesfed
lghspdaremlkqyyigdvhpndlkp
>d1awpb_ 4.94.1.1.2 Cytochrome b5 {Rat (Rattus norvegicus)}
dpavtyyrleevakrntaeetwmvihgrvyditrflsehpggeellleqagadatesfed
lghspdaremlkqyyigdvhpndlkp
>d1awqa_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awra_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awrb_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awrc_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awrd_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awre_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awrf_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awsa_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfx
cqggdftrhngtggksiygekfedenfilkhtgpgilsxanagpntngsqffictaktew
ldgkhvvfgkvkegxniveaxerfgsrngktskkitiadcgqle
>d1awta_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfx
cqggdftrhngtggksiygekfedenfilkhtgpgilsxanagpntngsqffictaktew
ldgkhvvfgkvkegxniveaxerfgsrngktskkitiadcgqle
>d1awtb_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfx
cqggdftrhngtggksiygekfedenfilkhtgpgilsxanagpntngsqffictaktew
ldgkhvvfgkvkegxniveaxerfgsrngktskkitiadcgqle
>d1awtc_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfx
cqggdftrhngtggksiygekfedenfilkhtgpgilsxanagpntngsqffictaktew
ldgkhvvfgkvkegxniveaxerfgsrngktskkitiadcgqle
>d1awtd_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfx
cqggdftrhngtggksiygekfedenfilkhtgpgilsxanagpntngsqffictaktew
ldgkhvvfgkvkegxniveaxerfgsrngktskkitiadcgqle
>d1awte_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfx
cqggdftrhngtggksiygekfedenfilkhtgpgilsxanagpntngsqffictaktew
ldgkhvvfgkvkegxniveaxerfgsrngktskkitiadcgqle
>d1awtf_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfx
cqggdftrhngtggksiygekfedenfilkhtgpgilsxanagpntngsqffictaktew
ldgkhvvfgkvkegxniveaxerfgsrngktskkitiadcgqle
>d1awua_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awva_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awvb_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awvc_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awvd_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awve_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awvf_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1aww__ 2.30.2.1.13 Bruton's tyrosine kinase {Human (Homo sapiens)}
gsmstselkkvvalydympmnandlqlrkgdeyfileesnlpwwrardkngqegyipsny
vteaeds
>d1awx__ 2.30.2.1.13 Bruton's tyrosine kinase {Human (Homo sapiens)}
gsmstselkkvvalydympmnandlqlrkgdeyfileesnlpwwrardkngqegyipsny
vteaeds
>d1awz__ 4.5.1.1.7 Angiogenin {Human (Homo sapiens)}
qdnsrythfltqhydakpqgrddrycesimrrrgltspckdintfihgnkrsikaicenk
ngnphrenlriskssfqvttcklhggspwppcqyratagfrnvvvacenglpvhldqsif
rrp
>d1ax0__ 2.26.1.1.6 Lectin {Coral tree (Erythrina corallodendron)}
vetisfsfsefepgndnltlqgaalitqsgvlqltkinqngmpawdstgrtlyakpvhiw
dmttgtvasfetrfsfsieqpytrplpadglvffmgptkskpaqgygylgifnnskqdns
yqtlgvefdtfsnpwdppqvphigidvnsirsiktqpfqldngqvanvvikydasskilh
avlvypssgaiytiaeivdvkqvlpewvdvglsgatgaqrdaaethdvyswsfqaslpe
>d1ax1__ 2.26.1.1.6 Lectin {Coral tree (Erythrina corallodendron)}
vetisfsfsefepgndnltlqgaalitqsgvlqltkinqngmpawdstgrtlyakpvhiw
dmttgtvasfetrfsfsieqpytrplpadglvffmgptkskpaqgygylgifnnskqdns
yqtlgvefdtfsnpwdppqvphigidvnsirsiktqpfqldngqvanvvikydasskilh
avlvypssgaiytiaeivdvkqvlpewvdvglsgatgaqrdaaethdvyswsfqaslpe
>d1ax2__ 2.26.1.1.6 Lectin {Coral tree (Erythrina corallodendron)}
vetisfsfsefepgndnltlqgaalitqsgvlqltkinqngmpawdstgrtlyakpvhiw
dmttgtvasfetrfsfsieqpytrplpadglvffmgptkskpaqgygylgifnnskqdns
yqtlgvefdtfsnpwdppqvphigidvnsirsiktqpfqldngqvanvvikydasskilh
avlvypssgaiytiaeivdvkqvlpewvdvglsgatgaqrdaaethdvyswsfqaslpe
>d1ax3__ 2.74.3.1.1 Glucose permease IIa domain, IIa-glc {Bacillus subtilis}
miaeplqneigeevfvspitgeihpitdvpdqvfsgkmmgdgfailpsegivvspvrgki
lnvfptkhaiglqsdggreilihfgidtvslkgegftsfvsegdrvepgqkllevdldav
kpnvpslmtpivftnlaegetvsikasgsvnreqedivkiek
>d1ax4a_ 3.57.1.2.2 Tryptophan indol-lyase (tryptophanase) {Proteus vulgaris}
akrivepfrikmvekirvpsreereaalkeagynpfllpssavyidlltdsgtnamsdhq
waamitgdeayagsrnyydlkdkakelfnydyiipahqgrgaenilfpvllkykqkegka
knpvfisnfhfdttaahvelngckainivtekafdsetyddwkgdfdikklkeniaqhga
dnivaivstvtcnsaggqpvsmsnlkevyeiakqhgifvvmdsarfcenayfikardpky
knatikevifdmykyadaltmsakxdpllnigglvairdneeiftlarqrcvpmegfvty
gglagrdmaamvqgleegteeeylhyrigqvkylgdrlreagipiqyptgghavfvdckk
lvpqipgdqfpaqavinalylesgvraveigsfllgrdpatgeqkhadmefmrltiarrv
ytndhmdyiadaliglkekfatlkglefeyeppvlrhftarlkpi
>d1ax4b_ 3.57.1.2.2 Tryptophan indol-lyase (tryptophanase) {Proteus vulgaris}
akrivepfrikmvekirvpsreereaalkeagynpfllpssavyidlltdsgtnamsdhq
waamitgdeayagsrnyydlkdkakelfnydyiipahqgrgaenilfpvllkykqkegka
knpvfisnfhfdttaahvelngckainivtekafdsetyddwkgdfdikklkeniaqhga
dnivaivstvtcnsaggqpvsmsnlkevyeiakqhgifvvmdsarfcenayfikardpky
knatikevifdmykyadaltmsakxdpllnigglvairdneeiftlarqrcvpmegfvty
gglagrdmaamvqgleegteeeylhyrigqvkylgdrlreagipiqyptgghavfvdckk
lvpqipgdqfpaqavinalylesgvraveigsfllgrdpatgeqkhadmefmrltiarrv
ytndhmdyiadaliglkekfatlkglefeyeppvlrhftarlkpi
>d1ax4c_ 3.57.1.2.2 Tryptophan indol-lyase (tryptophanase) {Proteus vulgaris}
akrivepfrikmvekirvpsreereaalkeagynpfllpssavyidlltdsgtnamsdhq
waamitgdeayagsrnyydlkdkakelfnydyiipahqgrgaenilfpvllkykqkegka
knpvfisnfhfdttaahvelngckainivtekafdsetyddwkgdfdikklkeniaqhga
dnivaivstvtcnsaggqpvsmsnlkevyeiakqhgifvvmdsarfcenayfikardpky
knatikevifdmykyadaltmsakxdpllnigglvairdneeiftlarqrcvpmegfvty
gglagrdmaamvqgleegteeeylhyrigqvkylgdrlreagipiqyptgghavfvdckk
lvpqipgdqfpaqavinalylesgvraveigsfllgrdpatgeqkhadmefmrltiarrv
ytndhmdyiadaliglkekfatlkglefeyeppvlrhftarlkpi
>d1ax4d_ 3.57.1.2.2 Tryptophan indol-lyase (tryptophanase) {Proteus vulgaris}
akrivepfrikmvekirvpsreereaalkeagynpfllpssavyidlltdsgtnamsdhq
waamitgdeayagsrnyydlkdkakelfnydyiipahqgrgaenilfpvllkykqkegka
knpvfisnfhfdttaahvelngckainivtekafdsetyddwkgdfdikklkeniaqhga
dnivaivstvtcnsaggqpvsmsnlkevyeiakqhgifvvmdsarfcenayfikardpky
knatikevifdmykyadaltmsakxdpllnigglvairdneeiftlarqrcvpmegfvty
gglagrdmaamvqgleegteeeylhyrigqvkylgdrlreagipiqyptgghavfvdckk
lvpqipgdqfpaqavinalylesgvraveigsfllgrdpatgeqkhadmefmrltiarrv
ytndhmdyiadaliglkekfatlkglefeyeppvlrhftarlkpi
>d1ax8__ 1.27.1.1.8 Leptin (obesity protein) {Human (Homo sapiens)}
iqkvqddtktliktivtrindishtqsvsskqkvtgldfipglhpiltlskmdqtlavyq
qiltsmpsrnviqisndlenlrdllhvlafskschlpeasgletldslggvleasgyste
vvalsrlqgslqdmlwqldlspgc
>d1ax9__ 3.59.1.1.1 Acetylcholinesterase {Electric ray (Torpedo californica)}
sellvntksgkvmgtrvpvlsshisaflgipfaeppvgnmrfrrpepkkpwsgvwnasty
pnncqqyvdeqfpgfsgsemwnpnremsedclylniwvpsprpksttvmvwiygggfysg
sstldvyngkylayteevvlvslsyrvgafgflalhgsqeapgnvglldqrmalqwvhdn
iqffggdpktvtifgesaggasvgmhilspgsrdlfrrailqsgspncpwasvsvaegrr
ravelgrnlncnlnsdeelihclrekkpqelidvewnvlpfdsifrfsfvpvidgeffpt
slesmlnsgnfkktqillgvnkdegsffllygapgfskdseskisredfmsgvklsvpha
ndlgldavtlqytdwmddnngiknrdglddivgdhnvicplmhfvnkytkfgngtylyff
nhrasnlvwpewmgvihgyeiefvfglplvkelnytaeeealsrrimhywatfaktgnpn
ephsqeskwplfttkeqkfidlntepmkvhqrlrvqmcvfwnqflpkllnat
>d1axaa_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgsddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1axab_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgsddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1axb__ 5.3.1.1.3 beta-Lactamase, class A {Escherichia coli, TEM-1}
hpetlvkvkdaedqlgarvgyieldlnsgkilesfrpeerfpmmstfkvllcgavlsrid
agqeqlgrrihysqndlveyspvtekhltdgmtvrelcsaaitmsdntaanlllttiggp
keltaflhnmgdhvtrldrwepelneaipnderdttmpvamattlrklltgelltlasrq
qlidwmeadkvagpllrsalpagwfiadksgagergsrgiiaalgpdgkpsrivviyttg
sqatmdernrqiaeigaslikhw
>d1axca1 4.105.1.2.3 (1-126) Prolifirating cell nuclear antigen (PCNA) {Human (Homo sapiens)}
mfearlvqgsilkkvlealkdlineacwdisssgvnlqsmdsshvslvqltlrsegfdty
rcdrnlamgvnltsmskilkcagnediitlraednadtlalvfeapnqekvsdyemklmd
ldveql
>d1axca2 4.105.1.2.3 (127-255) Prolifirating cell nuclear antigen (PCNA) {Human (Homo sapiens)}
gipeqeyscvvkmpsgefaricrdlshigdavviscakdgvkfsasgelgngniklsqts
nvdkeeeavtiemnepvqltfalrylnfftkatplsstvtlsmsadvplvveykiadmgh
lkyylapki
>d1axcc1 4.105.1.2.3 (1-126) Prolifirating cell nuclear antigen (PCNA) {Human (Homo sapiens)}
mfearlvqgsilkkvlealkdlineacwdisssgvnlqsmdsshvslvqltlrsegfdty
rcdrnlamgvnltsmskilkcagnediitlraednadtlalvfeapnqekvsdyemklmd
ldveql
>d1axcc2 4.105.1.2.3 (127-255) Prolifirating cell nuclear antigen (PCNA) {Human (Homo sapiens)}
gipeqeyscvvkmpsgefaricrdlshigdavviscakdgvkfsasgelgngniklsqts
nvdkeeeavtiemnepvqltfalrylnfftkatplsstvtlsmsadvplvveykiadmgh
lkyylapki
>d1axce1 4.105.1.2.3 (1-126) Prolifirating cell nuclear antigen (PCNA) {Human (Homo sapiens)}
mfearlvqgsilkkvlealkdlineacwdisssgvnlqsmdsshvslvqltlrsegfdty
rcdrnlamgvnltsmskilkcagnediitlraednadtlalvfeapnqekvsdyemklmd
ldveql
>d1axce2 4.105.1.2.3 (127-255) Prolifirating cell nuclear antigen (PCNA) {Human (Homo sapiens)}
gipeqeyscvvkmpsgefaricrdlshigdavviscakdgvkfsasgelgngniklsqts
nvdkeeeavtiemnepvqltfalrylnfftkatplsstvtlsmsadvplvveykiadmgh
lkyylapki
>d1axda1 1.48.1.1.17 (81-210) Glutathione S-transferase {Maize (Zea mays), type I}
ellregnleeaamvdvwieveanqytaalnpilfqvlispmlggttdqkvvdenleklkk
vlevyearltkckylagdflsladlnhvsvtlclfatpyasvldayphvkawwsglmerp
svqkvaalm
>d1axda2 3.38.1.5.17 (1-80) Glutathione S-transferase {Maize (Zea mays), type I}
apmklygavmswnltrcataleeagsdyeivpinfataehkspehlvrnpfgqvpalqdg
dlylfesraickyaarknkp
>d1axdb1 1.48.1.1.17 (81-210) Glutathione S-transferase {Maize (Zea mays), type I}
ellregnleeaamvdvwieveanqytaalnpilfqvlispmlggttdqkvvdenleklkk
vlevyearltkckylagdflsladlnhvsvtlclfatpyasvldayphvkawwsglmerp
svqkvaalm
>d1axdb2 3.38.1.5.17 (1-80) Glutathione S-transferase {Maize (Zea mays), type I}
apmklygavmswnltrcataleeagsdyeivpinfataehkspehlvrnpfgqvpalqdg
dlylfesraickyaarknkp
>d1axea1 2.31.1.2.2 (1-174,325-374) Alcohol dehydrogenase {Human (Homo sapiens)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplwtpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1axea2 3.2.1.1.2 (175-324) Alcohol dehydrogenase {Human (Homo sapiens), different isozymes}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1axeb1 2.31.1.2.2 (1-174,325-374) Alcohol dehydrogenase {Human (Homo sapiens)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplwtpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1axeb2 3.2.1.1.2 (175-324) Alcohol dehydrogenase {Human (Homo sapiens), different isozymes}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1axfa_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1axfb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahky
>d1axfc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1axfd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahky
>d1axga1 2.31.1.2.2 (1-174,325-374) Alcohol dehydrogenase {Human (Homo sapiens)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1axga2 3.2.1.1.2 (175-324) Alcohol dehydrogenase {Human (Homo sapiens), different isozymes}
gfstgygsavkvakvtqgstcavfglggaglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1axgb1 2.31.1.2.2 (1-174,325-374) Alcohol dehydrogenase {Human (Homo sapiens)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1axgb2 3.2.1.1.2 (175-324) Alcohol dehydrogenase {Human (Homo sapiens), different isozymes}
gfstgygsavkvakvtqgstcavfglggaglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1axgc1 2.31.1.2.2 (1-174,325-374) Alcohol dehydrogenase {Human (Homo sapiens)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1axgc2 3.2.1.1.2 (175-324) Alcohol dehydrogenase {Human (Homo sapiens), different isozymes}
gfstgygsavkvakvtqgstcavfglggaglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1axgd1 2.31.1.2.2 (1-174,325-374) Alcohol dehydrogenase {Human (Homo sapiens)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1axgd2 3.2.1.1.2 (175-324) Alcohol dehydrogenase {Human (Homo sapiens), different isozymes}
gfstgygsavkvakvtqgstcavfglggaglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1axh__ 7.3.6.2.3 Atracotoxin-hVI (versutoxin) {Australian funnel-web spider (Hadronyche versuta)}
sptcipsgqpcpynenccsqsctfkenengntvkrcd
>d1axia_ 1.27.1.1.6 Growth hormone, somatotropin {Human (Homo sapiens)}
tiplsrlfdnamlrahrlhqlafdtyqefeeayipkeqkysflqnpqtslcfsesiptps
nreetqqksnlellrisllliqswlepvqflrsvfanslvygasdsnvydllkdleeriq
tlmgrltdgsprtgqifkqtyskfdtnshnddallknygllycfrrdmtyvatylrivqc
rsvegscgf
>d1axib1 2.1.2.1.8 (32-130) Growth hormone receptor {Human (Homo sapiens)}
epkftkcrsperetfschwtdevhhgtknegpiqlfytrrntqewtqewkecpdyvsage
nscyfnssftsiaipycikltsnggtvdekcfsvdeivq
>d1axib2 2.1.2.1.8 (131-236) Growth hormone receptor {Human (Homo sapiens)}
pdppialnwtllnvsltgihadiqvrweaprnadiqkgwmvleyelqykevnetkwkmmd
pilttsvpvyslkvdkeyevrvrskqrnsgnygefsevlyvtlpqm
>d1axj__ 2.38.1.5.1 FMN-binding protein {Desulfovibrio vulgaris, strain Miyazaki F}
mlpgtffevlknegvvaiatqgedgphlvntwnsylkvldgnrivvpvggmhkteanvar
dervlmtlgsrkvagrngpgtgflirgsaafrtdgpefeaiarfkwaraalvitvvsaeq
tl
>d1axka1 2.26.1.2.3 (1-156,342-393) Bacillus 1-3,1-4-beta-glucanase {Bacillus macerans}
fdcaeyrstniygyglyevsmkpakntgivssfftytgpahgtqwdeidieflgkdttkv
qfnyytngvgghekvislgfdaskgfhtyafdwqpgyikwyvdgvlkhtatanipstpgk
immnlwngtgvddwlgsynganplyaeydwvkytsnXgsvfwepksyfnpstwekadgys
nggvfnctwrannvnftndgklklgltss
>d1axka2 2.26.1.10.2 (157-341) Xylanase II {Bacillus subtilis}
astdywqnwtdgggivnavngsggnysvnwsntgnfvvgkgwttgspfrtinynagvwap
ngngyltlygwtrsplieyyvvdswgtyrptgtykgtvksdggtydiytttrynapsidg
drttftqywsvrqskrptgsnatitfsnhvnawkshgmnlgsnwayqvmategyqssgss
nvtvw
>d1axkb1 2.26.1.2.3 (1-156,342-394) Bacillus 1-3,1-4-beta-glucanase {Bacillus macerans}
fdcaeyrstniygyglyevsmkpakntgivssfftytgpahgtqwdeidieflgkdttkv
qfnyytngvgghekvislgfdaskgfhtyafdwqpgyikwyvdgvlkhtatanipstpgk
immnlwngtgvddwlgsynganplyaeydwvkytsnXgsvfwepksyfnpstwekadgys
nggvfnctwrannvnftndgklklgltssa
>d1axkb2 2.26.1.10.2 (157-341) Xylanase II {Bacillus subtilis}
astdywqnwtdgggivnavngsggnysvnwsntgnfvvgkgwttgspfrtinynagvwap
ngngyltlygwtrsplieyyvvdswgtyrptgtykgtvksdggtydiytttrynapsidg
drttftqywsvrqskrptgsnatitfsnhvnawkshgmnlgsnwayqvmategyqssgss
nvtvw
>d1axma_ 2.37.1.1.3 Acidic FGF {Human (Homo sapiens)}
kkpkllycsngghflrilpdgtvdgtrdrsdqhiqlqlsaesvgevyikstetgqylaxd
tdgllygsqtpneeclflerleenhyntyiskkhaeknwfvglkkngsckrgprthygqk
ailflplpvs
>d1axmb_ 2.37.1.1.3 Acidic FGF {Human (Homo sapiens)}
pkllycsngghflrilpdgtvdgtrdrsdqhiqlqlsaesvgevyikstetgqylaxdtd
gllygsqtpneeclflerleenhyntyiskkhaeknwfvglkkngsckrgprthygqkai
lflplpv
>d1axmc_ 2.37.1.1.3 Acidic FGF {Human (Homo sapiens)}
kpkllycsngghflrilpdgtvdgtrdrsdqhiqlqlsaesvgevyikstetgqylaxdt
dgllygsqtpneeclflerleenhyntyiskkhaeknwfvglkkngsckrgprthygqka
ilflplpv
>d1axmd_ 2.37.1.1.3 Acidic FGF {Human (Homo sapiens)}
pkllycsngghflrilpdgtvdgtrdrsdqhiqlqlsaesvgevyikstetgqylaxdtd
gllygsqtpneeclflerleenhyntyiskkhaeknwfvglkkngsckrgprthygqkai
lflplpv
>d1axme_ 2.37.1.1.3 Acidic FGF {Human (Homo sapiens)}
kpkllycsngghflrilpdgtvdgtrdrsdqhiqlqlsaesvgevyikstetgqylaxdt
dgllygsqtpneeclflerleenhyntyiskkhaeknwfvglkkngsckrgprthygqka
ilflplpvs
>d1axmf_ 2.37.1.1.3 Acidic FGF {Human (Homo sapiens)}
kpkllycsngghflrilpdgtvdgtrdrsdqhiqlqlsaesvgevyikstetgqylaxdt
dgllygsqtpneeclflerleenhyntyiskkhaeknwfvglkkngsckrgprthygqka
ilflplpvs
>d1axn__ 1.66.1.1.2 Annexin III {Human (Homo sapiens)}
sasiwvghrgtvrdypdfspsvdaeaiqkairgigtdekmlisiltersnaqrqlivkey
qaaygkelkddlkgdlsghfehlmvalvtppavfdakqlkksmkgagtnedalieilttr
tsrqmkdisqayytvykkslgddissetsgdfrkalltladgrrdeslkvdehlakqdaq
ilykagenrwgtdedkfteilclrsfpqlkltfdeyrnisqkdivdsikgelsghfedll
laivncvrntpaflaerlhralkgigtdeftlnrimvsrseidlldirtefkkhygysly
saiksdtsgdyeitllkicggdd
>d1axq__ 4.47.1.2.1 Ferredoxin {Azotobacter vinelandii}
afvvtdncikckytdcvevcpvdcfyegpnflvihpdecidcalcepecpaqaifsedev
pedmqefiqlnaelaevwpnitekkdplpdaedwdgvkgklqhler
>d1axr__ 3.77.1.2.1 Glycogen phosphorylase {Rabbit (Oryctolagus cuniculus)}
svrglagvenvtelkknfnrhlhftlvkdrnvatprdyyfalahtvrdhlvgrwirtqqh
yyekdpkriyylslefymgrtlqntmvnlalenacdeatyqlgldmeeleeieedaglgn
gglgrlaacfldsmatlglaaygygiryefgifnqkicggwqmeeaddwlrygnpwekar
peftlpvhfygrvehtsqgakwvdtqvvlampydtpvpgyrnnvvntmrlwsakapndfn
lkdfnvggyiqavldrnlaenisrvlypndnffegkelrlkqeyfvvaatlqdiirrfks
skfgcrdpvrtnfdafpdkvaiqlndthpslaipelmrvlvdlerldwdkawevtvktca
ytnhtvlpealerwpvhlletllprhlqiiyeinqrflnrvaaafpgdvdrlrrmslvee
gavkrinmahlciagshavngvarihseilkktifkdfyelephkfqnktngitprrwlv
lcnpglaeiiaerigeeyisdldqlrkllsyvddeafirdvakvkqenklkfaaylerey
kvhinpnslfdvqvkriheykrqllnclhvitlynrikkepnkfvvprtvmiggkaapgy
hmakmiiklitaigdvvnhdpvvgdrlrviflenyrvslaekvipaadlseqistagtea
sgtgnmkfmlngaltigtmdganvemaeeageenffifgmrvedvdrldqrgynaqeyyd
ripelrqiieqlssgffspkqpdlfkdivnmlmhhdrfkvfadyeeyvkcqervsalykn
prewtrmvirniatsgkfssdrtiaqyareiwgvepsrqrlpapdekip
>d1axsa1 2.1.1.1.95 (1-107) Immunoglobulin (variable domains of L and H chains) {Oxy-cope catalytic Fab, chimeric (mouse V domains/human C1 domains)}
elvltqspssmyaslgervtitckasqdinsylnwfqqkpgkspktliyrtnrlvdgvps
rfsgsgsgqdysltissleyedmgiyyclqydefpytfgsgtkleik
>d1axsa2 2.1.1.2.97 (108-211) Immunoglobulin (constant domains of L and H chains) {Oxy-cope catalytic Fab, chimeric (mouse V domains/human C1 domains)}
rtvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqd
skdstyslsstltlskadyekhkvyacevthqglsspvtksfnr
>d1axsb1 2.1.1.1.95 (1-113) Immunoglobulin (variable domains of L and H chains) {Oxy-cope catalytic Fab, chimeric (mouse V domains/human C1 domains)}
qvqllesgaelmkpgasvkisckatgytfssfwiewvkqrpghglewigeilpgsggthy
nekfkgkatftadkssntaymqlssltsedsavyycarghsyyfydgdywgqgtsvtvss
>d1axsb2 2.1.1.2.97 (114-214) Immunoglobulin (constant domains of L and H chains) {Oxy-cope catalytic Fab, chimeric (mouse V domains/human C1 domains)}
astkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkvepk
>d1axsh1 2.1.1.1.95 (1-113) Immunoglobulin (variable domains of L and H chains) {Oxy-cope catalytic Fab, chimeric (mouse V domains/human C1 domains)}
qvqllesgaelmkpgasvkisckatgytfssfwiewvkqrpghglewigeilpgsggthy
nekfkgkatftadkssntaymqlssltsedsavyycarghsyyfydgdywgqgtsvtvss
>d1axsh2 2.1.1.2.97 (114-214) Immunoglobulin (constant domains of L and H chains) {Oxy-cope catalytic Fab, chimeric (mouse V domains/human C1 domains)}
astkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkvepk
>d1axsl1 2.1.1.1.95 (1-107) Immunoglobulin (variable domains of L and H chains) {Oxy-cope catalytic Fab, chimeric (mouse V domains/human C1 domains)}
elvltqspssmyaslgervtitckasqdinsylnwfqqkpgkspktliyrtnrlvdgvps
rfsgsgsgqdysltissleyedmgiyyclqydefpytfgsgtkleik
>d1axsl2 2.1.1.2.97 (108-211) Immunoglobulin (constant domains of L and H chains) {Oxy-cope catalytic Fab, chimeric (mouse V domains/human C1 domains)}
rtvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqd
skdstyslsstltlskadyekhkvyacevthqglsspvtksfnr
>d1axth1 2.1.1.1.119 (1-113) Immunoglobulin (variable domains of L and H chains) {Catalytic Fab 33F12 (mouse), kappa L chain}
evkleesggglvqpggsmklscvvsgltfsrfwmswvrqspekglewvaeirlksdnyat
hyaesvkgkftisrddsksrlylqmnslrtedtgiyyckiyfysfsywgqgtlvtvsa
>d1axth2 2.1.1.2.117 (114-228) Immunoglobulin (constant domains of L and H chains) {Catalytic Fab 33F12 (mouse), kappa L chain}
akttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsd
lytlsssvtvtsstwpsqsitcnvahpasstkvdkkiepr
>d1axtl1 2.1.1.1.119 (1-107) Immunoglobulin (variable domains of L and H chains) {Catalytic Fab 33F12 (mouse), kappa L chain}
elvmtqtplslpvslgdqasiscrssqslvhsygntflnwylqksgqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyfcsqgthvpytfgggtkleik
>d1axtl2 2.1.1.2.117 (108-211) Immunoglobulin (constant domains of L and H chains) {Catalytic Fab 33F12 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1axwa_ 4.91.1.1.1 Thymidylate synthase {Escherichia coli}
mkqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihell
wflqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlk
ndpdsrriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfnias
yallvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesif
dyrfedfeiegydphpgikapvai
>d1axwb_ 4.91.1.1.1 Thymidylate synthase {Escherichia coli}
mkqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihell
wflqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlk
ndpdsrriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfnias
yallvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesif
dyrfedfeiegydphpgikapvai
>d1axx__ 4.94.1.1.2 Cytochrome b5 {Rat (Rattus norvegicus)}
dkdvkyytleeiqkhkdskstwvilhhkvydltkfleehpggeevlreqaggdatenfed
vghstdarelsktyiigelhpddrskiakpsetl
>d1axy__ 2.26.1.1.6 Lectin {Coral tree (Erythrina corallodendron)}
vetisfsfsefepgndnltlqgaalitqsgvlqltkinqngmpawdstgrtlyakpvhiw
dmttgtvasfetrfsfsieqpytrplpadglvffmgptkskpaqgygylgifnnskqdns
yqtlgvefdtfsnpwdppqvphigidvnsirsiktqpfqldngqvanvvikydasskilh
avlvypssgaiytiaeivdvkqvlpewvdvglsgatgaqrdaaethdvyswsfqaslpe
>d1axz__ 2.26.1.1.6 Lectin {Coral tree (Erythrina corallodendron)}
vetisfsfsefepgndnltlqgaalitqsgvlqltkinqngmpawdstgrtlyakpvhiw
dmttgtvasfetrfsfsieqpytrplpadglvffmgptkskpaqgygylgifnnskqdns
yqtlgvefdtfsnpwdppqvphigidvnsirsiktqpfqldngqvanvvikydasskilh
avlvypssgaiytiaeivdvkqvlpewvdvglsgatgaqrdaaethdvyswsfqaslpe
>d1ay0a1 3.29.1.2.1 (3-337) Transketolase, TK {Baker's yeast (Saccharomyces cerevisiae)}
qftdidklavstirilavdtvskansghpgaplgmapaahvlwsqmrmnptnpdwinrdr
fvlsnghavallysmlhltgydlsiedlkqfrqlgsrtpghpefelpgvevttgplgqgi
snavgmamaqanlaatynkpgftlsdnytyvflgdgclqegisseasslaghlklgnlia
iyddnkitidgatsisfdedvakryeaygwevlyvengnedlagiakaiaqaklskdkpt
likmtttigygslhagshsvagaplkaddvkqlkskfgfnpdksfvvpqevydhyqktil
kpgveannkwnklfseyqkkfpelgaelarrlsgq
>d1ay0a2 3.29.1.2.1 (338-534) Transketolase, TK {Baker's yeast (Saccharomyces cerevisiae)}
lpanwesklptytakdsavatrklsetvledvynqlpeliggsadltpsnltrwkealdf
qppssgsgnysgryirygirehamgaimngisafganykpyggtflnfvsyaagavrlsa
lsghpviwvathdsigvgedgpthqpietlahfrslpniqvwrpadgnevsaayknsles
khtpsiialsrqnlpql
>d1ay0a3 3.39.1.1.1 (535-680) Transketolase {Baker's yeast (Saccharomyces cerevisiae)}
egssiesaskggyvlqdvanpdiilvatgsevslsveaaktlaaknikarvvslpdfftf
dkqpleyrlsvlpdnvpimsvevlattcwgkyahqsfgidrfgasgkapevfkffgftpe
gvaeraqktiafykgdklisplkkaf
>d1ay0b1 3.29.1.2.1 (3-337) Transketolase, TK {Baker's yeast (Saccharomyces cerevisiae)}
qftdidklavstirilavdtvskansghpgaplgmapaahvlwsqmrmnptnpdwinrdr
fvlsnghavallysmlhltgydlsiedlkqfrqlgsrtpghpefelpgvevttgplgqgi
snavgmamaqanlaatynkpgftlsdnytyvflgdgclqegisseasslaghlklgnlia
iyddnkitidgatsisfdedvakryeaygwevlyvengnedlagiakaiaqaklskdkpt
likmtttigygslhagshsvagaplkaddvkqlkskfgfnpdksfvvpqevydhyqktil
kpgveannkwnklfseyqkkfpelgaelarrlsgq
>d1ay0b2 3.29.1.2.1 (338-534) Transketolase, TK {Baker's yeast (Saccharomyces cerevisiae)}
lpanwesklptytakdsavatrklsetvledvynqlpeliggsadltpsnltrwkealdf
qppssgsgnysgryirygirehamgaimngisafganykpyggtflnfvsyaagavrlsa
lsghpviwvathdsigvgedgpthqpietlahfrslpniqvwrpadgnevsaayknsles
khtpsiialsrqnlpql
>d1ay0b3 3.39.1.1.1 (535-680) Transketolase {Baker's yeast (Saccharomyces cerevisiae)}
egssiesaskggyvlqdvanpdiilvatgsevslsveaaktlaaknikarvvslpdfftf
dkqpleyrlsvlpdnvpimsvevlattcwgkyahqsfgidrfgasgkapevfkffgftpe
gvaeraqktiafykgdklisplkkaf
>d1ay1h1 2.1.1.1.105 (1-115) Immunoglobulin (variable domains of L and H chains) {Fab TP7 (mouse), kappa L chain}
evqlqesgpglvkpyqslslsctvtgysitsdyawnwirqfpgnklewmgyitysgttdy
npslksrisitrdtsknqfflqlnsvttedtatyycaryyygywyfdvwgqgttltvss
>d1ay1h2 2.1.1.2.106 (116-209) Immunoglobulin (constant domains of L and H chains) {Fab TP7 (mouse), kappa L chain}
akttapsvyplapvssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsdlytlss
svtvtsstwpsqsitcnvahpasstkvdkkiepr
>d1ay1l1 2.1.1.1.105 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab TP7 (mouse), kappa L chain}
diqmtqspaimsaspgekvtmtcsasssvsymywyqqkpgssprlliydstnlasgvpvr
fsgsgsgtsysltisrmeaedaatyycqqwstypltfgagtklelk
>d1ay1l2 2.1.1.2.106 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab TP7 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1ay2__ 4.21.1.1.1 Pilin {Gc (Neisseria gonorrhoeae)}
ftlielmiviaivgilaavalpayqdytaraqvseaillaegqksavteyylnhgkwpen
ntsagvasppsdikgkyvkevevkngvvtatmlssgvnneikgkklslwarrengsvkwf
cgqpvtrtdddtvadakdgkeidtkhlpstcrdnfdak
>d1ay4a_ 3.57.1.1.7 Aromatic aminoacid aminotransferase, AroAT {Paracoccus denitrificans}
mlgnlkpqapdkilalmgefradprqgkidlgvgvykdatghtpimravhaaeqrmlete
ttktyaglsgepefqkamgelilgdglksettatlatvggtgalrqalelarmanpdlrv
fvsdptwpnhvsimnfmglpvqtyryfdaetrgvdfegmkadlaaakkgdmvllhgcchn
ptganltldqwaeiasilektgalplidlayqgfgdgleedaagtrliasripevliaas
csknfgiyrertgcllalcadaatrelaqgamaflnrqtysfppfhgakivstvlttpel
radwmaeleavrsgmlrlreqlagelrdlsgsdrfgfvaehrgmfsrlgatpeqvkrike
efgiymvgdsriniaglndntipilaraiievgv
>d1ay4b_ 3.57.1.1.7 Aromatic aminoacid aminotransferase, AroAT {Paracoccus denitrificans}
mlgnlkpqapdkilalmgefradprqgkidlgvgvykdatghtpimravhaaeqrmlete
ttktyaglsgepefqkamgelilgdglksettatlatvggtgalrqalelarmanpdlrv
fvsdptwpnhvsimnfmglpvqtyryfdaetrgvdfegmkadlaaakkgdmvllhgcchn
ptganltldqwaeiasilektgalplidlayqgfgdgleedaagtrliasripevliaas
csknfgiyrertgcllalcadaatrelaqgamaflnrqtysfppfhgakivstvlttpel
radwmaeleavrsgmlrlreqlagelrdlsgsdrfgfvaehrgmfsrlgatpeqvkrike
efgiymvgdsriniaglndntipilaraiievgv
>d1ay5a_ 3.57.1.1.7 Aromatic aminoacid aminotransferase, AroAT {Paracoccus denitrificans}
mlgnlkpqapdkilalmgefradprqgkidlgvgvykdatghtpimravhaaeqrmlete
ttktyaglsgepefqkamgelilgdglksettatlatvggtgalrqalelarmanpdlrv
fvsdptwpnhvsimnfmglpvqtyryfdaetrgvdfegmkadlaaakkgdmvllhgcchn
ptganltldqwaeiasilektgalplidlayqgfgdgleedaagtrliasripevliaas
csknfgiyrertgcllalcadaatrelaqgamaflnrqtysfppfhgakivstvlttpel
radwmaeleavrsgmlrlreqlagelrdlsgsdrfgfvaehrgmfsrlgatpeqvkrike
efgiymvgdsriniaglndntipilaraiievgv
>d1ay5b_ 3.57.1.1.7 Aromatic aminoacid aminotransferase, AroAT {Paracoccus denitrificans}
mlgnlkpqapdkilalmgefradprqgkidlgvgvykdatghtpimravhaaeqrmlete
ttktyaglsgepefqkamgelilgdglksettatlatvggtgalrqalelarmanpdlrv
fvsdptwpnhvsimnfmglpvqtyryfdaetrgvdfegmkadlaaakkgdmvllhgcchn
ptganltldqwaeiasilektgalplidlayqgfgdgleedaagtrliasripevliaas
csknfgiyrertgcllalcadaatrelaqgamaflnrqtysfppfhgakivstvlttpel
radwmaeleavrsgmlrlreqlagelrdlsgsdrfgfvaehrgmfsrlgatpeqvkrike
efgiymvgdsriniaglndntipilaraiievgv
>e1ay6.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>e1ay6.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
geadcglrplfekksledkterellesyi
>d1ay7a_ 4.1.1.1.1 RNase Sa {Streptomyces aureofaciens}
dvsgtvclsalppeatdtlnliasdgpfpysqdgvvfqnresvlptqsygyyheytvitp
gartrgtrriitgeatqedyytgdhyatfslidqtc
>d1ay7b_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdcltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegcditiils
>d1ay8a_ 3.57.1.1.7 Aromatic aminoacid aminotransferase, AroAT {Paracoccus denitrificans}
mlgnlkpqapdkilalmgefradprqgkidlgvgvykdatghtpimravhaaeqrmlete
ttktyaglsgepefqkamgelilgdglksettatlatvggtgalrqalelarmanpdlrv
fvsdptwpnhvsimnfmglpvqtyryfdaetrgvdfegmkadlaaakkgdmvllhgcchn
ptganltldqwaeiasilektgalplidlayqgfgdgleedaagtrliasripevliaas
csknfgiyrertgcllalcadaatrelaqgamaflnrqtysfppfhgakivstvlttpel
radwmaeleavrsgmlrlreqlagelrdlsgsdrfgfvaehrgmfsrlgatpeqvkrike
efgiymvgdsriniaglndntipilaraiievgv
>d1ay8b_ 3.57.1.1.7 Aromatic aminoacid aminotransferase, AroAT {Paracoccus denitrificans}
mlgnlkpqapdkilalmgefradprqgkidlgvgvykdatghtpimravhaaeqrmlete
ttktyaglsgepefqkamgelilgdglksettatlatvggtgalrqalelarmanpdlrv
fvsdptwpnhvsimnfmglpvqtyryfdaetrgvdfegmkadlaaakkgdmvllhgcchn
ptganltldqwaeiasilektgalplidlayqgfgdgleedaagtrliasripevliaas
csknfgiyrertgcllalcadaatrelaqgamaflnrqtysfppfhgakivstvlttpel
radwmaeleavrsgmlrlreqlagelrdlsgsdrfgfvaehrgmfsrlgatpeqvkrike
efgiymvgdsriniaglndntipilaraiievgv
>d1ay9a_ 2.30.1.2.1 UmuD' {Escherichia coli}
dyveqridlnqlliqhpsatyfvkasgdsmidggisdgdllivdsaitashgdiviaavd
geftvkklqlrptvqlipmnsayspitissedtldvfgvvihvvkamr
>d1ay9b_ 2.30.1.2.1 UmuD' {Escherichia coli}
dyveqridlnqlliqhpsatyfvkasgdsmidggisdgdllivdsaitashgdiviaavd
geftvkklqlrptvqlipmnsayspitissedtldvfgvvihvvkamr
>d1ayaa_ 4.72.1.1.6 Tyrosine phosphatase Syp {Mouse (Mus musculus)}
mrrwfhpnitgveaenllltrgvdgsflarpsksnpgdftlsvrrngavthikiqntgdy
ydlyggekfatlaelvqyymehhgqlkekngdvielkypln
>d1ayab_ 4.72.1.1.6 Tyrosine phosphatase Syp {Mouse (Mus musculus)}
mrrwfhpnitgveaenllltrgvdgsflarpsksnpgdftlsvrrngavthikiqntgdy
ydlyggekfatlaelvqyymehhgqlkekngdvielkypln
>d1ayba_ 4.72.1.1.6 Tyrosine phosphatase Syp {Mouse (Mus musculus)}
rrwfhpnitgveaenllltrgvdgsflarpsksnpgdftlsvrrngavthikiqntgdyy
dlyggekfatlaelvqyymehhgqlkekngdvielkypln
>d1ayca_ 4.72.1.1.6 Tyrosine phosphatase Syp {Mouse (Mus musculus)}
rrwfhpnitgveaenllltrgvdgsflarpsksnpgdftlsvrrngavthikiqntgdyy
dlyggekfatlaelvqyymehhgqlkekngdvielkypln
>d1ayd__ 4.72.1.1.6 Tyrosine phosphatase Syp {Mouse (Mus musculus)}
mrrwfhpnitgveaenllltrgvdgsflarpsksnpgdftlsvrrngavthikiqntgdy
ydlyggekfatlaelvqyymehhgqlkekngdvielkypln
>d1aye_1 3.47.4.1.3 (1-309) Carboxypeptidase A {Human (Homo sapiens)}
ersgnfnfgayhtleeisqemdnlvaehpglvskvnigssfenrpmnvlkfstggdkpai
wldagiharewvtqatalwtankivsdygkdpsitsildaldifllpvtnpdgyvfsqtk
nrmwrktrskvsgslcvgvdpnrnwdagfggpgassnpcsdsyhgpsansevevksivdf
ikshgkvkafiilhsysqllmfpygykctklddfdelsevaqkaaqslrslhgtkykvgp
icsviyqasggsidwsydygikysfafelrdtgrygfllparqilptaeetwlglkaime
hvrdhpy
>d1aye_2 4.47.3.1.3 (4a-99a) Procarboxypeptidase A {Human (Homo sapiens)}
letfvgdqvleivpsneeqiknllqleaqehlqldfwkspttpgetahvrvpfvnvqavk
vflesqgiaysimiedvqvlldkeneemlfnrrr
>d1ayfa_ 4.13.6.1.13 Adrenodoxin {Bovine (Bos taurus)}
kitvhfinrdgetlttkgkigdslldvvvqnnldidgfgacegtlacstchlifeqhife
kleaitdeendmldlaygltdrsrlgcqicltkamdnmtvrvp
>d1ayfb_ 4.13.6.1.13 Adrenodoxin {Bovine (Bos taurus)}
dkitvhfinrdgetlttkgkigdslldvvvqnnldidgfgacegtlacstchlifeqhif
ekleaitdeendmldlaygltdrsrlgcqicltkamdnmtvrvp
>d1ayg__ 1.3.1.1.23 Cytochrome c552 {Hydrogenobacter thermophilus}
neqlakqkgcmachdlkakkvgpayadvakkyagrkdavdylagkikkggsgvwgsvpmp
pqnvtdaeakqlaqwilsik
>d1ayi__ 1.29.2.1.1 ImmE7 protein {Escherichia coli}
melknsisdyteaefvqllkeiekenvaatddvldvllehfvkitehpdgtdliyypsdn
rddspegivkeikewraangkpgfkq
>d1ayj__ 7.3.7.4.3 Antifungal protein 1 (RS-AFP1) {Radish (Raphanus sativus)}
klcerpsgtwsgvcgnnnacknqcinlekarhgscnyvfpahkcicyfpc
>d1ayk__ 4.71.1.9.1 Fibroblast collagenase (MMP-1) {Human (Homo sapiens)}
vltegnprweqthltyrienytpdlpradvdhaiekafqlwsnvtpltftkvsegqadim
isfvrgdhrdnspfdgpggnlahafqpgpgiggdahfdederwtnnfreynlhrvaahel
ghslglshstdigalmypsytfsgdvqlaqddidgiqaiygrsqnpvqp
>d1ayl__ 3.81.1.1.1 Phosphoenolpyruvate carboxykinase (ATP-oxaloacetate carboxy-liase) {Escherichia coli}
mrvnngltpqeleaygisdvhdivynpsydllyqeeldpsltgyergvltnlgavavdtg
iftgrspkdkyivrddttrdtfwwadkgkgkndnkplspetwqhlkglvtrqlsgkrlfv
vdafcganpdtrlsvrfitevawqahfvknmfirpsdeelagfkpdfivmngakctnpqw
keqglnsenfvafnltermqliggtwyggemkkgmfsmmnyllplkgiasmhcsanvgek
gdvavffglsgtgkttlstdpkrrligddehgwdddgvfnfeggcyaktiklskeaepei
ynairrdallenvtvredgtidfddgsktentrvsypiyhidnivkpvskaghatkvifl
tadafgvlppvsrltadqtqyhflsgftaklagtergiteptptfsacfgaaflslhptq
yaevlvkrmqaagaqaylvntgwngtgkrisikdtraiidailngsldnaetftlpmfnl
aiptelpgvdtkildprntyaspeqwqekaetlaklfidnfdkytdtpagaalvaagpkl
>d1aym1_ 2.9.1.4.9 Rhinovirus coat protein {Human (Homo sapiens), rhinovirus 16}
npveryvdevlnevlvvpninqshpttsnaapvldaaetghtnkiqpedtietryvqssq
tldemsvesflgrsgcihesvldivdnyndqsftkwninlqemaqirrkfemftyarfds
eitmvpsvaakdghighivmqymyvppgapipttrddyawqsgtnasvfwqhgqpfprfs
lpflsiasayymfydgydgdtyksrygtvvtndmgtlcsrivtseqlhkvkvvtriyhka
khtkawcprppravqyshthttnyklssevhndvairprtnlttv
>d1aym2_ 2.9.1.4.9 Rhinovirus coat protein {Human (Homo sapiens), rhinovirus 16}
sdriiqitrgdstitsqdvanavvgygvwphyltpqdataidkptqpdtssnrfytldsk
mwnstskgwwwklpdalkdmgifgenmfyhflgrsgytvhvqcnaskfhqgtllvvmipe
hqlatvnkgnvnagykythpgeagrevgtqvenekqpsddnwlnfdgtllgnllifphqf
inlrsnnsatlivpyvnavpmdsmvrhnnwslviipvcqlqsnnisnivpitvsispmca
efsgaraktvvq
>d1aym3_ 2.9.1.4.9 Rhinovirus coat protein {Human (Homo sapiens), rhinovirus 16}
glpvyvtpgsgqfmttddmqspcalpwyhptkeifipgevknliemcqvdtlipinstqs
nignvsmytvtlspqtklaeeifaikvdiashplattligeiasyfthwtgslrfsfmfc
gtanttlkvllaytppgigkprsrkeamlgthvvwdvglqstvslvvpwisasqyrfttp
dtyssagyitcwyqtnfvvppntpntaemlcfvsgckdfclrmardtdlhkqtgpitq
>d1ayn1_ 2.9.1.4.9 Rhinovirus coat protein {Human (Homo sapiens), rhinovirus 16}
npveryvdevlnevlvvpninqshpttsnaapvldaaetghtnkiqpedtietryvqssq
tldemsvesflgrsgcihesvldivdnyndqsftkwninlqemaqirrkfemftyarfds
eitmvpsvaakdghighivmqymyvppgapipttrddyawqsgtnasvfwqhgqpfprfs
lpflsiasayymfydgydgdtyksrygtvvtndmgtlcsrivtseqlhkvkvvtriyhka
khtkawcprppravqyshthttnyklssevhndvairprtnlttv
>d1ayn2_ 2.9.1.4.9 Rhinovirus coat protein {Human (Homo sapiens), rhinovirus 16}
sdriiqitrgdstitsqdvanavvgygvwphyltpqdataidkptqpdtssnrfytldsk
mwnstskgwwwklpdalkdmgifgenmfyhflgrsgytvhvqcnaskfhqgtllvvmipe
hqlatvnkgnvnagykythpgeagrevgtqvenekqpsddnwlnfdgtllgnllifphqf
inlrsnnsatlivpyvnavpmdsmvrhnnwslviipvcqlqsnnisnivpitvsispmca
efsgaraktvvq
>d1ayn3_ 2.9.1.4.9 Rhinovirus coat protein {Human (Homo sapiens), rhinovirus 16}
glpvyvtpgsgqfmttddmqspcalpwyhptkeifipgevknliemcqvdtlipinstqs
nignvsmytvtlspqtklaeeifaikvdiashplattligeiasyfthwtgslrfsfmfc
gtanttlkvllaytppgigkprsrkeamlgthvvwdvglqstvslvvpwisasqyrfttp
dtyssagyitcwyqtnfvvppntpntaemlcfvsgckdfclrmardtdlhkqtgpitq
>d1ayoa_ 2.2.4.1.2 Receptor domain from alpha-2-macroglobulin {Bovine (Bos taurus)}
efpfalevqtlpqtcdgpkahtsfqislsvsyigsrpasnmaivdvkmvsgfiplkptvk
mlersnvsrtevsnnhvliyldkvtnetltltftvlqdipvrdlkpaivkvydyyetdef
avaeysapcs
>d1ayob_ 2.2.4.1.2 Receptor domain from alpha-2-macroglobulin {Bovine (Bos taurus)}
efpfalevqtlpqtcdgpkahtsfqislsvsyigsrpasnmaivdvkmvsgfiplkptvk
mlersnvsrtevsnnhvliyldkvtnetltltftvlqdipvrdlkpaivkvydyyetdef
avaeysapcs
>d1aypa_ 1.123.1.2.11 Phospholipase A2 {Human (Homo sapiens), synovial fluid}
nlvnfhrmiklttgkeaalsygfygchcgvggrgspkdatdrccvthdccykrlekrgcg
tkflsykfsnsgsritcakqdscrsqlcecdkaaatcfarnkttynkkyqyysnkhcrgs
tprc
>d1aypb_ 1.123.1.2.11 Phospholipase A2 {Human (Homo sapiens), synovial fluid}
nlvnfhrmiklttgkeaalsygfygchcgvggrgspkdatdrccvthdccykrlekrgcg
tkflsykfsnsgsritcakqdscrsqlcecdkaaatcfarnkttynkkyqyysnkhcrgs
tprc
>d1aypc_ 1.123.1.2.11 Phospholipase A2 {Human (Homo sapiens), synovial fluid}
nlvnfhrmiklttgkeaalsygfygchcgvggrgspkdatdrccvthdccykrlekrgcg
tkflsykfsnsgsritcakqdscrsqlcecdkaaatcfarnkttynkkyqyysnkhcrgs
tprc
>d1aypd_ 1.123.1.2.11 Phospholipase A2 {Human (Homo sapiens), synovial fluid}
nlvnfhrmiklttgkeaalsygfygchcgvggrgspkdatdrccvthdccykrlekrgcg
tkflsykfsnsgsritcakqdscrsqlcecdkaaatcfarnkttynkkyqyysnkhcrgs
tprc
>d1aype_ 1.123.1.2.11 Phospholipase A2 {Human (Homo sapiens), synovial fluid}
nlvnfhrmiklttgkeaalsygfygchcgvggrgspkdatdrccvthdccykrlekrgcg
tkflsykfsnsgsritcakqdscrsqlcecdkaaatcfarnkttynkkyqyysnkhcrgs
tprc
>d1aypf_ 1.123.1.2.11 Phospholipase A2 {Human (Homo sapiens), synovial fluid}
nlvnfhrmiklttgkeaalsygfygchcgvggrgspkdatdrccvthdccykrlekrgcg
tkflsykfsnsgsritcakqdscrsqlcecdkaaatcfarnkttynkkyqyysnkhcrgs
tprc
>d1ayra1 2.1.1.5.19 (1-182) Arrestin {Bovine (Bos taurus)}
mkankpapnhvifkkisrdksvtiylgkrdyidhvervepvdgvvlvdpelvkgkrvyvs
ltcafrygqedidvmglsfrrdlyfsqvqvfppvgasgattrlqeslikklgantypfll
tfpdylpcsvmlqpapqdvgkscgvdfeikafathstdveedkipkkssvrllirkvqha
pr
>d1ayra2 2.1.1.5.19 (183-368) Arrestin {Bovine (Bos taurus)}
dmgpqpraeaswqffmsdkplrlavslskeiyyhgepipvtvavtnstektvkkikvlve
qvtnvvlyssdyyiktvaaeeaqekvppnssltktltlvpllannrerrgialdgkikhe
dtnlasstiikegidktvmgilvsyqikvkltvsgllgeltssevatevpfrlmhpqped
pdtaka
>d1ayrb1 2.1.1.5.19 (1-182) Arrestin {Bovine (Bos taurus)}
mkankpapnhvifkkisrdksvtiylgkrdyidhvervepvdgvvlvdpelvkgkrvyvs
ltcafrygqedidvmglsfrrdlyfsqvqvfppvgasgattrlqeslikklgantypfll
tfpdylpcsvmlqpapqdvgkscgvdfeikafathstdveedkipkkssvrllirkvqha
pr
>d1ayrb2 2.1.1.5.19 (183-363) Arrestin {Bovine (Bos taurus)}
dmgpqpraeaswqffmsdkplrlavslskeiyyhgepipvtvavtnstektvkkikvlve
qvtnvvlyssdyyiktvaaeeaqekvppnssltktltlvpllannrerrgialdgkikhe
dtnlasstiikegidktvmgilvsyqikvkltvsgllgeltssevatevpfrlmhpqped
p
>d1ayrc1 2.1.1.5.19 (1-182) Arrestin {Bovine (Bos taurus)}
mkankpapnhvifkkisrdksvtiylgkrdyidhvervepvdgvvlvdpelvkgkrvyvs
ltcafrygqedidvmglsfrrdlyfsqvqvfppvgasgattrlqeslikklgantypfll
tfpdylpcsvmlqpapqdvgkscgvdfeikafathstdveedkipkkssvrllirkvqha
pr
>d1ayrc2 2.1.1.5.19 (183-368) Arrestin {Bovine (Bos taurus)}
dmgpqpraeaswqffmsdkplrlavslskeiyyhgepipvtvavtnstektvkkikvlve
qvtnvvlyssdyyiktvaaeeaqekvppnssltktltlvpllannrerrgialdgkikhe
dtnlasstiikegidktvmgilvsyqikvkltvsgllgeltssevatevpfrlmhpqped
pdtaka
>d1ayrd1 2.1.1.5.19 (1-182) Arrestin {Bovine (Bos taurus)}
mkankpapnhvifkkisrdksvtiylgkrdyidhvervepvdgvvlvdpelvkgkrvyvs
ltcafrygqedidvmglsfrrdlyfsqvqvfppvgasgattrlqeslikklgantypfll
tfpdylpcsvmlqpapqdvgkscgvdfeikafathstdveedkipkkssvrllirkvqha
pr
>d1ayrd2 2.1.1.5.19 (183-363) Arrestin {Bovine (Bos taurus)}
dmgpqpraeaswqffmsdkplrlavslskeiyyhgepipvtvavtnstektvkkikvlve
qvtnvvlyssdyyiktvaaeeaqekvppnssltktltlvpllannrerrgialdgkikhe
dtnlasstiikegidktvmgilvsyqikvkltvsgllgeltssevatevpfrlmhpqped
p
>d1ayu__ 4.3.1.1.13 (Pro)cathepsin K {Human (Homo sapiens)}
apdsvdyrkkgyvtpvknqgqcgscwafssvgalegqlkkktgkllnlspqnlvdcvsen
dgcgggymtnafqyvqknrgidsedaypyvgqeescmynptgkaakcrgyreipegneka
lkravarvgpvsvaidasltsfqfyskgvyydescnsdnlnhavlavgygiqkgnkhwii
knswgenwgnkgyilmarnknnacgianlasfpkm
>d1ayv__ 4.3.1.1.13 (Pro)cathepsin K {Human (Homo sapiens)}
apdsvdyrkkgyvtpvknqgqcgscwafssvgalegqlkkktgkllnlspqnlvdcvsen
dgcgggymtnafqyvqknrgidsedaypyvgqeescmynptgkaakcrgyreipegneka
lkravarvgpvsvaidasltsfqfyskgvyydescnsdnlnhavlavgygiqkgnkhwii
knswgenwgnkgyilmarnknnacgianlasfpkm
>d1ayw__ 4.3.1.1.13 (Pro)cathepsin K {Human (Homo sapiens)}
apdsvdyrkkgyvtpvknqgqcgscwafssvgalegqlkkktgkllnlspqnlvdcvsen
dgcgggymtnafqyvqknrgidsedaypyvgqeescmynptgkaakcrgyreipegneka
lkravarvgpvsvaidasltsfqfyskgvyydescnsdnlnhavlavgygiqkgnkhwii
knswgenwgnkgyilmarnknnacgianlasfpkm
>d1ayx__ 1.98.1.1.2 Glucoamylase {Yeast (Saccharomycopsis fibuligera)}
aypsfeaysnykvdrtdletfldkqkevslyyllqniaypegqfnngvpgtviaspstsn
pdyyyqwtrdsaitfltvlselednnfnttlakaveyyintsynlqrtsnpsgsfddenh
kglgepkfntdgsaytgawgrpqndgpalrayaisrylndvnslnegklvltdsgdinfs
stediykniikpdleyvigywdstgfdlweenqgrhfftslvqqkalayavdiaksfddg
dfantlsstastlesylsgsdggfvntdvnhivenpdllqqnsrqgldsatyigpllthd
igessstpfdvdneyvlqsyylllednkdrysvnsaysagaaigrypedvyngdgssegn
pwflatayaaqvpyklaydaksasnditinkinydffnkyivdlstinsayqssdsvtik
sgsdefntvadnlvtfgdsflqvildhinddgslneqlnrytgystgaysltwssgalle
airlrnkvkala
>e1ayy.1a 4.124.1.4.2 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Flavobacterium meningosepticum}
tnkpivlstwnfglhanveawkvlskggkaldavekgvrlveddptersvgyggrpdrdg
rvtldacimdenynigsvacmehiknpisvaravmektphvmlvgdgalefalsqgfkke
nlltaesekewkewlkts
>e1ayy.1b 4.124.1.4.2 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Flavobacterium meningosepticum}
tigmialdaqgnlsgacttsgmaykmhgrvgdspiigaglfvdneigaatatghgeevir
tvgthlvvelmnqgrtpqqackeaverivkivnrrgknlkdiqvgfialnkkgeygayci
qdgfnfavhdqkgnrletpgfal
>e1ayy.2c 4.124.1.4.2 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Flavobacterium meningosepticum}
tnkpivlstwnfglhanveawkvlskggkaldavekgvrlveddptersvgyggrpdrdg
rvtldacimdenynigsvacmehiknpisvaravmektphvmlvgdgalefalsqgfkke
nlltaesekewkewlktsqy
>e1ayy.2d 4.124.1.4.2 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Flavobacterium meningosepticum}
tigmialdaqgnlsgacttsgmaykmhgrvgdspiigaglfvdneigaatatghgeevir
tvgthlvvelmnqgrtpqqackeaverivkivnrrgknlkdiqvgfialnkkgeygayci
qdgfnfavhdqkgnrletpgfalk
>d1ayza_ 4.18.1.1.2 Ubiquitin conjugating enzyme {Baker's yeast (Saccharomyces cerevisiae), ubc2 (RAD6)}
stparrrlmrdfkrmkedappgvsasplpdnvmvwnamiigpadtpyedgtfrlllefde
eypnkpphvkflsemfhpnvyangeicldilqnrwtptydvasiltsiqslfndpnpasp
anveaatlfkdhksqyvkrvketveksweddmd
>d1ayzb_ 4.18.1.1.2 Ubiquitin conjugating enzyme {Baker's yeast (Saccharomyces cerevisiae), ubc2 (RAD6)}
stparrrlmrdfkrmkedappgvsasplpdnvmvwnamiigpadtpyedgtfrlllefde
eypnkpphvkflsemfhpnvyangeicldilqnrwtptydvasiltsiqslfndpnpasp
anveaatlfkdhksqyvkrvketveksweddmd
>d1ayzc_ 4.18.1.1.2 Ubiquitin conjugating enzyme {Baker's yeast (Saccharomyces cerevisiae), ubc2 (RAD6)}
stparrrlmrdfkrmkedappgvsasplpdnvmvwnamiigpadtpyedgtfrlllefde
eypnkpphvkflsemfhpnvyangeicldilqnrwtptydvasiltsiqslfndpnpasp
anveaatlfkdhksqyvkrvketveksweddmd
>d1az0a_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgrk
>d1az0b_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgrk
>d1az1__ 3.1.6.1.3 Aldose reductase (aldehyde reductase) {Human (Homo sapiens)}
srlllnngakmpilglgtwksppgqvteavkvaidvgyrhidcahvyqnenevgvaiqek
lreqvvkreelfivsklwctyhekglvkgacqktlsdlkldyldlylihwptgfkpgkef
fpldesgnvvpsdtnildtwaameelvdeglvkaigisnfnhlqvemilnkpglkykpav
nqiechpyltqekliqycqskgivvtaysplgspdrpyakpedpslledprikaiaakhn
kttaqvlirfpmqrnlvvipksvtperiaenfkvfdfelssqdmttllsynrnwrvaall
sctshkdypfheef
>d1az2__ 3.1.6.1.3 Aldose reductase (aldehyde reductase) {Human (Homo sapiens)}
srlllnngakmpilglgtwksppgqvteavkvaidvgyrhidcahvyqnenevgvaiqek
lreqvvkreelfivsklwctyhekglvkgacqktlsdlkldyldlylihwptgfkpgkef
fpldesgnvvpsdtnildtwaameelvdeglvkaigisnfnhlqvemilnkpglkykpav
nqiechpyltqekliqycqskgivvtaysplgspdrpyakpedpslledprikaiaakhn
kttaqvlirfpmqrnlvvipksvtperiaenfkvfdfelssqdmttllsynrnwrvaall
sctshkdypfheef
>d1az3a_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywr
>d1az3b_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
>d1az4a_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikatytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywr
>d1az4b_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikatytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
>d1az5__ 2.44.1.1.6 Simian immunodeficiency virus (SIV) protease {Simian immunodeficiency virus, Mac251 isolate}
pqfhlwkrpvvtahiegqpvevlldtgaddsivtgielgphytpkivggiggfintkeyk
nvevevlgkrikgtimtgdtpinifgrnlltalgmslnf
>d1az6__ 7.3.8.1.1 Cellobiohydrolase I {Trichoderma reesei, ct-cbh I}
tqshagqcggigysgptvcasgttcqvlnpyysqcl
>d1az8__ 2.41.1.2.1 Trypsin(ogen) {Bovine (Bos taurus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1az9__ 4.101.1.1.5 Aminopeptidase P {Escherichia coli}
seisrqefqrrrqalveqmqpgsaalifaapevtrsadseypyrqnsdfwyftgfnepea
vlvliksddthnhsvlfnrvrdltaeiwfgrrlgqdaapeklgvdralafseinqqlyql
lngldvvyhaqgeyayadvivnsaleklrkgsrqnltapatmidwrpvvhemrlfkspee
iavlrrageitamahtramekcrpgmfeyhlegeihhefnrhgarypsyntivgsgengc
ilhytenecemrdgdlvlidagceykgyagditrtfpvngkftqaqreiydivleslets
lrlyrpgtsilevtgevvrimvsglvklgilkgdvdeliaqnahrpffmhglshwlgldv
hdvgvygqdrsrilepgmvltvepglyiapdaevpeqyrgigirieddivitetgnenlt
asvvkkpeeiealmvaarkq
>d1azba_ 2.5.1.1.21 Azurin {Alcaligenes denitrificans}
aqceatiesndamqynlkemvvdksckqftvhlkhvgkmakvamghnwvltkeadkqgva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
mkgtlklsn
>d1azbb_ 2.5.1.1.21 Azurin {Alcaligenes denitrificans}
aqceatiesndamqynlkemvvdksckqftvhlkhvgkmakvamghnwvltkeadkqgva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
mkgtlklsn
>d1azca_ 2.5.1.1.21 Azurin {Alcaligenes denitrificans}
aqceatiesndamqynlkemvvdksckqftvhlkhvgkmakvamghnwvltkeadkqgva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
mkgtlklsn
>d1azcb_ 2.5.1.1.21 Azurin {Alcaligenes denitrificans}
aqceatiesndamqynlkemvvdksckqftvhlkhvgkmakvamghnwvltkeadkqgva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
mkgtlklsn
>d1azda_ 2.26.1.1.2 Concanavalin A {Brazilian jackbean (Canavalia brasiliensis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvgkr
lsavvsypngdsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtegnlrltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1azdb_ 2.26.1.1.2 Concanavalin A {Brazilian jackbean (Canavalia brasiliensis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvgkr
lsavvsypngdsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtegnlrltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1azdc_ 2.26.1.1.2 Concanavalin A {Brazilian jackbean (Canavalia brasiliensis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvgkr
lsavvsypngdsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtegnlrltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1azdd_ 2.26.1.1.2 Concanavalin A {Brazilian jackbean (Canavalia brasiliensis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvgkr
lsavvsypngdsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtegnlrltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1azea_ 2.30.2.1.15 Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {Mouse (Mus musculus)}
meaiakvdfkataddelsfkrgdilkvlneesdqnwykaelngkdgfipknyiemk
>d1azf__ 4.2.1.2.1 Lysozyme {Chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1azgb_ 2.30.2.1.2 Fyn proto-oncogene tyrosine kinase, SH3 domain {Human (Homo sapiens)}
vtlfvalydyearteddlsfhkgekfqilnssegdwwearslttgetgyipsnyvapv
>d1azh__ 7.3.8.1.1 Cellobiohydrolase I {Trichoderma reesei, ct-cbh I}
tqshagqcggigysgptvcasgttcqvlnpyysqcl
>d1azi__ 1.1.1.1.8 Myoglobin {Horse (Equus caballus)}
glsdgewqqvlnvwgkveadiaghgqevlirlftghpetlekfdkfkhlkteaemkased
lkkhgtvvltalggilkkkghheaelkplaqshatkhkipikylefisdaiihvlhskhp
gdfgadaqgamtkalelfrndiaakykelgfqg
>d1azj__ 7.3.8.1.1 Cellobiohydrolase I {Trichoderma reesei, ct-cbh I}
tqshygqcggigysgptvcasgttcqvlnpaysqcl
>d1azk__ 7.3.8.1.1 Cellobiohydrolase I {Trichoderma reesei, ct-cbh I}
tqshygqcggigysgptvcasgttcqvlnpyasqcl
>d1azl__ 3.16.4.1.2 Flavodoxin {Desulfovibrio vulgaris}
pkalivygsttgnteytaetiareladagyevdsrdaasveagglfegfdlvllgcstwv
ddsielqddfiplfdsleetgaqgrkvacfgcgdssyeyfcgavdaieeklknlgaeivq
dglridgdpraarddivgwahdvrgai
>d1azm__ 2.65.1.1.1 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme I}
pdwgyddkngpeqwsklypiangnnqspvdiktsetkhdtslkpisvsynpatakeiinv
ghsfhvnfedndnrsvlkggpfsdsyrlfqfhfhwgstnehgsehtvdgvkysaelhvah
wnsakysslaeaaskadglavigvlmkvgeanpklqkvldalqaiktkgkrapftnfdps
tllpssldfwtypgslthpplyesvtwiickesisvsseqlaqfrsllsnvegdnavpmq
hnnrptqplkgrtvrasf
>d1azna_ 2.5.1.1.23 Azurin {Pseudomonas aeruginosa}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctapghsal
mkgtltlk
>d1aznb_ 2.5.1.1.23 Azurin {Pseudomonas aeruginosa}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctapghsal
mkgtltlk
>d1aznc_ 2.5.1.1.23 Azurin {Pseudomonas aeruginosa}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctapghsal
mkgtltlk
>d1aznd_ 2.5.1.1.23 Azurin {Pseudomonas aeruginosa}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctapghsal
mkgtltlk
>d1azo__ 3.43.1.8.1 DNA mismatch repair protein MutH from {Escherichia coli}
prpllsppeteeqllaqaqqlsgytlgelaalvglvtpenlkrdkgwigvlleiwlgasa
gskpeqdfaalgvelktipvdslgrplettfvcvapltgnsgvtwetshvrhklkrvlwi
pvegeasiplaqrrvgspllwspneeedrqlredweelxdxivlgqveritarhgeylqi
rpkaanakalteaigargeriltlprgfylkknftsallarhfliq
>d1azpa_ 4.8.2.1.2 DNA-binding protein {Sulfolobus acidocaldarius, Sac7d}
mvkvkfkykgeekevdtskikkvwrvgkmvsftyddngktgrgavsekdapkelldmlar
aerekk
>d1azqa_ 4.8.2.1.2 DNA-binding protein {Sulfolobus acidocaldarius, Sac7d}
mvkvkfkykgeekevdtskikkvwrvgkmvsftyddngktgrgavsekdapkelldmlar
aerekk
>d1azra_ 2.5.1.1.23 Azurin {Pseudomonas aeruginosa}
aqcsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghdwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctfpghsal
mkgtltlk
>d1azrb_ 2.5.1.1.23 Azurin {Pseudomonas aeruginosa}
aqcsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghdwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctfpghsal
mkgtltlk
>d1azrc_ 2.5.1.1.23 Azurin {Pseudomonas aeruginosa}
aqcsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghdwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctfpghsal
mkgtltlk
>d1azrd_ 2.5.1.1.23 Azurin {Pseudomonas aeruginosa}
aqcsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghdwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctfpghsal
mkgtltlk
>d1azsa_ 4.47.24.1.2 Adenylyl cyclase VC1, domain C1a {Dog (Canis familiaris)}
dmmfhkiyiqkhdnvsilfadiegftslasqctaqelvmtlnelfarfdklaaenhclri
kilgdcyycvsglpearadhahccvemgmdmieaislvremtgvnvnmrvgihsgrvhcg
vlglrkwqfdvwsndvtlanhmeaggkagrihitkatlsylngdyevepgcggernaylk
ehsietflil
>d1azsb_ 4.47.24.1.3 Adenylyl cyclase IIC1, domain C2a {Rat (Rattus norvegicus)}
hqsydcvcvmfasipdfkefytesdvnkegleclrllneiiadfddllskpkfsgvekik
tigstymaatglsaipsqehaqeperqymhigtmvefayalvgkldainkhsfndfklrv
ginhgpviagvigaqkpqydiwgntvnvasrmdstgvldkiqvteetslilqtlgytctc
rgiinvkgkgdlktyfvnt
>d1azsc1 1.67.1.1.1 (86-201) Transducin (alpha subunit), insertion domain {Bovine (Bos taurus)}
gfngdgekatkvqdiknnlkeaietivaamsnlvppvelanpenqfrvdyilsvmnvpdf
dfppefyehakalwedegvracyersneyqlidcaqyfldkidvikqddyvpsdqdllrc
r
>d1azsc2 3.30.1.6.12 (36-66,202-393) Transducin (alpha subunit) {Bovine (Bos taurus)}
vyrathrllllgagesgkstivkqmrilhvnXvltsgifetkfqvdkvnfhmfdvggqrd
errkwiqcfndvtaiifvvasssynmvirednqtnrlqealnlfksiwnnrwlrtisvil
flnkqdllaekvlagkskiedyfpefaryttpedatpepgedprvtrakyfirdeflris
tasgdgrhycyphftcavdtenirrvfndcrdiiqrmhlrqyel
>d1azta1 1.67.1.1.1 (88-201) Transducin (alpha subunit), insertion domain {Bovine (Bos taurus)}
katkvqdiknnlkeaietivaamsnlvppvelanpenqfrvdyilsvmnvpdfdfppefy
ehakalwedegvracyersneyqlidcaqyfldkidvikqddyvpsdqdllrcr
>d1azta2 3.30.1.6.12 (35-65,202-391) Transducin (alpha subunit) {Bovine (Bos taurus)}
qvyrathrllllgagesgkstivkqmrilhvXvltsgifetkfqvdkvnfhmfdvggqrd
errkwiqcfndvtaiifvvasssynmvirednqtnrlqealnlfksiwnnrwlrtisvil
flnkqdllaekvlagkskiedyfpefaryttpedatpepgedprvtrakyfirdeflris
tasgdgrhycyphftcavdtenirrvfndcrdiiqrmhlrqy
>d1aztb1 1.67.1.1.1 (87-201) Transducin (alpha subunit), insertion domain {Bovine (Bos taurus)}
ekatkvqdiknnlkeaietivaamsnlvppvelanpenqfrvdyilsvmnvpdfdfppef
yehakalwedegvracyersneyqlidcaqyfldkidvikqddyvpsdqdllrcr
>d1aztb2 3.30.1.6.12 (35-69,202-391) Transducin (alpha subunit) {Bovine (Bos taurus)}
qvyrathrllllgagesgkstivkqmrilhvngfnXvltsgifetkfqvdkvnfhmfdvg
gqrderrkwiqcfndvtaiifvvasssynmvirednqtnrlqealnlfksiwnnrwlrti
svilflnkqdllaekvlagkskiedyfpefaryttpedatpepgedprvtrakyfirdef
lristasgdgrhycyphftcavdtenirrvfndcrdiiqrmhlrqy
>d1azu__ 2.5.1.1.23 Azurin {Pseudomonas aeruginosa}
csvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvvtd
gmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctfpghsalmk
gtltlk
>d1azva_ 2.1.8.1.2 Cu,Zn superoxide dismutase, SOD {Human (Homo sapiens)}
atkavcvlkgdgpvqgiinfeqkesngpvkvwgsikrlteglhgfhvhefgdntagctsa
gphfnplsrkhggpkdeerhvgdlgnvtadkdgvadvsiedsvislsgdhciigrtlvvh
ekaddlgkggneestktgnagsrlacgvigiaq
>d1azvb_ 2.1.8.1.2 Cu,Zn superoxide dismutase, SOD {Human (Homo sapiens)}
atkavcvlkgdgpvqgiinfeqkesngpvkvwgsikrlteglhgfhvhefgdntagctsa
gphfnplsrkhggpkdeerhvgdlgnvtadkdgvadvsiedsvislsgdhciigrtlvvh
ekaddlgkggneestktgnagsrlacgvigiaq
>d1azwa_ 3.59.1.5.1 Proline iminopeptidase {Xanthomonas campestris, pv. citri}
mrtlypeitpyqqgslkvddrhtlyfeqcgnphgkpvvmlhggpgggcndkmrrfhdpak
yrivlfdqrgsgrstphadlvdnttwdlvadierlrthlgvdrwqvfggswgstlalaya
qthpqqvtelvlrgifllrrfelewfyqegasrlfpdawehylnaippveradlmsafhr
rltsddeatrlaaakawsvwegatsflhvdedfvtghedahfalafarienhyfvnggff
evedqllrdahriadipgvivhgrydvvcplqsawdlhkawpkaqlqispasghsafepe
nvdalvratdgfa
>d1azwb_ 3.59.1.5.1 Proline iminopeptidase {Xanthomonas campestris, pv. citri}
mrtlypeitpyqqgslkvddrhtlyfeqcgnphgkpvvmlhggpgggcndkmrrfhdpak
yrivlfdqrgsgrstphadlvdnttwdlvadierlrthlgvdrwqvfggswgstlalaya
qthpqqvtelvlrgifllrrfelewfyqegasrlfpdawehylnaippveradlmsafhr
rltsddeatrlaaakawsvwegatsflhvdedfvtghedahfalafarienhyfvnggff
evedqllrdahriadipgvivhgrydvvcplqsawdlhkawpkaqlqispasghsafepe
nvdalvratdgfa
>d1azxi_ 5.1.1.1.6 Antithrombin {Human (Homo sapiens)}
gspvdictakprdipmnpmciyrspekkatedegseqkipeatnrrvwelskansrfatt
fyqhladskndndniflsplsistafamtklgacndtlqqlmevfkfdtisektsdqihf
ffaklncrlyrkankssklvsanrlfgdksltfnetyqdiselvygaklqpldfkenaeq
sraainkwvsnktegritdvipseaineltvlvlvntiyfkglwkskfspentrkelfyk
adgescsasmmyqegkfryrrvaegtqvlelpfkgdditmvlilpkpekslakvekeltp
evlqewldeleemmlvvhmprfriedgfslkeqlqdmglvdlfspeksklpgivaegrdd
lyvsdafhkaflevneegseaaastavviagrslnpnrvtfkanrpflvfirevplntii
fmgrvanpcv
>d1azxl_ 5.1.1.1.6 Antithrombin {Human (Homo sapiens)}
vdictakprdipmnpmciyrspekkatedegseqkipeatnrrvwelskansrfattfyq
hladskndndniflsplsistafamtklgacndtlqqlmevfkfdtisektsdqihfffa
klncrlyrkankssklvsanrlfgdksltfnetyqdiselvygaklqpldfkenaeqsra
ainkwvsnktegritdvipseaineltvlvlvntiyfkglwkskfspentrkelfykadg
escsasmmyqegkfryrrvaegtqvlelpfkgdditmvlilpkpekslakvekeltpevl
qewldeleemmlvvhmprfriedgfslkeqlqdmglvdlfspeksklpgivaegrddlyv
sdafhkaflevneegseaaastavviagrslnpnrvtfkanrpflvfirevplntiifmg
rvanpcv
>d1azya1 1.49.2.1.1 (1-70) Thymidine phosphorylase {Escherichia coli}
lflaqeiirkkrdghalsdeeirffingirdntisegqiaalamtiffhdmtmpervslt
mamrdsgtvl
>d1azya2 3.20.1.1.1 (71-335) Thymidine phosphorylase {Escherichia coli}
dwkslhlngpivdkhstggvgdvtslmlgpmvaacggyipmisgrglghtggtldklesi
pgfdifpddnrfreiikdvgvaiigqtsslapadkrfyatrditatvdsiplitasilak
klaegldalvmdvkvgsgafmptyelsealaeaivgvangagvrttalltdmnqvlassa
gnavevreavqfltgeyrnprlfdvtmalcvemlisgklakddaearaklqavldngkaa
evfgrmvaaqkgptdfvenyakylp
>d1azya3 4.34.3.1.1 (336-440) Thymidine phosphorylase {Escherichia coli}
tamltkavyadtegfvsemdtralgmavvamgggrrqasdtidysvgftdmarlgdqvdg
qrplavihakdennwqeaakavkaaikladkapestptvyrrise
>d1azyb1 1.49.2.1.1 (1-70) Thymidine phosphorylase {Escherichia coli}
lflaqeiirkkrdghalsdeeirffingirdntisegqiaalamtiffhdmtmpervslt
mamrdsgtvl
>d1azyb2 3.20.1.1.1 (71-335) Thymidine phosphorylase {Escherichia coli}
dwkslhlngpivdkhstggvgdvtslmlgpmvaacggyipmisgrglghtggtldklesi
pgfdifpddnrfreiikdvgvaiigqtsslapadkrfyatrditatvdsiplitasilak
klaegldalvmdvkvgsgafmptyelsealaeaivgvangagvrttalltdmnqvlassa
gnavevreavqfltgeyrnprlfdvtmalcvemlisgklakddaearaklqavldngkaa
evfgrmvaaqkgptdfvenyakylp
>d1azyb3 4.34.3.1.1 (336-440) Thymidine phosphorylase {Escherichia coli}
tamltkavyadtegfvsemdtralgmavvamgggrrqasdtidysvgftdmarlgdqvdg
qrplavihakdennwqeaakavkaaikladkapestptvyrrise
>d1azza_ 2.41.1.2.9 Crab collagenase {Atlantic sand fiddler crab (Uca pugilator)}
ivggveavpnswphqaalfiddmyfcggslispewiltaahcmdgagfvdvvlgahnire
deatqvtiqstdftvhenynsfvisndiavirlpvpvtltaaiatvglpstdvgvgtvvt
ptgwglpsdsalgisdvlrqvdvpimsnadcdavygivtdgnicidstggkgtcngdsgg
plnyngltygitsfgaaagceagypdaftrvtyfldwiqtqtgitp
>d1azzb_ 2.41.1.2.9 Crab collagenase {Atlantic sand fiddler crab (Uca pugilator)}
ivggveavpnswphqaalfiddmyfcggslispewiltaahcmdgagfvdvvlgahnire
deatqvtiqstdftvhenynsfvisndiavirlpvpvtltaaiatvglpstdvgvgtvvt
ptgwglpsdsalgisdvlrqvdvpimsnadcdavygivtdgnicidstggkgtcngdsgg
plnyngltygitsfgaaagceagypdaftrvtyfldwiqtqtgitp
>d1azzc_ 2.14.1.1.1 Ecotin, trypsin inhibitor {Escherichia coli}
plekiapypqaekgmkrqviqltpqedestlkvelligqtlevdcnlhrlggklenktle
gwgydyyvfdkvsspvstmmacpdgkkekkfvtaylgdagmlrynsklpivvytpdnvdv
kyrvwkaeekidnavvr
>d1azzd_ 2.14.1.1.1 Ecotin, trypsin inhibitor {Escherichia coli}
qplekiapypqaekgmkrqviqltpqedestlkvelligqtlevdcnlhrlggklenktl
egwgydyyvfdkvsspvstmmacpdgkkekkfvtaylgdagmlrynsklpivvytpdnvd
vkyrvwkaeekidnavvr
>d1b02a_ 4.91.1.1.3 Thymidylate synthase {Bacillus subtilis}
mtqfdkqynsiikdiinngisdeefdvrtkwdsdgtpahtlsviskqmrfdnsevpiltt
kkvawktaikellwiwqlksndvndlnmmgvhiwdqwkqedgtighaygfqlgkknrsln
gekvdqvdyllhqlknnpssrrhitmlwnpdeldamaltpcvyetqwyvkhgklhlevra
rsndmalgnpfnvfqynvlqrmiaqvtgyelgeyifnigdchvytrhidnlkiqmereqf
eapelwinpevkdfydftiddfklinykhgdkllfevav
>d1b05a_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b07a_ 2.30.2.1.1 C-Crk, N-terminal SH3 domain {Mouse (Mus musculus)}
saeyvralfdfngndeedlpfkkgdilrirdkpeeqwwnaedsegkrgmipvpyvekyh
>d1b0aa1 3.2.1.7.8 (123-288) Tetrahydrofolate dehydrogenase/cyclohydrolase {Escherichia coli}
fhpynvgrlcqraprlrpctprgivtllerynidtfglnavvigasnivgrpmsmellla
gctttvthrftknlrhhvenadllivavgkpgfipgdwikegaividvginrlengkvvg
dvvfedaakrasyitpvpggvgpmtvatlientlqacveyhdpqde
>d1b0aa2 3.48.1.2.2 (2-122) Tetrahydrofolate dehydrogenase/cyclohydrolase {Escherichia coli}
aakiidgktiaqqvrsevaqkvqariaaglrapglavvlvgsnpasqiyvaskrkaceev
gfvsrsydlpettseaellelidtlnadntidgilvqlplpagidnvkvlerihpdkdvd
g
>d1b0ca_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1b0cb_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1b0cc_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1b0cd_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1b0ce_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1b0d__ 4.2.1.2.1 Lysozyme {Chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1b0e__ 2.41.1.2.15 Elastase {Porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1b0f__ 2.41.1.2.14 Elastase {Human (Homo sapiens)}
ivggrrarphawpfmvslqlagghfcgatliapnfvmsaahcvanvnvravrvvlgahnl
srreptrqvfavqrifedgydpvnllndivilqlngsatinanvqvaqlpaqgrrlgngv
qclamgwgllgrnrgiasvlqelnvtvvtslcrrsnvctlvrgrqagvcfgdsgsplvcn
glihgiasfvrggcasglypdafapvaqfvnwidsiiq
>d1b0ga1 2.1.1.2.5 (182-275) Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-a2.1}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrdgedqtqdtelvetrpagdgtf
qkwaavvvpsgqeqrytchvqheglpkpltlrwe
>d1b0ga2 4.17.1.1.12 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-a2.1}
gshsmryfftsvsrpgrgeprfiavgyvddtqfvrfdsdaasqrmeprapwieqegpeyw
dgetrkvkahsqthrvdlgtlrgyynqseagshtvqrmygcdvgsdwrflrgyhqyaydg
kdyialkedlrswtaadmaaqttkhkweaahvaeqlraylegtcvewlrrylengketlq
r
>d1b0gb1 2.1.1.2.5 Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-a2.1}
miqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskd
wsfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1b0gd1 2.1.1.2.5 (182-275) Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-a2.1}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrdgedqtqdtelvetrpagdgtf
qkwaavvvpsgqeqrytchvqheglpkpltlrwe
>d1b0gd2 4.17.1.1.12 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-a2.1}
gshsmryfftsvsrpgrgeprfiavgyvddtqfvrfdsdaasqrmeprapwieqegpeyw
dgetrkvkahsqthrvdlgtlrgyynqseagshtvqrmygcdvgsdwrflrgyhqyaydg
kdyialkedlrswtaadmaaqttkhkweaahvaeqlraylegtcvewlrrylengketlq
r
>d1b0ge1 2.1.1.2.5 Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-a2.1}
miqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskd
wsfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1b0ha_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b0j_1 3.7.2.1.1 (529-754) Aconitase, C-terminal domain {Pig (Sus scrofa)}
vdvsptsqrlqllepfdkwdgkdledlqilikvkgkcttdhisaagpwlkfrghldnisn
nlligainienrkansvrnavtqefgpvpdtaryykqhgirwvvigdenygegasrehsa
leprhlggraiitksfarihetnlkkqgllpltfadpadynkihpvdkltiqglkdfapg
kplkciikhpngtqetillnhtfnetqiewfragsalnrmkelqqk
>d1b0j_2 3.72.1.1.1 (2-528) Aconitase, first 3 domains {Pig (Sus scrofa)}
rakvamshfepheyirydlleknidivrkrlnrpltlsekivyghlddpanqeiergkty
lrlrpdrvamqdataqmamlqfissglpkvavpstihcdhlieaqlggekdlrrakdinq
evynflatagakygvgfwrpgsgiihqiilenyaypgvlligtdshtpnggglggicigv
ggadavdvmagipwelkcpkvigvkltgslsgwtspkdvilkvagiltvkggtgaiveyh
gpgvdsisctgmaticnmgaeigattsvfpynhrmkkylsktgradianladefkdhlvp
dpgchydqvieinlselkphingpftpdlahpvaevgsvaekegwpldirvgligsctns
syedmgrsaavakqalahglkcksqftitpgseqiratierdgyaqvlrdvggivlanac
gpcigqwdrkdikkgekntivtsynrnftgrndanpethafvtspeivtalaiagtlkfn
petdfltgkdgkkfkleapdadelpraefdpgqdtyqhppkdssgqr
>d1b0k_1 3.7.2.1.1 (529-754) Aconitase, C-terminal domain {Pig (Sus scrofa)}
vdvsptsqrlqllepfdkwdgkdledlqilikvkgkcttdhisaagpwlkfrghldnisn
nlligainienrkansvrnavtqefgpvpdtaryykqhgirwvvigdenygegssrehra
leprhlggraiitksfarihetnlkkqgllpltfadpadynkihpvdkltiqglkdfapg
kplkciikhpngtqetillnhtfnetqiewfragsalnrmkelqqk
>d1b0k_2 3.72.1.1.1 (2-528) Aconitase, first 3 domains {Pig (Sus scrofa)}
rakvamshfepheyirydlleknidivrkrlnrpltlsekivyghlddpanqeiergkty
lrlrpdrvamqdataqmamlqfissglpkvavpstihcdhlieaqlggekdlrrakdinq
evynflatagakygvgfwrpgsgiihqiilenyaypgvlligtdshtpnggglggicigv
ggadavdvmagipwelkcpkvigvkltgslsgwtspkdvilkvagiltvkggtgaiveyh
gpgvdsisctgmaticnmgaeigattsvfpynhrmkkylsktgradianladefkdhlvp
dpgchydqvieinlselkphingpftpdlahpvaevgsvaekegwpldirvgligsctns
syedmgrsaavakqalahglkcksqftitpgseqiratierdgyaqvlrdvggivlanac
gpcigqwdrkdikkgekntivtsynrnftgrndanpethafvtspeivtalaiagtlkfn
petdfltgkdgkkfkleapdadelpraefdpgqdtyqhppkdssgqr
>d1b0l_1 3.84.1.2.1 (1-334) Lactoferrin {Human (Homo sapiens)}
grrrsvqwctvsqpeatkcfqwqrnmrkvrgppvscikrdspiqciqaiaenradavtld
ggfiyeaglapyklrpvaaevygterqprthyyavavvkkggsfqlnelqglkschtglr
rtagwnvpigtlrpflnwtgppepieaavarffsascvpgadkgqfpnlcrlcagtgenk
cafssqepyfsysgafkclrdgagdvafirestvfedlsdeaerdeyellcpdntrkpvd
kfkdchlarvpshavvarsvngkedaiwnllrqaqekfgkdkspkfqlfgspsgqkdllf
kdsaigfsrvppridsglylgsgyftaiqnlrks
>d1b0l_2 3.84.1.2.1 (335-691) Lactoferrin {Human (Homo sapiens)}
eeevaarrarvvwcavgeqelrkcnqwsglsegsvtcssasttedcialvlkgeadamsl
dggyvytagkcglvpvlaenyksqqssdpdpncvdrpvegylavavvrrsdtsltwnsvk
gkkschtavdrtagwnipmgllfnqtgsckfdeyfsqscapgsdprsnlcalcigdeqge
nkcvpnsneryygytgafrclaenagdvafvkdvtvlqntdgnnneawakdlkladfall
cldgkrkpvtearschlamapnhavvsrmdkverlkqvllhqqakfgrngsdcpdkfclf
qsetknllfndnteclarlhgkttyekylgpqyvagitnlkkcstsplleaceflrk
>d1b0m_1 3.7.2.1.1 (529-754) Aconitase, C-terminal domain {Pig (Sus scrofa)}
vdvsptsqrlqllepfdkwdgkdledlqilikvkgkcttdhisaagpwlkfrghldnisn
nlligainienrkansvrnavtqefgpvpdtaryykqhgirwvvigdenygegssrehra
leprhlggraiitksfarihetnlkkqgllpltfadpadynkihpvdkltiqglkdfapg
kplkciikhpngtqetillnhtfnetqiewfragsalnrmkelqqk
>d1b0m_2 3.72.1.1.1 (2-528) Aconitase, first 3 domains {Pig (Sus scrofa)}
rakvamshfepheyirydlleknidivrkrlnrpltlsekivyghlddpanqeiergkty
lrlrpdrvamqdataqmamlqfissglpkvavpstihcdhlieaqlggekdlrrakdinq
evynflatagakygvgfwrpgsgiihqiilenyaypgvlligtdshtpnggglggicigv
ggadavdvmagipwelkcpkvigvkltgslsgwtspkdvilkvagiltvkggtgaiveyh
gpgvdsisctgmaticnmgaeigattsvfpynhrmkkylsktgradianladefkdhlvp
dpgchydqvieinlselkphingpftpdlahpvaevgsvaekegwpldirvgligsctns
syedmgrsaavakqalahglkcksqftitpgseqiratierdgyaqvlrdvggivlanac
gpcigqwdrkdikkgekntivtsynrnftgrndanpethafvtspeivtalaiagtlkfn
petdfltgkdgkkfkleapdadelpraefdpgqdtyqhppkdssgqr
>d1b0na1 1.35.1.1.1 (74-108) SinR repressor (dimerisation domain)-SinI anti-repressor complex {Bacillus subtilis}
ldseweklvrdamtsgvskkqfrefldyqkwrksq
>d1b0na2 1.36.1.3.1 (1-68) SinR repressor, DNA-binding domain {Bacillus subtilis}
migqrikqyrkekgyslselaekagvaksylssiernlqtnpsiqflekvsavldvsvht
lldekhet
>d1b0nb1 1.35.1.1.1 SinR repressor (dimerisation domain)-SinI anti-repressor complex {Bacillus subtilis}
feldqewvelmveakeanispeeirkyllln
>d1b0o__ 2.53.1.1.8 beta-Lactoglobulin {Bovine (Bos taurus)}
ivtqtmkgldiqkvagtwyslamaasdislldaqsaplrvyveelkptpegdleillqkw
engecaqkkiiaektkipavfkidalnenkvlvldtdykkyllfcmensaepeqslacqc
lvrtpevddealekfdkalkalpmhirlsfnptqleeqchi
>d1b0pa1 3.29.1.4.1 (2-258) Pyruvate-ferredoxin oxidoreductase, PFOR, domains I and VI {Desulfovibrio africanus}
gkkmmttdgntatahvayamsevaaiypitpsstmgeeaddwaaqgrknifgqtltirem
qseagaagavhgalaagaltttftasqglllmipnmykisgellpgvfhvtaraiaahal
sifgdhqdiyaarqtgfamlasssvqeahdmalvahlaaiesnvpfmhffdgfrtsheiq
kievldyadmaslvnqkalaefraksmnpehphvrgtaqnpdiyfqgreaanpyylkvpg
ivaeymqkvasltgrsy
>d1b0pa2 3.29.1.4.1 (786-1232) Pyruvate-ferredoxin oxidoreductase, PFOR, domains I and VI {Desulfovibrio africanus}
vksevlprdslkgsqfqeplmefsgacsgcgetpyvrvitqlfgermfianatgcssiwg
asapsmpyktnrlgqgpawgnslfedaaeygfgmnmsmfarrthladlaakalesdasgd
vkealqgwlagkndpikskeygdklkkllagqkdgllgqiaamsdlytkksvwifggdgw
aydigyggldhvlasgedvnvfvmdtevysntggqsskatptgavakfaaagkrtgkkdl
armvmtygyvyvatvsmgyskqqflkvlkeaesfpgpslviayatcinqglrkgmgksqd
vmntavksgywplfrydprlaaqgknpfqldskapdgsveeflmaqnrfavldrsfpeda
krlraqvaheldvrfkelehmaatnifesfapaggkadgsvdfgegaefctrddtpmmar
pdsgeacdqnragtseqqgdlskrtkk
>d1b0pa3 3.39.1.3.1 (259-415) Pyruvate-ferredoxin oxidoreductase, PFOR, domain II {Desulfovibrio africanus}
klfdyvgapdaervivsmgsscetieevinhlaakgekiglikvrlyrpfvseaffaalp
asakvitvldrtkepgapgdplyldvcsafvergeampkilagryglgskefspamvksv
ydnmsgakknhftvgieddvtgtslpvdnafadttpk
>d1b0pa4 3.54.1.1.1 (416-668) Pyruvate-ferredoxin oxidoreductase, PFOR, domain III {Desulfovibrio africanus}
gtiqcqfwglgadgtvgankqaikiigdntdlfaqgyfsydskksggitishlrfgekpi
qstylvnradyvachnpayvgiydilegikdggtfvlnspwssledmdkhlpsgikrtia
nkklkfynidavkiatdvglggrinmimqtaffklagvlpfekavdllkksihkaygkkg
ekivkmntdavdqavtslqefkypdswkdapaetkaepmtneffknvvkpiltqqgdklp
vsafeadgrfplg
>d1b0pa5 4.47.1.5.3 (669-785) Pyruvate-ferredoxin oxidoreductase, PFOR, domain V {Desulfovibrio africanus}
tsqfekrgvainvpqwvpenciqcnqcafvcphsailpvlakeeelvgapanftaleakg
kelkgykfriqintldcmgcgncadicppkekalvmqpldtqrdaqvpnleyaarip
>d1b0pb1 3.29.1.4.1 (2-258) Pyruvate-ferredoxin oxidoreductase, PFOR, domains I and VI {Desulfovibrio africanus}
gkkmmttdgntatahvayamsevaaiypitpsstmgeeaddwaaqgrknifgqtltirem
qseagaagavhgalaagaltttftasqglllmipnmykisgellpgvfhvtaraiaahal
sifgdhqdiyaarqtgfamlasssvqeahdmalvahlaaiesnvpfmhffdgfrtsheiq
kievldyadmaslvnqkalaefraksmnpehphvrgtaqnpdiyfqgreaanpyylkvpg
ivaeymqkvasltgrsy
>d1b0pb2 3.29.1.4.1 (786-1232) Pyruvate-ferredoxin oxidoreductase, PFOR, domains I and VI {Desulfovibrio africanus}
vksevlprdslkgsqfqeplmefsgacsgcgetpyvrvitqlfgermfianatgcssiwg
asapsmpyktnrlgqgpawgnslfedaaeygfgmnmsmfarrthladlaakalesdasgd
vkealqgwlagkndpikskeygdklkkllagqkdgllgqiaamsdlytkksvwifggdgw
aydigyggldhvlasgedvnvfvmdtevysntggqsskatptgavakfaaagkrtgkkdl
armvmtygyvyvatvsmgyskqqflkvlkeaesfpgpslviayatcinqglrkgmgksqd
vmntavksgywplfrydprlaaqgknpfqldskapdgsveeflmaqnrfavldrsfpeda
krlraqvaheldvrfkelehmaatnifesfapaggkadgsvdfgegaefctrddtpmmar
pdsgeacdqnragtseqqgdlskrtkk
>d1b0pb3 3.39.1.3.1 (259-415) Pyruvate-ferredoxin oxidoreductase, PFOR, domain II {Desulfovibrio africanus}
klfdyvgapdaervivsmgsscetieevinhlaakgekiglikvrlyrpfvseaffaalp
asakvitvldrtkepgapgdplyldvcsafvergeampkilagryglgskefspamvksv
ydnmsgakknhftvgieddvtgtslpvdnafadttpk
>d1b0pb4 3.54.1.1.1 (416-668) Pyruvate-ferredoxin oxidoreductase, PFOR, domain III {Desulfovibrio africanus}
gtiqcqfwglgadgtvgankqaikiigdntdlfaqgyfsydskksggitishlrfgekpi
qstylvnradyvachnpayvgiydilegikdggtfvlnspwssledmdkhlpsgikrtia
nkklkfynidavkiatdvglggrinmimqtaffklagvlpfekavdllkksihkaygkkg
ekivkmntdavdqavtslqefkypdswkdapaetkaepmtneffknvvkpiltqqgdklp
vsafeadgrfplg
>d1b0pb5 4.47.1.5.3 (669-785) Pyruvate-ferredoxin oxidoreductase, PFOR, domain V {Desulfovibrio africanus}
tsqfekrgvainvpqwvpenciqcnqcafvcphsailpvlakeeelvgapanftaleakg
kelkgykfriqintldcmgcgncadicppkekalvmqpldtqrdaqvpnleyaarip
>d1b0ra1 2.1.1.2.4 (182-275) Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-a0201}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrqdtelvetrpagdgtfqkwaav
vvpsgqeqrytchvqheglpkpltlrwe
>d1b0ra2 4.17.1.1.11 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-a0201}
gshsmryfftsvsrpgrgeprfiavgyvddtqfvrfdsdaasqrmeprapwieqegpeyw
dgetrkvkahsqthrvdlgtlrgyynqseagshtvqrmygcdvgsdwrflrgyhqyaydg
kdyialkedlrswtaadmaaqttkhkweaahvaeqlraylegtcvewlrrylengketlq
r
>d1b0rb1 2.1.1.2.4 Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-a0201}
miqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskd
wsfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1b0t__ 4.47.1.2.1 Ferredoxin {Azotobacter vinelandii}
afvvtdncikckycdcvevcpvdcfyegpnflvihpdecidcalcepecpaqaifsedev
pedmqefiqlnaelaevwpnitekkdplpdaedwdgvkgklqhler
>d1b0wa_ 2.1.1.1.147 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (kappa) dimer BRE (human)}
diqmtqspsslsasvgdrvtitcqasqdisdyliwyqqklgkapnlliydastletgvps
rfsgsgsgteytftisslqpediatyycqqyddlpytfgqgtkveikr
>d1b0wb_ 2.1.1.1.147 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (kappa) dimer BRE (human)}
diqmtqspsslsasvgdrvtitcqasqdisdyliwyqqklgkapnlliydastletgvps
rfsgsgsgteytftisslqpediatyycqqyddlpytfgqgtkveikr
>d1b0wc_ 2.1.1.1.147 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (kappa) dimer BRE (human)}
diqmtqspsslsasvgdrvtitcqasqdisdyliwyqqklgkapnlliydastletgvps
rfsgsgsgteytftisslqpediatyycqqyddlpytfgqgtkveikr
>d1b0xa_ 1.61.1.2.1 EphA4 receptor tyrosine kinases {Mouse (Mus musculus)}
fsavvsvgdwlqaikmdrykdnftaagyttleavvhmsqddlarigitaithqnkilssv
qamrtqmqqmhg
>d1b0y__ 7.30.1.1.2 HIPIP (high potential iron protein) {Cromatium vinosum}
sapanavaaddataialkynqdatkservaaarpglppeeqqcancqfmqadaagatdew
kgcqlfpgklinvngwcaswtlkag
>d1b10__ 4.6.1.1.2 Prion protein domain {Golden hamster (Mesocricetus auratus)}
lggymlgsamsrpmmhfgndwedryyrenmnrypnqvyyrpvdqynnqnnfvhdcvniti
kqhtvttttkgenftetdikimervveqmcttqyqkesqayydg
>d1b11__ 2.44.1.1.2 Feline immunodeficiency virus (FIV) protease {Feline (Felis catus), immunodeficiency virus}
vgttttlekrpeilifvngypikflldtgaditilnrrdfqvknsiengrqnmigvgggk
rgtnyinvhleirdenyktqcifgnvcvlednsliqpllgrdnmikfnirlvm
>d1b13a_ 7.35.4.1.4 Rubredoxin {Clostridium pasteurianum}
mkkytctvcayiynpedgdpdngvnpgtdfkdipddwvcplcgvgkdqfeevee
>d1b1a__ 3.16.5.1.3 Glutamate mutase, small subunit {Clostridium cochlearium}
mekktivlgvigsdchavgnkildhaftnagfnvvnigvlspqevfikaaietkadaill
sslygqgeidckglrqkcdeaglegillyvggnivvgkqhwpdvekrfkdmgydrvyapg
tppevgiadlkkdlnie
>d1b1ea_ 4.5.1.1.7 Angiogenin {Human (Homo sapiens)}
qdnsrythfltqhydakpqgrddrycesimrrrgltspcqdintfihgnkrsikaicenk
ngnphrenlriskssfqvttcklhggspwppcqyratagfrnvvvacenglpvhldqsif
rrp
>d1b1ga_ 1.42.1.1.1 Calbindin D9K {Bovine (Bos taurus)}
kspeelkgifekyaakegdpnqlskeelklllqtefpsllkggstldelfeeldkngdge
vsfeefqvlvkkisq
>d1b1ha_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b1ia_ 4.5.1.1.7 Angiogenin {Human (Homo sapiens)}
dnsrythfltqhydakpqgrddrycesimrrrgltspckdintfihgnkrsikaicenkn
gnphrenlriskssfqvttcklhggspwppcqyratagfrnvvvacenglpvhldqsifr
rp
>d1b1ja_ 4.5.1.1.7 Angiogenin {Human (Homo sapiens)}
qdnsrythfltqaydakpqgrddrycesimrrrgltspckdintfihgnkrsikaicenk
ngnphrenlriskssfqvttcklhggspwppcqyratagfrnvvvacenglpvhldqsif
rrp
>d1b1u__ 1.54.1.2.2 Trypsin/alpha-amylase inhibitor RBI {Ragi (Elucine coracana gaertneri), seeds}
gtscipgmaiphnpldscrwyvstrtcgvgprlatqemkarccrqleaipaycrceavri
lmdgvvtpsgqhegrllqdlpgcprqvqrafapklvtevecnlatihggpfclsllg
>d1b1xa1 3.84.1.2.4 (1-333) Lactoferrin {Horse (Equus caballus)}
aprksvrwctispaeaakcakfqrnmkkvrgpsvscirktssfeciqaiaankadavtld
gglvyeaglhpyklrpvaaevyqtrgkpqtryyavavvkkgsgfqlnqlqgvkschtglg
rsagwnipigtlrpylnwtgppeplqkavanffsascvpcadgkqypnlcrlcagteadk
cacssqepyfgysgafkclengagdvafvkdstvfenlpdeaerdkyellcpdntrkpvd
afkechlarvpshavvarsvdgredliwkllhraqeefgrnkssafqlfgstpgeqdllf
kdsalgfvripsqidsglylganyltatqnlre
>d1b1xa2 3.84.1.2.4 (334-689) Lactoferrin {Horse (Equus caballus)}
taaevaarrervvwcavgpeeerkckqwsdvsnrkvacasastteecialvlkgeadaln
ldggfiyvagkcglvpvlaenqksqnsnapdcvhrppegylavavvrksdadltwnslsg
kkschtgvgrtaawnipmgllfnqtgsckfdkffsqscapgadpqsslcalcvgnnenen
kcmpnseeryygytgafrclaekagdvafvkdvtvlqntdgknsepwakdlkqedfellc
ldgtrkpvaeaeschlarapnhavvsqsdraqhlkkvlflqqdqfggngpdcpgkfclfk
setknllfndnteclaelqgkttyeqylgseyvtsitnlrrcsssplleacaflra
>d1b1y__ 3.1.7.2.2 beta-Amylase {Barley (Hordeum vulgare)}
mkgnyvqvyvmlpldavsvnnrfekgdelraqlrklveagvdgvmvdvwwglvegkgpka
ydwsaykqlfelvqkaglklqaimsfhqcggnvgdavnipipqwvrdvgtrdpdifytdg
hgtrnieyltlgvdnqplfhgrsavqmyadymtsfrenmkdfldagvivdievglgpage
lrypsypqshgwsfpgigeficydkylqadfkaaaaavghpewefpndagqyndtpertq
ffrdngtylsekgrfflawysnnlikhgdrildeankvflgykvqlaikiagvhwwykvp
shaaeltagyynlhdrdgyrtiarmlkrhrasinftcaemrdseqppdamsapeelvqqv
lsagwreglnvscenalprydptayntilrnarphginqsgppehklfgftylrlsnqlv
egqnyvnfktfvdrmhanlprdpyvdpmaplprsgpeisiemilqaaqpklqpfpfqeht
dlpvgptggmggqaegptcg
>d1b20a_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
qvintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnreg
klpgksgstwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1b20b_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgstwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1b20c_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
qvintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnreg
klpgksgstwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1b21a_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
qvintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnreg
klpgksgstwreadinytsgfrnsdrilyssnwliykttdhyqtftkir
>d1b21b_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgstwreadinytsgfrnsdrilyssnwliykttdhyqtftkir
>d1b21c_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
qvintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnreg
klpgksgstwreadinytsgfrnsdrilyssnwliykttdhyqtftkir
>d1b23p1 2.38.3.1.2 (213-312) Elongation factor Tu (EF-Tu), domain 2 {Thermus aquaticus}
pvrdvdkpflmpvedvftitgrgtvatgriergkvkvgdeveivglapetrktvvtgvem
hrktlqegiagdnvglllrgvsreevergqvlakpgsitp
>d1b23p2 2.39.1.1.2 (313-405) Elongation factor Tu (EF-Tu), C-terminal domain {Thermus aquaticus}
htkfeasvyilkkeeggrhtgfftgyrpqfyfrttdvtgvvrlpqgvemvmpgdnvtftv
elikpvaleeglrfaireggrtvgagvvtkile
>d1b23p3 3.30.1.6.15 (1-212) Elongation factor Tu (EF-Tu), N-terminal (G) domain {Thermus aquaticus}
akgefirtkphvnvgtighvdhgkttltaaltyvaaaenpnvevkdygdidkapeerarg
itintahveyetakrhyshvdcpghadyiknmitgaaqmdgailvvsaadgpmpqtrehi
llarqvgvpyivvfmnkvdmvddpelldlvemevrdllnqyefpgdevpvirgsallale
emhknpktkrgenewvdkiwelldaideyipt
>d1b24a1 4.74.2.1.2 (7-99) I-dmoI {Desulfurococcus mobilis}
vsgisayllgliigdgglyklkykgnrseyrvvitqksenlikqhiaplxqflidelnvk
skiqivkgdtryelrvsskklyyyfanxlerir
>d1b24a2 4.74.2.1.2 (100-179) I-dmoI {Desulfurococcus mobilis}
lfnxreqiafikglyvaegdktlkrlriwnknkalleivsrwlnnlgvrntihlddhrhg
vyvlnislrdrikfvhtils
>d1b25a1 1.104.1.1.2 (211-619) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
dkeelkklsqeayneilnspgypfwkrqgtmaavewcntnyalptrnfsdgyfefarsid
gytmegmkvqqrgcpycnmpcgnvvldaegqeseldyenvallgsnlgigklnevsvlnr
iademgmdtislgvsiahvmeavergilkegptfgdfkgakqlaldiayrkgelgnlaae
gvkamaeklgthdfamhvkglevsgyncyiypamalaygtsaigahhkeawviaweigta
piegekaekveykisydpikaqkvvelqrlrgglfemltacrlpwvevglsldyypkllk
aitgvtytwddlykaadrvysliraywvrefngkwdrkmdyppkrwfteglksgphkgeh
ldekkydellseyyrirgwdergipkketlkeldldfvipelekvtnle
>d1b25a2 4.123.1.1.2 (1-210) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
mygwwgrilrvnlttgevkvqeypeevakkfiggrglaawilwneargveplspenklif
aagpfnglptpsggklvvaakspltggygdgnlgtmasvhlrragydalvvegkakkpvy
iyieddnvsilsaeglwgkttfeterelkeihgknvgvltigpagenlvkyavvisqegr
aagrpgmgavmgskklkavvirgtkeipva
>d1b25b1 1.104.1.1.2 (211-619) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
dkeelkklsqeayneilnspgypfwkrqgtmaavewcntnyalptrnfsdgyfefarsid
gytmegmkvqqrgcpycnmpcgnvvldaegqeseldyenvallgsnlgigklnevsvlnr
iademgmdtislgvsiahvmeavergilkegptfgdfkgakqlaldiayrkgelgnlaae
gvkamaeklgthdfamhvkglevsgyncyiypamalaygtsaigahhkeawviaweigta
piegekaekveykisydpikaqkvvelqrlrgglfemltacrlpwvevglsldyypkllk
aitgvtytwddlykaadrvysliraywvrefngkwdrkmdyppkrwfteglksgphkgeh
ldekkydellseyyrirgwdergipkketlkeldldfvipelekvtnle
>d1b25b2 4.123.1.1.2 (1-210) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
mygwwgrilrvnlttgevkvqeypeevakkfiggrglaawilwneargveplspenklif
aagpfnglptpsggklvvaakspltggygdgnlgtmasvhlrragydalvvegkakkpvy
iyieddnvsilsaeglwgkttfeterelkeihgknvgvltigpagenlvkyavvisqegr
aagrpgmgavmgskklkavvirgtkeipva
>d1b25c1 1.104.1.1.2 (211-619) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
dkeelkklsqeayneilnspgypfwkrqgtmaavewcntnyalptrnfsdgyfefarsid
gytmegmkvqqrgcpycnmpcgnvvldaegqeseldyenvallgsnlgigklnevsvlnr
iademgmdtislgvsiahvmeavergilkegptfgdfkgakqlaldiayrkgelgnlaae
gvkamaeklgthdfamhvkglevsgyncyiypamalaygtsaigahhkeawviaweigta
piegekaekveykisydpikaqkvvelqrlrgglfemltacrlpwvevglsldyypkllk
aitgvtytwddlykaadrvysliraywvrefngkwdrkmdyppkrwfteglksgphkgeh
ldekkydellseyyrirgwdergipkketlkeldldfvipelekvtnle
>d1b25c2 4.123.1.1.2 (1-210) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
mygwwgrilrvnlttgevkvqeypeevakkfiggrglaawilwneargveplspenklif
aagpfnglptpsggklvvaakspltggygdgnlgtmasvhlrragydalvvegkakkpvy
iyieddnvsilsaeglwgkttfeterelkeihgknvgvltigpagenlvkyavvisqegr
aagrpgmgavmgskklkavvirgtkeipva
>d1b25d1 1.104.1.1.2 (211-619) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
dkeelkklsqeayneilnspgypfwkrqgtmaavewcntnyalptrnfsdgyfefarsid
gytmegmkvqqrgcpycnmpcgnvvldaegqeseldyenvallgsnlgigklnevsvlnr
iademgmdtislgvsiahvmeavergilkegptfgdfkgakqlaldiayrkgelgnlaae
gvkamaeklgthdfamhvkglevsgyncyiypamalaygtsaigahhkeawviaweigta
piegekaekveykisydpikaqkvvelqrlrgglfemltacrlpwvevglsldyypkllk
aitgvtytwddlykaadrvysliraywvrefngkwdrkmdyppkrwfteglksgphkgeh
ldekkydellseyyrirgwdergipkketlkeldldfvipelekvtnle
>d1b25d2 4.123.1.1.2 (1-210) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
mygwwgrilrvnlttgevkvqeypeevakkfiggrglaawilwneargveplspenklif
aagpfnglptpsggklvvaakspltggygdgnlgtmasvhlrragydalvvegkakkpvy
iyieddnvsilsaeglwgkttfeterelkeihgknvgvltigpagenlvkyavvisqegr
aagrpgmgavmgskklkavvirgtkeipva
>d1b27a_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
aqvintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnre
gklpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1b27b_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
aqvintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnre
gklpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1b27c_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1b27d_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
mkkavingeqirsisdlhqtlkkelalpeyygenldalwdaltgwveyplvlewrqfeqs
kqltengaesvlqvfreakaegaditiils
>d1b27e_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdaltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegaditiils
>d1b27f_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdaltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegaditiils
>d1b2ha_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b2ja_ 7.35.4.1.4 Rubredoxin {Clostridium pasteurianum}
mkkytctvcgyiynpedgdpdngvnpgtdfkdipddwvcplcavgkdqfeevee
>d1b2ma_ 4.1.1.1.3 RNase T1 {Aspergillus oryzae}
acdytcgsncysssdvstaqaagyqlhedgetvgsnsyphkynnyegfdfsvsspyyewp
ilssgdvysggspgadrvvfnennqlagvithtgasgnnfvect
>d1b2mb_ 4.1.1.1.3 RNase T1 {Aspergillus oryzae}
acdytcgsncysssdvstaqaagyqlhedgetvgsnsyphkynnyegfdfsvsspyyewp
ilssgdvysggspgadrvvfnennqlagvithtgasgnnfvect
>d1b2na_ 2.61.1.1.1 Methanol dehydrogenase, heavy chain {Methylophilus methylotrophus, w3a1}
dadldkqvntagawpiatggyysqhnsplaqinksnvknvkaawsfstgvlnghegaplv
igdmmyvhsafpnntyalnlndpgkivwqhkpkqdastkavmccdvvdrglaygagqivk
kqanghllaldaktgkinwevevcdpkvgstltqapfvakdtvlmgcsgaelgvrgavna
fdlktgelkwrafatgsddsvrlakdfnsanphygqfglgtktwegdawkigggtnwgwy
aydpklnlfyygsgnpapwnetmrpgdnkwtmtiwgrdldtgmakwgyqktphdewdfag
vnqmvltdqpvngkmtpllshidrngilytlnrengnlivaekvdpavnvfkkvdlktgt
pvrdpefatrmdhkgtnicpsamgfhnqgvdsydpesrtlyaglnhicmdwepfmlpyra
gqffvgatlamypgpngptkkemgqirafdlttgkakwtkwekfaawggtlytkgglvwy
atldgylkaldnkdgkelwnfkmpsggigspmtysfkgkqyigsmygvggwpgvglvfdl
tdpsaglgavgafrelqnhtqmggglmvfsl
>d1b2nb_ 1.125.1.1.1 Methanol dehydrogenase, light chain {Methylophilus w3a1}
ydgqnckepgncwenkpgypekiagskydpkhdpvelnkqeesikamdarnakrian
>d1b2nc_ 2.61.1.1.1 Methanol dehydrogenase, heavy chain {Methylophilus methylotrophus, w3a1}
dadldkqvntagawpiatggyysqhnsplaqinksnvknvkaawsfstgvlnghegaplv
igdmmyvhsafpnntyalnlndpgkivwqhkpkqdastkavmccdvvdrglaygagqivk
kqanghllaldaktgkinwevevcdpkvgstltqapfvakdtvlmgcsgaelgvrgavna
fdlktgelkwrafatgsddsvrlakdfnsanphygqfglgtktwegdawkigggtnwgwy
aydpklnlfyygsgnpapwnetmrpgdnkwtmtiwgrdldtgmakwgyqktphdewdfag
vnqmvltdqpvngkmtpllshidrngilytlnrengnlivaekvdpavnvfkkvdlktgt
pvrdpefatrmdhkgtnicpsamgfhnqgvdsydpesrtlyaglnhicmdwepfmlpyra
gqffvgatlamypgpngptkkemgqirafdlttgkakwtkwekfaawggtlytkgglvwy
atldgylkaldnkdgkelwnfkmpsggigspmtysfkgkqyigsmygvggwpgvglvfdl
tdpsaglgavgafrelqnhtqmggglmvfsl
>d1b2nd_ 1.125.1.1.1 Methanol dehydrogenase, light chain {Methylophilus w3a1}
ydgqnckepgncwenkpgypekiagskydpkhdpvelnkqeesikamdarnakrian
>d1b2oa_ 7.35.4.1.4 Rubredoxin {Clostridium pasteurianum}
mkkytctvcvyiynpedgdpdngvnpgtdfkdipddwvcplcavgkdqfeevee
>d1b2ob_ 7.35.4.1.4 Rubredoxin {Clostridium pasteurianum}
mkkytctvcvyiynpedgdpdngvnpgtdfkdipddwvcplcavgkdqfeevee
>d1b2pa_ 2.69.1.1.4 Lectin (agglutinin) {Bluebell (Scilla campanulata)}
nniifskqpddnhpqilhatesleilfgthvyrfimqtdcnlvlydnnnpiwatntgglg
ngcravlqpdgvlvvitnenvtvwqspvagkaghyvlvlqpdrnvviygdalwatqtvr
>d1b2pb_ 2.69.1.1.4 Lectin (agglutinin) {Bluebell (Scilla campanulata)}
nniifskqpddnhpqilhatesleilfgthvyrfimqtdcnlvlydnnnpiwatntgglg
ngcravlqpdgvlvvitnenvtvwqspvagkaghyvlvlqpdrnvviygdalwatqtvr
>d1b2sa_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
aqvintfdgvadylqtyhklpdnyitaseaqalgwvaskgnladvapgksiggdifsnre
gklpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1b2sb_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
aqvintfdgvadylqtyhklpdnyitaseaqalgwvaskgnladvapgksiggdifsnre
gklpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1b2sc_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
aqvintfdgvadylqtyhklpdnyitaseaqalgwvaskgnladvapgksiggdifsnre
gklpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1b2sd_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
mkkavingeqirsisdlhqtlkkelalpeyygenldalwdclagwveyplvlewrqfeqs
kqltengaesvlqvfreakaegcditiils
>d1b2se_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
mkkavingeqirsisdlhqtlkkelalpeyygenldalwdclagwveyplvlewrqfeqs
kqltengaesvlqvfreakaegcditiils
>d1b2sf_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdclagwveyplvlewrqfeqsk
qltengaesvlqvfreakaegcditiils
>d1b2ua_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
aqvintfdgvadylqtyhklpdnyitaseaqalgwvaskgnladvapgksiggdifsnre
gklpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1b2ub_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
aqvintfdgvadylqtyhklpdnyitaseaqalgwvaskgnladvapgksiggdifsnre
gklpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1b2uc_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitaseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1b2ud_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
mkkavingeqirsisdlhqtlkkelalpeyygenlaalwdcltgwveyplvlewrqfeqs
kqltengaesvlqvfreakaegcditiils
>d1b2ue_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenlaalwdcltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegcditiils
>d1b2uf_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenlaalwdcltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegcditiils
>d1b2va_ 4.29.1.1.1 Heme-binding protein A (HasA) {Serratia marcescens}
afsvnydssfggysihdylgqwastfgdvnhtngnvtdansggfyggslsgsqyaissta
nqvtafvaggnltytlfnepahtlygqldslsfgdglsggdtspysiqvpdvsfgglnls
slqaqghdgvvhqvvyglmsgdtgaletalngilddyglsvnstfdqvaaata
>d1b2wh1 2.1.1.1.120 (2-117) Immunoglobulin (variable domains of L and H chains) {Humanized and chimeric anti-gamma-interferon Fab}
vqlvqsgggvvqpgrslklsclasgyiftsswinwvkqrpgrglewigridpsdgevhyn
qdfkdrftisrdkskntlylqmnslrpedtavyycargflpwfadwgqgtlvtvss
>d1b2wh2 2.1.1.2.118 (118-220) Immunoglobulin (constant domains of L and H chains) {Humanized and chimeric anti-gamma-interferon Fab}
astkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkvepksc
>d1b2wl1 2.1.1.1.120 (1-107) Immunoglobulin (variable domains of L and H chains) {Humanized and chimeric anti-gamma-interferon Fab}
diqmtqspstlsasvgdrvtitckasenvdtyvswyqqkpgkapklliygasnrytgvps
rfsgsgsgtdftltisslqpddfatyycgqsynypftfgqgtkvevk
>d1b2wl2 2.1.1.2.118 (108-214) Immunoglobulin (constant domains of L and H chains) {Humanized and chimeric anti-gamma-interferon Fab}
rtvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqd
skdstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1b2xa_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
qvintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnreg
klpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1b2xb_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1b2xc_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1b2za_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssnwliykttdhyqtftkir
>d1b2zb_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssnwliykttdhyqtftkir
>d1b2zc_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
intfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregkl
pgksgrtwreadinytsgfrnsdrilyssnwliykttdhyqtftkir
>d1b30a_ 3.1.7.3.15 Xylanase A, catalytic core {Penicillium simplicissimum}
asvsidakfkahgkkylgtigdqytltkntknpaiikadfgqltpensmkwdatepnrgq
ftfsgsdylvnfaqsngklirghtlvwhsqlpgwvssitdkntlisvlknhittvmtryk
gkiyawdvlneifnedgslrnsvfynvigedyvriafetarsvdpnaklyindynldsag
yskvngmvshvkkwlaagipidgigsqthlgagagsavagalnalasagtkeiaiteldi
agasstdyvnvvnaclnqakcvgitvwgvadpdswrsssspllfdgnynpkaaynaiana
l
>d1b31a_ 3.1.7.3.15 Xylanase A, catalytic core {Penicillium simplicissimum}
asvsidakfkahgkkylgtigdqytltkntknpaiikadfgqltpensmkwdatepnrgq
ftfsgsdylvnfaqsngklirghtlvwhsqlpgwvssitdkntlisvlknhittvmtryk
gkiyawdvlneifnedgslrnsvfynvigedyvriafetarsvdpnaklyindynldsag
yskvngmvshvkkwlaagipidgigsqthlgagagsavagalnalasagtkeiaiteldi
agasstdyvnvvnaclnqakcvgitvwgvadpdswrsssspllfdgnynpkaaynaiana
l
>d1b32a_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b33a_ 1.1.1.2.4 Allophycocyanin {Cyanobacterium (Mastigocladus laminosus)}
sivtksivnadaearylspgeldriksfvssgekrlriaqiltdnrerivkqagdqlfqk
rpdvvspggnaygqemtatclrdldyylrlitygivagdvtpieeigivgvremykslgt
pidavaagvsamknvassilsaedaaeagayfdyvagala
>d1b33b_ 1.1.1.2.4 Allophycocyanin {Cyanobacterium (Mastigocladus laminosus)}
mqdaitavinssdvqgkyldtaaleklksyfstgelrvraattiaanaaaivkeavaksl
lysditrpggnmyttrryaacirdldyylryatyamlagdpsildervlnglketynslg
vpisatvqaiqamkevtaslvgpdagkemgvyfdyicsgls
>d1b33c_ 1.1.1.2.4 Allophycocyanin {Cyanobacterium (Mastigocladus laminosus)}
sivtksivnadaearylspgeldriksfvssgekrlriaqiltdnrerivkqagdqlfqk
rpdvvspggnaygqemtatclrdldyylrlitygivagdvtpieeigivgvremykslgt
pidavaagvsamknvassilsaedaaeagayfdyvagala
>d1b33d_ 1.1.1.2.4 Allophycocyanin {Cyanobacterium (Mastigocladus laminosus)}
mqdaitavinssdvqgkyldtaaleklksyfstgelrvraattiaanaaaivkeavaksl
lysditrpggnmyttrryaacirdldyylryatyamlagdpsildervlnglketynslg
vpisatvqaiqamkevtaslvgpdagkemgvyfdyicsgls
>d1b33e_ 1.1.1.2.4 Allophycocyanin {Cyanobacterium (Mastigocladus laminosus)}
sivtksivnadaearylspgeldriksfvssgekrlriaqiltdnrerivkqagdqlfqk
rpdvvspggnaygqemtatclrdldyylrlitygivagdvtpieeigivgvremykslgt
pidavaagvsamknvassilsaedaaeagayfdyvagala
>d1b33f_ 1.1.1.2.4 Allophycocyanin {Cyanobacterium (Mastigocladus laminosus)}
mqdaitavinssdvqgkyldtaaleklksyfstgelrvraattiaanaaaivkeavaksl
lysditrpggnmyttrryaacirdldyylryatyamlagdpsildervlnglketynslg
vpisatvqaiqamkevtaslvgpdagkemgvyfdyicsgls
>d1b33g_ 4.25.1.1.1 Allophycocyanin linker chain (domain) {Mastigocladus laminosus}
grlfkitacvpsqtrirtqrelqntyftklvpyenwfreqqriqkmggkivkvelatgkq
gintgla
>d1b33h_ 1.1.1.2.4 Allophycocyanin {Cyanobacterium (Mastigocladus laminosus)}
sivtksivnadaearylspgeldriksfvssgekrlriaqiltdnrerivkqagdqlfqk
rpdvvspggnaygqemtatclrdldyylrlitygivagdvtpieeigivgvremykslgt
pidavaagvsamknvassilsaedaaeagayfdyvagala
>d1b33i_ 1.1.1.2.4 Allophycocyanin {Cyanobacterium (Mastigocladus laminosus)}
mqdaitavinssdvqgkyldtaaleklksyfstgelrvraattiaanaaaivkeavaksl
lysditrpggnmyttrryaacirdldyylryatyamlagdpsildervlnglketynslg
vpisatvqaiqamkevtaslvgpdagkemgvyfdyicsgls
>d1b33j_ 1.1.1.2.4 Allophycocyanin {Cyanobacterium (Mastigocladus laminosus)}
sivtksivnadaearylspgeldriksfvssgekrlriaqiltdnrerivkqagdqlfqk
rpdvvspggnaygqemtatclrdldyylrlitygivagdvtpieeigivgvremykslgt
pidavaagvsamknvassilsaedaaeagayfdyvagala
>d1b33k_ 1.1.1.2.4 Allophycocyanin {Cyanobacterium (Mastigocladus laminosus)}
mqdaitavinssdvqgkyldtaaleklksyfstgelrvraattiaanaaaivkeavaksl
lysditrpggnmyttrryaacirdldyylryatyamlagdpsildervlnglketynslg
vpisatvqaiqamkevtaslvgpdagkemgvyfdyicsgls
>d1b33l_ 1.1.1.2.4 Allophycocyanin {Cyanobacterium (Mastigocladus laminosus)}
sivtksivnadaearylspgeldriksfvssgekrlriaqiltdnrerivkqagdqlfqk
rpdvvspggnaygqemtatclrdldyylrlitygivagdvtpieeigivgvremykslgt
pidavaagvsamknvassilsaedaaeagayfdyvagala
>d1b33m_ 1.1.1.2.4 Allophycocyanin {Cyanobacterium (Mastigocladus laminosus)}
mqdaitavinssdvqgkyldtaaleklksyfstgelrvraattiaanaaaivkeavaksl
lysditrpggnmyttrryaacirdldyylryatyamlagdpsildervlnglketynslg
vpisatvqaiqamkevtaslvgpdagkemgvyfdyicsgls
>d1b33n_ 4.25.1.1.1 Allophycocyanin linker chain (domain) {Mastigocladus laminosus}
grlfkitacvpsqtrirtqrelqntyftklvpyenwfreqqriqkmggkivkvelatgkq
gintgla
>d1b35a_ 2.9.1.3.3 Cricket paralysis virus (CRPV) {Host: australian black field cricket (Teleogryllus commodus)}
vmgedqqiprneaqhgvhpisidthrisnnwspqamcigekvvsirqlikrfgifgdant
lqadgssfvvapftvtsptktltstrnytqfdyyyylyafwrgsmrikmvaetqdgtgtp
rkktnftwfvrmfnslqdsfnslistsssavtttvlpsgtinmgpstqvidptvegliev
evpyynishitpavtiddgtpsmedylkghsppclltfsprdsisatnhiitasfmralg
ddfsfmyllgvpplvnvara
>d1b35b_ 2.9.1.3.3 Cricket paralysis virus (CRPV) {Host: australian black field cricket (Teleogryllus commodus)}
enshienedkrltseqkeivhfvsegvtpsttalpdivnlstnyldkntredrihsikdf
lsrpiiiatnlwsvsdpvekqlytanfpevlisnamyqdklkgfvglratlvvkvqvnsq
pfqqgrlmlqyipyaqympnrvtlinetlqgrsgcprtdlelsvgtevemripyvsphly
ynlitgqgsfgsiyvvvysqlhdqvsgtgsieytvwahledvdvqyptganiftgneayi
kgtsrydaaqkahaa
>d1b35c_ 2.9.1.3.3 Cricket paralysis virus (CRPV) {Host: australian black field cricket (Teleogryllus commodus)}
skptvqgkigecklrgqgrmanfdgmdmshkmalsstneietneglagtsldvmdlsrvl
sipnywdrftwktsdvintvlwdnyvspfkvkpysatitdrfrcthmgkvanaftywrgs
mvytfkfvktqyhsgrlrisfipyyynttistgtpdvsrtqkivvdlrtstavsftvpyi
gsrpwlycirpesswlskdntdgalmyncvsgivrvevlnqlvaaqnvfseidvicevng
gpdlefagptcpryvpyagdftladtrkieaertqeysnned
>d1b38a_ 4.117.1.1.1 Cyclin-dependent PK (different isozymes) {Human (Homo sapiens)}
menfqkvekigegtygvvykarnkltgevvalkkirldtetegvpstaireisllkelnh
pnivklldvihtenklylvfeflhqdlkkfmdasaltgiplpliksylfqllqglafchs
hrvlhrdlkpqnllintegaikladfglarafgvpvrtythevvtlwyrapeillgckyy
stavdiwslgcifaemvtrralfpgdseidqlfrifrtlgtpdevvwpgvtsmpdykpsf
pkwarqdfskvvppldedgrsllsqmlhydpnkrisakaalahpffqdvtkpvphlrl
>d1b39a_ 4.117.1.1.1 Cyclin-dependent PK (different isozymes) {Human (Homo sapiens)}
menfqkvekigegtygvvykarnkltgevvalkkirldtetegvpstaireisllkelnh
pnivklldvihtenklylvfeflhqdlkkfmdasaltgiplpliksylfqllqglafchs
hrvlhrdlkpqnllintegaikladfglarafgvpvrtythevvtlwyrapeillgckyy
stavdiwslgcifaemvtrralfpgdseidqlfrifrtlgtpdevvwpgvtsmpdykpsf
pkwarqdfskvvppldedgrsllsqmlhydpnkrisakaalahpffqdvtkpvphlrl
>d1b3aa_ 4.8.1.1.9 RANTES (regulated upon activation, normal T-cell expressed and secreted) {Human (Homo sapiens)}
pyssdttpccfayiarplprahikeyfytsgkcsnpavvfvtrknrqvcanpekkwvrey
inslems
>d1b3ab_ 4.8.1.1.9 RANTES (regulated upon activation, normal T-cell expressed and secreted) {Human (Homo sapiens)}
pyssdttpccfayiarplprahikeyfytsgkcsnpavvfvtrknrqvcanpekkwvrey
inslems
>d1b3ca_ 7.3.7.1.2 Scorpion toxin {Centruroides sculpturatus ewing, beta}
kdgylvektgckktcyklgendfcnreckwkhiggsygycygfgcyceglpdstqtwplp
nktc
>d1b3ea_ 3.84.1.2.8 Transferrin {Human (Homo sapiens)}
ktvrwcavseheatkcqsfrdhmksvipsdgpsvacvkkasyldciraiaaneadavtld
aglvydaylapnnlkpvvaefygskedpqtfyyavavvkkdsgfqmnqlrgkkschtglg
rsagwnipigllycdlpeprkplekavanffsgscapcadgtdfpqlcqlcpgcgcstln
qyfgysgafkclkdgagdvafvkhstifenlankadrdnyellcldntrkpvdeykdchl
aqvpshtvvarsmggkedliwellnqaqehfgkdkskefqlfssphgkdllfkdsahgfl
kvpprmdakmylgyeyvtairnlregtcpe
>d1b3fa_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b3ga_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b3ha_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b3ia_ 2.5.1.1.15 Plastocyanin {Photosynthetic prokaryote (Prochlorothrix hollandica)}
asvqikmgtdkyaplyepkalsisagdtvefvmnkvgphnvifdkvpagesapalsntkl
aiapgsfysvtlgtpgtysfyctphrgagmvgtitve
>d1b3ja1 2.1.1.2.19 (181-274) MHC I homolog Mic-a {Human (Homo sapiens)}
tvppmvnvtrseasegnitvtcrasgfypwnitlswrqdgvslshdtqqwgdvlpdgngt
yqtwvatricqgeeqrftcymehsgnhsthpvps
>d1b3ja2 4.17.1.1.26 (1-180) MHC I homolog Mic-a {Human (Homo sapiens)}
ephslrynltvlswdgsvqsgfltevhldgqpflrcdrqkcrakpqgqwaedvlgnktwd
retrdltgngkdlrmtlahikdqkeglhslqeirvceihednstrssqhfyydgelflsq
nletkewtmpqssraqtlamnvrnflkedamktkthyhamhadclqelrrylksgvvlrr
>d1b3la_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b3lc_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b3na1 3.85.1.1.2 (2-251) Beta-ketoacyl carrier protein synthase {Escherichia coli}
krrvvvtglgmlspvgntvestwkallagqsgislidhfdtsayatkfaglvkdfncedi
isrkeqrkmdafiqygivagvqamqdsgleiteenatrigaaigsgigglglieenhtsl
mnggprkispffvpstivnmvaghltimyglrgpsisiatactsgvhnighaariiaygd
advmvaggaekastplgvggfgaaralstrndnpqaasrpwdkerdgfvlgdgagmlvle
eyehakkrga
>d1b3na2 3.85.1.1.2 (252-412) Beta-ketoacyl carrier protein synthase {Escherichia coli}
kiyaelvgfgmssdayhmtsppengagaalamanalrdagieasqigyvnahgtstpagd
kaeaqavktifgeaasrvlvsstksmtghllgaagavesiysilalrdqavpptinldnp
degcdldfvphearqvsgmeytlcnsfgfggtngslifkki
>d1b3oa1 3.1.6.2.2 (10-109,232-499) Inosine monophosphate dehydrogenase (IMPDH) {Human (Homo sapiens)}
tsyvpddgltaqqlfncgdgltyndflilpgyidftadqvdltsaltkkitlktplvssp
mdtvteagmaiamaltggigfihhnctpefqanevrkvkkXdyplaskdakkqllcgaai
gtheddkyrldllaqagvdvvvldssqgnsifqinmikyikdkypnlqviggnvvtaaqa
knlidagvdalrvgmgsgsicitqevlacgrpqatavykvseyarrfgvpviadggiqnv
ghiakalalgastvmmgsllaatteapgeyffsdgirlkkyrgmgsldamdkhlssqnry
fseadkikvaqgvsgavqdkgsihkfvpyliagiqhscqdigaksltqvrammysgelkf
ekrtssaqv
>d1b3ob1 3.1.6.2.2 (10-111,232-499) Inosine monophosphate dehydrogenase (IMPDH) {Human (Homo sapiens)}
tsyvpddgltaqqlfncgdgltyndflilpgyidftadqvdltsaltkkitlktplvssp
mdtvteagmaiamaltggigfihhnctpefqanevrkvkkyeXdyplaskdakkqllcga
aigtheddkyrldllaqagvdvvvldssqgnsifqinmikyikdkypnlqviggnvvtaa
qaknlidagvdalrvgmgsgsicitqevlacgrpqatavykvseyarrfgvpviadggiq
nvghiakalalgastvmmgsllaatteapgeyffsdgirlkkyrgmgsldamdkhlssqn
ryfseadkikvaqgvsgavqdkgsihkfvpyliagiqhscqdigaksltqvrammysgel
kfekrtssaqv
>d1b3ob2 4.30.1.1.1 (112-159) Type II inosine monophosphate dehydrogenase {Human (Homo sapiens)}
qgfitdpvvlspkdrvrdvfeakarhgfcgipitdtgrmgsrlvgiis
>d1b3ob3 4.30.1.1.1 (178-231) Type II inosine monophosphate dehydrogenase {Human (Homo sapiens)}
imtkredlvvapagitlkeaneilqrskkgklpivneddelvaiiartdlkknr
>d1b3ra1 3.2.1.4.9 (190-352) S-adenosylhomocystein hydrolase {Rat (Rattus norvegicus)}
nlygcreslidgikratdvmiagkvavvagygdvgkgcaqalrgfgarviiteidpinal
qaamegyevttmdeackegnifvtttgcvdiilgrhfeqmkddaivcnighfdveidvkw
lnenavekvnikpqvdryllknghriillaegrlvnlgcamgh
>d1b3ra2 3.16.9.3.2 (4-189,353-431) S-adenosylhomocystein hydrolase {Rat (Rattus norvegicus)}
lpykvadiglaawgrkaldiaenempglmrmremysaskplkgariagclhmtvetavli
etlvalgaevrwsscnifstqdhaaaaiakagipvfawkgetdeeylwcieqtlhfkdgp
lnmilddggdltnlihtkhpqllsgirgiseetttgvhnlykmmangilkvpainvndsv
tkskfdXpsfvmsnsftnqvmaqielwthpdkypvgvhflpkkldeavaeahlgklnvkl
tkltekqaqylgmpingpfkpdhyry
>d1b3rb1 3.2.1.4.9 (190-352) S-adenosylhomocystein hydrolase {Rat (Rattus norvegicus)}
nlygcreslidgikratdvmiagkvavvagygdvgkgcaqalrgfgarviiteidpinal
qaamegyevttmdeackegnifvtttgcvdiilgrhfeqmkddaivcnighfdveidvkw
lnenavekvnikpqvdryllknghriillaegrlvnlgcamgh
>d1b3rb2 3.16.9.3.2 (4-189,353-431) S-adenosylhomocystein hydrolase {Rat (Rattus norvegicus)}
lpykvadiglaawgrkaldiaenempglmrmremysaskplkgariagclhmtvetavli
etlvalgaevrwsscnifstqdhaaaaiakagipvfawkgetdeeylwcieqtlhfkdgp
lnmilddggdltnlihtkhpqllsgirgiseetttgvhnlykmmangilkvpainvndsv
tkskfdXpsfvmsnsftnqvmaqielwthpdkypvgvhflpkkldeavaeahlgklnvkl
tkltekqaqylgmpingpfkpdhyry
>d1b3rc1 3.2.1.4.9 (190-352) S-adenosylhomocystein hydrolase {Rat (Rattus norvegicus)}
nlygcreslidgikratdvmiagkvavvagygdvgkgcaqalrgfgarviiteidpinal
qaamegyevttmdeackegnifvtttgcvdiilgrhfeqmkddaivcnighfdveidvkw
lnenavekvnikpqvdryllknghriillaegrlvnlgcamgh
>d1b3rc2 3.16.9.3.2 (4-189,353-431) S-adenosylhomocystein hydrolase {Rat (Rattus norvegicus)}
lpykvadiglaawgrkaldiaenempglmrmremysaskplkgariagclhmtvetavli
etlvalgaevrwsscnifstqdhaaaaiakagipvfawkgetdeeylwcieqtlhfkdgp
lnmilddggdltnlihtkhpqllsgirgiseetttgvhnlykmmangilkvpainvndsv
tkskfdXpsfvmsnsftnqvmaqielwthpdkypvgvhflpkkldeavaeahlgklnvkl
tkltekqaqylgmpingpfkpdhyry
>d1b3rd1 3.2.1.4.9 (190-352) S-adenosylhomocystein hydrolase {Rat (Rattus norvegicus)}
nlygcreslidgikratdvmiagkvavvagygdvgkgcaqalrgfgarviiteidpinal
qaamegyevttmdeackegnifvtttgcvdiilgrhfeqmkddaivcnighfdveidvkw
lnenavekvnikpqvdryllknghriillaegrlvnlgcamgh
>d1b3rd2 3.16.9.3.2 (4-189,353-431) S-adenosylhomocystein hydrolase {Rat (Rattus norvegicus)}
lpykvadiglaawgrkaldiaenempglmrmremysaskplkgariagclhmtvetavli
etlvalgaevrwsscnifstqdhaaaaiakagipvfawkgetdeeylwcieqtlhfkdgp
lnmilddggdltnlihtkhpqllsgirgiseetttgvhnlykmmangilkvpainvndsv
tkskfdXpsfvmsnsftnqvmaqielwthpdkypvgvhflpkkldeavaeahlgklnvkl
tkltekqaqylgmpingpfkpdhyry
>d1b3sa_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
aqvintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnre
gklpgksgrtwreadinytsgfrnsdrilyssdwliykttdayqtftkir
>d1b3sb_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
aqvintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnre
gklpgksgrtwreadinytsgfrnsdrilyssdwliykttdayqtftkir
>d1b3sc_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdayqtftkir
>d1b3sd_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
mkkavingeqirsisdlhqtlkkelalpefygenldalwdcltgwveyplvlewrqfeqs
kqltengaesvlqvfreakaegcditiils
>d1b3se_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpefygenldalwdcltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegcditiils
>d1b3sf_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpefygenldalwdcltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegcditiils
>d1b3ta_ 4.47.8.1.4 Epstein barr virus nuclear antigen-1 (ebna1) {Epstein-Barr virus}
kggwfgkhrgqggsnpkfeniaeglrallarshverttdegtwvagvfvyggsktslynl
rrgtalaipqcrltplsrlpfgmapgpgpqpgplresivcyfmvflqthifaevlkdaik
dlvmtkpaptcnirvtvcsfddgvdlp
>d1b3tb_ 4.47.8.1.4 Epstein barr virus nuclear antigen-1 (ebna1) {Epstein-Barr virus}
kggwfgkhrgqggsnpkfeniaeglrallarshverttdegtwvagvfvyggsktslynl
rrgtalaipqcrltplsrlpfgmapgpgpqpgplresivcyfmvflqthifaevlkdaik
dlvmtkpaptcnirvtvcsfddgvdlp
>d1b3ua_ 1.110.1.2.1 Constant regulatory domain of protein phosphatase 2a, pr65alpha {Human (Homo sapiens)}
aaadgddslypiavlidelrnedvqlrlnsikklstialalgvertrsellpfltdtiyd
edevllalaeqlgtfttlvggpeyvhcllppleslatveetvvrdkaveslraishehsp
sdleahfvplvkrlaggdwftsrtsacglfsvcyprvssavkaelrqyfrnlcsddtpmv
rraaasklgefakvleldnvkseiipmfsnlasdeqdsvrllaveacvniaqllpqedle
alvmptlrqaaedkswrvrymvadkftelqkavgpeitktdlvpafqnlmkdceaevraa
ashkvkefcenlsadcrenvimsqilpcikelvsdanqhvksalasvimglspilgkdnt
iehllplflaqlkdecpevrlniisnldcvnevigirqlsqsllpaivelaedakwrvrl
aiieympllagqlgveffdeklnslcmawlvdhvyaireaatsnlkklvekfgkewahat
iipkvlamsgdpnylhrmttlfcinvlsevcgqdittkhmlptvlrmagdpvanvrfnva
kslqkigpildnstlqsevkpilekltqdqdvdvkyfaqealtvlsla
>d1b3ub_ 1.110.1.2.1 Constant regulatory domain of protein phosphatase 2a, pr65alpha {Human (Homo sapiens)}
aaadgddslypiavlidelrnedvqlrlnsikklstialalgvertrsellpfltdtiyd
edevllalaeqlgtfttlvggpeyvhcllppleslatveetvvrdkaveslraishehsp
sdleahfvplvkrlaggdwftsrtsacglfsvcyprvssavkaelrqyfrnlcsddtpmv
rraaasklgefakvleldnvkseiipmfsnlasdeqdsvrllaveacvniaqllpqedle
alvmptlrqaaedkswrvrymvadkftelqkavgpeitktdlvpafqnlmkdceaevraa
ashkvkefcenlsadcrenvimsqilpcikelvsdanqhvksalasvimglspilgkdnt
iehllplflaqlkdecpevrlniisnldcvnevigirqlsqsllpaivelaedakwrvrl
aiieympllagqlgveffdeklnslcmawlvdhvyaireaatsnlkklvekfgkewahat
iipkvlamsgdpnylhrmttlfcinvlsevcgqdittkhmlptvlrmagdpvanvrfnva
kslqkigpildnstlqsevkpilekltqdqdvdvkyfaqealtvlsla
>d1b3va_ 3.1.7.3.15 Xylanase A, catalytic core {Penicillium simplicissimum}
asvsidakfkahgkkylgtigdqytltkntknpaiikadfgqltpensmkwdatepnrgq
ftfsgsdylvnfaqsngklirghtlvwhsqlpgwvssitdkntlisvlknhittvmtryk
gkiyawdvlneifnedgslrnsvfynvigedyvriafetarsvdpnaklyindynldsag
yskvngmvshvkkwlaagipidgigsqthlgagagsavagalnalasagtkeiaiteldi
agasstdyvnvvnaclnqakcvgitvwgvadpdswrsssspllfdgnynpkaaynaiana
l
>d1b3wa_ 3.1.7.3.15 Xylanase A, catalytic core {Penicillium simplicissimum}
asvsidakfkahgkkylgtigdqytltkntknpaiikadfgqltpensmkwdatepnrgq
ftfsgsdylvnfaqsngklirghtlvwhsqlpgwvssitdkntlisvlknhittvmtryk
gkiyawdvlneifnedgslrnsvfynvigedyvriafetarsvdpnaklyindynldsag
yskvngmvshvkkwlaagipidgigsqthlgagagsavagalnalasagtkeiaiteldi
agasstdyvnvvnaclnqakcvgitvwgvadpdswrsssspllfdgnynpkaaynaiana
l
>d1b3xa_ 3.1.7.3.15 Xylanase A, catalytic core {Penicillium simplicissimum}
asvsidakfkahgkkylgtigdqytltkntknpaiikadfgqltpensmkwdatepnrgq
ftfsgsdylvnfaqsngklirghtlvwhsqlpgwvssitdkntlisvlknhittvmtryk
gkiyawdvlneifnedgslrnsvfynvigedyvriafetarsvdpnaklyindynldsag
yskvngmvshvkkwlaagipidgigsqthlgagagsavagalnalasagtkeiaiteldi
agasstdyvnvvnaclnqakcvgitvwgvadpdswrsssspllfdgnynpkaaynaiana
l
>d1b3ya_ 3.1.7.3.15 Xylanase A, catalytic core {Penicillium simplicissimum}
asvsidakfkahgkkylgtigdqytltkntknpaiikadfgqltpensmkwdatepnrgq
ftfsgsdylvnfaqsngklirghtlvwhsqlpgwvssitdkntlisvlknhittvmtryk
gkiyawdvlneifnedgslrnsvfynvigedyvriafetarsvdpnaklyindynldsag
yskvngmvshvkkwlaagipidgigsqthlgagagsavagalnalasagtkeiaiteldi
agasstdyvnvvnaclnqakcvgitvwgvadpdswrsssspllfdgnynpkaaynaiana
l
>d1b3za_ 3.1.7.3.15 Xylanase A, catalytic core {Penicillium simplicissimum}
asvsidakfkahgkkylgtigdqytltkntknpaiikadfgqltpensmkwdatepnrgq
ftfsgsdylvnfaqsngklirghtlvwhsqlpgwvssitdkntlisvlknhittvmtryk
gkiyawdvlneifnedgslrnsvfynvigedyvriafetarsvdpnaklyindynldsag
yskvngmvshvkkwlaagipidgigsqthlgagagsavagalnalasagtkeiaiteldi
agasstdyvnvvnaclnqakcvgitvwgvadpdswrsssspllfdgnynpkaaynaiana
l
>d1b40a_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b42__ 3.56.1.4.1 Polymerase regulatory subunit VP39 {Vaccinia virus}
mdvvsldkpfmyfeeidneldyepesanevakklpyqgqlklllgelfflsklqrhgild
gatvvyigsapgthirylrdhfynlgviikwmlidgrhhdpilnglrdvtlvtrfvdeey
lrsikkqlhpskiilisdvrskrggnepstadllsnyalqnvmisilnpvasslkwrcpf
pdqwikdfyiphgnkmlqpfapsysaemrllsiytgenmrltrvtksdavnyekkmyyln
kivrnkvvvnfdypnqeydyfhmyfmlrtvycnktfpttkakvlflqqsifrflnip
>d1b44d_ 2.35.2.1.1 Heat-labile toxin {Escherichia coli, type IB}
apqsitelcseyhntqiytindkilsytesmagkremviitfksgatfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismeklag
>d1b44e_ 2.35.2.1.1 Heat-labile toxin {Escherichia coli, type IB}
apqsitelcseyhntqiytindkilsytesmagkremviitfksgatfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismeklagf
>d1b44f_ 2.35.2.1.1 Heat-labile toxin {Escherichia coli, type IB}
apqsitelcseyhntqiytindkilsytesmagkremviitfksgatfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismeklag
>d1b44g_ 2.35.2.1.1 Heat-labile toxin {Escherichia coli, type IB}
apqsitelcseyhntqiytindkilsytesmagkremviitfksgatfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismeklag
>d1b44h_ 2.35.2.1.1 Heat-labile toxin {Escherichia coli, type IB}
apqsitelcseyhntqiytindkilsytesmagkremviitfksgatfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismeklag
>d1b46a_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b47a1 1.42.1.7.4 (178-263) Cbl {Human (Homo sapiens)}
tfritkadaaefwrkafgektivpwksfrqalhevhpissgleamalkstidltcndyis
vfefdiftrlfqpwssllrnwnslav
>d1b47a2 1.51.1.1.1 (47-177) N-terminal domain of cbl (N-cbl) {Human (Homo sapiens)}
ppgtvdkkmvekcwklmdkvvrlcqnpklalknsppyildllpdtyqhlrtilsryegkm
etlgeneyfrvfmenlmkktkqtislfkegkermyeensqprrnltklslifshmlaelk
gifpsglfqgd
>d1b47a3 4.72.1.1.19 (264-350) Cbl {Human (Homo sapiens)}
thpgymafltydevkarlqkfihkpgsyifrlsctrlgqwaigyvtadgnilqtiphnkp
lfqalidgfregfylfpdgrnqnpdlt
>d1b47b1 1.42.1.7.4 (178-263) Cbl {Human (Homo sapiens)}
tfritkadaaefwrkafgektivpwksfrqalhevhpissgleamalkstidltcndyis
vfefdiftrlfqpwssllrnwnslav
>d1b47b2 1.51.1.1.1 (47-177) N-terminal domain of cbl (N-cbl) {Human (Homo sapiens)}
ppgtvdkkmvekcwklmdkvvrlcqnpklalknsppyildllpdtyqhlrtilsryegkm
etlgeneyfrvfmenlmkktkqtislfkegkermyeensqprrnltklslifshmlaelk
gifpsglfqgd
>d1b47b3 4.72.1.1.19 (264-350) Cbl {Human (Homo sapiens)}
thpgymafltydevkarlqkfihkpgsyifrlsctrlgqwaigyvtadgnilqtiphnkp
lfqalidgfregfylfpdgrnqnpdlt
>d1b47c1 1.42.1.7.4 (178-263) Cbl {Human (Homo sapiens)}
tfritkadaaefwrkafgektivpwksfrqalhevhpissgleamalkstidltcndyis
vfefdiftrlfqpwssllrnwnslav
>d1b47c2 1.51.1.1.1 (47-177) N-terminal domain of cbl (N-cbl) {Human (Homo sapiens)}
ppgtvdkkmvekcwklmdkvvrlcqnpklalknsppyildllpdtyqhlrtilsryegkm
etlgeneyfrvfmenlmkktkqtislfkegkermyeensqprrnltklslifshmlaelk
gifpsglfqgd
>d1b47c3 4.72.1.1.19 (264-350) Cbl {Human (Homo sapiens)}
thpgymafltydevkarlqkfihkpgsyifrlsctrlgqwaigyvtadgnilqtiphnkp
lfqalidgfregfylfpdgrnqnpdlt
>d1b48a1 1.48.1.1.10 (80-222) Glutathione S-transferase {Mouse (Mus musculus)}
nlygkdlkervridmyadgtqdlmmmiavapfktpkekeesydlilsraktryfpvfeki
lkdhgeaflvgnqlswadiqlleailmveelsapvlsdfpllqafktrisniptikkflq
pgsqrkpppdgpyvevvrivlkf
>d1b48a2 3.38.1.5.10 (2-79) Glutathione S-transferase {Mouse (Mus musculus)}
aakpklyyfngrgrmesirwllaaagvefeeefletreqyekmqkdghllfgqvplveid
gmmltqtrailsylaaky
>d1b48b1 1.48.1.1.10 (80-222) Glutathione S-transferase {Mouse (Mus musculus)}
nlygkdlkervridmyadgtqdlmmmiavapfktpkekeesydlilsraktryfpvfeki
lkdhgeaflvgnqlswadiqlleailmveelsapvlsdfpllqafktrisniptikkflq
pgsqrkpppdgpyvevvrivlkf
>d1b48b2 3.38.1.5.10 (2-79) Glutathione S-transferase {Mouse (Mus musculus)}
aakpklyyfngrgrmesirwllaaagvefeeefletreqyekmqkdghllfgqvplveid
gmmltqtrailsylaaky
>d1b49a_ 4.91.1.1.7 dCMP hydroxymethylase {Bacteriophage T4}
misdsmtveeirlhlglalkekdfvvdktgvktieiigasfvadepfifgalndeyiqre
lewykskslfvkdipgetpkiwqqvasskgeinsnygwaiwsednyaqydmclaelgqnp
dsrrgimiytrpsmqfdynkdgmsdfmctntvqylirdkkinavvnmrsndvvfgfrndy
awqkyvldklvsdlnagdstrqykagsiiwnvgslhvysrhfylvdhwwktgethiskkd
y
>d1b49c_ 4.91.1.1.7 dCMP hydroxymethylase {Bacteriophage T4}
misdsmtveeirlhlglalkekdfvvdktgvktieiigasfvadepfifgalndeyiqre
lewykskslfvkdipgetpkiwqqvasskgeinsnygwaiwsednyaqydmclaelgqnp
dsrrgimiytrpsmqfdynkdgmsdfmctntvqylirdkkinavvnmrsndvvfgfrndy
awqkyvldklvsdlnagdstrqykagsiiwnvgslhvysrhfylvdhwwktgethiskkd
y
>d1b4aa1 1.4.3.3.2 (4-78) Arginine repressor (ArgR), N-terminal DNA-binding domain {Bacillus stearothermophilus}
gqrhikireiimsndietqdelvdrlreagfnvtqatvsrdikemqlvkvpmangrykys
lpsdqrfnplqklkr
>d1b4aa2 4.56.2.1.2 (79-149) C-terminal domain of arginine repressor {Bacillus stearothermophilus}
alvdvfikldgtgnllvlrtlpgnahaigvlldnldwdeivgticgddtcliicrtpkda
kkvsnqllsml
>d1b4ab1 1.4.3.3.2 (4-78) Arginine repressor (ArgR), N-terminal DNA-binding domain {Bacillus stearothermophilus}
gqrhikireiimsndietqdelvdrlreagfnvtqatvsrdikemqlvkvpmangrykys
lpsdqrfnplqklkr
>d1b4ab2 4.56.2.1.2 (79-149) C-terminal domain of arginine repressor {Bacillus stearothermophilus}
alvdvfikldgtgnllvlrtlpgnahaigvlldnldwdeivgticgddtcliicrtpkda
kkvsnqllsml
>d1b4ac1 1.4.3.3.2 (4-78) Arginine repressor (ArgR), N-terminal DNA-binding domain {Bacillus stearothermophilus}
gqrhikireiimsndietqdelvdrlreagfnvtqatvsrdikemqlvkvpmangrykys
lpsdqrfnplqklkr
>d1b4ac2 4.56.2.1.2 (79-149) C-terminal domain of arginine repressor {Bacillus stearothermophilus}
alvdvfikldgtgnllvlrtlpgnahaigvlldnldwdeivgticgddtcliicrtpkda
kkvsnqllsml
>d1b4ad1 1.4.3.3.2 (4-78) Arginine repressor (ArgR), N-terminal DNA-binding domain {Bacillus stearothermophilus}
gqrhikireiimsndietqdelvdrlreagfnvtqatvsrdikemqlvkvpmangrykys
lpsdqrfnplqklkr
>d1b4ad2 4.56.2.1.2 (79-149) C-terminal domain of arginine repressor {Bacillus stearothermophilus}
alvdvfikldgtgnllvlrtlpgnahaigvlldnldwdeivgticgddtcliicrtpkda
kkvsnqllsml
>d1b4ae1 1.4.3.3.2 (4-78) Arginine repressor (ArgR), N-terminal DNA-binding domain {Bacillus stearothermophilus}
gqrhikireiimsndietqdelvdrlreagfnvtqatvsrdikemqlvkvpmangrykys
lpsdqrfnplqklkr
>d1b4ae2 4.56.2.1.2 (79-149) C-terminal domain of arginine repressor {Bacillus stearothermophilus}
alvdvfikldgtgnllvlrtlpgnahaigvlldnldwdeivgticgddtcliicrtpkda
kkvsnqllsml
>d1b4af1 1.4.3.3.2 (4-78) Arginine repressor (ArgR), N-terminal DNA-binding domain {Bacillus stearothermophilus}
gqrhikireiimsndietqdelvdrlreagfnvtqatvsrdikemqlvkvpmangrykys
lpsdqrfnplqklkr
>d1b4af2 4.56.2.1.2 (79-149) C-terminal domain of arginine repressor {Bacillus stearothermophilus}
alvdvfikldgtgnllvlrtlpgnahaigvlldnldwdeivgticgddtcliicrtpkda
kkvsnqllsml
>d1b4ba_ 4.56.2.1.2 C-terminal domain of arginine repressor {Bacillus stearothermophilus}
alvdvfikldgtgnllvlrtlpgnahaigvlldnldwdeivgticgddtcliicrtpkda
kkvsnqllsml
>d1b4bb_ 4.56.2.1.2 C-terminal domain of arginine repressor {Bacillus stearothermophilus}
alvdvfikldgtgnllvlrtlpgnahaigvlldnldwdeivgticgddtcliicrtpkda
kkvsnqllsml
>d1b4bc_ 4.56.2.1.2 C-terminal domain of arginine repressor {Bacillus stearothermophilus}
alvdvfikldgtgnllvlrtlpgnahaigvlldnldwdeivgticgddtcliicrtpkda
kkvsnqllsml
>d1b4ca_ 1.42.1.2.2 Calcyclin (S100) {Rat (Rattus norvegicus), s100b}
mselekamvalidvfhqysgregdkhklkkselkelinnelshfleeikeqevvdkvmet
ldedgdgecdfqefmafvsmvttacheffehe
>d1b4cb_ 1.42.1.2.2 Calcyclin (S100) {Rat (Rattus norvegicus), s100b}
mselekamvalidvfhqysgregdkhklkkselkelinnelshfleeikeqevvdkvmet
ldedgdgecdfqefmafvsmvttacheffehe
>d1b4d__ 3.77.1.2.1 Glycogen phosphorylase {Rabbit (Oryctolagus cuniculus)}
isvrglagvenvtelkknfnrhlhftlvkdrnvatprdyyfalahtvrdhlvgrwirtqq
hyyekdpkriyylslefymgrtlqntmvnlalenacdeatyqlgldmeeleeieedaglg
ngglgrlaacfldsmatlglaaygygiryefgifnqkicggwqmeeaddwlrygnpweka
rpeftlpvhfygrvehtsqgakwvdtqvvlampydtpvpgyrnnvvntmrlwsakapndf
nlkdfnvggyiqavldrnlaenisrvlypndnffegkelrlkqeyfvvaatlqdiirrfk
sskfgcrdpvrtnfdafpdkvaiqlndthpslaipelmrvlvdlerldwdkawevtvktc
aytnhtvipealerwpvhlletllprhlqiiyeinqrflnrvaaafpgdvdrlrrmslve
egavkrinmahlciagshavngvarihseilkktifkdfyelephkfqnktngitprrwl
vlcnpglaeiiaerigeeyisdldqlrkllsyvddeafirdvakvkqenklkfaaylere
ykvhinpnslfdvqvkriheykrqllnclhvitlynrikkepnkfvvprtvmiggkaapg
yhmakmiiklitaigdvvnhdpvvgdrlrviflenyrvslaekvipaadlseqistagte
asgtgnmxfmlngaltigtmdganvemaeeageenffifgmrvedvdrldqrgynaqeyy
dripelrqiieqlssgffspkqpdlfkdivnmlmhhdrfkvfadyeeyvkcqervsalyk
nprewtrmvirniatsgkfssdrtiaqyareiwgvepsrqrlp
>d1b4fa_ 1.61.1.2.2 EphB2 receptor {Human (Homo sapiens)}
pdytsfntvdewleaikmgqykesfanagftsfdvvsqmmmedilrvgvtlaghqkkiln
siqvmraqmnqiqs
>d1b4fb_ 1.61.1.2.2 EphB2 receptor {Human (Homo sapiens)}
trpdytsfntvdewleaikmgqykesfanagftsfdvvsqmmmedilrvgvtlaghqkki
lnsiqvmraqmnqiqsv
>d1b4fc_ 1.61.1.2.2 EphB2 receptor {Human (Homo sapiens)}
pdytsfntvdewleaikmgqykesfanagftsfdvvsqmmmedilrvgvtlaghqkkiln
siqvmraqmnqiqs
>d1b4fd_ 1.61.1.2.2 EphB2 receptor {Human (Homo sapiens)}
rpdytsfntvdewleaikmgqykesfanagftsfdvvsqmmmedilrvgvtlaghqkkil
nsiqvmraqmnqiqs
>d1b4fe_ 1.61.1.2.2 EphB2 receptor {Human (Homo sapiens)}
pdytsfntvdewleaikmgqykesfanagftsfdvvsqmmmedilrvgvtlaghqkkiln
siqvmraqmnqiqs
>d1b4ff_ 1.61.1.2.2 EphB2 receptor {Human (Homo sapiens)}
rpdytsfntvdewleaikmgqykesfanagftsfdvvsqmmmedilrvgvtlaghqkkil
nsiqvmraqmnqiqsve
>d1b4fg_ 1.61.1.2.2 EphB2 receptor {Human (Homo sapiens)}
pdytsfntvdewleaikmgqykesfanagftsfdvvsqmmmedilrvgvtlaghqkkiln
siqvmraqmnqi
>d1b4fh_ 1.61.1.2.2 EphB2 receptor {Human (Homo sapiens)}
rpdytsfntvdewleaikmgqykesfanagftsfdvvsqmmmedilrvgvtlaghqkkil
nsiqvmraqmnqiqsv
>d1b4ha_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b4jh1 2.1.1.1.120 (2-117) Immunoglobulin (variable domains of L and H chains) {Humanized and chimeric anti-gamma-interferon Fab}
vqlqqpgadlvmpgapvklsclasgyiftsswinwvkqrpgrglewigridpsdgevhyn
qdfkdkatltvdkssstayiqlnsltsedsavyycargflpwfadwgqgtlvtvsa
>d1b4jh2 2.1.1.2.118 (118-220) Immunoglobulin (constant domains of L and H chains) {Humanized and chimeric anti-gamma-interferon Fab}
astkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkvepksc
>d1b4jl1 2.1.1.1.120 (1-107) Immunoglobulin (variable domains of L and H chains) {Humanized and chimeric anti-gamma-interferon Fab}
nivmtqspksmyvsigervtlsckasenvdtyvswyqqkpeqspklliygasnrytgvpd
rftgsgsatdftltissvqaedladyhcgqsynypftfgsgtkleik
>d1b4jl2 2.1.1.2.118 (108-214) Immunoglobulin (constant domains of L and H chains) {Humanized and chimeric anti-gamma-interferon Fab}
rtvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqd
skdstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1b4ka_ 3.1.9.3.2 5-aminolevulinate dehydratase (porphobilinogen synthase) {Pseudomonas aeruginosa}
ypytrlrrnrrddfsrrlvrenvltvddlilpvfvldgvnqresipsmpgverlsidqll
ieaeewvalgipalalfpvtpvekksldaaeaynpegiaqratralrerfpelgiitdva
ldpftthgqdgildddgyvlndvsidvlvrqalshaeagaqvvapsdmmdgrigaireal
esaghtnvrimaysakyasayygpfrdavgsasnlgkgnkatyqmdpansdealhevaad
laegadmvmvkpgmpyldivrrvkdefraptfvyqvsgeyamhmgaiqngwlaesviles
ltafkragadgiltyfakqaaeqlrr
>d1b4kb_ 3.1.9.3.2 5-aminolevulinate dehydratase (porphobilinogen synthase) {Pseudomonas aeruginosa}
anraypytrlrrnrrddfsrrlvrenvltvddlilpvfvldgvnqresipsmpgverlsi
dqllieaeewvalgipalalfpvtpvekksldaaeaynpegiaqratralrerfpelgii
tdvaldpftthgqdgildddgyvlndvsidvlvrqalshaeagaqvvapsdmmdgrigai
realesaghtnvrimaysakyasayygpfrdavgsasnlgkgnkatyqmdpansdealhe
vaadlaegadmvmvkpgmpyldivrrvkdefraptfvyqvsgeyamhmgaiqngwlaesv
ilesltafkragadgiltyfakqaaeqlrr
>d1b4m__ 2.53.1.2.11 Cellular retinol-binding protein II (CRBP) {Rat (Rattus rattus)}
mtkdqngtwemesnenfegymkaldidfatrkiavrltqtkiivqdgdnfktktnstfrn
ydldftvgvefdehtkgldgrnvktlvtwegntlvcvqkgekenrgwkqwvegdklylel
tcgdqvcrqvfkkk
>d1b4na1 1.104.1.1.2 (211-619) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
dkeelkklsqeayneilnspgypfwkrqgtmaavewcntnyalptrnfsdgyfefarsid
gytmegmkvqqrgcpycnmpcgnvvldaegqeseldyenvallgsnlgigklnevsvlnr
iademgmdtislgvsiahvmeavergilkegptfgdfkgakqlaldiayrkgelgnlaae
gvkamaeklgthdfamhvkglevsgyncyiypamalaygtsaigahhkeawviaweigta
piegekaekveykisydpikaqkvvelqrlrgglfemltacrlpwvevglsldyypkllk
aitgvtytwddlykaadrvysliraywvrefngkwdrkmdyppkrwfteglksgphkgeh
ldekkydellseyyrirgwdergipkketlkeldldfvipelekvtnle
>d1b4na2 4.123.1.1.2 (1-210) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
mygwwgrilrvnlttgevkvqeypeevakkfiggrglaawilwneargveplspenklif
aagpfnglptpsggklvvaakspltggygdgnlgtmasvhlrragydalvvegkakkpvy
iyieddnvsilsaeglwgkttfeterelkeihgknvgvltigpagenlvkyavvisqegr
aagrpgmgavmgskklkavvirgtkeipva
>d1b4nb1 1.104.1.1.2 (211-619) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
dkeelkklsqeayneilnspgypfwkrqgtmaavewcntnyalptrnfsdgyfefarsid
gytmegmkvqqrgcpycnmpcgnvvldaegqeseldyenvallgsnlgigklnevsvlnr
iademgmdtislgvsiahvmeavergilkegptfgdfkgakqlaldiayrkgelgnlaae
gvkamaeklgthdfamhvkglevsgyncyiypamalaygtsaigahhkeawviaweigta
piegekaekveykisydpikaqkvvelqrlrgglfemltacrlpwvevglsldyypkllk
aitgvtytwddlykaadrvysliraywvrefngkwdrkmdyppkrwfteglksgphkgeh
ldekkydellseyyrirgwdergipkketlkeldldfvipelekvtnle
>d1b4nb2 4.123.1.1.2 (1-210) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
mygwwgrilrvnlttgevkvqeypeevakkfiggrglaawilwneargveplspenklif
aagpfnglptpsggklvvaakspltggygdgnlgtmasvhlrragydalvvegkakkpvy
iyieddnvsilsaeglwgkttfeterelkeihgknvgvltigpagenlvkyavvisqegr
aagrpgmgavmgskklkavvirgtkeipva
>d1b4nc1 1.104.1.1.2 (211-619) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
dkeelkklsqeayneilnspgypfwkrqgtmaavewcntnyalptrnfsdgyfefarsid
gytmegmkvqqrgcpycnmpcgnvvldaegqeseldyenvallgsnlgigklnevsvlnr
iademgmdtislgvsiahvmeavergilkegptfgdfkgakqlaldiayrkgelgnlaae
gvkamaeklgthdfamhvkglevsgyncyiypamalaygtsaigahhkeawviaweigta
piegekaekveykisydpikaqkvvelqrlrgglfemltacrlpwvevglsldyypkllk
aitgvtytwddlykaadrvysliraywvrefngkwdrkmdyppkrwfteglksgphkgeh
ldekkydellseyyrirgwdergipkketlkeldldfvipelekvtnle
>d1b4nc2 4.123.1.1.2 (1-210) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
mygwwgrilrvnlttgevkvqeypeevakkfiggrglaawilwneargveplspenklif
aagpfnglptpsggklvvaakspltggygdgnlgtmasvhlrragydalvvegkakkpvy
iyieddnvsilsaeglwgkttfeterelkeihgknvgvltigpagenlvkyavvisqegr
aagrpgmgavmgskklkavvirgtkeipva
>d1b4nd1 1.104.1.1.2 (211-619) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
dkeelkklsqeayneilnspgypfwkrqgtmaavewcntnyalptrnfsdgyfefarsid
gytmegmkvqqrgcpycnmpcgnvvldaegqeseldyenvallgsnlgigklnevsvlnr
iademgmdtislgvsiahvmeavergilkegptfgdfkgakqlaldiayrkgelgnlaae
gvkamaeklgthdfamhvkglevsgyncyiypamalaygtsaigahhkeawviaweigta
piegekaekveykisydpikaqkvvelqrlrgglfemltacrlpwvevglsldyypkllk
aitgvtytwddlykaadrvysliraywvrefngkwdrkmdyppkrwfteglksgphkgeh
ldekkydellseyyrirgwdergipkketlkeldldfvipelekvtnle
>d1b4nd2 4.123.1.1.2 (1-210) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
mygwwgrilrvnlttgevkvqeypeevakkfiggrglaawilwneargveplspenklif
aagpfnglptpsggklvvaakspltggygdgnlgtmasvhlrragydalvvegkakkpvy
iyieddnvsilsaeglwgkttfeterelkeihgknvgvltigpagenlvkyavvisqegr
aagrpgmgavmgskklkavvirgtkeipva
>d1b4r__ 2.1.3.1.1 Polycystein-1, PKD-1 {Human (Homo sapiens)}
atlvgphgplasgqlaafhiaaplpvtatrwdfgdgsaevdaagpaashryvlpgryhvt
avlalgagsallgtdvqvea
>d1b4sa_ 4.47.6.1.3 Nucleoside diphosphate kinases {Dictyostelium discodeum}
vnkertflavkpdgvarglvgeiiaryekkgfvlvglkqlvptkdlaeshyaehkerpff
gglvsfitsgpvvamvfegkgvvasarlmigvtnplasapgsirgdfgvdvgrniiggsd
svesanreialwfkpeelltevkpnpnlye
>d1b4sb_ 4.47.6.1.3 Nucleoside diphosphate kinases {Dictyostelium discodeum}
vnkertflavkpdgvarglvgeiiaryekkgfvlvglkqlvptkdlaeshyaehkerpff
gglvsfitsgpvvamvfegkgvvasarlmigvtnplasapgsirgdfgvdvgrniiggsd
svesanreialwfkpeelltevkpnpnlye
>d1b4sc_ 4.47.6.1.3 Nucleoside diphosphate kinases {Dictyostelium discodeum}
vnkertflavkpdgvarglvgeiiaryekkgfvlvglkqlvptkdlaeshyaehkerpff
gglvsfitsgpvvamvfegkgvvasarlmigvtnplasapgsirgdfgvdvgrniiggsd
svesanreialwfkpeelltevkpnpnlye
>d1b4ua_ 1.85.1.1.1 LigA subunit of an aromatic-ring-opening dioxygenase LigAB {Pseudomonas paucimobilis}
idvhaylaefddipgtrvftaqrarkgynlnqfamslmkaenrerfkadesayldewnlt
paakaavlardynamideggnvyflsklfstdgksfqfaagsmtgmtqeeyaqmmidggr
spagvrsikggy
>d1b4ub_ 3.47.5.1.1 LigB subunit of an aromatic-ring-opening dioxygenase LigAB {Pseudomonas paucimobilis}
arvttgitsshipalgaaiqtgtsdndywgpvfkgyqpirdwikqpgnmpdvvilvyndh
asafdmniiptfaigcaetfkpadegwgprpvpdvkghpdlawhiaqslildefdmtimn
qmdvdhgctvplsmifgepeewpckvipfpvnvvtypppsgkrcfalgdsiraavesfpe
dlnvhvwgtggmshqlqgpraglinkefdlnfidklisdpeelskmphiqylresgsegv
elvmwlimrgalpekvrdlytfyhipasntalgamilqpeetagtpleprkvmsghsl
>d1b4uc_ 1.85.1.1.1 LigA subunit of an aromatic-ring-opening dioxygenase LigAB {Pseudomonas paucimobilis}
idvhaylaefddipgtrvftaqrarkgynlnqfamslmkaenrerfkadesayldewnlt
paakaavlardynamideggnvyflsklfstdgksfqfaagsmtgmtqeeyaqmmidggr
spagvrsikggy
>d1b4ud_ 3.47.5.1.1 LigB subunit of an aromatic-ring-opening dioxygenase LigAB {Pseudomonas paucimobilis}
arvttgitsshipalgaaiqtgtsdndywgpvfkgyqpirdwikqpgnmpdvvilvyndh
asafdmniiptfaigcaetfkpadegwgprpvpdvkghpdlawhiaqslildefdmtimn
qmdvdhgctvplsmifgepeewpckvipfpvnvvtypppsgkrcfalgdsiraavesfpe
dlnvhvwgtggmshqlqgpraglinkefdlnfidklisdpeelskmphiqylresgsegv
elvmwlimrgalpekvrdlytfyhipasntalgamilqpeetagtpleprkvmsghsl
>d1b4v_1 3.3.1.2.2 (9-318,451-506) Cholesterol oxidase {Streptomyces}
gyvpavvigtgygaavsalrlgeagvqtlmlemgqlwnqpgpdgnifcgmlnpdkrsswf
knrteaplgsflwldvvnrnidpyagvldrvnydqmsvyvgrgvgggslvnggmavepkr
syfeeilprvdssemydryfpransmlrvnhidtkwfedtewykfarvsreqagkaglgt
vfvpnvydfgymqreaagevpksalateviygnnhgkqsldktylaaalgtgkvtiqtlh
qvktirqtkdggyaltveqkdtdgkllatkeiscrylflgagslgstellvrardtgtlp
nlnsevgagwXgcvlgkatddygrvagyknlyvtdgslipgsvgvnpfvtitalaernve
riikqdv
>d1b4v_2 4.14.1.1.2 (319-450) Cholesterol oxidase {Streptomyces}
gpngnimtaranhmwnptgahqssipalgidawdnsdssvfaeiapmpagletwvslyla
itknpqrgtfvydaatdraklnwtrdqnapavnaakalfdrinkangtiyrydlfgtqlk
afaddfcyhplg
>d1b4za_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b50a_ 4.8.1.1.7 Macrophage inflammatory protein, MIP {Human (Homo sapiens), 1-alpha}
slaadtptaccfsytsrqipqnfiaayfetssqcskpgvifltkrsrqvcadpseewvqk
yvsdlelsa
>d1b50b_ 4.8.1.1.7 Macrophage inflammatory protein, MIP {Human (Homo sapiens), 1-alpha}
slaadtptaccfsytsrqipqnfiaayfetssqcskpgvifltkrsrqvcadpseewvqk
yvsdlelsa
>d1b51a_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b52a_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b53a_ 4.8.1.1.7 Macrophage inflammatory protein, MIP {Human (Homo sapiens), 1-alpha}
slaadtptaccfsytsrqipqnfiaayfetssqcskpgvifltkrsrqvcadpseewvqk
yvsdlelsa
>d1b53b_ 4.8.1.1.7 Macrophage inflammatory protein, MIP {Human (Homo sapiens), 1-alpha}
slaadtptaccfsytsrqipqnfiaayfetssqcskpgvifltkrsrqvcadpseewvqk
yvsdlelsa
>d1b54__ 3.1.5.2.1 "Hypothetical" protein ybl036c {Baker's yeast (Saccharomyces cerevisiae)}
gitydedrktqliaqyesvrevvnaeaknvhvnenaskilllvvsklkpasdiqilydhg
vrefgenyvqeliekakllpddikwhfigglqtnkckdlakvpnlysvetidslkkakkl
nesrakfqpdcnpilcnvqintshedqksglnneaeifevidfflseeckyiklnglmti
gswnvshedskenrdfatlvewkkkidakfgtslklsmgmsadfreairqgtaevrigtd
ifg
>d1b55a_ 2.49.1.1.5 Bruton's tyrosine kinase {Human (Homo sapiens)}
aavilesiflkrsqqkkktsplnfkkrlflltvhklsyyeydfergrrgskkgsidveki
tcvetvvpeknppperqiprrgeessemeqisiierfpypfqvvydegplyvfspteelr
krwihqlknvirynsdlvqkyhpcfwidgqylccsqtaknamgcqilen
>d1b55b_ 2.49.1.1.5 Bruton's tyrosine kinase {Human (Homo sapiens)}
aavilesiflkrsqqkkktsplnfkkrlflltvhklsyyeydfergrrgskkgsidveki
tcvetvvpeknppperqiprrgeessemeqisiierfpypfqvvydegplyvfspteelr
krwihqlknvirynsdlvqkyhpcfwidgqylccsqtaknamgcqilen
>d1b56__ 2.53.1.2.5 Epidermal fatty acid binding protein {Human (Homo sapiens)}
tvqqlegrwrlvdskgfdeymkelgvgialrkmgamakpdciitcdgknltiktestlkt
tqfsctlgekfeettadgrktqtvcnftdgalvqhqewdgkestitrklkdgklvvecvm
nnvtctriyekve
>d1b58a_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b5a__ 4.94.1.1.2 Cytochrome b5 {Rat (Rattus norvegicus)}
dkdvkyytleeiqkhkdskstwvilhhkvydltkfleehpggeevlreqaggdatenfed
vghstdarelsktyiigelhpddrskiakpsetl
>d1b5b__ 4.94.1.1.2 Cytochrome b5 {Rat (Rattus norvegicus)}
dkdvkyytleeiqkhkdskstwvilhhkvydltkfleehpggeevlreqaggdatenfed
vghstdarelsktyiigelhpddrskiakpsetl
>d1b5da_ 4.91.1.1.7 dCMP hydroxymethylase {Bacteriophage T4}
misdsmtveeirlhlglalkekdfvvdktgvktieiigasfvadepfifgalndeyiqre
lewykskslfvkdipgetpkiwqqvasskgeinsnygwaiwsednyaqydmclaelgqnp
dsrrgimiytrpsmqfdynkdgmsdfmctntvqylirdkkinavvnmrsndvvfgfrndy
awqkyvldklvsdlnagdstrqykagsiiwnvgslhvysrhfylvdhwwktgethiskkd
yvgkya
>d1b5dc_ 4.91.1.1.7 dCMP hydroxymethylase {Bacteriophage T4}
misdsmtveeirlhlglalkekdfvvdktgvktieiigasfvadepfifgalndeyiqre
lewykskslfvkdipgetpkiwqqvasskgeinsnygwaiwsednyaqydmclaelgqnp
dsrrgimiytrpsmqfdynkdgmsdfmctntvqylirdkkinavvnmrsndvvfgfrndy
awqkyvldklvsdlnagdstrqykagsiiwnvgslhvysrhfylvdhwwktgethiskkd
yvgkya
>d1b5ea_ 4.91.1.1.7 dCMP hydroxymethylase {Bacteriophage T4}
misdsmtveeirlhlglalkekdfvvdktgvktieiigasfvadepfifgalndeyiqre
lewykskslfvkdipgetpkiwqqvasskgeinsnygwaiwsednyaqydmclaelgqnp
dsrrgimiytrpsmqfdynkdgmsdfmctntvqylirdkkinavvnmrsndvvfgfrndy
awqkyvldklvsdlnagdstrqykagsiiwnvgslhvysrhfylvdhwwktgethiskkd
y
>d1b5ec_ 4.91.1.1.7 dCMP hydroxymethylase {Bacteriophage T4}
misdsmtveeirlhlglalkekdfvvdktgvktieiigasfvadepfifgalndeyiqre
lewykskslfvkdipgetpkiwqqvasskgeinsnygwaiwsednyaqydmclaelgqnp
dsrrgimiytrpsmqfdynkdgmsdfmctntvqylirdkkinavvnmrsndvvfgfrndy
awqkyvldklvsdlnagdstrqykagsiiwnvgslhvysrhfylvdhwwktgethiskkd
y
>e1b5f.1a 2.44.1.2.7 Plant acid proteinase, phytepsin {Cynara cardunculus}
gsavvaltndrdtsyfgeigigtppqkftvifdtgssvlwvpsskcinskacrahsmyes
sdsstykengtfgaiiygtgsitgffsqdsvtigdlvvkeqdfieatdeadnvflhrlfd
gilglsfqtisvpvwynmlnqglvkerrfsfwlnrnvdeeeggelvfggldpnhfrgdht
yvpvtyqyywqfgigdvligdkstgfcapgcqafadsgtsllsgptaivtqinhaigan
>e1b5f.1b 2.44.1.2.7 Plant acid proteinase, phytepsin {Cynara cardunculus}
eelqvdcntlssmpnvsftiggkkfgltpeqyilkvgkgeatqcisgftamdatllgplw
ilgdvfmrpyhtvfdygnllvgfaeaa
>e1b5f.2c 2.44.1.2.7 Plant acid proteinase, phytepsin {Cynara cardunculus}
savvaltndrdtsyfgeigigtppqkftvifdtgssvlwvpsskcinskacrahsmyess
dsstykengtfgaiiygtgsitgffsqdsvtigdlvvkeqdfieatdeadnvflhrlfdg
ilglsfqtisvpvwynmlnqglvkerrfsfwlnrnvdeeeggelvfggldpnhfrgdhty
vpvtyqyywqfgigdvligdkstgfcapgcqafadsgtsllsgptaivtqinhaigan
>e1b5f.2d 2.44.1.2.7 Plant acid proteinase, phytepsin {Cynara cardunculus}
eelqvdcntlssmpnvsftiggkkfgltpeqyilkvgkgeatqcisgftamdatllgplw
ilgdvfmrpyhtvfdygnllvgfaeaa
>e1b5g.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1b5g.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
eadcglrplfekksledkterellesyid
>d1b5ha_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b5ia_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b5ja_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b5l__ 1.27.1.3.7 Interferon-tau {Sheep (Ovis aries)}
cylsrklmldarenlklldrmnrlsphsclqdrkdfglpqemvegdqlqkdqafpvlyem
lqqsfnlfytehssaawdttlleqlctglqqqldhldtcrgqvmgeedselgnmdpivtv
kkyfqgiydylqekgysdcaweivrvemmraltvsttlqkrltk
>d1b5m__ 4.94.1.1.2 Cytochrome b5 {Rat (Rattus norvegicus)}
avtyyrleevakrntaeetwmvihgrvyditrflsehpggeevlleqagadatesfedvg
hspdaremlkqyyigdvhpndlkp
>d1b5sa_ 3.35.1.1.4 Dihydrolipoamide acetyltransferase {Bacillus stearothermophilus}
aaakpattegefpetrekmsgirraiakamvhskhtaphvtlmdeadvtklvahrkkfka
iaaekgikltflpyvvkalvsalreypvlntsiddeteeiiqkhyynigiaadtdrgllv
pvikhadrkpifalaqeinelaekardgkltpgemkgasctitnigsaggqwftpvinhp
evailgigriaekpivrdgeivaapmlalslsfdhrmidgataqkalnhikrllsdpell
lm
>d1b5sb_ 3.35.1.1.4 Dihydrolipoamide acetyltransferase {Bacillus stearothermophilus}
aaakpattegefpetrekmsgirraiakamvhskhtaphvtlmdeadvtklvahrkkfka
iaaekgikltflpyvvkalvsalreypvlntsiddeteeiiqkhyynigiaadtdrgllv
pvikhadrkpifalaqeinelaekardgkltpgemkgasctitnigsaggqwftpvinhp
evailgigriaekpivrdgeivaapmlalslsfdhrmidgataqkalnhikrllsdpell
lm
>d1b5sc_ 3.35.1.1.4 Dihydrolipoamide acetyltransferase {Bacillus stearothermophilus}
aakpattegefpetrekmsgirraiakamvhskhtaphvtlmdeadvtklvahrkkfkai
aaekgikltflpyvvkalvsalreypvlntsiddeteeiiqkhyynigiaadtdrgllvp
vikhadrkpifalaqeinelaekardgkltpgemkgasctitnigsaggqwftpvinhpe
vailgigriaekpivrdgeivaapmlalslsfdhrmidgataqkalnhikrllsdpelll
m
>d1b5sd_ 3.35.1.1.4 Dihydrolipoamide acetyltransferase {Bacillus stearothermophilus}
aaakpattegefpetrekmsgirraiakamvhskhtaphvtlmdeadvtklvahrkkfka
iaaekgikltflpyvvkalvsalreypvlntsiddeteeiiqkhyynigiaadtdrgllv
pvikhadrkpifalaqeinelaekardgkltpgemkgasctitnigsaggqwftpvinhp
evailgigriaekpivrdgeivaapmlalslsfdhrmidgataqkalnhikrllsdpell
lm
>d1b5se_ 3.35.1.1.4 Dihydrolipoamide acetyltransferase {Bacillus stearothermophilus}
aaakpattegefpetrekmsgirraiakamvhskhtaphvtlmdeadvtklvahrkkfka
iaaekgikltflpyvvkalvsalreypvlntsiddeteeiiqkhyynigiaadtdrgllv
pvikhadrkpifalaqeinelaekardgkltpgemkgasctitnigsaggqwftpvinhp
evailgigriaekpivrdgeivaapmlalslsfdhrmidgataqkalnhikrllsdpell
lm
>d1b5ta_ 3.1.21.1.1 Methylenetetrahydrofolate reductase {Escherichia coli}
gainvsfeffpprtaemeatlwnsidrlsslapkfvsvtygansgerdathsiikgiadr
tgleaaphltcidatpdelrtiardywnngirhivalrgdlppgsgapamyasdlvtllk
evadfdisvaaypevhpeaksaqadllnlkrkvdaganraitqfffdvesylrfrdrcvs
agidveiipgilpvsnfkqakkfaamtnvripawmaqmfdgldddaetrklvganiamdm
vkilsaegvadfhfytlnraemsyaichtlgvrpa
>d1b5tb_ 3.1.21.1.1 Methylenetetrahydrofolate reductase {Escherichia coli}
qinvsfeffpprtaemeqtlwnsidrlsslapkfvsvtyganagaraathsiiagiadrt
gleaaphltcidatpdelrtiardywnngirhivalrgdlppgagapamyasdlvtllke
vadfdisvaaypevhpeaksaqadllnlkrkvdaganraitqfffdvesylrfrdrcvsa
gidvaiipgilpvsnfaqaaafadmtnvripawmaqmfdgldddaetrklvganiamdmv
ailsregvkdfhfytlnraemsyaichtlgvapg
>d1b5tc_ 3.1.21.1.1 Methylenetetrahydrofolate reductase {Escherichia coli}
qinvsfeffpprtaameqtlwnsidrlsslapafvsvtygaaageadathsiiagiadrt
gleaaphltcvdaapaelrtiaaaywaagiahivalrgdlppyasdlvtllkevadfdis
vaaypevhpeaasaqadllnlkrkvdaganraitqfffdvasylafrdrcvsagidveii
pgilpvsnfkqakafaamtnvripawmaqmfdgldddaetralvganiamdmvailsaeg
vadfhfytlnraemsyaichtlgvrpa
>d1b5u__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgialanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawnawrnrcqnrd
vrqyvqgcgv
>d1b5v__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
arywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawnawrnrcqnrd
vrqyvqgcgv
>d1b5w__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
arywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawnawrnrcqnrd
vrqyvqgcgv
>d1b5x__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlacsallqdniadavacakrvvrdpqgirawnawrnrcqnrd
vrqyvqgcgv
>d1b5y__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakweagyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawnawrnrcqnrd
vrqyvqgcgv
>d1b5za_ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscaallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1b5zb_ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscaallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1b62a1 4.12.1.3.1 (217-332) DNA mismatch repair protein MutL {Escherichia coli}
gtafleqalaiewqhgdltlrgwvadpnhttpalaeiqycyvngrmmrdrlinhairqac
edklgadqqpafvlyleidphqvdvnvhpakhevrfhqsrlvhdfiyqgvlsvlqq
>d1b62a2 4.96.1.2.2 (1-216) DNA mismatch repair protein MutL {Escherichia coli}
mpiqvlppqlanqiaagevverpasvvkelvensldagatrididierggaklirirdng
cgikkdelalalarhatskiaslddleaiislgfrgealasissvsrltltsrtaeqqea
wqayaegrdmnvtvkpaahpvgttlevldlfyntparrkflrtektefnhideiirrial
arfdvtinlshngkivrqyravpeggqkerrlgaic
>d1b63a1 4.12.1.3.1 (217-331) DNA mismatch repair protein MutL {Escherichia coli}
gtafleqalaiewqhgdltlrgwvadpnhttpalaeiqycyvngrmmrdrlinhairqac
edklgadqqpafvlyleidphqvdvnvhpakhevrfhqsrlvhdfiyqgvlsvlq
>d1b63a2 4.96.1.2.2 (1-216) DNA mismatch repair protein MutL {Escherichia coli}
mpiqvlppqlanqiaagevverpasvvkelvensldagatrididierggaklirirdng
cgikkdelalalarhatskiaslddleaiislgfrgealasissvsrltltsrtaeqqea
wqayaegrdmnvtvkpaahpvgttlevldlfyntparrkflrtektefnhideiirrial
arfdvtinlshngkivrqyravpeggqkerrlgaic
>d1b64__ 4.47.12.1.1 Guanine nucleotide exchange factor domain from elongation factor-1 beta {Human (Homo sapiens)}
mlvakssilldvkpwddetdmakleecvrsiqadglvwgssklvpvgygikklqiqcvve
ddkvgtdmleeqitafedyvqsmdvaafnki
>d1b65a_ 4.125.1.1.1 L-aminopeptidase D-Ala-esterase/amidase {Ochrobactrum anthropi}
kprardlglpftgvtgpynaitdvdgvgvgfqtiieneprpgrkrparsgvtailphmqs
etpvpvyagvhrfngngemtgthwiedggyflgpvvitnthgigmahhatvrwmvdryas
tyqtddflwimpvvaetydgalndingfpvteadvrkaldnvasgpvqegncgggtgmit
ygfkggtgtasrvvefggrsftigalvqanhgqrdwltiagvpvgqhmrdgtpqsqlqer
gsiivvlatdlplmphqlkrlarrasigigrngtpggnnsgdifiafstanqrpmqhrsa
pfldvemvndepldtvylaavdsveeavvnamiaaedmggtpfdrllvqaidherlravl
rqygrla
>d1b65b_ 4.125.1.1.1 L-aminopeptidase D-Ala-esterase/amidase {Ochrobactrum anthropi}
kprardlglpftgvtgpynaitdvdgvgvgfqtiieneprpgrkrparsgvtailphmqs
etpvpvyagvhrfngngemtgthwiedggyflgpvvitnthgigmahhatvrwmvdryas
tyqtddflwimpvvaetydgalndingfpvteadvrkaldnvasgpvqegncgggtgmit
ygfkggtgtasrvvefggrsftigalvqanhgqrdwltiagvpvgqhmrdgtpqsqlqer
gsiivvlatdlplmphqlkrlarrasigigrngtpggnnsgdifiafstanqrpmqhrsa
pfldvemvndepldtvylaavdsveeavvnamiaaedmggtpfdrllvqaidherlravl
rqygrla
>d1b65c_ 4.125.1.1.1 L-aminopeptidase D-Ala-esterase/amidase {Ochrobactrum anthropi}
kprardlglpftgvtgpynaitdvdgvgvgfqtiieneprpgrkrparsgvtailphmqs
etpvpvyagvhrfngngemtgthwiedggyflgpvvitnthgigmahhatvrwmvdryas
tyqtddflwimpvvaetydgalndingfpvteadvrkaldnvasgpvqegncgggtgmit
ygfkggtgtasrvvefggrsftigalvqanhgqrdwltiagvpvgqhmrdgtpqsqlqer
gsiivvlatdlplmphqlkrlarrasigigrngtpggnnsgdifiafstanqrpmqhrsa
pfldvemvndepldtvylaavdsveeavvnamiaaedmggtpfdrllvqaidherlravl
rqygrla
>d1b65d_ 4.125.1.1.1 L-aminopeptidase D-Ala-esterase/amidase {Ochrobactrum anthropi}
kprardlglpftgvtgpynaitdvdgvgvgfqtiieneprpgrkrparsgvtailphmqs
etpvpvyagvhrfngngemtgthwiedggyflgpvvitnthgigmahhatvrwmvdryas
tyqtddflwimpvvaetydgalndingfpvteadvrkaldnvasgpvqegncgggtgmit
ygfkggtgtasrvvefggrsftigalvqanhgqrdwltiagvpvgqhmrdgtpqsqlqer
gsiivvlatdlplmphqlkrlarrasigigrngtpggnnsgdifiafstanqrpmqhrsa
pfldvemvndepldtvylaavdsveeavvnamiaaedmggtpfdrllvqaidherlravl
rqygrla
>d1b65e_ 4.125.1.1.1 L-aminopeptidase D-Ala-esterase/amidase {Ochrobactrum anthropi}
kprardlglpftgvtgpynaitdvdgvgvgfqtiieneprpgrkrparsgvtailphmqs
etpvpvyagvhrfngngemtgthwiedggyflgpvvitnthgigmahhatvrwmvdryas
tyqtddflwimpvvaetydgalndingfpvteadvrkaldnvasgpvqegncgggtgmit
ygfkggtgtasrvvefggrsftigalvqanhgqrdwltiagvpvgqhmrdgtpqsqlqer
gsiivvlatdlplmphqlkrlarrasigigrngtpggnnsgdifiafstanqrpmqhrsa
pfldvemvndepldtvylaavdsveeavvnamiaaedmggtpfdrllvqaidherlravl
rqygrla
>d1b65f_ 4.125.1.1.1 L-aminopeptidase D-Ala-esterase/amidase {Ochrobactrum anthropi}
kprardlglpftgvtgpynaitdvdgvgvgfqtiieneprpgrkrparsgvtailphmqs
etpvpvyagvhrfngngemtgthwiedggyflgpvvitnthgigmahhatvrwmvdryas
tyqtddflwimpvvaetydgalndingfpvteadvrkaldnvasgpvqegncgggtgmit
ygfkggtgtasrvvefggrsftigalvqanhgqrdwltiagvpvgqhmrdgtpqsqlqer
gsiivvlatdlplmphqlkrlarrasigigrngtpggnnsgdifiafstanqrpmqhrsa
pfldvemvndepldtvylaavdsveeavvnamiaaedmggtpfdrllvqaidherlravl
rqygrla
>d1b66a_ 4.75.1.2.1 6-pyruvoyl tetrahydropterin synthase {Rat (Rattus rattus)}
lrrrarlsrlvsfsashrlhspslsaeenlkvfgkcnnpnghghnykvvvtihgeidpvt
gmvmnltdlkeymeeaimkpldhknldldvpyfadvvsttenvavyiwenlqrllpvgal
ykvkvyetdnnivvykge
>d1b66b_ 4.75.1.2.1 6-pyruvoyl tetrahydropterin synthase {Rat (Rattus rattus)}
lrrrarlsrlvsfsashrlhspslsaeenlkvfgkcnnpnghghnykvvvtihgeidpvt
gmvmnltdlkeymeeaimkpldhknldldvpyfadvvsttenvavyiwenlqrllpvgal
ykvkvyetdnnivvykge
>d1b69a_ 4.9.1.1.1 DNA-binding domain from tn916 integrase {Enterococcus faecalis}
ekrrdnrgrilktgesqrkdgrylykyidsfgepqfvyswklvatdrvpagkrdaislre
kiaelqkdi
>d1b6ca_ 4.23.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1b6cb_ 4.117.1.1.19 Type I TGF-beta recetor R4 {Human (Homo sapiens)}
ttlkdliydmttsgsgsglpllvqrtiartivlqesigkgrfgevwrgkwrgeevavkif
ssreerswfreaeiyqtvmlrhenilgfiaadnkdngtwtqlwlvsdyhehgslfdylnr
ytvtvegmiklalstasglahlhmeivgtqgkpaiahrdlksknilvkkngtcciadlgl
avrhdsatdtidiapnhrvgtkrymapevlddsinmkhfesfkradiyamglvfweiarr
csiggihedyqlpyydlvpsdpsveemrkvvceqklrpnipnrwqscealrvmakimrec
wyangaarltalrikktlsqlsqqeg
>d1b6cc_ 4.23.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1b6cd_ 4.117.1.1.19 Type I TGF-beta recetor R4 {Human (Homo sapiens)}
ttlkdliydmttsgsgsglpllvqrtiartivlqesigkgrfgevwrgkwrgeevavkif
ssreerswfreaeiyqtvmlrhenilgfiaadnkdngtwtqlwlvsdyhehgslfdylnr
ytvtvegmiklalstasglahlhmeivgtqgkpaiahrdlksknilvkkngtcciadlgl
avrhdsatdtidiapnhrvgtkrymapevlddsinmkhfesfkradiyamglvfweiarr
csiggihedyqlpyydlvpsdpsveemrkvvceqklrpnipnrwqscealrvmakimrec
wyangaarltalrikktlsqlsqqeg
>d1b6ce_ 4.23.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1b6cf_ 4.117.1.1.19 Type I TGF-beta recetor R4 {Human (Homo sapiens)}
ttlkdliydmttsgsgsglpllvqrtiartivlqesigkgrfgevwrgkwrgeevavkif
ssreerswfreaeiyqtvmlrhenilgfiaadnkdngtwtqlwlvsdyhehgslfdylnr
ytvtvegmiklalstasglahlhmeivgtqgkpaiahrdlksknilvkkngtcciadlgl
avrhdsatdtidiapnhrvgtkrymapevlddsinmkhfesfkradiyamglvfweiarr
csiggihedyqlpyydlvpsdpsveemrkvvceqklrpnipnrwqscealrvmakimrec
wyangaarltalrikktlsqlsqqeg
>d1b6cg_ 4.23.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1b6ch_ 4.117.1.1.19 Type I TGF-beta recetor R4 {Human (Homo sapiens)}
ttlkdliydmttsgsgsglpllvqrtiartivlqesigkgrfgevwrgkwrgeevavkif
ssreerswfreaeiyqtvmlrhenilgfiaadnkdngtwtqlwlvsdyhehgslfdylnr
ytvtvegmiklalstasglahlhmeivgtqgkpaiahrdlksknilvkkngtcciadlgl
avrhdsatdtidiapnhrvgtkrymapevlddsinmkhfesfkradiyamglvfweiarr
csiggihedyqlpyydlvpsdpsveemrkvvceqklrpnipnrwqscealrvmakimrec
wyangaarltalrikktlsqlsqqeg
>d1b6da1 2.1.1.1.153 (1-107) Immunoglobulin (variable domains of L and H chains) {Bence-Jones kappa L chain DEL (human)}
diqmtqspsslsasvgdrvtitcqasqdisrylrwyqqkpgkapkllihaassletgvps
rfsgsgsgtdfsftisslqpedlatyycqqydnlpltfgggtkveik
>d1b6da2 2.1.1.2.138 (108-212) Immunoglobulin (constant domains of L and H chains) {Bence-Jones kappa L chain DEL (human)}
rtvaapsvfifppsdeqlksgtasvvcllddfypreakvqwkvdnalqsgnsqesvteqd
skdstyslsstltlskadyekhkvyacevthqglsspvtksfnrg
>d1b6db1 2.1.1.1.153 (1-107) Immunoglobulin (variable domains of L and H chains) {Bence-Jones kappa L chain DEL (human)}
diqmtqspsslsasvgdrvtitcqasqdisrylrwyqqkpgkapkllihaassletgvps
rfsgsgsgtdfsftisslqpedlatyycqqydnlpltfgggtkveik
>d1b6db2 2.1.1.2.138 (108-212) Immunoglobulin (constant domains of L and H chains) {Bence-Jones kappa L chain DEL (human)}
rtvaapsvfifppsdeqlksgtasvvcllddfypreakvqwkvdnalqsgnsqesvteqd
skdstyslsstltlskadyekhkvyacevthqglsspvtksfnrg
>d1b6e__ 4.139.1.1.2 CD94 {Human (Homo sapiens)}
cscqekwvgyrcncyfisseqktwnesrhlcasqkssllqlqntdeldfmsssqqfywig
lsyseehtawlwengsalsqylfpsfetfntknciaynpngnaldescedknryickqql
i
>d1b6g__ 3.59.1.6.1 Haloalkane dehalogenase {Xanthobacter autotrophicus}
mvnairtpdqrfsnldqypfspnylddlpgypglrahyldegnsdaedvflclhgeptws
ylyrkmipvfaesgarviapdffgfgksdkpvdeedytfefhrnfllalierldlrnitl
vvqdwggflgltlpmadpsrfkrliimnaxlmtdpvtqpafsafvtqpadgftawkydlv
tpsdlrldqfmkrwaptlteaeasayaapfpdtsyqagvrkfpkmvaqrdqaxidistea
isfwqndwngqtfmaigmkdkllgpdvmypmkalingcpepleiadaghfvqefgeqvar
ealkhfaete
>d1b6ha_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b6q__ 1.31.1.1.1 ROP protein {Escherichia coli}
mtkqektalnmarfirsqtltlleklneldpdeqadiceslhdhadelyrsclarf
>d1b6va_ 4.5.1.1.6 Hybrid between ribonuclease A and seminal ribonuclease {Bos taurus}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvkavcsq
kkvtckngqtncyqskstmritdcretgsskypncaykttqankhiivacggkpyvpvhf
dasv
>d1b6vb_ 4.5.1.1.6 Hybrid between ribonuclease A and seminal ribonuclease {Bos taurus}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvkavcsq
kkvtckngqtncyqskstmritdcretgsskypncaykttqankhiivacggkpyvpvhf
dasv
>d1b72a_ 1.4.1.1.10 Homeobox protein hox-b1 {Human (Homo sapiens)}
artfdwmkvkrnppktakvsepglgspsglrtnfttrqltelekefhfnkylsrarrvei
aatlelnetqvkiwfqnrrmkqkkrere
>d1b72b_ 1.4.1.1.11 pbx1 {Human (Homo sapiens)}
rkrrnfnkqateilneyfyshlsnpypseeakeelakkcgitvsqvsnwfgnkrirykkn
igkfqeeaniyaa
>d1b76a1 3.42.1.1.3 (395-505) Glycyl-tRNA synthetase (GlyRS), C-terminal domain {Thermus thermophilus}
qlapikvaviplvknrpeiteyakrlkarllalglgrvlyedtgnigkayrrhdevgtpf
avtvdydtigqskdgttrlkdtvtvrdrdtmeqirlhvdelegflrerlrw
>d1b76a2 4.82.1.1.5 (1-394) Glycyl-tRNA synthetase (GlyRS) {Thermus thermophilus}
aassldelvalckrrgfifqsseiygglqgvydygplgvelknnlkqawwrrnvyerddm
egldasvlthrlvlhysgheatfadpmvdnakarywtppryfnmmfqdlrgprggrglla
ylrpetaqgifvnfknvldatsrklgfgiaqigkafrneitprnfifrvrefeqmeieyf
vrpgedeywhrywveerlkwwqemglsrenlvpyqqppessahyakatvdilyrfphgsl
elegiaqrtdfdlgshtkdqealgitarvlrnehstqrlayrdpetgkwfvpyviepsag
vdrgvlallaeaftreelpngeerivlklkp
>d1b76b1 3.42.1.1.3 (395-505) Glycyl-tRNA synthetase (GlyRS), C-terminal domain {Thermus thermophilus}
qlapikvaviplvknrpeiteyakrlkarllalglgrvlyedtgnigkayrrhdevgtpf
avtvdydtigqskdgttrlkdtvtvrdrdtmeqirlhvdelegflrerlrw
>d1b76b2 4.82.1.1.5 (1-394) Glycyl-tRNA synthetase (GlyRS) {Thermus thermophilus}
aassldelvalckrrgfifqsseiygglqgvydygplgvelknnlkqawwrrnvyerddm
egldasvlthrlvlhysgheatfadpmvdnakarywtppryfnmmfqdlrgprggrglla
ylrpetaqgifvnfknvldatsrklgfgiaqigkafrneitprnfifrvrefeqmeieyf
vrpgedeywhrywveerlkwwqemglsrenlvpyqqppessahyakatvdilyrfphgsl
elegiaqrtdfdlgshtkdqealgitarvlrnehstqrlayrdpetgkwfvpyviepsag
vdrgvlallaeaftreelpngeerivlklkp
>d1b77a1 4.105.1.2.1 (1-110) gp45 sliding clamp {Bacteriophage rb69}
mklskdtiailknfasinsgillsqgkfimtravngttyaeanisdeidfdvalydlnsf
lsilslvsddaeismhtdgnikiadtrstvywpaadkstivfpnkpiqfp
>d1b77a2 4.105.1.2.1 (111-228) gp45 sliding clamp {Bacteriophage rb69}
vasviteikaedlqqllrvsrglqidtiaitnkdgkivingynkvedsgltrpkysltlt
dydgsnnfnfvinmanmkiqpgnykvmlwgagdkvaakfessqvsyviameadsthdf
>d1b77b1 4.105.1.2.1 (1-110) gp45 sliding clamp {Bacteriophage rb69}
mklskdtiailknfasinsgillsqgkfimtravngttyaeanisdeidfdvalydlnsf
lsilslvsddaeismhtdgnikiadtrstvywpaadkstivfpnkpiqfp
>d1b77b2 4.105.1.2.1 (111-228) gp45 sliding clamp {Bacteriophage rb69}
vasviteikaedlqqllrvsrglqidtiaitnkdgkivingynkvedsgltrpkysltlt
dydgsnnfnfvinmanmkiqpgnykvmlwgagdkvaakfessqvsyviameadsthdf
>d1b77c1 4.105.1.2.1 (1-110) gp45 sliding clamp {Bacteriophage rb69}
mklskdtiailknfasinsgillsqgkfimtravngttyaeanisdeidfdvalydlnsf
lsilslvsddaeismhtdgnikiadtrstvywpaadkstivfpnkpiqfp
>d1b77c2 4.105.1.2.1 (111-228) gp45 sliding clamp {Bacteriophage rb69}
vasviteikaedlqqllrvsrglqidtiaitnkdgkivingynkvedsgltrpkysltlt
dydgsnnfnfvinmanmkiqpgnykvmlwgagdkvaakfessqvsyviameadsthdf
>d1b79a_ 1.78.1.1.1 N-terminal domain of DnaB helicase {Escherichia coli}
pphsieaeqsvlgglmldnerwddvaervvaddfytrphrhiftemarlqesgspidlit
laeslerqgqldsvggfaylaelskntpsaanisayadivre
>d1b79b_ 1.78.1.1.1 N-terminal domain of DnaB helicase {Escherichia coli}
pphsieaeqsvlgglmldnerwddvaervvaddfytrphrhiftemarlqesgspidlit
laeslerqgqldsvggfaylaelskntpsaanisayadivrer
>d1b79c_ 1.78.1.1.1 N-terminal domain of DnaB helicase {Escherichia coli}
pphsieaeqsvlgglmldnerwddvaervvaddfytrphrhiftemarlqesgspidlit
laeslerqgqldsvggfaylaelskntpsaanisayadivre
>d1b79d_ 1.78.1.1.1 N-terminal domain of DnaB helicase {Escherichia coli}
pphsieaeqsvlgglmldnerwddvaervvaddfytrphrhiftemarlqesgspidlit
laeslerqgqldsvggfaylaelskntpsaanisayadivrer
>d1b7aa_ 2.15.1.1.2 Phosphatidylethanolamine binding protein {Bovine (Bos taurus)}
pvdlskwsgplslqevderpqhplqvkyggaevdelgkvltptqvknrptsitwdgldpg
klytlvltdpdapsrkdpkyrewhhflvvnmkgnnissgtvlsdyvgsgppkgtglhryv
wlvyeqegplkcdepilsnrsgdhrgkfkvasfrkkyelgapvagtcyqaewddyvpkly
eqlsgg
>d1b7ab_ 2.15.1.1.2 Phosphatidylethanolamine binding protein {Bovine (Bos taurus)}
pvdlskwsgplslqevderpqhplqvkyggaevdelgkvltptqvknrptsitwdgldpg
klytlvltdpdapsrkdpkyrewhhflvvnmkgnnissgtvlsdyvgsgppkgtglhryv
wlvyeqegplkcdepilsnrsgdhrgkfkvasfrkkyelgapvagtcyqaewddyvpkly
eqlsgg
>d1b7da_ 7.3.7.1.9 Scorpion toxin {Scorpion (Tityus serrulatus)}
kegylmdhegcklscfirpsgycgrecgikkgssgycawpacycyglpnwvkvwdratnk
c
>d1b7ea_ 3.46.3.4.1 Transposase inhibitor (Tn5 transposase) {Escherichia coli}
saeairkagamqtvklaqefpellaiedttslsyrhqvaeelgklgsiqdksrgwwvhsv
llleattfrtvgllhqewwmrpddpadadekesgkwlaaaatsrlrmgsmmsnviavcdr
eadihaylqdklahnerfvvrskhprkdvesglylydhlknqpelggyqisipqkgvvdk
rgkrknrparkaslslrsgritlkqgnitlnavlaeeinppkgetplkwllltsepvesl
aqalrvidiythrwrieefhkawktgagaerqrmeepdnlermvsilsfvavrllqlres
ftlpqalraqgllkeaehvesqsaetvltpdecqllgyldkgkrkrkekagslqwaymai
arlggfmdskrtgiaswgalwegwealqskldgflaakdlmaq
>d1b7fa1 4.47.7.1.5 (123-204) Sex-lethal protein {Drosophila melanogaster}
sntnlivnylpqdmtdrelyalfraigpintcrimrdyktgysygyafvdftsemdsqra
ikvlngitvrnkrlkvsyarpg
>d1b7fa2 4.47.7.1.5 (205-289) Sex-lethal protein {Drosophila melanogaster}
gesikdtnlyvtnlprtitddqldtifgkygsivqknilrdkltgrprgvafvrynkree
aqeaisalnnvipeggsqplsvrla
>d1b7fb1 4.47.7.1.5 (123-204) Sex-lethal protein {Drosophila melanogaster}
sntnlivnylpqdmtdrelyalfraigpintcrimrdyktgysygyafvdftsemdsqra
ikvlngitvrnkrlkvsyarpg
>d1b7fb2 4.47.7.1.5 (205-289) Sex-lethal protein {Drosophila melanogaster}
gesikdtnlyvtnlprtitddqldtifgkygsivqknilrdkltgrprgvafvrynkree
aqeaisalnnvipeggsqplsvrla
>d1b7go1 3.2.1.3.5 (1-138,301-340) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Sulfolobus solfataricus)}
mvnvavngygtigkrvadaiikqpdmklvgvaktspnyeafiahrrgiriyvpqqsikkf
eesgipvagtvedliktsdivvdttpngvgaqykpiylqlqrnaifqggekaevadisfs
alcnynealgkkyirvvsXesivvpenidairasmklmsaedsmritneslgilkgyli
>d1b7go2 4.61.1.1.5 (139-300) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Sulfolobus solfataricus)}
cnttallrtictvnkvskvekvrativrraadqkevkkgpinslvpdpatvpshhakdvn
svirnldiatmaviapttlmhmhfinitlkdkvekkdilsvlentprivlisskydaeat
aelvevardlkrdrndipevmifsdsiyvkddevmlmyavhq
>d1b7gq1 3.2.1.3.5 (1-138,301-340) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Sulfolobus solfataricus)}
mvnvavngygtigkrvadaiikqpdmklvgvaktspnyeafiahrrgiriyvpqqsikkf
eesgipvagtvedliktsdivvdttpngvgaqykpiylqlqrnaifqggekaevadisfs
alcnynealgkkyirvvsXesivvpenidairasmklmsaedsmritneslgilkgyli
>d1b7gq2 4.61.1.1.5 (139-300) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Sulfolobus solfataricus)}
cnttallrtictvnkvskvekvrativrraadqkevkkgpinslvpdpatvpshhakdvn
svirnldiatmaviapttlmhmhfinitlkdkvekkdilsvlentprivlisskydaeat
aelvevardlkrdrndipevmifsdsiyvkddevmlmyavhq
>d1b7ha_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b7ia_ 2.75.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
anqasvvanqlipintaltlvmmrsevvtpvgipaediprlvsmqvnravplgttlmpdm
vrgyaa
>d1b7ja_ 2.75.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
anqasvvanqlipintaltlammrsevvtpvgipaediprlvsmqvnravplgttlmpdm
vkgyaa
>d1b7ka_ 2.75.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
anqasvvanqlipintaltlvmmrsevvtpvgipaediprlvsmqvnhavplgttlmpdm
vkgyaa
>d1b7l__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmcllkwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawnawrnrcqnrd
vrqyvqgcgv
>d1b7m__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavaclkrvvrdpqgirawnawrnrcqnrd
vrqyvqgcgv
>d1b7n__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwlsgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawnawrnrcqnrd
vrqyvqgcgv
>d1b7o__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesqyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawnawrnrcqnrd
vrqyvqgcgv
>d1b7p__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnacglscsallqdniadavacakrvvrdpqgirawnawrnrcqnrd
vrqyvqgcgv
>d1b7q__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislalwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawnawrnrcqnrd
vrqyvqgcgv
>d1b7r__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifgin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawnawrnrcqnrd
vrqyvqgcgv
>d1b7s__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgasnachlscsallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1b7ta1 2.30.3.1.2 (29-76) Myosin S1 fragment, N-terminal domain {Bay scallop (Aequipecten irradians)}
dgkkncwvpdekegfasaeiqsskgdeitvkivadsstrtvkkddiqs
>d1b7ta2 3.30.1.7.2 (5-28) Myosin S1, motor domain {Bay scallop (Aequipecten irradians)}
fsdpdfqylavdrkklmkeqtaaf
>d1b7ta3 3.30.1.7.2 (77-835) Myosin S1, motor domain {Bay scallop (Aequipecten irradians)}
mnppkfekledmanmtylneasvlynlrsrytsgliytysglfciavnpyrrlpiytdsv
iakyrgkrkteipphlfsvadnayqnmvtdrenqsclitgesgagktentkkvimylakv
acavkkkdeeasdkkegsledqiiqanpvleaygnakttrnnnssrfgkfirihfgptgk
iagadietylleksrvtyqqsaernyhifyqicsnaipelndvmlvtpdsglysfinqgc
ltvdniddveefklcdeafdilgftkeekqsmfkctasilhmgemkfkqrpreeqaesdg
taeaekvaflcginagdllkallkpkvkvgtemvtkgqnmnqvvnsvgalakslydrmfn
wlvrrvnktldtkakrnyyigvldiagfeifdfnsfeqlcinytnerlqqffnhhmfile
qeeykkegiawefidfgmdlqmcidliekpmgilsileeecmfpkaddksfqdklyqnhm
gknrmftkpgkptrpnqgpahfelhhyagnvpysitgwleknkdpinenvvallgaskep
lvaelfkapeepagggkkkkgkssafqtisavhreslnklmknlysthphfvrciipnel
kqpglvdaelvlhqlqcngvlegiricrkgfpsrliysefkqrysilapnaipqgfvdgk
tvsekilaglqmdpaeyrlgttkvffkagvlgnleemrderlskiismfqahirgylirk
aykklqdqriglsviqrnirkwlvlrnwqwwklyskvkp
>d1b7ty_ 1.42.1.5.15 Myosin Essential Chain {Bay scallop (Aequipecten irradians)}
pqkqiqemkeafsmidvdrdgfvskedikaiseqlgrapddkeltamlkeapgplnftmf
lsifsdklsgtdseetirnafamfdeqetkklnieyikdllenmgdnfnkdemrmtfkea
pveggkfdyvkftamikg
>d1b7tz_ 1.42.1.5.17 Myosin Regulatory Chain {Bay scallop (Aequipecten irradians)}
klsqdeiddlkdvfelfdfwdgrdgavdafklgdvcrclginprnedvfavggthkmgek
slpfeeflpayeglmdceqgtfadymeafktfdregqgfisgaelrhvltalgerlsded
vdeiikltdlqedlegnvkyedfvkkvmagpyp
>d1b7ua1 3.84.1.2.4 (1-333) Lactoferrin {Horse (Equus caballus)}
aprksvrwctispaeaakcakfqrnmkkvrgpsvscirktssfeciqaiaankadavtld
gglvyeaglhpyklrpvaaevyqtrgkpqtryyavavvkkgsgfqlnqlqgvkschtglg
rsagwnipigtlrpylnwtgppeplqkavanffsascvpcadgkqypnlcrlcagteadk
cacssqepyfgysgafkclengagdvafvkdstvfenlpdeaerdkyellcpdntrkpvd
afkechlarvpshavvarsvdgredliwkllhraqeefgrnkssafqlfgstpgeqdllf
kdsalgfvripsqidsglylganyltatqnlre
>d1b7ua2 3.84.1.2.4 (334-689) Lactoferrin {Horse (Equus caballus)}
taaevaarrervvwcavgpeeerkckqwsdvsnrkvacasastteecialvlkgeadaln
ldggfiyvagkcglvpvlaenqksqnsnapdcvhrppegylavavvrksdadltwnslsg
kkschtgvgrtaawnipmgllfnqtgsckfdkffsqscapgadpqsslcalcvgnnenen
kcmpnseeryygytgafrclaekagdvafvkdvtvlqntdgknsepwakdlkqedfellc
ldgtrkpvaeaeschlarapnhavvsqsdraqhlkkvlflqqdqfggngpdcpgkfclfk
setknllfndnteclaelqgkttyeqylgseyvtsitnlrrcsssplleacaflra
>e1b7x.1a 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1b7x.1b 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvclpd
retaasllqagykgrvtgwgnlkegqpsvlqvvnlpiverpvckdstriritdnmfcagy
kpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkigfythvfrlkkwi
qkvidq
>d1b7za1 3.84.1.2.4 (1-333) Lactoferrin {Horse (Equus caballus)}
aprksvrwctispaeaakcakfqrnmkkvrgpsvscirktssfeciqaiaankadavtld
gglvyeaglhpyklrpvaaevyqtrgkpqtryyavavvkkgsgfqlnqlqgvkschtglg
rsagwnipigtlrpylnwtgppeplqkavanffsascvpcadgkqypnlcrlcagteadk
cacssqepyfgysgafkclengagdvafvkdstvfenlpdeaerdkyellcpdntrkpvd
afkechlarvpshavvarsvdgredliwkllhraqeefgrnkssafqlfgstpgeqdllf
kdsalgfvripsqidsglylganyltatqnlre
>d1b7za2 3.84.1.2.4 (334-689) Lactoferrin {Horse (Equus caballus)}
taaevaarrervvwcavgpeeerkckqwsdvsnrkvacasastteecialvlkgeadaln
ldggfiyvagkcglvpvlaenqksqnsnapdcvhrppegylavavvrksdadltwnslsg
kkschtgvgrtaawnipmgllfnqtgsckfdkffsqscapgadpqsslcalcvgnnenen
kcmpnseeryygytgafrclaekagdvafvkdvtvlqntdgknsepwakdlkqedfellc
ldgtrkpvaeaeschlarapnhavvsqsdraqhlkkvlflqqdqfggngpdcpgkfclfk
setknllfndnteclaelqgkttyeqylgseyvtsitnlrrcsssplleacaflra
>d1b80a_ 1.90.1.1.1 Lignin peroxidase {White rot basidiomycete (Phanerochaete chrysosporium)}
viekratcsngktvgdasccawfdvlddiqqnlfhggqcgaeahesirlvfhdsiaispa
meaqgkfggggadgsimifddietafhpnigldeivklqkpfvqkhgvtpgdfiafagrv
alsncpgapqmnfftgrapatqpapdglvpepfhtvdqiinrvndagefdelelvxmlsa
hsvaavndvdptvqglpfdstpgifdsqffvetqlrgtafpgsggnqgevesplpgeiri
qsdhtiardsrtacewqsfvnnqsklvddfqfiflaltqlgqdpnamtdcsdvipqskpi
pgnlpfsffpagktikdveqacaetpfptlttlpgpetsvqrippppga
>d1b80b_ 1.90.1.1.1 Lignin peroxidase {White rot basidiomycete (Phanerochaete chrysosporium)}
ratcsngktvgdasccawfdvlddiqqnlfhggqcgaeahesirlvfhdsiaispameaq
gkfggggadgsimifddietafhpnigldeivklqkpfvqkhgvtpgdfiafagrvalsn
cpgapqmnfftgrapatqpapdglvpepfhtvdqiinrvndagefdelelvxmlsahsva
avndvdptvqglpfdstpgifdsqffvetqlrgtafpgsggnqgevesplpgeiriqsdh
tiardsrtacewqsfvnnqsklvddfqfiflaltqlgqdpnamtdcsdvipqskpipgnl
pfsffpagktikdveqacaetpfptlttlpgpetsvqrippppga
>d1b82a_ 1.90.1.1.1 Lignin peroxidase {White rot basidiomycete (Phanerochaete chrysosporium)}
viekratcsngktvgdasccawfdvlddiqqnlfhggqcgaeahesirlvfhdsiaispa
meaqgkfggggadgsimifddietafhpnigldeivklqkpfvqkhgvtpgdfiafagav
alsncpgapqmnfftgrapatqpapdglvpepfhtvdqiinrvndagefdelelvwmlsa
hsvaavndvdptvqglpfdstpgifdsqffvetqlrgtafpgsggnqgevesplpgeiri
qsdhtiardsrtacewqsfvnnqsklvddfqfiflaltqlgqdpnamtdcsdvipqskpi
pgnlpfsffpagktikdveqacaetpfptlttlpgpetsvqrippppga
>d1b82b_ 1.90.1.1.1 Lignin peroxidase {White rot basidiomycete (Phanerochaete chrysosporium)}
ratcsngktvgdasccawfdvlddiqqnlfhggqcgaeahesirlvfhdsiaispameaq
gkfggggadgsimifddietafhpnigldeivklqkpfvqkhgvtpgdfiafagavalsn
cpgapqmnfftgrapatqpapdglvpepfhtvdqiinrvndagefdelelvwmlsahsva
avndvdptvqglpfdstpgifdsqffvetqlrgtafpgsggnqgevesplpgeiriqsdh
tiardsrtacewqsfvnnqsklvddfqfiflaltqlgqdpnamtdcsdvipqskpipgnl
pfsffpagktikdveqacaetpfptlttlpgpetsvqrippppga
>d1b85a_ 1.90.1.1.1 Lignin peroxidase {White rot basidiomycete (Phanerochaete chrysosporium)}
iekratcsngktvgdasccawfdvlddiqqnlfhggqcgaeahesirlvfhdsiaispam
eaqgkfggggadgsimifddietafhpnigldeivklqkpfvqkhgvtpgdfiafagava
lsncpgapqmnfftgrapatqpapdglvpepfhtvdqiinrvndagefdelelvfmlsah
svaavndvdptvqglpfdstpgifdsqffvetqlrgtafpgsggnqgevesplpgeiriq
sdhtiardsrtacewqsfvnnqsklvddfqfiflaltqlgqdpnamtdcsdvipqskpip
gnlpfsffpagktikdveqacaetpfptlttlpgpetsvqrippppga
>d1b85b_ 1.90.1.1.1 Lignin peroxidase {White rot basidiomycete (Phanerochaete chrysosporium)}
ratcsngktvgdasccawfdvlddiqqnlfhggqcgaeahesirlvfhdsiaispameaq
gkfggggadgsimifddietafhpnigldeivklqkpfvqkhgvtpgdfiafagavalsn
cpgapqmnfftgrapatqpapdglvpepfhtvdqiinrvndagefdelelvfmlsahsva
avndvdptvqglpfdstpgifdsqffvetqlrgtafpgsggnqgevesplpgeiriqsdh
tiardsrtacewqsfvnnqsklvddfqfiflaltqlgqdpnamtdcsdvipqskpipgnl
pfsffpagktikdveqacaetpfptlttlpgpetsvqrippppga
>d1b86a_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1b86b_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1b86c_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1b86d_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1b87a_ 4.84.1.1.1 Aminoglycoside 6'-N-acetyltransferase {Enterococcus faecium}
miisefdrnnpvlkdqlsdllrltwpeeygdssaeeveemmnperiavaavdqdelvgfi
gaipqygitgwelhplvvessrrknqigtrlvnylekevasrggitiylgtddldhgttl
sqtdlyehtfdkvasiqnlrehpyefyeklgykivgvlpnangwdkpdiwmaktiiprpd
s
>d1b88a_ 2.1.1.1.155 T-cell antigen receptor {Human (Homo sapiens), alpha-chain}
mqqvrqspqsltvwegetailncsyensafdyfpwyqqfpgegpallisilsvsnkkedg
rftiffnkrekklslhiadsqpgdsatyfcaasasfgdnskliwglgtslvvnp
>d1b88b_ 2.1.1.1.155 T-cell antigen receptor {Human (Homo sapiens), alpha-chain}
mqqvrqspqsltvwegetailncsyensafdyfpwyqqfpgegpallisilsvsnkkedg
rftiffnkrekklslhiadsqpgdsatyfcaasasfgdnskliwglgtslvvnp
>d1b89a_ 1.110.1.3.1 Clathrin heavy chain proximal leg segment {Bovine (Bos taurus)}
rlaeleefingpnnahiqqvgdrcydekmydaakllynnvsnfgrlastlvhlgeyqaav
dgarkanstrtwkevcfacvdgkefrlaqxcglhivvhadeleelinyyqdrgyfeelit
xleaalglerahxgxftelailyskfkpqkxrehlelfwsrvnipkvlraaeqahlwael
vflydkyeeydnaiitxxnhptdawkegqfkdiitkvanvelyyraiqfylefkplllnd
llxvlsprldhtravnyfskvkqlplvkpylrsvqnhnnksvneslnnlfiteedyqalr
tsidaydnfdnislaqrlekheliefrriaaylfkg
>d1b8aa1 2.35.4.1.2 (1-103) Aspartyl-tRNA synthetase (AspRS) {Pyrococcus kodakaraensis}
myrthysseiteelngqkvkvagwvwevkdlggikflwirdrdgivqitapkkkvdpelf
klipklrsedvvavegvvnftpkaklgfeilpekivvlnraet
>d1b8aa2 4.82.1.1.8 (104-438) Aspartyl-tRNA synthetase (AspRS) {Pyrococcus kodakaraensis}
plpldptgkvkaeldtrlnnrfmdlrrpevmaifkirssvfkavrdffhengfieihtpk
iiatateggtelfpmkyfeedaflaespqlykeimmasgldrvyeiapifraeehnttrh
lneawsidsemafiedeeevmsflerlvahainyvrehnakeldilnfeleepklpfprv
sydkaleilgdlgkeipwgedidtegerllgkymmenenaplyflyqypseakpfyimky
dnkpeicrafdleyrgveissggqrehrhdilveqikekglnpesfefylkafrygmpph
ggfglgaerlikqmldlpnirevilfprdrrrltp
>d1b8ab1 2.35.4.1.2 (1001-1103) Aspartyl-tRNA synthetase (AspRS) {Pyrococcus kodakaraensis}
myrthysseiteelngqkvkvagwvwevkdlggikflwirdrdgivqitapkkkvdpelf
klipklrsedvvavegvvnftpkaklgfeilpekivvlnraet
>d1b8ab2 4.82.1.1.8 (1104-1438) Aspartyl-tRNA synthetase (AspRS) {Pyrococcus kodakaraensis}
plpldptgkvkaeldtrlnnrfmdlrrpevmaifkirssvfkavrdffhengfieihtpk
iiatateggtelfpmkyfeedaflaespqlykeimmasgldrvyeiapifraeehnttrh
lneawsidsemafiedeeevmsflerlvahainyvrehnakeldilnfeleepklpfprv
sydkaleilgdlgkeipwgedidtegerllgkymmenenaplyflyqypseakpfyimky
dnkpeicrafdleyrgveissggqrehrhdilveqikekglnpesfefylkafrygmpph
ggfglgaerlikqmldlpnirevilfprdrrrltp
>d1b8ba_ 3.6.1.2.1 Class III anaerobic ribonucleotide triphosphate reductase NRDD subunit {Bacteriophage T4}
srvfptqrdlmagivskhiaknmvpsfimkahesgiihvhdidyspalpftncclvdlkg
mlengfklgnaqietpksigvataimaqitaqvashqyggttfanvdkvlspyvkrtyak
hiedaekwqiadalnyaqsktekdvydafqayeyevntlfssngqtpfvtltfgtgtdwt
ermiqkailknrikglgrdgitpifpklvmfveegvnlykddpnydikqlalecaskrmy
pdiisaknnkaitgssvpvspmgcrsflsvwkdstgneildgrnnlgvvtlnlprialds
yigtqfneqkfvelfnermdlcfealmcrisslkgvkatvapilyqegafgvrlkpdddi
ielfkngrssvslgyigihelnilvgrdigreiltkmnahlkqwtertgfafslystpae
nlcyrfckldtekygsvkdvtdkgwytnsfhvsveenitpfekisreapyhfiatgghis
yvelpdmknnlkgleavwdyaaqhldyfgvnmpvdkcftcgsthemtptengfvcsicge
tdpkkmntirrtcgylgnpnerg
>d1b8ca_ 1.42.1.4.2 Parvalbumin {Carp (Cyprinus carpio)}
afagvlndadiaaaleackaadsfnhkaffakvgltsksaddvkkafaiiaqdksgfiee
delklflqnfkadaraltdgetktflkagdsdgdgkigvddwtalvka
>d1b8cb_ 1.42.1.4.2 Parvalbumin {Carp (Cyprinus carpio)}
afagvlndadiaaaleackaadsfnhkaffakvgltsksaddvkkafaiiaqdksgfiee
delklflqnfkadaraltdgetktflkagdsdgdgkigvddwtalvka
>d1b8da_ 1.1.1.2.6 Phycoerythrin {Red alga (Griffithsia monilis)}
mksvitttisaadaagrfpsssdlesiqgniqraaarleaaqklsgnheavvkeagdacf
akysylknageagdspekinkcyrdidhymrlinyslvvggtgpvdewgiagsrevyral
nlpgsayiaaftftrdrlcvprdmssqagveftsaldyvinslc
>d1b8db_ 1.1.1.2.6 Phycoerythrin {Red alga (Griffithsia monilis)}
mldafsrvvvtsdakaayvggsdlqslksfindgnkrldavnyivsnascivsdavsgmi
cenpgliapggxcytnrrmaaclrdgeiilryvsyallagdssvlddrclnglketyial
gvptasssravsimkatatafitntasgrkvevaagdcqalqaeaasyfdkvgssid
>d1b8dk_ 1.1.1.2.6 Phycoerythrin {Red alga (Griffithsia monilis)}
mksvitttisaadaagrfpsssdlesiqgniqraaarleaaqklsgnheavvkeagdacf
akysylknageagdspekinkcyrdidhymrlinyslvvggtgpvdewgiagsrevyral
nlpgsayiaaftftrdrlcvprdmssqagveftsaldyvinslc
>d1b8dl_ 1.1.1.2.6 Phycoerythrin {Red alga (Griffithsia monilis)}
mldafsrvvvtsdakaayvggsdlqslksfindgnkrldavnyivsnascivsdavsgmi
cenpgliapggxcytnrrmaaclrdgeiilryvsyallagdssvlddrclnglketyial
gvptasssravsimkatatafitntasgrkvevaagdcqalqaeaasyfdkvgssid
>d1b8fa_ 1.117.1.2.1 Histidine ammonia-lyase (HAL) {Pseudomonas putida}
teltlkpgtltlaqlraihaapvrlqldasaapaidasvacveqiiaedrtaygintgfg
llastriashdlenlqrslvlshaagigapldddlvrlimvlkinslsrgfsgirrkvid
alialvnaevyphiplkgsvgasgdlaplahmslvllgegkarykgqwlsatealavagl
epltlaakeglallngtqastayalrglfyaedlyaaaiacgglsveavlgsrspfdari
heargqrgqidtaacfrdllgdssevslshknadkvqdpyslrcqpqvmgacltqlrqaa
evlgieanavsdnplvfaaegdvisggnfhaepvamaadnlalaiaeigslserrislmm
dkhmsqlppflvenggvnsgfmiaqvtaaalasenkalshphsvdslptsanqedhvsma
paagkrlwemaentrgvlaiewlgacqgldlrkglktsaklekarqalrsevahydrdrf
fapdiekavellakgsltgllpagvlpsl
>d1b8ha1 4.105.1.2.1 (1-110) gp45 sliding clamp {Bacteriophage rb69}
mklskdtiailknfasinsgillsqgkfimtravngttyaeanisdeidfdvalydlnsf
lsilslvsddaeismhtdgnikiadtrstvywpaadkstivfpnkpiqfp
>d1b8ha2 4.105.1.2.1 (111-228) gp45 sliding clamp {Bacteriophage rb69}
vasviteikaedlqqllrvsrglqidtiaitnkdgkivingynkvedsgltrpkysltlt
dydgsnnfnfvinmanmkiqpgnykvmlwgagdkvaakfessqvsyviameadsthdf
>d1b8hb1 4.105.1.2.1 (1-110) gp45 sliding clamp {Bacteriophage rb69}
mklskdtiailknfasinsgillsqgkfimtravngttyaeanisdeidfdvalydlnsf
lsilslvsddaeismhtdgnikiadtrstvywpaadkstivfpnkpiqfp
>d1b8hb2 4.105.1.2.1 (111-228) gp45 sliding clamp {Bacteriophage rb69}
vasviteikaedlqqllrvsrglqidtiaitnkdgkivingynkvedsgltrpkysltlt
dydgsnnfnfvinmanmkiqpgnykvmlwgagdkvaakfessqvsyviameadsthdf
>d1b8hc1 4.105.1.2.1 (1-110) gp45 sliding clamp {Bacteriophage rb69}
mklskdtiailknfasinsgillsqgkfimtravngttyaeanisdeidfdvalydlnsf
lsilslvsddaeismhtdgnikiadtrstvywpaadkstivfpnkpiqfp
>d1b8hc2 4.105.1.2.1 (111-228) gp45 sliding clamp {Bacteriophage rb69}
vasviteikaedlqqllrvsrglqidtiaitnkdgkivingynkvedsgltrpkysltlt
dydgsnnfnfvinmanmkiqpgnykvmlwgagdkvaakfessqvsyviameadsthdf
>d1b8ia_ 1.4.1.1.14 Ultrabithorax (ubx) homeodomain {Drosophila melanogaster}
fypwmaiagtnglrrrgrqtytryqtlelekefhtnhyltrrrriemahalslterqiki
wfqnrrmklkkei
>d1b8ib_ 1.4.1.1.15 Extradenticle (exd) homeodomain {Drosophila melanogaster}
rrnfskqaseilneyfyshlsnpypseeakeelarkcgitvsqvsnwfgnkrirykkn
>d1b8ja_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdxaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1b8jb_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdxaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1b8ka_ 7.17.1.3.1 Brain-derived neurotrophic factor/neurotrophin 3 heterodimer, BDNF/NT3 {Human (Homo sapiens)}
ysvcdseslwvtdkssaidirghqvtvlgeiktgnspvkqyfyetrckearpvkngcrgi
ddkhwnsqcktsqtyvraltsennklvgwrwiridtscvcal
>d1b8la_ 1.42.1.4.2 Parvalbumin {Carp (Cyprinus carpio)}
afagvlndadiaaaleackaadsfnhkaffakvgltsksaddvkkafaiiaqdksgfiee
delklflqnfkadaraltdgetktflkagdsdgdgkigvddwtalvka
>d1b8ma_ 7.17.1.3.2 Neurotrophin 4 heterodimer {Human (Homo sapiens)}
gelsvcdsisewvtaadkktavdmsggtvtvlekvpvskgqlkqyfyetkcnpmgytkeg
crgidkrhwnsqcrttqsyvraltmdskkrigwrfiridtscvctltik
>d1b8mb_ 7.17.1.3.2 Neurotrophin 4 heterodimer {Human (Homo sapiens)}
gelavcdavsgwvtdrrtavdlrgrevevlgevpaaggsplrqyffetrckadnaeeggp
gaggggcrgvdrrhwvseckakqsyvraltadaqgrvgwrwiridtacvctllsrtgra
>d1b8na_ 3.47.1.1.2 Purine nucleoside phosphorylase, PNP {Bovine (Bos taurus)}
qngytyedyqdtakwllshteqrpqvavicgsglgglvnkltqaqtfdyseipnfpestv
pghagrlvfgilngracvmmqgrfhmyegypfwkvtfpvrvfrllgvetlvvtnaaggln
pnfevgdimlirdhinlpgfsgenplrgpneerfgvrfpamsdaydrdmrqkahstwkqm
geqrelqegtyvmlggpnfetvaecrllrnlgadavgmstvpevivarhcglrvfgfsli
tnkvimdyesqgkanheevleagkqaaqkleqfvsllm
>d1b8oa_ 3.47.1.1.2 Purine nucleoside phosphorylase, PNP {Bovine (Bos taurus)}
ngytyedyqdtakwllshteqrpqvavicgsglgglvnkltqaqtfdyseipnfpestvp
ghagrlvfgilngracvmmqgrfhmyegypfwkvtfpvrvfrllgvetlvvtnaagglnp
nfevgdimlirdhinlpgfsgenplrgpneerfgvrfpamsdaydrdmrqkahstwkqmg
eqrelqegtyvmlggpnfetvaecrllrnlgadavgmstvpevivarhcglrvfgfslit
nkvimdyesqgkanheevleagkqaaqkleqfvsllmasi
>d1b8pa1 3.2.1.5.6 (3-158) Malate dehydrogenase {Aquaspirillum arcticum}
ktpmrvavtgaagqicysllfriangdmlgkdqpvilqlleipnekaqkalqgvmmeidd
cafpllagmtahadpmtafkdadvallvgarprgpgmerkdlleanaqiftvqgkaidav
asrnikvlvvgnpantnayiamksapslpaknftam
>d1b8pa2 4.132.1.1.6 (159-329) Malate dehydrogenase {Aquaspirillum arcticum}
lrldhnralsqiaaktgkpvssieklfvwgnhsptmyadyryaqidgasvkdminddawn
rdtflptvgkrgaaiidargvssaasaanaaidhihdwvlgtagkwttmgipsdgsygip
egvifgfpvttengeykivqglsidafsqerinvtlnelleeqngvqhllg
>d1b8qa_ 2.32.1.1.6 Neuronal nitric oxide synthase, NNOS {Rat (Rattus norvegicus)}
gshmiepnvisvrlfkrkvgglgflvkervskppviisdlirggaaeqsgliqagdiila
vndrplvdlsydsalevlrgiasethvvlilrgpegftthlettftgdgtpktirvtqpl
gpptkav
>d1b8ra_ 1.42.1.4.2 Parvalbumin {Carp (Cyprinus carpio)}
afagvlndadiaaaleackaadsfnhkaffakvgltsksaddvkkafaiidqdksgfiee
delklflqnfkadaraltdgetktflkagdsdgdgkigvdewtalvka
>d1b8sa1 3.3.1.2.2 (9-318,451-506) Cholesterol oxidase {Streptomyces}
gyvpavvigtgygaavsalrlgeagvqtlmlemgqlwnqpgpdgnifcgmlnpdkrsswf
knrteaplgsflwldvvnrnidpyagvldrvnydqmsvyvgrgvgggslvnggmavepkr
syfeeilprvdssemydryfpransmlrvnhidtkwfedtewykfarvsreqagkaglgt
vfvpnvydfgymqreaagevpksalateviygnnhgkqsldktylaaalgtgkvtiqtlh
qvktirqtkdggyaltveqkdtdgkllatkeiscrylflgagslgstellvrardtgtlp
nlnsevgagwXgcvlgkatddygrvagyknlyvtdgslipgsvgvnpfvtitalaernve
riikqdv
>d1b8sa2 4.14.1.1.2 (319-450) Cholesterol oxidase {Streptomyces}
gpngnimtaranhmwnptgahqssipalgidawdnsdssvfaqiapmpagletwvslyla
itknpqrgtfvydaatdraklnwtrdqnapavnaakalfdrinkangtiyrydlfgtqlk
afaddfcyhplg
>d1b8ta1 7.33.1.3.1 (1-35) Cysteine-rich (intestinal) protein, CRP, CRIP {Chicken (Gallus gallus)}
mpnwgggkkcgvcqkavyfaeevqcegssfhkscf
>d1b8ta2 7.33.1.3.1 (36-100) Cysteine-rich (intestinal) protein, CRP, CRIP {Chicken (Gallus gallus)}
lcmvckknldsttvavhgdeiyckscygkkygpkgkgkgmgagtlstdkgeslgikyeeg
qshrp
>d1b8ta3 7.33.1.3.1 (101-143) Cysteine-rich (intestinal) protein, CRP, CRIP {Chicken (Gallus gallus)}
tnpnasrmaqkvggsdgcprcgqavyaaekvigagkswhkscf
>d1b8ta4 7.33.1.3.1 (144-192) Cysteine-rich (intestinal) protein, CRP, CRIP {Chicken (Gallus gallus)}
rcakcgkslesttladkdgeiyckgcyaknfgpkgfgfgqgagalihsq
>d1b8ua1 3.2.1.5.6 (3-158) Malate dehydrogenase {Aquaspirillum arcticum}
ktpmrvavtgaagqicysllfriangdmlgkdqpvilqlleipnekaqkalqgvmmeidd
cafpllagmtahadpmtafkdadvallvgarprgpgmerkdlleanaqiftvqgkaidav
asrnikvlvvgnpantnayiamksapslpaknftam
>d1b8ua2 4.132.1.1.6 (159-329) Malate dehydrogenase {Aquaspirillum arcticum}
lrldhnralsqiaaktgkpvssieklfvwgnhsptmyadyryaqidgasvkdminddawn
rdtflptvgkrgaaiidargvssaasaanaaidhihdwvlgtagkwttmgipsdgsygip
egvifgfpvttengeykivqglsidafsqerinvtlnelleeqngvqhllg
>d1b8va1 3.2.1.5.6 (3-158) Malate dehydrogenase {Aquaspirillum arcticum}
ktpmrvavtgaagqicysllfriangdmlgkdqpvilqlleipnekaqkalqgvmmeidd
cafpllagmtahadpmtafkdadvallvgarprgpgmerkdlleanaqiftvqgkaidav
asrnikvlvvgnpantnayiamksapslpaknftam
>d1b8va2 4.132.1.1.6 (159-329) Malate dehydrogenase {Aquaspirillum arcticum}
lrldhnralsqiaaktgkpvssieklfvwgnhsptmyadyryaqidgasvkdminddawn
rdtflptvgkrgaaiidargvssaasaanaaidhihdwvlgtagkwttmgipsdgsygip
egvifgfpvttengeykivqglsidafsqerinvtlnelleeqngvqhllg
>d1b8wa_ 7.9.1.1.3 Defensin-like peptide 1 {Duckbilled platypus (Ornithorhynchus anatinus)}
fvqhrprdcesingvcrhkdtvncreifladcyndgqkccrk
>d1b8xa1 1.48.1.1.19 (81-260) Glutathione S-transferase {Escherichia coli}
lggcpkeraeismlegavldirygvsriayskdfetlkvdflsklpemlkmfedrlchkt
ylngdhvthpdfmlydaldvvlymdpmcldafpklvcfkkrieaipqidkylksskyiaw
plqgwqatfgggdhppksdlvprgsrrasvgsrmhypgaftysptpvtsgigigmsamgs
>d1b8xa2 3.38.1.5.19 (1-80) Glutathione S-transferase {Escherichia coli}
spilgywkikglvqptrllleyleekyeehlyerdegdkwrnkkfelglefpnlpyyidg
dvkltqsmaiiryiadkhnm
>d1b8ya_ 4.71.1.9.4 Stromelysin-1 (MMP-3) {Human (Homo sapiens), fibroblast}
frtfpgipkwrkthltyrivnytpdlpkdavdsavekalkvweevtpltfsrlyegeadi
misfavrehgdfypfdgpgnvlahayapgpgingdahfdddeqwtkdttgtnlflvaahe
ighslglfhsantealmyplyhsltdltrfrlsqddingiqslygpp
>d1b90a1 2.3.1.1.6 (418-516) beta-amylase {Bacillus cereus}
tpvmqtivvknvpttigdtvyitgnraelgswdtkqypiqlyydshsndwrgnvvlpaer
niefkafikskdgtvkswqtiqqswnpvplkttshtssw
>d1b90a2 3.1.7.2.3 (1-417) Bacterial beta-amylase, catalytic domain {Bacillus cereus}
avngkgmnpdykaylmaplkkipevtnwetfendlrwakqngfyaitvdfwwgdmekngd
qqfdfsyaqrfaqsvknagmkmipiisthqcggnvgddcnvpipswvwnqksddslyfks
etgtvnketlnplasdvirkeygelytafaaamkpykdviakiylsggpagelrypsytt
sdgtgypsrgkfqaytefakskfrlwvlnkygslnevnkawgtkliselailppsdgeqf
lmngylsmygkdylewyqgilenhtkligelahnafdttfqvpigakiagvhwqynnpti
phgaekpagyndyshlldafksakldvtftclemtdkgsypeysmpktlvqniatlanek
givlngenalsigneeeykrvaemafnynfagftllryqdvmynnslmgkfkdllgv
>d1b92a_ 3.46.3.2.2 HIV-1 integrase, catalytic domain {Human immunodeficiency virus, type 1}
cspgiwqldcthlegkvilvavhvasgyieaevipaetgqetayfllklagrwpvktvht
dngsnftsttvkaacwwagikqefgipynpqsqaviesmnkelkkiigqvrdqaehlkta
vqmavfihnkkrkggiggysagerivdiiatdiqt
>d1b93a_ 3.17.1.2.1 Methylglyoxal synthase, MgsA {Escherichia coli}
melttrtlparkhialvahdhckqmlmswverhqplleqhvlyatgttgnlisratgmnv
namlsgpmggdqqvgalisegkidvliffwdplnavphdpdvkallrlatvwnipvatnv
atadfiiqsphfndavdilipdyqryla
>d1b93b_ 3.17.1.2.1 Methylglyoxal synthase, MgsA {Escherichia coli}
melttrtlparkhialvahdhckqmlmswverhqplleqhvlyatgttgnlisratgmnv
namlsgpmggdqqvgalisegkidvliffwdplnavphdpdvkallrlatvwnipvatnv
atadfiiqsphfndavdilipdyqryladrl
>d1b93c_ 3.17.1.2.1 Methylglyoxal synthase, MgsA {Escherichia coli}
melttrtlparkhialvahdhckqmlmswverhqplleqhvlyatgttgnlisratgmnv
namlsgpmggdqqvgalisegkidvliffwdplnavphdpdvkallrlatvwnipvatnv
atadfiiqsphfndavdilipdyq
>d1b94a_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgrk
>d1b94b_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgrk
>d1b95a_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgrk
>d1b95b_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgrk
>d1b96a_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqenhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgrk
>d1b96b_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqenhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgrk
>d1b97a_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqlnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgrk
>d1b97b_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqlnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgrk
>d1b98a_ 7.17.1.3.2 Neurotrophin 4 heterodimer {Human (Homo sapiens)}
elavcdavsgwvtdrrtavdlrgrevevlgevpaaggsplrqyffetrckadnaeeggpg
aggggcrgvdrrhwvseckakqsyvraltadaqgrvgwrwiridtacvctllsrtgraaa
qyffetrckadnaeaggpgaggggcrgvdrrhwvseckakqsyvraltavgwrwiridta
cvctllsat
>d1b98m_ 7.17.1.3.2 Neurotrophin 4 heterodimer {Human (Homo sapiens)}
agelavcdavsgwvtdrrtavdlrgrevevlgevpaaggsplrqyffetrckadgggpga
ggggcrgvdrrhwvseckakqsyvraltadaqgrvgwrwiridtacvctllsa
>d1b99a_ 4.47.6.1.3 Nucleoside diphosphate kinases {Dictyostelium discodeum}
vnkertflavkpdgvarglvgeiiaryekkgfvlvglkqlvptkdlaeshyaehkerpff
gglvsfitsgpvvamvfegkgvvasarlmigvtnplasapgsirgdfgvdvgrniihgsd
svesanreialwfkpeelltevkpnpnlye
>d1b99b_ 4.47.6.1.3 Nucleoside diphosphate kinases {Dictyostelium discodeum}
vnkertflavkpdgvarglvgeiiaryekkgfvlvglkqlvptkdlaeshyaehkerpff
gglvsfitsgpvvamvfegkgvvasarlmigvtnplasapgsirgdfgvdvgrniihgsd
svesanreialwfkpeelltevkpnpnlye
>d1b99c_ 4.47.6.1.3 Nucleoside diphosphate kinases {Dictyostelium discodeum}
vnkertflavkpdgvarglvgeiiaryekkgfvlvglkqlvptkdlaeshyaehkerpff
gglvsfitsgpvvamvfegkgvvasarlmigvtnplasapgsirgdfgvdvgrniihgsd
svesanreialwfkpeelltevkpnpnlye
>d1b99d_ 4.47.6.1.3 Nucleoside diphosphate kinases {Dictyostelium discodeum}
vnkertflavkpdgvarglvgeiiaryekkgfvlvglkqlvptkdlaeshyaehkerpff
gglvsfitsgpvvamvfegkgvvasarlmigvtnplasapgsirgdfgvdvgrniihgsd
svesanreialwfkpeelltevkpnpnlye
>d1b99e_ 4.47.6.1.3 Nucleoside diphosphate kinases {Dictyostelium discodeum}
vnkertflavkpdgvarglvgeiiaryekkgfvlvglkqlvptkdlaeshyaehkerpff
gglvsfitsgpvvamvfegkgvvasarlmigvtnplasapgsirgdfgvdvgrniihgsd
svesanreialwfkpeelltevkpnpnlye
>d1b99f_ 4.47.6.1.3 Nucleoside diphosphate kinases {Dictyostelium discodeum}
vnkertflavkpdgvarglvgeiiaryekkgfvlvglkqlvptkdlaeshyaehkerpff
gglvsfitsgpvvamvfegkgvvasarlmigvtnplasapgsirgdfgvdvgrniihgsd
svesanreialwfkpeelltevkpnpnlye
>d1b9aa_ 1.42.1.4.2 Parvalbumin {Carp (Cyprinus carpio)}
afagvlndadiaaaleackaadsfnhkaffakvgltsksaddvkkafaiiaqdksgfiee
delklflqnfkadaraltdgetktflkagdsdgdgkigvdewtalvka
>d1b9da_ 3.46.3.2.2 HIV-1 integrase, catalytic domain {Human immunodeficiency virus, type 1}
spgiwqldcthlegkvilvavhvasgyieaevipaetgqetayfllklagrwpvktvhtd
ngsnftsttvkaacwwagikqefgipynpqsqgviesmnkelkkiigqvrdqaehlktav
qmavfihnkkrkggiggysagerivdiiatdiqt
>d1b9fa_ 3.46.3.2.2 HIV-1 integrase, catalytic domain {Human immunodeficiency virus, type 1}
cspgiwqldcthlegkvilvavhvasgyieaevipaetgqetayfllklagrwpvktvht
dngsnftsttvkaacwwagikqefaipynpqsqaviesmnkelkkiigqvrdqaehlkta
vqmavfihnkkrkggiggysagerivdiiatdiqt
>d1b9ga_ 7.1.1.1.5 Insulin-like growth factor {Human (Homo sapiens)}
gpetlcgaelvdalqfvcgdrgfyfnkpgivdeccfrscdlrrlemycaplkpaksa
>d1b9ha_ 3.57.1.4.8 3-amino-5-hydroxybenzoic acid synthase (AHBA synthase) {Amycolatopsis mediterranei}
kapefpawpqyddaernglvraleqgqwwrmggdevnsferefaahhgaahalavtngth
alelalqvmgvgpgtevivpaftfisssqaaqrlgavtvpvdvdaatynldpeavaaavt
prtkvimpvhmaglmadmdalakisadtgvpllqdaahahgarwqgkrvgeldsiatfsf
qngklmtageggavvfpdgetekyetaflrhscgrprddrryfhkiagsnmrlnefsasv
lraqlarldeqiavrderwtllsrllgaidgvvpqggdvradrnshymamfripglteer
rnalvdrlveaglpafaafraiyrtdafwelgapdesvdaiarrcpntdaissdcvwlhh
rvllagepelhataeiiadavara
>d1b9ia_ 3.57.1.4.8 3-amino-5-hydroxybenzoic acid synthase (AHBA synthase) {Amycolatopsis mediterranei}
kapefpawpqyddaernglvraleqgqwwrmggdevnsferefaahhgaahalavtngth
alelalqvmgvgpgtevivpaftfisssqaaqrlgavtvpvdvdaatynldpeavaaavt
prtkvimpvhmaglmadmdalakisadtgvpllqdaahahgarwqgkrvgeldsiatfsf
qngklmtageggavvfpdgetekyetaflrhscgrprddrryfhkiagsnmrlnefsasv
lraqlarldeqiavrderwtllsrllgaidgvvpqggdvradrnshymamfripglteer
rnalvdrlveaglpafaafraiyrtdafwelgapdesvdaiarrcpntdaissdcvwlhh
rvllagepelhataeiiadavgra
>d1b9ja_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b9ka1 2.1.9.1.1 (702-824) Alpa-adaptin AP2, N-terminal subdomain {Mouse (Mus musculus)}
ednfarfvcknngvlfenqllqiglksefrqnlgrmfifygnktstqflnftptlicadd
lqtnlnlqtkpvdptvdggaqvqqviniecisdfteapvlniqfryggtfqnvsvklpit
lnk
>d1b9ka2 4.83.1.1.1 (825-938) Alpa-adaptin AP2, C-terminal subdomain {Mouse (Mus musculus)}
ffqptemasqdffqrwkqlsnpqqevqnifkakhpmdteitkakiigfgsalleevdpnp
anfvgagiihtkttqigcllrlepnlqaqmyrltlrtskdtvsqrlcellseqf
>d1b9oa_ 4.2.1.2.14 alpha-Lactalbumin {Human (Homo sapiens)}
kqftkcelsqllkdidgyggialpelictmfhtsgydtqaivendesteyglfqisnklw
ckssqvpqsrnicdiscdkflddditddimcakkildikgidywlahkalctekleqwlc
ekl
>d1b9ra_ 4.13.6.1.12 Terpredoxin {Pseudomonas}
prvvfideqsgeyavdaqdgqslmevatqngvpgivaecggscvcatcrieiedawveiv
geanpdendllqstgepmtagtrlscqvfidpsmdglivrvplpa
>d1b9sa_ 2.59.1.1.3 Influenza neuraminidase {Influenza virus B, different strains}
epewtyprlscqgstfqkallisphrfgeikgnsapliirepfvacgpkecrhfalthya
aqpggyyngtrkdrnklrhlvsvklgkiptvensifhmaawsgsachdgrewtyigvdgp
dndalvkikygeaytdtyhsyahnilrtqesacnciggdcylmitdgsasgiskcrflki
regriikeilptgrvehteectcgfasnktiecacrdnsytakrpfvklnvetdtaeirl
mctktyldtprpddgsiagpcesngdkwlggikggfvhqrmaskigrwysrtmsktnrmg
melyvrydgdpwtdsdaltlsgvmvsieepgwysfgfeikdkkcdvpcigiemvhdggkd
twhsaataiyclmgsgqllwdtvtgvdmal
>d1b9ta_ 2.59.1.1.3 Influenza neuraminidase {Influenza virus B, different strains}
epewtyprlscqgstfqkallisphrfgeikgnsapliirepfvacgpkecrhfalthya
aqpggyyngtrkdrnklrhlvsvklgkiptvensifhmaawsgsachdgrewtyigvdgp
dndalvkikygeaytdtyhsyahnilrtqesacnciggdcylmitdgsasgiskcrflki
regriikeilptgrvehteectcgfasnktiecacrdnsytakrpfvklnvetdtaeirl
mctktyldtprpddgsiagpcesngdkwlggikggfvhqrmaskigrwysrtmsktnrmg
melyvrydgdpwtdsdaltlsgvmvsieepgwysfgfeikdkkcdvpcigiemvhdggkd
twhsaataiyclmgsgqllwdtvtgvdmal
>d1b9va_ 2.59.1.1.3 Influenza neuraminidase {Influenza virus B, different strains}
epewtyprlscqgstfqkallisphrfgeikgnsapliirepfvacgpkecrhfalthya
aqpggyyngtrkdrnklrhlvsvklgkiptvensifhmaawsgsachdgrewtyigvdgp
dndalvkikygeaytdtyhsyahnilrtqesacnciggdcylmitdgsasgiskcrflki
regriikeilptgrvehteectcgfasnktiecacrdnsytakrpfvklnvetdtaeirl
mctktyldtprpddgsiagpcesngdkwlggikggfvhqrmaskigrwysrtmsktnrmg
melyvrydgdpwtdsdaltlsgvmvsieepgwysfgfeikdkkcdvpcigiemvhdggkd
twhsaataiyclmgsgqllwdtvtgvdmal
>d1b9wa1 7.3.11.4.1 (1-45) Merozoite surface protein 1 (MSP-1) {Plasmodium cynomolgi}
mssehrcidtnvpenaacyryldgteewrcllyfkedagkcvpap
>d1b9wa2 7.3.11.4.1 (46-89) Merozoite surface protein 1 (MSP-1) {Plasmodium cynomolgi}
nmtckdknggcapeaeckmndkneivckctkegseplfegvfcs
>d1b9xa_ 2.60.3.1.1 beta1-subunit of the signal-transducing G protein heterotrimer {Bovine (Bos taurus)}
mseldqlrqeaeqlknqirdarkacadatlsqitnnidpvgriqmrtrrtlrghlakiya
mhwgtdsrlllsasqdgkliiwdsyttnkvhaiplrsswvmtcayapsgnyvacggldni
csiynlktregnvrvsrelaghtgylsccrflddnqivtssgdttcalwdietgqqtttf
tghtgdvmslslapdtrlfvsgacdasaklwdvregmcrqtftghesdinaicffpngna
fatgsddatcrlfdlradqelmtyshdniicgitsvsfsksgrlllagyddfncnvwdal
kadragvlaghdnrvsclgvtddgmavatgswdsflkiwn
>d1b9xb_ 1.125.2.1.1 Transducin (heterotrimeric G protein), gamma chain {Bovine (Bos taurus)}
mpviniedltekdklkmevdqlkkevtlermlvskcceefrdyveersgedplvkgiped
knpfkelk
>d1b9xc_ 3.38.1.6.1 Phosducin {Rat (Rattus norvegicus)}
egqathtgpkgvindwrkfklesedgdsippskkeilrqmsspqsrddkdskermsrkme
iqeyelihqdkedegclrkyrrqcmqdmhqklsfgprygfvyeletgeqfletiekeqkv
ttivvniyedgvrgcdalnssleclaaeypmvkfckirasntgagdrfssdvlptllvyk
ggelisnfisvaeqfaedffaadvesflneygllper
>d1b9ya_ 2.60.3.1.1 beta1-subunit of the signal-transducing G protein heterotrimer {Bovine (Bos taurus)}
mseldqlrqeaeqlknqirdarkacadatlsqitnnidpvgriqmrtrrtlrghlakiya
mhwgtdsrlllsasqdgkliiwdsyttnkvhaiplrsswvmtcayapsgnyvacggldni
csiynlktregnvrvsrelaghtgylsccrflddnqivtssgdttcalwdietgqqtttf
tghtgdvmslslapdtrlfvsgacdasaklwdvregmcrqtftghesdinaicffpngna
fatgsddatcrlfdlradqelmtyshdniicgitsvsfsksgrlllagyddfncnvwdal
kadragvlaghdnrvsclgvtddgmavatgswdsflkiwn
>d1b9yb_ 1.125.2.1.1 Transducin (heterotrimeric G protein), gamma chain {Bovine (Bos taurus)}
mpviniedltekdklkmevdqlkkevtlermlvskcceefrdyveersgedplvkgiped
knpfkelk
>d1b9yc_ 3.38.1.6.1 Phosducin {Rat (Rattus norvegicus)}
egqathtgpkgvindwrkfklesedgdsippskkeilrqmsspqsrddkdskermsrkms
iqeyelihqdkedegclrkyrrqcmqdmhqklsfgprygfvyeletgeqfletiekeqkv
ttivvniyedgvrgcdalnssleclaaeypmvkfckirasntgagdrfssdvlptllvyk
ggelisnfisvaeqfaedffaadvesflneygllper
>d1b9za1 2.3.1.1.6 (418-516) beta-amylase {Bacillus cereus}
tpvmqtivvknvpttigdtvyitgnraelgswdtkqypiqlyydshsndwrgnvvlpaer
niefkafikskdgtvkswqtiqqswnpvplkttshtssw
>d1b9za2 3.1.7.2.3 (1-417) Bacterial beta-amylase, catalytic domain {Bacillus cereus}
avngkgmnpdykaylmaplkkipevtnwetfendlrwakqngfyaitvdfwwgdmekngd
qqfdfsyaqrfaqsvknagmkmipiisthqcggnvgddcnvpipswvwnqksddslyfks
etgtvnketlnplasdvirkeygelytafaaamkpykdviakiylsggpagelrypsytt
sdgtgypsrgkfqaytefakskfrlwvlnkygslnevnkawgtkliselailppsdgeqf
lmngylsmygkdylewyqgilenhtkligelahnafdttfqvpigakiagvhwqynnpti
phgaekpagyndyshlldafksakldvtftclemtdkgsypeysmpktlvqniatlanek
givlngenalsigneeeykrvaemafnynfagftllryqdvmynnslmgkfkdllgv
>d1ba0_1 3.46.1.1.1 (4-188) Heat shock protein 70kDa, ATPase fragment {Bovine (Bos taurus)}
gpavgidlgttyscvgvfqhgkveiiandqgnrttpsyvaftdterligdaaknqvamnp
tntvfdakrligrrfddavvqsdmkhwpfmvvndagrpkvqveykgetksfypeevssmv
ltkmkeiaeaylgktvtnavvtvpayfndsqrqatkdagtiaglnvlriineptaaaiay
gldkk
>d1ba0_2 3.46.1.1.1 (189-381) Heat shock protein 70kDa, ATPase fragment {Bovine (Bos taurus)}
vgaernvlifdlgggtfkvsiltiedgifevkstagdthlggedfdnrmvnhfiaefkrk
hkkdisenkravrrlrtacerakrtlssstqasieidslyegidfytsitrarfeelnad
lfrgtldpvekalrdakldksqihdivlvggstripkiqkllqdffngkelnksinpdea
vaygaavqaails
>d1ba1_1 3.46.1.1.1 (4-188) Heat shock protein 70kDa, ATPase fragment {Bovine (Bos taurus)}
gpavgidlgttyskvgvfqhgkveiiandqgnrttpsyvaftdterligdaaknqvamnp
tntvfdakrligrrfddavvqsdmkhwpfmvvndagrpkvqveykgetksfypeevssmv
ltkmkeiaeaylgktvtnavvtvpayfndsqrqatkdagtiaglnvlriineptaaaiay
gldkk
>d1ba1_2 3.46.1.1.1 (189-381) Heat shock protein 70kDa, ATPase fragment {Bovine (Bos taurus)}
vgaernvlifdlgggtfdvsiltiedgifevkstagdthlggedfdnrmvnhfiaefkrk
hkkdisenkravrrlrtacerakrtlssstqasieidslyegidfytsitrarfeelnad
lfrgtldpvekalrdakldksqihdivlvggstripkiqkllqdffngkelnksinpdea
vaygaavqaails
>d1ba2a_ 3.83.1.1.1 D-ribose-binding protein {Escherichia coli, strain k-12}
kdtialvvstlnnpffvslkdgaqkeadklgynlvvldsqnnpakelanvqdltvrgtki
llinptrsdavgnavkmanqanipvitldrqatkgevvshiasdnvlggkiagdyiakka
gegakvielqgiagtsaarergegfqqavaahkfnvlasqpadfdrikglnvmqnlltah
pdvqavfaqndemalgalralqtagksdvmvvgfdgtpdgekavndgklaatiaqlpdqi
gakgvetadkvlkgekvqakypvdlklvvkq
>d1ba2b_ 3.83.1.1.1 D-ribose-binding protein {Escherichia coli, strain k-12}
kdtialvvstlnnpffvslkdgaqkeadklgynlvvldsqnnpakelanvqdltvrgtki
llinptrsdavgnavkmanqanipvitldrqatkgevvshiasdnvlggkiagdyiakka
gegakvielqgiagtsaarergegfqqavaahkfnvlasqpadfdrikglnvmqnlltah
pdvqavfaqndemalgalralqtagksdvmvvgfdgtpdgekavndgklaatiaqlpdqi
gakgvetadkvlkgekvqakypvdlklvvkq
>d1ba3__ 5.19.1.1.1 Luciferase {Firefly (Phontinus pyralis)}
daknikkgpapfypledgtageqlhkamkryalvpgtiaftdahievnityaeyfemsvr
laeamkryglntnhrivvcsenslqffmpvlgalfigvavapandiynerellnsmnisq
ptvvfvskkglqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfv
pesfdrdktialimnssgstglpkgvalphrtacvrfshardpifgnqiipdtailsvvp
fhhgfgmfttlgylicgfrvvlmyrfeeelflrslqdykiqsallvptlfsffakstlid
kydlsnlheiasggaplskevgeavakrfhlpgirqgygltettsailitpegddkpgav
gkvvpffeakvvdldtgktlgvnqrgelcvrgpmimsgyvnnpeatnalidkdgwlhsgd
iaywdedehffivdrlkslikykgyqvapaelesillqhpnifdagvaglpdddagelpa
avvvlehgktmtekeivdyvasqvttakklrggvvfvdevpkgltgkldarkireilika
kk
>d1ba5__ 1.4.1.4.1 DNA-binding domain of human telomeric protein, htrf1 {Human (Homo sapiens)}
rkrqawlweedknlrsgvrkygegnwskillhykfnnrtsvmlkdrwrtmkkl
>d1ba7a_ 2.37.4.1.4 Soybean trypsin inhibitor {Soybean (Glycine max)}
dfvldnegnplenggtyyilsditafggiraaptgnercpltvvqsrneldkgigtiiss
pyrirfiaeghplslkfdsfavimlcvgiptewsvvedlpegpavkigenkdamdgwfrl
ervsddefnnyklvfcpqqaeddkcgdigisidhddgtrrlvvsknkplvvqfqkl
>d1ba7b_ 2.37.4.1.4 Soybean trypsin inhibitor {Soybean (Glycine max)}
dfvldnegnplenggtyyilsditafggiraaptgnercpltvvqsrneldkgigtiiss
pyrirfiaeghplslkfdsfavimlcvgiptewsvvedlpegpavkigenkdamdgwfrl
ervsddefnnyklvfcpqqaeddkcgdigisidhddgtrrlvvsknkplvvqfqkl
>e1ba8.1a 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
sgeadcglrplfekksledkterellesyi
>e1ba8.1b 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>d1ba9__ 2.1.8.1.2 Cu,Zn superoxide dismutase, SOD {Human (Homo sapiens)}
atkavavlkgdgpvqgiinfeqkesngpvkvwgsikglteglhgfhvheeedntagctsa
gphfnplsrkhggpkdeerhvgdlgnvtadkdgvadvsiedsvislsgdhsiigrtlvvh
ekaddlgkggneqstktgnagsrlacgvigiaq
>d1baba_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
xmelspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkgh
gkkvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeft
pavhasldkflasvstvltskyr
>d1babb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1babc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
xmelspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkgh
gkkvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeft
pavhasldkflasvstvltskyr
>d1babd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1bafh1 2.1.1.1.14 (1-115) Immunoglobulin (variable domains of L and H chains) {Fab ANO2 (mouse), kappa L chain}
dvqlqesgpglvkpsqsqsltctvtgysitsdyawnwirqfpgnklewmgymsysgstry
npslrsrisitrdtsknqfflqlksvttedtatyfcargwplaywgqgtqvsvse
>d1bafh2 2.1.1.2.24 (116-217) Immunoglobulin (constant domains of L and H chains) {Fab ANO2 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpssprpsetvtcnvahpasstkvdkkivprdc
>d1bafl1 2.1.1.1.14 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab ANO2 (mouse), kappa L chain}
qivltqspaimsaspgekvtmtcsasssvyymywyqqkpgssprlliydtsnlasgvpvr
fsgsgsgtsysltisrmeaedaatyycqqwssyppitfgvgtklelkr
>d1bafl2 2.1.1.2.24 (109-214) Immunoglobulin (constant domains of L and H chains) {Fab ANO2 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1bag_1 2.62.1.1.3 (348-425) Bacterial alpha-Amylase (BLA) {Bacillus subtilis}
qpeelsnpngnnqifmnqrgshgvvlanagsssvsintatklpdgrydnkagagsfqvnd
gkltgtinarsvavlypd
>d1bag_2 3.1.7.1.3 (1-347) Bacterial alpha-amylase (BLA) {Bacillus subtilis}
ltapsiksgtilhawnwsfntlkhnmkdihdagytaiqtspinqvkegnqgdksmsnwyw
lyqptsyqignrylgteqefkemcaaaeeygikvivdavinhttfdyaaisnevksipnw
thgntqiknwsdrwdvtqnsllglydwntqntqvqsylkrfleralndgadgfrfdaakh
ielpddgsygsqfwpnitntsaefqygqilqdsasrdaayanymdvtasnyghsirsalk
nrnlgvsnishyasdvsadklvtwveshdtyanddeestwmsdddirlgwaviasrsgst
plffsrpegggngvrfpgksqigdrgsalfedqaitavnrfhnvmag
>d1bah__ 7.3.7.2.7 Charybdotoxin {Scorpion (Leiurus quinquestriatus hebraeus)}
ftnvscttskexwsvcqrlhntsrgkcmnkkxrcys
>d1baia_ 2.44.1.1.4 Rous sarcoma virus protease {Rous sarcoma virus, strain pr-C}
lamtmehkdrplvrviltntgshpvkqrsvyitalldtgaddtviseedwptdwpvmeaa
npqihgigggipvrksrdmielgvinrdgslerplllfplvamtpvnilgrdclqglglr
ltnl
>d1baib_ 2.44.1.1.4 Rous sarcoma virus protease {Rous sarcoma virus, strain pr-C}
lamtmehkdrplvrviltntgshpvkqrsvyitalldtgaddtviseedwptdwpvmeaa
npqihgigggipvrksrdmielgvinrdgslerplllfplvamtpvnilgrdclqglglr
ltnl
>d1baj__ 1.29.3.1.3 HIV capsid protein, dimerisation domain {Human immunodeficiency virus, type 1, HIV-1}
tsildirqgpkepfrdyvdrfyktlraeqasqevknwmtetllvqnanpdcktilkalgp
gatleemmtac
>d1bak__ 2.49.1.1.9 G-protein coupled receptor kinase 2 (beta-adrenergic receptor kinase 1) {Human (Homo sapiens)}
gshmgkdcimhgymskmgnpfltqwqrryfylfpnrlewrgegeapqslltmeeiqsvee
tqikerkclllkirggkqfilqcdsdpelvqwkkelrdayreaqqlvqrvpkmknkprs
>d1bal__ 1.9.1.1.2 E3-binding domain of dihydrolipoamide succinyltransferase {Escherichia coli}
yasleeqnndalspairrllaehnldasaikgtgvggrltredvekhlaka
>d1bam__ 3.43.1.3.1 Restriction endonuclease BamHI {Bacillus amyloliquefaciens}
mevekefitdeakellskdkliqqaynevktsicspiwpatsktftinntekncngvvpi
kelcytlledtynwyrekpldilklekkkggpidvykefienselkrvgmefetgnissa
hrsmnklllglkhgeidlaiilmpikqlayyltdrvtnfeelepyfeltegqpfifigfn
aeaynsnvplipkgsdgmskrsikkwkdkvenk
>d1bana_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyasdwliykttdhyqtftkir
>d1banb_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyasdwliykttdhyqtftkir
>d1banc_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
qvintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnreg
klpgksgrtwreadinytsgfrnsdrilyasdwliykttdhyqtftkir
>d1baoa_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinftsgfrnsdrilyssdwliykttdhyqtftkir
>d1baob_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinftsgfrnsdrilyssdwliykttdhyqtftkir
>d1baoc_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
intfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregkl
pgksgrtwreadinftsgfrnsdrilyssdwliykttdhyqtftkir
>d1bap__ 3.83.1.1.2 L-arabinose-binding protein {Escherichia coli}
nlklgflvkqpeepwfqtewkfadkagkdlgfevikiavpdgektlnaidslaasgakgf
victpdpklgsaivakargydmkviavddqfvnakgkpmdtvplvmmaatkigerqgqel
ykemqkrgwdvkesavmaitaneldtarrrttgsmdalkaagfpekqiyqvptksndipg
afdaansmlvqhpevkhwlivgmndstvlggvrategqgfkaadiigigingvdavsels
kaqatgfygsllgspdvhgykssemlynwvakdveppkftevtdvvlitrdnfkeelekk
glggk
>d1baq__ 1.77.1.1.1 Antitermination factor NusB {Escherichia coli}
mkpaarrrarecavqalyswqlsqndiadveyqflaeqdvkdvdvlyfrellagvatnta
yldglmkpylsrlleelgqvekavlrialyelskrsdvpykvaineaielaksfgaedsh
kfvngvldkaapvirpnkk
>d1bara_ 2.37.1.1.2 Acidic FGF {Bovine (Bos taurus)}
pkllycsnggyflrilpdgtvdgtkdrsdqhiqlqlaaesigevyikstetgqflamdtd
gllygsqtpneeclflerleengyntyiskkhaekhwfvglkkngrsklgprthfgqkai
lflplpv
>d1barb_ 2.37.1.1.2 Acidic FGF {Bovine (Bos taurus)}
fnlplgnykkpkllycsnggyflrilpdgtvdgtkdrsdqhiqlqlaaesigevyikste
tgqflamdtdgllygsqtpneeclflerleengyntyiskkhaekhwfvglkkngrsklg
prthfgqkailflplpvs
>d1bas__ 2.37.1.1.1 Basic FGF {Human (Homo sapiens)}
dpkrlycknggfflrihpdgrvdgvreksdphiklqlqaeergvvsikgvsanrylamke
dgrllasksvtdecffferlesnnyntyrsrkytswyvalkrtgqyklgsktgpgqkail
flpms
>d1bava_ 3.47.4.1.1 Carboxypeptidase A {Bovine (Bos taurus)}
arstntfnyatyhtldeiydfmdllvaqhpelvsklqigrsyegrpiyvlkfstggsnrp
aiwidlgihsrewitqatgvwfakkftenygqnpsftaildsmdifleivtnpngfafth
senrlwrktrsvtssslcvgvdanrnwdagfgkagassspcsetyhgkyansevevksiv
dfvknhgnfkaflsihsysqlllypygyttqsipdktelnqvaksavaalkslygtsyky
gsiittiyqasggsidwsynqgikysftfelrdtgrygfllpasqiiptaqetwlgvlti
mehtvnn
>d1bavb_ 3.47.4.1.1 Carboxypeptidase A {Bovine (Bos taurus)}
arstntfnyatyhtldeiydfmdllvaqhpelvsklqigrsyegrpiyvlkfstggsnrp
aiwidlgihsrewitqatgvwfakkftenygqnpsftaildsmdifleivtnpngfafth
senrlwrktrsvtssslcvgvdanrnwdagfgkagassspcsetyhgkyansevevksiv
dfvknhgnfkaflsihsysqlllypygyttqsipdktelnqvaksavaalkslygtsyky
gsiittiyqasggsidwsynqgikysftfelrdtgrygfllpasqiiptaqetwlgvlti
mehtvnn
>d1bavc_ 3.47.4.1.1 Carboxypeptidase A {Bovine (Bos taurus)}
arstntfnyatyhtldeiydfmdllvaqhpelvsklqigrsyegrpiyvlkfstggsnrp
aiwidlgihsrewitqatgvwfakkftenygqnpsftaildsmdifleivtnpngfafth
senrlwrktrsvtssslcvgvdanrnwdagfgkagassspcsetyhgkyansevevksiv
dfvknhgnfkaflsihsysqlllypygyttqsipdktelnqvaksavaalkslygtsyky
gsiittiyqasggsidwsynqgikysftfelrdtgrygfllpasqiiptaqetwlgvlti
mehtvnn
>d1bavd_ 3.47.4.1.1 Carboxypeptidase A {Bovine (Bos taurus)}
arstntfnyatyhtldeiydfmdllvaqhpelvsklqigrsyegrpiyvlkfstggsnrp
aiwidlgihsrewitqatgvwfakkftenygqnpsftaildsmdifleivtnpngfafth
senrlwrktrsvtssslcvgvdanrnwdagfgkagassspcsetyhgkyansevevksiv
dfvknhgnfkaflsihsysqlllypygyttqsipdktelnqvaksavaalkslygtsyky
gsiittiyqasggsidwsynqgikysftfelrdtgrygfllpasqiiptaqetwlgvlti
mehtvnn
>d1bawa_ 2.5.1.1.12 Plastocyanin {Cyanobacterium (Phormidium laminosum)}
etftvkmgadsgllqfepanvtvhpgdtvkwvnnklpphnilfddkqvpgaskeladkls
hsqlmfspgesyeitfssdfpagtytyycaphrgagmvgkitveg
>d1bawb_ 2.5.1.1.12 Plastocyanin {Cyanobacterium (Phormidium laminosum)}
etftvkmgadsgllqfepanvtvhpgdtvkwvnnklpphnilfddkqvpgaskeladkls
hsqlmfspgesyeitfssdfpagtytyycaphrgagmvgkitveg
>d1bawc_ 2.5.1.1.12 Plastocyanin {Cyanobacterium (Phormidium laminosum)}
etftvkmgadsgllqfepanvtvhpgdtvkwvnnklpphnilfddkqvpgaskeladkls
hsqlmfspgesyeitfssdfpagtytyycaphrgagmvgkitveg
>d1bax__ 1.62.1.3.1 Mason-pfizer monkey virus matrix protein {Simian mason-pfizer virus, MPMV}
mgqelsqheryveqlkqalktrgvkvkyadllkffdfvkdtcpwfpqegtidikrwrrvg
dcfqdyyntfgpekvpvtafsywnlikelidkke
>d1baya1 1.48.1.1.2 (79-209) Glutathione S-transferase {Mouse (Mus musculus)}
ygknqreaaqmdmvndgvedlrgkyvtliytnyengkndyvkalpghlkpfetllsqnqg
gkafivgdqisfadynlldlllihqvlapgcldnfpllsayvarlsarpkikaflsspeh
vnrpingngkq
>d1baya2 3.38.1.5.2 (1-78) Glutathione S-transferase {Mouse (Mus musculus), class pi}
ppytivyfpvrgrceamrmlladqgqswkeevvtidtwmqglkptclygqlpkfedgdlt
lyqsnailrhlgrslgl
>d1bayb1 1.48.1.1.2 (79-209) Glutathione S-transferase {Mouse (Mus musculus)}
ygknqreaaqmdmvndgvedlrgkyvtliytnyengkndyvkalpghlkpfetllsqnqg
gkafivgdqisfadynlldlllihqvlapgcldnfpllsayvarlsarpkikaflsspeh
vnrpingngkq
>d1bayb2 3.38.1.5.2 (1-78) Glutathione S-transferase {Mouse (Mus musculus), class pi}
ppytivyfpvrgrceamrmlladqgqswkeevvtidtwmqglkptclygqlpkfedgdlt
lyqsnailrhlgrslgl
>d1baza_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
skmpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1bazb_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
kmpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfk
>d1bazc_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegrig
>d1bazd_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfk
>e1bb0.1a 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1bb0.1b 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>d1bb3a_ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavaclkrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1bb3b_ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavaclkrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1bb4a_ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavaclkrvvrdpqgirahvawrnrcqnrd
vrqyvqgcgv
>d1bb4b_ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavaclkrvvrdpqgirahvawrnrcqnrd
vrqyvqgcgv
>d1bb5a_ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavaclkrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1bb5b_ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavaclkrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1bb6__ 4.2.1.2.11 Lysozyme {Rainbow trout (Oncorhynchus mykiss)}
kvydrcelaralkasgmdgyagnslpnwvclskwessyntqatnrntdgstdygifqins
rywcddgrtpgaknvcgircsqlltddltvaircakrvvldpngigawvawrlhcqnqdl
rsyvagcgv
>d1bb7__ 4.2.1.2.11 Lysozyme {Rainbow trout (Oncorhynchus mykiss)}
kvydrcelaralkasgmdgyagnslpnwvclskwessyntqatnrntdgstdygifqins
rywcddgrtpgaknvcgircsqlltddltvaircakrvvldpngigawvawrlhcqnqdl
rsyvagcgv
>d1bb8__ 4.9.1.1.1 DNA-binding domain from tn916 integrase {Enterococcus faecalis}
ekrrdnrgrilktgesqrkdgrylykyidsfgepqfvyswklvatdrvpagkrdcislre
kiaelqkdihd
>d1bb9__ 2.30.2.1.23 Amphiphysin 2 {Rat (Rattus norvegicus)}
ttgrldlppgfmfkvqaqhdytatdtdelqlkagdvvlvipfqnpeeqdegwlmgvkesd
wnqhkelekcrgvfpenftervq
>d1bbba_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1bbbb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1bbbc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1bbbd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1bbc__ 1.123.1.2.11 Phospholipase A2 {Human (Homo sapiens), synovial fluid}
nlvnfhrmiklttgkeaalsygfygchcgvggrgspkdatdrccvthdccykrlekrgcg
tkflsykfsnsgsritcakqdscrsqlcecdkaaatcfarnkttynkkyqyysnkhcrgs
tprc
>d1bbdh1 2.1.1.1.15 (1-119) Immunoglobulin (variable domains of L and H chains) {Fab 8F5 (mouse), kappa L chain}
evqlqqsgaelvrpgasvklscttsgfnikdiyihwvkqrpeqglewigrldpangytky
dpkfqgkatitvdtssntaylhlssltsedtavyycdgyysyydmdywgpgtsvtvssa
>d1bbdh2 2.1.1.2.25 (120-218) Immunoglobulin (constant domains of L and H chains) {Fab 8F5 (mouse), kappa L chain}
kttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsdl
ytlsssvtvtsstwpsqsitcnvahpasstkvdkkiepr
>d1bbdl1 2.1.1.1.15 (1-114) Immunoglobulin (variable domains of L and H chains) {Fab 8F5 (mouse), kappa L chain}
divmtqspssltvttgekvtmtckssqsllnsrtqknyltwyqqkpgqspklliywastr
esgvpdrftgsgsgtdftlsisgvqaedlavyycqnnynypltfgagtklelkr
>d1bbdl2 2.1.1.2.25 (115-219) Immunoglobulin (constant domains of L and H chains) {Fab 8F5 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrne
>d1bbg__ 7.6.1.1.1 <i>Amb</i> V allergen {Giant ragweed (Ambrosia trifida), pollen}
ddglcyegtncgkvgkyccspigkycvcydskaicnknct
>d1bbha_ 1.25.3.2.2 Cytochrome c' {Chromatium vinosum}
aglspeeqietrqagyefmgwnmgkikanlegeynaaqveaaanviaaiansgmgalygp
gtdknvgdvktrvkpeffqnmedvgkiarefvgaantlaevaatgeaeavktafgdvgaa
ckschekyrak
>d1bbhb_ 1.25.3.2.2 Cytochrome c' {Chromatium vinosum}
aglspeeqietrqagyefmgwnmgkikanlegeynaaqveaaanviaaiansgmgalygp
gtdknvgdvktrvkpeffqnmedvgkiarefvgaantlaevaatgeaeavktafgdvgaa
ckschekyrak
>d1bbi__ 7.3.13.1.1 Bowman-Birk inhibitor {Soybean (Glycine max)}
ddesskpccdqcactksnppqcrcsdmrlnschsackscicalsypaqcfcvditdfcye
pckpseddken
>d1bbjh1 2.1.1.1.16 (1-115) Immunoglobulin (variable domains of L and H chains) {Fab B72.3 (mouse/human chimera), kappa L chain}
xvqlqqsdaelvkpgasvkisckasgytftdhaihwakqkpeqglewigyispgnddiky
nekfkgkatltadkssstaymqlnsltsedsavyfckrsyyghwgqgttltvssa
>d1bbjh2 2.1.1.2.26 (116-212) Immunoglobulin (constant domains of L and H chains) {Fab B72.3 (mouse/human chimera), kappa L chain}
stkgpsvfplapcsrstsestaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqssg
lyslssvvtvpssslgtktytcnvdhkpsntkvdkrv
>d1bbjl1 2.1.1.1.16 (1-109) Immunoglobulin (variable domains of L and H chains) {Fab B72.3 (mouse/human chimera), kappa L chain}
diqmtqspaslsvsvgetvtitcraseniysnlawyqqkqgkspqllvyaatnladgvps
rfsgsgsgtqyslkinslqsedfgsyycqhfwgtpytfgggtrleikra
>d1bbjl2 2.1.1.2.26 (110-211) Immunoglobulin (constant domains of L and H chains) {Fab B72.3 (mouse/human chimera), kappa L chain}
daaptvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqdsk
dstyslsstltlskadyekhkvyacevthqglsspvtksfnr
>d1bbl__ 1.9.1.1.2 E3-binding domain of dihydrolipoamide succinyltransferase {Escherichia coli}
lspairrllaehnldasaikgtgvggrltredvekhl
>d1bbn__ 1.27.1.2.3 Interleukin-4 (IL-4) {Human (Homo sapiens)}
eaeahkcditlqeiiktlnslteqktlcteltvtdifaaskdtteketfcraatvlrqfy
shhekdtrclgataqqfhrhkqlirflkrldrnlwglaglnscpvkeadqstlenflerl
ktimrekyskcss
>d1bbo_1 7.31.1.1.9 (1-28) Enhancer binding protein {Human (Homo sapiens)}
kyiceecgirxkkpsmlkkhirthtdvr
>d1bbo_2 7.31.1.1.9 (29-57) Enhancer binding protein {Human (Homo sapiens)}
pyhctycnfsfktkgnltkhmkskahskk
>d1bbpa_ 2.53.1.1.13 Bilin-binding protein {Cabbage butterfly (Pieris brassicae)}
nvyhdgacpevkpvdnfdwsnyhgkwwevakypnsvekygkcgwaeytpegksvkvsnyh
vihgkeyfiegtaypvgdskigkiyhkltyggvtkenvfnvlstdnknyiigyyckyded
kkghqdfvwvlsrskvltgeaktavenyligspvvdsqklvysdfseaackvn
>d1bbpb_ 2.53.1.1.13 Bilin-binding protein {Cabbage butterfly (Pieris brassicae)}
nvyhdgacpevkpvdnfdwsnyhgkwwevakypnsvekygkcgwaeytpegksvkvsnyh
vihgkeyfiegtaypvgdskigkiyhkltyggvtkenvfnvlstdnknyiigyyckyded
kkghqdfvwvlsrskvltgeaktavenyligspvvdsqklvysdfseaackvn
>d1bbpc_ 2.53.1.1.13 Bilin-binding protein {Cabbage butterfly (Pieris brassicae)}
nvyhdgacpevkpvdnfdwsnyhgkwwevakypnsvekygkcgwaeytpegksvkvsnyh
vihgkeyfiegtaypvgdskigkiyhkltyggvtkenvfnvlstdnknyiigyyckyded
kkghqdfvwvlsrskvltgeaktavenyligspvvdsqklvysdfseaackvn
>d1bbpd_ 2.53.1.1.13 Bilin-binding protein {Cabbage butterfly (Pieris brassicae)}
nvyhdgacpevkpvdnfdwsnyhgkwwevakypnsvekygkcgwaeytpegksvkvsnyh
vihgkeyfiegtaypvgdskigkiyhkltyggvtkenvfnvlstdnknyiigyyckyded
kkghqdfvwvlsrskvltgeaktavenyligspvvdsqklvysdfseaackvn
>e1bbr.1e 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
svaevqpsvlqvvnlplverpvckastriritdnmfcagykpgegkrgdacegdsggpfv
mkspynnrwyqmgivswgegcdrdgkygfythvfrlkkwiqkvidrlgs
>e1bbr.1h 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
ivegqdaevglspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftvddll
vrigkhsrtryerkvekismldkiyihprynwkenldrdiallklkrpielsdyihpvcl
pdkqtaakllhagfkgrvtgwgnrretwtt
>e1bbr.1l 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1bbr.2j 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1bbr.2k 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
ivegqdaevglspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftvddll
vrigkhsrtryerkvekismldkiyihprynwkenldrdiallklkrpielsdyihpvcl
pdkqtaakllhagfkgrvtgwgnrretwttsvaevqpsvlqvvnlplverpvckastrir
itdnmfcagykpgegkrgdacegdsggpfvmkspynnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidrlgs
>e1bbr.3m 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1bbr.3n 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
ivegqdaevglspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftvddll
vrigkhsrtryerkvekismldkiyihprynwkenldrdiallklkrpielsdyihpvcl
pdkqtaakllhagfkgrvtgwgnrretwttsvaevqpsvlqvvnlplverpvckastrir
itdnmfcagykpgegkrgdacegdsggpfvmkspynnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidrlgs
>d1bbs__ 2.44.1.2.16 Chymosin (synonim: renin) {Human (Homo sapiens)}
ttssviltnymdtqyygeigigtppqtfkvvfdtgssnvwvpsskcsrlytacvyhklfd
asdsssykhngteltlrystgtvsgflsqdiitvggitvtqmfgevtempalpfmlaefd
gvvgmgfieqaigrvtpifdniisqgvlkedvfsfyynrdsensqslggqivlggsdpqh
yegnfhyinliktgvwqiqmkgvsvgsstllcedgclalvdtgasyisgstssieklmea
lgakkrlfdyvvkcnegptlpdisfhlggkeytltsadyvfqesysskklctlaihamdi
ppptgptwalgatfirkfytefdrrnnrigfalar
>d1bbt1_ 2.9.1.4.2 Foot-and-mouth desease virus {Foot-and-mouth disease virus (strain bfs, 1860)}
ttsagesadpvtttvenyggetqiqrrqhtdvsfimdrfvkvtpqnqinildlmqvpsht
lvggllrastyyfsdleiavkhegdltwvpngapekaldnttnptayhkapltrlalpyt
aphrvlatvyngecrysrnavpnlrgdlqvlaqkvartlptsfnygaikatrvtellyrm
kraetycprpllaihptearhkqkivap
>d1bbt2_ 2.9.1.4.2 Foot-and-mouth desease virus {Foot-and-mouth disease virus (strain bfs, 1860)}
lledrilttrnghttsttqssvgvtygyataedfvsgpntsgletrvvqaerffkthlfd
wvtsdsfgrchllelptdhkgvygsltdsyaymrngwdvevtavgnqfnggcllvamvpe
lcsiqkrelyqltlfphqfinprtnmtahitvpfvgvnrydqykvhkpwtlvvmvvaplt
vntegapqikvyaniaptnvhvagefpske
>d1bbt3_ 2.9.1.4.2 Foot-and-mouth desease virus {Foot-and-mouth disease virus (strain bfs, 1860)}
gifpvacsdgygglvttdpktadpvygkvfnpprnqlpgrftnlldvaeacptflrfegg
vpyvttktdsdrvlaqfdmslaakhmsntflaglaqyytqysgtinlhfmftgptdakar
ymvayappgmeppktpeaaahcihaewdtglnskftfsipylsaadytytasdvaettnv
qgwvclfqithgkadgdalvvlasagkdfelrlpvdarae
>d1bbxc_ 4.8.2.1.1 DNA-binding protein {Sulfolobus solfataricus, Sso7d}
atvkfkykgeekqvdiskikkvwrvgkmisftydegggktgrgavsekdapkellqmlek
qkk
>d1bbxd_ 4.8.2.1.1 DNA-binding protein {Sulfolobus solfataricus, Sso7d}
atvkfkykgeekqvdiskikkvwrvgkmisftydegggktgrgavsekdapkellqmlek
qkk
>d1bby__ 1.4.3.13.1 DNA-binding domain from rap30 {Human (Homo sapiens)}
raradkqhvldmlfsafekhqyynlkdlvditkqpvvylkeilkeigvqnvkgihkntwe
lkpeyrhyq
>d1bbza_ 2.30.2.1.5 Abl tyrosine kinase, SH3 domain {Human (Homo sapiens)}
nlfvalydfvasgdntlsitkgeklrvlgynhngewceaqtkngqgwvpsnyitpvns
>d1bbzc_ 2.30.2.1.5 Abl tyrosine kinase, SH3 domain {Human (Homo sapiens)}
nlfvalydfvasgdntlsitkgeklrvlgynhngewceaqtkngqgwvpsnyitpvns
>d1bbze_ 2.30.2.1.5 Abl tyrosine kinase, SH3 domain {Human (Homo sapiens)}
alfvalydfvasgdntlsitkgeklrvlgynhngewceaqtkngqgwvpsnyitpvas
>d1bbzg_ 2.30.2.1.5 Abl tyrosine kinase, SH3 domain {Human (Homo sapiens)}
nlfvalydfvasgdntlsitkgeklrvlgynhngewceaqtkngqgwvpsnyitpvns
>d1bc0__ 1.66.1.1.6 Annexin V {Rat (Rattus norvegicus)}
alrgtvtdfsgfdgradaevlrkamkglgtdedsilnlltarsnaqrqqiaeefktlfgr
dlvndmkseltgkfeklivalmkpsrlydayelkhalkgagtdekvlteiiasrtpeelr
aikqayeeeygsnleddvvgdtsgyyqrmlvvllqanrdpdtaiddaqveldaqalfqag
elkagtdeekfitilgtrsvshlrrvfdkymtisgfqieetidretsgnlenlllavvks
irsipaylaetlyyamkgagtddhtlirvivsrseidlfnirkefrknfatslysmikgd
tsgdykkallllcggedd
>d1bc1__ 1.66.1.1.6 Annexin V {Rat (Rattus norvegicus)}
alrgtvtdfsgfdgradaevlrkamkglgtdedsilnlltarsnaqrqqiaeefktlfgr
dlvndmkselkgkfeklivalmkpsrlydayelkhalkgagtdekvlteiiasrtpeelr
aikqayeeeygsnleddvvgdtkgyyqrmlvvllqanrdpdtaiddaqveldaqalfqag
elkwgtdeekfitilgtrsvshlrrvfdkymtisgfqieetidretkgnlenlllavvks
irsipaylaetlyyamkgagtddhtlirvivsrseidlfnirkefrknfatslysmikgd
tkgdykkallllcggedd
>d1bc2a_ 4.128.1.1.1 Zn metallo-beta-lactamase {Bacillus cereus}
tviknetgtisisqlnknvwvhtelgsfngeavpsnglvlntskglvlvdsswddkltke
liemvekkfqkrvtdviithahadriggiktlkergikahstaltaelakkngyeeplgd
lqtvtnlkfgnmkvetfypgkghtednivvwlpqynilvggclvkstsakdlgnvadayv
newstsienvlkryrninavvpghgevgdkglllhtldllk
>d1bc2b_ 4.128.1.1.1 Zn metallo-beta-lactamase {Bacillus cereus}
tviknetgtisisqlnknvwvhtelgsfngeavpsnglvlntskglvlvdsswddkltke
liemvekkfqkrvtdviithahadriggiktlkergikahstaltaelakkngyeeplgd
lqtvtnlkfgnmkvetfypgkghtednivvwlpqynilvggclvkstsakdlgnvadayv
newstsienvlkryrninavvpghgevgdkglllhtldllk
>d1bc3__ 1.66.1.1.6 Annexin V {Rat (Rattus norvegicus)}
alrgtvtdfsgfdgradaevlrkamkglgtdedsilnlltarsnaqrqqiaeefktlfgr
dlvndmkselkgkfeklivalmkpsrlydayelkhalkgagtdekvlteiiasrtpeelr
aikqayeeeygsnleddvvgdtkgyyqrmlvvllqanrdpdtaiddaqveldaqalfqag
elkwgtdeekfitilgtrsvshlrrvfdkymtisgfqieetidretkgnlenlllavvks
irsipaylaetlyyamkgagtddhtlirvivsrseidlfnirkefrknfatslysmikgd
tsgdykkallllcggedd
>d1bc4__ 4.5.1.1.4 Cytotoxic ribonuclease {Bullfrog (Rana catesbeiana)}
nwatfqqkhiintpiincntimdnniyivggqckrvntfiissattvkaictgvinmnvl
sttrfqlntctrtsitprpcpyssrtetnyicvkcenqypvhfagigrcp
>d1bc5a1 1.60.1.1.1 (16-91) Chemotaxis receptor methyltransferase CheR, N-terminal domain {Salmonella typhimurium}
mtqrlalsdahfrricqliyqragivladhkrdmvynrlvrrlralglddfgrylsmlea
nqnsaewqafinaltt
>d1bc5a2 3.56.1.3.1 (92-284) Chemotaxis receptor methyltransferase CheR, C-terminal domain {Salmonella typhimurium}
nltaffreahhfpilaeharrrhgeyrvwsaaastgeepysiaitladalgmapgrwkvf
asdidtevlekarsgiyrlselktlspqqlqryfmrgtgpheglvrvrqelanyvefssv
nllekqynvpgpfdaifcrnvmiyfdkttqedilrrfvpllkpdgllfaghsenfsnlvr
efslrgqtvyals
>d1bc6__ 4.47.1.2.2 Ferredoxin {Bacillus schlegelii}
ayvitepcigtkdascvevcpvdcihegedqyyidpdvcidcgaceavcpvsaiyhedfv
peewksyiqknrdffkk
>d1bc7c_ 1.4.3.16.6 Serum responce factor accessory protein 1a, SAP-1 {Human (Homo sapiens)}
mdsaitlwqfllqllqkpqnkhmicwtsndgqfkllqaeevarlwgirknkpnmnydkls
ralryyyvkniikkvngqkfvykfvsypeilnm
>d1bc8c_ 1.4.3.16.6 Serum responce factor accessory protein 1a, SAP-1 {Human (Homo sapiens)}
mdsaitlwqfllqllqkpqnkhmicwtsndgqfkllqaeevarlwgirknkpnmnydkls
ralryyyvkniikkvngqkfvykfvsypeilnm
>d1bc9__ 1.110.3.1.2 Cytohesin-1/b2-1 {Human (Homo sapiens)}
mknmqrnkqvamgrkkfnmdpkkgiqfliendllkntcediaqflykgeglnktaigdyl
gerdefniqvlhafvelheftdlnlvqalrqflwsfrlpgeaqkidrmmeafaqrycqcn
ngvfqstdtcyvlsfaiimlntslhnpnvkdkptverfiamnrgindggdlpeellrnly
esiknepfkipelehhhhhh
>d1bcca_ 4.106.1.1.2 Core 1 subunit {Chicken (Gallus gallus)}
yaqalqsvpetqvsqldngvrvaseqssqptctvgvwidagsryeseknngagyflehla
fkgtknrpqnalekevesmgahlnayssrehtayyikalskdvpkavelladivqncsle
dsqiekerdvivrelqendtsmrevvfnylhatafqgtglaqsvegpsenirklsradlt
eylsthytaprmvlaaaggvehqqllelaqkhfggvpftydddavptlskcrftgsqirh
redglplahvaiavegpgwahpdlvalqvanaiighydrtyggglhsssplasiavtnkl
cqsfqtfsicysetglfgfyfvcdrmsiddmmfvlqgqwmrlctsisesevlrgknflrn
alvshldgttpvcedigrelltygrripleeweerlaevdarmvrevcskyiydqcpava
gpgpieqlpdynrirsgmfwlr
>d1bccb_ 4.106.1.1.4 Core 2 subunit {Chicken (Gallus gallus)}
pphpqdleitklpnglviaslenyspgstigvfikagsryenssnlgtshllrlassltt
kgassfkitrgieavggklsvestrenmaytveclrddveilmefllnvttapefrpwev
adlqpqlkidkavafqnpqthvienlhaaayrnaladslycpdyrigkvtsvelhdfvqn
hftsarmalvglgvshpvlknvaeqllnirgglglsgakakyrggeireqngdslvhaai
vaesaaiggaeanafsvlqhvlganphvkrglnatsslyqavakgvhqpfdvsafnasys
dsglfgfytisqaayagqvikaaynqvktiaqgnvsnenvqaaknklkakylmsvesseg
fleevgsqalaagsynppstvlqqidavadadvikaakkfvsrqksmaasgnlghtpfvd
el
>d1bccc1 6.2.1.1.10 Cytochrome bc1 transmembrane subunits {Chicken (Gallus gallus)}
apnirkshpllkminnslidlpapsnisawwnfgsllavclmtqiltglllamhytadts
lafssvahtcrnvqygwlirnlhangasffficiflhigrglyygsylyketwntgvill
ltlmatafvgyvlpwgqmsfwgatvitnlfsaipyightlvewawggfsvdnptltrffa
lhfllpfaiagitiihltflhesgsnnplgissdsdkipfhpyysfkdilgltlmltpfl
tlalfspnllgdpenftpanplvtpphikpewyflfayailrsipnklggvlalaasvli
lflipflhkskqrtmtfrplsqtlfwllvanlliltwigsqpvehpfiiigqmaslsyft
illilfptigtlenkmlny
>d1bccd1 6.2.1.1.10 Cytochrome bc1 transmembrane subunits {Chicken (Gallus gallus)}
sdlelhppsypwshrgplssldhtsirrgfqvykqvcsschsmdyvayrhlvgvcytede
akalaeevevqdgpnedgemfmrpgklsdyfpkpypnpeaaraanngalppdlsyivrar
hggedyvfslltgycepptgvsvreglyfnpyfpgqaigmappiyndvlefddgtpatms
qvakdvctflrwaaepehdhrkrmglkmllmmgllvplvyymkrhkwsvlksrklayrpp
k
>d1bcce1 2.29.1.1.2 (70-196) ISP subunit of the mitochondrial cytochrome bc1-complex {Chicken (Gallus gallus)}
amskieiklsdipegknmafkwrgkplfvrhrtkkeidqeaavevsqlrdpqhdlervkk
pewviligvcthlgcvpianagdfggyycpchgshydasgrirkgpaplnlevpsyefts
ddmvivg
>d1bcce2 6.2.1.1.10 (1-69) Cytochrome bc1 transmembrane subunits {Chicken (Gallus gallus)}
shtdikvpnfsdyrrppddystkssresdpsrkgfsylvtavttlgvayaaknvvtqfvs
smsasadvl
>d1bccf1 6.2.1.1.10 Cytochrome bc1 transmembrane subunits {Chicken (Gallus gallus)}
srwlegirkwyynaagfnkyglmrddtiyenddvkeairrlpenlyddrmfrikraldln
mrqqilpkeqwtkyeedvpylepylkevirerkereewdk
>d1bccg1 6.2.1.1.10 Cytochrome bc1 transmembrane subunits {Chicken (Gallus gallus)}
rqfghltrvrhlityslspfeqrpfphyfskgvpnvwrrlracilrvappflafyllytw
gtqefekskrknpaayvn
>d1bcch1 6.2.1.1.10 Cytochrome bc1 transmembrane subunits {Chicken (Gallus gallus)}
lvdplttvreqceqlekcvkarerlelcdervssrsqteedcteelfdflhardhcvahk
lfnslk
>d1bccj1 6.2.1.1.10 Cytochrome bc1 transmembrane subunits {Chicken (Gallus gallus)}
tltarlysllfrrtstfaltivvgallferafdqgadaiyehinegklwkhikhkyenk
>d1bcd__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnn
ghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvh
wntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprg
llpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvd
nwrpaqplknrqikasfk
>d1bcfa_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bcfb_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bcg__ 7.3.7.1.7 Scorpion toxin {Scorpion (Buthotus judaicus), BJXTR-IT}
mkkngypldrngkttecsgvnaiaphycnsectkvyyaesgyccwgacycfgleddkpig
pmkditkkycdvqi
>d1bch11 4.139.1.1.7 (105-226) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvhivdnglwndiscqashtavcef
pa
>d1bch21 4.139.1.1.7 (105-226) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvhivdnglwndiscqashtavcef
pa
>d1bch31 4.139.1.1.7 (105-226) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvhivdnglwndiscqashtavcef
pa
>d1bci__ 2.6.1.1.2 Domain from cytosolic phospholipase A2 {Human (Homo sapiens)}
yshkftvvvlratkvtkgafgdmldtpdpyvelfisttpdsrkrtrhfnndinpvwnetf
efildpnqenvleitlmdanyvmdetlgtatftvssmkvgekkevpfifnqvtemvlems
lev
>d1bcj11 4.139.1.1.7 (105-226) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktvaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvhivdnglwndiscqashtavcef
pa
>d1bcj21 4.139.1.1.7 (105-226) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktvaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvhivdnglwndiscqashtavcef
pa
>d1bcj31 4.139.1.1.7 (105-226) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktvaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvhivdnglwndiscqashtavcef
pa
>d1bcka_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
mvnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgf
mcqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictakte
wldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1bcma1 2.42.1.1.1 (481-560) mu transposase, C-terminal domain {Bacteriophage mu}
teeqkrmlllpaeavnvsrkgeftlkvggslkgaknvyynmalmnagvkkvvvrfdpqql
hstvycytldgrficeaecl
>d1bcma2 3.46.3.3.1 (257-480) mu transposase, core domain {Bacteriophage mu}
vehldamqwingdgylhnvfvrwfngdvirpktwfwqdvktrkilgwrcdvsenidsirl
sfmdvvtrygipedfhitidntrgaankwltggapnryrfkvkeddpkglfllmgakmhw
tsvvagkgwgqakpverafgvggleeyvdkhpalagaytgpnpqakpdnygdravdaelf
lktlaegvamfnartgretemcggklsfddvfereyartivrkp
>d1bcmb1 2.42.1.1.1 (481-560) mu transposase, C-terminal domain {Bacteriophage mu}
teeqkrmlllpaeavnvsrkgeftlkvggslkgaknvyynmalmnagvkkvvvrfdpqql
hstvycytldgrficeaecl
>d1bcmb2 3.46.3.3.1 (258-480) mu transposase, core domain {Bacteriophage mu}
ehldamqwingdgylhnvfvrwfngdvirpktwfwqdvktrkilgwrcdvsenidsirls
fmdvvtrygipedfhitidntrgaankwltggapnryrfkvkeddpkglfllmgakmhwt
svvagkgwgqakpverafgvggleeyvdkhpalagaytgpnpqakpdnygdravdaelfl
ktlaegvamfnartgretemcggklsfddvfereyartivrkp
>d1bcn__ 1.27.1.2.3 Interleukin-4 (IL-4) {Human (Homo sapiens)}
eaeahkcditlqeiiktlnslteqktlcteltvtdifaaskdtteketfcraatvlrqfy
shhekdtrclgataqqfhrhkqlirflkrldrnlwglaglnscpvkeadqstlenflerl
ktimrekyskcss
>d1bco_1 2.42.1.1.1 (481-560) mu transposase, C-terminal domain {Bacteriophage mu}
teeqkrmlllpaeavnvsrkgeftlkvggslkgaknvyynmalmnagvkkvvvrfdpqql
hstvycytldgrficeaecl
>d1bco_2 3.46.3.3.1 (258-480) mu transposase, core domain {Bacteriophage mu}
ehldamqwingdgylhnvfvrwfngdvirpktwfwqdvktrkilgwrcdvsenidsirls
fmdvvtrygipedfhitidntrgaankwltggapnryrfkvkeddpkglfllmgakmhwt
svvagkgwgqakpverafgvggleeyvdkhpalagaytgpnpqakpdnygdravdaelfl
ktlaegvamfnartgretemcggklsfddvfereyartivrkp
>d1bcpa_ 4.136.1.1.5 Pertussis toxin, S1 subunit {Bordetella pertussis}
dppatvyrydsrppedvfqngftawgnndnvlehltgrscqvgssnsafvstsssrryte
vylehrmqeaveaeragrgtghfigyiyevradnnfygaassyfeyvdtygdnagrilag
alatyqseylahrrippenirrvtrvyhngitgetttteysnaryvsqqtranpnpytsr
rsvasivgtlvrmapvvgacmarqaesseamaawserageamvlvyyesiaysf
>d1bcpb1 2.35.2.1.6 (90-199) Pertussis toxin S2/S3 subunits, C-terminal domain {Bordetella pertussis}
ttrntgqpatdhyysnvtatrllsstnsrlcavfvrsgqpvigactspydgkywsmysrl
rkmlyliyvagisvrvhvskeeqyydyedatfetyaltgisicnpgsslc
>d1bcpb2 4.139.1.2.1 (3-89) Pertussis toxin, S2/S3 subunits, N-terminal domain {Bordetella pertussis}
pgivippqeqitqhgspygrcanktraltvaelrgsgdlqeylrhvtrgwsifalydgty
lggeyggvikdgtpggafdlkttfcim
>d1bcpc1 2.35.2.1.6 (90-199) Pertussis toxin S2/S3 subunits, C-terminal domain {Bordetella pertussis}
tiyktgqpaadhyyskvtatrllastnsrlcavfvrdgqsvigacaspyegryrdmydal
rrllymiymsglavrvhvskeeqyydyedatfqtyaltgislcnpaasic
>d1bcpc2 4.139.1.2.1 (4-89) Pertussis toxin, S2/S3 subunits, N-terminal domain {Bordetella pertussis}
givippkalftqqggaygrcpngtraltvaelrgnaelqtylrqitpgwsiyglydgtyl
gqayggiikdappgagfiyretfcit
>d1bcpd_ 2.35.2.1.7 Pertussis toxin S4 subunit {Bordetella pertussis}
dvpyvlvktnmvvtsvamkpyevtptrmlvcgiaaklgaaasspdahvpfcfgkdlkrpg
sspmevmlravfmqqrplrmflgpkqltfegkpalelirmvecsgkqdcp
>d1bcpe_ 2.35.2.1.7 Pertussis toxin S4 subunit {Bordetella pertussis}
dvpyvlvktnmvvtsvamkpyevtptrmlvcgiaaklgaaasspdahvpfcfgkdlkrpg
sspmevmlravfmqqrplrmflgpkqltfegkpalelirmvecsgkqdcp
>d1bcpf_ 2.35.2.1.8 Pertussis toxin S5 subunit {Bordetella pertussis}
lpthlyknftvqelalklkgknqefcltafmsgrslvraclsdaghehdtwfdtmlgfai
sayalksrialtvedspypgtpgdllelqicplngyce
>d1bcpg_ 4.136.1.1.5 Pertussis toxin, S1 subunit {Bordetella pertussis}
dppatvyrydsrppedvfqngftawgnndnvlehltgrscqvgssnsafvstsssrryte
vylehrmqeaveaeragrgtghfigyiyevradnnfygaassyfeyvdtygdnagrilag
alatyqseylahrrippenirrvtrvyhngitgetttteysnaryvsqqtranpnpytsr
rsvasivgtlvrmapvvgacmarqaesseamaawserageamvlvyyesiaysf
>d1bcph1 2.35.2.1.6 (90-199) Pertussis toxin S2/S3 subunits, C-terminal domain {Bordetella pertussis}
ttrntgqpatdhyysnvtatrllsstnsrlcavfvrsgqpvigactspydgkywsmysrl
rkmlyliyvagisvrvhvskeeqyydyedatfetyaltgisicnpgsslc
>d1bcph2 4.139.1.2.1 (3-89) Pertussis toxin, S2/S3 subunits, N-terminal domain {Bordetella pertussis}
pgivippqeqitqhgspygrcanktraltvaelrgsgdlqeylrhvtrgwsifalydgty
lggeyggvikdgtpggafdlkttfcim
>d1bcpi1 2.35.2.1.6 (90-199) Pertussis toxin S2/S3 subunits, C-terminal domain {Bordetella pertussis}
tiyktgqpaadhyyskvtatrllastnsrlcavfvrdgqsvigacaspyegryrdmydal
rrllymiymsglavrvhvskeeqyydyedatfqtyaltgislcnpaasic
>d1bcpi2 4.139.1.2.1 (4-89) Pertussis toxin, S2/S3 subunits, N-terminal domain {Bordetella pertussis}
givippkalftqqggaygrcpngtraltvaelrgnaelqtylrqitpgwsiyglydgtyl
gqayggiikdappgagfiyretfcit
>d1bcpj_ 2.35.2.1.7 Pertussis toxin S4 subunit {Bordetella pertussis}
dvpyvlvktnmvvtsvamkpyevtptrmlvcgiaaklgaaasspdahvpfcfgkdlkrpg
sspmevmlravfmqqrplrmflgpkqltfegkpalelirmvecsgkqdcp
>d1bcpk_ 2.35.2.1.7 Pertussis toxin S4 subunit {Bordetella pertussis}
dvpyvlvktnmvvtsvamkpyevtptrmlvcgiaaklgaaasspdahvpfcfgkdlkrpg
sspmevmlravfmqqrplrmflgpkqltfegkpalelirmvecsgkqdcp
>d1bcpl_ 2.35.2.1.8 Pertussis toxin S5 subunit {Bordetella pertussis}
lpthlyknftvqelalklkgknqefcltafmsgrslvraclsdaghehdtwfdtmlgfai
sayalksrialtvedspypgtpgdllelqicplngyce
>e1bcr.1a 3.59.1.4.1 Serine carboxypeptidase II {Wheat (Triticum vulgaris)}
haadriarlpgqpavdfdmysgyitvdegagrslfyllqeapedaqpaplvlwlnggpgc
ssvaygaseelgafrvkprgaglvlneyrwnkvanvlfldspagvgfsytntssdiytsg
dnrtahdsyaflakwferfphykyrdfyiagesyaghyvpelsqlvhrsknpvinlkgfm
vgngliddyhdyvgtfefwwnhgivsddtyrrlkeaclhdsfihpspacdaatdvataeq
gnidmyslytpvcn
>e1bcr.1b 3.59.1.4.1 Serine carboxypeptidase II {Wheat (Triticum vulgaris)}
sydpcterystayynrrdvqmalhanvtgamnytwatcsdtinthwhdaprsmlpiyrel
iaaglriwvfsgdtdavvpltatrysigalglptttswypwyddqevggwsqvykgltlv
svrgaghevplhrprqalvlfqyflqgkpmpg
>e1bcs.1a 3.59.1.4.1 Serine carboxypeptidase II {Wheat (Triticum vulgaris)}
haadriarlpgqpavdfdmysgyitvdegagrslfyllqeapedaqpaplvlwlnggpgc
ssvaygaseelgafrvkprgaglvlneyrwnkvanvlfldspagvgfsytntssdiytsg
dnrtahdsyaflakwferfphykyrdfyiagesyaghyvpelsqlvhrsknpvinlkgfm
vgngliddyhdyvgtfefwwnhgivsddtyrrlkeaclhdsfihpspacdaatdvataeq
gnidmyslytpvcni
>e1bcs.1b 3.59.1.4.1 Serine carboxypeptidase II {Wheat (Triticum vulgaris)}
sydpcterystayynrrdvqmalhanvtgamnytwatcsdtinthwhdaprsmlpiyrel
iaaglriwvfsgdtdavvpltatrysigalglptttswypwyddqevggwsqvykgltlv
svrgaghevplhrprqalvlfqyflqgkpmpgq
>e1bcu.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqf
>e1bcu.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>d1bcw__ 1.66.1.1.6 Annexin V {Rat (Rattus norvegicus)}
alrgtvtdfsgfdgradaevlrkamkglgtdedsilnlltarsnaqrqqiaeefktlfgr
dlvndmkselagkfeklivalmkpsrlydayelkhalkgagtdekvlteiiasrtpeelr
aikqayeeeygsnleddvvgdtsgyyqrmlvvllqanrdpdtaiddaqveldaqalfqag
elkwgtdeekfitilgtrsvshlrrvfdkymtisgfqieetidretsgnlenlllavvks
irsipaylaetlyyamkgagtddhtlirvivsrseidlfnirkefrknfatslysmikgd
tsgdykkallllcggedd
>d1bcx__ 2.26.1.10.1 Xylanase II {Bacillus circulans}
astdywqnwtdgggivnavngsggnysvnwsntgnfvvgkgwttgspfrtinynagvwap
ngngyltlygwtrsplieyyvvdswgtyrptgtykgtvksdggtydiytttrynapsidg
drttftqywsvrqskrptgsnatitftnhvnawkshgmnlgsnwayqvmatcgyqssgss
nvtvw
>d1bcy__ 1.66.1.1.6 Annexin V {Rat (Rattus norvegicus)}
alrgtvtdfsgfdgradaevlrkamkglgtdedsilnlltarsnaqrqqiaeefktlfgr
dlvndmkselkgkfeklivalmkpsrlydayelkhalkgagtdekvlteiiasrtpeelr
aikqayeeeygsnleddvvgdtsgyyqrmlvvllqanrdpdtaiddaqveldaqalfqag
elkwgtdeekfitilgtrsvshlrrvfdkymtisgfqieetidretsgnlenlllavvks
irsipaylaetlyyamkgagtddhtlirvivsrseidlfnirkefrknfatslysmikgd
tsgdykkallllcggedd
>d1bcz__ 1.66.1.1.6 Annexin V {Rat (Rattus norvegicus)}
alrgtvtdfsgfdgradaevlrkamkglgtdedsilnlltarsnaqrqqiaeefktlfgr
dlvndmkselsgkfeklivalmkpsrlydayelkhalkgagtdekvlteiiasrtpeelr
aikqayeeeygsnleddvvgdtsgyyqrmlvvllqanrdpdtaiddaqveldaqalfqag
elkwgtdeekfitilgtrsvshlrrvfdkymtisgfqieetidretsgnlenlllavvks
irsipaylaetlyyamkgagtddhtlirvivsrseidlfnirkefrknfatslysmikgd
tsgdykkallllcggedd
>d1bd0a1 2.43.2.1.1 (2-11,245-382) Alanine racemase {Bacillus stearothermophilus}
ndfhrdtwaeXfslhsrlvhvkklqpgekvsygatytaqteewigtipigyadgwlrrlq
hfhvlvdgqkapivgricmdqcmirlpgplpvgtkvtligrqgdevisiddvarhletin
yevpctisyrvpriffrhkrimevrnaig
>d1bd0a2 3.1.5.1.1 (12-244) Alanine racemase {Bacillus stearothermophilus}
vdldaiydnvenlrrllpddthimavvkanayghgdvqvartaleagasrlavafldeal
alrekgieapilvlgasrpadaalaaqqrialtvfrsdwleeasalysgpfpihfhlkmd
tgmgrlgvkdeeetkrivalierhphfvleglythfatadevntdyfsyqytrflhmlew
lpsrpplvhcansaaslrfpdrtfnmvrfgiamyglapspgikpllpyplkea
>d1bd0b1 2.43.2.1.1 (2-11,245-381) Alanine racemase {Bacillus stearothermophilus}
ndfhrdtwaeXfslhsrlvhvkklqpgekvsygatytaqteewigtipigyadgwlrrlq
hfhvlvdgqkapivgricmdqcmirlpgplpvgtkvtligrqgdevisiddvarhletin
yevpctisyrvpriffrhkrimevrnai
>d1bd0b2 3.1.5.1.1 (12-244) Alanine racemase {Bacillus stearothermophilus}
vdldaiydnvenlrrllpddthimavvkanayghgdvqvartaleagasrlavafldeal
alrekgieapilvlgasrpadaalaaqqrialtvfrsdwleeasalysgpfpihfhlkmd
tgmgrlgvkdeeetkrivalierhphfvleglythfatadevntdyfsyqytrflhmlew
lpsrpplvhcansaaslrfpdrtfnmvrfgiamyglapspgikpllpyplkea
>d1bd2a1 2.1.1.2.4 (182-275) Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-a0201}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrdgedqtqdtelvetrpagdgtf
qkwaavvvpsgqeqrytchvqheglpkpltlrwe
>d1bd2a2 4.17.1.1.11 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-a0201}
gshsmryfftsvsrpgrgeprfiavgyvddtqfvrfdsdaasqrmeprapwieqegpeyw
dgetrkvkahsqthrvdlgtlrgyynqseagshtvqrmygcdvgsdwrflrgyhqyaydg
kdyialkedlrswtaadmaaqttkhkweaahvaeqlraylegtcvewlrrylengketlq
r
>d1bd2b1 2.1.1.2.4 Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-a0201}
iqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskdw
sfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1bd2d1 2.1.1.1.155 (1-117) T-cell antigen receptor {Human (Homo sapiens), alpha-chain}
qqvkqnspslsvqegrisilncdytnsmfdyflwykkypaegptflisissikdknadgr
ftvflnksakhlslhivpsqpgdsavyfcaamegaqklvfgqgtrltinpn
>d1bd2d2 2.1.1.2.144 (118-203) T-cell antigen receptor {Human (Homo sapiens)}
iqnpdpavyqlrdskssdksvclftdfdsqtnvsqskdsdvyitdktvldmrsmdfksns
avawsnksdfacanafnnsiipedtf
>d1bd2e1 2.1.1.1.157 (3-118) T-cell antigen receptor {Human (Homo sapiens), beta-chain}
gvtqtpkfqvlktgqsmtlqcaqdmnheymswyrqdpgmglrlihysvgagitdqgevpn
gynvsrsttedfplrllsaapsqtsvyfcassypgggfyeqyfgpgtrltvte
>d1bd2e2 2.1.1.2.146 (119-247) T-cell antigen receptor {Human (Homo sapiens), beta-chain}
dlknvfppevavfepseaeishtqkatlvclatgfypdhvelswwvngkevhsgvstdpq
plkeqpalndsryalssrlrvsatfwqdprnhfrcqvqfyglsendewtqdrakpvtqiv
saeawgrad
>d1bd3a_ 3.51.1.1.13 Uracil PRTase {Toxoplasma gondii}
qeesilqdiitrfpnvvlmkqtaqlrammtiirdketpkeefvfyadrlirllieealne
lpfqkkevttpldvsyhgvsfyskicgvsivragesmesglravcrgvrigkiliqrdet
taepkliyeklpadirerwvmlldpmcatagsvckaievllrlgvkeeriifvnilaapq
giervfkeypkvrmvtaavdiclnsryyivpgigdfgdryfgtm
>d1bd3b_ 3.51.1.1.13 Uracil PRTase {Toxoplasma gondii}
qeesilqdiitrfpnvvlmkqtaqlrammtiirdketpkeefvfyadrlirllieealne
lpfqkkevttpldvsyhgvsfyskicgvsivragesmesglravcrgvrigkiliqrdet
taepkliyeklpadirerwvmlldpmcatagsvckaievllrlgvkeeriifvnilaapq
giervfkeypkvrmvtaavdiclnsryyivpgigdfgdryfgtm
>d1bd3c_ 3.51.1.1.13 Uracil PRTase {Toxoplasma gondii}
qeesilqdiitrfpnvvlmkqtaqlrammtiirdketpkeefvfyadrlirllieealne
lpfqkkevttpldvsyhgvsfyskicgvsivragesmesglravcrgvrigkiliqrdet
taepkliyeklpadirerwvmlldpmcatagsvckaievllrlgvkeeriifvnilaapq
giervfkeypkvrmvtaavdiclnsryyivpgigdfgdryfgtm
>d1bd3d_ 3.51.1.1.13 Uracil PRTase {Toxoplasma gondii}
qeesilqdiitrfpnvvlmkqtaqlrammtiirdketpkeefvfyadrlirllieealne
lpfqkkevttpldvsyhgvsfyskicgvsivragesmesglravcrgvrigkiliqrdet
taepkliyeklpadirerwvmlldpmcatagsvckaievllrlgvkeeriifvnilaapq
giervfkeypkvrmvtaavdiclnsryyivpgigdfgdryfgtm
>d1bd4a_ 3.51.1.1.13 Uracil PRTase {Toxoplasma gondii}
qeesilqdiitrfpnvvlmkqtaqlrammtiirdketpkeefvfyadrlirllieealne
lpfqkkevttpldvsyhgvsfyskicgvsivragesmesglravcrgvrigkiliqrdet
taepkliyeklpadirerwvmlldpmcatagsvckaievllrlgvkeeriifvnilaapq
giervfkeypkvrmvtaavdiclnsryyivpgigdfgdryfgtm
>d1bd4b_ 3.51.1.1.13 Uracil PRTase {Toxoplasma gondii}
qeesilqdiitrfpnvvlmkqtaqlrammtiirdketpkeefvfyadrlirllieealne
lpfqkkevttpldvsyhgvsfyskicgvsivragesmesglravcrgvrigkiliqrdet
taepkliyeklpadirerwvmlldpmcatagsvckaievllrlgvkeeriifvnilaapq
giervfkeypkvrmvtaavdiclnsryyivpgigdfgdryfgtm
>d1bd4c_ 3.51.1.1.13 Uracil PRTase {Toxoplasma gondii}
qeesilqdiitrfpnvvlmkqtaqlrammtiirdketpkeefvfyadrlirllieealne
lpfqkkevttpldvsyhgvsfyskicgvsivragesmesglravcrgvrigkiliqrdet
taepkliyeklpadirerwvmlldpmcatagsvckaievllrlgvkeeriifvnilaapq
giervfkeypkvrmvtaavdiclnsryyivpgigdfgdryfgtm
>d1bd4d_ 3.51.1.1.13 Uracil PRTase {Toxoplasma gondii}
qeesilqdiitrfpnvvlmkqtaqlrammtiirdketpkeefvfyadrlirllieealne
lpfqkkevttpldvsyhgvsfyskicgvsivragesmesglravcrgvrigkiliqrdet
taepkliyeklpadirerwvmlldpmcatagsvckaievllrlgvkeeriifvnilaapq
giervfkeypkvrmvtaavdiclnsryyivpgigdfgdryfgtm
>d1bd6__ 4.47.1.2.2 Ferredoxin {Bacillus schlegelii}
ayvitepcigtkdascvevcpvdcihegedqyyidpdvcidcgaceavcpvsaiyhedfv
peewksyiqknrdffkk
>d1bd7a_ 2.10.1.1.6 beta-Crystallin {Rat (Rattus norvegicus), isoform E}
ehkiilyenpnftgkkmeivdddvpsfhahgyqekvssvrvqsgtwvgyqypgyrglqyl
lekgdykdnsdfgaphpqvqsvrrirdmqgnpkiiifeqenfqghshelsgpcpnlketg
mekagsvlvqagpwvgyeqanckgeqfvfekgeyprwdswtssrrtdslsslrpik
>d1bd7b_ 2.10.1.1.6 beta-Crystallin {Rat (Rattus norvegicus), isoform E}
ehkiilyenpnftgkkmeivdddvpsfhahgyqekvssvrvqsgtwvgyqypgyrglqyl
lekgdykdnsdfgaphpqvqsvrrirdmqgnpkiiifeqenfqghshelsgpcpnlketg
mekagsvlvqagpwvgyeqanckgeqfvfekgeyprwdswtssrrtdslsslrpik
>d1bd8__ 1.110.2.1.3 Cell cycle inhibitor p19ink4D {Human (Homo sapiens)}
ragdrlsgaaargdvqevrrllhrelvhpdalnrfgktalqvmmfgstaialellkqgas
pnvqdtsgtspvhdaartgfldtlkvlvehgadvnvpdgtgalpihlavqeghtavvsfl
aaesdlhrrdargltplelalqrgaqdlvdilqghm
>d1bd9a_ 2.15.1.1.1 Phosphatidylethanolamine binding protein {Human (Homo sapiens)}
lskwsgplslqevdeqpqhplhvtyagaavdelgkvltptqvknrptsiswdgldsgkly
tlvltdpdapsrkdpkyrewhhflvvnmkgndissgtvlsdyvgsgppkgtglhryvwlv
yeqdrplkcdepilsnrsgdhrgkfkvasfrkkyelrapvagtcyqaewddyvpklyeql
>d1bd9b_ 2.15.1.1.1 Phosphatidylethanolamine binding protein {Human (Homo sapiens)}
pvdlskwsgplslqevdeqpqhplhvtyagaavdelgkvltptqvknrptsiswdgldsg
klytlvltdpdapsrkdpkyrewhhflvvnmkgndissgtvlsdyvgsgppkgtglhryv
wlvyeqdrplkcdepilsnrsgdhrgkfkvasfrkkyelrapvagtcyqaewddyvpkly
eqlsg
>d1bdaa_ 2.41.1.2.29 Single chain tissue plasminogen activator {Human (Homo sapiens)}
tcglrqysqpqfrikgglfadiashpwqaaifakhrrspgerflcggilisscwilsaah
cfqerfpphhltvilgrtyrvvpgeeeqkfevekyivhkefdddtydndiallqlksdss
rcaqessvvrtvclppadlqlpdwtecelsgygkhealspfyserlkeahvrlypssrct
sqhllnrtvtdnmlcagdtrsggpqanlhdacqgdsggplvclndgrmtlvgiiswglgc
gqkdvpgvytkvtnyldwirdnmrp
>d1bdab_ 2.41.1.2.29 Single chain tissue plasminogen activator {Human (Homo sapiens)}
tcglrqysqpqfrikgglfadiashpwqaaifakhrrspgerflcggilisscwilsaah
cfqerfpphhltvilgrtyrvvpgeeeqkfevekyivhkefdddtydndiallqlksdss
rcaqessvvrtvclppadlqlpdwtecelsgygkhealspfyserlkeahvrlypssrct
sqhllnrtvtdnmlcagdtrsggpqanlhdacqgdsggplvclndgrmtlvgiiswglgc
gqkdvpgvytkvtnyldwirdnmrp
>d1bdb__ 3.2.1.2.11 Cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase {Pseudomonas lb400}
mklkgeavlitggasglgralvdrfvaegakvavldksaerlaeletdhgdnvlgivgdv
rsledqkqaasrcvarfgkidtlipnagiwdystalvdlpeesldaafdevfhinvkgyi
havkaclpalvasrgnviftisnagfypngggplytaakhaivglvrelafelapyvrvn
gvgsgginsdlrgpsslgmgskaistvpladmlksvlpigrmpeveeytgayvffatrgd
aapatgallnydgglgvrgffsgaggndlleqlnih
>d1bdc__ 1.8.1.1.1 Immunoglobulin-binding protein A modules {Staphylococcus aureus}
tadnkfnkeqqnafyeilhlpnlneeqrngfiqslkddpsqsanllaeakklndaqapka
>d1bdd__ 1.8.1.1.1 Immunoglobulin-binding protein A modules {Staphylococcus aureus}
tadnkfnkeqqnafyeilhlpnlneeqrngfiqslkddpsqsanllaeakklndaqapka
>d1bdfa1 4.56.3.1.1 (2-52,179-232) Dimerization subdomain of RNA polymerase alpha subunit N-terminal domain {Escherichia coli}
qgsvteflkprlvdieqvssthakvtleplergfghtlgnalraillssmpXpveriayn
veaarveqrtdldklviemetngtidpeeairraatilaeqleafv
>d1bdfa2 4.150.1.1.1 (53-178) Insert subdomain of RNA polymerase alpha subunit N-terminal domain {Escherichia coli}
gcavteveidgvlheystkegvqedileillnlkglavrvqgkdeviltlnksgigpvta
adithdgdveivkpqhvichltdenasismrikvqrgrgyvpastrihseederpigrll
vdacys
>d1bdfb1 4.56.3.1.1 (1-52,179-235) Dimerization subdomain of RNA polymerase alpha subunit N-terminal domain {Escherichia coli}
mqgsvteflkprlvdieqvssthakvtleplergfghtlgnalraillssmpXpveriay
nveaarveqrtdldklviemetngtidpeeairraatilaeqleafvdlr
>d1bdfb2 4.150.1.1.1 (53-178) Insert subdomain of RNA polymerase alpha subunit N-terminal domain {Escherichia coli}
gcavteveidgvlheystkegvqedileillnlkglavrvqgkdeviltlnksgigpvta
adithdgdveivkpqhvichltdenasismrikvqrgrgyvpastrihseederpigrll
vdacys
>d1bdfc1 4.56.3.1.1 (1-52,179-235) Dimerization subdomain of RNA polymerase alpha subunit N-terminal domain {Escherichia coli}
mqgsvteflkprlvdieqvssthakvtleplergfghtlgnalraillssmpXpveriay
nveaarveqrtdldklviemetngtidpeeairraatilaeqleafvdlr
>d1bdfc2 4.150.1.1.1 (53-178) Insert subdomain of RNA polymerase alpha subunit N-terminal domain {Escherichia coli}
gcavteveidgvlheystkegvqedileillnlkglavrvqgkdeviltlnksgigpvta
adithdgdveivkpqhvichltdenasismrikvqrgrgyvpastrihseederpigrll
vdacys
>d1bdfd1 4.56.3.1.1 (1-52,179-235) Dimerization subdomain of RNA polymerase alpha subunit N-terminal domain {Escherichia coli}
mqgsvteflkprlvdieqvssthakvtleplergfghtlgnalraillssmpXpveriay
nveaarveqrtdldklviemetngtidpeeairraatilaeqleafvdlr
>d1bdfd2 4.150.1.1.1 (53-178) Insert subdomain of RNA polymerase alpha subunit N-terminal domain {Escherichia coli}
gcavteveidgvlheystkegvqedileillnlkglavrvqgkdeviltlnksgigpvta
adithdgdveivkpqhvichltdenasismrikvqrgrgyvpastrihseederpigrll
vdacys
>d1bdg_1 3.46.1.2.1 (13-222) Hexokinase {Blood fluke (Schistosoma mansoni)}
fsdqqlfekvveilkpfdlsvvdyeeicdrmgesmrlglqkstnekssikmfpsyvtktp
ngtetgnflaldlggtnyrvlsvtlegkgkspriqertycipaekmsgsgtelfkyiaet
ladflenngmkdkkfdlgftfsfpcvqkglthatlvrwtkgfsadgveghnvaellqtel
dkrelnvkcvavvndtvgtlascaledp
>d1bdg_2 3.46.1.2.1 (223-460) Hexokinase {Blood fluke (Schistosoma mansoni)}
kcavglivgtgtnvayiedsskvelmdgvkepevvintewgafgekgeldcwrtqfdksm
didslhpgkqlyekmvsgmylgelvrhiivylveqkilfrgdlperlkvrnslltryltd
verdpahllynthymltddlhvpvvepidnrivryacemvvkraaylagagiacilrrin
rsevtvgvdgslykfhpkfcermtdmvdklkpkntrfclrlsedgsgkgaaaiaasc
>d1bdha1 1.36.1.4.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslavnh
>d1bdha2 3.83.1.1.7 (59-340) Purine repressor (PurR), C-terminal domain {Escherichia coli}
tksigllatsseaayfaeiieavekncfqkgytlilgnawnnlekqraylsmmaqkrvdg
llvmcseypepllamleeyrhipmvvmdwgeakadftdavidnafeggymagryliergh
reigvipgplerntgagrlagfmkameeamikvpeswivqgdfepesgyramqqilsqph
rptavfcggdimamgalcaademglrvpqdvsligydnvrnaryftpalttihqpkdslg
etafnmlldrivnkreepqsievhprlierrsvadgpfrdyr
>d1bdia1 1.36.1.4.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkvnh
>d1bdia2 3.83.1.1.7 (59-340) Purine repressor (PurR), C-terminal domain {Escherichia coli}
tksigllatsseaayfaeiieavekncfqkgytlilgnawnnlekqraylsmmaqkrvdg
llvmcseypepllamleeyrhipmvvmdwgeakadftdavidnafeggymagryliergh
reigvipgplerntgagrlagfmkameeamikvpeswivqgdfepesgyramqqilsqph
rptavfcggdimamgalcaademglrvpqdvsligydnvrnaryftpalttihqpkdslg
etafnmlldrivnkreepqsievhprlierrsvadgpfrdyr
>d1bdja_ 3.16.2.1.1 CheY protein {Escherichia coli}
adkelkflvvddfstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmp
nmdglellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleekln
kifeklgm
>d1bdjb_ 1.25.9.1.1 Aerobic respiration control sensor protein, ArcB {Escherichia coli}
ksealldipmleqylelvgpklitdglavfekmmpgyvsvlesnltaqdkkgiveeghki
kgaagsvglrhlqqlgqqiqspdlpawednvgewieemkeewrhdvevlkawvakat
>d1bdla_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddsivagielpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1bdlb_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddsivagielpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1bdma1 3.2.1.5.4 (0-154) Malate dehydrogenase {Thermus flavus}
mkapvrvavtgaagqigysllfriaagemlgkdqpvilqlleipqamkalegvvmeledc
afpllagleatddpdvafkdadyallvgaaprkagmerrdllqvngkifteqgralaeva
kkdvkvlvvgnpantnaliayknapglnprnftam
>d1bdma2 4.132.1.1.4 (155-332) Malate dehydrogenase {Thermus flavus}
trldhnrakaqlakktgtgvdrirrmtvwgnhssimfpdlfhaevdgrpalelvdmewye
kvfiptvaqrgaaiiqargassaasaanaaiehirdwalgtpegdwvsmavpsqgeygip
egivysfpvtakdgayrvvegleinefarkrmeitaqelldemeqvkalgli
>d1bdmb1 3.2.1.5.4 (0-154) Malate dehydrogenase {Thermus flavus}
mkapvrvavtgaagqigysllfriaagemlgkdqpvilqlleipqamkalegvvmeledc
afpllagleatddpdvafkdadyallvgaaprkagmerrdllqvngkifteqgralaeva
kkdvkvlvvgnpantnaliayknapglnprnftam
>d1bdmb2 4.132.1.1.4 (155-332) Malate dehydrogenase {Thermus flavus}
trldhnrakaqlakktgtgvdrirrmtvwgnhssimfpdlfhaevdgrpalelvdmewye
kvfiptvaqrgaaiiqargassaasaanaaiehirdwalgtpegdwvsmavpsqgeygip
egivysfpvtakdgayrvvegleinefarkrmeitaqelldemeqvkalgli
>d1bdo__ 2.74.1.1.1 Biotinyl domain of acetyl-CoA carboxylase {Escherichia coli}
eisghivrspmvgtfyrtpspdakafievgqkvnvgdtlciveamkmmnqieadksgtvk
ailvesgqpvefdeplvvie
>d1bdqa_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddsivagielpgrwkpkmvggiggfikvrqyd
qilieicghkaigtvlvgptpiniigrnlltqigctlnf
>d1bdqb_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddsivagielpgrwkpkmvggiggfikvrqyd
qilieicghkaigtvlvgptpiniigrnlltqigctlnf
>d1bdra_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddsvvagielpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1bdrb_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddsvvagielpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1bds__ 7.9.1.1.4 BDs-I defensin {Sea anemone (Anemonia sulcata)}
aapcfcsgkpgrgdlwilrgtcpggygytsncykwpniccyph
>d1bdta_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegrig
>d1bdtb_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1bdtc_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegr
>d1bdtd_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegr
>d1bdu__ 4.91.1.1.1 Thymidylate synthase {Escherichia coli}
mkqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihell
wflqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlk
ndpdsrriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfnias
yallvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesif
dyrfedfeiegydphpgikapvai
>d1bdva_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegrig
>d1bdvb_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1bdvc_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkeg
>d1bdvd_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegr
>d1bdxa1 1.5.1.1.1 (156-203) DNA helicase RuvA subunit, C-terminal domain {Escherichia coli}
tddaeqeavaalvalgykpqeasrmvskiarpdassetlirealraal
>d1bdxa2 1.61.6.1.1 (65-142) DNA helicase RuvA subunit, middle domain {Escherichia coli}
nkqertlfkeliktngvgpklalailsgmsaqqfvnavereevgalvklpgigkktaerl
ivemkdrfkglhgdlftp
>d1bdxa3 2.35.4.2.1 (1-64) DNA helicase RuvA subunit, N-terminal domain {Escherichia coli}
migrlrgiiiekqpplvlievggvgyevhmpmtcfyelpeagqeaivfthfvvredaqll
ygfn
>d1bdxb1 1.5.1.1.1 (156-203) DNA helicase RuvA subunit, C-terminal domain {Escherichia coli}
tddaeqeavaalvalgykpqeasrmvskiarpdassetlirealraal
>d1bdxb2 1.61.6.1.1 (65-142) DNA helicase RuvA subunit, middle domain {Escherichia coli}
nkqertlfkeliktngvgpklalailsgmsaqqfvnavereevgalvklpgigkktaerl
ivemkdrfkglhgdlftp
>d1bdxb3 2.35.4.2.1 (1-64) DNA helicase RuvA subunit, N-terminal domain {Escherichia coli}
migrlrgiiiekqpplvlievggvgyevhmpmtcfyelpeagqeaivfthfvvredaqll
ygfn
>d1bdxc1 1.5.1.1.1 (156-203) DNA helicase RuvA subunit, C-terminal domain {Escherichia coli}
tddaeqeavaalvalgykpqeasrmvskiarpdassetlirealraal
>d1bdxc2 1.61.6.1.1 (65-142) DNA helicase RuvA subunit, middle domain {Escherichia coli}
nkqertlfkeliktngvgpklalailsgmsaqqfvnavereevgalvklpgigkktaerl
ivemkdrfkglhgdlftp
>d1bdxc3 2.35.4.2.1 (1-64) DNA helicase RuvA subunit, N-terminal domain {Escherichia coli}
migrlrgiiiekqpplvlievggvgyevhmpmtcfyelpeagqeaivfthfvvredaqll
ygfn
>d1bdxd1 1.5.1.1.1 (156-203) DNA helicase RuvA subunit, C-terminal domain {Escherichia coli}
tddaeqeavaalvalgykpqeasrmvskiarpdassetlirealraal
>d1bdxd2 1.61.6.1.1 (65-142) DNA helicase RuvA subunit, middle domain {Escherichia coli}
nkqertlfkeliktngvgpklalailsgmsaqqfvnavereevgalvklpgigkktaerl
ivemkdrfkglhgdlftp
>d1bdxd3 2.35.4.2.1 (1-64) DNA helicase RuvA subunit, N-terminal domain {Escherichia coli}
migrlrgiiiekqpplvlievggvgyevhmpmtcfyelpeagqeaivfthfvvredaqll
ygfn
>e1bdy.1a 2.6.1.1.3 Domain from protein kinase C delta {Rat (Rattus norvegicus)}
mapflrisfnsyelgslqaeddasqpfcavkmkealttdrgktlvqkkptmypewkstfd
ahiyegrviqivlmraaedpmsevtvgvsvlaerckknngkaefwldlqpqakvlmcvqy
fle
>e1bdy.1b 2.6.1.1.3 Domain from protein kinase C delta {Rat (Rattus norvegicus)}
mapflrisfnsyelgslqaeddasqpfcavkmkealttdrgktlvqkkptmypewkstfd
ahiyegrviqivlmraaedpmsevtvgvsvlaerckknngkaefwldlqpqakvlmcvqy
fle
>d1be0__ 3.59.1.6.1 Haloalkane dehalogenase {Xanthobacter autotrophicus}
mvnairtpdqrfsnldqypfspnylddlpgypglrahyldegnsdaedvflclhgeptws
ylyrkmipvfaesgarviapdffgfgksdkpvdeedytfefhrnfllalierldlrnitl
vvqdwggflgltlpmadpsrfkrliimnaclmtdpvtqpafsafvtqpadgftawkydlv
tpsdlrldqfmkrwaptlteaeasayaapfpdtsyqagvrkfpkmvaqrdqacidistea
isfwqndwngqtfmaigmkdkllgpdvmypmkalingcpepleiadaghfvqefgeqvar
ealkhfaete
>d1be1__ 3.16.5.1.2 Glutamate mutase, small subunit {Clostridium tetanomorphum}
mekktivlgvigsdchavgnkildhsftnagfnvvnigvlssqedfinaaietkadlicv
sslygqgeidckglrekcdeaglkgiklfvggnivvgkqnwpdveqrfkamgfdrvyppg
tspettiadmkevlgve
>d1be2__ 1.54.1.1.3 Plant non-specific lipid-transfer protein (ns-LTP) {Barley (Hordeum vulgare)}
lncgqvdskmkpcltyvqggpgpsgeccngvrdlhnqaqssgdrqtvcnclkgiargihn
lnlnnaasipskcnvnvpytispdidcsriy
>d1be3a_ 4.106.1.1.1 Core 1 subunit {Bovine (Bos taurus)}
tatyaqalqsvpetqvsqldnglrvaseqssqptctvgvwidagsryeseknngagyfve
hlafkgtknrpgnalekevesmgahlnaystrehtayyikalskdlpkavelladivqnc
sledsqiekerdvilqelqendtsmrdvvfnylhatafqgtplaqsvegpsenvrklsra
dlteylsrhykaprmvlaaagglehrqlldlaqkhfsglsgtydedavptlspcrftgsq
ichredglplahvaiavegpgwahpdnvalqvanaiighydctygggahlssplasiaat
nklcqsfqtfnicyadtgllgahfvcdhmsiddmmfvlqgqwmrlctsatesevlrgknl
lrnalvshldgttpvcedigrslltygrriplaewesriaevdarvvrevcskyfydqcp
avagfgpieqlpdynrirsgmfwlrf
>d1be3b_ 4.106.1.1.3 Core 2 subunit {Bovine (Bos taurus)}
pqdleftrlpnglviaslenyapasriglfikagsryensnnlgtshllrlasslttkga
ssfkitrgieavggklsvtstrenmaytveclrddvdilmefllnvttapefrrwevaal
qpqlridkavalqnpqahvienlhaaayrnalanslycpdyrigkvtpvelhdyvqnhft
sarmaliglgvshpvlkqvaeqflnirgglglsgakakyhggeireqngdslvhaalvae
saaigsaeanafsvlqhvlgagphvkrgsnatsslyqavakgvhqpfdvsafnasysdsg
lfgfytisqaasagdvikaaynqvktiaqgnlsnpdvqaaknklkagylmsvessegfld
evgsqalaagsytppstvlqqidavadadvinaakkfvsgrksmaasgnlghtpfidel
>d1be3c1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
mtnirkshplmkivnnafidlpapsnisswwnfgsllgiclilqiltglflamhytsdtt
tafssvthicrdvnygwiirymhangasmfficlymhvgrglyygsytfletwnigvill
ltvmatafmgyvlpwgqmsfwgatvitnllsaipyigtnlvewiwggfsvdkatltrffa
fhfilpfiimaiamvhllflhetgsnnptgissdvdkipfhpyytikdilgalllilalm
llvlfapdllgdpdnytpanplntpphikpewyflfayailrsipnklggvlalafsili
lalipllhtskqrsmmfrplsqclfwalvadlltltwiggqpvehpyitigqlasvlyfl
lilvlmptagtienkllkw
>d1be3d1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
sdlelhppsypwshrgllssldhtsirrgfqvykqvcsschsmdyvayrhlvgvcytede
akalaeevevqdgpnedgemfmrpgklsdyfpkpypnpeaaraanngalppdlsyivrar
hggedyvfslltgycepptgvslreglyfnpyfpgqaigmappiynevlefddgtpatms
qvakdvctflrwaaepehdhrkrmglkmllmmglllplvyamkrhkwsvlksrklayrpp
k
>d1be3e1 2.29.1.1.1 (70-196) ISP subunit of the mitochondrial cytochrome bc1-complex {Bovine (Bos taurus)}
amskieiklsdipegknmafkwrgkplfvrhrtkkeidqeaavevsqlrdpqhdlervkk
pewviligvcthlgcvpianagdfggyycpchgshydasgrirkgpaplnlevpsyefts
ddmvivg
>d1be3e2 6.2.1.1.9 (1-69) Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
shtdikvpdfsdyrrpevldstksskessearkgfsylvtatttvgvayaaknvvsqfvs
smsasadvl
>d1be3f1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
avsassrwlegirkwyynaagfnklglmrddtihenddvkeairrlpenlyddrvfrikr
aldlsmrqqilpkeqwtkyeedksylepylkevirerkereewakk
>d1be3g1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
grqfghltrvrhvityslspfeqrafphyfskgipnvlrrtracilrvappfvafylvyt
wgtqefekskrknpaayendr
>d1be3h1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
dplttvreqceqlekcvkarerlelcdervssrsqteedcteelldflhardhcvahklf
nslk
>d1be3j1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
vaptltarlysllfrrtstfaltivvgalfferafdqgadaiyehinegklwkhikhkye
nk
>d1be3k1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
rnwvptaqlwgavgavglvsat
>d1be4a_ 4.47.6.1.2 Nucleoside diphosphate kinases {Bovine (Bos taurus)}
ansertfiaikpdgvqrglmgeiikrfeqkgfrlvamkfmrasedllkehyidlkdrpff
aglvkymhsgpvvamvweglnvvktgrvmlgetnpadskpgtirgdfciqvgrniihgsd
svesaekeialwfrpeelvnykscaqnwiye
>d1be4b_ 4.47.6.1.2 Nucleoside diphosphate kinases {Bovine (Bos taurus)}
ansertfiaikpdgvqrglmgeiikrfeqkgfrlvamkfmrasedllkehyidlkdrpff
aglvkymhsgpvvamvweglnvvktgrvmlgetnpadskpgtirgdfciqvgrniihgsd
svesaekeialwfrpeelvnykscaqnwiye
>d1be4c_ 4.47.6.1.2 Nucleoside diphosphate kinases {Bovine (Bos taurus)}
ansertfiaikpdgvqrglmgeiikrfeqkgfrlvamkfmrasedllkehyidlkdrpff
aglvkymhsgpvvamvweglnvvktgrvmlgetnpadskpgtirgdfciqvgrniihgsd
svesaekeialwfrpeelvnykscaqnwiye
>d1be6__ 3.33.1.1.2 Subtilisin Carlsberg {Bacillus licheniformis}
aqtvpygiplikadkvqaqgfkganvkvavldtgiqashpdlnvvggasfvageayntdg
nghgthvagtvaaldnttgvlgvapsvslyavkvlnssgsgsysgivsgiewattngmdv
inmslggasgstamkqavdnayargvvvvaaagnsgnsgstntigypakydsviavgavd
snsnrasfssvgaelevmapgagvystyptntyatlngtsmasphvagaaalilskhpnl
sasqvrnrlsstatylgssfyygkglinveaaaq
>d1be7__ 7.35.4.1.4 Rubredoxin {Clostridium pasteurianum}
mkkytctvcgyiynpedgdpdngvnpgtdfkdipddwvcplsgvgkdqfeevee
>d1be8__ 3.33.1.1.2 Subtilisin Carlsberg {Bacillus licheniformis}
aqtvpygiplikadkvqaqgfkganvkvavldtgiqashpdlnvvggasfvageayntdg
nghgthvagtvaaldnttgvlgvapsvslyavkvlnssgsgsysgivsgiewattngmdv
inmslggasgstamkqavdnayargvvvvaaagnsgnsgstntigypakydsviavgavd
snsnrasfssvgaelevmapgagvystyptntyatlngtsmasphvagaaalilskhpnl
sasqvrnrlsstatylgssfyygkglinveaaaq
>d1be9a_ 2.32.1.1.3 Synaptic protein PSD-95, 3rd PDZ domain {Rat (Rattus norvegicus)}
flgeedipreprrivihrgstglgfniiggedgegifisfilaggpadlsgelrkgdqil
svngvdlrnasheqaaialknagqtvtiiaqykpeeysrfeansrvnssgrivtn
>d1bea__ 1.54.1.2.3 Hageman factor/amylase inhibitor {Maize (Zea mays)}
scvpgwaiphnplpscrwyvtsrtcgigprlpwpelkrrccreladipaycrctalsilm
dgaippgpdaqlegrledlpgcprevqrgfaatlvteaecnlatisgvaecpwilg
>d1beba_ 2.53.1.1.8 beta-Lactoglobulin {Bovine (Bos taurus)}
qtmkgldiqkvagtwyslamaasdislldaqsaplrvyveelkptpegdleillqkweng
ecaqkkiiaektkipavfkidalnenkvlvldtdykkyllfcmensaepeqslvcqclvr
tpevddealekfdkalkalpmhirlsfnptqleeqc
>d1bebb_ 2.53.1.1.8 beta-Lactoglobulin {Bovine (Bos taurus)}
qtmkgldiqkvagtwyslamaasdislldaqsaplrvyveelkptpegdleillqkweng
ecaqkkiiaektkipavfkidalnenkvlvldtdykkyllfcmensaepeqslvcqclvr
tpevddealekfdkalkalpmhirlsfnptqleeqc
>d1bec_1 2.1.1.1.156 (3-117) T-cell antigen receptor {Mouse (Mus musculus), beta-chain}
avtqsprnkvavtggkvtlscqqtnnhnnmywyrqdtghglrlihysygagstekgdipd
gykasrpsqeqfslilelatpsqtsvyfcasgggrgsyaeqffgpgtrltvle
>d1bec_2 2.1.1.2.145 (118-246) T-cell antigen receptor {Mouse (Mus musculus), beta-chain}
dlrqvtppkvslfepskaeiankqkatlvclargffpdhvelswwvngkevhsgvstdpq
aykesnysyclssrlrvsatfwhnprnhfrcqvqfhglseedkwpegspkpvtqnisaea
wgrad
>d1bed_1 1.47.1.1.2 (63-126) Disulphide-bond formation facilitator (DSBA), insertion domain {Vibrio cholerae}
gnmgqamskayatmialevedkmvpvmfnrihtlrkppkdeqelrqifldegidaakfda
ayng
>d1bed_2 3.38.1.4.2 (1-62,127-181) Disulphide-bond formation facilitator (DSBA) {Vibrio cholerae}
aqfkegehyqvlktpassspvvseffsfycphcntfepiiaqlkqqlpegakfqknhvsf
mgXfavdsmvrrfdkqfqdsgltgvpavvvnnrylvqgqsvksldeyfdlvnylltlk
>d1bee__ 3.59.1.6.1 Haloalkane dehalogenase {Xanthobacter autotrophicus}
mvnairtpdqrfsnldqypfspnylddlpgypglrahyldegnsdaedvflclhgeptws
ylyrkmipvfaesgarviapdffgfgksdkpvdeedytfefhrnfllalierldlrnitl
vvqdwggflgltlpmadpsrfkrliimnaclmtdpvtqpafsafvtqpadgftaykydlv
tpsdlrldqfmkrwaptlteaeasayaapfpdtsyqagvrkfpkmvaqrdqacidistea
isfwqndwngqtfmaigmkdkllgpdvmypmkalingcpepleiadaghfvqefgeqvar
ealkhfaete
>d1befa_ 2.41.1.3.4 NS3 protease {Dengue virus serotype 2}
wdvpspppvgkaeledgayrikqkgilgysqigagvykegtfhtmwhvtrgavlmhkgkr
iepswadvkkdlvscgggwklegewkegeevqvlalepgknpravqtkpglfktnagtig
avsldfspgtsgspiidkkgkvvgiygngvvtrsgayvsaiaqteksiednpeiedd
>d1beg__ 1.124.1.1.1 beta-cryptogein {Phytophthora cryptogea}
tactatqqtaayktlvsilsdasfnqcstdsgysmltakalpttaqyklmcastacntmi
kkivtlnppncdltvptsglvlnvysyangfsnkcssl
>d1beha_ 2.15.1.1.1 Phosphatidylethanolamine binding protein {Human (Homo sapiens)}
vdlskwsgplslqevdeqpqhplhvtyagaavdelgkvltptqvknrptsiswdgldsgk
lytlvltdpdapsrkdpkyrewhhflvvnmkgndissgtvlsdyvgsgppkgtglhryvw
lvyeqdrplkcdepilsnrsgdhrgkfkvasfrkkyelrapvagtcyqaewddyvpklye
qlsg
>d1behb_ 2.15.1.1.1 Phosphatidylethanolamine binding protein {Human (Homo sapiens)}
dlskwsgplslqevdeqpqhplhvtyagaavdelgkvltptqvknrptsiswdgldsgkl
ytlvltdpdapsrkdpkyrewhhflvvnmkgndissgtvlsdyvgsgppkgtglhryvwl
vyeqdrplkcdepilsnrsgdhrgkfkvasfrkkyelrapvagtcyqaewddyvpklyeq
lsg
>d1bei__ 7.19.1.1.2 Sea anemone toxin k {Sun anemone (Stichodactyla helianthus), SHK}
rscidtipksrctafqckhsmxyrlsfcrktcgtc
>d1bej__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1bek__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnaigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpwgaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1bela_ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1bem__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpqgaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>e1ben.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1ben.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1ben.2c 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1ben.2d 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytp
>d1beo__ 1.124.1.1.1 beta-cryptogein {Phytophthora cryptogea}
tactatqqtaayktlvsilsdasfnqcstdsgysmltakalpttaqyklmcastacntmi
kkivtlnppncdltvptsglvlnvysyangfsnkcssl
>d1bep__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpwgaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1beq__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpygaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1bera1 1.4.3.4.1 (138-207) Catabolite gene activator protein (CAP), C-terminal domain {Escherichia coli}
dvtgriaqtllnlakqpdamthpdgmqikitrqeigqivgcsretvgrilkmledqnlis
ahgktivvyg
>d1bera2 2.73.4.1.1 (9-137) Catabolite gene activator protein, N-terminal domain {Escherichia coli}
ptlewflshchihkypskstlihqgekaetlyyivkgsvavlikdeegkemilsylnqgd
figelglfeegqersawvraktacevaeisykkfrqliqvnpdilmrlsaqmarrlqvts
ekvgnlafl
>d1berb1 1.4.3.4.1 (138-205) Catabolite gene activator protein (CAP), C-terminal domain {Escherichia coli}
dvtgriaqtllnlakqpdamthpdgmqikitrqeigqivgcsretvgrilkmledqnlis
ahgktivv
>d1berb2 2.73.4.1.1 (9-137) Catabolite gene activator protein, N-terminal domain {Escherichia coli}
ptlewflshchihkypskstlihqgekaetlyyivkgsvavlikdeegkemilsylnqgd
figelglfeegqersawvraktacevaeisykkfrqliqvnpdilmrlsaqmarrlqvts
ekvgnlafl
>d1bes__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpygaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1bet__ 7.17.1.3.3 beta-Nerve growth factor {Mouse (Mus musculus)}
gefsvcdsvsvwvgdkttatdikgkevtvlaevninnsvfrqyffetkcrasnpvesgcr
gidskhwnsycttthtfvkalttdekqaawrfiridtacvcvlsrka
>d1beua_ 3.1.2.2.5 Trp synthase alpha-subunit {Salmonella typhimurium}
meryenlfaqlndrregafvpfvtlgdpgieqslkiidtlidagadalelgvpfsdplan
gptiqnanlrafaagvtpaqcfemlalirekhptipigllmyanlvfnngidafyarceq
vgvdsvlvadvpveesapfrqaalrhniapificppnadddllrqvasygrgytyllsrs
gvtgaenrgalplhhlieklkeyhaapalqgfgisspeqvsaavragaagaisgsaivki
ieknlaspkqmlaelrsfvsamkaasra
>d1beub_ 3.67.1.1.1 Tryptophan synthase, beta-subunit {Salmonella typhimurium}
tllnpyfgefggmyvpqilmpalnqleeafvraqkdpefqaqfadllknyagrptaltkc
qnitagtrttlylkredllhggahktnqvlgqallakrmgkseiiaetgagqhgvasala
sallglkcriymgakdverqspnvfrmrlmgaevipvhsgsatlkdacnealrdwsgsye
tahymlgtaagphpyptivrefqrmigeetkaqildkegrlpdaviacvgggsnaigmfa
dfindtsvgligvepgghgietgehgaplkhgrvgiyfgmkapmmqtadgqieesysisa
gldfpsvgpqhaylnsigradyvsitddealeafktlcrhegiipalesshalahalkmm
reqpekeqllvvnlsgrgdkdiftvhdil
>d1bev1_ 2.9.1.4.12 Bovine enterovirus coat protein {Bovine enterovirus, VG-5-27}
qaagalvagtststhsvatdstpalqaaetgatstardesmietrtivpthgihetsves
ffgrsslvgmpllatgtsithwridfrefvqlrakmswftymrfdveftiiatsstgqnv
tteqhttyqvmyvppgapvpsnqdsfqwqsgcnpsvfadtdgppaqfsvpfmssanayst
vydgyarfmdtdpdrygilpsnflgfmyfrtledaahqvrfriyakikhtscwipraprq
apykkrynlvfsgdsdricsnrasltsy
>d1bev2_ 2.9.1.4.12 Bovine enterovirus coat protein {Bovine enterovirus, VG-5-27}
eacgysdrvaqltlgnstittqeaanicvaygcwpaklsdtdatsvdkptepgvsadrfy
tlrskpwqadskgwywklpdalnntgmfgqnaqfhylyrggwavhvqcnatkfhqgtllv
laipehqiatqeqpafdrtmpgseggtfqepfwledgtslgnsliyphqwinlrtnnsat
lilpyvnaipmdsairhsnwtlaiipvaplkyaaettplvpitvtiapmeteynglrrai
asnq
>d1bev3_ 2.9.1.4.12 Bovine enterovirus coat protein {Bovine enterovirus, VG-5-27}
glptkpgpgsyqfmttdedcspcilpdfqptpeifipgkvnnlleiaqvesileannreg
vegveryvipvsvqdaldaqiyalrlelggsgplsssllgtlakhytqwsgsveitcmft
gtfmttgkvllaytppggdmprnreeamlgthviwdfglqssitlvipwisashfrgvsn
ddvlnyqyyaaghvtiwyqtnmvippgfpntagiimmiaaqpnfsfriqkdredmtqtai
lq
>d1bexa_ 2.5.1.1.23 Azurin {Pseudomonas aeruginosa}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctfpghsal
mkgtltlk
>d1bexb_ 2.5.1.1.23 Azurin {Pseudomonas aeruginosa}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctfpghsal
mkgtltlk
>d1beyh1 2.1.1.1.123 (1-121) Immunoglobulin (variable domains of L and H chains) {Antibody to CAMPATH-1H humanized fab, kappa L chain}
qvqlqesgpglvrpsqtlsltctvsgftftdfymnwvrqppgrglewigfirdkakgytt
eynpsvkgrvtmlvdtsknqfslrlssvtaadtavyycareghtaapfdywgqgslvtvs
s
>d1beyh2 2.1.1.2.121 (122-219) Immunoglobulin (constant domains of L and H chains) {Antibody to CAMPATH-1H humanized fab, kappa L chain}
astkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkv
>d1beyl1 2.1.1.1.123 (1-107) Immunoglobulin (variable domains of L and H chains) {Antibody to CAMPATH-1H humanized fab, kappa L chain}
diqmtqspsslsasvgdrvtitckasqnidkylnwyqqkpgkapklliyntnnlqtgvps
rfsgsgsgtdftftisslqpediatyyclqhisrprtfgqgtkveik
>d1beyl2 2.1.1.2.121 (108-214) Immunoglobulin (constant domains of L and H chains) {Antibody to CAMPATH-1H humanized fab, kappa L chain}
rtvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqd
skdstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1bez__ 3.59.1.6.1 Haloalkane dehalogenase {Xanthobacter autotrophicus}
mvnairtpdqrfsnldqypfspnylddlpgypglrahyldegnsdaedvflclhgeptws
ylyrkmipvfaesgarviapdffgfgksdkpvdeedytfefhrnfllalierldlrnitl
vvqdwggflgltlpmadpsrfkrliimnaclmtdpvtqpafsafvtqpadgftaykydlv
tpsdlrldqfmkrwaptlteaeasayaapfpdtsyqagvrkfpkmvaqrdqacidistea
isfwqndwngqtfmaigmkdkllgpdvmypmkalingcpepleiadaghfvqefgeqvar
ealkhfaete
>d1bf0__ 7.8.1.1.11 Calcicludine (cac) {Green mamba (Dendroaspis angusticeps)}
wqppwyckepvrigsckkqfssfyfkwtakkclpflfsgcggnanrfqtigecrkkclgk
>d1bf2_1 2.1.1.5.9 (1-162) Isoamylase, N-terminal domain {Pseudomonas amyloderamosa}
ainsmslgasydaqqanitfrvyssqatrivlylysagygvqesatytlspagsgvwavt
vpvssikaagitgavyygyrawgpnwpyasnwgkgsqagfvsdvdangdrfnpnkllldp
yaqevsqdplnpsnqngnvfasgasyrttdsgiyapkgvvlv
>d1bf2_2 2.62.1.1.14 (638-750) Isoamylase {Pseudomonas amyloderamosa}
ysgsqltwyqpsgavadsnywnntsnyaiayaingpslgdsnsiyvayngwsssvtftlp
appsgtqwyrvtdtcdwndgastfvapgsetliggagttygqcgqsllllisk
>d1bf2_3 3.1.7.1.14 (163-637) Isoamylase, central domain {Pseudomonas amyloderamosa}
pstqstgtkptraqkddviyevhvrgfteqdtsipaqyrgtyygaglkasylaslgvtav
eflpvqetqndandvvpnsdanqnywgymtenyfspdrryaynkaaggptaefqamvqaf
hnagikvymdvvynhtaeggtwtssdpttatiyswrgldnatyyeltsgnqyfydntgig
anfntyntvaqnlivdslaywantmgvdgfrfdlasvlgnsclngaytasapncpnggyn
fdaadsnvainrilreftvrpaaggsgldlfaepwaiggnsyqlggfpqgwsewnglfrd
slrqaqnelgsmtiyvtqdandfsgssnlfqssgrspwnsinfidvhdgmtlkdvyscng
annsqawpygpsdggtstnyswdqgmsagtgaavdqrraartgmafemlsagtplmqggd
eylrtlqcnnnaynldssanwltyswttdqsnfytfaqrliafrkahpalrpssw
>d1bf3_1 3.3.1.2.4 (1-173,276-391) p-Hydroxybenzoate hydroxylase (PHBH) {Pseudomonas aeruginosa}
mktqvaiigagpsglllgqllhkagidnvilerqtpdyvlgkiragvleqgmvdllreag
vdrrmardglvhegveiafagqrrridlkrlsggktvtvygqtevtrdlmeareasgatt
vyqaaevrlhdlqgerpyvtferdgerlrldcdyiagcdgfhgisrqsipaerXmqhgrl
flagdaahivpptgakglnlaasdvstlyrlllkayregrgellerysaiclrriwkaer
fswwmtsvlhrfpdtdafsqriqqteleyylgseaglatiaenyvglpye
>d1bf3_2 4.14.1.2.2 (174-275) p-Hydroxybenzoate hydroxylase, PHBH {Pseudomonas aeruginosa}
lkvfervypfgwlglladtppvsheliyanhprgfalcsqrsatrsryyvqvpltekved
wsderfwtelkarlpaevaeklvtgpsleksiaplrsfvvep
>d1bf4a_ 4.8.2.1.1 DNA-binding protein {Sulfolobus solfataricus, Sso7d}
atvkfkykgeekevdiskikkvwrvgkmisftydegggktgrgavsekdapkellqmlek
qkk
>d1bf5a1 1.50.1.1.1 (136-316) STAT-1, coiled coil domain {Human (Homo sapiens)}
ldkqkeldskvrnvkdkvmcieheiksledlqdeydfkcktlqnrehlllkkmylmldnk
rkevvhkiiellnvteltqnalindelvewkrrqqsaciggppnacldqlqnwftivaes
lqqvrqqlkkleeleqkytyehdpitknkqvlwdrtfslfqqliqss
>d1bf5a2 2.2.5.1.9 (317-568) STAT-1, DNA-binding domain {Human (Homo sapiens)}
fvverqpcmpthpqrplvlktgvqftvklrllvklqelnynlkvkvlfdkdvnerntvkg
frkfnilgthtkvmnmeestngslaaefrhlqlkeqknagtrtnegplivteelhslsfe
tqlcqpglvidlettslpvvvisnvsqlpsgwasilwynmlvaeprnlsffltppcarwa
qlsevlswqfssvtkrglnvdqlnmlgekllgpnaspdglipwtrfckenindknfpfwl
wiesilelikkh
>d1bf5a3 4.72.1.1.17 (569-710) STAT-1 {Human (Homo sapiens)}
llplwndgcimgfiskererallkdqqpgtfllrfsessregaitftwversqnggepdf
havepytkkelsavtfpdiirnykvmaaenipenplkylypnidkdhafgkyysrgxikt
elisvs
>d1bf6a_ 3.1.8.3.2 Phosphotriesterase homology protein {Escherichia coli}
sfdptgytlahehlhidlsgfknnvdcrldqyaficqemndlmtrgvrnviemtnrymgr
naqfmldvmretginvvactgyyqdaffpehvatrsvqelaqemvdeieqgidgtelkag
iiaeigtsegkitpleekvfiaaalahnqtgrpisthtsfstmgleqlallqahgvdlsr
vtvghcdlkdnldnilkmidlgayvqfdtigknsyypdekriamlhalrdrgllnrvmls
mditrrshlkanggygydyllttfipqlrqsgfsqadvdvmlrenpsqffq
>d1bf6b_ 3.1.8.3.2 Phosphotriesterase homology protein {Escherichia coli}
sfdptgytlahehlhidlsgfknnvdcrldqyaficqemndlmtrgvrnviemtnrymgr
naqfmldvmretginvvactgyyqdaffpehvatrsvqelaqemvdeieqgidgtelkag
iiaeigtsegkitpleekvfiaaalahnqtgrpisthtsfstmgleqlallqahgvdlsr
vtvghcdlkdnldnilkmidlgayvqfdtigknsyypdekriamlhalrdrgllnrvmls
mditrrshlkanggygydyllttfipqlrqsgfsqadvdvmlrenpsqffq
>d1bf8_1 2.1.10.1.2 (1-121) Periplasmic chaperone FimC {Escherichia coli}
gvalgatrviypagqkqeqlavtnndenstyliqswvenadgvkdgrfivtpplfamkgk
kentlrildatnnqlpqdreslfwmnvkaipsmdkskltentlqlaiisriklyyrpakl
a
>d1bf8_2 2.6.2.1.2 (122-205) FimC {Escherichia coli}
lppdqaaeklrfrrsansltlinptpyyltvtelnagtrvlenalvppmgestvklpsda
gsnityrtindygaltpkmtgvme
>d1bf9__ 7.3.11.1.8 Factor VII, N-terminal domain {Human (Homo sapiens)}
sdgdqcasspcqnggsckdqlqsyicfclpafegrncethk
>d1bfa__ 1.54.1.2.3 Hageman factor/amylase inhibitor {Maize (Zea mays)}
scvpgwaiphnplpscrwyvtsrtcgigprlpwpelkrrccreladipaycrctalsilm
dgaippgpdaqlegrledlpgcprevqrgfaatlvteaecnlatisgvaecpwilg
>d1bfb__ 2.37.1.1.1 Basic FGF {Human (Homo sapiens)}
pkrlycknggfflrihpdgrvdgvreksdphiklqlqaeergvvsikgvsanrylamked
grllasksvtdecffferlesnnyntyrsrkytswyvalkrtgqyklgsktgpgqkailf
lpms
>d1bfc__ 2.37.1.1.1 Basic FGF {Human (Homo sapiens)}
pkrlycknggfflrihpdgrvdgvreksdphiklqlqaeergvvsikgvsanrylamked
grllasksvtdecffferlesnnyntyrsrkytswyvalkrtgqyklgsktgpgqkailf
lpms
>d1bfd_1 3.25.1.3.5 (182-341) Benzoylformate decarboxylase {Pseudomonas putida}
svrlndqdldilvkalnsasnpaivlgpdvdaananadcvmlaerlkapvwvapsaprcp
fptrhpcfrglmpagiaaisqlleghdvvlvigapvfryhqydpgqylkpgtrlisvtcd
pleaarapmgdaivadigamasalanlveessrqlptaap
>d1bfd_2 3.29.1.1.5 (2-181) Benzoylformate decarboxylase {Pseudomonas putida}
asvhgttyellrrqgidtvfgnpgsnelpflkdfpedfryilalqeacvvgiadgyaqas
rkpafinlhsaagtgnamgalsnawnshsplivtagqqtramigvealltnvdaanlprp
lvkwsyepasaaevphamsraihmasmapqgpvylsvpyddwdkdadpqshhlfdrhvss
>d1bfd_3 3.29.1.1.5 (342-524) Benzoylformate decarboxylase {Pseudomonas putida}
epakvdqdagrlhpetvfdtlndmapenaiylneststtaqmwqrlnmrnpgsyyfcaag
glgfalpaaigvqlaeperqviavigdgsanysisalwtaaqyniptifvimnngtygal
rwfagvleaenvpgldvpgidfralakgygvqalkadnleqlkgslqealsakgpvliev
stv
>d1bfea_ 2.32.1.1.3 Synaptic protein PSD-95, 3rd PDZ domain {Rat (Rattus norvegicus)}
dipreprrivihrgstglgfniiggedgegifisfilaggpadlsgelrkgdqilsvngv
dlrnasheqaaialknagqtvtiiaqykpeeysrfeansrvnssgrivtn
>d1bff__ 2.37.1.1.1 Basic FGF {Human (Homo sapiens)}
kdpkrlycknggfflrihpdgrvdgvreksdphiklqlqaeergvvsikgvcanrylamk
edgrllaskcvtdecffferlesnnyntyrsrkytswyvalkrtgqyklgsktgpgqkai
lflpmsaks
>d1bfg__ 2.37.1.1.1 Basic FGF {Human (Homo sapiens)}
dpkrlycknggfflrihpdgrvdgvreksdphiklqlqaeergvvsikgvsanrylamke
dgrllasksvtdecffferlesnnyntyrsrkytswyvalkrtgqyklgsktgpgqkail
flpmsa
>d1bfi__ 4.72.1.1.11 Phosphatidylinositol 3-kinase, p85-alpha subunit {Human (Homo sapiens)}
edlphhdektwnvgssnrnkaenllrgkrdgtflvresskqgcyacsvvvdgevkhcvin
ktatgygfaepynlysslkelvlhyqhtslvqhndslnvtlaypvyaqqrr
>d1bfj__ 4.72.1.1.11 Phosphatidylinositol 3-kinase, p85-alpha subunit {Human (Homo sapiens)}
edlphhdektwnvgssnrnkaenllrgkrdgtflvresskqgcyacsvvvdgevkhcvin
ktatgygfaepynlysslkelvlhyqhtslvqhndslnvtlaypvyaqqrr
>d1bfk__ 3.33.1.1.2 Subtilisin Carlsberg {Bacillus licheniformis}
aqtvpygiplikadkvqaqgfkganvkvavldtgiqashpdlnvvggasfvageayntdg
nghgthvagtvaaldnttgvlgvapsvslyavkvlnssgsgsysgivsgiewattngmdv
inmslggasgstamkqavdnayargvvvvaaagnsgnsgstntigypakydsviavgavd
snsnrasfssvgaelevmapgagvystyptntyatlngtsmasphvagaaalilskhpnl
sasqvrnrlsstatylgssfyygkglinveaaaq
>d1bfma_ 1.23.1.2.2 Histone B {Methanothermus fervidus}
melpiapigriikdagaervsddaritlakileemgrdiaseaiklarhagrktikaedi
elavrrfkk
>d1bfmb_ 1.23.1.2.2 Histone B {Methanothermus fervidus}
melpiapigriikdagaervsddaritlakileemgrdiaseaiklarhagrktikaedi
elavrrfkk
>d1bfn__ 3.1.7.2.1 beta-Amylase {Soybean (Glycine max)}
nmllnyvpvyvmlplgvvnvdnvfedpdglkeqllqlraagvdgvmvdvwwgiielkgpk
qydwrayrsllqlvqecgltlqaimsfhqcggnvgdivnipipqwvldigesnhdifytn
rsgtrnkeyltvgvdnepifhgrtaieiysdymksfrenmsdflesgliidievglgpag
elrypsypqsqgwefpgigefqcydkylkadfkaavaraghpewelpddagkyndvpest
gffksngtyvtekgkffltwysnkllnhgdqildeankaflgckvklaikvsgihwwykv
enhaaeltagyynlndrdgyrpiarmlsrhhailnftclemrdseqpsdaksgpqelvqq
vlsggwredirvagenalprydataynqiilnarpqgvnnngppklsmfgvtylrlsddl
lqksnfnifkkfvlkmhadqdycanpqkynhaitplkpsapkipievlleatkptlpfpw
lpetdmkvdg
>d1bfoa1 2.1.1.1.121 (1-107) Immunoglobulin (variable domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
dikmtqspsflsasvgdrvtlnckasqnidkylnwyqqklgespklliyntnnlqtgips
rfsgsgsgtdftltisslqpedvatyfclqhisrprtfgtgtklelk
>d1bfoa2 2.1.1.2.119 (108-214) Immunoglobulin (constant domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
ranaaptvsifppsteqlatggasvvclmnkfyprdisvkwkidgterngvlnsvtdqds
adstysmsstlsltkadyqshnlytcqvvhktssspvvaknfnrnec
>d1bfob1 2.1.1.1.121 (1-121) Immunoglobulin (variable domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
evkllesggglvqpggsmrlscagsgftftdfymnwirqpagkapewlgfirdkakgytt
eynpsvkgrftisrdntqnmlylqmntlraedtatyycareghtaapfdywgqgvmvtvs
s
>d1bfob2 2.1.1.2.119 (122-216) Immunoglobulin (constant domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
aqttapsvyplapgcgdttsstvtlgclvkgyfpepvtvtwnsgalssdvhtfpavlqsg
lytltssvtsstwpsqtvtcnvahpasstkvdkkv
>d1bfoc1 2.1.1.1.121 (1-107) Immunoglobulin (variable domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
dikmtqspsflsasvgdrvtlnckasqnidkylnwyqqklgespklliyntnnlqtgips
rfsgsgsgtdftltisslqpedvatyfclqhisrprtfgtgtklelk
>d1bfoc2 2.1.1.2.119 (108-214) Immunoglobulin (constant domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
ranaaptvsifppsteqlatggasvvclmnkfyprdisvkwkidgterngvlnsvtdqds
adstysmsstlsltkadyqshnlytcqvvhktssspvvaknfnrnec
>d1bfod1 2.1.1.1.121 (1-121) Immunoglobulin (variable domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
evkllesggglvqpggsmrlscagsgftftdfymnwirqpagkapewlgfirdkakgytt
eynpsvkgrftisrdntqnmlylqmntlraedtatyycareghtaapfdywgqgvmvtvs
s
>d1bfod2 2.1.1.2.119 (122-216) Immunoglobulin (constant domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
aqttapsvyplapgcgdttsstvtlgclvkgyfpepvtvtwnsgalssdvhtfpavlqsg
lytltssvtsstwpsqtvtcnvahpasstkvdkkv
>d1bfoe1 2.1.1.1.121 (1-107) Immunoglobulin (variable domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
dikmtqspsflsasvgdrvtlnckasqnidkylnwyqqklgespklliyntnnlqtgips
rfsgsgsgtdftltisslqpedvatyfclqhisrprtfgtgtklelk
>d1bfoe2 2.1.1.2.119 (108-214) Immunoglobulin (constant domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
ranaaptvsifppsteqlatggasvvclmnkfyprdisvkwkidgterngvlnsvtdqds
adstysmsstlsltkadyqshnlytcqvvhktssspvvaknfnrnec
>d1bfof1 2.1.1.1.121 (1-121) Immunoglobulin (variable domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
evkllesggglvqpggsmrlscagsgftftdfymnwirqpagkapewlgfirdkakgytt
eynpsvkgrftisrdntqnmlylqmntlraedtatyycareghtaapfdywgqgvmvtvs
s
>d1bfof2 2.1.1.2.119 (122-216) Immunoglobulin (constant domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
aqttapsvyplapgcgdttsstvtlgclvkgyfpepvtvtwnsgalssdvhtfpavlqsg
lytltssvtsstwpsqtvtcnvahpasstkvdkkv
>d1bfog1 2.1.1.1.121 (1-107) Immunoglobulin (variable domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
dikmtqspsflsasvgdrvtlnckasqnidkylnwyqqklgespklliyntnnlqtgips
rfsgsgsgtdftltisslqpedvatyfclqhisrprtfgtgtklelk
>d1bfog2 2.1.1.2.119 (108-214) Immunoglobulin (constant domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
ranaaptvsifppsteqlatggasvvclmnkfyprdisvkwkidgterngvlnsvtdqds
adstysmsstlsltkadyqshnlytcqvvhktssspvvaknfnrnec
>d1bfoh1 2.1.1.1.121 (1-121) Immunoglobulin (variable domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
evkllesggglvqpggsmrlscagsgftftdfymnwirqpagkapewlgfirdkakgytt
eynpsvkgrftisrdntqnmlylqmntlraedtatyycareghtaapfdywgqgvmvtvs
s
>d1bfoh2 2.1.1.2.119 (122-216) Immunoglobulin (constant domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
aqttapsvyplapgcgdttsstvtlgclvkgyfpepvtvtwnsgalssdvhtfpavlqsg
lytltssvtsstwpsqtvtcnvahpasstkvdkkv
>d1bfp__ 4.20.1.1.1 Green fluorescent protein, GFP {Jellyfish (Aequorea victoria)}
mskgeelftgvvpilveldgdvnghkfsvsgegegdatygkltlkficttgklpvpwptl
vttfxvqcfsrypdhmkrhdffksampegyvqertiffkddgnyktraevkfegdtlvnr
ielkgidfkedgnilghkleynfnshnvyimadkqkngikvnfkirhniedgsvqladhy
qqntpigdgpvllpdnhylstqsalskdpnekrdhmvllefvtaagi
>d1bfra_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrb_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrc_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrd_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfre_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrf_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrg_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrh_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfri_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrj_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrk_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrl_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrm_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrn_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfro_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrp_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrq_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrr_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrs_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrt_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfru_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrv_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrw_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrx_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfs__ 2.1.1.5.22 p50 subunit of NF-kappa B transcription factor, C-terminal domain {Mouse (Mus musculus)}
asnlkivrmdrtagcvtggeeiyllcdkvqkddiqirfyeeeenggvwegfgdfsptdvh
rqfaivfktpkykdvnitkpasvfvqlrrksdletsepkpflyype
>d1bfta_ 2.1.1.5.22 p50 subunit of NF-kappa B transcription factor, C-terminal domain {Mouse (Mus musculus)}
taelkicrvnrnsgsclggdeifllcdkvqkedievyftgpgweargsfsqadvhrqvai
vfrtppyadpslqapvrvsmqlrrpsdrelsepmefqylpd
>d1bftb_ 2.1.1.5.22 p50 subunit of NF-kappa B transcription factor, C-terminal domain {Mouse (Mus musculus)}
taelkicrvnrnsgsclggdeifllcdkvqkedievyftgpgweargsfsqadvhrqvai
vfrtppyadpslqapvrvsmqlrrpsdrelsepmefqylpd
>d1bfu__ 3.33.1.1.2 Subtilisin Carlsberg {Bacillus licheniformis}
aqtvpygiplikadkvqaqgfkganvkvavldtgiqashpdlnvvggasfvageayntdg
nghgthvagtvaaldnttgvlgvapsvslyavkvlnssgsgsysgivsgiewattngmdv
inmslggasgstamkqavdnayargvvvvaaagnsgnsgstntigypakydsviavgavd
snsnrasfssvgaelevmapgagvystyptntyatlngtsmasphvagaaalilskhpnl
sasqvrnrlsstatylgssfyygkglinveaaaq
>d1bfvh_ 2.1.1.1.88 Immunoglobulin (variable domains of L and H chains) {Fv 4155 (mouse), kappa L chain}
qvqlqesggglvnlggsmtlscvasgftfntyymswvrqtpektlelvaainsdgepiyy
pdtlkgrvtisrdnakktlylqmsslnfedtalyycarlnyavygmdywgqgttvtvss
>d1bfvl_ 2.1.1.1.88 Immunoglobulin (variable domains of L and H chains) {Fv 4155 (mouse), kappa L chain}
dieltqsppslpvslgdqvsiscrssqslvsnnrrnylhwylqkpgqspklviykvsnrf
sgvpdrfsgsgsgtdftlkisrvaaedlglyfcsqsshvpltfgsgtkleikr
>d1bfx__ 4.94.1.1.2 Cytochrome b5 {Rat (Rattus norvegicus)}
dkdvkyytleeiqkhkdskstwvilhhkvydltkfleehpggeevlreqaggdatenfed
vghstdarelsktyiigelhpddrskiakpsetl
>d1bfy__ 7.35.4.1.4 Rubredoxin {Clostridium pasteurianum}
mkkytctvcgyiynpedgdpdngvnpgtdfkdipddwvcplcgvgkdqfeevee
>d1bg0_1 1.80.1.1.3 (2-95) Arginine kinase {Horseshoe crab (Limulus polyphemus)}
vdqatldkleagfkklqeasdcksllkkhltkdvfdsiknkktgmgatlldviqsgvenl
dsgvgiyapdaesyrtfgplfdpiiddyhggfkl
>d1bg0_2 4.102.1.2.3 (96-357) Arginine kinase {Horseshoe crab (Limulus polyphemus)}
tdkhppkqwgdintlvgldpagqfiistrvrcgrslqgypfnpcltaeqykemeekvsst
lssmedelkgtyypltgmskatqqqliddhflfkegdrflqtanacrywptgrgifhnda
ktflvwvneedhlriismqkggdlktvykrlvtavdniesklpfshddrfgfltfcptnl
gttmrasvhiqlpklakdrkvlediaskfnlqvrgtrgehteseggvydisnkrrlglte
yqavremqdgilemikmekaaa
>d1bg1a1 1.50.1.1.2 (136-321) STAT3b {Mouse (Mus musculus)}
vvtekqqmleqhlqdvrkrvqdleqkmkvvenlqddfdfnyktlksqgdmqdlngnnqsv
trqkmqqleqmltaldqmrrsivselagllsameyvqktltdeeladwkrrqqiaciggp
pnicldrlenwitslaesqlqtrqqikkleelqqkvsykgdpivqhrpmleerivelfrn
lmksaf
>d1bg1a2 2.2.5.1.10 (322-575) STAT3b {Mouse (Mus musculus)}
vverqpcmpmhpdrplviktgvqfttkvrllvkfpelnyqlkikvcidkdsgdvaalrgs
rkfnilgtntkvmnmeesnngslsaefkhltlreqrcgnggrancdaslivteelhlitf
etevyhqglkidlethslpvvvisnicqmpnawasilwynmltnnpknvnfftkppigtw
dqvaevlswqfssttkrglsieqlttlaekllgpgvnysgcqitwakfckenmagkgfsf
wvwldniidlvkky
>d1bg1a3 4.72.1.1.18 (576-716) STAT3b {Mouse (Mus musculus)}
ilalwnegyimgfiskererailstkppgtfllrfsesskeggvtftwvekdisgstqiq
svepytkqqlnnmsfaeiimgykimdatnilvsplvylypdipkeeafgkycrpesqehp
eadpgsaapxlktkficvtpf
>d1bg2__ 3.30.1.7.4 Kinesin {Human (Homo sapiens)}
dlaecnikvmcrfrplnesevnrgdkyiakfqgedtvviaskpyafdrvfqsstsqeqvy
ndcakkivkdvlegyngtifaygqtssgkthtmegklhdpegmgiiprivqdifnyiysm
denlefhikvsyfeiyldkirdlldvsktnlsvhedknrvpyvkgcterfvcspdevmdt
idegksnrhvavtnmnehssrshsiflinvkqentqteqklsgklylvdlagsekvsktg
aegavldeakninkslsalgnvisalaegstyvpyrdskmtrilqdslggncrttivicc
spssynesetkstllfgqrakti
>d1bg3a1 3.46.1.2.3 (1-222) Mammalian type I hexokinase {Rat (Rattus norvegicus)}
miaaqllayyftelkddqvkkidkylyamrlsdeilidiltrfkkemknglsrdynptas
vkmlptfvrsipdgsekgdfialdlggssfrilrvqvnheknqnvsmeseiydtpenivh
gsgtqlfdhvadclgdfmekkkikdkklpvgftfsfpcrqskideavlitwtkrfkasgv
egadvvkllnkaikkrgdydanivavvndtvgtmmtcgyddq
>d1bg3a2 3.46.1.2.3 (223-465) Mammalian type I hexokinase {Rat (Rattus norvegicus)}
qcevgliigtgtnacymeelrhidlvegdegrmcintewgafgddgsledirtefdreld
rgslnpgkqlfekmvsgmymgelvrlilvkmakegllfegritpelltrgkfntsdvsai
ekdkegiqnakeiltrlgvepsdvdcvsvqhictivsfrsanlvaatlgailnrlrdnkg
tprlrttvgvdgslykmhpqysrrfhktlrrlvpdsdvrfllsesgtgkgaamvtavayr
lae
>d1bg3a3 3.46.1.2.3 (466-670) Mammalian type I hexokinase {Rat (Rattus norvegicus)}
qhirqieetlahfrlskqtlmevkkrlrtememglrketnskatvkmlpsfvrsipdgte
hgdflaldlggtnfrvllvkirsgkkrtvemhnkiysipleimqgtgdelfdhivscisd
fldymgikgprmplgftfsfpchqtnldcgiliswtkgfkatdceghdvasllrdavkrr
eefdldvvavvndtvgtmmtcayeep
>d1bg3a4 3.46.1.2.3 (671-911) Mammalian type I hexokinase {Rat (Rattus norvegicus)}
tceiglivgtgtnacymeemknvemvegnqgqmcinmewgafgdngclddirtdfdkvvd
eyslnsgkqrfekmisgmylgeivrnilidftkkgflfrgqiseplktrgifetkflsqi
esdrlallqvrailqqlglnstcddsilvktvcgvvskraaqlcgagmaavvekirenrg
ldhlnvtvgvdgtlyklhphfsrimhqtvkelspkctvsfllsedgsgkgaalitavgvr
lrgdpsia
>d1bg3b1 3.46.1.2.3 (1-222) Mammalian type I hexokinase {Rat (Rattus norvegicus)}
miaaqllayyftelkddqvkkidkylyamrlsdeilidiltrfkkemknglsrdynptas
vkmlptfvrsipdgsekgdfialdlggssfrilrvqvnheknqnvsmeseiydtpenivh
gsgtqlfdhvadclgdfmekkkikdkklpvgftfsfpcrqskideavlitwtkrfkasgv
egadvvkllnkaikkrgdydanivavvndtvgtmmtcgyddq
>d1bg3b2 3.46.1.2.3 (223-465) Mammalian type I hexokinase {Rat (Rattus norvegicus)}
qcevgliigtgtnacymeelrhidlvegdegrmcintewgafgddgsledirtefdreld
rgslnpgkqlfekmvsgmymgelvrlilvkmakegllfegritpelltrgkfntsdvsai
ekdkegiqnakeiltrlgvepsdvdcvsvqhictivsfrsanlvaatlgailnrlrdnkg
tprlrttvgvdgslykmhpqysrrfhktlrrlvpdsdvrfllsesgtgkgaamvtavayr
lae
>d1bg3b3 3.46.1.2.3 (466-670) Mammalian type I hexokinase {Rat (Rattus norvegicus)}
qhirqieetlahfrlskqtlmevkkrlrtememglrketnskatvkmlpsfvrsipdgte
hgdflaldlggtnfrvllvkirsgkkrtvemhnkiysipleimqgtgdelfdhivscisd
fldymgikgprmplgftfsfpchqtnldcgiliswtkgfkatdceghdvasllrdavkrr
eefdldvvavvndtvgtmmtcayeep
>d1bg3b4 3.46.1.2.3 (671-911) Mammalian type I hexokinase {Rat (Rattus norvegicus)}
tceiglivgtgtnacymeemknvemvegnqgqmcinmewgafgdngclddirtdfdkvvd
eyslnsgkqrfekmisgmylgeivrnilidftkkgflfrgqiseplktrgifetkflsqi
esdrlallqvrailqqlglnstcddsilvktvcgvvskraaqlcgagmaavvekirenrg
ldhlnvtvgvdgtlyklhphfsrimhqtvkelspkctvsfllsedgsgkgaalitavgvr
l
>d1bg4__ 3.1.7.3.2 Xylanase {Penicillium simplicissimum}
asvsidakfkahgkkylgtigdqytltkntknpaiikadfgqltpensmkwdatepnrgq
ftfsgsdylvnfaqsngklirghtlvwhsqlpgwvssitdkntlisvlknhittvmtryk
gkiyawdvlneifnedgslrnsvfynvigedyvriafetarsvdpnaklyindynldsag
yskvngmvshvkkwlaagipidgigsqthlgagagsavagalnalasagtkeiaiteldi
agasstdyvnvvnaclnqakcvgitvwgvadpdswrsssspllfdgnynpkaaynaiana
l
>d1bg5_1 1.48.1.1.14 (81-254) Glutathione S-transferase {Schistosoma japonicum}
mlggcpkeraeismlegavldirygvsriayskdfetlkvdflsklpemlkmfedrlchk
tylngdhvthpdfmlydaldvvlymdpmcldafpklvcfkkrieaipqidkylksskyia
wplqgwqatfgggdhppksdlvprgssyyqeaksskimesfknmvpqqalvnss
>d1bg5_2 3.38.1.5.14 (1-80) Glutathione S-transferase {Schistosoma japonicum}
mspilgywkikglvqptrllleyleekyeehlyerdegdkwrnkkfelglefpnlpyyid
gdvkltqsmaiiryiadkhn
>d1bg6_1 1.96.1.4.1 (188-359) N-(1-D-carboxylethyl)-L-norvaline dehydrogenase {Arthrobacter strain 1c}
nvlhtsltnvnavmhplptllnaarcesgtpfqyylegitpsvgslaekvdaeriaiaka
fdlnvpsvcewykesygqspatiyeavqgnpayrgiagpinlntryffedvstglvplse
lgravnvptplidavldlisslidtdfrkegrtleklglsgltaagirsave
>d1bg6_2 3.2.1.6.6 (4-187) N-(1-D-carboxylethyl)-L-norvaline dehydrogenase {Arthrobacter strain 1c}
sktyavlglgngghafaaylalkgqsvlawdidaqrikeiqdrgaiiaegpglagtahpd
lltsdiglavkdadvilivvpaihhasiaaniasyisegqliilnpgatggalefrkilr
engapevtigetssmlftcrserpgqvtvnaikgamdfaclpaakagwaleqigsvlpqy
vave
>d1bg7__ 1.26.1.1.6 (Apo)ferritin {Bullfrog (Rana catesbeiana)}
dsqvrqnfhrdceaainrmvnmelyasytylsmafyfdrddialhnvakffkeqsheere
haeklmkdqnkrggrivlqdvqkperdewgntleamqaalqlektvnqalldlhkvgsdk
vdphlcdfleteypeeqvksikqlgdyitnlkrlglpqngmgeylfdkhtmge
>d1bg8a_ 1.59.1.1.1 HdeA {Escherichia coli}
kkpvnswtcedflavdesfqptavgfaealnnkdkpedavldvqgiatvtpaivqactqd
kqanfkdkvkgewdki
>d1bg8b_ 1.59.1.1.1 HdeA {Escherichia coli}
kkpvnswtcedflavdesfqptavgfaealnnkdkpedavldvqgiatvtpaivqactqd
kqanfkdkvkgewdki
>d1bg8c_ 1.59.1.1.1 HdeA {Escherichia coli}
kkpvnswtcedflavdesfqptavgfaealnnkdkpedavldvqgiatvtpaivqactqd
kqanfkdkvkgewdki
>d1bg9_1 2.62.1.1.16 (347-403) Plant alpha-amylase {Barley (Hordeum vulgare), seeds, AMY2 isozyme}
hnesklqiieadadlylaeidgkvivklgprydvgnlipggfkvaahgndyavweki
>d1bg9_2 3.1.7.1.16 (1-346) Plant alpha-amylase {Barley (Hordeum vulgare), seeds, AMY2 isozyme}
qvlfqgfnweswkhnggwynflmgkvddiaaagithvwlppasqsvaeqgympgrlydld
askygnkaqlksligalhgkgvkaiadivinhrtaehkdgrgiycifeggtpdarldwgp
hmicrddrpyadgtgnpdtgadfgaapdidhlnlrvqkelvewlnwlkadigfdgwrfdf
akgysadvakiyidrsepsfavaeiwtslayggdgkpnlnqdqhrqelvnwvdkvggkgp
attfdfttkgilnvavegelwrlrgtdgkapgmigwwpakavtfvdnhdtgstqhmwpfp
sdrvmqgyayilthpgtpcifydhffdwglkeeidrlvsvrtrhgi
>d1bgaa_ 3.1.7.4.4 Beta-glucosidase A {Bacillus polymyxa}
tifqfpqdfmwgtataayqiegayqedgrglsiwdtfahtpgkvfngdngnvacdsyhry
eedirlmkelgirtyrfsvswprifpngdgevnqegldyyhrvvdllndngiepfctlyh
wdlpqalqdaggwgnrrtiqafvqfaetmfrefhgkiqhwltfnepwciaflsnmlgvha
pgltnlqtaidvghhllvahglsvrrfrelgtsgqigiapnvswavpystseedkaacar
tislhsdwflqpiyqgsypqflvdwfaeqgatvpiqdgdmdiigepidmiginyysmsvn
rfnpeagflqseeinmglpvtdigwpvesrglyevlhylqkygnidiyitengacindev
vngkvqddrrisymqqhlvqvhrtihdglhvkgymawslldnfewaegynmrfgmihvdf
rtqvrtpkesyywyrnvvsnnwletrr
>d1bgab_ 3.1.7.4.4 Beta-glucosidase A {Bacillus polymyxa}
tifqfpqdfmwgtataayqiegayqedgrglsiwdtfahtpgkvfngdngnvacdsyhry
eedirlmkelgirtyrfsvswprifpngdgevnqegldyyhrvvdllndngiepfctlyh
wdlpqalqdaggwgnrrtiqafvqfaetmfrefhgkiqhwltfnepwciaflsnmlgvha
pgltnlqtaidvghhllvahglsvrrfrelgtsgqigiapnvswavpystseedkaacar
tislhsdwflqpiyqgsypqflvdwfaeqgatvpiqdgdmdiigepidmiginyysmsvn
rfnpeagflqseeinmglpvtdigwpvesrglyevlhylqkygnidiyitengacindev
vngkvqddrrisymqqhlvqvhrtihdglhvkgymawslldnfewaegynmrfgmihvdf
rtqvrtpkesyywyrnvvsnnwletrr
>d1bgac_ 3.1.7.4.4 Beta-glucosidase A {Bacillus polymyxa}
tifqfpqdfmwgtataayqiegayqedgrglsiwdtfahtpgkvfngdngnvacdsyhry
eedirlmkelgirtyrfsvswprifpngdgevnqegldyyhrvvdllndngiepfctlyh
wdlpqalqdaggwgnrrtiqafvqfaetmfrefhgkiqhwltfnepwciaflsnmlgvha
pgltnlqtaidvghhllvahglsvrrfrelgtsgqigiapnvswavpystseedkaacar
tislhsdwflqpiyqgsypqflvdwfaeqgatvpiqdgdmdiigepidmiginyysmsvn
rfnpeagflqseeinmglpvtdigwpvesrglyevlhylqkygnidiyitengacindev
vngkvqddrrisymqqhlvqvhrtihdglhvkgymawslldnfewaegynmrfgmihvdf
rtqvrtpkesyywyrnvvsnnwletrr
>d1bgad_ 3.1.7.4.4 Beta-glucosidase A {Bacillus polymyxa}
tifqfpqdfmwgtataayqiegayqedgrglsiwdtfahtpgkvfngdngnvacdsyhry
eedirlmkelgirtyrfsvswprifpngdgevnqegldyyhrvvdllndngiepfctlyh
wdlpqalqdaggwgnrrtiqafvqfaetmfrefhgkiqhwltfnepwciaflsnmlgvha
pgltnlqtaidvghhllvahglsvrrfrelgtsgqigiapnvswavpystseedkaacar
tislhsdwflqpiyqgsypqflvdwfaeqgatvpiqdgdmdiigepidmiginyysmsvn
rfnpeagflqseeinmglpvtdigwpvesrglyevlhylqkygnidiyitengacindev
vngkvqddrrisymqqhlvqvhrtihdglhvkgymawslldnfewaegynmrfgmihvdf
rtqvrtpkesyywyrnvvsnnwletrr
>d1bgba_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgrk
>d1bgbb_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgrk
>d1bgc__ 1.27.1.1.2 Granulocyte-colony stimulating factor (G-CSF) {Bovine (Bos taurus)}
slpqsfllkcleqvrkiqadgaelqerlcaahklchpeelmllrhslgipqaplsscssq
slqlrgclnqlhgglflyqgllqalagispelaptldtlqldvtdfatniwlqmedlgaa
pavqptqgamptftsafqrraggvlvasqlhrflelayrglryla
>d1bgd__ 1.27.1.1.3 Granulocyte-colony stimulating factor (G-CSF) {Canine (Canis familiaris)}
lpqsfllkcleqmrkvqadgtalqetlcathqlchpeelvllghalgipqpplsscssqa
lqlmgclrqlhsglflyqgllqalagispelaptldtlqldttdfainiwqqmedlgmap
avpptqgtmpaftsafqrraggvlvasnlqsflelayralrhfa
>d1bgea_ 1.27.1.1.3 Granulocyte-colony stimulating factor (G-CSF) {Canine (Canis familiaris)}
plpqsfllkcleqmrkvqadgtalqetlcathqlchpeelvllghalgipqpplsscssq
alqlmgclrqlhsglflyqgllqalagispelaptldtlqldttdfainiwqqmedlgma
pavpptqgtmpaftsafqrraggvlvasnlqsflelayralrhfak
>d1bgeb_ 1.27.1.1.3 Granulocyte-colony stimulating factor (G-CSF) {Canine (Canis familiaris)}
plpqsfllkcleqmrkvqadgtalqetlcathqlchpeelvllghalgipqpplsscssq
alqlmgclrqlhsglflyqgllqalagispelaptldtlqldttdfainiwqqmedlgma
pavpptqgtmpaftsafqrraggvlvasnlqsflelayralrhfa
>d1bgf__ 1.87.1.1.1 Transcription factor STAT-4 N-domain {Mouse (Mus musculus)}
ggsqwnqvqqleikfleqvdqfyddnfpmeirhllaqwietqdwevasnnetmatillqn
lliqldeqlgrvskeknlllihnlkrirkvlqgkfhgnpmhvavvisnclreerrilaaa
nmpi
>d1bgga_ 3.1.7.4.4 Beta-glucosidase A {Bacillus polymyxa}
tifqfpqdfmwgtataayqiegayqedgrglsiwdtfahtpgkvfngdngnvacdsyhry
eedirlmkelgirtyrfsvswprifpngdgevnqegldyyhrvvdllndngiepfctlyh
wdlpqalqdaggwgnrrtiqafvqfaetmfrefhgkiqhwltfnepwciaflsnmlgvha
pgltnlqtaidvghhllvahglsvrrfrelgtsgqigiapnvswavpystseedkaacar
tislhsdwflqpiyqgsypqflvdwfaeqgatvpiqdgdmdiigepidmiginyysmsvn
rfnpeagflqseeinmglpvtdigwpvesrglyevlhylqkygnidiyitengacindev
vngkvqddrrisymqqhlvqvhrtihdglhvkgymawslldnfewaegynmrfgmihvdf
rtqvrtpkesyywyrnvvsnnwletrr
>d1bggb_ 3.1.7.4.4 Beta-glucosidase A {Bacillus polymyxa}
tifqfpqdfmwgtataayqiegayqedgrglsiwdtfahtpgkvfngdngnvacdsyhry
eedirlmkelgirtyrfsvswprifpngdgevnqegldyyhrvvdllndngiepfctlyh
wdlpqalqdaggwgnrrtiqafvqfaetmfrefhgkiqhwltfnepwciaflsnmlgvha
pgltnlqtaidvghhllvahglsvrrfrelgtsgqigiapnvswavpystseedkaacar
tislhsdwflqpiyqgsypqflvdwfaeqgatvpiqdgdmdiigepidmiginyysmsvn
rfnpeagflqseeinmglpvtdigwpvesrglyevlhylqkygnidiyitengacindev
vngkvqddrrisymqqhlvqvhrtihdglhvkgymawslldnfewaegynmrfgmihvdf
rtqvrtpkesyywyrnvvsnnwletrr
>d1bggc_ 3.1.7.4.4 Beta-glucosidase A {Bacillus polymyxa}
tifqfpqdfmwgtataayqiegayqedgrglsiwdtfahtpgkvfngdngnvacdsyhry
eedirlmkelgirtyrfsvswprifpngdgevnqegldyyhrvvdllndngiepfctlyh
wdlpqalqdaggwgnrrtiqafvqfaetmfrefhgkiqhwltfnepwciaflsnmlgvha
pgltnlqtaidvghhllvahglsvrrfrelgtsgqigiapnvswavpystseedkaacar
tislhsdwflqpiyqgsypqflvdwfaeqgatvpiqdgdmdiigepidmiginyysmsvn
rfnpeagflqseeinmglpvtdigwpvesrglyevlhylqkygnidiyitengacindev
vngkvqddrrisymqqhlvqvhrtihdglhvkgymawslldnfewaegynmrfgmihvdf
rtqvrtpkesyywyrnvvsnnwletrr
>d1bggd_ 3.1.7.4.4 Beta-glucosidase A {Bacillus polymyxa}
tifqfpqdfmwgtataayqiegayqedgrglsiwdtfahtpgkvfngdngnvacdsyhry
eedirlmkelgirtyrfsvswprifpngdgevnqegldyyhrvvdllndngiepfctlyh
wdlpqalqdaggwgnrrtiqafvqfaetmfrefhgkiqhwltfnepwciaflsnmlgvha
pgltnlqtaidvghhllvahglsvrrfrelgtsgqigiapnvswavpystseedkaacar
tislhsdwflqpiyqgsypqflvdwfaeqgatvpiqdgdmdiigepidmiginyysmsvn
rfnpeagflqseeinmglpvtdigwpvesrglyevlhylqkygnidiyitengacindev
vngkvqddrrisymqqhlvqvhrtihdglhvkgymawslldnfewaegynmrfgmihvdf
rtqvrtpkesyywyrnvvsnnwletrr
>d1bgi__ 4.2.1.2.1 Lysozyme {Chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1bgj_1 3.3.1.2.4 (1-173,276-391) p-Hydroxybenzoate hydroxylase (PHBH) {Pseudomonas aeruginosa}
mktqvaiigagpsglllgqllhkagidnvilerqtpdyvlgriragvleqgmvdllreag
vdrrmardglvhegveiafagqrrridlkrlsggktvtvygqtevtrdlmeareasgatt
vyqaaevrlhdlqgerpyvtferdgerlrldcdyiagcdgfrgisrqsipaerXmqhgrl
flagdaahivpptgakglnlaasdvstlyrlllkayregrgellerysaiclrriwkaer
fswwmtsvlhrfpdtdafsqriqqteleyylgseaglatiaenyvglpye
>d1bgj_2 4.14.1.2.2 (174-275) p-Hydroxybenzoate hydroxylase, PHBH {Pseudomonas aeruginosa}
lkvfervypfgwlglladtppvsheliyanhprgfalcsqrsatrsryyvqvpltekved
wsderfwtelkarlpaevaeklvtgpsleksiaplrsfvvep
>d1bgk__ 7.19.1.1.1 Sea anemone toxin k {Sea anemone (Bunodosoma granulifera), BGK}
vcrdwfketacrhakslgncrtsqkyrancaktcelc
>d1bgla1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgla2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgla3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgla4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgla5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bglb1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bglb2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bglb3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bglb4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bglb5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bglc1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bglc2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bglc3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bglc4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bglc5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgld1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgld2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgld3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgld4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgld5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgle1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgle2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgle3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgle4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgle5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bglf1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bglf2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bglf3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bglf4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bglf5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bglg1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bglg2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bglg3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bglg4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bglg5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bglh1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bglh2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bglh3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bglh4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bglh5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgmi1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgmi2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgmi3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgmi4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgmi5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgmj1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgmj2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgmj3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgmj4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgmj5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgmk1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgmk2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgmk3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgmk4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgmk5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgml1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgml2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgml3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgml4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgml5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgmm1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgmm2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgmm3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgmm4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgmm5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgmn1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgmn2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgmn3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgmn4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgmn5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgmo1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgmo2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgmo3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgmo4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgmo5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgmp1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgmp2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgmp3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgmp4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgmp5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgn_1 3.3.1.2.4 (1-173,276-391) p-Hydroxybenzoate hydroxylase (PHBH) {Pseudomonas aeruginosa}
mktqvaiigagpsglllgqllhkagidnvilerqtpdyvlgriragvleqgmvdllreag
vdrrmardglvhegveiafagqrrridlkrlsggktvtvygqtevtrdlmeareasgatt
vyqaaevrlhdlqgerpyvtferdgerlrldcdyiagcdgfhgisrqsipaerXmqhgrl
flagdaahivpptgakglnlaasdvstlyrlllkayregrgellerysaiclrriwkaer
fswwmtsvlhrfpdtdafsqriqqteleyylgseaglatiaenyvglpye
>d1bgn_2 4.14.1.2.2 (174-275) p-Hydroxybenzoate hydroxylase, PHBH {Pseudomonas aeruginosa}
lkvfervypfgwlglladtppvsheliyanhprgfalcsqrsatrsryyvqvpltekved
wsderfwtelkarlpaevaeklvtgpsleksiapltsfvvep
>d1bgo__ 4.3.1.1.13 (Pro)cathepsin K {Human (Homo sapiens)}
apdsvdyrkkgyvtpvknqgqcgscwafssvgalegqlkkktgkllnlspqnlvdcvsen
dgcgggymtnafqyvqknrgidsedaypyvgqeescmynptgkaakcrgyreipegneka
lkravarvgpvsvaidasltsfqfyskgvyydescnsdnlnhavlavgygiqkgnkhwii
knswgenwgnkgyilmarnknnacgianlasfpkm
>d1bgp__ 1.90.1.1.8 Peroxidase 1 {Barley (Hordeum vulgare), grain}
aeppvapglsfdfywqtcpraesivrefvqeavrkdiglaagllrlhfhdcfvqgcdasv
lldgsatgpgeqqappnltlrpsafkavndirdrlerecrgavvscsdilalaardsvvv
sggpdyrvplgrrdsrsfastqdvlsdlpgpssnvqsllallgrlgldatdlvtisgght
iglahcssfedrlfprpdptisptflsrlkrtcpakgtdrrtvldvrtpnvfdnkyyidl
vnreglfvsdqdlftnaitrpiverfaqsqqdffeqfgvsigkmgqmrvrtsdqgevrrn
csvrnpgpg
>d1bgq__ 4.96.1.1.1 HSP90 {Baker's yeast (Saccharomyces cerevisiae)}
masetfefqaeitqlmsliintvysnkeiflrelisnasdaldkirykslsdpkqletep
dlfiritpkpeqkvleirdsgigmtkaelinnlgtiaksgtkafmealsagadvsmigqf
gvgfyslflvadrvqvisksnddeqyiwesnaggsftvtldevnerigrgtilrlflkdd
qleyleekrikevikrhsefvaypiqlvvtkeve
>d1bgsa_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
aqvintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnre
gklpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1bgsb_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
aqvintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnre
gklpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1bgsc_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
aqvintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnre
gklpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1bgse_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdaltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegaditiils
>d1bgsf_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdaltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegaditiils
>d1bgsg_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdaltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegaditiils
>d1bgt__ 3.77.1.1.1 beta-Glucosyltransferase (DNA-modifying) {Bacteriophage T4}
mkiaiinmgnnvinfktvpssetiylfkvisemglnvdiislkngvytksfdevdvndyd
rlivvnssinffggkpnlailsaqkfmakykskiyylftdirlpfsqswpnvknrpwayl
yteeellikspikvisqginldiakaahkkvdnviefeyfpieqykihmndfqlskptkk
tldviyggsfrsgqreskmveflfdtglnieffgnarekqfknpkypwtkapvftgkipm
nmvseknsqaiaaliigdknyndnfitlrvwetmasdavmlideefdtkhriindarfyv
nnraelidrvnelkhsdvlrkemlsiqhdilnktrakkaewqdafkkaidl
>d1bgu__ 3.77.1.1.1 beta-Glucosyltransferase (DNA-modifying) {Bacteriophage T4}
mkiaiinmgnnvinfktvpssetiylfkvisemglnvdiislkngvytksfdevdvndyd
rlivvnssinffggkpnlailsaqkfmakykskiyylftdirlpfsqswpnvknrpwayl
yteeellikspikvisqginldiakaahkkvdnviefeyfpieqykihmndfqlskptkk
tldviyggsfrsgqreskmveflfdtglnieffgnarekqfknpkypwtkapvftgkipm
nmvseknsqaiaaliigdknyndnfitlrvwetmasdavmlideefdtkhriindarfyv
nnraelidrvnelkhsdvlrkemlsiqhdilnktrakkaewqdafkkaidl
>d1bgva1 3.2.1.7.1 (195-449) Glutamate dehydrogenase {Clostridium symbiosum}
karsfggslvrpeatgygsvyyveavmkhendtlvgktvalagfgnvawgaakklaelga
kavtlsgpdgyiydpegitteekinymlemrasgrnkvqdyadkfgvqffpgekpwgqkv
diimpcatqndvdleqakkivannvkyyievanmpttnealrflmqqpnmvvapskavna
ggvlvsgfemsqnserlswtaeevdsklhqvmtdihdgsaaaaeryglgynlvaganivg
fqkiadammaqgiaw
>d1bgva2 3.48.1.1.1 (1-194) Glutamate dehydrogenase {Clostridium symbiosum}
skyvdrviaevekkyadepefvqtveevlsslgpvvdahpeyeevallermvipervief
rvpweddngkvhvntgyrvqfngaigpykgglrfapsvnlsimkflgfeqafkdslttlp
mggakggsdfdpngksdrevmrfcqafmtelyrhigpdidvpagdlgvgareigymygqy
rkivggfyngvltg
>d1bgw__ 5.11.1.1.1 DNA topoisomerase II, C-terminal fragment (residues 410-1202) {Baker's yeast (Saccharomyces cerevisiae)}
rksritnypkledankagtkegykctlvltegdsalslavaglavvgrdyygcyplrgkm
lnvreasadqilknaeiqaikkimglqhrkkyedtkslryghlmimtdqdhdgshikgli
inflessflglldiqgfllefitpiikvsitkptkntiafynmpdyekwreeeshkftwk
qkyykglgtslaqevreyfsnldrhlkifhslqgndkdyidlafskkkaddrkewlrqye
pgtvldptlkeipisdfinkelilfsladnirsipnvldgfkpgqrkvlygcfkknlkse
lkvaqlapyvsectayhhgeqslaqtiiglaqnfvgsnniylllpngafgtratggkdaa
aaryiytelnkltrkifhpaddplykyiqedektvepewylpilpmilvngaegigtgws
tyippfnpleiiknirhlmndeeleqmhpwfrgwtgtieeieplryrmygrieqigdnvl
eitelpartwtstikeylllglsgndkikpwikdmeeqhddnikfiitlspeemaktrki
gfyerfklispislmnmvafdphgkikkynsvneilsefyyvrleyyqkrkdhmserlqw
evekysfqvkfikmiiekeltvtnkprnaiiqelenlgfprfnkegkpyygspndeiaeq
indvkgatsdeedeesshedtenvingpeelygtyeyllgmriwsltkeryqkllkqkqe
ketelenllklsakdiwntdlkafevgyqeflqrdaear
>d1bgxh1 2.1.1.1.105 (5-115) Immunoglobulin (variable domains of L and H chains) {Fab TP7 (mouse), kappa L chain}
qesgpglvkpyqslslsctvtgysitsdyawnwirqfpgnklewmgyitysgttdynpsl
ksrisitrdtsknqfflqlnsvttedtatyycaryyygywyfdvwgqgttltvss
>d1bgxh2 2.1.1.2.106 (116-209) Immunoglobulin (constant domains of L and H chains) {Fab TP7 (mouse), kappa L chain}
akttapsvyplapvssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsdlytlss
svtvtsstwpsqsitcnvahpasstkvdkkiepr
>d1bgxl1 2.1.1.1.105 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab TP7 (mouse), kappa L chain}
diqmtqspaimsaspgekvtmtcsasssvsymywyqqkpgssprlliydstnlasgvpvr
fsgsgsgtsysltisrmeaedaatyycqqwstypltfgagtklelk
>d1bgxl2 2.1.1.2.106 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab TP7 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1bgxt1 1.61.3.1.2 (174-289) 5' to 3' exonuclease domain of DNA polymerase <i>Taq</i> {Thermus aquaticus}
lrpdqwadyraltgdesdnlpgvkgigektarklleewgsleallknldrlkpairekil
ahmddlklswdlakvrtdlplevdfakrrepdrerlraflerlefgsllhefglle
>d1bgxt2 3.44.1.2.2 (1-173) 5' to 3' exonuclease domain of DNA polymerase <i>Taq</i> {Thermus aquaticus}
mrgmlplfepkgrvllvdghhlayrtfhalkglttsrgepvqavygfaksllkalkedgd
avivvfdakapsfrheayggykagraptpedfprqlalikelvdllglarlevpgyeadd
vlaslakkaekegyevriltadkdlyqllsdrihvlhpegylitpawlwekyg
>d1bgxt3 3.46.3.5.2 (290-450) Exonuclease domain of DNA polymerase {Thermus aquaticus}
spkaleeapwpppegafvgfvlsrkepmwadllalaaarggrvhrapepykalrdlkear
gllakdlsvlalreglglppgddpmllaylldpsnttpegvarryggewteeageraals
erlfanlwgrlegeerllwlyreverplsavlahmeatgvr
>d1bgxt4 5.8.1.1.2 (451-832) DNA polymerase I (Klenow fragment) {Thermus aquaticus}
ldvaylralslevaeeiarleaevfrlaghpfnlnsrdqlervlfdelglpaigktektg
krstsaavlealreahpivekilqyreltklkstyidplpdlihprtgrlhtrfnqtata
tgrlsssdpnlqnipvrtplgqrirrafiaeegwllvaldysqielrvlahlsgdenlir
vfqegrdihtetaswmfgvpreavdplmrraaktinfgvlygmsahrlsqelaipyeeaq
afieryfqsfpkvrawiektleegrrrgyvetlfgrrryvpdlearvksvreaaermafn
mpvqgtaadlmklamvklfprleemgarmllqvhdelvleapkeraeavarlakevmegv
yplavplevevgigedwlsake
>d1bgya_ 4.106.1.1.1 Core 1 subunit {Bovine (Bos taurus)}
tatyaqalqsvpetqvsqldnglrvaseqssqptctvgvwidagsryeseknngagyfve
hlafkgtknrpgnalekevesmgahlnaystrehtayyikalskdlpkavelladivqnc
sledsqiekerdvilqelqendtsmrdvvfnylhatafqgtplaqsvegpsenvrklsra
dlteylsrhykaprmvlaaagglehrqlldlaqkhfsglsgtydedavptlspcrftgsq
ichredglplahvaiavegpgwahpdnvalqvanaiighydctygggahlssplasiaat
nklcqsfqtfnicyadtgllgahfvcdhmsiddmmfvlqgqwmrlctsatesevlrgknl
lrnalvshldgttpvcedigrslltygrriplaewesriaevdarvvrevcskyfydqcp
avagfgpieqlpdynrirsgmfwlrf
>d1bgyb_ 4.106.1.1.3 Core 2 subunit {Bovine (Bos taurus)}
pqdleftrlpnglviaslenyapasriglfikagsryensnnlgtshllrlasslttkga
ssfkitrgieavggklsvtstrenmaytveclrddvdilmefllnvttapefrrwevaal
qpqlridkavalqnpqahvienlhaaayrnalanslycpdyrigkvtpvelhdyvqnhft
sarmaliglgvshpvlkqvaeqflnirgglglsgakakyhggeireqngdslvhaalvae
saaigsaeanafsvlqhvlgagphvkrgsnatsslyqavakgvhqpfdvsafnasysdsg
lfgfytisqaasagdvikaaynqvktiaqgnlsnpdvqaaknklkagylmsvessegfld
evgsqalaagsytppstvlqqidavadadvinaakkfvsgrksmaasgnlghtpfidel
>d1bgyc1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
mtnirkshplmkivnnafidlpapsnisswwnfgsllgiclilqiltglflamhytsdtt
tafssvthicrdvnygwiirymhangasmfficlymhvgrglyygsytfletwnigvill
ltvmatafmgyvlpwgqmsfwgatvitnllsaipyigtnlvewiwggfsvdkatltrffa
fhfilpfiimaiamvhllflhetgsnnptgissdvdkipfhpyytikdilgalllilalm
llvlfapdllgdpdnytpanplntpphikpewyflfayailrsipnklggvlalafsili
lalipllhtskqrsmmfrplsqclfwalvadlltltwiggqpvehpyitigqlasvlyfl
lilvlmptagtienkllkw
>d1bgyd1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
sdlelhppsypwshrgllssldhtsirrgfqvykqvcsschsmdyvayrhlvgvcytede
akalaeevevqdgpnedgemfmrpgklsdyfpkpypnpeaaraanngalppdlsyivrar
hggedyvfslltgycepptgvslreglyfnpyfpgqaigmappiynevlefddgtpatms
qvakdvctflrwaaepehdhrkrmglkmllmmglllplvyamkrhkwsvlksrklayrpp
k
>d1bgye1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
shtdikvpdfsdyrrpevldstksskessearkgfsylvtatttvgvayaaknvvsqfvs
smsasadvlamskie
>d1bgyf1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
avsassrwlegirkwyynaagfnklglmrddtihenddvkeairrlpenlyddrvfrikr
aldlsmrqqilpkeqwtkyeedksylepylkevirerkereewakk
>d1bgyg1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
grqfghltrvrhvityslspfeqrafphyfskgipnvlrrtracilrvappfvafylvyt
wgtqefekskrknpaayendr
>d1bgyh1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
dplttvreqceqlekcvkarerlelcdervssrsqteedcteelldflhardhcvahklf
nslk
>d1bgyj1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
vaptltarlysllfrrtstfaltivvgalfferafdqgadaiyehinegklwkhikhkye
nk
>d1bgyk1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
rnwvptaqlwgavgavglvsat
>d1bgym_ 4.106.1.1.1 Core 1 subunit {Bovine (Bos taurus)}
tatyaqalqsvpetqvsqldnglrvaseqssqptctvgvwidagsryeseknngagyfve
hlafkgtknrpgnalekevesmgahlnaystrehtayyikalskdlpkavelladivqnc
sledsqiekerdvilqelqendtsmrdvvfnylhatafqgtplaqsvegpsenvrklsra
dlteylsrhykaprmvlaaagglehrqlldlaqkhfsglsgtydedavptlspcrftgsq
ichredglplahvaiavegpgwahpdnvalqvanaiighydctygggahlssplasiaat
nklcqsfqtfnicyadtgllgahfvcdhmsiddmmfvlqgqwmrlctsatesevlrgknl
lrnalvshldgttpvcedigrslltygrriplaewesriaevdarvvrevcskyfydqcp
avagfgpieqlpdynrirsgmfwlrf
>d1bgyn_ 4.106.1.1.3 Core 2 subunit {Bovine (Bos taurus)}
pqdleftrlpnglviaslenyapasriglfikagsryensnnlgtshllrlasslttkga
ssfkitrgieavggklsvtstrenmaytveclrddvdilmefllnvttapefrrwevaal
qpqlridkavalqnpqahvienlhaaayrnalanslycpdyrigkvtpvelhdyvqnhft
sarmaliglgvshpvlkqvaeqflnirgglglsgakakyhggeireqngdslvhaalvae
saaigsaeanafsvlqhvlgagphvkrgsnatsslyqavakgvhqpfdvsafnasysdsg
lfgfytisqaasagdvikaaynqvktiaqgnlsnpdvqaaknklkagylmsvessegfld
evgsqalaagsytppstvlqqidavadadvinaakkfvsgrksmaasgnlghtpfidel
>d1bgyo1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
mtnirkshplmkivnnafidlpapsnisswwnfgsllgiclilqiltglflamhytsdtt
tafssvthicrdvnygwiirymhangasmfficlymhvgrglyygsytfletwnigvill
ltvmatafmgyvlpwgqmsfwgatvitnllsaipyigtnlvewiwggfsvdkatltrffa
fhfilpfiimaiamvhllflhetgsnnptgissdvdkipfhpyytikdilgalllilalm
llvlfapdllgdpdnytpanplntpphikpewyflfayailrsipnklggvlalafsili
lalipllhtskqrsmmfrplsqclfwalvadlltltwiggqpvehpyitigqlasvlyfl
lilvlmptagtienkllkw
>d1bgyp1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
sdlelhppsypwshrgllssldhtsirrgfqvykqvcsschsmdyvayrhlvgvcytede
akalaeevevqdgpnedgemfmrpgklsdyfpkpypnpeaaraanngalppdlsyivrar
hggedyvfslltgycepptgvslreglyfnpyfpgqaigmappiynevlefddgtpatms
qvakdvctflrwaaepehdhrkrmglkmllmmglllplvyamkrhkwsvlksrklayrpp
k
>d1bgyq1 2.29.1.1.1 (70-196) ISP subunit of the mitochondrial cytochrome bc1-complex {Bovine (Bos taurus)}
amskieiklsdipegknmafkwrgkplfvrhrtkkeidqeaavevsqlrdpqhdlervkk
pewviligvcthlgcvpianagdfggyycpchgshydasgrirkgpaplnlevpsyefts
ddmvivg
>d1bgyq2 6.2.1.1.9 (1-69) Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
shtdikvpdfsdyrrpevldstksskessearkgfsylvtatttvgvayaaknvvsqfvs
smsasadvl
>d1bgyr1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
avsassrwlegirkwyynaagfnklglmrddtihenddvkeairrlpenlyddrvfrikr
aldlsmrqqilpkeqwtkyeedksylepylkevirerkereewakk
>d1bgys1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
grqfghltrvrhvityslspfeqrafphyfskgipnvlrrtracilrvappfvafylvyt
wgtqefekskrknpaayendr
>d1bgyt1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
dplttvreqceqlekcvkarerlelcdervssrsqteedcteelldflhardhcvahklf
nslk
>d1bgyv1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
vaptltarlysllfrrtstfaltivvgalfferafdqgadaiyehinegklwkhikhkye
nk
>d1bgyw1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
rnwvptaqlwgavgavglvsat
>d1bh2_1 1.67.1.1.2 (61-181) Transducin (alpha subunit), insertion domain {Rat (Rattus rattus)}
yseeeckqykavvysntiqsiiaiiramgrlkidfgdaaraddarqlfvlagaaeegfmt
aelagvikrlwkdsgvqacfnrsreyqlndsaayylndldriaqpnyiptqqdvlrtrvk
t
>d1bh2_2 3.30.1.6.13 (32-60,182-346) Transducin (alpha subunit) {Rat (Rattus rattus)}
revkllllgagesgkstivkqmkiiheagXtgivethftfkdlhfkmfdvggqrserkkw
ihcfegvtaiifcvalsdydlvlaedeemnrmhesmklfdsicnnkwftdtsiilflnkk
dlfeekikksplticypeyagsntyeeaaayiqcqfedlnkrkdtkeiythftcstdtkn
vqfvfdavtdviikn
>d1bh3__ 6.4.3.1.3 Porin {Rhodopseudomonas blastica, strain DSM2131}
mislngygrfglqyvedrgvgledtiissrlrinivgttetdqgvtfgaklrmqwddgda
fagtagnaaqfwtsyngvtvsvgnvdtafdsvaltydsemgyeassfgdaqssffkynsk
ydasgaldnyngiavtysisgvnlylsyvdpdqtvdsslvteefgiaadwsndmislaaa
yttdaggivdndiafvgaaykfndagtvglnwydnglstagdqvtlygnyafgattvray
vsdidragadtaygigadyqfaegvkvsgsvqsgfanetvadvgvrfdf
>d1bh4__ 7.3.5.1.1 Circulin A {Chassalia parviflora}
cgescvwipcisaalgcscknkvcyrngip
>d1bh5a_ 4.27.1.1.1 Glyoxalase I {Human (Homo sapiens)}
sggltdeaalsccsdadpstkdfllqetmlrvkdpkksldfytrvlgmtliqkcdfpimk
fslyflayedkndipkekdekiawalsrkatlelthnwgteddetqsyhngnsdprgfgh
igiavpdvysackrfeelgvkfvkkpddgkmkglafiqdpdgywiqilnpnkmatlm
>d1bh5b_ 4.27.1.1.1 Glyoxalase I {Human (Homo sapiens)}
epqppsggltdeaalsccsdadpstkdfllqetmlrvkdpkksldfytrvlgmtliqkcd
fpimkfslyflayedkndipkekdekiawalsrkatlelthnwgteddetqsyhngnsdp
rgfghigiavpdvysackrfeelgvkfvkkpddgkmkglafiqdpdgywiqilnpnkmat
lm
>d1bh5c_ 4.27.1.1.1 Glyoxalase I {Human (Homo sapiens)}
sggltdeaalsccsdadpstkdfllqetmlrvkdpkksldfytrvlgmtliqkcdfpimk
fslyflayedkndipkekdekiawalsrkatlelthnwgteddetqsyhngnsdprgfgh
igiavpdvysackrfeelgvkfvkkpddgkmkglafiqdpdgywiqilnpnkmatlm
>d1bh5d_ 4.27.1.1.1 Glyoxalase I {Human (Homo sapiens)}
epqppsggltdeaalsccsdadpstkdfllqetmlrvkdpkksldfytrvlgmtliqkcd
fpimkfslyflayedkndipkekdekiawalsrkatlelthnwgteddetqsyhngnsdp
rgfghigiavpdvysackrfeelgvkfvkkpddgkmkglafiqdpdgywiqilnpnkmat
lm
>d1bh6a_ 3.33.1.1.2 Subtilisin Carlsberg {Bacillus licheniformis}
aqtvpygiplikadkvqaqgykganvkvgiidtgiasshtdlkvvggasfvsgesyntdg
nghgthvagtvaaldnttgvlgvapnvslyaikvlnssgsgsysaivsgiewatqngldv
inmslggpsgstalkqavdkayasgivvvaaagnsgnsgsqntigypakydsviavgavd
snknrasfssvgselevmapgvsvystypsntytslngtsmasphvagaaalilskyptl
sasqvrnrlsstatnlgdsfyygkglinveaaaq
>d1bh8a_ 1.23.1.3.3 TAF(II)18 {Human (Homo sapiens)}
lfskelrcmmygfgddqnpytesvdiledlviefitemthkamsi
>d1bh8b_ 1.23.1.3.4 TAF(II)28 {Human (Homo sapiens)}
fseeqlnryemyrrsafpkaaikrliqsitgtsvsqnvviamsgiskvfvgevveealdv
cekwgempplqpkhmreavrrlkskgqip
>d1bh9a_ 1.23.1.3.3 TAF(II)18 {Human (Homo sapiens)}
lfskelrcmmygfgddqnpytesvdiledlviefitemthkamsi
>d1bh9b_ 1.23.1.3.4 TAF(II)28 {Human (Homo sapiens)}
fseeqlnryemyrrsafpkaaikrliqsitgtsvsqnvviamsgiskvfvgevveealdv
cekwgempplqpkhmreavrrlkskgqip
>d1bhca_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bhcb_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bhcc_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bhcd_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bhce_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bhcf_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bhcg_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bhch_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bhci_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bhcj_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bhda_ 1.43.1.1.3 Utrophin {Human (Homo sapiens)}
lqqtnsekillswvrqttrpysqvnvlnfttswtdglafnavlhrhkpdlfswdkvvkms
pierlehafskaqtylgieklldpedvavrlpdkksiimyltslfevl
>d1bhdb_ 1.43.1.1.3 Utrophin {Human (Homo sapiens)}
nsekillswvrqttrpysqvnvlnfttswtdglafnavlhrhkpdlfswdkvvkmspier
lehafskaqtylgieklldpedvavrlpdkksiimyltslfevlpqqv
>d1bhe__ 2.71.1.5.1 Polygalacturonase {Erwinia carotovora}
sdsrtvsepktpsscttlkadsstatstiqkalnncdqgkavrlsagstsvflsgplslp
sgvsllidkgvtlravnnaksfenapsscgvvdkngkgcdafitavsttnsgiygpgtid
gqggvklqdkkvswwelaadakvkklkqntprliqinksknftlynvslinspnfhvvfs
dgdgftawkttiktpstarntdgidpmssknitiaysniatgddnvaikaykgraetrni
silhndfgtghgmsigsetmgvynvtvddlkmngttnglriksdksaagvvngvrysnvv
mknvakpividtvyekkegsnvpdwsditfkdvtsetkgvvvlngenakkpievtmknvk
ltsdstwqiknvnvkk
>d1bhfa_ 4.72.1.1.1 p56-lck tyrosine kinase {Human (Homo sapiens)}
lepepwffknlsrkdaerqllapgnthgsfliresestagsfslsvrdfdqnqgevvkhy
kirnldnggfyispritfpglhelvrhytnasdglctrlsrpcqt
>d1bhga1 2.1.4.1.2 (226-328) beta-Glucuronidase {Human (Homo sapiens)}
tyidditvttsveqdsglvnyqisvkgsnlfklevrlldaenkvvangtgtqgqlkvpgv
slwwpylmherpaylyslevqltaqtslgpvsdfytlpvgirt
>d1bhga2 2.16.1.4.2 (22-225) beta-Glucuronidase {Human (Homo sapiens)}
glqggmlypqespsreckeldglwsfradfsdnrrrgfeeqwyrrplwesgptvdmpvps
sfndisqdwrlrhfvgwvwyerevilperwtqdlrtrvvlrigsahsyaivwvngvdtle
heggylpfeadisnlvqvgplpsrlritiainntltpttlppgtiqyltdtskypkgyfv
qntyfdffnyaglqrsvllyttpt
>d1bhga3 3.1.7.3.13 (329-632) beta-Glucuronidase, domain 3 {Human (Homo sapiens)}
vavtksqflingkpfyfhgvnkhedadirgkgfdwpllvkdfnllrwlganafrtshypy
aeevmqmcdrygivvidecpgvglalpqffnnvslhhhmqvmeevvrrdknhpavvmwsv
anepashlesagyylkmviahtksldpsrpvtfvsnsnyaadkgapyvdviclnsyyswy
hdyghleliqlqlatqfenwykkyqkpiiqseygaetiagfhqdpplmfteeyqkslleq
yhlgldqkrrkyvvgeliwnfadfmteqsptrvlgnkkgiftrqrqpksaafllrerywk
iane
>d1bhgb1 2.1.4.1.2 (226-328) beta-Glucuronidase {Human (Homo sapiens)}
tyidditvttsveqdsglvnyqisvkgsnlfklevrlldaenkvvangtgtqgqlkvpgv
slwwpylmherpaylyslevqltaqtslgpvsdfytlpvgirt
>d1bhgb2 2.16.1.4.2 (22-225) beta-Glucuronidase {Human (Homo sapiens)}
glqggmlypqespsreckeldglwsfradfsdnrrrgfeeqwyrrplwesgptvdmpvps
sfndisqdwrlrhfvgwvwyerevilperwtqdlrtrvvlrigsahsyaivwvngvdtle
heggylpfeadisnlvqvgplpsrlritiainntltpttlppgtiqyltdtskypkgyfv
qntyfdffnyaglqrsvllyttpt
>d1bhgb3 3.1.7.3.13 (329-632) beta-Glucuronidase, domain 3 {Human (Homo sapiens)}
vavtksqflingkpfyfhgvnkhedadirgkgfdwpllvkdfnllrwlganafrtshypy
aeevmqmcdrygivvidecpgvglalpqffnnvslhhhmqvmeevvrrdknhpavvmwsv
anepashlesagyylkmviahtksldpsrpvtfvsnsnyaadkgapyvdviclnsyyswy
hdyghleliqlqlatqfenwykkyqkpiiqseygaetiagfhqdpplmfteeyqkslleq
yhlgldqkrrkyvvgeliwnfadfmteqsptrvlgnkkgiftrqrqpksaafllrerywk
iane
>d1bhha_ 4.72.1.1.1 p56-lck tyrosine kinase {Human (Homo sapiens)}
epepwffknlsrkdaerqllapgnthgsfliresestagsfslsvrdfdqnqgevvkhyk
irnldnggfyispritfpglhelvrhytnasdglctrlsrpcqt
>d1bhhb_ 4.72.1.1.1 p56-lck tyrosine kinase {Human (Homo sapiens)}
pepwffknlsrkdaerqllapgnthgsfliresestagsfslsvrdfdqnqgevvkhyki
rnldnggfyispritfpglhelvrhytnasdglctrlsrpcqt
>d1bhi__ 7.31.1.1.11 Transactivation domain of cre-bp1/atf-2 {Human (Homo sapiens)}
msddkpflctapgcgqrftnedhlavhkhkhemtlkfg
>d1bhja_ 3.56.1.2.1 Glycine <i>N</i>-methyltransferase {Rat (Rattus norvegicus)}
vdsvyrtrslgvaaegipdqyadgeaarvwqlyigdtrsrtaeykawllgllrqhgchrv
ldvacgtgvdsimlveegfsvtsvdasdkmlkyalkerwnrrkepafdkwvieeanwltl
dkdvpagdgfdaviclgnsfahlpdskgdqsehrlalkniasmvrpggllvidhrnydyi
lstgcappgkniyyksdltkdittsvltvnnkahmvtldytvqvpgagrdgapgfskfrl
syyphclasftelvqeafggrcqhsvlgdfkpyrpgqayvpcyfihvlkktg
>d1bhjb_ 3.56.1.2.1 Glycine <i>N</i>-methyltransferase {Rat (Rattus norvegicus)}
vdsvyrtrslgvaaegipdqyadgeaarvwqlyigdtrsrtaeykawllgllrqhgchrv
ldvacgtgvdsimlveegfsvtsvdasdkmlkyalkerwnrrkepafdkwvieeanwltl
dkdvpagdgfdaviclgnsfahlpdskgdqsehrlalkniasmvrpggllvidhrnydyi
lstgcappgkniyyksdltkdittsvltvnnkahmvtldytvqvpgagrdgapgfskfrl
syyphclasftelvqeafggrcqhsvlgdfkpyrpgqayvpcyfihvlkktg
>d1bhl__ 3.46.3.2.2 HIV-1 integrase, catalytic domain {Human immunodeficiency virus, type 1}
spgiwqldxthlegkvilvavhvasgyieaevipaetgqetayfllklagrwpvktvhtd
ngsnftsttvkaaxwwagikqefgipynpqsqgviesmnkelkkiigqvrdqaehlktav
qmavfihnhkrkggiggysagerivdiiatd
>d1bhma_ 3.43.1.3.1 Restriction endonuclease BamHI {Bacillus amyloliquefaciens}
mevekefitdeakellskdkliqqaynevktsicspiwpatsktftinntekncngvvpi
kelcytlledtynwyrekpldilklekkkggpidvykefienselkrvgmefetgnissa
hrsmnklllglkhgeidlaiilmpikqlayyltdrvtnfeelepyfeltegqpfifigfn
aeaynsnvplipkgsdgm
>d1bhmb_ 3.43.1.3.1 Restriction endonuclease BamHI {Bacillus amyloliquefaciens}
mevekefitdeakellskdkliqqaynevktsicspiwpatsktftinntekncngvvpi
kelcytlledtynwyrekpldilklekkkggpidvykefienselkrvgmefetgnissa
hrsmnklllglkhgeidlaiilmpikqlayyltdrvtnfeelepyfeltegqpfifigfn
aeaynsnvplipkgsdgmskrsikkwkd
>d1bhna_ 4.47.6.1.2 Nucleoside diphosphate kinases {Bovine (Bos taurus)}
ansertfiaikpdgvqrgligeiikrfeqkgfrlvamkfmrasedllkehyidlkdrpff
aglvkymhsgpvvamvweglnvvktgrvmlgetnpadskpgtirgdfciqvgrniihgsd
svesaekeialwfhpeelvnykscaqnwiye
>d1bhnb_ 4.47.6.1.2 Nucleoside diphosphate kinases {Bovine (Bos taurus)}
ansertfiaikpdgvqrgligeiikrfeqkgfrlvamkfmrasedllkehyidlkdrpff
aglvkymhsgpvvamvweglnvvktgrvmlgetnpadskpgtirgdfciqvgrniihgsd
svesaekeialwfhpeelvnykscaqnwiye
>d1bhnc_ 4.47.6.1.2 Nucleoside diphosphate kinases {Bovine (Bos taurus)}
ansertfiaikpdgvqrgligeiikrfeqkgfrlvamkfmrasedllkehyidlkdrpff
aglvkymhsgpvvamvweglnvvktgrvmlgetnpadskpgtirgdfciqvgrniihgsd
svesaekeialwfhpeelvnykscaqnwiye
>d1bhnd_ 4.47.6.1.2 Nucleoside diphosphate kinases {Bovine (Bos taurus)}
ansertfiaikpdgvqrgligeiikrfeqkgfrlvamkfmrasedllkehyidlkdrpff
aglvkymhsgpvvamvweglnvvktgrvmlgetnpadskpgtirgdfciqvgrniihgsd
svesaekeialwfhpeelvnykscaqnwiye
>d1bhne_ 4.47.6.1.2 Nucleoside diphosphate kinases {Bovine (Bos taurus)}
ansertfiaikpdgvqrgligeiikrfeqkgfrlvamkfmrasedllkehyidlkdrpff
aglvkymhsgpvvamvweglnvvktgrvmlgetnpadskpgtirgdfciqvgrniihgsd
svesaekeialwfhpeelvnykscaqnwiye
>d1bhnf_ 4.47.6.1.2 Nucleoside diphosphate kinases {Bovine (Bos taurus)}
ansertfiaikpdgvqrgligeiikrfeqkgfrlvamkfmrasedllkehyidlkdrpff
aglvkymhsgpvvamvweglnvvktgrvmlgetnpadskpgtirgdfciqvgrniihgsd
svesaekeialwfhpeelvnykscaqnwiye
>d1bho1_ 3.52.1.1.4 Integrin CR3 (CD11b/CD18, Mac-1), alpha subunit {Human (Homo sapiens)}
xsdiaflidgsgsiiphdfrrmkefvstvmeqlkksktlfslmqyseefrihftfkefqn
npnprslvkpitqllgrthtatgirkvvrelfnitngarknafkilvvitdgekfgdplg
yedvipeadregviryvigvgdafrseksrqelntiaskpprdhvfqvnnfealktiqnq
lrekifaieg
>d1bho2_ 3.52.1.1.4 Integrin CR3 (CD11b/CD18, Mac-1), alpha subunit {Human (Homo sapiens)}
xsdiaflidgsgsiiphdfrrmkefvstvmeqlkksktlfslmqyseefrihftfkefqn
npnprslvkpitqllgrthtatgirkvvrelfnitngarknafkilvvitdgekfgdplg
yedvipeadregviryvigvgdafrseksrqelntiaskpprdhvfqvnnfealktiqnq
lrekifaieg
>d1bhp__ 7.13.1.1.2 beta-Purothionin {Wheat (Triticum aestivum)}
kscckstlgrncynlcrargaqklcanvcrckltsglscpkdfpk
>d1bhq1_ 3.52.1.1.4 Integrin CR3 (CD11b/CD18, Mac-1), alpha subunit {Human (Homo sapiens)}
xsdiaflidgsgsiiphdfrrmkefvstvmeqlkksktlfslmqyseefrihftfkefqn
npnprslvkpitqllgrthtatgirkvvrelfnitngarknafkilvvitdgekfgdplg
yedvipeadregviryvigvgdafrseksrqelntiaskpprdhvfqvnnfealktiqnq
lrekifaieg
>d1bhq2_ 3.52.1.1.4 Integrin CR3 (CD11b/CD18, Mac-1), alpha subunit {Human (Homo sapiens)}
xsdiaflidgsgsiiphdfrrmkefvstvmeqlkksktlfslmqyseefrihftfkefqn
npnprslvkpitqllgrthtatgirkvvrelfnitngarknafkilvvitdgekfgdplg
yedvipeadregviryvigvgdafrseksrqelntiaskpprdhvfqvnnfealktiqnq
lrekifaieg
>d1bhs__ 3.2.1.2.8 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylahskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevf
>d1bhta1 7.10.1.1.1 (35-126) Hairpin loop containing domain of hepatocyte growth factor {Human (Homo sapiens)}
rrntihefkksakttlikidpalkiktkkvntadqcanrctrnkglpftckafvfdkark
qclwfpfnsmssgvkkefghefdlyenkdyir
>d1bhta2 7.14.1.1.9 (127-210) NK1 fragment of hepatocyte growth factor {Human (Homo sapiens)}
nciigkgrsykgtvsitksgikcqpwssmiphehsflpssyrgkdlqenycrnprgeegg
pwcftsnpevryevcdipqcseve
>d1bhtb1 7.10.1.1.1 (336-426) Hairpin loop containing domain of hepatocyte growth factor {Human (Homo sapiens)}
rntihefkksakttlikidpalkiktkkvntadqcanrctrnkglpftckafvfdkarkq
clwfpfnsmssgvkkefghefdlyenkdyir
>d1bhtb2 7.14.1.1.9 (427-509) NK1 fragment of hepatocyte growth factor {Human (Homo sapiens)}
nciigkgrsykgtvsitksgikcqpwssmiphehsflpssyrgkdlqenycrnprgeegg
pwcftsnpevryevcdipqcsev
>d1bhu__ 2.10.1.4.1 Streptomyces metalloproteinase inhibitor, SMPI {Streptomyces nigrescens}
apscpagslctysgtglsgartvipasdmekagtdgvklpasarsfangthftlrygpar
kvtcvrfpcyqyatvgkvapgaqlrslpspgatvtvgqdlgd
>d1bhwa_ 3.1.13.2.6 D-xylose isomerase {Actinoplanes missouriensis}
vqatredkfsfglwtvgwqardafgdatrtaldpveavhklaeigaygitfhdddlvpfg
sdaqtrdgiiagfkkaldetglivpmvttnlfthpvfkdggftsndrsvrryairkvlrq
mdlgaelgaktlvlwggregaeydsakdvsaaldryrealnllaqysedrgyglrfaiep
kpneprgdillptaghaiafvqelerpelfginpetgneqmsnlnftqgiaqalwhkklf
hidlngqhgpkfdqdlvfghgdllnafslvdllengpdgapaydgprhfdykpsrtedyd
gvwesakanirmylllkerakafradpevqealaaskvaelktptlnpgegyaelladrs
afedydadavgakgfgfvklnqlaiehllgar
>d1bhwb_ 3.1.13.2.6 D-xylose isomerase {Actinoplanes missouriensis}
vqatredkfsfglwtvgwqardafgdatrtaldpveavhklaeigaygitfhdddlvpfg
sdaqtrdgiiagfkkaldetglivpmvttnlfthpvfkdggftsndrsvrryairkvlrq
mdlgaelgaktlvlwggregaeydsakdvsaaldryrealnllaqysedrgyglrfaiep
kpneprgdillptaghaiafvqelerpelfginpetgneqmsnlnftqgiaqalwhkklf
hidlngqhgpkfdqdlvfghgdllnafslvdllengpdgapaydgprhfdykpsrtedyd
gvwesakanirmylllkerakafradpevqealaaskvaelktptlnpgegyaelladrs
afedydadavgakgfgfvklnqlaiehllgar
>d1bhwc_ 3.1.13.2.6 D-xylose isomerase {Actinoplanes missouriensis}
vqatredkfsfglwtvgwqardafgdatrtaldpveavhklaeigaygitfhdddlvpfg
sdaqtrdgiiagfkkaldetglivpmvttnlfthpvfkdggftsndrsvrryairkvlrq
mdlgaelgaktlvlwggregaeydsakdvsaaldryrealnllaqysedrgyglrfaiep
kpneprgdillptaghaiafvqelerpelfginpetgneqmsnlnftqgiaqalwhkklf
hidlngqhgpkfdqdlvfghgdllnafslvdllengpdgapaydgprhfdykpsrtedyd
gvwesakanirmylllkerakafradpevqealaaskvaelktptlnpgegyaelladrs
afedydadavgakgfgfvklnqlaiehllgar
>d1bhwd_ 3.1.13.2.6 D-xylose isomerase {Actinoplanes missouriensis}
vqatredkfsfglwtvgwqardafgdatrtaldpveavhklaeigaygitfhdddlvpfg
sdaqtrdgiiagfkkaldetglivpmvttnlfthpvfkdggftsndrsvrryairkvlrq
mdlgaelgaktlvlwggregaeydsakdvsaaldryrealnllaqysedrgyglrfaiep
kpneprgdillptaghaiafvqelerpelfginpetgneqmsnlnftqgiaqalwhkklf
hidlngqhgpkfdqdlvfghgdllnafslvdllengpdgapaydgprhfdykpsrtedyd
gvwesakanirmylllkerakafradpevqealaaskvaelktptlnpgegyaelladrs
afedydadavgakgfgfvklnqlaiehllgar
>e1bhx.1a 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
sgeadcglrplfekksledkterellesyi
>e1bhx.1b 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlket
>e1bhx.1f 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
gqpsvlqvvnlpiverpvckdstriritdnmfcagykpdegkrgdacegdsggpfvmksp
fnnrwyqmgivswgegcdrdgkygfythvfrlkkwiqkvidqfge
>d1bhy_1 3.3.1.5.10 (117-275,401-470) Dihydrolipoamide dehydrogenase {Neisseria meningitidis}
gsadaeydvvvlgggpggysaafaaadeglkvaiveryktlggvclnvgcipskallhna
avidevrhlaangikypepeldidmlraykdgvvsrltgglagmaksrkvdviqgdgqfl
dphhlevsltagdayeqaaptgekkivafknciiaagsrXapngklisaekagvavtdrg
fievdkqmrtnvphiyaigdivgqpmlahkavheghvaaencaghkayfd
>d1bhy_2 3.3.1.5.10 (276-400) Dihydrolipoamide dehydrogenase {Neisseria meningitidis}
vtklpfipedpriidssgalalkevpgklliigggiiglemgtvystlgsrldvvemmdg
lmqgadrdlvkvwqkqneyrfdnimvntktvavepkedgvyvtfeganapkepqrydavl
vaagr
>d1bhy_3 4.67.1.1.8 (471-598) Dihydrolipoamide dehydrogenase {Neisseria meningitidis}
arvipgvaytspevawvgetelsakasarkitkanfpwaasgraiangcdkpftklifda
etgriigggivgpnggdmigevylaiemgcdaadigktihphptlgesigmaaevalgtc
tdlppqkk
>d1bhz__ 4.2.1.2.1 Lysozyme {Chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1bi0_1 1.4.3.19.1 (4-64) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
lvdttemylrtiyeleeegvtplrariaerleqsgptvsqtvarmerdglvvvasdrslq
m
>d1bi0_2 1.75.1.1.1 (65-140) Diphtheria toxin repressor (DtxR) dimerization domain {Corynebacterium diphtheriae}
tptgrtlatavmrkhrlaerlltdiigldinkvhdeaxrwehvmsdeverrlvkvlkdvs
rspfgnpipgldelgv
>d1bi0_3 2.30.1.3.1 (148-226) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
pgtrvidaatsmprkvrivqineifqvetdqftqlldadirvgseveivdrdghitlshn
gkdvellddlahtirieel
>d1bi1_1 1.4.3.19.1 (4-64) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
lvdttemylrtiyeleeegvtplrariaerleqsgptvsqtvarmerdglvvvasdrslq
m
>d1bi1_2 1.75.1.1.1 (65-140) Diphtheria toxin repressor (DtxR) dimerization domain {Corynebacterium diphtheriae}
tptgrtlatavmrkhrlaerlltdiigldinkvhdeaxrwehvmsdeverrlvkvlkdvs
rspfgnpipgldelgv
>d1bi1_3 2.30.1.3.1 (148-225) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
pgtrvidaatsmprkvrivqineifqvetdqftqlldadirvgseveivdrdghitlshn
gkdvellddlahtiriee
>d1bi2a1 1.4.3.19.1 (3-64) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
dlvdttemylrtiyeleeegvtplrariaerleqsgptvsqtvarmerdglvvvasdrsl
qm
>d1bi2a2 1.75.1.1.1 (65-140) Diphtheria toxin repressor (DtxR) dimerization domain {Corynebacterium diphtheriae}
tptgrtlatavmrkhrlaerlltdiigldinkvhdeacrwehvmsdeverrlvkvlkdvs
rspfgnpipgldelgv
>d1bi2a3 2.30.1.3.1 (148-225) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
pgtrvidaatsmprkvrivqineifqvetdqftqlldadirvgseveivdrdghitlshn
gkdvellddlahtiriee
>d1bi2b1 1.4.3.19.1 (3-64) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
dlvdttemylrtiyeleeegvtplrariaerleqsgptvsqtvarmerdglvvvasdrsl
qm
>d1bi2b2 1.75.1.1.1 (65-140) Diphtheria toxin repressor (DtxR) dimerization domain {Corynebacterium diphtheriae}
tptgrtlatavmrkhrlaerlltdiigldinkvhdeacrwehvmsdeverrlvkvlkdvs
rspfgnpipgldelgv
>d1bi3a1 1.4.3.19.1 (4-64) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
lvdttemylrtiyeleeegvtplrariaerleqsgptvsqtvarmerdglvvvasdrslq
m
>d1bi3a2 1.75.1.1.1 (65-140) Diphtheria toxin repressor (DtxR) dimerization domain {Corynebacterium diphtheriae}
tptgrtlatavmrkhrlaerlltdiigldinkvhdeaxrwehvmsdeverrlvkvlkdvs
rspfgnpipgldelgv
>d1bi3a3 2.30.1.3.1 (148-225) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
pgtrvidaatsmprkvrivqineifqvetdqftqlldadirvgseveivdrdghitlshn
gkdvellddlahtiriee
>d1bi3b1 1.4.3.19.1 (4-64) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
lvdttemylrtiyeleeegvtplrariaerleqsgptvsqtvarmerdglvvvasdrslq
m
>d1bi3b2 1.75.1.1.1 (65-140) Diphtheria toxin repressor (DtxR) dimerization domain {Corynebacterium diphtheriae}
tptgrtlatavmrkhrlaerlltdiigldinkvhdeaxrwehvmsdeverrlvkvlkdvs
rspfgnpipgldelgv
>d1bi4a_ 3.46.3.2.2 HIV-1 integrase, catalytic domain {Human immunodeficiency virus, type 1}
spgiwqldcthlegkvilvavhvasgyieaevipaetgqetayfllklagrwpvktvhtd
ngsnftsttvkaacwwagikqefgipynpqsqgviesmnkelkkiigqvrdqaehlktav
qmavfihnhkrkggiggysagerivdiiatdi
>d1bi4b_ 3.46.3.2.2 HIV-1 integrase, catalytic domain {Human immunodeficiency virus, type 1}
spgiwqldcthlegkvilvavhvasgyieaevipaetgqetayfllklagrwpvktvhtd
ngsnftsttvkaacwwagikqefgipynpqsqgliesmnkelkkiigqvrdqaehlktav
qmavfihnhkrkggiggysagerivdiiatdiq
>d1bi4c_ 3.46.3.2.2 HIV-1 integrase, catalytic domain {Human immunodeficiency virus, type 1}
mhgqvdcspgiwqldcthlegkvilvavhvasgyieaevipaetgqetayfllklagrwp
vktvhtdngsnftsttvkaacwwagikqefgipynpqsqgviesmnkelkkiigqvrdqa
ehlktavqmavfihnhkrkggiggysagerivdiiatdiq
>d1bi5a_ 3.85.1.2.1 Chalcone synthase {Alfalfa (Medicago sativa)}
mvsvseirkaqraegpatilaigtanpancveqstypdfyfkitnsehktelkekfqrmc
dksmikrrymylteeilkenpnvceymapsldarqdmvvvevprlgkeaavkaikewgqp
kskithlivcttsgvdmpgadyqltkllglrpyvkrymmyqqgxfaggtvlrlakdlaen
nkgarvlvvcsevtavtfrgpsdthldslvgqalfgdgaaalivgsdpvpeiekpifemv
wtaqtiapdsegaidghlreagltfhllkdvpgivsknitkalveafeplgisdynsifw
iahpggpaildqveqklalkpekmnatrevlseygnmssacvlfildemrkkstqnglkt
tgeglewgvlfgfgpgltietvvlrsvai
>d1bi6h1 7.3.12.1.1 (8-31) Bromelain inhibitor VI (cysteine protease inhibitor) {Pineapple (Ananas comosus)}
tdtysdcpgfcktckaefgkyicl
>d1bi7a_ 4.117.1.1.1 Cyclin-dependent PK (different isozymes) {Human (Homo sapiens)}
dqqyecvaeigegaygkvfkardlknggrfvalkrvrvqtgeegmplstirevavlrhle
tfehpnvvrlfdvctvsrtdretkltlvfehvdqdlttyldkvpepgvptetikdmmfql
lrgldflhshrvvhrdlkpqnilvtssgqikladfglariysfqmaltsvvvtlwyrape
vllqssyatpvdlwsvgcifaemfrrkplfrgssdvdqlgkildviglpgeedwprdval
prqafhsksaqpiekfvtdidelgkdlllkcltfnpakrisaysalshpyfq
>d1bi7b_ 1.110.2.1.5 Cell cycle inhibitor p16ink4A {Human (Homo sapiens)}
epsadwlataaargrveevralleaganpnapnsygrrpiqvmmmgsarvaellllhgae
pncadpatltrpvhdaaregfldtlvvlhragarldvrdawgrlpvdlaeelghrdvary
lraaa
>d1bi8a_ 4.117.1.1.1 Cyclin-dependent PK (different isozymes) {Human (Homo sapiens)}
qqyecvaeigegaygkvfkardlknggrfvalkrvrvqtgeegmplstirevavlrhlet
fehpnvvrlfdvctvsrtdretkltlvfehvdqdlttyldkvpepgvptetikdmmfqll
rgldflhshrvvhrdlkpqnilvtssgqikladfglariysfqmaltsvvvtlwyrapev
llqssyatpvdlwsvgcifaemfrrkplfrgssdvdqlgkildviglpgeedwprdvalp
rqafhsksaqpiekfvtdidelgkdlllkcltfnpakrisaysalshpyfq
>d1bi8b_ 1.110.2.1.3 Cell cycle inhibitor p19ink4D {Human (Homo sapiens)}
vragdrlsgaaargdvqevrrllhrelvhpdalnrfgktalqvmmfgstaialellkqga
spnvqdtsgtspvhdaartgfldtlkvlvehgadvnvpdgtgalpihlavqeghtavvsf
laaesdlhrrdargltplelalqrgaqdlvdilqg
>d1bi8c_ 4.117.1.1.1 Cyclin-dependent PK (different isozymes) {Human (Homo sapiens)}
qqyecvaeigegaygkvfkardlknggrfvalkrvrvqtgeegmplstirevavlrhlet
fehpnvvrlfdvctvsrtdretkltlvfehvdqdlttyldkvpepgvptetikdmmfqll
rgldflhshrvvhrdlkpqnilvtssgqikladfglariysfqmaltsvvvtlwyrapev
llqssyatpvdlwsvgcifaemfrrkplfrgssdvdqlgkildviglpgeedwprdvalp
rqafhsksaqpiekfvtdidelgkdlllkcltfnpakrisaysalshpyfq
>d1bi8d_ 1.110.2.1.3 Cell cycle inhibitor p19ink4D {Human (Homo sapiens)}
vragdrlsgaaargdvqevrrllhrelvhpdalnrfgktalqvmmfgstaialellkqga
spnvqdtsgtspvhdaartgfldtlkvlvehgadvnvpdgtgalpihlavqeghtavvsf
laaesdlhrrdargltplelalqrgaqdlvdilqg
>d1bi9a_ 3.71.1.1.2 Aldehyde reductase (dehydrogenase), ALDH {Rat (Rattus norvegicus), retinal type II}
maslqllpsptpnleikytkifinnewqnsesgrvfpvcnpatgeqvcevqeadkvdidk
avqaarlafslgsvwrrmdasergrlldkladlverdratlatmeslnggkpflqafyid
lqgviktlryyagwadkihgmtipvdgdyftftrhepigvcgqiipwnfpllmftwkiap
alccgntvvikpaeqtplsalymgalikeagfppgvvnilpgygptagaaiashigidki
aftgstevgkliqeaagrsnlkrvtlelggkspniifadadldyaveqahqgvffnqgqc
ctagsrifveesiyeefvkrsverakrrivgspfdptteqgpqidkkqynkileliqsgv
aegaklecggkglgrkgffieptvfsnvtddmriakeeifgpvqeilrfktmdevieran
nsdfglvaavftndinkalmvssamqagtvwincynalnaqspfggfkmsgngremgefg
lreysevktvtvkipqkns
>d1bi9b_ 3.71.1.1.2 Aldehyde reductase (dehydrogenase), ALDH {Rat (Rattus norvegicus), retinal type II}
aslqllpsptpnleikytkifinnewqnsesgrvfpvcnpatgeqvcevqeadkvdidka
vqaarlafslgsvwrrmdasergrlldkladlverdratlatmeslnggkpflqafyidl
qgviktlryyagwadkihgmtipvdgdyftftrhepigvcgqiipwnfpllmftwkiapa
lccgntvvikpaeqtplsalymgalikeagfppgvvnilpgygptagaaiashigidkia
ftgstevgkliqeaagrsnlkrvtlelggkspniifadadldyaveqahqgvffnqgqcc
tagsrifveesiyeefvkrsverakrrivgspfdptteqgpqidkkqynkileliqsgva
egaklecggkglgrkgffieptvfsnvtddmriakeeifgpvqeilrfktmdevierann
sdfglvaavftndinkalmvssamqagtvwincynalnaqspfggfkmsgngremgefgl
reysevktvtvkipqkns
>d1bi9c_ 3.71.1.1.2 Aldehyde reductase (dehydrogenase), ALDH {Rat (Rattus norvegicus), retinal type II}
maslqllpsptpnleikytkifinnewqnsesgrvfpvcnpatgeqvcevqeadkvdidk
avqaarlafslgsvwrrmdasergrlldkladlverdratlatmeslnggkpflqafyid
lqgviktlryyagwadkihgmtipvdgdyftftrhepigvcgqiipwnfpllmftwkiap
alccgntvvikpaeqtplsalymgalikeagfppgvvnilpgygptagaaiashigidki
aftgstevgkliqeaagrsnlkrvtlelggkspniifadadldyaveqahqgvffnqgqc
ctagsrifveesiyeefvkrsverakrrivgspfdptteqgpqidkkqynkileliqsgv
aegaklecggkglgrkgffieptvfsnvtddmriakeeifgpvqeilrfktmdevieran
nsdfglvaavftndinkalmvssamqagtvwincynalnaqspfggfkmsgngremgefg
lreysevktvtvkipqkns
>d1bi9d_ 3.71.1.1.2 Aldehyde reductase (dehydrogenase), ALDH {Rat (Rattus norvegicus), retinal type II}
maslqllpsptpnleikytkifinnewqnsesgrvfpvcnpatgeqvcevqeadkvdidk
avqaarlafslgsvwrrmdasergrlldkladlverdratlatmeslnggkpflqafyid
lqgviktlryyagwadkihgmtipvdgdyftftrhepigvcgqiipwnfpllmftwkiap
alccgntvvikpaeqtplsalymgalikeagfppgvvnilpgygptagaaiashigidki
aftgstevgkliqeaagrsnlkrvtlelggkspniifadadldyaveqahqgvffnqgqc
ctagsrifveesiyeefvkrsverakrrivgspfdptteqgpqidkkqynkileliqsgv
aegaklecggkglgrkgffieptvfsnvtddmriakeeifgpvqeilrfktmdevieran
nsdfglvaavftndinkalmvssamqagtvwincynalnaqspfggfkmsgngremgefg
lreysevktvtvkipqkns
>d1bia_1 1.4.3.1.1 (1-63) Biotin repressor, N-terminal domain {Escherichia coli}
mkdntvplkliallangefhsgeqlgetlgmsraainkhiqtlrdwgvdvftvpgkgysl
pep
>d1bia_2 2.30.1.1.1 (271-317) Biotin repressor/biotin holoenzyme synthetase, C-terminal domain {Escherichia coli}
finrpvkliigdkeifgisrgidkqgallleqdgiikpwmggeislr
>d1bia_3 4.82.1.2.1 (64-270) Biotin repressor/biotin holoenzyme synthetase, catalytic (central) domain {Escherichia coli}
iqllnakqilgqldggsvavlpvidstnqylldrigelksgdaciaeyqqagrgrrgrkw
fspfganlylsmfwrleqgpaaaiglslvigivmaevlrklgadkvrvkwpndlylqdrk
lagilveltgktgdaaqivigaginmamrrveesvvnqgwitlqeaginldrntlaamli
relraalelfeqeglapylsrwekldn
>d1bib_1 1.4.3.1.1 (2-63) Biotin repressor, N-terminal domain {Escherichia coli}
kdntvplkliallangefhsgeqlgetlgmsraainkhiqtlrdwgvdvftvpgkgyslp
ep
>d1bib_2 2.30.1.1.1 (271-317) Biotin repressor/biotin holoenzyme synthetase, C-terminal domain {Escherichia coli}
finrpvkliigdkeifgisrgidkqgallleqdgiikpwmggeislr
>d1bib_3 4.82.1.2.1 (64-270) Biotin repressor/biotin holoenzyme synthetase, catalytic (central) domain {Escherichia coli}
iqllnakqilgqldggsvavlpvidstnqylldrigelksgdaciaeyqqagrgrrgrkw
fspfganlylsmfwrleqgpaaaiglslvigivmaevlrklgadkvrvkwpndlylqdrk
lagilveltgktgdaaqivigaginmamrrveesvvnqgwitlqeaginldrntlaamli
relraalelfeqeglapylsrwekldn
>d1bic__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnn
ghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvh
wntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprg
llpesldywtypgslthppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvd
nwrpaqplknrqikasfk
>d1bid__ 4.91.1.1.1 Thymidylate synthase {Escherichia coli}
mkqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihell
wflqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlk
ndpdsrriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfnias
yallvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesif
dyrfedfeiegydphpgikapvai
>d1bif_1 3.30.1.5.1 (37-249) 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, kinase domain {Rat (Rattus norvegicus)}
cptlivmvglpargktyiskkltrylnfigvptrefnvgqyrrdmvktyksfefflpdne
eglkirkqcalaalndvrkflseegghvavfdatnttrerramifnfgeqngyktffves
icvdpeviaanivqvklgspdyvnrdsdeatedfmrriecyensyesldeeqdrdlsyik
imdvgqsyvvnrvadhiqsrivyylmnihvtpr
>d1bif_2 3.50.1.4.1 (250-468) 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, phosphatase domain {Rat (Rattus norvegicus)}
siylcrhgeselnlkgriggdpglsprgrefskhlaqfisdqnikdlkvftsqmkrtiqt
aealsvpyeqfkvlneidagvceemtyeeiqdhyplefalrdqdkyryrypkgesyedlv
qrlepvimelerqenvlvichqavmrcllayfldkaaeelpylkcplhtvlkltpvaygc
kvesiflnvaavnthrdrpqnvdisrpseealvtvpahq
>d1big__ 7.3.7.2.1 Bmtx1 {Buthus martensii karsch}
ftdvkctgskqcwpvckqmfgkpngkcmngkcrcys
>d1biha1 2.1.1.4.11 (5-98) Hemolin {Moth (Hyalophora cecropia)}
kypvlkdqpaevlfrennptvleciiegndqgvkyswkkdgksynwqehnaalrkdegsl
vflrpqasdeghyqcfaetpagvassrvisfrkt
>d1biha2 2.1.1.4.11 (99-209) Hemolin {Moth (Hyalophora cecropia)}
yliaspakthektpiegrpfqldcvlpnaypkplitwkkrlsgadpnadvtdfdrritag
pdgnlyftivtkedvsdiykyvctaknaavdeevvlveyeikgvtkdnsgy
>d1biha3 2.1.1.4.11 (210-306) Hemolin {Moth (Hyalophora cecropia)}
kgepvpqyvskdmmakagdvtmiycmygsnpmgypnyfkngkdvngnpedritrhnrtsg
krllfkttlpedegvytcevdngvgkpqkhslkltvv
>d1biha4 2.1.1.4.11 (307-395) Hemolin {Moth (Hyalophora cecropia)}
sapkyeqkpekvivvkqgqdvtipckvtglpapnvvwshnakplsggratvtdsglvikg
vkngdkgyygcratnehgdkyfetlvqvn
>d1bihb1 2.1.1.4.11 (5-98) Hemolin {Moth (Hyalophora cecropia)}
kypvlkdqpaevlfrennptvleciiegndqgvkyswkkdgksynwqehnaalrkdegsl
vflrpqasdeghyqcfaetpagvassrvisfrkt
>d1bihb2 2.1.1.4.11 (99-209) Hemolin {Moth (Hyalophora cecropia)}
yliaspakthektpiegrpfqldcvlpnaypkplitwkkrlsgadpnadvtdfdrritag
pdgnlyftivtkedvsdiykyvctaknaavdeevvlveyeikgvtkdnsgy
>d1bihb3 2.1.1.4.11 (210-306) Hemolin {Moth (Hyalophora cecropia)}
kgepvpqyvskdmmakagdvtmiycmygsnpmgypnyfkngkdvngnpedritrhnrtsg
krllfkttlpedegvytcevdngvgkpqkhslkltvv
>d1bihb4 2.1.1.4.11 (307-395) Hemolin {Moth (Hyalophora cecropia)}
sapkyeqkpekvivvkqgqdvtipckvtglpapnvvwshnakplsggratvtdsglvikg
vkngdkgyygcratnehgdkyfetlvqvn
>d1biia1 2.1.1.2.17 (182-274) Class I MHC, beta2-microglobulin and alpha-3 domain {Mouse (Mus musculus), H-2DD}
tdppkahvthhrrpegdvtlrcwalgfypaditltwqlngeeltqemelvetrpagdgtf
qkwasvvvplgkeqkytchveheglpepltlrw
>d1biia2 4.17.1.1.24 (1-181) MHC class I, alpha-1 and alpha-2 domains {Mouse (Mus musculus), H-2DD}
gshslryfvtavsrpgfgeprymevgyvdntefvrfdsdaenpryeprarwieqegpeyw
eretrrakgneqsfrvdlrtalryynqsaggshtlqwmagcdvesdgrllrgywqfaydg
cdyialnedlktwtaadmaaqitrrkweqagaaerdraylegecvewlrrylkngnatll
r
>d1biib1 2.1.1.2.17 Class I MHC, beta2-microglobulin and alpha-3 domain {Mouse (Mus musculus), H-2DD}
iqktpqiqvysrhppengkpnilncyvtqfhpphieiqmlkngkkipkvemsdmsfskdw
sfyilahteftptetdtyacrvkhdsmaepktvywdrdm
>d1bija_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1bijb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1bijc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1bijd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1bik_1 7.8.1.1.5 (25-78) Bikunin from inter-alpha-inhibitor complex {Human (Homo sapiens)}
scqlgysagpcmgmtsryfyngtsmacetfqyggcmgngnnfvtekeclqtcrt
>d1bik_2 7.8.1.1.5 (79-134) Bikunin from inter-alpha-inhibitor complex {Human (Homo sapiens)}
vaacnlpivrgpcrafiqlwafdavkgkcvlfpyggcqgngnkfysekecreycgv
>d1bila_ 2.44.1.2.16 Chymosin (synonim: renin) {Human (Homo sapiens)}
gnttssviltnymdtqyygeigigtppqtfkvvfdtgssnvwvpsskcsrlytacvyhkl
fdasdsssykhngteltlrystgtvsgflsqdiitvggitvtqmfgevtempalpfmlae
fdgvvgmgfieqaigrvtpifdniisqgvlkedvfsfyynrdsensqslggqivlggsdp
qhyegnfhyinliktgvwqiqmkgvsvgsstllcedgclalvdtgasyisgstssieklm
ealgakkrlfdyvvkcnegptlpdisfhlggkeytltsadyvfqesysskklctlaiham
dippptgptwalgatfirkfytefdrrnnrigfalar
>d1bilb_ 2.44.1.2.16 Chymosin (synonim: renin) {Human (Homo sapiens)}
gnttssviltnymdtqyygeigigtppqtfkvvfdtgssnvwvpsskcsrlytacvyhkl
fdasdsssykhngteltlrystgtvsgflsqdiitvggitvtqmfgevtempalpfmlae
fdgvvgmgfieqaigrvtpifdniisqgvlkedvfsfyynrdsensqslggqivlggsdp
qhyegnfhyinliktgvwqiqmkgvsvgsstllcedgclalvdtgasyisgstssieklm
ealgakkrlfdyvvkcnegptlpdisfhlggkeytltsadyvfqesysskklctlaiham
dippptgptwalgatfirkfytefdrrnnrigfalar
>d1bima_ 2.44.1.2.16 Chymosin (synonim: renin) {Human (Homo sapiens)}
gnttssviltnymdtqyygeigigtppqtfkvvfdtgssnvwvpsskcsrlytacvyhkl
fdasdsssykhngteltlrystgtvsgflsqdiitvggitvtqmfgevtempalpfmlae
fdgvvgmgfieqaigrvtpifdniisqgvlkedvfsfyynrdsensqslggqivlggsdp
qhyegnfhyinliktgvwqiqmkgvsvgsstllcedgclalvdtgasyisgstssieklm
ealgakkrlfdyvvkcnegptlpdisfhlggkeytltsadyvfqesysskklctlaiham
dippptgptwalgatfirkfytefdrrnnrigfalar
>d1bimb_ 2.44.1.2.16 Chymosin (synonim: renin) {Human (Homo sapiens)}
gnttssviltnymdtqyygeigigtppqtfkvvfdtgssnvwvpsskcsrlytacvyhkl
fdasdsssykhngteltlrystgtvsgflsqdiitvggitvtqmfgevtempalpfmlae
fdgvvgmgfieqaigrvtpifdniisqgvlkedvfsfyynrdsensqslggqivlggsdp
qhyegnfhyinliktgvwqiqmkgvsvgsstllcedgclalvdtgasyisgstssieklm
ealgakkrlfdyvvkcnegptlpdisfhlggkeytltsadyvfqesysskklctlaiham
dippptgptwalgatfirkfytefdrrnnrigfalar
>d1bina_ 1.1.1.1.15 Leghemoglobin {Soybean (Glycine max), isoform A}
vaftekqdalvsssfeafkanipqysvvfytsilekapaakdlfsflangvdptnpkltg
haeklfalvrdsagqlkasgtvvadaalgsvhaqkavtdpqfvvvkeallktikaavgdk
wsdelsrawevaydelaaaikka
>d1binb_ 1.1.1.1.15 Leghemoglobin {Soybean (Glycine max), isoform A}
vaftekqdalvsssfeafkanipqysvvfytsilekapaakdlfsflangvdptnpkltg
haeklfalvrdsagqlkasgtvvadaalgsvhaqkavtdpqfvvvkeallktikaavgdk
wsdelsrawevaydelaaaikka
>d1bio__ 2.41.1.2.27 Factor D {Human (Homo sapiens)}
ilggreaeaharpymasvqlngahlcggvlvaeqwvlsaahcledaadgkvqvllgahsl
sqpepskrlydvlravphpdsqpdtidhdllllqlsekatlgpavrplpwqrvdrdvapg
tlcdvagwgivnhagrrpdslqhvllpvldratcnrrthhdgaiterlmcaesnrrdsck
gdsggplvcggvlegvvtsgsrvcgnrkkpgiytrvasyaawidsvla
>d1bip__ 1.54.1.2.2 Trypsin/alpha-amylase inhibitor RBI {Ragi (Elucine coracana gaertneri), seeds}
svgtscipgmaiphnpldscrwyvstrtcgvgprlatqemkarccrqleaipaycrceav
rilmdgvvtssgqhegrllqdlpgcprqvqrafapklvtevecnlatihggpfclsllga
ge
>d1biqa_ 1.26.1.2.3 Ribonucleotide reductase R2 {Escherichia coli}
ayttfsqtkndqlkepmffgqpvnvarydqqkydifekliekqlsffwrpeevdvsrdri
dyqalpehekhifisnlkyqtlldsiqgrspnvallplisipeletwvetwafsetihsr
sfthiirnivndpsvvfddivtneqiqkraegissyydeliemtsywhllgegthtvngk
tvtvslrelkkklylclmsvnaleairxyvsfacsfafaerelmegnakiirliardaal
hltgtqhmlnllrsgaddpemaeiaeeckqecydlfvqaaqqekdwadylfrdgsmigln
kdilcqyveyitnirmqavgldlpfqtrsnpipwintwlv
>d1biqb_ 1.26.1.2.3 Ribonucleotide reductase R2 {Escherichia coli}
ayttfsqtkndqlkepmffgqpvnvarydqqkydifekliekqlsffwrpeevdvsrdri
dyqalpehekhifisnlkyqtlldsiqgrspnvallplisipeletwvetwafsetihsr
sfthiirnivndpsvvfddivtneqiqkraegissyydeliemtsywhllgegthtvngk
tvtvslrelkkklylclmsvnaleairfyvsfacsfafaerelmegnakiirliardaal
hltgtqhmlnllrsgaddpemaeiaeeckqecydlfvqaaqqekdwadylfrdgsmigln
kdilcqyveyitnirmqavgldlpfqtrsnpipwintwlvs
>d1bira_ 4.1.1.1.3 RNase T1 {Aspergillus oryzae}
acdytcgsncysssdvstaqaagyklhedgetvgsnsyphkynnyegfdfsvsspyyewp
ilssgdvysggspgadrvvfnennqlagvithtgasgnnavect
>d1birb_ 4.1.1.1.3 RNase T1 {Aspergillus oryzae}
acdytcgsncysssdvstaqaagyklhedgetvgsnsyphkynnyegfdfsvsspyyewp
ilssgdvysggspgadrvvfnennqlagvithtgasgnnavect
>d1bisa_ 3.46.3.2.2 HIV-1 integrase, catalytic domain {Human immunodeficiency virus, type 1}
cspgiwqldcthlegkvilvavhvasgyieaevipaetgqetayfllklagrwpvktvht
dngsnftsttvkaacewagikqefgipynpqsqgviesmnkelkkiigqvrdqaehlkta
vqmavfihnkkrkggiggysagerivdiiatdiq
>d1bisb_ 3.46.3.2.2 HIV-1 integrase, catalytic domain {Human immunodeficiency virus, type 1}
cspgiwqldcthlegkvilvavhvasgyieaevipaetgqetayfllklagrwpvktvht
dngsnftsttvkaacewagikqefgipynpqsqgviesmnkelkkiigqvrdqaehlkta
vqmavfihnkkrkggiggysagerivdiiatdiq
>d1bit__ 2.41.1.2.5 Trypsin(ogen) {North atlantic salmon (Salmo salar)}
ivggyeckaysqahqvslnsgyhfcggslvnenwvvsaahcyksrvevrlgehnikvteg
seqfisssrvirhpnyssynidndimliklskpatlntyvqpvalptscapagtmctvsg
wgntmsstadsnklqclnipilsysdcnnsypgmitnamfcagyleggkdscqgdsggpv
vcngelqgvvswgygcaepgnpgvyakvcifndwltstmasy
>d1biua_ 3.46.3.2.2 HIV-1 integrase, catalytic domain {Human immunodeficiency virus, type 1}
cspgiwqldcthlegkvilvavhvasgyieaevipaetgqetayfllklagrwpvktvht
dngsnftsttvkaacewggikqefgipynpqsqgviesmnkelkkiigqvrdqaehlkta
vqmavfihnkkrkggiggysagerivdiiatdiq
>d1biub_ 3.46.3.2.2 HIV-1 integrase, catalytic domain {Human immunodeficiency virus, type 1}
cspgiwqldcthlegkvilvavhvasgyieaevipaetgqetayfllklagrwpvktvht
dngsnftsttvkaacewggikqefgipynpqsqgviesmnkelkkiigqvrdqaehlkta
vqmavfihnkkrkggiggysagerivdiiatdiq
>d1biuc_ 3.46.3.2.2 HIV-1 integrase, catalytic domain {Human immunodeficiency virus, type 1}
cspgiwqldcthlegkvilvavhvasgyieaevipaetgqetayfllklagrwpvktvht
dngsnftsttvkaacewggikqefgipynpqsqgviesmnkelkkiigqvrdqaehlkta
vqmavfihnkkrkggiggysagerivdiiatdiq
>d1biwa_ 4.71.1.9.4 Stromelysin-1 (MMP-3) {Human (Homo sapiens), fibroblast}
frtfpgipkwrkthltyrivnytpdlpkdavdsavekalkvweevtpltfsrlyegeadi
misfavrehgdfypfdgpgnvlahayapgpgingdahfdddeqwtkdttgtnlflvaahe
ighslglfhsantealmyplyhsltdltrfrlsqddingiqslygpppd
>d1biwb_ 4.71.1.9.4 Stromelysin-1 (MMP-3) {Human (Homo sapiens), fibroblast}
frtfpgipkwrkthltyrivnytpdlpkdavdsavekalkvweevtpltfsrlyegeadi
misfavrehgdfypfdgpgnvlahayapgpgingdahfdddeqwtkdttgtnlflvaahe
ighslglfhsantealmyplyhsltdltrfrlsqddingiqslygpppdspet
>d1bix__ 4.122.1.1.2 DNA repair endonuclease Hap1 {Human (Homo sapiens)}
lyedppdqktspsgkpatlkicswnvdglrawikkkgldwvkeeapdilclqetkcsenk
lpaelqelpglshqywsapsdkegysgvgllsrqcplkvsygigdeehdqegrvivaefd
sfvlvtayvpnagrglvrleyrqrwdeafrkflkglasrkplvlcgdlnvaheeidlrnp
kgnkknagftpqerqgfgellqavpladsfrhlypntpyaytfwtymmnarsknvgwrld
yfllshsllpalcdskirskalgsdhcpitlylal
>d1biy_1 3.84.1.2.3 (1-333) Lactoferrin {Domestic water buffalo (Bubalus arnee bubalis)}
aprknvrwctisqpewlkchrwqwrmkklgapsitcvrrafvleciraitekkadavtld
ggmvfeagldpyklrpvaaeiygtkespqthyyavavvkkgsnfqldqlqgrnschtglg
rsagwnipmgilrpylswtesleplqgavakffsascvpcvdrqaypnlcqlckgegenq
cacsprepyfgysgafkclqdgagdvafvkettvfenlpekadrdqyellclnntrapvd
afkechlaqvpshavvarsvdgkedliwkllskaqekfgknksgsfqlfgsppgqrdllf
kdsalgflripskvdsalylgsryltalknlre
>d1biy_2 3.84.1.2.3 (334-689) Lactoferrin {Domestic water buffalo (Bubalus arnee bubalis)}
taeevqarrarvvwcavgpeeqkkcqqwsqqsgqivtcatasttddcialvlkgeadals
ldggyiytagkcglvpvlaenrksskhssldcvlrptegylavavvkkanegltwnslkg
kkschtavdrtagwnipmglianqtgscafdeffsqscapgadpksrlcalcagddqgld
kcvpnskekyygytgafrclaedvgdvafvkndtvwentngestadwaknlnredfrllc
ldgtrkpvteaqschlavapnhavvslseraahveqvllhqqalfgengkncpdkfclfk
setknllfndnteclaklggrptyeeylgteyvtaianlkkcstsplleacafltr
>d1biza_ 3.46.3.2.2 HIV-1 integrase, catalytic domain {Human immunodeficiency virus, type 1}
vdsspgiwqldcthlegkvilvavhvasgyieaevipaetgqetayfllklagrwpvktv
htdngsnftsttvkaacwwagikqefgipynpqsqgviesmnkelkkiigqvrdqaehlk
tavqmavfihnkkrkggiggysagerivdiiatdi
>d1bizb_ 3.46.3.2.2 HIV-1 integrase, catalytic domain {Human immunodeficiency virus, type 1}
pgiwqldcthlegkvilvavhvasgyieaevipaetgqetayfllklagrwpvktvhtdn
gsnftsttvkaacwwagikqefgipynpqsqgviesmnkelkkiigqvrdqaehlktavq
mavfihnkkrkggiggysagerivdiiatdiqtke
>d1bj0_1 1.37.1.1.1 (2-67) Tetracyclin repressor (Tet-repressor, TetR), N-terminal domain {Escherichia coli}
srlnresvidaalellnetgidglttrklaqklgieqptlywhvknkralldalaveila
rhhdys
>d1bj0_2 1.113.1.1.1 (68-208) Tetracyclin repressor (Tet-repressor, TetR), C-terminal domain {Escherichia coli}
lpaageswqsflrnnamsfrrallryrdgakvhlgtrpdekqydtvetqlrfmtengfsl
rdglyaisavshftlgavleqqehtaaltdrpaapdenlppllrealqimdsddgeqafl
hgleslirgfevqltallqiv
>d1bj1h1 2.1.1.1.124 (1-123) Immunoglobulin (variable domains of L and H chains) {VEGF neutralizing Fab-12 (mouse), kappa L chain}
evqlvesggglvqpggslrlscaasgytftnygmnwvrqapgkglewvgwintytgepty
aadfkrrftfsldtskstaylqmnslraedtavyycakyphyygsshwyfdvwgqgtlvt
vss
>d1bj1h2 2.1.1.2.122 (124-224) Immunoglobulin (constant domains of L and H chains) {VEGF neutralizing Fab-12 (mouse), kappa L chain}
astkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkvepk
>d1bj1j1 2.1.1.1.124 (1-107) Immunoglobulin (variable domains of L and H chains) {VEGF neutralizing Fab-12 (mouse), kappa L chain}
diqmtqspsslsasvgdrvtitcsasqdisnylnwyqqkpgkapkvliyftsslhsgvps
rfsgsgsgtdftltisslqpedfatyycqqystvpwtfgqgtkveik
>d1bj1j2 2.1.1.2.122 (108-213) Immunoglobulin (constant domains of L and H chains) {VEGF neutralizing Fab-12 (mouse), kappa L chain}
rtvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqd
skdstyslsstltlskadyekhkvyacevthqglsspvtksfnrge
>d1bj1k1 2.1.1.1.124 (1-123) Immunoglobulin (variable domains of L and H chains) {VEGF neutralizing Fab-12 (mouse), kappa L chain}
evqlvesggglvqpggslrlscaasgytftnygmnwvrqapgkglewvgwintytgepty
aadfkrrftfsldtskstaylqmnslraedtavyycakyphyygsshwyfdvwgqgtlvt
vss
>d1bj1k2 2.1.1.2.122 (124-224) Immunoglobulin (constant domains of L and H chains) {VEGF neutralizing Fab-12 (mouse), kappa L chain}
astkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkvepk
>d1bj1l1 2.1.1.1.124 (1-107) Immunoglobulin (variable domains of L and H chains) {VEGF neutralizing Fab-12 (mouse), kappa L chain}
diqmtqspsslsasvgdrvtitcsasqdisnylnwyqqkpgkapkvliyftsslhsgvps
rfsgsgsgtdftltisslqpedfatyycqqystvpwtfgqgtkveik
>d1bj1l2 2.1.1.2.122 (108-213) Immunoglobulin (constant domains of L and H chains) {VEGF neutralizing Fab-12 (mouse), kappa L chain}
rtvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqd
skdstyslsstltlskadyekhkvyacevthqglsspvtksfnrge
>d1bj1v_ 7.17.1.1.2 Vascular endothelial growth factor {Human (Homo sapiens)}
vvkfmdvyqrsychpietlvdifqeypdeieyifkpscvplmrcggccndeglecvptee
snitmqimrikphqgqhigemsflqhnkcecrpk
>d1bj1w_ 7.17.1.1.2 Vascular endothelial growth factor {Human (Homo sapiens)}
vvkfmdvyqrsychpietlvdifqeypdeieyifkpscvplmrcggccndeglecvptee
snitmqimrikphqgqhigemsflqhnkcecrpk
>d1bj3a_ 4.139.1.1.3 Coagulation factors IX/X-binding protein (IX/X-BP) {Habu snake (Trimeresurus flavoviridis)}
dcpsgwssyeghcykpfklyktwddaerfcteqakgghlvsiesageadfvaqlvteniq
ntksyvwiglrvqgkekqcssewsdgssvsyenwieaesktclgleketgfrkwvniycg
qqnpfvcea
>d1bj3b_ 4.139.1.1.3 Coagulation factors IX/X-binding protein (IX/X-BP) {Habu snake (Trimeresurus flavoviridis)}
dcpsdwssyeghcykpfsepknwadaenfctqqhagghlvsfqsseeadfvvklafqtfg
hsifwmglsnvwnqcnwqwsnaamlrykawaeesycvyfkstnnkwrsracrmmaqfvce
fqa
>d1bj4a_ 3.57.1.4.7 Serine hydroxymethyltransferase {Human (Homo sapiens)}
dadlwsshdamlaqplkdsdvevyniikkesnrqrvgleliasenfasravlealgscln
nkysegypgqryyggtefideletlcqkralqaykldpqcwgvnvqpysgspanfavyta
lvephgrimgldlpdgghlthgfmtdkkkisatsiffesmpykvnpdtgyinydqleena
rlfhpkliiagtscysrnleyarlrkiadengaylmadmahisglvaagvvpspfehchv
vtttthktlrgcragmifyrkgvksvdpatgkeilynleslinsavfpglqggphnhaia
gvavalkqamtlefkvyqhqvvancralsealtelgykivtggsdnhlilvdlrskgtdg
graekvleacsiacnkntcpgdrsalrpsglrlgtpaltsrgllekdfqkvahfihrgie
ltlqiqsdtgvaatlkefkerlagdkyqaavqalreevesfaslfplpgl
>d1bj5_1 1.116.1.1.1 (3-196) Serum albumin {Human (Homo sapiens)}
hksevahrfkdlgeenfkalvliafaqylqqcpfedhvklvnevtefaktcvadesaenc
dkslhtlfgdklctvatlretygemadccakqepernecflqhkddnpnlprlvrpevdv
mctafhdneetflkkylyeiarrhpyfyapellffakrykaafteccqaadkaacllpkl
delrdegkassakq
>d1bj5_2 1.116.1.1.1 (197-388) Serum albumin {Human (Homo sapiens)}
rlkcaslqkfgerafkawavarlsqrfpkaefaevsklvtdltkvhtecchgdllecadd
radlakyicenqdsissklkeccekpllekshciaevendempadlpslaadfveskdvc
knyaeakdvflgmflyeyarrhpdysvvlllrlaktyettlekccaaadphecyakvfde
fkplveepqnli
>d1bj5_3 1.116.1.1.1 (389-584) Serum albumin {Human (Homo sapiens)}
kqncelfeqlgeykfqnallvrytkkvpqvstptlvevsrnlgkvgskcckhpeakrmpc
aedylsvvlnqlcvlhektpvsdrvtkccteslvnrrpcfsalevdetyvpkefnaetft
fhadictlsekerqikkqtalvelvkhkpkatkeqlkavmddfaafvekcckaddketcf
aeegkklvaasqaalg
>d1bj6a_ 7.34.1.1.2 HIV nucleocapsid {Human immunodeficiency virus, type 1, Mn isolate}
nvkcfncgkeghtarncraprkkgcwkcgkeghqmkdcterq
>d1bj7__ 2.53.1.1.7 Lipocalin allergen {Bovine (Bos taurus), bos d 2}
idpskipgewriiyaaadnkdkiveggplrnyyrriecindceslsitfylkdqgtclll
tevakrqegyvyvlefygtntlevihvsenmlvtyvenydgeritkmteglakgtsftpe
elekyqqlnsergvpnenienliktdncpp
>d1bj8__ 2.1.2.1.13 Cytokyne receptor gp130 cytokine-binding domains {Human (Homo sapiens)}
mdkvkpnpphnlsvinseelssilkltwtnpsiksviilkyniqyrtkdastwsqipped
tastrssftvqdlkpfteyvfrircmkedgkgywsdwseeasgityedr
>d1bj9__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpwgaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1bjaa_ 1.4.3.8.1 Transcription factor MotA, activation domain {Bacteriophage T4}
skvtyiikasndvlnektatilitiakkdfitaaevrevhpdlgnavvnsnigvlikkgl
veksgdgliitgeaqdiisnaatlyaqenapellk
>d1bjab_ 1.4.3.8.1 Transcription factor MotA, activation domain {Bacteriophage T4}
skvtyiikasndvlnektatilitiakkdfitaaevrevhpdlgnavvnsnigvlikkgl
veksgdgliitgeaqdiisnaatlyaqenapellk
>d1bje__ 1.1.1.1.8 Myoglobin {Horse (Equus caballus)}
glsdgewqqvlnvwgkveadiaghgqevlirlftghpetlekfdkfkhlkteaemkased
lkktgtvvltalggilkkkghheaelkplaqshatkhkipikylefisdaiihvlhskhp
gdfgadaqgamtkalelfrndiaakykelgfqg
>d1bjfa_ 1.42.1.5.23 Neurocalcin {Bovine (Bos taurus)}
nsklrpevmqdllestdfteheiqewykgflrdcpsghlsmeefkkiygnffpygdaskf
aehvfrtfdangdgtidfrefiialsvtsrgkleqklkwafsmydldgngyiskaemlei
vqaiykmvssvmkmpedestpekrtekifrqmdtnrdgklsleefirgaksdpsivrllq
c
>d1bjfb_ 1.42.1.5.23 Neurocalcin {Bovine (Bos taurus)}
nsklrpevmqdllestdfteheiqewykgflrdcpsghlsmeefkkiygnffpygdaskf
aehvfrtfdangdgtidfrefiialsvtsrgkleqklkwafsmydldgngyiskaemlei
vqaiykmvssvmkmpedestpekrtekifrqmdtnrdgklsleefirgaksdpsivrllq
c
>d1bjg__ 4.91.1.1.1 Thymidylate synthase {Escherichia coli}
kqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihellw
flqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlkn
dpdsrriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscnvflglpfniasy
allvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesifd
yrfedfeiegydphpgikapvai
>d1bji__ 2.59.1.1.2 Influenza neuraminidase {Influenza virus A, different strains}
rdfnnltkglctinswhiygkdnavrigedsdvlvtrepyvscdpdecrfyalsqgttir
gkhsngtihdrsqyraliswplsspptvynsrvecigwsstschdgktrmsicisgpnnn
asaviwynrrpvteintwarnilrtqesecvchngvcpvvftdgsatgpaetriyyfkeg
kilkweplagtakhieecscygeraeitctcrdnwqgsnrpviridpvamthtsqyicsp
vltdnprpndptvgkcndpypgnnnngvkgfsyldgvntwlgrtisiasrsgyemlkvpn
altddkskptqgqtivlntdwsgysgsfmdywaegecyracfyvelirgrpkedkvwwts
nsivsmcssteflgqwdwpdgakieyfl
>d1bjja_ 1.123.1.2.4 Snake phospholipase A2 {Chinese water moccasin (Agkistrodon halys pallas), different isoforms}
nllqfnkmikeetgknaipfyafygcycgwggqgkpkdgtdrccfvhdccygrlvncntk
sdiysyslkegyitcgkgtnceeqicecdrvaaecfrrnldtynngymfyrdskctetse
ec
>d1bjjb_ 1.123.1.2.4 Snake phospholipase A2 {Chinese water moccasin (Agkistrodon halys pallas), different isoforms}
nllqfnkmikeetgknaipfyafygcycgwggqgkpkdgtdrccfvhdccygrlvncntk
sdiysyslkegyitcgkgtnceeqicecdrvaaecfrrnldtynngymfyrdskctetse
ec
>d1bjjc_ 1.123.1.2.4 Snake phospholipase A2 {Chinese water moccasin (Agkistrodon halys pallas), different isoforms}
nllqfnkmikeetgknaipfyafygcycgwggqgkpkdgtdrccfvhdccygrlvncntk
sdiysyslkegyitcgkgtnceeqicecdrvaaecfrrnldtynngymfyrdskctetse
ec
>d1bjjd_ 1.123.1.2.4 Snake phospholipase A2 {Chinese water moccasin (Agkistrodon halys pallas), different isoforms}
nllqfnkmikeetgknaipfyafygcycgwggqgkpkdgtdrccfvhdccygrlvncntk
sdiysyslkegyitcgkgtnceeqicecdrvaaecfrrnldtynngymfyrdskctetse
ec
>d1bjje_ 1.123.1.2.4 Snake phospholipase A2 {Chinese water moccasin (Agkistrodon halys pallas), different isoforms}
nllqfnkmikeetgknaipfyafygcycgwggqgkpkdgtdrccfvhdccygrlvncntk
sdiysyslkegyitcgkgtnceeqicecdrvaaecfrrnldtynngymfyrdskctetse
ec
>d1bjjf_ 1.123.1.2.4 Snake phospholipase A2 {Chinese water moccasin (Agkistrodon halys pallas), different isoforms}
nllqfnkmikeetgknaipfyafygcycgwggqgkpkdgtdrccfvhdccygrlvncntk
sdiysyslkegyitcgkgtnceeqicecdrvaaecfrrnldtynngymfyrdskctetse
ec
>d1bjk_1 2.38.1.1.3 (9-141) Ferredoxin reductase (flavodoxin reductase) {Cyanobacterium (Anabaena), PCC 7119}
dvpvnlyrpnapfigkvisneplvkeggigivqhikfdltggnlkyiegqsigiippgvd
kngkpeklrlysiastrhgddvddktislcvrqleykhpesgetvygvcstylthiepgs
evkitgpvgkeml
>d1bjk_2 3.18.1.1.3 (142-303) Ferredoxin reductase (flavodoxin reductase) {Cyanobacterium (Anabaena), PCC 7119}
lpddpeanvimlatgtgiapmrtylwrmfkdaeraanpeyqfkgfswlvfgvpttpnily
keeleeiqqkypdnfrltyaisreqknpqggrmyiqdrvaehadqlwqliknqkthtyic
glegmeegidaalsaaaakegvtwsdyqkdlkkagrwhvety
>d1bjma_ 2.1.1.1.145 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (lambda) dimer LOC (human)}
xsvltqppsasgtpgqrvtiscsgsssnigensvtwyqhlsgtapklliyednsrasgvs
drfsasksgtsaslaisglqpedetdyycaawddsldvavfgtgtkvtvlgqpkanptvt
lfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskqsnnkyaass
ylsltpeqwkshrsyscqvthegstvektvaptecs
>d1bjmb_ 2.1.1.1.145 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (lambda) dimer LOC (human)}
xsvltqppsasgtpgqrvtiscsgsssnigensvtwyqhlsgtapklliyednsrasgvs
drfsasksgtsaslaisglqpedetdyycaawddsldvavfgtgtkvtvlgqpkanptvt
lfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskqsnnkyaass
ylsltpeqwkshrsyscqvthegstvektvaptecs
>d1bjna_ 3.57.1.4.5 Phosphoserine aminotransferase, PSAT {Escherichia coli}
qifnfssgpamlpaevlkqaqqelrdwnglgtsvmevshrgkefiqvaeeaekdfrdlln
vpsnykvlfchgggrgqfaavplnilgdkttadyvdagywaasaikeakkyctpnvfdak
vtvdglravkpmrewqlsdnaaymhycpnetidgiaidetpdfgadvvvaadfsstilsr
pidvsrygviyagaqxnigpagltivivredllgkaniacpsildysilndngsmfntpp
tfawylsglvfkwlkanggvaemdkinqqkaellygvidnsdfyrndvakrnrsrmnvpf
qladsaldklfleesfaaglhalkghrvvggmrasiynamplegvkaltdfmveferrhg
>d1bjnb_ 3.57.1.4.5 Phosphoserine aminotransferase, PSAT {Escherichia coli}
qifnfssgpamlpaevlkqaqqelrdwnglgtsvmevshrgkefiqvaeeaekdfrdlln
vpsnykvlfchgggrgqfaavplnilgdkttadyvdagywaasaikeakkyctpnvfdak
vtvdglravkpmrewqlsdnaaymhycpnetidgiaidetpdfgadvvvaadfsstilsr
pidvsrygviyagaqxnigpagltivivredllgkaniacpsildysilndngsmfntpp
tfawylsglvfkwlkanggvaemdkinqqkaellygvidnsdfyrndvakrnrsrmnvpf
qladsaldklfleesfaaglhalkghrvvggmrasiynamplegvkaltdfmveferrhg
>d1bjoa_ 3.57.1.4.5 Phosphoserine aminotransferase, PSAT {Escherichia coli}
qifnfssgpamlpaevlkqaqqelrdwnglgtsvmevshrgkefiqvaeeaekdfrdlln
vpsnykvlfchgggrgqfaavplnilgdkttadyvdagywaasaikeakkyctpnvfdak
vtvdglravkpmrewqlsdnaaymhycpnetidgiaidetpdfgadvvvaadfsstilsr
pidvsrygviyagaqknigpagltivivredllgkaniacpsildysilndngsmfntpp
tfawylsglvfkwlkanggvaemdkinqqkaellygvidnsdfyrndvakrnrsrmnvpf
qladsaldklfleesfaaglhalkghrvvggmrasiynamplegvkaltdfmveferrhg
>d1bjob_ 3.57.1.4.5 Phosphoserine aminotransferase, PSAT {Escherichia coli}
qifnfssgpamlpaevlkqaqqelrdwnglgtsvmevshrgkefiqvaeeaekdfrdlln
vpsnykvlfchgggrgqfaavplnilgdkttadyvdagywaasaikeakkyctpnvfdak
vtvdglravkpmrewqlsdnaaymhycpnetidgiaidetpdfgadvvvaadfsstilsr
pidvsrygviyagaqxnigpagltivivredllgkaniacpsildysilndngsmfntpp
tfawylsglvfkwlkanggvaemdkinqqkaellygvidnsdfyrndvakrnrsrmnvpf
qladsaldklfleesfaaglhalkghrvvggmrasiynamplegvkaltdfmveferrhg
>d1bjpa_ 4.60.1.1.1 4-oxalocrotonate tautomerase {Pseudomonas}
piaqihilegrsdeqketlirevseaisrsldapltsvrviitemakghfgiggelaskv
rr
>d1bjpb_ 4.60.1.1.1 4-oxalocrotonate tautomerase {Pseudomonas}
piaqihilegrsdeqketlirevseaisrsldapltsvrviitemakghfgiggelaskv
rr
>d1bjpc_ 4.60.1.1.1 4-oxalocrotonate tautomerase {Pseudomonas}
piaqihilegrsdeqketlirevseaisrsldapltsvrviitemakghfgiggelas
>d1bjpd_ 4.60.1.1.1 4-oxalocrotonate tautomerase {Pseudomonas}
piaqihilegrsdeqketlirevseaisrsldapltsvrviitemakghfgiggelaskv
>d1bjpe_ 4.60.1.1.1 4-oxalocrotonate tautomerase {Pseudomonas}
piaqihilegrsdeqketlirevseaisrsldapltsvrviitemakghfgiggelaskv
rr
>d1bjqa_ 2.26.1.1.13 Lectin {Horse gram (Dolichos biflorus), different isoforms}
aniqsfsfknfnspsfilqgdatvssgklqltkvkengiptpsslgrafysspiqiydks
tgavaswatsftvkisapskasfadgiafalvpvgseprrnggylgvfdsdvynnsaqtv
avefdtlsnsgwdpsmkhigidvnsiksiatvswdlangenaeilitynaatsllvaslv
hpsrrtsyilservditnelpeyvsvgfsattglsegyiethdvlswsfasklpddstae
pldlasylvrnvl
>d1bjqb_ 2.26.1.1.13 Lectin {Horse gram (Dolichos biflorus), different isoforms}
aniqsfsfknfnspsfilqgdatvssgklqltkvkengiptpsslgrafysspiqiydks
tgavaswatsftvkisapskasfadgiafalvpvgseprrnggylgvfdsdvynnsaqtv
avefdtlsnsgwdpsmkhigidvnsiksiatvswdlangenaeilitynaatsllvaslv
hpsrrtsyilservditnelpeyvsvgfsattglsegyiethdvlswsfasklpddstae
pldlasylvrnvl
>d1bjqc_ 2.26.1.1.13 Lectin {Horse gram (Dolichos biflorus), different isoforms}
aniqsfsfknfnspsfilqgdatvssgklqltkvkengiptpsslgrafysspiqiydks
tgavaswatsftvkisapskasfadgiafalvpvgseprrnggylgvfdsdvynnsaqtv
avefdtlsnsgwdpsmkhigidvnsiksiatvswdlangenaeilitynaatsllvaslv
hpsrrtsyilservditnelpeyvsvgfsattglsegyiethdvlswsfasklpd
>d1bjqd_ 2.26.1.1.13 Lectin {Horse gram (Dolichos biflorus), different isoforms}
aniqsfsfknfnspsfilqgdatvssgklqltkvkengiptpsslgrafysspiqiydks
tgavaswatsftvkisapskasfadgiafalvpvgseprrnggylgvfdsdvynnsaqtv
avefdtlsnsgwdpsmkhigidvnsiksiatvswdlangenaeilitynaatsllvaslv
hpsrrtsyilservditnelpeyvsvgfsattglsegyiethdvlswsfasklpd
>d1bjqe_ 2.26.1.1.13 Lectin {Horse gram (Dolichos biflorus), different isoforms}
aniqsfsfknfnspsfilqgdatvssgklqltkvkengiptpsslgrafysspiqiydks
tgavaswatsftvkisapskasfadgiafalvpvgseprrnggylgvfdsdvynnsaqtv
avefdtlsnsgwdpsmkhigidvnsiksiatvswdlangenaeilitynaatsllvaslv
hpsrrtsyilservditnelpeyvsvgfsattglsegyiethdvlswsfasklpd
>d1bjqf_ 2.26.1.1.13 Lectin {Horse gram (Dolichos biflorus), different isoforms}
aniqsfsfknfnspsfilqgdatvssgklqltkvkengiptpsslgrafysspiqiydks
tgavaswatsftvkisapskasfadgiafalvpvgseprrnggylgvfdsdvynnsaqtv
avefdtlsnsgwdpsmkhigidvnsiksiatvswdlangenaeilitynaatsllvaslv
hpsrrtsyilservditnelpeyvsvgfsattglsegyiethdvlswsfasklpd
>d1bjqg_ 2.26.1.1.13 Lectin {Horse gram (Dolichos biflorus), different isoforms}
aniqsfsfknfnspsfilqgdatvssgklqltkvkengiptpsslgrafysspiqiydks
tgavaswatsftvkisapskasfadgiafalvpvgseprrnggylgvfdsdvynnsaqtv
avefdtlsnsgwdpsmkhigidvnsiksiatvswdlangenaeilitynaatsllvaslv
hpsrrtsyilservditnelpeyvsvgfsattglsegyiethdvlswsfasklpddstae
pldlasylvrnvl
>d1bjqh_ 2.26.1.1.13 Lectin {Horse gram (Dolichos biflorus), different isoforms}
aniqsfsfknfnspsfilqgdatvssgklqltkvkengiptpsslgrafysspiqiydks
tgavaswatsftvkisapskasfadgiafalvpvgseprrnggylgvfdsdvynnsaqtv
avefdtlsnsgwdpsmkhigidvnsiksiatvswdlangenaeilitynaatsllvaslv
hpsrrtsyilservditnelpeyvsvgfsattglsegyiethdvlswsfasklpddstae
pldlasylvrnvl
>d1bjre_ 3.33.1.1.12 Proteinase K {Fungus (Tritirachium album), strain limber}
aaqtnapwglarisstspgtstyyydesagqgscvyvidtgieashpefegraqmvktyy
yssrdgnghgthcagtvgsrtygvakktqlfgvkvlddngsgqystiiagmdfvasdknn
rncpkgvvaslslgggysssvnsaaarlqssgvmvavaagnnnadarnyspasepsvctv
gasdrydrrssfsnygsvldifgpgtsilstwiggstrsisgtsmatphvaglaaylmtl
gkttaasacryiadtankgdlsnipfgtvnllaynnyqa
>d1bjt__ 5.11.1.1.1 DNA topoisomerase II, C-terminal fragment (residues 410-1202) {Baker's yeast (Saccharomyces cerevisiae)}
rksritnypkledankagtkegykctlvltegdsalslavaglavvgrdyygcyplrgkm
lnvreasadqilknaeiqaikkimglqhrkkyedtkslryghlmimtdqdhdgshikgli
inflessflglldiqgfllefitpiikvsitkptkntiafynmpdyekwreeeshkftwk
qkyykglgtslaqevreyfsnldrhlkifhslqgndkdyidlafskkkaddrkewlrqye
pgtvldptlkeipisdfinkelilfsladnirsipnvldgfkpgqrkvlygcfkknlkse
lkvaqlapyvsectayhhgeqslaqtiiglaqnfvgsnniylllpngafgtratggkdaa
aaryiytelnkltrkifhpaddplykyiqedektvepewylpilpmilvngaegigtgws
tyippfnpleiiknirhlmndeeleqmhpwfrgwtgtieeieplryrmygrieqigdnvl
eitelpartwtstikeylllglsgndkikpwikdmeeqhddnikfiitlspeemaktrki
gfyerfklispislmnmvafdphgkikkynsvneilsefyyvrleyyqkrkdhmserlqw
evekysfqvkfikmiiekeltvtnkprnaiiqelenlgfprfnkegkpyygspndeiaeq
indvkgatsdeedeesshedtenvingpeelygtyeyllgmriwsltkeryqkllkqkqe
ketelenllklsakdiwntdlkafevgyqeflqrdaearg
>d1bju__ 2.41.1.2.1 Trypsin(ogen) {Bovine (Bos taurus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1bjv__ 2.41.1.2.1 Trypsin(ogen) {Bovine (Bos taurus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1bjwa_ 3.57.1.1.6 Aspartate aminotransferase, AAT {Thermus thermophilus}
mrglsrrvqamkpsatvavnakalelrrqgvdlvaltagepdfdtpehvkeaarralaqg
ktkyappagipelrealaekfrrenglsvtpeetivtvggkqalfnlfqaildpgdeviv
lspywvsypemvrfaggvvvevetlpeegfvpdpervrraitprtkalvvnspnnptgav
ypkevlealarlavehdfylvsdeiyehllyegehfspgrvapehtltvngaaxafamtg
wrigyacgpkevikamasvssqsttspdtiaqwatlealtnqeasrafvemareayrrrr
dlllegltalglkavrpsgafyvlmdtspiapdevraaerlleagvavvpgtdfaafghv
rlsyatseenlrkalerfarvl
>d1bjwb_ 3.57.1.1.6 Aspartate aminotransferase, AAT {Thermus thermophilus}
mrglsrrvqamkpsatvavnakalelrrqgvdlvaltagepdfdtpehvkeaarralaqg
ktkyappagipelrealaekfrrenglsvtpeetivtvggkqalfnlfqaildpgdeviv
lspywvsypemvrfaggvvvevetlpeegfvpdpervrraitprtkalvvnspnnptgav
ypkevlealarlavehdfylvsdeiyehllyegehfspgrvapehtltvngaaxafamtg
wrigyacgpkevikamasvssqsttspdtiaqwatlealtnqeasrafvemareayrrrr
dlllegltalglkavrpsgafyvlmdtspiapdevraaerlleagvavvpgtdfaafghv
rlsyatseenlrkalerfarvl
>d1bjx__ 3.38.1.2.1 Protein disulfide isomerase {Human (Homo sapiens)}
aattlpdgaaaeslvessevavigffkdvesdsakqflqaaeaiddipfgitsnsdvfsk
yqldkdgvvlfkkfdegrnnfegevtkenlldfikhnqlplviefteqta
>d1bjya1 1.37.1.1.1 (2-67) Tetracyclin repressor (Tet-repressor, TetR), N-terminal domain {Escherichia coli}
srlnresvidaalellnetgidglttrklaqklgieqptlywhvknkralldalaveila
rhhdys
>d1bjya2 1.113.1.1.1 (68-208) Tetracyclin repressor (Tet-repressor, TetR), C-terminal domain {Escherichia coli}
lpaageswqsflrnnamsfrrallryrdgakvhlgtrpdekqydtvetqlrfmtengfsl
rdglyaisavshftlgavleqqehtaaltdrpaapdenlppllrealqimdsddgeqafl
hgleslirgfevqltallqiv
>d1bjyb1 1.37.1.1.1 (2-67) Tetracyclin repressor (Tet-repressor, TetR), N-terminal domain {Escherichia coli}
srlnresvidaalellnetgidglttrklaqklgieqptlywhvknkralldalaveila
rhhdys
>d1bjyb2 1.113.1.1.1 (68-208) Tetracyclin repressor (Tet-repressor, TetR), C-terminal domain {Escherichia coli}
lpaageswqsflrnnamsfrrallryrdgakvhlgtrpdekqydtvetqlrfmtengfsl
rdglyaisavshftlgavleqqehtaaltdrpaapdenlppllrealqimdsddgeqafl
hgleslirgfevqltallqiv
>d1bjz_1 1.37.1.1.1 (2-67) Tetracyclin repressor (Tet-repressor, TetR), N-terminal domain {Escherichia coli}
srlnresvidaalellnetgidglttrklaqklgieqptlywhvknkralldalaveila
rhhdys
>d1bjz_2 1.113.1.1.1 (68-208) Tetracyclin repressor (Tet-repressor, TetR), C-terminal domain {Escherichia coli}
lpaageswqsflrnnamsfrrallryrdgakvhlgtrpdekqydtvetqlrfmtengfsl
rdglyaisavshftlgavleqqehtaaltdrpaapdenlppllrealqimdsddgeqafl
hgleslirgfevqltallqiv
>d1bk0__ 2.73.3.1.1 Isopenicillin N synthase {Emericella nidulans}
svskanvpkidvsplfgddqaakmrvaqqidaasrdtgffyavnhginvqrlsqktkefh
msitpeekwdlairaynkehqdqvragyylsipgkkavesfcylnpnftpdhpriqaktp
thevnvwpdetkhpgfqdfaeqyywdvfglssallkgyalalgkeenffarhfkpddtla
svvlirypyldpypeaaiktaadgtklsfewhedvslitvlyqsnvqnlqvetaagyqdi
eaddtgylincgsymahltnnyykapihrvkwvnaerqslpffvnlgydsvidpfdprep
ngksdreplsygdylqnglvslinkngqt
>d1bk1__ 2.26.1.10.8 Xylanase II {Aspergillus kawachii}
aginyvqnyngnlgdftydesagtfsmywedgvssdfvvglgwttgssnaitysaeysas
gsssylavygwvnypqaeyyivedygdynpcssatslgtvysdgstyqvctdtrtnepsi
tgtstftqyfsvrestrtsgtvtvanhfnfwaqhgfgnsdfnyqvmaveawsgagsasvt
is
>d1bk2__ 2.30.2.1.8 alpha-Spectrin, SH3 domain {Chicken (Gallus gallus)}
kelvlalydyqeksprevtmkkgdiltllnstnkdwwkvevngrqgfvpaayvkkld
>d1bk4__ 5.7.1.1.3 Fructose-1,6-bisphosphatase {Rabbit (Oryctolagus cuniculus)}
fdtdistmtrfvmeegrkaggtgemtqllnslctavkaistavrkagiahlygiagstnv
tgdqvkkldvlsndlvmnmlkssfatcvlvseedknaiivepekrgkyvvcfdpldgssn
idclvsigtifgiyrkkstdepstkdalqpgrnlvaagyalygsatmlvlaggsgvnsfm
ldpaigefilvdknvkikkkgniyslnegyakdfdpavteyiqkkkfppdnsspygaryv
gsmvadvhrtlvyggiflypankkspdgklrllyecnpmafimekaggmattgkeaildi
vptdihqrapvilgspddvqefleiykkhavk
>d1bk5a_ 1.110.1.1.5 Karyopherin alpha {Baker's yeast (Saccharomyces cerevisiae)}
lpqmtqqlnsddmqeqlsatvkfrqilsrehrppidvviqagvvprlvefmrenqpemlq
leaawaltniasgtsaqtkvvvdadavplfiqllytgsvevkeqaiwalgnvagdstdyr
dyvlqcnamepilglfnsnkpslirtatwtlsnlcrgkkpqpdwsvvsqalptlakliys
mdtetlvdacwaisylsdgpqeaiqavidvripkrlvellshestlvqtpalravgnivt
gndlqtqvvinagvlpalrlllsspkenikkeacwtisnitagnteqiqavidanlippl
vkllevaeyktkkeacwaisnassgglqrpdiirylvsqgcikplcdlleiadnriievt
ldalenilkmgeadkearglninenadfiekaggmekifncqqnendkiyekaykiiety
fg
>d1bk5b_ 1.110.1.1.5 Karyopherin alpha {Baker's yeast (Saccharomyces cerevisiae)}
lpqmtqqlnsddmqeqlsatvkfrqilsrehrppidvviqagvvprlvefmrenqpemlq
leaawaltniasgtsaqtkvvvdadavplfiqllytgsvevkeqaiwalgnvagdstdyr
dyvlqcnamepilglfnsnkpslirtatwtlsnlcrgkkpqpdwsvvsqalptlakliys
mdtetlvdacwaisylsdgpqeaiqavidvripkrlvellshestlvqtpalravgnivt
gndlqtqvvinagvlpalrlllsspkenikkeacwtisnitagnteqiqavidanlippl
vkllevaeyktkkeacwaisnassgglqrpdiirylvsqgcikplcdlleiadnriievt
ldalenilkmgeadkearglninenadfiekaggmekifncqqnendkiyekaykiiety
fg
>d1bk6a_ 1.110.1.1.5 Karyopherin alpha {Baker's yeast (Saccharomyces cerevisiae)}
lpqmtqqlnsddmqeqlsatvkfrqilsrehrppidvviqagvvprlvefmrenqpemlq
leaawaltniasgtsaqtkvvvdadavplfiqllytgsvevkeqaiwalgnvagdstdyr
dyvlqcnamepilglfnsnkpslirtatwtlsnlcrgkkpqpdwsvvsqalptlakliys
mdtetlvdacwaisylsdgpqeaiqavidvripkrlvellshestlvqtpalravgnivt
gndlqtqvvinagvlpalrlllsspkenikkeacwtisnitagnteqiqavidanlippl
vkllevaeyktkkeacwaisnassgglqrpdiirylvsqgcikplcdlleiadnriievt
ldaleniikmgeadkearglninenadfiekaggmekifncqqnendkiyekaykiiety
fg
>d1bk6b_ 1.110.1.1.5 Karyopherin alpha {Baker's yeast (Saccharomyces cerevisiae)}
lpqmtqqlnsddmqeqlsatvkfrqilsrehrppidvviqagvvprlvefmrenqpemlq
leaawaltniasgtsaqtkvvvdadavplfiqllytgsvevkeqaiwalgnvagdstdyr
dyvlqcnamepilglfnsnkpslirtatwtlsnlcrgkkpqpdwsvvsqalptlakliys
mdtetlvdacwaisylsdgpqeaiqavidvripkrlvellshestlvqtpalravgnivt
gndlqtqvvinagvlpalrlllsspkenikkeacwtisnitagnteqiqavidanlippl
vkllevaeyktkkeacwaisnassgglqrpdiirylvsqgcikplcdlleiadnriievt
ldaleniikmgeadkearglninenadfiekaggmekifncqqnendkiyekaykiiety
fg
>d1bk7a_ 4.98.1.1.2 Ribonuclease MC1 {Bitter gourd (Momordica charantia)}
fdsfwfvqqwppavcsfqksgscpgsglrtftihglwpqqsgtsltncpgspfditkish
lqsqlntlwpnvlrannqqfwshewtkhgtcsestfnqaayfklavdmrnnydiigalrp
haagpngrtksrqaikgflkakfgkfpglrcrtdpqtkvsylvqvvacfaqdgstlidct
rdtcganfif
>d1bk9__ 1.123.1.2.4 Snake phospholipase A2 {Chinese water moccasin (Agkistrodon halys pallas), different isoforms}
sliqfetlimkvakksgmfwysnygcycgwggqgrpqdatdrccfvhdccygkvtgcdpk
mdvysfseengdivcggddpckkeicecdraaaicfrdnltlyndkkywafgakncpqee
sepc
>d1bka_1 3.84.1.2.1 (4-334) Lactoferrin {Human (Homo sapiens)}
rsvqwcavsqpeatkcfqwqrnmrkvrgppvscikrdspiqciqaiaenradavtldggf
iyeaglapyklrpvaaevygterqprthyyavavvkkggsfqlnelqglkschtglrrta
gwnvpigtlrpflnwtgppepieaavarffsascvpgadkgqfpnlcrlcagtgenkcaf
ssqepyfsysgafkclrdgagdvafirestvfedlsdeaerdeyellcpdntrkpvdkfk
dchlarvpshavvarsvngkedaiwnllrqaqekfgkdkspkfqlfgspsgqkdllfkds
aigfsrvppridsglylgsgyftaiqnlrks
>d1bka_2 3.84.1.2.1 (335-691) Lactoferrin {Human (Homo sapiens)}
eeevaarrarvvwcavgeqelrkcnqwsglsegsvtcssasttedcialvlkgeadamsl
dggyvytagkcglvpvlaenyksqqssdpdpncvdrpvegylavavvrrsdtsltwnsvk
gkkschtavdrtagwnipmgllfnqtgsckfdeyfsqscapgsdprsnlcalcigdeqge
nkcvpnsneryygytgafrclaenagdvafvkdvtvlqntdgnnneawakdlkladfall
cldgkrkpvtearschlamapnhavvsrmdkverlkqvllhqqakfgrngsdcpdkfclf
qsetknllfndnteclarlhgkttyekylgpqyvagitnlkkcstsplleaceflrk
>d1bkb_1 2.30.7.1.2 (4-74) N-terminal domain of eukaryotic initiation translation factor 5a {Pyrobaculum aerophilum}
kwvxstkyveagelkegsyvvidgepcrvveieksktgkhgsakarivavgvfdggkrtl
slpvdaqvevp
>d1bkb_2 2.35.4.5.7 (75-139) C-terminal domain of eukaryotic initiation translation factor 5a {Pyrobaculum aerophilum}
iiekftaqilsvsgdviqlxdxrdyktievpxkyveeeakgrlapgaevevwqildryki
irvkg
>d1bkca_ 4.71.1.8.1 TNF-alpha converting enzyme, TACE, catalytic domain {Human (Homo sapiens)}
dpmkntckllvvadhrfyrymgrgeestttnylielidrvddiyrntawdnagfkgygiq
ieqirilkspqevkpgekhynmaksypneekdawdvkmlleqfsfdiaeeaskvclahlf
tyqdfdmgtlglayvgspranshggvcpkayyspvgkkniylnsgltstknygktiltke
adlvtthelghnfgaehdpdglaecapnedqggkyvmypiavsgdhennkmfsqcskqsi
yktieskaqecfqer
>d1bkcc_ 4.71.1.8.1 TNF-alpha converting enzyme, TACE, catalytic domain {Human (Homo sapiens)}
mkntckllvvadhrfyrymgrgeestttnylielidrvddiyrntawdnagfkgygiqie
qirilkspqevkpgekhynmaksypneekdawdvkmlleqfsfdiaeeaskvclahlfty
qdfdmgtlglayvgspranshggvcpkayyspvgkkniylnsgltstknygktiltkead
lvtthelghnfgaehdpdglaecapnedqggkyvmypiavsgdhennkmfsqcskqsiyk
tieskaqecfqers
>d1bkce_ 4.71.1.8.1 TNF-alpha converting enzyme, TACE, catalytic domain {Human (Homo sapiens)}
dpmkntckllvvadhrfyrymgrgeestttnylielidrvddiyrntawdnagfkgygiq
ieqirilkspqevkpgekhynmaksypneekdawdvkmlleqfsfdiaeeaskvclahlf
tyqdfdmgtlglayvgspranshggvcpkayyspvgkkniylnsgltstknygktiltke
adlvtthelghnfgaehdpdgkaecapnedqggkyvmypiavsgdhennkmfsqcskqsi
yktieskaqecfqers
>d1bkci_ 4.71.1.8.1 TNF-alpha converting enzyme, TACE, catalytic domain {Human (Homo sapiens)}
mkntckllvvadhrfyrymgrgeestttnylielidrvddiyrntawdnagfkgygiqie
qirilkspqevkpgekhynmaksypneekdawdvkmlleqfsfdiaeeaskvclahlfty
qdfdmgtlglayvgspranshggvcpkayyspvgkkniylnsgltstknygktiltkead
lvtthelghnfgaehdpdglaecapneeqggkyvmypiavsgdhennkmfsqcskqsiyk
tieskaqecfqers
>d1bkdr_ 3.30.1.6.1 cH-p21 Ras protein {Human (Homo sapiens)}
mteyklvvvgaggvgksaltiqliqnhfvdeydptiedsyrkqvvidgetclldildtag
qeeysamrdqymrtgegflcvfainntksfedihqyreqikrvkdsddvpmvlvgnkcdl
aartvesrqaqdlarsygipyietsaktrqgvedafytlvreirqh
>d1bkds_ 1.109.1.1.1 Son of sevenless-1 (sos-1) {Human (Homo sapiens)}
rlpsadvyrfaepdseeniifeegipiikagtviklierltyhmyadpnfvrtflttyrs
fckpqellsliierfeipeprfrkeyiqpvqlrvlnvcrhwvehhfydferdayllqrme
efigtvrgkamkkwvesitkiiqrkkitfqsspptvewhisrpghietfdlltlhpieia
rqltllesdlyravqpselvgsvwtkedkeinspnllkmirhttnltlwfekcivetenl
eervavvsriieilqvfqelnnfngvlevvsamnsspvyrldhtfeqipsrqkkileeah
elsedhykkylaklrsinppcvpffgiyltnilkteegnpevlkrhgkelinfskrrkva
eitgeiqqyqnqpyclrvesdikrffenlnpmgnsmekeftdylfnksleieprnpkplp
rfpkkysyplkspgvrpsn
>d1bke_1 1.116.1.1.1 (4-196) Serum albumin {Human (Homo sapiens)}
ksevahrfkdlgeenfkalvliafaqylqqcpfedhvklvnevtefaktcvadesaencd
kslhtlfgdklctvatlretygemadccakqepernecflqhkddnpnlprlvrpevdvm
ctafhdneetflkkylyeiarrhpyfyapellffakrykaafteccqaadkaacllpkld
elrdegkassakq
>d1bke_2 1.116.1.1.1 (197-388) Serum albumin {Human (Homo sapiens)}
rlkcaslqkfgerafkawavarlsqrfpkaefaevsklvtdltkvhtecchgdllecadd
radlakyicenqdsissklkeccekpllekshciaevendempadlpslaadfveskdvc
knyaeakdvflgmflyeyarrhpdysvvlllrlaktyettlekccaaadphecyakvfde
fkplveepqnli
>d1bke_3 1.116.1.1.1 (389-584) Serum albumin {Human (Homo sapiens)}
kqncelfeqlgeykfqnallvrytkkvpqvstptlvevsrnlgkvgskcckhpeakrmpc
aedylsvvlnqlcvlhektpvsdrvtkccteslvnrrpcfsalevdetyvpkefnaetft
fhadictlsekerqikkqtalvelvkhkpkatkeqlkavmddfaafvekcckaddketcf
aeegkklvaasqaalg
>d1bkf__ 4.23.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdknkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatgvpgiipphatlvfdvellkle
>d1bkga_ 3.57.1.1.6 Aspartate aminotransferase, AAT {Thermus thermophilus}
mrglsrrvqamkpsatvavnakalelrrqgvdlvaltagepdfdtpehvkeaarralaqg
ktkyappagipelrealaekfrrenglsvtpeetivtvggkqalfnlfqaildpgdeviv
lspywvsypemvrfaggvvvevetlpeegfvpdpervrraitprtkalvvnspnnptgav
ypkevlealarlavehdfylvsdeiyehllyegehfspgrvapehtltvngaakafamtg
wrigyacgpkevikamasvssqsttspdtiaqwatlealtnqeasrafvemareayrrrr
dlllegltalglkavrpsgafyvlmdtspiapdevraaerlleagvavvpgtdfaafghv
rlsyatseenlrkalerfarvl
>d1bkgb_ 3.57.1.1.6 Aspartate aminotransferase, AAT {Thermus thermophilus}
mrglsrrvqamkpsatvavnakalelrrqgvdlvaltagepdfdtpehvkeaarralaqg
ktkyappagipelrealaekfrrenglsvtpeetivtvggkqalfnlfqaildpgdeviv
lspywvsypemvrfaggvvvevetlpeegfvpdpervrraitprtkalvvnspnnptgav
ypkevlealarlavehdfylvsdeiyehllyegehfspgrvapehtltvngaakafamtg
wrigyacgpkevikamasvssqsttspdtiaqwatlealtnqeasrafvemareayrrrr
dlllegltalglkavrpsgafyvlmdtspiapdevraaerlleagvavvpgtdfaafghv
rlsyatseenlrkalerfarvl
>d1bkgc_ 3.57.1.1.6 Aspartate aminotransferase, AAT {Thermus thermophilus}
mrglsrrvqamkpsatvavnakalelrrqgvdlvaltagepdfdtpehvkeaarralaqg
ktkyappagipelrealaekfrrenglsvtpeetivtvggkqalfnlfqaildpgdeviv
lspywvsypemvrfaggvvvevetlpeegfvpdpervrraitprtkalvvnspnnptgav
ypkevlealarlavehdfylvsdeiyehllyegehfspgrvapehtltvngaakafamtg
wrigyacgpkevikamasvssqsttspdtiaqwatlealtnqeasrafvemareayrrrr
dlllegltalglkavrpsgafyvlmdtspiapdevraaerlleagvavvpgtdfaafghv
rlsyatseenlrkalerfarvl
>d1bkgd_ 3.57.1.1.6 Aspartate aminotransferase, AAT {Thermus thermophilus}
mrglsrrvqamkpsatvavnakalelrrqgvdlvaltagepdfdtpehvkeaarralaqg
ktkyappagipelrealaekfrrenglsvtpeetivtvggkqalfnlfqaildpgdeviv
lspywvsypemvrfaggvvvevetlpeegfvpdpervrraitprtkalvvnspnnptgav
ypkevlealarlavehdfylvsdeiyehllyegehfspgrvapehtltvngaakafamtg
wrigyacgpkevikamasvssqsttspdtiaqwatlealtnqeasrafvemareayrrrr
dlllegltalglkavrpsgafyvlmdtspiapdevraaerlleagvavvpgtdfaafghv
rlsyatseenlrkalerfarvl
>d1bkha1 3.1.10.2.2 (131-372) Muconate-lactonizing enzyme {Pseudomonas putida}
rvrdslevawtlasgdtardiaearhmleirrhrvfklkiganpveqdlkhvvtikrelg
dsasvrvdvnqywdesqairacqvlgdngidlieqpisrinrggqvrlnqrtpapimade
siesvedafslaadgaasifalkiaknggpravlrtaqiaeaagiglyggtmlegsigtl
asahafltlrqltwgtelfgplllteeivneppqyrdfqlhiprtpglgltldeqrlarf
ar
>d1bkha2 4.44.1.1.4 (4-130) Muconate-lactonizing enzyme (cis muconate cycloisomerase) {Pseudomonas putida}
alieridaiivdlptiqqtlvvlrvrcsdgvegigeattigglaygyespegikanidah
lapaliglaadninaamlkldklakgntfaksgiesalldaqgkrlglpvsellgg
>d1bkhb1 3.1.10.2.2 (131-372) Muconate-lactonizing enzyme {Pseudomonas putida}
rvrdslevawtlasgdtardiaearhmleirrhrvfklkiganpveqdlkhvvtikrelg
dsasvrvdvnqywdesqairacqvlgdngidlieqpisrinrggqvrlnqrtpapimade
siesvedafslaadgaasifalkiaknggpravlrtaqiaeaagiglyggtmlegsigtl
asahafltlrqltwgtelfgplllteeivneppqyrdfqlhiprtpglgltldeqrlarf
ar
>d1bkhb2 4.44.1.1.4 (4-130) Muconate-lactonizing enzyme (cis muconate cycloisomerase) {Pseudomonas putida}
alieridaiivdlptirpqqqtlvvlrvrcsdgvegigeattigglaygyespegikani
dahlapaliglaadninaamlkldklakgntfaksgiesalldaqgkrlglpvsellgg
>d1bkhc1 3.1.10.2.2 (131-372) Muconate-lactonizing enzyme {Pseudomonas putida}
rvrdslevawtlasgdtardiaearhmleirrhrvfklkiganpveqdlkhvvtikrelg
dsasvrvdvnqywdesqairacqvlgdngidlieqpisrinrggqvrlnqrtpapimade
siesvedafslaadgaasifalkiaknggpravlrtaqiaeaagiglyggtmlegsigtl
asahafltlrqltwgtelfgplllteeivneppqyrdfqlhiprtpglgltldeqrlarf
ar
>d1bkhc2 4.44.1.1.4 (4-130) Muconate-lactonizing enzyme (cis muconate cycloisomerase) {Pseudomonas putida}
alieridaiivdlptiqqqtlvvlrvrcsdgvegigeattigglaygyespegikanida
hlapaliglaadninaamlkldklakgntfaksgiesalldaqgkrlglpvsellgg
>d1bkja_ 4.70.1.1.2 Flavin reductase P (NADPH:FMN oxidoreductase) {Vibrio harveyi}
nntietilahrsirkftavpitdeqrqtiiqaglaassssmlqvvsivrvtdsekrnela
qfagnqayvesaaeflvfcidyqrhatinpdvqadfteltligavdsgimaqncllaaes
mglggvyigglrnsaaqvdellglpensavlfgmclghpdqnpevkprlpahvvvhenqy
qelnlddiqsydqtmqayyasrtsnqklstwsqevtgklagesrphilpylnskglakr
>d1bkjb_ 4.70.1.1.2 Flavin reductase P (NADPH:FMN oxidoreductase) {Vibrio harveyi}
nntietilahrsirkftavpitdeqrqtiiqaglaassssmlqvvsivrvtdsekrnela
qfagnqayvesaaeflvfcidyqrhatinpdvqadfteltligavdsgimaqncllaaes
mglggvyigglrnsaaqvdellglpensavlfgmclghpdqnpevkprlpahvvvhenqy
qelnlddiqsydqtmqayyasrtsnqklstwsqevtgklagesrphilpylnskglakr
>d1bkl__ 4.72.1.1.2 v-src tyrosine kinase {Rous sarcoma virus, Schmidt-ruppin strain a}
eewyfgkitrreseslllnpenprgtflvresettkgayclsvsdfdnakglnvkhykir
kldsggfyitsrtqfsslqqlvayyskhadglchrltnvcptskefivtd
>d1bkm__ 4.72.1.1.2 v-src tyrosine kinase {Rous sarcoma virus, Schmidt-ruppin strain a}
eewyfgkitrresealllnpenprgtflvresettkgayclsvsdfdnakglnvkhykir
kldsggfyitsrtqfsslqqlvayyskhadglchrltnvcpt
>d1bkna1 4.12.1.3.1 (217-331) DNA mismatch repair protein MutL {Escherichia coli}
gtafleqalaiewqhgdltlrgwvadpnhttpalaeiqycyvngrmmrdrlinhairqac
edklgadqqpafvlyleidphqvdvnvhpakhevrfhqsrlvhdfiyqgvlsvlq
>d1bkna2 4.96.1.2.2 (20-216) DNA mismatch repair protein MutL {Escherichia coli}
verpasvvkelvensldagatrididierggaklirirdngcgikkdelalalarhatsk
iaslddleaiislgfrgealasissvsrltltsrtaeqqeawqayaegrdmnvtvkpaah
pvgttlevldlfyntparrkflrtektefnhideiirrialarfdvtinlshngkivrqy
ravpeggqkerrlgaic
>d1bknb1 4.12.1.3.1 (617-731) DNA mismatch repair protein MutL {Escherichia coli}
gtafleqalaiewqhgdltlrgwvadpnhttpalaeiqycyvngrmmrdrlinhairqac
edklgadqqpafvlyleidphqvdvnvhpakhevrfhqsrlvhdfiyqgvlsvlq
>d1bknb2 4.96.1.2.2 (420-616) DNA mismatch repair protein MutL {Escherichia coli}
verpasvvkelvensldagatrididierggaklirirdngcgikkdelalalarhatsk
iaslddleaiislgfrgealasissvsrltltsrtaeqqeawqayaegrdmnvtvkpaah
pvgttlevldlfyntparrkflrtektefnhideiirrialarfdvtinlshngkivrqy
ravpeggqkerrlgaic
>d1bkoa_ 4.91.1.1.3 Thymidylate synthase {Bacillus subtilis}
tqfdkqynsiikdiinngisdeefdvrtkwdsdgtpahtlsviskqmrfdnsevpilttk
kvawktaikellwiwqlksndvndlnmmgvhiwdqwkqedgtighaygfqlgkknrslng
ekvdqvdyllhqlknnpssrrhitmlwnpdeldamaltpcvyetqwyvkhgklhlevrar
sndmalgnpfnvfqynvlqrmiaqvtgyelgeyifnigdchvytrhidnlkiqmereqfe
apelwinpevkdfydftiddfklinykhgdkllfevav
>d1bkob_ 4.91.1.1.3 Thymidylate synthase {Bacillus subtilis}
tqfdkqynsiikdiinngisdeefdvrtkwdsdgtpahtlsviskqmrfdnsevpilttk
kvawktaikellwiwqlksndvndlnmmgvhiwdqwkqedgtighaygfqlgkknrslng
ekvdqvdyllhqlknnpssrrhitmlwnpdeldamaltpcvyetqwyvkhgklhlevrar
sndmalgnpfnvfqynvlqrmiaqvtgyelgeyifnigdchvytrhidnlkiqmereqfe
apelwinpevkdfydftiddfklinykhgdkllfevav
>d1bkoc_ 4.91.1.1.3 Thymidylate synthase {Bacillus subtilis}
tqfdkqynsiikdiinngisdeefdvrtkwdsdgtpahtlsviskqmrfdnsevpilttk
kvawktaikellwiwqlksndvndlnmmgvhiwdqwkqedgtighaygfqlgkknrslng
ekvdqvdyllhqlknnpssrrhitmlwnpdeldamaltpcvyetqwyvkhgklhlevrar
sndmalgnpfnvfqynvlqrmiaqvtgyelgeyifnigdchvytrhidnlkiqmereqfe
apelwinpevkdfydftiddfklinykhgdkllfevav
>d1bkod_ 4.91.1.1.3 Thymidylate synthase {Bacillus subtilis}
tqfdkqynsiikdiinngisdeefdvrtkwdsdgtpahtlsviskqmrfdnsevpilttk
kvawktaikellwiwqlksndvndlnmmgvhiwdqwkqedgtighaygfqlgkknrslng
ekvdqvdyllhqlknnpssrrhitmlwnpdeldamaltpcvyetqwyvkhgklhlevrar
sndmalgnpfnvfqynvlqrmiaqvtgyelgeyifnigdchvytrhidnlkiqmereqfe
apelwinpevkdfydftiddfklinykhgdkllfevav
>d1bkpa_ 4.91.1.1.3 Thymidylate synthase {Bacillus subtilis}
tqfdkqynsiikdiinngisdeefdvrtkwdsdgtpahtlsviskqmrfdnsevpilttk
kvawktaikellwiwqlksndvndlnmmgvhiwdqwkqedgtighaygfqlgkknrslng
ekvdqvdyllhqlknnpssrrhitmlwnpdeldamaltpcvyetqwyvkhgklhlevrar
sndmalgnpfnvfqynvlqrmiaqvtgyelgeyifnigdchvytrhidnlkiqmereqfe
apelwinpevkdfydftiddfklinykhgdkllfevav
>d1bkpb_ 4.91.1.1.3 Thymidylate synthase {Bacillus subtilis}
tqfdkqynsiikdiinngisdeefdvrtkwdsdgtpahtlsviskqmrfdnsevpilttk
kvawktaikellwiwqlksndvndlnmmgvhiwdqwkqedgtighaygfqlgkknrslng
ekvdqvdyllhqlknnpssrrhitmlwnpdeldamaltpcvyetqwyvkhgklhlevrar
sndmalgnpfnvfqynvlqrmiaqvtgyelgeyifnigdchvytrhidnlkiqmereqfe
apelwinpevkdfydftiddfklinykhgdkllfevav
>d1bkq__ 4.32.1.1.1 PIN, a protein inhibitor of neuronal nitric oxide synthase {Rabbit (Oryctolagus cuniculus)}
mcdrkaviknadmseemqqdsvecatqalekyniekdiaahikkefdkkynptwhcivgr
nfgsyvthetkhfiyfylgqvaillfksg
>d1bkra_ 1.43.1.1.1 beta-spectrin {Human (Homo sapiens)}
ksakdalllwcqmktagypnvnihnfttswrdgmafnalihkhrpdlidfdklkksnahy
nlqnafnlaeqhlgltklldpedisvdhpdeksiityvvtyyhyfskm
>d1bksa_ 3.1.2.2.5 Trp synthase alpha-subunit {Salmonella typhimurium}
meryenlfaqlndrregafvpfvtlgdpgieqslkiidtlidagadalelgvpfsdplad
gptiqnanlrafaagvtpaqcfemlalirekhptipigllmyanlvfnngidafyarceq
vgvdsvlvadvpveesapfrqaalrhniapificppnadddllrqvasygrgytyllsrs
gvtgaenrgalplhhlieklkeyhaapalqgfgisspeqvsaavragaagaisgsaivki
ieknlaspkqmlaelrsfvsamkaasr
>d1bksb_ 3.67.1.1.1 Tryptophan synthase, beta-subunit {Salmonella typhimurium}
tllnpyfgefggmyvpqilmpalnqleeafvraqkdpefqaqfadllknyagrptaltkc
qnitagtrttlylkredllhggahktnqvlgqallakrmgkseiiaetgagqhgvasala
sallglkcriymgakdverqspnvfrmrlmgaevipvhsgsatlkdacnealrdwsgsye
tahymlgtaagphpyptivrefqrmigeetkaqildkegrlpdaviacvgggsnaigmfa
dfindtsvgligvepgghgietgehgaplkhgrvgiyfgmkapmmqtadgqieesysisa
gldfpsvgpqhaylnsigradyvsitddealeafktlcrhegiipalesshalahalkmm
reqpekeqllvvnlsgrgdkdiftvhdilkar
>d1bkt__ 7.3.7.2.2 Bmktx {Buthus martensii}
vginvkckhsgqclkpckdagmrfgkcingkcdctpk
>d1bkw_1 3.3.1.2.3 (1-173,276-391) p-Hydroxybenzoate hydroxylase (PHBH) {Pseudomonas fluorescens}
mktqvaiigagpsglllgqllhkagidnvilerqtpdyvlgriragvleqgmvdllreag
vdrrmardglvhegveiafagqrrridlkrlsggktvtvygqtevtrdlmeareacgatt
vyqaaevrlhdlqgerpyvtferdgerlrldcdyiagcdgfhgisrqsipaerXmqhgrl
flagdaahivpptgakglnlaasdvstlyrlllkayregrgellerysaiclrriwkaer
fswwmtsvlhrfpdtdafsqriqqteleyylgseaglatiaenyvglpye
>d1bkw_2 4.14.1.2.1 (174-275) p-Hydroxybenzoate hydroxylase, PHBH {Pseudomonas fluorescens}
lkvfervypfgwlglladtppvsheliyanhprgfalcsqrsatrsryyvqvpltekved
wsderfwtelkarlpaevaeklvtgpsleksiaplrsfvvep
>d1bkxa_ 4.117.1.1.5 cAMP-dependent PK, catalytic subunit {Mouse (Mus musculus)}
qesvkeflakakedflkkwetpsqntaqldqfdriktlgtgsfgrvmlvkhkesgnhyam
kildkqkvvklkqiehtlnekrilqavnfpflvklefsfkdnsnlymvmeyvaggemfsh
lrrigrfsepharfyaaqivltfeylhsldliyrdlkpenllidqqgyiqvtdfgfakrv
kgrtwxlcgtpeylapeiilskgynkavdwwalgvliyemaagyppffadqpiqiyekiv
sgkvrfpshfssdlkdllrnllqvdltkrfgnlkngvndiknhkwfattdwiaiyqrkve
apfipkfkgpgdtsnfddyeeeeirvxinekcgkeftef
>d1bky__ 3.56.1.4.1 Polymerase regulatory subunit VP39 {Vaccinia virus}
mdvvsldkpfmyfeeidneldyepesanevakklpyqgqlklllgelfflsklqrhgild
gatvvyigsapgthirylrdhfynlgviikwmlidgrhhdpilnglrdvtlvtrfvdeey
lrsikkqlhpskiilisdvrskrggnepstadllsnyalqnvmisilnpvasslkwrcpf
pdqwikdfyiphgnkmlqpfapsysaemrllsiytgenmrltrvtksdavnyekkmyyln
kivrnkvvvnfdypnqeydyfhmyfmlrtvycnktfpttkakvlflqqsifrflnip
>d1bkza_ 2.26.1.3.2 S-lectin, different isoforms {Human (Homo sapiens)}
snvphksslpegirpgtvlrirglvppnasrfhvnllcgeeqgsdaalhfnprldtsevv
fnskeqgswgreergpgvpfqrgqpfevliiasddgfkavvgdaqyhhfrhrlplarvrl
vevggdvqldsvrif
>d1bkzb_ 2.26.1.3.2 S-lectin, different isoforms {Human (Homo sapiens)}
snvphksslpegirpgtvlrirglvppnasrfhvnllcgeeqgsdaalhfnprldtsevv
fnskeqgswgreergpgvpfqrgqpfevliiasddgfkavvgdaqyhhfrhrlplarvrl
vevggdvqldsvrif
>d1bl0a1 1.4.1.8.1 (9-62) MarA {Escherichia coli}
daitihsildwiednlesplslekvsersgyskwhlqrmfkketghslgqyirs
>d1bl0a2 1.4.1.8.1 (63-124) MarA {Escherichia coli}
rkmteiaqklkesnepilylaerygfesqqtltrtfknyfdvpphkyrmtnmqgesrflh
pl
>d1bl3a_ 3.46.3.2.2 HIV-1 integrase, catalytic domain {Human immunodeficiency virus, type 1}
spgiwqldcthlegkvilvavhvasgyieaevipaetgqetayfllklagrwpvktvhtd
ngsnftsttvkaacwwagikqefgipynpqsqgviesmnkelkkiigqvrdqaehlktav
qmavfihnhkrkggiggysagerivdiiatdi
>d1bl3b_ 3.46.3.2.2 HIV-1 integrase, catalytic domain {Human immunodeficiency virus, type 1}
spgiwqldcthlegkvilvavhvasgyieaevipaetgqetayfllklagrwpvktvhtd
ngsnftsttvkaacwwagikqefgipynpqsqgviesmnkelkkiigqvrdqaehlktav
qmavfihnhkrkggiggysagerivdiiatdiq
>d1bl3c_ 3.46.3.2.2 HIV-1 integrase, catalytic domain {Human immunodeficiency virus, type 1}
mhgqvdcspgiwqldcthlegkvilvavhvasgyieaevipaetgqetayfllklagrwp
vktvhtdngsnftsttvkaacwwagikqefgipynpqsqgviesmnkelkkiigqvrdqa
ehlktavqmavfihnhkrkggiggysagerivdiiatdiq
>d1bl4a_ 4.23.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1bl4b_ 4.23.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1bl5__ 3.65.1.1.7 Isocitrate dehydrogenase, ICDH {Escherichia coli}
skvvvpaqgkkitlqngklnvpenpiipyiegdgigvdvtpamlkvvdaavekaykgerk
iswmeiytgekstqvygqdvwlpaetldlireyrvaikgplttpvgggirslnvalrqel
dlyiclrpvryyqgtpspvkhpeltdmvifrensediyagiewkadsadaekvikflree
mgvkkirfpehcgigikpcseegtkrlvraaieyaiandrdsvtlvhkgnimkftegafk
dwgyqlareefggelidggpwlkvknpntgkeivikdviadaflqqillrpaeydviacm
nlngdyisdalaaqvggigiapganigdecalfeathgtapkyagqdkvnpgsiilsaem
mlrhmgwteaadlivkgmegainaktvtydferlmdgakllkcsefgdaiienm
>d1bl6a_ 4.117.1.1.11 MAP kinase p38 {Human (Homo sapiens)}
erptfyrqelnktiwevperyqnlspvgsgaygsvcaafdtktglrvavkklsrpfqsii
hakrtyrelrllkhmkhenviglldvftparsleefndvylvthlmgadlnnivkcqklt
ddhvqfliyqilrglkyihsadiihrdlkpsnlavnedcelkildfglarhtddemtgyv
atrwyrapeimlnwmhynqtvdiwsvgcimaelltgrtlfpgtdhidqlklilrlvgtpg
aellkkissesarnyiqsltqmpkmnfanvfiganplavdllekmlvldsdkritaaqal
ahayfaqyhdpddepvadpydqsfesrdllidewksltydevisfvpppld
>d1bl7a_ 4.117.1.1.11 MAP kinase p38 {Human (Homo sapiens)}
erptfyrqelnktiwevperyqnlspvgsgaygsvcaafdtktglrvavkklsrpfqsii
hakrtyrelrllkhmkhenviglldvftparsleefndvylvthlmgadlnnivkcqklt
ddhvqfliyqilrglkyihsadiihrdlkpsnlavnedcelkildfglarhtddemtgyv
atrwyrapeimlnwmhynqtvdiwsvgcimaelltgrtlfpgtdhidqlklilrlvgtpg
aellkkissesarnyiqsltqmpkmnfanvfiganplavdllekmlvldsdkritaaqal
ahayfaqyhdpddepvadpydqsfesrdllidewksltydevisfvpppld
>d1bl8a_ 6.2.1.1.8 Potassium chanel protein {Streptomyces lividans}
alhwraagaatvllvivllagsylavlaergapgaqlitypralwwsvetattvgygdly
pvtlwgrcvavvvmvagitsfglvtaalatwfvgreq
>d1bl8b_ 6.2.1.1.8 Potassium chanel protein {Streptomyces lividans}
alhwraagaatvllvivllagsylavlaergapgaqlitypralwwsvetattvgygdly
pvtlwgrcvavvvmvagitsfglvtaalatwfvgreq
>d1bl8c_ 6.2.1.1.8 Potassium chanel protein {Streptomyces lividans}
alhwraagaatvllvivllagsylavlaergapgaqlitypralwwsvetattvgygdly
pvtlwgrcvavvvmvagitsfglvtaalatwfvgreq
>d1bl8d_ 6.2.1.1.8 Potassium chanel protein {Streptomyces lividans}
alhwraagaatvllvivllagsylavlaergapgaqlitypralwwsvetattvgygdly
pvtlwgrcvavvvmvagitsfglvtaalatwfvgreq
>d1bl9a1 1.3.1.2.2 (7-117) N-terminal (heme c) domain of cytochrome cd1-nitrite reductase {Pseudomonas aeruginosa}
aeqyqgaasavdpahvvrtngapdmsesefneakqiyfqrcagchgvlrkgatgkpltpd
itqqrgqqylealitygtplgmpnwgssgelskeqitlmakyiqhtppqpp
>d1bl9a2 2.61.2.1.2 (118-543) C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase {Pseudomonas aeruginosa}
ewgmpemreswkvlvkpedrpkkqlndldlpnlfsvtlrdagqialvdgdskkivkvidt
gyavhisrmsasgryllvigrdaridmidlwakeptkvaeikigiearsvesskfkgyed
rytiagaywppqfaimdgetlepkqivstrgmtvdtqtyhpeprvaaiiashehpefivn
vketgkvllvnykdidnltvtsigaapflhdggwdsshryfmtaannsnkvavidskdrr
lsalvdvgktphpgrganfvhpkygpvwstshlgdgsisligtdpknhpqyawkkvaelq
gqgggslfikthpksshlyvdttfnpdarisqsvavfdlknldakyqvlpiaewadlgeg
akrvvqpeynkrgdevwfsvwngkndssalvvvddktlklkavvkdprlitptgkfnvyn
tqhdvy
>d1bl9b1 1.3.1.2.2 (7-117) N-terminal (heme c) domain of cytochrome cd1-nitrite reductase {Pseudomonas aeruginosa}
aeqyqgaasavdpahvvrtngapdmsesefneakqiyfqrcagchgvlrkgatgkpltpd
itqqrgqqylealitygtplgmpnwgssgelskeqitlmakyiqhtppqpp
>d1bl9b2 2.61.2.1.2 (118-543) C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase {Pseudomonas aeruginosa}
ewgmpemreswkvlvkpedrpkkqlndldlpnlfsvtlrdagqialvdgdskkivkvidt
gyavhisrmsasgryllvigrdaridmidlwakeptkvaeikigiearsvesskfkgyed
rytiagaywppqfaimdgetlepkqivstrgmtvdtqtyhpeprvaaiiashehpefivn
vketgkvllvnykdidnltvtsigaapflhdggwdsshryfmtaannsnkvavidskdrr
lsalvdvgktphpgrganfvhpkygpvwstshlgdgsisligtdpknhpqyawkkvaelq
gqgggslfikthpksshlyvdttfnpdarisqsvavfdlknldakyqvlpiaewadlgeg
akrvvqpeynkrgdevwfsvwngkndssalvvvddktlklkavvkdprlitptgkfnvyn
tqhdvy
>d1bla__ 2.37.1.1.1 Basic FGF {Human (Homo sapiens)}
maegeittlpalpedggsgafppghfkdpkrlycknggfflrihpdgrvdgvreksdphi
klqlqaeergvvsikgvsanrylamkedgrllasksvtdecffferlesnnyntyrsrky
tswyvalkrtgqyklgsktgpgqkailflpmsaks
>d1blba1 2.10.1.1.5 (-6-85) beta-Crystallin {Bovine (Bos taurus)}
apqplnpkiiifeqenfqghshelngpcpnlketgvekagsvlvqagpwvgyeqanckge
qfvfekgeyprwdswtssrrtdslsslrpikvds
>d1blba2 2.10.1.1.5 (86-175) beta-Crystallin {Bovine (Bos taurus)}
qehkitlyenpnftgkkmevidddvpsfhahgyqekvssvrvqsgtwvgyqypgyrglqy
llekgdykdsgdfgapqpqvqsvrrirdmqw
>d1blbb1 2.10.1.1.5 (-2-85) beta-Crystallin {Bovine (Bos taurus)}
lnpkiiifeqenfqghshelngpcpnlketgvekagsvlvqagpwvgyeqanckgeqfvf
ekgeyprwdswtssrrtdslsslrpikvds
>d1blbb2 2.10.1.1.5 (86-175) beta-Crystallin {Bovine (Bos taurus)}
qehkitlyenpnftgkkmevidddvpsfhahgyqekvssvrvqsgtwvgyqypgyrglqy
llekgdykdsgdfgapqpqvqsvrrirdmqw
>d1blbc1 2.10.1.1.5 (-8-85) beta-Crystallin {Bovine (Bos taurus)}
agkpqplnpkiiifeqenfqghshelngpcpnlketgvekagsvlvqagpwvgyeqanck
geqfvfekgeyprwdswtssrrtdslsslrpikvds
>d1blbc2 2.10.1.1.5 (86-175) beta-Crystallin {Bovine (Bos taurus)}
qehkitlyenpnftgkkmevidddvpsfhahgyqekvssvrvqsgtwvgyqypgyrglqy
llekgdykdsgdfgapqpqvqsvrrirdmqw
>d1blbd1 2.10.1.1.5 (-4-85) beta-Crystallin {Bovine (Bos taurus)}
qplnpkiiifeqenfqghshelngpcpnlketgvekagsvlvqagpwvgyeqanckgeqf
vfekgeyprwdswtssrrtdslsslrpikvds
>d1blbd2 2.10.1.1.5 (86-175) beta-Crystallin {Bovine (Bos taurus)}
qehkitlyenpnftgkkmevidddvpsfhahgyqekvssvrvqsgtwvgyqypgyrglqy
llekgdykdsgdfgapqpqvqsvrrirdmqw
>d1blc__ 5.3.1.1.6 beta-Lactamase, class A {Staphylococcus aureus}
kelndlekkynahigvyaldtksgkevkfnsdkrfayastskainsailleqvpynklnk
kvhinkddivayspilekyvgkditlkalieasmtysdntannkiikeiggikkvkqrlk
elgdkvtnpvryeielnyyspkskkdtstpaafgktlnkliangklskenkkflldlmln
nksgdtlikdgvpkdykvadksgqaityasrndvafvypkgqsepivlviftnkdnksdk
pndklisetaksvmkef
>d1bld__ 2.37.1.1.1 Basic FGF {Human (Homo sapiens)}
maegeittlpalpedggsgafppghfkdpkrlycknggfflrihpdgrvdgvreksdphi
klqlqaeergvvsikgvsanrylamkedgrllasksvtdecffferlesnnyntyrsrky
tswyvalkrtgqyklgsktgpgqkailflpmsaks
>d1ble__ 3.31.1.1.1 Fructose permease, subunit IIb {Bacillus subtilis}
mnivlariddrfihgqiltrwikvhaadriivvsddiaqdemrktlilsvapsnvkasav
svskmakafhspryegvtamllfenpsdivslieagvpiktvnvggmrfenhrrqitksv
svteqdikafetlsdkgvklelrqlpsdasedfvqilrnvt
>d1blf_1 3.84.1.2.2 (5-333) Lactoferrin {Bovine (Bos taurus)}
nvrwctisqpewfkcrrwqwrmkklgapsitcvrrafaleciraiaekkadavtldggmv
feagrdpyklrpvaaeiygtkespqthyyavavvkkgsnfqldqlqgrkschtglgrsag
wiipmgilrpylswtesleplqgavakffsascvpcidrqaypnlcqlckgegenqcacs
srepyfgysgafkclqdgagdvafvkettvfenlpekadrdqyellclnnsrapvdafke
chlaqvpshavvarsvdgkedliwkllskaqekfgknksrsfqlfgsppgqrdllfkdsa
lgflripskvdsalylgsrylttlknlre
>d1blf_2 3.84.1.2.2 (334-689) Lactoferrin {Bovine (Bos taurus)}
taeevkarytrvvwcavgpeeqkkcqqwsqqsgqnvtcatasttddcivlvlkgeadaln
ldggyiytagkcglvpvlaenrksskhssldcvlrptegylavavvkkanegltwnslkd
kkschtavdrtagwnipmglivnqtgscafdeffsqscapgadpksrlcalcagddqgld
kcvpnskekyygytgafrclaedvgdvafvkndtvwentngestadwaknlnredfrllc
ldgtrkpvteaqschlavapnhavvsrsdraahvkqvllhqqalfgkngkncpdkfclfk
setknllfndnteclaklggrptyeeylgteyvtaianlkkcstsplleacafltr
>d1blh__ 5.3.1.1.6 beta-Lactamase, class A {Staphylococcus aureus}
kelndlekkynahigvyaldtksgkevkfnsdkrfayastskainsailleqvpynklnk
kvhinkddivayspilekyvgkditlkalieasmtysdntannkiikeiggikkvkqrlk
elgdkvtnpvryeielnyyspkskkdtstpaafgktlnkliangklskenkkflldlmln
nksgdtlikdgvpkdykvadksgqaityasrndvafvypkgqsepivlviftnkdnksdk
pndklisetaksvmkef
>d1bli_1 2.62.1.1.1 (394-483) Bacterial alpha-Amylase (BLA) {Bacillus licheniformis}
yaygaqhdyfdhhdivgwtregdssvansglaalitdgpggakrmyvgrqnagetwhdit
gnrsepvvinsagwgefhvnggsvsiyvqr
>d1bli_2 3.1.7.1.1 (3-393) Bacterial alpha-amylase (BLA) {Bacillus licheniformis}
lngtlmqyfewympndgqhwkrlqndsaylaehgitavwippaykgtsqadvgygaydly
dlgefhqkgtvrtkygtkgelqsaikslhsrdinvygdvvinhkggadatedvtavevdp
adrnrvisgehlikawthfhfpgrgstysdfkwhwyhfdgtdwdesrklnriykfqgkaw
dwevsnefgnydylmyadidydhpdvaaeikrwgtwyanelqldgfrldavkhikfsflr
dwvnhvrektgkemftvaeywsydlgalenylnktnfnhsvfdvplhyqfhaastqgggy
dmrkllngtvvskhplksvtfvdnhdtqpgqslestvqtwfkplayafiltresgypqvf
ygdmygtkgdsqreipalkhkiepilkarkq
>d1blj__ 4.72.1.1.15 P55 Blk protein tyrosine kinase {Mouse (Mus musculus)}
gsvapvetlevekwffrtisrkdaerqllapmnkagsfliresesnkgafslsvkdittq
gevvkhykirsldnggyyispritfptlqalvqhyskkgdglcqkltlpcvnla
>d1blk__ 4.72.1.1.15 P55 Blk protein tyrosine kinase {Mouse (Mus musculus)}
gsvapvetlevekwffrtisrkdaerqllapmnkagsfliresesnkgafslsvkdittq
gevvkhykirsldnggyyispritfptlqalvqhyskkgdglcqkltlpcvnla
>d1blle1 3.41.1.1.1 (1-159) Leucine aminopeptidase, N-terminal domain {Bovine (Bos taurus)}
tkglvlgiyskekeedepqftsagenfnklvsgklreilnisgpplkagktrtfyglhed
fpsvvvvglgkktagideqenwhegkeniraavaagcrqiqdleipsvevdpcgdaqaaa
egavlglyeyddlkqkrkvvvsaklhgsedqeawqrgvl
>d1blle2 3.47.4.3.1 (160-484) Leucine aminopeptidase, C-terminal domain {Bovine (Bos taurus)}
fasgqnlarrlmetpanemtptkfaeiveenlksasiktdvfirpkswieeqemgsflsv
akgseeppvfleihykgspnasepplvfvgkgitfdsggisikaaanmdlmradmggaat
icsaivsaakldlpinivglaplcenmpsgkankpgdvvrarngktiqvdntdaegrlil
adalcyahtfnpkviinaatltgamdialgsgatgvftnsswlwnklfeasietgdrvwr
mplfehytrqvidcqladvnnigkyrsagactaaaflkefvthpkwahldiagvmtnkde
vpylrkgmagrptrtlieflfrfsq
>d1blna1 2.1.1.1.125 (1-107) Immunoglobulin (variable domains of L and H chains) {Anti-p-glycoprotein Fab MRK-16 (mouse), kappa L chain}
dvlmtqtpvslsvslgdqasiscrssqsivhstgntylewylqkpgqspklliykisnrf
sgvpdrfsgsgsgtdftdgserqngvlnswtdqdskdstysmsstltltkdeyerhdsyt
ceatspivksfnrnec
>d1blna2 2.1.1.2.123 (108-214) Immunoglobulin (constant domains of L and H chains) {Anti-p-glycoprotein Fab MRK-16 (mouse), kappa L chain}
dvlmtqtpvslsvslgdqasiscrssqsivhstgntylewylqkpgqspklliykisnrf
sgvpdrfsgsgsgtdftdgserqngvlnswtdqdskdstysmsstltltkdeyerhdsyt
ceatspivksfnrnec
>d1blnb1 2.1.1.1.125 (1-113) Immunoglobulin (variable domains of L and H chains) {Anti-p-glycoprotein Fab MRK-16 (mouse), kappa L chain}
evilvesggglvkpggslklscaasgftfssytmswvrqtpekrlewvatissgggntyy
pdsvkgrftisrdnaknlqmsslrsedtalyycaryyryeawfaswgqgtlvtvsa
>d1blnb2 2.1.1.2.123 (114-227) Immunoglobulin (constant domains of L and H chains) {Anti-p-glycoprotein Fab MRK-16 (mouse), kappa L chain}
akttapsvyplapvcgdttgssvtlgclvkgyfpepvt
>d1blnc1 2.1.1.1.125 (1-107) Immunoglobulin (variable domains of L and H chains) {Anti-p-glycoprotein Fab MRK-16 (mouse), kappa L chain}
dvlmtqtpvslsvslgdqasiscrssqsivhstgntylewylqkpgqspklliykisnrf
sgvpdrfsgsgsgtdftdgserqngvlnswtdqdskdstysmsstltltkdeyerhdsyt
ceatspivksfnrnec
>d1blnc2 2.1.1.2.123 (108-214) Immunoglobulin (constant domains of L and H chains) {Anti-p-glycoprotein Fab MRK-16 (mouse), kappa L chain}
dvlmtqtpvslsvslgdqasiscrssqsivhstgntylewylqkpgqspklliykisnrf
sgvpdrfsgsgsgtdftdgserqngvlnswtdqdskdstysmsstltltkdeyerhdsyt
ceatspivksfnrnec
>d1blnd1 2.1.1.1.125 (1-113) Immunoglobulin (variable domains of L and H chains) {Anti-p-glycoprotein Fab MRK-16 (mouse), kappa L chain}
evilvesggglvkpggslklscaasgftfssytmswvrqtpekrlewvatissgggntyy
pdsvkgrftisrdnaknlqmsslrsedtalyycaryyryeawfaswgqgtlvtvsa
>d1blnd2 2.1.1.2.123 (114-227) Immunoglobulin (constant domains of L and H chains) {Anti-p-glycoprotein Fab MRK-16 (mouse), kappa L chain}
akttapsvyplapvcgdttgssvtlgclvkgyfpepvt
>d1blp__ 5.3.1.1.6 beta-Lactamase, class A {Staphylococcus aureus}
kelndlekkynahigvyaldtksgkevkfnsdkrfayastskainsailleqvpynklnk
kvhinkddivayspilekyvgkditlkalieasmtysdntannkiikeiggikkvkqrlk
elgdkvtnpvryeielnyyspkskkntstpaafgktlnkliangklskenkkflldlmln
nksgdtlikdgvpkdykvadksgqaityasrndvafvypkgqsepivlviftnkdnksdk
pndklisetaksvmkef
>d1blq__ 1.42.1.5.1 Troponin C {Chicken (Gallus gallus)}
asmtdqqaearaflseemiaefkaafdmfdadgggdistkelgtvmrmlgqnptkeelda
iieevdedgsgtidfeeflvmmvrqmkeda
>d1blr__ 2.53.1.2.9 Cellular retinoic-acid-binding protein (CRABP) {Human (Homo sapiens), CRABP-II}
pnfsgnwkiirsenfeellkvlgvnvmlrkiavaaaskpaveikqegdtfyiktsttvrt
teinfkvgeefeeqtvdgrpckslvkwesenkmvceqkllkgegpktswtreltndgeli
ltmtaddvvctrvyvre
>d1blsa_ 5.3.1.1.12 AMPC beta-Lactamase, class C {Enterobacter cloacae, P99, cephalosporinase}
pvsekqlaevvantitplmkaqsvpgmavaviyqgkphyytfgkadiaankpvtpqtlfe
lgsisktftgvlggdaiargeislddavtrywpqltgkqwqgirmldlatytagglplqv
pdevtdnasllrfyqnwqpqwkpgttrlyanasiglfgalavkpsgmpyeqamttrvlkp
lkldhtwinvpkaeeahyawgyrdgkavrvspgmldaqaygvktnvqdmanwvmanmape
nvadaslkqgialaqsrywrigsmyqglgwemlnwpveantvvegsdskvalaplpvaev
nppappvkaswvhktgstggfgsyvafipekqigivmlantsypnparveaayhileal
>d1blsb_ 5.3.1.1.12 AMPC beta-Lactamase, class C {Enterobacter cloacae, P99, cephalosporinase}
pvsekqlaevvantitplmkaqsvpgmavaviyqgkphyytfgkadiaankpvtpqtlfe
lgsisktftgvlggdaiargeislddavtrywpqltgkqwqgirmldlatytagglplqv
pdevtdnasllrfyqnwqpqwkpgttrlyanasiglfgalavkpsgmpyeqamttrvlkp
lkldhtwinvpkaeeahyawgyrdgkavrvspgmldaqaygvktnvqdmanwvmanmape
nvadaslkqgialaqsrywrigsmyqglgwemlnwpveantvvegsdskvalaplpvaev
nppappvkaswvhktgstggfgsyvafipekqigivmlantsypnparveaayhileal
>d1blu__ 4.47.1.1.5 Ferredoxin II {Cromatium vinosum}
almitdecincdvcepecpngaisqgdetyviepslctecvghyetsqcvevcpvdciik
dpsheetedelrakyeritg
>d1blv__ 4.94.1.1.2 Cytochrome b5 {Rat (Rattus norvegicus)}
dkdvkyytleeiqkhkdskstwvilhhkvydltkfleehpggeevlreqaggdatenfed
vghstdarelsktyiigelhpddrskiakpsetl
>d1blxa_ 4.117.1.1.2 Cyclin-dependent PK (different isozymes) {Mouse (Mus musculus)}
glcradqqyecvaeigegaygkvfkardlknggrfvalkrvrvqtgeegmplstirevav
lrhletfehpnvvrlfdvctvsrtdretkltlvfehvdqdlttyldkvpepgvptetikd
mmfqllrgldflhshrvvhrdlkpqnilvtssgqikladfglariysfqmaltsvvvtlw
yrapevllqssyatpvdlwsvgcifaemfrrkplfrgssdvdqlgkildviglpgeedwp
rdvalprqafhsksaqpiekfvtdidelgkdlllkcltfnpakrisaysalshpyfqdle
rcken
>d1blxb_ 1.110.2.1.3 Cell cycle inhibitor p19ink4D {Human (Homo sapiens)}
vcvgdrlsgaaargdvqevrrllhrelvhpdalnrfgktalqvmmfgspavalellkqga
spnvqdasgtspvhdaartgfldtlkvlvehgadvnaldstgslpihlaireghssvvsf
lapesdlhhrdasgltplelarqrgaqnlmdilqghmmip
>d1blz__ 2.73.3.1.1 Isopenicillin N synthase {Emericella nidulans}
skanvpkidvsplfgddqaakmrvaqqidaasrdtgffyavnhginvqrlsqktkefhms
itpeekwdlairaynkehqdqvragyylsipgkkavesfcylnpnftpdhpriqaktpth
evnvwpdetkhpgfqdfaeqyywdvfglssallkgyalalgkeenffarhfkpddtlasv
vlirypyldpypeaaiktaadgtklsfewhedvslitvlyqsnvqnlqvetaagyqdiea
ddtgylincgsymahltnnyykapihrvkwvnaerqslpffvnlgydsvidpfdprepng
ksdreplsygdylqnglvslinkngqt
>d1bm0a1 1.116.1.1.1 (5-196) Serum albumin {Human (Homo sapiens)}
sevahrfkdlgeenfkalvliafaqylqqcpfedhvklvnevtefaktcvadesaencdk
slhtlfgdklctvatlretygemadccakqepernecflqhkddnpnlprlvrpevdvmc
tafhdneetflkkylyeiarrhpyfyapellffakrykaafteccqaadkaacllpklde
lrdegkassakq
>d1bm0a2 1.116.1.1.1 (197-388) Serum albumin {Human (Homo sapiens)}
rlkcaslqkfgerafkawavarlsqrfpkaefaevsklvtdltkvhtecchgdllecadd
radlakyicenqdsissklkeccekpllekshciaevendempadlpslaadfveskdvc
knyaeakdvflgmflyeyarrhpdysvvlllrlaktyettlekccaaadphecyakvfde
fkplveepqnli
>d1bm0a3 1.116.1.1.1 (389-582) Serum albumin {Human (Homo sapiens)}
kqncelfeqlgeykfqnallvrytkkvpqvstptlvevsrnlgkvgskcckhpeakrmpc
aedylsvvlnqlcvlhektpvsdrvtkccteslvnrrpcfsalevdetyvpkefnaetft
fhadictlsekerqikkqtalvelvkhkpkatkeqlkavmddfaafvekcckaddketcf
aeegkklvaasqaa
>d1bm0b1 1.116.1.1.1 (5-196) Serum albumin {Human (Homo sapiens)}
sevahrfkdlgeenfkalvliafaqylqqcpfedhvklvnevtefaktcvadesaencdk
slhtlfgdklctvatlretygemadccakqepernecflqhkddnpnlprlvrpevdvmc
tafhdneetflkkylyeiarrhpyfyapellffakrykaafteccqaadkaacllpklde
lrdegkassakq
>d1bm0b2 1.116.1.1.1 (197-388) Serum albumin {Human (Homo sapiens)}
rlkcaslqkfgerafkawavarlsqrfpkaefaevsklvtdltkvhtecchgdllecadd
radlakyicenqdsissklkeccekpllekshciaevendempadlpslaadfveskdvc
knyaeakdvflgmflyeyarrhpdysvvlllrlaktyettlekccaaadphecyakvfde
fkplveepqnli
>d1bm0b3 1.116.1.1.1 (389-582) Serum albumin {Human (Homo sapiens)}
kqncelfeqlgeykfqnallvrytkkvpqvstptlvevsrnlgkvgskcckhpeakrmpc
aedylsvvlnqlcvlhektpvsdrvtkccteslvnrrpcfsalevdetyvpkefnaetft
fhadictlsekerqikkqtalvelvkhkpkatkeqlkavmddfaafvekcckaddketcf
aeegkklvaasqaa
>d1bm1__ 6.2.1.1.1 Bacteriorhodopsin {Halobacterium halobium}
rpewiwlalgtalmglgtlyflvkgmgvsdpdakkfyaittlvpaiaftmylsmllgygl
tmvpfggeqnpiywaryadwlfttplllldlallvdadqgtilalvgadgimigtglvga
ltkvysyrfvwwaistaamlyilyvlffgftskaesmrpevastfkvlrnvtvvlwsayp
vvwligsegagivplnietllfmvldvsakvgfglillrsr
>d1bm2a_ 4.72.1.1.7 Growth factor receptor-bound protein 2 (GRB2) {Human (Homo sapiens)}
mkphpwffgkiprakaeemlskqrhdgafliresesapgdfslllsvvvkfgndvqhfkv
lrdgagkyflwvvkfnslnelvdyhrstsvsrnqqiflrdie
>d1bm3h1 2.1.1.1.63 (1-125) Immunoglobulin (variable domains of L and H chains) {Anti-integrin Fab OPG2 (mouse), kappa L chain}
evqlvqsggglvnpgrslklscaasgftfssygmswvrqtpekrlewvaaisgggtyihy
pdsvkgrftisrdnaknnlylqmsslrsedtalyyctrhpfyrydggnyyamdhwgqgts
vtvsa
>d1bm3h2 2.1.1.2.68 (126-227) Immunoglobulin (constant domains of L and H chains) {Anti-integrin Fab OPG2 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpssprpsetvtcnvahpasstkvdkkivprdc
>d1bm3l1 2.1.1.1.63 (1-107) Immunoglobulin (variable domains of L and H chains) {Anti-integrin Fab OPG2 (mouse), kappa L chain}
delltqspatlsvtpgdsvslscrasqsisnnlhwyqqkshesprllikyasqsisgips
rfsgsgsgtdftlsinsvetedfgmyfcqqsnswpltfgggskleik
>d1bm3l2 2.1.1.2.68 (108-214) Immunoglobulin (constant domains of L and H chains) {Anti-integrin Fab OPG2 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1bm5__ 2.53.1.2.9 Cellular retinoic-acid-binding protein (CRABP) {Human (Homo sapiens), CRABP-II}
pnfsgnwkiirsenfeellkvlgvnvmlrkiavaaaskpaveikqegdtfyiktsttvrt
teinfkvgeefeeqtvdgrpckslvkwesenkmvceqkllkgegpktswtmeltndgeli
ltmtaddvvctrvyvre
>d1bm6__ 4.71.1.9.4 Stromelysin-1 (MMP-3) {Human (Homo sapiens), fibroblast}
frtfpgipkwrkthltyrivnytpdlpkdavdsavekalkvweevtpltfsrlyegeadi
misfavrehgdfypfdgpgnvlahayapgpgingdahfdddeqwtkdttgtnlflvaahe
ighslglfhsantealmyplyhsltdltrfrlsqddingiqslygpppdspet
>d1bm7a_ 2.3.3.1.1 Transthyretin (synonym: prealbumin) {Human (Homo sapiens)}
cplmvkvldavrgspainvavhvfrkaaddtwepfasgktsesgelhgltteeefvegiy
kveidtksywkalgispfhehaevvftandsgprrytiaallspysysttavvt
>d1bm7b_ 2.3.3.1.1 Transthyretin (synonym: prealbumin) {Human (Homo sapiens)}
cplmvkvldavrgspainvavhvfrkaaddtwepfasgktsesgelhgltteeefvegiy
kveidtksywkalgispfhehaevvftandsgprrytiaallspysysttavvt
>d1bm8__ 4.28.1.1.1 DNA-binding domain of Mlu1-box binding protein MBP1 {Baker's yeast (Saccharomyces cerevisiae)}
qiysarysgvdvyefihstgsimkrkkddwvnathilkaanfakakrtrilekevlketh
ekvqggfgkyqgtwvplniakqlaekfsvydqlkplfdf
>d1bm9a_ 1.4.3.7.1 Replication terminator protein (RTP) {Bacillus subtilis}
eekrsstgflvkqraflklymitmteqerlyglkllevlrsefkeigfkpnhtevyrslh
ellddgilkqikvkkegaklqevvlyqfkdyeaaklykkqlkveldrckkliekalsdnf
>d1bm9b_ 1.4.3.7.1 Replication terminator protein (RTP) {Bacillus subtilis}
eekrsstgflvkqraflklymitmteqerlyglkllevlrsefkeigfkpnhtevyrslh
ellddgilkqikvkkegaklqevvlyqfkdyeaaklykkqlkveldrckkliekalsdnf
>d1bmaa_ 2.41.1.2.15 Elastase {Porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1bmb__ 4.72.1.1.7 Growth factor receptor-bound protein 2 (GRB2) {Human (Homo sapiens)}
kphpwffgkiprakaeemlskqrhdgafliresesapgdfslllsvvvkfgndvqhfkvl
rdgagkyflwvvkfnslnelvdyhrstsvsrnqqiflrdieq
>d1bmc__ 4.128.1.1.1 Zn metallo-beta-lactamase {Bacillus cereus}
tviknetgtisisqlnknvwvhtelgsfngeavpsnglvlntskglvlvdsswddkltke
liemvekkfqkrvtdviithahadriggiktlkergikahstaltaelakkngyeeplgd
lqtvtnlkfgnmkvetfypgkghtednivvwlpqynilvggclvkstsakdlgnvadayv
newstsienvlkryrninavvpghgevgdkglllhtldllk
>d1bmda1 3.2.1.5.4 (0-154) Malate dehydrogenase {Thermus flavus}
mkapvrvavtgaagqigysllfriaagemlgkdqpvilqlleipqamkalegvvmeledc
afpllagleatddpdvafkdadyallvgaaprkagmerrdllqvngkifteqgralaeva
kkdvkvlvvgnpantnaliayknapglnprnftam
>d1bmda2 4.132.1.1.4 (155-332) Malate dehydrogenase {Thermus flavus}
trldhnrakaqlakktgtgvdrirrmtvwgnhsstmfpdlfhaevdgrpalelvdmewye
kvfiptvaqrgaaiiqargassaasaanaaiehirdwalgtpegdwvsmavpsqgeygip
egivysfpvtakdgayrvvegleinefarkrmeitaqelldemeqvkalgli
>d1bmdb1 3.2.1.5.4 (0-154) Malate dehydrogenase {Thermus flavus}
mkapvrvavtgaagqigysllfriaagemlgkdqpvilqlleipqamkalegvvmeledc
afpllagleatddpdvafkdadyallvgaaprkagmerrdllqvngkifteqgralaeva
kkdvkvlvvgnpantnaliayknapglnprnftam
>d1bmdb2 4.132.1.1.4 (155-332) Malate dehydrogenase {Thermus flavus}
trldhnrakaqlakktgtgvdrirrmtvwgnhsstmfpdlfhaevdgrpalelvdmewye
kvfiptvaqrgaaiiqargassaasaanaaiehirdwalgtpegdwvsmavpsqgeygip
egivysfpvtakdgayrvvegleinefarkrmeitaqelldemeqvkalgli
>d1bme__ 4.128.1.1.1 Zn metallo-beta-lactamase {Bacillus cereus}
tviknetgtisisqlnknvwvhtelgsfngeavpsnglvlntskglvlvdsswddkltke
liemvekkfqkrvtdviithahadriggiktlkergikahstaltaelakkngyeeplgd
lqtvtnlkfgnmkvetfypgkghtednivvwlpqynilvggclvkstsakdlgnvadayv
newstsienvlkryrninavvpghgevgdkglllhtldllk
>d1bmfa1 1.70.1.1.1 (380-510) C-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
tramkqvagtmklelaqyrevaafaqfgsdldaatqqllsrgvrltellkqgqyspmaie
eqvaviyagvrgyldklepskitkfenaflshvisqhqallgkirtdgkiseesdaklke
ivtnflagfea
>d1bmfa2 2.43.1.1.1 (24-94) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
dleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgndklik
egdivkrtgai
>d1bmfa3 3.30.1.9.2 (95-379) Central domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
vdvpvgeellgrvvdalgnaidgkgpigskarrrvglkapgiiprisvrepmqtgikavd
slvpigrgqreliigdrqtgktsiaidtiinqkrfndgtdekkklyciyvaigqkrstva
qlvkrltdadamkytivvsatasdaaplqylapysgcsmgeyfrdngkhaliiyddlskq
avayrqmslllrrppgreaypgdvfylhsrlleraakmndafgggsltalpvietqagdv
sayiptnvisitdgqifletelfykgirpainvglsvsrvgsaaq
>d1bmfb1 1.70.1.1.1 (380-510) C-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
tramkqvagtmklelaqyrevaafaqfgsdldaatqqllsrgvrltellkqgqyspmaie
eqvaviyagvrgyldklepskitkfenaflshvisqhqallgkirtdgkiseesdaklke
ivtnflagfea
>d1bmfb2 2.43.1.1.1 (24-94) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
dleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgndklik
egdivkrtgai
>d1bmfb3 3.30.1.9.2 (95-379) Central domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
vdvpvgeellgrvvdalgnaidgkgpigskarrrvglkapgiiprisvrepmqtgikavd
slvpigrgqreliigdrqtgktsiaidtiinqkrfndgtdekkklyciyvaigqkrstva
qlvkrltdadamkytivvsatasdaaplqylapysgcsmgeyfrdngkhaliiyddlskq
avayrqmslllrrppgreaypgdvfylhsrlleraakmndafgggsltalpvietqagdv
sayiptnvisitdgqifletelfykgirpainvglsvsrvgsaaq
>d1bmfc1 1.70.1.1.1 (380-510) C-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
tramkqvagtmklelaqyrevaafaqfgsdldaatqqllsrgvrltellkqgqyspmaie
eqvaviyagvrgyldklepskitkfenaflshvisqhqallgkirtdgkiseesdaklke
ivtnflagfea
>d1bmfc2 2.43.1.1.1 (19-94) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
adtsvdleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgn
dklikegdivkrtgai
>d1bmfc3 3.30.1.9.2 (95-379) Central domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
vdvpvgeellgrvvdalgnaidgkgpigskarrrvglkapgiiprisvrepmqtgikavd
slvpigrgqreliigdrqtgktsiaidtiinqkrfndgtdekkklyciyvaigqkrstva
qlvkrltdadamkytivvsatasdaaplqylapysgcsmgeyfrdngkhaliiyddlskq
avayrqmslllrrppgreaypgdvfylhsrlleraakmndafgggsltalpvietqagdv
sayiptnvisitdgqifletelfykgirpainvglsvsrvgsaaq
>d1bmfd1 1.70.1.1.1 (358-475) C-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
mdpnivgsehydvargvqkilqdykslqdiiailgmdelseedkltvsrarkiqrflsqp
fqvaevftghlgklvplketikgfqqilageydhlpeqafymvgpieeavakadklae
>d1bmfd2 2.43.1.1.1 (9-81) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1bmfd3 3.30.1.9.2 (82-357) Central domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
iripvgpetlgrimnvigepidergpiktkqfaaihaeapefvemsveqeilvtgikvvd
llapyakggkiglfggagvgktvlimelinnvakahggysvfagvgertregndlyhemi
esgvinlkdatskvalvygqmneppgararvaltgltvaeyfrdqegqdvllfidnifrf
tqagsevsallgripsavgyqptlatdmgtmqeritttkkgsitsvqaiyvpaddltdpa
pattfahldattvlsraiaelgiypavdpldstsri
>d1bmfe1 1.70.1.1.1 (358-474) C-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
mdpnivgsehydvargvqkilqdykslqdiiailgmdelseedkltvsrarkiqrflsqp
fqvaevftghlgklvplketikgfqqilageydhlpeqafymvgpieeavakadkla
>d1bmfe2 2.43.1.1.1 (9-81) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1bmfe3 3.30.1.9.2 (82-357) Central domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
iripvgpetlgrimnvigepidergpiktkqfaaihaeapefvemsveqeilvtgikvvd
llapyakggkiglfggagvgktvlimelinnvakahggysvfagvgertregndlyhemi
esgvinlkdatskvalvygqmneppgararvaltgltvaeyfrdqegqdvllfidnifrf
tqagsevsallgripsavgyqptlatdmgtmqeritttkkgsitsvqaiyvpaddltdpa
pattfahldattvlsraiaelgiypavdpldstsri
>d1bmff1 1.70.1.1.1 (358-474) C-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
mdpnivgsehydvargvqkilqdykslqdiiailgmdelseedkltvsrarkiqrflsqp
fqvaevftghlgklvplketikgfqqilageydhlpeqafymvgpieeavakadkla
>d1bmff2 2.43.1.1.1 (9-81) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1bmff3 3.30.1.9.2 (82-357) Central domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
iripvgpetlgrimnvigepidergpiktkqfaaihaeapefvemsveqeilvtgikvvd
llapyakggkiglfggagvgktvlimelinnvakahggysvfagvgertregndlyhemi
esgvinlkdatskvalvygqmneppgararvaltgltvaeyfrdqegqdvllfidnifrf
tqagsevsallgripsavgyqptlatdmgtmqeritttkkgsitsvqaiyvpaddltdpa
pattfahldattvlsraiaelgiypavdpldstsri
>d1bmfg_ 1.20.1.1.1 ATP syntase (F1-ATPase), gamma subunit {Bovine (Bos taurus)}
atlkditrrlksikniqkitksmkmvaaakyaraerelkparvygvgslalyekadiktp
edkkkhliigvssdrglcgaihssvakqmkseaanlaaagkevkiigvgdkirsilhrth
sdqflvtfkevgrrpptfgdasvialellnsgyefdegsiifnrfrsvisykteekpifs
ldtissaesmsiyddidadvlrnyqeyslaniiyyslkesttseqsarmtamdnasknas
emidkltltfnrtrqavitkelieiisgaaal
>d1bmg__ 2.1.1.2.2 Class I MHC, beta2-microglobulin and alpha-3 domain {Bovine (Bos taurus)}
iqrppkiqvysrhppedgkpnylncyvygfhppqieidllkngekikseqsdlsfskdws
fyllshaeftpnskdqyscrvkhvtleqprivkwdrdl
>d1bmia_ 4.128.1.1.2 Zn metallo-beta-lactamase {Bacteroides fragilis}
svkisddisitqlsdkvytyvslaeiegwgmvpsngmivinnhqaalldtpindaqteml
vnwvtdslhakvttfipnhwhgdcigglgylqrkgvqsyanqmtidlakekglpvpehgf
tdsltvsldgmplqcyylggghatdnivvwlptenilfggcmlkdnqatsignisdadvt
awpktldkvkakfpsaryvvpghgdyggteliehtkqivnqyiestsk
>d1bmib_ 4.128.1.1.2 Zn metallo-beta-lactamase {Bacteroides fragilis}
ksvkisddisitqlsdkvytyvslaeiegwgmvpsngmivinnhqaalldtpindaqtem
lvnwvtdslhakvttfipnhwhgdcigglgylqrkgvqsyanqmtidlakekglpvpehg
ftdsltvsldgmplqcyylggghatdnivvwlptenilfggcmlkdnqatsignisdadv
tawpktldkvkakfpsaryvvpghgdyggteliehtkqivnqyiestskp
>d1bmka_ 4.117.1.1.11 MAP kinase p38 {Human (Homo sapiens)}
erptfyrqelnktiwevperyqnlspvgsgaygsvcaafdtktghrvavkklsrpfqsii
hakrtyrelrllkhmkhenviglldvftparsleefndvylvthlmgadlnnivkcqklt
ddhvqfliyqilrglkyihsadiihrdlkpsnlavnedcelkildfglarhtddemtgyv
atrwyrapeimlnwmhynqtvdiwsvgcimaelltgrtlfpgtdhidqlklilrlvgtpg
aellkkissesarnyiqslaqmpkmnfanvfiganplavdllekmlvldsdkritaaqal
ahayfaqyhdpddepvadpydqsfesrdllidewksltydevisfvpppld
>d1bmla_ 2.41.1.2.41 Plasmin, catalytic domain {Human (Homo sapiens)}
aapsfdcgkpqvepkkcpgrvvggcvahphswpwqvslrtrfgmhfcggtlispewvlta
ahcleksprpssykvilgahqevnlephvqeievsrlfleptrkdiallklsspavitdk
vipaclpspnyvvadrtecfitgwgetqgtfgagllkeaqlpvienkvcnryeflngrvq
stelcaghlaggtdscqgdaggplvcfekdkyilqgvtswglgcarpnkpgvyvrvsrfv
twiegvmrnn
>d1bmlb_ 2.41.1.2.41 Plasmin, catalytic domain {Human (Homo sapiens)}
aapsfdcgkpqvepkkcpgrvvggcvahphswpwqvslrtrfgmhfcggtlispewvlta
ahcleksprpssykvilgahqevnlephvqeievsrlfleptrkdiallklsspavitdk
vipaclpspnyvvadrtecfitgwgetqgtfgagllkeaqlpvienkvcnryeflngrvq
stelcaghlaggtdscqgdaggplvcfekdkyilqgvtswglgcarpnkpgvyvrvsrfv
twiegvmrnn
>d1bmlc1 4.13.4.1.2 (12-148) Streptokinase {Streptoccocal bacteria (Streptococcus equisimilis)}
svnnsqlvvsvagtvegtnqdislkffeidltsrpahggkteqglspkskpfatdsgamp
hklekadllkaiqeqlianvhsnddyfevidfasdatitdrngkvyfadkdgsvtlptqp
vqefllsghvrvrpyke
>d1bmlc2 4.13.4.1.2 (149-284) Streptokinase {Streptoccocal bacteria (Streptococcus equisimilis)}
kpiqnqaksvdveytvqftplnpdddfrpglkdtkllktlaigdtitsqellaqaqsiln
kthpgytiyerdssivthdndifrtilpmdqeftyhvknreqayeinkksglneeinntd
lisekyyvlkkgekpy
>d1bmlc3 4.13.4.1.2 (285-372) Streptokinase {Streptoccocal bacteria (Streptococcus equisimilis)}
dpfdrshlklftikyvdvntnellkseqlltasernldfrdlydprdkakllynnldafg
imdytltgkvednhddtnriitvymgkr
>d1bmld1 4.13.4.1.2 (12-148) Streptokinase {Streptoccocal bacteria (Streptococcus equisimilis)}
svnnsqlvvsvagtvegtnqdislkffeidltsrpahggkteqglspkskpfatdsgamp
hklekadllkaiqeqlianvhsnddyfevidfasdatitdrngkvyfadkdgsvtlptqp
vqefllsghvrvrpyke
>d1bmld2 4.13.4.1.2 (149-284) Streptokinase {Streptoccocal bacteria (Streptococcus equisimilis)}
kpiqnqaksvdveytvqftplnpdddfrpglkdtkllktlaigdtitsqellaqaqsiln
kthpgytiyerdssivthdndifrtilpmdqeftyhvknreqayeinkksglneeinntd
lisekyyvlkkgekpy
>d1bmld3 4.13.4.1.2 (285-372) Streptokinase {Streptoccocal bacteria (Streptococcus equisimilis)}
dpfdrshlklftikyvdvntnellkseqlltasernldfrdlydprdkakllynnldafg
imdytltgkvednhddtnriitvymgkr
>e1bmm.1h 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1bmm.1l 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
geadcglrplfekksledkterellesy
>e1bmn.1h 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqf
>e1bmn.1l 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
adcglrplfekksledkterellesy
>d1bmoa1 1.42.1.3.1 (136-286) C-terminal (EC) domain of BM-40/SPARC/osteonectin {Human (Homo sapiens)}
ppcldseltefplrmrdwlknvlvtlyerdednnlltekqklrvkkihenekrleagdhp
vellardfeknynmyifpvhwqfgqldqhpidgylshtelaplraplipmehcttrffet
cdldndkyialdewagcfgikqkdidkdlvi
>d1bmoa2 7.3.11.3.1 (54-77) Domain of BM-40/SPARC/osteonectin {Human (Homo sapiens)}
pcqnhhckhgkvceldenntpmcv
>d1bmoa3 7.15.1.1.7 (78-135) Domain of BM-40/SPARC/osteonectin {Human (Homo sapiens)}
cqdptscpapigefekvcsndnktfdsschffatkctlegtkkghklhldyigpckyi
>d1bmob1 1.42.1.3.1 (136-286) C-terminal (EC) domain of BM-40/SPARC/osteonectin {Human (Homo sapiens)}
ppcldseltefplrmrdwlknvlvtlyerdednnlltekqklrvkkihenekrleagdhp
vellardfeknynmyifpvhwqfgqldqhpidgylshtelaplraplipmehcttrffet
cdldndkyialdewagcfgikqkdidkdlvi
>d1bmob2 7.3.11.3.1 (54-77) Domain of BM-40/SPARC/osteonectin {Human (Homo sapiens)}
pcqnhhckhgkvceldenntpmcv
>d1bmob3 7.15.1.1.7 (78-135) Domain of BM-40/SPARC/osteonectin {Human (Homo sapiens)}
cqdptscpapigefekvcsndnktfdsschffatkctlegtkkghklhldyigpckyi
>d1bmp__ 7.17.1.2.4 Bone morphogenetic protein-7 (BMP-7) {Human (Homo sapiens)}
qackkhelyvsfrdlgwqdwiiapegyaayycegecafplnsymnatnhaivqtlvhfin
petvpkpccaptqlnaisvlyfddssnvilkkyrnmvvracgch
>e1bmq.1a 3.13.1.1.2 Interleukin-1beta converting enzyme (a cysteine protease) {Human (Homo sapiens)}
gnvklcsleeaqriwkqksaeiypimdkssrtrlaliicneefdsiprrtgaevditgmt
mllqnlgysvdvkknltasdmtteleafahrpehktsdstflvfmshgiregicgkkhse
qvpdilqlnaifnmlntkncpslkdkpkviiiqacrgdspgvvwfkd
>e1bmq.1b 3.13.1.1.2 Interleukin-1beta converting enzyme (a cysteine protease) {Human (Homo sapiens)}
aikkahiekdfiafcsstpdnvswrhptmgsvfigrliehmqeyacscdveeifrkvrfs
feqpdgraqmpttervtltrcfylfpgh
>d1bmr__ 7.3.7.2.18 Alpha toxin {Hebraei scorpion (Leiurus quinquestriatus hebraeus), Lqh}
vrdgyiaqpencvyhcfpgssgcdtlckekggtsghcgfkvghglacwcnalpdnvgiiv
egekchs
>d1bmsa_ 4.65.1.1.1 MS2 virus coat protein {Bacteriophage MS2}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvtcsvrqssaqnrkyti
kvevpkvatqtvggvelnvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1bmsb_ 4.65.1.1.1 MS2 virus coat protein {Bacteriophage MS2}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvtcsvrqssaqnrkyti
kvevpkvatqtvggvelnvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1bmsc_ 4.65.1.1.1 MS2 virus coat protein {Bacteriophage MS2}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvtcsvrqssaqnrkyti
kvevpkvatqtvggvelnvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1bmta1 1.49.1.1.1 (651-740) Methionine synthase domain {Escherichia coli}
qaewrswevnkrleyslvkgitefieqdteearqqatrpieviegplmdgmnvvgdlfge
gkmflpqvvksarvmkqavaylepfieask
>d1bmta2 3.16.5.1.1 (741-896) Methionine synthase, C-terminal domain {Escherichia coli}
eqgktngkmviatvkgdvhdigknivgvvlqcnnyeivdlgvmvpaekilrtakevnadl
iglsglitpsldemvnvakemerqgftiplliggattskahtavkieqnysgptvyvqna
srtvgvvaallsdtqrddfvartrkeyetvriqhgr
>d1bmtb1 1.49.1.1.1 (651-740) Methionine synthase domain {Escherichia coli}
qaewrswevnkrleyslvkgitefieqdteearqqatrpieviegplmdgmnvvgdlfge
gkmflpqvvksarvmkqavaylepfieask
>d1bmtb2 3.16.5.1.1 (741-896) Methionine synthase, C-terminal domain {Escherichia coli}
eqgktngkmviatvkgdvhdigknivgvvlqcnnyeivdlgvmvpaekilrtakevnadl
iglsglitpsldemvnvakemerqgftiplliggattskahtavkieqnysgptvyvqna
srtvgvvaallsdtqrddfvartrkeyetvriqhgr
>d1bmv1_ 2.9.1.2.5 BPMV coat protein {Bean pod mottle virus}
sisqqtvwnqmatvrtplnfdsskqsfcqfsvdllgggisvdktgdwitlvqnspisnll
rvaawkkgclmvkvvmsgnaavkrsdwaslvqvfltnsnstehfdacrwtksephsweli
fpievcgpnngfemwssewanqtswhlsflvdnpkqsttfdvllgisqnfeiagntlmpa
fsvpq
>d1bmv2_ 2.9.1.2.5 BPMV coat protein {Bean pod mottle virus}
metnlfklslddvetpkgsmldlkisqskialpkntvggtilrsdllanfltegnfrasv
dlqrthrikgmikmvatvgipentgialacamnssirgrassdiyticsqdcelwnpact
kamtmsfnpnpcsdawsleflkrtgfhcdiicvtgwtatpmqdvqvtidwfissqecvpr
tycvlnpqnpfvlnrwmgkltfpqgtsrsvkrmplsigggagaksailmnmpnavlsmwr
yfvgdlvfevskmtspyikctvsffiafgnladdtinfeafphklvqfgeiqekvvlkfs
qeefltawstqvrpattlladgcpylyamvhdssvstipgdfvigvkltiienmcaygln
pgisgsrllgtipq
>d1bmw__ 2.6.3.1.1 Pollen allergen PHL P 2 {Timothy grass (Phleum pratense)}
vpkvtftvekgsnekhlavlvkyegdtmaevelrehgsdewvamtkgeggvwtfdseepl
qgpfnfrfltekgmknvfddvvpekytigatyap
>d1bmx__ 1.29.3.1.3 HIV capsid protein, dimerisation domain {Human immunodeficiency virus, type 1, HIV-1}
csildirqgpkepfrdyvdrfyktlraeqas
>d1bmy__ 1.61.4.1.1 MRF-2 DNA-binding domain {Human (Homo sapiens)}
radeqaflvalykymkerktpieripylgfkqinlwtmfqaaqklggyetitarrqwkhi
ydelggnpgstsaatctrrhyerlilpyerfikgeedkplppikprk
>d1bmza_ 2.3.3.1.1 Transthyretin (synonym: prealbumin) {Human (Homo sapiens)}
cplmvkvldavrgspainvavhvfrkaaddtwepfasgktsesgelhgltteeefvegiy
kveidtksywkalgispfhehaevvftandsgprrytiaallspysysttavvt
>d1bmzb_ 2.3.3.1.1 Transthyretin (synonym: prealbumin) {Human (Homo sapiens)}
cplmvkvldavrgspainvavhvfrkaaddtwepfasgktsesgelhgltteeefvegiy
kveidtksywkalgispfhehaevvftandsgprrytiaallspysysttavvt
>d1bn1__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasfk
>d1bn3__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasfk
>d1bn4__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasfk
>d1bn5_1 1.4.3.20.2 (375-448) Methionine aminopeptidase, insert domain {Human (Homo sapiens)}
hddmecshymknfdvghvpirlprtkhllnvinenfgtlafcrrwldrlgeskylmalkn
lcdlgivdpypplc
>d1bn5_2 4.101.1.1.4 (110-374,449-478) Methionine aminopeptidase {Human (Homo sapiens)}
kvqtdppsvpicdlypngvfpkgqeceypptqdgrtaawrttseekkaldqaseeiwndf
reaaeahrqvrkyvmswikpgmtmieicekledcsrklikenglnaglafptgcslnnca
ahytpnagdttvlqyddickidfgthisgriidcaftvtfnpkydtllkavkdatntgik
cagidvrlcdvgeaiqevmesyeveidgktyqvkpirnlnghsigqyrihagktvpiikg
geatrmeegevyaietfgstgkgvvXdikgsytaqfehtillrptckevvsrgddy
>d1bn8__ 2.71.1.1.3 Pectate lyase {Bacillus subtilis}
adlghqtlgsndgwgaystgttggskasssnvytvsnrnqlvsalgketnttpkiiyikg
tidmnvddnlkplglndykdpeydldkylkaydpstwgkkepsgtqeeararsqknqkar
vmvdipanttivgsgtnakvvggnfqiksdnviirniefqdaydyfpqwdptdgssgnwn
sqydnitinggthiwidhctfndgsrpdstspkyygrkyqhhdgqtdasnganyitmsyn
yyhdhdkssifgssdsktsddgklkitlhhnryknivqraprvrfgqvhvynnyyegsts
sssypfsyawgigksskiyaqnnvidvpglsaaktisvfsggtalydsgtllngtqinas
aanglsssvgwtpslhgsidasanvksnvinqagagkln
>d1bnb__ 7.9.1.1.2 Beta-defensin 12 {Bovine (Bos taurus)}
aplscgrnggvcipircpvpmrqigtcfgrpvkccrsw
>d1bnca1 2.74.2.1.1 (331-446) Biotin carboxylase subunit of acetyl-CoA carboxylase, C-terminal domain {Escherichia coli}
rghavecrinaedpntflpspgkitrfhapggfgvrweshiyagytvppyydsmigklic
ygenrdvaiarmknalqeliidgiktnvdlqirimndenfqhggtnihylekklgl
>d1bnca2 3.24.1.1.1 (1-114) Biotin carboxylase (BC) subunit of acetyl-CoA carboxylase {Escherichia coli}
mldkivianrgeialrilrackelgiktvavhssadrdlkhvlladetvcigpapsvksy
lnipaiisaaeitgavaihpgygflsenanfaeqversgfifigpkaetirlmg
>d1bnca3 4.115.1.2.1 (115-330) Biotin carboxylase subunit of acetyl-CoA carboxylase {Escherichia coli}
dkvsaiaamkkagvpcvpgsdgplgddmdknraiakrigypviikasgggggrgmrvvrg
daelaqsismtraeakaafsndmvymekylenprhveiqvladgqgnaiylaerdcsmqr
rhqkvveeapapgitpelrryigercakacvdigyrgagtfeflfengefyfiemntriq
vehpvtemitgvdlikeqlriaagqplsikqeevhv
>d1bncb1 2.74.2.1.1 (331-448) Biotin carboxylase subunit of acetyl-CoA carboxylase, C-terminal domain {Escherichia coli}
rghavecrinaedpntflpspgkitrfhapggfgvrweshiyagytvppyydsmigklic
ygenrdvaiarmknalqeliidgiktnvdlqirimndenfqhggtnihylekklglqe
>d1bncb2 3.24.1.1.1 (1-114) Biotin carboxylase (BC) subunit of acetyl-CoA carboxylase {Escherichia coli}
mldkivianrgeialrilrackelgiktvavhssadrdlkhvlladetvcigpapsvksy
lnipaiisaaeitgavaihpgygflsenanfaeqversgfifigpkaetirlmg
>d1bncb3 4.115.1.2.1 (115-330) Biotin carboxylase subunit of acetyl-CoA carboxylase {Escherichia coli}
dkvsaiaamkkagvpcvpgsdgplgddmdknraiakrigypviikasgggggrgmrvvrg
daelaqsismtraeakaafsndmvymekylenprhveiqvladgqgnaiylaerdcsmqr
rhqkvveeapapgitpelrryigercakacvdigyrgagtfeflfengefyfiemntriq
vehpvtemitgvdlikeqlriaagqplsikqeevhv
>d1bnda_ 7.17.1.3.1 Brain-derived neurotrophic factor/neurotrophin 3 heterodimer, BDNF/NT3 {Human (Homo sapiens)}
gqlsvcdsisewvtaadkktavdmsggtvtvlekvpvskgqlkqyfyetkcnpmgytkeg
crgidkrhwnsqcrttqsyvraltmdskkrigwrfiridtscvctltik
>d1bndb_ 7.17.1.3.1 Brain-derived neurotrophic factor/neurotrophin 3 heterodimer, BDNF/NT3 {Human (Homo sapiens)}
rgevsvcdseslwvtdkssaidirghqvtvlgeiktqnspvkqyfyetrckearpvkngc
rgiddkhwnsqcktsqtyvraltsennklvgwrwiridtscvcalsrk
>d1bnea_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnlcdvapgksiggdifsnregk
lpgksgrtwreadinytcgfrnsdrilyssdwliykttdhyqtftkir
>d1bneb_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnlcdvapgksiggdifsnregk
lpgksgrtwreadinytcgfrnsdrilyssdwliykttdhyqtftkir
>d1bnec_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnlcdvapgksiggdifsnregk
lpgksgrtwreadinytcgfrnsdrilyssdwliykttdhyqtftkir
>d1bnfa_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrcwreadinytsgfrnsdrilyscdwliykttdhyqtftkir
>d1bnfb_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
intfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregkl
pgksgrcwreadinytsgfrnsdrilyscdwliykttdhyqtftkir
>d1bnfc_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
intfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregkl
pgksgrcwreadinytsgfrnsdrilyscdwliykttdhyqtftkir
>d1bnga_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrncdrilyssdwliykttdcyqtftkir
>d1bngb_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
intfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregkl
pgksgrtwreadinytsgfrncdrilyssdwliykttdcyqtftkir
>d1bngc_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
intfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregkl
pgksgrtwreadinytsgfrncdrilyssdwliykttdcyqtftkir
>d1bnia_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1bnib_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1bnic_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1bnja_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
qvintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnreg
klpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1bnjb_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1bnjc_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
intfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregkl
pgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>e1bnk.1a 2.40.1.2.1 3-methyladenine DNA glycosylase (AAG, ANPG, MPG) {Human (Homo sapiens)}
kghltrlgleffdqpavplaraflgqvlvrrlpngtelrgriveteaylgpedeaahsrg
grqtprnrgmfmkpgtlyvyiiygmyfcmnissqgdgacvllraleplegletmrqlrst
lrkgta
>e1bnk.1b 2.40.1.2.1 3-methyladenine DNA glycosylase (AAG, ANPG, MPG) {Human (Homo sapiens)}
vlkdrelcsgpsklcqalainksfdqrdlaqdeavwler
>e1bnk.1c 2.40.1.2.1 3-methyladenine DNA glycosylase (AAG, ANPG, MPG) {Human (Homo sapiens)}
avvaaarvgvghagewarkplrfyvrgspwvsvvdrvaeqd
>d1bnla_ 4.139.1.5.1 Endostatin {Human (Homo sapiens)}
hshrdfqpvlhlvalnaplsggmrgirgadfqcfqqaravglagtfraflssrlqdlysi
vrradraavpivnlkdellfpswealfsgsegplkpgarifsfdgkdvlrhptwpqksvw
hgsdpngrrltesycetwrteapsatgqassllggrllgqsaaschhayivlciensf
>d1bnlb_ 4.139.1.5.1 Endostatin {Human (Homo sapiens)}
hshrdfqpvlhlvalnaplsggmrgirgadfqcfqqaravglagtfraflssrlqdlysi
vrradraavpivnlkdellfpswealfsgsegplkpgarifsfdgkdvlrhptwpqksvw
hgsdpngrrltesycetwrteapsatgqassllggrllgqsaaschhayivlciensf
>d1bnlc_ 4.139.1.5.1 Endostatin {Human (Homo sapiens)}
hshrdfqpvlhlvalnaplsggmrgirgadfqcfqqaravglagtfraflssrlqdlysi
vrradraavpivnlkdellfpswealfsgsegplkpgarifsfdgkdvlrhptwpqksvw
hgsdpngrrltesycetwrteapsatgqassllggrllgqsaaschhayivlciensf
>d1bnld_ 4.139.1.5.1 Endostatin {Human (Homo sapiens)}
hshrdfqpvlhlvalnaplsggmrgirgadfqcfqqaravglagtfraflssrlqdlysi
vrradraavpivnlkdellfpswealfsgsegplkpgarifsfdgkdvlrhptwpqksvw
hgsdpngrrltesycetwrteapsatgqassllggrllgqsaaschhayivlciensf
>d1bnm__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasfk
>d1bnn__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasfk
>d1bno__ 1.61.5.1.2 DNA polymerase beta, N-terminal (8 kD)-domain {Rat (Rattus norvegicus)}
mskrkapqetlnggitdmlvelanfeknvsqaihkynayrkaasviakyphkiksgaeak
klpgvgtkiaekideflatgklrklek
>d1bnp__ 1.61.5.1.2 DNA polymerase beta, N-terminal (8 kD)-domain {Rat (Rattus norvegicus)}
mskrkapqetlnggitdmlvelanfeknvsqaihkynayrkaasviakyphkiksgaeak
klpgvgtkiaekideflatgklrklek
>d1bnq__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasf
>d1bnr__ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
aqvintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnre
gklpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1bnsa_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyiakseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1bnsb_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyiakseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1bnsc_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
intfdgvadylqtyhklpdnyiakseaqalgwvaskgnladvapgksiggdifsnregkl
pgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1bnt__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasf
>d1bnu__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasf
>d1bnv__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasfk
>d1bnw__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasf
>d1bnza_ 4.8.2.1.1 DNA-binding protein {Sulfolobus solfataricus, Sso7d}
matvkfkykgeekevdiskikkvwrvgkmisftydegggktgrgavsekdapkellqmle
kqkk
>d1bo0__ 4.8.1.1.12 Monocyte chemoattractant protein-3 (MCP-3) {Human (Homo sapiens)}
qpvgintsttccyrfinkkipkqrlesyrrttsshcpreavifktkldkeicadptqkwv
qdfmkhldkktqtpkl
>d1bo1a_ 4.116.1.2.1 Phosphatidylinositol phosphate kinase IIbeta, PIPK IIbeta {Human (Homo sapiens)}
klfrasepilsvlmwgvnhtinelsnvpvpvmlmpddfkayskikvdnhlfnkenlpsrf
kfkeycpmvfrnlrerfgiddqdyqnsvtrsapinsdsqgrcgtrflttydrrfviktvs
sedvaemhnilkkyhqfivechgntllpqflgmyrltvdgvetymvvtrnvfshrltvhr
kydlkgstvareasdkekakdlptfkdndflnegqklhvgeeskknfleklkrdveflaq
lkimdysllvgihdvdraeqeemeveeraedeecendgvggnllcsygtppdspgnllsf
prffgpgefdpsvdvyamkshesspkkevyfmaiidiltpydtkkkaahaaktvkhgaga
eistvnpeqyskrfnefmsnilt
>d1bo1b_ 4.116.1.2.1 Phosphatidylinositol phosphate kinase IIbeta, PIPK IIbeta {Human (Homo sapiens)}
frasepilsvlmwgvnhtinelsnvpvpvmlmpddfkayskikvdnhlfnkenlpsrfkf
keycpmvfrnlrerfgiddqdyqnsvtrsapinsdsqgrcgtrflttydrrfviktvsse
dvaemhnilkkyhqfivechgntllpqflgmyrltvdgvetymvvtrnvfshrltvhrky
dlkgstvareasdkekakdlptfkdndflnegqklhvgeeskknfleklkrdveflaqlk
imdysllvgihdvdraeqeemeveeraedeecendgvggnllcsygtppdspgnllsfpr
ffgpgefdpsvdvyamkshesspkkevyfmaiidiltpydtkkkaahaaktvkhgagaei
stvnpeqyskrfnefmsnilt
>d1bo4a_ 4.84.1.1.2 Aminoglycoside 3-N-acetyltransferase {Serratia marcescens}
giirtcrlgpdqvksmraaldlfgrefgdvatysqhqpdsdylgnllrsktfialaafdq
eavvgalaayvlpkfeqprseiyiydlavsgehrrqgiatalinllkheanalgayviyv
qadygddpavalytklg
>d1bo4b_ 4.84.1.1.2 Aminoglycoside 3-N-acetyltransferase {Serratia marcescens}
giirtcrlgpdqvksmraaldlfgrefgdvatysqhqpdsdylgnllrsktfialaafdq
eavvgalaayvlpkfeqprseiyiydlavsgehrrqgiatalinllkheanalgayviyv
qadygddpavalytkl
>d1bo5o1 3.46.1.3.1 (2-253) Glycerol kinase {Escherichia coli}
ekkyivaldqgttssravvmdhdaniisvsqrefeqiypkpgwvehdpmeiwatqsstlv
evlakadissdqiaaigitnqrettivweketgkpiynaivwqcrrtaeicehlkrdgle
dyirsntglvidpyfsgtkvkwildhvegsrerarrgellfgtvdtwliwkmtqgrvhvt
dytnasrtmlfnihtldwddkmlevldipremlpevrrssevygqtniggkggtripisg
iagdqqaalfgq
>d1bo5o2 3.46.1.3.1 (254-499) Glycerol kinase {Escherichia coli}
lcvkegmakntygtgcfmlmntgekavksengllttiacgptgevnyalegavfmagasi
qwlrdemklindaydseyfatkvqntngvyvvpaftglgapywdpyargaifgltrgvna
nhiiratlesiayqtrdvleamqadsgirlhalrvdggavannflmqfqsdilgtrverp
evrevtalgaaylaglavgfwqnldelqekavierefrpgietternyryagwkkavkra
maweeh
>d1bo5z1 3.46.1.3.1 (2-253) Glycerol kinase {Escherichia coli}
ekkyivaldqgttssravvmdhdaniisvsqrefeqiypkpgwvehdpmeiwatqsstlv
evlakadissdqiaaigitnqrettivweketgkpiynaivwqcrrtaeicehlkrdgle
dyirsntglvidpyfsgtkvkwildhvegsrerarrgellfgtvdtwliwkmtqgrvhvt
dytnasrtmlfnihtldwddkmlevldipremlpevrrssevygqtniggkggtripisg
iagdqqaalfgq
>d1bo5z2 3.46.1.3.1 (254-499) Glycerol kinase {Escherichia coli}
lcvkegmakntygtgcfmlmntgekavksengllttiacgptgevnyalegavfmagasi
qwlrdemklindaydseyfatkvqntngvyvvpaftglgapywdpyargaifgltrgvna
nhiiratlesiayqtrdvleamqadsgirlhalrvdggavannflmqfqsdilgtrverp
evrevtalgaaylaglavgfwqnldelqekavierefrpgietternyryagwkkavkra
maweeh
>d1bo6a_ 3.30.1.3.1 Estrogen sulfotransferase {Mouse (Mus musculus)}
peyyevfgefrgvlmdkrftkywedvemflarpddlviatypksgttwisevvymiykeg
dvekckedaifnripylecrnedlingikqlkekesprivkthlppkllpasfweknckm
iylcrnakdvavsyyyfllmitsypnpksfsefvekfmqgqvpygswydhvkawwekskn
srvlfmfyedmkedirrevvklieflerkpsaelvdriiqhtsfqemknnpstnytmmpe
emmnqkvspfmrkgiigdwknhfpealrerfdehykqqmkdctvkfrme
>d1bo6b_ 3.30.1.3.1 Estrogen sulfotransferase {Mouse (Mus musculus)}
eyyevfgefrgvlmdkrftkywedvemflarpddlviatypksgttwisevvymiykegd
vekckedaifnripylecrnedlingikqlkekesprivkthlppkllpasfweknckmi
ylcrnakdvavsyyyfllmitsypnpksfsefvekfmqgqvpygswydhvkawwekskns
rvlfmfyedmkedirrevvklieflerkpsaelvdriiqhtsfqemknnpstnytmmpee
mmnqkvspfmrkgiigdwknhfpealrerfdehykqqmkdctvkfrme
>d1bo7__ 4.91.1.1.2 Thymidylate synthase {Lactobacillus casei}
mleqpyldlakkvldeghfkpdrthtgtysifghqmrfdlskgfpllttkkvpfglikse
llwflhgdtnirfllqhrnhiwdewafekwvksdeyhgpdmtdfghrsqkdpefaavyhe
emakfddrvlhddafaakygdlglvygsqwrawhtskgdtidqlgdvieqikthpysrtl
ivsawnpedvptmalppchtlyqfyvndgklslqlyqrsadiflgvpfniasyallthlv
ahecglevgefihtfgdahlyvnhldqikeqlsrtprpaptlqlnpdkhdifdfdmkdik
llnydpypaikapvav
>d1bo8__ 4.91.1.1.2 Thymidylate synthase {Lactobacillus casei}
mleqpyldlakkvldeghfkpdrthtgtysifghqmrfdlskgfpllttkkvpfglikse
llwflhgdtnirfllqhrnhiwdewafekwvksdeyhgpdmtdfghrsqkdpefaavyhe
emakfddrvlhddafaakygdlglvygsqwrawhtskgdtidqlgdvieqikthpystrl
ivsawnpedvptmalppchtlyqfyvndgklslqlyqrsadiflgvpfniasyallthlv
ahecglevgefihtfgdahlyvnhldqikeqlsrtprpaptlqlnpdkhdifdfdmkdik
llnydpypaikapvav
>d1bo9__ 1.66.1.1.1 Annexin I {Human (Homo sapiens)}
tfnpssdvaalhkaimvkgvdeatiidiltkrnnaqrqqikaaylqetgkpldetlkkal
tghleevvlallk
>d1boa_1 1.4.3.20.2 (375-448) Methionine aminopeptidase, insert domain {Human (Homo sapiens)}
hddmecshymknfdvghvpirlprtkhllnvinenfgtlafcrrwldrlgeskylmalkn
lcdlgivdpypplc
>d1boa_2 4.101.1.1.4 (110-374,449-478) Methionine aminopeptidase {Human (Homo sapiens)}
kvqtdppsvpicdlypngvfpkgqeceypptqdgrtaawrttseekkaldqaseeiwndf
reaaeahrqvrkyvmswikpgmtmieicekledcsrklikenglnaglafptgcslnnca
ahytpnagdttvlqyddickidfgthisgriidcaftvtfnpkydtllkavkdatntgik
cagidvrlcdvgeaiqevmesyeveidgktyqvkpirnlnghsigqyrihagktvpiikg
geatrmeegevyaietfgstgkgvvXdikgsytaqfehtillrptckevvsrgddy
>d1bob__ 4.84.1.1.6 Histone acetyltransferase HAT1 {Baker's yeast (Saccharomyces cerevisiae)}
fkpetwtssanealrvsivgenavqfsplftypiygdsekiygykdliihlafdsvtfkp
yvnvkysaklgddnivdvekkllsflpkddvivrdeakwvdcfaeerkthnlsdvfekvs
eyslngeefvvyksslvddfarrmhrrvqifsllfieaanyidetdpswqiywllnkktk
eligfvttykywhylgaksfdedidkkfrakisqflifppyqnkghgsclyeaiiqswle
dksiteitvedpneafddlrdrndiqrlrklgydavfqkhsdlsdeflessrkslkleer
qfnrlvemllllnns
>d1boc__ 1.42.1.1.1 Calbindin D9K {Bovine (Bos taurus)}
mkspeelkgifekyadkegdgnqlskeelklllqtefpsllkgmstldelfeeldkngdg
evsfeefqvlvkkisq
>d1bod__ 1.42.1.1.1 Calbindin D9K {Bovine (Bos taurus)}
mkspeelkgifekydkegdgqlskeelklllqtefpsllkgmstldelfeeldkngdgev
sfeefqvlvkkisq
>d1boe__ 7.3.9.1.1 Insulin-like growth factor-binding protein-5 (IGFBP-5) {Human (Homo sapiens)}
alaegqscgvytercaqglrclprqdeekplhallhgrgvclneks
>d1bof_1 1.67.1.1.2 (61-181) Transducin (alpha subunit), insertion domain {Rat (Rattus rattus)}
yseeeckqykavvysntiqsiiaiiramgrlkidfgdaaraddarqlfvlagaaeegfmt
aelagvikrlwkdsgvqacfnrsreyqlndsaayylndldriaqpnyiptqqdvlrtrvk
t
>d1bof_2 3.30.1.6.13 (10-60,182-354) Transducin (alpha subunit) {Rat (Rattus rattus)}
kaaverskmidrnlredgekaarevkllllgagesgkstivkqmkiiheagXtgivethf
tfkdlhfkmfdvggqrserkkwihcfegvtaiifcvalsdydlvlaedeemnrmhesmkl
fdsicnnkwftdtsiilflnkkdlfeekikksplticypeyagsntyeeaaayiqcqfed
lnkrkdtkeiythftcatdtknvqfvfdavtdviiknnlkdcglf
>d1boga1 2.1.1.1.126 (1-107) Immunoglobulin (variable domains of L and H chains) {Anti-p24 (HIV-1) Fab CB 4-1 (mouse), kappa L chain}
dikmtqspssmytslgervtitckasqdinsfltwflqkpgkspktliyranrlmigvps
rfsgsgsgqtysltissleyedmgiyyclqyddfpltfgagtkldlk
>d1boga2 2.1.1.2.124 (108-214) Immunoglobulin (constant domains of L and H chains) {Anti-p24 (HIV-1) Fab CB 4-1 (mouse), kappa L chain}
radaaptvsifppsseqltsgtasvvcflnnfypkeinvkwkidgserqngvldswteqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1bogb1 2.1.1.1.126 (1-112) Immunoglobulin (variable domains of L and H chains) {Anti-p24 (HIV-1) Fab CB 4-1 (mouse), kappa L chain}
qdqlqqsgaelvrpgasvklsckalgyiftdyeihwvkqtpvhglewiggihpgssgtay
nqkfkgkatltadkssttafmelssltsedsavyyctrkdywgqgtlvtvsa
>d1bogb2 2.1.1.2.124 (113-213) Immunoglobulin (constant domains of L and H chains) {Anti-p24 (HIV-1) Fab CB 4-1 (mouse), kappa L chain}
akttapsvyplvpvcggttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpallqsg
lytlsssvtvtsntwpsqtitcnvahpasstkvdkkieprv
>d1boh_1 3.68.1.1.1 (1-149) Rhodanese {Bovine (Bos taurus)}
vhqvlyralvstkwlaesvragkvgpglrvldaswyspgtrearkeylerhvpgasffdi
eecrdkaspyevmlpseagfadyvgslgisndthvvvydgddlgsfyaprvwwmfrvfgh
rtvsvlnggfrnwlkeghpvtsepsrpep
>d1boh_2 3.68.1.1.1 (150-293) Rhodanese {Bovine (Bos taurus)}
aifkatlnrsllktyeqvlenleskrfqlvdsraqgrylgtqpepdavgldsghirgsvn
mpfmnfltedgfekspeelramfeakkvdltkpliatxrkgvtachialaaylcgkpdva
iydgswfewfhrappetwvsqgkg
>d1boi_1 3.68.1.1.1 (8-149) Rhodanese {Bovine (Bos taurus)}
alvstkwlaesvragkvgpglrvldaswyspgtrearkeylerhvpgasffdieecrdka
spyevmlpseagfadyvgslgisndthvvvydgddlgsfyaprvwwmfrvfghrtvsvln
ggfrnwlkeghpvtsepsrpep
>d1boi_2 3.68.1.1.1 (150-293) Rhodanese {Bovine (Bos taurus)}
aifkatlnrsllktyeqvlenleskrfqlvdsraqgrylgtqpepdavgldsghirgsvn
mpfmnfltedgfekspeelramfeakkvdltkpliatxrkgvtachialaaylcgkpdva
iydgswfewfhrappetwvsqgkg
>d1bol__ 4.98.1.1.1 Ribonuclease Rh {Rhizopus niveus}
sscsstalscsnsansdtccspeyglvvlnmqwapgygpdnaftlhglwpdkcsgayaps
ggcdsnrasssiasvikskdsslynsmltywpsnqgnnnvfwshewskhgtcvstydpdc
ydnyeegedivdyfqkamdlrsqynvykafssngitpggtytatemqsaiesyfgakaki
dcssgtlsdvalyfyvrgrdtyvitdalstgscsgdveyptk
>e1bom.1a 7.1.1.1.6 Bombyxin-II {Silkmoth (Bombyx mori)}
givdecclrpcsvdvllsyc
>e1bom.1b 7.1.1.1.6 Bombyxin-II {Silkmoth (Bombyx mori)}
xqpqavhtycgrhlartladlcweagvd
>e1bon.1a 7.1.1.1.6 Bombyxin-II {Silkmoth (Bombyx mori)}
givdecclrpcsvdvllsyc
>e1bon.1b 7.1.1.1.6 Bombyxin-II {Silkmoth (Bombyx mori)}
xqpqavhtycgrhlartladlcweagvd
>d1boo__ 3.56.1.6.1 PvuII DNA methyltransferase {Proteus vulgaris}
nfgkkpayttsngsmyigdslellesfpeesislvmtsppfalqrkkeygnleqheyvdw
flsfakvvnkklkpdgsfvvdfggaymkgvparsiynfrvlirmidevgfflaedfywfn
psklpspiewvnkrkirvkdavntvwwfsktewpksditkvlapysdrmkkliedpdkfy
tpktrpsghdigksfskdnggsippnllqisnsesngqylancklmgikahparfpaklp
effirmltepddlvvdifggsnttglvaeresrkwisfemkpeyvaasafrfldnnisee
kitdiynrilngesldlnsi
>d1boq__ 2.41.1.1.2 alpha-Lytic protease {Lysobacter enzymogenes, 495}
anivggieysinnaslcsvgfsvtrgatkgfvtaghcgtvnatariggavvgtfaarvfp
gndrawvsltsaqtllprvangssfvtvrgsteaavgaavcrsgrttgyqcgtitaknvt
anyaegavrgltqgnacmgrgdsggswitsagqaqgvmsggnvqsngnncgipasqrssl
ferlqpilsqyglslvtg
>d1bor__ 7.37.1.1.3 Acute promyelocytic leukaemia proto-onkoprotein PML {Human (Homo sapiens)}
eeefqflrcqqcqaeakcpkllpclhtlcsgcleasgmqcpicqapwplgadtpal
>d1bosa_ 2.35.2.1.4 Verotoxin-1 {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bosb_ 2.35.2.1.4 Verotoxin-1 {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bosc_ 2.35.2.1.4 Verotoxin-1 {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bosd_ 2.35.2.1.4 Verotoxin-1 {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bose_ 2.35.2.1.4 Verotoxin-1 {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bosf_ 2.35.2.1.4 Verotoxin-1 {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bosg_ 2.35.2.1.4 Verotoxin-1 {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bosh_ 2.35.2.1.4 Verotoxin-1 {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bosi_ 2.35.2.1.4 Verotoxin-1 {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bosj_ 2.35.2.1.4 Verotoxin-1 {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bosk_ 2.35.2.1.4 Verotoxin-1 {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bosl_ 2.35.2.1.4 Verotoxin-1 {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bosm_ 2.35.2.1.4 Verotoxin-1 {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bosn_ 2.35.2.1.4 Verotoxin-1 {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1boso_ 2.35.2.1.4 Verotoxin-1 {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bosp_ 2.35.2.1.4 Verotoxin-1 {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bosq_ 2.35.2.1.4 Verotoxin-1 {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bosr_ 2.35.2.1.4 Verotoxin-1 {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1boss_ 2.35.2.1.4 Verotoxin-1 {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bost_ 2.35.2.1.4 Verotoxin-1 {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1boto1 3.46.1.3.1 (3-253) Glycerol kinase {Escherichia coli}
kkyivaldqgttssravvmdhdaniisvsqrefeqiypkpgwvehdpmeiwatqsstlve
vlakadissdqiaaigitnqrettivweketgkpiynaivwqcrrtaeicehlkrdgled
yirsntglvidpyfsgtkvkwildhvegsrerarrgellfgtvdtwliwkmtqgrvhvtd
ytnasrtmlfnihtldwddkmlevldipremlpevrrssevygqtniggkggtripisgi
agdqqaalfgq
>d1boto2 3.46.1.3.1 (254-499) Glycerol kinase {Escherichia coli}
lcvkegmakntygtgcfmlmntgekavksengllttiacgptgevnyalegavfmagasi
qwlrdemklindaydseyfatkvqntngvyvvpaftglgapywdpyargaifgltrgvna
nhiiratlesiayqtrdvleamqadsgirlhalrvdggavannflmqfqsdilgtrverp
evrevtalgaaylaglavgfwqnldelqekavierefrpgietternyryagwkkavkra
maweeh
>d1botz1 3.46.1.3.1 (2-253) Glycerol kinase {Escherichia coli}
ekkyivaldqgttssravvmdhdaniisvsqrefeqiypkpgwvehdpmeiwatqsstlv
evlakadissdqiaaigitnqrettivweketgkpiynaivwqcrrtaeicehlkrdgle
dyirsntglvidpyfsgtkvkwildhvegsrerarrgellfgtvdtwliwkmtqgrvhvt
dytnasrtmlfnihtldwddkmlevldipremlpevrrssevygqtniggkggtripisg
iagdqqaalfgq
>d1botz2 3.46.1.3.1 (254-499) Glycerol kinase {Escherichia coli}
lcvkegmakntygtgcfmlmntgekavksengllttiacgptgevnyalegavfmagasi
qwlrdemklindaydseyfatkvqntngvyvvpaftglgapywdpyargaifgltrgvna
nhiiratlesiayqtrdvleamqadsgirlhalrvdggavannflmqfqsdilgtrverp
evrevtalgaaylaglavgfwqnldelqekavierefrpgietternyryagwkkavkra
maweeh
>d1boua_ 1.85.1.1.1 LigA subunit of an aromatic-ring-opening dioxygenase LigAB {Pseudomonas paucimobilis}
idvhaylaefddipgtrvftaqrarkgynlnqfamslmkaenrerfkadesayldewnlt
paakaavlardynamideggnvyflsklfstdgksfqfaagsmtgmtqeeyaqmmidggr
spagvrsikggy
>d1boub_ 3.47.5.1.1 LigB subunit of an aromatic-ring-opening dioxygenase LigAB {Pseudomonas paucimobilis}
arvttgitsshipalgaaiqtgtsdndywgpvfkgyqpirdwikqpgnmpdvvilvyndh
asafdmniiptfaigcaetfkpadegwgprpvpdvkghpdlawhiaqslildefdmtimn
qmdvdhgctvplsmifgepeewpckvipfpvnvvtypppsgkrcfalgdsiraavesfpe
dlnvhvwgtggmshqlqgpraglinkefdlnfidklisdpeelskmphiqylresgsegv
elvmwlimrgalpekvrdlytfyhipasntalgamilqpeetagtpleprkvmsghsl
>d1bouc_ 1.85.1.1.1 LigA subunit of an aromatic-ring-opening dioxygenase LigAB {Pseudomonas paucimobilis}
idvhaylaefddipgtrvftaqrarkgynlnqfamslmkaenrerfkadesayldewnlt
paakaavlardynamideggnvyflsklfstdgksfqfaagsmtgmtqeeyaqmmidggr
spagvrsikggy
>d1boud_ 3.47.5.1.1 LigB subunit of an aromatic-ring-opening dioxygenase LigAB {Pseudomonas paucimobilis}
arvttgitsshipalgaaiqtgtsdndywgpvfkgyqpirdwikqpgnmpdvvilvyndh
asafdmniiptfaigcaetfkpadegwgprpvpdvkghpdlawhiaqslildefdmtimn
qmdvdhgctvplsmifgepeewpckvipfpvnvvtypppsgkrcfalgdsiraavesfpe
dlnvhvwgtggmshqlqgpraglinkefdlnfidklisdpeelskmphiqylresgsegv
elvmwlimrgalpekvrdlytfyhipasntalgamilqpeetagtpleprkvmsghsl
>d1bova_ 2.35.2.1.4 Verotoxin-1 {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bovb_ 2.35.2.1.4 Verotoxin-1 {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bovc_ 2.35.2.1.4 Verotoxin-1 {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bovd_ 2.35.2.1.4 Verotoxin-1 {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bove_ 2.35.2.1.4 Verotoxin-1 {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bowa_ 4.48.1.1.1 Multidrug-binding domain of transcription activator BmrR {Bacillus subtilis}
rlgevfvldeeeiriiqteaegigpenvlnasysklkkfiesadgftnnsygatfsfqpy
tsidemtyrhiftpvltnkqissitpdmeittipkgryaciaynfspehyflnlqkliky
iadrqltvvsdvyeliipihyspkkqeeyrvemkiril
>d1boxa_ 4.1.1.1.1 RNase Sa {Streptomyces aureofaciens}
vsgtvclsalppeatdtlnliasdgpfpysqdgvvfqsresvlptqsygyyheytvitpg
artrgtrriitgeatqedyytgdhyatfslidqtc
>d1boy_1 2.1.2.1.1 (3-106) Extracellular region of human tissue factor {Human (Homo sapiens)}
ttntvaaynltwkstnfktilewepkpvnqvytvqistksgdwkskcfyttdtecdltde
ivkdvkqtylarvfsypagnvestgsageplyenspeftpylet
>d1boy_2 2.1.2.1.1 (107-213) Extracellular region of human tissue factor {Human (Homo sapiens)}
nlgqptiqsfeqvgtkvnvtvedertlvrrnntflslrdvfgkdliytlyywkssssgkk
taktntneflidvdkgenycfsvqavipsrtvnrkstdspvecmgqe
>d1boza_ 3.61.1.1.6 Dihydrofolate reductases, eukaryotic type {Fungus (Pneumocystis carinii)}
vgslncivavsqnmgigkngdlpwpplrnegryfqrmtttssvegkqnlvimgkktwfsi
peknrplkgrinlvlsrelkeppqgahflsrslddalklteqpelankvdmvwivggssv
ykeamnhpghlklfvtrimqdfesdtffpeidlekykllpeypgvlsdvqeekgikykfe
vyeknd
>d1bp0__ 4.91.1.1.2 Thymidylate synthase {Lactobacillus casei}
mleqpyldlakkvldeghfkpdithtgtysifghqmrfdlskgfpllttkkvpfglikse
llwflhgdtnirfllqhrnhiwdewafekwvksdeyhgpdmtdfghrsqkdpefaavyhe
emakfddrvlhddafaakygdlglvygsqwrawhtskgdtidqlgdvieqikthpysrrl
ivsawnpedvptmalppchtlyqfyvndgklslqlyqrsadiflgvpfniasyallthlv
ahecglevgefihtfgdahlyvnhldqikeqlsrtprpaptlqlnpdkhdifdfdmkdik
llnydpypaikapvav
>d1bp1_1 4.63.1.1.1 (1-217) Bactericidal permeability-increasing protein, BPI {Human (Homo sapiens)}
vnpgvvvrisqkgldyasqqgtaalqkelkrikipdysdsfkikhlgkghysfysmdire
fqlpssqismvpnvglkfsisnanikisgkwkaqkrflkmsgnfdlsiegmsisadlklg
snptsgkptitcsscsshinsvhvhiskskvgwliqlfhkkiesalrnkmnsqvcekvtn
svssklqpyfqtlpvmtkidsvaginyglvappatta
>d1bp1_2 4.63.1.1.1 (218-456) Bactericidal permeability-increasing protein, BPI {Human (Homo sapiens)}
etldvqmkgefysenhhnpppfappvmefpaahdrmvylglsdyffntaglvyqeagvlk
mtlrddmipkeskfrlttkffgtflpevakkfpnmkiqihvsastpphlsvqptgltfyp
avdvqafavlpnsalaslfligmhttgsmevsaesnrlvgelkldrlllelkhsnigpfp
vellqdimnyivpilvlprvneklqkgfplptparvqlynvvlqphqnfllfgadvvyk
>d1bp2__ 1.123.1.2.12 Phospholipase A2 {Bovine (Bos taurus), pancreas}
alwqfngmikckipsseplldfnnygcycglggsgtpvddldrccqthdncykqakklds
ckvlvdnpytnnysyscsnneitcssennaceaficncdrnaaicfskvpynkehknldk
knc
>d1bp3a_ 1.27.1.1.6 Growth hormone, somatotropin {Human (Homo sapiens)}
fptiplsrlfdnamlrahrlhqlafdtyqefeeayipkeqkysflqnpqtslcfsesipt
psnreetqqksnlellrisllliqswlepvqflrsvfanslvygasdsnvydllkdleer
iqtlmgrledgsprtgqifkqtyskfdtnshnddallknygllycfrkdmdkvetflriv
qcrsvegscg
>d1bp3b1 2.1.2.1.10 (202-300) Prolactin receptor {Human (Homo sapiens)}
ppgkpeifkcrspnketftcwwrpgtdgglptnysltyhregetlmhecpdyitggpnsc
hfgkqytsmwrtyimmvnatnqmgssfsdelyvdvtyi
>d1bp3b2 2.1.2.1.10 (301-404) Prolactin receptor {Human (Homo sapiens)}
vqpdpplelavevkqpedrkpylwikwspptlidlktgwftllyeirlkpekaaeweihf
agqqtefkilslhpgqkylvqvrckpdhgywsawspatfiqips
>d1bp4__ 4.3.1.1.2 Papain {Papaya (Carica papaya)}
ipeyvdwrqkgavtpvknqgscgscwafsavvtiegiikirtgnlnqyseqelldcdrrs
ygcnggypwsalqlvaqygihyrntypyegvqrycrsrekgpyaaktdgvrqvqpynqga
llysianqpvsvvlqaagkdfqlyrggifvgpcgnkvdhavaavgygpnyiliknswgtg
wgengyirikrgtgnsygvcglytssfypvkn
>d1bp5a_ 3.84.1.2.8 Transferrin {Human (Homo sapiens)}
ktvrwcavseheatkcqsfrdhmksvipsdgpsvacvkkasyldciraiaaneadavtld
aglvydaylapnnlkpvvaefygskedpqtfyyavavvkkdsgfqmnqlrgkkschtglg
rsagwnipigllycdlpeprkplekavanffsgscapcadgtdfpqlcqlcpgcgcstln
qyfgysgafkclkdgagdvafvkhstifenlankadrdqyellcldntrkpvdeykdchl
aqvpshtvvarsmggkedliwellnqaqehfgkdkskefqlfssphgkdllfkdsahgfl
kvpprmdakmylgyeyvtairnlregtc
>d1bp5b_ 3.84.1.2.8 Transferrin {Human (Homo sapiens)}
ktvrwcavseheatkcqsfrdhmksvipsdgpsvacvkkasyldciraiaaneadavtld
aglvydaylapnnlkpvvaefygskedpqtfyyavavvkkdsgfqmnqlrgkkschtglg
rsagwnipigllycdlpeprkplekavanffsgscapcadgtdfpqlcqlcpgcgcstln
qyfgysgafkclkdgagdvafvkhstifenlankadrdqyellcldntrkpvdeykdchl
aqvpshtvvarsmggkedliwellnqaqehfgkdkskefqlfssphgkdllfkdsahgfl
kvpprmdakmylgyeyvtairnlregtc
>d1bp5c_ 3.84.1.2.8 Transferrin {Human (Homo sapiens)}
ktvrwcavseheatkcqsfrdhmksvipsdgpsvacvkkasyldciraiaaneadavtld
aglvydaylapnnlkpvvaefygskedpqtfyyavavvkkdsgfqmnqlrgkkschtglg
rsagwnipigllycdlpeprkplekavanffsgscapcadgtdfpqlcqlcpgcgcstln
qyfgysgafkclkdgagdvafvkhstifenlankadrdqyellcldntrkpvdeykdchl
aqvpshtvvarsmggkedliwellnqaqehfgkdkskefqlfssphgkdllfkdsahgfl
kvpprmdakmylgyeyvtairnlregtcpeaptd
>d1bp5d_ 3.84.1.2.8 Transferrin {Human (Homo sapiens)}
ktvrwcavseheatkcqsfrdhmksvipsdgpsvacvkkasyldciraiaaneadavtld
aglvydaylapnnlkpvvaefygskedpqtfyyavavvkkdsgfqmnqlrgkkschtglg
rsagwnipigllycdlpeprkplekavanffsgscapcadgtdfpqlcqlcpgcgcstln
qyfgysgafkclkdgagdvafvkhstifenlankadrdqyellcldntrkpvdeykdchl
aqvpshtvvarsmggkedliwellnqaqehfgkdkskefqlfssphgkdllfkdsahgfl
kvpprmdakmylgyeyvtairnlregtcpeaptd
>d1bp6__ 4.91.1.1.2 Thymidylate synthase {Lactobacillus casei}
mleqpyldlakkvldeghfkpdithtgtysifghqmrfdlskgfpllttkkvpfglikse
llwflhgdtnirfllqhrnhiwdewafekwvksdeyhgpdmtdfghrsqkdpefaavyhe
emakfddrvlhddafaakygdlglvygsqwrawhtskgdtidqlgdvieqikthpysrtl
ivsawnpedvptmalppchtlyqfyvndgklslqlyqrsadiflgvpfniasyallthlv
ahecglevgefihtfgdahlyvnhldqikeqlsrtprpaptlqlnpdkhdifdfdmkdik
llnydpypaikapvav
>d1bp7a_ 4.74.2.1.1 DNA endonuclease I-CreI {Chlamydomonas reinhardtii}
ntkynkefllylagfvdgdgsiiaqikpnqsykfkhqlsltfqvtqktqrrwfldklvde
igvgyvrdrgsvsdyilseikplhnfltqlqpflklkqkqanlvlkiieqlpsakespdk
flevctwvdqiaalndsktrkttsetvravld
>d1bp7b_ 4.74.2.1.1 DNA endonuclease I-CreI {Chlamydomonas reinhardtii}
ntkynkefllylagfvdgdgsiiaqikpnqsykfkhqlsltfqvtqktqrrwfldklvde
igvgyvrdrgsvsdyilseikplhnfltqlqpflklkqkqanlvlkiieqlpsakespdk
flevctwvdqiaalndsktrkttsetvravld
>d1bp7c_ 4.74.2.1.1 DNA endonuclease I-CreI {Chlamydomonas reinhardtii}
ntkynkefllylagfvdgdgsiiaqikpnqsykfkhqlsltfqvtqktqrrwfldklvde
igvgyvrdrgsvsdyilseikplhnfltqlqpflklkqkqanlvlkiieqlpsakespdk
flevctwvdqiaalndsktrkttsetvravld
>d1bp7d_ 4.74.2.1.1 DNA endonuclease I-CreI {Chlamydomonas reinhardtii}
ntkynkefllylagfvdgdgsiiaqikpnqsykfkhqlsltfqvtqktqrrwfldklvde
igvgyvrdrgsvsdyilseikplhnfltqlqpflklkqkqanlvlkiieqlpsakespdk
flevctwvdqiaalndsktrkttsetvravld
>d1bpb__ 5.9.1.1.2 DNA polymerase beta, catalytic (31 kD) fragment {Rat (Rattus norvegicus)}
ddtsssinfltrvtgigpsaarklvdegiktledlrknedklnhhqriglkyfedfekri
preemlqmqdivlnevkkldpeyiatvcgsfrrgaessgdmdvllthpnftsesskqpkl
lhrvveqlqkvrfitdtlskgetkfmgvcqlpsendeneyphrridirlipkdqyycgvl
yftgsdifnknmrahalekgftineytirplgvtgvageplpvdseqdifdyiqwryrep
kdrse
>d1bpd_1 1.61.5.1.2 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Rat (Rattus norvegicus)}
etlnggitdmlvelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d1bpd_2 5.9.1.1.2 (92-335) DNA polymerase beta, catalytic (31 kD) fragment {Rat (Rattus norvegicus)}
dtsssinfltrvtgigpsaarklvdegiktledlrknedklnhhqriglkyfedfekrip
reemlqmqdivlnevkkldpeyiatvcgsfrrgaessgdmdvllthpnftsesskqpkll
hrvveqlqkvrfitdtlskgetkfmgvcqlpsendeneyphrridirlipkdqyycgvly
ftgsdifnknmrahalekgftineytirplgvtgvageplpvdseqdifdyiqwryrepk
drse
>d1bpe_1 1.61.5.1.2 (12-91) DNA polymerase beta, N-terminal (8 kD)-domain {Rat (Rattus norvegicus)}
nggitdmlvelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtkiae
kideflatgklrklekirrd
>d1bpe_2 5.9.1.1.2 (92-335) DNA polymerase beta, catalytic (31 kD) fragment {Rat (Rattus norvegicus)}
dtsssinfltrvtgigpsaarklvdegiktledlrknedklnhhqriglkyfedfekrip
reemlqmqdivlnevkkldpeyiatvcgsfrrgaessgdmdvllthpnftsesskqpkll
hrvveqlqkvrfitdtlskgetkfmgvcqlpsendeneyphrridirlipkdqyycgvly
ftgsdifnknmrahalekgftineytirplgvtgvageplpvdseqdifdyiqwryrepk
drse
>e1bph.1a 7.1.1.1.1 Insulin {Bovine (Bos taurus)}
giveqccasvcslyqlenycn
>e1bph.1b 7.1.1.1.1 Insulin {Bovine (Bos taurus)}
fvnqhlcgshlvealylvcgergffytpka
>d1bpi__ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d1bpj__ 4.91.1.1.2 Thymidylate synthase {Lactobacillus casei}
mleqpyldlakkvldeghfkpdrthtgtysifghqmrfdlskgfpllttkkvpfglikse
llwflhgdtnirfllqhrnhiwdewafekwvksdeyhgpdmtdfghrsqkdpefaavyhe
emakfddrvlhddafaakygdlglvygsqwrawhtskgdtidqlgdvieqikthpysttl
ivsawnpedvptmalppchtlyqfyvndgklslqlyqrsadiflgvpfniasyallthlv
ahecglevgefihtfgdahlyvnhldqikeqlsrtprpaptlqlnpdkhdifdfdmkdik
llnydpypaikapvav
>e1bpl.1a 3.1.7.1.1 Bacterial alpha-amylase (BLA) {Bacillus licheniformis}
lngtlmqyfewympndgqhwkrlqndsaylaehgitavwippaykgtsqadvgygaydly
dlgefhqkgtvrtkygtkgelqsaikslhsrdinvygdvvinhkggadatedvtavevdp
adrnrvisgehlikawthfhfpgrgstysdfkwhwyhfdgtdwdesrklnriykfqgka
>e1bpl.1b 3.1.7.1.1 (193-393) Bacterial alpha-amylase (BLA) {Bacillus licheniformis}
ydylmyadidydhpdvaaeikrwgtwyanelqldgfrldavkhikfsflrdwvnhvrekt
gkemftvaeywqndlgalenylnktnfnhsvfdvplhyqfhaastqgggydmrkllnstv
vskhplkavtfvdnhdtqpgqslestvqtwfkplayafiltresgypqvfygdmygtkgd
sqreipalkhkiepilkarkq
>d1bplb1 2.62.1.1.1 (394-482) Bacterial alpha-Amylase (BLA) {Bacillus licheniformis}
yaygaqhdyfdhhdivgwtregdssvansglaalitdgpggakrmyvgrqnagetwhdit
gnrsepvvinsegwgefhvnggsvsiyvq
>d1bpm_1 3.41.1.1.1 (1-159) Leucine aminopeptidase, N-terminal domain {Bovine (Bos taurus)}
tkglvlgiyskekeedepqftsagenfnklvsgklreilnisgpplkagktrtfyglhed
fpsvvvvglgkktagideqenwhegkeniraavaagcrqiqdleipsvevdpcgdaqaaa
egavlglyeyddlkqkrkvvvsaklhgsedqeawqrgvl
>d1bpm_2 3.47.4.3.1 (160-484) Leucine aminopeptidase, C-terminal domain {Bovine (Bos taurus)}
fasgqnlarrlmetpanemtptkfaeiveenlksasiktdvfirpkswieeqemgsflsv
akgseeppvfleihykgspnasepplvfvgkgitfdsggisikaaanmdlmradmggaat
icsaivsaakldlpinivglaplcenmpsgkankpgdvvrarngktiqvdntdaegrlil
adalcyahtfnpkviinaatltgamdialgsgatgvftnsswlwnklfeasietgdrvwr
mplfehytrqvidcqladvnnigkyrsagactaaaflkefvthpkwahldiagvmtnkde
vpylrkgmagrptrtlieflfrfsq
>d1bpn_1 3.41.1.1.1 (1-159) Leucine aminopeptidase, N-terminal domain {Bovine (Bos taurus)}
tkglvlgiyskekeedepqftsagenfnklvsgklreilnisgpplkagktrtfyglhed
fpsvvvvglgkktagideqenwhegkeniraavaagcrqiqdleipsvevdpcgdaqaaa
egavlglyeyddlkqkrkvvvsaklhgsedqeawqrgvl
>d1bpn_2 3.47.4.3.1 (160-484) Leucine aminopeptidase, C-terminal domain {Bovine (Bos taurus)}
fasgqnlarrlmetpanemtptkfaeiveenlksasiktdvfirpkswieeqemgsflsv
akgseeppvfleihykgspnasepplvfvgkgitfdsggisikaaanmdlmradmggaat
icsaivsaakldlpinivglaplcenmpsgkankpgdvvrarngktiqvdntdaegrlil
adalcyahtfnpkviinaatltgamdialgsgatgvftnsswlwnklfeasietgdrvwr
mplfehytrqvidcqladvnnigkyrsagactaaaflkefvthpkwahldiagvmtnkde
vpylrkgmagrptrtlieflfrfsq
>d1bpoa1 1.110.9.1.1 (331-487) Clathrin heavy-chain linker domain {Rat (Rattus norvegicus)}
eeniipyitnvlqnpdlalrmavrnnlagaeelfarkfnalfaqgnyseaakvaanapkg
ilrtpdtirrfqsvpaqpgqtspllqyfgilldqgqlnkyeslelcrpvlqqgrkqllek
wlkedklecseelgdlvksvdptlalsvylranvpnk
>d1bpoa2 2.60.5.1.1 (1-330) Clathrin heavy-chain terminal domain {Rat (Rattus norvegicus)}
maqilpirfqehlqlqnlginpanigfstltmesdkficirekvgeqaqvviidmndpsn
pirrpisadsaimnpaskvialkagktlqifniemkskmkahtmtddvtfwkwislntva
lvtdnavyhwsmegesqpvkmfdrhsslagcqiinyrtdakqkwllltgisaqqnrvvga
mqlysvdrkvsqpieghaasfaqfkmegnaeestlfcfavrgqaggklhiievgtpptgn
qpfpkkavdvffppeaqndfpvamqisekhdvvflitkygyihlydletgtciymnrisg
etifvtapheatagiigvnrkgqvlsvcve
>d1bpob1 1.110.9.1.1 (331-493) Clathrin heavy-chain linker domain {Rat (Rattus norvegicus)}
eeniipyitnvlqnpdlalrmavrnnlagaeelfarkfnalfaqgnyseaakvaanapkg
ilrtpdtirrfqsvpaqpgqtspllqyfgilldqgqlnkyeslelcrpvlqqgrkqllek
wlkedklecseelgdlvksvdptlalsvylranvpnkviqcfa
>d1bpob2 2.60.5.1.1 (1-330) Clathrin heavy-chain terminal domain {Rat (Rattus norvegicus)}
maqilpirfqehlqlqnlginpanigfstltmesdkficirekvgeqaqvviidmndpsn
pirrpisadsaimnpaskvialkagktlqifniemkskmkahtmtddvtfwkwislntva
lvtdnavyhwsmegesqpvkmfdrhsslagcqiinyrtdakqkwllltgisaqqnrvvga
mqlysvdrkvsqpieghaasfaqfkmegnaeestlfcfavrgqaggklhiievgtpptgn
qpfpkkavdvffppeaqndfpvamqisekhdvvflitkygyihlydletgtciymnrisg
etifvtapheatagiigvnrkgqvlsvcve
>d1bpoc1 1.110.9.1.1 (331-487) Clathrin heavy-chain linker domain {Rat (Rattus norvegicus)}
eeniipyitnvlqnpdlalrmavrnnlagaeelfarkfnalfaqgnyseaakvaanapkg
ilrtpdtirrfqsvpaqpgqtspllqyfgilldqgqlnkyeslelcrpvlqqgrkqllek
wlkedklecseelgdlvksvdptlalsvylranvpnk
>d1bpoc2 2.60.5.1.1 (1-330) Clathrin heavy-chain terminal domain {Rat (Rattus norvegicus)}
maqilpirfqehlqlqnlginpanigfstltmesdkficirekvgeqaqvviidmndpsn
pirrpisadsaimnpaskvialkagktlqifniemkskmkahtmtddvtfwkwislntva
lvtdnavyhwsmegesqpvkmfdrhsslagcqiinyrtdakqkwllltgisaqqnrvvga
mqlysvdrkvsqpieghaasfaqfkmegnaeestlfcfavrgqaggklhiievgtpptgn
qpfpkkavdvffppeaqndfpvamqisekhdvvflitkygyihlydletgtciymnrisg
etifvtapheatagiigvnrkgqvlsvcve
>d1bpq__ 1.123.1.2.12 Phospholipase A2 {Bovine (Bos taurus), pancreas}
alwqfngmikckipsseplldfnnygcycglggsgtpvddldrccqthdncykqamklds
ckvlvdnpytnnysyscsnneitcssennaceaficncdrnaaicfskvpynkehknldk
knc
>d1bpr__ 5.16.1.1.1 DnaK {Escherichia coli}
siegrvkdvllldvtplslgietmggvmttliaknttiptkhsqvfstaednqsavtihv
lqgerkraadnkslgqfnldginpaprgmpqievtfdidadgilhvsakdknsgkeqkit
ikassglnedeiqkmvrdaeanaeadrkfeelvqtrnqgdhllhstrkqveea
>d1bpt__ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfanakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bpv__ 2.1.2.1.17 Type I titin module {Human (Homo sapiens)}
spidppgkpvplnitrhtvtlkwakpeytggfkitsyivekrdlpngrwlkanfsnilen
eftvsgltedaayefrviaknaagaisppsepsdaitcrddvea
>d1bpwa_ 3.71.1.1.6 Aldehyde reductase (dehydrogenase), ALDH {Baltic cod (Gadus callarias)}
aqlvdsmpsastgsvvvtddlnywggrrikskdgattepvfepatgrvlcqmvpcgaeev
dqavqsaqaaylkwskmagiersrvmleaariirerrdniaklevinngktiteaeydid
aawqcieyyaglaptlsgqhiqlpggafaytrreplgvcagilawnypfmiaawkcapal
acgnavvfkpspmtpvtgvilaeifheagvpvglvnvvqggaetgsllchhpnvakvsft
gsvptgkkvmemsaktvkhvtlelggkspllifkdcelenavrgalmanfltqgqvctng
trvfvqreimpqfleevvkrtkaivvgdplltetrmggliskpqldkvlgfvaqakkega
rvlcggepltpsdpklkngyfmspcvldncrddmtcvkeeifgpvmsvlpfdteeevlqr
annttfglasgvftrdisrahrvaanleagtcyintysispvevpfggykmsgfgrengq
atvdyysqlktvivemgdvdslf
>d1bpxa1 1.61.5.1.1 (5-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
kapqetlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpg
vgtkiaekideflatgklrklekirqd
>d1bpxa2 5.9.1.1.1 (92-335) DNA polymerase beta, catalytic (31 kD) fragment {Human (Homo sapiens)}
dtsssinfltrvsgigpsaarkfvdegiktledlrknedklnhhqriglkyfgdfekrip
reemlqmqdivlnevkkvdseyiatvcgsfrrgaessgdmdvllthpsftsestkqpkll
hqvveqlqkvhfitdtlskgetkfmgvcqlpskndekeyphrridirlipkdqyycgvly
ftgsdifnknmrahalekgftineytirplgvtgvageplpvdsekdifdyiqwkyrepk
drse
>d1bpya1 1.61.5.1.1 (10-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
tlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtki
aekideflatgklrklekirqd
>d1bpya2 5.9.1.1.1 (92-335) DNA polymerase beta, catalytic (31 kD) fragment {Human (Homo sapiens)}
dtsssinfltrvsgigpsaarkfvdegiktledlrknedklnhhqriglkyfgdfekrip
reemlqmqdivlnevkkvdseyiatvcgsfrrgaessgdmdvllthpsftsestkqpkll
hqvveqlqkvhfitdtlskgetkfmgvcqlpskndekeyphrridirlipkdqyycgvly
ftgsdifnknmrahalekgftineytirplgvtgvageplpvdsekdifdyiqwkyrepk
drse
>d1bpza1 1.61.5.1.1 (5-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
kapqetlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpg
vgtkiaekideflatgklrklekirqd
>d1bpza2 5.9.1.1.1 (92-335) DNA polymerase beta, catalytic (31 kD) fragment {Human (Homo sapiens)}
dtsssinfltrvsgigpsaarkfvdegiktledlrknedklnhhqriglkyfgdfekrip
reemlqmqdivlnevkkvdseyiatvcgsfrrgaessgdmdvllthpsftsestkqpkll
hqvveqlqkvhfitdtlskgetkfmgvcqlpskndekeyphrridirlipkdqyycgvly
ftgsdifnknmrahalekgftineytirplgvtgvageplpvdsekdifdyiqwkyrepk
drse
>d1bq0__ 1.2.2.1.2 DnaJ chaperone, N-terminal (J) domain {Escherichia coli}
akqdyyeilgvsktaeereirkaykrlamkyhpdrnqgdkeaeakfkeikeayevltdsq
kraaydqyghaafeqgg
>d1bq1a_ 4.91.1.1.1 Thymidylate synthase {Escherichia coli}
kqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihellw
flqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlkn
dpdsrriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfaiasy
allvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesifd
yrfedfeiegydphpgikapvai
>d1bq1b_ 4.91.1.1.1 Thymidylate synthase {Escherichia coli}
kqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihellw
flqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlkn
dpdsrriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfaiasy
allvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesifd
yrfedfeiegydphpgikapvai
>d1bq2__ 4.91.1.1.1 Thymidylate synthase {Escherichia coli}
mkqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihell
wflqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlk
ndpdsrriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfaias
yallvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesif
dyrfedfeiegydphpgikapvai
>d1bq3a_ 3.50.1.1.1 Phosphoglycerate mutase {Baker's yeast (Saccharomyces cerevisiae)}
pklvlvrhgqsewneknlftgwvdvklsakgqqeaaragellkekkvypdvlytsklsra
iqtanialekadrlwipvnrswrlnerhygdlqgkdkaetlkkfgeekfntyrrsfdvpp
ppidasspfsqkgderykyvdpnvlpeteslalvidrllpywqdviakdllsgktvmiaa
hgnslrglvkhlegisdadiaklniptgiplvfeldenlkpskpsyyldpeaaa
>d1bq3b_ 3.50.1.1.1 Phosphoglycerate mutase {Baker's yeast (Saccharomyces cerevisiae)}
pklvlvrhgqsewneknlftgwvdvklsakgqqeaaragellkekkvypdvlytsklsra
iqtanialekadrlwipvnrswrlnerhygdlqgkdkaetlkkfgeekfntyrrsfdvpp
ppidasspfsqkgderykyvdpnvlpeteslalvidrllpywqdviakdllsgktvmiaa
hgnslrglvkhlegisdadiaklniptgiplvfeldenlkpskpsyyldpeaaaa
>d1bq3c_ 3.50.1.1.1 Phosphoglycerate mutase {Baker's yeast (Saccharomyces cerevisiae)}
pklvlvrhgqsewneknlftgwvdvklsakgqqeaaragellkekkvypdvlytsklsra
iqtanialekadrlwipvnrswrlnerhygdlqgkdkaetlkkfgeekfntyrrsfdvpp
ppidasspfsqkgderykyvdpnvlpeteslalvidrllpywqdviakdllsgktvmiaa
hgnslrglvkhlegisdadiaklniptgiplvfeldenlkpskpsyyldpeaaaa
>d1bq3d_ 3.50.1.1.1 Phosphoglycerate mutase {Baker's yeast (Saccharomyces cerevisiae)}
pklvlvrhgqsewneknlftgwvdvklsakgqqeaaragellkekkvypdvlytsklsra
iqtanialekadrlwipvnrswrlnerhygdlqgkdkaetlkkfgeekfntyrrsfdvpp
ppidasspfsqkgderykyvdpnvlpeteslalvidrllpywqdviakdllsgktvmiaa
hgnslrglvkhlegisdadiaklniptgiplvfeldenlkpskpsyyldpeaaa
>d1bq4a_ 3.50.1.1.1 Phosphoglycerate mutase {Baker's yeast (Saccharomyces cerevisiae)}
pklvlvrhgqsewneknlftgwvdvklsakgqqeaaragellkekkvypdvlytsklsra
iqtanialekadrlwipvnrswrlnerhygdlqgkdkaetlkkfgeekfntyrrsfdvpp
ppidasspfsqkgderykyvdpnvlpeteslalvidrllpywqdviakdllsgktvmiaa
hgnslrglvkhlegisdadiaklniptgiplvfeldenlkpskpsyyldpeaaa
>d1bq4b_ 3.50.1.1.1 Phosphoglycerate mutase {Baker's yeast (Saccharomyces cerevisiae)}
pklvlvrhgqsewneknlftgwvdvklsakgqqeaaragellkekkvypdvlytsklsra
iqtanialekadrlwipvnrswrlnerhygdlqgkdkaetlkkfgeekfntyrrsfdvpp
ppidasspfsqkgderykyvdpnvlpeteslalvidrllpywqdviakdllsgktvmiaa
hgnslrglvkhlegisdadiaklniptgiplvfeldenlkpskpsyyldpeaaaa
>d1bq4c_ 3.50.1.1.1 Phosphoglycerate mutase {Baker's yeast (Saccharomyces cerevisiae)}
pklvlvrhgqsewneknlftgwvdvklsakgqqeaaragellkekkvypdvlytsklsra
iqtanialekadrlwipvnrswrlnerhygdlqgkdkaetlkkfgeekfntyrrsfdvpp
ppidasspfsqkgderykyvdpnvlpeteslalvidrllpywqdviakdllsgktvmiaa
hgnslrglvkhlegisdadiaklniptgiplvfeldenlkpskpsyyldpeaaaa
>d1bq4d_ 3.50.1.1.1 Phosphoglycerate mutase {Baker's yeast (Saccharomyces cerevisiae)}
pklvlvrhgqsewneknlftgwvdvklsakgqqeaaragellkekkvypdvlytsklsra
iqtanialekadrlwipvnrswrlnerhygdlqgkdkaetlkkfgeekfntyrrsfdvpp
ppidasspfsqkgderykyvdpnvlpeteslalvidrllpywqdviakdllsgktvmiaa
hgnslrglvkhlegisdadiaklniptgiplvfeldenlkpskpsyyldpeaaa
>d1bq5_1 2.5.1.3.3 (8-159) Nitrite reductase, NIR {Alcaligenes xylosoxidans}
dadklphtkvtlvappqvhpheqatksgpkvveftmtieekkmviddkgttlqamtfngs
mpgptlvvhegdyvqltlvnpatnamphnvdfhgatgalggakltnvnpgeqatlrfkad
rsgtfvyhcapegmvpwhvvsgmsgtlmvlpr
>d1bq5_2 2.5.1.3.3 (160-340) Nitrite reductase, NIR {Alcaligenes xylosoxidans}
dglkdpqgkplhydraytigefdlyipkgpdgkykdyatlaesygdtvqvmrtltpshiv
fngkvgaltgadaltakvgetvllihsqanrdtrphligghgdwvwetgkfanppqrdle
twfirggsagaalytfkqpgvyaylnhnlieafelgaaghikvegkwnddlmkqikapap
i
>d1bq6a_ 3.85.1.2.1 Chalcone synthase {Alfalfa (Medicago sativa)}
vsvseirkaqraegpatilaigtanpancveqstypdfyfkitnsehktelkekfqrmcd
ksmikrrymylteeilkenpnvceymapsldarqdmvvvevprlgkeaavkaikewgqpk
skithlivcttsgvdmpgadyqltkllglrpyvkrymmyqqgxfaggtvlrlakdlaenn
kgarvlvvcsevtavtfrgpsdthldslvgqalfgdgaaalivgsdpvpeiekpifemvw
taqtiapdsegaidghlreagltfhllkdvpgivsknitkalveafeplgisdynsifwi
ahpggpaildqveqklalkpekmnatrevlseygnmssacvlfildemrkkstqnglktt
geglewgvlfgfgpgltietvvlrsvai
>d1bq7a1 1.47.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1bq7a2 3.38.1.4.1 (2-64,129-187) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
qyedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyhv
nfmXfvvkslvaqqekaaadvqlrgvaamfvngkyqlnpqgmdtsnmdvfvqqyadtvky
lse
>d1bq7b1 1.47.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1bq7b2 3.38.1.4.1 (2-64,129-187) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
qyedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyhv
nfmXfvvkslvaqqekaaadvqlrgvaamfvngkyqlnpqgmdtsnmdvfvqqyadtvky
lse
>d1bq7c1 1.47.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1bq7c2 3.38.1.4.1 (2-64,129-187) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
qyedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyhv
nfmXfvvkslvaqqekaaadvqlrgvaamfvngkyqlnpqgmdtsnmdvfvqqyadtvky
lse
>d1bq7d1 1.47.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1bq7d2 3.38.1.4.1 (2-64,129-187) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
qyedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyhv
nfmXfvvkslvaqqekaaadvqlrgvaamfvngkyqlnpqgmdtsnmdvfvqqyadtvky
lse
>d1bq7e1 1.47.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1bq7e2 3.38.1.4.1 (2-64,129-187) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
qyedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyhv
nfmXfvvkslvaqqekaaadvqlrgvaamfvngkyqlnpqgmdtsnmdvfvqqyadtvky
lse
>d1bq7f1 1.47.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1bq7f2 3.38.1.4.1 (2-64,129-187) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
qyedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyhv
nfmXfvvkslvaqqekaaadvqlrgvaamfvngkyqlnpqgmdtsnmdvfvqqyadtvky
lse
>d1bq8__ 7.35.4.1.5 Rubredoxin {Pyrococcus furiosus}
makwvckicgyiydedagdpdngispgtkfeelpddwvcpicgapksefekled
>d1bq9__ 7.35.4.1.5 Rubredoxin {Pyrococcus furiosus}
akwvckicgyiydedagdpdngispgtkfeelpddwvcpicgapksefekled
>d1bqaa_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnatgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysxnfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1bqab_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnatgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysxnfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1bqb_1 1.68.1.1.4 (155-301) Aureolysin {Staphylococcus aureus}
anleykdqsgalnesfsdvfgyfvddedflmgedvytpgkegdalrsmsnpeqfgqpshm
kdyvytekdnggvhtnsgipnkaaynviqaigkskseqiyyralteyltsnsnfkdlkda
lyqaakdlyeqqtaeqvyeawnevgve
>d1bqb_2 4.71.1.2.4 (1-154) Aureolysin {Staphylococcus aureus}
aaatgtgkgvlgdtkdininsidggfsledlthqgklsaynfndqtgqatlitnedenfv
kddqragvdanyyakqtydyykntfgresydnhgspivslthvnhyggqdnrnnaawigd
kmiygdgdgrtftnlsgandvvaheithgvtqqt
>d1bqca_ 3.1.7.3.9 Beta-mannanase {Thermomonospora fusca}
atglhvkngrlyeangqefiirgvshphnwypqhtqafadikshgantvrvvlsngvrws
kngpsdvanvislckqnrlicmlevhdttgygeqsgastldqavdywielksvlqgeedy
vlinignepygndsatvaawatdtsaaiqrlraagfehtlvvdapnwgqdwtntmrnnad
qvyasdptgntvfsihmygvysqastitsylehfvnaglpliigefghdhsdgnpdedti
maeaerlklgyigwswsgngggveyldmvynfdgdnlspwgerifygpngiastakeavi
fg
>d1bqda_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnaswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnatgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysxnfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1bqdb_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnaswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnatgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysxnfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1bqg_1 3.1.10.2.1 (144-422) D-glucarate dehydratase {Pseudomonas putida}
egqqrdavemlgylfyvgdrnktdlgyrseheadnewfrlrnkealtpesvvalaeaayd
rygfkdfklkggvlrgedeiaavtalserfpdaritldpngawslkeavalcrdqhhvla
yaedpcgaengysgrevmaefrrstglrtatnmiatdwrqmghaiqlqsvdipladphfw
tmqgsvrvaqmcnewgltwgshsnnhfdislamfthvaaaapgnitaidthwiwqdgqrl
tkeplqikgglvevpkkpglgveldwdalmkahevyksm
>d1bqg_2 4.44.1.1.3 (12-143) D-glucarate dehydratase {Pseudomonas putida}
gapvitdlkvvpvaghdsmllnlsgahgplftrnililtdssghvgvgevpggegirktl
edarhllinqsignyqsllnkvrnafadrdvggrglqtfdlriavhavtavesalldllg
qhlqvpvaallg
>d1bqha1 2.1.1.2.13 (182-274) Class I MHC, beta2-microglobulin and alpha-3 domain {Mouse (Mus musculus), H-2KB}
tdspkahvthhsrpedkvtlrcwalgfypaditltwqlngeeliqdmelvetrpagdgtf
qkwasvvvplgkeqyytchvyhqglpepltlrw
>d1bqha2 4.17.1.1.20 (1-181) MHC class I, alpha-1 and alpha-2 domains {Mouse (Mus musculus), H-2KB}
gphslryfvtavsrpglgeprymevgyvddtefvrfdsdaenpryeprarwmeqegpeyw
eretqkakgneqsfrvdlrtllgyynqskggshtiqvisgcevgsdgrllrgyqqyaydg
cdyialnedlktwtaadmaalitkhkweqageaerlraylegtcvewlrrylkngnatll
r
>d1bqhb1 2.1.1.2.13 Class I MHC, beta2-microglobulin and alpha-3 domain {Mouse (Mus musculus), H-2KB}
iqktpqiqvysrhppengkpnilncyvtqfhpphieiqmlkngkkipkvemsdmsfskdw
sfyilahteftptetdtyacrvkhdsmaepktvywdrdm
>d1bqhd1 2.1.1.2.13 (182-274) Class I MHC, beta2-microglobulin and alpha-3 domain {Mouse (Mus musculus), H-2KB}
tdspkahvthhsrpedkvtlrcwalgfypaditltwqlngeeliqdmelvetrpagdgtf
qkwasvvvplgkeqyytchvyhqglpepltlrw
>d1bqhd2 4.17.1.1.20 (1-181) MHC class I, alpha-1 and alpha-2 domains {Mouse (Mus musculus), H-2KB}
gphslryfvtavsrpglgeprymevgyvddtefvrfdsdaenpryeprarwmeqegpeyw
eretqkakgneqsfrvdlrtllgyynqskggshtiqvisgcevgsdgrllrgyqqyaydg
cdyialnedlktwtaadmaalitkhkweqageaerlraylegtcvewlrrylkngnatll
r
>d1bqhg_ 2.1.1.1.4 CD8 {Mouse (Mus musculus)}
kpqapelrifpkkmdaelgqkvdlvcevlgsvsqgcswlfqnsssklpqptfvvymassh
nkitwdeklnssklfsamrdtnnkyvltlnkfskenegyyfcsvisnsvmyfssvvpvlq
kv
>d1bqhh_ 2.1.1.1.4 CD8 {Mouse (Mus musculus)}
kpqapelrifpkkmdaelgqkvdlvcevlgsvsqgcswlfqnsssklpqptfvvymassh
nkitwdeklnssklfsamrdtnnkyvltlnkfskenegyyfcsvisnsvmyfssvvpvlq
kvssa
>d1bqhi_ 2.1.1.1.4 CD8 {Mouse (Mus musculus)}
apelrifpkkmdaelgqkvdlvcevlgsvsqgcswlfqnsssklpqptfvvymasshnki
twdeklnssklfsamrdtnnkyvltlnkfskenegyyfcsvisnsvmyfssvvpvlqkvs
sa
>d1bqhk_ 2.1.1.1.4 CD8 {Mouse (Mus musculus)}
kpqapelrifpkkmdaelgqkvdlvcevlgsvsqgcswlfqnsssklpqptfvvymassh
nkitwdeklnssklfsamrdtnnkyvltlnkfskenegyyfcsvisnsvmyfssvvpvlq
kvssa
>d1bqi__ 4.3.1.1.2 Papain {Papaya (Carica papaya)}
ipeyvdwrqkgavtpvknqgscgscwafsavvtiegiikirtgnlnqyseqelldcdrrs
ygcnggypwsalqlvaqygihyrntypyegvqrycrsrekgpyaaktdgvrqvqpynqga
llysianqpvsvvlqaagkdfqlyrggifvgpcgnkvdhavaavgygpnyiliknswgtg
wgengyirikrgtgnsygvcglytssfypvkn
>d1bqk__ 2.5.1.1.18 Pseudoazurin {Achromobacter cycloclastes}
adfevhmlnkgkdgamvfepaslkvapgdtvtfiptdkghnvetikgmipdgaeafkski
nenykvtftapgvygvkctphygmgmvgvvqvgdapanleavkgaknpkkaqerldaala
algn
>d1bqlh1 2.1.1.1.45 (2-116) Immunoglobulin (variable domains of L and H chains) {Fab HyHEL-5 (mouse), kappa L chain}
vqlqqsgaelmkpgasvkisckasgytfsdywiewvkqrpghglewigeilpgsgstnyh
erfkgkatftadtssstaymqlnsltsedsgvyyclhgnydfdgwgqgttltvss
>d1bqlh2 2.1.1.2.53 (117-215) Immunoglobulin (constant domains of L and H chains) {Fab HyHEL-5 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpssprpsetvtcnvahpasstkvdkkivp
>d1bqll1 2.1.1.1.45 (1-106) Immunoglobulin (variable domains of L and H chains) {Fab HyHEL-5 (mouse), kappa L chain}
divltqspaimsaspgekvtmtcsasssvnymywyqqksgtspkrwiydtsklasgvpvr
fsgsgsgtsysltissmetedaatyycqqwgrnptfgggtkleikr
>d1bqll2 2.1.1.2.53 (107-212) Immunoglobulin (constant domains of L and H chains) {Fab HyHEL-5 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1bqly_ 4.2.1.2.5 Lysozyme {Bobwhite quail (Colinus virginianus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfnsqatnrntdgstdygvlqins
rwwcndgktpgsrnlcnipcsallssditatvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1bqma1 3.46.3.1.4 (430-556) HIV RNase H (Domain of reverse transcriptase) {Human immunodeficiency virus, type 1}
ekepivgaetfyvdgaanretklgkagyvtnkgrqkvvpltnttnqktelqaiylalqds
glevnivtdsqyalgiiqaqpdkseselvnqiieqlikkekvylawvpahkgiggneqvd
klvsagi
>d1bqma2 5.8.1.2.2 (1-429) HIV-1 reverse transcriptase {Human immunodeficiency virus, type 1, HIV-1}
pispietvpvklkpgmdgpkvkqwplteekikalveictemekegkiskigpenpyntpv
faikkkdstkwrklvdfrelnkrtqdfwevqlgiphpaglkkkksvtvldvgdayfsvpl
dedfrkytaftipsinnetpgiryqynvlpqgwkgspaifqssmtkilepfkkqnpdivi
yqymddlyvgsdleigqhrtkieelrqhllrwglttpdkkhqkeppflwmgyelhpdkwt
vqpivlpekdswtvndiqklvgklnwasqiypgikvrqlskllrgtkalteviplteeae
lelaenreilkepvhgvyydpskdliaeiqkqgqgqwtyqiyqepfknlktgkyarmrga
htndvkqlteavqkittesiviwgktpkfklpiqketwetwwteywqatwipewefvntp
plvklwyql
>d1bqmb1 5.8.1.2.2 HIV-1 reverse transcriptase {Human immunodeficiency virus, type 1, HIV-1}
pispietvpvklkpgmdgpkvkqwplteekikalveictemekegkiskigpenpyntpv
faikkkdstkwrklvdfrelnkrtqdfwevqlgiphpaglkkkksvtvldvgdayfsvpl
dedfrkytaftipsinnetpgiryqynvlpqgwkgspaifqssmtkilepfkkqnpdivi
yqymddlyvgsdleigqhrtkieelrqhllrwglttpdkkhqkeppflwmgyelhpdkwt
vqpivlpekdswtvndiqklvgklnwasqiypgikvrqlskllrgtkalteviplteeae
lelaenreilkepvhgvyydpskdliaeiqkqgqgqwtyqiyqepfknlktgkyarmrga
htndvkqlteavqkittesiviwgktpkfklpiqketwetwwteywqatwipewefvntp
plvklwyqle
>d1bqna1 3.46.3.1.4 (430-558) HIV RNase H (Domain of reverse transcriptase) {Human immunodeficiency virus, type 1}
ekepivgaetfyvdgaanretklgkagyvtnkgrqkvvpltnttnqktelqaiylalqds
glevnivtdsqyalgiiqaqpdkseselvnqiieqlikkekvylawvpahkgiggnqqvd
klvsagirk
>d1bqna2 5.8.1.2.2 (1-429) HIV-1 reverse transcriptase {Human immunodeficiency virus, type 1, HIV-1}
pispietvpvklkpgmdgpkvkqwplteekikalveictemekegkiskigpenpyntpv
faikkkdstkwrklvdfrelnkrtqdfwevqlgiphpaglkkkksvtvldvgdayfsvpl
dedfrkytaftipsinnetpgiryqynvlpqgwkgspaifqssmtkilepfkkqnpdivi
yqymddllvgsdleigqhrtkieelrqhllrwglttpdkkhqkeppflwmgyelhpdkwt
vqpivlpqkdswtvndiqklvgklnwasqiypgikvrqlskllrgtkalteviplteeae
lelaenreilkepvhgvyydpskdliaeiqkqgqgqwtyqiyqepfknlktgkyarmrga
htndvkqlteavqkittesiviwgktpkfklpiqketwetwwteywqatwipewefvntp
plvklwyql
>d1bqnb1 5.8.1.2.2 HIV-1 reverse transcriptase {Human immunodeficiency virus, type 1, HIV-1}
pispietvpvklkpgmdgpkvkqwplteekikalveictemekegkiskigpenpyntpv
faikkkdstkwrklvdfrelnkrtqdfwevqlgiphpaglkkkksvtvldvgdayfsvpl
dedfrkytaftipsinnetpgiryqynvlpqgwkgspaifqssmtkilepfkkqnpdivi
yqymddllvgsdleigqhrtkieelrqhllrwglttpdkkhqkeppflwmgyelhpdkwt
vepivlpekdswtvndiqklvgklnwasqiypgikvralskllrgtkalteviplteeae
lelaenreilkepvhgvyydpskdliaeiqkqgqgqwtyqiyqepfknlktgkyarmrga
htndvkqlteavqkittesiviwgktpkfklpiqketwetwwteywqatwipewefvntp
plvklwyqle
>d1bqoa_ 4.71.1.9.4 Stromelysin-1 (MMP-3) {Human (Homo sapiens), fibroblast}
frtfpgipkwrkthltyrivnytpdlpkdavdsavekalkvweevtpltfsrlyegeadi
misfavrehgdfypfdgpgnvlahayapgpgingdahfdddeqwtkdttgtnlflvaahe
ighslglfhsantealmyplyhsltdltrfrlsqddingiqslygpppd
>d1bqob_ 4.71.1.9.4 Stromelysin-1 (MMP-3) {Human (Homo sapiens), fibroblast}
frtfpgipkwrkthltyrivnytpdlpkdavdsavekalkvweevtpltfsrlyegeadi
misfavrehgdfypfdgpgnvlahayapgpgingdahfdddeqwtkdttgtnlflvaahe
ighslglfhsantealmyplyhsltdltrfrlsqddingiqslygpppdspet
>e1bqp.1a 2.26.1.1.3 Lectin {Garden pea (Pisum sativum)}
tettsflitkfspdqqnlifqgdgyttkekltltkavkntvgralysspihiwdretgnv
anfvtsftfvinapnsynvadgftffiapvdtkpqtgggylgvfnsaeydkttqtvavef
dtfynaawdpsnrdrhigidvnsiksvntkswklqngeeanvviafnaatnvltvsltyp
n
>e1bqp.1b 2.26.1.1.3 Lectin {Garden pea (Pisum sativum)}
vtsytlsdvvslkdvvpewvrigfsattgaeyaahevlswsfhsels
>e1bqp.2c 2.26.1.1.3 Lectin {Garden pea (Pisum sativum)}
tettsflitkfspdqqnlifqgdgyttkekltltkavkntvgralysspihiwdretgnv
anfvtsftfvinapnsynvadgftffiapvdtkpqtgggylgvfnsaeydkttqtvavef
dtfynaawdpsnrdrhigidvnsiksvntkswklqngeeanvviafnaatnvltvsltyp
n
>e1bqp.2d 2.26.1.1.3 Lectin {Garden pea (Pisum sativum)}
vtsytlsdvvslkdvvpewvrigfsattgaeyaahevlswsfhsels
>d1bqqm_ 4.71.1.9.8 Membrane-type matrix metalloproteinase (CDMT1-MMP) {Human (Homo sapiens)}
iqglkwqhneitfciqnytpkvgeyatyeairkafrvwesatplrfrevpyayireghek
qadimiffaegfhgdstpfdgeggflahayfpgpniggdthfdsaepwtvrnedlngndi
flvavhelghalglehssdpsaimapfyqwmdtenfvlpdddrrgiqqlygges
>d1bqqt_ 2.35.3.1.3 TIMP-2 {Bovine (Bos taurus)}
cscspvhpqqafcnadivirakavnkkevdsgndiygnpikriqyeikqikmfkgpdqdi
efiytapaaavcgvsldiggkkeyliagkaegngnmhitlcdfivpwdtlsatqkkslnh
ryqmgceckitrcpmipcyisspdeclwmdwvtekninghqakffacikrsdgscawyrg
aapp
>d1bqr__ 2.5.1.1.18 Pseudoazurin {Achromobacter cycloclastes}
adfevhmlnkgkdgamvfepaslkvapgdtvtfiptdkghnvetikgmipdgaeafkski
nenykvtftapgvygvkctphygmgmvgvvqvgdapanleavkgaknpkkaqerldaala
algn
>d1bqsa1 2.1.1.4.5 (1-90) Mucosal addressin cell adhesion molecule-1 (MADCAM-1) {Human (Homo sapiens)}
vkplqveppepvvavalgasrqltcrlacadrgasvqwrgldtslgavqsdtgrsvltvr
naslsaagtrvcvgscggrtfqhtvqllvy
>d1bqsa2 2.1.1.4.5 (91-209) Mucosal addressin cell adhesion molecule-1 (MADCAM-1) {Human (Homo sapiens)}
afpnqltvspaalvpgdpevactahkvtpvdpnalsfsllvggqelegaqalgpevqeee
eepqgdedvlfrvterwrlpplgtpvppalycqatmrlpglelshrqaipvlhsptspe
>d1bqt__ 7.1.1.1.5 Insulin-like growth factor {Human (Homo sapiens)}
gpetlcgaelvdalqfvcgdrgfyfnkptgygsssrrapqtgivdeccfrscdlrrlemy
caplkpaksa
>d1bqua1 2.1.2.1.13 (5-99) Cytokyne receptor gp130 cytokine-binding domains {Human (Homo sapiens)}
glppekpknlscivnegkkmrcewdggrethletnftlksewathkfadckakaatptsc
tvdystvyfvnievwveaenalgkvtsdhinfdpv
>d1bqua2 2.1.2.1.13 (100-214) Cytokyne receptor gp130 cytokine-binding domains {Human (Homo sapiens)}
ykvkpnpphnlsvinseelssilkltwtnpsiksviilkyniqyrtkdastwsqippedt
astrssftvqdlkpfteyvfrircmkedgkgywsdwseeasgityedraaaeaaa
>d1bqub1 2.1.2.1.13 (1-99) Cytokyne receptor gp130 cytokine-binding domains {Human (Homo sapiens)}
pgssglppekpknlscivnegkkmrcewdggrethletnftlksewathkfadckakadt
ptsctvdystvyfvnievwveaenalgkvtsdhinfdpv
>d1bqub2 2.1.2.1.13 (100-215) Cytokyne receptor gp130 cytokine-binding domains {Human (Homo sapiens)}
ykvkpnpphnlsvinseelssilkltwtnpsiksviilkyniqyrtkdastwsqippedt
astrssftvqdlkpfteyvfrircmkedgkgywsdwseeasgityedraaaeaaaa
>d1bqv__ 1.61.1.1.1 Ets-1 transcription factor pointed domain {Mouse (Mus musculus)}
mecadvplltpsskemmsqalkatfsgftkeqqrlgipkdprqwtethvrdwvmwavnef
slkgvdfqkfcmsgaalcalgkecflelapdfvgdilwehleilqkedvk
>d1bqx__ 4.47.1.2.2 Ferredoxin {Bacillus schlegelii}
ayvitepcigtkcascvevcpvdcihegedqyyidpdvcidcgaceavcpvsaiyhedfv
peewksyiqknrdffkk
>d1bqya_ 2.41.1.2.31 Plasminogen activator from snake venom, TSV-PA {Chinese green tree viper (Trimeresurus stejnejeri)}
vfggdecninehrslvvlfnsngflcggtlinqdwvvtaahcdsnnfqllfgvhskkiln
edeqtrdpkekffcpnrkkddevdkdimlikldssvsnsehiaplslpssppsvgsvcri
mgwgktiptkeiypdvphcaninildhavcrtayswrqvanttlcagilqggrdtchfds
ggplicngifqgivswgghpcgqpgepgvytkvfdyldwiksiiagnkdatcpp
>d1bqyb_ 2.41.1.2.31 Plasminogen activator from snake venom, TSV-PA {Chinese green tree viper (Trimeresurus stejnejeri)}
vfggdecninehrslvvlfnsngflcggtlinqdwvvtaahcdsnnfqllfgvhskkiln
edeqtrdpkekffcpnrkkddevdkdimlikldssvsnsehiaplslpssppsvgsvcri
mgwgktiptkeiypdvphcaninildhavcrtayswrqvanttlcagilqggrdtchfds
ggplicngifqgivswgghpcgqpgepgvytkvfdyldwiksiiagnkdatcpp
>d1bqz__ 1.2.2.1.2 DnaJ chaperone, N-terminal (J) domain {Escherichia coli}
akqdyyeilgvsktaeereirkaykrlamkyhpdrnqgdkeaeakfkeikeayevltdsq
kraaydqyghaafeqgg
>d1br0__ 1.7.2.1.1 Syntaxin 1-A N-terminal domain {Rat (Rattus norvegicus)}
drfmdeffeqveeirgfidkiaenveevkrkhsailaspnpdektkeeleelmsdikkta
nkvrsklksieqsieqeeglnrssadlrirktqhstlsrkfvevmseynatqsdyrersk
>d1br1a1 2.30.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br1a2 3.30.1.7.1 (2-33,80-821) Myosin S1, motor domain {Chicken (Gallus gallus), pectoral muscle}
aqkplsddekflfvdknfvnnplaqadwsakkXppkfskvedmaeltclneasvlhnlre
ryfsgliytysglfcvvinpykqlpiysekiidmykgkkrhempphiyaiadtayrsmlq
dredqsilctgesgagktentkkviqylavvasshkgkkdtsitqgpsfsygelekqllq
anpileafgnaktvkndnssrfgkfirinfdvtgyivganietylleksrairqakdert
fhifyyliagaseqmrndlllegfnnytflsnghvpipaqqddemfqetleamtimgfte
eeqtsilrvvssvlqlgnivfkkerntdqasmpdntaaqkvchlmginvtdftrsiltpr
ikvgrdvvqkaqtkeqadfaiealakakferlfrwiltrvnkaldktkrqgasflgildi
agfeifeinsfeqlcinytneklqqlfnhtmfileqeeyqregiewnfidfgldlqpcie
lierptnppgvlalldeecwfpkatdtsfvekliqeqgnhakfqkskqlkdktefcilhy
agkvtynasawltknmdplndnvtsllnqssdkfvadlwkdvdrivgldqmakmtesslp
sasktkkgmfrtvgqlykeqltklmttlrntnpnfvrciipnhekragkldahlvleqlr
cngvlegiricrqgfpnrivfqefrqryeilaanaipkgfmdgkqacilmikaleldpnl
yrigqskiffrtgvlahleeerdlkitdviiafqaqcrgylarkafakrqqqlgs
>d1br1b_ 1.42.1.5.16 Myosin Essential Chain {Chicken (Gallus gallus)}
fseeqtaefkeafqlfdrtgdgkilysqcgdvmralgqnptnaevmkvlgnpksdemnlk
tlkfeqflpmmqtiaknkdqgcfedyveglrvfdkegngtvmgaeirhvlvtlgekmtee
eveqlvaghedsngcinyeelvrmvlsg
>d1br1c1 2.30.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br1c2 3.30.1.7.1 (2-33,80-821) Myosin S1, motor domain {Chicken (Gallus gallus), pectoral muscle}
aqkplsddekflfvdknfvnnplaqadwsakkXppkfskvedmaeltclneasvlhnlre
ryfsgliytysglfcvvinpykqlpiysekiidmykgkkrhempphiyaiadtayrsmlq
dredqsilctgesgagktentkkviqylavvasshkgkkdtsitqgpsfsygelekqllq
anpileafgnaktvkndnssrfgkfirinfdvtgyivganietylleksrairqakdert
fhifyyliagaseqmrndlllegfnnytflsnghvpipaqqddemfqetleamtimgfte
eeqtsilrvvssvlqlgnivfkkerntdqasmpdntaaqkvchlmginvtdftrsiltpr
ikvgrdvvqkaqtkeqadfaiealakakferlfrwiltrvnkaldktkrqgasflgildi
agfeifeinsfeqlcinytneklqqlfnhtmfileqeeyqregiewnfidfgldlqpcie
lierptnppgvlalldeecwfpkatdtsfvekliqeqgnhakfqkskqlkdktefcilhy
agkvtynasawltknmdplndnvtsllnqssdkfvadlwkdvdrivgldqmakmtesslp
sasktkkgmfrtvgqlykeqltklmttlrntnpnfvrciipnhekragkldahlvleqlr
cngvlegiricrqgfpnrivfqefrqryeilaanaipkgfmdgkqacilmikaleldpnl
yrigqskiffrtgvlahleeerdlkitdviiafqaqcrgylarkafakrqqqlgs
>d1br1d_ 1.42.1.5.16 Myosin Essential Chain {Chicken (Gallus gallus)}
fseeqtaefkeafqlfdrtgdgkilysqcgdvmralgqnptnaevmkvlgnpksdemnlk
tlkfeqflpmmqtiaknkdqgcfedyveglrvfdkegngtvmgaeirhvlvtlgekmtee
eveqlvaghedsngcinyeelvrmvlsg
>d1br1e1 2.30.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br1e2 3.30.1.7.1 (2-33,80-821) Myosin S1, motor domain {Chicken (Gallus gallus), pectoral muscle}
aqkplsddekflfvdknfvnnplaqadwsakkXppkfskvedmaeltclneasvlhnlre
ryfsgliytysglfcvvinpykqlpiysekiidmykgkkrhempphiyaiadtayrsmlq
dredqsilctgesgagktentkkviqylavvasshkgkkdtsitqgpsfsygelekqllq
anpileafgnaktvkndnssrfgkfirinfdvtgyivganietylleksrairqakdert
fhifyyliagaseqmrndlllegfnnytflsnghvpipaqqddemfqetleamtimgfte
eeqtsilrvvssvlqlgnivfkkerntdqasmpdntaaqkvchlmginvtdftrsiltpr
ikvgrdvvqkaqtkeqadfaiealakakferlfrwiltrvnkaldktkrqgasflgildi
agfeifeinsfeqlcinytneklqqlfnhtmfileqeeyqregiewnfidfgldlqpcie
lierptnppgvlalldeecwfpkatdtsfvekliqeqgnhakfqkskqlkdktefcilhy
agkvtynasawltknmdplndnvtsllnqssdkfvadlwkdvdrivgldqmakmtesslp
sasktkkgmfrtvgqlykeqltklmttlrntnpnfvrciipnhekragkldahlvleqlr
cngvlegiricrqgfpnrivfqefrqryeilaanaipkgfmdgkqacilmikaleldpnl
yrigqskiffrtgvlahleeerdlkitdviiafqaqcrgylarkafakrqqqlgs
>d1br1f_ 1.42.1.5.16 Myosin Essential Chain {Chicken (Gallus gallus)}
fseeqtaefkeafqlfdrtgdgkilysqcgdvmralgqnptnaevmkvlgnpksdemnlk
tlkfeqflpmmqtiaknkdqgcfedyveglrvfdkegngtvmgaeirhvlvtlgekmtee
eveqlvaghedsngcinyeelvrmvlsg
>d1br1g1 2.30.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br1g2 3.30.1.7.1 (2-33,80-821) Myosin S1, motor domain {Chicken (Gallus gallus), pectoral muscle}
aqkplsddekflfvdknfvnnplaqadwsakkXppkfskvedmaeltclneasvlhnlre
ryfsgliytysglfcvvinpykqlpiysekiidmykgkkrhempphiyaiadtayrsmlq
dredqsilctgesgagktentkkviqylavvasshkgkkdtsitqgpsfsygelekqllq
anpileafgnaktvkndnssrfgkfirinfdvtgyivganietylleksrairqakdert
fhifyyliagaseqmrndlllegfnnytflsnghvpipaqqddemfqetleamtimgfte
eeqtsilrvvssvlqlgnivfkkerntdqasmpdntaaqkvchlmginvtdftrsiltpr
ikvgrdvvqkaqtkeqadfaiealakakferlfrwiltrvnkaldktkrqgasflgildi
agfeifeinsfeqlcinytneklqqlfnhtmfileqeeyqregiewnfidfgldlqpcie
lierptnppgvlalldeecwfpkatdtsfvekliqeqgnhakfqkskqlkdktefcilhy
agkvtynasawltknmdplndnvtsllnqssdkfvadlwkdvdrivgldqmakmtesslp
sasktkkgmfrtvgqlykeqltklmttlrntnpnfvrciipnhekragkldahlvleqlr
cngvlegiricrqgfpnrivfqefrqryeilaanaipkgfmdgkqacilmikaleldpnl
yrigqskiffrtgvlahleeerdlkitdviiafqaqcrgylarkafakrqqqlgs
>d1br1h_ 1.42.1.5.16 Myosin Essential Chain {Chicken (Gallus gallus)}
fseeqtaefkeafqlfdrtgdgkilysqcgdvmralgqnptnaevmkvlgnpksdemnlk
tlkfeqflpmmqtiaknkdqgcfedyveglrvfdkegngtvmgaeirhvlvtlgekmtee
eveqlvaghedsngcinyeelvrmvlsg
>d1br2a1 2.30.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br2a2 3.30.1.7.1 (80-789) Myosin S1, motor domain {Chicken (Gallus gallus), pectoral muscle}
ppkfskvedmaeltclneasvlhnlreryfsgliytysglfcvvinpykqlpiysekiid
mykgkkrhempphiyaiadtayrsmlqdredqsilctgesgagktentkkviqylavvas
shkgkkdtsitqgpsfsygelekqllqanpileafgnaktvkndnssrfgkfirinfdvt
gyivganietylleksrairqakdertfhifyyliagaseqmrndlllegfnnytflsng
hvpipaqqddemfqetleamtimgfteeeqtsilrvvssvlqlgnivfkkerntdqasmp
dntaaqkvchlmginvtdftrsiltprikvgrdvvqkaqtkeqadfaiealakakferlf
rwiltrvnkaldktkrqgasflgildiagfeifeinsfeqlcinytneklqqlfnhtmfi
leqeeyqregiewnfidfgldlqpcielierptnppgvlalldeecwfpkatdtsfvekl
iqeqgnhakfqkskqlkdktefcilhyagkvtynasawltknmdplndnvtsllnqssdk
fvadlwkdvdrivgldqmakmtesslpsasktkkgmfrtvgqlykeqltklmttlrntnp
nfvrciipnhekragkldahlvleqlrcngvlegiricrqgfpnrivfqefrqryeilaa
naipkgfmdgkqacilmikaleldpnlyrigqskiffrtgvlahleeerd
>d1br2b1 2.30.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br2b2 3.30.1.7.1 (80-789) Myosin S1, motor domain {Chicken (Gallus gallus), pectoral muscle}
ppkfskvedmaeltclneasvlhnlreryfsgliytysglfcvvinpykqlpiysekiid
mykgkkrhempphiyaiadtayrsmlqdredqsilctgesgagktentkkviqylavvas
shkgkkdtsitqgpsfsygelekqllqanpileafgnaktvkndnssrfgkfirinfdvt
gyivganietylleksrairqakdertfhifyyliagaseqmrndlllegfnnytflsng
hvpipaqqddemfqetleamtimgfteeeqtsilrvvssvlqlgnivfkkerntdqasmp
dntaaqkvchlmginvtdftrsiltprikvgrdvvqkaqtkeqadfaiealakakferlf
rwiltrvnkaldktkrqgasflgildiagfeifeinsfeqlcinytneklqqlfnhtmfi
leqeeyqregiewnfidfgldlqpcielierptnppgvlalldeecwfpkatdtsfvekl
iqeqgnhakfqkskqlkdktefcilhyagkvtynasawltknmdplndnvtsllnqssdk
fvadlwkdvdrivgldqmakmtesslpsasktkkgmfrtvgqlykeqltklmttlrntnp
nfvrciipnhekragkldahlvleqlrcngvlegiricrqgfpnrivfqefrqryeilaa
naipkgfmdgkqacilmikaleldpnlyrigqskiffrtgvlahleeerd
>d1br2c1 2.30.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br2c2 3.30.1.7.1 (80-789) Myosin S1, motor domain {Chicken (Gallus gallus), pectoral muscle}
ppkfskvedmaeltclneasvlhnlreryfsgliytysglfcvvinpykqlpiysekiid
mykgkkrhempphiyaiadtayrsmlqdredqsilctgesgagktentkkviqylavvas
shkgkkdtsitqgpsfsygelekqllqanpileafgnaktvkndnssrfgkfirinfdvt
gyivganietylleksrairqakdertfhifyyliagaseqmrndlllegfnnytflsng
hvpipaqqddemfqetleamtimgfteeeqtsilrvvssvlqlgnivfkkerntdqasmp
dntaaqkvchlmginvtdftrsiltprikvgrdvvqkaqtkeqadfaiealakakferlf
rwiltrvnkaldktkrqgasflgildiagfeifeinsfeqlcinytneklqqlfnhtmfi
leqeeyqregiewnfidfgldlqpcielierptnppgvlalldeecwfpkatdtsfvekl
iqeqgnhakfqkskqlkdktefcilhyagkvtynasawltknmdplndnvtsllnqssdk
fvadlwkdvdrivgldqmakmtesslpsasktkkgmfrtvgqlykeqltklmttlrntnp
nfvrciipnhekragkldahlvleqlrcngvlegiricrqgfpnrivfqefrqryeilaa
naipkgfmdgkqacilmikaleldpnlyrigqskiffrtgvlahleeerd
>d1br2d1 2.30.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br2d2 3.30.1.7.1 (80-789) Myosin S1, motor domain {Chicken (Gallus gallus), pectoral muscle}
ppkfskvedmaeltclneasvlhnlreryfsgliytysglfcvvinpykqlpiysekiid
mykgkkrhempphiyaiadtayrsmlqdredqsilctgesgagktentkkviqylavvas
shkgkkdtsitqgpsfsygelekqllqanpileafgnaktvkndnssrfgkfirinfdvt
gyivganietylleksrairqakdertfhifyyliagaseqmrndlllegfnnytflsng
hvpipaqqddemfqetleamtimgfteeeqtsilrvvssvlqlgnivfkkerntdqasmp
dntaaqkvchlmginvtdftrsiltprikvgrdvvqkaqtkeqadfaiealakakferlf
rwiltrvnkaldktkrqgasflgildiagfeifeinsfeqlcinytneklqqlfnhtmfi
leqeeyqregiewnfidfgldlqpcielierptnppgvlalldeecwfpkatdtsfvekl
iqeqgnhakfqkskqlkdktefcilhyagkvtynasawltknmdplndnvtsllnqssdk
fvadlwkdvdrivgldqmakmtesslpsasktkkgmfrtvgqlykeqltklmttlrntnp
nfvrciipnhekragkldahlvleqlrcngvlegiricrqgfpnrivfqefrqryeilaa
naipkgfmdgkqacilmikaleldpnlyrigqskiffrtgvlahleeerd
>d1br2e1 2.30.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br2e2 3.30.1.7.1 (80-789) Myosin S1, motor domain {Chicken (Gallus gallus), pectoral muscle}
ppkfskvedmaeltclneasvlhnlreryfsgliytysglfcvvinpykqlpiysekiid
mykgkkrhempphiyaiadtayrsmlqdredqsilctgesgagktentkkviqylavvas
shkgkkdtsitqgpsfsygelekqllqanpileafgnaktvkndnssrfgkfirinfdvt
gyivganietylleksrairqakdertfhifyyliagaseqmrndlllegfnnytflsng
hvpipaqqddemfqetleamtimgfteeeqtsilrvvssvlqlgnivfkkerntdqasmp
dntaaqkvchlmginvtdftrsiltprikvgrdvvqkaqtkeqadfaiealakakferlf
rwiltrvnkaldktkrqgasflgildiagfeifeinsfeqlcinytneklqqlfnhtmfi
leqeeyqregiewnfidfgldlqpcielierptnppgvlalldeecwfpkatdtsfvekl
iqeqgnhakfqkskqlkdktefcilhyagkvtynasawltknmdplndnvtsllnqssdk
fvadlwkdvdrivgldqmakmtesslpsasktkkgmfrtvgqlykeqltklmttlrntnp
nfvrciipnhekragkldahlvleqlrcngvlegiricrqgfpnrivfqefrqryeilaa
naipkgfmdgkqacilmikaleldpnlyrigqskiffrtgvlahleeerd
>d1br2f1 2.30.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br2f2 3.30.1.7.1 (80-789) Myosin S1, motor domain {Chicken (Gallus gallus), pectoral muscle}
ppkfskvedmaeltclneasvlhnlreryfsgliytysglfcvvinpykqlpiysekiid
mykgkkrhempphiyaiadtayrsmlqdredqsilctgesgagktentkkviqylavvas
shkgkkdtsitqgpsfsygelekqllqanpileafgnaktvkndnssrfgkfirinfdvt
gyivganietylleksrairqakdertfhifyyliagaseqmrndlllegfnnytflsng
hvpipaqqddemfqetleamtimgfteeeqtsilrvvssvlqlgnivfkkerntdqasmp
dntaaqkvchlmginvtdftrsiltprikvgrdvvqkaqtkeqadfaiealakakferlf
rwiltrvnkaldktkrqgasflgildiagfeifeinsfeqlcinytneklqqlfnhtmfi
leqeeyqregiewnfidfgldlqpcielierptnppgvlalldeecwfpkatdtsfvekl
iqeqgnhakfqkskqlkdktefcilhyagkvtynasawltknmdplndnvtsllnqssdk
fvadlwkdvdrivgldqmakmtesslpsasktkkgmfrtvgqlykeqltklmttlrntnp
nfvrciipnhekragkldahlvleqlrcngvlegiricrqgfpnrivfqefrqryeilaa
naipkgfmdgkqacilmikaleldpnlyrigqskiffrtgvlahleeerd
>d1br4a1 2.30.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br4a2 3.30.1.7.1 (2-33,80-821) Myosin S1, motor domain {Chicken (Gallus gallus), pectoral muscle}
aqkplsddekflfvdknfvnnplaqadwsakkXppkfskvedmaeltclneasvlhnlre
ryfsgliytysglfcvvinpykqlpiysekiidmykgkkrhempphiyaiadtayrsmlq
dredqsilctgesgagktentkkviqylavvasshkgkkdtsitqgpsfsygelekqllq
anpileafgnaktvkndnssrfgkfirinfdvtgyivganietylleksrairqakdert
fhifyyliagaseqmrndlllegfnnytflsnghvpipaqqddemfqetleamtimgfte
eeqtsilrvvssvlqlgnivfkkerntdqasmpdntaaqkvchlmginvtdftrsiltpr
ikvgrdvvqkaqtkeqadfaiealakakferlfrwiltrvnkaldktkrqgasflgildi
agfeifeinsfeqlcinytneklqqlfnhtmfileqeeyqregiewnfidfgldlqpcie
lierptnppgvlalldeecwfpkatdtsfvekliqeqgnhakfqkskqlkdktefcilhy
agkvtynasawltknmdplndnvtsllnqssdkfvadlwkdvdrivgldqmakmtesslp
sasktkkgmfrtvgqlykeqltklmttlrntnpnfvrciipnhekragkldahlvleqlr
cngvlegiricrqgfpnrivfqefrqryeilaanaipkgfmdgkqacilmikaleldpnl
yrigqskiffrtgvlahleeerdlkitdviiafqaqcrgylarkafakrqqqlgs
>d1br4b_ 1.42.1.5.16 Myosin Essential Chain {Chicken (Gallus gallus)}
fseeqtaefkeafqlfdrtgdgkilysqcgdvmralgqnptnaevmkvlgnpksdemnlk
tlkfeqflpmmqtiaknkdqgcfedyveglrvfdkegngtvmgaeirhvlvtlgekmtee
eveqlvaghedsngcinyeelvrmvlsg
>d1br4c1 2.30.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br4c2 3.30.1.7.1 (2-33,80-821) Myosin S1, motor domain {Chicken (Gallus gallus), pectoral muscle}
aqkplsddekflfvdknfvnnplaqadwsakkXppkfskvedmaeltclneasvlhnlre
ryfsgliytysglfcvvinpykqlpiysekiidmykgkkrhempphiyaiadtayrsmlq
dredqsilctgesgagktentkkviqylavvasshkgkkdtsitqgpsfsygelekqllq
anpileafgnaktvkndnssrfgkfirinfdvtgyivganietylleksrairqakdert
fhifyyliagaseqmrndlllegfnnytflsnghvpipaqqddemfqetleamtimgfte
eeqtsilrvvssvlqlgnivfkkerntdqasmpdntaaqkvchlmginvtdftrsiltpr
ikvgrdvvqkaqtkeqadfaiealakakferlfrwiltrvnkaldktkrqgasflgildi
agfeifeinsfeqlcinytneklqqlfnhtmfileqeeyqregiewnfidfgldlqpcie
lierptnppgvlalldeecwfpkatdtsfvekliqeqgnhakfqkskqlkdktefcilhy
agkvtynasawltknmdplndnvtsllnqssdkfvadlwkdvdrivgldqmakmtesslp
sasktkkgmfrtvgqlykeqltklmttlrntnpnfvrciipnhekragkldahlvleqlr
cngvlegiricrqgfpnrivfqefrqryeilaanaipkgfmdgkqacilmikaleldpnl
yrigqskiffrtgvlahleeerdlkitdviiafqaqcrgylarkafakrqqqlgs
>d1br4d_ 1.42.1.5.16 Myosin Essential Chain {Chicken (Gallus gallus)}
fseeqtaefkeafqlfdrtgdgkilysqcgdvmralgqnptnaevmkvlgnpksdemnlk
tlkfeqflpmmqtiaknkdqgcfedyveglrvfdkegngtvmgaeirhvlvtlgekmtee
eveqlvaghedsngcinyeelvrmvlsg
>d1br4e1 2.30.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br4e2 3.30.1.7.1 (2-33,80-821) Myosin S1, motor domain {Chicken (Gallus gallus), pectoral muscle}
aqkplsddekflfvdknfvnnplaqadwsakkXppkfskvedmaeltclneasvlhnlre
ryfsgliytysglfcvvinpykqlpiysekiidmykgkkrhempphiyaiadtayrsmlq
dredqsilctgesgagktentkkviqylavvasshkgkkdtsitqgpsfsygelekqllq
anpileafgnaktvkndnssrfgkfirinfdvtgyivganietylleksrairqakdert
fhifyyliagaseqmrndlllegfnnytflsnghvpipaqqddemfqetleamtimgfte
eeqtsilrvvssvlqlgnivfkkerntdqasmpdntaaqkvchlmginvtdftrsiltpr
ikvgrdvvqkaqtkeqadfaiealakakferlfrwiltrvnkaldktkrqgasflgildi
agfeifeinsfeqlcinytneklqqlfnhtmfileqeeyqregiewnfidfgldlqpcie
lierptnppgvlalldeecwfpkatdtsfvekliqeqgnhakfqkskqlkdktefcilhy
agkvtynasawltknmdplndnvtsllnqssdkfvadlwkdvdrivgldqmakmtesslp
sasktkkgmfrtvgqlykeqltklmttlrntnpnfvrciipnhekragkldahlvleqlr
cngvlegiricrqgfpnrivfqefrqryeilaanaipkgfmdgkqacilmikaleldpnl
yrigqskiffrtgvlahleeerdlkitdviiafqaqcrgylarkafakrqqqlgs
>d1br4f_ 1.42.1.5.16 Myosin Essential Chain {Chicken (Gallus gallus)}
fseeqtaefkeafqlfdrtgdgkilysqcgdvmralgqnptnaevmkvlgnpksdemnlk
tlkfeqflpmmqtiaknkdqgcfedyveglrvfdkegngtvmgaeirhvlvtlgekmtee
eveqlvaghedsngcinyeelvrmvlsg
>d1br4g1 2.30.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br4g2 3.30.1.7.1 (2-33,80-821) Myosin S1, motor domain {Chicken (Gallus gallus), pectoral muscle}
aqkplsddekflfvdknfvnnplaqadwsakkXppkfskvedmaeltclneasvlhnlre
ryfsgliytysglfcvvinpykqlpiysekiidmykgkkrhempphiyaiadtayrsmlq
dredqsilctgesgagktentkkviqylavvasshkgkkdtsitqgpsfsygelekqllq
anpileafgnaktvkndnssrfgkfirinfdvtgyivganietylleksrairqakdert
fhifyyliagaseqmrndlllegfnnytflsnghvpipaqqddemfqetleamtimgfte
eeqtsilrvvssvlqlgnivfkkerntdqasmpdntaaqkvchlmginvtdftrsiltpr
ikvgrdvvqkaqtkeqadfaiealakakferlfrwiltrvnkaldktkrqgasflgildi
agfeifeinsfeqlcinytneklqqlfnhtmfileqeeyqregiewnfidfgldlqpcie
lierptnppgvlalldeecwfpkatdtsfvekliqeqgnhakfqkskqlkdktefcilhy
agkvtynasawltknmdplndnvtsllnqssdkfvadlwkdvdrivgldqmakmtesslp
sasktkkgmfrtvgqlykeqltklmttlrntnpnfvrciipnhekragkldahlvleqlr
cngvlegiricrqgfpnrivfqefrqryeilaanaipkgfmdgkqacilmikaleldpnl
yrigqskiffrtgvlahleeerdlkitdviiafqaqcrgylarkafakrqqqlgs
>d1br4h_ 1.42.1.5.16 Myosin Essential Chain {Chicken (Gallus gallus)}
fseeqtaefkeafqlfdrtgdgkilysqcgdvmralgqnptnaevmkvlgnpksdemnlk
tlkfeqflpmmqtiaknkdqgcfedyveglrvfdkegngtvmgaeirhvlvtlgekmtee
eveqlvaghedsngcinyeelvrmvlsg
>d1br5a_ 4.135.1.1.7 Ricin A-chain {Castor bean (Ricinus communis)}
ifpkqypiinfttagatvqsytnfiravrgrlttgadvrheipvlpnrvglpinqrfilv
elsnhaelsvtlaldvtnayvvgyragnsayffhpdnqedaeaithlftdvqnrytfafg
gnydrleqlagnlrenielgngpleeaisalyyystggtqlptlarsfiiciqmiseaar
fqyiegemrtrirynrrsapdpsvitlenswgrlstaiqesnqgafaspiqlqrrngskf
svydvsilipiialmvyrcapppssqf
>d1br6a_ 4.135.1.1.7 Ricin A-chain {Castor bean (Ricinus communis)}
mifpkqypiinfttagatvqsytnfiravrgrlttgadvrheipvlpnrvglpinqrfil
velsnhaelsvtlaldvtnayvvgyragnsayffhpdnqedaeaithlftdvqnrytfaf
ggnydrleqlagnlrenielgngpleeaisalyyystggtqlptlarsfiiciqmiseaa
rfqyiegemrtrirynrrsapdpsvitlenswgrlstaiqesnqgafaspiqlqrrngsk
fsvydvsilipiialmvyrcapppssqf
>d1br8i_ 5.1.1.1.6 Antithrombin {Human (Homo sapiens)}
ictakprdipmnpmciyrspetnrrvwelskansrfattfyqhladskndndniflspls
istafamtklgacndtlqqlmevfkfdtisektsdqihfffaklncrlyrkankssklvs
anrlfgdksltfnetyqdiselvygaklqpldfkenaeqsraainkwvsnktegritdvi
pseaineltvlvlvntiyfkglwkskfspentrkelfykadgescsasmmyqegkfryrr
vaegtqvlelpfkgdditmvlilpkpekslakvekeltpevlqewldeleemmlvvhmpr
friedgfslkeqlqdmglvdlfspeksklpgivaegrddlyvsdafhkaflevneeasta
vviagrslnpnrvtfkanrpflvfirevplntiifmgrvanpcv
>d1br8l_ 5.1.1.1.6 Antithrombin {Human (Homo sapiens)}
ctakprdipmnpmciyrsatnrrvwelskansrfattfyqhladskndndniflsplsis
tafamtklgacndtlqqlmevfkfdtisektsdqihfffaklncrlyrkankssklvsan
rlfgdksltfnetyqdiselvygaklqpldfkenaeqsraainkwvsnktegritdvips
eaineltvlvlvntiyfkglwkskfspentrkelfykadgescsasmmyqegkfryrrva
egtqvlelpfkgdditmvlilpkpekslakvekeltpevlqewldeleemmlvvhmprfr
iedgfslkeqlqdmglvdlfspeksklpgivaegrddlyvsdafhkaflevneegseaaa
stavviagrslnrpflvfirevplntiifmgrvanpcv
>d1br9__ 2.35.3.1.2 TIMP-2 {Human (Homo sapiens)}
cscspvhpqqafcnadvvirakavsekevdsgndiygnpikriqyeikqikmfkgpekdi
efiytapssavcgvsldvggkkeyliagkaegdgkmhitlcdfivpwdtlsttqkkslnh
ryqmgceckitrcpmipcyisspdeclwmdwvtekninghqakffacikrsdgscawyrg
aa
>d1bra__ 2.41.1.2.3 Trypsin(ogen) {Rat (Rattus rattus)}
ivggytcqensvpyqvslnsgyhfcggslindqwvvsaahcyksriqvrlgehninvleg
neqfvnaakiikhpnfdrktlnndimliklsspvklnarvatvalpsscapagtqclisg
wgntlssgvnepdllqcldapllpqadceasypgkitdnmvcvgfleggkgscqgdsggp
vvcngelqgivswgygcalpdnpdvytkvcnyvdwiqdtiaan
>d1brbe_ 2.41.1.2.3 Trypsin(ogen) {Rat (Rattus rattus)}
ivggytcqensvpyqvslnsgyhfcggslindqwvvsaahcyksriqvrlgehninvleg
neqfvnaakiikhpnfdrktlnndimliklsspvklnarvatvalpsscapagtqclisg
wgntlssgvnepdllqcldapllpqadceasypgkitdnmvcvgfleggkgscqgdsggp
vvcngelqgivswgygcalpdnpdvytkvcnyvdwiqdtiaan
>d1brbi_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
ageppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrta
>d1brce_ 2.41.1.2.3 Trypsin(ogen) {Rat (Rattus rattus)}
ivggytcqensvpyqvslnsgyhfcggslindqwvvsaahcyksriqvrlgehninvleg
neqfvnaakiikhpnfdrktlnndimliklsspvklnarvatvalpsscapagtqclisg
wgntlssgvnepdllqcldapllpqadceasypgkitdnmvcvgfleggkgscqgdsggp
vvcngelqgivswgygcalpdnpdvytkvcnyvdwiqdtiaan
>d1brci_ 7.8.1.1.4 Alzheimer's amyloid B-protein precursor, APPI {Human (Homo sapiens)}
vrevcseqaetgpcramisrwyfdvtegkcapffyggcggnrnnfdteeycmavcg
>d1brd__ 6.2.1.1.1 Bacteriorhodopsin {Halobacterium halobium}
pewiwlalgtalmglgtlyflvkgmgvsdpdakkfyaittlvpaiaftmylsmllgyglt
mvpfggeqnpiywaryadwlfttplllldlallvdadqgtilalvgadgimigtglvgal
tkvysyrfvwwaistaamlyilyvlffgftskaesmrpevastfkvlrnvtvvlwsaypv
vwligsegagivplnietllfmvldvsakvgfglillrs
>d1brea_ 2.1.1.1.147 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (kappa) dimer BRE (human)}
diqmtqspsslsasvgdrvtitcqasqdisdyliwyqqklgkapnlliydastletgvps
rfsgsgsgteytftisslqpediatyycqqyddlpytfgqgtkveik
>d1breb_ 2.1.1.1.147 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (kappa) dimer BRE (human)}
diqmtqspsslsasvgdrvtitcqasqdisdyliwyqqklgkapnlliydastletgvps
rfsgsgsgteytftisslqpediatyycqqyddlpytfgqgtkveik
>d1brec_ 2.1.1.1.147 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (kappa) dimer BRE (human)}
diqmtqspsslsasvgdrvtitcqasqdisdyliwyqqklgkapnlliydastletgvps
rfsgsgsgteytftisslqpediatyycqqyddlpytfgqgtkveik
>d1bred_ 2.1.1.1.147 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (kappa) dimer BRE (human)}
diqmtqspsslsasvgdrvtitcqasqdisdyliwyqqklgkapnlliydastletgvps
rfsgsgsgteytftisslqpediatyycqqyddlpytfgqgtkveik
>d1bree_ 2.1.1.1.147 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (kappa) dimer BRE (human)}
diqmtqspsslsasvgdrvtitcqasqdisdyliwyqqklgkapnlliydastletgvps
rfsgsgsgteytftisslqpediatyycqqyddlpytfgqgtkveik
>d1bref_ 2.1.1.1.147 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (kappa) dimer BRE (human)}
diqmtqspsslsasvgdrvtitcqasqdisdyliwyqqklgkapnlliydastletgvps
rfsgsgsgteytftisslqpediatyycqqyddlpytfgqgtkveik
>d1brf__ 7.35.4.1.5 Rubredoxin {Pyrococcus furiosus}
akwvckicgyiydedagdpdngispgtkfeelpddwvcpicgapksefekled
>d1brga_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintldgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1brgb_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintldgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1brgc_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintldgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1brha_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadyaqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1brhb_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadyaqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1brhc_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadyaqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1bria_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadanytsgfrnsdrilyssdwliykttdhyqtftkir
>d1brib_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadanytsgfrnsdrilyssdwliykttdhyqtftkir
>d1bric_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
intfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregkl
pgksgrtwreadanytsgfrnsdrilyssdwliykttdhyqtftkir
>d1brja_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdralyssdwliykttdhyqtftkir
>d1brjb_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdralyssdwliykttdhyqtftkir
>d1brjc_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdralyssdwliykttdhyqtftkir
>d1brka_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwlaykttdhyqtftkir
>d1brkb_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwlaykttdhyqtftkir
>d1brkc_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
intfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregkl
pgksgrtwreadinytsgfrnsdrilyssdwlaykttdhyqtftkir
>d1brla_ 3.1.14.1.1 Bacterial luciferase (alkanal monooxygenase) {Vibrio harveyi}
mkfgnflltyqppelsqtevmkrlvnlgkasegcgfdtvwllehhftefgllgnpyvaaa
hllgatetlnvgtaaivlptahpvrqaedvnlldqmskgrfrfgicrglydkdfrvfgtd
mdnsralmdcwydlmkegfnegyiaadnehikfpkiqlnpsaytqggapvyvvaesastt
ewaaerglpmilswiinthekkaqldlynevatehgydvtkidhclsyitsvdhdsnrak
dicrnflghwydsyvnatkifddsdqtkgydfnkgqwrdfvlkghkdtnrridysyeinp
vgtpeeciaiiqqdidatgidniccgfeangseeeiiasmklfqsdvmpylkekq
>d1brlb_ 3.1.14.1.1 Bacterial luciferase (alkanal monooxygenase) {Vibrio harveyi}
mkfglfflnfmnskrssdqvieemldtahyvdqlkfdtlavyenhfsnngvvgapltvag
fllgmtknakvaslnhvitthhpvrvaeeaclldqmsegrfafgfsdceksadmrffnrp
tdsqfqlfsechkiindafttgychpnndfysfpkisvnphafteggpaqfvnatskevv
ewaaklglplvfrwddsnaqrkeyaglyhevaqahgvdvsqvrhkltllvnqnvdgeaar
aearvyleefvresysntdfeqkmgellsenaigtyeestqaarvaieccgaadllmsfe
smedkaqqravidvvnani
>d1brma1 3.2.1.3.11 (1-133,355-367) Aspartate beta-semialdehyde dehydrogenase {Escherichia coli}
mknvgfigwrgmvgsvlmqrmveerdfdairpvffstsqlgqaapsfggttgtlqdafdl
ealkaldiivtcqggdytneiypklresgwqgywidaasslrmkddaiiildpvnqdvit
dglnngirtfvggXaaeplrrmlrqla
>d1brma2 4.61.1.1.11 (134-354) Aspartate beta-semialdehyde dehydrogenase {Escherichia coli}
nctvslmlmslgglfandlvdwvsvatyqaasgggarhmrelltqmghlyghvadelatp
ssaildierkvttltrsgelpvdnfgvplagslipwidkqldngqsreewkgqaetnkil
ntssvipvdglcvrvgalrchsqaftiklkkdvsiptveellaahnpwakvvpndreitm
reltpaavtgtlttpvgrlrklnmgpeflsaftvgdqllwg
>d1brmb1 3.2.1.3.11 (1-133,355-367) Aspartate beta-semialdehyde dehydrogenase {Escherichia coli}
mknvgfigwrgmvgsvlmqrmveerdfdairpvffstsqlgqaapsfggttgtlqdafdl
ealkaldiivtcqggdytneiypklresgwqgywidaasslrmkddaiiildpvnqdvit
dglnngirtfvggXaaeplrrmlrqla
>d1brmb2 4.61.1.1.11 (134-354) Aspartate beta-semialdehyde dehydrogenase {Escherichia coli}
nctvslmlmslgglfandlvdwvsvatyqaasgggarhmrelltqmghlyghvadelatp
ssaildierkvttltrsgelpvdnfgvplagslipwidkqldngqsreewkgqaetnkil
ntssvipvdglcvrvgalrchsqaftiklkkdvsiptveellaahnpwakvvpndreitm
reltpaavtgtlttpvgrlrklnmgpeflsaftvgdqllwg
>d1brmc1 3.2.1.3.11 (1-133,355-367) Aspartate beta-semialdehyde dehydrogenase {Escherichia coli}
mknvgfigwrgmvgsvlmqrmveerdfdairpvffstsqlgqaapsfggttgtlqdafdl
ealkaldiivtcqggdytneiypklresgwqgywidaasslrmkddaiiildpvnqdvit
dglnngirtfvggXaaeplrrmlrqla
>d1brmc2 4.61.1.1.11 (134-354) Aspartate beta-semialdehyde dehydrogenase {Escherichia coli}
nctvslmlmslgglfandlvdwvsvatyqaasgggarhmrelltqmghlyghvadelatp
ssaildierkvttltrsgelpvdnfgvplagslipwidkqldngqsreewkgqaetnkil
ntssvipvdglcvrvgalrchsqaftiklkkdvsiptveellaahnpwakvvpndreitm
reltpaavtgtlttpvgrlrklnmgpeflsaftvgdqllwg
>d1brnl_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1brnm_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1broa_ 3.59.1.10.1 Bromoperoxidase A2 {Streptomyces aureofaciens}
pfitvgqenstsidlyyedhgtgqpvvlihgfplsghswerqsaalldagyrvitydrrg
fgqssqpttgydydtfaadlntvletldlqdavlvgfsmgtgevaryvssygtariakva
flaslepfllktddnpdgaapqeffdgivaavkadryafytgffndfynldenlgtrise
eavrnswntaasggffaaaaapttwytdfradipridvpalilhgtgdrtlpientarvf
hkalpsaeyvevegaphgllwthaeevntallaflak
>d1brob_ 3.59.1.10.1 Bromoperoxidase A2 {Streptomyces aureofaciens}
pfitvgqenstsidlyyedhgtgqpvvlihgfplsghswerqsaalldagyrvitydrrg
fgqssqpttgydydtfaadlntvletldlqdavlvgfsmgtgevaryvssygtariakva
flaslepfllktddnpdgaapqeffdgivaavkadryafytgffndfynldenlgtrise
eavrnswntaasggffaaaaapttwytdfradipridvpalilhgtgdrtlpientarvf
hkalpsaeyvevegaphgllwthaeevntallaflak
>d1brp__ 2.53.1.1.3 Retinol binding protein {Human (Homo sapiens)}
erdcrvssfrvkenfdkarfsgtwyamakkdpeglflqdnivaefsvdetgqmsatakgr
vrllnnwdvcadmvgtftdtedpakfkmkywgvasflqkgnddhwivdtdydtyavqysc
rllnldgtcadsysfvfsrdpnglppeaqkivrqrqeelclarqyrlivhngycd
>d1brq__ 2.53.1.1.3 Retinol binding protein {Human (Homo sapiens)}
erdcrvssfrvkenfdkarfsgtwyamakkdpeglflqdnivaefsvdetgqmsatakgr
vrllnnwdvcadmvgtftdtedpakfkmkywgvasflqkgnddhwivdtdydtyavqysc
rllnldgtcadsysfvfsrdpnglppeaqkivrqrqeelclarqyrlivhngycd
>d1brra_ 6.2.1.1.2 Bacteriorhodopsin {Halobacterium salinarium}
itgrpewiwlalgtalmglgtlyflvkgmgvsdpdakkfyaittlvpaiaftmylsmllg
ygltmvpfggeqnpiywaryadwlfttplllldlallvdadqgtilalvgadgimigtgl
vgaltkvysyrfvwwaistaamlyilyvlffgftskaesmrpevastfkvlrnvtvvlws
aypvvwligsegagivplnietllfmvldvsakvgfglillrsraifgea
>d1brrb_ 6.2.1.1.2 Bacteriorhodopsin {Halobacterium salinarium}
tgrpewiwlalgtalmglgtlyflvkgmgvsdpdakkfyaittlvpaiaftmylsmllgy
gltmvpfggeqnpiywaryadwlfttplllldlallvdadqgtilalvgadgimigtglv
galtkvysyrfvwwaistaamlyilyvlffgftskaesmrpevastfkvlrnvtvvlwsa
ypvvwligsegagivplnietllfmvldvsakvgfglillrsraifgea
>d1brrc_ 6.2.1.1.2 Bacteriorhodopsin {Halobacterium salinarium}
aqitgrpewiwlalgtalmglgtlyflvkgmgvsdpdakkfyaittlvpaiaftmylsml
lgygltmvpfggeqnpiywaryadwlfttplllldlallvdadqgtilalvgadgimigt
glvgaltkvysyrfvwwaistaamlyilyvlffgftskaesmrpevastfkvlrnvtvvl
wsaypvvwligsegagivplnietllfmvldvsakvgfglillrsraifgea
>d1brsa_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1brsb_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
aqvintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnre
gklpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1brsc_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1brsd_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdaltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegaditiils
>d1brse_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kavingeqirsisdlhqtlkkelalpeyygenldalwdaltgwveyplvlewrqfeqskq
ltengaesvlqvfreakaegaditiils
>d1brsf_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdaltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegaditiils
>d1brt__ 3.59.1.10.1 Bromoperoxidase A2 {Streptomyces aureofaciens}
pfitvgqenstsidlyyedhgtgqpvvlihgfplsghswerqsaalldagyrvitydrrg
fgqssqpttgydydtfaadlntvletldlqdavlvgfstgtgevaryvssygtariakva
flaslepfllktddnpdgaapqeffdgivaavkadryafytgffndfynldenlgtrise
eavrnswntaasggffaaaaapttwytdfradipridvpalilhgtgdrtlpientarvf
hkalpsaeyvevegaphgllwthaeevntallaflak
>d1brup_ 2.41.1.2.15 Elastase {Porcine (Sus scrofa)}
vvggedarpnswpwqvslqydssgqwrhtcggtlvdqswvltaahcisssrtyrvvlgrh
slstnepgslavkvsklvvhqdwnsnqlsngndiallklaspvsltdkiqlgclpaagti
lpnnyvcyvtgwgrlqtngaspdilqqgqllvvdyatcskpgwwgstvktnmicaggdgi
isscngdsggplncqgangqwqvhgivsfgsslgcnyyhkpsvftrvsnyidwinsvian
n
>d1brwa1 1.49.2.1.2 (1-70) Pyrimidine nucleoside phosphorylase {Bacillus stearothermophilus}
mrmvdliakkrdgkaltkeeiewivrgytngdipdyqmsalamaiyfrgmteeetaaltm
amvqsgemld
>d1brwa2 3.20.1.1.2 (71-330) Pyrimidine nucleoside phosphorylase {Bacillus stearothermophilus}
lssirgvkvdkhstggvgdtttlvlgplvasvgvpvakmsgrglghtggtidklesvpgf
hveiskdefirlvnengiaiigqtgdltpadkklyalrdvtatvnsipliassimskkia
agadaivldvktgagafmkkldearrlarvmvdigkrvgrrtmavisdmsqplgyavgna
levkeaietlkgngphdltelcltlgshmvylaekapsldearrlleeairsgaaiaafk
tflaaqggdasvvddldklp
>d1brwa3 4.34.3.1.2 (331-433) Pyrimidine nucleoside phosphorylase {Bacillus stearothermophilus}
kaaytstvtaaadgyvaemaaddigtaamwlgagrakaedvidlavgivlhkkigdrvqk
gealatihsnrpdvldvkekieaairlspqpvarppliyetiv
>d1brwb1 1.49.2.1.2 (1001-1070) Pyrimidine nucleoside phosphorylase {Bacillus stearothermophilus}
mrmvdliakkrdgkaltkeeiewivrgytngdipdyqmsalamaiyfrgmteeetaaltm
amvqsgemld
>d1brwb2 3.20.1.1.2 (1071-1330) Pyrimidine nucleoside phosphorylase {Bacillus stearothermophilus}
lssirgvkvdkhstggvgdtttlvlgplvasvgvpvakmsgrglghtggtidklesvpgf
hveiskdefirlvnengiaiigqtgdltpadkklyalrdvtatvnsipliassimskkia
agadaivldvktgagafmkkldearrlarvmvdigkrvgrrtmavisdmsqplgyavgna
levkeaietlkgngphdltelcltlgshmvylaekapsldearrlleeairsgaaiaafk
tflaaqggdasvvddldklp
>d1brwb3 4.34.3.1.2 (1331-1433) Pyrimidine nucleoside phosphorylase {Bacillus stearothermophilus}
kaaytstvtaaadgyvaemaaddigtaamwlgagrakkedvidlavgivlhkkigdrvqk
gealatihsnrpdvldvkekieaairlspqpvarppliyetiv
>d1brx__ 6.2.1.1.2 Bacteriorhodopsin {Halobacterium salinarium}
grpewiwlalgtalmglgtlyflvkgmgvsdpdakkfyaittlvpaiaftmylsmllgyg
ltmvpfggeqnpiywaryadwlfttplllldlallvdadqgtilalvgadgimigtglvg
altkvysyrfvwwaistaamlyilyvlffgftskaesmrpevastfkvlrnvtvvlwsay
pvvwligsegagivplnietllfmvldvsakvgfglillrsra
>d1bryy_ 4.135.1.1.2 Bryodin {Red briony (Bryonia dioica)}
dvsfrlsgatttsygvfiknlrealpyerkvynipllrssisgsgrytllhltnyadeti
svavdvtnvyimgylagdvsyffneasateaakfvfkdakkkvtlpysgnyerlqtaagk
ireniplglpaldsaittlyyytassaasallvliqstaesarykfieqqigkrvdktfl
pslatislennwsalskqiqiastnngqfespvvlidgnnqrvsitnasarvvtsniall
lnrnnia
>d1bryz_ 4.135.1.1.2 Bryodin {Red briony (Bryonia dioica)}
dvsfrlsgatttsygvfiknlrealpyerkvynipllrssisgsgrytllhltnyadeti
svavdvtnvyimgylagdvsyffneasateaakfvfkdakkkvtlpysgnyerlqtaagk
ireniplglpaldsaittlyyytassaasallvliqstaesarykfieqqigkrvdktfl
pslatislennwsalskqiqiastnngqfespvvlidgnnqrvsitnasarvvtsniall
lnrnnia
>d1brz__ 7.3.7.4.4 Brazzein {J'oublie (Pentadiplandra brazzeana)}
dkckkvyenypvskcqlanqcnydckldkharsgecfydekrnlqcicdycey
>d1bs0a_ 3.57.1.4.9 PLP-dependent acyl-CoA synthase (8-amino-7-oxonanoate synthase, AONS) {Escherichia coli}
swqekinaaldarraadalrrrypvaqgagrwlvaddrqylnfssndylglshhpqiira
wqqgaeqfgigsggsghvsgysvvhqaleeelaewlgysrallfisgfaanqaviaamma
kedriaadrlshaslleaaslspsqlrrfahndvthlarllaspcpgqqmvvtegvfsmd
gdsaplaeiqqvtqqhngwlmvddahgtgvigeqgrgscwlqkvkpellvvtfgkgfgvs
gaavlcsstvadyllqfarhliystsmppaqaqalraslavirsdegdarreklaalitr
fragvqdlpftladscsaiqplivgdnsralqlaeklrqqgcwvtairpptvpagtarlr
ltltaahemqdidrllevlhgng
>d1bs1a_ 3.30.1.8.1 Dethiobiotin synthetase {Escherichia coli}
skryfvtgtdtevgktvascallqaakaagyrtagykpvasgsektpeglrnsdalalqr
nsslqldyatvnpytfaeptsphiisaqegrpieslvmsaglraleqqadwvlvegaggw
ftplsdtftfadwvtqeqlpvilvvgvklgcinhamltaqviqhagltlagwvandvtpp
gkrhaeymttltrmipapllgeipwlaenpenaatgkyinlall
>d1bs2a1 1.28.1.1.4 (484-607) Arginyl-tRNA synthetase (ArgRS) {Baker's yeast (Saccharomyces cerevisiae)}
dtgpylqyahsrlrsvernasgitqekwinadfsllkepaakllirllgqypdvlrnaik
thepttvvtylfklthqvsscydvlwvagqteelatarlalygaarqvlyngmrllgltp
verm
>d1bs2a2 3.19.1.1.8 (136-483) Arginyl-tRNA synthetase (ArgRS) {Baker's yeast (Saccharomyces cerevisiae)}
scklvenkkviiefsspniakpfhaghlrstiiggflanlyeklgwevirmnylgdwgkq
fgllavgferygneealvkdpihhlfdvyvrinkdieeegdsipleqstngkareyfkrm
edgdeealkiwkrfrefsiekyidtyarlnikydvysgesqvskesmlkaidlfkekglt
hedkgavlidltkfnkklgkaivqksdgttlyltrdvgaamdryekyhfdkmiyviasqq
dlhaaqffeilkqmgfewakdlqhvnfgmvqgmstrkgtvvfldnileetkekmhevmkk
nenkyaqiehpeevadlvgisavmiqdmqgkrinnyefkwermlsfeg
>d1bs2a3 4.51.2.1.1 (5-135) Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain {Baker's yeast (Saccharomyces cerevisiae)}
anmisqlkklsiaepavakdshpdvnivdlmrnyisqelskisgvdsslifpalewtntm
ergdllipiprlrikganpkdlavqwaekfpcgdflekveangpfiqfffnpqflaklvi
pdiltrkedyg
>d1bs3a1 1.2.7.1.9 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1bs3a2 4.37.1.1.9 (87-201) Cambialistic superoxide dismutase {Propionibacterium freudenreichii, shermani}
saperptdelgaaideffgsfdnmkaqftaaatgiqgsgwaslvwdplgkrintlqfydh
qnnlpagsipllqldmwehafylqyknvkgdyvkswwnvvnwddvalrfsearva
>d1bs3b1 1.2.7.1.9 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1bs3b2 4.37.1.1.9 (87-201) Cambialistic superoxide dismutase {Propionibacterium freudenreichii, shermani}
saperptdelgaaideffgsfdnmkaqftaaatgiqgsgwaslvwdplgkrintlqfydh
qnnlpagsipllqldmwehafylqyknvkgdyvkswwnvvnwddvalrfsearva
>d1bs4a_ 4.137.1.1.1 Peptide deformylase {Escherichia coli}
svlqvlhipderlrkvakpveevnaeiqrivddmfetmyaeegiglaatqvdihqriivi
dvsenrderlvlinpelleksgetgieegclsipeqralvpraekvkiraldrdgkpfel
eadgllaiciqhemdhlvgklfmdylsplkqqrirqkvekldrlkara
>d1bs4b_ 4.137.1.1.1 Peptide deformylase {Escherichia coli}
svlqvlhipderlrkvakpveevnaeiqrivddmfetmyaeegiglaatqvdihqriivi
dvsenrderlvlinpelleksgetgieegclsipeqralvpraekvkiraldrdgkpfel
eadgllaiciqhemdhlvgklfmdylsplkqqrirqkvekldrlkara
>d1bs4c_ 4.137.1.1.1 Peptide deformylase {Escherichia coli}
svlqvlhipderlrkvakpveevnaeiqrivddmfetmyaeegiglaatqvdihqriivi
dvsenrderlvlinpelleksgetgieegclsipeqralvpraekvkiraldrdgkpfel
eadgllaiciqhemdhlvgklfmdylsplkqqrirqkvekldrlkara
>d1bs5a_ 4.137.1.1.1 Peptide deformylase {Escherichia coli}
svlqvlhipderlrkvakpveevnaeiqrivddmfetmyaeegiglaatqvdihqriivi
dvsenrderlvlinpelleksgetgieegclsipeqralvpraekvkiraldrdgkpfel
eadgllaiciqhemdhlvgklfmdylsplkqqrirqkvekldrlkara
>d1bs5b_ 4.137.1.1.1 Peptide deformylase {Escherichia coli}
svlqvlhipderlrkvakpveevnaeiqrivddmfetmyaeegiglaatqvdihqriivi
dvsenrderlvlinpelleksgetgieegclsipeqralvpraekvkiraldrdgkpfel
eadgllaiciqhemdhlvgklfmdylsplkqqrirqkvekldrlkara
>d1bs5c_ 4.137.1.1.1 Peptide deformylase {Escherichia coli}
svlqvlhipderlrkvakpveevnaeiqrivddmfetmyaeegiglaatqvdihqriivi
dvsenrderlvlinpelleksgetgieegclsipeqralvpraekvkiraldrdgkpfel
eadgllaiciqhemdhlvgklfmdylsplkqqrirqkvekldrlkara
>d1bs6a_ 4.137.1.1.1 Peptide deformylase {Escherichia coli}
svlqvlhipderlrkvakpveevnaeiqrivddmfetmyaeegiglaatqvdihqriivi
dvsenrderlvlinpelleksgetgieegclsipeqralvpraekvkiraldrdgkpfel
eadgllaiciqhemdhlvgklfmdylsplkqqrirqkvekldrlkara
>d1bs6b_ 4.137.1.1.1 Peptide deformylase {Escherichia coli}
svlqvlhipderlrkvakpveevnaeiqrivddmfetmyaeegiglaatqvdihqriivi
dvsenrderlvlinpelleksgetgieegclsipeqralvpraekvkiraldrdgkpfel
eadgllaiciqhemdhlvgklfmdylsplkqqrirqkvekldrlkara
>d1bs6c_ 4.137.1.1.1 Peptide deformylase {Escherichia coli}
svlqvlhipderlrkvakpveevnaeiqrivddmfetmyaeegiglaatqvdihqriivi
dvsenrderlvlinpelleksgetgieegclsipeqralvpraekvkiraldrdgkpfel
eadgllaiciqhemdhlvgklfmdylsplkqqrirqkvekldrlkara
>d1bs7a_ 4.137.1.1.1 Peptide deformylase {Escherichia coli}
svlqvlhipderlrkvakpveevnaeiqrivddmfetmyaeegiglaatqvdihqriivi
dvsenrderlvlinpelleksgetgieegclsipeqralvpraekvkiraldrdgkpfel
eadgllaiciqhemdhlvgklfmdylsplkqqrirqkvekldrlkara
>d1bs7b_ 4.137.1.1.1 Peptide deformylase {Escherichia coli}
svlqvlhipderlrkvakpveevnaeiqrivddmfetmyaeegiglaatqvdihqriivi
dvsenrderlvlinpelleksgetgieegclsipeqralvpraekvkiraldrdgkpfel
eadgllaiciqhemdhlvgklfmdylsplkqqrirqkvekldrlkara
>d1bs7c_ 4.137.1.1.1 Peptide deformylase {Escherichia coli}
svlqvlhipderlrkvakpveevnaeiqrivddmfetmyaeegiglaatqvdihqriivi
dvsenrderlvlinpelleksgetgieegclsipeqralvpraekvkiraldrdgkpfel
eadgllaiciqhemdhlvgklfmdylsplkqqrirqkvekldrlkara
>d1bs8a_ 4.137.1.1.1 Peptide deformylase {Escherichia coli}
svlqvlhipderlrkvakpveevnaeiqrivddmfetmyaeegiglaatqvdihqriivi
dvsenrderlvlinpelleksgetgieegclsipeqralvpraekvkiraldrdgkpfel
eadgllaiciqhemdhlvgklfmdylsplkqqrirqkvekldrlkara
>d1bs8b_ 4.137.1.1.1 Peptide deformylase {Escherichia coli}
svlqvlhipderlrkvakpveevnaeiqrivddmfetmyaeegiglaatqvdihqriivi
dvsenrderlvlinpelleksgetgieegclsipeqralvpraekvkiraldrdgkpfel
eadgllaiciqhemdhlvgklfmdylsplkqqrirqkvekldrlkara
>d1bs8c_ 4.137.1.1.1 Peptide deformylase {Escherichia coli}
svlqvlhipderlrkvakpveevnaeiqrivddmfetmyaeegiglaatqvdihqriivi
dvsenrderlvlinpelleksgetgieegclsipeqralvpraekvkiraldrdgkpfel
eadgllaiciqhemdhlvgklfmdylsplkqqrirqkvekldrlkara
>d1bs9__ 3.16.7.1.2 Acetylxylan esterase {Penicillium purpurogenum}
scpaihvfgarettaspgygssstvvngvlsaypgstaeainypacggqsscggasysss
vaqgiaavasavnsfnsqcpstkivlvgysqggeimdvalcgggdpnqgytntavqlsss
avnmvkaaifmgdpmfraglsyevgtcaaggfdqrpagfscpsaakiksycdasdpyccn
gsnaathqgygseygsqalafvksklg
>d1bsaa_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
intfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksvggdifsnregkl
pgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1bsab_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
intfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksvggdifsnregkl
pgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1bsac_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
intfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksvggdifsnregkl
pgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1bsba_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadvnytsgfrnsdrilyssdwliykttdhyqtftkir
>d1bsbb_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadvnytsgfrnsdrilyssdwliykttdhyqtftkir
>d1bsbc_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadvnytsgfrnsdrilyssdwliykttdhyqtftkir
>d1bsca_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrvlyssdwliykttdhyqtftkir
>d1bscb_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
intfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregkl
pgksgrtwreadinytsgfrnsdrvlyssdwliykttdhyqtftkir
>d1bscc_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrvlyssdwliykttdhyqtftkir
>d1bsda_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
intfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregkl
pgksgrtwreadinytsgfrnsdrilyssdwlvykttdhyqtftkir
>d1bsdb_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
intfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregkl
pgksgrtwreadinytsgfrnsdrilyssdwlvykttdhyqtftkir
>d1bsdc_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
intfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregkl
pgksgrtwreadinytsgfrnsdrilyssdwlvykttdhyqtftkir
>d1bsea_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrivyssdwliykttdhyqtftkir
>d1bseb_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrivyssdwliykttdhyqtftkir
>d1bsec_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrivyssdwliykttdhyqtftkir
>d1bsfa_ 4.91.1.1.3 Thymidylate synthase {Bacillus subtilis}
tqfdkqynsiikdiinngisdeefdvatkwdsdgtpahtlsviskqmrfdnsevpilttk
kvawktaikellwiwqlksndvndlnmmgvhiwdqwkqedgtighaygfqlgkknrslng
ekvdqvdyllhqlknnpssrrhitmlwnpdeldamaltpcvyetqwyvkhgklhlevrar
sndmalgnpfnvfqynvlqrmiaqvtgyelgeyifnigdchvytrhidnlkiqmereqfe
apelwinpevkdfydftiddfklinykhgdkllfevav
>d1bsfb_ 4.91.1.1.3 Thymidylate synthase {Bacillus subtilis}
tqfdkqynsiikdiinngisdeefdvatkwdsdgtpahtlsviskqmrfdnsevpilttk
kvawktaikellwiwqlksndvndlnmmgvhiwdqwkqedgtighaygfqlgkknrslng
ekvdqvdyllhqlknnpssrrhitmlwnpdeldamaltpcvyetqwyvkhgklhlevrar
sndmalgnpfnvfqynvlqrmiaqvtgyelgeyifnigdchvytrhidnlkiqmereqfe
apelwinpevkdfydftiddfklinykhgdkllfevav
>d1bsg__ 5.3.1.1.9 beta-Lactamase, class A {Streptomyces albus G}
sdaerrlaglerasgarlgvyaydtgsgrtvayradelfpmcsvfktlssaavlrdldrn
geflsrrilytqddveqadgapetgkpqnlangmtveelcevsitasdncaanlmlrelg
gpaavtrfvrslgdrvtrldrwepelnsaepgrvtdttspraitrtygrlvlgdalnprd
rrlltswllanttsgdrfraglpddwtlgdktgagrygtnndagvtwppgrapivltvlt
akteqdaarddglvadaarvlaetlg
>d1bsh_1 1.2.6.1.1 (87-138) Epsilon subunit of F1F0-ATP synthase C-terminal domain {Escherichia coli}
qdldearameakrkaeehissshgdvdyaqasaelakaiaqlrvieltkkam
>d1bsh_2 2.81.1.1.1 (1-86) Epsilon subunit of F1F0-ATP synthase N-terminal domain {Escherichia coli}
amtyhldvvsaeqqmfsglvekiqvtgsegelgiypghaplltaikpgmirivkqhghee
fiylsggilevqpgnvtvladtairg
>d1bsi_1 2.62.1.1.9 (404-496) Animal alpha-amylase {Human (Homo sapiens)}
qpftnwydngsnqvafgrgnrgfivfnnddwsfsltlqtglpagtycdvisgdkingnct
gikiyvsddgkahfsisnsaedpfiaihaeskl
>d1bsi_2 3.1.7.1.9 (2-403) Animal alpha-amylase {Human (Homo sapiens)}
yspntqqgrtsivhlfewrwvdialecerylapkgfggvqvsppnenvaiynpfrpwwer
yqpvsyklctrsgnedefrnmvtrcnnvgvriyvdavinhmcgnavsagtsstcgsyfnp
gsrdfpavpysgwdfndgkcktgsgdienyndatqvrdcrltglldlalekdyvrskiae
ymnhlidigvagfrldaskhmwpgdikaildklhnlnsnwfpagskpfiyqevidlggep
ikssdyfgngrvtefkygaklgtvirkwngekmsylknwgegwgfvpsdralvfvdnhdn
qrghgaggasiltfwdarlykmavgfmlahpygftrvmssyrwprqfqngndvndwvgpp
nnngvikevtinpdttcgndwvcehrwrqirnmvifrnvvdg
>d1bsla_ 3.1.14.1.1 Bacterial luciferase (alkanal monooxygenase) {Vibrio harveyi}
mkfglfflnfmnskrssdqvieemldtahyvdqlkfdtlavyenhfsnngvvgapltvag
fllgmtknakvaslnhvitthhpvrvaeeaclldqmsegrfafgfsdceksadmrffnrp
tdsqfqlfsechkiindafttgychpnndfysfpkisvnphafteggpaqfvnatskevv
ewaaklglplvfrwddsnaqrkeyaglyhevaqahgvdvsqvrhkltllvnqnvdgeaar
aearvyleefvresysntdfeqkmgellsenaigtyeestqaarvaieccgaadllmsfe
smedkaqqravidvvnanivkyh
>d1bslb_ 3.1.14.1.1 Bacterial luciferase (alkanal monooxygenase) {Vibrio harveyi}
mkfglfflnfmnskrssdqvieemldtahyvdqlkfdtlavyenhfsnngvvgapltvag
fllgmtknakvaslnhvitthhpvrvaeeaclldqmsegrfafgfsdceksadmrffnrp
tdsqfqlfsechkiindafttgychpnndfysfpkisvnphafteggpaqfvnatskevv
ewaaklglplvfrwddsnaqrkeyaglyhevaqahgvdvsqvrhkltllvnqnvdgeaar
aearvyleefvresysntdfeqkmgellsenaigtyeestqaarvaieccgaadllmsfe
smedkaqqravidvvnanivkyhs
>d1bsma1 1.2.7.1.9 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1bsma2 4.37.1.1.9 (87-201) Cambialistic superoxide dismutase {Propionibacterium freudenreichii, shermani}
saperptdelgaaideffgsfdnmkaqftaaatgiqgsgwaslvwdplgkrintlqfydh
qnnlpagsipllqldmwehafylqyknvkgdyvkswwnvvnwddvalrfsearva
>d1bsmb1 1.2.7.1.9 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1bsmb2 4.37.1.1.9 (87-201) Cambialistic superoxide dismutase {Propionibacterium freudenreichii, shermani}
saperptdelgaaideffgsfdnmkaqftaaatgiqgsgwaslvwdplgkrintlqfydh
qnnlpagsipllqldmwehafylqyknvkgdyvkswwnvvnwddvalrfsearva
>d1bsn_1 1.2.6.1.1 (87-138) Epsilon subunit of F1F0-ATP synthase C-terminal domain {Escherichia coli}
qdldearameakrkaeehissshgdvdyaqasaelakaiaqlrvieltkkam
>d1bsn_2 2.81.1.1.1 (1-86) Epsilon subunit of F1F0-ATP synthase N-terminal domain {Escherichia coli}
amtyhldvvsaeqqmfsglvekiqvtgsegelgiypghaplltaikpgmirivkqhghee
fiylsggilevqpgnvtvladtairg
>d1bso__ 2.53.1.1.8 beta-Lactoglobulin {Bovine (Bos taurus)}
livtqtmkgldiqkvagtwyslamaasdislldaqsaplrvyveelkptpegdleillqk
wendecaqkkiiaektkipavfkidalnenkvlvldtdykkyllfcmensaepeqslvcq
clvrtpevddealekfdkalkalpmhirlsfnptqleeqchi
>d1bspa_ 4.91.1.1.3 Thymidylate synthase {Bacillus subtilis}
tqfdkqynsiikdiinngisdeefdvrtkwdsdgtpahtlsviskqmrfdnsevpilttk
kvawktaikellwiwqlksndvndlnmmgvhiwdqwkqedgtighaygfqlgkknrslng
ekvdqvdyllhqlknnpssrrhitmlwnpdeldamaltpcvyetqwyvkhgklhlevrar
sndmalgnpfnvfqynvlqrmiaqvtgyelgeyifnigdchvytrhidnlkiqmereqfe
apelwinpevkdfydftiddfklinykhgdkllfevav
>d1bspb_ 4.91.1.1.3 Thymidylate synthase {Bacillus subtilis}
tqfdkqynsiikdiinngisdeefdvrtkwdsdgtpahtlsviskqmrfdnsevpilttk
kvawktaikellwiwqlksndvndlnmmgvhiwdqwkqedgtighaygfqlgkknrslng
ekvdqvdyllhqlknnpssrrhitmlwnpdeldamaltpcvyetqwyvkhgklhlevrar
sndmalgnpfnvfqynvlqrmiaqvtgyelgeyifnigdchvytrhidnlkiqmereqfe
apelwinpevkdfydftiddfklinykhgdkllfevav
>d1bsq__ 2.53.1.1.8 beta-Lactoglobulin {Bovine (Bos taurus)}
livtqtmkgldiqkvagtwyslamaasdislldaqsaplrvyveelkptpegdleillqk
wendecaqkkiiaektkipavfkidalnenkvlvldtdykkyllfcmensaepeqslvcq
clvrtpevddealekfdkalkalpmhirlsfnptqleeqchi
>d1bsra_ 4.5.1.1.5 Seminal ribonucleasease {Bovine (Bos taurus)}
kesaaakferqhmdsgnspssssnycnlmmccrkmtqgkckpvntfvhesladvkavcsq
kkvtckngqtncyqskstmritdcretgsskypncaykttqvekhiivacggkpsvpvhf
dasv
>d1bsrb_ 4.5.1.1.5 Seminal ribonucleasease {Bovine (Bos taurus)}
kesaaakferqhmdsgnspssssnycnlmmccrkmtqgkckpvntfvhesladvkavcsq
kkvtckngqtncyqskstmritdcretgsskypncaykttqvekhiivacggkpsvpvhf
dasv
>d1bssa_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
lrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgyi
veepkqqnhypdftlykpsepnkkiaidikatytnkenekikftlggytsfirnntkniv
ypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdlag
sgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiyr
grk
>d1bssb_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikatytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgrk
>d1bsua_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgr
>d1bsub_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgr
>d1bsva_ 3.2.1.2.3 GDP-4-keto-6-deoxy-d-mannose epimerase/reductase (GDP-fucose synthetase) {Escherichia coli}
kqrvfiaghrgmvgsairrqleqrgdvelvlrtrdelnlldsravhdffaseridqvyla
aakvggivanntypadfiyqnmmiesniihaahqndvnkllflgssciypklakqpmaes
ellqgtleptnepyaiakiagiklcesynrqygrdyrsvmptnlygphdnfhpsnshvip
allrrfheataqnapdvvvwgsgtpmreflhvddmaaasihvmelahevwlentqpmlsh
invgtgvdctirelaqtiakvvgykgrvvfdaskpdgtprklldvtrlhqlgwyheisle
aglastyqwflenqdrf
>d1bswa_ 4.71.1.7.3 Snake venom metalloprotease {Five-pace snake (AgkistrodCH Aon acutus), acutolysin A}
fqrymeivivvdhsmvkkyngdsdsikawvyemintitesysylkidislsgleiwsgkd
lidveasagntlksfgewrakdlihrishdnaqlltatdfdgatiglayvasmcnpkrsv
gviqdhssvnrlvaitlahemahnlgvshdegscscggkscimspsisdetikyfsdcsy
iqcrdyiakenppciln
>d1bsxa_ 1.114.1.1.6 Thyroid hormone receptor beta (TR-beta) {Human (Homo sapiens)}
kpeptdeeweliktvteahvatnaqgshwkqkrkflpedigqapivnapeggkvdleafs
hftkiitpaitrvvdfakklpmfcelpcedqiillkgccmeimslraavrydpesetltl
ngemavtrgqlkngglgvvsdaifdlgmslssfnlddtevallqavllmssdrpglacve
riekyqdsfllafehyinyrkhhvthfwpkllmkvtdlrmigachasrflhmkvecptel
fpplflevfed
>d1bsxb_ 1.114.1.1.6 Thyroid hormone receptor beta (TR-beta) {Human (Homo sapiens)}
kpeptdeeweliktvteahvatnaqgshwkqkrkflpedigqapivnapeggkvdleafs
hftkiitpaitrvvdfakklpmfcelpcedqiillkgccmeimslraavrydpesetltl
ngemavtrgqlkngglgvvsdaifdlgmslssfnlddtevallqavllmssdrpglacve
riekyqdsfllafehyinyrkhhvthfwpkllmkvtdlrmigachasrflhmkvecptel
fpplflevfed
>d1bsy__ 2.53.1.1.8 beta-Lactoglobulin {Bovine (Bos taurus)}
livtqtmkgldiqkvagtwyslamaasdislldaqsaplrvyveelkptpegdleillqk
wendecaqkkiiaektkipavfkidalnenkvlvldtdykkyllfcmensaepeqslvcq
clvrtpevddealekfdkalkalpmhirlsfnptqleeqchi
>d1bsza_ 4.137.1.1.1 Peptide deformylase {Escherichia coli}
svlqvlhipderlrkvakpveevnaeiqrivddmfetmyaeegiglaatqvdihqriivi
dvsenrderlvlinpelleksgetgieegclsipeqralvpraekvkiraldrdgkpfel
eadgllaiciqhemdhlvgklfmdylsplkqqrirqkvekldrlkara
>d1bszb_ 4.137.1.1.1 Peptide deformylase {Escherichia coli}
svlqvlhipderlrkvakpveevnaeiqrivddmfetmyaeegiglaatqvdihqriivi
dvsenrderlvlinpelleksgetgieegclsipeqralvpraekvkiraldrdgkpfel
eadgllaiciqhemdhlvgklfmdylsplkqqrirqkvekldrlkara
>d1bszc_ 4.137.1.1.1 Peptide deformylase {Escherichia coli}
svlqvlhipderlrkvakpveevnaeiqrivddmfetmyaeegiglaatqvdihqriivi
dvsenrderlvlinpelleksgetgieegclsipeqralvpraekvkiraldrdgkpfel
eadgllaiciqhemdhlvgklfmdylsplkqqrirqkvekldrlkara
>d1bt0__ 4.13.2.1.6 Rub1 {Mouse-ear cress (Arabidopsis thaliana)}
mlikvktltgkeieidieptdtidrikerveekegippvqqrliyagkqladdktakdyn
ieggsvlhlvlal
>d1bt1a_ 1.83.1.2.1 Catechol oxidase {Sweet potato (Ipomoea batatas)}
apiqapeiskcvvppadlppgavvdnccppvasnivdyklpavttmkvrpaahtmdkdai
akfakavelmkalpaddprnfyqqalvhcaycnggydqvnfpdqeiqvhnswlffpfhrw
ylyfyerilgkligdpsfglpfwnwdnpggmvlpdflndstsslydsnrnqshlppvvvd
lgyngadtdvtdqqritdnlalmykqmvtnagtaelflgkayragdapspgagsietsph
ipihrwvgdprntnnedmgnfysagrdiafychhsnvdrmwtiwqqlagkprkrdytdsd
wlnatflfydengqavkvrigdsldnqkmgykyaktplpwl
>d1bt1b_ 1.83.1.2.1 Catechol oxidase {Sweet potato (Ipomoea batatas)}
apiqapeiskcvvppadlppgavvdnccppvasnivdyklpavttmkvrpaahtmdkdai
akfakavelmkalpaddprnfyqqalvhcaycnggydqvnfpdqeiqvhnswlffpfhrw
ylyfyerilgkligdpsfglpfwnwdnpggmvlpdflndstsslydsnrnqshlppvvvd
lgyngadtdvtdqqritdnlalmykqmvtnagtaelflgkayragdapspgagsietsph
ipihrwvgdprntnnedmgnfysagrdiafychhsnvdrmwtiwqqlagkprkrdytdsd
wlnatflfydengqavkvrigdsldnqkmgykyaktplpwl
>d1bt2a_ 1.83.1.2.1 Catechol oxidase {Sweet potato (Ipomoea batatas)}
apiqapeiskcvvppadlppgavvdnccppvasnivdyklpavttmkvrpaahtmdkdai
akfakavelmkalpaddprnfyqqalvhcaycnggydqvnfpdqeiqvhnswlffpfhrw
ylyfyerilgkligdpsfglpfwnwdnpggmvlpdflndstsslydsnrnqshlppvvvd
lgyngadtdvtdqqritdnlalmykqmvtnagtaelflgkayragdapspgagsietsph
ipihrwvgdprntnnedmgnfysagrdiafychhsnvdrmwtiwqqlagkprkrdytdsd
wlnatflfydengqavkvrigdsldnqkmgykyaktplpwl
>d1bt2b_ 1.83.1.2.1 Catechol oxidase {Sweet potato (Ipomoea batatas)}
apiqapeiskcvvppadlppgavvdnccppvasnivdyklpavttmkvrpaahtmdkdai
akfakavelmkalpaddprnfyqqalvhcaycnggydqvnfpdqeiqvhnswlffpfhrw
ylyfyerilgkligdpsfglpfwnwdnpggmvlpdflndstsslydsnrnqshlppvvvd
lgyngadtdvtdqqritdnlalmykqmvtnagtaelflgkayragdapspgagsietsph
ipihrwvgdprntnnedmgnfysagrdiafychhsnvdrmwtiwqqlagkprkrdytdsd
wlnatflfydengqavkvrigdsldnqkmgykyaktplpwl
>d1bt3a_ 1.83.1.2.1 Catechol oxidase {Sweet potato (Ipomoea batatas)}
apiqapeiskcvvppadlppgavvdnccppvasnivdyklpavttmkvrpaahtmdkdai
akfakavelmkalpaddprnfyqqalvhcaycnggydqvnfpdqeiqvhnswlffpfhrw
ylyfyerilgkligdpsfglpfwnwdnpggmvlpdflndstsslydsnrnqshlppvvvd
lgyngadtdvtdqqritdnlalmykqmvtnagtaelflgkayragdapspgagsietsph
ipihrwvgdprntnnedmgnfysagrdiafychhsnvdrmwtiwqqlagkprkrdytdsd
wlnatflfydengqavkvrigdsldnqkmgykyaktplpwl
>d1bt4__ 3.57.1.4.4 Phosphoserine aminotransferase, PSAT {Bacillus circulans alkalophilus}
seraynfnagpaalplevleraqaefvdyqhtgmsimemshrgavyeavhneaqarllal
lgnptgykvlfiqggastqfamipmnflkegqtanyvmtgswaskalkeakligdthvaa
sseasnymtlpklqeiqlqdnaaylhltsnetiegaqfkafpdtgsvpligdmssdilsr
pfdlnqfglvyagaqknlgpsgvtvvivredlvaespkhlptmlrydtyvknnslyntpp
sfgiymvnevlkwieergglegvqqanrkkasliydaidqsggfyrgcvdvdsrsdmnit
frlaseelekefvkaseqegfvglkghrsvgglrasiynavpyescealvqfmehfkrsr
g
>d1bt5a_ 5.3.1.1.3 beta-Lactamase, class A {Escherichia coli, TEM-1}
hpetlvkvkdaedqlgarvgyieldlnsgkilesfrpeerfpmmstfkvllcgavlsrid
agqeqlgrrihysqndlveyspvtekhltdgmtvrelcsaaitmsdntaanlllttiggp
keltaflhnmgdhvtrldrwepelneaipnderdttmpvamattlrklltgelltlasrq
qlidwmeadkvagpllrsalpagwfiadksgagergsrgiiaalgpdgkpsrivviyttg
sqatmdernrqiaeigaslikhw
>d1bt6a_ 1.42.1.2.5 Calcyclin (S100) {Human (Homo sapiens), P11 s100a10, calpactin}
psqmehametmmftfhkfagdkgyltkedlrvlmekefpgflenqkdplavdkimkdldq
crdgkvgfqsffsliagltiacndyfvvhmk
>d1bt6b_ 1.42.1.2.5 Calcyclin (S100) {Human (Homo sapiens), P11 s100a10, calpactin}
psqmehametmmftfhkfagdkgyltkedlrvlmekefpgflenqkdplavdkimkdldq
crdgkvgfqsffsliagltiacndyfvvhmk
>d1bt7__ 2.41.1.3.3 NS3 protease {Human hepatitis C virus, Bk strain}
tgrdknqvegevqvvstatqsflatcvngvcwtvyhgagsktlagpkgpitqmytnvdqd
lvgwqappgarsltpctcgssdlylvtrhadvipvrrrgdsrgsllsprpvsylkgssgg
pllcpsghavgifraavctrgvakavdfvpvesmettmraskkkk
>d1bt8a1 1.2.7.1.9 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1bt8a2 4.37.1.1.9 (87-201) Cambialistic superoxide dismutase {Propionibacterium freudenreichii, shermani}
saperptdelgaaideffgsfdnmkaqftaaatgiqgsgwaslvwdplgkrintlqfydh
qnnlpagsipllqldmwehafylqyknvkgdyvkswwnvvnwddvalrfsearva
>d1bt8b1 1.2.7.1.9 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1bt8b2 4.37.1.1.9 (87-201) Cambialistic superoxide dismutase {Propionibacterium freudenreichii, shermani}
saperptdelgaaideffgsfdnmkaqftaaatgiqgsgwaslvwdplgkrintlqfydh
qnnlpagsipllqldmwehafylqyknvkgdyvkswwnvvnwddvalrfsearva
>d1bt9__ 6.4.3.1.1 Porin {Escherichia coli, different sequences}
aeiynkdgnkvdlygkavglhyfskgngensyggngdmtyarlgfkgetqinsdltgygq
weynfqgnnsegaaaqtgnktrlafaglkyadvgsfdygrnygvvydalgytdmlpefgg
dtaysddffvgrvggvatyrnsnffglvdglnfavqylgknerdtarrsngdgvggsisy
eyegfgivgaygaadrtnlqeaqplgngkkaeqwatglkydanniylaanygetrnatpi
tnkftntsgfanktqdvllvaqyqfdfglrpsiaytkskakdvegigdvdlvnyfevgat
yyfnknmstyvdyiinqidsdnklgvgsddtvavgivyqf
>d1bta__ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdcltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegcditiils
>d1btb__ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdcltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegcditiils
>d1btc__ 3.1.7.2.1 beta-Amylase {Soybean (Glycine max)}
snmllnyvpvyvmlplgvvnvdnvfedpdglkeqllqlraagvdgvmvdvwwgiielkgp
kqydwrayrslfqlvqecgltlqaimsfhqcggnvgdivnipipqwvldigesnhdifyt
nrsgtrnkeyltvgvdnepifhgrtaieiysdymksfrenmsdflesgliidievglgpa
gelrypsypqsqgwefprigefqcydkylkadfkaavaraghpewelpddagkyndvpes
tgffksngtyvtekgkffltwysnkllnhgdqildeankaflgckvklaikvsgihwwyk
venhaaeltagyynlndrdgyrpiarmlsrhhailnftclemrdseqpsdaksgpqelvq
qvlsggwredirvagenalprydataynqiilnakpqgvnnngppklsmfgvtylrlsdd
llqksnfnifkkfvlkmhadqdycanpqkynhaitplkpsapkipievlleatkptlpfp
wlpetdmkvdg
>d1btea_ 7.7.1.4.1 Extracellular domain of the type II activin receptor {Mouse (Mus musculus)}
etqeclffnanwerdrtnqtgvepcygdkdkrrhcfatwknisgsieivkqgcwlddinc
ydrtdciekkdspevyfcccegnmcnekfsyfpeme
>d1bteb_ 7.7.1.4.1 Extracellular domain of the type II activin receptor {Mouse (Mus musculus)}
tqeclffnanwerdrtnqtgvepcygdkdkrrhcfatwknisgsieivkqgcwlddincy
drtdciekkdspevyfcccegnmcnekfsyfp
>d1btga_ 7.17.1.3.3 beta-Nerve growth factor {Mouse (Mus musculus)}
gefsvcdsvsvwvgdkttatdikgkevtvlaevninnsvfrqyffetkcrasnpvesgcr
gidskhwnsycttthtfvkalttdekqaawrfiridtacvcvlsrkat
>d1btgb_ 7.17.1.3.3 beta-Nerve growth factor {Mouse (Mus musculus)}
gefsvcdsvsvwvgdkttatdikgkevtvlaevninnsvfrqyffetkcrasnpvesgcr
gidskhwnsycttthtfvkalttdekqaawrfiridtacvcvlsrkatr
>d1btgc_ 7.17.1.3.3 beta-Nerve growth factor {Mouse (Mus musculus)}
gefsvcdsvsvwvgdkttatdikgkevtvlaevninnsvfrqyffetkcrasnpvesgcr
gidskhwnsycttthtfvkalttdekqaawrfiridtacvcvlsrkatr
>e1bth.1h 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwttnvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacqgdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvi
>e1bth.1l 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
geadcglrplfekksledkterellesyidg
>e1bth.2j 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
geadcglrplfekksledkterellesyidg
>e1bth.2k 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwttnvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacqgdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvi
>d1bthp_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d1bthq_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d1bti__ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryaynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d1btja_ 3.84.1.2.8 Transferrin {Human (Homo sapiens)}
ktvrwcavseheatkcqsfrdhmksvipsdgpsvacvkkasyldciraiaaneadavtld
aglvydaylapnnlkpvvaefygskedpqtfyyavavvkkdsgfqmnqlrgkkschtglg
rsagwnipigllycdlpeprkplekavanffsgscapcadgtdfpqlcqlcpgcgcstln
qyfgysgafkclkdgagdvafvkhstifenlankadrdqyellcldntrkpvdeykdchl
aqvpshtvvarsmggkedliwellnqaqehfgkdkskefqlfssphgkdllfkdsahgfl
kvpprmdakmylgyeyvtairnlregtcpeapt
>d1btjb_ 3.84.1.2.8 Transferrin {Human (Homo sapiens)}
ktvrwcavseheatkcqsfrdhmksvipsdgpsvacvkkasyldciraiaaneadavtld
aglvydaylapnnlkpvvaefygskedpqtfyyavavvkkdsgfqmnqlrgkkschtglg
rsagwnipigllycdlpeprkplekavanffsgscapcadgtdfpqlcqlcpgcgcstln
qyfgysgafkclkdgagdvafvkhstifenlankadrdqyellcldntrkpvdeykdchl
aqvpshtvvarsmggkedliwellnqaqehfgkdkskefqlfssphgkdllfkdsahgfl
kvpprmdakmylgyeyvtairnlregtcpeapt
>d1btka_ 2.49.1.1.5 Bruton's tyrosine kinase {Human (Homo sapiens)}
aavilesiflkrsqqkkktsplnfkkclflltvhklsyyeydfergrrgskkgsidveki
tcvetvvpeknppperqiprrgeessemeqisiierfpypfqvvydegplyvfspteelr
krwihqlknvirynsdlvqkyhpcfwidgqylccsqtaknamgcqilen
>d1btkb_ 2.49.1.1.5 Bruton's tyrosine kinase {Human (Homo sapiens)}
aavilesiflkrsqqkkktsplnfkkclflltvhklsyyeydfergrrgskkgsidveki
tcvetvvpeknppperqiprrgeessemeqisiierfpypfqvvydegplyvfspteelr
krwihqlknvirynsdlvqkyhpcfwidgqylccsqtaknamgcqilen
>d1btl__ 5.3.1.1.3 beta-Lactamase, class A {Escherichia coli, TEM-1}
hpetlvkvkdaedqlgarvgyieldlnsgkilesfrpeerfpmmstfkvllcgavlsrid
agqeqlgrrihysqndlveyspvtekhltdgmtvrelcsaaitmsdntaanlllttiggp
keltaflhnmgdhvtrldrwepelneaipnderdttmpvamattlrklltgelltlasrq
qlidwmeadkvagpllrsalpagwfiadksgagergsrgiiaalgpdgkpsrivviyttg
sqatmdernrqiaeigaslikhw
>d1btma_ 3.1.1.1.10 Triosephosphate isomerase {Bacillus stearothermophilus}
rkpiiagnwkmhktlaeavqfvedvkghvppadevisvvcapflfldrlvqaadgtdlki
gaqtmhfadqgaytgevspvmlkdlgvtyvilghserrqmfaetdetvnkkvlaaftrgl
ipiiccgesleereagqtnavvasqvekalagltpeqvkqaviayepiwaigtgksstpe
dansvcghirsvvsrlfgpeaaeairiqyggsvkpdnirdflaqqqidgplvggaslepa
sflqlveagrh
>d1btmb_ 3.1.1.1.10 Triosephosphate isomerase {Bacillus stearothermophilus}
rkpiiagnwkmhktlaeavqfvedvkghvppadevisvvcapflfldrlvqaadgtdlki
gaqtmhfadqgaytgevspvmlkdlgvtyvilghserrqmfaetdetvnkkvlaaftrgl
ipiiccgesleereagqtnavvasqvekalagltpeqvkqaviayepiwaigtgksstpe
dansvcghirsvvsrlfgpeaaeairiqyggsvkpdnirdflaqqqidgplvggaslepa
sflqlveagrh
>d1btn__ 2.49.1.1.2 beta-spectrin {Mouse (Mus musculus), brain}
megflnrkheweahnkkassrswhnvycvinnqemgfykdaksaasgipyhsevpvslke
aicevaldykkkkhvfklrlsdgneylfqakddeemntwiqaissa
>d1btoa1 2.31.1.2.1 (1-174,325-374) Alcohol dehydrogenase {Horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1btoa2 3.2.1.1.1 (175-324) Alcohol dehydrogenase {Horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1btob1 2.31.1.2.1 (1-174,325-374) Alcohol dehydrogenase {Horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1btob2 3.2.1.1.1 (175-324) Alcohol dehydrogenase {Horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1btoc1 2.31.1.2.1 (1-174,325-374) Alcohol dehydrogenase {Horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1btoc2 3.2.1.1.1 (175-324) Alcohol dehydrogenase {Horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1btod1 2.31.1.2.1 (1-174,325-374) Alcohol dehydrogenase {Horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1btod2 3.2.1.1.1 (175-324) Alcohol dehydrogenase {Horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1btp__ 2.41.1.2.1 Trypsin(ogen) {Bovine (Bos taurus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1btu__ 2.41.1.2.15 Elastase {Porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1btv__ 4.103.3.1.1 Major birch pollen allergen Bet v 1 {White birch (Betula verrucosa)}
gvfnyetettsvipaarlfkafildgdnlfpkvapqaissveniegnggpgtikkisfpe
glpfkyvkdrvdevdhtnfkynysvieggpigdtlekisneikivatpdggsilkisnky
htkgdhevkaeqvkaskemgetllravesyllahsdayn
>d1btwa_ 2.41.1.2.1 Trypsin(ogen) {Bovine (Bos taurus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1btxa_ 2.41.1.2.1 Trypsin(ogen) {Bovine (Bos taurus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1bty__ 2.41.1.2.1 Trypsin(ogen) {Bovine (Bos taurus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1btza_ 2.41.1.2.1 Trypsin(ogen) {Bovine (Bos taurus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1bu1a_ 2.30.2.1.10 Hemapoetic cell kinase Hck {Human (Homo sapiens)}
iivvalydyeaihhedlsfqkgdqmvvleesgewwkarslatrkegyipsnyvarvd
>d1bu1b_ 2.30.2.1.10 Hemapoetic cell kinase Hck {Human (Homo sapiens)}
iivvalydyeaihhedlsfqkgdqmvvleesgewwkarslatrkegyipsnyvarvd
>d1bu1c_ 2.30.2.1.10 Hemapoetic cell kinase Hck {Human (Homo sapiens)}
iivvalydyeaihhedlsfqkgdqmvvleesgewwkarslatrkegyipsnyvarv
>d1bu1d_ 2.30.2.1.10 Hemapoetic cell kinase Hck {Human (Homo sapiens)}
iivvalydyeaihhedlsfqkgdqmvvleesgewwkarslatrkegyipsnyvarv
>d1bu1e_ 2.30.2.1.10 Hemapoetic cell kinase Hck {Human (Homo sapiens)}
iivvalydyeaihhedlsfqkgdqmvvleesgewwkarslatrkegyipsnyvarvd
>d1bu1f_ 2.30.2.1.10 Hemapoetic cell kinase Hck {Human (Homo sapiens)}
iivvalydyeaihhedlsfqkgdqmvvleesgewwkarslatrkegyipsnyvarv
>d1bu2a1 1.73.1.1.4 (22-148) Viral cyclin {Herpes virus saimiri}
rvlnnlklrelllpkftslweiqtevtvdnrtilltwmhllcesfeldksvfplsvsild
rylckkqgtkktlqkigaacvligskirtvkpmtvskltylscdcftnlelinqekdile
alkwdte
>d1bu2a2 1.73.1.1.4 (149-250) Viral cyclin {Herpes virus saimiri}
avlatdfliplcnalkipedlwpqlyeaasttickaliqpniallspglicaggllttie
tdntncrpwtcyledlssilnfstntvrtvkdqvseafslyd
>d1bu3__ 1.42.1.4.6 Parvalbumin {Silver hake (Merluccius bilinearis)}
afsgiladadvaaalkaceaadsfnykaffakvgltaksaddikkaffvidqdksgfiee
delklflqvfsagaraltdaetkaflkagdsdgdgaigvdewaalvka
>d1bu4__ 4.1.1.1.3 RNase T1 {Aspergillus oryzae}
acdytcgsncysssdvstaqaagyklhedgetvgsnsyphkynnyegfdfsvsspyyewp
ilssgdvysggspgadrvvfnennqlagvithtgasgnnfvect
>d1bu5a_ 3.16.4.1.2 Flavodoxin {Desulfovibrio vulgaris}
pkalivygsttgnteytaetiareladagyevdsrdaasveagglfegfdlvllgcstwg
ddsielqddfiplfdsleetgaqgrkvacfgcgdssyeyfcgavdaieeklknlgaeivq
dglridgdpraarddivgwahdvrgai
>d1bu5b_ 3.16.4.1.2 Flavodoxin {Desulfovibrio vulgaris}
pkalivygsttgnteytaetiareladagyevdsrdaasveagglfegfdlvllgcstwg
ddsielqddfiplfdsleetgaqgrkvacfgcgdssyeyfcgavdaieeklknlgaeivq
dglridgdpraarddivgwahdvrgai
>d1bu6o1 3.46.1.3.1 (3-253) Glycerol kinase {Escherichia coli}
kkyivaldqgttssravvmdhdaniisvsqrefeqiypkpgwvehdpmeiwatqsstlve
vlakadissdqiaaigitnqrettivweketgkpiynaivwqcrrtaeicehlkrdgled
yirsntglvidpyfsgtkvkwildhvegsrerarrgellfgtvdtwliwkmtqgrvhvtd
ytnasrtmlfnihtldwddkmlevldipremlpevrrssevygqtniggkggtripisgi
agdqqaalfgq
>d1bu6o2 3.46.1.3.1 (254-499) Glycerol kinase {Escherichia coli}
lcvkegmakntygtgcfmlmntgekavksengllttiacgptgevnyalegavfmagasi
qwlrdemklindaydseyfatkvqntngvyvvpaftglgapywdpyargaifgltrgvna
nhiiratlesiayqtrdvleamqadsgirlhalrvdggavannflmqfqsdilgtrverp
evrevtalgaaylaglavgfwqnldelqekavierefrpgietternyryagwkkavkra
maweeh
>d1bu6x1 3.46.1.3.1 (3-253) Glycerol kinase {Escherichia coli}
kkyivaldqgttssravvmdhdaniisvsqrefeqiypkpgwvehdpmeiwatqsstlve
vlakadissdqiaaigitnqrettivweketgkpiynaivwqcrrtaeicehlkrdgled
yirsntglvidpyfsgtkvkwildhvegsrerarrgellfgtvdtwliwkmtqgrvhvtd
ytnasrtmlfnihtldwddkmlevldipremlpevrrssevygqtniggkggtripisgi
agdqqaalfgq
>d1bu6x2 3.46.1.3.1 (254-500) Glycerol kinase {Escherichia coli}
lcvkegmakntygtgcfmlmntgekavksengllttiacgptgevnyalegavfmagasi
qwlrdemklindaydseyfatkvqntngvyvvpaftglgapywdpyargaifgltrgvna
nhiiratlesiayqtrdvleamqadsgirlhalrvdggavannflmqfqsdilgtrverp
evrevtalgaaylaglavgfwqnldelqekavierefrpgietternyryagwkkavkra
maweehd
>d1bu6y1 3.46.1.3.1 (2-253) Glycerol kinase {Escherichia coli}
ekkyivaldqgttssravvmdhdaniisvsqrefeqiypkpgwvehdpmeiwatqsstlv
evlakadissdqiaaigitnqrettivweketgkpiynaivwqcrrtaeicehlkrdgle
dyirsntglvidpyfsgtkvkwildhvegsrerarrgellfgtvdtwliwkmtqgrvhvt
dytnasrtmlfnihtldwddkmlevldipremlpevrrssevygqtniggkggtripisg
iagdqqaalfgq
>d1bu6y2 3.46.1.3.1 (254-500) Glycerol kinase {Escherichia coli}
lcvkegmakntygtgcfmlmntgekavksengllttiacgptgevnyalegavfmagasi
qwlrdemklindaydseyfatkvqntngvyvvpaftglgapywdpyargaifgltrgvna
nhiiratlesiayqtrdvleamqadsgirlhalrvdggavannflmqfqsdilgtrverp
evrevtalgaaylaglavgfwqnldelqekavierefrpgietternyryagwkkavkra
maweehd
>d1bu6z1 3.46.1.3.1 (3-253) Glycerol kinase {Escherichia coli}
kkyivaldqgttssravvmdhdaniisvsqrefeqiypkpgwvehdpmeiwatqsstlve
vlakadissdqiaaigitnqrettivweketgkpiynaivwqcrrtaeicehlkrdgled
yirsntglvidpyfsgtkvkwildhvegsrerarrgellfgtvdtwliwkmtqgrvhvtd
ytnasrtmlfnihtldwddkmlevldipremlpevrrssevygqtniggkggtripisgi
agdqqaalfgq
>d1bu6z2 3.46.1.3.1 (254-500) Glycerol kinase {Escherichia coli}
lcvkegmakntygtgcfmlmntgekavksengllttiacgptgevnyalegavfmagasi
qwlrdemklindaydseyfatkvqntngvyvvpaftglgapywdpyargaifgltrgvna
nhiiratlesiayqtrdvleamqadsgirlhalrvdggavannflmqfqsdilgtrverp
evrevtalgaaylaglavgfwqnldelqekavierefrpgietternyryagwkkavkra
maweehd
>d1bu7a_ 1.100.1.1.2 Cytochrome P450 {Bacillus megaterium}
tikempqpktfgelknlpllntdkpvqalmkiadelgeifkfeapgrvtrylssqrlike
acdesrfdknlsqalkfvrdfagdglftswtheknwkkahnillpsfsqqamkgyhammv
diavqlvqkwerlnadehievpedmtrltldtiglcgfnyrfnsfyrdqphpfitsmvra
ldeamnklqranpddpaydenkrqfqedikvmndlvdkiiadrkasgeqsddllthmlng
kdpetgeplddeniryqiitfliaghettsgllsfalyflvknphvlqkaaeeaarvlvd
pvpsykqvkqlkyvgmvlnealrlwptapafslyakedtvlggeyplekgdelmvlipql
hrdktiwgddveefrperfenpsaipqhafkpfgngqracigqqfalheatlvlgmmlkh
fdfedhtnyeldiketltlkpegfvvkakskkipl
>d1bu7b_ 1.100.1.1.2 Cytochrome P450 {Bacillus megaterium}
tikempqpktfgelknlpllntdkpvqalmkiadelgeifkfeapgrvtrylssqrlike
acdesrfdknlsqalkfvrdfagdglftswtheknwkkahnillpsfsqqamkgyhammv
diavqlvqkwerlnadehievpedmtrltldtiglcgfnyrfnsfyrdqphpfitsmvra
ldeamnklqranpddpaydenkrqfqedikvmndlvdkiiadrkasgeqsddllthmlng
kdpetgeplddeniryqiitfliaghettsgllsfalyflvknphvlqkaaeeaarvlvd
pvpsykqvkqlkyvgmvlnealrlwptapafslyakedtvlggeyplekgdelmvlipql
hrdktiwgddveefrperfenpsaipqhafkpfgngqracigqqfalheatlvlgmmlkh
fdfedhtnyeldiketltlkpegfvvkakskkipl
>d1bu8_1 2.11.1.2.6 (337-449) Pancreatic lipase, C-terminal domain {Rat (Rattus norvegicus)}
rwrykvsvtlsgakklsgyilvalygnngnskqyeifkgslkpearhvrdidvdinvgei
qkvkflwnnkvinlfrptlgasqitvqsgvdgkeynfcssdtvredvlqslypc
>d1bu8_2 3.59.1.16.6 (1-336) Pancreatic lipase, N-terminal domain {Rat (Rattus norvegicus)}
kevcyghlgcfsndkpwagmlqrplkifpwspedidtrfllytnenpnnyqkisatepdt
ikfsnfqldrktrfivhgfidkgedgwlldmckkmfqvekvncicvdwrrgsrteytqas
yntrvvgaeiaflvqvlstemgyspenvhlighslgahvvgeagrrleghvgritgldpa
epcfqglpeevrldpsdamfvdvihtdsapiipylgfgmsqkvghldffpnggkempgcq
knilstivdingiwegtqnfvacnhlrsykyyassilnpdgflgypcssyekfqqndcfp
cpeegcpkmghyadqfegktatveqtvylntgdsgnft
>d1bu9a_ 1.110.2.1.4 p18ink4C(ink6) {Human (Homo sapiens)}
maepwgnelasaaargdleqltsllqnnvnvnaqngfgrtalqvmklgnpeiarrlllrg
anpdlkdrtgfavihdaaragfldtlqtllefqadvniednegnlplhlaakeghlrvve
flvkhtasnvghrnhkgdtacdlarlygrnevvslmqangaggatnlq
>d1buaa_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgr
>d1buab_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgr
>d1buca1 1.25.6.1.1 (233-383) Butyryl-CoA dehydrogenase {Megasphaera elsdenii}
gkgfkiammtldggrigvaaqalgiaeaaladaveyskqrvqfgkplckfqsisfkladm
kmqieaarnlvykaackkqegkpftvdaaiakrvasdvamrvtteavqifggygyseeyp
varhmrdakitqiyegtnevqlmvtggallr
>d1buca2 5.6.1.1.1 (1-232) Butyryl-CoA dehydrogenase {Megasphaera elsdenii}
mdfnltdiqqdflklahdfgekklaptvterdhkgiydkelidellslgitgayfeekyg
gsgddggdvlsyilaveelakydagvaitlsatvslcanpiwqfgteaqkekflvplveg
tklgafgltepnagtdasgqqtiatknddgtytlngskifitnggaadiyivfamtdksk
gnhgitafiledgtpgftygkkedkmgihtsqtmelvfqdvkvpaenmlgee
>d1bucb1 1.25.6.1.1 (233-383) Butyryl-CoA dehydrogenase {Megasphaera elsdenii}
gkgfkiammtldggrigvaaqalgiaeaaladaveyskqrvqfgkplckfqsisfkladm
kmqieaarnlvykaackkqegkpftvdaaiakrvasdvamrvtteavqifggygyseeyp
varhmrdakitqiyegtnevqlmvtggallr
>d1bucb2 5.6.1.1.1 (1-232) Butyryl-CoA dehydrogenase {Megasphaera elsdenii}
mdfnltdiqqdflklahdfgekklaptvterdhkgiydkelidellslgitgayfeekyg
gsgddggdvlsyilaveelakydagvaitlsatvslcanpiwqfgteaqkekflvplveg
tklgafgltepnagtdasgqqtiatknddgtytlngskifitnggaadiyivfamtdksk
gnhgitafiledgtpgftygkkedkmgihtsqtmelvfqdvkvpaenmlgee
>d1buda_ 4.71.1.7.3 Snake venom metalloprotease {Five-pace snake (AgkistrodCH Aon acutus), acutolysin A}
fqrymeivivvdhsmvkkyngdsdsikawvyemintitesysylkidislsgleiwsgkd
lidveasagntlksfgewrakdlihrishdnaqlltatdfdgatiglayvasmcnpkrsv
gviqdhssvnrlvaitlahemahnlgvshdegscscggkscimspsisdetikyfsdcsy
iqcrdyiskenppciln
>d1buea_ 5.3.1.1.8 beta-Lactamase, class A {Enterobacter cloacae, NMC-A carbapenemase}
ntkgideiknletdfngrigvyaldtgsgksfsyranerfplcssfkgflaaavlkgsqd
nrlnlnqivnyntrslefhspittkykdngmslgdmaaaalqysdngatniileryiggp
egmtkfmrsigdedfrldrweldlntaipgderdtstpaavakslktlalgnilseheke
tyqtwlkgnttgaarirasvpsdwvvgdktgscgaygtandyavvwpknrapliisvytt
knekeakhedkviaeasriaidnlk
>d1buga_ 1.83.1.2.1 Catechol oxidase {Sweet potato (Ipomoea batatas)}
apiqapeiskcvvppadlppgavvdnccppvasnivdyklpavttmkvrpaahtmdkdai
akfakavelmkalpaddprnfyqqalvhcaycnggydqvnfpdqeiqvhnswlffpfhrw
ylyfyerilgkligdpsfglpfwnwdnpggmvlpdflndstsslydsnrnqshlppvvvd
lgyngadtdvtdqqritdnlalmykqmvtnagtaelflgkayragdapspgagsietsph
ipihrwvgdprntnnedmgnfysagrdiafychhsnvdrmwtiwqqlagkprkrdytdsd
wlnatflfydengqavkvrigdsldnqkmgykyaktplpwl
>d1bugb_ 1.83.1.2.1 Catechol oxidase {Sweet potato (Ipomoea batatas)}
apiqapeiskcvvppadlppgavvdnccppvasnivdyklpavttmkvrpaahtmdkdai
akfakavelmkalpaddprnfyqqalvhcaycnggydqvnfpdqeiqvhnswlffpfhrw
ylyfyerilgkligdpsfglpfwnwdnpggmvlpdflndstsslydsnrnqshlppvvvd
lgyngadtdvtdqqritdnlalmykqmvtnagtaelflgkayragdapspgagsietsph
ipihrwvgdprntnnedmgnfysagrdiafychhsnvdrmwtiwqqlagkprkrdytdsd
wlnatflfydengqavkvrigdsldnqkmgykyaktplpwl
>d1buha_ 4.117.1.1.1 Cyclin-dependent PK (different isozymes) {Human (Homo sapiens)}
menfqkvekigegtygvvykarnkltgevvalkkirldttaireisllkelnhpnivkll
dvihtenklylvfeflhqdlkkfmdasaltgiplpliksylfqllqglafchshrvlhrd
lkpqnllintegaikladfglarafgvpvrtythevvtlwyrapeillgckyystavdiw
slgcifaemvtrralfpgdseidqlfrifrtlgtpdevvwpgvtsmpdykpsfpkwarqd
fskvvppldedgrsllsqmlhydpnkrisakaalahpffqdvtkpvp
>d1buhb_ 4.76.1.1.3 CksHs1 {Human (Homo sapiens)}
qiyysdkyddeefeyrhvmlpkdiaklvpkthlmsesewrnlgvqqsqgwvhymihepep
hillfrrplp
>d1buia_ 2.41.1.2.41 Plasmin, catalytic domain {Human (Homo sapiens)}
psfdcgkpqvepkkcpgrvvggcvahphswpwqvslrtrfgmhfcggtlispewvltaah
cleksprpssykvilgahqevnlephvqeievsrlfleptrkdiallklsspavitdkvi
paclpspnyvvadrtecfitgwgetqgtfgagllkeaqlpvienkvcnryeflngrvqst
elcaghlaggtdscqgdsggplvcfekdkyilqgvtswglgcarpnkpgvyvrvsrfvtw
iegvmrnn
>d1buib_ 2.41.1.2.41 Plasmin, catalytic domain {Human (Homo sapiens)}
apsfdcgkpqvepkkcpgrvvggcvahphswpwqvslrtrfgmhfcggtlispewvltaa
hcleksprpssykvilgahqevnlephvqeievsrlfleptrkdiallklsspavitdkv
ipaclpspnyvvadrtecfitgwgetqgtfgagllkeaqlpvienkvcnryeflngrvqs
telcaghlaggtdscqgdsggplvcfekdkyilqgvtswglgcarpnkpgvyvrvsrfvt
wiegvmrnn
>d1buic_ 4.13.4.1.1 Staphylokinase {Staphylococcus aureus, sakstar variant}
asyfeptgpylmvnvtgvdskgnellsphyvefpikpgttltkekieyyvewaldatayk
efrvveldpsakievtyydknkkkeetksfpitekgfvvpdlsehiknpgfnlitkvvie
kk
>d1buj__ 4.1.1.1.6 Barnase/Binase {Bacillus intermedius}
avintfdgvadylirykrlpdnyitksqasalgwvaskgnlaevapgksiggdvfsnreg
rlpsasgrtwreadinyvsgfrnadrlvyssdwliykttdhyatftrir
>d1bul__ 5.3.1.1.8 beta-Lactamase, class A {Enterobacter cloacae, NMC-A carbapenemase}
ntkgideiknletdfngrigvyaldtgsgksfsyranerfplcssfkgflaaavlkgsqd
nrlnlnqivnyntrslefhspittkykdngmslgdmaaaalqysdngatniileryiggp
egmtkfmrsigdedfrldrweldlntaipgderdtstpaavakslktlalgnilseheke
tyqtwlkgnttgaarirasvpsdwvvgdktgscgaygtandyavvwpknrapliisvytt
knekeakhedkviaeasriaidnlk
>d1buna_ 1.123.1.2.14 beta2-bungarotoxin, phospholipase A2 chain {Many-banded krait (elapid) (Bungarus multicinctus)}
nlinfmemirytipcektwgeyadygcycgaggsgrpidaldrccyvhdncygdaekkhk
cnpktqsysykltkrtiicygaagtcarivcdcdrtaalcfgnseyieghknidtarfcq
>d1bunb_ 7.8.1.1.7 beta2-bungarotoxin, neurotoxin chain {Many-banded krait (elapid) (Bungarus multicinctus)}
rkrhpdcdkppdtkicqtvvrafyykpsakrcvqfryggcngngnhfksdhlcrcecley
r
>d1buoa_ 4.35.1.1.1 Promyelocytic leukemia zinc finger (PLZF) protein BTB domain {Human (Homo sapiens)}
mgmiqlqnpshptgllckanqmrlagtlcdvvimvdsqefhahrtvlactskmfeilfhr
nsqhytldflspktfqqileyaytatlqakaedlddllyaaeileieyleeqclkmleti
q
>d1bupa1 3.46.1.1.1 (4-188) Heat shock protein 70kDa, ATPase fragment {Bovine (Bos taurus)}
gpavgidlgttyscvgvfqhgkveiiandqgnrttpsyvaftdterligdaaknqvamnp
tntvfdakrligrrfddavvqsdmkhwpfmvvndagrpkvqveykgetksfypeevssmv
ltkmkeiaeaylgktvtnavvtvpayfndsqrqatkdagtiaglnvlriineptaaaiay
gldkkv
>d1bupa2 3.46.1.1.1 (189-381) Heat shock protein 70kDa, ATPase fragment {Bovine (Bos taurus)}
vgaernvlifdlgggtfdvsiltiedgifevkstagdthlggedfdnrmvnhfiaefkrk
hkkdisenkravrrlrtacerakrtlssstqasieidslyegidfytsitrarfeelnad
lfrgtldpvekalrdakldksqihdivlvggstripkiqkllqdffngkelnksinpdea
vaygaavqaails
>d1buqa_ 4.15.3.3.1 Delta-5-3-ketosteroid isomerase, steroid delta-isomerase, KSI {Comamonas Testosteroni, also known as Pseudomonas testosteroni}
mntpehmtavvqryvaalnagdldgivalfaddatvedpvgseprsgtaaireffanslk
lplaveltqevravaneaafaftvsfefqgrktvvapixhfrfngagkvvsmralfgekn
ihaga
>d1buqb_ 4.15.3.3.1 Delta-5-3-ketosteroid isomerase, steroid delta-isomerase, KSI {Comamonas Testosteroni, also known as Pseudomonas testosteroni}
mntpehmtavvqryvaalnagdldgivalfaddatvedpvgseprsgtaaireffanslk
lplaveltqevravaneaafaftvsfefqgrktvvapixhfrfngagkvvsmralfgekn
ihaga
>d1bura1 3.1.12.1.2 (148-475) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
fqgpphgiqverdklnkygrpllgctikpklglsaknygravyeclrggldftxddenvn
sqpfmrwrdrflfcaealykaqaetgeikghylnatagtcedmmkravfarelgvpivmh
dyltggftanttlshycrdnglllhihramhavidrqknhgmhfrvlakalrlsggdhih
sgtvvgklegerditlgfvdllrddytekdrsrgiyftqswvstpgvlpvasggihvwhm
palteifgddsvlqfgggtlghpwgnapgavanrvaleacvqarnegrdlaregntiire
atkwspelaaacevwkeikfefpamdtv
>d1bura2 4.47.9.1.2 (12-147) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
efkagvkdykltyytpeyetldtdilaafrvspqpgvppeeagaavaaesstgtwttvwt
dgltnldrykgrcyhiepvageenqyicyvaypldlfeegsvtnmftsivgnvfgfkalr
alrledlripvayvkt
>d1burb1 3.1.12.1.2 (148-475) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
fqgpphgiqverdklnkygrpllgctikpklglsaknygravyeclrggldftxddenvn
sqpfmrwrdrflfcaealykaqaetgeikghylnatagtcedmmkravfarelgvpivmh
dyltggftanttlshycrdnglllhihramhavidrqknhgmhfrvlakalrlsggdhih
sgtvvgklegerditlgfvdllrddytekdrsrgiyftqswvstpgvlpvasggihvwhm
palteifgddsvlqfgggtlghpwgnapgavanrvaleacvqarnegrdlaregntiire
atkwspelaaacevwkeikfefpamdtv
>d1burb2 4.47.9.1.2 (12-147) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
efkagvkdykltyytpeyetldtdilaafrvspqpgvppeeagaavaaesstgtwttvwt
dgltnldrykgrcyhiepvageenqyicyvaypldlfeegsvtnmftsivgnvfgfkalr
alrledlripvayvkt
>d1burc1 3.1.12.1.2 (148-475) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
fqgpphgiqverdklnkygrpllgctikpklglsaknygravyeclrggldftxddenvn
sqpfmrwrdrflfcaealykaqaetgeikghylnatagtcedmmkravfarelgvpivmh
dyltggftanttlshycrdnglllhihramhavidrqknhgmhfrvlakalrlsggdhih
sgtvvgklegerditlgfvdllrddytekdrsrgiyftqswvstpgvlpvasggihvwhm
palteifgddsvlqfgggtlghpwgnapgavanrvaleacvqarnegrdlaregntiire
atkwspelaaacevwkeikfefpamdtv
>d1burc2 4.47.9.1.2 (12-147) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
efkagvkdykltyytpeyetldtdilaafrvspqpgvppeeagaavaaesstgtwttvwt
dgltnldrykgrcyhiepvageenqyicyvaypldlfeegsvtnmftsivgnvfgfkalr
alrledlripvayvkt
>d1burd1 3.1.12.1.2 (148-475) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
fqgpphgiqverdklnkygrpllgctikpklglsaknygravyeclrggldftxddenvn
sqpfmrwrdrflfcaealykaqaetgeikghylnatagtcedmmkravfarelgvpivmh
dyltggftanttlshycrdnglllhihramhavidrqknhgmhfrvlakalrlsggdhih
sgtvvgklegerditlgfvdllrddytekdrsrgiyftqswvstpgvlpvasggihvwhm
palteifgddsvlqfgggtlghpwgnapgavanrvaleacvqarnegrdlaregntiire
atkwspelaaacevwkeikfefpamdtv
>d1burd2 4.47.9.1.2 (12-147) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
efkagvkdykltyytpeyetldtdilaafrvspqpgvppeeagaavaaesstgtwttvwt
dgltnldrykgrcyhiepvageenqyicyvaypldlfeegsvtnmftsivgnvfgfkalr
alrledlripvayvkt
>d1burs_ 4.55.1.1.2 Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
mqvwpilgmkkyetlsylppltteqllaevnyllvnnwipclefevkdgfvyrehlkspg
yydgrywtmwklpmfgctdpaqvlneleeckkaypdafiriigfdnkrqvqcisfiaykp
agy
>d1burt_ 4.55.1.1.2 Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
mqvwpilgmkkyetlsylppltteqllaevnyllvnnwipclefevkdgfvyrehhkspg
yydgrywtmwklpmfgctdpaqvlneleeckkaypdafiriigfdnkrqvqcisfiaykp
agy
>d1buru_ 4.55.1.1.2 Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
mqvwpilgmkkyetlsylppltteqllaevnyllvnnwipclefevkdgfvyrehlkspg
yydgrywtmwklpmfgctdpaqvlneleeckkaypdafiriigfdnkrqvqcisfiaykp
agy
>d1burv_ 4.55.1.1.2 Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
mqvwpilgmkkyetlsylppltteqllaevnyllvnnwipclefevkdgfvyrehhkspg
yydgrywtmwklpmfgctdpaqvlneleeckkaypdafiriigfdnkrqvqcisfiaykp
agy
>d1bus__ 7.15.1.1.8 Seminal plasma inhibitor IIa {Bovine (Bos taurus)}
xgaqvdcaefkdpkvyctresnphcgsngetygnkcafckavmksggkinlkhrgkc
>d1buua1 4.139.1.1.7 (105-221) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdepndhgsgedcvtivdnglwndiscqashtavcefpa
>d1buvm_ 4.71.1.9.8 Membrane-type matrix metalloproteinase (CDMT1-MMP) {Human (Homo sapiens)}
iqglkwqhneitfciqnytpkvgeyatyeairkafrvwesatplrfrevpyayireghek
qadimiffaegfhgdstpfdgeggflahayfpgpniggdthfdsaepwtvrnedlngndi
flvavhelghalglehssdpsaimapfyqwmdtenfvlpdddrrgiqqlygges
>d1buvt_ 2.35.3.1.3 TIMP-2 {Bovine (Bos taurus)}
cscspvhpqqafcnadivirakavnkkevdsgndiygnpikriqyeikqikmfkgpdqdi
efiytapaaavcgvsldiggkkeyliagkaegngnmhitlcdfivpwdtlsatqkkslnh
ryqmgceckitrcpmipcyisspdeclwmdwvtekninghqakffacikrsdgscawyrg
aapp
>d1buwa_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1buwb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhxdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahk
>d1buwc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1buwd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhxdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahk
>d1buxa_ 4.47.6.1.3 Nucleoside diphosphate kinases {Dictyostelium discodeum}
vnkertflavkpdgvarglvgeiiaryekkgfvlvglkqlvptkdlaeshyaehkerpff
gglvsfitsgpvvamvfegkgvvasarlmigvtnplasapgsirgdfgvdvgrniihgsd
svesanreialwfkpeelltevkpnpnlye
>d1buxb_ 4.47.6.1.3 Nucleoside diphosphate kinases {Dictyostelium discodeum}
vnkertflavkpdgvarglvgeiiaryekkgfvlvglkqlvptkdlaeshyaehkerpff
gglvsfitsgpvvamvfegkgvvasarlmigvtnplasapgsirgdfgvdvgrniihgsd
svesanreialwfkpeelltevkpnpnlye
>d1buxc_ 4.47.6.1.3 Nucleoside diphosphate kinases {Dictyostelium discodeum}
vnkertflavkpdgvarglvgeiiaryekkgfvlvglkqlvptkdlaeshyaehkerpff
gglvsfitsgpvvamvfegkgvvasarlmigvtnplasapgsirgdfgvdvgrniihgsd
svesanreialwfkpeelltevkpnpnlye
>d1buya_ 1.27.1.2.1 Erythropoietin {Human (Homo sapiens)}
apprlicdsrvlerylleakeaekittgcaehcslnekitvpdtkvnfyawkrmevgqqa
vevwqglallseavlrgqallvkssqpweplqlhvdkavsglrslttllralgaqkeais
ppdaasaaplrtitadtfrklfrvysnflrgklklytgeacrtgdr
>d1buz__ 3.10.2.1.1 SpoIIaa {Bacillus subtilis}
slgidmnvkesvlcirltgeldhhtaetlkqkvtqslekddirhivlnledlsfmdssgl
gvilgrykqikqiggemvvcaispavkrlfdmsglfkiirfeqseqqalltlgvas
>d1bv1__ 4.103.3.1.1 Major birch pollen allergen Bet v 1 {White birch (Betula verrucosa)}
gvfnyetettsvipaarlfkafildgdnlfpkvapqaissveniegnggpgtikkisfpe
glpfkyvkdrvdevdhtnfkynysvieggpigdtlekisneikivatpdggsilkisnky
htkgdhevkaeqvkaskemgetllravesyllahsdayn
>d1bv2__ 1.54.1.1.5 Plant non-specific lipid-transfer protein (ns-LTP) {Rice (Oryza sativa)}
itcgqvnsavgpcltyarggagpsaaccsgvrslkaaasttadrrtacnclknaargikg
lnagnaasipskcgvsvpytisasidcsrvs
>d1bv3__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasfk
>d1bv41_ 4.139.1.1.7 Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kyfmssvrrmplnrakalcselqgtvatprnaeenraiqnvakdvaflgitdqrtenvfe
dltgnrvrytnwnegepnnvgsgencvvlltngkwndvpcsdsflvvcefsd
>d1bv42_ 4.139.1.1.7 Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kyfmssvrrmplnrakalcselqgtvatprnaeenraiqnvakdvaflgitdqrtenvfe
dltgnrvrytnwnegepnnvgsgencvvlltngkwndvpcsdsflvvcefsd
>d1bv43_ 4.139.1.1.7 Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kyfmssvrrmplnrakalcselqgtvatprnaeenraiqnvakdvaflgitdqrtenvfe
dltgnrvrytnwnegepnnvgsgencvvlltngkwndvpcsdsflvvcefs
>d1bv44_ 4.139.1.1.7 Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kkyfmssvrrmplnrakalcselqgtvatprnaeenraiqnvakdvaflgitdqrtenvf
edltgnrvrytnwnegepnnvgsgencvvlltngkwndvpcsdsflvvcefsd
>d1bv5__ 4.86.2.2.1 Histidine kinase FixL heme domain {Bradyrhizobium japonicum}
damividghgiiqlfstaaerlfgwseleaigqnvnilmpepdrsrhdsyisryrttsdp
hiigigrivtgkrrdgttfpmhlsigemqsggepyftgfvrdltehqqtqarlqelq
>d1bv6__ 4.86.2.2.1 Histidine kinase FixL heme domain {Bradyrhizobium japonicum}
ipdamividghgiiqlfstaaerlfgwseleaigqnvnilmpepdrsrhdsyisryrtts
dphiigigrivtgkrrdgttfpmhlsigemqsggepyftgfvrdltehqqtqarlqelq
>d1bv7a_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpfniigrnlltqigctlnf
>d1bv7b_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpfniigrnlltqigctlnf
>d1bv8__ 2.2.4.1.1 Receptor domain from alpha-2-macroglobulin {Human (Homo sapiens)}
eefpfalgvqtlpqtcdepkahtsfqlslsvsytgsrsasnmaivdvkmvsgfiplkptv
kmlersnhvsrtevssnhvliyldkvsnqtlslfftvlqdvpvrdlkpaivkvydyyetd
efaiaeynapcskdlgna
>d1bv9a_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvnvigrnlltqigctlnf
>d1bv9b_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvnvigrnlltqigctlnf
>d1bva__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeyenyigygddlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpwgaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1bvb__ 1.126.1.4.2 Cytochrome c554 {Nitrosomonas europaea}
adapfegrkkcsschkaqaqswkdtahakameslkpnvkkeakqkakldpakdytqdkdc
vgchvdgfgqkggytiespkpmltgvgceschgpgrnfrgdhrksgqafeksgkktprkd
lakkgqdfhfeercsachlnyegspwkgakapytpftpevdakytfkfdemvkevkamhe
hyklegvfegepkfkfhdefqasakpakkgk
>d1bvc__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgyqg
>d1bvd__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgyqg
>d1bvea_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigatlnf
>d1bveb_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigatlnf
>d1bvga_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigatlnf
>d1bvgb_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigatlnf
>d1bvh__ 3.36.1.1.1 Tyrosine phosphatase {Bovine (Bos taurus)}
aeqvtksvlfvclgnicrspiaeavfrklvtdqnisdnwvidsgavsdwnvgrspdprav
sclrnhgintahkarqvtkedfvtfdyilcmdesnlrdlnrksnqvkncrakiellgsyd
pqkqliiedpyygndadfetvyqqcvrccraflekvr
>d1bvia_ 4.1.1.1.3 RNase T1 {Aspergillus oryzae}
acdytcgsncysssdvstaqaagyklhedgetvgsnsyphkynnyegfdfsvsspyyewp
ilssgdvysggspgadrvvfnennqlagvithtgasgnnfvect
>d1bvib_ 4.1.1.1.3 RNase T1 {Aspergillus oryzae}
acdytcgsncysssdvstaqaagyklhedgetvgsnsyphkynnyegfdfsvsspyyewp
ilssgdvysggspgadrvvfnennqlagvithtgasgnnfvect
>d1bvic_ 4.1.1.1.3 RNase T1 {Aspergillus oryzae}
acdytcgsncysssdvstaqaagyklhedgetvgsnsyphkynnyegfdfsvsspyyewp
ilssgdvysggspgadrvvfnennqlagvithtgasgnnfvect
>d1bvid_ 4.1.1.1.3 RNase T1 {Aspergillus oryzae}
acdytcgsncysssdvstaqaagyklhedgetvgsnsyphkynnyegfdfsvsspyyewp
ilssgdvysggspgadrvvfnennqlagvithtgasgnnfvect
>d1bvka_ 2.1.1.1.113 Immunoglobulin (variable domains of L and H chains) {Humanized anti-lysozyme Fv HuLys11 (mouse), kappa L chain}
diqmtqspsslsasvgdrvtitcrasgnihnylawyqqkpgkapklliyytttladgvps
rfsgsgsgtdytftisslqpediatyycqhfwstprtfgqgtkveikr
>d1bvkb_ 2.1.1.1.113 Immunoglobulin (variable domains of L and H chains) {Humanized anti-lysozyme Fv HuLys11 (mouse), kappa L chain}
qvqlqesgpglvrpsqtlsltctvsgfsltgygvnwvrqppgrglewigmiwgdgntdyn
salksrvtmlkdtsknqfslrlssvtaadtavyycarerdyrldywgqgslvtvss
>d1bvkc_ 4.2.1.2.1 Lysozyme {Chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1bvkd_ 2.1.1.1.113 Immunoglobulin (variable domains of L and H chains) {Humanized anti-lysozyme Fv HuLys11 (mouse), kappa L chain}
diqmtqspsslsasvgdrvtitcrasgnihnylawyqqkpgkapklliyytttladgvps
rfsgsgsgtdytftisslqpediatyycqhfwstprtfgqgtkveikr
>d1bvke_ 2.1.1.1.113 Immunoglobulin (variable domains of L and H chains) {Humanized anti-lysozyme Fv HuLys11 (mouse), kappa L chain}
qvqlqesgpglvrpsqtlsltctvsgfsltgygvnwvrqppgrglewigmiwgdgntdyn
salksrvtmlkdtsknqfslrlssvtaadtavyycarerdyrldywgqgslvtvss
>d1bvkf_ 4.2.1.2.1 Lysozyme {Chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1bvla_ 2.1.1.1.113 Immunoglobulin (variable domains of L and H chains) {Humanized anti-lysozyme Fv HuLys11 (mouse), kappa L chain}
qvqlqesgpglvrpsqtlsltctvsgfsltgygvnwvrqppgrglewigmiwgdgntdyn
salksrvtmlkdtsknqfslrlssvtaadtavyycarerdyrldywgqgslvtvss
>d1bvlb_ 2.1.1.1.113 Immunoglobulin (variable domains of L and H chains) {Humanized anti-lysozyme Fv HuLys11 (mouse), kappa L chain}
diqmtqspsslsasvgdrvtitcrasgnihnylawyqqkpgkapklliyytttladgvps
rfsgsgsgtdytftisslqpediatyycqhfwstprtfgqgtkveikr
>d1bvlc_ 2.1.1.1.113 Immunoglobulin (variable domains of L and H chains) {Humanized anti-lysozyme Fv HuLys11 (mouse), kappa L chain}
qvqlqesgpglvrpsqtlsltctvsgfsltgygvnwvrqppgrglewigmiwgdgntdyn
salksrvtmlkdtsknqfslrlssvtaadtavyycarerdyrldywgqgslvtvss
>d1bvld_ 2.1.1.1.113 Immunoglobulin (variable domains of L and H chains) {Humanized anti-lysozyme Fv HuLys11 (mouse), kappa L chain}
diqmtqspsslsasvgdrvtitcrasgnihnylawyqqkpgkapklliyytttladgvps
rfsgsgsgtdytftisslqpediatyycqhfwstprtfgqgtkveikr
>d1bvma_ 1.123.1.2.12 Phospholipase A2 {Bovine (Bos taurus), pancreas}
alwqfngmikckipsseplldfnnygcycglggsgtpvddldrccqthdncykqakklds
ckvlvdnpytnnysyscsnneitcssennaceaficncdrnaaicfskvpynkehknldk
knc
>d1bvnp1 2.62.1.1.8 (404-496) Animal alpha-amylase {Porcine (Sus scrofa)}
qpfanwwdngsnqvafgrgnrgfivfnnddwqlsstlqtglpggtycnvisgdkvgnsct
gikvyvssdgtaqfsisnsaqdpfiaihaeskl
>d1bvnp2 3.1.7.1.8 (1-403) Animal alpha-amylase {Porcine (Sus scrofa)}
qyapqtqsgrtdivhlfewrwvdialecerylgpkgfggvqvsppnenvvvtnpsrpwwe
ryqpvsyklctrsgnenefrdmvtrcnnvgvriyvdavinhmcgsgaaagtgttcgsycn
pgsrefpavpysawdfndgkcktasggiesyndpyqvrdcqlvglldlalekdyvrsmia
dylnklidigvagfrldaskhmwpgdikavldklhnlntnwfpagsrpfifqevidlgge
aissseyfgngrvtefkygaklgtvvrkwsgekmsylknwgegwgfmpsdralvfvdnhd
nqrghgaggssiltfwdarlykvavgfmlahpygftrvmssyrwarnfvngedvndwigp
pnnngvikevtinadttcgndwvcehrwreirnmvwfrnvvdg
>d1bvnt_ 2.4.1.1.1 alpha-Amylase inhibitor tendamistat {Streptomyces tendae}
vsepapscvtlyqswrysqadngcaetvtvkvvyeddteglcyavapgqittvgdgyigs
hgharylarcl
>d1bvoa_ 2.2.5.1.7 Dorsal homologue gambif1 {African malaria mosquito (Anopheles gambiae)}
pyveiteqphpkalrfryecegrsagsipgvnttaeqktfpsiqvhgyrgravvvvscvt
kegpehkphphnlvgkegckkgvctveinsttmsytfnnlgiqcvkkkdveealrlrqei
rvdpfrtgfghakepgsidlnavrlcfqvflegqqrgrftepltpvvsdiiydkk
>d1bvp11 1.107.1.1.1 (1-120,255-349) Bluetongue virus coat protein vp7 (BTV-10 vp7), alpha-helical domain {Bluetongue virus}
mdtiaaraltvmracatlqearivleanvmeilgiainryngltlrgvtmrptslaqrne
mffmcldmmlsaaginvgpispdytqhmatigvlatpeipftteaaneiarvtgetstwg
Xktlnqypaltaeifnvysfrdhtwhglrtailnrttlpnmlppifppndrdsiltllll
stladvytvlrpefaihgvnpmpgpltraiaraayv
>d1bvp12 2.17.1.1.1 (121-254) Virus coat protein vp7 (BTV-10 vp7), central (top) domain {Bluetongue virus}
parqpygffleteetfqpgrwfmraaqavtavvcgpdmiqvslnagargdvqqifqgrnd
pmmiylvwrrienfamaqgnsqqtqagvtvsvggvdmragriiawdgqaalhvhnptqqn
amvqiqvvfyismd
>d1bvp21 1.107.1.1.1 (1-120,255-349) Bluetongue virus coat protein vp7 (BTV-10 vp7), alpha-helical domain {Bluetongue virus}
mdtiaaraltvmracatlqearivleanvmeilgiainryngltlrgvtmrptslaqrne
mffmcldmmlsaaginvgpispdytqhmatigvlatpeipftteaaneiarvtgetstwg
Xktlnqypaltaeifnvysfrdhtwhglrtailnrttlpnmlppifppndrdsiltllll
stladvytvlrpefaihgvnpmpgpltraiaraayv
>d1bvp22 2.17.1.1.1 (121-254) Virus coat protein vp7 (BTV-10 vp7), central (top) domain {Bluetongue virus}
parqpygffleteetfqpgrwfmraaqavtavvcgpdmiqvslnagargdvqqifqgrnd
pmmiylvwrrienfamaqgnsqqtqagvtvsvggvdmragriiawdgqaalhvhnptqqn
amvqiqvvfyismd
>d1bvp31 1.107.1.1.1 (1-120,255-349) Bluetongue virus coat protein vp7 (BTV-10 vp7), alpha-helical domain {Bluetongue virus}
mdtiaaraltvmracatlqearivleanvmeilgiainryngltlrgvtmrptslaqrne
mffmcldmmlsaaginvgpispdytqhmatigvlatpeipftteaaneiarvtgetstwg
Xktlnqypaltaeifnvysfrdhtwhglrtailnrttlpnmlppifppndrdsiltllll
stladvytvlrpefaihgvnpmpgpltraiaraayv
>d1bvp32 2.17.1.1.1 (121-254) Virus coat protein vp7 (BTV-10 vp7), central (top) domain {Bluetongue virus}
parqpygffleteetfqpgrwfmraaqavtavvcgpdmiqvslnagargdvqqifqgrnd
pmmiylvwrrienfamaqgnsqqtqagvtvsvggvdmragriiawdgqaalhvhnptqqn
amvqiqvvfyismd
>d1bvp41 1.107.1.1.1 (1-120,255-349) Bluetongue virus coat protein vp7 (BTV-10 vp7), alpha-helical domain {Bluetongue virus}
mdtiaaraltvmracatlqearivleanvmeilgiainryngltlrgvtmrptslaqrne
mffmcldmmlsaaginvgpispdytqhmatigvlatpeipftteaaneiarvtgetstwg
Xktlnqypaltaeifnvysfrdhtwhglrtailnrttlpnmlppifppndrdsiltllll
stladvytvlrpefaihgvnpmpgpltraiaraayv
>d1bvp42 2.17.1.1.1 (121-254) Virus coat protein vp7 (BTV-10 vp7), central (top) domain {Bluetongue virus}
parqpygffleteetfqpgrwfmraaqavtavvcgpdmiqvslnagargdvqqifqgrnd
pmmiylvwrrienfamaqgnsqqtqagvtvsvggvdmragriiawdgqaalhvhnptqqn
amvqiqvvfyismd
>d1bvp51 1.107.1.1.1 (1-120,255-349) Bluetongue virus coat protein vp7 (BTV-10 vp7), alpha-helical domain {Bluetongue virus}
mdtiaaraltvmracatlqearivleanvmeilgiainryngltlrgvtmrptslaqrne
mffmcldmmlsaaginvgpispdytqhmatigvlatpeipftteaaneiarvtgetstwg
Xktlnqypaltaeifnvysfrdhtwhglrtailnrttlpnmlppifppndrdsiltllll
stladvytvlrpefaihgvnpmpgpltraiaraayv
>d1bvp52 2.17.1.1.1 (121-254) Virus coat protein vp7 (BTV-10 vp7), central (top) domain {Bluetongue virus}
parqpygffleteetfqpgrwfmraaqavtavvcgpdmiqvslnagargdvqqifqgrnd
pmmiylvwrrienfamaqgnsqqtqagvtvsvggvdmragriiawdgqaalhvhnptqqn
amvqiqvvfyismd
>d1bvp61 1.107.1.1.1 (1-120,255-349) Bluetongue virus coat protein vp7 (BTV-10 vp7), alpha-helical domain {Bluetongue virus}
mdtiaaraltvmracatlqearivleanvmeilgiainryngltlrgvtmrptslaqrne
mffmcldmmlsaaginvgpispdytqhmatigvlatpeipftteaaneiarvtgetstwg
Xktlnqypaltaeifnvysfrdhtwhglrtailnrttlpnmlppifppndrdsiltllll
stladvytvlrpefaihgvnpmpgpltraiaraayv
>d1bvp62 2.17.1.1.1 (121-254) Virus coat protein vp7 (BTV-10 vp7), central (top) domain {Bluetongue virus}
parqpygffleteetfqpgrwfmraaqavtavvcgpdmiqvslnagargdvqqifqgrnd
pmmiylvwrrienfamaqgnsqqtqagvtvsvggvdmragriiawdgqaalhvhnptqqn
amvqiqvvfyismd
>d1bvq__ 4.31.1.1.1 4-hydroxybenzoyl-CoA thioesterase {Pseudomonas CBS-3}
arsitmqqriefgdcdpagivwfpnyhrwldaasrnyfikcglppwrqtvvergivgtpi
vscnasfvctasyddvltietcikewrrksfvqrhsvsrttpggdvqlvmradeirvfam
ndgerlraievpadyielc
>d1bvra_ 3.2.1.2.14 Enoyl-ACP reductase {Mycobacterium tuberculosis, TB, gene InhA}
tglldgkrilvsgiitdssiafhiarvaqeqgaqlvltgfdrlrliqritdrlpakapll
eldvqneehlaslagrvteaigagnkldgvvhsigfmpqtgmginpffdapyadvskgih
isaysyasmakallpimnpggsivgmdfdpsrampaynwmtvaksalesvnrfvareagk
ygvrsnlvaagpirtlamsaivggalgeeagaqiqlleegwdqrapigwnmkdatpvakt
vcallsdwlpattgdiiyadggahtqll
>d1bvrb_ 3.2.1.2.14 Enoyl-ACP reductase {Mycobacterium tuberculosis, TB, gene InhA}
tglldgkrilvsgiitdssiafhiarvaqeqgaqlvltgfdrlrliqritdrlpakapll
eldvqneehlaslagrvteaigagnkldgvvhsigfmpqtgmginpffdapyadvskgih
isaysyasmakallpimnpggsivgmdfdpsrampaynwmtvaksalesvnrfvareagk
ygvrsnlvaagpirtlamsaivggalgeeagaqiqlleegwdqrapigwnmkdatpvakt
vcallsdwlpattgdiiyadggahtqll
>d1bvrc_ 3.2.1.2.14 Enoyl-ACP reductase {Mycobacterium tuberculosis, TB, gene InhA}
tglldgkrilvsgiitdssiafhiarvaqeqgaqlvltgfdrlrliqritdrlpakapll
eldvqneehlaslagrvteaigagnkldgvvhsigfmpqtgmginpffdapyadvskgih
isaysyasmakallpimnpggsivgmdfdpsrampaynwmtvaksalesvnrfvareagk
ygvrsnlvaagpirtlamsaivggalgeeagaqiqlleegwdqrapigwnmkdatpvakt
vcallsdwlpattgdiiyadggahtqll
>d1bvrd_ 3.2.1.2.14 Enoyl-ACP reductase {Mycobacterium tuberculosis, TB, gene InhA}
tglldgkrilvsgiitdssiafhiarvaqeqgaqlvltgfdrlrliqritdrlpakapll
eldvqneehlaslagrvteaigagnkldgvvhsigfmpqtgmginpffdapyadvskgih
isaysyasmakallpimnpggsivgmdfdpsrampaynwmtvaksalesvnrfvareagk
ygvrsnlvaagpirtlamsaivggalgeeagaqiqlleegwdqrapigwnmkdatpvakt
vcallsdwlpattgdiiyadggahtqll
>d1bvre_ 3.2.1.2.14 Enoyl-ACP reductase {Mycobacterium tuberculosis, TB, gene InhA}
tglldgkrilvsgiitdssiafhiarvaqeqgaqlvltgfdrlrliqritdrlpakapll
eldvqneehlaslagrvteaigagnkldgvvhsigfmpqtgmginpffdapyadvskgih
isaysyasmakallpimnpggsivgmdfdpsrampaynwmtvaksalesvnrfvareagk
ygvrsnlvaagpirtlamsaivggalgeeagaqiqlleegwdqrapigwnmkdatpvakt
vcallsdwlpattgdiiyadggahtqll
>d1bvrf_ 3.2.1.2.14 Enoyl-ACP reductase {Mycobacterium tuberculosis, TB, gene InhA}
tglldgkrilvsgiitdssiafhiarvaqeqgaqlvltgfdrlrliqritdrlpakapll
eldvqneehlaslagrvteaigagnkldgvvhsigfmpqtgmginpffdapyadvskgih
isaysyasmakallpimnpggsivgmdfdpsrampaynwmtvaksalesvnrfvareagk
ygvrsnlvaagpirtlamsaivggalgeeagaqiqlleegwdqrapigwnmkdatpvakt
vcallsdwlpattgdiiyadggahtqll
>d1bvsa1 1.5.1.1.2 (148-203) DNA helicase RuvA subunit, C-terminal domain {Mycobacterium leprae}
navrgsvvealvglgfaakqaeeatdqvldgelgkdgavatssalraalsllgktr
>d1bvsa2 1.61.6.1.2 (64-134) DNA helicase RuvA subunit, middle domain {Mycobacterium leprae}
daenrdlflallsvsgvgprlamatlavhdaaalrqaladsdvasltavpgigargaeri
vleladkvgpv
>d1bvsa3 2.35.4.2.2 (1-63) DNA helicase RuvA subunit, N-terminal domain {Mycobacterium leprae}
mifsvrgevlevaldhavieaagigyrvnatpsalatlaqgsqarlvtamvvredsmtly
gfs
>d1bvsb1 1.5.1.1.2 (147-203) DNA helicase RuvA subunit, C-terminal domain {Mycobacterium leprae}
gnavrgsvvealvglgfaakqaeeatdqvldgelgkdgavatssalraalsllgktr
>d1bvsb2 1.61.6.1.2 (64-133) DNA helicase RuvA subunit, middle domain {Mycobacterium leprae}
daenrdlflallsvsgvgprlamatlavhdaaalrqaladsdvasltavpgigargaeri
vleladkvgp
>d1bvsb3 2.35.4.2.2 (1-63) DNA helicase RuvA subunit, N-terminal domain {Mycobacterium leprae}
mifsvrgevlevaldhavieaagigyrvnatpsalatlaqgsqarlvtamvvredsmtly
gfs
>d1bvsc1 1.5.1.1.2 (148-203) DNA helicase RuvA subunit, C-terminal domain {Mycobacterium leprae}
navrgsvvealvglgfaakqaeeatdqvldgelgkdgavatssalraalsllgktr
>d1bvsc2 1.61.6.1.2 (64-134) DNA helicase RuvA subunit, middle domain {Mycobacterium leprae}
daenrdlflallsvsgvgprlamatlavhdaaalrqaladsdvasltavpgigargaeri
vleladkvgpv
>d1bvsc3 2.35.4.2.2 (1-63) DNA helicase RuvA subunit, N-terminal domain {Mycobacterium leprae}
mifsvrgevlevaldhavieaagigyrvnatpsalatlaqgsqarlvtamvvredsmtly
gfs
>d1bvsd1 1.5.1.1.2 (147-203) DNA helicase RuvA subunit, C-terminal domain {Mycobacterium leprae}
gnavrgsvvealvglgfaakqaeeatdqvldgelgkdgavatssalraalsllgktr
>d1bvsd2 1.61.6.1.2 (64-133) DNA helicase RuvA subunit, middle domain {Mycobacterium leprae}
daenrdlflallsvsgvgprlamatlavhdaaalrqaladsdvasltavpgigargaeri
vleladkvgp
>d1bvsd3 2.35.4.2.2 (1-63) DNA helicase RuvA subunit, N-terminal domain {Mycobacterium leprae}
mifsvrgevlevaldhavieaagigyrvnatpsalatlaqgsqarlvtamvvredsmtly
gfs
>d1bvse1 1.5.1.1.2 (148-203) DNA helicase RuvA subunit, C-terminal domain {Mycobacterium leprae}
navrgsvvealvglgfaakqaeeatdqvldgelgkdgavatssalraalsllgktr
>d1bvse2 1.61.6.1.2 (64-134) DNA helicase RuvA subunit, middle domain {Mycobacterium leprae}
daenrdlflallsvsgvgprlamatlavhdaaalrqaladsdvasltavpgigargaeri
vleladkvgpv
>d1bvse3 2.35.4.2.2 (1-63) DNA helicase RuvA subunit, N-terminal domain {Mycobacterium leprae}
mifsvrgevlevaldhavieaagigyrvnatpsalatlaqgsqarlvtamvvredsmtly
gfs
>d1bvsf1 1.5.1.1.2 (147-203) DNA helicase RuvA subunit, C-terminal domain {Mycobacterium leprae}
gnavrgsvvealvglgfaakqaeeatdqvldgelgkdgavatssalraalsllgktr
>d1bvsf2 1.61.6.1.2 (64-133) DNA helicase RuvA subunit, middle domain {Mycobacterium leprae}
daenrdlflallsvsgvgprlamatlavhdaaalrqaladsdvasltavpgigargaeri
vleladkvgp
>d1bvsf3 2.35.4.2.2 (1-63) DNA helicase RuvA subunit, N-terminal domain {Mycobacterium leprae}
mifsvrgevlevaldhavieaagigyrvnatpsalatlaqgsqarlvtamvvredsmtly
gfs
>d1bvsg1 1.5.1.1.2 (148-203) DNA helicase RuvA subunit, C-terminal domain {Mycobacterium leprae}
navrgsvvealvglgfaakqaeeatdqvldgelgkdgavatssalraalsllgktr
>d1bvsg2 1.61.6.1.2 (64-134) DNA helicase RuvA subunit, middle domain {Mycobacterium leprae}
daenrdlflallsvsgvgprlamatlavhdaaalrqaladsdvasltavpgigargaeri
vleladkvgpv
>d1bvsg3 2.35.4.2.2 (1-63) DNA helicase RuvA subunit, N-terminal domain {Mycobacterium leprae}
mifsvrgevlevaldhavieaagigyrvnatpsalatlaqgsqarlvtamvvredsmtly
gfs
>d1bvsh1 1.5.1.1.2 (147-203) DNA helicase RuvA subunit, C-terminal domain {Mycobacterium leprae}
gnavrgsvvealvglgfaakqaeeatdqvldgelgkdgavatssalraalsllgktr
>d1bvsh2 1.61.6.1.2 (64-133) DNA helicase RuvA subunit, middle domain {Mycobacterium leprae}
daenrdlflallsvsgvgprlamatlavhdaaalrqaladsdvasltavpgigargaeri
vleladkvgp
>d1bvsh3 2.35.4.2.2 (1-63) DNA helicase RuvA subunit, N-terminal domain {Mycobacterium leprae}
mifsvrgevlevaldhavieaagigyrvnatpsalatlaqgsqarlvtamvvredsmtly
gfs
>d1bvt__ 4.128.1.1.1 Zn metallo-beta-lactamase {Bacillus cereus}
tviknetgtisisqlnknvwvhtelgsfngeavpsnglvlntskglvlvdsswddkltke
liemvekkfqkrvtdviithahadriggiktlkergikahstaltaelakkngyeeplgd
lqtvtnlkfgnmkvetfypgkghtednivvwlpqynilvggclvkstsakdlgnvadayv
newstsienvlkryrninavvpghgevgdkglllhtldllk
>d1bvua1 3.2.1.7.3 (181-418) Glutamate dehydrogenase {Thermococcus litoralis}
ggivarmdatargasytvreaakalgmdlkgktiaiqgygnagyymakimseeygmkvva
vsdtkggiynpdglnadevlawkkktgsvkdfpgatnitneellelevdvlapsaieevi
tkknadnikakivaelangpttpeadeilyekgiliipdflcnaggvtvsyfewvqnitg
dywtveetrakldkkmtkafwdvynthkekninmrdaayvvavsrvyqamkdrgwikk
>d1bvua2 3.48.1.1.3 (3-180) Glutamate dehydrogenase {Thermococcus litoralis}
qdpfeiavkqleraaqymdiseealeflkrpqrivevsipvemddgsvkvftgfrvqynw
argptkggirwhpeetlstvkalaawmtwktavmdlpygggkggvicnpkemsdrekerl
argyvraiydvispytdipapdvytnpqimawmmdeyetisrrkdpsfgvitgkppsv
>d1bvub1 3.2.1.7.3 (181-418) Glutamate dehydrogenase {Thermococcus litoralis}
ggivarmdatargasytvreaakalgmdlkgktiaiqgygnagyymakimseeygmkvva
vsdtkggiynpdglnadevlawkkktgsvkdfpgatnitneellelevdvlapsaieevi
tkknadnikakivaelangpttpeadeilyekgiliipdflcnaggvtvsyfewvqnitg
dywtveetrakldkkmtkafwdvynthkekninmrdaayvvavsrvyqamkdrgwikk
>d1bvub2 3.48.1.1.3 (3-180) Glutamate dehydrogenase {Thermococcus litoralis}
qdpfeiavkqleraaqymdiseealeflkrpqrivevsipvemddgsvkvftgfrvqynw
argptkggirwhpeetlstvkalaawmtwktavmdlpygggkggvicnpkemsdrekerl
argyvraiydvispytdipapdvytnpqimawmmdeyetisrrkdpsfgvitgkppsv
>d1bvuc1 3.2.1.7.3 (181-418) Glutamate dehydrogenase {Thermococcus litoralis}
ggivarmdatargasytvreaakalgmdlkgktiaiqgygnagyymakimseeygmkvva
vsdtkggiynpdglnadevlawkkktgsvkdfpgatnitneellelevdvlapsaieevi
tkknadnikakivaelangpttpeadeilyekgiliipdflcnaggvtvsyfewvqnitg
dywtveetrakldkkmtkafwdvynthkekninmrdaayvvavsrvyqamkdrgwikk
>d1bvuc2 3.48.1.1.3 (3-180) Glutamate dehydrogenase {Thermococcus litoralis}
qdpfeiavkqleraaqymdiseealeflkrpqrivevsipvemddgsvkvftgfrvqynw
argptkggirwhpeetlstvkalaawmtwktavmdlpygggkggvicnpkemsdrekerl
argyvraiydvispytdipapdvytnpqimawmmdeyetisrrkdpsfgvitgkppsv
>d1bvud1 3.2.1.7.3 (181-418) Glutamate dehydrogenase {Thermococcus litoralis}
ggivarmdatargasytvreaakalgmdlkgktiaiqgygnagyymakimseeygmkvva
vsdtkggiynpdglnadevlawkkktgsvkdfpgatnitneellelevdvlapsaieevi
tkknadnikakivaelangpttpeadeilyekgiliipdflcnaggvtvsyfewvqnitg
dywtveetrakldkkmtkafwdvynthkekninmrdaayvvavsrvyqamkdrgwikk
>d1bvud2 3.48.1.1.3 (3-180) Glutamate dehydrogenase {Thermococcus litoralis}
qdpfeiavkqleraaqymdiseealeflkrpqrivevsipvemddgsvkvftgfrvqynw
argptkggirwhpeetlstvkalaawmtwktavmdlpygggkggvicnpkemsdrekerl
argyvraiydvispytdipapdvytnpqimawmmdeyetisrrkdpsfgvitgkppsv
>d1bvue1 3.2.1.7.3 (181-418) Glutamate dehydrogenase {Thermococcus litoralis}
ggivarmdatargasytvreaakalgmdlkgktiaiqgygnagyymakimseeygmkvva
vsdtkggiynpdglnadevlawkkktgsvkdfpgatnitneellelevdvlapsaieevi
tkknadnikakivaelangpttpeadeilyekgiliipdflcnaggvtvsyfewvqnitg
dywtveetrakldkkmtkafwdvynthkekninmrdaayvvavsrvyqamkdrgwikk
>d1bvue2 3.48.1.1.3 (3-180) Glutamate dehydrogenase {Thermococcus litoralis}
qdpfeiavkqleraaqymdiseealeflkrpqrivevsipvemddgsvkvftgfrvqynw
argptkggirwhpeetlstvkalaawmtwktavmdlpygggkggvicnpkemsdrekerl
argyvraiydvispytdipapdvytnpqimawmmdeyetisrrkdpsfgvitgkppsv
>d1bvuf1 3.2.1.7.3 (181-418) Glutamate dehydrogenase {Thermococcus litoralis}
ggivarmdatargasytvreaakalgmdlkgktiaiqgygnagyymakimseeygmkvva
vsdtkggiynpdglnadevlawkkktgsvkdfpgatnitneellelevdvlapsaieevi
tkknadnikakivaelangpttpeadeilyekgiliipdflcnaggvtvsyfewvqnitg
dywtveetrakldkkmtkafwdvynthkekninmrdaayvvavsrvyqamkdrgwikk
>d1bvuf2 3.48.1.1.3 (3-180) Glutamate dehydrogenase {Thermococcus litoralis}
qdpfeiavkqleraaqymdiseealeflkrpqrivevsipvemddgsvkvftgfrvqynw
argptkggirwhpeetlstvkalaawmtwktavmdlpygggkggvicnpkemsdrekerl
argyvraiydvispytdipapdvytnpqimawmmdeyetisrrkdpsfgvitgkppsv
>d1bvv__ 2.26.1.10.1 Xylanase II {Bacillus circulans}
astdywqnwtdgggivnavngsggnysvnwsntgnfvvgkgwttgspfrtinynagvwap
ngngyltlygwtrsplieyyvvdswgtyrptgtykgtvksdggtydiytttrynapsidg
drttftqywsvrqskrptgsnatitftnhvnawkshgmnlgsnwayqvmategyqssgss
nvtvw
>d1bvwa_ 3.5.1.1.3 Cellobiohydrolase II (Cel6a) {Humicola insolens}
gnpfegvqlwannyyrsevhtlaipqitdpalraaasavaevpsfqwldrnvtvdtllvq
tlseireanqaganpqyaaqivvydlpdrdcaaaasngewaianngvnnykayinrirei
lisfsdvrtilviepdslanmvtnmnvpkcsgaastyreltiyalkqldlphvamymdag
hagwlgwpaniqpaaelfakiyedagkpravrglatnvanynawsvsspppytspnpnyd
ekhyieafrplleargfpaqfivdqgrsgkqptgqkewghwcnaigtgfgmrptantghq
yvdafvwvkpggecdgtsdttaarydyhcgledalkpapeagqwfneyfiqllrnanppf
>d1bvx__ 4.2.1.2.1 Lysozyme {Chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1bvya_ 1.100.1.1.2 Cytochrome P450 {Bacillus megaterium}
lntdkpvqalmkiadelgeifkfeapgrvtrylssqrlikeacdesrfdknlsqalkfvr
dfagdglftswtheknwkkahnillpsfsqqamkgyhammvdiavqlvqkwerlnadehi
evpedmtrltldtiglcgfnyrfnsfyrdqphpfitsmvraldeamnklqranpddpayd
enkrqfqedikvmndlvdkiiadrkasgeqsddllthmlngkdpetgeplddeniryqii
tfliaghettsgllsfalyflvknphvlqkaaeeaarvlvdpvpsykqvkqlkyvgmvln
ealrlwptapafslyakedtvlggeyplekgdelmvlipqlhrdktiwgddveefrperf
enpsaipqhafkpfgngqracigqqfalheatlvlgmmlkhfdfedhtnyeldiketltl
kpegfvvkakskkiplggi
>d1bvyb_ 1.100.1.1.2 Cytochrome P450 {Bacillus megaterium}
ntdkpvqalmkiadelgeifkfeapgrvtrylssqrlikeacdesrfdknlsqalkfvrd
fagdglftswtheknwkkahnillpsfsqqamkgyhammvdiavqlvqkwerlnadehie
vpedmtrltldtiglcgfnyrfnsfyrdqphpfitsmvraldeamnklqranpddpayde
nkrqfqedikvmndlvdkiiadrkasgeqsddllthmlngkdpetgeplddeniryqiit
fliaghettsgllsfalyflvknphvlqkaaeeaarvlvdpvpsykqvkqlkyvgmvlne
alrlwptapafslyakedtvlggeyplekgdelmvlipqlhrdktiwgddveefrperfe
npsaipqhafkpfgngqracigqqfalheatlvlgmmlkhfdfedhtnyeldiketltlk
pegfvvkakskkiplggi
>d1bvyf_ 3.16.4.1.7 FMN-binding domain of the cytochrome P450bm-3 {Bacillus megaterium}
ntpllvlygsnmgtaegtardladiamskgfapqvatldshagnlpregavlivtasyng
hppdnakqfvdwldqasadevkgvrysvfgcgdknwattyqkvpafidetlaakgaenia
drgeadasddfegtyeewrehmwsdvaayfnl
>d1bvza1 2.1.1.5.8 (1-120) Alpha-amylase II (TVAII), N-terminal domain {Thermoactinomyces vulgaris, r-47}
mlleaifheakgsyaypisetqlrvrlrakkgdvvrcevlyadryaspeeelahalagka
gsderfdyfeallecstkrvkyvflltgpqgeavyfgetgfsaerskagvfqyayihrse
>d1bvza2 2.62.1.1.13 (503-585) Alpha-amylase II (TVAII) {Thermoactinomyces vulgaris, r-47}
gnvrswhadkqanlyafvrtvqdqhvgvvlnnrgekqtvllqvpesggktwldcltgeev
hgkqgqlkltlrpyqgmilwngr
>d1bvza3 3.1.7.1.13 (121-502) Alpha-amylase II (TVAII), central domain {Thermoactinomyces vulgaris, r-47}
vfttpewakeaviyqifperfangdpsndppgteqwakdarprhdsfyggdlkgvidrlp
yleelgvtalyftpifaspshhkydtadylaidpqfgdlptfrrlvdeahrrgikiilda
vfnhagdqffafrdvlqkgeqsrykdwffiedfpvsktsrtnyetfavqvpampklrten
pevkeylfdvarfwmeqgidgwrldvanevdhafwrefrrlvkslnpdalivgeiwhdas
gwlmgdqfdsvmnylfresvirffatgeihaerfdaeltrarmlypeqaaqglwnlldsh
dterfltscggneakfrlavlfqmtylgtpliyygdeigmagatdpdcrrpmiweekeqn
rglfefykelirlrhrlasltr
>d1bvzb1 2.1.1.5.8 (1-120) Alpha-amylase II (TVAII), N-terminal domain {Thermoactinomyces vulgaris, r-47}
mlleaifheakgsyaypisetqlrvrlrakkgdvvrcevlyadryaspeeelahalagka
gsderfdyfeallecstkrvkyvflltgpqgeavyfgetgfsaerskagvfqyayihrse
>d1bvzb2 2.62.1.1.13 (503-585) Alpha-amylase II (TVAII) {Thermoactinomyces vulgaris, r-47}
gnvrswhadkqanlyafvrtvqdqhvgvvlnnrgekqtvllqvpesggktwldcltgeev
hgkqgqlkltlrpyqgmilwngr
>d1bvzb3 3.1.7.1.13 (121-502) Alpha-amylase II (TVAII), central domain {Thermoactinomyces vulgaris, r-47}
vfttpewakeaviyqifperfangdpsndppgteqwakdarprhdsfyggdlkgvidrlp
yleelgvtalyftpifaspshhkydtadylaidpqfgdlptfrrlvdeahrrgikiilda
vfnhagdqffafrdvlqkgeqsrykdwffiedfpvsktsrtnyetfavqvpampklrten
pevkeylfdvarfwmeqgidgwrldvanevdhafwrefrrlvkslnpdalivgeiwhdas
gwlmgdqfdsvmnylfresvirffatgeihaerfdaeltrarmlypeqaaqglwnlldsh
dterfltscggneakfrlavlfqmtylgtpliyygdeigmagatdpdcrrpmiweekeqn
rglfefykelirlrhrlasltr
>d1bw0a_ 3.57.1.1.9 Tyrosine aminotransferase (TAT) {Trypanosoma cruzi}
wdvsmsnhaglvfnpirtvsdnakpspspkpiiklsvgdptldknlltsaaqikklkeai
dsqecngyfptvgspeareavatwwrnsfvhkeelkstivkdnvvlcsggshgilmaita
icdagdyalvpqpgfphyetvckaygigmhfyncrpendweadldeirrlkddktklliv
tnpsnpcgsnfsrkhvedivrlaeelrlplfsdeiyagmvfkgkdpnatftsvadfettv
prvilggtaxnlvvpgwrlgwllyvdphgngpsfleglkrvgmlvcgpctvvqaalgeal
lntpqehldqivakieesamylynhigeciglaptmprgamylmsridlekyrdiktdve
ffeklleeenvqvlpgtifhapgftrltttrpvevyreaverikafcqrhaa
>d1bw0b_ 3.57.1.1.9 Tyrosine aminotransferase (TAT) {Trypanosoma cruzi}
wdvsmsnhaglvfnpirtvsdnakpspspkpiiklsvgdptldknlltsaaqikklkeai
dsqecngyfptvgspeareavatwwrnsfvhkeelkstivkdnvvlcsggshgilmaita
icdagdyalvpqpgfphyetvckaygigmhfyncrpendweadldeirrlkddktklliv
tnpsnpcgsnfsrkhvedivrlaeelrlplfsdeiyagmvfkgkdpnatftsvadfettv
prvilggtaxnlvvpgwrlgwllyvdphgngpsfleglkrvgmlvcgpctvvqaalgeal
lntpqehldqivakieesamylynhigeciglaptmprgamylmsridlekyrdiktdve
ffeklleeenvqvlpgtifhapgftrltttrpvevyreaverikafcqrhaav
>d1bw3__ 2.46.1.2.1 Barwin {Barley (Hordeum vulgare)}
eqandvratyhyyrpaqnnwdlgapavsaycatwdaskplswrskygwtafcgpagprgq
aacgkclrvtnpatgaqitarivdqcanggldldwdtvftkidtngigyqqghlnvnyqf
vdcrd
>d1bw4__ 2.46.1.2.1 Barwin {Barley (Hordeum vulgare)}
eqandvratyhyyrpaqnnwdlgapavsaycatwdaskplswrskygwtafcgpagprgq
aacgkclrvtnpatgaqitarivdqcanggldldwdtvftkidtngigyqqghlnvnyqf
vdcrd
>d1bw5__ 1.4.1.1.12 Insulin gene enhancer protein isl-1 {Rat (Rattus norvegicus)}
mkttrvrtvlnekqlhtlrtcyaanprpdalmkeqlvemtglsprvirvwfqnkrckdkk
rsimmk
>d1bw6__ 1.4.1.7.1 DNA-binding domain of centromere binding protein B (CENP-B) {Human (Homo sapiens)}
mgpkrrqltfreksriiqeveenpdlrkgeiarrfnippstlstilknkrailase
>d1bw8__ 2.2.7.1.1 Second domain of Mu2 adaptin subunit (ap50) of ap2 adaptor {Rat (Rattus norvegicus)}
igwrregikyrrnelfldvlesvnllmspqgqvlsahvsgrvvmksylsgmpeckfgmnd
kiviekqgkgtadetsksgkqsiaiddctfhqcvrlskfdsersisfippdgefelmryr
ttkdiilpfrviplvrevgrtklevkvviksnfkpsllaqkievriptplntsgvqvicm
kgkakykasenaivwkikrmagmkesqisaeiellptndkkkwarppismnfevpfapsg
lkvrylkvfepklnysdhdvikwvryigrsgiyetrc
>d1bw9a1 3.2.1.7.6 (149-350) Phenylalanine dehydrogenase {Rhodococcus M4}
safttavgvfeamkatvahrglgsldgltvlvqglgavggslaslaaeagaqllvadtdt
ervahavalghtavaledvlstpcdvfapcamggvittevartldcsvvagaannviade
aasdilhargilyapdfvanaggaihlvgrevlgwsesvvheravaigdtlnqvfeisdn
dgvtpdeaartlagrrareast
>d1bw9a2 3.48.1.1.6 (1-148) Phenylalanine dehydrogenase {Rhodococcus M4}
sidsalnwdgemtvtrfdsmtgahfvirldstqlgpaaggtraaqysnladaltdagkla
gamtlkmavsnlpmgggksvialpaprhsidpstwarilrihaenidklsgnywtgpdvn
tnsadmdtlndttefvfgrslerggags
>d1bw9b1 3.2.1.7.6 (549-747) Phenylalanine dehydrogenase {Rhodococcus M4}
safttavgvfeamkatvahrglgsldgltvlvqglgavggslaslaaeagaqllvadtdt
ervahavalghtavaledvlstpcdvfapcamggvittevartldcsvvagaannviade
aasdilhargilyapdfvanaggaihlvgrevlgwsesvvheravaigdtlnqvfeisdn
dgvtpdeaartlagrrare
>d1bw9b2 3.48.1.1.6 (401-548) Phenylalanine dehydrogenase {Rhodococcus M4}
sidsalnwdgemtvtrfdkmtgahfvirldstqlgpaaggtraaqysqladaltdagkla
gamtlkmavsnlpmgggksvialpaprhsidpstwarilrihaenidklsgnywtgpdvn
tnsadmdtlndttefvfgrslerggags
>d1bwaa_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpfnvigrnlltqigctlnf
>d1bwab_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpfnvigrnlltqigctlnf
>d1bwba_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpfnvigrnlltqigatlnf
>d1bwbb_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpfnvigrnlltqigatlnf
>d1bwca1 3.3.1.5.1 (18-165,291-363) Glutathione reductase {Human (Homo sapiens)}
vasydylvigggsgglasarraaelgaraavveshklggtcvnvgcvpkkvmwntavhse
fmhdhadygfpscegkfnwrvikekrdayvsrlnaiyqnnltkshieiirghaaftsdpk
ptievsgkkytaphiliatggmpstpheXrvpntkdlslnklgiqtddkghiivdefqnt
nvkgiyavgdvcgkalltpvaiaagrklahrlfeykedskld
>d1bwca2 3.3.1.5.1 (166-290) Glutathione reductase {Human (Homo sapiens)}
sqipgaslgitsdgffqleelpgrsvivgagyiavemagilsalgsktslmirhdkvlrs
fdsmistncteelenagvevlkfsqvkevkktlsglevsmvtavpgrlpvmtmipdvdcl
lwaig
>d1bwca3 4.67.1.1.1 (364-478) Glutathione reductase {Human (Homo sapiens)}
ynniptvvfshppigtvgltedeaihkygienvktystsftpmyhavtkrktkcvmkmvc
ankeekvvgihmqglgcdemlqgfavavkmgatkadfdntvaihptsseelvtlr
>d1bwda_ 4.100.1.1.2 L-arginine: inosamine-phosphate amidinotransferase {Streptomyces griseus}
slvsvhnewdpleevivgtavgarvptadrsvfaveyagdyesqeqipsgaypdrvlket
eeelhvlaaeltklgvtvrrpgprdhsaliktpdwetdgfhdycprdgllsvgqtiietp
malrsrfleslaykdllleyfasgsrwlsapkprltddsyapqapagerltdeepvfdaa
nvlrfgtdllylvsdsgnelgakwlqsavgdtytvhpcrklyasthvdstivplrpglvl
tnpsrvndenmpdflrswenitcpelvdigftgdkphcsvwigmnllvvrpdlavvdrrq
talirllekhgmnvlplqlthsrtlgggfhcatldvrrtgaletyqf
>d1bwdb_ 4.100.1.1.2 L-arginine: inosamine-phosphate amidinotransferase {Streptomyces griseus}
slvsvhnewdpleevivgtavgarvptadrsvfaveyagdyesqeqipsgaypdrvlket
eeelhvlaaeltklgvtvrrpgprdhsaliktpdwetdgfhdycprdgllsvgqtiietp
malrsrfleslaykdllleyfasgsrwlsapkprltddsyapqapagerltdeepvfdaa
nvlrfgtdllylvsdsgnelgakwlqsavgdtytvhpcrklyasthvdstivplrpglvl
tnpsrvndenmpdflrswenitcpelvdigftgdkphcsvwigmnllvvrpdlavvdrrq
talirllekhgmnvlplqlthsrtlgggfhcatldvrrtaretyqf
>d1bwe__ 4.47.1.2.2 Ferredoxin {Bacillus schlegelii}
ayvitepcigtkcascvevcpvdcihegedqyyidpdvcidcgaceavcpvsaiyhedfv
peewksyiqknrdffkk
>d1bwfo1 3.46.1.3.1 (2-253) Glycerol kinase {Escherichia coli}
ekkyivaldqgttssravvmdhdaniisvsqrefeqiypkpgwvehdpmeiwatqswtlv
evlakadissdqiaaigitnqrettivweketgkpiynaivwqcrrtaeicehlkrdgle
dyirsntglvidpyfsgtkvkwildhvegsrerarrgellfgtvdtwliwkmtqgrvhvt
dytnasrtmlfnihtldwddkmlevldipremlpevrrssevygqtniggkggtripisg
iagdqqaalfgq
>d1bwfo2 3.46.1.3.1 (254-499) Glycerol kinase {Escherichia coli}
lcvkegmakntygtgcfmlmntgekavksengllttiacgptgevnyalegavfmagasi
qwlrdemklindaydseyfatkvqntngvyvvpaftglgapywdpyargaifgltrgvna
nhiiratlesiayqtrdvleamqadsgirlhalrvdggavannflmqfqsdilgtrverp
evrevtalgaaylaglavgfwqnldelqekavierefrpgietternyryagwkkavkra
maweeh
>d1bwfy1 3.46.1.3.1 (2-253) Glycerol kinase {Escherichia coli}
ekkyivaldqgttssravvmdhdaniisvsqrefeqiypkpgwvehdpmeiwatqswtlv
evlakadissdqiaaigitnqrettivweketgkpiynaivwqcrrtaeicehlkrdgle
dyirsntglvidpyfsgtkvkwildhvegsrerarrgellfgtvdtwliwkmtqgrvhvt
dytnasrtmlfnihtldwddkmlevldipremlpevrrssevygqtniggkggtripisg
iagdqqaalfgq
>d1bwfy2 3.46.1.3.1 (254-499) Glycerol kinase {Escherichia coli}
lcvkegmakntygtgcfmlmntgekavksengllttiacgptgevnyalegavfmagasi
qwlrdemklindaydseyfatkvqntngvyvvpaftglgapywdpyargaifgltrgvna
nhiiratlesiayqtrdvleamqadsgirlhalrvdggavannflmqfqsdilgtrverp
evrevtalgaaylaglavgfwqnldelqekavierefrpgietternyryagwkkavkra
maweeh
>d1bwh__ 4.2.1.2.1 Lysozyme {Chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1bwi__ 4.2.1.2.1 Lysozyme {Chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1bwj__ 4.2.1.2.1 Lysozyme {Chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1bwk__ 3.1.4.1.3 Old yellow enzyme (OYE) {Candida albicans}
sfvkdfkpqalgdtnlfkpikignnellhravippltrmralhpgnipnrdwaveyytqr
aqrpgtmiitegafispqaggydnapgvwseeqmvewtkifnaihekksfvwvqlwvlgw
aafpdnlardglrydsasdnvfmdaeqeakakkannpqhsltkdeikqyikeyvqaakns
iaagadgveinsangyllnqfldphsntrtdeyggsienrarftlevvdalveaighekv
glrlspygvfnsmsggaetgivaqyayvagelekrakagkrlafvhlveprvtnpflteg
egeyeggsndfvysiwkgpviragnfalhpevvreevkdkrtligygrffisnpdlvdrl
ekglplnkydrdtfyqmsahgyidyptyeealklgwdks
>d1bwl__ 3.1.4.1.3 Old yellow enzyme (OYE) {Candida albicans}
sfvkdfkpqalgdtnlfkpikignnellhravippltrmralhpgnipnrdwaveyytqr
aqrpgtmiitegafispqaggydnapgvwseeqmvewtkifnaihekksfvwvqlwvlgw
aafpdnlardglrydsasdnvfmdaeqeakakkannpqhsltkdeikqyikeyvqaakns
iaagadgveinsahgyllnqfldphsntrtdeyggsienrarftlevvdalveaighekv
glrlspygvfnsmsggaetgivaqyayvagelekrakagkrlafvhlveprvtnpflteg
egeyeggsndfvysiwkgpviragnfalhpevvreevkdkrtligygrffisnpdlvdrl
ekglplnkydrdtfyqmsahgyidyptyeealklgwdks
>d1bwma1 2.1.1.1.154 (301-417) T-cell antigen receptor {Mouse (Mus musculus), alpha-chain}
qqqvrqspqsltvwegettilncsyedstfdyfpwyrqfpgkspalliaislvsnkkedg
rftiffnkrekklslhitdsqpgdsatyfcaatgsfnkltfgagtrlavspy
>d1bwma2 2.1.1.1.156 (3-116a) T-cell antigen receptor {Mouse (Mus musculus), beta-chain}
avtqsprnkvavtggkvtlscnqtnnhnnmywyrqdtghglrlihysygagstekgdipd
gykasrpsqenfslilelatpsqtsvyfcasggqgraeqffgpgtrltvl
>d1bwna_ 2.49.1.1.5 Bruton's tyrosine kinase {Human (Homo sapiens)}
aavilesiflkrsqqkkktsplnfkkrlflltvhklsyykydfergrrgskkgsidveki
tcvetvvpeknppperqiprrgeessemeqisiierfpypfqvvydegplyvfspteelr
krwihqlknvirynsdlvqkyhpcfwidgqylccsqtaknamgcqilen
>d1bwnb_ 2.49.1.1.5 Bruton's tyrosine kinase {Human (Homo sapiens)}
aavilesiflkrsqqkkktsplnfkkrlflltvhklsyykydfergrrgskkgsidveki
tcvetvvpeknppperqiprrgeessemeqisiierfpypfqvvydegplyvfspteelr
krwihqlknvirynsdlvqkyhpcfwidgqylccsqtaknamgcqilen
>d1bwoa_ 1.54.1.1.2 Plant non-specific lipid-transfer protein (ns-LTP) {Wheat (Triticum aestivum), L. seeds}
idcghvdslvrpclsyvqggpgpsgqccdgvknlhnqarsqsdrqsacnclkgiargihn
lnednarsippkcgvnlpytislnidcsrv
>d1bwob_ 1.54.1.1.2 Plant non-specific lipid-transfer protein (ns-LTP) {Wheat (Triticum aestivum), L. seeds}
idcghvdslvrpclsyvqggpgpsgqccdgvknlhnqarsqsdrqsacnclkgiargihn
lnednarsippkcgvnlpytislnidcsrv
>d1bwp__ 3.16.8.2.1 Platelet-activating factor acetylhydrolase {Bovine (Bos taurus)}
enpaskptpvqdvqgdgrwmslhhrfvadskdkepevvfigdsavqlmhqceiwrelfsp
lhalnfgiggdstqhvlwrlengelehirpkivvvwvgtnnhghtaeqvtggikaivqlv
nerqpqarvvvlgllprgqhpnplreknrrvnelvraalaghprahfldadpgfvhsdgt
ishhdmydylhlsrlgytpvcralhslllrll
>d1bwq__ 3.16.8.2.1 Platelet-activating factor acetylhydrolase {Bovine (Bos taurus)}
enpaskptpvqdvqgdgrwmslhhrfvadskdkepevvfigdslvqlmhqceiwrelfsp
lhalnfgiggdstqhvlwrlengelehirpkivvvwvgtnnhghtaeqvtggikaivqlv
nerqpqarvvvlgllprgqhpnplreknrrvnelvraalaghprahfldadpgfvhsdgt
ishhdmydyahlsrlgytpvcralhslllrll
>d1bwr__ 3.16.8.2.1 Platelet-activating factor acetylhydrolase {Bovine (Bos taurus)}
enpaskptpvqdvqgdgrwmslhhrfvadskdkepevvfigdslvqlmhqceiwrelfsp
lhalnfgiggdstqhvlwrlengelehirpkivvvwvgsnnhghtaeqvtggikaivqlv
nerqpqarvvvlgllprgqhpnplreknrrvnelvraalaghprahfldadpgfvhsdgt
ishhdmydylhlsrlgytpvcralhslllrll
>d1bwsa_ 3.2.1.2.3 GDP-4-keto-6-deoxy-d-mannose epimerase/reductase (GDP-fucose synthetase) {Escherichia coli}
kqrvfiaghrgmvgsairrqleqrgdvelvlrtrdelnlldsravhdffaseridqvyla
aakvggivanntypadfiyqnmmiesniihaahqndvnkllflgssciypklakqpmaes
ellqgtleptnepyaiakiagiklcesynrqygrdyrsvmptnlygphdnfhpsnshvip
allrrfheataqnapdvvvwgsgtpmreflhvddmaaasihvmelahevwlentqpmlsh
invgtgvdctirdvaqtiakvvgykgrvvfdaskpdgtprklldvtrlhqlgwyheisle
aglastyqwflenq
>d1bwua_ 2.69.1.1.2 Lectin (agglutinin) {Garlic (Allium sativum)}
rnilrndeglyggqsldvnpyhfimqedcnlvlydhstsvwasntgilgkkgcravlqsd
gnfvvydaegrslwashsvrgngnyvlvlqedgnvviyrsdiwstn
>d1bwud_ 2.69.1.1.2 Lectin (agglutinin) {Garlic (Allium sativum)}
rniltndeglyggqsldvnpyhlimqedcnlvlydhstavwssntdipgkkgckavlqsd
gnfvvydaegaslwashsvrgngnyvlvlqedgnvviyrsdiwstntyr
>d1bwup_ 2.69.1.1.2 Lectin (agglutinin) {Garlic (Allium sativum)}
rniltndeglyagqsldvnpyhfimqedcnlvlydhstsvwasntgilgkkgckavlqad
gnfvvydaegrslwashsvrgngnyvlvlqedgnvviygsdiwstn
>d1bwuq_ 2.69.1.1.2 Lectin (agglutinin) {Garlic (Allium sativum)}
rniltndeglyagqsldvnpyhlimqedcnlvlydhstavwssntdipgkkgckavlqsd
gnfvvydaegaslwashsvrgngnyvlvlqedgnvviygsdiwstntyk
>d1bwva1 3.1.12.1.3 (150-478) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Galdieria partita}
gpatgvilererldkfgrpllgcttkpklglsgknygrvvyealkggldfvxddeninsq
pfmrwrerylftmeavnkasaatgevkghylnvtaatmeemyaranfakelgsviimidl
vigytaiqtmakwardndmilhlhragnstysrqknhgmnfrvickwmrmagvdhihagt
vvgklegdpiitrgfyktlllpklernlqeglffdmewaslrkvmpvasggihagqmhql
ihylgedvvlqfgggtighpdgiqagatanrvaleamilarnenrdyltegpeilreaak
tcgalrtaldlwkditfnytstdtsdfv
>d1bwva2 4.47.9.1.3 (7-149) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Galdieria partita}
riknsryesgvipyakmgywnpdyqvkdtdvlalfrvtpqpgvdpieaaaavagesstat
wtvvwtdlltaadlyrakaykvdqvpnnpeqyfayiayeldlfeegsianltasiignvf
gfkavkalrledmrlplaylktfq
>d1bwvc1 3.1.12.1.3 (150-478) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Galdieria partita}
gpatgvilererldkfgrpllgcttkpklglsgknygrvvyealkggldfvxddeninsq
pfmrwrerylftmeavnkasaatgevkghylnvtaatmeemyaranfakelgsviimidl
vigytaiqtmakwardndmilhlhragnstysrqknhgmnfrvickwmrmagvdhihagt
vvgklegdpiitrgfyktlllpklernlqeglffdmewaslrkvmpvasggihagqmhql
ihylgedvvlqfgggtighpdgiqagatanrvaleamilarnenrdyltegpeilreaak
tcgalrtaldlwkditfnytstdtsdfv
>d1bwvc2 4.47.9.1.3 (7-149) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Galdieria partita}
riknsryesgvipyakmgywnpdyqvkdtdvlalfrvtpqpgvdpieaaaavagesstat
wtvvwtdlltaadlyrakaykvdqvpnnpeqyfayiayeldlfeegsianltasiignvf
gfkavkalrledmrlplaylktfq
>d1bwve1 3.1.12.1.3 (150-478) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Galdieria partita}
gpatgvilererldkfgrpllgcttkpklglsgknygrvvyealkggldfvxddeninsq
pfmrwrerylftmeavnkasaatgevkghylnvtaatmeemyaranfakelgsviimidl
vigytaiqtmakwardndmilhlhragnstysrqknhgmnfrvickwmrmagvdhihagt
vvgklegdpiitrgfyktlllpklernlqeglffdmewaslrkvmpvasggihagqmhql
ihylgedvvlqfgggtighpdgiqagatanrvaleamilarnenrdyltegpeilreaak
tcgalrtaldlwkditfnytstdtsdfv
>d1bwve2 4.47.9.1.3 (7-149) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Galdieria partita}
riknsryesgvipyakmgywnpdyqvkdtdvlalfrvtpqpgvdpieaaaavagesstat
wtvvwtdlltaadlyrakaykvdqvpnnpeqyfayiayeldlfeegsianltasiignvf
gfkavkalrledmrlplaylktfq
>d1bwvg1 3.1.12.1.3 (150-478) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Galdieria partita}
gpatgvilererldkfgrpllgcttkpklglsgknygrvvyealkggldfvxddeninsq
pfmrwrerylftmeavnkasaatgevkghylnvtaatmeemyaranfakelgsviimidl
vigytaiqtmakwardndmilhlhragnstysrqknhgmnfrvickwmrmagvdhihagt
vvgklegdpiitrgfyktlllpklernlqeglffdmewaslrkvmpvasggihagqmhql
ihylgedvvlqfgggtighpdgiqagatanrvaleamilarnenrdyltegpeilreaak
tcgalrtaldlwkditfnytstdtsdfv
>d1bwvg2 4.47.9.1.3 (7-149) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Galdieria partita}
riknsryesgvipyakmgywnpdyqvkdtdvlalfrvtpqpgvdpieaaaavagesstat
wtvvwtdlltaadlyrakaykvdqvpnnpeqyfayiayeldlfeegsianltasiignvf
gfkavkalrledmrlplaylktfq
>d1bwvs_ 4.55.1.1.3 Ribulose 1,5-bisphosphate carboxylase-oxygenase {Galdieria partita}
vritqgtfsflpdltdeqikkqidymiskklaigieytndihprnayweiwglplfdvtd
paavlfeinacrkarsnfyikvvgfssvrgiestiisfivnrpkhepgfnlmrqedksrs
ikytihsyesykpedery
>d1bwvu_ 4.55.1.1.3 Ribulose 1,5-bisphosphate carboxylase-oxygenase {Galdieria partita}
vritqgtfsflpdltdeqikkqidymiskklaigieytndihprnayweiwglplfdvtd
paavlfeinacrkarsnfyikvvgfssvrgiestiisfivnrpkhepgfnlmrqedksrs
ikytihsyesykpedery
>d1bwvw_ 4.55.1.1.3 Ribulose 1,5-bisphosphate carboxylase-oxygenase {Galdieria partita}
vritqgtfsflpdltdeqikkqidymiskklaigieytndihprnayweiwglplfdvtd
paavlfeinacrkarsnfyikvvgfssvrgiestiisfivnrpkhepgfnlmrqedksrs
ikytihsyesykpedery
>d1bwvy_ 4.55.1.1.3 Ribulose 1,5-bisphosphate carboxylase-oxygenase {Galdieria partita}
vritqgtfsflpdltdeqikkqidymiskklaigieytndihprnayweiwglplfdvtd
paavlfeinacrkarsnfyikvvgfssvrgiestiisfivnrpkhepgfnlmrqedksrs
ikytihsyesykpedery
>d1bwwa_ 2.1.1.1.143 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (kappa) dimer REI (human)}
tpdiqmtqspsslsasvgdrvtitcqasqdiikylnwyqqkpgkapklliyeasnlqagv
psrfsgsgsgtdytftisslqpediatyycqqyqslpytfgqgtklqit
>d1bwwb_ 2.1.1.1.143 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (kappa) dimer REI (human)}
tpdiqmtqspsslsasvgdrvtitcqasqdiikylnwyqqkpgkapklliyeasnlqagv
psrfsgsgsgtdytftisslqpediatyycqqyqslpytfgqgtklqit
>d1bwy__ 2.53.1.2.2 Muscle fatty acid binding protein (m-fabp) {Bovine (Bos taurus)}
vdafvgtwklvdsknfddymkslgvgfatrqvgnmtkpttiievngdtviiktqstfknt
eisfklgvefdettaddrkvksivtldggklvhvqkwngqetslvremvdgkliltlthg
tavctrtyekqa
>d1bwz_1 4.19.1.1.1 (1-130) Diaminopimelate epimerase {Haemophilus influenzae}
mqfskmhglgndfvvvdgvtqnvfftpetirrlanrhcgigfdqlliveapydpeldfhy
rifnadgsevsqcgngarcfarfvtlkgltnkkdisvstqkgnmvltvkddnqirvnmge
piwepakipf
>d1bwz_2 4.19.1.1.1 (131-274) Diaminopimelate epimerase {Haemophilus influenzae}
tankfeknyilrtdiqtvlcgavsmgnphcvvqvddiqtanveqlgpllesherfpervn
agfmqiinkehiklrvyergagetqacgsgacaavavgimqgllnnnvqvdlpggslmie
wngvghplymtgeathiydgfi
>d1bx0_1 2.38.1.1.1 (19-154) Ferredoxin reductase (flavodoxin reductase) {Spinach (Spinacia oleracea)}
hskkmeegitvnkfkpktpyvgrcllntkitgddapgetwhmvfshegeipyregqsvgv
ipdgedkngkphklrlysiassalgdfgdaksvslcvkrliytndagetikgvcsnflcd
lkpgaevkltgpvgke
>d1bx0_2 3.18.1.1.1 (155-314) Ferredoxin reductase (flavodoxin reductase) {Spinach (Spinacia oleracea)}
mlmpkdpnatiimlgtgtgiapfrsflwkmffekhddykfnglawlflgvptsssllyke
efekmkekapdnfrldfavsreqtnekgekmyiqtrmaqyavelwemlkkdntyfymcgl
kgmekgiddimvslaaaegidwieykrqlkkaeqwnvlvy
>d1bx1_1 2.38.1.1.1 (19-154) Ferredoxin reductase (flavodoxin reductase) {Spinach (Spinacia oleracea)}
hskkmeegitvnkfkpktpyvgrcllntkitgddapgetwhmvfshegeipyregqsvgv
ipdgedkngkphklrlysiassalgdfgdaksvslcvkrliytndagetikgvcsnflcd
lkpgaevkltgpvgke
>d1bx1_2 3.18.1.1.1 (155-314) Ferredoxin reductase (flavodoxin reductase) {Spinach (Spinacia oleracea)}
mlmpkdpnatiimlgtgtgiapfrsflwkmffekhddykfnglawlflgvptsssllyke
efekmkekapdnfrldfavsreqtnekgekmyiqtrmaqyavelwemlkkdntyfymcgl
kgmekgiddimvslaaaegidwieykrqlkkaeqwnvqvy
>d1bx2a1 2.1.1.2.150 (82-181) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dr2}
itnvppevtvltnspvelrepnvlicfidkftppvvnvtwlrngkpvttgvsetvflpre
dhlfrkfhylpflpstedvydcrvehwgldepllkhwefd
>d1bx2a2 4.17.1.1.5 (2-81) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr2}
aeehviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgala
niavdkanleimtkrsnytp
>d1bx2b1 2.1.1.2.150 (93-193) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dr2}
rrvqpkvtvypsktqplqhhnllvcsvsgfypgsievrwflngqeekagmvstgliqngd
wtfqtlvmletvprsgevytcqvehpsvtspltvewrarse
>d1bx2b2 4.17.1.1.5 (3-92) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr2}
trprflwqpkrechffngtervrfldryfynqeesvrfdsdvgefravtelgrpdaeywn
sqkdileqaraavdtycrhnygvvesftvq
>d1bx3__ 3.77.1.2.1 Glycogen phosphorylase {Rabbit (Oryctolagus cuniculus)}
isvrglagvenvtelkknfnrhlhftlvkdrnvatprdyyfalahtvrdhlvgrwirtqq
hyyekdpkriyylslefymgrtlqntmvnlalenacdeatyqlgldmeeleeieedaglg
ngglgrlaacfldsmatlglaaygygiryefgifnqkicggwqmeeaddwlrygnpweka
rpeftlpvhfygrvehtsqgakwvdtqvvlampydtpvpgyrnnvvntmrlwsakapndf
nlkdfnvggyiqavldrnlaenisrvlypndnffegkelrlkqeyfvvaatlqdiirrfk
sskfgcrdpvrtnfdafpdkvaiqlndthpslaipelmrvlvdlerldwdkawevtvktc
aytnhtvipealerwpvhlletllprhlqiiyeinqrflnrvaaafpgdvdrlrrmslve
egavkrinmahlciagshavngvarihseilkktifkdfyelephkfqnktngitprrwl
vlcnpglaeiiaerigeeyisdldqlrkllsyvddeafirdvakvkqenklkfaaylere
ykvhinpnslfdvqvkriheykrqllnclhvitlynrikkepnkfvvprtvmiggkaapg
yhmakmiiklitaigdvvnhdpvvgdrlrviflenyrvslaekvipaadlseqistagte
asgtgnmxfmlngaltigtmdganvemaeeageenffifgmrvedvdrldqrgynaqeyy
dripelrqiieqlssgffspkqpdlfkdivnmlmhhdrfkvfadyeeyvkcqervsalyk
nprewtrmvirniatsgkfssdrtiaqyareiwgvepsrqrlp
>d1bx4a_ 3.62.1.1.2 Adenosine kinase {Human (Homo sapiens)}
vrenilfgmgnplldisavvdkdfldkyslkpndqilaedkhkelfdelvkkfkveyhag
gstqnsikvaqwmiqqphkaatffgcigidkfgeilkrkaaeahvdahyyeqneqptgtc
aacitgdnrslianlaaancykkekhldleknwmlvekarvcyiagffltvspesvlkva
hhasennriftlnlsapfisqfykeslmkvmpyvdilfgneteaatfareqgfetkdike
iakktqalpkmnskrqriviftqgrddtimatesevtafavldqdqkeiidtngagdafv
ggflsqlvsdkplteciraghyaasiiirrtgctfpekpdfh
>d1bx6__ 4.117.1.1.5 cAMP-dependent PK, catalytic subunit {Mouse (Mus musculus)}
qesvkeflakakedflkkwetpsqntaqldqfdriktlgtgsfgrvmlvkhkesgnhyam
kildkqkvvklkqiehtlnekrilqavnfpflvklefsfkdnsnlymvmeyvaggemfsh
lrrigrfsepharfyaaqivltfeylhsldliyrdlkpenllidqqgyiqvtdfgfakrv
kgrtwxlcgtpeylapeiilskgynkavdwwalgvliyemaagyppffadqpiqiyekiv
sgkvrfpshfssdlkdllrnllqvdltkrfgnlkngvndiknhkwfattdwiaiyqrkve
apfipkfkgpgdtsnfddyeeeeirvxinekcgkeftef
>d1bx7__ 7.3.15.1.1 Hirustasin {Medicinal leech (Hirudo medicinalis)}
gntcggetcsaaqvclkgkcvcnevhcrirckyglkkdengceypcscaka
>d1bx8__ 7.3.15.1.1 Hirustasin {Medicinal leech (Hirudo medicinalis)}
tcggetcsaaqvclkgkcvcnevhcrirckyglkkdengceypcscaka
>d1bx9_1 1.48.1.1.16 (86-210) Glutathione S-transferase {Mouse-ear cress (Arabidopsis thaliana)}
qtdsknisqyaimaigmqvedhqfdpvasklafeqifksiyglttdeavvaeeeaklakv
ldvyearlkefkylagetftltdlhhipaiqyllgtptkklfterprvnewvaeitkrpa
sekvq
>d1bx9_2 3.38.1.5.16 (1-85) Glutathione S-transferase {Mouse-ear cress (Arabidopsis thaliana)}
gikvfghpasiatrrvlialheknldfelvhvelkdgehkkepflsrnpfgqvpafedgd
lklfesraitqyiahryenqgtnll
>d1bxa__ 2.5.1.1.1 Amicyanin {Paracoccus denitrificans}
dkatipsespfaaaevadgaivvdiakmkyetpelhvkvgdtvtwinreamphnvhfvag
vlgeaalkgpmmkkeqaysltfteagtydyhctphpfmrgkvvve
>d1bxba_ 3.1.13.2.11 D-xylose isomerase {Thermus aquaticus, subsp. Thermophilus}
myepkpehrftfglwtvgnvgrdpfgdavrerldpvyvvhklaelgaygvnlhdedlipr
gtppqerdqivrrfkkaldetglkvpmvtanlfsdpafkdgaftspdpwvrayalrksle
tmdlgaelgaeiyvvwpgregaeveatgkarkvwdwvrealnfmaayaedqgygyrfale
pkpneprgdiyfatvgsmlafihtldrperfglnpefahetmaglnfvhavaqaldagkl
fhidlndqrmsrfdqdlrfgsenlkaafflvdllessgyqgprhfdahalrtedeegvwa
fargcmrtylilkeraeafredpevkellaayyqedpaalallgpysrekaealkraelp
leakrrrgyalerldqlaveyllgvrg
>d1bxbb_ 3.1.13.2.11 D-xylose isomerase {Thermus aquaticus, subsp. Thermophilus}
myepkpehrftfglwtvgnvgrdpfgdavrerldpvyvvhklaelgaygvnlhdedlipr
gtppqerdqivrrfkkaldetglkvpmvtanlfsdpafkdgaftspdpwvrayalrksle
tmdlgaelgaeiyvvwpgregaeveatgkarkvwdwvrealnfmaayaedqgygyrfale
pkpneprgdiyfatvgsmlafihtldrperfglnpefahetmaglnfvhavaqaldagkl
fhidlndqrmsrfdqdlrfgsenlkaafflvdllessgyqgprhfdahalrtedeegvwa
fargcmrtylilkeraeafredpevkellaayyqedpaalallgpysrekaealkraelp
leakrrrgyalerldqlaveyllgvrg
>d1bxbc_ 3.1.13.2.11 D-xylose isomerase {Thermus aquaticus, subsp. Thermophilus}
myepkpehrftfglwtvgnvgrdpfgdavrerldpvyvvhklaelgaygvnlhdedlipr
gtppqerdqivrrfkkaldetglkvpmvtanlfsdpafkdgaftspdpwvrayalrksle
tmdlgaelgaeiyvvwpgregaeveatgkarkvwdwvrealnfmaayaedqgygyrfale
pkpneprgdiyfatvgsmlafihtldrperfglnpefahetmaglnfvhavaqaldagkl
fhidlndqrmsrfdqdlrfgsenlkaafflvdllessgyqgprhfdahalrtedeegvwa
fargcmrtylilkeraeafredpevkellaayyqedpaalallgpysrekaealkraelp
leakrrrgyalerldqlaveyllgvrg
>d1bxbd_ 3.1.13.2.11 D-xylose isomerase {Thermus aquaticus, subsp. Thermophilus}
myepkpehrftfglwtvgnvgrdpfgdavrerldpvyvvhklaelgaygvnlhdedlipr
gtppqerdqivrrfkkaldetglkvpmvtanlfsdpafkdgaftspdpwvrayalrksle
tmdlgaelgaeiyvvwpgregaeveatgkarkvwdwvrealnfmaayaedqgygyrfale
pkpneprgdiyfatvgsmlafihtldrperfglnpefahetmaglnfvhavaqaldagkl
fhidlndqrmsrfdqdlrfgsenlkaafflvdllessgyqgprhfdahalrtedeegvwa
fargcmrtylilkeraeafredpevkellaayyqedpaalallgpysrekaealkraelp
leakrrrgyalerldqlaveyllgvrg
>d1bxca_ 3.1.13.2.10 D-xylose isomerase {Thermus aquaticus, subsp. Caldophilus}
myepkpehrftfglwtvgnvgrdpfgdavrerldpvyvghklaelgvhgvnlhdedlipr
gtppqerdqivrrfkraldetglkvpmvtgnlfsdpgfkdggftsrdpwvrayafrksle
tmdlgaelgaeiyvvwpgregaeveatgkarkvwdwvreplnfmaayaedqgygyrfale
pkpneprgdiyfatvgsmlalihtlerperfglnpefahetmaglnfvhavaqaldagkl
lhidlngqrmnrfdqdlrfgsenlkaafllvdllessgyqgprhfdahalrtedeegvwa
fargcmrtylilkeraeafredpevkellaayyqedpaalplmdpyshekaealkraelp
leakrhrgyalerldqlaveyllgvrg
>d1bxcb_ 3.1.13.2.10 D-xylose isomerase {Thermus aquaticus, subsp. Caldophilus}
myepkpehrftfglwtvgnvgrdpfgdavrerldpvyvghklaelgvhgvnlhdedlipr
gtppqerdqivrrfkraldetglkvpmvtgnlfsdpgfkdggftsrdpwvrayafrksle
tmdlgaelgaeiyvvwpgregaeveatgkarkvwdwvreplnfmaayaedqgygyrfale
pkpneprgdiyfatvgsmlalihtlerperfglnpefahetmaglnfvhavaqaldagkl
lhidlngqrmnrfdqdlrfgsenlkaafllvdllessgyqgprhfdahalrtedeegvwa
fargcmrtylilkeraeafredpevkellaayyqedpaalplmdpyshekaealkraelp
leakrhrgyalerldqlaveyllgvrg
>d1bxcc_ 3.1.13.2.10 D-xylose isomerase {Thermus aquaticus, subsp. Caldophilus}
myepkpehrftfglwtvgnvgrdpfgdavrerldpvyvghklaelgvhgvnlhdedlipr
gtppqerdqivrrfkraldetglkvpmvtgnlfsdpgfkdggftsrdpwvrayafrksle
tmdlgaelgaeiyvvwpgregaeveatgkarkvwdwvreplnfmaayaedqgygyrfale
pkpneprgdiyfatvgsmlalihtlerperfglnpefahetmaglnfvhavaqaldagkl
lhidlngqrmnrfdqdlrfgsenlkaafllvdllessgyqgprhfdahalrtedeegvwa
fargcmrtylilkeraeafredpevkellaayyqedpaalplmdpyshekaealkraelp
leakrhrgyalerldqlaveyllgvrg
>d1bxcd_ 3.1.13.2.10 D-xylose isomerase {Thermus aquaticus, subsp. Caldophilus}
myepkpehrftfglwtvgnvgrdpfgdavrerldpvyvghklaelgvhgvnlhdedlipr
gtppqerdqivrrfkraldetglkvpmvtgnlfsdpgfkdggftsrdpwvrayafrksle
tmdlgaelgaeiyvvwpgregaeveatgkarkvwdwvreplnfmaayaedqgygyrfale
pkpneprgdiyfatvgsmlalihtlerperfglnpefahetmaglnfvhavaqaldagkl
lhidlngqrmnrfdqdlrfgsenlkaafllvdllessgyqgprhfdahalrtedeegvwa
fargcmrtylilkeraeafredpevkellaayyqedpaalplmdpyshekaealkraelp
leakrhrgyalerldqlaveyllgvrg
>d1bxda_ 4.96.1.3.1 Histidine kinase domain of the osmosensor EnvZ {(Escherichia coli)}
tgqempmemadlnavlgeviaaesgyereietalypgsievkmhplsikravanmvvnaa
rygngwikvssgtepnrawfqveddgpgiapeqrkhlfqpfvrgdsartisgtglglaiv
qrivdnhngmlelgtsergglsirawlpvpvtraqgttkeg
>d1bxe__ 4.45.1.1.1 Ribosomal protein L22 {Thermus acuaticus, subsp. Thermus thermophilus}
eakaiaryvrisprkvrlvvdlirgksleearnilrytnkrgayfvakvlesaaanavnn
hdmledrlyvkaayvdegpalkrvlprargradiikkr
>d1bxga1 3.2.1.7.6 (149-349) Phenylalanine dehydrogenase {Rhodococcus M4}
safttavgvfeamkatvahrglgsldgltvlvqglgavggslaslaaeagaqllvadtdt
ervahavalghtavaledvlstpcdvfapcamggvittevartldcsvvagaannviade
aasdilhargilyapdfvanaggaihlvgrevlgwsesvvheravaigdtlnqvfeisdn
dgvtpdeaartlagrrareas
>d1bxga2 3.48.1.1.6 (1-148) Phenylalanine dehydrogenase {Rhodococcus M4}
sidsalnwdgemtvtrfdsktgahfvirldstqlgpaaggtraaqysqladaltdagkla
gamtlkmavsnlpmgggksvialpaprhsidpstwarilrihaenidklsgnywtgpdvn
tnsadmdtlndttefvfgrslerggags
>d1bxgb1 3.2.1.7.6 (549-747) Phenylalanine dehydrogenase {Rhodococcus M4}
safttavgvfeamkatvahrglgsldgltvlvqglgavggslaslaaeagaqllvadtdt
ervahavalghtavaledvlstpcdvfapcamggvittevartldcsvvagaannviade
aasdilhargilyapdfvanaggaihlvgrevlgwsesvvheravaigdtlnqvfeisdn
dgvtpdeaartlagrrare
>d1bxgb2 3.48.1.1.6 (401-548) Phenylalanine dehydrogenase {Rhodococcus M4}
sidsalnwdgemtvtrfdrmtgahfvirldstqlgpaaggtraaqysqladaltdagkla
gamtlkmavsnlpmgggksvialpaprhsidpstwarilrihaenidklsgnywtgpdvn
tnsadmdtlndttefvfgrslerggags
>d1bxha_ 2.26.1.1.1 Concanavalin A {Jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1bxhb_ 2.26.1.1.1 Concanavalin A {Jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1bxhc_ 2.26.1.1.1 Concanavalin A {Jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1bxhd_ 2.26.1.1.1 Concanavalin A {Jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1bxia_ 1.29.2.1.3 ImE9 protein {Escherichia coli}
lkasisdyteaeflqlvtticnadtsseeelvklvthfeemtehpsgsdliyypkegddd
spsgivntvqqwraangksgfkq
>d1bxib_ 4.4.1.1.2 DNase domain of colicin E9 {Escherichia coli}
eskrnkpgkatgkgkpvgdkwlddagkdsgapipdriadklrdkefksfddfrkavweev
skdpelsknlnpsnkssvskgyspftpknqqvggrkvyelhhdkpisqggevydxdnirv
ttpkrhidih
>d1bxj__ 7.3.2.1.2 Trypsin inhibitor {Squash (Cucurbita maxima)}
rvcprilleckkdsdclaecvclehgycg
>d1bxka_ 3.2.1.2.2 dTDP-glucose 4,6-dehydratase {Escherichia coli}
mrkilitggagfigsalvryiinetsdavvvvdkltyagnlmslapvaqserfafekvdi
cdraelarvftehqpdcvmhlaaeshvdrsidgpaafietnivgtytlleaaraywnalt
edkksafrfhhistdevygdlhstddfftettpyapsspysaskassdhlvrawlrtygl
ptlitncsnnygpyhfpekliplmilnalagkslpvygngqqirdwlyvedharalycva
ttgkvgetynigghnerknldvveticelleelapnkphgvahyrdlitfvadrpghdlr
yaidaskiarelgcvpqetfesgmrktvqwylaneswwkqvqdgsyqge
>d1bxkb_ 3.2.1.2.2 dTDP-glucose 4,6-dehydratase {Escherichia coli}
mrkilitggagfigsalvryiinetsdavvvvdkltyagnlmslapvaqserfafekvdi
cdraelarvftehqpdcvmhlaaeshvdrsidgpaafietnivgtytlleaaraywnalt
edkksafrfhhistdevygdlhstddfftettpyapsspysaskassdhlvrawlrtygl
ptlitncsnnygpyhfpekliplmilnalagkslpvygngqqirdwlyvedharalycva
ttgkvgetynigghnerknldvveticelleelapnkphgvahyrdlitfvadrpghdlr
yaidaskiarelgcvpqetfesgmrktvqwylaneswwkqvqdgsyqge
>d1bxla_ 6.1.4.1.1 Apoptosis regulator Bcl-xL {Human (Homo sapiens)}
msmamsqsnrelvvdflsyklsqkgyswsqfsdveenrteapegteseavkqalreagde
felryrrafsdltsqlhitpgtayqsfeqvvnelfrdgvnwgrivaffsfggalcvesvd
kemqvlvsriaawmatylndhlepwiqenggwdtfvelygnnaaaesrkgqerlehhhhh
h
>d1bxm__ 1.124.1.1.1 beta-cryptogein {Phytophthora cryptogea}
rgtctatqqtaayhtlvsilsdasfnqcstdsgysmltakalpttaqyklmcastacntm
ikkivtlnppncdltvptsglvlnvysyangfsnkcssl
>d1bxna1 3.1.12.1.4 (151-467) Ribulose 1,5-bisphosphate carboxylase-oxygenase {(Alcaligenes eutrophus)}
fagpstgiivererldkfgrpllgattkpklglsgrnygrvvyeglkggldfmkddenin
sqpfmhwrdrflfvmdavnkasaatgevkgsylnvtagtmeemyrraefakslgsviimv
dlivgwtciqsmsnwcrqndmilhlhraghgtytrqknhgvsfrviakwlrlagvdhmht
gtavgklegdpltvqgyynvcrdaytqtdltrglffdqdwaslrkvmpvasggihagqmh
qlihlfgddvvlqfgggtighpqgiqagatanrvaleamvlarnegrdilnegpeilrda
arwcgplraaldtwgdi
>d1bxna2 4.47.9.1.4 (22-150) Ribulose 1,5-bisphosphate carboxylase-oxygenase {(Alcaligenes eutrophus)}
ykemgywdgdyvpkdtdllalfritpqdgvdpveaaaavagesstatwtvvwtdrltacd
myrakayrvdpvpnnpeqffcyvaydlslfeegsianltasiignvfsfkpikaarledm
rfpvayvkt
>d1bxnc1 3.1.12.1.4 (151-467) Ribulose 1,5-bisphosphate carboxylase-oxygenase {(Alcaligenes eutrophus)}
fagpstgiivererldkfgrpllgattkpklglsgrnygrvvyeglkggldfmkddenin
sqpfmhwrdrflfvmdavnkasaatgevkgsylnvtagtmeemyrraefakslgsviimv
dlivgwtciqsmsnwcrqndmilhlhraghgtytrqknhgvsfrviakwlrlagvdhmht
gtavgklegdpltvqgyynvcrdaytqtdltrglffdqdwaslrkvmpvasggihagqmh
qlihlfgddvvlqfgggtighpqgiqagatanrvaleamvlarnegrdilnegpeilrda
arwcgplraaldtwgdi
>d1bxnc2 4.47.9.1.4 (22-150) Ribulose 1,5-bisphosphate carboxylase-oxygenase {(Alcaligenes eutrophus)}
ykemgywdgdyvpkdtdllalfritpqdgvdpveaaaavagesstatwtvvwtdrltacd
myrakayrvdpvpnnpeqffcyvaydlslfeegsianltasiignvfsfkpikaarledm
rfpvayvkt
>d1bxne1 3.1.12.1.4 (151-467) Ribulose 1,5-bisphosphate carboxylase-oxygenase {(Alcaligenes eutrophus)}
fagpstgiivererldkfgrpllgattkpklglsgrnygrvvyeglkggldfmkddenin
sqpfmhwrdrflfvmdavnkasaatgevkgsylnvtagtmeemyrraefakslgsviimv
dlivgwtciqsmsnwcrqndmilhlhraghgtytrqknhgvsfrviakwlrlagvdhmht
gtavgklegdpltvqgyynvcrdaytqtdltrglffdqdwaslrkvmpvasggihagqmh
qlihlfgddvvlqfgggtighpqgiqagatanrvaleamvlarnegrdilnegpeilrda
arwcgplraaldtwgdi
>d1bxne2 4.47.9.1.4 (22-150) Ribulose 1,5-bisphosphate carboxylase-oxygenase {(Alcaligenes eutrophus)}
ykemgywdgdyvpkdtdllalfritpqdgvdpveaaaavagesstatwtvvwtdrltacd
myrakayrvdpvpnnpeqffcyvaydlslfeegsianltasiignvfsfkpikaarledm
rfpvayvkt
>d1bxng1 3.1.12.1.4 (151-467) Ribulose 1,5-bisphosphate carboxylase-oxygenase {(Alcaligenes eutrophus)}
fagpstgiivererldkfgrpllgattkpklglsgrnygrvvyeglkggldfmkddenin
sqpfmhwrdrflfvmdavnkasaatgevkgsylnvtagtmeemyrraefakslgsviimv
dlivgwtciqsmsnwcrqndmilhlhraghgtytrqknhgvsfrviakwlrlagvdhmht
gtavgklegdpltvqgyynvcrdaytqtdltrglffdqdwaslrkvmpvasggihagqmh
qlihlfgddvvlqfgggtighpqgiqagatanrvaleamvlarnegrdilnegpeilrda
arwcgplraaldtwgdi
>d1bxng2 4.47.9.1.4 (22-150) Ribulose 1,5-bisphosphate carboxylase-oxygenase {(Alcaligenes eutrophus)}
ykemgywdgdyvpkdtdllalfritpqdgvdpveaaaavagesstatwtvvwtdrltacd
myrakayrvdpvpnnpeqffcyvaydlslfeegsianltasiignvfsfkpikaarledm
rfpvayvkt
>d1bxni_ 4.55.1.1.4 Ribulose 1,5-bisphosphate carboxylase-oxygenase {(Alcaligenes eutrophus)}
mritqgtfsflpeltdeqitkqleyclnqgwavgleytddphprntywemfglpmfdlrd
aagilmeinnarntfpnhyirvtafdsthtvesvvmsfivnrpadepgfrlvrqeepgrt
lrysiesya
>d1bxnj_ 4.55.1.1.4 Ribulose 1,5-bisphosphate carboxylase-oxygenase {(Alcaligenes eutrophus)}
mritqgtfsflpeltdeqitkqleyclnqgwavgleytddphprntywemfglpmfdlrd
aagilmeinnarntfpnhyirvtafdsthtvesvvmsfivnrpadepgfrlvrqeepgrt
lrysiesya
>d1bxnk_ 4.55.1.1.4 Ribulose 1,5-bisphosphate carboxylase-oxygenase {(Alcaligenes eutrophus)}
mritqgtfsflpeltdeqitkqleyclnqgwavgleytddphprntywemfglpmfdlrd
aagilmeinnarntfpnhyirvtafdsthtvesvvmsfivnrpadepgfrlvrqeepgrt
lrysiesya
>d1bxnl_ 4.55.1.1.4 Ribulose 1,5-bisphosphate carboxylase-oxygenase {(Alcaligenes eutrophus)}
mritqgtfsflpeltdeqitkqleyclnqgwavgleytddphprntywemfglpmfdlrd
aagilmeinnarntfpnhyirvtafdsthtvesvvmsfivnrpadepgfrlvrqeepgrt
lrysiesya
>d1bxo__ 2.44.1.2.2 Acid protease {Fungus (Penicillium janthinellum), penicillopepsin}
aasgvatntptandeeyitpvtiggttlnlnfdtgsadlwvfstelpasqqsghsvynps
atgkelsgytwsisygdgssasgnvftdsvtvggvtahgqavqaaqqisaqfqqdtnndg
llglafssintvqpqsqttffdtvksslaqplfavalkhqqpgvydfgfidsskytgslt
ytgvdnsqgfwsfnvdsytagsqsgdgfsgiadtgttllllddsvvsqyysqvsgaqqds
naggyvfdcstnlpdfsvsisgytatvpgslinygpsgdgstclggiqsnsgigfsifgd
iflksqyvvfdsdgpqlgfapqa
>d1bxpa_ 7.7.1.1.10 Bungarotoxin {Alpha-bungarotoxin (Bungarus multicinctus)}
ivchttatspisavtcppgenlcyrkmwcdafcssrgkvvelgcaatcpskkpyeevtcc
stdkcnphpkqrpg
>d1bxq__ 2.44.1.2.2 Acid protease {Fungus (Penicillium janthinellum), penicillopepsin}
aasgvatntptandeeyitpvtiggttlnlnfdtgsadlwvfstelpasqqsghsvynps
atgkelsgytwsisygdgssasgnvftdsvtvggvtahgqavqaaqqisaqfqqdtnndg
llglafssintvqpqsqttffdtvksslaqplfavalkhqqpgvydfgfidsskytgslt
ytgvdnsqgfwsfnvdsytagsqsgdgfsgiadtgttllllddsvvsqyysqvsgaqqds
naggyvfdcstnlpdfsvsisgytatvpgslinygpsgdgstclggiqsnsgigfsifgd
iflksqyvvfdsdgpqlgfapqa
>d1bxra1 1.89.1.1.1 (403-555) Carbamoyl phosphate synthetase, large subunit connection domain {Escherichia coli}
evgatgfdpkvslddpealtkirrelkdagadriwyiadafraglsvdgvfnltnidrwf
lvqieelvrleekvaevgitglnadflrqlkrkgfadarlaklagvreaeirklrdqydl
hpvykrvdtcaaefatdtaymystyeeeceanp
>d1bxra2 3.17.1.1.1 (936-1073) Carbamoyl phosphate synthetase, large subunit allosteric, C-terminal domain {Escherichia coli}
nstmkkhgrallsvregdkervvdlaakllkqgfeldathgtaivlgeaginprlvnkvh
egrphiqdrikngeytyiinttsgrraiedsrvirrsalqykvhydttlnggfatamaln
adatekvisvqemhaqik
>d1bxra3 3.24.1.1.3 (1-127) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
mpkrtdiksililgagpivigqacefdysgaqackalreegyrvilvnsnpatimtdpem
adatyiepihwevvrkiiekerpdavlptmggqtalncalelerqgvleefgvtmigata
daidkae
>d1bxra4 3.24.1.1.3 (556-676) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
stdrekimvlgggpnrigqgiefdyccvhaslalredgyetimvncnpetvstdydtsdr
lyfepvtledvleivriekpkgvivqyggqtplklaraleaagvpvigtspdaidraedr
e
>d1bxra5 4.115.1.2.3 (128-402) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
drrrfdvamkkigletarsgiahtmeealavaadvgfpciirpsftmggsgggiaynree
feeicargldlsptkellidesligwkeyemevvrdkndnciivcsienfdamgihtgds
itvapaqtltdkeyqimrnasmavlreigvetggsnvqfavnpkngrliviemnprvsrs
salaskatgfpiakvaaklavgytldelmnditggrtpasfepsidyvvtkiprfnfekf
agandrlttqmksvgevmaigrtqqeslqkalrgl
>d1bxra6 4.115.1.2.3 (677-935) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
rfqhaverlklkqpanatvtaiemavekakeigyplvvrpsyvlggrameivydeadlrr
yfqtavsvsndapvlldhflddavevdvdaicdgemvliggimehieqagvhsgdsacsl
paytlsqeiqdvmrqqvqklafelqvrglmnvqfavknnevylievnpraartvpfvska
tgvplakvaarvmagkslaeqgvtkevippyysvkevvlpfnkfpgvdpllgpemrstge
vmgvgrtfaeafakaqlgs
>d1bxrb1 3.7.3.1.1 (2-152) Carbamoyl phosphate synthetase, small subunit N-terminal domain {Escherichia coli}
iksallvledgtqfhgraigatgsavgevvfntsmtgyqeiltdpsysrqivtltyphig
nvgtndadeessqvhaqglvirdlpliasnfrntedlssylkrhnivaiadidtrkltrl
lrekgaqngciiagdnpdaalalekarafpg
>d1bxrb2 3.58.1.1.2 (153-380) Carbamoyl phosphate synthetase, small subunit C-terminal domain {Escherichia coli}
lngmdlakevttaeayswtqgswtltgglpqakkedelpfhvvaydfgakrnilrmlvdr
gcrltivpaqtsaedvlkmnpdgiflsngpgdpapcdyaitaiqkfletdipvfgiclgh
qllalasgaktvkmkfghhggnhpvkdveknvvmitaqnhgfavdeatlpanlrvthksl
fdgtlqgihrtdkpafsfqghpeaspgphdaaplfdhfielieqyrkt
>d1bxrc1 1.89.1.1.1 (403-555) Carbamoyl phosphate synthetase, large subunit connection domain {Escherichia coli}
evgatgfdpkvslddpealtkirrelkdagadriwyiadafraglsvdgvfnltnidrwf
lvqieelvrleekvaevgitglnadflrqlkrkgfadarlaklagvreaeirklrdqydl
hpvykrvdtcaaefatdtaymystyeeeceanp
>d1bxrc2 3.17.1.1.1 (936-1073) Carbamoyl phosphate synthetase, large subunit allosteric, C-terminal domain {Escherichia coli}
nstmkkhgrallsvregdkervvdlaakllkqgfeldathgtaivlgeaginprlvnkvh
egrphiqdrikngeytyiinttsgrraiedsrvirrsalqykvhydttlnggfatamaln
adatekvisvqemhaqik
>d1bxrc3 3.24.1.1.3 (1-127) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
mpkrtdiksililgagpivigqacefdysgaqackalreegyrvilvnsnpatimtdpem
adatyiepihwevvrkiiekerpdavlptmggqtalncalelerqgvleefgvtmigata
daidkae
>d1bxrc4 3.24.1.1.3 (556-676) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
stdrekimvlgggpnrigqgiefdyccvhaslalredgyetimvncnpetvstdydtsdr
lyfepvtledvleivriekpkgvivqyggqtplklaraleaagvpvigtspdaidraedr
e
>d1bxrc5 4.115.1.2.3 (128-402) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
drrrfdvamkkigletarsgiahtmeealavaadvgfpciirpsftmggsgggiaynree
feeicargldlsptkellidesligwkeyemevvrdkndnciivcsienfdamgihtgds
itvapaqtltdkeyqimrnasmavlreigvetggsnvqfavnpkngrliviemnprvsrs
salaskatgfpiakvaaklavgytldelmnditggrtpasfepsidyvvtkiprfnfekf
agandrlttqmksvgevmaigrtqqeslqkalrgl
>d1bxrc6 4.115.1.2.3 (677-935) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
rfqhaverlklkqpanatvtaiemavekakeigyplvvrpsyvlggrameivydeadlrr
yfqtavsvsndapvlldhflddavevdvdaicdgemvliggimehieqagvhsgdsacsl
paytlsqeiqdvmrqqvqklafelqvrglmnvqfavknnevylievnpraartvpfvska
tgvplakvaarvmagkslaeqgvtkevippyysvkevvlpfnkfpgvdpllgpemrstge
vmgvgrtfaeafakaqlgs
>d1bxrd1 3.7.3.1.1 (2-152) Carbamoyl phosphate synthetase, small subunit N-terminal domain {Escherichia coli}
iksallvledgtqfhgraigatgsavgevvfntsmtgyqeiltdpsysrqivtltyphig
nvgtndadeessqvhaqglvirdlpliasnfrntedlssylkrhnivaiadidtrkltrl
lrekgaqngciiagdnpdaalalekarafpg
>d1bxrd2 3.58.1.1.2 (153-380) Carbamoyl phosphate synthetase, small subunit C-terminal domain {Escherichia coli}
lngmdlakevttaeayswtqgswtltgglpqakkedelpfhvvaydfgakrnilrmlvdr
gcrltivpaqtsaedvlkmnpdgiflsngpgdpapcdyaitaiqkfletdipvfgiclgh
qllalasgaktvkmkfghhggnhpvkdveknvvmitaqnhgfavdeatlpanlrvthksl
fdgtlqgihrtdkpafsfqghpeaspgphdaaplfdhfielieqyrkt
>d1bxre1 1.89.1.1.1 (403-555) Carbamoyl phosphate synthetase, large subunit connection domain {Escherichia coli}
evgatgfdpkvslddpealtkirrelkdagadriwyiadafraglsvdgvfnltnidrwf
lvqieelvrleekvaevgitglnadflrqlkrkgfadarlaklagvreaeirklrdqydl
hpvykrvdtcaaefatdtaymystyeeeceanp
>d1bxre2 3.17.1.1.1 (936-1073) Carbamoyl phosphate synthetase, large subunit allosteric, C-terminal domain {Escherichia coli}
nstmkkhgrallsvregdkervvdlaakllkqgfeldathgtaivlgeaginprlvnkvh
egrphiqdrikngeytyiinttsgrraiedsrvirrsalqykvhydttlnggfatamaln
adatekvisvqemhaqik
>d1bxre3 3.24.1.1.3 (1-127) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
mpkrtdiksililgagpivigqacefdysgaqackalreegyrvilvnsnpatimtdpem
adatyiepihwevvrkiiekerpdavlptmggqtalncalelerqgvleefgvtmigata
daidkae
>d1bxre4 3.24.1.1.3 (556-676) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
stdrekimvlgggpnrigqgiefdyccvhaslalredgyetimvncnpetvstdydtsdr
lyfepvtledvleivriekpkgvivqyggqtplklaraleaagvpvigtspdaidraedr
e
>d1bxre5 4.115.1.2.3 (128-402) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
drrrfdvamkkigletarsgiahtmeealavaadvgfpciirpsftmggsgggiaynree
feeicargldlsptkellidesligwkeyemevvrdkndnciivcsienfdamgihtgds
itvapaqtltdkeyqimrnasmavlreigvetggsnvqfavnpkngrliviemnprvsrs
salaskatgfpiakvaaklavgytldelmnditggrtpasfepsidyvvtkiprfnfekf
agandrlttqmksvgevmaigrtqqeslqkalrgl
>d1bxre6 4.115.1.2.3 (677-935) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
rfqhaverlklkqpanatvtaiemavekakeigyplvvrpsyvlggrameivydeadlrr
yfqtavsvsndapvlldhflddavevdvdaicdgemvliggimehieqagvhsgdsacsl
paytlsqeiqdvmrqqvqklafelqvrglmnvqfavknnevylievnpraartvpfvska
tgvplakvaarvmagkslaeqgvtkevippyysvkevvlpfnkfpgvdpllgpemrstge
vmgvgrtfaeafakaqlgs
>d1bxrf1 3.7.3.1.1 (2-152) Carbamoyl phosphate synthetase, small subunit N-terminal domain {Escherichia coli}
iksallvledgtqfhgraigatgsavgevvfntsmtgyqeiltdpsysrqivtltyphig
nvgtndadeessqvhaqglvirdlpliasnfrntedlssylkrhnivaiadidtrkltrl
lrekgaqngciiagdnpdaalalekarafpg
>d1bxrf2 3.58.1.1.2 (153-380) Carbamoyl phosphate synthetase, small subunit C-terminal domain {Escherichia coli}
lngmdlakevttaeayswtqgswtltgglpqakkedelpfhvvaydfgakrnilrmlvdr
gcrltivpaqtsaedvlkmnpdgiflsngpgdpapcdyaitaiqkfletdipvfgiclgh
qllalasgaktvkmkfghhggnhpvkdveknvvmitaqnhgfavdeatlpanlrvthksl
fdgtlqgihrtdkpafsfqghpeaspgphdaaplfdhfielieqyrkt
>d1bxrg1 1.89.1.1.1 (403-555) Carbamoyl phosphate synthetase, large subunit connection domain {Escherichia coli}
evgatgfdpkvslddpealtkirrelkdagadriwyiadafraglsvdgvfnltnidrwf
lvqieelvrleekvaevgitglnadflrqlkrkgfadarlaklagvreaeirklrdqydl
hpvykrvdtcaaefatdtaymystyeeeceanp
>d1bxrg2 3.17.1.1.1 (936-1073) Carbamoyl phosphate synthetase, large subunit allosteric, C-terminal domain {Escherichia coli}
nstmkkhgrallsvregdkervvdlaakllkqgfeldathgtaivlgeaginprlvnkvh
egrphiqdrikngeytyiinttsgrraiedsrvirrsalqykvhydttlnggfatamaln
adatekvisvqemhaqik
>d1bxrg3 3.24.1.1.3 (1-127) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
mpkrtdiksililgagpivigqacefdysgaqackalreegyrvilvnsnpatimtdpem
adatyiepihwevvrkiiekerpdavlptmggqtalncalelerqgvleefgvtmigata
daidkae
>d1bxrg4 3.24.1.1.3 (556-676) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
stdrekimvlgggpnrigqgiefdyccvhaslalredgyetimvncnpetvstdydtsdr
lyfepvtledvleivriekpkgvivqyggqtplklaraleaagvpvigtspdaidraedr
e
>d1bxrg5 4.115.1.2.3 (128-402) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
drrrfdvamkkigletarsgiahtmeealavaadvgfpciirpsftmggsgggiaynree
feeicargldlsptkellidesligwkeyemevvrdkndnciivcsienfdamgihtgds
itvapaqtltdkeyqimrnasmavlreigvetggsnvqfavnpkngrliviemnprvsrs
salaskatgfpiakvaaklavgytldelmnditggrtpasfepsidyvvtkiprfnfekf
agandrlttqmksvgevmaigrtqqeslqkalrgl
>d1bxrg6 4.115.1.2.3 (677-935) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
rfqhaverlklkqpanatvtaiemavekakeigyplvvrpsyvlggrameivydeadlrr
yfqtavsvsndapvlldhflddavevdvdaicdgemvliggimehieqagvhsgdsacsl
paytlsqeiqdvmrqqvqklafelqvrglmnvqfavknnevylievnpraartvpfvska
tgvplakvaarvmagkslaeqgvtkevippyysvkevvlpfnkfpgvdpllgpemrstge
vmgvgrtfaeafakaqlgs
>d1bxrh1 3.7.3.1.1 (2-152) Carbamoyl phosphate synthetase, small subunit N-terminal domain {Escherichia coli}
iksallvledgtqfhgraigatgsavgevvfntsmtgyqeiltdpsysrqivtltyphig
nvgtndadeessqvhaqglvirdlpliasnfrntedlssylkrhnivaiadidtrkltrl
lrekgaqngciiagdnpdaalalekarafpg
>d1bxrh2 3.58.1.1.2 (153-380) Carbamoyl phosphate synthetase, small subunit C-terminal domain {Escherichia coli}
lngmdlakevttaeayswtqgswtltgglpqakkedelpfhvvaydfgakrnilrmlvdr
gcrltivpaqtsaedvlkmnpdgiflsngpgdpapcdyaitaiqkfletdipvfgiclgh
qllalasgaktvkmkfghhggnhpvkdveknvvmitaqnhgfavdeatlpanlrvthksl
fdgtlqgihrtdkpafsfqghpeaspgphdaaplfdhfielieqyrkt
>d1bxsa_ 3.71.1.1.5 Aldehyde reductase (dehydrogenase), ALDH {Sheep (Ovis aries)}
dvpapltnlqfkytkifinnewhssvsgkkfpvfnpateeklceveegdkedvdkavkaa
rqafqigspwrtmdasergrllnkladlierdrlllatmeamnggklfsnaylmdlggci
ktlrycagwadkiqgrtipmdgnfftytrsepvgvcgqiipwnfpllmflwkigpalscg
ntvvvkpaeqtpltalhmgslikeagfppgvvnivpgygptagaaisshmdvdkvaftgs
tevgklikeaagksnlkrvslelggkspcivfadadldnavefahqgvfyhqgqcciaas
rlfveesiydefvrrsverakkyvlgnpltpgvsqgpqidkeqyekildliesgkkegak
lecgggpwgnkgyfiqptvfsdvtddmriakeeifgpvqqimkfkslddvikranntfyg
lsagiftndidkaitvssalqsgtvwvncysvvsaqcpfggfkmsgngrelgeygfheyt
evktvtikisqkns
>d1bxsb_ 3.71.1.1.5 Aldehyde reductase (dehydrogenase), ALDH {Sheep (Ovis aries)}
dvpapltnlqfkytkifinnewhssvsgkkfpvfnpateeklceveegdkedvdkavkaa
rqafqigspwrtmdasergrllnkladlierdrlllatmeamnggklfsnaylmdlggci
ktlrycagwadkiqgrtipmdgnfftytrsepvgvcgqiipwnfpllmflwkigpalscg
ntvvvkpaeqtpltalhmgslikeagfppgvvnivpgygptagaaisshmdvdkvaftgs
tevgklikeaagksnlkrvslelggkspcivfadadldnavefahqgvfyhqgqcciaas
rlfveesiydefvrrsverakkyvlgnpltpgvsqgpqidkeqyekildliesgkkegak
lecgggpwgnkgyfiqptvfsdvtddmriakeeifgpvqqimkfkslddvikranntfyg
lsagiftndidkaitvssalqsgtvwvncysvvsaqcpfggfkmsgngrelgeygfheyt
evktvtikisqkns
>d1bxsc_ 3.71.1.1.5 Aldehyde reductase (dehydrogenase), ALDH {Sheep (Ovis aries)}
dvpapltnlqfkytkifinnewhssvsgkkfpvfnpateeklceveegdkedvdkavkaa
rqafqigspwrtmdasergrllnkladlierdrlllatmeamnggklfsnaylmdlggci
ktlrycagwadkiqgrtipmdgnfftytrsepvgvcgqiipwnfpllmflwkigpalscg
ntvvvkpaeqtpltalhmgslikeagfppgvvnivpgygptagaaisshmdvdkvaftgs
tevgklikeaagksnlkrvslelggkspcivfadadldnavefahqgvfyhqgqcciaas
rlfveesiydefvrrsverakkyvlgnpltpgvsqgpqidkeqyekildliesgkkegak
lecgggpwgnkgyfiqptvfsdvtddmriakeeifgpvqqimkfkslddvikranntfyg
lsagiftndidkaitvssalqsgtvwvncysvvsaqcpfggfkmsgngrelgeygfheyt
evktvtikisqkns
>d1bxsd_ 3.71.1.1.5 Aldehyde reductase (dehydrogenase), ALDH {Sheep (Ovis aries)}
dvpapltnlqfkytkifinnewhssvsgkkfpvfnpateeklceveegdkedvdkavkaa
rqafqigspwrtmdasergrllnkladlierdrlllatmeamnggklfsnaylmdlggci
ktlrycagwadkiqgrtipmdgnfftytrsepvgvcgqiipwnfpllmflwkigpalscg
ntvvvkpaeqtpltalhmgslikeagfppgvvnivpgygptagaaisshmdvdkvaftgs
tevgklikeaagksnlkrvslelggkspcivfadadldnavefahqgvfyhqgqcciaas
rlfveesiydefvrrsverakkyvlgnpltpgvsqgpqidkeqyekildliesgkkegak
lecgggpwgnkgyfiqptvfsdvtddmriakeeifgpvqqimkfkslddvikranntfyg
lsagiftndidkaitvssalqsgtvwvncysvvsaqcpfggfkmsgngrelgeygfheyt
evktvtikisqkns
>d1bxtb1 2.35.2.2.7 (1-119) Streptococcal superantigen SSA {Streptococcus pyogenes}
ssqpdptpeqlnkssqftgvmgnlrclydnhfvegtnvrstgqllqhdlifpikdlklkn
ydsvktefnskdlatkyknkdvdifgsnyyyncyysegnscknakktcmyggvtehhrn
>d1bxtb2 4.13.7.1.7 (120-234) Streptococcal superantigen SSA {Streptococcus pyogenes}
qiegkfpnitvkvyednenilsfdittnkkqvtvqeldcktrkilvsrknlyefnnspye
tgyikfiessgdsfwydmmpapgaifdqskylmlyndnktvsssaiaievhltkk
>d1bxua_ 2.5.1.1.14 Plastocyanin {Cyanobacterium (Synechocystis), pcc 7942}
qtvaikmgadngmlafepstieiqagdtvqwvnnklaphnvvvegqpelshkdlafspge
tfeatfsepgtytyycephrgagmvgkivvq
>d1bxva_ 2.5.1.1.14 Plastocyanin {Cyanobacterium (Synechocystis), pcc 7942}
qtvaikmgadngmlafepstieiqagdtvqwvnnklaphnvvvegqpelshkdlafspge
tfeatfsepgtytyycephrgagmvgkivvq
>d1bxwa_ 6.4.1.1.1 Outer membrane protein A (OMPA) transmembrane domain {Escherichia coli}
mapkdntwytgaklgwsqyhdtglinnngpthenklgagafggyqvnpyvgfemgydwlg
rmpykgsvengaykaqgvqltaklgypitddldiytrlggmvwradtysnvygknhdtgv
spvfaggveyaitpeiatrleyqwtnnigdahtigtrpdngmlslgvsyrfg
>d1bxx__ 2.2.7.1.1 Second domain of Mu2 adaptin subunit (ap50) of ap2 adaptor {Rat (Rattus norvegicus)}
igwrregikyrrnelfldvlesvnllmspqgqvlsahvsgrvvmksylsgmpeckfgmnd
kiviekqgkgtadetsksgkqsiaiddctfhqcvrlskfdsersisfippdgefelmryr
ttkdiilpfrviplvrevgrtklevkvviksnfkpsllaqkievriptplntsgvqvicm
kgkakykasenaivwkikrmagmkesqisaeiellptndkkkwarppismnfevpfapsg
lkvrylkvfepklnysdhdvikwvryigrsgiyetrc
>d1bxya_ 4.47.15.1.1 Ribosomal protein L30 {Thermus thermophilus}
mprlkvklvkspigypkdqkaalkalglrrlqqervledtpairgnvekvahlvrvevve
>d1bxyb_ 4.47.15.1.1 Ribosomal protein L30 {Thermus thermophilus}
mprlkvklvkspigypkdqkaalkalglrrlqqervledtpairgnvekvahlvrvevve
>d1by1a_ 1.84.1.1.2 beta-pix {Human (Homo sapiens) |A|}
mkgfdttainksyynvvlqnileteneyskelqtvlstylrplqtseklssanisylmgn
leeicsfqqmlvqsleectklpeaqqrvggcflnlmpqmktlyltycanhpsavnvlteh
seelgefmetkgasspgilvlttglskpfmrldkyptllkelerhmedyhtdrqdiqksm
aafknlsaqcqevrkrkelelqilteair
>d1by2__ 4.140.1.1.1 M2BP {Human (Homo sapiens)}
avndgdmrladggatnqgrveifyrgqwgtvcdnlwdltdasvvcralgfenatqalgra
afgqgsgpimldevqctgteasladckslgwlksncrherdagvvctnetrsthtl
>d1by3a_ 6.4.3.3.1 Ferric hydroxamate uptake receptor FhuA {Escherichia coli}
sawgpaatiaarqsatgtktdtpiqkvpqsisvvtaeemalhqpksvkealsytpgvsvg
trgasntydhliirgfaaegqsqnnylnglklqgnfyndavidpymleraeimrgpvsvl
ygksspggllnmvskrptteplkevqfkagtdslfqtgfdfsdsldddgvysyrltglar
sanaqqkgseeqryaiapaftwrpddktnftflsyfqnepetgyygwlpkegtveplpng
krlptdfnegaknntysrnekmvgysfdhefndtftvrqnlrfaenktsqnsvygygvcs
dpanayskqcaalapadkghylarkyvvddeklqnfsvdtqlqskfatgdidhtlltgvd
fmrmrndinawfgyddsvpllnlynpvntdfdfnakdpansgpyrilnkqkqtgvyvqdq
aqwdkvlvtlggrydwadqeslnrvagttdkrddkqftwrggvnylfdngvtpyfsyses
fepssqvgkdgnifapskgkqyevgvkyvpedrpivvtgavynltktnnlmadpegsffs
veggeirargveieakrplsasvnvvgsytytdaeyttdttykgntpaqvpkhmaslwad
ytffdgplsgltlgtggrytgssygdpansfkvgsytvvdalvrydlarvgmagsnvalh
vnnlfdreyvascfntygcfwgaerqvvatatfrf
>d1by5a_ 6.4.3.3.1 Ferric hydroxamate uptake receptor FhuA {Escherichia coli}
qesawgpaatiaarqsatgtktdtpiqkvpqsisvvtaeemalhqpksvkealsytpgvs
vgtrgasntydhliirgfaaegqsqnnylnglklqgnfyndavidpymleraeimrgpvs
vlygksspggllnmvskrptteplkevqfkagtdslfqtgfdfsdsldddgvysyrltgl
arsanaqqkgseeqryaiapaftwrpddktnftflsyfqnepetgyygwlpkegtveplp
ngkrlptdfnegaknntysrnekmvgysfdhefndtftvrqnlrfaenktsqnsvygygv
csdpanayskqcaalapadkghylarkyvvddeklqnfsvdtqlqskfatgdidhtlltg
vdfmrmrndinawfgyddsvpllnlynpvntdfdfnakdpansgpyrilnkqkqtgvyvq
dqaqwdkvlvtlggrydwadqeslnrvagttdkrddkqftwrggvnylfdngvtpyfsys
esfepssqvgkdgnifapskgkqyevgvkyvpedrpivvtgavynltktnnlmadpegsf
fsveggeirargveieakrplsasvnvvgsytytdaeyttdttykgntpaqvpkhmaslw
adytffdgplsgltlgtggrytgssygdpansfkvgsytvvdalvrydlarvgmagsnva
lhvnnlfdreyvascfntygcfwgaerqvvatatfrf
>d1by7a_ 5.1.1.1.8 Plasminogen activator inhibitor-2 {Human (Homo sapiens)}
edlcvantlfalnlfkhlakasptqnlflspwsisstmamvymgsrgstedqmakvlqfn
evgaaadkihssfrslssainastgnyllesvnklfgeksasfreeyirlcqkyyssepq
avdflecaeearkkinswvktqtkgkipnllpegsvdgdtrmvlvnavyfkgkwktpfek
klnglypfrvnsaqrtpvqmmylreklnigyiedlkaqilelpyagdvsmflllpdeiad
vstglelleseitydklnkwtskdkmaedevevyipqfkleehyelrsilrsmgmedafn
kgranfsgmserndlflsevfhqamvdvneegteaaagtggvmtgrtghggpqfvadhpf
lflimhkitncilffgrfssp
>d1by8a_ 4.3.1.1.13 (Pro)cathepsin K {Human (Homo sapiens)}
eildthwelwkkthrkqynnkvdeisrrliweknlkyisihnleaslgvhtyelamnhlg
dmtseevvqkmtglkvplshsrsndtlyipewegrapdsvdyrkkgyvtpvknqgqcgsc
wafssvgalegqlkkktgkllnlspqnlvdcvsendgcgggymtnafqyvqknrgidsed
aypyvgqeescmynptgkaakcrgyreipegnekalkravarvgpvsvaidasltsfqfy
skgvyydescnsdnlnhavlavgygiqkgnkhwiiknswgenwgnkgyilmarnknnacg
ianlasfpkm
>d1by9__ 4.47.8.1.3 Papillomavirus-1 E2 protein {Human papillomavirus, type 16}
ttpivhlkgdantlkclryrfkkhctlytavsstwhwtghnvkhksaivtltydsewqrd
qflsqvkipktitvstgfms
>d1bya__ 3.1.7.2.1 beta-Amylase {Soybean (Glycine max)}
snmllnyvpvyvmlplgvvnvdnvfedpdglkeqllqlraagvdgvmvdvwwgiielkgp
kqydwrayrslfqlvqecgltlqaimsfhqcggnvgdivnipipqwvldigesnhdifyt
nrsgtrnkeyltvgvdnepifhgrtaieiysdymksfrenmsdflesgliidievglgpa
gelrypsypqsqgwefprigefqcydkylkadfkaavaraghpewelpddagkyndvpes
tgffksngtyvtekgkffltwysnkllnhgdqildeankaflgckvklaikvsgihwwyk
venhaaeltagyynlndrdgyrpiarmlsrhhailnftclemrdseqpsdaksgpqelvq
qvlsggwredirvagenalprydataynqiilnakpqgvnnngppklsmfgvtylrlsdd
llqksnfnifkkfvlkmhadqdycanpqkynhaitplkpsapkipievlleatkptlpfp
wlpetdmkvdg
>d1byb__ 3.1.7.2.1 beta-Amylase {Soybean (Glycine max)}
snmllnyvpvyvmlplgvvnvdnvfedpdglkeqllqlraagvdgvmvdvwwgiielkgp
kqydwrayrslfqlvqecgltlqaimsfhqcggnvgdivnipipqwvldigesnhdifyt
nrsgtrnkeyltvgvdnepifhgrtaieiysdymksfrenmsdflesgliidievglgpa
gelrypsypqsqgwefprigefqcydkylkadfkaavaraghpewelpddagkyndvpes
tgffksngtyvtekgkffltwysnkllnhgdqildeankaflgckvklaikvsgihwwyk
venhaaeltagyynlndrdgyrpiarmlsrhhailnftclemrdseqpsdaksgpqelvq
qvlsggwredirvagenalprydataynqiilnakpqgvnnngppklsmfgvtylrlsdd
llqksnfnifkkfvlkmhadqdycanpqkynhaitplkpsapkipievlleatkptlpfp
wlpetdmkvdg
>d1byc__ 3.1.7.2.1 beta-Amylase {Soybean (Glycine max)}
snmllnyvpvyvmlplgvvnvdnvfedpdglkeqllqlraagvdgvmvdvwwgiielkgp
kqydwrayrslfqlvqecgltlqaimsfhqcggnvgdivnipipqwvldigesnhdifyt
nrsgtrnkeyltvgvdnepifhgrtaieiysdymksfrenmsdflesgliidievglgpa
gelrypsypqsqgwefprigefqcydkylkadfkaavaraghpewelpddagkyndvpes
tgffksngtyvtekgkffltwysnkllnhgdqildeankaflgckvklaikvsgihwwyk
venhaaeltagyynlndrdgyrpiarmlsrhhailnftclemrdseqpsdaksgpqelvq
qvlsggwredirvagenalprydataynqiilnakpqgvnnngppklsmfgvtylrlsdd
llqksnfnifkkfvlkmhadqdycanpqkynhaitplkpsapkipievlleatkptlpfp
wlpetdmkvdg
>d1byd__ 3.1.7.2.1 beta-Amylase {Soybean (Glycine max)}
snmllnyvpvyvmlplgvvnvdnvfedpdglkeqllqlraagvdgvmvdvwwgiielkgp
kqydwrayrslfqlvqecgltlqaimsfhqcggnvgdivnipipqwvldigesnhdifyt
nrsgtrnkeyltvgvdnepifhgrtaieiysdymksfrenmsdflesgliidievglgpa
gelrypsypqsqgwefprigefqcydkylkadfkaavaraghpewelpddagkyndvpes
tgffksngtyvtekgkffltwysnkllnhgdqildeankaflgckvklaikvsgihwwyk
venhaaeltagyynlndrdgyrpiarmlsrhhailnftclemrdseqpsdaksgpqelvq
qvlsggwredirvagenalprydataynqiilnakpqgvnnngppklsmfgvtylrlsdd
llqksnfnifkkfvlkmhadqdycanpqkynhaitplkpsapkipievlleatkptlpfp
wlpetdmkvdg
>d1byea1 1.48.1.1.17 (81-213) Glutathione S-transferase {Maize (Zea mays), type I}
ellregnleeaamvdvwieveanqytaalnpilfqvlispmlggttdqkvvdenleklkk
vlevyearltkckylagdflsladlnhvsvtlclfatpyasvldayphvkawwsglmerp
svqkvaalmkpsa
>d1byea2 3.38.1.5.17 (1-80) Glutathione S-transferase {Maize (Zea mays), type I}
apmklygavmswnltrcataleeagsdyeivpinfataehkspehlvrnpfgqvpalqdg
dlylfesraickyaarknkp
>d1byeb1 1.48.1.1.17 (81-213) Glutathione S-transferase {Maize (Zea mays), type I}
ellregnleeaamvdvwieveanqytaalnpilfqvlispmlggttdqkvvdenleklkk
vlevyearltkckylagdflsladlnhvsvtlclfatpyasvldayphvkawwsglmerp
svqkvaalmkpsa
>d1byeb2 3.38.1.5.17 (1-80) Glutathione S-transferase {Maize (Zea mays), type I}
apmklygavmswnltrcataleeagsdyeivpinfataehkspehlvrnpfgqvpalqdg
dlylfesraickyaarknkp
>d1byec1 1.48.1.1.17 (81-213) Glutathione S-transferase {Maize (Zea mays), type I}
ellregnleeaamvdvwieveanqytaalnpilfqvlispmlggttdqkvvdenleklkk
vlevyearltkckylagdflsladlnhvsvtlclfatpyasvldayphvkawwsglmerp
svqkvaalmkpsa
>d1byec2 3.38.1.5.17 (1-80) Glutathione S-transferase {Maize (Zea mays), type I}
apmklygavmswnltrcataleeagsdyeivpinfataehkspehlvrnpfgqvpalqdg
dlylfesraickyaarknkp
>d1byed1 1.48.1.1.17 (81-213) Glutathione S-transferase {Maize (Zea mays), type I}
ellregnleeaamvdvwieveanqytaalnpilfqvlispmlggttdqkvvdenleklkk
vlevyearltkckylagdflsladlnhvsvtlclfatpyasvldayphvkawwsglmerp
svqkvaalmkpsa
>d1byed2 3.38.1.5.17 (1-80) Glutathione S-transferase {Maize (Zea mays), type I}
apmklygavmswnltrcataleeagsdyeivpinfataehkspehlvrnpfgqvpalqdg
dlylfesraickyaarknkp
>d1byfa_ 4.139.1.1.8 Lectin TC14 {Tunicate (Polyandrocarpa misakiensis)}
dyeilfsdetmnyadagtycqsrgmalvssamrdstmvkailaftevkghdywvgadnlq
dgaynflwndgvslptdsdlwspnepsnpqswqlcvqiwskynllddvgcggarrvicek
eld
>d1byfb_ 4.139.1.1.8 Lectin TC14 {Tunicate (Polyandrocarpa misakiensis)}
dyeilfsdetmnyadagtycqsrgmalvssamrdstmvkailaftevkghdywvgadnlq
dgaynflwndgvslptdsdlwspnepsnpqswqlcvqiwskynllddvgcggarrvicek
eld
>d1byga_ 4.117.1.2.7 C-terminal src kinase (csk) {Human (Homo sapiens)}
gwalnmkelkllqtigkgefgdvmlgdyrgnkvavkcikndataqaflaeasvmtqlrhs
nlvqllgviveekgglyivteymakgslvdylrsrgrsvlggdcllkfsldvceameyle
gnnfvhrdlaarnvlvsednvakvsdfgltkeasstqdtgklpvkwtapealrekkfstk
sdvwsfgillweiysfgrvpypriplkdvvprvekgykmdapdgcppavyevmkncwhld
aamrpsflqlreqlehikthel
>d1byh__ 2.26.1.2.2 Bacillus 1-3,1-4-beta-glucanase {Hybrid protein: residues 1-16 from Bacillus Amyloliquefaciens and Bacillus macerans}
qtggsffepfnsynsgtwekadgysnggvfnctwrannvnftndgklklgltssaynkfd
caeyrstniygyglyevsmkpakntgivssfftytgpahgtqwdeidieflgkdttkvqf
nyytngvgghekvislgfdaskgfhtyafdwqpgyikwyvdgvlkhtatanipstpgkim
mnlwngtgvddwlgsynganplyaeydwvkytsn
>d1byi__ 3.30.1.8.1 Dethiobiotin synthetase {Escherichia coli}
skryfvtgtdtevgktvascallqaakaagyrtagykpvasgsektpeglrnsdalalqr
nsslqldyatvnpytfaeptsphiisaqegrpieslvmsaglraleqqadwvlvegaggw
ftplsdtftfadwvtqeqlpvilvvgvklgcinhamltaqviqhagltlagwvandvtpp
gkrhaeymttltrmipapllgeipwlaenpenaatgkyinlall
>d1byka_ 3.83.1.1.9 Trehalose repressor, C-terminal domain {Escherichia coli}
sdkvvaiivtrldslsenlavqtmlpafyeqgydpimmesqfspqlvaehlgvlkrrnid
gvvlfgftgiteemlahwqsslvllardakgfasvcyddegaikilmqrlydqghrnisy
lgvphsdvttgkrrheaylafckahklhpvaalpglamkqgyenvakvitpettallcat
dtlalgaskylqeqridtlqlasvgntplmkflhpeivtvdpgyaeagrqaacqliaqvt
grsepqqiiipatls
>d1bykb_ 3.83.1.1.9 Trehalose repressor, C-terminal domain {Escherichia coli}
sdkvvaiivtrldslsenlavqtmlpafyeqgydpimmesqfspqlvaehlgvlkrrnid
gvvlfgftgiteemlahwqsslvllardakgfasvcyddegaikilmqrlydqghrnisy
lgvphsdvttgkrrheaylafckahklhpvaalpglamkqgyenvakvitpettallcat
dtlalgaskylqeqridtlqlasvgntplmkflhpeivtvdpgyaeagrqaacqliaqvt
grsepqqiiipatls
>d1byl__ 4.27.1.2.1 Bleomycin resistance protein, BRP {Streptoalloteichus hindustanus}
fmakltsavpvltardvagavefwtdrlgfsrdfveddfagvvrddvtlfisavqdqvvp
dntlawvwvrgldelyaewsevvstnfrdasgpamteigeqpwgrefalrdpagncvhfv
ae
>d1bym__ 2.30.1.3.1 Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
npipgldelgvgnsdaaapgtrvidaatsmprkvrivqineifqvetdqftqlldadirv
gseveivdrdghitlshngkdvellddlahtirieel
>d1byn__ 2.6.1.2.1 Synaptogamin I, first C2 domain {Rat (Rattus norvegicus)}
eklgklqysldydfqnnqllvgiiqaaelpaldmggtsdpyvkvfllpdkkkkfetkvhr
ktlnpvfneqftfkvpyselggktlvmavydfdrfskhdiigefkvpmntvdfghvteew
rdlqsaek
>d1byoa_ 2.5.1.1.6 Plastocyanin {White campion (Silene pratensis)}
aevllgssdgglafvpsdlsiasgekitfknnagfphndlfdedevpagvdvtkismpee
dllnapgeeysvtltekgtykfycaphagagmvgkvtvn
>d1byob_ 2.5.1.1.6 Plastocyanin {White campion (Silene pratensis)}
aevllgssdgglafvpsdlsiasgekitfknnagfphndlfdedevpagvdvtkismpee
dllnapgeeysvtltekgtykfycaphagagmvgkvtvn
>d1bypa_ 2.5.1.1.6 Plastocyanin {White campion (Silene pratensis)}
aevllgssdgglafvpsdlsiasgekitfknnagfphndlfdkkevpagvdvtkismpee
dllnapgeeysvtltekgtykfycaphagagmvgkvtvn
>d1byqa_ 4.96.1.1.2 HSP90 {Human (Homo sapiens)}
pmeeeevetfafqaeiaqlmsliintfysnkeiflrelisnssdaldkiryetltdpskl
dsgkelhinlipnkqdrtltivdtgigmtkadlinnlgtiaksgtkafmealqagadism
igqfgvgfysaylvaekvtvitkhnddeqyawessaggsftvrtdtgepmgrgtkvilhl
kedqteyleerrikeivkkhsqfigypitlfve
>d1byra_ 4.109.1.1.1 Nuclease Nuc {(Salmonella typhimurium) |A|}
epsvqvgyspegsarvlvlsaidsaktsirmmaysftapdimkalvaakkrgvdvkivid
ergntgrasiaamnyiansgiplrtdsnfpiqhdkviivdnvtvetgsfnftkaaetkns
enavviwnmpklaesflehwqdrwnqgrdyrs
>d1bysa_ 4.109.1.1.1 Nuclease Nuc {(Salmonella typhimurium) |A|}
epsvqvgyspegsarvlvlsaidsaktsirmmaysftapdimkalvaakkrgvdvkivid
ergntgrasiaamnyiansgiplrtdsnfpiqhdkviivdnvtvetgsfnftkaaetkns
enavviwnmpklaesflehwqdrwnqgrdyrs
>d1byt_1 1.111.1.1.2 (168-857) Lipoxigenase, C-terminal domain {Soybean (Glycine max), isozyme L3}
lpsetpaplvkyreeelhnlrgdgtgerkeweriydydvyndlgdpdkgenharpvlggn
dtfpyprrgrtgrkptrkdpnsesrsndvylprdeafghlkssdfltyglksvsqnvlpl
lqsafdlnftprefdsfdevhglysggiklptdiiskisplpvlkeifrtdgeqalkfpp
pkviqvsksawmtdeefaremlagvnpnlirclkdfpprskldsqvygdhtsqitkehle
pnlegltvdeaiqnkrlflldhhdpimpylrrinatstkayatrtilflkndgtlrplai
elslphpqgdqsgafsqvflpadegvessiwllakayvvvndscyhqlvshwlnthavve
pfiiatnrhlsvvhpiykllhphyrdtmninglarlslvndggvieqtflwgrysvemsa
vvykdwvftdqalpadlikrgmaiedpscphgirlviedypytvdgleiwdaiktwvhey
vflyyksddtlredpelqacwkelvevghgdkknepwwpkmqtreelveacaiiiwtasa
lhaavnfgqypygglilnrptlsrrfmpekgsaeyeelrknpqkaylktitpkfqtlidl
svieilsrhasdevylgerdnpnwtsdtraleafkrfgnklaqienklsernndeklrnr
cgpvqmpytlllpsskegltfrgipnsisi
>d1byt_2 2.11.1.1.2 (9-167) Plant lipoxigenase {Soybean (Glycine max), isozyme L3}
ghkikgtvvlmrknvldvnsvtsvggiigqgldlvgstldtltaflgrsvslqlisatka
dangkgklgkatflegiitslptlgagqsafkinfewddgsgipgafyiknfmqtefflv
sltledipnhgsihfvcnswiynaklfksdriffanqty
>d1byua_ 3.30.1.6.6 Ran {Dog (Canis familiaris)}
epqvqfklvlvgdggtgkttfvkrhltgefekkyvatlgvevhplvfhtnrgpikfnvwd
tagqekfgglrdgyyiqaqcaiimfdvtsrvtyknvpnwhrdlvrvcenipivlcgnkvd
ikdrkvkaksivfhrkknlqyydisaksnynfekpflwlarkligdpnlefvampalapp
evvmdpalaaqyehdlevaqtt
>d1byub_ 3.30.1.6.6 Ran {Dog (Canis familiaris)}
aaqgepqvqfklvlvgdggtgkttfvkrhltgefekkyvatlgvevhplvfhtnrgpikf
nvwdtagqekfgglrdgyyiqaqcaiimfdvtsrvtyknvpnwhrdlvrvcenipivlcg
nkvdikdrkvkaksivfhrkknlqyydisaksnynfekpflwlarkligdpnlefvampa
lappevvmdpalaaqyehdlevaqttalpdedddl
>d1byw__ 4.86.2.3.1 Erg potassium channel, N-terminal domain {Human (Homo sapiens)}
srkfiianarvencaviycndgfcelcgysraevmqrpctcdflhgpctqrraaaqiaqa
llgaeerkveiafyrkdgscflclvdvvpvknedgavimfilnfevvmek
>d1bz0a_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1bz0b_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1bz0c_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1bz0d_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1bz1a_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
mvlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghg
kkvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftp
avhasldkflasvstvltskyr
>d1bz1b_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1bz1c_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
mvlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghg
kkvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftp
avhasldkflasvstvltskyr
>d1bz1d_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1bz4a_ 1.25.1.1.1 Apolipoprotein E3 {Human (Homo sapiens)}
sgqrwelalgrfwdylrwvqtlseqvqeellssqvtqelrrralmdetmkelkayksele
eqltpvaeetrarlskkkelqaaqarrrlgadmedvcgrlvqyrgevqamlgqsteelrv
rlashlrrrkkklrkrllrrrdaddlqqqkrlavyqag
>d1bz5a_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bz5b_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bz5c_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bz5d_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bz5e_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bz6a_ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgyqg
>d1bz8a_ 2.3.3.1.1 Transthyretin (synonym: prealbumin) {Human (Homo sapiens)}
gptgtgeskcplmvkvldavrgspainvavhvfrkaaddtwepfasgktsesgelhgltt
eeefvegiykveidtksywkalgispfhehaevvftandsgprrytiaallspysystma
vtnpke
>d1bz8b_ 2.3.3.1.1 Transthyretin (synonym: prealbumin) {Human (Homo sapiens)}
gptgtgeskcplmvkvldavrgspainvavhvfrkaaddtwepfasgktsesgelhgltt
eeefvegiykveidtksywkalgispfhehaevvftandsgprrytiaallspysystma
vtnpke
>d1bz9a1 2.1.1.2.14 (182-274) Class I MHC, beta2-microglobulin and alpha-3 domain {Mouse (Mus musculus), H-2DB}
tdspkahvthhprskgevtlrcwalgfypaditltwqlngeeltqdmelvetrpagdgtf
qkwasvvvplgkeqnytcrvyheglpepltlrw
>d1bz9a2 4.17.1.1.21 (2-181) MHC class I, alpha-1 and alpha-2 domains {Mouse (Mus musculus), H-2DB}
phsmryfetavsrpgleepryisvgyvdnkefvrfdsdaenpryeprapwmeqegpeywe
retqkakgqeqwfrvslrnllgyynqsaggshtlqqmsgcdlgsdwrllrgylqfayegr
dyialnedlktwtaadmaaqitrrkweqsgaaehykaylegecvewlhrylkngnatllr
>d1bz9b1 2.1.1.2.14 Class I MHC, beta2-microglobulin and alpha-3 domain {Mouse (Mus musculus), H-2DB}
miqktpqiqvysrhppengkpnilncyvtqfhpphieiqmlkngkkipkvemsdmsfskd
wsfyilahteftptetdtyacrvkhdsmaepktvywdrdm
>d1bza__ 5.3.1.1.4 beta-Lactamase, class A {Escherichia coli, TOHO-1}
svqqqlealekssggrlgvalintadnsqilyraderfamcstskvmaaaavlkqsesdk
hllnqrveikksdlvnynpiaekhvngtmtlaelgaaalqysdntamnkliahlggpdkv
tafarslgdetfrldrtaptlntaipgdprdtttplamaqtlknltlgkalaetqraqlv
twlkgnttgsasiraglpkswvvgdktgsgdygttndiaviwpenhaplvlvtyftqpeq
kaerrrdilaaaakivt
>d1bzca_ 3.37.1.3.1 Tyrosine phosphatase {Human (Homo sapiens), 1B}
emekefeqidksgswaaiyqdirheasdfpcrvaklpknknrnryrdvspfdhsriklhq
edndyinaslikmeeaqrsyiltqgplpntcghfwemvweqksrgvvmlnrvmekgslkc
aqywpqkeekemifedtnlkltlisediksyytvrqlelenlttqetreilhfhyttwpd
fgvpespasflnflfkvresgslspehgpvvvhcsagigrsgtfcladtclllmdkrkdp
ssvdikkvllemrkfrmgliqtadqlrfsylaviegakfimgdssvqdqwkelshed
>d1bzda_ 2.3.3.1.1 Transthyretin (synonym: prealbumin) {Human (Homo sapiens)}
gptgtseskcplmvkvldavrgspainvavhvfrkaaddtwepfasgktsesgelhgltt
eeefvegiykveidtksywkalgispfhehaevvftandsgprrytiaallspysystta
vvtnpke
>d1bzdb_ 2.3.3.1.1 Transthyretin (synonym: prealbumin) {Human (Homo sapiens)}
gptgtseskcplmvkvldavrgspainvavhvfrkaaddtwepfasgktsesgelhgltt
eeefvegiykveidtksywkalgispfhehaevvftandsgprrytiaallspysystta
vvtnpke
>d1bzea_ 2.3.3.1.1 Transthyretin (synonym: prealbumin) {Human (Homo sapiens)}
gptgtgeskcplmvkvldavrgspainvavhvfrkaaddtwepfasgktsesgelhgltt
eeefvegiykveidtksywkalgispfhehaevvftandsgprrytiaallspysystma
vvtnpke
>d1bzeb_ 2.3.3.1.1 Transthyretin (synonym: prealbumin) {Human (Homo sapiens)}
gptgtgeskcplmvkvldavrgspainvavhvfrkaaddtwepfasgktsesgelhgltt
eeefvegiykveidtksywkalgispfhehaevvftandsgprrytiaallspysystma
vvtnpke
>d1bzf__ 3.61.1.1.2 Dihydrofolate reductase, prokaryotic type {Lactobacillus casei}
taflwaqdrdgligkdghlpwhlpddlhyfraqtvgkimvvgrrtyesfpkrplpertnv
vlthqedyqaqgavvvhdvaavfayakqhpdqelviaggaqiftafkddvdtllvtrlag
sfegdtkmiplnwddftkvssrtvedtnpalthtyevwqkka
>d1bzha_ 3.37.1.3.1 Tyrosine phosphatase {Human (Homo sapiens), 1B}
emekefeqidksgswaaiyqdirheasdfpcrvaklpknknrnryrdvspfdhsriklhq
edndyinaslikmeeaqrsyiltqgplpntcghfwemvweqksrgvvmlnrvmekgslkc
aqywpqkeekemifedtnlkltlisediksyytvrqlelenlttqetreilhfhyttwpd
fgvpespasflnflfkvresgslspehgpvvvhcsagigrsgtfcladtclllmdkrkdp
ssvdikkvllemrkfrmgliqtadqlrfsylaviegakfimgdssvqdqwkelshed
>d1bzj__ 3.37.1.3.1 Tyrosine phosphatase {Human (Homo sapiens), 1B}
emekefeqidksgswaaiyqdirheasdfpcrvaklpknknrnryrdvspfdhsriklhq
edndyinaslikmeeaqrsyiltqgplpntcghfwemvweqksrgvvmlnrvmekgslkc
aqywpqkeekemifedtnlkltlisediksyytvrqlelenlttqetreilhfhyttwpd
fgvpespasflnflfkvresgslspehgpvvvhcsagigrsgtfcladtclllmdkrkdp
ssvdikkvllemrkfrmgliqtadqlrfsylaviegakfimgdssvqdqwkelshed
>d1bzm__ 2.65.1.1.1 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme I}
aspdwgyddkngpeqwsklypiangnnqspvdiktsetkhdtslkpisvsynpatakeii
nvghsfhvnfedndnrsvlkggpfsdsyrlfqfhfhwgstnehgsehtvdgvkysaelhv
ahwnsakysslaeaaskadglavigvlmkvgeanpklqkvldalqaiktkgkrapftnfd
pstllpssldfwtypgslthpplyesvtwiickesisvsseqlaqfrsllsnvegdnavp
mqhnnrptqplkgrtvrasf
>d1bzoa_ 2.1.8.1.6 Cu,Zn superoxide dismutase, SOD {Photobacterium leiognathi}
qdltvkmtdlqtgkpvgtielsqnkygvvfipeladltpgmhgfhihqngscassekdgk
vvlggaagghydpehtnkhgfpwtddnhkgdlpalfvsanglatnpvlaprltlkelkgh
aimihaggdnhsdmpkalggggarvacgviq
>d1bzpa_ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgyqg
>d1bzqa_ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1bzqb_ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1bzqc_ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1bzqd_ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1bzqk_ 2.1.1.1.140 Immunoglobulin (variable domains of L and H chains) {Camel (Camelus dromedarius), anti-RNase A antibody}
qvqlvesggglvqaggslrlscaasgyaytyiymgwfrqapgkeregvaamdsggggtly
adsvkgrftisrdkgkntvylqmdslkpedtatyycaaggyelrdrtygqwgqgtqvtvs
srgr
>d1bzql_ 2.1.1.1.140 Immunoglobulin (variable domains of L and H chains) {Camel (Camelus dromedarius), anti-RNase A antibody}
qvqlvesggglvqaggslrlscaasgyaytyiymgwfrqapgkeregvaamdsggggtly
adsvkgrftisrdkgkntvylqmdslkpedtatyycaaggyelrdrtygqwgqgtqvtvs
srgr
>d1bzqm_ 2.1.1.1.140 Immunoglobulin (variable domains of L and H chains) {Camel (Camelus dromedarius), anti-RNase A antibody}
qvqlvesggglvqaggslrlscaasgyaytyiymgwfrqapgkeregvaamdsggggtly
adsvkgrftisrdkgkntvylqmdslkpedtatyycaaggyelrdrtygqwgqgtqvtvs
srgr
>d1bzqn_ 2.1.1.1.140 Immunoglobulin (variable domains of L and H chains) {Camel (Camelus dromedarius), anti-RNase A antibody}
qvqlvesggglvqaggslrlscaasgyaytyiymgwfrqapgkeregvaamdsggggtly
adsvkgrftisrdkgkntvylqmdslkpedtatyycaaggyelrdrtygqwgqgtqvtvs
srgr
>d1bzra_ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgyqg
>e1bzv.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1bzv.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergff
>d1bzwa_ 2.26.1.1.10 Lectin {Peanut (Arachis hypogaea)}
aetvsfnfnsfsegnpainfqgdvtvlsngniqltnlnkvnsvgrvlyampvriwssatg
nvasfltsfsfemkdikdydpadgiiffiapedtqipagsigggtlgvsdtkgaghfvgv
efdtysnseyndpptdhvgidvnsvdsvktvpwnsvsgavvkvtviydsstktlsvavtn
dngdittiaqvvdlkaklpervkfgfsasgslggrqihlirswsftstlitt
>d1bzwb_ 2.26.1.1.10 Lectin {Peanut (Arachis hypogaea)}
aetvsfnfnsfsegnpainfqgdvtvlsngniqltnlnkvnsvgrvlyampvriwssatg
nvasfltsfsfemkdikdydpadgiiffiapedtqipagsigggtlgvsdtkgaghfvgv
efdtysnseyndpptdhvgidvnsvdsvktvpwnsvsgavvkvtviydsstktlsvavtn
dngdittiaqvvdlkaklpervkfgfsasgslggrqihlirswsftstlitt
>d1bzwc_ 2.26.1.1.10 Lectin {Peanut (Arachis hypogaea)}
aetvsfnfnsfsegnpainfqgdvtvlsngniqltnlnkvnsvgrvlyampvriwssatg
nvasfltsfsfemkdikdydpadgiiffiapedtqipagsigggtlgvsdtkgaghfvgv
efdtysnseyndpptdhvgidvnsvdsvktvpwnsvsgavvkvtviydsstktlsvavtn
dngdittiaqvvdlkaklpervkfgfsasgslggrqihlirswsftstlitt
>d1bzwd_ 2.26.1.1.10 Lectin {Peanut (Arachis hypogaea)}
aetvsfnfnsfsegnpainfqgdvtvlsngniqltnlnkvnsvgrvlyampvriwssatg
nvasfltsfsfemkdikdydpadgiiffiapedtqipagsigggtlgvsdtkgaghfvgv
efdtysnseyndpptdhvgidvnsvdsvktvpwnsvsgavvkvtviydsstktlsvavtn
dngdittiaqvvdlkaklpervkfgfsasgslggrqihlirswsftstlitt
>d1bzxe_ 2.41.1.2.5 Trypsin(ogen) {North atlantic salmon (Salmo salar)}
ivggyeckaysqthqvslnsgyhfcggslvnenwvvsaahcyksrvevrlgehnikvteg
seqfisssrvirhpnyssynidndimliklskpatlntyvqpvalptscapagtmctvsg
wgntmsstadsnklqclnipilsysdcnnsypgmitnamfcagyleggkdscqgdsggpv
vcngelqgvvswgygcaepgnpgvyakvcifndwltstmasy
>d1bzxi_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d1bzya_ 3.51.1.1.6 Hypoxantine-guanine PRTase {Human (Homo sapiens)}
spgvvisddepgydldlfcipnhyaedlervfiphglimdrterlardvmkemgghhiva
lcvlkggykffadlldyikalnrnsdrsipmtvdfirlksycndqstgdikviggddlst
ltgknvlivediidtgktmqtllslvrqynpkmvkvasllvkrtprsvgykpdfvgfeip
dkfvvgyaldyneyfrdlnhvcvisetgkakyka
>d1bzyb_ 3.51.1.1.6 Hypoxantine-guanine PRTase {Human (Homo sapiens)}
spgvvisddepgydldlfcipnhyaedlervfiphglimdrterlardvmkemgghhiva
lcvlkggykffadlldyikalnrnsdrsipmtvdfirlksycndqstgdikviggddlst
ltgknvlivediidtgktmqtllslvrqynpkmvkvasllvkrtprsvgykpdfvgfeip
dkfvvgyaldyneyfrdlnhvcvisetgkakyka
>d1bzyc_ 3.51.1.1.6 Hypoxantine-guanine PRTase {Human (Homo sapiens)}
spgvvisddepgydldlfcipnhyaedlervfiphglimdrterlardvmkemgghhiva
lcvlkggykffadlldyikalnrnsdrsipmtvdfirlksycndqstgdikviggddlst
ltgknvlivediidtgktmqtllslvrqynpkmvkvasllvkrtprsvgykpdfvgfeip
dkfvvgyaldyneyfrdlnhvcvisetgkakyka
>d1bzyd_ 3.51.1.1.6 Hypoxantine-guanine PRTase {Human (Homo sapiens)}
spgvvisddepgydldlfcipnhyaedlervfiphglimdrterlardvmkemgghhiva
lcvlkggykffadlldyikalnrnsdrsipmtvdfirlksycndqstgdikviggddlst
ltgknvlivediidtgktmqtllslvrqynpkmvkvasllvkrtprsvgykpdfvgfeip
dkfvvgyaldyneyfrdlnhvcvisetgkakyka
>d1bzza_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
mlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1bzzb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1bzzc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
mlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1bzzd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1c00a_ 3.59.1.1.5 Thermophylic para-nitrobenzyl esterase (PNB esterase) {Bacillus subtilis}
thqivttqygkvkgttengvhkwkgipyakppvgqwrfkapeppevwedvldatvygpvc
pqpsdllslsykelprqsedclyvnvfapdtpsqnlpvmvwihggafylgagseplydgs
klaaqgevivvtlnyrlgpfgflhlssfdeaysdnlglldqaaalkwvrenisafggdpd
nvtvfgesaggmsiaallampaakglfqkaimesgasrtmtkeqaastaaaflqvlgine
sqldrlhtvaaedllkaadqlriaekenifqlffqpaldpktlpeepeksiaegaasgip
lligttrdegyffftpdsdvysqetldaaleyllgkplaekvadlyprslesqihmvtdl
lfwrpavafasaqshyapvwmyrfdwhpekppynkafhtlelpfvfgnldelermakagi
tdevkqlshtiqsawttfaktgnpsteavnwpayheesretvildseitiendpesekrq
klf
>d1c05a_ 4.51.3.1.1 Ribosomal protein S4 {Bacillus stearothermophilus}
mklseyglqlqekqklrhmygvnerqfrktfeeagkmpgkhgenfmillesrldnlvyrl
glartrrqarqlvthghilvdgsrvnipsyrvkpgqtiavreksrnlqvikealeannyi
pdylsfdpekmegtytrlperselpaeinealivefysr
>d1c06a_ 4.51.3.1.1 Ribosomal protein S4 {Bacillus stearothermophilus}
mklseyglqlqekqklrhmygvnerqfrktfeeagkmpgkhgenfmillesrldnlvyrl
glartrrqarqlvthghilvdgsrvnipsyrvkpgqtiavreksrnlqvikealeannyi
pdylsfdpekmegtytrlperselpaeinealivefysr
>d1c0ba_ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1c0ca_ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1c0da_ 3.1.7.3.6 Endocellulase E1 {Acidothermus cellulolyticus}
agggywhtsgreildannvpvriaginwfgfetcnyvvhglwsrdyrsmldqikslgynt
irlpysddilkpgtmpnsinfyqmnqdlqgltslqvmdkivayagqiglriildrhrpdc
sgqsalwytssvseatwisdlqalaqrykgnptvvgfdlhnephdpacwgcgdpsidwrl
aaeragnavlsvnpnllifvegvqsyngdsywwggnlqgagqypvvlnvpnrlvysahdy
atsvgpqtwfsdptfpnnmpgiwnknwgylfnqniapvwlgefgttlqsttdqtwlktlv
qylrptaqygadsfqwtfwswnpdsgdtggilkddwqtvdtdkdgylapikssifdpv
>d1c0db_ 3.1.7.3.6 Endocellulase E1 {Acidothermus cellulolyticus}
agggywhtsgreildannvpvriaginwfgfetcnyvvhglwsrdyrsmldqikslgynt
irlpysddilkpgtmpnsinfyqmnqdlqgltslqvmdkivayagqiglriildrhrpdc
sgqsalwytssvseatwisdlqalaqrykgnptvvgfdlhnephdpacwgcgdpsidwrl
aaeragnavlsvnpnllifvegvqsyngdsywwggnlqgagqypvvlnvpnrlvysahdy
atsvgpqtwfsdptfpnnmpgiwnknwgylfnqniapvwlgefgttlqsttdqtwlktlv
qylrptaqygadsfqwtfwswnpdsgdtggilkddwqtvdtdkdgylapikssifdpv
>d1c0ea_ 3.36.1.1.1 Tyrosine phosphatase {Bovine (Bos taurus)}
vtksvlfvclgnicrapiaeavfrklvtdqnisdnwvidsgavsdwnvgrspdpravscl
rnhgintahkarqvtkedfvtfdyilcmdesnlrdlnrksnqvkncrakiellgsydpqk
qliiedpyygndadfetvyqqcvrccraflekvr
>d1c0eb_ 3.36.1.1.1 Tyrosine phosphatase {Bovine (Bos taurus)}
vtksvlfvclgnicrapiaeavfrklvtdqnisdnwvidsgavsdwnvgrspdpravscl
rnhgintahkarqvtkedfvtfdyilcmdesnlrdlnrksnqvkncrakiellgsydpqk
qliiedpyygndadfetvyqqcvrccraflekvr
>d1c0va_ 6.2.1.1.7 Subunit C of the F1F0 ATP synthase {Escherichia coli}
menlnmdllymaaavmmglaaigaaigigilggkflegaarqpdlipllrtqffivmglv
daipmiavglglyvmfava
>d1c10a_ 4.2.1.2.1 Lysozyme {Chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1c12a1 2.1.1.1.135 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab directed agains the musk odorant traseolide, (mouse), kappa L chain}
dieltqspssmsvslgdtvsitchasqgissnigwlqqkpgksfkgliyhgtnledgvps
rfsgsgsgadysltisslesedfadyycvqyvqfpftfgsgtkleik
>d1c12a2 2.1.1.2.133 (108-214) Immunoglobulin (constant domains of L and H chains) {Fab directed agains the musk odorant traseolide, (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnea
>d1c12b1 2.1.1.1.135 (301-413) Immunoglobulin (variable domains of L and H chains) {Fab directed agains the musk odorant traseolide, (mouse), kappa L chain}
qvqlqesgpglvkpsqslsltctvtgysitsdyawnwirqfpgnklewmgyisysgstsy
spslksrisltrdtsknqfflqlnsvttedtatyycvtsltwllrrkrsywgqgttvtvs
s
>d1c12b2 2.1.1.2.133 (414-513) Immunoglobulin (constant domains of L and H chains) {Fab directed agains the musk odorant traseolide, (mouse), kappa L chain}
astkgpsvyplapgskaaasmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsdl
ytlsssvtvpssprpsetvtcnvahpasstkvdkkivpe
>d1c13a_ 3.33.1.1.6 Subtilisin BL {Bacillus lentus}
aqsvpwgisrvqapaahnrgltgsgvkvavldtgisthpdlnirggasfvpgepstqdgn
ghgthvagtiaalnnsigvlgvapnaelyavkvlgasgsgsvssiaqglewagnngmhva
nlslgspspsatleqavnsatsrgvlvvaasgnsgagsisyparyanamavgatdqnnnr
asfsqygagldivapgvnvqstypgstyaslngtsmatphvagaaalvkqknpswsnvqi
rnhlkntatslgstnlygsglvnaeaatr
>d1c15a_ 1.76.1.1.6 Apoptotic protease activating factor 1, APAF-1 {Human (Homo sapiens)}
mdakarncllqhrealekdiktsyimdhmisdgfltiseeekvrneptqqqraamlikmi
lkkdndsyvsfynallhegykdlaallhdgipvvsss
>d1c1fa_ 2.26.1.3.6 Congerin I {Conger eel (Conger myriaster)}
gglqvknfdftvgkfltvggfinnspqrfsvnvgesmnslslhldhrfnygadqntivmn
stlkgdngweteqrstnftlsagqyfeitlsydinkfyidildgpnlefpnryskeflpf
lslagdarltlvkle
>d1c1la_ 2.26.1.3.6 Congerin I {Conger eel (Conger myriaster)}
gglqvknfdftvgkfltvggfinnspqrfsvnvgesmnslslhldhrfnygadqntivmn
stlkgdngweteqrstnftlsagqyfeitlsydinkfyidildgpnlefpnryskeflpf
lslagdarltlvkle
>d1c1ma_ 2.41.1.2.15 Elastase {Porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqndgteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1c1ya_ 3.30.1.6.3 Rap1A {Human (Homo sapiens)}
mreyklvvlgsggvgksaltvqfvqgifvekydptiedsyrkqvevdcqqcmleildtag
teqftamrdlymkngqgfalvysitaqstfndlqdlreqilrvkdtedvpmilvgnkcdl
edervvgkeqgqnlarqwcncaflessakskinvneifydlvrqinr
>d1c1yb_ 4.13.3.1.1 c-Raf1 RBD {Human (Homo sapiens)}
sntirvflpnkqrtvvnvrngmslhdclmkalkvrglqpeccavfrllhehkgkkarldw
ntdaasligeelqvdfl
>d1c25__ 3.37.1.1.1 CDC25a {Human (Homo sapiens)}
mligdfskgylfhtvagkhqdlkyispeimasvlngkfanlikefviidcrypyeyeggh
ikgavnlhmeeevedfllkkpivptdgkrvivvfhcefssergprmcryvrerdrlgney
pklhypelyvlkggykeffmkcqsyceppsyrpmhhedfke
>d1c26a_ 1.55.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
geyftlqirgrerfemfrelnealelkdaqag
>d1c28a_ 2.20.1.1.2 30 kd adipocyte complement-related protein {Mouse (Mus musculus)}
myrsafsvgletrvtvpnvpirftkifynqqnhydgstgkfycnipglyyfsyhitvymk
dvkvslfkkdkavlftydqyqeknvdqasgsvllhlevgdqvwlqvygdgdhnglyadnv
ndstftgfllyhdt
>d1c28b_ 2.20.1.1.2 30 kd adipocyte complement-related protein {Mouse (Mus musculus)}
myrsafsvgletrvtvpnvpirftkifynqqnhydgstgkfycnipglyyfsyhitvymk
dvkvslfkkdkavlftydqyqeknvdqasgsvllhlevgdqvwlqvygdgdhnglyadnv
ndstftgfllyhd
>d1c28c_ 2.20.1.1.2 30 kd adipocyte complement-related protein {Mouse (Mus musculus)}
myrsafsvgletrvtvpnvpirftkifynqqnhydgstgkfycnipglyyfsyhitvymk
dvkvslfkkdkavlftydqyqeknvdqasgsvllhlevgdqvwlqvygdgdhnglyadnv
ndstftgfllyhd
>d1c2n__ 1.3.1.1.13 Cytochrome c2 {Rhodobacter capsulatus}
gdaakgekefnkcktchsiiapdgteivkgaktgpnlygvvgrtagtypefkykdsival
gasgfawteediatyvkdpgaflkeklddkkaktgmafklakggedvaaylasvvk
>d1c2ra_ 1.3.1.1.13 Cytochrome c2 {Rhodobacter capsulatus}
gdaakgekefnkcktchsiiapdgteivkgaktgpnlygvvgrtagtypefkykdsival
gasgfawteediatyvkdpgaflkeklddkkaktgmafklakggedvaaylasvvk
>d1c2rb_ 1.3.1.1.13 Cytochrome c2 {Rhodobacter capsulatus}
gdaakgekefnkcktchsiiapdgteivkgaktgpnlygvvgrtagtypefkykdsival
gasgfawteediatyvkdpgaflkeklddkkaktgmafklakggedvaaylasvvk
>d1c3d__ 1.98.3.4.1 C3D, a C3 fragment and ligand for complement receptor 2 {Human (Homo sapiens)}
mldaerlkhlivtpsgageqnmigmtptviavhyldeteqwekfglekrqgalelikkgy
tqqlafrqpssafaafvkrapstwltayvvkvfslavnliaidsqvlcgavkwlilekqk
pdgvfqedapvihqemigglrnnnekdmaltafvlislqeakdiceeqvnslpgsitkag
dfleanymnlqrsytvaiagyalaqmgrlkgpllnkflttakdknrwedpgkqlynveat
syallallqlkdfdfvppvvrwlneqryygggygstqatfmvfqalaqyqkdap
>d1c3ja_ 3.77.1.1.1 beta-Glucosyltransferase (DNA-modifying) {Bacteriophage T4}
mkiaiinmgnnvinfktvpssetiylfkvisemglnvdiislkngvytksfdevdvndyd
rlivvnsnlailsaqkfmakykskiyylftdirlpfsqsaylyteeellikspikvisqg
inldiakaahkkvdnviefeyfpieqykihmndfqlskptkktldviyggsfrsgqresk
mveflfdtglnieffgnarekqfknpkypwtkapvftgkipmnmvseknsqaiaaliigd
knyndnfitlrvwetmasdavmlideefdtkhriindarfyvnnraelidrvnelkhsdv
lrkemlsiqhdilnktrakkaewqdafkkaidl
>d1c3la_ 3.33.1.1.2 Subtilisin Carlsberg {Bacillus licheniformis}
aqtvpygiplikadkvqaqgfkganvkvavldtgiqashpdlnvvggasfvageayntdg
nghgthvagtvaaldnttgvlgvapsvslyavkvlnssgsgsysgivsgiewattngmdv
inmslggasgstamkqavdnayargvvvvaaagnsgssgstntigypakydsviavgavd
snsnrasfssvgaelevmapgagvystyptntyatlngtsmasphvagaaalilskhpnl
sasqvrnrlsstatylgssfyygkglinveaaaq
>d1c3pa_ 3.34.1.2.1 HDAC homologue {Aquifex aeolicus |A|}
kkvkligtldygkyrypknhplkiprvslllrfkdamnlidekeliksrpatkeelllfh
tedyintlmeaercqcvpkgarekyniggyenpvsyamftgsslatgstvqaieeflkgn
vafnpaggmhhafksrangfcyinnpavgieylrkkgfkrilyidldahhcdgvqeafyd
tdqvfvlslhqspeyafpfekgfleeigegkgkgynlniplpkglndneflfalekslei
vkevfepevyllqlgtdplledylskfnlsnvaflkafnivrevfgegvylggggyhpya
larawtliwcelsgrevpeklnnkakellksidfeefddevdrsymletlkdpwrggevr
kevkdtlekaka
>d1c3qa_ 3.62.1.2.1 Thiazole kinase {Bacillus subtilis}
mdaqsaakcltavrrhsplvhsitnnvvtnftangllalgaspvmayakeevadmakiag
alvlnigtlskesveamiiagksanehgvpvildpvgagatpfrtesardiirevrlaai
rgnaaeiahtvgvtdwlikgvdagegggdiirlaqqaaqklntviaitgevdviadtshv
ytlhnghklltkvtgagclltsvvgafcaveenplfaaiaaissygvaaqlaaqqtadkg
pgsfqiellnklstvteqdvqewatiervtvs
>d1c3qb_ 3.62.1.2.1 Thiazole kinase {Bacillus subtilis}
mdaqsaakcltavrrhsplvhsitnnvvtnftangllalgaspvmayakeevadmakiag
alvlnigtlskesveamiiagksanehgvpvildpvgagatpfrtesardiirevrlaai
rgnaaeiahtvgvtdwlikgvdagegggdiirlaqqaaqklntviaitgevdviadtshv
ytlhnghklltkvtgagclltsvvgafcaveenplfaaiaaissygvaaqlaaqqtadkg
pgsfqiellnklstvteqdvqewatiervtvs
>d1c3qc_ 3.62.1.2.1 Thiazole kinase {Bacillus subtilis}
mdaqsaakcltavrrhsplvhsitnnvvtnftangllalgaspvmayakeevadmakiag
alvlnigtlskesveamiiagksanehgvpvildpvgagatpfrtesardiirevrlaai
rgnaaeiahtvgvtdwlikgvdagegggdiirlaqqaaqklntviaitgevdviadtshv
ytlhnghklltkvtgagclltsvvgafcaveenplfaaiaaissygvaaqlaaqqtadkg
pgsfqiellnklstvteqdvqewatiervtvs
>d1c3ra_ 3.34.1.2.1 HDAC homologue {Aquifex aeolicus |A|}
kkvkligtldygkyrypknhplkiprvslllrfkdamnlidekeliksrpatkeelllfh
tedyintlmeaersqsvpkgarekyniggyenpvsyamftgsslatgstvqaieeflkgn
vafnpaggmhhafksrangfcyinnpavgieylrkkgfkrilyidldahhcdgvqeafyd
tdqvfvlslhqspeyafpfekgfleeigegkgkgynlniplpkglndneflfalekslei
vkevfepevyllqlgtdplledylskfnlsnvaflkafnivrevfgegvylggggyhpya
larawtliwcelsgrevpeklnnkakellksidfeefddevdrsymletlkdpwrggevr
kevkdtlekaka
>d1c3rb_ 3.34.1.2.1 HDAC homologue {Aquifex aeolicus |A|}
kkvkligtldygkyrypknhplkiprvslllrfkdamnlidekeliksrpatkeelllfh
tedyintlmeaersqsvpkgarekyniggyenpvsyamftgsslatgstvqaieeflkgn
vafnpaggmhhafksrangfcyinnpavgieylrkkgfkrilyidldahhcdgvqeafyd
tdqvfvlslhqspeyafpfekgfleeigegkgkgynlniplpkglndneflfalekslei
vkevfepevyllqlgtdplledylskfnlsnvaflkafnivrevfgegvylggggyhpya
larawtliwcelsgrevpeklnnkakellksidfeefddevdrsymletlkdpwrggevr
kevkdtlekaka
>d1c3sa_ 3.34.1.2.1 HDAC homologue {Aquifex aeolicus |A|}
kkvkligtldygkyrypknhplkiprvslllrfkdamnlidekeliksrpatkeelllfh
tedyintlmeaersqsvpkgarekyniggyenpvsyamftgsslatgstvqaieeflkgn
vafnpaggmhhafksrangfcyinnpavgieylrkkgfkrilyidldahhcdgvqeafyd
tdqvfvlslhqspeyafpfekgfleeigegkgkgynlniplpkglndneflfalekslei
vkevfepevyllqlgtdplledylskfnlsnvaflkafnivrevfgegvylggggyhpya
larawtliwcelsgrevpeklnnkakellksidfeefddevdrsymletlkdpwrggevr
kevkdtlekaka
>d1c3ta_ 4.13.2.1.1 Ubiquitin {Human (Homo sapiens)}
mqlfvktltgktltvelepsdtvenlkakiqdkegippdqqrlifagkqledgrtlsdyn
lqkestihlvlrlrgg
>d1c3wa_ 6.2.1.1.2 Bacteriorhodopsin {Halobacterium salinarium}
tgrpewiwlalgtalmglgtlyflvkgmgvsdpdakkfyaittlvpaiaftmylsmllgy
gltmvpfggeqnpiywaryadwlfttplllldlallvdadqgtilalvgadgimigtglv
galtkvysyrfvwwaistaamlyilyvlffgfsmrpevastfkvlrnvtvvlwsaypvvw
ligsegagivplnietllfmvldvsakvgfglillrsraifg
>d1c40a_ 1.1.1.1.22 Hemoglobin D {Bar-headed goose (Anser indicus)}
vlsaadktnvkgvfskisghaeeygaetlermftaypqtktyfphfdlqhgsaqikahgk
kvvaalveavnhiddiagalsklsnlhaqklrvdpvnfkflghcflvvvaihhpsaltae
vhasldkflcavgtvltakyr
>d1c40b_ 1.1.1.1.37 Hemoglobin D {Bar-headed goose (Anser indicus)}
vhwsaeekqlitglwgkvnvadcgaealarllivypwtqrffssfgnlssptailgnpmv
rahgkkvltsfgdavknldnikntfaqlselhcdklhvdpenfrllgdiliivlaahfak
eftpdcqaawqklvrvvahalarkyh
>d1c43a_ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
mvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1c45a_ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
avfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1c46a_ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
gkvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqi
nsrywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawvawrnrcqnr
dvrqyvqgcgv
>d1c47a1 3.73.1.1.1 (1-190) Phosphoglucomutase, first 3 domains {Rabbit (Oryctolagus cuniculus)}
vkivtvktkaypdqkpgtsglrkrvkvfqsstnyaenfiqsiistvepaqrqeatlvvgg
dgrfymkeaiqlivriaaangigrlvigqngilstpavsciirkikaiggiiltashnpg
gpngdfgikfnisnggpapeaitdkifqisktieeyaicpdlkvdlgvlgkqqfdlenkf
kpftveivds
>d1c47a2 3.73.1.1.1 (191-303) Phosphoglucomutase, first 3 domains {Rabbit (Oryctolagus cuniculus)}
veayatmlrnifdfnalkellsgpnrlkiridamhgvvgpyvkkilceelgapansavnc
vpledfgghhpdpnltyaadlvetmksgehdfgaafdgdgdrnmilgkhgffv
>d1c47a3 3.73.1.1.1 (304-420) Phosphoglucomutase, first 3 domains {Rabbit (Oryctolagus cuniculus)}
npsdsvaviaanifsipyfqqtgvrgfarsmptsgaldrvanatkialyetptgwkffgn
lmdasklslcgeesfgtgsdhirekdglwavlawlsilatrkqsvedilkdhwhkfg
>d1c47a4 4.103.2.1.1 (421-561) Phosphoglucomutase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
rnfftrydyeeveaegatkmmkdlealmfdrsfvgkqfsandkvytvekadnfeyhdpvd
gsvsknqglrlifadgsriifrlsgtgsagatirlyidsyekdnakinqdpqvmlaplis
ialkvsqlqertgrtaptvit
>d1c47b1 3.73.1.1.1 (1-190) Phosphoglucomutase, first 3 domains {Rabbit (Oryctolagus cuniculus)}
vkivtvktkaypdqkpgtsglrkrvkvfqsstnyaenfiqsiistvepaqrqeatlvvgg
dgrfymkeaiqlivriaaangigrlvigqngilstpavsciirkikaiggiiltashnpg
gpngdfgikfnisnggpapeaitdkifqisktieeyaicpdlkvdlgvlgkqqfdlenkf
kpftveivds
>d1c47b2 3.73.1.1.1 (191-303) Phosphoglucomutase, first 3 domains {Rabbit (Oryctolagus cuniculus)}
veayatmlrnifdfnalkellsgpnrlkiridamhgvvgpyvkkilceelgapansavnc
vpledfgghhpdpnltyaadlvetmksgehdfgaafdgdgdrnmilgkhgffv
>d1c47b3 3.73.1.1.1 (304-420) Phosphoglucomutase, first 3 domains {Rabbit (Oryctolagus cuniculus)}
npsdsvaviaanifsipyfqqtgvrgfarsmptsgaldrvanatkialyetptgwkffgn
lmdasklslcgeesfgtgsdhirekdglwavlawlsilatrkqsvedilkdhwhkfg
>d1c47b4 4.103.2.1.1 (421-561) Phosphoglucomutase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
rnfftrydyeeveaegatkmmkdlealmfdrsfvgkqfsandkvytvekadnfeyhdpvd
gsvsknqglrlifadgsriifrlsgtgsagatirlyidsyekdnakinqdpqvmlaplis
ialkvsqlqertgrtaptvit
>d1c4ea_ 7.3.4.1.1 Gurmarin, a sweet taste-suppressing polypeptide {Gymnema sylveste}
qcvkkdelcipyyldccepleckkvnwwdhkcig
>d1c4fa_ 4.20.1.1.1 Green fluorescent protein, GFP {Jellyfish (Aequorea victoria)}
kgeelftgvvpilveldgdvnghkfsvsgegegdatygkltlkficttgklpvpwptlvt
tfxvqcfsrypdhmkrhdffksampegyvqertiffkddgnyktraevkfegdtlvnrie
lkgidfkedgnilghkleynynshnvyimadkqkngikvnfkirhniedgsvqladhyqq
ntpigdgpvllpdnhylstqsalskdpnekrdhmvllefvtaagi
>d1c4ga1 3.73.1.1.1 (1-190) Phosphoglucomutase, first 3 domains {Rabbit (Oryctolagus cuniculus)}
vkivtvktkaypdqkpgtsglrkrvkvfqsstnyaenfiqsiistvepaqrqeatlvvgg
dgrfymkeaiqlivriaaangigrlvigqngilstpavsciirkikaiggiiltashnpg
gpngdfgikfnisnggpapeaitdkifqisktieeyaicpdlkvdlgvlgkqqfdlenkf
kpftveivds
>d1c4ga2 3.73.1.1.1 (191-303) Phosphoglucomutase, first 3 domains {Rabbit (Oryctolagus cuniculus)}
veayatmlrnifdfnalkellsgpnrlkiridamhgvvgpyvkkilceelgapansavnc
vpledfgghhpdpnltyaadlvetmksgehdfgaafdgdgdrnmilgkhgffv
>d1c4ga3 3.73.1.1.1 (304-420) Phosphoglucomutase, first 3 domains {Rabbit (Oryctolagus cuniculus)}
npsdsvaviaanifsipyfqqtgvrgfarsmptsgaldrvanatkialyetptgwkffgn
lmdasklslcgeesfgtgsdhirekdglwavlawlsilatrkqsvedilkdhwhkfg
>d1c4ga4 4.103.2.1.1 (421-561) Phosphoglucomutase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
rnfftrydyeeveaegatkmmkdlealmfdrsfvgkqfsandkvytvekadnfeyhdpvd
gsvsknqglrlifadgsriifrlsgtgsagatirlyidsyekdnakinqdpqvmlaplis
ialkvsqlqertgrtaptvit
>d1c4gb1 3.73.1.1.1 (1-190) Phosphoglucomutase, first 3 domains {Rabbit (Oryctolagus cuniculus)}
vkivtvktkaypdqkpgtsglrkrvkvfqsstnyaenfiqsiistvepaqrqeatlvvgg
dgrfymkeaiqlivriaaangigrlvigqngilstpavsciirkikaiggiiltashnpg
gpngdfgikfnisnggpapeaitdkifqisktieeyaicpdlkvdlgvlgkqqfdlenkf
kpftveivds
>d1c4gb2 3.73.1.1.1 (191-303) Phosphoglucomutase, first 3 domains {Rabbit (Oryctolagus cuniculus)}
veayatmlrnifdfnalkellsgpnrlkiridamhgvvgpyvkkilceelgapansavnc
vpledfgghhpdpnltyaadlvetmksgehdfgaafdgdgdrnmilgkhgffv
>d1c4gb3 3.73.1.1.1 (304-420) Phosphoglucomutase, first 3 domains {Rabbit (Oryctolagus cuniculus)}
npsdsvaviaanifsipyfqqtgvrgfarsmptsgaldrvanatkialyetptgwkffgn
lmdasklslcgeesfgtgsdhirekdglwavlawlsilatrkqsvedilkdhwhkfg
>d1c4gb4 4.103.2.1.1 (421-561) Phosphoglucomutase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
rnfftrydyeeveaegatkmmkdlealmfdrsfvgkqfsandkvytvekadnfeyhdpvd
gsvsknqglrlifadgsriifrlsgtgsagatirlyidsyekdnakinqdpqvmlaplis
ialkvsqlqertgrtaptvit
>d1c4pa_ 4.13.4.1.2 Streptokinase {Streptoccocal bacteria (Streptococcus equisimilis)}
kpiqnqaksvdveytvqftplnpdddfrpglkdtkllktlaigdtitsqellaqaqsiln
kthpgytiyerdssivthdndifrtilpmdqeftyhvknreqayeinkksglneeinntd
lisekyyvlkkgekpyd
>d1c4pb_ 4.13.4.1.2 Streptokinase {Streptoccocal bacteria (Streptococcus equisimilis)}
kpiqnqaksvdveytvqftplnpdddfrpglkdtkllktlaigdtitsqellaqaqsiln
kthpgytiyerdssivthdndifrtilpmdqeftyhvknreqayeinkksglneeinntd
lisekyyvlkkgekpyd
>d1c4pc_ 4.13.4.1.2 Streptokinase {Streptoccocal bacteria (Streptococcus equisimilis)}
kpiqnqaksvdveytvqftplnpdddfrpglkdtkllktlaigdtitsqellaqaqsiln
kthpgytiyerdssivthdndifrtilpmdqeftyhvknreqayeinkksglneeinntd
lisekyyvlkkg
>d1c4pd_ 4.13.4.1.2 Streptokinase {Streptoccocal bacteria (Streptococcus equisimilis)}
kpiqnqaksvdveytvqftplnpdddfrpglkdtkllktlaigdtitsqellaqaqsiln
kthpgytiyerdssivthdndifrtilpmdqeftyhvknreqayeinkksglneeinntd
lisekyyvlkkg
>d1c4xa_ 3.59.1.8.1 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase (BPHD) {Rhodococcus sp. strain rha1}
tveiiekrfpsgtlashalvagdpqspavvllhgagpgahaasnwrpiipdlaenffvva
pdligfgqseypetypghimswvgmrveqilglmnhfgiekshivgnsmggavtlqlvve
aperfdkvalmgsvgapmnarppelarllafyadprltpyrelihsfvydpenfpgmeei
vksrfevandpevrriqevmfesmkagmeslvippatlgrlphdvlvfhgrqdrivpldt
slyltkhlkhaelvvldrcghwaqlerwdamgpmlmehfra
>d1c52__ 1.3.1.1.5 Cytochrome c552 {Thermus thermophilus}
qadgakiyaqcagchqqngqgipgafpplaghvaeilakeggreylilvllyglqgqiev
kgmkyngvmssfaqlkdeeiaavlnhiatawgdakkvkgfkpftaeevkklrakkltpqq
vlaerkklglk
>d1c53__ 1.3.1.1.2 Cytochrome c6 (synonym: cytochrome c553) {Desulfovibrio vulgaris, different strains}
adgaalykscvgchgadgskqamgvghavkgqkadelfkklkgyadgsyggekkavmtnl
vkrysdeemkamadymskl
>d1c5a__ 1.52.1.1.2 C5a anaphylotoxin {Pig (Sus scrofa domestica)}
mlqkkieeeaakykyamlkkccydgayrnddetceeraarikigpkcvkafkdccyianq
vraeqs
>d1c6s__ 1.3.1.1.4 Cytochrome c6 (synonym: cytochrome c553) {Blue-green alga cyanobacterium (Synechococcus elongatus)}
adlangakvfsgncaachmgggnvvmanktlkkealeqfgmysedaiiyqvqhgknampa
fagrltdeqiqdvaayvldqaakgwag
>d1c8ra_ 6.2.1.1.2 Bacteriorhodopsin {Halobacterium salinarium}
tgrpewiwlalgtalmglgtlyflvkgmgvsdpdakkfyaittlvpaiaftmylsmllgy
gltmvpfggeqnpiywaryadwlfttpllllnlallvdadqgtilalvgadgimigtglv
galtkvysyrfvwwaistaamlyilyvlffgfsmrpevastfkvlrnvtvvlwsaypvvw
ligsegagivplnietllfmvldvsakvgfglillrsraifg
>d1c8sa_ 6.2.1.1.2 Bacteriorhodopsin {Halobacterium salinarium}
tgrpewiwlalgtalmglgtlyflvkgmgvsdpdakkfyaittlvpaiaftmylsmllgy
gltmvpfggeqnpiywaryadwlfttpllllnlallvdadqgtilalvgadgimigtglv
galtkvysyrfvwwaistaamlyilyvlfnvtvvlwsaypvvwligsegagivplnietl
lfmvldvsakvgfgli
>d1c96a1 3.7.2.1.2 (529-754) Aconitase, C-terminal domain {Bovine (Bos taurus)}
vavsptsqrlqllepfdkwdgkdledlqilikvkgkcttdhisaagpwlkfrghldnisn
nlligainienrkansvrnavtqefgpvpdtaryykqhgirwvvigdenygegasrehsa
leprhlggraiitksfarihetnlkkqgllpltfadpadynkihpvdkltiqglkdfapg
kplkciikhpngtqetillnhtfnetqiewfragsalnrmkelqqk
>d1c96a2 3.72.1.1.2 (2-528) Aconitase, first 3 domains {Bovine (Bos taurus)}
rakvamshfepheyirydlleknidivrkrlnrpltlsekivyghlddpanqeiergkty
lrlrpdrvamqdataqmamlqfissglpkvavpstihcdhlieaqlggekdlrrakdinq
evynflatagakygvgfwrpgsgiihqiilenyaypgvlligtdshtpnggglggicigv
ggadavdvmagipwelkcpkvigvkltgslsgwtspkdvilkvagiltvkggtgaiveyh
gpgvdsisctgmaticnmgaeigattsvfpynhrmkkylsktgradianladefkdhlvp
dpgchydqvieinlselkphingpftpdlahpvaevgsvaekegwpldirvgligsctns
syedmgrsaavakqalahglkcksqftitpgseqiratierdgyaqvlrdvggivlanac
gpcigqwdrkdikkgekntivtsynrnftgrndanpethafvtspeivtalaiagtlkfn
petdfltgkdgkkfkleapdadelpraefdpgqdtyqhppkdssgqr
>d1c97a1 3.7.2.1.2 (529-754) Aconitase, C-terminal domain {Bovine (Bos taurus)}
vdvsptsqrlqllepfdkwdgkdledlqilikvkgkcttdhisaagpwlkfrghldnisn
nlligainienrkansvrnavtqefgpvpdtaryykqhgirwvvigdenygegasrehsa
leprhlggraiitksfarihetnlkkqgllpltfadpadynkihpvdkltiqglkdfapg
kplkciikhpngtqetillnhtfnetqiewfragsalnrmkelqqk
>d1c97a2 3.72.1.1.2 (2-528) Aconitase, first 3 domains {Bovine (Bos taurus)}
rakvamshfepheyirydlleknidivrkrlnrpltlsekivyghlddpanqeiergkty
lrlrpdrvamqdataqmamlqfissglpkvavpstihcdhlieaqlggekdlrrakdinq
evynflatagakygvgfwrpgsgiihqiilenyaypgvlligtdshtpnggglggicigv
ggadavdvmagipwelkcpkvigvkltgslsgwtspkdvilkvagiltvkggtgaiveyh
gpgvdsisctgmaticnmgaeigattsvfpynhrmkkylsktgradianladefkdhlvp
dpgchydqvieinlselkphingpftpdlahpvaevgsvaekegwpldirvgligsctns
syedmgrsaavakqalahglkcksqftitpgseqiratierdgyaqvlrdvggivlanac
gpcigqwdrkdikkgekntivtsynrnftgrndanpethafvtspeivtalaiagtlkfn
petdfltgkdgkkfkleapdadelpraefdpgqdtyqhppkdssgqr
>d1c9ga_ 4.71.1.7.4 Snake venom metalloprotease {Snake (Bothrops jararaca), jararhagin}
ydpykyieffvvvdqgtvtknngdldkikarmyelanivneifrylymhvalvgleiwsn
gdkitvkpdvdytlnsfaewrktdlltrkkhdnaqlltaidfngptigyayigsmchpkr
svgivqdyspinlvvavimahemghnlgihhdtgscscgdypcimgptisnepskffsnc
syiqcwdfimnhnpeciinep
>d1c9ja_ 3.33.1.1.6 Subtilisin BL {Bacillus lentus}
aqsvpwgisrvqapaahnrgltgsgvrvavldtgisthpdlnirggasfvpgepstqdgn
ghgthvagtiaalnnsigvlgvapsaelyavkvlgasgsgsyssiaqglewagnngmhva
slslgspspsatleqavnsatsrgvlvvaasgnsgagsisyparyanamavgatdqnnnr
asfsqygagldivapgvnvqstypgstyaslngtsmatphvagaaalvkqknpswsnvqi
rnhlkntatslgstnlygsglvnaeaaar
>d1c9ka_ 3.30.1.9.5 Adenosylcobinamide kinase/adenosylcobinamide phosphate guanylyltransferase CobU {Salmonella typhimurium}
milvtggarsgksrhaealigdapqvlyiatsqilddemaariqhhkdgrpahwrtaecw
rhldtlitadlapddaillecittmvtnllfalggendpeqwdyaameraiddeiqilia
acqrcpakvvlvtnevgmgivpenrlarhfrdiagrvnqrlaaaadevwlvvsgigvkik
>d1c9kb_ 3.30.1.9.5 Adenosylcobinamide kinase/adenosylcobinamide phosphate guanylyltransferase CobU {Salmonella typhimurium}
milvtggarsgksrhaealigdapqvlyiatsqilddemaariqhhkdgrpahwrtaecw
rhldtlitadlapddaillecittmvtnllfalggendpeqwdyaameraiddeiqilia
acqrcpakvvlvtnevgmgivpenrlarhfrdiagrvnqrlaaaadevwlvvsgigvkik
>d1c9kc_ 3.30.1.9.5 Adenosylcobinamide kinase/adenosylcobinamide phosphate guanylyltransferase CobU {Salmonella typhimurium}
milvtggarsgksrhaealigdapqvlyiatsqilddemaariqhhkdgrpahwrtaecw
rhldtlitadlapddaillecittmvtnllfalggendpeqwdyaameraiddeiqilia
acqrcpakvvlvtnevgmgivpenrlarhfrdiagrvnqrlaaaadevwlvvsgigvkik
>d1c9ma_ 3.33.1.1.6 Subtilisin BL {Bacillus lentus}
aqsvpwgisrvqapaahnrgltgsgvkvavldtgisthpdlnirggasfvpgepstqdgn
ghgthvagtiaaldnsigvlgvapsaelyavkvlgasgsgaissiaqglewagnngmhva
nlslgspspsatleqavnsatsrgvlvvaasgnsgagsisyparyanamavgatdqnnnr
asfsqygagldivapgvnvqstypgstyaslngtxmatphvagaaalvkqknpswsnvqi
rnhlkntatslgstnlygsglvnaeaatr
>d1c9na_ 3.33.1.1.6 Subtilisin BL {Bacillus lentus}
aqsvpwgisrvqapaahnrgltgsgvrvavldtgisthpdlnirggasfvpgepstqdgn
ghgthvagtiaalnnsigvlgvapsaelyavkvlgasgsgsyssiaqglewagnngmhva
slslgspspsatleqavnsatsrgvlvvaasgnsgagsisyparyanamavgatdqnnnr
asfsqygagldivapgvnvqstypgstyaslngtxmatphvagaaalvkqknpswsnvqi
rnhlkntatslgstnlygsglvnaeaaar
>d1c9ra1 3.46.3.1.4 (430-558) HIV RNase H (Domain of reverse transcriptase) {Human immunodeficiency virus, type 1}
ekepivgaetfyvdgaanaatklgkagyvtnkgrqkvvpltnttnqktelqaiylalqds
glevnivtdsqyalgiiqaqpdkseselvnqiiealikkeavylawvpahagiggnaavd
alvsagiaa
>d1c9ra2 5.8.1.2.2 (1-429) HIV-1 reverse transcriptase {Human immunodeficiency virus, type 1, HIV-1}
pispietvpvklapgmdgpkvkqwpltaeaiaalvaictameaegkiskigpenpyntpv
faikkaaaaaaaalvdfrelnkrtqdfwevqlgiphpaglkkkksvtvldvgdayfsvpl
dedfrkytaftipsianatpgiryqynvlpqgwkgspaifqssmtkilepfkkqnpdivi
yqyiddlyvgsdleigqhatkiaelrqhllawglttpdkkhaaeppflwmgyelhpdawt
vapaalaaaasaavndiqklvgklnwasqiypgiavralsaaaagtkaaaeaaaataaaa
lalaaarealaapvhgvyydpskdliaeiqaqgqgqwtyqiyqepfknlktgkyarmrga
htndvkqlteavqkittesiviwgktpkfklpiqketwetwwteywqatwipewefvntp
plvklwyql
>d1c9rb1 5.8.1.2.2 HIV-1 reverse transcriptase {Human immunodeficiency virus, type 1, HIV-1}
pispietvpvklapgmdgpkvkqwplteekikalveictemekegkiskigpenpyntpv
faikkkdstkwrklvdfrelnkrtqdfweaalgiphpaglkkkksvtvldvgdayfsvpl
dedfrkytaftipsinnetpgiryqynvlpqgwkgspaifqssmtkilepfkaqnpdivi
yqyiddlyvgsdleigqhrtkieelrqhllrwglttpdkkhqkeppflwmgyelhpdkwa
aaaaaaaaaaaatvndiqklvgklnwaaqiypgiaaaalsaalagtkaltaaapltaaaa
lelaanraaaaaaaagvyydpskdliaeiqkqgqgqwtyqiyqepfknlktgkyarmrga
htndvkqlteavqkittesiviwgktpkfklpiqketwetwwteywqatwipewefvntp
plvalwyale
>d1c9rh1 2.1.1.1.112 (1-123) Immunoglobulin (variable domains of L and H chains) {Fab 28 against HIV-1 RT (mouse), kappa L chain}
qitlkesgpgivqpsqpfrltctfsgfslstsgigvtwirqpsgkglewlatiwwdddnr
ynpslksrltvskdtsnnqaflnmmtvetadtaiyycaqsaitsvtdsamdhwgqgtsvt
vss
>d1c9rh2 2.1.1.2.111 (124-220) Immunoglobulin (constant domains of L and H chains) {Fab 28 against HIV-1 RT (mouse), kappa L chain}
aattppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpsstwpsetvtcnvahpasstkvdkki
>d1c9rl1 2.1.1.1.112 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab 28 against HIV-1 RT (mouse), kappa L chain}
diqmtqttsslsaslgdrvtiscsasqdissylnwyqqkpegtvklliyytsslhsgvps
afsgsgsgtdysltisnlepedfatyycqqyskfpwtfgggtkleik
>d1c9rl2 2.1.1.2.111 (108-214) Immunoglobulin (constant domains of L and H chains) {Fab 28 against HIV-1 RT (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvawaidgsaaangvlnswtdqd
skdstysmsstltltadeyeaansytcaathktstspivksfnanec
>d1c9sa_ 2.73.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
sdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqtr
hgviesegk
>d1c9sb_ 2.73.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
sdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqtr
hgvieseg
>d1c9sc_ 2.73.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
nsdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqt
rhgvieseg
>d1c9sd_ 2.73.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
sdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqtr
hgviesegk
>d1c9se_ 2.73.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
sdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqtr
hgvieseg
>d1c9sf_ 2.73.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
sdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqtr
hgviesegk
>d1c9sg_ 2.73.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
nsdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqt
rhgviesegk
>d1c9sh_ 2.73.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
sdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqtr
hgviesegk
>d1c9si_ 2.73.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
sdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqtr
hgviesegk
>d1c9sj_ 2.73.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
sdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqtr
hgviese
>d1c9sk_ 2.73.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
sdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqtr
hgviesegk
>d1c9sl_ 2.73.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
tnsdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiq
trhgvieseg
>d1c9sm_ 2.73.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
tnsdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiq
trhgviesegk
>d1c9sn_ 2.73.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
tnsdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiq
trhgvieseg
>d1c9so_ 2.73.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
tnsdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiq
trhgviesegk
>d1c9sp_ 2.73.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
tnsdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiq
trhgvieseg
>d1c9sq_ 2.73.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
tnsdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiq
trhgvieseg
>d1c9sr_ 2.73.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
tnsdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiq
trhgvieseg
>d1c9ss_ 2.73.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
tnsdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiq
trhgvieseg
>d1c9st_ 2.73.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
tnsdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiq
trhgvieseg
>d1c9su_ 2.73.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
tnsdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiq
trhgvieseg
>d1c9sv_ 2.73.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
tnsdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiq
trhgvieseg
>e1ca0.1b 2.41.1.2.7 (alpha,gamma)-chymotrypsin(ogen) {Bovine (Bos taurus)}
ivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgvttsdvvvagefdqgs
ssekiqklkiakvfknskynsltinnditllklstaasfsqtvsavclpsasddfaagtt
cvttgwgltry
>e1ca0.1c 2.41.1.2.7 (alpha,gamma)-chymotrypsin(ogen) {Bovine (Bos taurus)}
antpdrlqqaslpllsntnckkywgtkikdamicagasgvsscmgdsggplvckkngawt
lvgivswgsstcststpgvyarvtalvnwvqqtlaan
>e1ca0.2g 2.41.1.2.7 (alpha,gamma)-chymotrypsin(ogen) {Bovine (Bos taurus)}
ivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgvttsdvvvagefdqgs
ssekiqklkiakvfknskynsltinnditllklstaasfsqtvsavclpsasddfaagtt
cvttgwgltry
>e1ca0.2h 2.41.1.2.7 (alpha,gamma)-chymotrypsin(ogen) {Bovine (Bos taurus)}
antpdrlqqaslpllsntnckkywgtkikdamicagasgvsscmgdsggplvckkngawt
lvgivswgsstcststpgvyarvtalvnwvqqtlaan
>d1ca0d_ 7.8.1.1.4 Alzheimer's amyloid B-protein precursor, APPI {Human (Homo sapiens)}
evcseqaetgpcramisrwyfdvtegkcapffyggcggnrnnfdteeycmavcg
>d1ca0i_ 7.8.1.1.4 Alzheimer's amyloid B-protein precursor, APPI {Human (Homo sapiens)}
evcseqaetgpcramisrwyfdvtegkcapffyggcggnrnnfdteeycmavcg
>d1ca1_1 1.115.1.1.2 (1-249) Alpha-toxin, N-terminal domain {Clostridium perfringens}
wdgkidgtgthamivtqgvsilendlsknepesvrknleilkenmhelqlgstypdydkn
aydlyqdhfwdpdtdnnfskdnswylaysipdtgesqirkfsalaryewqrgnykqatfy
lgeamhyfgdidtpyhpanvtavdsaghvkfetfaeerkeqykintvgcktnedfyadil
knkdfnawskeyargfaktgksiyyshasmshswddwdyaakvtlansqkgtagyiyrfl
hdvsegndp
>d1ca1_2 2.11.1.3.1 (250-370) Alpha-toxin, C-terminal domain {Clostridium perfringens}
svgknvkelvayistsgekdagtddymyfgiktkdgktqewemdnpgndfmtgskdtytf
klkdenlkiddiqnmwirkrkytafpdaykpenikviangkvvvdkdinewisgnstyni
k
>d1ca2__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasf
>d1ca3__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1ca4a1 2.7.1.1.1 (350-501) TNF receptor associated factor 2 (TRAF2) {Human (Homo sapiens)}
ydgvfiwkisdfarkrqeavagripaifspafytsrygykmclriylngdgtgrgthlsl
ffvvmkgpndallrwpfnqkvtlmlldqnnrehvidafrpdvtsssfqrpvndmniasgc
plfcpvskmeaknsyvrddaifikaivdltgl
>d1ca4b1 2.7.1.1.1 (350-501) TNF receptor associated factor 2 (TRAF2) {Human (Homo sapiens)}
ydgvfiwkisdfarkrqeavagripaifspafytsrygykmclriylngdgtgrgthlsl
ffvvmkgpndallrwpfnqkvtlmlldqnnrehvidafrpdvtsssfqrpvndmniasgc
plfcpvskmeaknsyvrddaifikaivdltgl
>d1ca4c1 2.7.1.1.1 (350-501) TNF receptor associated factor 2 (TRAF2) {Human (Homo sapiens)}
ydgvfiwkisdfarkrqeavagripaifspafytsrygykmclriylngdgtgrgthlsl
ffvvmkgpndallrwpfnqkvtlmlldqnnrehvidafrpdvtsssfqrpvndmniasgc
plfcpvskmeaknsyvrddaifikaivdltgl
>d1ca4d1 2.7.1.1.1 (350-501) TNF receptor associated factor 2 (TRAF2) {Human (Homo sapiens)}
ydgvfiwkisdfarkrqeavagripaifspafytsrygykmclriylngdgtgrgthlsl
ffvvmkgpndallrwpfnqkvtlmlldqnnrehvidafrpdvtsssfqrpvndmniasgc
plfcpvskmeaknsyvrddaifikaivdltgl
>d1ca4e1 2.7.1.1.1 (350-501) TNF receptor associated factor 2 (TRAF2) {Human (Homo sapiens)}
ydgvfiwkisdfarkrqeavagripaifspafytsrygykmclriylngdgtgrgthlsl
ffvvmkgpndallrwpfnqkvtlmlldqnnrehvidafrpdvtsssfqrpvndmniasgc
plfcpvskmeaknsyvrddaifikaivdltgl
>d1ca4f1 2.7.1.1.1 (350-501) TNF receptor associated factor 2 (TRAF2) {Human (Homo sapiens)}
ydgvfiwkisdfarkrqeavagripaifspafytsrygykmclriylngdgtgrgthlsl
ffvvmkgpndallrwpfnqkvtlmlldqnnrehvidafrpdvtsssfqrpvndmniasgc
plfcpvskmeaknsyvrddaifikaivdltgl
>d1ca7a_ 4.60.1.3.1 Microphage migration inhibition factor (MIF) {Human (Homo sapiens)}
pmfivntnvprasvpdgflseltqqlaqatgkppqyiavhvvpdqlmafggssepcalcs
lhsigkiggaqnrsyskllcgllaerlrispdrvyinyydmnaanvgwnnstfa
>d1ca7b_ 4.60.1.3.1 Microphage migration inhibition factor (MIF) {Human (Homo sapiens)}
pmfivntnvprasvpdgflseltqqlaqatgkppqyiavhvvpdqlmafggssepcalcs
lhsigkiggaqnrsyskllcgllaerlrispdrvyinyydmnaanvgwnnstfa
>d1ca7c_ 4.60.1.3.1 Microphage migration inhibition factor (MIF) {Human (Homo sapiens)}
pmfivntnvprasvpdgflseltqqlaqatgkppqyiavhvvpdqlmafggssepcalcs
lhsigkiggaqnrsyskllcgllaerlrispdrvyinyydmnaanvgwnnstfa
>e1ca8.1a 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1ca8.1b 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>d1ca9a1 2.7.1.1.1 (350-501) TNF receptor associated factor 2 (TRAF2) {Human (Homo sapiens)}
ydgvfiwkisdfarkrqeavagripaifspafytsrygykmclriylngdgtgrgthlsl
ffvvmkgpndallrwpfnqkvtlmlldqnnrehvidafrpdvtsssfqrpvndmniasgc
plfcpvskmeaknsyvrddaifikaivdltgl
>d1ca9b1 2.7.1.1.1 (350-501) TNF receptor associated factor 2 (TRAF2) {Human (Homo sapiens)}
ydgvfiwkisdfarkrqeavagripaifspafytsrygykmclriylngdgtgrgthlsl
ffvvmkgpndallrwpfnqkvtlmlldqnnrehvidafrpdvtsssfqrpvndmniasgc
plfcpvskmeaknsyvrddaifikaivdltgl
>d1ca9c1 2.7.1.1.1 (350-501) TNF receptor associated factor 2 (TRAF2) {Human (Homo sapiens)}
ydgvfiwkisdfarkrqeavagripaifspafytsrygykmclriylngdgtgrgthlsl
ffvvmkgpndallrwpfnqkvtlmlldqnnrehvidafrpdvtsssfqrpvndmniasgc
plfcpvskmeaknsyvrddaifikaivdltgl
>d1ca9d1 2.7.1.1.1 (350-501) TNF receptor associated factor 2 (TRAF2) {Human (Homo sapiens)}
ydgvfiwkisdfarkrqeavagripaifspafytsrygykmclriylngdgtgrgthlsl
ffvvmkgpndallrwpfnqkvtlmlldqnnrehvidafrpdvtsssfqrpvndmniasgc
plfcpvskmeaknsyvrddaifikaivdltgl
>d1ca9e1 2.7.1.1.1 (350-501) TNF receptor associated factor 2 (TRAF2) {Human (Homo sapiens)}
ydgvfiwkisdfarkrqeavagripaifspafytsrygykmclriylngdgtgrgthlsl
ffvvmkgpndallrwpfnqkvtlmlldqnnrehvidafrpdvtsssfqrpvndmniasgc
plfcpvskmeaknsyvrddaifikaivdltgl
>d1ca9f1 2.7.1.1.1 (350-501) TNF receptor associated factor 2 (TRAF2) {Human (Homo sapiens)}
ydgvfiwkisdfarkrqeavagripaifspafytsrygykmclriylngdgtgrgthlsl
ffvvmkgpndallrwpfnqkvtlmlldqnnrehvidafrpdvtsssfqrpvndmniasgc
plfcpvskmeaknsyvrddaifikaivdltgl
>d1caa__ 7.35.4.1.5 Rubredoxin {Pyrococcus furiosus}
akwvckicgyiydedagdpdngispgtkfeelpddwvcpicgapksefekled
>d1cad__ 7.35.4.1.5 Rubredoxin {Pyrococcus furiosus}
akwvckicgyiydedagdpdngispgtkfeelpddwvcpicgapksefekled
>d1cah__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnn
ghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvh
wntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprg
llpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvd
nwrpaqplknrqikasfk
>d1cai__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnn
ghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsahtvdkkkyaaelhlvh
wntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprg
llpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvd
nwrpaqplknrqikasfk
>d1caj__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnn
ghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsdhtvdkkkyaaelhlvh
wntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprg
llpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvd
nwrpaqplknrqikasfk
>d1cak__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnn
ghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsqhtvdkkkyaaelhlvh
wntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprg
llpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvd
nwrpaqplknrqikasfk
>d1cal__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnn
ghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvh
wntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprg
llpesldywtypgslatppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvd
nwrpaqplknrqikasfk
>d1cam__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnn
ghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvh
wntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprg
llpesldywtypgslatppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvd
nwrpaqplknrqikasfk
>d1can__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
xshhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslril
nnghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhl
vhwntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdp
rgllpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelm
vdnwrpaqplknrqikasfk
>d1cao__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
xshhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslril
nnghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhl
vhwntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdp
rgllpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelm
vdnwrpaqplknrqikasfk
>d1caqa_ 4.71.1.9.4 Stromelysin-1 (MMP-3) {Human (Homo sapiens), fibroblast}
frtfpgipkwrkthltyrivnytpdlpkdavdsavekalkvweevtpltfsrlyegeadi
misfavrehgdfypfdgpgnvlahayapgpgingdahfdddeqwtkdttgtnlflvaahe
ighslglfhsantealmyplyhsltdltrfrlsqddingiqslygppp
>d1caua_ 2.73.1.1.2 Canavalin 7S vicilin {Jack bean (Canavalia ensiformis)}
aqnnpylfrsnkfltlfknqhgslrllqrfnedteklenlrdyrvleycskpntlllphh
sdsdllvlvlegqailvlvnpdgrdtykldqgdaikiqagtpfylinpdnnqnlrilkfa
itfrrpgtvedfflsstkrlpsylsafsknfleasydspydeieqtllqeeqegvivkmp
k
>d1caub_ 2.73.1.1.2 Canavalin 7S vicilin {Jack bean (Canavalia ensiformis)}
tlssqdkpfnlrsrdpiysnnygklyeitpeknsqlrdldillnclqmnegalfvphyns
ratvilvanegraevelvgleqqqqqglesmqlrryaatlsegdiivipssfpvalkaas
dlnmvgigvnaennernflaghkenvirqiprqvsdltfpgsgeeveellenqkesyfvd
gqpr
>d1cava_ 2.73.1.1.2 Canavalin 7S vicilin {Jack bean (Canavalia ensiformis)}
aqnnpylfrsnkfltlfknqhgslrllqrfnedteklenlrdyrvleycskpntlllphh
sdsdllvlvlegqailvlvnpdgrdtykldqgdaikiqagtpfylinpdnnqnlrilkfa
itfrrpgtvedfflsstkrlpsylsafsknfleasydspydeieqtllqeeqegvivkmp
k
>d1cavb_ 2.73.1.1.2 Canavalin 7S vicilin {Jack bean (Canavalia ensiformis)}
tlssqdkpfnlrsrdpiysnnygklyeitpeknsqlrdldillnclqmnegalfvphyns
ratvilvanegraevelvgleqqqqqglesmqlrryaatlsegdiivipssfpvalkaas
dlnmvgigvnaennernflaghkenvirqiprqvsdltfpgsgeeveellenqkesyfvd
gqpr
>d1cawa_ 2.73.1.1.2 Canavalin 7S vicilin {Jack bean (Canavalia ensiformis)}
aqnnpylfrsnkfltlfknqhgslrllqrfnedteklenlrdyrvleycskpntlllphh
sdsdllvlvlegqailvlvnpdgrdtykldqgdaikiqagtpfylinpdnnqnlrilkfa
itfrrpgtvedfflsstkrlpsylsafsknfleasydspydeieqtllqeeqegvivkmp
k
>d1cawb_ 2.73.1.1.2 Canavalin 7S vicilin {Jack bean (Canavalia ensiformis)}
tlssqdkpfnlrsrdpiysnnygklyeitpeknsqlrdldillnclqmnegalfvphyns
ratvilvanegraevelvgleqqqqqglesmqlrryaatlsegdiivipssfpvalkaas
dlnmvgigvnaennernflaghkenvirqiprqvsdltfpgsgeeveellenqkesyfvd
gqpr
>d1caxa_ 2.73.1.1.2 Canavalin 7S vicilin {Jack bean (Canavalia ensiformis)}
aqnnpylfrsnkfltlfknqhgslrllqrfnedteklenlrdyrvleycskpntlllphh
sdsdllvlvlegqailvlvnpdgrdtykldqgdaikiqagtpfylinpdnnqnlrilkfa
itfrrpgtvedfflsstkrlpsylsafsknfleasydspydeieqtllqeeqegvivkmp
k
>d1caxb_ 2.73.1.1.2 Canavalin 7S vicilin {Jack bean (Canavalia ensiformis)}
tlssqdkpfnlrsrdpiysnnygklyeitpeknsqlrdldillnclqmnegalfvphyns
ratvilvanegraevelvgleqqqqqglesmqlrryaatlsegdiivipssfpvalkaas
dlnmvgigvnaennernflaghkenvirqiprqvsdltfpgsgeeveellenqkesyfvd
gqpr
>d1caxc_ 2.73.1.1.2 Canavalin 7S vicilin {Jack bean (Canavalia ensiformis)}
aqnnpylfrsnkfltlfknqhgslrllqrfnedteklenlrdyrvleycskpntlllphh
sdsdllvlvlegqailvlvnpdgrdtykldqgdaikiqagtpfylinpdnnqnlrilkfa
itfrrpgtvedfflsstkrlpsylsafsknfleasydspydeieqtllqeeqegvivkmp
k
>d1caxd_ 2.73.1.1.2 Canavalin 7S vicilin {Jack bean (Canavalia ensiformis)}
tlssqdkpfnlrsrdpiysnnygklyeitpeknsqlrdldillnclqmnegalfvphyns
ratvilvanegraevelvgleqqqqqglesmqlrryaatlsegdiivipssfpvalkaas
dlnmvgigvnaennernflaghkenvirqiprqvsdltfpgsgeeveellenqkesyfvd
gqpr
>d1caxe_ 2.73.1.1.2 Canavalin 7S vicilin {Jack bean (Canavalia ensiformis)}
aqnnpylfrsnkfltlfknqhgslrllqrfnedteklenlrdyrvleycskpntlllphh
sdsdllvlvlegqailvlvnpdgrdtykldqgdaikiqagtpfylinpdnnqnlrilkfa
itfrrpgtvedfflsstkrlpsylsafsknfleasydspydeieqtllqeeqegvivkmp
k
>d1caxf_ 2.73.1.1.2 Canavalin 7S vicilin {Jack bean (Canavalia ensiformis)}
tlssqdkpfnlrsrdpiysnnygklyeitpeknsqlrdldillnclqmnegalfvphyns
ratvilvanegraevelvgleqqqqqglesmqlrryaatlsegdiivipssfpvalkaas
dlnmvgigvnaennernflaghkenvirqiprqvsdltfpgsgeeveellenqkesyfvd
gqpr
>d1cay__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnn
ghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvh
wntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprg
llpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvd
nwrpaqplknrqikasfk
>d1caz__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnn
ghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsqhtvdkkkyaaelhlvh
wntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprg
llpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvd
nwrpaqplknrqikasfk
>d1cb0a_ 3.47.1.1.4 5'-deoxy-5'-methylthioadenosine phosphorylase {Human (Homo sapiens)}
avkigiiggtglddpeilegrtekyvdtpfgkpsdalilgkiknvdcvllarhgrqhtim
pskvnyqaniwalkeegcthvivttacgslreeiqpgdiviidqfidrttmrpqsfydgs
hscargvchipmaepfcpktrevlietakklglrchskgtmvtiegprfssraesfmfrt
wgadvinmttvpevvlakeagicyasiamatdydcwkeheeavsvdrvlktlkenankak
slllttipqigstewsetlhnlknmaqfsvllp
>d1cb1__ 1.42.1.1.2 Calbindin D9K {Porcine (Sus scrofa)}
saqkspaelksifekyaakegdpnqlskeelkqliqaefpsllkgprtlddlfqeldkng
dgevsfeefqvlvkkisq
>d1cb2a_ 3.5.1.1.2 Cellobiohydrolase II (Cel6a) {Trichoderma reesei}
tatysgnpfvgvtpwanayyasevsslaipsltgamataaaavakvpsfmwldtldktpl
meqtladirtanknggnyagqfvvfdlpdrdcaalasngeysiadggvakyknyidtirq
ivveysdirtllviepdslanlvtnlgtpkcanaqsaylecinyavtqlnlpnvamylda
ghagwlgwpanqdpaaqlfanvyknasspralrglatnvanyngwnitsppsytqgnavy
neklyihaigpllanhgwsnaffitdqgrsgkqptgqqqwgdwcnvigtgfgirpsantg
dslldsfvwvkpggecdgtsdssaprfdshcalpdalqpapqagawfqayfvqlltnanp
sfl
>d1cb2b_ 3.5.1.1.2 Cellobiohydrolase II (Cel6a) {Trichoderma reesei}
tatysgnpfvgvtpwanayyasevsslaipsltgamataaaavakvpsfmwldtldktpl
meqtladirtanknggnyagqfvvfdlpdrdcaalasngeysiadggvakyknyidtirq
ivveysdirtllviepdslanlvtnlgtpkcanaqsaylecinyavtqlnlpnvamylda
ghagwlgwpanqdpaaqlfanvyknasspralrglatnvanyngwnitsppsytqgnavy
neklyihaigpllanhgwsnaffitdqgrsgkqptgqqqwgdwcnvigtgfgirpsantg
dslldsfvwvkpggecdgtsdssaprfdshcalpdalqpapqagawfqayfvqlltnanp
sfl
>d1cb4a_ 2.1.8.1.2 Cu,Zn superoxide dismutase, SOD {Human (Homo sapiens)}
atkavcvlkgdgpvqgtihfeakgdtvvvtgsitgltegdhgfhvhqfgdntqgctsagp
hfnplskkhggpkdderhvgdlgnvtadkngvaivdivdplislsgeysiigrtmvvhek
pddlgrggneestktgnagsrlacgvigiak
>d1cb4b_ 2.1.8.1.2 Cu,Zn superoxide dismutase, SOD {Human (Homo sapiens)}
atkavcvlkgdgpvqgtihfeakgdtvvvtgsitgltegdhgfhvhqfgdntqgctsagp
hfnplskkhggpkdderhvgdlgnvtadkngvaivdivdplislsgeysiigrtmvvhek
pddlgrggneestktgnagsrlacgvigiak
>d1cb6a1 3.84.1.2.1 (1001-1334) Lactoferrin {Human (Homo sapiens)}
grrrsvqwcavsqpeatkcfqwqrnmrkvrgppvscikrdspiqciqaiaenradavtld
ggfiyeaglapyklrpvaaevygterqprthyyavavvkkggsfqlnelqglkschtglr
rtagwnvpigtlrpflnwtgppepieaavarffsascvpgadkgqfpnlcrlcagtgenk
cafssqepyfsysgafkclrdgagdvafirestvfedlsdeaerdeyellcpdntrkpvd
kfkdchlarvpshavvarsvngkedaiwnllrqaqekfgkdkspkfqlfgspsgqkdllf
kdsaigfsrvppridsglylgsgyftaiqnlrks
>d1cb6a2 3.84.1.2.1 (1335-1691) Lactoferrin {Human (Homo sapiens)}
eeevaarrarvvwcavgeqelrkcnqwsglsegsvtcssasttedcialvlkgeadamsl
dggyvytagkcglvpvlaenyksqqssdpdpncvdrpvegylavavvrrsdtsltwnsvk
gkkschtavdrtagwnipmgllfnqtgsckfdeyfsqscapgsdprsnlcalcigdeqge
nkcvpnsneryygytgafrclaenagdvafvkdvtvlqntdgnnneawakdlkladfall
cldgkrkpvtearschlamapnhavvsrmdkverlkqvllhqqakfgrngsdcpdkfclf
qsetknllfndnteclarlhgkttyekylgpqyvagitnlkkcstsplleaceflrk
>d1cb8a1 1.98.2.2.1 (26-335) Chondroitinase AC, N-terminal domain {Flavobacterium heparinum}
gtaelimkrvmldlkkplrnmdkvaeknlntlqpdgswkdvpykddamtnwlpnnhllql
etiiqayiekdshyygddkvfdqiskafkywydsdpksrnwwhneiatpqalgemlilmr
ygkkpldealvhkltermkrgepekktganktdialhyfyralltsdeallsfavkelfy
pvqfvhyeeglqydysylqhgpqlqissygavfitgvlklanyvrdtpyalsteklaifs
kyyrdsylkairgsymdfnvegrgvsrpdilnkkaekkrllvakmidlkhteewadaiar
tdstvaagyk
>d1cb8a2 2.22.1.1.1 (600-700) Chondroitinase AC, C-terminal domain {Flavobacterium heparinum}
pkvlantnqlqavyhqqldmvqaifytagklsvagieietdkpcavlikhingkqviwaa
dplqkektavlsirdlktgktnrvkidfpqqefagatvelk
>d1cb8a3 2.27.3.1.1 (336-599) Chondroitinase AC, central domain {Flavobacterium heparinum}
iepyhhqfwngdyvqhlrpaysfnvrmvskrtrrsesgnkenllgrylsdgatniqlrgp
eyynimpvwewdkipgitsrdyltdrpltklwgeqgsndfaggvsdgvygasayaldyds
lqakkawfffdkeivclgaginsnapenitttlnqswlngpvistagktgrgkittfkaq
gqfwllhdaigyyfpeganlslstqsqkgnwfhinnshskdevsgdvfklwinhgarpen
aqyayivlpginkpeeikkyngta
>d1cb9a_ 7.7.1.1.16 Cardiotoxin II {Central asian cobra (Naja naja oxiana)}
lkckklvplfsktcpagknlcykmfmvaaphvpvkrgcidvcpkssllvkyvccntdkcn
>d1cbf__ 3.80.1.1.1 Cobalt precorrin-4 methyltransferase CbiF {Bacillus megaterium}
glvprgshmklyiigagpgdpdlitvkglkllqqadvvlyadslvsqdliakskpgaevl
ktagmhleemvgtmldrmregkmvvrvhtgdpamygaimeqmvllkregvdieivpgvts
vfaaaaaaeaeltipdltqtviltraegrtpvpefekltdlakhkctialflsstltkkv
mkefinagwsedtpvvvvykatwpdekivrttvkdlddamrtngirkqamilagwaldp
>d1cbg__ 3.1.7.4.2 Cyanogenic beta glucosidase {Creeping white clover (Trifolium repens)}
fkplpisfddfsdlnrscfapgfvfgtassafqyegaafedgkgpsiwdtfthkypekik
drtngdvaideyhrykedigimkdmnldayrfsiswprvlpkgklsggvnreginyynnl
inevlangmqpyvtlfhwdvpqaledeyrgflgrnivddfrdyaelcfkefgdrvkhwit
lnepwgvsmnayaygtfapgrcsdwlklnctggdsgrepylaahyqllahaaaarlyktk
yqasqngiigitlvshwfepaskekadvdaakrgldfmlgwfmhpltkgrypesmrylvr
krlpkfsteeskeltgsfdflglnyyssyyaakapripnarpaiqtdslinatfehngkp
lgpmaasswlciypqgirklllyvknhynnpviyitengrnefndptlslqeslldtpri
dyyyrhlyyvltaigdgvnvkgyfawslfdnmewdsgytvrfglvfvdfknnlkrhpkls
ahwfksflkk
>d1cbh__ 7.3.8.1.1 Cellobiohydrolase I {Trichoderma reesei, ct-cbh I}
tqshygqcggigysgptvcasgttcqvlnpyysqcl
>d1cbia_ 2.53.1.2.10 Cellular retinoic-acid-binding protein (CRABP) {Bovine/murine (identical sequences) (Bos taurus/Mus musculus), CRABP-I}
pnfagtwkmrssenfdellkalgvnamlrkvavaaaskphveirqdgdqfyiktsttvrt
teinfkvgegfeeetvdgrkcrslptwenenkihctqtllegdgpktywtrelandelil
tfgaddvvctriyvre
>d1cbib_ 2.53.1.2.10 Cellular retinoic-acid-binding protein (CRABP) {Bovine/murine (identical sequences) (Bos taurus/Mus musculus), CRABP-I}
pnfagtwkmrssenfdellkalgvnamlrkvavaaaskphveirqdgdqfyiktsttvrt
teinfkvgegfeeetvdgrkcrslptwenenkihctqtllegdgpktywtrelandelil
tfgaddvvctriyvre
>d1cbja_ 2.1.8.1.1 Cu,Zn superoxide dismutase, SOD {Bovine (Bos taurus)}
atkavcvlkgdgpvqgtihfeakgdtvvvtgsitgltegdhgfhvhqfgdntqgctsagp
hfnplskkhggpkdeerhvgdlgnvtadkngvaivdivdplislsgeysiigrtmvvhek
pddlgrggneestktgnagsrlacgvigiak
>d1cbjb_ 2.1.8.1.1 Cu,Zn superoxide dismutase, SOD {Bovine (Bos taurus)}
atkavcvlkgdgpvqgtihfeakgdtvvvtgsitgltegdhgfhvhqfgdntqgctsagp
hfnplskkhggpkdeerhvgdlgnvtadkngvaivdivdplislsgeysiigrtmvvhek
pddlgrggneestktgnagsrlacgvigiak
>d1cbla_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1cblb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1cblc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1cbld_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1cbma_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1cbmb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1cbmc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1cbmd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1cbn__ 7.13.1.1.1 Crambin {Abyssinian cabbage (Crambe abyssinica)}
ttccpsivarsnfnvcrlpgtpealcatytgciiipgatcpgdyan
>d1cboa1 3.3.1.2.2 (9-318,451-506) Cholesterol oxidase {Streptomyces}
gyvpavvigtgygaavsalrlgeagvqtlmlemgqlwnqpgpdgnifcgmlnpdkrsswf
knrteaplgsflwldvvnrnidpyagvldrvnydqmsvyvgrgvgggslvnggmavepkr
syfeeilprvdssemydryfpransmlrvnhidtkwfedtewykfarvsreqagkaglgt
vfvpnvydfgymqreaagevpksalateviygnnhgkqsldktylaaalgtgkvtiqtlh
qvktirqtkdggyaltveqkdtdgkllatkeiscrylflgagslgstellvrardtgtlp
nlnsevgagwXgcvlgkatddygrvagyknlyvtdgslipgsvgvnpfvtitalaernve
riikqdv
>d1cboa2 4.14.1.1.2 (319-450) Cholesterol oxidase {Streptomyces}
gpngnimtaranhmwnptgahqssipalgidawdnsdssvfaeiapmpagletwvslyla
itknpqrgtfvydaatdraklnwtrdqnapavnaakalfdrinkangtiyrydlfgtqlk
afaddfcynplg
>d1cbq__ 2.53.1.2.9 Cellular retinoic-acid-binding protein (CRABP) {Human (Homo sapiens), CRABP-II}
pnfsgnwkiirsenfeellkvlgvnvmlrkiavaaaskpaveikqegdtfyiktsttvrt
teinfkvgeefeeqtvdgrpckslvkwesenkmvceqkllkgegpktswtreltndgeli
ltmtaddvvctrvyvre
>d1cbra_ 2.53.1.2.10 Cellular retinoic-acid-binding protein (CRABP) {Bovine/murine (identical sequences) (Bos taurus/Mus musculus), CRABP-I}
pnfagtwkmrssenfdellkalgvnamlrkvavaaaskphveirqdgdqfyiktsttvrt
teinfkvgegfeeetvdgrkcrslptwenenkihctqtllegdgpktywtrelandelil
tfgaddvvctriyvre
>d1cbrb_ 2.53.1.2.10 Cellular retinoic-acid-binding protein (CRABP) {Bovine/murine (identical sequences) (Bos taurus/Mus musculus), CRABP-I}
pnfagtwkmrssenfdellkalgvnamlrkvavaaaskphveirqdgdqfyiktsttvrt
teinfkvgegfeeetvdgrkcrslptwenenkihctqtllegdgpktywtrelandelil
tfgaddvvctriyvre
>d1cbs__ 2.53.1.2.9 Cellular retinoic-acid-binding protein (CRABP) {Human (Homo sapiens), CRABP-II}
pnfsgnwkiirsenfeellkvlgvnvmlrkiavaaaskpaveikqegdtfyiktsttvrt
teinfkvgeefeeqtvdgrpckslvkwesenkmvceqkllkgegpktswtreltndgeli
ltmtaddvvctrvyvre
>d1cbua_ 3.30.1.9.5 Adenosylcobinamide kinase/adenosylcobinamide phosphate guanylyltransferase CobU {Salmonella typhimurium}
milvtggarsgksrhaealigdapqvlyiatsqilddemaariqhhkdgrpahwrtaecw
rhldtlitadlapddaillecittmvtnllfalggendpeqwdyaameraiddeiqilia
acqrcpakvvlvtnevgmgivpenrlarhfrdiagrvnqrlaaaadevwlvvsgigvkik
>d1cbub_ 3.30.1.9.5 Adenosylcobinamide kinase/adenosylcobinamide phosphate guanylyltransferase CobU {Salmonella typhimurium}
milvtggarsgksrhaealigdapqvlyiatsqilddemaariqhhkdgrpahwrtaecw
rhldtlitadlapddaillecittmvtnllfalggendpeqwdyaameraiddeiqilia
acqrcpakvvlvtnevgmgivpenrlarhfrdiagrvnqrlaaaadevwlvvsgigvkik
>d1cbuc_ 3.30.1.9.5 Adenosylcobinamide kinase/adenosylcobinamide phosphate guanylyltransferase CobU {Salmonella typhimurium}
milvtggarsgksrhaealigdapqvlyiatsqilddemaariqhhkdgrpahwrtaecw
rhldtlitadlapddaillecittmvtnllfalggendpeqwdyaameraiddeiqilia
acqrcpakvvlvtnevgmgivpenrlarhfrdiagrvnqrlaaaadevwlvvsgigvkik
>d1cbvh1 2.1.1.1.34 (1-122) Immunoglobulin (variable domains of L and H chains) {Fab BV04-01 (mouse), kappa L chain}
evqpvetggglvqpkgslklscaasgfsfntnamnwvrqapgkglewvarirsksnnyat
yyadsvkdrftisrddsqnmlylqmnnlktedtamyycvrdqtgtawfaywgqgtlvtvs
aa
>d1cbvh2 2.1.1.2.43 (123-219) Immunoglobulin (constant domains of L and H chains) {Fab BV04-01 (mouse), kappa L chain}
kttppsvyplapgcgdttgssvtlgclvkgyfpesvtvtwnsgslsssvhtfpallqsgl
ytmsssvtvpsstwpsqtvtcsvahpassttvdkkle
>d1cbvl1 2.1.1.1.34 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab BV04-01 (mouse), kappa L chain}
dvvmtqtplslpvslgdqasiscrssqslvhsngntylhwylqkpgqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyfcsqsthvpltfgagtklelk
>d1cbvl2 2.1.1.2.43 (113-219) Immunoglobulin (constant domains of L and H chains) {Fab BV04-01 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>e1cbw.1b 2.41.1.2.7 (alpha,gamma)-chymotrypsin(ogen) {Bovine (Bos taurus)}
ivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgvttsdvvvagefdqgs
ssekiqklkiakvfknskynsltinnditllklstaasfsqtvsavclpsasddfaagtt
cvttgwgltry
>e1cbw.1c 2.41.1.2.7 (alpha,gamma)-chymotrypsin(ogen) {Bovine (Bos taurus)}
antpdrlqqaslpllsntnckkywgtkikdamicagasgvsscmgdsggplvckkngawt
lvgivswgsstcststpgvyarvtalvnwvqqtlaan
>e1cbw.2g 2.41.1.2.7 (alpha,gamma)-chymotrypsin(ogen) {Bovine (Bos taurus)}
ivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgvttsdvvvagefdqgs
ssekiqklkiakvfknskynsltinnditllklstaasfsqtvsavclpsasddfaagtt
cvttgwgltry
>e1cbw.2h 2.41.1.2.7 (alpha,gamma)-chymotrypsin(ogen) {Bovine (Bos taurus)}
antpdrlqqaslpllsntnckkywgtkikdamicagasgvsscmgdsggplvckkngawt
lvgivswgsstcststpgvyarvtalvnwvqqtlaan
>d1cbwd_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d1cbwi_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d1cbx__ 3.47.4.1.1 Carboxypeptidase A {Bovine (Bos taurus)}
arstntfnyatyhtldeiydfmdllvaehpqlvsklqigrsyegrpiyvlkfstggsnrp
aiwidlgihsrewitqatgvwfakkftenygqnpsftaildsmdifleivtnpngfafth
senrlwrktrsvtssslcvgvdanrnwdagfgkagassspcsetyhgkyansevevksiv
dfvknhgnfkaflsihsysqlllypygyttqsipdktelnqvaksavaalkslygtsyky
gsiittiyqasggsidwsynqgikysftfelrdtgrygfllpasqiiptaqetwlgvlti
mehtvnn
>d1cby__ 4.81.1.1.1 Mosquitocidal delta-endotoxin CytB {Bacillus thuringiensis, strain Kyushuensis}
csapiirkpfkhivltvpssdldnfntvfyvqpqyinqalhlanafqgaidplnlnfnfe
kalqiangipnsaivktlnqsviqqtveisvmveqlkkiiqevlglvinstsfwnsveat
ikgtftnldtqideawifwhslsahntsyyynilfsiqnedtgavmavlplafevsvdve
kqkvlfftikdsaryevkmkaltlvqalhssnapivdifnvnnynly
>d1cc1l_ 5.14.1.1.3 Nickel-iron hydrogenase, large subunit {Desulfomicrobium baculatum}
vkisidpltrveghlkievevkdgkvvdakcsggmfrgfeqilrgrdprdssqivqricg
vcptahctasvmaqddafgvkvttngritrnlifganylqshilhfyhlaaldyvkgpdv
spfvpryanadlltdrikdgakadatntyglnqylkaleirrichemvamfggrmphvqg
mvvggateiptadkvaeyaarfkevqkfvieeylpliytlgsvytdlfetgigwknviaf
gvfpedddyktfllkpgvyidgkdeefdsklvkeyvghsffdhsapgglhysvgetnpnp
dkpgaysfvkaprykdkpcevgplarmwvqnpelspvgqkllkelygieakkfrdlgdka
fsimgrhvlraeetwltavavekwlkqvqpgaetyvkseipdaaegtgfteaprgallhy
lkikdkkienyqivsatlwnanprddmgqrgpieealigvpvpdiknpvnvgrlvrsydp
xlgcavh
>d1cc1s_ 5.15.1.1.3 Nickel-iron hydrogenase, small subunit {Desulfomicrobium baculatum}
kkapviwvqgqgctgcsvsllnavhprikeilldvislefhptvmasegemalahmyeia
ekfngnffllvegaiptakegrycivgetldakahhhevtmmelirdlapkslatvavgt
csayggipaaegnvtgsksvrdffadekiekllvnvpgcpphpdwmvgtlvaawshvlnp
tehplpeldddgrpllffgdnihencpyldkydnsefaetftkpgckaelgckgpstyad
cakrrwnnginwcvenavcigcvepdfpdgkspfyvae
>d1cc2a1 3.3.1.2.2 (9-318,451-506) Cholesterol oxidase {Streptomyces}
gyvpavvigtgygaavsalrlgeagvqtlmlemgqlwnqpgpdgnifcgmlnpdkrsswf
knrteaplgsflwldvvnrnidpyagvldrvnydqmsvyvgrgvgggslvnggmavepkr
syfeeilprvdssemydryfpransmlrvnhidtkwfedtewykfarvsreqagkaglgt
vfvpnvydfgymqreaagevpksalateviygnnhgkqsldktylaaalgtgkvtiqtlh
qvktirqtkdggyaltveqkdtdgkllatkeiscrylflgagslgstellvrardtgtlp
nlnsevgagwXgcvlgkatddygrvagyknlyvtdgslipgsvgvnpfvtitalaernve
riikqdv
>d1cc2a2 4.14.1.1.2 (319-450) Cholesterol oxidase {Streptomyces}
gpngnimtaranhmwnptgahqssipalgidawdnsdssvfaeiapmpagletwvslyla
itknpqrgtfvydaatdraklnwtrdqnapavnaakalfdrinkangtiyrydlfgtqlk
afaddfcyqplg
>d1cc4a1 3.3.1.2.3 (1-173,276-391) p-Hydroxybenzoate hydroxylase (PHBH) {Pseudomonas fluorescens}
mktqvaiigagpsglllgqllhkagidnvilerqtpdyvlgriragvleqgmvdllreag
vdrrmardglvhegveiafagqrrridlkrlsggktvtvygqtevtrdlmeareacgatt
vyqaaevrlhdlqgerpyvtferdgerlrldcdyiagcdgfhgisrqsipaerXmqhgrl
flagdaahivpptgakglnlaasdvstlyrlllkayregrgellerysaiclrriwkaer
fswwmtsvlhrfpdtdafsqriqqteleyylgseaglatiaenyvglpye
>d1cc4a2 4.14.1.2.1 (174-275) p-Hydroxybenzoate hydroxylase, PHBH {Pseudomonas fluorescens}
lkvfervypfgwlglladtppvsheliyanhprgfalcsqrsatrsryyvqvpltekved
wsderfwtelkarlpaevaeklvtgpsleksiaplrsfvvep
>d1cc5__ 1.3.1.1.18 Cytochrome c5 {Azotobacter vinelandii}
gggarsgddvvakycnachgtgllnapkvgdsaawktradakggldgllaqslsglnamp
pkgtcadcsddelkaaigkmsgl
>d1cc6a1 3.3.1.2.3 (1-173,276-391) p-Hydroxybenzoate hydroxylase (PHBH) {Pseudomonas fluorescens}
mktqvaiigagpsglllgqllhkagidnvilerqtpdyvlgriragvleqgmvdllreag
vdrrmardglvhegveiafagqrrridlkrlsggktvtvygqtevtrdlmeareacgatt
vyqaaevrlhdlqgerpyvtferdgerlrldcdyiagcdgfhgisrqsipaerXmqhgrl
flagdaahivpptgakglnlaasdvstlyrlllkayregrgellerysaiclrriwkaer
fswwmtsvlhrfpdtdafsqriqqteleyylgseaglatiaenyvglpye
>d1cc6a2 4.14.1.2.1 (174-275) p-Hydroxybenzoate hydroxylase, PHBH {Pseudomonas fluorescens}
lkvfervypfgwlglladtppvsheliyanhprgfalcsqrsatrsryyvqvpltekved
wsderfwtelkarlpaevaeklvtgpsleksiaplrsfvvep
>d1cca__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpwgaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1ccb__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpwgaannvftnefylnllnedwklekndanneqwdsksgymmlpteysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1ccc__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpwgaannvftnefylnllnedwklekndanneqwdsksgymmlptaysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1ccd__ 1.97.1.1.2 Clara cell 17kDa protein {Rat (Rattus rattus)}
ssdicpgflqvlealllgsesnyeaalkpfnpasdlqnagtqlkrlvdtlpqetrinivk
ltekiltsplceqdlrv
>d1cce__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgagalgkthlk
nsgyegpwgaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1ccf__ 7.3.11.1.6 Factor X, N-terminal module {Bovine (Bos taurus)}
kdgdqceghpclnqghckdgigdytctcaegfegkncefstr
>d1ccg__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgagalgkthlk
nsgyegpwgaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1cch__ 1.3.1.1.19 Cytochrome c551 {Pseudomonas stutzeri}
qdgealfkskpcaachsvdtkmvgpalkevaaknagvegaadtlalhikngsqgvwgpip
mppnpvteeeakilaewvlslk
>d1cci__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpwgaannvftnegylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1ccj__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpwgaannvftnegylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1cck__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpwgaannvftneyylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1ccl__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpwgaannvftnekylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1ccm__ 7.13.1.1.1 Crambin {Abyssinian cabbage (Crambe abyssinica)}
ttccpsivarsnfnvcrlpgtpealcatytgciiipgatcpgdyan
>d1ccn__ 7.13.1.1.1 Crambin {Abyssinian cabbage (Crambe abyssinica)}
ttccpsivarsnfnvcrlpgtpealcatytgciiipgatcpgdyan
>d1ccp__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
tplvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhd
ntggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqg
pkipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkth
lknsgyegpwgaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqd
pkylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1ccqa_ 7.7.1.1.16 Cardiotoxin II {Central asian cobra (Naja naja oxiana)}
lkckklvplfsktcpagknlcykmfmvaaphvpvkrgcidvcpkssllvkyvccntdkcn
>d1ccr__ 1.3.1.1.9 Mitochondrial cytochrome c {Rice embryos (Oryza sativa)}
xasfseappgnpkagekifktkcaqchtvdkgaghkqgpnlnglfgrqsgttpgysysta
dknmaviweentlydyllnpkkyipgtkmvfpglkkpqeradlisylkeats
>d1ccs__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgsldtppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1cct__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgsletppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1ccu__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslhtppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1ccva_ 7.22.1.1.4 Chymotrypsin inhibitor AMCI {Honeybee (Apis mellifera)}
eecgpnevfntcgsacaptcaqpktrictmqcrigcqcqegflrngegacvlpenc
>d1ccza1 2.1.1.1.9 (1-93) CD2-binding domain of CD58, first domain {Human (Homo sapiens)}
fsqqiygvvygnvtfhvpsnvplkevlwkkqkdkvaelensefrafssfknrvyldtvsg
sltiynltssdedeyemespnitdtmkfflyvl
>d1ccza2 2.1.1.3.8 (94-171) CD2-binding domain of CD58, second domain {Human (Homo sapiens)}
emvskpmiywecsnatltcevlegtdvelklyqgkehlrslrqktmsyqwtnlrapfkck
avnrvsqesemevvncpe
>d1cd1a1 2.1.1.2.147 (186-279) CD1, beta2-microglobulin and alpha-3 domain {Mouse (Mus musculus)}
qekpvawlssvpssahghrqlvchvsgfypkpvwvmwmrgdqeqqgthrgdflpnadetw
ylqatldveageeaglacrvkhsslggqdiilyw
>d1cd1a2 4.17.1.1.2 (7-185) CD1, alpha-1 and alpha-2 domains {Mouse (Mus musculus)}
nytfrclqmssfanrswsrtdsvvwlgdlqthrwsndsatisftkpwsqgklsnqqwekl
qhmfqvyrvsftrdiqelvkmmspkedypieiqlsagcemypgnasesflhvafqgkyvv
rfwgtswqtvpgapswldlpikvlnadqgtsatvqmllndtcplfvrglleagksdlek
>d1cd1b1 2.1.1.2.147 CD1, beta2-microglobulin and alpha-3 domain {Mouse (Mus musculus)}
iqktpqiqvysrhppengkpnilncyvtqfhpphieiqmlkngkkipkvemsdmsfskdw
sfyilahteftptetdtyacrvkhdsmaepktvywdrdm
>d1cd1c1 2.1.1.2.147 (186-279) CD1, beta2-microglobulin and alpha-3 domain {Mouse (Mus musculus)}
qekpvawlssvpssahghrqlvchvsgfypkpvwvmwmrgdqeqqgthrgdflpnadetw
ylqatldveageeaglacrvkhsslggqdiilyw
>d1cd1c2 4.17.1.1.2 (7-185) CD1, alpha-1 and alpha-2 domains {Mouse (Mus musculus)}
nytfrclqmssfanrswsrtdsvvwlgdlqthrwsndsatisftkpwsqgklsnqqwekl
qhmfqvyrvsftrdiqelvkmmspkedypieiqlsagcemypgnasesflhvafqgkyvv
rfwgtswqtvpgapswldlpikvlnadqgtsatvqmllndtcplfvrglleagksdlek
>d1cd1d1 2.1.1.2.147 CD1, beta2-microglobulin and alpha-3 domain {Mouse (Mus musculus)}
iqktpqiqvysrhppengkpnilncyvtqfhpphieiqmlkngkkipkvemsdmsfskdw
sfyilahteftptetdtyacrvkhdsmaepktvywdrdm
>d1cd31_ 1.81.1.1.1 Scaffolding protein gpD of bacteriophage procapsid {Bacteriophage phi-x174}
eqsvrfqtalasikliqasavldlteddfdfltsnkvwiatdrsrarrcveacvygtldf
vgyprfpapvefiaaviayyvhpvniqtaclimegaefteniingverpvkaaelfaftl
rvragntdvltdaeenvrqklra
>d1cd32_ 1.81.1.1.1 Scaffolding protein gpD of bacteriophage procapsid {Bacteriophage phi-x174}
eqsvrfqtalasikliqasavldlteddfdfltsnkvwiatdrsrarrcveacvygtldf
vgyprfpapvefiaaviayyvhpvniqtaclimegaefteniingverpvkaaelfaftl
rvragntdvltdaee
>d1cd33_ 1.81.1.1.1 Scaffolding protein gpD of bacteriophage procapsid {Bacteriophage phi-x174}
teqsvrfqtalasikliqasavldlteddfdfltsnkvwiatdrsrarrcveacvygtld
fvgyprfpapvefiaaviayyvhpvniqtaclimegaefteniingverpvkaaelfaft
lrvragntdvltdaeenvrq
>d1cd34_ 1.81.1.1.1 Scaffolding protein gpD of bacteriophage procapsid {Bacteriophage phi-x174}
qsvrfqtalasikliqasavldlteddfdfltsnkvwiatdrsrarrcveacvygtldfv
gyprfpapvefiaaviayyvhpvniqtaclimegaefteniingverpvkaaelfaftlr
vragntdvltdaeenvrqklraegvm
>d1cd3f_ 2.9.1.1.1 Bacteriophage capsid proteins {Bacteriophage phiX174}
sniqtgaermphdlshlgflagqigrlitisttpviagdsfemdavgalrlsplrrglai
dstvdiftfyvphrhvygeqwikfmkdgvnatplptvnttgyidhaaflgtinpdtnkip
khlfqgylniynnyfkapwmpdrteanpnelnqddarfgfrcchlkniwtaplppetels
rqmttsttsidimglqaayanlhtdqerdyfmqryrdvissfggktsydadnrpllvmrs
nlwasgydvdgtdqtslgqfsgrvqqtykhsvprffvpehgtmftlalvrfpptatkeiq
ylnakgaltytdiagdpvlygnlppreismkdvfrsgdsskkfkiaegqwyryapsyvsp
ayhllegfpfiqeppsgdlqervlirhhdydqcfqsvqllqwnsqvkfnvtvyrnlpttr
dsimts
>d1cd3g_ 2.9.1.1.1 Bacteriophage capsid proteins {Bacteriophage phiX174}
mfqtfisrhnsnffsdklvltsvtpassapvlqtpkatsstlyfdsltvnagnggflhci
qmdtsvnaanqvvsvgadiafdadpkffaclvrfesssvpttlptaydvyplngrhdggy
ytvkdcvtidvlprtpgnnvyvgfmvwsnftatkcrglvslnqvikeiiclqplk
>d1cd8__ 2.1.1.1.3 CD8 {Human (Homo sapiens)}
sqfrvspldrtwnlgetvelkcqvllsnptsgcswlfqprgaaasptfllylsqnkpkaa
egldtqrfsgkrlgdtfvltlsdfrrenegyyfcsalsnsimyfshfvpvflpa
>d1cdb__ 2.1.1.1.7 CD2, first domain {Human (Homo sapiens)}
keitnaletwgalgqdinldipsfqmsddiddikwektsdkkkiaqfrkeketfkekdty
klfkngtlkikhlktddqdiykvsiydtkgknvlekifdlkiqer
>d1cdca_ 2.1.1.1.8 CD2, first domain {Rat (Rattus rattus)}
gtvwgalghginlnipnfqmtddidevrwergstlvaefkrkmkpflksgafeilangdl
kiknltrddsgtynvtvystngtrildkaldlrile
>d1cdcb_ 2.1.1.1.8 CD2, first domain {Rat (Rattus rattus)}
gtvwgalghginlnipnfqmtddidevrwergstlvaefkrkmkpflksgafeilangdl
kiknltrddsgtynvtvystngtrildkaldlrile
>d1cdda_ 3.55.1.1.1 Glycinamide ribonucleotide transformylase {Escherichia coli, k12 strain tx635, with plasmid pjs167}
mnivvlisgngsnlqaiidacktnkikgtvravfsnkadafglerarqagiathtliasa
fdsreaydreliheidmyapdvvvlagfmrilspafvshyagrllnihpsllpkypglht
hrqalengdeehgtsvhfvtdeldggpvilqakvpvfagdsedditarvqtqehaiyplv
iswfadgrlkmhenaawldgqrlppqgyaade
>d1cddb_ 3.55.1.1.1 Glycinamide ribonucleotide transformylase {Escherichia coli, k12 strain tx635, with plasmid pjs167}
mnivvlisgngsnlqaiidacktnkikgtvravfsnkadafglerarqagiathtliasa
fdsreaydreliheidmyapdvvvlagfmrilspafvshyagrllnihpsllpkypglht
hrqalengdeehgtsvhfvtdeldggpvilqakvpvfagdsedditarvqtqehaiyplv
iswfadgrlkmhenaawldgqrlppqgyaade
>d1cde__ 3.55.1.1.1 Glycinamide ribonucleotide transformylase {Escherichia coli, k12 strain tx635, with plasmid pjs167}
mnivvlisgngsnlqaiidacktnkikgtvravfsnkadafglerarqagiathtliasa
fdsreaydreliheidmyapdvvvlagfmrilspafvshyagrllnihpsllpkypglht
hrqalengdeehgtsvhfvtdeldggpvilqakvpvfagdsedditarvqtqehaiyplv
iswfadgrlkmhenaawldgqrlppqgya
>d1cdg_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d1cdg_2 2.3.1.1.1 (582-686) Cyclodextrin glycosyltransferase, C-terminal domain {Bacillus circulans}
lsgdqvsvrfvvnnattalgqnvyltgsvselgnwdpakaigpmynqvvyqypnwyydvs
vpagktiefkflkkqgstvtweggsnhtftapssgtatinvnwqp
>d1cdg_3 2.62.1.1.4 (407-495) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqerwinndvliyerkfgsnvavvavnrnlnapasisglvtslpqgsyndvlggllng
ntlsvgsggaasnftlaaggtavwqytaa
>d1cdg_4 3.1.7.1.4 (1-406) Cyclodextrin glycosyltransferase {Bacillus circulans}
apdtsvsnkqnfstdviyqiftdrfsdgnpannptgaafdgtctnlrlycggdwqgiink
indgyltgmgvtaiwisqpveniysiinysgvnntayhgywardfkktnpaygtiadfqn
liaaahaknikviidfapnhtspassdqpsfaengrlydngtllggytndtqnlfhhngg
tdfsttengiyknlydladlnhnnstvdvylkdaikmwldlgidgirmdavkhmpfgwqk
sfmaavnnykpvftfgewflgvnevspenhkfanesgmslldfrfaqkvrqvfrdntdnm
yglkamlegsaadyaqvddqvtfidnhdmerfhasnanrrkleqalaftltsrgvpaiyy
gteqymsggtdpdnraripsfststtayqviqklaplrkcnpaiay
>d1cdh_1 2.1.1.1.5 (1-97) CD4 {Human (Homo sapiens)}
kkvvlgkkgdtveltctasqkksiqfhwknsnqikilgnqgsfltkgpsklndradsrrs
lwdqgnfpliiknlkiedsdtyicevedqkeevqllv
>d1cdh_2 2.1.1.3.4 (98-178) CD4 {Human (Homo sapiens)}
fgltansdthllqgqsltltlesppgsspsvqcrsprgkniqggktlsvsqlelqdsgtw
tctvlqnqkkvefkidivvla
>d1cdi_1 2.1.1.1.5 (1-97) CD4 {Human (Homo sapiens)}
kkvvlgkkgdtveltctasqkksiqfhwknsnqikilgnqgsfltkgpsklndradsrrs
lwdqgnfpliiknlkiedsdtyicevedqkeevqllv
>d1cdi_2 2.1.1.3.4 (98-178) CD4 {Human (Homo sapiens)}
fgltansdthllqgqsltltlesppgsspsvqcrsprgkniqggktlsvsqlelqdsgtw
tctvlqnqkkvefkidivvla
>d1cdj_1 2.1.1.1.5 (1-97) CD4 {Human (Homo sapiens)}
kkvvlgkkgdtveltctasqkksiqfhwknsnqikilgnqgsfltkgpsklndradsrrs
lwdqgnfpliiknlkiedsdtyicevedqkeevqllv
>d1cdj_2 2.1.1.3.4 (98-178) CD4 {Human (Homo sapiens)}
fgltansdthllqgqsltltlesppgsspsvqcrsprgkniqggktlsvsqlelqdsgtw
tctvlqnqkkvefkidivvla
>d1cdka_ 4.117.1.1.3 cAMP-dependent PK, catalytic subunit {Pig (Sus scrofa)}
kgseqesvkeflakakedflkkwenpaqntahldqferiktlgtgsfgrvmlvkhketgn
hfamkildkqkvvklkqiehtlnekrilqavnfpflvkleysfkdnsnlymvmeyvpgge
mfshlrrigrfsepharfyaaqivltfeylhsldliyrdlkpenllidqqgyiqvtdfgf
akrvkgrtwtlcgtpeylapeiilskgynkavdwwalgvliyemaagyppffadqpiqiy
ekivsgkvrfpshfssdlkdllrnllqvdltkrfgnlkdgvndiknhkwfattdwiaiyq
rkveapfipkfkgpgdtsnfddyeeeeirvsinekcgkefsef
>d1cdkb_ 4.117.1.1.3 cAMP-dependent PK, catalytic subunit {Pig (Sus scrofa)}
kgseqesvkeflakakedflkkwenpaqntahldqferiktlgtgsfgrvmlvkhketgn
hfamkildkqkvvklkqiehtlnekrilqavnfpflvkleysfkdnsnlymvmeyvpgge
mfshlrrigrfsepharfyaaqivltfeylhsldliyrdlkpenllidqqgyiqvtdfgf
akrvkgrtwtlcgtpeylapeiilskgynkavdwwalgvliyemaagyppffadqpiqiy
ekivsgkvrfpshfssdlkdllrnllqvdltkrfgnlkdgvndiknhkwfattdwiaiyq
rkveapfipkfkgpgdtsnfddyeeeeirvsinekcgkefsef
>d1cdla_ 1.42.1.5.8 Calmodulin {Bovine (Bos taurus)}
teeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngtid
fpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevdem
ireadidgdgqvnyeefvqmmt
>d1cdlb_ 1.42.1.5.8 Calmodulin {Bovine (Bos taurus)}
teeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngtid
fpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevdem
ireadidgdgqvnyeefvqmmt
>d1cdlc_ 1.42.1.5.8 Calmodulin {Bovine (Bos taurus)}
teeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngtid
fpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevdem
ireadidgdgqvnyeefvqmmt
>d1cdld_ 1.42.1.5.8 Calmodulin {Bovine (Bos taurus)}
teeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngtid
fpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevdem
ireadidgdgqvnyeefvqmmt
>d1cdma_ 1.42.1.5.8 Calmodulin {Bovine (Bos taurus)}
lteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngti
dfpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevde
mireadidgdgqvnyeefvqmmt
>d1cdn__ 1.42.1.1.1 Calbindin D9K {Bovine (Bos taurus)}
kspeelkgifekyaakegdpnqlskeelklllqtefpsllkggstldelfeeldkngdge
vsfeefqvlvkkisq
>d1cdoa1 2.31.1.2.1 (1-175,325-374) Alcohol dehydrogenase {Horse (Equus caballus)}
atvgkvikckaavaweankplvieeievdvphaneirikiiatgvchtdlyhlfegkhkd
gfpvvlghegagivesvgpgvtefqpgekviplfisqcgecrfcqspktnqcvkgwanes
pdvmspketrftckgrkvlqflgtstfsqytvvnqiavakidpsapldtvcllgcXkdgv
pkmvkayldkkvkldefithrmplesvndaidlmkhgkcirtvlsl
>d1cdoa2 3.2.1.1.1 (176-324) Alcohol dehydrogenase {Horse (Equus caballus)}
gvstgfgaavntakvepgstcavfglgavglaavmgchsagakriiavdlnpdkfekakv
fgatdfvnpndhsepisqvlskmtnggvdfslecvgnvgvmrnalesclkgwgvsvlvgw
tdlhdvatrpiqliagrtwkgsmfggfkg
>d1cdob1 2.31.1.2.1 (1-175,325-374) Alcohol dehydrogenase {Horse (Equus caballus)}
atvgkvikckaavaweankplvieeievdvphaneirikiiatgvchtdlyhlfegkhkd
gfpvvlghegagivesvgpgvtefqpgekviplfisqcgecrfcqspktnqcvkgwanes
pdvmspketrftckgrkvlqflgtstfsqytvvnqiavakidpsapldtvcllgcXkdgv
pkmvkayldkkvkldefithrmplesvndaidlmkhgkcirtvlsl
>d1cdob2 3.2.1.1.1 (176-324) Alcohol dehydrogenase {Horse (Equus caballus)}
gvstgfgaavntakvepgstcavfglgavglaavmgchsagakriiavdlnpdkfekakv
fgatdfvnpndhsepisqvlskmtnggvdfslecvgnvgvmrnalesclkgwgvsvlvgw
tdlhdvatrpiqliagrtwkgsmfggfkg
>d1cdp__ 1.42.1.4.2 Parvalbumin {Carp (Cyprinus carpio)}
xafagvlndadiaaaleackaadsfnhkaffakvgltsksaddvkkafaiidqdksgfie
edelklflqnfkadaraltdgetktflkagdsdgdgkigvdeftalvka
>d1cdq__ 7.7.1.3.1 CD59, extracellular domain {Human (Homo sapiens)}
lqcyncpnptadcktavncssdfdaclitkaglqvynkcwkfehcnfndvttrlrenelt
yycckkdlcnfneqlen
>d1cdr__ 7.7.1.3.1 CD59, extracellular domain {Human (Homo sapiens)}
lqcyncpnptadcktavncssdfdaclitkaglqvynkcwkfehcnfndvttrlrenelt
yycckkdlcnfneqlen
>d1cds__ 7.7.1.3.1 CD59, extracellular domain {Human (Homo sapiens)}
lqcyncpnptadcktavncssdfdaclitkaglqvynkcwkfehcnfndvttrlrenelt
yycckkdlcnfneqlen
>d1cdta_ 7.7.1.1.6 Cardiotoxin V {Taiwan cobra (Naja naja atra)}
lkcnklipiayktcpegknlcykmmlaskkmvpvkrgcinvcpknsalvkyvccstdrcn
>d1cdtb_ 7.7.1.1.6 Cardiotoxin V {Taiwan cobra (Naja naja atra)}
lkcnklipiayktcpegknlcykmmlaskkmvpvkrgcinvcpknsalvkyvccstdrcn
>d1cdu_1 2.1.1.1.5 (1-97) CD4 {Human (Homo sapiens)}
kkvvlgkkgdtveltctasqkksiqfhwknsnqikilgnqgsvltkgpsklndradsrrs
lwdqgnfpliiknlkiedsdtyicevedqkeevqllv
>d1cdu_2 2.1.1.3.4 (98-178) CD4 {Human (Homo sapiens)}
fgltansdthllqgqsltltlesppgsspsvqcrsprgkniqggktlsvsqlelqdsgtw
tctvlqnqkkvefkidivvla
>d1cdwa_ 4.103.1.1.1 TATA-box binding protein (TBP), C-terminal domain {Human (Homo sapiens)}
sgivpqlqnivstvnlgckldlktialrarnaeynpkrfaavimrireprttalifssgk
mvctgakseensrlaarkyarvvqklgfpakfldfkiqnmvgscdvkfpirleglvlthq
qfssyepelfpgliyrmikprivllifvsgkvvltgakvraeiyeafeniypilkgfrk
>d1cdy_1 2.1.1.1.5 (1-97) CD4 {Human (Homo sapiens)}
kkvvlgkkgdtveltctasqkksiqfhwknsnqikilgnqgsfltkspsklndradsrrs
lwdqgnfpliiknlkiedsdtyicevedqkeevqllv
>d1cdy_2 2.1.1.3.4 (98-178) CD4 {Human (Homo sapiens)}
fgltansdthllqgqsltltlesppgsspsvqcrsprgkniqggktlsvsqlelqdsgtw
tctvlqnqkkvefkidivvla
>d1ce1h1 2.1.1.1.122 (1-121) Immunoglobulin (variable domains of L and H chains) {Therapeutic CAMPATH-1H fab (rat), kappa L chain}
qvqlqesgpglvrpsqtlsltctvsgftftdfymnwvrqppgrglewigfirdkakgytt
eynpsvkgrvtmlvdtsknqfslrlssvtaadtavyycareghtaapfdywgqgslvtvs
s
>d1ce1h2 2.1.1.2.120 (122-220) Immunoglobulin (constant domains of L and H chains) {Therapeutic CAMPATH-1H humanized fab, kappa L chain}
astkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkve
>d1ce1l1 2.1.1.1.122 (1-107) Immunoglobulin (variable domains of L and H chains) {Therapeutic CAMPATH-1H fab (rat), kappa L chain}
diqmtqspsslsasvgdrvtitckasqnidkylnwyqqkpgkapklliyntnnlqtgvps
rfsgsgsgtdftftisslqpediatyyclqhisrprtfgqgtkveik
>d1ce1l2 2.1.1.2.120 (108-211) Immunoglobulin (constant domains of L and H chains) {Therapeutic CAMPATH-1H humanized fab, kappa L chain}
rtvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqd
skdstyslsstltlskadyekhkvyacevthqglsspvtksfnr
>d1ce2a1 3.84.1.2.3 (1-333) Lactoferrin {Domestic water buffalo (Bubalus arnee bubalis)}
aprknvrwctisqpewlkchrwqwrmkklgapsitcvrrasvleciraitekkadavtld
ggmvfeagrdpyklrpvaaeiygtkespqthyyavavvkkgsnfqldqlqgrnschtglg
rsagwnipmgilrpylswtesleplqgavakffsascvpcvdrqaypnlcqlckgegenq
cacsprepyfgysgafkclqdgagdvafvkettvfenlpekadrdqyellclnntrapvd
afkechlaqvpshavvarsvdgkedliwkllskaqekfgknksgsfqlfgsppgqrdllf
kdsalgflripskvdsalylgsryltalknlre
>d1ce2a2 3.84.1.2.3 (334-689) Lactoferrin {Domestic water buffalo (Bubalus arnee bubalis)}
taeevqarrarvvwcavgpeeqkkcqqwsqqsgqivtcatasttddcialvlkgeadals
ldggyiytagkcglvpvlaenrksskhssldcvlrptegylavavvkkanegltwnslkg
kkschtavdrtagwnipmglianqtgscafdeffsqscapgadpksrlcalcagddqgld
kcvpnskekyygytgafrclaedvgdvafvkndtvwentngestadwaknlnredfrllc
ldgtrkpvteaqschlavapnhavvslseraahveqvllhqqalfgengkncpdkfclfk
setknllfndnteclaklggrptyeeylgteyvtaianlkkcstsplleacafltr
>d1ce3a_ 7.15.1.2.4 Multidomain proteinase inhibitor {Winged tobacco (Nicotiana alata)}
mkactlncdpriaygvcprseekkndrictnccagtkgckyfsddgtfvceges
>d1ce5a_ 2.41.1.2.1 Trypsin(ogen) {Bovine (Bos taurus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1ce6a1 2.1.1.2.14 (182-274) Class I MHC, beta2-microglobulin and alpha-3 domain {Mouse (Mus musculus), H-2DB}
tdspkahvthhprskgevtlrcwalgfypaditltwqlngeeltqdmelvetrpagdgtf
qkwasvvvplgkeqnytcrvyheglpepltlrw
>d1ce6a2 4.17.1.1.21 (1-181) MHC class I, alpha-1 and alpha-2 domains {Mouse (Mus musculus), H-2DB}
gphsmryfetavsrpgleepryisvgyvdnkefvrfdsdaenpryeprapwmeqegpeyw
eretqkakgqeqwfrvslrnllgyynqsaggshtlqqmsgcdlgsdwrllrgylqfayeg
rdyialnedlktwtaadmaaqitrrkweqsgaaehykaylegecvewlhrylkngnatll
r
>d1ce6b1 2.1.1.2.14 Class I MHC, beta2-microglobulin and alpha-3 domain {Mouse (Mus musculus), H-2DB}
iqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskdw
sfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1ce8a1 1.89.1.1.1 (403-555) Carbamoyl phosphate synthetase, large subunit connection domain {Escherichia coli}
evgatgfdpkvslddpealtkirrelkdagadriwyiadafraglsvdgvfnltnidrwf
lvqieelvrleekvaevgitglnadflrqlkrkgfadarlaklagvreaeirklrdqydl
hpvykrvdtcaaefatdtaymystyeeeceanp
>d1ce8a2 3.17.1.1.1 (936-1073) Carbamoyl phosphate synthetase, large subunit allosteric, C-terminal domain {Escherichia coli}
nstmkkhgrallsvregdkervvdlaakllkqgfeldathgtaivlgeaginprlvnkvh
egrphiqdrikngeytyiinttsgrraiedsrvirrsalqykvhydttlnggfatamaln
adatekvisvqemhaqik
>d1ce8a3 3.24.1.1.3 (1-127) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
mpkrtdiksililgagpivigqacefdysgaqackalreegyrvinvnsnpatimtdpem
adatyiepihwevvrkiiekerpdavlptmggqtalncalelerqgvleefgvtmigata
daidkae
>d1ce8a4 3.24.1.1.3 (556-676) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
stdrekimvlgggpnrigqgiefdyccvhaslalredgyetimvncnpetvstdydtsdr
lyfepvtledvleivriekpkgvivqyggqtplklaraleaagvpvigtspdaidraedr
e
>d1ce8a5 4.115.1.2.3 (128-402) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
drrrfdvamkkigletarsgiahtmeealavaadvgfpciirpsftmggsgggiaynree
feeicargldlsptkellidesligwkeyemevvrdkndnciivcsienfdamgihtgds
itvapaqtltdkeyqimrnasmavlreigvetggsnvqfavnpkngrliviemnprvsrs
salaskatgfpiakvaaklavgytldelmnditggrtpasfepsidyvvtkiprfnfekf
agandrlttqmksvgevmaigrtqqeslqkalrgl
>d1ce8a6 4.115.1.2.3 (677-935) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
rfqhaverlklkqpanatvtaiemavekakeigyplvvrpsyvlggrameivydeadlrr
yfqtavsvsndapvlldhflddavevdvdaicdgemvliggimehieqagvhsgdsacsl
paytlsqeiqdvmrqqvqklafelqvrglmnvqfavknnevylievnpraartvpfvska
tgvplakvaarvmagkslaeqgvtkevippyysvkevvlpfnkfpgvdpllgpemrstge
vmgvgrtfaeafakaqlgs
>d1ce8b1 3.7.3.1.1 (2-152) Carbamoyl phosphate synthetase, small subunit N-terminal domain {Escherichia coli}
iksallvledgtqfhgraigatgsavgevvfntsmtgyqeiltdpsysrqivtltyphig
nvgtndadeessqvhaqglvirdlpliasnfrntedlssylkrhnivaiadidtrkltrl
lrekgaqngciiagdnpdaalalekarafpg
>d1ce8b2 3.58.1.1.2 (153-380) Carbamoyl phosphate synthetase, small subunit C-terminal domain {Escherichia coli}
lngmdlakevttaeayswtqgswtltgglpqakkedelpfhvvaydfgakrnilrmlvdr
gcrltivpaqtsaedvlkmnpdgiflsngpgdpapcdyaitaiqkfletdipvfgiclgh
qllalasgaktvkmkfghhggnhpvkdveknvvmitaqnhgfavdeatlpanlrvthksl
fdgtlqgihrtdkpafsfqghpeaspgphdaaplfdhfielieqyrkt
>d1ce8c1 1.89.1.1.1 (403-555) Carbamoyl phosphate synthetase, large subunit connection domain {Escherichia coli}
evgatgfdpkvslddpealtkirrelkdagadriwyiadafraglsvdgvfnltnidrwf
lvqieelvrleekvaevgitglnadflrqlkrkgfadarlaklagvreaeirklrdqydl
hpvykrvdtcaaefatdtaymystyeeeceanp
>d1ce8c2 3.17.1.1.1 (936-1073) Carbamoyl phosphate synthetase, large subunit allosteric, C-terminal domain {Escherichia coli}
nstmkkhgrallsvregdkervvdlaakllkqgfeldathgtaivlgeaginprlvnkvh
egrphiqdrikngeytyiinttsgrraiedsrvirrsalqykvhydttlnggfatamaln
adatekvisvqemhaqik
>d1ce8c3 3.24.1.1.3 (1-127) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
mpkrtdiksililgagpivigqacefdysgaqackalreegyrvinvnsnpatimtdpem
adatyiepihwevvrkiiekerpdavlptmggqtalncalelerqgvleefgvtmigata
daidkae
>d1ce8c4 3.24.1.1.3 (556-676) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
stdrekimvlgggpnrigqgiefdyccvhaslalredgyetimvncnpetvstdydtsdr
lyfepvtledvleivriekpkgvivqyggqtplklaraleaagvpvigtspdaidraedr
e
>d1ce8c5 4.115.1.2.3 (128-402) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
drrrfdvamkkigletarsgiahtmeealavaadvgfpciirpsftmggsgggiaynree
feeicargldlsptkellidesligwkeyemevvrdkndnciivcsienfdamgihtgds
itvapaqtltdkeyqimrnasmavlreigvetggsnvqfavnpkngrliviemnprvsrs
salaskatgfpiakvaaklavgytldelmnditggrtpasfepsidyvvtkiprfnfekf
agandrlttqmksvgevmaigrtqqeslqkalrgl
>d1ce8c6 4.115.1.2.3 (677-935) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
rfqhaverlklkqpanatvtaiemavekakeigyplvvrpsyvlggrameivydeadlrr
yfqtavsvsndapvlldhflddavevdvdaicdgemvliggimehieqagvhsgdsacsl
paytlsqeiqdvmrqqvqklafelqvrglmnvqfavknnevylievnpraartvpfvska
tgvplakvaarvmagkslaeqgvtkevippyysvkevvlpfnkfpgvdpllgpemrstge
vmgvgrtfaeafakaqlgs
>d1ce8d1 3.7.3.1.1 (2-152) Carbamoyl phosphate synthetase, small subunit N-terminal domain {Escherichia coli}
iksallvledgtqfhgraigatgsavgevvfntsmtgyqeiltdpsysrqivtltyphig
nvgtndadeessqvhaqglvirdlpliasnfrntedlssylkrhnivaiadidtrkltrl
lrekgaqngciiagdnpdaalalekarafpg
>d1ce8d2 3.58.1.1.2 (153-380) Carbamoyl phosphate synthetase, small subunit C-terminal domain {Escherichia coli}
lngmdlakevttaeayswtqgswtltgglpqakkedelpfhvvaydfgakrnilrmlvdr
gcrltivpaqtsaedvlkmnpdgiflsngpgdpapcdyaitaiqkfletdipvfgiclgh
qllalasgaktvkmkfghhggnhpvkdveknvvmitaqnhgfavdeatlpanlrvthksl
fdgtlqgihrtdkpafsfqghpeaspgphdaaplfdhfielieqyrkt
>d1ce8e1 1.89.1.1.1 (403-555) Carbamoyl phosphate synthetase, large subunit connection domain {Escherichia coli}
evgatgfdpkvslddpealtkirrelkdagadriwyiadafraglsvdgvfnltnidrwf
lvqieelvrleekvaevgitglnadflrqlkrkgfadarlaklagvreaeirklrdqydl
hpvykrvdtcaaefatdtaymystyeeeceanp
>d1ce8e2 3.17.1.1.1 (936-1073) Carbamoyl phosphate synthetase, large subunit allosteric, C-terminal domain {Escherichia coli}
nstmkkhgrallsvregdkervvdlaakllkqgfeldathgtaivlgeaginprlvnkvh
egrphiqdrikngeytyiinttsgrraiedsrvirrsalqykvhydttlnggfatamaln
adatekvisvqemhaqik
>d1ce8e3 3.24.1.1.3 (1-127) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
mpkrtdiksililgagpivigqacefdysgaqackalreegyrvinvnsnpatimtdpem
adatyiepihwevvrkiiekerpdavlptmggqtalncalelerqgvleefgvtmigata
daidkae
>d1ce8e4 3.24.1.1.3 (556-676) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
stdrekimvlgggpnrigqgiefdyccvhaslalredgyetimvncnpetvstdydtsdr
lyfepvtledvleivriekpkgvivqyggqtplklaraleaagvpvigtspdaidraedr
e
>d1ce8e5 4.115.1.2.3 (128-402) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
drrrfdvamkkigletarsgiahtmeealavaadvgfpciirpsftmggsgggiaynree
feeicargldlsptkellidesligwkeyemevvrdkndnciivcsienfdamgihtgds
itvapaqtltdkeyqimrnasmavlreigvetggsnvqfavnpkngrliviemnprvsrs
salaskatgfpiakvaaklavgytldelmnditggrtpasfepsidyvvtkiprfnfekf
agandrlttqmksvgevmaigrtqqeslqkalrgl
>d1ce8e6 4.115.1.2.3 (677-935) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
rfqhaverlklkqpanatvtaiemavekakeigyplvvrpsyvlggrameivydeadlrr
yfqtavsvsndapvlldhflddavevdvdaicdgemvliggimehieqagvhsgdsacsl
paytlsqeiqdvmrqqvqklafelqvrglmnvqfavknnevylievnpraartvpfvska
tgvplakvaarvmagkslaeqgvtkevippyysvkevvlpfnkfpgvdpllgpemrstge
vmgvgrtfaeafakaqlgs
>d1ce8f1 3.7.3.1.1 (2-152) Carbamoyl phosphate synthetase, small subunit N-terminal domain {Escherichia coli}
iksallvledgtqfhgraigatgsavgevvfntsmtgyqeiltdpsysrqivtltyphig
nvgtndadeessqvhaqglvirdlpliasnfrntedlssylkrhnivaiadidtrkltrl
lrekgaqngciiagdnpdaalalekarafpg
>d1ce8f2 3.58.1.1.2 (153-380) Carbamoyl phosphate synthetase, small subunit C-terminal domain {Escherichia coli}
lngmdlakevttaeayswtqgswtltgglpqakkedelpfhvvaydfgakrnilrmlvdr
gcrltivpaqtsaedvlkmnpdgiflsngpgdpapcdyaitaiqkfletdipvfgiclgh
qllalasgaktvkmkfghhggnhpvkdveknvvmitaqnhgfavdeatlpanlrvthksl
fdgtlqgihrtdkpafsfqghpeaspgphdaaplfdhfielieqyrkt
>d1ce8g1 1.89.1.1.1 (403-555) Carbamoyl phosphate synthetase, large subunit connection domain {Escherichia coli}
evgatgfdpkvslddpealtkirrelkdagadriwyiadafraglsvdgvfnltnidrwf
lvqieelvrleekvaevgitglnadflrqlkrkgfadarlaklagvreaeirklrdqydl
hpvykrvdtcaaefatdtaymystyeeeceanp
>d1ce8g2 3.17.1.1.1 (936-1073) Carbamoyl phosphate synthetase, large subunit allosteric, C-terminal domain {Escherichia coli}
nstmkkhgrallsvregdkervvdlaakllkqgfeldathgtaivlgeaginprlvnkvh
egrphiqdrikngeytyiinttsgrraiedsrvirrsalqykvhydttlnggfatamaln
adatekvisvqemhaqik
>d1ce8g3 3.24.1.1.3 (1-127) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
mpkrtdiksililgagpivigqacefdysgaqackalreegyrvinvnsnpatimtdpem
adatyiepihwevvrkiiekerpdavlptmggqtalncalelerqgvleefgvtmigata
daidkae
>d1ce8g4 3.24.1.1.3 (556-676) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
stdrekimvlgggpnrigqgiefdyccvhaslalredgyetimvncnpetvstdydtsdr
lyfepvtledvleivriekpkgvivqyggqtplklaraleaagvpvigtspdaidraedr
e
>d1ce8g5 4.115.1.2.3 (128-402) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
drrrfdvamkkigletarsgiahtmeealavaadvgfpciirpsftmggsgggiaynree
feeicargldlsptkellidesligwkeyemevvrdkndnciivcsienfdamgihtgds
itvapaqtltdkeyqimrnasmavlreigvetggsnvqfavnpkngrliviemnprvsrs
salaskatgfpiakvaaklavgytldelmnditggrtpasfepsidyvvtkiprfnfekf
agandrlttqmksvgevmaigrtqqeslqkalrgl
>d1ce8g6 4.115.1.2.3 (677-935) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
rfqhaverlklkqpanatvtaiemavekakeigyplvvrpsyvlggrameivydeadlrr
yfqtavsvsndapvlldhflddavevdvdaicdgemvliggimehieqagvhsgdsacsl
paytlsqeiqdvmrqqvqklafelqvrglmnvqfavknnevylievnpraartvpfvska
tgvplakvaarvmagkslaeqgvtkevippyysvkevvlpfnkfpgvdpllgpemrstge
vmgvgrtfaeafakaqlgs
>d1ce8h1 3.7.3.1.1 (2-152) Carbamoyl phosphate synthetase, small subunit N-terminal domain {Escherichia coli}
iksallvledgtqfhgraigatgsavgevvfntsmtgyqeiltdpsysrqivtltyphig
nvgtndadeessqvhaqglvirdlpliasnfrntedlssylkrhnivaiadidtrkltrl
lrekgaqngciiagdnpdaalalekarafpg
>d1ce8h2 3.58.1.1.2 (153-380) Carbamoyl phosphate synthetase, small subunit C-terminal domain {Escherichia coli}
lngmdlakevttaeayswtqgswtltgglpqakkedelpfhvvaydfgakrnilrmlvdr
gcrltivpaqtsaedvlkmnpdgiflsngpgdpapcdyaitaiqkfletdipvfgiclgh
qllalasgaktvkmkfghhggnhpvkdveknvvmitaqnhgfavdeatlpanlrvthksl
fdgtlqgihrtdkpafsfqghpeaspgphdaaplfdhfielieqyrkt
>d1ceaa_ 7.14.1.1.3 Plasminogen kringles {Human (Homo sapiens)}
ecktgngknyrgtmsktkngitcqkwsstsphrprfspathpsegleenycrnpdndpqg
pwcyttdpekrydycdilec
>d1ceab_ 7.14.1.1.3 Plasminogen kringles {Human (Homo sapiens)}
ecktgngknyrgtmsktkngitcqkwsstsphrprfspathpsegleenycrnpdndpqg
pwcyttdpekrydycdilec
>d1ceba_ 7.14.1.1.3 Plasminogen kringles {Human (Homo sapiens)}
ecktgngknyrgtmsktkngitcqkwsstsphrprfspathpsegleenycrnpdndpqg
pwcyttdpekrydycdilec
>d1cebb_ 7.14.1.1.3 Plasminogen kringles {Human (Homo sapiens)}
ecktgngknyrgtmsktkngitcqkwsstsphrprfspathpsegleenycrnpdndpqg
pwcyttdpekrydycdilec
>d1cec__ 3.1.7.3.5 Endoglucanase CelC {Clostridium thermocellum}
vsfkaginlggwisqyqvfskehfdtfitekdietiaeagfdhvrlpfdypiiesddnvg
eykedglsyidrclewckkynlglvldmhhapgyrfqdfktstlfedpnqqkrfvdiwrf
lakryinerehiafellnevvepdstrwnklmlecikaireidstmwlyiggnnynspde
lknladidddyivynfhfynpfffthqkahwsesamaynrtvkypgqyegieefvknnpk
ysfmmelnnlklnkellrkdlkpaiefrekkkcklycgefgviaiadlesrikwhedyis
lleeydiggavwnykkmdfeiynedrkpvsqelvnilar
>d1ced__ 1.3.1.1.1 Cytochrome c6 (synonym: cytochrome c553) {Monoraphidium braunii}
eadlalgkavfdgncaachagggnnvipdhtlqkaaieqfldggfnieaivyqiengkga
mpawdgrldedeiagvaayvydqaagnkw
>d1ceea_ 3.30.1.6.11 CDC42 {Human (Homo sapiens)}
mqtikcvvvgdgavgktcllisyttnkfpseyvptvfdnyavtvmiggepytlglfdtag
qedydrlrplsypqtdvflvcfsvvspssfenvkekwvpeithhcpktpfllvgtqidlr
ddpstieklaknkqkpitpetaeklardlkavkyvecsaltqkglknvfdeailaalep
>d1cef__ 5.3.1.1.2 D-ala carboxypeptidase/transpeptidase {Streptomyces R61}
adlpapddtglqavlhtalsqgapgamvrvddngtihqlsegvadratgraitttdrfrv
gsvtksfsavvllqlvdegkldldasvntylpgllpddritvrqvmshrsglydytndmf
aqtvpgfesvrnkvfsyqdlitlslkhgvtnapgaaysysntnfvvagmliekltghsva
teyqnriftplnltdtfyvhpdtvipgthangyltpdeaggalvdsteqtvswaqsagav
isstqdldtffsalmsgqlmsaaqlaqmqqwttvnstqgyglglrrrdlscgisvyghtg
tvqgyytyafaskdgkrsvtalantsnnvnvlntmartlesafcgkp
>d1ceg__ 5.3.1.1.2 D-ala carboxypeptidase/transpeptidase {Streptomyces R61}
adlpapddtglqavlhtalsqgapgamvrvddngtihqlsegvadratgraitttdrfrv
gsvtksfsavvllqlvdegkldldasvntylpgllpddritvrqvmshrsglydytndmf
aqtvpgfesvrnkvfsyqdlitlslkhgvtnapgaaysysntnfvvagmliekltghsva
teyqnriftplnltdtfyvhpdtvipgthangyltpdeaggalvdsteqtvswaqsagav
isstqdldtffsalmsgqlmsaaqlaqmqqwttvnstqgyglglrrrdlscgisvyghtg
tvqgyytyafaskdgkrsvtalantsnnvnvlntmartlesafcgkp
>d1ceh__ 1.123.1.2.12 Phospholipase A2 {Bovine (Bos taurus), pancreas}
alwqfngmikckipsseplldfnnygcycglggsgtpvddldrccqthdncykqakklds
ckvlvdnpytnnysyscsnneitcssennaceaficncnrnaaicfskvpynkehknldk
knc
>d1cei__ 1.29.2.1.1 ImmE7 protein {Escherichia coli}
lknsisdyteaefvqllkeiekenvaatddvldvllehfvkitehpdgtdliyypsdnrd
dspegivkeikewraangkpgfkqg
>d1ceja1 7.3.11.4.2 (1-45) Merozoite surface protein 1 (MSP-1) {Plasmodium falciparum}
nisqhqcvkkqcpqnsgcfrhldereeckcllnykqegdkcvenp
>d1ceja2 7.3.11.4.2 (46-96) Merozoite surface protein 1 (MSP-1) {Plasmodium falciparum}
nptcnennggcdadakcteedsgsngkkitcectkpdsyplfdgifcsssn
>d1cela_ 2.26.1.9.1 Cellobiohydrolase I (cellulase) {Trichoderma reesei}
xsactlqsethppltwqkcssggtctqqtgsvvidanwrwthatnsstncydgntwsstl
cpdnetcaknccldgaayastygvttsgnslsigfvtqsaqknvgarlylmasdttyqef
tllgnefsfdvdvsqlpcglngalyfvsmdadggvskyptntagakygtgycdsqcprdl
kfingqanvegwepssnnantgigghgsccsemdiweansisealtphpcttvgqeiceg
dgcggtysdnryggtcdpdgcdwnpyrlgntsfygpgssftldttkkltvvtqfetsgai
nryyvqngvtfqqpnaelgsysgnelnddyctaeeaefggssfsdkggltqfkkatsggm
vlvmslwddyyanmlwldstyptnetsstpgavrgscstssgvpaqvesqspnakvtfsn
ikfgpigstgnpsg
>d1celb_ 2.26.1.9.1 Cellobiohydrolase I (cellulase) {Trichoderma reesei}
xsactlqsethppltwqkcssggtctqqtgsvvidanwrwthatnsstncydgntwsstl
cpdnetcaknccldgaayastygvttsgnslsigfvtqsaqknvgarlylmasdttyqef
tllgnefsfdvdvsqlpcglngalyfvsmdadggvskyptntagakygtgycdsqcprdl
kfingqanvegwepssnnantgigghgsccsemdiweansisealtphpcttvgqeiceg
dgcggtysdnryggtcdpdgcdwnpyrlgntsfygpgssftldttkkltvvtqfetsgai
nryyvqngvtfqqpnaelgsysgnelnddyctaeeaefggssfsdkggltqfkkatsggm
vlvmslwddyyanmlwldstyptnetsstpgavrgscstssgvpaqvesqspnakvtfsn
ikfgpigstgnpsg
>d1cem__ 1.98.1.2.1 CelA cellulase {Clostridium thermocellum}
agvpfntkypygptsiadnqsevtamlkaewedwkskritsngaggykrvqrdastnydt
vsegmgyglllavcfneqalfddlyryvkshfngnglmhwhidannnvtshdggdgaatd
adedialalifadkqwgssgainygqeartlinnlynhcvehgsyvlkpgdrwggssvtn
psyfapawykvyaqytgdtrwnqvadkcyqiveevkkynngtglvpdwctasgtpasgqs
ydykydatrygwrtavdyswfgdqrakancdmltkffardgakgivdgytiqgskisnnh
nasfigpvaaasmtgydlnfakelyretvavkdseyygyygnslrlltllyitgnfpnpl
sdl
>d1cen__ 3.1.7.3.5 Endoglucanase CelC {Clostridium thermocellum}
mvsfkaginlggwisqyqvfskehfdtfitekdietiaeagfdhvrlpfdypiiesddnv
geykedglsyidrclewckkynlglvldmhhapgyrfqdfktstlfedpnqqkrfvdiwr
flakryinerehiafellnqvvepdstrwnklmlecikaireidstmwlyiggnnynspd
elknladidddyivynfhfynpfffthqkahwsesamaynrtvkypgqyegieefvknnp
kysfmmelnnlklnkellrkdlkpaiefrekkkcklycgefgviaiadlesrikwhedyi
slleeydiggavwnykkmdfeiynedrkpvsqelvnilar
>d1ceo__ 3.1.7.3.5 Endoglucanase CelC {Clostridium thermocellum}
mvsfkaginlggwisqyqvfskehfdtfitekdietiaeagfdhvrlpfdypiiesddnv
geykedglsyidrclewckkynlglvldmhhapgyrfqdfktstlfedpnqqkrfvdiwr
flakryinerehiafellnqvvepdstrwnklmlecikaireidstmwlyiggnnynspd
elknladidddyivynfhfynpfffthqkahwsesamaynrtvkypgqyegieefvknnp
kysfmmelnnlklnkellrkdlkpaiefrekkkcklycgefgviaiadlesrikwhedyi
slleeydiggavwnykkmdfeiynedrkpvsqelvnilar
>d1ceqa1 3.2.1.5.11 (19-163) Lactate dehydrogenase {Malarial parasite (Plasmodium falciparum)}
pkakivlvgsgmiggvmatlivqknlgdvvlfdivknmphgkaldtshtnvmaysnckvs
gsntyddlagsdvvivtagftkapgksdkewnrddllplnnkimieigghikkncpnafi
ivvtnpvdvmvqllhqhsgvpknkiigl
>d1ceqa2 4.132.1.1.11 (164-329) Lactate dehydrogenase {Malarial parasite (Plasmodium falciparum)}
ggvldtsrlkyyisqklnvcprdvnahivgahgnkmvllkryitvggiplqefinnklis
daeleaifdrtvntaleivnlhaspyvapaaaiiemaesylkdlkkvlicstllegqygh
sdifggtpvvlgangveqvielqlnseekakfdeaiaetkrmkala
>d1cero1 3.2.1.3.3 (1-148,313-333) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Thermus aquaticus}
mkvgingfgrigrqvfrilhsrgvevalindltdnktlahllkydsiyhrfpgevayddq
ylyvdgkairatavkdpkeipwaeagvgvviestgvftdadkakahleggakkviitapa
kgeditivmgvnheaydpsrhhiisnasXnewgyanrvadlvelvlrkgv
>d1cero2 4.61.1.1.3 (149-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Thermus aquaticus}
cttnslapvmkvleeafgvekalmttvhsytndqrlldlphkdlrraraaainiiptttg
aakatalvlpslkgrfdgmalrvptatgsisditallkrevtaeevnaalkaaaegplkg
ilaytedeivlqdivmdphssivdakltkalgnmvkvfawyd
>d1cerp1 3.2.1.3.3 (1-148,313-333) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Thermus aquaticus}
mkvgingfgrigrqvfrilhsrgvevalindltdnktlahllkydsiyhrfpgevayddq
ylyvdgkairatavkdpkeipwaeagvgvviestgvftdadkakahleggakkviitapa
kgeditivmgvnheaydpsrhhiisnasXnewgyanrvadlvelvlrkgv
>d1cerp2 4.61.1.1.3 (149-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Thermus aquaticus}
cttnslapvmkvleeafgvekalmttvhsytndqrlldlphkdlrraraaainiiptttg
aakatalvlpslkgrfdgmalrvptatgsisditallkrevtaeevnaalkaaaegplkg
ilaytedeivlqdivmdphssivdakltkalgnmvkvfawyd
>d1cerq1 3.2.1.3.3 (1-148,313-333) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Thermus aquaticus}
mkvgingfgrigrqvfrilhsrgvevalindltdnktlahllkydsiyhrfpgevayddq
ylyvdgkairatavkdpkeipwaeagvgvviestgvftdadkakahleggakkviitapa
kgeditivmgvnheaydpsrhhiisnasXnewgyanrvadlvelvlrkgv
>d1cerq2 4.61.1.1.3 (149-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Thermus aquaticus}
cttnslapvmkvleeafgvekalmttvhsytndqrlldlphkdlrraraaainiiptttg
aakatalvlpslkgrfdgmalrvptatgsisditallkrevtaeevnaalkaaaegplkg
ilaytedeivlqdivmdphssivdakltkalgnmvkvfawyd
>d1cerr1 3.2.1.3.3 (1-148,313-333) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Thermus aquaticus}
mkvgingfgrigrqvfrilhsrgvevalindltdnktlahllkydsiyhrfpgevayddq
ylyvdgkairatavkdpkeipwaeagvgvviestgvftdadkakahleggakkviitapa
kgeditivmgvnheaydpsrhhiisnasXnewgyanrvadlvelvlrkgv
>d1cerr2 4.61.1.1.3 (149-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Thermus aquaticus}
cttnslapvmkvleeafgvekalmttvhsytndqrlldlphkdlrraraaainiiptttg
aakatalvlpslkgrfdgmalrvptatgsisditallkrevtaeevnaalkaaaegplkg
ilaytedeivlqdivmdphssivdakltkalgnmvkvfawyd
>d1cesa_ 2.26.1.1.1 Concanavalin A {Jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1cesb_ 2.26.1.1.1 Concanavalin A {Jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1ceta1 3.2.1.5.11 (18-163) Lactate dehydrogenase {Malarial parasite (Plasmodium falciparum)}
apkakivlvgsgmiggvmatlivqknlgdvvlfdivknmphgkaldtshtnvmaysnckv
sgsntyddlagsdvvivtagftkapgksdkewnrldllplnnkimieigghikkncpnaf
iivvtnpvdvmvqllhqhsgvpknkiigl
>d1ceta2 4.132.1.1.11 (164-329) Lactate dehydrogenase {Malarial parasite (Plasmodium falciparum)}
ggvldtsrlkyyisqklnvcprdvnahivgahgnkmvllkryitvggiplqefinnklis
daeleaifdrtvntaleivnlhaspyvapaaaiiemaesylkdlkkvlicstllegqygh
sdifggtpvvlgangveqvielqlnseekakfdeaiaetkrmkala
>d1ceva_ 3.34.1.1.2 Arginase {Bacillus caldevelox}
mkpisiigvpmdlgqtrrgvdmgpsamryagvierlerlhydiedlgdipigkaerlheq
gdsrlrnlkavaeaneklaaavdqvvqrgrfplvlggdhsiaigtlagvakhyerlgviw
ydahgdvntaetspsgnihgmplaaslgfghpaltqiggyspkikpehvvligvrsldeg
ekkfirekgikiytmhevdrlgmtrvmeetiaylkertdgvhlsldldgldpsdapgvgt
pviggltyreshlamemlaeaqiitsaefvevnpildernktasvavalmgslfgeklm
>d1cevb_ 3.34.1.1.2 Arginase {Bacillus caldevelox}
mkpisiigvpmdlgqtrrgvdmgpsamryagvierlerlhydiedlgdipigkaerlheq
gdsrlrnlkavaeaneklaaavdqvvqrgrfplvlggdhsiaigtlagvakhyerlgviw
ydahgdvntaetspsgnihgmplaaslgfghpaltqiggyspkikpehvvligvrsldeg
ekkfirekgikiytmhevdrlgmtrvmeetiaylkertdgvhlsldldgldpsdapgvgt
pviggltyreshlamemlaeaqiitsaefvevnpildernktasvavalmgslfgeklm
>d1cevc_ 3.34.1.1.2 Arginase {Bacillus caldevelox}
mkpisiigvpmdlgqtrrgvdmgpsamryagvierlerlhydiedlgdipigkaerlheq
gdsrlrnlkavaeaneklaaavdqvvqrgrfplvlggdhsiaigtlagvakhyerlgviw
ydahgdvntaetspsgnihgmplaaslgfghpaltqiggyspkikpehvvligvrsldeg
ekkfirekgikiytmhevdrlgmtrvmeetiaylkertdgvhlsldldgldpsdapgvgt
pviggltyreshlamemlaeaqiitsaefvevnpildernktasvavalmgslfgeklm
>d1cevd_ 3.34.1.1.2 Arginase {Bacillus caldevelox}
mkpisiigvpmdlgqtrrgvdmgpsamryagvierlerlhydiedlgdipigkaerlheq
gdsrlrnlkavaeaneklaaavdqvvqrgrfplvlggdhsiaigtlagvakhyerlgviw
ydahgdvntaetspsgnihgmplaaslgfghpaltqiggyspkikpehvvligvrsldeg
ekkfirekgikiytmhevdrlgmtrvmeetiaylkertdgvhlsldldgldpsdapgvgt
pviggltyreshlamemlaeaqiitsaefvevnpildernktasvavalmgslfgeklm
>d1ceve_ 3.34.1.1.2 Arginase {Bacillus caldevelox}
mkpisiigvpmdlgqtrrgvdmgpsamryagvierlerlhydiedlgdipigkaerlheq
gdsrlrnlkavaeaneklaaavdqvvqrgrfplvlggdhsiaigtlagvakhyerlgviw
ydahgdvntaetspsgnihgmplaaslgfghpaltqiggyspkikpehvvligvrsldeg
ekkfirekgikiytmhevdrlgmtrvmeetiaylkertdgvhlsldldgldpsdapgvgt
pviggltyreshlamemlaeaqiitsaefvevnpildernktasvavalmgslfgeklm
>d1cevf_ 3.34.1.1.2 Arginase {Bacillus caldevelox}
mkpisiigvpmdlgqtrrgvdmgpsamryagvierlerlhydiedlgdipigkaerlheq
gdsrlrnlkavaeaneklaaavdqvvqrgrfplvlggdhsiaigtlagvakhyerlgviw
ydahgdvntaetspsgnihgmplaaslgfghpaltqiggyspkikpehvvligvrsldeg
ekkfirekgikiytmhevdrlgmtrvmeetiaylkertdgvhlsldldgldpsdapgvgt
pviggltyreshlamemlaeaqiitsaefvevnpildernktasvavalmgslfgeklm
>d1cewi_ 4.15.1.2.1 Cystatin {Chicken (Gallus gallus)}
gapvpvdendeglqralqfamaeynrasndkyssrvvrvisakrqlvsgikyilqveigr
ttcpkssgdlqscefhdepemakyttctfvvysipwlnqiklleskcq
>d1cex__ 3.16.7.1.1 Cutinase {Fungus (Fusarium solani), subsp. Pisi}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1cey__ 3.16.2.1.2 CheY protein {Salmonella typhimurium}
adkelkflvvddfstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmp
nmdglellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleekln
kifeklgm
>d1ceza_ 5.8.1.3.1 T7 RNA polymerase {Bacteriophage T7}
iakndfsdielaaipfntladhygerlareqlalehesyemgearfrkmferqlkageva
dnaaakplittllpkmiarindwfeevkakrgkrptafqflqeikpeavayitikttlac
ltsadnttvqavasaigraiedearfgrirdleakhfkknveeqlnkrvghvykkafmqv
veadmlskgllggeawsswhkedsihvgvrciemliestgmvslhrqnagvvgqdsetie
lapeyaeaiatragalagispmfqpcvvppkpwtgitgggywangrrplalvrthskkal
mryedvympevykainiaqntawkinkkvlavanvitkwkhcpvedipaiereelpmkpe
didmnpealtawkraaaavyrkdkarksrrislefmleqankfanhkaiwfpynmdwrgr
vyavsmfnpqgndmtkglltlakgkpigkegyywlkihgancagvdkvpfperikfieen
henimacaksplentwwaeqdspfcflafcfeyagvqhhglsyncslplafdgscsgiqh
fsamlrdevggravnllpsetvqdiygivakkvneilqadaingtdnevvtvtdentgei
sekvklgtkalagqwlaygvtrsvtkrsvmtlaygskefgfrqqvledtiqpaidsgkgl
mftqpnqaagymakliwesvsvtvvaaveamnwlksaakllaaevkdkktgeilrkrcav
hwvtpdgfpvwqeykkpiqtrlnlmflgqfrlqptintnkdseidahkqesgiapnfvhs
qdgshlrktvvwahekygiesfalihdsfgtipadaanlfkavretmvdtyescdvladf
ydqfadqlhesqldkmpalpakgnlnlrdilesdfafa
>d1cf0a_ 4.86.1.1.2 Profilin (actin-binding protein) {Human (Homo sapiens)}
gwnayidnlmadgtcqdaaivgykdspsvwaavpgktfvnitpaevgvlvgkdrssfyvn
gltlggqkcsvirdsllqdgefsmdlrtkstggaptfnvtvtktdktlvllmgkegvhgg
linkkcyemashlrrsqy
>d1cf0b_ 4.86.1.1.2 Profilin (actin-binding protein) {Human (Homo sapiens)}
gwnayidnlmadgtcqdaaivgykdspsvwaavpgktfvnitpaevgvlvgkdrssfyvn
gltlggqkcsvirdsllqdgefsmdlrtkstggaptfnvtvtktdktlvllmgkegvhgg
linkkcyemashlrrsqy
>d1cf1a1 2.1.1.5.19 (10-182) Arrestin {Bovine (Bos taurus)}
hvifkkisrdksvtiylgkrdyidhvervepvdgvvlvdpelvkgkrvyvsltcafrygq
edidvmglsfrrdlyfsqvqvfppvgasgattrlqeslikklgantypflltfpdylpcs
vmlqpapqdvgkscgvdfeikafathstdveedkipkkssvrllirkvqhapr
>d1cf1a2 2.1.1.5.19 (183-393) Arrestin {Bovine (Bos taurus)}
dmgpqpraeaswqffmsdkplrlavslskeiyyhgepipvtvavtnstektvkkikvlve
qvtnvvlyssdyyiktvaaeeaqekvppnssltktltlvpllannrerrgialdgkikhe
dtnlasstiikegidktvmgilvsyqikvkltvsgllgeltssevatevpfrlmhpqped
pdtakesfqdenfvfeefarqnlkdageyke
>d1cf1b1 2.1.1.5.19 (9-182) Arrestin {Bovine (Bos taurus)}
nhvifkkisrdksvtiylgkrdyidhvervepvdgvvlvdpelvkgkrvyvsltcafryg
qedidvmglsfrrdlyfsqvqvfppvgasgattrlqeslikklgantypflltfpdylpc
svmlqpapqdvgkscgvdfeikafathstdveedkipkkssvrllirkvqhapr
>d1cf1b2 2.1.1.5.19 (183-385) Arrestin {Bovine (Bos taurus)}
dmgpqpraeaswqffmsdkplrlavslskeiyyhgepipvtvavtnstektvkkikvlve
qvtnvvlyssdyyiktvaaeeaqekvppnssltktltlvpllannrerrgialdgkikhe
dtnlasstiikegidktvmgilvsyqikvkltvsgllgeltssevatevpfrlmhpqped
pdtakesfqdenfvfeefarqnl
>d1cf1c1 2.1.1.5.19 (7-182) Arrestin {Bovine (Bos taurus)}
apnhvifkkisrdksvtiylgkrdyidhvervepvdgvvlvdpelvkgkrvyvsltcafr
ygqedidvmglsfrrdlyfsqvqvfppvgasgattrlqeslikklgantypflltfpdyl
pcsvmlqpapqdvgkscgvdfeikafathstdveedkipkkssvrllirkvqhapr
>d1cf1c2 2.1.1.5.19 (183-393) Arrestin {Bovine (Bos taurus)}
dmgpqpraeaswqffmsdkplrlavslskeiyyhgepipvtvavtnstektvkkikvlve
qvtnvvlyssdyyiktvaaeeaqekvppnssltktltlvpllannrerrgialdgkikhe
dtnlasstiikegidktvmgilvsyqikvkltvsgllgeltssevatevpfrlmhpqped
pdtakesfqdenfvfeefarqnlkdageyke
>d1cf1d1 2.1.1.5.19 (9-182) Arrestin {Bovine (Bos taurus)}
nhvifkkisrdksvtiylgkrdyidhvervepvdgvvlvdpelvkgkrvyvsltcafryg
qedidvmglsfrrdlyfsqvqvfppvgasgattrlqeslikklgantypflltfpdylpc
svmlqpapqdvgkscgvdfeikafathstdveedkipkkssvrllirkvqhapr
>d1cf1d2 2.1.1.5.19 (183-386) Arrestin {Bovine (Bos taurus)}
dmgpqpraeaswqffmsdkplrlavslskeiyyhgepipvtvavtnstektvkkikvlve
qvtnvvlyssdyyiktvaaeeaqekvppnssltktltlvpllannrerrgialdgkikhe
dtnlasstiikegidktvmgilvsyqikvkltvsgllgeltssevatevpfrlmhpqped
pdtakesfqdenfvfeefarqnlk
>d1cf3a1 3.3.1.2.6 (3-324,521-583) Glucose oxidase {Aspergillus niger}
gieaslltdpkdvsgrtvdyiiagggltglttaarltenpnisvlviesgsyesdrgpii
edlnaygdifgssvdhayetvelatnnqtalirsgnglggstlvnggtwtrphkaqvdsw
etvfgnegwnwdnvaayslqaerarapnakqiaaghyfnaschgvngtvhagprdtgddy
spivkalmsavedrgvptkkdfgcgdphgvsmfpntlhedqvrsdaarewllpnyqrpnl
qvltgqyvgkvllsqngttpravgvefgthkgnthnvyakhevllaagsavsptileysg
igmksileplgidtvvdlpvglXcsmmpkemggvvdnaarvygvqglrvidgsipptqms
shvmtvfyamalkisdailedyasmq
>d1cf3a2 4.14.1.4.1 (325-520) Glucose oxidase {Aspergillus niger}
nlqdqttatvrsritsagagqgqaawfatfnetfgdysekahellntkleqwaeeavarg
gfhnttalliqyenyrdwivnhnvayselfldtagvasfdvwdllpftrgyvhildkdpy
lhhfaydpqyflneldllgqaaatqlarnisnsgamqtyfagetipgdnlaydadlsawt
eyipyhfrpnyhgvgt
>d1cf4a_ 3.30.1.6.11 CDC42 {Human (Homo sapiens)}
mqtikcvvvgdgavgktcllisyttnkfpseyvptvfdnyavtvmiggepytlglfdtag
ledydrlrplsypqtdvflvcfsvvspssfenvkekwvpeithhcpktpfllvgtqidlr
ddpstieklaknkqkpitpetaeklardlkavkyvecsaltqkglknvfdeailaalepp
epkk
>d1cf5a_ 4.135.1.1.4 Beta-momorcharin {Bitter gourd (Momordica charantia)}
dvnfdlstataktytkfiedfratlpfshkvydipllystisdsrrfillnltsyayeti
svaidvtnvyvvayrtrdvsyffkesppeaynilfkgtrkitlpytgnyenlqtaahkir
enidlglpalssaittlfyynaqsapsallvliqttaeaarfkyierhvakyvatnfkpn
laiislenqwsalskqiflaqnqggkfrnpvdlikptgqrfqvtnvdsdvvkgnikllln
srastaden
>d1cf5b_ 4.135.1.1.4 Beta-momorcharin {Bitter gourd (Momordica charantia)}
dvnfdlstataktytkfiedfratlpfshkvydipllystisdsrrfillnltsyayeti
svaidvtnvyvvayrtrdvsyffkesppeaynilfkgtrkitlpytgnyenlqtaahkir
enidlglpalssaittlfyynaqsapsallvliqttaeaarfkyierhvakyvatnfkpn
laiislenqwsalskqiflaqnqggkfrnpvdlikptgqrfqvtnvdsdvvkgnikllln
srastaden
>d1cf7a_ 1.4.3.14.1 Cell cycle transcription factor e2f-dp {Human (Homo sapiens)}
srhekslgllttkfvsllqeakdgvldlklaadtlavrqkrriyditnvlegigliekks
knsiqwk
>d1cf7b_ 1.4.3.14.1 Cell cycle transcription factor e2f-dp {Human (Homo sapiens)}
gkglrhfsmkvcekvqrkgttsynevadelvseftnsnnhlaadsaydqknirrrvydal
nvlmamniiskekkeikwiglp
>d1cf8h1 2.1.1.1.134 (1-113) Immunoglobulin (variable domains of L and H chains) {Catalytic Fab 19A4 (mouse), kappa L chain}
dvqlqesgpglvkpsqslsltctvtgysitsgyawnwirqfpgnklewmgyirysgdtry
npslksrisitrdtsknqfflqlnsvttedtatyycaigygnsdywgqgtlvtvsa
>d1cf8h2 2.1.1.2.132 (114-215) Immunoglobulin (constant domains of L and H chains) {Catalytic Fab 19A4 (mouse), kappa L chain}
akttppsvyplapgcgdttgssvtlgclvkgyfpesvtvtwnsgslsssvhafpallqsd
lytmsssvtvpsstwpsqtvtcsvahpassttvdkklepkdc
>d1cf8l1 2.1.1.1.134 (1-107) Immunoglobulin (variable domains of L and H chains) {Catalytic Fab 19A4 (mouse), kappa L chain}
divltqsptimsvspgekvtltcsasssvssnyvywyqqkpgsspkvwiystsnlasgvp
arfsgsgsgtsysltissmeaedaasyfclqwssfpytfgggtklelk
>d1cf8l2 2.1.1.2.132 (108-214) Immunoglobulin (constant domains of L and H chains) {Catalytic Fab 19A4 (mouse), kappa L chain}
radvaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1cf9a1 3.16.1.1.1 (598-753) Catalase, C-terminal domain {Escherichia coli, HPII}
vkgrvvaillndevrsadllailkalkakgvhakllysrmgevtaddgtvlpiaatfaga
psltvdavivpcgniadiadngdanyylmeaykhlkpialagdarkfkatikiadqgeeg
iveadsadgsfmdelltlmaahrvwsripkidkipa
>d1cf9a2 5.5.1.1.6 (27-597) Catalase II {Escherichia coli, PHII}
dslapedgshrpaaeptppgaqptapgslkapdtrneklnsledvrkgsenyalttnqgv
riaddqnslragsrgptlledfilrekithfdheriperivhargsaahgyfqpykslsd
itkadflsdpnkitpvfvrfstcqggagsadtvrdirgfatkfyteegifdlvgnntpif
fiqdahkfpdfvhavkpephwaipqgqsahdtfwdyvslqpetlhnvmwamsdrgiprsy
rtmegfgihtfrlinaegkatfvrfhwkplagkaslvwdeaqkltgrdpdfhrrelweai
eagdfpeyelgfqlipeedefkfdfdlldptklipeelvpvqrvgkmvlnrnpdnffaen
eqaafhpghivpgldftndpllqgrlfsytdtqisrlggpnfheipinrptcpyhnfqrd
gmhrmgidtnpanyepnsindnwpretppgpkrggfesyqervegnkvrerspsfgeyys
hprlfwlsqtpfeqrhivdgfsfelskvvrpyirervvdqlahidltlaqavaknlgiel
tddqlnitpppdvnglkkdpslslyaipdgd
>d1cf9b1 3.16.1.1.1 (598-753) Catalase, C-terminal domain {Escherichia coli, HPII}
vkgrvvaillndevrsadllailkalkakgvhakllysrmgevtaddgtvlpiaatfaga
psltvdavivpcgniadiadngdanyylmeaykhlkpialagdarkfkatikiadqgeeg
iveadsadgsfmdelltlmaahrvwsripkidkipa
>d1cf9b2 5.5.1.1.6 (27-597) Catalase II {Escherichia coli, PHII}
dslapedgshrpaaeptppgaqptapgslkapdtrneklnsledvrkgsenyalttnqgv
riaddqnslragsrgptlledfilrekithfdheriperivhargsaahgyfqpykslsd
itkadflsdpnkitpvfvrfstcqggagsadtvrdirgfatkfyteegifdlvgnntpif
fiqdahkfpdfvhavkpephwaipqgqsahdtfwdyvslqpetlhnvmwamsdrgiprsy
rtmegfgihtfrlinaegkatfvrfhwkplagkaslvwdeaqkltgrdpdfhrrelweai
eagdfpeyelgfqlipeedefkfdfdlldptklipeelvpvqrvgkmvlnrnpdnffaen
eqaafhpghivpgldftndpllqgrlfsytdtqisrlggpnfheipinrptcpyhnfqrd
gmhrmgidtnpanyepnsindnwpretppgpkrggfesyqervegnkvrerspsfgeyys
hprlfwlsqtpfeqrhivdgfsfelskvvrpyirervvdqlahidltlaqavaknlgiel
tddqlnitpppdvnglkkdpslslyaipdgd
>d1cf9c1 3.16.1.1.1 (598-753) Catalase, C-terminal domain {Escherichia coli, HPII}
vkgrvvaillndevrsadllailkalkakgvhakllysrmgevtaddgtvlpiaatfaga
psltvdavivpcgniadiadngdanyylmeaykhlkpialagdarkfkatikiadqgeeg
iveadsadgsfmdelltlmaahrvwsripkidkipa
>d1cf9c2 5.5.1.1.6 (27-597) Catalase II {Escherichia coli, PHII}
dslapedgshrpaaeptppgaqptapgslkapdtrneklnsledvrkgsenyalttnqgv
riaddqnslragsrgptlledfilrekithfdheriperivhargsaahgyfqpykslsd
itkadflsdpnkitpvfvrfstcqggagsadtvrdirgfatkfyteegifdlvgnntpif
fiqdahkfpdfvhavkpephwaipqgqsahdtfwdyvslqpetlhnvmwamsdrgiprsy
rtmegfgihtfrlinaegkatfvrfhwkplagkaslvwdeaqkltgrdpdfhrrelweai
eagdfpeyelgfqlipeedefkfdfdlldptklipeelvpvqrvgkmvlnrnpdnffaen
eqaafhpghivpgldftndpllqgrlfsytdtqisrlggpnfheipinrptcpyhnfqrd
gmhrmgidtnpanyepnsindnwpretppgpkrggfesyqervegnkvrerspsfgeyys
hprlfwlsqtpfeqrhivdgfsfelskvvrpyirervvdqlahidltlaqavaknlgiel
tddqlnitpppdvnglkkdpslslyaipdgd
>d1cf9d1 3.16.1.1.1 (598-753) Catalase, C-terminal domain {Escherichia coli, HPII}
vkgrvvaillndevrsadllailkalkakgvhakllysrmgevtaddgtvlpiaatfaga
psltvdavivpcgniadiadngdanyylmeaykhlkpialagdarkfkatikiadqgeeg
iveadsadgsfmdelltlmaahrvwsripkidkipa
>d1cf9d2 5.5.1.1.6 (27-597) Catalase II {Escherichia coli, PHII}
dslapedgshrpaaeptppgaqptapgslkapdtrneklnsledvrkgsenyalttnqgv
riaddqnslragsrgptlledfilrekithfdheriperivhargsaahgyfqpykslsd
itkadflsdpnkitpvfvrfstcqggagsadtvrdirgfatkfyteegifdlvgnntpif
fiqdahkfpdfvhavkpephwaipqgqsahdtfwdyvslqpetlhnvmwamsdrgiprsy
rtmegfgihtfrlinaegkatfvrfhwkplagkaslvwdeaqkltgrdpdfhrrelweai
eagdfpeyelgfqlipeedefkfdfdlldptklipeelvpvqrvgkmvlnrnpdnffaen
eqaafhpghivpgldftndpllqgrlfsytdtqisrlggpnfheipinrptcpyhnfqrd
gmhrmgidtnpanyepnsindnwpretppgpkrggfesyqervegnkvrerspsfgeyys
hprlfwlsqtpfeqrhivdgfsfelskvvrpyirervvdqlahidltlaqavaknlgiel
tddqlnitpppdvnglkkdpslslyaipdgd
>d1cfaa_ 1.52.1.1.1 C5a anaphylotoxin {Human (Homo sapiens)}
mlqkkieeiaakykhsvvkkccydgasvnndetceqraarislgprcikafteccvvasq
lranishkdmc
>d1cfb_1 2.1.2.1.6 (610-709) Neuroglian, two amino proximal Fn3 repeats {Drosophila melanogaster}
ivqdvpnapkltgitcqadkaeihweqqgdnrspilhytiqfntsftpaswdaayekvpn
tdssfvvqmspwanytfrviafnkigasppsahsdscttq
>d1cfb_2 2.1.2.1.6 (710-814) Neuroglian, two amino proximal Fn3 repeats {Drosophila melanogaster}
pdvpfknpdnvvgqgtepnnlviswtpmpeiehnapnfhyyvswkrdipaaawennnifd
wrqnniviadqptfvkylikvvaindrgesnvaaeevvgysgedr
>d1cfc__ 1.42.1.5.11 Calmodulin {African frog (Xenopus laevis)}
adqlteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgn
gtidfpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdee
vdemireadidgdgqvnyeefvqmmtak
>d1cfd__ 1.42.1.5.11 Calmodulin {African frog (Xenopus laevis)}
adqlteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgn
gtidfpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdee
vdemireadidgdgqvnyeefvqmmtak
>d1cfe__ 4.87.1.1.1 P14a {Tomato (Lycopersicon esculentum)}
qnspqdylavhndaraqvgvgpmswdanlasraqnyansragdcnlihsgagenlakggg
dftgraavqlwvserpsynyatnqcvggkkcrhytqvvwrnsvrlgcgrarcnngwwfis
cnydpvgnwigqrpy
>d1cffa_ 1.42.1.5.11 Calmodulin {African frog (Xenopus laevis)}
adqlteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgn
gtidfpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdee
vdemireadidgdgqvnyeefvqmmtak
>d1cfh__ 7.28.1.1.3 Coagulation factor IX (IXa) {Human (Homo sapiens)}
ynsgkleefvqgnlerecmeekcsfeearevfenterttefwkqyvd
>d1cfja_ 3.59.1.1.1 Acetylcholinesterase {Electric ray (Torpedo californica)}
sellvntksgkvmgtrvpvlsshisaflgipfaeppvgnmrfrrpepkkpwsgvwnasty
pnncqqyvdeqfpgfsgsemwnpnremsedclylniwvpsprpksttvmvwiygggfysg
sstldvyngkylayteevvlvslsyrvgafgflalhgsqeapgnvglldqrmalqwvhdn
iqffggdpktvtifgesaggasvgmhilspgsrdlfrrailqsgspncpwasvsvaegrr
ravelgrnlncnlnsdeelihclrekkpqelidvewnvlpfdsifrfsfvpvidgeffpt
slesmlnsgnfkktqillgvnkdegsffllygapgfskdseskisredfmsgvklsvpha
ndlgldavtlqytdwmddnngiknrdglddivgdhnvicplmhfvnkytkfgngtylyff
nhrasnlvwpewmgvihgyeiefvfglplvkelnytaeeealsrrimhywatfaktgnpn
ephsqeskwplfttkeqkfidlntepmkvhqrlrvqmcvfwnqflpkllnat
>d1cfma1 2.2.6.1.2 (1-168,233-251) Cytochrome f, large domain {Chlamydomonas reinhardtii}
ypvfaqqnyanpreangrivcanchlaqkaveievpqavlpdtvfeavielpydkqvkqv
langkkgdlnvgmvlilpegfelappdrvpaeikekvgnlyyqpyspeqknilvvgpvpg
kkysemvvpilspdpaknknvsylkypiyfggnrgrgqvypdgkksnnXnvggfgqaete
ivlqnpar
>d1cfma2 2.74.2.2.2 (169-232) Cytochrome f, small domain {Chlamydomonas reinhardtii}
tiynasaagkivaitalsekkggfevsiekangevvvdkipagpdlivkegqtvqadqpl
tnnp
>d1cfmb1 2.2.6.1.2 (1-168,233-251) Cytochrome f, large domain {Chlamydomonas reinhardtii}
ypvfaqqnyanpreangrivcanchlaqkaveievpqavlpdtvfeavielpydkqvkqv
langkkgdlnvgmvlilpegfelappdrvpaeikekvgnlyyqpyspeqknilvvgpvpg
kkysemvvpilspdpaknknvsylkypiyfggnrgrgqvypdgkksnnXnvggfgqaete
ivlqnpar
>d1cfmb2 2.74.2.2.2 (169-232) Cytochrome f, small domain {Chlamydomonas reinhardtii}
tiynasaagkivaitalsekkggfevsiekangevvvdkipagpdlivkegqtvqadqpl
tnnp
>d1cfmc1 2.2.6.1.2 (1-168,233-251) Cytochrome f, large domain {Chlamydomonas reinhardtii}
ypvfaqqnyanpreangrivcanchlaqkaveievpqavlpdtvfeavielpydkqvkqv
langkkgdlnvgmvlilpegfelappdrvpaeikekvgnlyyqpyspeqknilvvgpvpg
kkysemvvpilspdpaknknvsylkypiyfggnrgrgqvypdgkksnnXnvggfgqaete
ivlqnpar
>d1cfmc2 2.74.2.2.2 (169-232) Cytochrome f, small domain {Chlamydomonas reinhardtii}
tiynasaagkivaitalsekkggfevsiekangevvvdkipagpdlivkegqtvqadqpl
tnnp
>d1cfna1 2.1.1.1.126 (1-107) Immunoglobulin (variable domains of L and H chains) {Anti-p24 (HIV-1) Fab CB 4-1 (mouse), kappa L chain}
dikmtqspssmytslgervtitckasqdinsfltwflqkpgkspktliyranrlmigvps
rfsgsgsgqtysltissleyedmgiyyclqyddfpltfgagtkldlk
>d1cfna2 2.1.1.2.124 (108-214) Immunoglobulin (constant domains of L and H chains) {Anti-p24 (HIV-1) Fab CB 4-1 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkeinvkwkidgserqngvldswteqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1cfnb1 2.1.1.1.126 (1-112) Immunoglobulin (variable domains of L and H chains) {Anti-p24 (HIV-1) Fab CB 4-1 (mouse), kappa L chain}
qdqlqqsgaelvrpgasvklsckalgyiftdyeihwvkqtpvhglewiggihpgssgtay
nqkfkgkatltadkssttafmelssltsedsavyyctrkdywgqgtlvtvsa
>d1cfnb2 2.1.1.2.124 (113-213) Immunoglobulin (constant domains of L and H chains) {Anti-p24 (HIV-1) Fab CB 4-1 (mouse), kappa L chain}
akttapsvyplvpvcggttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpallqsg
lytlsssvtvtsntwpsqtitcnvahpasstkvdkkieprv
>d1cfpa_ 1.42.1.2.3 Calcyclin (S100) {Bovine (Bos taurus), s100b}
mselekavvalidvfhqysgregdkhklkkselkelinnelshfleeikeqevvdkvmet
ldsdgdgecdfqefmafvamittacheffehe
>d1cfpb_ 1.42.1.2.3 Calcyclin (S100) {Bovine (Bos taurus), s100b}
mselekavvalidvfhqysgregdkhklkkselkelinnelshfleeikeqevvdkvmet
ldsdgdgecdfqefmafvamittacheffehe
>d1cfqa1 2.1.1.1.126 (1-107) Immunoglobulin (variable domains of L and H chains) {Anti-p24 (HIV-1) Fab CB 4-1 (mouse), kappa L chain}
dikmtqspssmytslgervtitckasqdinsfltwflqkpgkspktliyranrlmigvps
rfsgsgsgqtysltissleyedmgiyyclqyddfpltfgagtkldlk
>d1cfqa2 2.1.1.2.124 (108-214) Immunoglobulin (constant domains of L and H chains) {Anti-p24 (HIV-1) Fab CB 4-1 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkeinvkwkidgserqngvldswteqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1cfqb1 2.1.1.1.126 (1-112) Immunoglobulin (variable domains of L and H chains) {Anti-p24 (HIV-1) Fab CB 4-1 (mouse), kappa L chain}
qdqlqqsgaelvrpgasvklsckalgyiftdyeihwvkqtpvhglewiggihpgssgtay
nqkfkgkatltadkssttafmelssltsedsavyyctrkdywgqgtlvtvsa
>d1cfqb2 2.1.1.2.124 (113-213) Immunoglobulin (constant domains of L and H chains) {Anti-p24 (HIV-1) Fab CB 4-1 (mouse), kappa L chain}
akttapsvyplvpvcggttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpallqsg
lytlsssvtvtsntwpsqtitcnvahpasstkvdkkieprv
>d1cfr__ 3.43.1.5.1 Restriction endonuclease Cfr10I {Citrobacter freundii}
mdiisksgegnkytinsaiafvayashidinttefskvlsglrdfindeairlggkisdg
sfnkcngdwyewligiraiefflesetnfivvkmpnatsfdvmsiyksclsefiydlrsk
lslnnvnlitsnpdfsiidirgrreelksmlkdisfsnislstiseidnlyknfidyael
ehiksflsvkttfrpdrrlqlahegslmkalythlqtrtwtinptgiryyaaatsignad
viglktvathsitdvkslpqsavdeifkinsvldvdsclshil
>d1cfsa1 2.1.1.1.126 (1-107) Immunoglobulin (variable domains of L and H chains) {Anti-p24 (HIV-1) Fab CB 4-1 (mouse), kappa L chain}
dikmtqspssmytslgervtitckasqdinsfltwflqkpgkspktliyranrlmigvps
rfsgsgsgqtysltissleyedmgiyyclqyddfpltfgagtkldlk
>d1cfsa2 2.1.1.2.124 (108-214) Immunoglobulin (constant domains of L and H chains) {Anti-p24 (HIV-1) Fab CB 4-1 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkeinvkwkidgserqngvldswteqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1cfsb1 2.1.1.1.126 (1-112) Immunoglobulin (variable domains of L and H chains) {Anti-p24 (HIV-1) Fab CB 4-1 (mouse), kappa L chain}
qdqlqqsgaelvrpgasvklsckalgyiftdyeihwvkqtpvhglewiggihpgssgtay
nqkfkgkatltadkssttafmelssltsedsavyyctrkdywgqgtlvtvsa
>d1cfsb2 2.1.1.2.124 (113-213) Immunoglobulin (constant domains of L and H chains) {Anti-p24 (HIV-1) Fab CB 4-1 (mouse), kappa L chain}
akttapsvyplvpvcggttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpallqsg
lytlsssvtvtsntwpsqtitcnvahpasstkvdkkieprv
>d1cfta1 2.1.1.1.126 (1-107) Immunoglobulin (variable domains of L and H chains) {Anti-p24 (HIV-1) Fab CB 4-1 (mouse), kappa L chain}
dikmtqspssmytslgervtitckasqdinsfltwflqkpgkspktliyranrlmigvps
rfsgsgsgqtysltissleyedmgiyyclqyddfpltfgagtkldlk
>d1cfta2 2.1.1.2.124 (108-214) Immunoglobulin (constant domains of L and H chains) {Anti-p24 (HIV-1) Fab CB 4-1 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkeinvkwkidgserqngvldswteqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1cftb1 2.1.1.1.126 (1-112) Immunoglobulin (variable domains of L and H chains) {Anti-p24 (HIV-1) Fab CB 4-1 (mouse), kappa L chain}
qdqlqqsgaelvrpgasvklsckalgyiftdyeihwvkqtpvhglewiggihpgssgtay
nqkfkgkatltadkssttafmelssltsedsavyyctrkdywgqgtlvtvsa
>d1cftb2 2.1.1.2.124 (113-213) Immunoglobulin (constant domains of L and H chains) {Anti-p24 (HIV-1) Fab CB 4-1 (mouse), kappa L chain}
akttapsvyplvpvcggttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpallqsg
lytlsssvtvtsntwpsqtitcnvahpasstkvdkkieprv
>d1cfvh_ 2.1.1.1.88 Immunoglobulin (variable domains of L and H chains) {Fv 4155 (mouse), kappa L chain}
qvqlqesggglvnlggsmtlscvasgftfntyymswvrqtpektlelvaainsdgepiyy
pdtlkgrvtisrdnakktlylqmsslnfedtalyycarlnyavygmdywgqgttvtvss
>d1cfvl_ 2.1.1.1.88 Immunoglobulin (variable domains of L and H chains) {Fv 4155 (mouse), kappa L chain}
dieltqsppslpvslgdqvsiscrssqslvsnnrrnylhwylqkpgqspklviykvsnrf
sgvpdrfsgsgsgtdftlkisrvaaedlglyfcsqsshvpltfgsgtkleikr
>d1cfwa_ 7.35.4.2.1 Desulforedoxin {Desulfovibrio gigas}
anegdvykcelcgqvvkvleegggtlvccgedmvkq
>d1cfwb_ 7.35.4.2.1 Desulforedoxin {Desulfovibrio gigas}
anegdvykcelcgqvvkvleegggtlvccgedmvkq
>d1cfya_ 4.85.1.2.1 Yeast cofilin, monoclinic crystal form {Baker's yeast (Saccharomyces cerevisiae)}
vavadesltafndlklgkkykfilfglndakteivvketstdpsydafleklpendclya
iydfeyeingnegkrskivfftwspdtapvrskmvyasskdalrralngvstdvqgtdfs
evsydsvlervsr
>d1cfyb_ 4.85.1.2.1 Yeast cofilin, monoclinic crystal form {Baker's yeast (Saccharomyces cerevisiae)}
vavadesltafndlklgkkykfilfglndakteivvketstdpsydafleklpendclya
iydfeyeingnegkrskivfftwspdtapvrskmvyasskdalrralngvstdvqgtdfs
evsydsvlervsr
>d1cg0a_ 3.30.1.8.2 Adenylosuccinate synthetase (gene purA product) {Escherichia coli}
gnnvvvlgtqwgdegkgkivdllterakyvvryqgghnaghtlvingektvlhlipsgil
renvtsiigngvvlspaalmkemkeledrgipvrerlllseacplildyhvaldnareka
rgakaigttgrgigpayedkvarrglrvgdlfdketfaeklkevmeyhnfqlvnyykaea
vdyqkvlddtmavadiltsmvvdvsdlldqarqrgdfvmfegaqgtlldidhgtypyvts
snttaggvatgsglgpryvdyvlgilkaystrvgagpfptelfdetgeflckqgnefgat
tgrrrrtgwldtvavrravqlnslsgfcltkldvldglkevklcvayrmpdgrevtttpl
aaddwkgvepiyetmpgwsestfgvkdrsglpqaalnyikrieeltgvpidiistgpdrt
etmilrdpfda
>d1cg1a_ 3.30.1.8.2 Adenylosuccinate synthetase (gene purA product) {Escherichia coli}
gnnvvvlgtqwgdegqgkivdllterakyvvryqgghnaghtlvingektvlhlipsgil
renvtsiigngvvlspaalmkemkeledrgipvrerlllseacplildyhvaldnareka
rgakaigttgrgigpayedkvarrglrvgdlfdketfaeklkevmeyhnfqlvnyykaea
vdyqkvlddtmavadiltsmvvdvsdlldqarqrgdfvmfegaqgtlldidhgtypyvts
snttaggvatgsglgpryvdyvlgilkaystrvgagpfptelfdetgeflckqgnefgat
tgrrrrtgwldtvavrravqlnslsgfcltkldvldglkevklcvayrmpdgrevtttpl
aaddwkgvepiyetmpgwsestfgvkdrsglpqaalnyikrieeltgvpidiistgpdrt
etmilrdpfda
>d1cg2a1 3.47.4.4.3 (26-213,327-414) Carboxypeptidase G2, catalytic domain {Pseudomonas strain rs-16}
qkrdnvlfqaatdeqpaviktleklvnietgtgdaegiaaagnfleaelknlgftvtrsk
saglvvgdnivgkikgrggknlllmshmdtvylkgilakapfrvegdkaygpgiaddkgg
navilhtlkllkeygvrdygtitvlfntdeekgsfgsrdliqeeakladyvlsfeptsag
deklslgtXfnageggkklvdkavayykeaggtlgveertgggtdaayaalsgkpviesl
glpgfgyhsdkaeyvdisaiprrlymaarlimdlgag
>d1cg2a2 4.47.18.1.1 (214-326) Carboxypeptidase G2, dimerisation domain {Pseudomonas strain rs-16}
sgiayvqvnitgkashagaapelgvnalveasdlvlrtmniddkaknlrfnwtiakagnv
sniipasatlnadvryarnedfdaamktleeraqqkklpeadvkvivtrgrpa
>d1cg2b1 3.47.4.4.3 (26-213,327-414) Carboxypeptidase G2, catalytic domain {Pseudomonas strain rs-16}
qkrdnvlfqaatdeqpaviktleklvnietgtgdaegiaaagnfleaelknlgftvtrsk
saglvvgdnivgkikgrggknlllmshmdtvylkgilakapfrvegdkaygpgiaddkgg
navilhtlkllkeygvrdygtitvlfntdeekgsfgsrdliqeeakladyvlsfeptsag
deklslgtXfnageggkklvdkavayykeaggtlgveertgggtdaayaalsgkpviesl
glpgfgyhsdkaeyvdisaiprrlymaarlimdlgag
>d1cg2b2 4.47.18.1.1 (214-326) Carboxypeptidase G2, dimerisation domain {Pseudomonas strain rs-16}
sgiayvqvnitgkashagaapelgvnalveasdlvlrtmniddkaknlrfnwtiakagnv
sniipasatlnadvryarnedfdaamktleeraqqkklpeadvkvivtrgrpa
>d1cg2c1 3.47.4.4.3 (26-213,327-414) Carboxypeptidase G2, catalytic domain {Pseudomonas strain rs-16}
qkrdnvlfqaatdeqpaviktleklvnietgtgdaegiaaagnfleaelknlgftvtrsk
saglvvgdnivgkikgrggknlllmshmdtvylkgilakapfrvegdkaygpgiaddkgg
navilhtlkllkeygvrdygtitvlfntdeekgsfgsrdliqeeakladyvlsfeptsag
deklslgtXfnageggkklvdkavayykeaggtlgveertgggtdaayaalsgkpviesl
glpgfgyhsdkaeyvdisaiprrlymaarlimdlgag
>d1cg2c2 4.47.18.1.1 (214-326) Carboxypeptidase G2, dimerisation domain {Pseudomonas strain rs-16}
sgiayvqvnitgkashagaapelgvnalveasdlvlrtmniddkaknlrfnwtiakagnv
sniipasatlnadvryarnedfdaamktleeraqqkklpeadvkvivtrgrpa
>d1cg2d1 3.47.4.4.3 (26-213,327-414) Carboxypeptidase G2, catalytic domain {Pseudomonas strain rs-16}
qkrdnvlfqaatdeqpaviktleklvnietgtgdaegiaaagnfleaelknlgftvtrsk
saglvvgdnivgkikgrggknlllmshmdtvylkgilakapfrvegdkaygpgiaddkgg
navilhtlkllkeygvrdygtitvlfntdeekgsfgsrdliqeeakladyvlsfeptsag
deklslgtXfnageggkklvdkavayykeaggtlgveertgggtdaayaalsgkpviesl
glpgfgyhsdkaeyvdisaiprrlymaarlimdlgag
>d1cg2d2 4.47.18.1.1 (214-326) Carboxypeptidase G2, dimerisation domain {Pseudomonas strain rs-16}
sgiayvqvnitgkashagaapelgvnalveasdlvlrtmniddkaknlrfnwtiakagnv
sniipasatlnadvryarnedfdaamktleeraqqkklpeadvkvivtrgrpa
>d1cg3a_ 3.30.1.8.2 Adenylosuccinate synthetase (gene purA product) {Escherichia coli}
gnnvvvlgtqwgdegkgkivdllterakyvvryqgghnaghtlvingektvlhlipsgil
renvtsiigngvvlspaalmkemkeledrgipvrerlllseacplildyhvaldnareka
rgakaigttgrgigpayedkvalrglrvgdlfdketfaeklkevmeyhnfqlvnyykaea
vdyqkvlddtmavadiltsmvvdvsdlldqarqrgdfvmfegaqgtlldidhgtypyvts
snttaggvatgsglgpryvdyvlgilkaystrvgagpfptelfdetgeflckqgnefgat
tgrrrrtgwldtvavrravqlnslsgfcltkldvldglkevklcvayrmpdgrevtttpl
aaddwkgvepiyetmpgwsestfgvkdrsglpqaalnyikrieeltgvpidiistgpdrt
etmilrdpfda
>d1cg4a_ 3.30.1.8.2 Adenylosuccinate synthetase (gene purA product) {Escherichia coli}
gnnvvvlgtqwgdegkgkivdllterakyvvryqgghnaghtlvingektvlhlipsgil
renvtsiigngvvlspaalmkemkeledrgipvrerlllseacplildyhvaldnareka
rgakaigttgrgigpayedkvarrglrvgdlfdketfaeklkevmeyhnfqlvnyykaea
vdyqkvlddtmavadiltsmvvdvsdlldqarqrgdfvmfegaqgtlldidhgtypyvts
snttaggvatgsglgpryvdyvlgilkaystrvgagpfptelfdetgeflckqgnefgat
tglrrrtgwldtvavrravqlnslsgfcltkldvldglkevklcvayrmpdgrevtttpl
aaddwkgvepiyetmpgwsestfgvkdrsglpqaalnyikrieeltgvpidiistgpdrt
etmilrdpfda
>d1cg5a_ 1.1.1.1.25 Hemoglobin D {Cartilaginous fish akaei (Dasyatis akajei)}
vlssqnkkaieelgnlikanaeawgadalarlfelhpqtktyfskfsgfeacneqvkkhg
krvmnaladathhldnlhlhledlarkhgenllvdphnfhlfadcivvtlavnlqaftpv
thcavdkflelvayelsscyr
>d1cg5b_ 1.1.1.1.40 Hemoglobin D {Cartilaginous fish akaei (Dasyatis akajei)}
vklsedqehyikgvwkdvdhkqitakalervfvvypwttrlfsklqglfsandigvqqha
dkvqralgeaiddlkkveinfqnlsgkhqeigvdtqnfkllgqtfmvelalhykktfrpk
ehaaaykffrlvaealssnyh
>d1cg6a_ 3.47.1.1.4 5'-deoxy-5'-methylthioadenosine phosphorylase {Human (Homo sapiens)}
avkigiiggtglddpeilegrtekyvdtpfgkpsdalilgkiknvdcvllarhgrqhtim
pskvnyqaniwalkeegcthvivttacgslreeiqpgdiviidqfidrttmrpqsfydgs
hscargvchipmaepfcpktrevlietakklglrchskgtmvtiegprfssraesfmfrt
wgadvinmttvpevvlakeagicyasiamatdydcwkeheeavsvdrvlktlkenankak
slllttipqigstewsetlhnlknmaqfsvllp
>d1cg8a_ 1.1.1.1.25 Hemoglobin D {Cartilaginous fish akaei (Dasyatis akajei)}
vlssqnkkaieelgnlikanaeawgadalarlfelhpqtktyfskfsgfeacneqvkkhg
krvmnaladathhldnlhlhledlarkhgenllvdphnfhlfadcivvtlavnlqaftpv
thcavdkflelvayelsscyr
>d1cg8b_ 1.1.1.1.40 Hemoglobin D {Cartilaginous fish akaei (Dasyatis akajei)}
vklsedqehyikgvwkdvdhkqitakalervfvvypwttrlfsklqglfsandigvqqha
dkvqralgeaiddlkkveinfqnlsgkhqeigvdtqnfkllgqtfmvelalhykktfrpk
ehaaaykffrlvaealssnyh
>d1cge__ 4.71.1.9.1 Fibroblast collagenase (MMP-1) {Human (Homo sapiens)}
ltegnprweqthlryrienytpdlpradvdhaiekafqlwsnvtpltftkvsegqadimi
sfvrgdhrdnspfdgpggnlahafqpgpgiggdahfdederwtnnfreynlhrvaahelg
hslglshstdigalmypsytfsgdvqlaqddidgiqaiygrs
>d1cgfa_ 4.71.1.9.1 Fibroblast collagenase (MMP-1) {Human (Homo sapiens)}
ltegnprweqthlryrienytpdlpradvdhaiekafqlwsnvtpltftkvsegqadimi
sfvrgdhrdnspfdgpggnlahafqpgpgiggdahfdederwtnnfreynlhrvaahelg
hslglshstdigalmypsytfsgdvqlaqddidgiqaiygrs
>d1cgfb_ 4.71.1.9.1 Fibroblast collagenase (MMP-1) {Human (Homo sapiens)}
ltegnprweqthlryrienytpdlpradvdhaiekafqlwsnvtpltftkvsegqadimi
sfvrgdhrdnspfdgpggnlahafqpgpgiggdahfdederwtnnfreynlhrvaahelg
hslglshstdigalmypsytfsgdvqlaqddidgiqaiygrs
>d1cgha_ 2.41.1.2.20 Cathepsin G {Human (Homo sapiens)}
iiggresrphsrpymaylqiqspagqsrcggflvredfvltaahcwgsninvtlgahniq
rrentqqhitarrairhpqynqrtiqndimllqlsrrvrrnrnvnpvalpraqeglrpgt
lctvagwgrvsmrrgtdtlrevqlrvqrdrqclrifgsydprrqicvgdrrerkaafkgd
sggpllcnnvahgivsygkssgvppevftrvssflpwirttmrs
>d1cgie_ 2.41.1.2.7 (alpha,gamma)-chymotrypsin(ogen) {Bovine (Bos taurus)}
cgvpaiqpvlsglsrivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgv
ttsdvvvagefdqgsssekiqklkiakvfknskynsltinnditllklstaasfsqtvsa
vclpsasddfaagttcvttgwgltrytnantpdrlqqaslpllsntnckkywgtkikdam
icagasgvsscmgdsggplvckkngawtlvgivswgsstcststpgvyarvtalvnwvqq
tlaan
>d1cgii_ 7.15.1.1.4 Secretory trypsin inhibitor {Human (Homo sapiens)}
dslgreakcynelngctyeyrpvcgtdgdtypnecvlcfenrkrqtsiliqksgpc
>d1cgje_ 2.41.1.2.7 (alpha,gamma)-chymotrypsin(ogen) {Bovine (Bos taurus)}
cgvpaiqpvlsglsrivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgv
ttsdvvvagefdqgsssekiqklkiakvfknskynsltinnditllklstaasfsqtvsa
vclpsasddfaagttcvttgwgltrytnantpdrlqqaslpllsntnckkywgtkikdam
icagasgvsscmgdsggplvckkngawtlvgivswgsstcststpgvyarvtalvnwvqq
tlaan
>d1cgji_ 7.15.1.1.4 Secretory trypsin inhibitor {Human (Homo sapiens)}
dslgreakcynelngctleyrpvcgtdgdtypnecvlcfenrkrqtsiliqksgpc
>d1cgka_ 3.85.1.2.1 Chalcone synthase {Alfalfa (Medicago sativa)}
svseirkaqraegpatilaigtanpancveqstypdfyfkitnsehktelkekfqrmcdk
smikrrymylteeilkenpnvceymapsldarqdmvvvevprlgkeaavkaikewgqpks
kithlivcttsgvdmpgadyqltkllglrpyvkrymmyqqgcfaggtvlrlakdlaennk
garvlvvcsevtavtfrgpsdthldslvgqalfgdgaaalivgsdpvpeiekpifemvwt
aqtiapdsegaidghlreagltfhllkdvpgivsknitkalveafeplgisdynsifwia
hpggpaildqveqklalkpekmnatrevlseygnmssacvlfildemrkkstqnglkttg
eglewgvlfgfgpgltietvvlrsvai
>d1cgla_ 4.71.1.9.1 Fibroblast collagenase (MMP-1) {Human (Homo sapiens)}
vltegnprweqthlryrienytpdlpradvdhaiekafqlwsdvtpltftkvsegqadim
isfvrgdhrdnspfdgpggnlahafdpgpgiggdahfdederwtnnfreynlhrvaahel
ghslglshstdigalmypsytfsgdvqlaqddidgiqaiygrsqnpvq
>d1cglb_ 4.71.1.9.1 Fibroblast collagenase (MMP-1) {Human (Homo sapiens)}
nprweqthlryrienytpdlpradvdhaiekafqlwsdvtpltftkvsegqadimisfvr
gdhrdnspfdgpggnlahafdpgpgiggdahfdederwtnnfreynlhrvaahelghslg
lshstdigalmypsytfsgdvqlaqddidgiqaiygrsqn
>d1cgme_ 1.25.5.1.2 Cucumber green mottle mosaic virus {Cucumber green mottle mosaic virus, watermelon strain}
xaynpitpskliafsasyvpvrtllnflvasqgtafqtqagrdsfreslsalpssvvdin
srfpdagfyaflngpvlrpifvsllsstdtrnrvievvdpsnpttaeslnavkrtddast
aaraeidnliesiskgfdvydrasfeaafsvvwseattska
>d1cgn__ 1.25.3.2.3 Cytochrome c' {Alcaligenes denitrificans}
xfakpedavkyrqsaltlmashfgrmapvvkgqapydaaqikanvevlktltalpwaafg
agteggdarpeiwsdaagfkqkqqafqdnivklsaaadagdldklraafgdvgasckach
dsyrk
>d1cgo__ 1.25.3.2.4 Cytochrome c' {Alcaligenes}
xfakpedavkyrqsaltlmashfgrmtpvvkgqapydaaqikanvevlktltalpwaafg
pgteggdarpeiwsdaasfkqkqqafqdnivklsaaadagdldklraafgdvgasckach
dayrk
>d1cgpa1 1.4.3.4.1 (138-205) Catabolite gene activator protein (CAP), C-terminal domain {Escherichia coli}
dvtgriaqtllnlakqpdamthpdgmqikitrqeigqivgcsretvgrilkmledqnlis
ahgktivv
>d1cgpa2 2.73.4.1.1 (9-137) Catabolite gene activator protein, N-terminal domain {Escherichia coli}
ptlewflshchihkypskstlihqgekaetlyyivkgsvavlikdeegkemilsylnqgd
figelglfeegqersawvraktacevaeisykkfrqliqvnpdilmrlsaqmarrlqvts
ekvgnlafl
>d1cgpb1 1.4.3.4.1 (138-205) Catabolite gene activator protein (CAP), C-terminal domain {Escherichia coli}
dvtgriaqtllnlakqpdamthpdgmqikitrqeigqivgcsretvgrilkmledqnlis
ahgktivv
>d1cgpb2 2.73.4.1.1 (9-137) Catabolite gene activator protein, N-terminal domain {Escherichia coli}
ptlewflshchihkypskstlihqgekaetlyyivkgsvavlikdeegkemilsylnqgd
figelglfeegqersawvraktacevaeisykkfrqliqvnpdilmrlsaqmarrlqvts
ekvgnlafl
>d1cgqa_ 4.60.1.3.1 Microphage migration inhibition factor (MIF) {Human (Homo sapiens)}
pamfivntnvprasvpdgflseltqqlaqatgkppqyiavhvvpdqlmafggssepcalc
slhsigkiggaqnrsyskllcgllaerlrispdrvyinyydmnaanvgwnnstfa
>d1cgqb_ 4.60.1.3.1 Microphage migration inhibition factor (MIF) {Human (Homo sapiens)}
pamfivntnvprasvpdgflseltqqlaqatgkppqyiavhvvpdqlmafggssepcalc
slhsigkiggaqnrsyskllcgllaerlrispdrvyinyydmnaanvgwnnstfa
>d1cgqc_ 4.60.1.3.1 Microphage migration inhibition factor (MIF) {Human (Homo sapiens)}
pamfivntnvprasvpdgflseltqqlaqatgkppqyiavhvvpdqlmafggssepcalc
slhsigkiggaqnrsyskllcgllaerlrispdrvyinyydmnaanvgwnnstfa
>d1cgsh1 2.1.1.1.39 (1-117) Immunoglobulin (variable domains of L and H chains) {Fab, anti-sweetener (mouse), kappa L chain}
rvqllesgaelmkpgasvqisckatgytfseywiewvkerpghglewigeilpgsgrtny
rekfkgkatftadtssntaymqlssltsedsavyyctrgyssmdywgqgtsvtvsaa
>d1cgsh2 2.1.1.2.48 (118-214) Immunoglobulin (constant domains of L and H chains) {Fab, anti-sweetener (mouse), kappa L chain}
kttppsvyplapgcgdttgssvtlgclvkgyfpesvtvtwnsgslsssvhtfpallqsgl
ytmsssvtvpsstwpsqtvtcsvahpassttvdkkle
>d1cgsl1 2.1.1.1.39 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab, anti-sweetener (mouse), kappa L chain}
elvmtqsplslpvslgdqasiscrpsqslvhsngntylhwylqkpgqspklliyrvsnrf
sgvpdrfsgsgsgtaftlkisrveaedlgvyfcsqgthvpytfgggtklelk
>d1cgsl2 2.1.1.2.48 (113-219) Immunoglobulin (constant domains of L and H chains) {Fab, anti-sweetener (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1cgt_1 2.1.1.5.4 (495-579) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
ettptighvgpvmgkpgnvvtidgrgfgstkgtvyfgttavtgaaitswedtqikvtips
vaagnyavkvaasgvnsnaynnfti
>d1cgt_2 2.3.1.1.1 (580-684) Cyclodextrin glycosyltransferase, C-terminal domain {Bacillus circulans}
ltgdqvtvrfvvnnasttlgqnlyltgnvaelgnwstgstaigpafnqvihqyptwyydv
svpagkqlefkffkkngstitwesgsnhtfttpasgtatvtvnwq
>d1cgt_3 2.62.1.1.4 (407-494) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqqrwinndvyvyerkfgksvavvavnrnlstsasitglstslptgsytdvlggvlng
nnitstngsinnftlaagatavwqytta
>d1cgt_4 3.1.7.1.4 (1-406) Cyclodextrin glycosyltransferase {Bacillus circulans}
dpdtavtnkqsfstdviyqvftdrfldgnpsnnptgaaydatcsnlklycggdwqglink
indnyfsdlgvtalwisqpvenifatinysgvtntayhgywardfkktnpyfgtmadfqn
littahakgikividfapnhtspametdtsfaengrlydngtlvggytndtngyfhhngg
sdfsslengiyknlydladfnhnnatidkyfkdaiklwldmgvdgirvdavkhmplgwqk
swmssiyahkpvftfgewflgsaasdadntdfanksgmslldfrfnsavrnvfrdntsnm
yaldsminstatdynqvndqvtfidnhdmdrfktsavnnrrleqalaftltsrgvpaiyy
gteqyltgngdpdnrakmpsfsksttafnvisklaplrksnpaiay
>d1cgu_1 2.1.1.5.4 (495-579) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
ettptighvgpvmgkpgnvvtidgrgfgstkgtvyfgttavtgaaitswedtqikvtips
vaagnyavkvaasgvnsnaynnfti
>d1cgu_2 2.3.1.1.1 (580-684) Cyclodextrin glycosyltransferase, C-terminal domain {Bacillus circulans}
ltgdqvtvrfvvnnasttlgqnlyltgnvaelgnwstgstaigpafnqvihqyptwyydv
svpagkqlefkffkkngstitwesgsnhtfttpasgtatvtvnwq
>d1cgu_3 2.62.1.1.4 (407-494) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqqrwinndvyvyerkfgksvavvavnrnlstsasitglstslptgsytdvlggvlng
nnitstngsinnftlaagatavwqytta
>d1cgu_4 3.1.7.1.4 (1-406) Cyclodextrin glycosyltransferase {Bacillus circulans}
dpdtavtnkqsfstdviyqvftdrfldgnpsnnptgaaydatcsnlklycggdwqglink
indnyfsdlgvtalwisqpvenifatinysgvtntayhgywardfkktnpyfgtmadfqn
littahakgikividfapnhtspametdtsfaengrlydngtlvggytndtngyfhhngg
sdfsslengiyknlydladfnhnnatidkyfkdaiklwldmgvdgirvaavkhmplgwqk
swmssiyahkpvftfgewflgsaasdadntdfanksgmslldfrfnsavrnvfrdntsnm
yaldsminstatdynqvndqvtfidnhdmdrfktsavnnrrleqalaftltsrgvpaiyy
gteqyltgngdpdnrakmpsfsksttafnvisklaplrksnpaiay
>d1cgv_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d1cgv_2 2.3.1.1.1 (582-686) Cyclodextrin glycosyltransferase, C-terminal domain {Bacillus circulans}
lsgdqvsvrfvvnnattalgqnvyltgsvselgnwdpakaigpmynqvvyqypnwyydvs
vpagktiefkflkkqgstvtweggsnhtftapssgtatinvnwqp
>d1cgv_3 2.62.1.1.4 (407-495) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqerwinndvliyerkfgsnvavvavnrnlnapasisglvtslpqgsyndvlggllng
ntlsvgsggaasnftlaaggtavwqytaa
>d1cgv_4 3.1.7.1.4 (1-406) Cyclodextrin glycosyltransferase {Bacillus circulans}
apdtsvsnkqnfstdviyqiftdrfsdgnpannptgaafdgtctnlrlycggdwqgiink
indgyltgmgvtaiwisqpveniysiinysgvnntayhgywardfkktnpaygtiadfqn
liaaahaknikviidfapnhtspassdqpsfaengrlydngtllggytndtqnlfhhngg
tdfsttengiyknlfdladlnhnnstvdvylkdaikmwldlgidgirmdavkhmpfgwqk
sfmaavnnykpvftfgewflgvnevspenhkfanesgmslldfrfaqkvrqvfrdntdnm
yglkamlegsaadyaqvddqvtfidnhdmerfhasnanrrkleqalaftltsrgvpaiyy
gteqymsggtdpdnraripsfststtayqviqklaplrkcnpaiay
>d1cgw_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d1cgw_2 2.3.1.1.1 (582-686) Cyclodextrin glycosyltransferase, C-terminal domain {Bacillus circulans}
lsgdqvsvrfvvnnattalgqnvyltgsvselgnwdpakaigpmynqvvyqypnwyydvs
vpagktiefkflkkqgstvtweggsnhtftapssgtatinvnwqp
>d1cgw_3 2.62.1.1.4 (407-495) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqerwinndvliyerkfgsnvavvavnrnlnapasisglvtslpqgsyndvlggllng
ntlsvgsggaasnftlaaggtavwqytaa
>d1cgw_4 3.1.7.1.4 (1-406) Cyclodextrin glycosyltransferase {Bacillus circulans}
apdtsvsnkqnfstdviyqiftdrfsdgnpannptgaafdgtctnlrlycggdwqgiink
indgyltgmgvtaiwisqpveniysiinysgvnntayhgywardfkktnpaygtiadfqn
liaaahaknikviidfapnhtspassdqpsfaengrlydngtllggytndtqnlfhhngg
tdfsttengiyknlgdladlnhnnstvdvylkdaikmwldlgidgirmdavkhmpfgwqk
sfmaavnnykpvftfgewflgvnevspenhkfanesgmslldfrfaqkvrqvfrdntdnm
yglkamlegsaadyaqvddqvtfidnhdmerfhasnanrrkleqalaftltsrgvpaiyy
gteqymsggtdpdnraripsfststtayqviqklaplrkcnpaiay
>d1cgx_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d1cgx_2 2.3.1.1.1 (582-686) Cyclodextrin glycosyltransferase, C-terminal domain {Bacillus circulans}
lsgdqvsvrfvvnnattalgqnvyltgsvselgnwdpakaigpmynqvvyqypnwyydvs
vpagktiefkflkkqgstvtweggsnhtftapssgtatinvnwqp
>d1cgx_3 2.62.1.1.4 (407-495) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqerwinndvliyerkfgsnvavvavnrnlnapasisglvtslpqgsyndvlggllng
ntlsvgsggaasnftlaaggtavwqytaa
>d1cgx_4 3.1.7.1.4 (1-406) Cyclodextrin glycosyltransferase {Bacillus circulans}
apdtsvsnkqnfstdviyqiftdrfsdgnpannptgaafdgtctnlrlycggdwqgiink
indgyltgmgvtaiwisqpveniysiinysgvnntayhgywardfkktnpaygtiadfqn
liaaahaknikviidfapnhtspassdqpsfaengrlydngtllggytndtqnlfhhngg
tdfsttengiyknlldladlnhnnstvdvylkdaikmwldlgidgirmdavkhmpfgwqk
sfmaavnnykpvftfgewflgvnevspenhkfanesgmslldfrfaqkvrqvfrdntdnm
yglkamlegsaadyaqvddqvtfidnhdmerfhasnanrrkleqalaftltsrgvpaiyy
gteqymsggtdpdnraripsfststtayqviqklaplrkcnpaiay
>d1cgy_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d1cgy_2 2.3.1.1.1 (582-686) Cyclodextrin glycosyltransferase, C-terminal domain {Bacillus circulans}
lsgdqvsvrfvvnnattalgqnvyltgsvselgnwdpakaigpmynqvvyqypnwyydvs
vpagktiefkflkkqgstvtweggsnhtftapssgtatinvnwqp
>d1cgy_3 2.62.1.1.4 (407-495) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqerwinndvliyerkfgsnvavvavnrnlnapasisglvtslpqgsyndvlggllng
ntlsvgsggaasnftlaaggtavwqytaa
>d1cgy_4 3.1.7.1.4 (1-406) Cyclodextrin glycosyltransferase {Bacillus circulans}
apdtsvsnkqnfstdviyqiftdrfsdgnpannptgaafdgtctnlrlycggdwqgiink
indgyltgmgvtaiwisqpveniysiinysgvnntayhgywardfkktnpaygtiadfqn
liaaahaknikviidfapnhtspassdqpsfaengrlydngtllggytndtqnlfhhngg
tdfsttengiyknlwdladlnhnnstvdvylkdaikmwldlgidgirmdavkhmpfgwqk
sfmaavnnykpvftfgewflgvnevspenhkfanesgmslldfrfaqkvrqvfrdntdnm
yglkamlegsaadyaqvddqvtfidnhdmerfhasnanrrkleqalaftltsrgvpaiyy
gteqymsggtdpdnraripsfststtayqviqklaplrkcnpaiay
>d1cgza_ 3.85.1.2.1 Chalcone synthase {Alfalfa (Medicago sativa)}
svseirkaqraegpatilaigtanpancveqstypdfyfkitnsehktelkekfqrmcdk
smikrrymylteeilkenpnvceymapsldarqdmvvvevprlgkeaavkaikewgqpks
kithlivcttsgvdmpgadyqltkllglrpyvkrymmyqqgcfaggtvlrlakdlaennk
garvlvvcsevtavtfrgpsdthldslvgqalfgdgaaalivgsdpvpeiekpifemvwt
aqtiapdsegaidghlreagltfhllkdvpgivsknitkalveafeplgisdynsifwia
hpggpaildqveqklalkpekmnatrevlseygnmssacvlfildemrkkstqnglkttg
eglewgvlfgfgpgltietvvlrsvai
>d1ch1a_ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkpgaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1ch2a_ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkpfaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1ch3a_ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkpwaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1ch4a_ 1.1.1.1.35 Chimeric hemoglobin beta-alpha {Synthetic, based on human Homo sapiens sequences}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklrvdpvnfkllshcllvtlaahlpa
eftpavhasldkvlasvstvltskyr
>d1ch4b_ 1.1.1.1.35 Chimeric hemoglobin beta-alpha {Synthetic, based on human Homo sapiens sequences}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklrvdpvnfkllshcllvtlaahlpa
eftpavhasldkvlasvstvltskyr
>d1ch4c_ 1.1.1.1.35 Chimeric hemoglobin beta-alpha {Synthetic, based on human Homo sapiens sequences}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklrvdpvnfkllshcllvtlaahlpa
eftpavhasldkvlasvstvltskyr
>d1ch4d_ 1.1.1.1.35 Chimeric hemoglobin beta-alpha {Synthetic, based on human Homo sapiens sequences}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklrvdpvnfkllshcllvtlaahlpa
eftpavhasldkvlasvstvltskyr
>d1ch5a_ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkplaqshatkvkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1ch6a1 3.2.1.7.4 (209-501) Glutamate dehydrogenase {Bovine (Bos taurus)}
hgrisatgrgvfhgienfienasymsilgmtpgfgdktfavqgfgnvglhsmrylhrfga
kcvavgesdgsiwnpdgidpkeledfklqhgtilgfpkakiyegsilevdcdilipaase
kqltksnaprvkakiiaegangpttpqadkiflernimvipdlylnaggvtvsyfqilkn
lnhvsygrltfkyerdsnyhllmsvqeslerkfgkhggtipivptaefqdrisgasekdi
vhsglaytmersarqimrtamkynlgldlrtaayvnaiekvfrvyneagvtft
>d1ch6a2 3.48.1.1.4 (6-208) Glutamate dehydrogenase {Bovine (Bos taurus)}
dpnffkmvegffdrgasivedklvedlktrqtqeqkrnrvrgilriikpcnhvlslsfpi
rrddgsweviegyraqhshqrtpckggirystdvsvdevkalaslmtykcavvdvpfgga
kagvkinpknytdedlekitrrftmelakkgfigpgvdvpapnmstgeremswiadtyas
tighydinahacvtgkpisqggi
>d1ch7a_ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkplaqshatkfkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1ch9a_ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkplaqshatkqkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1chc__ 7.37.1.1.2 Immediate early protein, IEEHV {Equine herpes virus-1}
matvaercpicledpsnysmalpclhafcyvcitrwirqnptcplckvpvesvvhtiesd
sefgdqli
>d1chd__ 3.32.1.1.1 Methylesterase CheB, C-terminal domain {Salmonella typhimurium}
llssekliaigastggteairhvlqplplsspaviitqhmppgftrsfaerlnklcqisv
keaedgervlpghayiapgdkhmelarsganyqikihdgppvnrhrpsvdvlfhsvakha
grnavgviltgmgndgaagmlamyqagawtiaqneascvvfgmpreainmggvsevvdls
qvsqqmlakisagqairi
>d1chg__ 2.41.1.2.7 (alpha,gamma)-chymotrypsin(ogen) {Bovine (Bos taurus)}
cgvpaiqpvlsglsrivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgv
ttsdvvvagefdqgsssekiqklkiakvfknskynsltinnditllklstaasfsqtvsa
vclpsasddfaagttcvttgwgltrytnantpdrlqqaslpllsntnckkywgtkikdam
icagasgvsscmgdsggplvckkngawtlvgivswgsstcststpgvyarvtalvnwvqq
tlaan
>d1chh__ 1.3.1.1.7 Mitochondrial cytochrome c {Baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdanikk
nvlwdennmseyltnpkkyipgtkmaygglkkekdrndlitylkkate
>d1chi__ 1.3.1.1.7 Mitochondrial cytochrome c {Baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdanikk
nvlwdennmseyltnpkkyipgtkmayggakkekdrndlitylkkate
>d1chj__ 1.3.1.1.7 Mitochondrial cytochrome c {Baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdanikk
nvlwdennmseyltnpkkyipgtkmafggakkekdrndlitylkkate
>d1chka_ 4.2.1.7.1 Endochitosanase {Streptomyces sp., strain N174}
agaglddphkkeiamelvssaenssldwkaqykyiedigdgrgytggiigfcsgtgdmle
lvqhytdlepgnilakylpalkkvngsashsglgtpftkdwataakdtvfqqaqnderdr
vyfdpavsqakadglralgqfayydaivmhgpgndptsfggirktamkkartpaqggdet
tylngfldarkaamlteaahddtsrvdteqrvflkagnldlnpplkwktygdpyvins
>d1chkb_ 4.2.1.7.1 Endochitosanase {Streptomyces sp., strain N174}
agaglddphkkeiamelvssaenssldwkaqykyiedigdgrgytggiigfcsgtgdmle
lvqhytdlepgnilakylpalkkvngsashsglgtpftkdwataakdtvfqqaqnderdr
vyfdpavsqakadglralgqfayydaivmhgpgndptsfggirktamkkartpaqggdet
tylngfldarkaamlteaahddtsrvdteqrvflkagnldlnpplkwktygdpyvins
>d1chl__ 7.3.7.2.10 Chlorootoxin {Scorpion (Leiurus quinquestriatus), venom}
mcmpcfttdhqmarkcddccggkgrgkcygpqclcr
>d1chma1 3.46.2.1.1 (2-156) Creatinase, N-terminal domain {Pseudomonas putida}
qmpktlrirngdkvrstfsaqeyanrqarlrahlaaenidaaiftsyhninyysdflycs
fgrpyalvvteddvisisanidggqpwrrtvgtdnivytdwqrdnyfaaiqqalpkarri
giehdhlnlqnrdklaarypdaelvdvaaacmrmr
>d1chma2 4.101.1.1.1 (157-402) Creatinase, catalytic (C-terminal) domain {Pseudomonas putida}
miksaeehvmirhgariadiggaavvealgdqvpeyevalhatqamvraiadtfedvelm
dtwtwfqsgintdgahnpvttrkvnkgdilslncfpmiagyytalertlfldhcsddhlr
lwqvnvevheaglklikpgarcsdiarelneiflkhdvlqyrtfgyghsfgtlshyygre
aglelredidtvlepgmvvsmepmimlpeglpgaggyrehdilivnengaenitkfpygp
ekniir
>d1chmb1 3.46.2.1.1 (2-156) Creatinase, N-terminal domain {Pseudomonas putida}
qmpktlrirngdkvrstfsaqeyanrqarlrahlaaenidaaiftsyhninyysdflycs
fgrpyalvvteddvisisanidggqpwrrtvgtdnivytdwqrdnyfaaiqqalpkarri
giehdhlnlqnrdklaarypdaelvdvaaacmrmr
>d1chmb2 4.101.1.1.1 (157-402) Creatinase, catalytic (C-terminal) domain {Pseudomonas putida}
miksaeehvmirhgariadiggaavvealgdqvpeyevalhatqamvraiadtfedvelm
dtwtwfqsgintdgahnpvttrkvnkgdilslncfpmiagyytalertlfldhcsddhlr
lwqvnvevheaglklikpgarcsdiarelneiflkhdvlqyrtfgyghsfgtlshyygre
aglelredidtvlepgmvvsmepmimlpeglpgaggyrehdilivnengaenitkfpygp
ekniir
>d1chn__ 3.16.2.1.1 CheY protein {Escherichia coli}
kelkflvvddfstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmpnm
dglellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleeklnki
feklgm
>d1choe_ 2.41.1.2.7 (alpha,gamma)-chymotrypsin(ogen) {Bovine (Bos taurus)}
cgvpaiqpvlsglxxivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgv
ttsdvvvagefdqgsssekiqklkiakvfknskynsltinnditllklstaasfsqtvsa
vclpsasddfaagttcvttgwgltryxxantpdrlqqaslpllsntnckkywgtkikdam
icagasgvsscmgdsggplvckkngawtlvgivswgsstcststpgvyarvtalvnwvqq
tlaan
>d1choi_ 7.15.1.1.1 Ovomucoid III domain {Turkey (Meleagris gallopavo)}
vsvdcseypkpactleyrplcgsdnktygnkcnfcnavvesngtltlshfgkc
>d1chpd_ 2.35.2.1.3 Cholera toxin {Vibrio cholerae}
tpqnitdlcaeyhntqihtlndkifsytesladkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1chpe_ 2.35.2.1.3 Cholera toxin {Vibrio cholerae}
tpqnitdlcaeyhntqihtlndkifsytesladkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1chpf_ 2.35.2.1.3 Cholera toxin {Vibrio cholerae}
tpqnitdlcaeyhntqihtlndkifsytesladkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1chpg_ 2.35.2.1.3 Cholera toxin {Vibrio cholerae}
tpqnitdlcaeyhntqihtlndkifsytesladkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1chph_ 2.35.2.1.3 Cholera toxin {Vibrio cholerae}
tpqnitdlcaeyhntqihtlndkifsytesladkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1chqd_ 2.35.2.1.3 Cholera toxin {Vibrio cholerae}
tpqnitdlcaeyhntqihtlndkifsyteslagkdemaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1chqe_ 2.35.2.1.3 Cholera toxin {Vibrio cholerae}
tpqnitdlcaeyhntqihtlndkifsyteslagkdemaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1chqf_ 2.35.2.1.3 Cholera toxin {Vibrio cholerae}
tpqnitdlcaeyhntqihtlndkifsyteslagkdemaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1chqg_ 2.35.2.1.3 Cholera toxin {Vibrio cholerae}
tpqnitdlcaeyhntqihtlndkifsyteslagkdemaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1chqh_ 2.35.2.1.3 Cholera toxin {Vibrio cholerae}
tpqnitdlcaeyhntqihtlndkifsyteslagkdemaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1chra1 3.1.10.2.4 (127-370) Chlormuconate cycloisomerase {Alcaligenes eutrophus}
plrsaipiawtlasgdtkrdldsavemierrrhnrfkvklgfrspqddlihmealsnslg
skaylrvdvnqawdeqvasvyipelealgvelieqpvgrentqalrrlsdnnrvaimade
slstlasafdlardrsvdvfslklcnmggvsatqkiaavaeasgiasyggtmldstigts
valqlystvpslpfgceligpfvladtlshepleirdyelqvptgvghgmtldedkvrqy
arvs
>d1chra2 4.44.1.1.6 (1-126) Chlormuconate cycloisomerase {Alcaligenes eutrophus}
mkidaieavivdvptkrpiqmsittvhqqsyvivrvyseglvgvgeggsvggpvwsaeca
etikiiverylaphllgtdafnvsgalqtmaravtgnasakaavemalldlkaralgvsi
aellgg
>d1chrb1 3.1.10.2.4 (127-370) Chlormuconate cycloisomerase {Alcaligenes eutrophus}
plrsaipiawtlasgdtkrdldsavemierrrhnrfkvklgfrspqddlihmealsnslg
skaylrvdvnqawdeqvasvyipelealgvelieqpvgrentqalrrlsdnnrvaimade
slstlasafdlardrsvdvfslklcnmggvsatqkiaavaeasgiasyggtmldstigts
valqlystvpslpfgceligpfvladtlshepleirdyelqvptgvghgmtldedkvrqy
arvs
>d1chrb2 4.44.1.1.6 (1-126) Chlormuconate cycloisomerase {Alcaligenes eutrophus}
mkidaieavivdvptkrpiqmsittvhqqsyvivrvyseglvgvgeggsvggpvwsaeca
etikiiverylaphllgtdafnvsgalqtmaravtgnasakaavemalldlkaralgvsi
aellgg
>d1chua1 1.7.4.1.1 (423-533) L-aspartate oxidase {Escherichia coli}
desrvenpdervviqhnwhelrlfmwdyvgivrttkrleralrritmlqqeideyyahfr
vsnnllelrnlvqvaelivrcammrkesrglhftldypellthsgpsi
>d1chua2 3.3.1.4.1 (2-237,354-422) L-aspartate oxidase {Escherichia coli}
ntlpehscdvliigsgaaglslalrladqhqvivlskgpvtegstfyaqggiaavfdetd
sidshvedtliagagicdrhavefvasnarscvqwlidqgvlfdthiqpngeesyhltre
gghshrrilhaadatgrevettlvskalnhpnirvlertnavdlivsdkiglpgtrrvvg
awvwnrnketvetchakavvlatggaskvyqyttnpdissgdgiamawragcrvanXcgg
vmvddhgrtdveglyaigevsytglhganrmasnslleclvygwsaaeditrrmpyahdi
stlppw
>d1chua3 4.138.1.1.1 (238-353) L-aspartate oxidase {Escherichia coli}
lefnqfhptalyhpqarnflltealrgegaylkrpdgtrfmpdfdergelaprdivarai
dhemkrlgadcmfldishkpadfirqhfpmiyekllglgidltqepvpivpaahyt
>d1chwa_ 3.85.1.2.1 Chalcone synthase {Alfalfa (Medicago sativa)}
mvsvseirkaqraegpatilaigtanpancveqstypdfyfkitnsehktelkekfqrmc
dksmikrrymylteeilkenpnvceymapsldarqdmvvvevprlgkeaavkaikewgqp
kskithlivcttsgvdmpgadyqltkllglrpyvkrymmyqqgsfaggtvlrlakdlaen
nkgarvlvvcsevtavtfrgpsdthldslvgqalfgdgaaalivgsdpvpeiekpifemv
wtaqtiapdsegaidghlreagltfhllkdvpgivsknitkalveafeplgisdynsifw
iahpggpaildqveqklalkpekmnatrevlseygnmssacvlfildemrkkstqnglkt
tgeglewgvlfgfgpgltietvvlrsvai
>d1chwb_ 3.85.1.2.1 Chalcone synthase {Alfalfa (Medicago sativa)}
mvsvseirkaqraegpatilaigtanpancveqstypdfyfkitnsehktelkekfqrmc
dksmikrrymylteeilkenpnvceymapsldarqdmvvvevprlgkeaavkaikewgqp
kskithlivcttsgvdmpgadyqltkllglrpyvkrymmyqqgsfaggtvlrlakdlaen
nkgarvlvvcsevtavtfrgpsdthldslvgqalfgdgaaalivgsdpvpeiekpifemv
wtaqtiapdsegaidghlreagltfhllkdvpgivsknitkalveafeplgisdynsifw
iahpggpaildqveqklalkpekmnatrevlseygnmssacvlfildemrkkstqnglkt
tgeglewgvlfgfgpgltietvvlrsvai
>d1ci0a_ 2.38.1.5.2 PNP oxidase {Baker's yeast (Saccharomyces cerevisiae)}
ftlnekqltddpidlftkwfneakedpretlpeaitfssaelpsgrvssrillfkeldhr
gftiysnwgtsrkahdiatnpnaaivffwkdlqrqvrvegitehvnretseryfktrprg
skigawasrqsdviknreeldeltqknterfkdaedipcpdywgglrivpleiefwqgrp
srlhdrfvyrrktendpwkvvrlap
>d1ci0b_ 2.38.1.5.2 PNP oxidase {Baker's yeast (Saccharomyces cerevisiae)}
tlnekqltddpidlftkwfneakedpretlpeaitfssaelpsgrvssrillfkeldhrg
ftiysnwgtsrkahdiatnpnaaivffwkdlqrqvrvegitehvnretseryfktrprgs
kigawasrqsdviknreeldeltqknterfkdaedipcpdywgglrivpleiefwqgrps
rlhdrfvyrrktendpwkvvrlap
>d1ci1a_ 3.1.1.1.5 Triosephosphate isomerase {Trypanosoma cruzi}
kpqpiaaanwkcngsesllvplietlnaatfdhdvqcvvaptflhipmtkarltnpkfqi
aaqnaitrsgaftgevslqilkdygiswvvlghserrlyygetneivaekvaqacaagfh
vivcvgetneereagrtaavvltqlaavaqklskeawsrvviayepvwaigtgkvatpqq
aqevhellrrwvrsklgtdiaaqlrilyggsvtaknartlyqmrdingflvggaslkpef
veiieatk
>d1ci1b_ 3.1.1.1.5 Triosephosphate isomerase {Trypanosoma cruzi}
skpqpiaaanwkcngsesllvplietlnaatfdhdvqcvvaptflhipmtkarltnpkfq
iaaqnaitrsgaftgevslqilkdygiswvvlghserrlyygetneivaekvaqacaagf
hvivcvgetneereagrtaavvltqlaavaqklskeawsrvviayepvwaigtgkvatpq
qaqevhellrrwvrsklgtdiaaqlrilyggsvtaknartlyqmrdingflvggaslkpe
fveiieatk
>d1ci3m1 2.2.6.1.3 (1-169,232-249) Cytochrome f, large domain {Phormidium laminosum}
ypfwaqqnyanpreatgrivcanchlaakpaeievpqavlpdsvfkavvkipydhsvqqv
qadgskgplnvgavlmlpegftiapedripeemkeevgpsylfqpyaddkqnivlvgplp
gdeyeeivfpvlspnpatnksvafgkysihlganrgrgqiyptgeksnnXnvggfgqkdt
eivlqspn
>d1ci3m2 2.74.2.2.3 (170-231) Cytochrome f, small domain {Phormidium laminosum}
avynasaagvitaiakaddgsaevkirtedgttivdkipagpelivsegeevaagaaltn
np
>d1ci5a1 2.1.1.1.9 (1-95) CD2-binding domain of CD58, first domain {Human (Homo sapiens)}
ssqqiygvkygnvtfhvpsnqplkevlwkkqkdkvaelensefrafssfknrvyldtksg
sltiynltssdedeyemespnitdsmkfflyvges
>d1cia__ 3.35.1.1.1 Chloramphenicol acetyltransferase {Escherichia coli}
mnytkfdvknwvrrehfefyrhrlpcgfsltskidittlkkslddsaykfypvmiyliaq
avnqfdelrmaikddelivwdsvdpqftvfhqetetfsalscpyssdidqfmvnylsvme
ryksdtklfpqgvtpenhlnisalpwvnfdsfnlnvanftdyfapiitmakyqqegdrll
lplsvqvhqavcdgfhvarfinrlqelcnsklk
>d1cica1 2.1.1.1.43 (1-107) Immunoglobulin (variable domains of L and H chains) {Anti-idiotope (D1.3) Fab E225, (mouse), kappa L chain}
divmtqshkfmstsvgdrvsitckasqdvriavawyqqkpgqspklliywastrhtgvpd
rftgsgsgtdftltisnvqsedladyfcqhcgsypftfgsgtkleik
>d1cica2 2.1.1.2.52 (108-214) Immunoglobulin (constant domains of L and H chains) {Anti-idiotope (D1.3) Fab E225, (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvldswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1cicb1 2.1.1.1.43 (1-117) Immunoglobulin (variable domains of L and H chains) {Anti-idiotope (D1.3) Fab E225, (mouse), kappa L chain}
qvqlqqpgselvrpgasvklsckasgytftnywmhwvkqrpgqglewigniypgsgdsny
dekfkskatltvdtssstaymqlsgltsedsavyycarglafyfdhwgqgttltvss
>d1cicb2 2.1.1.2.52 (118-217) Immunoglobulin (constant domains of L and H chains) {Anti-idiotope (D1.3) Fab E225, (mouse), kappa L chain}
alttppsvyplapgcgdttgssvtlgclvkgyfpepvtvtwnsgslsssvhtfpallqsg
lytmsssvtvpsstwpsetvtcsvahpassttvdkkleps
>d1cicc1 2.1.1.1.42 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
diqmtqspaslsasvgetvtitcrasgnihnylawyqqkqgkspqllvyytttladgvps
rfsgsgsgtqyslkinslqpedfgsyycqhfwstprtfgggtklelk
>d1cicc2 2.1.1.2.51 (108-214) Immunoglobulin (constant domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvldswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1cicd1 2.1.1.1.42 (1-116) Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
qvqlkesgpglvapsqslsitctvsgfsltgygvnwvrqppgkglewlgmiwgdgntdyn
salksrlsiskdnsksqvflkmnslhtddtaryycarerdyrldywgqgttltvss
>d1cicd2 2.1.1.2.51 (117-218) Immunoglobulin (constant domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
asttppsvfplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpssprpsetvtcnvahpasstkvdkkivprdc
>d1cid_1 2.1.1.1.6 (1-105) CD4 {Rat (Rattus rattus)}
tsitayksegesaefsfplnlgeeslqgelrwkaekapssqswitfslknqkvsvqksts
npkfqlsetlpltlqipqvslqfagsgnltltldrgilyqevnlv
>d1cid_2 2.1.1.3.5 (106-177) CD4 {Rat (Rattus rattus)}
vmkvtqpdsntltcevmgptspkmrlilkqenqearvsrqekviqvqapeagvwqcllse
geevkmdskiqv
>d1cie__ 1.3.1.1.7 Mitochondrial cytochrome c {Baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdaiikk
nvlwdennmseyltnpkkyipgtkmasgglkkekdrndlitylkkaae
>d1cif__ 1.3.1.1.7 Mitochondrial cytochrome c {Baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgahsgqaegysytdanikk
nvlwdennmseyltnpkkyipgtkmasgglkkekdrndlitylkkaae
>d1cig__ 1.3.1.1.7 Mitochondrial cytochrome c {Baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgahsgqaegysytdaiikk
nvlwdennmseyltnpkkyipgtkmafgglkkekdrndlitylkkaae
>d1cih__ 1.3.1.1.7 Mitochondrial cytochrome c {Baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgahsgqaegysytdaiikk
nvlwdennmseyltnpkkyipgtkmasgglkkekdrndlitylkkaae
>d1cii_1 6.1.1.1.3 (451-624) Colicin Ia {Escherichia coli}
dainftteflksvsekygakaeqlaremagqakgkkirnveealktyekyradinkkina
kdraaiaaalesvklsdissnlnrfsrglgyagkftsladwitefgkavrtenwrplfvk
tetiiagnaatalvalvfsiltgsalgiigygllmavtgalideslvekankfw
>d1cija_ 3.59.1.6.1 Haloalkane dehalogenase {Xanthobacter autotrophicus}
mvnairtpdqrfsnldqypfspnylddlpgypglrahyldegnsdaedvflclhgeptws
ylyrkmipvfaesgarviapdffgfgksdkpvdeedytfefhrnfllalierldlrnitl
vvqdwggflgltlpmadpsrfkrliimnaclmtdpvtqpafsafvtqpadgftawkydlv
tpsdlrldqfmkrwaptlteaeasayaapfpdtsyqagvrkfpkmvaqrdqacidistea
isfwqndwngqtfmaigmkdkllgpdvmypmkalingcpepleiadaghfvqefgeqvar
ealkhfaete
>d1cika_ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkplaqshatkhkapikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1cil__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasf
>d1cim__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasf
>d1cin__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasf
>d1cioa_ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkplaqshatkhkvpikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1cipa1 1.67.1.1.2 (61-181) Transducin (alpha subunit), insertion domain {Rat (Rattus rattus)}
yseeeckqykavvysntiqsiiaiiramgrlkidfgdaaraddarqlfvlagaaeegfmt
aelagvikrlwkdsgvqacfnrsreyqlndsaayylndldriaqpnyiptqqdvlrtrvk
t
>d1cipa2 3.30.1.6.13 (32-60,182-347) Transducin (alpha subunit) {Rat (Rattus rattus)}
revkllllgagesgkstivkqmkiiheagXtgivethftfkdlhfkmfdvggqrserkkw
ihcfegvtaiifcvalsdydlvlaedeemnrmhesmklfdsicnnkwftdtsiilflnkk
dlfeekikksplticypeyagsntyeeaaayiqcqfedlnkrkdtkeiythftcatdtkn
vqfvfdavtdviiknn
>e1ciq.1a 4.33.1.1.2 Chymotrypsin inhibitor CI-2 {Barley (Hordeum vulgare)}
ktewpelvgksveeakkvilqdkpeaqiivlpvgtiv
>e1ciq.1b 4.33.1.1.2 Chymotrypsin inhibitor CI-2 {Barley (Hordeum vulgare)}
eyridrvrlfvdkldniaqvprvg
>e1cir.1a 4.33.1.1.2 Chymotrypsin inhibitor CI-2 {Barley (Hordeum vulgare)}
mktewpelvgksveeakkvilqdkpeaqiivlpvgtivt
>e1cir.1b 4.33.1.1.2 Chymotrypsin inhibitor CI-2 {Barley (Hordeum vulgare)}
eyridrvrlfvdkldniaqvprvg
>d1cita_ 7.33.1.2.3 Orphan nuclear receptor NGFI-B {Rat (Rattus norvegicus)}
grcavcgdnascqhygvrtcegckgffkrtvqksakyiclankdcpvdkrrrnrcqfcrf
qkclavgmvkevvrtdslkgrrgrlpskp
>d1ciu_1 2.1.1.5.7 (496-578) Cyclodextrin glycosyltransferase, domain E {Thermoanaerobacterium thermosulfurigenes, EM1}
snsplighvgptmtkagqtitidgrgfgttsgqvlfgstagtivswddtevkvkvpsvtp
gkynislktssgatsntynnini
>d1ciu_2 2.3.1.1.4 (579-683) Cyclodextrin glycosyltransferase, C-terminal domain {Thermoanaerobacterium thermosulfurigenes, EM1}
ltgnqicvrfvvnnastvygenvyltgnvaelgnwdtskaigpmfnqvvyqyptwyydvs
vpagttiqfkfikkngntitweggsnhtytvpssstgtvivnwqq
>d1ciu_3 2.62.1.1.7 (407-495) Cyclodextrin glycosyltransferase {Thermoanaerobacterium thermosulfurigenes, EM1}
gttqqrwinndvyiyerkfgnnvalvainrnlstsynitglytalpagtytdvlggllng
nsisvasdgsvtpftlsagevavwqyvss
>d1ciu_4 3.1.7.1.7 (1-406) Cyclodextrin glycosyltransferase {Thermoanaerobacterium thermosulfurigenes, EM1}
asdtavsnvvnystdviyqivtdrfvdgntsnnptgdlydpthtslkkyfggdwqgiink
indgyltgmgvtaiwisqpveniyavlpdstfggstsyhgywardfkrtnpyfgsftdfq
nlintahahnikviidfapnhtspasetdptyaengrlydngtllggytndtngyfhhyg
gtdfssyedgiyrnlfdladlnqqnstidsylksaikvwldmgidgirldavkhmpfgwq
knfmdsilsyrpvftfgewflgtneidvnntyfanesgmslldfrfsqkvrqvfrdntdt
mygldsmiqstasdynfindmvtfidnhdmdrfynggstrpveqalaftltsrgvpaiyy
gteqymtgngdpynrammtsfntsttaynvikklaplrksnpaiay
>d1ciwa_ 2.26.1.1.10 Lectin {Peanut (Arachis hypogaea)}
aetvsfnfnsfsegnpainfqgdvtvlsngniqltnlnkvnsvgrvlyampvriwssatg
nvasfltsfsfemkdikdydpadgiiffiapedtqipagsigggtlgvsdtkgaghfvgv
efdtysnseyndpptdhvgidvnsvdsvktvpwnsvsgavvkvtviydsstktlsvavtn
dngdittiaqvvdlkaklpervkfgfsasgslggrqihlirswsftstlitt
>d1ciwb_ 2.26.1.1.10 Lectin {Peanut (Arachis hypogaea)}
aetvsfnfnsfsegnpainfqgdvtvlsngniqltnlnkvnsvgrvlyampvriwssatg
nvasfltsfsfemkdikdydpadgiiffiapedtqipagsigggtlgvsdtkgaghfvgv
efdtysnseyndpptdhvgidvnsvdsvktvpwnsvsgavvkvtviydsstktlsvavtn
dngdittiaqvvdlkaklpervkfgfsasgslggrqihlirswsftstlitt
>d1ciwc_ 2.26.1.1.10 Lectin {Peanut (Arachis hypogaea)}
aetvsfnfnsfsegnpainfqgdvtvlsngniqltnlnkvnsvgrvlyampvriwssatg
nvasfltsfsfemkdikdydpadgiiffiapedtqipagsigggtlgvsdtkgaghfvgv
efdtysnseyndpptdhvgidvnsvdsvktvpwnsvsgavvkvtviydsstktlsvavtn
dngdittiaqvvdlkaklpervkfgfsasgslggrqihlirswsftstlitt
>d1ciwd_ 2.26.1.1.10 Lectin {Peanut (Arachis hypogaea)}
aetvsfnfnsfsegnpainfqgdvtvlsngniqltnlnkvnsvgrvlyampvriwssatg
nvasfltsfsfemkdikdydpadgiiffiapedtqipagsigggtlgvsdtkgaghfvgv
efdtysnseyndpptdhvgidvnsvdsvktvpwnsvsgavvkvtviydsstktlsvavtn
dngdittiaqvvdlkaklpervkfgfsasgslggrqihlirswsftstlitt
>d1ciy_1 2.16.1.2.2 (462-609) delta-Endotoxin, C-terminal domain {Bacillus thuringiensis, CRYIA (A)}
nniipssqitqipltkstnlgsgtsvvkgpgftggdilrrtspgqistlrvnitaplsqr
yrvriryasttnlqfhtsidgrpinqgnfsatmssgsnlqsgsfrtvgfttpfnfsngss
vftlsahvfnsgnevyidriefvpaevt
>d1ciy_2 2.68.2.1.2 (256-461) delta-Endotoxin (insectocide), middle domain {Bacillus thuringiensis, CRYIA (A)}
pirtvsqltreiytnpvlenfdgsfrgmaqrieqnirqphlmdilnsitiytdvhrgfny
wsghqitaspvgfsgpefafplfgnagnaappvlvsltglgifrtlssplyrriilgsgp
nnqelfvldgtefsfaslttnlpstiyrqrgtvdsldvippqdnsvppragfshrlshvt
mlsqaagavytlraptfswqhrsaef
>d1ciy_3 6.1.3.1.2 (33-255) delta-Endotoxin (insectocide), N-terminal domain {Bacillus thuringiensis, CRYIA (A)}
ytpidislsltqfllsefvpgagfvlglvdiiwgifgpsqwdaflvqieqlinqrieefa
rnqaisrleglsnlyqiyaesfreweadptnpalreemriqfndmnsalttaipllavqn
yqvpllsvyvqaanlhlsvlrdvsvfgqrwgfdaatinsryndltrlignytdyavrwyn
tglervwgpdsrdwvrynqfrreltltvldivalfsnydsrry
>d1ciza_ 4.71.1.9.4 Stromelysin-1 (MMP-3) {Human (Homo sapiens), fibroblast}
frtfpgipkwrkthltyrivnytpdlpkdavdsavekalkvweevtpltfsrlyegeadi
misfavrehgdfypfdgpgnvlahayapgpgingdahfdddeqwtkdttgtnlflvaahe
ighslglfhsantealmyplyhsltdltrfrlsqddingiqslygppp
>d1cj0a_ 3.57.1.4.6 Serine hydroxymethyltransferase {Rabbit (Oryctolagus cuniculus)}
wssheqmlaqplkdsdaevydiikkesnrqrvgleliasenfasravlealgsclnnkys
egypgqryyggtehideletlcqkralqaygldpqcwgvnvqpysgspanfavytalvep
hgrimgldlpdgghlthgfmtdkkkisatsiffesmaykvnpdtgyidydrleenarlfh
pkliiagtscysrnldygrlrkiadengaylmadmahisglvvagvvpspfehchvvttt
thktlrgcragmifyrrgvrsvdpktgkeilynleslinsavfpglqggphnhaiagvav
alkqamtpefkeyqrqvvancralsaalvelgykivtggsdnhlilvdlrskgtdggrae
kvleacsiacnkntcpgdksalrpsglrlgtpaltsrgllekdfqkvahfihrgieltvq
iqddtgpratlkefkeklagdekhqravralrqevesfaalfplpglpgf
>d1cj0b_ 3.57.1.4.6 Serine hydroxymethyltransferase {Rabbit (Oryctolagus cuniculus)}
wssheqmlaqplkdsdaevydiikkesnrqrvgleliasenfasravlealgsclnnkys
egypgqryyggtehideletlcqkralqaygldpqcwgvnvqpysgspanfavytalvep
hgrimgldlpdgghlthgfmtdkkkisatsiffesmaykvnpdtgyidydrleenarlfh
pkliiagtscysrnldygrlrkiadengaylmadmahisglvvagvvpspfehchvvttt
thktlrgcragmifyrrgvrsvdpktgkeilynleslinsavfpglqggphnhaiagvav
alkqamtpefkeyqrqvvancralsaalvelgykivtggsdnhlilvdlrskgtdggrae
kvleacsiacnkntcpgdksalrpsglrlgtpaltsrgllekdfqkvahfihrgieltvq
iqddtgpratlkefkeklagdekhqravralrqevesfaalfplpglpgf
>d1cj2a1 3.3.1.2.3 (1-173,276-391) p-Hydroxybenzoate hydroxylase (PHBH) {Pseudomonas fluorescens}
mktqvaiigagpsglllgqllhkagidnvilerrtpdyvlgriragvleqgmvdllreag
vdrrmardglvhegveiafagqrrridlkrlsggktvtvygqtevtrdlmeareasgatt
vyqaaevrlhdlqgerpyvtferdgerlrldcdyiagcdgfhgisrqsipaerXmqhgrl
flagdaahivpptgakglnlaasdvstlyrlllkayregrgellerysaiclrriwkaer
fswwmtsvlhrfpdtdafsqriqqteleyylgseaglatiaenyvglpye
>d1cj2a2 4.14.1.2.1 (174-275) p-Hydroxybenzoate hydroxylase, PHBH {Pseudomonas fluorescens}
lkvfervypfgwlglladtppvsheliyanhprgfalcsqrsatrsryyvqvpltekved
wsderfwtelkarlpaevaeklvtgpsleksiaplrsfvvep
>d1cj3a1 3.3.1.2.3 (1-173,276-392) p-Hydroxybenzoate hydroxylase (PHBH) {Pseudomonas fluorescens}
mktqvaiigagpsglllgqllhkagidnvilerqtpdevlgriragvleqgmvdllreag
vdrrmardglvhegveiafagqrrridlkrlsggktvtvygqtevtrdlmeareasgatt
vyqaaevrlhdlqgerpyvtferdgerlrldcdyiagcdgfhgisrqsipaerXmqhgrl
flagdaahivpptgakglnlaasdvstlyrlllkayregrgellerysaiclrriwkaer
fswwmtsvlhrfpdtdafsqriqqteleyylgseaglatiaenyvglpyee
>d1cj3a2 4.14.1.2.1 (174-275) p-Hydroxybenzoate hydroxylase, PHBH {Pseudomonas fluorescens}
lkvfervypfgwlglladtppvsheliyanhprgfalcsqrsatrsryyvqvpltekved
wsderfwtelkarlpaevaeklvtgpsleksiaplrsfvvep
>d1cj4a1 3.3.1.2.3 (1-173,276-392) p-Hydroxybenzoate hydroxylase (PHBH) {Pseudomonas fluorescens}
mktqvaiigagpsglllgqllhkagidnvilerttpdyvlgriragvleqgmvdllreag
vdrrmardglvhegveiafagqrrridlkrlsggktvtvygqtevtrdlmeareasgatt
vyqaaevrlhdlqgerpyvtferdgerlrldcdyiagcdgfhgisrqsipaerXmqhgrl
flagdaahivpptgakglnlaasdvstlyrlllkayregrgellerysaiclrriwkaer
fswwmtsvlhrfpdtdafsqriqqteleyylgseaglatiaenyvglpyee
>d1cj4a2 4.14.1.2.1 (174-275) p-Hydroxybenzoate hydroxylase, PHBH {Pseudomonas fluorescens}
lkvfervypfgwlglladtppvsheliyanhprgfalcsqrsatrsryyvqvpltekved
wsderfwtelkarlpaevaeklvtgpsleksiaplrsfvvep
>d1cj6a_ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelaralkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1cj7a_ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelarvlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1cj8a_ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgynaratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1cj9a_ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgynvratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1cjaa_ 4.117.1.3.1 Actin-fragmin kinase {Slime mold (Physarum polycephalum)}
agalweiekelftklpapssainshlqpakpkvpqkkpskwdppaefkvdlstavsyndi
gdinwknlqqfkgiersekgteglffvetesgvfivkrstniesetfcsllcmrlglhap
kvrvvssnseegtnmleclaaidksfrvittlanqanillmelvrgitlnkltttsapev
ltkstmqqlgslmaldvivnnsdrlpiawtnegnldnimlsergatvvpidskiipldas
hphgervrellrtliahpghessqfhsirdiitlytgydvgtegsismqegflatvreca
sfdldaferellswqeslqkchnlsispqaipfilrmlrifh
>d1cjab_ 4.117.1.3.1 Actin-fragmin kinase {Slime mold (Physarum polycephalum)}
agalweiekelftklpapssainshlqpakpkvpqkkpskwdppaefkvdlstavsyndi
gdinwknlqqfkgiersekgteglffvetesgvfivkrstniesetfcsllcmrlglhap
kvrvvssnseegtnmleclaaidksfrvittlanqanillmelvrgitlnkltttsapev
ltkstmqqlgslmaldvivnnsdrlpiawtnegnldnimlsergatvvpidskiipldas
hphgervrellrtliahpghessqfhsirdiitlytgydvgtegsismqegflatvreca
sfdldaferellswqeslqkchnlsispqaipfilrmlrifh
>d1cjba_ 3.51.1.1.7 Hypoxantine-guanine PRTase {Plasmodium falciparum}
pipnnpgagenafdpvfvndddgydldsfmipahykkyltkvlvpngviknrieklaydi
kkvynneefhilcllkgsrgfftallkhlsrihnysavetskplfgehyvrvksycndqs
tgtleivsedlsclkgkhvlivediidtgktlvkfceylkkfeiktvaiaclfikrtplw
ngfkadfvgfsipdhfvvgysldyneifrdldhcclvndegkkkykat
>d1cjbb_ 3.51.1.1.7 Hypoxantine-guanine PRTase {Plasmodium falciparum}
pipnnpgagenafdpvfvndddgydldsfmipahykkyltkvlvpngviknrieklaydi
kkvynneefhilcllkgsrgfftallkhlsrihnysavetskplfgehyvrvksycndqs
tgtleivsedlsclkgkhvlivediidtgktlvkfceylkkfeiktvaiaclfikrtplw
ngfkadfvgfsipdhfvvgysldyneifrdldhcclvndegkkkykat
>d1cjbc_ 3.51.1.1.7 Hypoxantine-guanine PRTase {Plasmodium falciparum}
pipnnpgagenafdpvfvndddgydldsfmipahykkyltkvlvpngviknrieklaydi
kkvynneefhilcllkgsrgfftallkhlsrihnysavetskplfgehyvrvksycndqs
tgtleivsedlsclkgkhvlivediidtgktlvkfceylkkfeiktvaiaclfikrtplw
ngfkadfvgfsipdhfvvgysldyneifrdldhcclvndegkkkykatsl
>d1cjbd_ 3.51.1.1.7 Hypoxantine-guanine PRTase {Plasmodium falciparum}
pipnnpgagenafdpvfvndddgydldsfmipahykkyltkvlvpngviknrieklaydi
kkvynneefhilcllkgsrgfftallkhlsrihnysavetskplfgehyvrvksycndqs
tgtleivsedlsclkgkhvlivediidtgktlvkfceylkkfeiktvaiaclfikrtplw
ngfkadfvgfsipdhfvvgysldyneifrdldhcclvndegkkkykat
>d1cjca1 3.3.1.1.2 (107-331) Adrenodoxin reductase of mitochondrial p450 systems {Bovine (Bos taurus)}
hqaldipgeelpgvfsarafvgwynglpenrelapdlscdtavilgqgnvaldvarillt
ppdhlektditeaalgalrqsrvktvwivgrrgplqvaftikelremiqlpgtrpmldpa
dflglqdrikeaarprkrlmelllrtatekpgveeaarrasasrawglrffrspqqvlps
pdgrraagirlavtrlegigeatravptgdvedlpcglvlssigy
>d1cjca2 3.4.1.1.2 (6-106,332-460) Adrenodoxin reductase of mitochondrial p450 systems {Bovine (Bos taurus)}
tpqicvvgsgpagfytaqhllkhhsrahvdiyekqlvpfglvrfgvapdhpevknvintf
tqtarsdrcafygnvevgrdvtvqelqdayhavvlsygaedXksrpidpsvpfdpklgvv
pnmegrvvdvpglycsgwvkrgptgvitttmtdsfltgqillqdlkaghlpsgprpgsaf
ikalldsrgvwpvsfsdwekldaeevsrgqasgkpreklldpqemlrllgh
>d1cjda_ 2.12.2.1.1 Coat protein p3 {Bacteriophage prd1}
lrnqqamaanlqarqivlqqsypviqqvetqtfdpanrsvfdvtpanvgivkgflvkvta
aitnnhateavaltdfgpanlvqrviyydpdnqrhtetsgwhlhfvntakqgapflssmv
tdspikygdvmnvidapatiaagatgeltmyywvplaysetdltgavlanvpqskqrlkl
efannntafaavganpleaiyqgagaadcefeeisytvyqsyldqlpvgqngyilplidl
stlynlensaqagltpnvdfvvqyanlyrylstiavfdnggsfnagtdinylsqrtanfs
dtrkldpktwaaqtrrriatdfpkgvyycdnrdkpiytlqygnvgfvvnpktvnqnarll
mgyeyftsr
>d1cjdb_ 2.12.2.1.1 Coat protein p3 {Bacteriophage prd1}
aalrnqqamaanlqarqivlqqsypviqqvetqtfdpanrsvfdvtpanvgivkgflvkv
taaitnnhateavaltdfgpanlvqrviyydpdnqrhtetsgwhlhfvntakqgapflss
mvtdspikygdvmnvidapatiaagatgeltmyywvplaysetdltgavlanvpqskqrl
klefannntafaavganpleaiyqgagaadcefeeisytvyqsyldqlpvgqngyilpli
dlstlynlensaqagltpnvdfvvqyanlyrylstiavfdnggsfnagtdinylsqrtan
fsdtrkldpktwaaqtrrriatdfpkgvyycdnrdkpiytlqygnvgfvvnpktvnqnar
llmgyeyftsrt
>d1cjdc_ 2.12.2.1.1 Coat protein p3 {Bacteriophage prd1}
rnqqamaanlqarqivlqqsypviqqvetqtfdpanrsvfdvtpanvgivkgflvkvtaa
itnnhateavaltdfgpanlvqrviyydpdnqrhtetsgwhlhfvntakqgapflssmvt
dspikygdvmnvidapatiaagatgeltmyywvplaysetdltgavlanvpqskqrlkle
fannntafaavganpleaiyqgagaadcefeeisytvyqsyldqlpvgqngyilplidls
tlynlensaqagltpnvdfvvqyanlyrylstiavfdnggsfnagtdinylsqrtanfsd
trkldpktwaaqtrrriatdfpkgvyycdnrdkpiytlqygnvgfvvnpktvnqnarllm
gyeyftsrt
>d1cjfa_ 4.86.1.1.2 Profilin (actin-binding protein) {Human (Homo sapiens)}
gwnayidnlmadgtcqdaaivgykdspsvwaavpgktfvnitpaevgvlvgkdrssfyvn
gltlggqkcsvirdsllqdgefsmdlrtkstggaptfnvtvtktdktlvllmgkegvhgg
linkkcyemashlrrsqy
>d1cjfb_ 4.86.1.1.2 Profilin (actin-binding protein) {Human (Homo sapiens)}
gwnayidnlmadgtcqdaaivgykdspsvwaavpgktfvnitpaevgvlvgkdrssfyvn
gltlggqkcsvirdsllqdgefsmdlrtkstggaptfnvtvtktdktlvllmgkegvhgg
linkkcyemashlrrsqy
>d1cjka_ 4.47.24.1.2 Adenylyl cyclase VC1, domain C1a {Dog (Canis familiaris)}
mmfhkiyiqkhdnvsilfadiegftslasqctaqelvmtlnelfarfdklaaenhclrik
ilgdcyycvsglpearadhahccvemgmdmieaislvrevtgvnvnmrvgihsgrvhcgv
lglrkwqfdvwsndvtlanhmeaggkagrihitkatlsylngdyevepgcggernaylke
hsietflil
>d1cjkb_ 4.47.24.1.3 Adenylyl cyclase IIC1, domain C2a {Rat (Rattus norvegicus)}
lyhqsydcvcvmfasipdfkefytesdvnkegleclrllneiiadfddllskpkfsgvek
iktigstymaatglsaipsqehaqeperqymhigtmvefayalvgkldainkhsfndfkl
rvginhgpviagvigaqkpqydiwgntvnvasrmdstgvldkiqvteetslilqtlgytc
tcrgiinvkgkgdlktyfvnt
>d1cjkc1 1.67.1.1.1 (86-201) Transducin (alpha subunit), insertion domain {Bovine (Bos taurus)}
gekatkvqdiknnlkeaietivaamsnlvppvelanpenqfrvdyilsvmnvpdfdfppe
fyehakalwedegvracyersneyqlidcaqyfldkidvikqddyvpsdqdllrcr
>d1cjkc2 3.30.1.6.12 (39-65,202-388) Transducin (alpha subunit) {Bovine (Bos taurus)}
athrllllgagesgkstivkqmrilhvXvltsgifetkfqvdkvnfhmfdvggqrderrk
wiqcfndvtaiifvvasssynmvirednqtnrlqealnlfksiwnnrwlrtisvilflnk
qdllaekvlagkskiedyfpefaryttpedatpepgedprvtrakyfirdeflristasg
dgrhycyphftcavdtenirrvfndcrdiiqrmhl
>d1cjl__ 4.3.1.1.12 (Pro)cathepsin L {Human (Homo sapiens)}
dhsleaqwtkwkamhnrlygmneegwrravweknmkmielhnqeyregkhsftmamnafg
dmtseefrqvmnglqnrkprkgkvfqeplfyeaprsvdwrekgyvtpvknqgqcgsswaf
satgalegqmfrktgrlislseqnlvdcsgpegnegcngglmdyafqyvqdnggldsees
ypyeateesckynpkysvandagfvdipkqekalmkavatvgpisvaidaghesflfyke
giyfepdcssedmdhgvlvvgygfestesdgnkywlvknswgeewgmggyvkmakdrrnh
cgiasaasyptv
>d1cjpa_ 2.26.1.1.1 Concanavalin A {Jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1cjpb_ 2.26.1.1.1 Concanavalin A {Jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1cjpc_ 2.26.1.1.1 Concanavalin A {Jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1cjpd_ 2.26.1.1.1 Concanavalin A {Jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>e1cjq.1b 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
nycnqmmksrnltkdrckpvntfvhesladvqavcsqknvackngqtncyqsystmsitd
cretgsskypncaykttqankhiivacegnpyvpvhfdasv
>e1cjr.1b 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
nycnqmmksrnltkdrckpvntfvhesladvqavcsqknvackngqtncyqsystmsitd
cretgsskypncaykttqankhiivacegnpyvpvhfdasv
>d1cjta_ 4.47.24.1.2 Adenylyl cyclase VC1, domain C1a {Dog (Canis familiaris)}
mmfhkiyiqkhdnvsilfadiegftslasqctaqelvmtlnelfarfdklaaenhclrik
ilgdcyycvsglpearadhahccvemgmdmieaislvrevtgvnvnmrvgihsgrvhcgv
lglrkwqfdvwsndvtlanhmeaggkagrihitkatlsylngdyevepgcggernaylke
hsietflil
>d1cjtb_ 4.47.24.1.3 Adenylyl cyclase IIC1, domain C2a {Rat (Rattus norvegicus)}
yhqsydcvcvmfasipdfkefytesdvnkegleclrllneiiadfddllskpkfsgveki
ktigstymaatglsaipsqehaqeperqymhigtmvefayalvgkldainkhsfndfklr
vginhgpviagvigaqkpqydiwgntvnvasrmdstgvldkiqvteetslilqtlgytct
crgiinvkgkgdlktyfvnt
>d1cjtc1 1.67.1.1.1 (86-201) Transducin (alpha subunit), insertion domain {Bovine (Bos taurus)}
gekatkvqdiknnlkeaietivaamsnlvppvelanpenqfrvdyilsvmnvpdfdfppe
fyehakalwedegvracyersneyqlidcaqyfldkidvikqddyvpsdqdllrcr
>d1cjtc2 3.30.1.6.12 (39-65,202-388) Transducin (alpha subunit) {Bovine (Bos taurus)}
athrllllgagesgkstivkqmrilhvXvltsgifetkfqvdkvnfhmfdvggqrderrk
wiqcfndvtaiifvvasssynmvirednqtnrlqealnlfksiwnnrwlrtisvilflnk
qdllaekvlagkskiedyfpefaryttpedatpepgedprvtrakyfirdeflristasg
dgrhycyphftcavdtenirrvfndcrdiiqrmhl
>d1cjua_ 4.47.24.1.2 Adenylyl cyclase VC1, domain C1a {Dog (Canis familiaris)}
mmfhkiyiqkhdnvsilfadiegftslasqctaqelvmtlnelfarfdklaaenhclrik
ilgdcyycvsglpearadhahccvemgmdmieaislvrevtgvnvnmrvgihsgrvhcgv
lglrkwqfdvwsndvtlanhmeaggkagrihitkatlsylngdyevepgcggernaylke
hsietflil
>d1cjub_ 4.47.24.1.3 Adenylyl cyclase IIC1, domain C2a {Rat (Rattus norvegicus)}
yhqsydcvcvmfasipdfkefytesdvnkegleclrllneiiadfddllskpkfsgveki
ktigstymaatglsaipsqehaqeperqymhigtmvefayalvgkldainkhsfndfklr
vginhgpviagvigaqkpqydiwgntvnvasrmdstgvldkiqvteetslilqtlgytct
crgiinvkgkgdlktyfvnt
>d1cjuc1 1.67.1.1.1 (86-201) Transducin (alpha subunit), insertion domain {Bovine (Bos taurus)}
gekatkvqdiknnlkeaietivaamsnlvppvelanpenqfrvdyilsvmnvpdfdfppe
fyehakalwedegvracyersneyqlidcaqyfldkidvikqddyvpsdqdllrcr
>d1cjuc2 3.30.1.6.12 (39-66,202-388) Transducin (alpha subunit) {Bovine (Bos taurus)}
athrllllgagesgkstivkqmrilhvnXvltsgifetkfqvdkvnfhmfdvggqrderr
kwiqcfndvtaiifvvasssynmvirednqtnrlqealnlfksiwnnrwlrtisvilfln
kqdllaekvlagkskiedyfpefaryttpedatpepgedprvtrakyfirdeflristas
gdgrhycyphftcavdtenirrvfndcrdiiqrmhl
>d1cjva_ 4.47.24.1.2 Adenylyl cyclase VC1, domain C1a {Dog (Canis familiaris)}
mmfhkiyiqkhdnvsilfadiegftslasqctaqelvmtlnelfarfdklaaenhclrik
ilgdcyycvsglpearadhahccvemgmdmieaislvrevtgvnvnmrvgihsgrvhcgv
lglrkwqfdvwsndvtlanhmeaggkagrihitkatlsylngdyevepgcggernaylke
hsietflil
>d1cjvb_ 4.47.24.1.3 Adenylyl cyclase IIC1, domain C2a {Rat (Rattus norvegicus)}
hqsydcvcvmfasipdfkefytesdvnkegleclrllneiiadfddllskpkfsgvekik
tigstymaatglsaipsqehaqeperqymhigtmvefayalvgkldainkhsfndfklrv
ginhgpviagvigaqkpqydiwgntvnvasrmdstgvldkiqvteetslilqtlgytctc
rgiinvkgkgdlktyfvnt
>d1cjvc1 1.67.1.1.1 (87-201) Transducin (alpha subunit), insertion domain {Bovine (Bos taurus)}
ekatkvqdiknnlkeaietivaamsnlvppvelanpenqfrvdyilsvmnvpdfdfppef
yehakalwedegvracyersneyqlidcaqyfldkidvikqddyvpsdqdllrcr
>d1cjvc2 3.30.1.6.12 (39-65,202-388) Transducin (alpha subunit) {Bovine (Bos taurus)}
athrllllgagesgkstivkqmrilhvXvltsgifetkfqvdkvnfhmfdvggqrderrk
wiqcfndvtaiifvvasssynmvirednqtnrlqealnlfksiwnnrwlrtisvilflnk
qdllaekvlagkskiedyfpefaryttpedatpepgedprvtrakyfirdeflristasg
dgrhycyphftcavdtenirrvfndcrdiiqrmhl
>d1cjwa_ 4.84.1.1.7 Serotonin N-acetyltranferase {Sheep (Ovis aries)}
htlpanefrcltpedaagvfeiereafisvsgncplnldevqhfltlcpelslgwfvegr
lvafiigslwdeerltqeslalhrprghsahlhalavhrsfrqqgkgsvllwrylhhvga
qpavrravlmcedalvpfyqrfgfhpagpcaivvgsltftemhcsl
>d1ck2a_ 4.59.3.1.1 Eukaryotic ribosomal protein L30 (eL30) {Baker's yeast (Saccharomyces cerevisiae)}
apvksqesinqklalviksgkytlgykstvkslrqgkskliiiaantpvlrkseleyyam
lsktkvyyfqggnnelgtavgklfrvgvvsileagdsdilttla
>d1ck3a_ 5.3.1.1.3 beta-Lactamase, class A {Escherichia coli, TEM-1}
hpetlvkvkdaedqlgarvgyieldlnsgailesfrpeerfpmmstfkvllcgavlsrid
agqeqlgrrihysandlveyspvteshltdgmtvrelcsaaitmsdntaanlllttiggp
aeltaflhnmgdhvtrldrwepelneaipnderdttmpvamattlrklltgaaltlasrq
qlidwmeadsvagpllrsalpagwfiadksgagergsrgiiaalgpdgapsrivviyttg
sqatmderdrqiaeigaslikhw
>d1ck7a1 2.58.1.1.2 (461-660) Gelatinase A (MMP-2), C-terminal domain {Human (Homo sapiens)}
lgpvtpeickqdivfdgiaqirgeifffkdrfiwrtvtprdkpmgpllvatfwpelpeki
davyeapqeekavffagneywiysastlergypkpltslglppdvqrvdaafnwsknkkt
yifagdkfwrynevkkkmdpgfpkliadawnaipdnldavvdlqggghsyffkgayylkl
enqslksvkfgsiksdwlgc
>d1ck7a2 4.71.1.9.3 (31-216,394-449) Gelatinase A {Human (Homo sapiens)}
pspiikfpgdvapktdkelavqylntfygcpkescnlfvlkdtlkkmqkffglpqtgdld
qntietmrkprcgnpdvanynffprkpkwdknqityriigytpdldpetvddafarafqv
wsdvtplrfsrihdgeadiminfgrwehgdgypfdgkdgllahafapgtgvggdshfddd
elwtlgXgyslflvaahafghamglehsqdpgalmapiytytknfrlsqddikgiqelyg
asp
>d1ck7a3 7.14.1.2.3 (217-277) Gelatinase A modules {Human (Homo sapiens)}
egqvvrvkygnadgeyckfpflfngkeynsctdtgrsdgflwcsttynfekdgkygfcph
e
>d1ck7a4 7.14.1.2.3 (278-335) Gelatinase A modules {Human (Homo sapiens)}
alftmggnaegqpckfpfrfqgtsydscttegrtdgyrwcgttedydrdkkygfcpet
>d1ck7a5 7.14.1.2.3 (336-393) Gelatinase A modules {Human (Homo sapiens)}
amstvggnsegapcvfpftflgnkyesctsagrsdgkmwcattanydddrkwgfcpdq
>d1ck9a_ 4.59.3.1.1 Eukaryotic ribosomal protein L30 (eL30) {Baker's yeast (Saccharomyces cerevisiae)}
apvksqesinqklalviksgkytlgykstvkslrqgkskliiiaantpvlrkseleyyam
lsktkvyyfqggnnelgtavgklfrvgvvsileagdsdilttla
>d1ckaa_ 2.30.2.1.1 C-Crk, N-terminal SH3 domain {Mouse (Mus musculus)}
aeyvralfdfngndeedlpfkkgdilrirdkpeeqwwnaedsegkrgmipvpyveky
>d1ckba_ 2.30.2.1.1 C-Crk, N-terminal SH3 domain {Mouse (Mus musculus)}
aeyvralfdfngndeedlpfkkgdilrirdkpeeqwwnaedsegkrgmipvpyveky
>d1ckca_ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntraanynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1ckda_ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntravnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1ckea_ 3.30.1.1.4 CMP kinase {Escherichia coli}
aiapvitidgpsgagkgtlckamaealqwhlldsgaiyrvlalaalhhhvdvasedalvp
lashldvrfvstngnlevilegedvsgeirtqevanaasqvaafprvreallrrqrafre
lpgliadgrdmgtvvfpdapvkifldasseerahrrmlqlqvkgfsvnferllaeikerd
drdrnravaplvpaadalvldsttlsieqviekalqyarqklala
>d1ckfa_ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrsadygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1ckga_ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrsvdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1ckgb_ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrsvdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1ckha_ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgkvpgavnachlscsallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1ckia_ 4.117.1.1.16 Casein kinase-1, CK1 {Rat (Rattus norvegicus)}
melrvgnryrlgrkigsgsfgdiylgtdiaageevaiklecvktkhpqlhieskiykmmq
ggvgiptirwcgaegdynvmvmellgpsledlfnfcsrkfslktvllladqmisrieyih
sknfihrdvkpdnflmglgkkgnlvyiidfglakkyrdarthqhipyrenknltgtarya
sinthlgieqsrrddleslgyvlmyfnlgslpwqglkaatkrqkyerisekkmstpievl
ckgypsefatylnfcrslrfddkpdysylrqlfrnlfhrqgfsydyvfdwnmlkfgasr
>d1ckib_ 4.117.1.1.16 Casein kinase-1, CK1 {Rat (Rattus norvegicus)}
melrvgnryrlgrkigsgsfgdiylgtdiaageevaiklecvktkhpqlhieskiykmmq
ggvgiptirwcgaegdynvmvmellgpsledlfnfcsrkfslktvllladqmisrieyih
sknfihrdvkpdnflmglgkkgnlvyiidfglakkyrdarthqhipyrenknltgtarya
sinthlgieqsrrddleslgyvlmyfnlgslpwqglkaatkrqkyerisekkmstpievl
ckgypsefatylnfcrslrfddkpdysylrqlfrnlfhrqgfsydyvfdwnml
>d1ckja_ 4.117.1.1.16 Casein kinase-1, CK1 {Rat (Rattus norvegicus)}
melrvgnryrlgrkigsgsfgdiylgtdiaageevaiklecvktkhpqlhieskiykmmq
ggvgiptirwcgaegdynvmvmellgpsledlfnfcsrkfslktvllladqmisrieyih
sknfihrdvkpdnflmglgkkgnlvyiidfglakkyrdarthqhipyrenknltgtarya
sinthlgieqsrrddleslgyvlmyfnlgslpwqglkaatkrqkyerisekkmstpievl
ckgypsefatylnfcrslrfddkpdysylrqlfrnlfhrqgfsydyvfdwnmlkfg
>d1ckjb_ 4.117.1.1.16 Casein kinase-1, CK1 {Rat (Rattus norvegicus)}
melrvgnryrlgrkigsgsfgdiylgtdiaageevaiklecvktkhpqlhieskiykmmq
ggvgiptirwcgaegdynvmvmellgpsledlfnfcsrkfslktvllladqmisrieyih
sknfihrdvkpdnflmglgkkgnlvyiidfglakkyrdarthqhipyrenknltgtarya
sinthlgieqsrrddleslgyvlmyfnlgslpwqglkaatkrqkyerisekkmstpievl
ckgypsefatylnfcrslrfddkpdysylrqlfrnlfhrqgfsydyvfdwnml
>d1ckka_ 1.42.1.5.11 Calmodulin {African frog (Xenopus laevis)}
adqlteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgn
gtidfpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdee
vdemireadidgdgqvnyeefvqmmtak
>d1ckla1 7.18.1.1.3 (1-62) CD46 (membrane cofactor protein, MCP) {Human (Homo sapiens)}
ceepptfeameligkpkpyyeigervdykckkgyfyipplathticdrnhtwlpvsddac
yr
>d1ckla2 7.18.1.1.3 (63-126) CD46 (membrane cofactor protein, MCP) {Human (Homo sapiens)}
etcpyirdplngqavpangtyefgyqmhficnegyyligeeilycelkgsvaiwsgkppi
cekv
>d1cklb1 7.18.1.1.3 (1-62) CD46 (membrane cofactor protein, MCP) {Human (Homo sapiens)}
ceepptfeameligkpkpyyeigervdykckkgyfyipplathticdrnhtwlpvsddac
yr
>d1cklb2 7.18.1.1.3 (63-126) CD46 (membrane cofactor protein, MCP) {Human (Homo sapiens)}
etcpyirdplngqavpangtyefgyqmhficnegyyligeeilycelkgsvaiwsgkppi
cekv
>d1cklc1 7.18.1.1.3 (1-62) CD46 (membrane cofactor protein, MCP) {Human (Homo sapiens)}
ceepptfeameligkpkpyyeigervdykckkgyfyipplathticdrnhtwlpvsddac
yr
>d1cklc2 7.18.1.1.3 (63-126) CD46 (membrane cofactor protein, MCP) {Human (Homo sapiens)}
etcpyirdplngqavpangtyefgyqmhficnegyyligeeilycelkgsvaiwsgkppi
cekv
>d1ckld1 7.18.1.1.3 (1-62) CD46 (membrane cofactor protein, MCP) {Human (Homo sapiens)}
ceepptfeameligkpkpyyeigervdykckkgyfyipplathticdrnhtwlpvsddac
yr
>d1ckld2 7.18.1.1.3 (63-126) CD46 (membrane cofactor protein, MCP) {Human (Homo sapiens)}
etcpyirdplngqavpangtyefgyqmhficnegyyligeeilycelkgsvaiwsgkppi
cekv
>d1ckle1 7.18.1.1.3 (1-62) CD46 (membrane cofactor protein, MCP) {Human (Homo sapiens)}
ceepptfeameligkpkpyyeigervdykckkgyfyipplathticdrnhtwlpvsddac
yr
>d1ckle2 7.18.1.1.3 (63-126) CD46 (membrane cofactor protein, MCP) {Human (Homo sapiens)}
etcpyirdplngqavpangtyefgyqmhficnegyyligeeilycelkgsvaiwsgkppi
cekv
>d1cklf1 7.18.1.1.3 (1-62) CD46 (membrane cofactor protein, MCP) {Human (Homo sapiens)}
ceepptfeameligkpkpyyeigervdykckkgyfyipplathticdrnhtwlpvsddac
yr
>d1cklf2 7.18.1.1.3 (63-126) CD46 (membrane cofactor protein, MCP) {Human (Homo sapiens)}
etcpyirdplngqavpangtyefgyqmhficnegyyligeeilycelkgsvaiwsgkppi
cekv
>d1ckma1 2.35.4.6.1 (239-327) RNA guanylyltransferase (mRNA capping enzyme) {Chlorella virus, PBCV-1}
thhtidfiimsedgtigifdpnlrknvpvgkldgyynkgsivecgfadgtwkyiqgrsdk
nqandrltyektllnieenitidelldlf
>d1ckma2 4.115.2.2.1 (11-238) RNA guanylyltransferase (mRNA capping enzyme), N-terminal domain {Chlorella virus, PBCV-1}
nitteravltlnglqiklhkvvgesrddivakmkdlamddhkfprlpgpnpvsierkdfe
klkqnkyvvsektdgirfmmfftrvfgfkvctiidramtvyllpfkniprvlfqgsifdg
elcvdivekkfafvlfdavvvsgvtvsqmdlasrffamkrslkefknvpedpailrykew
iplehptiikdhlkkanaiyhtdgliimsvdepviygrnfnlfklkpg
>d1ckmb1 2.35.4.6.1 (239-327) RNA guanylyltransferase (mRNA capping enzyme) {Chlorella virus, PBCV-1}
thhtidfiimsedgtigifdpnlrknvpvgkldgyynkgsivecgfadgtwkyiqgrsdk
nqandrltyektllnieenitidelldlf
>d1ckmb2 4.115.2.2.1 (11-238) RNA guanylyltransferase (mRNA capping enzyme), N-terminal domain {Chlorella virus, PBCV-1}
nitteravltlnglqiklhkvvgesrddivakmkdlamddhkfprlpgpnpvsierkdfe
klkqnkyvvsektdgirfmmfftrvfgfkvctiidramtvyllpfkniprvlfqgsifdg
elcvdivekkfafvlfdavvvsgvtvsqmdlasrffamkrslkefknvpedpailrykew
iplehptiikdhlkkanaiyhtdgliimsvdepviygrnfnlfklkpg
>d1ckna1 2.35.4.6.1 (239-327) RNA guanylyltransferase (mRNA capping enzyme) {Chlorella virus, PBCV-1}
thhtidfiimsedgtigifdpnlrknvpvgkldgyynkgsivecgfadgtwkyiqgrsdk
nqandrltyektllnieenitidelldlf
>d1ckna2 4.115.2.2.1 (11-238) RNA guanylyltransferase (mRNA capping enzyme), N-terminal domain {Chlorella virus, PBCV-1}
nitteravltlnglqiklhkvvgesrddivakmkdlamddhkfprlpgpnpvsierkdfe
klkqnkyvvsektdgirfmmfftrvfgfkvctiidramtvyllpfkniprvlfqgsifdg
elcvdivekkfafvlfdavvvsgvtvsqmdlasrffamkrslkefknvpedpailrykew
iplehptiikdhlkkanaiyhtdgliimsvdepviygrnfnlfklkpg
>d1cknb1 2.35.4.6.1 (239-327) RNA guanylyltransferase (mRNA capping enzyme) {Chlorella virus, PBCV-1}
thhtidfiimsedgtigifdpnlrknvpvgkldgyynkgsivecgfadgtwkyiqgrsdk
nqandrltyektllnieenitidelldlf
>d1cknb2 4.115.2.2.1 (11-238) RNA guanylyltransferase (mRNA capping enzyme), N-terminal domain {Chlorella virus, PBCV-1}
nitteravltlnglqiklhkvvgesrddivakmkdlamddhkfprlpgpnpvsierkdfe
klkqnkyvvsextdgirfmmfftrvfgfkvctiidramtvyllpfkniprvlfqgsifdg
elcvdivekkfafvlfdavvvsgvtvsqmdlasrffamkrslkefknvpedpailrykew
iplehptiikdhlkkanaiyhtdgliimsvdepviygrnfnlfklkpg
>d1cko_1 2.35.4.6.1 (239-327) RNA guanylyltransferase (mRNA capping enzyme) {Chlorella virus, PBCV-1}
thhtidfiimsedgtigifdpnlrknvpvgkldgyynkgsivecgfadgtwkyiqgrsdk
nqandrltyektllnieenitidelldlf
>d1cko_2 4.115.2.2.1 (11-238) RNA guanylyltransferase (mRNA capping enzyme), N-terminal domain {Chlorella virus, PBCV-1}
nitteravltlnglqiklhkvvgesrddivakmkdlamddhkfprlpgpnpvsierkdfe
klkqnkyvvsektdgirfmmfftrvfgfkvctiidramtvyllpfkniprvlfqgsifdg
elcvdivekkfafvlfdavvvsgvtvsqmdlasrffamkrslkefknvpedpailrykew
iplehptiikdhlkkanaiyhtdgliimsvdepviygrnfnlfklkpg
>d1ckp__ 4.117.1.1.1 Cyclin-dependent PK (different isozymes) {Human (Homo sapiens)}
menfqkvekigegtygvvykarnkltgevvalkkirldtetegvpstaireisllkelnh
pnivklldvihtenklylvfeflhqdlkkfmdasaltgiplpliksylfqllqglafchs
hrvlhrdlkpqnllintegaikladfglarafgvpvrtythevvtlwyrapeillgckyy
stavdiwslgcifaemvtrralfpgdseidqlfrifrtlgtpdevvwpgvtsmpdykpsf
pkwarqdfskvvppldedgrsllsqmlhydpnkrisakaalahpffqdvtkpvphlrl
>d1ckqa_ 3.43.1.1.1 Restriction endonuclease EcoRI {Escherichia coli}
sqgvigifgdyakahdlavgevsklvkkalsneypqlsfryrdsikkteinealkkidpd
lggtlfvsnssikpdggivevkddygewrvvlvaeakhqgkdiinirngllvgkrgdqdl
maagnaiershkniseianfmlseshfpyvlflegsnfltenisitrpdgrvvnleynsg
ilnrldrltaanygmpinsnlcinkfvnhkdksimlqaasiytqgdgrewdskimfeimf
disttslrvlgrdlfeqltsk
>d1ckra_ 5.16.1.1.2 DnaK {Rat (Rattus norvegicus)}
senvqdlllldvtplslgietaggvmtvlikrnttiptkqtqtfttysdnqpgvliqvye
geramtkdnnllgkfeltgippaprgvpqievtfdidangilnvsavdkstgkenkitit
ndkgrlskediermvqeaekykaedekqrdkvssknsle
>d1cksa_ 4.76.1.1.2 CksHs2 {Human (Homo sapiens)}
ahkqiyysdkyfdehyeyrhvmlprelskqvpkthlmseeewrrlgvqqslgwvhymihe
pephillfrrplpk
>d1cksb_ 4.76.1.1.2 CksHs2 {Human (Homo sapiens)}
ahkqiyysdkyfdehyeyrhvmlprelskqvpkthlmseeewrrlgvqqslgwvhymihe
pephillfrrplpkdqqk
>d1cksc_ 4.76.1.1.2 CksHs2 {Human (Homo sapiens)}
ahkqiyysdkyfdehyeyrhvmlprelskqvpkthlmseeewrrlgvqqslgwvhymihe
pephillfrrplpkdqqk
>d1ckta_ 1.22.1.1.1 HMG1, domains A and B {Rat/Hamster (Rattus norvegicus/Cricetulus griseus)}
kprgkmssyaffvqtcreehkkkhpdasvnfsefskkcserwktmsakekgkfedmakad
karyeremkty
>d1ckua_ 7.30.1.1.2 HIPIP (high potential iron protein) {Cromatium vinosum}
sapanavaaddataialkynqdatkservaaarpglppeeqhcancqfmqadaagatdew
kgcqlfpgklinvngwcaswtlkag
>d1ckub_ 7.30.1.1.2 HIPIP (high potential iron protein) {Cromatium vinosum}
sapanavaaddataialkynqdatkservaaarpglppeeqhcancqfmqadaagatdew
kgcqlfpgklinvngwcaswtlkag
>d1ckv__ 4.110.1.1.1 Soluble methane monooxygenase regulatory protein B {Escherichia coli}
msvnsnaydagimglkgkdfadqffadenqvvhesdtvvlvlkksdeintfieeilltdy
kknvnptvnvedragywwikangkievdcdeisellgrqfnvydflvdvsstigraytlg
nkftitselmgldrkledyha
>d1cl1a_ 3.57.1.3.1 Cystathionine beta-lyase, CBL {Escherichia coli}
kldtqlvnagrskkytlgavnsviqrasslvfdsveakkhatrnrangelfygrrgtlth
fslqqamceleggagcvlfpcgaaavansilafieqgdhvlmtntayepsqdfcskilsk
lgvttswfdpligadivkhlqpntkivflespgsitmevhdvpaivaavrsvvpdaiimi
dntwaagvlfkaldfgidvsiqaatxylvghsdamigtavcnarcweqlrenaylmgqmv
dadtayitsrglrtlgvrlrqhhesslkvaewlaehpqvarvnhpalpgskghefwkrdf
tgssglfsfvlkkklnneelanyldnfslfsmayswggyeslilanqpehiaairpqgei
dfsgtlirlhigledvddliadldagfariv
>d1cl1b_ 3.57.1.3.1 Cystathionine beta-lyase, CBL {Escherichia coli}
kkldtqlvnagrskkytlgavnsviqrasslvfdsveakkhatrnrangelfygrrgtlt
hfslqqamceleggagcvlfpcgaaavansilafieqgdhvlmtntayepsqdfcskils
klgvttswfdpligadivkhlqpntkivflespgsitmevhdvpaivaavrsvvpdaiim
idntwaagvlfkaldfgidvsiqaatxylvghsdamigtavcnarcweqlrenaylmgqm
vdadtayitsrglrtlgvrlrqhhesslkvaewlaehpqvarvnhpalpgskghefwkrd
ftgssglfsfvlkkklnneelanyldnfslfsmayswggyeslilanqpehiaairpqge
idfsgtlirlhigledvddliadldagfariv
>d1cl2a_ 3.57.1.3.1 Cystathionine beta-lyase, CBL {Escherichia coli}
kldtqlvnagrskkytlgavnsviqrasslvfdsveakkhatrnrangelfygrrgtlth
fslqqamceleggagcvlfpcgaaavansilafieqgdhvlmtntayepsqdfcskilsk
lgvttswfdpligadivkhlqpntkivflespgsitmevhdvpaivaavrsvvpdaiimi
dntwaagvlfkaldfgidvsiqaatkylvghsdamigtavcnarcweqlrenaylmgqmv
dadtayitsrglrtlgvrlrqhhesslkvaewlaehpqvarvnhpalpgskghefwkrdf
tgssglfsfvlkkklnneelanyldnfslfsmayswggyeslilanqpehiaairpqgei
dfsgtlirlhigledvddliadldagfariv
>d1cl2b_ 3.57.1.3.1 Cystathionine beta-lyase, CBL {Escherichia coli}
kkldtqlvnagrskkytlgavnsviqrasslvfdsveakkhatrnrangelfygrrgtlt
hfslqqamceleggagcvlfpcgaaavansilafieqgdhvlmtntayepsqdfcskils
klgvttswfdpligadivkhlqpntkivflespgsitmevhdvpaivaavrsvvpdaiim
idntwaagvlfkaldfgidvsiqaatkylvghsdamigtavcnarcweqlrenaylmgqm
vdadtayitsrglrtlgvrlrqhhesslkvaewlaehpqvarvnhpalpgskghefwkrd
ftgssglfsfvlkkklnneelanyldnfslfsmayswggyeslilanqpehiaairpqge
idfsgtlirlhigledvddliadldagfariv
>d1cl4a_ 7.34.1.1.4 Nucleocapsid protein from mason-pfizer monkey virus (MPMV) {Mason-pfizer monkey virus}
vpglcprckrgkhwanecksktdnqgnpipph
>d1cl5a_ 1.123.1.2.6 Snake phospholipase A2 {Snake (Daboia russelli pulchella)}
sllefgkmileetgklaipsyssygcycgwggkgtpkdatdrccfvhdccygnlpdcnpk
sdrykykrvngaivcekgtscenricecdkaaaicfrqnlntyskkymlypdflckgelk
c
>d1cl5b_ 1.123.1.2.6 Snake phospholipase A2 {Snake (Daboia russelli pulchella)}
sllefgkmileetgklaipsyssygcycgwggkgtpkdatdrccfvhdccygnlpdcnpk
sdrykykrvngaivcekgtscenricecdkaaaicfrqnlntyskkymlypdflckgelk
c
>d1cl8a_ 3.43.1.1.1 Restriction endonuclease EcoRI {Escherichia coli}
sqgvigifgdyakahdlavgevsklvkkalsneypqlsfryrdsikkteinealkkidpd
lggtlfvsnssikpdggivevkddygewrvvlvaeakhqgkdiinirngllvgkrgdqdl
maagnaiershkniseianfmlseshfpyvlflegsnfltenisitrpdgrvvnleynsg
ilnrldrltaanygmpinsnlcinkfvnhkdksimlqaasiytqgdgrewdskimfeimf
disttslrvlgrdlfeqltsk
>d1cla__ 3.35.1.1.1 Chloramphenicol acetyltransferase {Escherichia coli}
mnytkfdvknwvrrehfefyrhrlpcgfsltskidittlkkslddsaykfypvmiyliaq
avnqfdelrmaikddelivwdsvdpqftvfhqetetfsalscpyssdidqfmvnylsvme
ryksdtklfpqgvtpenhlniaalpwvnfdsfnlnvanftdyfapiitmakyqqegdrll
lplsvqvhhavcdgfhvarfinrlqelcnsklk
>d1clb__ 1.42.1.1.1 Calbindin D9K {Bovine (Bos taurus)}
kspeelkgifekyaakegdpnqlskeelklllqtefpsllkggstldelfeeldkngdge
vsfeefqvlvkkisq
>d1clc_1 1.98.1.2.3 (135-575) CelD cellulase {Clostridium thermocellum}
amnvyedafktamlgmyllrcgtsvsatyngihyshgpchtndayldyingqhtkkdstk
gwhdagdynkyvvnagitvgsmflawehfkdqlepvaleipeknnsipdfldelkyeidw
iltmqypdgsgrvahkvstrnfggfimpenehderffvpwssaatadfvamtamaarifr
pydpqyaekcinaakvsyeflknnpanvfanqsgfstgeyatvsdaddrlwaaaemwetl
gdeeylrdfenraaqfskkieadfdwdnvanlgmftyllserpgknpalvqsikdsllst
adsivrtsqnhgygrtlgttyywgcngtvvrqtmilqvankispnndyvnaaldaishvf
grnyynrsyvtglginppmnphdrrsgadgiwepwpgylvgggwpgpkdwvdiqdsyqtn
eiainwnaaliyalagfvnyn
>d1clc_2 2.1.1.5.12 (35-134) CelD cellulase, N-terminal domain {Clostridium thermocellum}
ietkvsaakitenyqfdsrirlnsigfipnhskkatiaancstfyvvkedgtivytgtat
smfdndtketvyiadfssvneegtyylavpgvgksvnfki
>d1clea_ 3.59.1.14.9 Type-B carboxylesterase/lipase {Candida cylindracea, cholesterol esterase}
aptaklangdtitglnaiineaflgipfaeppvgnlrfkdpvpysgslngqkftsygpsc
mqqnpegtfeenlgktaldlvmqskvfqavlpqsedcltinvvrppgtkaganlpvmlwi
fgggfeigsptifppaqmvtksvlmgkpiihvavnyrvaswgflagddikaegsgnaglk
dqrlgmqwvadniagfggdpskvtifgesagsmsvlchliwndgdntykgkplfragimq
sgamvpsdpvdgtygneiydlfvssagcgsasdklaclrsassdtlldatnntpgflays
slrlsylprpdgknitddmyklvrdgkyasvpviigdqndegtvfglsslnvttnaqara
yfkqsfihasdaeidtlmaaypqditqgspfdtgifnaitpqfkrisavlgdlafiharr
yflnhfqggtkysflskqlsglpimgtfhandivwqdyllgsgsviynnafiafatdldp
ntagllvnwpkytsssqsgnnlmminalglytgkdnfrtagydalmtnpssffv
>d1cleb_ 3.59.1.14.9 Type-B carboxylesterase/lipase {Candida cylindracea, cholesterol esterase}
aptaklangdtitglnaiineaflgipfaeppvgnlrfkdpvpysgslngqkftsygpsc
mqqnpegtfeenlgktaldlvmqskvfqavlpqsedcltinvvrppgtkaganlpvmlwi
fgggfeigsptifppaqmvtksvlmgkpiihvavnyrvaswgflagddikaegsgnaglk
dqrlgmqwvadniagfggdpskvtifgesagsmsvlchliwndgdntykgkplfragimq
sgamvpsdpvdgtygneiydlfvssagcgsasdklaclrsassdtlldatnntpgflays
slrlsylprpdgknitddmyklvrdgkyasvpviigdqndegtvfglsslnvttnaqara
yfkqsfihasdaeidtlmaaypqditqgspfdtgifnaitpqfkrisavlgdlafiharr
yflnhfqggtkysflskqlsglpimgtfhandivwqdyllgsgsviynnafiafatdldp
ntagllvnwpkytsssqsgnnlmminalglytgkdnfrtagydalmtnpssffv
>d1clf__ 4.47.1.1.4 Ferredoxin II {Closridium pasteurianum}
aykiadscvscgacasecpvnaisqgdsifvidadtcidcgncanvcpvgapvqe
>d1clh__ 2.55.1.1.5 Bacterial cyclophilin {Escherichia coli}
akgdphvllttsagnieleldkqkapvsvqnfvdyvnsgfynnttfhrvipgfmiqgggf
teqmqqkkpnppikneadnglrntrgtiamartadkdsatsqffinvadnafldhgqrdf
gyavfgkvvkgmdvadkisqvpthdvgpyqnvpskpvvilsakvlp
>d1clia1 4.59.4.1.1 (5-170) Aminoimidazole ribonucleotide synthetase (PurM) N-terminal domain {(Escherichia coli) |A,B,C,D|}
tslsykdagvdidagnalvgrikgvvkktrrpevmgglggfgalcalpqkyrepvlvsgt
dgvgtklrlamdlkrhdtigidlvamcvndlvvqgaeplffldyyatgkldvdtasavis
giaegclqsgcslvggetaempgmyhgedydvagfcvgvvekseii
>d1clia2 4.112.1.1.1 (171-345) Aminoimidazole ribonucleotide synthetase (PurM) C-terminal domain {(Escherichia coli) |A,B,C,D|}
dgskvsdgdvlialgssgphsngyslvrkilevsgcdpqtteldgkpladhllaptriyv
ksvleliekvdvhaiahltgggfweniprvlpdntqavidesswqwpevfnwlqtagnve
hhemyrtfncgvgmiialpapevdkalallnangenawkigiikasdseqrvvie
>d1clib1 4.59.4.1.1 (1021-1170) Aminoimidazole ribonucleotide synthetase (PurM) N-terminal domain {(Escherichia coli) |A,B,C,D|}
alvgrikgvvkktrrpevmgglggfgalcalpqkyrepvlvsgtdgvgtklrlamdlkrh
dtigidlvamcvndlvvqgaeplffldyyatgkldvdtasavisgiaegclqsgcslvgg
etaempgmyhgedydvagfcvgvvekseii
>d1clib2 4.112.1.1.1 (1171-1345) Aminoimidazole ribonucleotide synthetase (PurM) C-terminal domain {(Escherichia coli) |A,B,C,D|}
dgskvsdgdvlialgssgphsngyslvrkilevsgcdpqtteldgkpladhllaptriyv
ksvleliekvdvhaiahltgggfweniprvlpdntqavidesswqwpevfnwlqtagnve
hhemyrtfncgvgmiialpapevdkalallnangenawkigiikasdseqrvvie
>d1clic1 4.59.4.1.1 (2005-2170) Aminoimidazole ribonucleotide synthetase (PurM) N-terminal domain {(Escherichia coli) |A,B,C,D|}
tslsykdagvdidagnalvgrikgvvkktrrpevmgglggfgalcalpqkyrepvlvsgt
dgvgtklrlamdlkrhdtigidlvamcvndlvvqgaeplffldyyatgkldvdtasavis
giaegclqsgcslvggetaempgmyhgedydvagfcvgvvekseii
>d1clic2 4.112.1.1.1 (2171-2345) Aminoimidazole ribonucleotide synthetase (PurM) C-terminal domain {(Escherichia coli) |A,B,C,D|}
dgskvsdgdvlialgssgphsngyslvrkilevsgcdpqtteldgkpladhllaptriyv
ksvleliekvdvhaiahltgggfweniprvlpdntqavidesswqwpevfnwlqtagnve
hhemyrtfncgvgmiialpapevdkalallnangenawkigiikasdseqrvvie
>d1clid1 4.59.4.1.1 (3021-3170) Aminoimidazole ribonucleotide synthetase (PurM) N-terminal domain {(Escherichia coli) |A,B,C,D|}
alvgrikgvvkktrrpevmgglggfgalcalpqkyrepvlvsgtdgvgtklrlamdlkrh
dtigidlvamcvndlvvqgaeplffldyyatgkldvdtasavisgiaegclqsgcslvgg
etaempgmyhgedydvagfcvgvvekseii
>d1clid2 4.112.1.1.1 (3171-3345) Aminoimidazole ribonucleotide synthetase (PurM) C-terminal domain {(Escherichia coli) |A,B,C,D|}
dgskvsdgdvlialgssgphsngyslvrkilevsgcdpqtteldgkpladhllaptriyv
ksvleliekvdvhaiahltgggfweniprvlpdntqavidesswqwpevfnwlqtagnve
hhemyrtfncgvgmiialpapevdkalallnangenawkigiikasdseqrvvie
>d1cll__ 1.42.1.5.7 Calmodulin {Human (Homo sapiens)}
lteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngti
dfpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevde
mireadidgdgqvnyeefvqmmta
>d1clm__ 1.42.1.5.13 Calmodulin {Paramecium tetraurelia}
lteeqiaefkeafalfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngti
dfpeflslmarkmkeqdseeelieafkvfdrdgnglisaaelrhvmtnlgekltddevde
mireadidgdghinyeefvrmmvs
>d1cloh1 2.1.1.1.79 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab A5B7 (mouse), kappa L chain}
evklvesggglvqpggslrlscatsgftftdyymnwvrqppgkalewlgfignkangytt
eysasvkgrftisrdksqsilylqmntlraedsatyyctrdrglrfyfdywgqgttltvs
s
>d1cloh2 2.1.1.2.83 (114-214) Immunoglobulin (constant domains of L and H chains) {Fab A5B7 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpssprpsetvtcnvahpasstkvdkkivprd
>d1clol1 2.1.1.1.79 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab A5B7 (mouse), kappa L chain}
qtvlsqspailsaspgekvtmtcrasssvtyihwyqqkpgsspkswiyatsnlasgvpar
fsgsgsgtsysltisrveaedaatyycqhwsskpptfgggtkleik
>d1clol2 2.1.1.2.83 (108-214) Immunoglobulin (constant domains of L and H chains) {Fab A5B7 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1clpa_ 1.123.1.2.15 Myotoxin II {Terciopelo (Bothrops asper)}
slfelgkmilqetgknpaksygaygcncgvlgrgkpkdatdrccyvhkccykkltgcnpk
kdrysyswkdktivcgennsclkelcecdkavaiclrenlntynkkyryylkplckkada
c
>d1clpb_ 1.123.1.2.15 Myotoxin II {Terciopelo (Bothrops asper)}
slfelgkmilqetgknpaksygaygcncgvlgrgkpkdatdrccyvhkccykkltgcnpk
kdrysyswkdktivcgennsclkelcecdkavaiclrenlntynkkyryylkplckkada
c
>d1clsa_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1clsb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1clsc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1clsd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1clua_ 3.30.1.6.1 cH-p21 Ras protein {Human (Homo sapiens)}
mteyklvvvgapgvgksaltiqliqnhfvdeydptiedsyrkqvvidgetclldildtag
qeeysamrdqymrtgegflcvfainntksfedihqyreqikrvkdsddvpmvlvgnkcdl
aartvesrqaqdlarsygipyietsaktrqgvedafytlvreirqh
>d1clxa_ 3.1.7.3.16 Xylanase A, catalytic core {Pseudomonas fluorescens}
glasladfpigvavaasggnadiftssarqnivraefnqitaenimkmsymysgsnfsft
nsdrlvswaaqngqtvhghalvwhpsyqlpnwasdsnanfrqdfarhidtvaahfagqvk
swdvvnealfdsaddpdgrgsangyrqsvfyrqfggpeyideafrraraadptaelyynd
fnteengakttalvnlvqrllnngvpidgvgfqmhvmndypsianirqamqkivalsptl
kikiteldvrlnnpydgnssndytnrndcavscagldrqkarykeivqaylevvppgrrg
gitvwgiadpdswlythqnlpdwpllfndnlqpkpayqgvveals
>d1clxb_ 3.1.7.3.16 Xylanase A, catalytic core {Pseudomonas fluorescens}
glasladfpigvavaasggnadiftssarqnivraefnqitaenimkmsymysgsnfsft
nsdrlvswaaqngqtvhghalvwhpsyqlpnwasdsnanfrqdfarhidtvaahfagqvk
swdvvnealfdsaddpdgrgsangyrqsvfyrqfggpeyideafrraraadptaelyynd
fnteengakttalvnlvqrllnngvpidgvgfqmhvmndypsianirqamqkivalsptl
kikiteldvrlnnpydgnssndytnrndcavscagldrqkarykeivqaylevvppgrrg
gitvwgiadpdswlythqnlpdwpllfndnlqpkpayqgvveals
>d1clxc_ 3.1.7.3.16 Xylanase A, catalytic core {Pseudomonas fluorescens}
glasladfpigvavaasggnadiftssarqnivraefnqitaenimkmsymysgsnfsft
nsdrlvswaaqngqtvhghalvwhpsyqlpnwasdsnanfrqdfarhidtvaahfagqvk
swdvvnealfdsaddpdgrgsangyrqsvfyrqfggpeyideafrraraadptaelyynd
fnteengakttalvnlvqrllnngvpidgvgfqmhvmndypsianirqamqkivalsptl
kikiteldvrlnnpydgnssndytnrndcavscagldrqkarykeivqaylevvppgrrg
gitvwgiadpdswlythqnlpdwpllfndnlqpkpayqgvveals
>d1clxd_ 3.1.7.3.16 Xylanase A, catalytic core {Pseudomonas fluorescens}
glasladfpigvavaasggnadiftssarqnivraefnqitaenimkmsymysgsnfsft
nsdrlvswaaqngqtvhghalvwhpsyqlpnwasdsnanfrqdfarhidtvaahfagqvk
swdvvnealfdsaddpdgrgsangyrqsvfyrqfggpeyideafrraraadptaelyynd
fnteengakttalvnlvqrllnngvpidgvgfqmhvmndypsianirqamqkivalsptl
kikiteldvrlnnpydgnssndytnrndcavscagldrqkarykeivqaylevvppgrrg
gitvwgiadpdswlythqnlpdwpllfndnlqpkpayqgvveals
>d1clyh1 2.1.1.1.72 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab CBR96 (mouse/human), kappa L chain}
evnlvesggglvqpggslkvscvtsgftfsdyymywvrqtpekrlewvayisqggditdy
pdtvkgrftisrdnaknslylqmsrlksedtamyycarglddgawfaywgqgtlvtvsv
>d1clyh2 2.1.1.2.77 (114-227) Immunoglobulin (constant domains of L and H chains) {Fab CBR96 (mouse/human), kappa L chain}
astkgpsvfplapsskstsggtaalgclvkdyfpqpvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkrvep
>d1clyl1 2.1.1.1.72 (3-108) Immunoglobulin (variable domains of L and H chains) {Fab CBR96 (mouse/human), kappa L chain}
lmtqipvslpvslgdqasiscrssqiivhnngntylewylqkpgqspqlliykvsnrfsg
vpdrfsgsgsgtdftlkisrveaedlgvyycfqgshvpftfgsgtkleikr
>d1clyl2 2.1.1.2.77 (109-214) Immunoglobulin (constant domains of L and H chains) {Fab CBR96 (mouse/human), kappa L chain}
tvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqds
kdstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1clzh1 2.1.1.1.73 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab MBR96 (mouse), kappa L chain}
evnlvesggglvqpggslkvscvtsgftfsdyymywvrqtpekrlewvayisqggditdy
pdtvkgrftisrdnaknslylqmsrlksedtamyycarglddgawfaywgqgtlvtvsv
>d1clzh2 2.1.1.2.78 (115-231) Immunoglobulin (constant domains of L and H chains) {Fab MBR96 (mouse), kappa L chain}
tttapsvyplvpgcsdtsgssvtlgclvkgyfpepvtvkwnygalssgvrtvssvlqsgf
yslsslvtvpsstwpsqtvicnvahpasktelikriepr
>d1clzl1 2.1.1.1.73 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab MBR96 (mouse), kappa L chain}
dvlmtqipvslpvslgdqasiscrssqiivhnngntylewylqkpgqspqlliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyycfqgshvpftfgsgtkleikr
>d1clzl2 2.1.1.2.78 (109-214) Immunoglobulin (constant domains of L and H chains) {Fab MBR96 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1cm0a_ 4.84.1.1.3 Histone acetyltransferase domain of P300/CBP associating factor, PCAF {Human (Homo sapiens)}
kviefhvvgnslnqkpnkkilmwlvglqnvfshqlprmpkeyitrlvfdpkhktlalikd
grviggicfrmfpsqgfteivfcavtsneqvkgygthlmnhlkeyhikhdilnfltyade
yaigyfkkqgfskeikipktkyvgyikdyegatlmgcelnpri
>d1cm0b_ 4.84.1.1.3 Histone acetyltransferase domain of P300/CBP associating factor, PCAF {Human (Homo sapiens)}
kviefhvvgnslnqkpnkkilmwlvglqnvfshqlprmpkeyitrlvfdpkhktlalikd
grviggicfrmfpsqgfteivfcavtsneqvkgygthlmnhlkeyhikhdilnfltyade
yaigyfkkqgfskeikipktkyvgyikdyegatlmgcelnpr
>d1cm1a_ 1.42.1.5.8 Calmodulin {Bovine (Bos taurus)}
lteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngti
dfpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevde
mireadidgdgqvnyeefvqmmt
>d1cm4a_ 1.42.1.5.8 Calmodulin {Bovine (Bos taurus)}
lteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngti
dfpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevde
mireadidgdgqvnyeefvqmmt
>d1cm4c_ 1.42.1.5.8 Calmodulin {Bovine (Bos taurus)}
lteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngti
dfpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevde
mireadidgdgqvnyeefvqmmt
>d1cm4e_ 1.42.1.5.8 Calmodulin {Bovine (Bos taurus)}
lteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngti
dfpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevde
mireadidgdgqvnyeefvqmmt
>d1cm4g_ 1.42.1.5.8 Calmodulin {Bovine (Bos taurus)}
lteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngti
dfpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevde
mireadidgdgqvnyeefvqmmt
>d1cm7a_ 3.65.1.1.6 3-isopropylmalate dehydrogenase, IPMDH {Escherichia coli}
msknyhiavlpgdgigpevmtqalkvldavrnrfamrittshydvggaaidnhgqplppa
tvegceqadavlfgsvggpkwehlppdqqpergallplrkhfklfsnlrpaklyqgleaf
cplradiaangfdilcvreltggiyfgqpkgregsgqyekafdtevyhrfeieriariaf
esarkrrhkvtsidkanvlqssilwreivneiateypdvelahmyidnatmqlikdpsqf
dvllcsnlfgdilsdecamitgsmgmlpsaslneqgfglyepaggsapdiagknianpia
qilslalllrysldaddaacaierainraleegirtgdlargaaavstdemgdiiaryva
egv
>d1cm7b_ 3.65.1.1.6 3-isopropylmalate dehydrogenase, IPMDH {Escherichia coli}
msknyhiavlpgdgigpevmtqalkvldavrnrfamrittshydvggaaidnhgqplppa
tvegceqadavlfgsvggpkwehlppdqqpergallplrkhfklfsnlrpaklyqgleaf
cplradiaangfdilcvreltggiyfgqpkgregsgqyekafdtevyhrfeieriariaf
esarkrrhkvtsidkanvlqssilwreivneiateypdvelahmyidnatmqlikdpsqf
dvllcsnlfgdilsdecamitgsmgmlpsaslneqgfglyepaggsapdiagknianpia
qilslalllrysldaddaacaierainraleegirtgdlargaaavstdemgdiiaryva
egv
>d1cm9a_ 4.8.1.1.8 Macrophage inflammatory protein, MIP {Kaposi's sarcoma herpes virus-8}
swhrpdkcclgyqkrplpqvllsswyptsqlcskpgvifltkrgrqvcadkskdwvkklx
qqlpvtar
>d1cm9b_ 4.8.1.1.8 Macrophage inflammatory protein, MIP {Kaposi's sarcoma herpes virus-8}
whrpdkcclgyqkrplpqvllsswyptsqlcskpgvifltkrgrqvcadkskdwvkklxq
qlpvtar
>d1cmaa_ 1.46.1.2.1 Met repressor {Escherichia coli}
aewsgeyispyaehgkkseqvkkitvsiplkvlkiltdertrrqvnnlrhatnsellcea
flhaftgqplpddadlrkersdeipeaakeimremginpetwey
>d1cmab_ 1.46.1.2.1 Met repressor {Escherichia coli}
aewsgeyispyaehgkkseqvkkitvsiplkvlkiltdertrrqvnnlrhatnsellcea
flhaftgqplpddadlrkersdeipeaakeimremginpetwey
>d1cmba_ 1.46.1.2.1 Met repressor {Escherichia coli}
aewsgeyispyaehgkkseqvkkitvsiplkvlkiltdertrrqvnnlrhatnsellcea
flhaftgqplpddadlrkersdeipeaakeimremginpetwey
>d1cmbb_ 1.46.1.2.1 Met repressor {Escherichia coli}
aewsgeyispyaehgkkseqvkkitvsiplkvlkiltdertrrqvnnlrhatnsellcea
flhaftgqplpddadlrkersdeipeaakeimremginpetwey
>d1cmca_ 1.46.1.2.1 Met repressor {Escherichia coli}
aewsgeyispyaehgkkseqvkkitvsiplkvlkiltdertrrqvnnlrhatnsellcea
flhaftgqplpddadlrkersdeipeaakeimremginpetwey
>d1cmcb_ 1.46.1.2.1 Met repressor {Escherichia coli}
aewsgeyispyaehgkkseqvkkitvsiplkvlkiltdertrrqvnnlrhatnsellcea
flhaftgqplpddadlrkersdeipeaakeimremginpetwey
>d1cmf__ 1.42.1.5.8 Calmodulin {Bovine (Bos taurus)}
mkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevdemireadidgdgq
vnyeefvqmmtak
>d1cmg__ 1.42.1.5.8 Calmodulin {Bovine (Bos taurus)}
mkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevdemireadidgdgq
vnyeefvqmmtak
>d1cmke_ 4.117.1.1.3 cAMP-dependent PK, catalytic subunit {Pig (Sus scrofa)}
gnaaaakkgseqesvkeflakakedflkkwenpaqntahldqferiktlgtgsfgrvmlv
khketgnhfamkildkqkvvklkqiehtlnekrilqavnfpflvkleysfkdnsnlymvm
eyvpggemfshlrrigrfsepharfyaaqivltfeylhsldliyrdlkpenllidqqgyi
qvtdfgfakrvkgrtwtlcgtpeylapeiilskgynkavdwwalgvliyemaagyppffa
dqpiqiyekivsgkvrfpshfssdlkdllrnllqvdltkrfgnlkdgvndiknhkwfatt
dwiaiyqrkveapfipkfkgpgdtsnfddyeeeeirvsinekcgkefsef
>d1cmla_ 3.85.1.2.1 Chalcone synthase {Alfalfa (Medicago sativa)}
mvsvseirkaqraegpatilaigtanpancveqstypdfyfkitnsehktelkekfqrmc
dksmikrrymylteeilkenpnvceymapsldarqdmvvvevprlgkeaavkaikewgqp
kskithlivcttsgvdmpgadyqltkllglrpyvkrymmyqqgafaggtvlrlakdlaen
nkgarvlvvcsevtavtfrgpsdthldslvgqalfgdgaaalivgsdpvpeiekpifemv
wtaqtiapdsegaidghlreagltfhllkdvpgivsknitkalveafeplgisdynsifw
iahpggpaildqveqklalkpekmnatrevlseygnmssacvlfildemrkkstqnglkt
tgeglewgvlfgfgpgltietvvlrsvai
>d1cmp__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1cmq__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1cmr__ 7.3.7.2.7 Charybdotoxin {Scorpion (Leiurus quinquestriatus hebraeus)}
cttskecwsvcqrlhntskgwcdhrgcices
>d1cms__ 2.44.1.2.15 Chymosin (synonim: renin) {Bovine (Bos taurus)}
gevasvpltnyldsqyfgkiylgtppqeftvlfdtgssdfwvpsiycksnacknhqrfdp
rksstfqnlgkplsihygtgsmqgilgydtvtvsnivdiqqtvglstqepgdvftyaefd
gilgmaypslaseysipvfdnmmnrhlvaqdlfsvymdrngqesmltlgaidpsyytgsl
hwvpvtvqqywqftvdsvtisgvvvaceggcqaildtgtsklvgpssdilniqqaigatq
nqygefdidcdnlsymptvvfeingkmypltpsaytsqdqgfctsgfqsenhsqkwilgd
vfireyysvfdrannlvglakai
>d1cmt__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1cmu__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptnysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1cmva_ 2.51.1.1.1 Human cytomegalovirus protease {Human cytomegalovirus, hCMV}
apvyvggflarydqspdeaelllprdvvehwlhaqgqgqpslsvalplninhddtavvgh
vaamqsvrdglfclgcvtsprfleivrrasekselvsrgpvsplqpdkvveflsgsyagl
slssrrcddaeaptslsgsettpfkhvalcsvgrrrgtlavygrdpewvtqrfpdltaad
rdglraqwqrcgstavdasgdpfrsdsygllgnsvdalyirerlpklrydkqlvgvtere
syvka
>d1cmvb_ 2.51.1.1.1 Human cytomegalovirus protease {Human cytomegalovirus, hCMV}
vapvyvggflarydqspdeaelllprdvvehwlhaqgqgqpslsvalplninhddtavvg
hvaamqsvrdglfclgcvtsprfleivrrasekselvsrgpvsplqpdkvveflsgsyag
lslssrrcddaeaptslsgsettpfkhvalcsvgrrrgtlavygrdpewvtqrfpdltaa
drdglraqwqrcgstavdasgdpfrsdsygllgnsvdalyirerlpklrydkqlvgvter
esyvka
>d1cmxa_ 4.3.1.3.2 Ubiquitin C-terminal hydrolase UCH-l3 {Synthetic, based on Saccharomyces cerevisiae sequence}
ravvpiesnpevftnfahklglknewayfdiysltepellaflprpvkaivllfpinedr
ksstsqqitssydviwfkqsvknacglyailhslsnnqsllepgsdldnflksqsdtsss
knrfddvttdqfvlnvikenvqtfstgqseapeatadtnlhyityveenggifeldgrnl
sgplylgksdptatdlieqelvrvrvasymenaneedvlnfamlglgpn
>d1cmxb_ 4.13.2.1.2 Ubiquitin {Synthetic, based on Saccharomyces cerevisiae sequence}
mqifvktltgktitlevepsdtienvkakiqdkegippdqqrlifagkqledgrtlsdyn
iqkestlhlvlrlrg
>d1cmxc_ 4.3.1.3.2 Ubiquitin C-terminal hydrolase UCH-l3 {Synthetic, based on Saccharomyces cerevisiae sequence}
avvpiesnpevftnfahklglknewayfdiysltepellaflprpvkaivllfpinedrk
sstsqqitssydviwfkqsvknacglyailhslsnnqsllepgsdldnflksqsdtsssk
nrfddvttdqfvlnvikenvqtfstgqseapeatadtnlhyityveenggifeldgrnls
gplylgksdptatdlieqelvrvrvasymenaneedvlnfamlglgpn
>d1cmya_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1cmyb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvypenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1cmyc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1cmyd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvypenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1cn1a_ 2.26.1.1.1 Concanavalin A {Jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqdgkvgtahiiynsvdkr
lsavvsypnadatsvsydvdlndvlpewvrvglsastglyketntilswsftsklksnst
hqtdalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspegssvgralfyapvh
iwessaatvsfeatfaflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1cn1b_ 2.26.1.1.1 Concanavalin A {Jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqdgkvgtahiiynsvdkr
lsavvsypnadatsvsydvdlndvlpewvrvglsastglyketntilswsftsklksnst
hqtdalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspegssvgralfyapvh
iwessaatvsfeatfaflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1cn2__ 7.3.7.1.6 Scorpion toxin {Mexican scorpion (Centruroides noxius hoffmann), toxin II}
kegylvdkntgckyeclklgdndyclreckqqygkgaggycyafacwcthlyeqaivwpl
pnkrcs
>d1cn3a_ 2.9.1.4.1 Murine polyomavirus coat protein vp1 {Murine polyoma virus, strain small-plaque 16}
mevldlvtgpdsvteieaflnprmgqpptpeslteggqyygwsrginlatsdtedspgnn
tlptwsmaklqlpmlnedltcdtlqmweavsvktevvgsgslldvhgfnkptdtvntkgi
stpvegsqyhvfavggepldlqglvtdartkykeegvvtiktitkkdmvnkdqvlnpisk
akldkdgmypveiwhpdpaknentryfgnytggtttppvlqftntlttvlldengvgplc
kgeglylscvdimgwrvtrnydvhhwrglpryfkitlrkrwvk
>d1cn3b_ 2.9.1.4.1 Murine polyomavirus coat protein vp1 {Murine polyoma virus, strain small-plaque 16}
mevldlvtgpdsvteieaflnprmgqpptpeslteggqyygwsrginlatsdtedspgnn
tlptwsmaklqlpmlnedltcdtlqmweavsvktevvgsgslldvhgfnkptdtvntkgi
stpvegsqyhvfavggepldlqglvtdartkykeegvvtiktitkkdmvnkdqvlnpisk
akldkdgmypveiwhpdpaknentryfgnytggtttppvlqftntlttvlldengvgplc
kgeglylscvdimgwrvtrnydvhhwrglpryfkitlrkrwvk
>d1cn3c_ 2.9.1.4.1 Murine polyomavirus coat protein vp1 {Murine polyoma virus, strain small-plaque 16}
mevldlvtgpdsvteieaflnprmgqpptpeslteggqyygwsrginlatsdtedspgnn
tlptwsmaklqlpmlnedltcdtlqmweavsvktevvgsgslldvhgfnkptdtvntkgi
stpvegsqyhvfavggepldlqglvtdartkykeegvvtiktitkkdmvnkdqvlnpisk
akldkdgmypveiwhpdpaknentryfgnytggtttppvlqftntlttvlldengvgplc
kgeglylscvdimgwrvtrnydvhhwrglpryfkitlrkrwvk
>d1cn3d_ 2.9.1.4.1 Murine polyomavirus coat protein vp1 {Murine polyoma virus, strain small-plaque 16}
mevldlvtgpdsvteieaflnprmgqpptpeslteggqyygwsrginlatsdtedspgnn
tlptwsmaklqlpmlnedltcdtlqmweavsvktevvgsgslldvhgfnkptdtvntkgi
stpvegsqyhvfavggepldlqglvtdartkykeegvvtiktitkkdmvnkdqvlnpisk
akldkdgmypveiwhpdpaknentryfgnytggtttppvlqftntlttvlldengvgplc
kgeglylscvdimgwrvtrnydvhhwrglpryfkitlrkrwvk
>d1cn3e_ 2.9.1.4.1 Murine polyomavirus coat protein vp1 {Murine polyoma virus, strain small-plaque 16}
mevldlvtgpdsvteieaflnprmgqpptpeslteggqyygwsrginlatsdtedspgnn
tlptwsmaklqlpmlnedltcdtlqmweavsvktevvgsgslldvhgfnkptdtvntkgi
stpvegsqyhvfavggepldlqglvtdartkykeegvvtiktitkkdmvnkdqvlnpisk
akldkdgmypveiwhpdpaknentryfgnytggtttppvlqftntlttvlldengvgplc
kgeglylscvdimgwrvtrnydvhhwrglpryfkitlrkrwvk
>d1cn4a1 2.1.2.1.9 (7-116) Erythropoietin (EPO) receptor {Human (Homo sapiens)}
pdpkfeskaallaargpeellcfterledlvcfweeaasagvgpgqysfsyqledepwkl
crlhqaptargavrfwcslptadtssfvplelrvtaasgapryhrvihin
>d1cn4a2 2.1.2.1.9 (117-223) Erythropoietin (EPO) receptor {Human (Homo sapiens)}
evvlldapvglvarladesghvvlrwlpppetpmtshiryevdvsagqgagsvqrveile
grtecvlsnlrgrtrytfavrarmaepsfggfwsewsepvslltpsd
>d1cn4b1 2.1.2.1.9 (8-116) Erythropoietin (EPO) receptor {Human (Homo sapiens)}
dpkfeskaallaargpeellcfterledlvcfweeaasagvgpgqysfsyqledepwklc
rlhqaptargavrfwcslptadtssfvplelrvtaasgapryhrvihin
>d1cn4b2 2.1.2.1.9 (117-225) Erythropoietin (EPO) receptor {Human (Homo sapiens)}
evvlldapvglvarladesghvvlrwlpppetpmtshiryevdvsagqgagsvqrveile
grtecvlsnlrgrtrytfavrarmaepsfggfwsewsepvslltpsdld
>d1cn4c_ 1.27.1.2.1 Erythropoietin {Human (Homo sapiens)}
pprlicdsrvlerylleakeaekittgcaehcslnekitvpdtkvnfyawkrmevgqqav
evwqglallseavlrgqallvkssqpweplqlhvdkavsglrslttllralgaqkeaisp
pdaasaaplrtitadtfrklfrvysnflrgklklytgeacr
>d1cn7a_ 4.59.3.1.1 Eukaryotic ribosomal protein L30 (eL30) {Baker's yeast (Saccharomyces cerevisiae)}
apvksqesinqklalviksgkytlgykstvkslrqgkskliiiaantpvlrkseleyyam
lsktkvyyfqggnnelgtavgklfrvgvvsileagdsdilttla
>d1cnb__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfcfhwgsldgqgsehtvdkkkyaaelhlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1cnc__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfcfhwgsldgqgsehtvdkkkyaaelhlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1cne_1 2.38.1.1.7 (11-124) Nitrate reductase core domain {Corn (Zea mays)}
grihcrlvakkelsrdvrlfrfslpspdqvlglpigkhifvcatiegklcmraytptsmv
deighfdllvkvyfknehpkfpngglmtqyldslpvgsyidvkgplghveytgr
>d1cne_2 3.18.1.1.7 (125-270) Nitrate reductase {Corn (Zea mays)}
gsfvingkqrnarrlamicggsgitpmyqiiqavlrdqpedhtemhlvyanrteddillr
deldrwaaeypdrlkvwyvidqvkrpeegwkysvgfvteavlrehvpeggddtlalasgp
ppmiqfaispnlekmkydmansfvvf
>d1cnf_1 2.38.1.1.7 (11-124) Nitrate reductase core domain {Corn (Zea mays)}
grihcrlvakkelsrdvrlfrfslpspdqvlglpigkhifvcatiegklcmraytptsmv
deighfdllvkvyfknehpkfpngglmtqyldslpvgsyidvkgplghveytgr
>d1cnf_2 3.18.1.1.7 (125-270) Nitrate reductase {Corn (Zea mays)}
gsfvingkqrnarrlamicggsgitpmyqiiqavlrdqpedhtemhlvyanrteddillr
deldrwaaeypdrlkvwyvidqvkrpeegwkysvgfvteavlrehvpeggddtlalacgp
ppmiqfaispnlekmkydmansfvvf
>d1cng__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaalhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasfk
>d1cnh__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliefhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasfk
>d1cni__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliafhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasfk
>d1cnj__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrlinfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasfk
>d1cnk__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrlilfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasfk
>d1cnma_ 3.33.1.1.12 Proteinase K {Fungus (Tritirachium album), strain limber}
aaqtnapwglarisstspgtstyyydesagqgscvyvidtgieashpefegraqmvktyy
yssrdgnghgthcagtvgsrtygvakktqlfgvkvlddngsgqystiiagmdfvasdknn
rncpkgvvaslslgggysssvnsaaarlqssgvmvavaagnnnadarnyspasepsvctv
gasdrydrrssfsnygsvldifgpgtsilstwiggstrsisgtsmatphvaglaaylmtl
gkttaasacryiadtankgdlsnipfgtvnllaynnyqa
>d1cnoa_ 1.3.1.1.6 Cytochrome c552 {Pseudomonas nautica}
agdieagkakaavcaachgqngisqvpiypnlagqkeqylvaalkaykagqrqggqapvm
qgqatalsdadianlaayyasnpaaa
>d1cnob_ 1.3.1.1.6 Cytochrome c552 {Pseudomonas nautica}
agdieagkakaavcaachgqngisqvpiypnlagqkeqylvaalkaykagqrqggqapvm
qgqatalsdadianlaayyasnpaaa
>d1cnoc_ 1.3.1.1.6 Cytochrome c552 {Pseudomonas nautica}
agdieagkakaavcaachgqngisqvpiypnlagqkeqylvaalkaykagqrqggqapvm
qgqatalsdadianlaayyasnpaaa
>d1cnod_ 1.3.1.1.6 Cytochrome c552 {Pseudomonas nautica}
agdieagkakaavcaachgqngisqvpiypnlagqkeqylvaalkaykagqrqggqapvm
qgqatalsdadianlaayyasnpaaa
>d1cnoe_ 1.3.1.1.6 Cytochrome c552 {Pseudomonas nautica}
agdieagkakaavcaachgqngisqvpiypnlagqkeqylvaalkaykagqrqggqapvm
qgqatalsdadianlaayyasnpaaa
>d1cnof_ 1.3.1.1.6 Cytochrome c552 {Pseudomonas nautica}
agdieagkakaavcaachgqngisqvpiypnlagqkeqylvaalkaykagqrqggqapvm
qgqatalsdadianlaayyasnpaaa
>d1cnog_ 1.3.1.1.6 Cytochrome c552 {Pseudomonas nautica}
agdieagkakaavcaachgqngisqvpiypnlagqkeqylvaalkaykagqrqggqapvm
qgqatalsdadianlaayyasnpaaaa
>d1cnoh_ 1.3.1.1.6 Cytochrome c552 {Pseudomonas nautica}
agdieagkakaavcaachgqngisqvpiypnlagqkeqylvaalkaykagqrqggqapvm
qgqatalsdadianlaayyasnpaaa
>d1cnpa_ 1.42.1.2.1 Calcyclin (S100) {Rabbit (Oryctolagus cuniculus)}
maspldqaiglligifhkysgkegdkhtlskkelkeliqkeltigsklqdaeivklmddl
drnkdqevnfqeyitflgalamiynealkg
>d1cnpb_ 1.42.1.2.1 Calcyclin (S100) {Rabbit (Oryctolagus cuniculus)}
maspldqaiglligifhkysgkegdkhtlskkelkeliqkeltigsklqdaeivklmddl
drnkdqevnfqeyitflgalamiynealkg
>d1cnqa_ 5.7.1.1.1 Fructose-1,6-bisphosphatase {Pig (Sus scrofa)}
fdtnivtltrfvmeegrkargtgemtqllnslctavkaistavrkagiahlygiagstnv
tgdqvkkldvlsndlvinvlkssfatcvlvseedknaiivepekrgkyvvcfdpldgssn
idclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfm
ldpaigefilvdrdvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryv
gsmvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldi
vptdihqrapiilgspedvtelleiyqkhaak
>d1cnr__ 7.13.1.1.1 Crambin {Abyssinian cabbage (Crambe abyssinica)}
ttccpsivarsnfnvcrlpgtpealcatytgciiipgatcpgdyan
>d1cnsa_ 4.2.1.1.1 Barley endochitinase {Pearled barley (Hordeum vulgare)}
svssivsraqfdrmllhrndgacqakgfytydafvaaaaafsgfgttgsadvqkrevaaf
laqtshettggwatapdgafawgycfkqergassdyctpsaqwpcapgkryygrgpiqls
hnynygpagraigvdllanpdlvatdatvsfktamwfwmtaqppkpsshavivgqwspsg
adraagrvpgfgvitniinggiecghgqdsrvadrigfykrycdilgvgygnnldcysqr
pfa
>d1cnsb_ 4.2.1.1.1 Barley endochitinase {Pearled barley (Hordeum vulgare)}
svssivsraqfdrmllhrndgacqakgfytydafvaaaaafsgfgttgsadvqkrevaaf
laqtshettggwatapdgafawgycfkqergassdyctpsaqwpcapgkryygrgpiqls
hnynygpagraigvdllanpdlvatdatvsfktamwfwmtaqppkpsshavivgqwspsg
adraagrvpgfgvitniinggiecghgqdsrvadrigfykrycdilgvgygnnldcysqr
pfa
>d1cnt1_ 1.27.1.1.7 Ciliary neurotrophic factor (CNTF) {Human (Homo sapiens)}
phrrdlcsrsiwlarkirsdltaltesyvkhqglnkninldsadgmpvastdqwseltea
erlqenlqayrtfhvllarlledqqvhftptegdfhqaihtlllqvaafayqieelmill
eykiprneadgmpinvgdgglfekklwglkvlqelsqwtvrsihdlrfisshqtgip
>d1cnt2_ 1.27.1.1.7 Ciliary neurotrophic factor (CNTF) {Human (Homo sapiens)}
hrrdlcsrsiwlarkirsdltaltesyvkhqglnkninldsadgmpvastdqwselteae
rlqenlqayrtfhvllarlledqqvhftptegdfhqaihtlllqvaafayqieelmille
ykiprneadgmpinvgdgglfekklwglkvlqelsqwtvrsihdlrfisshqtgip
>d1cnt3_ 1.27.1.1.7 Ciliary neurotrophic factor (CNTF) {Human (Homo sapiens)}
phrrdlcsrsiwlarkirsdltaltesyvkhqglnkninldsadgmpvastdqwseltea
erlqenlqayrtfhvllarlledqqvhftptegdfhqaihtlllqvaafayqieelmill
eykiprneadgmpinvgdgglfekklwglkvlqelsqwtvrsihdlrfissh
>d1cnt4_ 1.27.1.1.7 Ciliary neurotrophic factor (CNTF) {Human (Homo sapiens)}
hrrdlcsrsiwlarkirsdltaltesyvkhqglnkninldsadgmpvastdqwselteae
rlqenlqayrtfhvllarlledqqvhftptegdfhqaihtlllqvaafayqieelmille
ykiprneadgmpinvgdgglfekklwglkvlqelsqwtvrsihdlrfis
>d1cnua_ 4.85.1.2.2 Actophorin {Amoeba (Acanthamoeba castellanii)}
giavsddcvqkfnelklghqhryvtfkmnasntevvvehvggpnatyedfksqlperdcr
yaifdyefqvdggqrnkitfilwapdsapikskmmytstkdsikkklvgiqvevqatdaa
eisedavserakkd
>d1cnv__ 3.1.7.5.3 Seed storage protein {Jack bean (Canavalia ensiformis), Concanavalin B}
dissteiavywgqredgllrdtcktnnykivfisfldkfgceirkpelelegvcgpsvgn
pcsflesqikecqrmgvkvflalggpkgtysacsadyakdlaeylhtyflserregplgk
valdgihfdiqkpvdelnwdnlleelyqikdvyqstfllsaapgclspdeyldnaiqtrh
fdyifvrfyndrscqystgniqrirnawlswtksvyprdknlflelpasqatapgggyip
psaligqvlpylpdlqtryagialwnrqadketgystniiryl
>d1cnw__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasf
>d1cnx__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasf
>d1cny__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasf
>d1cnza_ 3.65.1.1.5 3-isopropylmalate dehydrogenase, IPMDH {Salmonella typhimurium}
msknyhiavlpgdgigpevmaqalkvmdavrsrfdmrittshydvggiaidnhghplpka
tvegceqadailfgsvggpkwenlppesqpergallplrkhfklfsnlrpaklyqgleaf
cplradiaangfdilcvreltggiyfgqpkgregsgqyekafdtevyhrfeieriariaf
esarkrrrkvtsidkanvlqssilwreivndvaktypdvelahmyidnatmqlikdpsqf
dvllcsnlfgdilsdecamitgsmgmlpsaslneqgfglyepaggsapdiagknianpia
qilslalllrysldandaataieqainraleegvrtgdlargaaavstdemgdiiaryva
egv
>d1cnzb_ 3.65.1.1.5 3-isopropylmalate dehydrogenase, IPMDH {Salmonella typhimurium}
msknyhiavlpgdgigpevmaqalkvmdavrsrfdmrittshydvggiaidnhghplpka
tvegceqadailfgsvggpkwenlppesqpergallplrkhfklfsnlrpaklyqgleaf
cplradiaangfdilcvreltggiyfgqpkgregsgqyekafdtevyhrfeieriariaf
esarkrrrkvtsidkanvlqssilwreivndvaktypdvelahmyidnatmqlikdpsqf
dvllcsnlfgdilsdecamitgsmgmlpsaslneqgfglyepaggsapdiagknianpia
qilslalllrysldandaataieqainraleegvrtgdlargaaavstdemgdiiaryva
egv
>d1co4a_ 7.39.1.1.1 Zinc domain conserved in yeast copper-regulated transcription factors {Synthetic}
mvvingvkyacdscikshkaaqcehndrplkilkprgrpptt
>d1co6a_ 1.3.1.1.15 Cytochrome c2 {Rhodopseudomonas viridis}
qdaasgeqvfkqclvchsigpgaknkvgpvlnglfgrhsgtiegfaysdanknsgitwte
evfreyirdpkakipgtkmifagvkdeqkvsdliayikqfnadgskk
>d1co8a_ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkplaqshatkhkipikyaefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1co9a_ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkplaqshatkhkipikyvefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1coai_ 4.33.1.1.2 Chymotrypsin inhibitor CI-2 {Barley (Hordeum vulgare)}
mktewpelvgksveeakkvilqdkpeaqiivlpvgtivtmeyridrvrlfvdkldnvaev
prvg
>d1coba_ 2.1.8.1.1 Cu,Zn superoxide dismutase, SOD {Bovine (Bos taurus)}
atkavcvlkgdgpvqgtihfeakgdtvvvtgsitgltegdhgfhvhqfgdntqgctsagp
hfnplskkhggpkdeerhvgdlgnvtadkngvaivdivdplislsgeysiigrtmvvhek
pddlgrggneestktgnagsrlacgvigiak
>d1cobb_ 2.1.8.1.1 Cu,Zn superoxide dismutase, SOD {Bovine (Bos taurus)}
atkavcvlkgdgpvqgtihfeakgdtvvvtgsitgltegdhgfhvhqfgdntqgctsagp
hfnplskkhggpkdeerhvgdlgnvtadkngvaivdivdplislsgeysiigrtmvvhek
pddlgrggneestktgnagsrlacgvigiak
>d1cod__ 7.7.1.1.19 Cobrotoxin II {Taiwan cobra (Naja naja atra)}
lechnqqssqtptttgcsggetncykkrwrdhrgyrtergcgcpsvkngieinccttdrc
nn
>d1coe__ 7.7.1.1.19 Cobrotoxin II {Taiwan cobra (Naja naja atra)}
lechnqqssqtptttgcsggetncykkrwrdhrgyrtergcgcpsvkngieinccttdrc
nn
>d1cof__ 4.85.1.2.1 Yeast cofilin, monoclinic crystal form {Baker's yeast (Saccharomyces cerevisiae)}
vavadesltafndlklgkkykfilfglndakteivvketstdpsydafleklpendclya
iydfeyeingnegkrskivfftwspdtapvrskmvyasskdalrralngvstdvqgtdfs
evsydsvlervsrga
>d1coha_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1cohb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1cohc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1cohd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1coja1 1.2.7.1.4 (2-90) Fe superoxide dismutase (FeSOD) {Aquifex pyrophilus}
vhklepkdhlkpqnlegisneqiephfeahykgyvakyneiqekladqnfadrskanqny
seyrelkveetfnymgvvlhelyfgmltp
>d1coja2 4.37.1.1.7 (91-212) Fe superoxide dismutase (FeSOD) {Aquifex pyrophilus}
ggkgepsealkkkieediggldactnelkaaamafrgwailgldifsgrlvvngldahnv
ynltgliplividtyehayyvdyknkrppyidaffkninwdvvnerfekamkayealkdf
ik
>d1coka_ 1.61.1.2.4 C-terminal domain of p73 {Human (Homo sapiens)}
yhadpslvsfltglgcpncieyftsqglqsiyhlqnltiedlgalkipeqyrmtiwrglq
dlkqghdy
>d1cola_ 6.1.1.1.1 Colicin A {Escherichia coli}
akderellektseliagmgdkigehlgdkykaiakdiadniknfqgktirsfddamasln
kitanpamkinkadrdalvnawkhvdaqdmanklgnlskafkvadvvmkvekvreksieg
yetgnwgplmleveswvlsgiassvalgifsatlgayalslgvpaiavgiagillaavvg
aliddkfadalnneiir
>d1colb_ 6.1.1.1.1 Colicin A {Escherichia coli}
akderellektseliagmgdkigehlgdkykaiakdiadniknfqgktirsfddamasln
kitanpamkinkadrdalvnawkhvdaqdmanklgnlskafkvadvvmkvekvreksieg
yetgnwgplmleveswvlsgiassvalgifsatlgayalslgvpaiavgiagillaavvg
aliddkfadalnneiir
>d1coma_ 4.59.1.1.1 Chorismate mutase {Bacillus subtilis}
mirgirgattverdteeeilqktkqllekiieenhtkpedvvqmllsatpdlhavfpaka
vrelsgwqyvpvtcmqemdvtgglkkcirvmmtvqtdvpqdqirhvylekavvl
>d1comb_ 4.59.1.1.1 Chorismate mutase {Bacillus subtilis}
mirgirgattverdteeeilqktkqllekiieenhtkpedvvqmllsatpdlhavfpaka
vrelsgwqyvpvtcmqemdvtgglkkcirvmmtvqtdvpqdqirhvylekavvlrpdl
>d1comc_ 4.59.1.1.1 Chorismate mutase {Bacillus subtilis}
mirgirgattverdteeeilqktkqllekiieenhtkpedvvqmllsatpdlhavfpaka
vrelsgwqyvpvtcmqemdvtgglkkcirvmmtvqtdvpqdqirhvylekavvlrpdls
>d1comd_ 4.59.1.1.1 Chorismate mutase {Bacillus subtilis}
mirgirgattverdteeeilqktkqllekiieenhtkpedvvqmllsatpdlhavfpaka
vrelsgwqyvpvtcmqemdvtgglkkcirvmmtvqtdvpqdqirhvylekavvl
>d1come_ 4.59.1.1.1 Chorismate mutase {Bacillus subtilis}
mirgirgattverdteeeilqktkqllekiieenhtkpedvvqmllsatpdlhavfpaka
vrelsgwqyvpvtcmqemdvtgglkkcirvmmtvqtdvpqdqirhvylekavvlrpdl
>d1comf_ 4.59.1.1.1 Chorismate mutase {Bacillus subtilis}
mirgirgattverdteeeilqktkqllekiieenhtkpedvvqmllsatpdlhavfpaka
vrelsgwqyvpvtcmqemdvtgglkkcirvmmtvqtdvpqdqirhvylekavvlrpd
>d1comg_ 4.59.1.1.1 Chorismate mutase {Bacillus subtilis}
mirgirgattverdteeeilqktkqllekiieenhtkpedvvqmllsatpdlhavfpaka
vrelsgwqyvpvtcmqemdvtgglkkcirvmmtvqtdvpqdqirhvylekavvl
>d1comh_ 4.59.1.1.1 Chorismate mutase {Bacillus subtilis}
mirgirgattverdteeeilqktkqllekiieenhtkpedvvqmllsatpdlhavfpaka
vrelsgwqyvpvtcmqemdvtgglkkcirvmmtvqtdvpqdqirhvylekavvl
>d1comi_ 4.59.1.1.1 Chorismate mutase {Bacillus subtilis}
mirgirgattverdteeeilqktkqllekiieenhtkpedvvqmllsatpdlhavfpaka
vrelsgwqyvpvtcmqemdvtgglkkcirvmmtvqtdvpqdqirhvylekavvl
>d1comj_ 4.59.1.1.1 Chorismate mutase {Bacillus subtilis}
mirgirgattverdteeeilqktkqllekiieenhtkpedvvqmllsatpdlhavfpaka
vrelsgwqyvpvtcmqemdvtgglkkcirvmmtvqtdvpqdqirhvylekavvl
>d1comk_ 4.59.1.1.1 Chorismate mutase {Bacillus subtilis}
mirgirgattverdteeeilqktkqllekiieenhtkpedvvqmllsatpdlhavfpaka
vrelsgwqyvpvtcmqemdvtgglkkcirvmmtvqtdvpqdqirhvylekavvlrp
>d1coml_ 4.59.1.1.1 Chorismate mutase {Bacillus subtilis}
mirgirgattverdteeeilqktkqllekiieenhtkpedvvqmllsatpdlhavfpaka
vrelsgwqyvpvtcmqemdvtgglkkcirvmmtvqtdvpqdqirhvylekavvl
>d1cona_ 2.26.1.1.1 Concanavalin A {Jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1coo__ 1.38.1.1.1 C-terminal domain of RNA polymerase alpha subunit {Escherichia coli}
fdpillrpvddleltvrsanclkaeaihyigdlvqrtevellktpnlgkkslteikdvla
srglslgmrlenwppasiade
>d1copd_ 1.36.1.2.5 cro lambda repressor {Bacteriophage lambda (Escherichia coli)}
meqritlkdyamrfgqtktakdlgvyqsainkaihagrkifltinadgsvyaeevkpfps
nkktta
>d1cope_ 1.36.1.2.5 cro lambda repressor {Bacteriophage lambda (Escherichia coli)}
meqritlkdyamrfgqtktakdlgvyqsainkaihagrkifltinadgsvyaeevkpfps
nkktta
>d1cor__ 1.3.1.1.19 Cytochrome c551 {Pseudomonas stutzeri}
xdgealfkskpcaachsidaklvgpafkevaakyagqdgaadllaghikngsqgvwgpip
mppnpvteeeakilaewilsqk
>d1cot__ 1.3.1.1.17 Cytochrome c2 {Paracoccus denitrificans}
dgdaakgekefnkckachmiqapdgtdiikggktgpnlygvvgrkiaseegfkygegile
vaeknpdltwteadlieyvtdpkpwlvkmtddkgaktkmtfkmgknqadvvaflaqnspd
a
>d1coua_ 7.22.1.1.3 Anticoagulant protein {Dog hookworm (Ancylostoma caninum)}
katmqcgenekydscgskecdkkckydgveeeddeepnvpclvrvchqdcvceegfyrnk
ddkcvsaedceldnmdfiypgtrnp
>d1cov1_ 2.9.1.4.14 Coxsackievirus B3 {Host: human (Homo sapiens)}
rvadtvgtgptnseaipaltaaetghtsqvvpsdtmqtrhvknyhsrsestienflcrsa
cvyfteyensgakryaewvitprqaaqlrrklefftyvrfdleltfvitstqqpsttqnq
daqilthqimyvppggpvpdkvdsyvwqtstnpsvfwtegnapprmsvpflsignaysnf
ydgwsefsrngvygintlnnmgtlyarhvnagstgpikstiriyfkpkhvkawiprpprl
cqyekaknvnfqpsgvtttrqsittmtnt
>d1cov2_ 2.9.1.4.14 Coxsackievirus B3 {Host: human (Homo sapiens)}
gysdrvrsitlgnstittqecanvvvgygvwpdylkdseataedqptqpdvatcrfytld
svqwqktspgwwwklpdalsnlglfgqnmqyhylgrtgytihvqcnaskfhqgcllvvcv
peaemgcatlnntpssaellggdtakefadkpvasgsnklvqrvvynagmgvgvgnltif
phqwinlrtnnsativmpytnsvpmdnmfrhnnvtlmvipfvpldycpgsttyvpitvti
apmcaeynglrlaghq
>d1cov3_ 2.9.1.4.14 Coxsackievirus B3 {Host: human (Homo sapiens)}
glptmntpgscqfltsddfqspsampqydvtpemripgevknlmeiaevdsvvpvqnvge
kvnsmeayqipvrsnegsgtqvfgfplqpgyssvfsrtllgeilnyythwsgsikltfmf
cgsamatgkfllaysppgagaptkrvdamlgthvvwdvglqsscvlcipwisqthyryva
sdeytaggfitcwyqtnivvpadaqsscyimcfvsacndfsvrllkdtpfisqenffq
>d1cowa1 1.70.1.1.1 (380-510) C-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
tramkqvagtmklelaqyrevaafaqfgsdldaatqqllsrgvrltellkqgqyspmaie
eqvaviyagvrgyldklepskitkfenaflshvisqhqallgkirtdgkiseesdaklke
ivtnflagfea
>d1cowa2 2.43.1.1.1 (24-94) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
dleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgndklik
egdivkrtgai
>d1cowa3 3.30.1.9.2 (95-379) Central domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
vdvpvgeellgrvvdalgnaidgkgpigskarrrvglkapgiiprisvrepmqtgikavd
slvpigrgqreliigdrqtgktsiaidtiinqkrfndgtdekkklyciyvaigqkrstva
qlvkrltdadamkytivvsatasdaaplqylapysgcsmgeyfrdngkhaliiyddlskq
avayrqmslllrrppgreaypgdvfylhsrlleraakmndafgggsltalpvietqagdv
sayiptnvisitdgqifletelfykgirpainvglsvsrvgsaaq
>d1cowb1 1.70.1.1.1 (380-510) C-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
tramkqvagtmklelaqyrevaafaqfgsdldaatqqllsrgvrltellkqgqyspmaie
eqvaviyagvrgyldklepskitkfenaflshvisqhqallgkirtdgkiseesdaklke
ivtnflagfea
>d1cowb2 2.43.1.1.1 (24-94) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
dleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgndklik
egdivkrtgai
>d1cowb3 3.30.1.9.2 (95-379) Central domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
vdvpvgeellgrvvdalgnaidgkgpigskarrrvglkapgiiprisvrepmqtgikavd
slvpigrgqreliigdrqtgktsiaidtiinqkrfndgtdekkklyciyvaigqkrstva
qlvkrltdadamkytivvsatasdaaplqylapysgcsmgeyfrdngkhaliiyddlskq
avayrqmslllrrppgreaypgdvfylhsrlleraakmndafgggsltalpvietqagdv
sayiptnvisitdgqifletelfykgirpainvglsvsrvgsaaq
>d1cowc1 1.70.1.1.1 (380-510) C-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
tramkqvagtmklelaqyrevaafaqfgsdldaatqqllsrgvrltellkqgqyspmaie
eqvaviyagvrgyldklepskitkfenaflshvisqhqallgkirtdgkiseesdaklke
ivtnflagfea
>d1cowc2 2.43.1.1.1 (19-94) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
adtsvdleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgn
dklikegdivkrtgai
>d1cowc3 3.30.1.9.2 (95-379) Central domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
vdvpvgeellgrvvdalgnaidgkgpigskarrrvglkapgiiprisvrepmqtgikavd
slvpigrgqreliigdrqtgktsiaidtiinqkrfndgtdekkklyciyvaigqkrstva
qlvkrltdadamkytivvsatasdaaplqylapysgcsmgeyfrdngkhaliiyddlskq
avayrqmslllrrppgreaypgdvfylhsrlleraakmndafgggsltalpvietqagdv
sayiptnvisitdgqifletelfykgirpainvglsvsrvgsaaq
>d1cowd1 1.70.1.1.1 (358-475) C-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
mdpnivgsehydvargvqkilqdykslqdiiailgmdelseedkltvsrarkiqrflsqp
fqvaevftghlgklvplketikgfqqilageydhlpeqafymvgpieeavakadklae
>d1cowd2 2.43.1.1.1 (9-81) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1cowd3 3.30.1.9.2 (82-357) Central domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
iripvgpetlgrimnvigepidergpiktkqfaaihaeapefvemsveqeilvtgikvvd
llapyakggkiglfggagvgktvlimelinnvakahggysvfagvgertregndlyhemi
esgvinlkdatskvalvygqmneppgararvaltgltvaeyfrdqegqdvllfidnifrf
tqagsevsallgripsavgyqptlatdmgtmqeritttkkgsitsvqaiyvpaddltdpa
pattfahldattvlsraiaelgiypavdpldstsri
>d1cowe1 1.70.1.1.1 (358-474) C-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
mdpnivgsehydvargvqkilqdykslqdiiailgmdelseedkltvsrarkiqrflsqp
fqvaevftghlgklvplketikgfqqilageydhlpeqafymvgpieeavakadkla
>d1cowe2 2.43.1.1.1 (9-81) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1cowe3 3.30.1.9.2 (82-357) Central domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
iripvgpetlgrimnvigepidergpiktkqfaaihaeapefvemsveqeilvtgikvvd
llapyakggkiglfggagvgktvlimelinnvakahggysvfagvgertregndlyhemi
esgvinlkdatskvalvygqmneppgararvaltgltvaeyfrdqegqdvllfidnifrf
tqagsevsallgripsavgyqptlatdmgtmqeritttkkgsitsvqaiyvpaddltdpa
pattfahldattvlsraiaelgiypavdpldstsri
>d1cowf1 1.70.1.1.1 (358-474) C-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
mdpnivgsehydvargvqkilqdykslqdiiailgmdelseedkltvsrarkiqrflsqp
fqvaevftghlgklvplketikgfqqilageydhlpeqafymvgpieeavakadkla
>d1cowf2 2.43.1.1.1 (9-81) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1cowf3 3.30.1.9.2 (82-357) Central domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
iripvgpetlgrimnvigepidergpiktkqfaaihaeapefvemsveqeilvtgikvvd
llapyakggkiglfggagvgktvlimelinnvakahggysvfagvgertregndlyhemi
esgvinlkdatskvalvygqmneppgararvaltgltvaeyfrdqegqdvllfidnifrf
tqagsevsallgripsavgyqptlatdmgtmqeritttkkgsitsvqaiyvpaddltdpa
pattfahldattvlsraiaelgiypavdpldstsri
>d1cowg_ 1.20.1.1.1 ATP syntase (F1-ATPase), gamma subunit {Bovine (Bos taurus)}
atlkditrrlksikniqkitksmkmvaaakyaraerelkparvygvgslalyekadiktp
edkkkhliigvssdrglcgaihssvakqmkseaanlaaagkevkiigvgdkirsilhrth
sdqflvtfkevgrrpptfgdasvialellnsgyefdegsiifnrfrsvisykteekpifs
ldtissaesmsiyddidadvlrnyqeyslaniiyyslkesttseqsarmtamdnasknas
emidkltltfnrtrqavitkelieiisgaaal
>d1coy_1 3.3.1.2.1 (4-318,451-506) Cholesterol oxidase {Brevibacterium sterolicum}
rtladgdrvpalvigsgyggavaalrltqagiptqivemgrswdtpgsdgkifcgmlnpd
krsmwladktdqpvsnfmgfginksidryvgvldserfsgikvyqgrgvgggslvnggma
vtpkrnyfeeilpsvdsnemynkyfprantglgvnnidqawfestewykfartgrktaqr
sgfttafvpnvydfeymkkeaagqvtksglggeviygnnagkksldktylaqaaatgklt
ittlhrvtkvapatgsgysvtmeqideqgnvvatkvvtadrvffaagsvgtskllvsmka
qghlpnlssqvgegwXgvllnkatdnfgrlpeypglyvvdgslvpgnvgvnpfvtitala
ernmdkiissdi
>d1coy_2 4.14.1.1.1 (319-450) Cholesterol oxidase {Brevibacterium sterolicum}
gnngnimvgranhmwdatgskqatiptmgidnwadptapifaeiaplpagletyvslyla
itknperarfqfnsgtgkvdltwaqsqnqkgidmakkvfdkinqkegtiyrtdlfgvyyk
twgddftyhplg
>d1coza_ 3.19.1.2.1 CTP:glycerol-3-phosphate cytidylyltransferase {(Bacillus subtilis)}
mkkvitygtfdllhwghikllerakqlgdylvvaistdefnlqkqkkayhsyehrklile
tiryvdevipeknweqkkqdiidhnidvfvmgddwegkfdflkdqcevvylprtegistt
kikeei
>d1cozb_ 3.19.1.2.1 CTP:glycerol-3-phosphate cytidylyltransferase {(Bacillus subtilis)}
mkkvitygtfdllhwghikllerakqlgdylvvaistdefnlqkqkkayhsyehrklile
tiryvdevipeknweqkkqdiidhnidvfvmgddwegkfdflkdqcevvylprtegistt
kikeei
>d1cp0a_ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkplaqshatkhkipikynefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1cp2a_ 3.30.1.8.4 Nitrogenase iron protein {Clostridium pasteurianum}
mrqvaiygkggigkstttqnltsglhamgktimvvgcdpkadstrlllgglaqksvldtl
reegedveldsilkegyggircvesggpepgvgcagrgiitsinmleqlgaytddldyvf
ydvlgdvvcggfampiregkaqeiyivasgemmalyaanniskgiqkyaksggvrlggii
cnsrkvaneyelldafakelgsqlihfvprspmvtkaeinkqtvieydptceqaeeyrel
arkvdanelfvipkpmtqerleeilmqyg
>d1cp2b_ 3.30.1.8.4 Nitrogenase iron protein {Clostridium pasteurianum}
mrqvaiygkggigkstttqnltsglhamgktimvvgcdpkadstrlllgglaqksvldtl
reegedveldsilkegyggircvesggpepgvgcagrgiitsinmleqlgaytddldyvf
ydvlgdvvcggfampiregkaqeiyivasgemmalyaanniskgiqkyaksggvrlggii
cnsrkvaneyelldafakelgsqlihfvprspmvtkaeinkqtvieydptceqaeeyrel
arkvdanelfvipkpmtqerleeilmqyg
>d1cp3a_ 3.13.1.1.1 Apopain {Human (Homo sapiens)}
nsykmdypemglciiinnknfhkstgmtsrsgtdvdaanlretfrnlkyevrnkndltre
eivelmrdvskedhskrssfvcvllshgeegiifgtngpvdlkkitnffrgdrcrsltgk
pklfiiqacrgteldcgietdsgvdddmachkipvdadflyaystapgyyswrnskdgsw
fiqslcamlkqyadklefmhiltrvnrkvatefesfsfdatfhakkqipcivsmltkely
fyh
>d1cp3b_ 3.13.1.1.1 Apopain {Human (Homo sapiens)}
nsykmdypemglciiinnknfhkstgmtsrsgtdvdaanlretfrnlkyevrnkndltre
eivelmrdvskedhskrssfvcvllshgeegiifgtngpvdlkkitnffrgdrcrsltgk
pklfiiqacrgteldcgietdsgvdddmachkipvdadflyaystapgyyswrnskdgsw
fiqslcamlkqyadklefmhiltrvnrkvatefesfsfdatfhakkqipcivsmltkely
fyh
>d1cp4__ 1.100.1.1.1 Cytochrome P450 {Pseudomonas putida}
nlaplpphvpehlvfdfdmynpsnlsagvqeawavlqesnvpdlvwtrcngghwiatrgq
lireayedyrhfssecpfipreageaydfiptsmdppeqrqfralanqvvgmpvvdklen
riqelacslieslrpqgqcnftedyaepfpirifmllaglpeediphlkyltdqmtrpdg
smtfaeakealydylipiieqrrqkpgtdaisivangqvngrpitsdeakrmcglllvgg
ldtvvnflsfsmeflakspehrqelierperipaaceellrrfslvadgriltsdyefhg
vqlkkgdqillpqmlsglderenacpmhvdfsrqkvshttfghgshlclgqhlarreiiv
tlkewltripdfsiapgaqiqhksgivsgvqalplvwdpattkav
>d1cp5a_ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkplaqshatkhkipikyfefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1cp6a_ 3.47.4.4.1 Aminopeptidase {Aeromonas proteolytica}
mppitqqatvtawlpqvdasqitgtisslesftnrfytttsgaqasdwiasewqalsasl
pnasvkqvshsgynqksvvmtitgseapdewivigghldstigshtneqsvapgadddas
giaavtevirvlsennfqpkrsiafmayaaeevglrgsqdlanqyksegknvvsalqldm
tnykgsaqdvvfitdytdsnftqyltqlmdeylpsltygfdtcgyacsdhaswhnagypa
ampfeskfndynprihttqdtlansdptgshakkftqlglayaiemgsatg
>e1cp9.1a 4.124.1.2.2 Penicillin acylase, catalytic domain {Providencia rettgeri}
stqikierdnygvphiyandtyslfygygyavaqdrlfqmemakrstqgtvsevfgkdyi
sfdkeirnnywpdsihkqinqlpsqeqdilrgyadgmnawikqintkpddlmpkqfidyd
flpsqwtsfdvamimvgtlanrfsdmnseidnlalltalkdkygeqlgveffnqinwlnn
pnapttisseeftysd
>e1cp9.1b 4.124.1.2.2 Penicillin acylase, catalytic domain {Providencia rettgeri}
snvwlvgktkasgakaillngpqfgwfnpaytygiglhgagfnivgntpfaypailfghn
ghvswgstagfgdgvdifaeqvspedpnsylhqgqwkkmlsrqetlnvkgeqpitfeiyr
tvhgnvvkrdktthtayskarawdgkeltslmawvkqgqaqnwqqwldqaqnqaltinwy
yadkdgnigyvhtghypdrqinhdprlpvsgtgewdwkgiqpfannpkvynpksgyianw
nnspaknypasdlfaflwgsadrvkeidnrieaydkltaddmwailqqtsrvdlnhrlft
pfltqatqglpsndnsvklvsmlqqwdginqlssdgkhyihpgsaildiwlkemlkatlg
qtvpapfdkwylasgyettqegptgslnistgakllyeslledkspisqsidlfsgqpqn
dvirktlnttyqkmiekygdnpanwqtpataltfrennffgipqalpqenfhqneyhnrg
tendlivfteegvsawdvvapgqsgfispqgkpsphyqdqlslyqqfgkkplwlnsedva
pyiestetliier
>d1cpb__ 3.47.4.1.5 Carboxypeptidase B {Bovine (Bos taurus)}
ttghsyekynnwetieawteqvasenpdlisrsaigttflgntiyllkvgkpgsnkpavf
mdcgfharewispafcqwfvrexxxxxxxeihmtefldkldfyvlpvvnidgyiytwttn
rmwrktrstragssctgtdlnrnfdagwcsigasnnpcsetycgsaaesekeskavadfi
rnhlssikayltihsysqmmlypysydyklpknnvelntlakgavkklaslhgttysygp
gattiypasggsddwaydqgikysftfelrdkgrygfvlpesqiqptceetmlaikyvts
yvlehl
>d1cpca_ 1.1.1.2.2 C-phycocyanin {Cyanobacterium (Fremyella diplosiphon)}
mktplteavaaadsqgrflssteiqtafgrfrqasaslaaakaltekasslasgaanavy
skfpyttsqngpnfastqtgkdkcvrdigyylrmvtyclvvggtgplddyliggiaeinr
tfdlspswyvealkyikanhglsgdpaveansyidyainals
>d1cpcb_ 1.1.1.2.2 C-phycocyanin {Cyanobacterium (Fremyella diplosiphon)}
mldafakvvsqadargeylsgsqidalsalvadgnkrmdvvnritgnsstivanaarslf
aeqpqliapggnaytsrrmaaclrdmeiilryvtyaifagdasvlddrclnglketylal
gtpgssvavgvqkmkdaalaiagdtngitrgdcaslmaevasyfdkaasava
>d1cpck_ 1.1.1.2.2 C-phycocyanin {Cyanobacterium (Fremyella diplosiphon)}
mktplteavaaadsqgrflssteiqtafgrfrqasaslaaakaltekasslasgaanavy
skfpyttsqngpnfastqtgkdkcvrdigyylrmvtyclvvggtgplddyliggiaeinr
tfdlspswyvealkyikanhglsgdpaveansyidyainals
>d1cpcl_ 1.1.1.2.2 C-phycocyanin {Cyanobacterium (Fremyella diplosiphon)}
mldafakvvsqadargeylsgsqidalsalvadgnkrmdvvnritgnsstivanaarslf
aeqpqliapggnaytsrrmaaclrdmeiilryvtyaifagdasvlddrclnglketylal
gtpgssvavgvqkmkdaalaiagdtngitrgdcaslmaevasyfdkaaaava
>d1cpd__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1cpe__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1cpf__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1cpg__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpqgaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>e1cph.1a 7.1.1.1.1 Insulin {Bovine (Bos taurus)}
giveqccasvcslyqlenycn
>e1cph.1b 7.1.1.1.1 Insulin {Bovine (Bos taurus)}
fvnqhlcgshlvealylvcgergffytpka
>d1cpia_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtiriggqlkealldtgaddtvleemnlpgkwkpkmiggiggfikvrqyd
qipveixghkaigtvlvgptpvniigrnlltqigxtlnf
>d1cpib_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtiriggqlkealldtgaddtvleemnlpgkwkpkmiggiggfikvrqyd
qipveixghkaigtvlvgptpvniigrnlltqigxtlnf
>d1cpja_ 4.3.1.1.11 (Pro)cathepsin B {Rat (Rattus norvegicus)}
lpesfdareqwsncptiaqirdqgscgscwafgaveamsdricihtngrvnvevsaedll
tccgiqcgdgcnggypsgawnfwtrkglvsggvynshigclpytippcehhvngarppct
gegdtpkcnkmceagystsykedkhygytsysvsdsekeimaeiykngpvegaftvfsdf
ltyksgvykheagdvmgghairilgwgiengvpywlvanswnadwgdngffkilrgenhc
gieseivagiprt
>d1cpjb_ 4.3.1.1.11 (Pro)cathepsin B {Rat (Rattus norvegicus)}
lpesfdareqwsncptiaqirdqgscgscwafgaveamsdricihtngrvnvevsaedll
tccgiqcgdgcnggypsgawnfwtrkglvsggvynshigclpytippcehhvngarppct
gegdtpkcnkmceagystsykedkhygytsysvsdsekeimaeiykngpvegaftvfsdf
ltyksgvykheagdvmgghairilgwgiengvpywlvanswnadwgdngffkilrgenhc
gieseivagiprt
>d1cpm__ 2.26.1.2.3 Bacillus 1-3,1-4-beta-glucanase {Bacillus macerans}
fdcaeyrstniygyglyevsmkpakntgivssfftytgpahgtqwdeidieflgkdttkv
qfnyytngvgghekvislgfdaskgfhtyafdwqpgyikwyvdgvlkhtatanipstpgk
immnlwngtgvddwlgsynganplyaeydwvkytsnqtggsffepfnsynsgtwekadgy
snggvfnctwrannvnftndgklklgltssayna
>d1cpn__ 2.26.1.2.3 Bacillus 1-3,1-4-beta-glucanase {Bacillus macerans}
fdcaeyrstniygyglyevsmkpakntgivssfftytgpahgtqwdeidieflgkdttkv
qfnyytngvgghekvislgfdaskgfhtyafdwqpgyikwyvdgvlkhtatanipstpgk
immnlwngtgvddwlgsynganplyaeydwvkytsngsvfwepksyfnpstwekadgysn
ggvfnctwrannvnftndgklklgltss
>d1cpo_1 1.42.2.1.1 (1-119) Cloroperoxidase {Fungus (Caldariomyces fumago)}
epgsgigypydnntlpyvapgptdsrapcpalnalanhgyiphdgraisretlqnaflnh
mgiansvielaltnafvvceyvtgsdcgdslvnltllaephafehdhsfsrkdykqgva
>d1cpo_2 1.42.2.1.1 (120-298) Cloroperoxidase {Fungus (Caldariomyces fumago)}
nsndfidnrnfdaetfqtsldvvagkthfdyadmneirlqreslsneldfpgwfteskpi
qnvesgfifalvsdfnlpdndenplvridwwkywftnesfpyhlgwhppspareiefvts
assavlaasvtstpsslpsgaigpgaeavplsfastmtpfllatnapyyaqdptlgpnd
>d1cpq__ 1.25.3.2.6 Cytochrome c' {Rhodobacter capsulatus}
adtkevleareayfkslggsmkamtgvakafdaeaakveaaklekilatdvaplfpagts
stdlpgqteakaaiwanmddfgakgkamheaggaviaaanagdgaafgaalqklggtcka
chddyreed
>d1cpr__ 1.25.3.2.6 Cytochrome c' {Rhodobacter capsulatus}
adtkevleareayfkslggsmkamtgvakafdaeaakveaaklekilatdvaplfpagts
stdlpgqteakaaiwanmddfgakgkamhdaggaviaaanagdgaafgaalqklggtcka
chddyreed
>d1cps__ 3.47.4.1.1 Carboxypeptidase A {Bovine (Bos taurus)}
arstntfnyatyhtldeiydfmdllvaehpqlvsklqigrsyegrpiyvlkfstggsnrp
aiwidlgihsrewitqatgvwfakkftenygqnpsftaildsmdifleivtnpngfafth
senrlwrktrsvtssslcvgvdanrnwdagfgkagassspcsetyhgkyansevevksiv
dfvknhgnfkaflsihsysqlllypygyttqsipdktelnqvaksavaalkslygtsyky
gsiittiyqasggsidwsynqgikysftfelrdtgrygfllpasqiiptaqetwlgvlti
mehtvnn
>d1cpt__ 1.100.1.1.5 Cytochrome P450-TERP {Pseudomonas}
mdaratipehiartvilpqgyaddeviypafkwlrdeqplamahiegydpmwiatkhadv
mqigkqpglfsnaegseilydqnneafmrsisggcphvidsltsmdppthtayrgltlnw
fqpasirkleenirriaqasvqrlldfdgecdfmtdcalyyplhvvmtalgvpeddeplm
lkltqdffgveaarrfhetiatfydyfngftvdrrscpkddvmsllanskldgnyiddky
inayyvaiataghdttssssggaiiglsrnpeqlalaksdpaliprlvdeavrwtapvks
fmrtaladtevrgqnikrgdrimlsypsanrdeevfsnpdefditrfpnrhlgfgwgahm
clgqhlaklemkiffeellpklksvelsgpprlvatnfvggpknvpirftka
>d1cpua1 2.62.1.1.9 (404-496) Animal alpha-amylase {Human (Homo sapiens)}
qpftnwydngsnqvafgrgnrgfivfnnddwsfsltlqtglpagtycdvisgdkingnct
gikiyvsddgkahfsisnsaedpfiaihaeskl
>d1cpua2 3.1.7.1.9 (2-403) Animal alpha-amylase {Human (Homo sapiens)}
yspntqqgrtsivhlfewrwvdialecerylapkgfggvqvsppnenvaiynpfrpwwer
yqpvsyklctrsgnedefrnmvtrcnnvgvriyvdavinhmcgnavsagtsstcgsyfnp
gsrdfpavpysgwdfndgkcktgsgdienyndatqvrdcrltglldlalekdyvrskiae
ymnhlidigvagfrldaskhmwpgdikaildklhnlnsnwfpagskpfiyqevidlggep
ikssdyfgngrvtefkygaklgtvirkwngekmsylknwgegwgfvpsdralvfvdnhdn
qrghgaggasiltfwdarlykmavgfmlahpygftrvmssyrwprqfqngndvndwvgpp
nnngvikevtinpdttcgndwvcehrwrqirnmvifrnvvdg
>d1cpwa_ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkplaqshatkhkipikywefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1cpx__ 3.47.4.1.1 Carboxypeptidase A {Bovine (Bos taurus)}
stntfnyatyhtldeiydfmdllvaehpqlvsklqigrsyegrpiyvlkfstggsnrpai
widlgihsrewitqatgvwfakkftedygqdpsftaildsmdifleivtnpdgfafthsq
nrlwrktrsvtssslcvgvdanrnwdagfgkagassspcsetyhgkyansevevksivdf
vkdhgnfkaflsihsysqlllypygyttqsipdktelnqvaksavaalkslygtsykygs
iittiyqasggsidwsynqgikysftfelrdtgrygfllpasqiiptaqetwlgvltime
htvnn
>d1cpy__ 3.59.1.4.2 Serine carboxypeptidase II {Baker's yeast (Saccharomyces cerevisiae)}
kikdpkilgidpnvtqytgyldvededkhfffwtfesrndpakdpvilwlnggpgcsslt
glffalgpssigpdlkpignpyswnsnatvifldqpvnvgfsysgssgvsntvaagkdvy
nflelffdqfpeyvnkgqdfhiagasyaghyipvfaseilshkdrnfnltsvligngltd
pltqynyyepmacgeggepsvlpseecsamedslerclgliescydsqsvwscvpatiyc
nnaqlapyqrtgrnvydirkdceggnlcyptlqdiddylnqdyvkeavgaevdhyescnf
dinrnflfagdwmkpyhtavtdllnqdlpilvyagdkdficnwlgnkawtdvlpwkydee
fasqkvrnwtasitdevagevksykhftylrvfngghmvpfdvpenalsmvnewihggfs
l
>d1cpza_ 4.47.16.1.3 Copper chaperone {Enterococcus hirae}
aqefsvkgmscnhcvarieeavgrisgvkkvkvqlkkekavvkfdeanvqateicqaine
lgyqaevi
>d1cq2a_ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgyqg
>e1cq4.1a 4.33.1.1.2 Chymotrypsin inhibitor CI-2 {Barley (Hordeum vulgare)}
ktewpelvgksveeakkvilqdkpeaqiivlpvgtiv
>e1cq4.1b 4.33.1.1.2 Chymotrypsin inhibitor CI-2 {Barley (Hordeum vulgare)}
yridrvrlfvdkldniaqvprvg
>d1cqa__ 4.86.1.1.5 Profilin (actin-binding protein) {Birch (Betula verrucosa)}
swqtyvdehlmcdidgqgeelaasaivghdgsvwaqsssfpqfkpqeitgimkdfeepgh
laptglhlggikymviqgeagavirgkkgsggitikktgqalvfgiyeepvtpgqcnmvv
erlgdylidqgl
>d1cqda_ 4.3.1.1.6 Proline-specific cysteine protease {Ginger rhizome (Zingiber officinale)}
lpdsidwrengavvpvknqggcgscwafstvaaveginqivtgdlislseqqlvdcttan
hgcrggwmnpafqfivnngginseetypyrgqdgicnstvnapvvsidsyenvpshneqs
lqkavanqpvsvtmdaagrdfqlyrsgiftgscnisanhaltvvgygtendkdfwivkns
wgknwgesgyiraernienpdgkcgitrfasypvkk
>d1cqdb_ 4.3.1.1.6 Proline-specific cysteine protease {Ginger rhizome (Zingiber officinale)}
lpdsidwrengavvpvknqggcgscwafstvaaveginqivtgdlislseqqlvdcttan
hgcrggwmnpafqfivnngginseetypyrgqdgicnstvnapvvsidsyenvpshneqs
lqkavanqpvsvtmdaagrdfqlyrsgiftgscnisanhaltvvgygtendkdfwivkns
wgknwgesgyiraernienpdgkcgitrfasypvkk
>d1cqdc_ 4.3.1.1.6 Proline-specific cysteine protease {Ginger rhizome (Zingiber officinale)}
lpdsidwrengavvpvknqggcgscwafstvaaveginqivtgdlislseqqlvdcttan
hgcrggwmnpafqfivnngginseetypyrgqdgicnstvnapvvsidsyenvpshneqs
lqkavanqpvsvtmdaagrdfqlyrsgiftgscnisanhaltvvgygtendkdfwivkns
wgknwgesgyiraernienpdgkcgitrfasypvkk
>d1cqdd_ 4.3.1.1.6 Proline-specific cysteine protease {Ginger rhizome (Zingiber officinale)}
lpdsidwrengavvpvknqggcgscwafstvaaveginqivtgdlislseqqlvdcttan
hgcrggwmnpafqfivnngginseetypyrgqdgicnstvnapvvsidsyenvpshneqs
lqkavanqpvsvtmdaagrdfqlyrsgiftgscnisanhaltvvgygtendkdfwivkns
wgknwgesgyiraernienpdgkcgitrfasypvkk
>d1cqea1 1.90.1.2.3 (74-583) Prostaglandin H2 synthase-1 {Sheep (Ovis aries)}
iwtwlrttlrpspsfihfllthgrwlwdfvnatfirdtlmrlvltvrsnlipspptynia
hdyiswesfsnvsyytrilpsvprdcptpmgtkgkkqlpdaeflsrrfllrrkfipdpqg
tnlmfaffaqhfthqffktsgkmgpgftkalghgvdlghiygdnlerqyqlrlfkdgklk
yqmlngevyppsveeapvlmhyprgippqsqmavgqevfgllpglmlyatiwlrehnrvc
dllkaehptwgdeqlfqtarliligetikivieeyvqqlsgyflqlkfdpellfgaqfqy
rnriamefnqlyhwhplmpdsfrvgpqdysyeqflfntsmlvdygvealvdafsrqpagr
igggrnidhhilhvavdvikesrvlrlqpfneyrkrfgmkpytsfqeltgekemaaelee
lygdidalefypglllekchpnsifgesmiemgapfslkgllgnpicspeywkastfgge
vgfnlvktatlkklvclntktcpyvsfhvp
>d1cqea2 7.3.11.1.9 (32-73) Prostaglandin H2 synthase-1, EGF-like module {Sheep (Ovis aries)}
pvnpccyypcqhqgicvrfgldryqcdctrtgysgpnctipe
>d1cqeb1 1.90.1.2.3 (74-583) Prostaglandin H2 synthase-1 {Sheep (Ovis aries)}
iwtwlrttlrpspsfihfllthgrwlwdfvnatfirdtlmrlvltvrsnlipspptynia
hdyiswesfsnvsyytrilpsvprdcptpmgtkgkkqlpdaeflsrrfllrrkfipdpqg
tnlmfaffaqhfthqffktsgkmgpgftkalghgvdlghiygdnlerqyqlrlfkdgklk
yqmlngevyppsveeapvlmhyprgippqsqmavgqevfgllpglmlyatiwlrehnrvc
dllkaehptwgdeqlfqtarliligetikivieeyvqqlsgyflqlkfdpellfgaqfqy
rnriamefnqlyhwhplmpdsfrvgpqdysyeqflfntsmlvdygvealvdafsrqpagr
igggrnidhhilhvavdvikesrvlrlqpfneyrkrfgmkpytsfqeltgekemaaelee
lygdidalefypglllekchpnsifgesmiemgapfslkgllgnpicspeywkastfgge
vgfnlvktatlkklvclntktcpyvsfhvp
>d1cqeb2 7.3.11.1.9 (31-73) Prostaglandin H2 synthase-1, EGF-like module {Sheep (Ovis aries)}
apvnpccyypcqhqgicvrfgldryqcdctrtgysgpnctipe
>d1cqga_ 3.38.1.1.4 Thioredoxin {Human (Homo sapiens)}
mvkqiesktafqealdaagdklvvvdfsatwcgpakmikpffhslsekysnviflevdvd
daqdvaseaevkatptfqffkkgqkvgefsgankekleatinelv
>d1cqha_ 3.38.1.1.4 Thioredoxin {Human (Homo sapiens)}
mvkqiesktafqealdaagdklvvvdfsatwcgpakmikpffhslsekysnviflevdvd
daqdvaseaevkatptfqffkkgqkvgefsgankekleatinelv
>d1cqka_ 2.1.1.2.142 Immunoglobulin (constant domains of L and H chains) {Fc MAK33 (mouse)}
paapqvytipppleqmakdlvsltcmitdffpeditvewqwngqpaenykntqpimdtdg
syfvysklnvqksnweagntftcsvlheglhnhhtekslsh
>d1cqkb_ 2.1.1.2.142 Immunoglobulin (constant domains of L and H chains) {Fc MAK33 (mouse)}
paapqvytipppleqmakdlvsltcmitdffpeditvewqwngqpaenykntqpimdtdg
syfvysklnvqksnweagntftcsvlheglhnhhtekslsh
>d1cqqa_ 2.41.1.4.1 3C cysteine protease (picornain 3C) {Human type 2 rhinovirus}
gpeeefgmslikhnscvittengkftglgvydrfvvvpthadpgkeiqvdgittkvidsy
dlynkngikleitvlkldrnekfrdirryipnneddypncnlallanqpeptiinvgdvv
sygnillsgnqtarmlkysyptksgycggvlykigqvlgihvggngrdgfsamllrsyft
>d1cqva1 2.35.2.2.2 (1-120) Staphylococcal enterotoxin C2, SEC2 {Staphylococcus aureus}
esqpdptpdelhksseftgtmgnmkylyddhyvsatkvmsvdkflahdliynisdkklkn
ydkvktellnedlakkykdevvdvygsnyyvncyfsskdnvgkvtggktcmyggitkheg
>d1cqva2 4.13.7.1.2 (121-239) Staphylococcal enterotoxin C2, SEC2 {Staphylococcus aureus}
nhfdngnlqnvlirvyenkrntisfevqtdkksvtaqeldikarnflinkknlyefnssp
yetgyikfienngntfwydmmpapgdkfdqskylmmyndnktvdsksvkievhlttkng
>d1cqwa_ 3.59.1.6.2 Haloalkane dehalogenase {Rhodococcus sp.}
igtgfpfdphyvevlgermhyvdvgprdgtpvlflhgnptssylwrniiphvapshrcia
pdligmgksdkpdldyffddhvryldafiealgleevvlvihdwgsalgfhwakrnperv
kgiacmefirpiptwdewpefaretfqafrtadvgreliidqnafiegvlpkcvvrplte
vemdhyrepflkpvdreplwrfpneipiagepanivalveaymnwlhqspvpkllfwgtp
gvlippaeaarlaeslpncktvdigpglhylqednpdligseiarwlpglasglg
>d1cqxa1 1.1.1.1.48 (1-150) Flavohemoglobin, N-terminal domain {Alcaligenes eutrophus}
mltqktkdivkatapvlaehgydiikcfyqrmfeahpelknvfnmahqeqgqqqqalara
vyayaeniedpnslmavlkniankhaslgvkpeqypivgehllaaikevlgnaatddiis
awaqaygnladvlmgmeselyersaeqpgg
>d1cqxa2 2.38.1.3.1 (151-261) Flavohemoglobin, central domain {Alcaligenes eutrophus}
wkgwrtfvirekrpesdvitsfilepadggpvvnfepgqytsvaidvpalglqqirqysl
sdmpngrtyrisvkregggpqppgyvsnllhdhvnvgdqvklaapygsfhi
>d1cqxa3 3.18.1.4.1 (262-403) Flavohemoglobin, C-terminal domain {Alcaligenes eutrophus}
dvdaktpivlisggvgltpmvsmlkvalqapprqvvfvhgarnsavhamrdrlreaakty
enldlfvfydqplpedvqgrdydypglvdvkqieksillpdadyyicgpipfmrmqhdal
knlgihearihyevfgpdlfae
>d1cqxb1 1.1.1.1.48 (1-150) Flavohemoglobin, N-terminal domain {Alcaligenes eutrophus}
mltqktkdivkatapvlaehgydiikcfyqrmfeahpelknvfnmahqeqgqqqqalara
vyayaeniedpnslmavlkniankhaslgvkpeqypivgehllaaikevlgnaatddiis
awaqaygnladvlmgmeselyersaeqpgg
>d1cqxb2 2.38.1.3.1 (151-261) Flavohemoglobin, central domain {Alcaligenes eutrophus}
wkgwrtfvirekrpesdvitsfilepadggpvvnfepgqytsvaidvpalglqqirqysl
sdmpngrtyrisvkregggpqppgyvsnllhdhvnvgdqvklaapygsfhi
>d1cqxb3 3.18.1.4.1 (262-403) Flavohemoglobin, C-terminal domain {Alcaligenes eutrophus}
dvdaktpivlisggvgltpmvsmlkvalqapprqvvfvhgarnsavhamrdrlreaakty
enldlfvfydqplpedvqgrdydypglvdvkqieksillpdadyyicgpipfmrmqhdal
knlgihearihyevfgpdlfae
>d1cqya_ 2.3.1.1.6 beta-amylase {Bacillus cereus}
tpvmqtivvknvpttigdtvyitgnraelgswdtkqypiqlyydshsndwrgnvvlpaer
niefkafikskdgtvkswqtiqqswnpvplkttshtssw
>d1cr8__ 7.12.1.1.1 Ligand-binding domain of low-density lipoprotein receptor {Human (Homo sapiens)}
pggchtdefqcrldglciplrwrcdgdtdcmdssdekscegv
>d1cra__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
xshhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslril
nnghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhl
vhwntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdp
rgllpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelm
vdnwrpaqplknrqikasfk
>d1crb__ 2.53.1.2.11 Cellular retinol-binding protein II (CRBP) {Rat (Rattus rattus)}
pvdfngywkmlsnenfeeylraldvnvalrkianllkpdkeivqdgdhmiirtlstfrny
imdfqvgkefeedltgiddrkcmttvswdgdklqcvqkgekegrgwtqwiegdelhlemr
aegvtckqvfkkvh
>d1crca_ 1.3.1.1.8 Mitochondrial cytochrome c {Horse (Equus caballus)}
xgdvekgkkifvqkcaqchtvekggkhktgpnlhglfgrktgqapgftytdanknkgitw
keetlmeylenpkkyipgtkmifagikkkteredliaylkkatne
>d1crcb_ 1.3.1.1.8 Mitochondrial cytochrome c {Horse (Equus caballus)}
xgdvekgkkifvqkcaqchtvekggkhktgpnlhglfgrktgqapgftytdanknkgitw
keetlmeylenpkkyipgtkmifagikkkteredliaylkkatne
>d1cre__ 7.7.1.1.15 Cardiotoxin II {Taiwan cobra (Naja naja atra)}
lkcnklvplfyktcpagknlcykmfmvsnltvpvkrgcidvcpknsalvkyvccntdrcn
>d1crf__ 7.7.1.1.15 Cardiotoxin II {Taiwan cobra (Naja naja atra)}
lkcnklvplfyktcpagknlcykmfmvsnltvpvkrgcidvcpknsalvkyvccntdrcn
>d1crg__ 1.3.1.1.7 Mitochondrial cytochrome c {Baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdaiikk
nvlwdennmseyltnpkkyipgtkmafgglkkekdrndlitylkkate
>d1crh__ 1.3.1.1.7 Mitochondrial cytochrome c {Baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdaiikk
nvlwdennmseyltnpkkyipgtkmafgglkkekdrndlitylkkace
>d1cri__ 1.3.1.1.7 Mitochondrial cytochrome c {Baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdaiikk
nvlwdennmsefltnpkkyipgtkmafgglkkekdrndlitylkkate
>d1crj__ 1.3.1.1.7 Mitochondrial cytochrome c {Baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdaiikk
nvlwdennmsefltnpkkyipgtkmafgglkkekdrndlitylkkate
>d1crka1 1.80.1.1.1 (1-98) Creatine kinase, N-terminal domain {Chicken (Gallus gallus), mitochondria}
tvhekrklfppsadypdlrkhnncmaecltpaiyaklrdkltpngysldqciqtgvdnpg
hpfiktvgmvagdeesyevfaeifdpvikarhngydpr
>d1crka2 4.102.1.2.1 (99-380) Creatine kinase, C-terminal domain {Chicken (Gallus gallus), mitochondria}
tmkhhtdldaskithgqfderyvlssrvrtgrsirglslppacsraerrevenvvvtala
glkgdlsgkyysltnmserdqqqliddhflfdkpvsplltcagmardwpdargiwhnndk
tflvwineedhtrvismekggnmkrvferfcrglkeverlikergwefmwnerlgyvltc
psnlgtglragvhvklprlskdprfpkilenlrlqkrgtggvdtaavadvydisnldrmg
rsevelvqividgvnylvdcekklekgqdikvppplpqfgrk
>d1crkb1 1.80.1.1.1 (1-98) Creatine kinase, N-terminal domain {Chicken (Gallus gallus), mitochondria}
tvhekrklfppsadypdlrkhnncmaecltpaiyaklrdkltpngysldqciqtgvdnpg
hpfiktvgmvagdeesyevfaeifdpvikarhngydpr
>d1crkb2 4.102.1.2.1 (99-380) Creatine kinase, C-terminal domain {Chicken (Gallus gallus), mitochondria}
tmkhhtdldaskithgqfderyvlssrvrtgrsirglslppacsraerrevenvvvtala
glkgdlsgkyysltnmserdqqqliddhflfdkpvsplltcagmardwpdargiwhnndk
tflvwineedhtrvismekggnmkrvferfcrglkeverlikergwefmwnerlgyvltc
psnlgtglragvhvklprlskdprfpkilenlrlqkrgtggvdtaavadvydisnldrmg
rsevelvqividgvnylvdcekklekgqdikvppplpqfgrk
>d1crkc1 1.80.1.1.1 (1-98) Creatine kinase, N-terminal domain {Chicken (Gallus gallus), mitochondria}
tvhekrklfppsadypdlrkhnncmaecltpaiyaklrdkltpngysldqciqtgvdnpg
hpfiktvgmvagdeesyevfaeifdpvikarhngydpr
>d1crkc2 4.102.1.2.1 (99-380) Creatine kinase, C-terminal domain {Chicken (Gallus gallus), mitochondria}
tmkhhtdldaskithgqfderyvlssrvrtgrsirglslppacsraerrevenvvvtala
glkgdlsgkyysltnmserdqqqliddhflfdkpvsplltcagmardwpdargiwhnndk
tflvwineedhtrvismekggnmkrvferfcrglkeverlikergwefmwnerlgyvltc
psnlgtglragvhvklprlskdprfpkilenlrlqkrgtggvdtaavadvydisnldrmg
rsevelvqividgvnylvdcekklekgqdikvppplpqfgrk
>d1crkd1 1.80.1.1.1 (1-98) Creatine kinase, N-terminal domain {Chicken (Gallus gallus), mitochondria}
tvhekrklfppsadypdlrkhnncmaecltpaiyaklrdkltpngysldqciqtgvdnpg
hpfiktvgmvagdeesyevfaeifdpvikarhngydpr
>d1crkd2 4.102.1.2.1 (99-380) Creatine kinase, C-terminal domain {Chicken (Gallus gallus), mitochondria}
tmkhhtdldaskithgqfderyvlssrvrtgrsirglslppacsraerrevenvvvtala
glkgdlsgkyysltnmserdqqqliddhflfdkpvsplltcagmardwpdargiwhnndk
tflvwineedhtrvismekggnmkrvferfcrglkeverlikergwefmwnerlgyvltc
psnlgtglragvhvklprlskdprfpkilenlrlqkrgtggvdtaavadvydisnldrmg
rsevelvqividgvnylvdcekklekgqdikvppplpqfgrk
>d1crl__ 3.59.1.14.8 Type-B carboxylesterase/lipase {Fungus (Candida rugosa,), formerly Cylindracea}
aptatlangdtitglnaiineaflgipfaeppvgnlrfkdpvpysgsldgqkftsygpsc
mqqnpegtyeenlpkaaldlvmqskvfeavspssedcltinvvrppgtkaganlpvmlwi
fgggfevggtstfppaqmitksiamgkpiihvsvnyrvsswgflagdeikaegsanaglk
dqrlgmqwvadniaafggdptkvtifgesagsmsvmchilwndgdntykgkplfragimq
sgamvpsdavdgiygneifdllasnagcgsasdklaclrgvssdtledatnntpgflays
slrlsylprpdgvnitddmyalvregkyanipviigdqndegtffgtsslnvttdaqare
yfkqsfvhasdaeidtlmtaypgditqgspfdtgilnaltpqfkrisavlgdlgftlarr
yflnhytggtkysflskqlsglpvlgtfhsndivfqdyllgsgsliynnafiafatdldp
ntagllvkwpeytsssqsgnnlmminalglytgkdnfrtagydalfsnppsffv
>d1crm__ 2.65.1.1.1 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme I}
wgyddkngpeqwsklypiangnnqspvdiktsetkhdtslkpisvsynpatakeiinvgh
sfhvnfednqdrsvlkggpfsdsyrlfqfhfhwgstnehgsehtvdgvkysaelhvahwn
sakysslaeaaskadglavigvlmkvgeanpklqkvldalqaiktkgkrapftnfdpstl
lpssldfwtypgslthpplyesvtwiickesisvsseqlaqfrsllsnvegdnavpmqhn
nrptqplkgrtvrasf
>d1crn__ 7.13.1.1.1 Crambin {Abyssinian cabbage (Crambe abyssinica)}
ttccpsivarsnfnvcrlpgtpeaicatytgciiipgatcpgdyan
>d1crp__ 3.30.1.6.1 cH-p21 Ras protein {Human (Homo sapiens)}
mteyklvvvgaggvgksaltiqliqnhfvdeydptiedsyrkqvvidgetclldildtag
qeeysamrdqymrtgegflcvfainntksfedihqyreqikrvkdsddvpmvlvgnkcdl
aartvesrqaqdlarsygipyietsaktrqgvedafytlvreirqh
>d1crq__ 3.30.1.6.1 cH-p21 Ras protein {Human (Homo sapiens)}
mteyklvvvgaggvgksaltiqliqnhfvdeydptiedsyrkqvvidgetclldildtag
qeeysamrdqymrtgegflcvfainntksfedihqyreqikrvkdsddvpmvlvgnkcdl
aartvesrqaqdlarsygipyietsaktrqgvedafytlvreirqh
>d1crr__ 3.30.1.6.1 cH-p21 Ras protein {Human (Homo sapiens)}
mteyklvvvgaggvgksaltiqliqnhfvdeydptiedsyrkqvvidgetclldildtag
qeeysamrdqymrtgegflcvfainntksfedihqyreqikrvkdsddvpmvlvgnkcdl
aartvesrqaqdlarsygipyietsaktrqgvedafytlvreirqh
>d1crxa1 1.61.2.1.1 (20-129) Cre recombinase {Bacteriophage P1}
sdevrknlmdmfrdrqafsehtwkmllsvcrswaawcklnnrkwfpaepedvrdyllylq
arglavktiqqhlgqlnmlhrrsglprpsdsnavslvmrrirkenvdage
>d1crxa2 4.133.1.1.3 (130-341) Cre recombinase {Bacteriophage P1}
rakqalafertdfdqvrslmensdrcqdirnlaflgiayntllriaeiarirvkdisrtd
ggrmlihigrtktlvstagvekalslgvtklverwisvsgvaddpnnylfcrvrkngvaa
psatsqlstralegifeathrliygakddsgqrylawsghsarvgaardmaragvsipei
mqaggwtnvnivmnyirnldsetgamvrlled
>d1crxb1 1.61.2.1.1 (20-129) Cre recombinase {Bacteriophage P1}
sdevrknlmdmfrdrqafsehtwkmllsvcrswaawcklnnrkwfpaepedvrdyllylq
arglavktiqqhlgqlnmlhrrsglprpsdsnavslvmrrirkenvdage
>d1crxb2 4.133.1.1.3 (130-341) Cre recombinase {Bacteriophage P1}
rakqalafertdfdqvrslmensdrcqdirnlaflgiayntllriaeiarirvkdisrtd
ggrmlihigrtktlvstagvekalslgvtklverwisvsgvaddpnnylfcrvrkngvaa
psatsqlstralegifeathrliygakddsgqrylawsghsarvgaardmaragvsipei
mqaggwtnvnivmnxirnldsetgamvrlled
>d1cry__ 1.3.1.1.15 Cytochrome c2 {Rhodopseudomonas viridis}
qdaasgeqvfkqclvchsigpgaknkvgpvlnglfgrhsgtiegfaysdanknsgitwte
evfreyirdpkakipgtkmifagvkdeqkvsdliayikqfnadgskk
>d1cs1a_ 3.57.1.3.2 Cystathionine gamma-synthase {Escherichia coli}
rkqatiavrsglnddeqygcvvppihlsstynftgfneprahdysrrgnptrdvvqrala
eleggagavltntgmsaihlvttvflkpgdllvaphdcyggsyrlfdslakrgcyrvlfv
dqgdeqalraalaekpklvlvespsnpllrvvdiakichlarevgavsvvdntflspalq
nplalgadlvlhsctxylnghsdvvagvviakdpdvvtelawwannigvtggafdsylll
rglrtlvprmelaqrnaqaivkylqtqplvkklyhpslpenqgheiaarqqkgfgamlsf
eldgdeqtlrrflgglslftlaeslggveslishaatmthagmapearaaagisetllri
stgiedgedliadlengfraankg
>d1cs1b_ 3.57.1.3.2 Cystathionine gamma-synthase {Escherichia coli}
rkqatiavrsglnddeqygcvvppihlsstynftgfneprahdysrrgnptrdvvqrala
eleggagavltntgmsaihlvttvflkpgdllvaphdcyggsyrlfdslakrgcyrvlfv
dqgdeqalraalaekpklvlvespsnpllrvvdiakichlarevgavsvvdntflspalq
nplalgadlvlhsctxylnghsdvvagvviakdpdvvtelawwannigvtggafdsylll
rglrtlvprmelaqrnaqaivkylqtqplvkklyhpslpenqgheiaarqqkgfgamlsf
eldgdeqtlrrflgglslftlaeslggveslishaatmthagmapearaaagisetllri
stgiedgedliadlengfraankg
>d1cs1c_ 3.57.1.3.2 Cystathionine gamma-synthase {Escherichia coli}
rkqatiavrsglnddeqygcvvppihlsstynftgfneprahdysrrgnptrdvvqrala
eleggagavltntgmsaihlvttvflkpgdllvaphdcyggsyrlfdslakrgcyrvlfv
dqgdeqalraalaekpklvlvespsnpllrvvdiakichlarevgavsvvdntflspalq
nplalgadlvlhsctxylnghsdvvagvviakdpdvvtelawwannigvtggafdsylll
rglrtlvprmelaqrnaqaivkylqtqplvkklyhpslpenqgheiaarqqkgfgamlsf
eldgdeqtlrrflgglslftlaeslggveslishaatmthagmapearaaagisetllri
stgiedgedliadlengfraankg
>d1cs1d_ 3.57.1.3.2 Cystathionine gamma-synthase {Escherichia coli}
rkqatiavrsglnddeqygcvvppihlsstynftgfneprahdysrrgnptrdvvqrala
eleggagavltntgmsaihlvttvflkpgdllvaphdcyggsyrlfdslakrgcyrvlfv
dqgdeqalraalaekpklvlvespsnpllrvvdiakichlarevgavsvvdntflspalq
nplalgadlvlhsctxylnghsdvvagvviakdpdvvtelawwannigvtggafdsylll
rglrtlvprmelaqrnaqaivkylqtqplvkklyhpslpenqgheiaarqqkgfgamlsf
eldgdeqtlrrflgglslftlaeslggveslishaatmthagmapearaaagisetllri
stgiedgedliadlengfraankg
>d1cs3a_ 4.35.1.1.1 Promyelocytic leukemia zinc finger (PLZF) protein BTB domain {Human (Homo sapiens)}
gmiqlqnpshptgllckanqmrlagtlcdvvimvdsqefhahrtvlactskmfeilfhrn
sqhytldflspktfqqileyaytatlqakaedlddllyaaeileieyleeqclkml
>d1cs8a_ 4.3.1.1.12 (Pro)cathepsin L {Human (Homo sapiens)}
sltfdhsleaqwtkwkamhnrlygmneegwrravweknmkmielhnqeyregkhsftmam
nafgdmtseefrqvmngfqnrkprkgkvfqeplfyeaprsvdwrekgyvtpvknqgqcgs
xwafsatgalegqmfrktgrlislseqnlvdcsgpqgnegcngglmdyafqyvqdnggld
seesypyeateesckynpkysvandagfvdipkqekalmkavatvgpisvaidaghesfl
fykegiyfepdcssedmdhgvlvvgygfestesdnnkywlvknswgeewgmggyvkmakd
rrnhcgiasaasyptv
>e1csb.1a 4.3.1.1.10 (Pro)cathepsin B {Human (Homo sapiens)}
lpasfdareqwpqcptikeirdqgscgscwafgaveaisdricihtn
>e1csb.1b 4.3.1.1.10 (Pro)cathepsin B {Human (Homo sapiens)}
vsvevsaedlltccgsmcgdgcnggypaeawnfwtrkglvsgglyeshvgcrpysippce
hhvngsrppctgegdtpkcskicepgysptykqdkhygynsysvsnsekdimaeiykngp
vegafsvysdfllyksgvyqhvtgemmgghairilgwgvengtpywlvanswntdwgdng
ffkilrgqdhcgiesevvagiprtd
>e1csb.2d 4.3.1.1.10 (Pro)cathepsin B {Human (Homo sapiens)}
lpasfdareqwpqcptikeirdqgscgscwafgaveaisdricihtn
>e1csb.2e 4.3.1.1.10 (Pro)cathepsin B {Human (Homo sapiens)}
vsvevsaedlltccgsmcgdgcnggypaeawnfwtrkglvsgglyeshvgcrpysippce
hhvngsrppctgegdtpkcskicepgysptykqdkhygynsysvsnsekdimaeiykngp
vegafsvysdfllyksgvyqhvtgemmgghairilgwgvengtpywlvanswntdwgdng
ffkilrgqdhcgiesevvagiprtd
>d1csc__ 1.99.1.1.1 Citrate synthase {Chicken (Gallus gallus)}
asstnlkdvlaalipkeqariktfrqqhggtalgqitvdmsyggmrgmkglvyetsvldp
degirfrgfsipecqkllpkggxggeplpeglfwllvtgqiptgaqvswlskewakraal
pshvvtmldnfptnlhpmsqlsaaitalnsesnfarayaegilrtkywemvyesamdlia
klpcvaakiyrnlyragssigaidskldwshnftnmlgytdaqftelmrlyltihsdheg
gnvsahtshlvgsalsdpylsfaaamnglagplhglanqevlgwlaqlqkaxxxagadas
lrdyiwntlnsgrvvpgyghavlrktdprytcqrefalkhlpgdpmfklvaqlykivpnv
lleqgaaanpwpnvdahsgvllqyygmtemnyytvlfgvsralgvlaqliwsralgfple
rpksmstdglial
>d1csee_ 3.33.1.1.1 Subtilisin Carlsberg {Bacillus subtilis}
aqtvpygiplikadkvqaqgfkganvkvavldtgiqashpdlnvvggasfvageayntdg
nghgthvagtvaaldnttgvlgvapsvslyavkvlnssgsgsysgivsgiewattngmdv
inmslggasgstamkqavdnayargvvvvaaagnsgnsgstntigypakydsviavgavd
snsnrasfssvgaelevmapgagvystyptntyatlngtsmasphvagaaalilskhpnl
sasqvrnrlsstatylgssfyygkglinveaaaq
>d1csei_ 4.33.1.1.1 Eglin C {Leech (Hirudo medicinalis)}
ksfpevvgktvdqareyftlhypqynvyflpegspvtldlrynrvrvfynpgtnvvnhvp
hvg
>d1csga_ 1.27.1.2.2 Granulocyte-macrophage colony-stimulating factor (GM-CSF) {Human (Homo sapiens)}
spspstqpwehvnaiqearrllnlsrdtaaemnetvevisemfdlqeptclqtrlelykq
glrgsltklkgpltmmashykqhcpptpetscatqiitfesfkenlkdfllvipfdcwep
>d1csgb_ 1.27.1.2.2 Granulocyte-macrophage colony-stimulating factor (GM-CSF) {Human (Homo sapiens)}
spspstqpwehvnaiqearrllnlsrdtaaemnetvevisemfdlqeptclqtrlelykq
glrgsltklkgpltmmashykqhcpptpetscatqiitfesfkenlkdfllvipfdcwep
>d1csh__ 1.99.1.1.1 Citrate synthase {Chicken (Gallus gallus)}
stnlkdvlaslipkeqariktfrqqhgntavgqitvdmsyggmrgmkgliyetsvldpde
girfrgfsipecqkllpkagggeeplpeglfwllvtgqiptpeqvswvskewakraalps
hvvtmldnfptnlhpmsqlsaaitalnsesnfarayaeginrtkywefvyedamdliakl
pcvaakiyrnlyragssigaidskldwshnftnmlgytdpqftelmrlyltihsdheggn
vsahtshlvgsalsdpylsfaaamnglagplhglanqevllwlsqlqkdlgadasdeklr
dyiwntlnsgrvvpgyghavlrktdprytcqrefalkhlpsdpmfklvaqlykivpnvll
eqgkaknpwpnvdahsgvllqyygmtemnyytvlfgvsralgvlaqliwsralgfplerp
ksmstagleklsagg
>d1csi__ 1.99.1.1.1 Citrate synthase {Chicken (Gallus gallus)}
stnlkdvlaslipkeqariktfrqqhgntavgqitvdmsyggmrgmkgliyetsvldpde
girfrgfsipecqkllpkagggeeplpeglfwllvtgqiptpeqvswvskewakraalps
hvvtmldnfptnlhpmsqlsaaitalnsesnfarayaeginrtkywefvyedamdliakl
pcvaakiyrnlyragssigaidskldwshnftnmlgytdpqftelmrlyltihsdheggn
vsahtshlvgsalsdpylsfaaamnglagplhglanqevllwlsqlqkdlgadasdeklr
dyiwntlnsgrvvpgyghavlrktdprytcqrefalkhlpsdpmfklvaqlykivpnvll
eqgkaknpwpnvdahsgvllqyygmtemnyytvlfgvsralgvlaqliwsralgfplerp
ksmstagleklsagg
>d1cska_ 2.30.2.1.19 Src kinase, SH3 domain {Human (Homo sapiens)}
gteciakynfhgtaeqdlpfckgdvltivavtkdpnwykaknkvgregiipanyvqkr
>d1cskb_ 2.30.2.1.19 Src kinase, SH3 domain {Human (Homo sapiens)}
gteciakynfhgtaeqdlpfckgdvltivavtkdpnwykaknkvgregiipanyvqkr
>d1cskc_ 2.30.2.1.19 Src kinase, SH3 domain {Human (Homo sapiens)}
gteciakynfhgtaeqdlpfckgdvltivavtkdpnwykaknkvgregiipanyvqkr
>d1cskd_ 2.30.2.1.19 Src kinase, SH3 domain {Human (Homo sapiens)}
gteciakynfhgtaeqdlpfckgdvltivavtkdpnwykaknkvgregiipanyvqkr
>d1csma_ 1.120.1.2.1 Allosteric chorismate mutase {Baker's yeast (Saccharomyces cerevisiae)}
mdftkpetvlnlqnirdelvrmedsiifkfiershfatcpsvyeanhpgleipnfkgsfl
dwalsnleiahsrirrfespdetpffpdkiqksflpsinypqilapyapevnyndkikkv
yiekiipliskrdgddknnfgsvatrdieclqslsrrihfgkfvaeakfqsdiplytkli
kskdvegimknitnsaveekilerltkkaevygvdptnesgerriipeylvkiykeivip
itkeveveyllrrlee
>d1csmb_ 1.120.1.2.1 Allosteric chorismate mutase {Baker's yeast (Saccharomyces cerevisiae)}
mdftkpetvlnlqnirdelvrmedsiifkfiershfatcpsvyeanhpgleipnfkgsfl
dwalsnleiahsrirrfespdetpffpdkiqksflpsinypqilapyapevnyndkikkv
yiekiipliskrdgddknnfgsvatrdieclqslsrrihfgkfvaeakfqsdiplytkli
kskdvegimknitnsaveekilerltkkaevygvdptnesgerriipeylvkiykeivip
itkeveveyllrrlee
>d1csn__ 4.117.1.1.17 Casein kinase-1, CK1 {Schizosaccharomyces pombe}
nvvgvhykvgrrigegsfgvifegtnllnnqqvaikfeprrsdapqlrdeyrtykllagc
tgipnvyyfgqeglhnvlvidllgpsledlldlcgrkfsvktvamaakqmlarvqsihek
slvyrdikpdnfligrpnsknanmiyvvdfgmvkfyrdpvtkqhipyrekknlsgtarym
sinthlgreqsrrddlealghvfmyflrgslpwqglkaatnkqkyerigekkqstplrel
cagfpeefykymhyarnlafdatpdydylqglfskvlerlnttedenfdwnll
>d1csp__ 2.35.4.5.2 Major cold shock protein {Bacillus subtilis}
mlegkvkwfnsekgfgfievegqddvfvhfsaiqgegfktleegqavsfeivegnrgpqa
anvtkea
>d1csq__ 2.35.4.5.2 Major cold shock protein {Bacillus subtilis}
mlegkvkwfnsekgfgfievegqddvfvhfsaiqgegfktleegqavsfeivegnrgpqa
anvtkea
>d1csr__ 1.99.1.1.1 Citrate synthase {Chicken (Gallus gallus)}
stnlkdvlaslipkeqariktfrqqhgntavgqitvdmsyggmrgmkgliyetsvldpde
girfrgfsipecqkllpkagggeeplpeglfwllvtgqiptpeqvswvskewakraalps
hvvtmldnfptnlhpmsqlsaaitalnsesnfarayaeginrtkywefvyedamdliakl
pcvaakiyrnlyragssigaidskldwshnftnmlgytdpqftelmrlyltihsdheggn
vsahtshlvgsalsdpylsfaaamnglagplhglanqevllwlsqlqkdlgadasdeklr
dyiwntlnsgrvvpgyghavlrktdprytcqrefalkhlpsdpmfklvaqlykivpnvll
eqgkaknpwpnvdahsgvllqyygmtemnyytvlfgvsralgvlaqliwsralgfplerp
ksmstagleklsagg
>d1css__ 1.99.1.1.1 Citrate synthase {Chicken (Gallus gallus)}
stnlkdvlaslipkeqariktfrqqhgntavgqitvdmsyggmrgmkgliyetsvldpde
girfrgfsipecqkllpkagggeeplpeglfwllvtgqiptpeqvswvskewakraalps
hvvtmldnfptnlhpmsqlsaaitalnsesnfarayaeginrtkywefvyedamdliakl
pcvaakiyrnlyragssigaidskldwshnftnmlgytdpqftelmrlyltihsdheggn
vsahtshlvgsalsdpylsfaaamnglagplhglanqevllwlsqlqkdlgadasdeklr
dyiwntlnsgrvvpgyghavlrktdprytcqrefalkhlpsdpmfklvaqlykivpnvll
eqgkaknpwpnvdahsgvllqyygmtemnyytvlfgvsralgvlaqliwsralgfplerp
ksmstagleklsagg
>d1csu__ 1.3.1.1.7 Mitochondrial cytochrome c {Baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdanikk
nvlwdennmseyltnpkkyipgtkmafggckkekdrndlitylkkate
>d1csv__ 1.3.1.1.7 Mitochondrial cytochrome c {Baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdanikk
nvlwdennmseyltnpkkyipgtkmafggfkkekdrndlitylkkate
>d1csw__ 1.3.1.1.7 Mitochondrial cytochrome c {Baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdanikk
nvlwdennmseyltnpkkyipgtkmafggmkkekdrndlitylkkate
>d1csx__ 1.3.1.1.7 Mitochondrial cytochrome c {Baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdanikk
nvlwdennmseyltnpkkyipgtkmafgglkkekdrndsitylkkate
>d1csya_ 4.72.1.1.13 Syk tyrosine kinase {Human (Homo sapiens)}
gsrrasvgshekmpwfhgkisreeseqivligsktngkflirardnngsyalcllhegkv
lhyridkdktgklsipegkkfdtlwqlvehysykadgllrvltvpcqkigtq
>d1csza_ 4.72.1.1.13 Syk tyrosine kinase {Human (Homo sapiens)}
gsrrasvgshekmpwfhgkisreeseqivligsktngkflirardnngsyalcllhegkv
lhyridkdktgklsipegkkfdtlwqlvehysykadgllrvltvpcqkigtq
>d1ct1d_ 2.35.2.1.3 Cholera toxin {Vibrio cholerae}
tpqnitdlcaeyhntqihtlndkifsyteslarkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1ct1e_ 2.35.2.1.3 Cholera toxin {Vibrio cholerae}
tpqnitdlcaeyhntqihtlndkifsyteslarkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1ct1f_ 2.35.2.1.3 Cholera toxin {Vibrio cholerae}
tpqnitdlcaeyhntqihtlndkifsyteslarkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1ct1g_ 2.35.2.1.3 Cholera toxin {Vibrio cholerae}
tpqnitdlcaeyhntqihtlndkifsyteslarkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1ct1h_ 2.35.2.1.3 Cholera toxin {Vibrio cholerae}
tpqnitdlcaeyhntqihtlndkifsyteslarkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1ct5a_ 3.1.5.2.1 "Hypothetical" protein ybl036c {Baker's yeast (Saccharomyces cerevisiae)}
tgitydedrktqliaqyesvrevvnaeaknvhvnenaskilllvvsklkpasdiqilydh
gvrefgenyvqeliekakllpddikwhfigglqtnkckdlakvpnlysvetidslkkakk
lnesrakfqpdcnpilcnvqintshedqksglnneaeifevidfflseeckyiklnglxt
igswnvshedskenrdfatlvewkkkidakfgtslklsxgxsadfreairqgtaevrigt
difg
>d1ctaa_ 1.42.1.5.1 Troponin C {Chicken (Gallus gallus)}
xkseeelanafrifdknadgyidieelgeilratg
>d1ctab_ 1.42.1.5.1 Troponin C {Chicken (Gallus gallus)}
xkseeelanafrifdknadgyidieelgeilratg
>d1ctda_ 1.42.1.5.1 Troponin C {Chicken (Gallus gallus)}
xkseeelanafrifdknadgyidieelgeilratg
>d1ctdb_ 1.42.1.5.1 Troponin C {Chicken (Gallus gallus)}
xkseeelanafrifdknadgyidieelgeilratg
>d1ctea_ 4.3.1.1.11 (Pro)cathepsin B {Rat (Rattus norvegicus)}
lpesfdareqwsncptiaqirdqgscgscwafgaveamsdricihtngrvnvevsaedll
tccgiqcgdgcnggypsgawnfwtrkglvsggvynshigclpytippcehhvngarppct
gegdtpkcnkmceagystsykedkhygytsysvsdsekeimaeiykngpvegaftvfsdf
ltyksgvykheagdvmgghairilgwgiengvpywlvanswnadwgdngffkilrgenhc
gieseivagiprt
>d1cteb_ 4.3.1.1.11 (Pro)cathepsin B {Rat (Rattus norvegicus)}
lpesfdareqwsncptiaqirdqgscgscwafgaveamsdricihtngrvnvevsaedll
tccgiqcgdgcnggypsgawnfwtrkglvsggvynshigclpytippcehhvngarppct
gegdtpkcnkmceagystsykedkhygytsysvsdsekeimaeiykngpvegaftvfsdf
ltyksgvykheagdvmgghairilgwgiengvpywlvanswnadwgdngffkilrgenhc
gieseivagiprt
>d1ctf__ 4.38.1.1.1 Ribosomal protein L7/12, C-terminal fragment {Escherichia coli}
efdvilkaagankvavikavrgatglglkeakdlvesapaalkegvskddaealkkalee
agaevevk
>d1cti__ 7.3.2.1.2 Trypsin inhibitor {Squash (Cucurbita maxima)}
rvcprilmeckkdsdclaecvclehgycg
>d1ctj__ 1.3.1.1.1 Cytochrome c6 (synonym: cytochrome c553) {Monoraphidium braunii}
eadlalgkavfdgncaachagggnnvipdhtlqkaaieqfldggfnieaivyqiengkga
mpawdgrldedeiagvaayvydqaagnkw
>d1ctl_1 7.33.1.3.1 (1-35) Cysteine-rich (intestinal) protein, CRP, CRIP {Chicken (Gallus gallus)}
maqkvggsdgcprcgqavyaaekvigagkswhksc
>d1ctl_2 7.33.1.3.1 (36-85) Cysteine-rich (intestinal) protein, CRP, CRIP {Chicken (Gallus gallus)}
frcakcgkslesttladkdgeiyckgcyaknfgpkgfgfgqgagalihsq
>d1ctm_1 2.2.6.1.1 (1-167,231-250) Cytochrome f, large domain {Turnip (Brassica rapa)}
ypifaqqnyenpreatgrivcanchlaskpvdievpqavlpdtvfeavvkipydmqlkqv
langkkgalnvgavlilpegfelappdrispemkekignlsfqnyrpnkknilvigpvpg
qkyseitfpilapdpatnkdvhflkypiyvggnrgrgqiypdgsksnXpnvggfgqgdae
ivlqdplr
>d1ctm_2 2.74.2.2.1 (168-230) Cytochrome f, small domain {Turnip (Brassica rapa)}
ntvynataggiiskilrkekggyeitivdasnerqvidiiprglellvsegesikldqpl
tsn
>d1ctn_1 2.1.1.5.13 (24-132) Chitinase A, N-terminal domain {Serratia marcescens}
aapgkptiawgntkfaivevdqaataynnlvkvknaadvsvswnlwngdtgttakillng
keawsgpstgssgtanfkvnkggryqmqvalcnadgctasdateivvad
>d1ctn_2 3.1.7.5.6 (133-443,517-561) Chitinase A, central domain {Serratia marcescens}
tdgshlaplkeplleknkpykqnsgkvvgsyfvewgvygrnftvdkipaqnlthllygfi
picggngindslkeiegsfqalqrscqgredfkisihdpfaalqkaqkgvtawddpykgn
fgqlmalkqahpdlkilpsiggwtlsdpfffmgdkvkrdrfvgsvkeflqtwkffdgvdi
dwefpggkganpnlgspqdgetyvllmkelramldqlstetgrkyeltsaisagkdkidk
vaynvaqnsmdhiflmsydfygafdlknlghqtalnapawkpdtayttvngvnallaqgv
kpgkivvgtamXdarsvqakgkyvldkqlgglfsweidadngdilnsmnaslgnsag
>d1ctn_3 4.23.3.1.1 (444-516) Chitinase A, insertion domain {Serratia marcescens}
ygrgwtgvngyqnnipftgtatgpvkgtwengivdyrqiagqfmsgewqytydataeapy
vfkpstgdlitfd
>d1cto__ 2.1.2.1.11 Granulocyte colony-stimulating factor (GC-SF) receptor {Mouse (Mus musculus)}
gssleppmlqaldigpdvvshqpgclwlswkpwkpseymeqecelryqpqlkganwtlvf
hlpsskdqfelcglhqapvytlqmrcirsslpgfwspwspglqlrptmk
>d1ctpe_ 4.117.1.1.3 cAMP-dependent PK, catalytic subunit {Pig (Sus scrofa)}
kkgseqesvkeflakakedflkkwenpaqntahldqferiktlgtgsfgrvmlvkhketg
nhfamkildkqkvvklkqiehtlnekrilqavnfpflvkleysfkdnsnlymvmeyvpgg
emfshlrrigrfsepharfyaaqivltfeylhsldliyrdlkpenllidqqgyiqvtdfg
fakrvkgrtwtlcgtpeylapeiilskgynkavdwwalgvliyemaagyppffadqpiqi
yekivsgkvrfpshfssdlkdllrnllqvdltkrfgnlkngvndiknhkwfattdwiaiy
qrkveapfipkfkgpgdtsnfddyeeeeirvsinekcgkefsef
>d1ctr__ 1.42.1.5.7 Calmodulin {Human (Homo sapiens)}
adqlteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgn
gtidfpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdee
vdemireadidgdgqvnyeefvqmmta
>d1cts__ 1.99.1.1.2 Citrate synthase {Pig (Sus scrofa)}
asstnlkdiladlipkeqariktfrqqhgntvvgqitvdmmyggmrgmkglvyetsvldp
degirfrgysipecqkmlpkakggeeplpeglfwllvtgqipteeqvswlskewakraal
pshvvtmldnfptnlhpmsqlsaaitalnsesnfarayaegihrtkyweliyedcmdlia
klpcvaakiyrnlyregssigaidskldwshnftnmlgytdaqftelmrlyltihsdheg
gnvsahtshlvgsalsdpylsfaaamnglagplhglanqevlvwltqlqkevgkdvsdek
lrdyiwntlnsgrvvpgyghavlrktdprytcqrefalkhlphdpmfklvaqlykivpnv
lleqgkaknpwpnvdahsgvllqyygmtemnyytvlfgvsralgvlaqliwsralgfple
rpksmstdgliklvdsk
>d1ctt_1 3.87.1.1.1 (1-150) Cytidine deaminase {Escherichia coli}
mhprfqtafaqladnlqsalepiladkyfpalltgeqvsslksatgldedalafallpla
aacartplsnfnvgaiargvsgtwyfganmefigatmqqtvhaeqsaishawlsgekala
aitvnytpcghcrqfmnelnsgldlrihlp
>d1ctt_2 3.87.1.1.1 (151-294) Cytidine deaminase {Escherichia coli}
greahalrdylpdafgpkdleiktllmdeqdhgyaltgdalsqaaiaaanrshmpysksp
sgvaleckdgrifsgsyaenaafnptlpplqgalillnlkgydypdiqravlaekadapl
iqwdatsatlkalgchsidrvlla
>d1ctu_1 3.87.1.1.1 (1-150) Cytidine deaminase {Escherichia coli}
mhprfqtafaqladnlqsalepiladkyfpalltgeqvsslksatgldedalafallpla
aacartplsnfnvgaiargvsgtwyfganmefigatmqqtvhaeqsaishawlsgekala
aitvnytpcghcrqfmnelnsgldlrihlp
>d1ctu_2 3.87.1.1.1 (151-294) Cytidine deaminase {Escherichia coli}
greahalrdylpdafgpkdleiktllmdeqdhgyaltgdalsqaaiaaanrshmpysksp
sgvaleckdgrifsgsyaenaafnptlpplqgalillnlkgydypdiqravlaekadapl
iqwdatsatlkalgchsidrvlla
>d1ctx__ 7.7.1.1.7 alpha-Cobratoxin {Cobra (Naja naja siamensis)}
ircfitpditskdcpnghvcytktwcdafcsirgkrvdlgcaatcptvktgvdiqccstd
ncnpfptrkrp
>d1cty__ 1.3.1.1.7 Mitochondrial cytochrome c {Baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdanikk
nvlwdennmsefltnpkkyipgtkmafgglkkekdrndlitylkkate
>d1ctz__ 1.3.1.1.7 Mitochondrial cytochrome c {Baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdanikk
nvlwdennmsefltnpkkyipgtkmafgglkkekdrndlitylkkate
>d1cu7a_ 2.41.1.2.1 Trypsin(ogen) {Bovine (Bos taurus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1cu8a_ 2.41.1.2.1 Trypsin(ogen) {Bovine (Bos taurus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1cu9a_ 2.41.1.2.1 Trypsin(ogen) {Bovine (Bos taurus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1cua__ 3.16.7.1.1 Cutinase {Fungus (Fusarium solani), subsp. Pisi}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcktgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1cub__ 3.16.7.1.1 Cutinase {Fungus (Fusarium solani), subsp. Pisi}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcktgdlvctgslivaaphlaygpdae
gpapefliekvravrgs
>d1cuc__ 3.16.7.1.1 Cutinase {Fungus (Fusarium solani), subsp. Pisi}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcktgdlvctgslivaaphlaygpdae
gpapefliekvravrgs
>d1cuda_ 3.16.7.1.1 Cutinase {Fungus (Fusarium solani), subsp. Pisi}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcktgdlvctgslivaaphlaygpdae
gpapefliekvravrgs
>d1cudb_ 3.16.7.1.1 Cutinase {Fungus (Fusarium solani), subsp. Pisi}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcktgdlvctgslivaaphlaygpdae
gpapefliekvravrgs
>d1cudc_ 3.16.7.1.1 Cutinase {Fungus (Fusarium solani), subsp. Pisi}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcktgdlvctgslivaaphlaygpdae
gpapefliekvravrgs
>d1cue__ 3.16.7.1.1 Cutinase {Fungus (Fusarium solani), subsp. Pisi}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggyslgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1cuf__ 3.16.7.1.1 Cutinase {Fungus (Fusarium solani), subsp. Pisi}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnlgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1cug__ 3.16.7.1.1 Cutinase {Fungus (Fusarium solani), subsp. Pisi}
ettrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcktgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1cuh__ 3.16.7.1.1 Cutinase {Fungus (Fusarium solani), subsp. Pisi}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdae
gpapefliekvravrgs
>d1cui__ 3.16.7.1.1 Cutinase {Fungus (Fusarium solani), subsp. Pisi}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggyaqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1cuj__ 3.16.7.1.1 Cutinase {Fungus (Fusarium solani), subsp. Pisi}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggycqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1cuk_1 1.5.1.1.1 (156-203) DNA helicase RuvA subunit, C-terminal domain {Escherichia coli}
tddaeqeavarlvalgykpqeasrmvskiarpdassetlirealraal
>d1cuk_2 1.61.6.1.1 (65-142) DNA helicase RuvA subunit, middle domain {Escherichia coli}
nkqertlfkeliktngvgpklalailsgmsaqqfvnavereevgalvklpgigkktaerl
ivemkdrfkglhgdlftp
>d1cuk_3 2.35.4.2.1 (1-64) DNA helicase RuvA subunit, N-terminal domain {Escherichia coli}
migrlrgiiiekqpplvlievggvgyevhmpmtcfyelpeagqeaivfthfvvredaqll
ygfn
>d1cuna1 1.7.1.1.2 (7-115) Spectrin {Chicken (Gallus gallus)}
mvhqffrdmddeeswikekkllvssedygrdltgvqnlrkkhkrleaelaahepaiqsvl
dtgkklsddntigkeeiqqrlaqfvdhwkelkqlaaargqrleesleyq
>d1cuna2 1.7.1.1.2 (116-219) Spectrin {Chicken (Gallus gallus)}
qfvanveeeeawinekmtlvasedygdtlaaiqgllkkheafetdftvhkdrvndvcang
edlikknnhhvenitakmkglkgkvsdlekaaaqrkakldensa
>d1cunb1 1.7.1.1.2 (7-115) Spectrin {Chicken (Gallus gallus)}
mvhqffrdmddeeswikekkllvssedygrdltgvqnlrkkhkrleaelaahepaiqsvl
dtgkklsddntigkeeiqqrlaqfvdhwkelkqlaaargqrleesleyq
>d1cunb2 1.7.1.1.2 (116-219) Spectrin {Chicken (Gallus gallus)}
qfvanveeeeawinekmtlvasedygdtlaaiqgllkkheafetdftvhkdrvndvcang
edlikknnhhvenitakmkglkgkvsdlekaaaqrkakldensa
>d1cunc1 1.7.1.1.2 (7-115) Spectrin {Chicken (Gallus gallus)}
mvhqffrdmddeeswikekkllvssedygrdltgvqnlrkkhkrleaelaahepaiqsvl
dtgkklsddntigkeeiqqrlaqfvdhwkelkqlaaargqrleesleyq
>d1cunc2 1.7.1.1.2 (116-219) Spectrin {Chicken (Gallus gallus)}
qfvanveeeeawinekmtlvasedygdtlaaiqgllkkheafetdftvhkdrvndvcang
edlikknnhhvenitakmkglkgkvsdlekaaaqrkakldensa
>d1cur__ 2.5.1.1.26 Rusticyanin {Thiobacillus ferrooxidans}
gtldttwkeatlpqvkamlekdtgkvsgdtvtysgktvhvvaaavlpgfpfpsfevhdkk
nptleipagatvdvtfintnkgfghsfditkkgppyavmpvidpivagtgfspvpkdgkf
gytdftwhptagtyyyvcqipghaatgmfgkivvk
>d1cus__ 3.16.7.1.1 Cutinase {Fungus (Fusarium solani), subsp. Pisi}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1cuu__ 3.16.7.1.1 Cutinase {Fungus (Fusarium solani), subsp. Pisi}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpcpefliekvravrgs
>d1cuv__ 3.16.7.1.1 Cutinase {Fungus (Fusarium solani), subsp. Pisi}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnflprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1cuwa_ 3.16.7.1.1 Cutinase {Fungus (Fusarium solani), subsp. Pisi}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratladnflprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgsliilaphfaygpdar
gpapefliekvravrgs
>d1cuwb_ 3.16.7.1.1 Cutinase {Fungus (Fusarium solani), subsp. Pisi}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratladnflprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgsliilaphfaygpdar
gpapefliekvravrgs
>d1cux__ 3.16.7.1.1 Cutinase {Fungus (Fusarium solani), subsp. Pisi}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatyiaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1cuy__ 3.16.7.1.1 Cutinase {Fungus (Fusarium solani), subsp. Pisi}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphfaygpdar
gpapefliekvravrgs
>d1cuz__ 3.16.7.1.1 Cutinase {Fungus (Fusarium solani), subsp. Pisi}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratggdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgsgivaaphlaygpdar
gpapefliekvravrg
>d1cv3a_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
mqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1cv8__ 4.3.1.1.15 Staphopain {Staphylococcus aureus}
neqyvnklenfkiretqgnngwcagytmsallnatyntnkyhaeavmrflhpnlqgqqfq
ftgltpremiyfgqtqgrspqllnrmttynevdnltknnkgiailgsrvesrngmhagha
mavvgnaklnngqeviiiwnpwdngfmtqdaknnvipvsngdhyqwyssiygy
>d1cva__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslvtppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1cvb__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslvtppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1cvc__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfdfhwgsldgqgsehtvdkkkyaaelhlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1cvd__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelclvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1cve__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaeldlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1cvf__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfafhwgsldgqgsehtvdkkkyaaelhlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1cvh__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfhfcwgsldgqgsehtvdkkkyaaelhlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1cvia_ 3.50.1.2.2 Acid phosphatase {Human (Homo sapiens)}
kelkfvtlvfrhgdrspidtfptdpikesswpqgfgqltqlgmeqhyelgeyirkryrkf
lnesykheqvyirstdvdrtlmsamtnlaalfppegvsiwnpillwqpipvhtvplsedq
llylpfrncprfqelesetlkseefqkrlhpykdfiatlgklsglhgqdlfgiwskvydp
lycesvhnftlpswatedtmtklrelselsllslygihkqkeksrlqggvlvneilnhmk
ratqipsykklimysahdttvsglqmaldvyngllppyaschltelyfekgeyfvemyyr
netqhepyplmlpgcspscplerfaelvgpvipqdwstecmt
>d1cvib_ 3.50.1.2.2 Acid phosphatase {Human (Homo sapiens)}
kelkfvtlvfrhgdrspidtfptdpikesswpqgfgqltqlgmeqhyelgeyirkryrkf
lnesykheqvyirstdvdrtlmsamtnlaalfppegvsiwnpillwqpipvhtvplsedq
llylpfrncprfqelesetlkseefqkrlhpykdfiatlgklsglhgqdlfgiwskvydp
lycesvhnftlpswatedtmtklrelselsllslygihkqkeksrlqggvlvneilnhmk
ratqipsykklimysahdttvsglqmaldvyngllppyaschltelyfekgeyfvemyyr
netqhepyplmlpgcspscplerfaelvgpvipqdwstecmt
>d1cvic_ 3.50.1.2.2 Acid phosphatase {Human (Homo sapiens)}
kelkfvtlvfrhgdrspidtfptdpikesswpqgfgqltqlgmeqhyelgeyirkryrkf
lnesykheqvyirstdvdrtlmsamtnlaalfppegvsiwnpillwqpipvhtvplsedq
llylpfrncprfqelesetlkseefqkrlhpykdfiatlgklsglhgqdlfgiwskvydp
lycesvhnftlpswatedtmtklrelselsllslygihkqkeksrlqggvlvneilnhmk
ratqipsykklimysahdttvsglqmaldvyngllppyaschltelyfekgeyfvemyyr
netqhepyplmlpgcspscplerfaelvgpvipqdwstecmt
>d1cvid_ 3.50.1.2.2 Acid phosphatase {Human (Homo sapiens)}
kelkfvtlvfrhgdrspidtfptdpikesswpqgfgqltqlgmeqhyelgeyirkryrkf
lnesykheqvyirstdvdrtlmsamtnlaalfppegvsiwnpillwqpipvhtvplsedq
llylpfrncprfqelesetlkseefqkrlhpykdfiatlgklsglhgqdlfgiwskvydp
lycesvhnftlpswatedtmtklrelselsllslygihkqkeksrlqggvlvneilnhmk
ratqipsykklimysahdttvsglqmaldvyngllppyaschltelyfekgeyfvemyyr
netqhepyplmlpgcspscplerfaelvgpvipqdwstecmt
>d1cvja1 4.47.7.1.6 (11-90) Poly(A)-binding protein {Human (Homo sapiens)}
aslyvgdlhpdvteamlyekfspagpilsirvcrdmitrrslgyayvnfqqpadaerald
tmnfdvikgkpvrimwsqrd
>d1cvja2 4.47.7.1.6 (91-179) Poly(A)-binding protein {Human (Homo sapiens)}
pslrksgvgnifiknldksidnkalydtfsafgnilsckvvcdengskgygfvhfetqea
aeraiekmngmllndrkvfvgrfksrker
>d1cvjb1 4.47.7.1.6 (11-90) Poly(A)-binding protein {Human (Homo sapiens)}
aslyvgdlhpdvteamlyekfspagpilsirvcrdmitrrslgyayvnfqqpadaerald
tmnfdvikgkpvrimwsqrd
>d1cvjb2 4.47.7.1.6 (91-175) Poly(A)-binding protein {Human (Homo sapiens)}
pslrksgvgnifiknldksidnkalydtfsafgnilsckvvcdengskgygfvhfetqea
aeraiekmngmllndrkvfvgrfks
>d1cvjc1 4.47.7.1.6 (11-90) Poly(A)-binding protein {Human (Homo sapiens)}
aslyvgdlhpdvteamlyekfspagpilsirvcrdmitrrslgyayvnfqqpadaerald
tmnfdvikgkpvrimwsqrd
>d1cvjc2 4.47.7.1.6 (91-178) Poly(A)-binding protein {Human (Homo sapiens)}
pslrksgvgnifiknldksidnkalydtfsafgnilsckvvcdengskgygfvhfetqea
aeraiekmngmllndrkvfvgrfksrke
>d1cvjd1 4.47.7.1.6 (11-90) Poly(A)-binding protein {Human (Homo sapiens)}
aslyvgdlhpdvteamlyekfspagpilsirvcrdmitrrslgyayvnfqqpadaerald
tmnfdvikgkpvrimwsqrd
>d1cvjd2 4.47.7.1.6 (91-175) Poly(A)-binding protein {Human (Homo sapiens)}
pslrksgvgnifiknldksidnkalydtfsafgnilsckvvcdengskgygfvhfetqea
aeraiekmngmllndrkvfvgrfks
>d1cvje1 4.47.7.1.6 (11-90) Poly(A)-binding protein {Human (Homo sapiens)}
aslyvgdlhpdvteamlyekfspagpilsirvcrdmitrrslgyayvnfqqpadaerald
tmnfdvikgkpvrimwsqrd
>d1cvje2 4.47.7.1.6 (91-178) Poly(A)-binding protein {Human (Homo sapiens)}
pslrksgvgnifiknldksidnkalydtfsafgnilsckvvcdengskgygfvhfetqea
aeraiekmngmllndrkvfvgrfksrke
>d1cvjf1 4.47.7.1.6 (11-90) Poly(A)-binding protein {Human (Homo sapiens)}
aslyvgdlhpdvteamlyekfspagpilsirvcrdmitrrslgyayvnfqqpadaerald
tmnfdvikgkpvrimwsqrd
>d1cvjf2 4.47.7.1.6 (91-173) Poly(A)-binding protein {Human (Homo sapiens)}
pslrksgvgnifiknldksidnkalydtfsafgnilsckvvcdengskgygfvhfetqea
aeraiekmngmllndrkvfvgrf
>d1cvjg1 4.47.7.1.6 (11-90) Poly(A)-binding protein {Human (Homo sapiens)}
aslyvgdlhpdvteamlyekfspagpilsirvcrdmitrrslgyayvnfqqpadaerald
tmnfdvikgkpvrimwsqrd
>d1cvjg2 4.47.7.1.6 (91-175) Poly(A)-binding protein {Human (Homo sapiens)}
pslrksgvgnifiknldksidnkalydtfsafgnilsckvvcdengskgygfvhfetqea
aeraiekmngmllndrkvfvgrfks
>d1cvjh1 4.47.7.1.6 (11-90) Poly(A)-binding protein {Human (Homo sapiens)}
aslyvgdlhpdvteamlyekfspagpilsirvcrdmitrrslgyayvnfqqpadaerald
tmnfdvikgkpvrimwsqrd
>d1cvjh2 4.47.7.1.6 (91-175) Poly(A)-binding protein {Human (Homo sapiens)}
pslrksgvgnifiknldksidnkalydtfsafgnilsckvvcdengskgygfvhfetqea
ae
>d1cvl__ 3.59.1.15.4 Lipase {Chromobacterium viscosum}
adtyaatrypvilvhglagtdkfanvvdywygiqsdlqshgakvyvanlsgfqsddgpng
rgeqllayvkqvlaatgatkvnlighsqggltsryvaavapqlvasvttigtphrgsefa
dfvqdvlktdptglsstviaafvnvfgtlvssshntdqdalaalrtlttaqtatynrnfp
saglgapgscqtgaatetvggsqhllyswggtaiqptstvlgvtgatdtstgtldvanvt
dpstlallatgavminrasgqndglvsrcsslfgqvistsyhwnhldeinqllgvrgana
edpvavirthvnrlklqgv
>d1cvna_ 2.26.1.1.1 Concanavalin A {Jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1cvnb_ 2.26.1.1.1 Concanavalin A {Jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1cvnc_ 2.26.1.1.1 Concanavalin A {Jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1cvnd_ 2.26.1.1.1 Concanavalin A {Jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1cvo__ 7.7.1.1.6 Cardiotoxin V {Taiwan cobra (Naja naja atra)}
lkchntqlpfiyktcpegknlcfkatlkkfplkfpvkrgcadncpknsallkyvccstdk
cn
>d1cvwh_ 2.41.1.2.21 Coagulation factor VIIa {Human (Homo sapiens)}
ivggkvcpkgecpwqvlllvngaqlcggtlintiwvvsaahcfdkiknwrnliavlgehd
lsehdgdeqsrrvaqviipstyvpgttnhdiallrlhqpvvltdhvvplclpertfsert
lafvrfslvsgwgqlldrgatalelmvlnvprlmtqdclqqsrkvgdspniteymfcagy
sdgskdsckgdsggphathyrgtwyltgivswgqgcatvghfgvytrvsqyiewlqklmr
seprpgvllrapfp
>d1cvwl_ 7.3.11.1.3 Coagulation factor VIIa {Human (Homo sapiens)}
icvnenggceqycsdhtgtkrscrchegyslladgvsctptveypcgkipilekr
>d1cw1a_ 3.65.1.1.7 Isocitrate dehydrogenase, ICDH {Escherichia coli}
eskvvvpaqgkkitlqngklnvpenpiipyiegdgigvdvtpamlkvvdaavekaykger
kiswmeiytgekstqvygqdvwlpaetldlireyrvaikgplttpvgggirslnvalrqe
ldlyiclrpvryyqgtpspvkhpeltdmvifrensediyagiewkadsadaekvikflre
emgvkkirfpehcgigikpcseegtkrlvraaieyaiandrdsvtlvhmgnimkftegaf
kdwgyqlareefggelidggpwlkvknpntgkeivikdviadaflqqillrpaeydviac
mnlngdyisdalaaqvggigiapganigdecalfeathgtapkyagqdkvnpgsiilsae
mmlrhmgwteaadlivkgmegainaktvtydferlmdgakllkcsefgdaiienm
>d1cw3a_ 3.71.1.1.4 Aldehyde reductase (dehydrogenase), ALDH {Human (Homo sapiens), mitochondrial}
avpapnqqpevfcnqifinnewhdavsrktfptvnpstgevicqvaegdkedvdkavkaa
raafqlgspwrrmdashrgrllnrladlierdrtylaaletldngkpyvisylvdldmvl
kclryyagwadkyhgktipidgdffsytrhepvgvcgqiipwnfpllmqawklgpalatg
nvvvmkvaeqtpltalyvanlikeagfppgvvnivpgfgptagaaiashedvdkvaftgs
teigrviqvaagssnlkrvtlelggkspniimsdadmdwaveqahfalffnqgqcccags
rtfvqediydefversvaraksrvvgnpfdskteqgpqvdetqfkkilgyintgkqegak
llcgggiaadrgyfiqptvfgdvqdgmtiakeeifgpvmqilkfktieevvgrannstyg
laaavftkdldkanylsqalqagtvwvncydvfgaqspfggykmsgsgrelgeyglqayt
evktvtvkvpqkns
>d1cw3b_ 3.71.1.1.4 Aldehyde reductase (dehydrogenase), ALDH {Human (Homo sapiens), mitochondrial}
avpapnqqpevfcnqifinnewhdavsrktfptvnpstgevicqvaegdkedvdkavkaa
raafqlgspwrrmdashrgrllnrladlierdrtylaaletldngkpyvisylvdldmvl
kclryyagwadkyhgktipidgdffsytrhepvgvcgqiipwnfpllmqawklgpalatg
nvvvmkvaeqtpltalyvanlikeagfppgvvnivpgfgptagaaiashedvdkvaftgs
teigrviqvaagssnlkrvtlelggkspniimsdadmdwaveqahfalffnqgqcccags
rtfvqediydefversvaraksrvvgnpfdskteqgpqvdetqfkkilgyintgkqegak
llcgggiaadrgyfiqptvfgdvqdgmtiakeeifgpvmqilkfktieevvgrannstyg
laaavftkdldkanylsqalqagtvwvncydvfgaqspfggykmsgsgrelgeyglqayt
evktvtvkvpqkns
>d1cw3c_ 3.71.1.1.4 Aldehyde reductase (dehydrogenase), ALDH {Human (Homo sapiens), mitochondrial}
avpapnqqpevfcnqifinnewhdavsrktfptvnpstgevicqvaegdkedvdkavkaa
raafqlgspwrrmdashrgrllnrladlierdrtylaaletldngkpyvisylvdldmvl
kclryyagwadkyhgktipidgdffsytrhepvgvcgqiipwnfpllmqawklgpalatg
nvvvmkvaeqtpltalyvanlikeagfppgvvnivpgfgptagaaiashedvdkvaftgs
teigrviqvaagssnlkrvtlelggkspniimsdadmdwaveqahfalffnqgqcccags
rtfvqediydefversvaraksrvvgnpfdskteqgpqvdetqfkkilgyintgkqegak
llcgggiaadrgyfiqptvfgdvqdgmtiakeeifgpvmqilkfktieevvgrannstyg
laaavftkdldkanylsqalqagtvwvncydvfgaqspfggykmsgsgrelgeyglqayt
evktvtvkvpqkns
>d1cw3d_ 3.71.1.1.4 Aldehyde reductase (dehydrogenase), ALDH {Human (Homo sapiens), mitochondrial}
avpapnqqpevfcnqifinnewhdavsrktfptvnpstgevicqvaegdkedvdkavkaa
raafqlgspwrrmdashrgrllnrladlierdrtylaaletldngkpyvisylvdldmvl
kclryyagwadkyhgktipidgdffsytrhepvgvcgqiipwnfpllmqawklgpalatg
nvvvmkvaeqtpltalyvanlikeagfppgvvnivpgfgptagaaiashedvdkvaftgs
teigrviqvaagssnlkrvtlelggkspniimsdadmdwaveqahfalffnqgqcccags
rtfvqediydefversvaraksrvvgnpfdskteqgpqvdetqfkkilgyintgkqegak
llcgggiaadrgyfiqptvfgdvqdgmtiakeeifgpvmqilkfktieevvgrannstyg
laaavftkdldkanylsqalqagtvwvncydvfgaqspfggykmsgsgrelgeyglqayt
evktvtvkvpqkns
>d1cw3e_ 3.71.1.1.4 Aldehyde reductase (dehydrogenase), ALDH {Human (Homo sapiens), mitochondrial}
avpapnqqpevfcnqifinnewhdavsrktfptvnpstgevicqvaegdkedvdkavkaa
raafqlgspwrrmdashrgrllnrladlierdrtylaaletldngkpyvisylvdldmvl
kclryyagwadkyhgktipidgdffsytrhepvgvcgqiipwnfpllmqawklgpalatg
nvvvmkvaeqtpltalyvanlikeagfppgvvnivpgfgptagaaiashedvdkvaftgs
teigrviqvaagssnlkrvtlelggkspniimsdadmdwaveqahfalffnqgqcccags
rtfvqediydefversvaraksrvvgnpfdskteqgpqvdetqfkkilgyintgkqegak
llcgggiaadrgyfiqptvfgdvqdgmtiakeeifgpvmqilkfktieevvgrannstyg
laaavftkdldkanylsqalqagtvwvncydvfgaqspfggykmsgsgrelgeyglqayt
evktvtvkvpqkns
>d1cw3f_ 3.71.1.1.4 Aldehyde reductase (dehydrogenase), ALDH {Human (Homo sapiens), mitochondrial}
avpapnqqpevfcnqifinnewhdavsrktfptvnpstgevicqvaegdkedvdkavkaa
raafqlgspwrrmdashrgrllnrladlierdrtylaaletldngkpyvisylvdldmvl
kclryyagwadkyhgktipidgdffsytrhepvgvcgqiipwnfpllmqawklgpalatg
nvvvmkvaeqtpltalyvanlikeagfppgvvnivpgfgptagaaiashedvdkvaftgs
teigrviqvaagssnlkrvtlelggkspniimsdadmdwaveqahfalffnqgqcccags
rtfvqediydefversvaraksrvvgnpfdskteqgpqvdetqfkkilgyintgkqegak
llcgggiaadrgyfiqptvfgdvqdgmtiakeeifgpvmqilkfktieevvgrannstyg
laaavftkdldkanylsqalqagtvwvncydvfgaqspfggykmsgsgrelgeyglqayt
evktvtvkvpqkns
>d1cw3g_ 3.71.1.1.4 Aldehyde reductase (dehydrogenase), ALDH {Human (Homo sapiens), mitochondrial}
avpapnqqpevfcnqifinnewhdavsrktfptvnpstgevicqvaegdkedvdkavkaa
raafqlgspwrrmdashrgrllnrladlierdrtylaaletldngkpyvisylvdldmvl
kclryyagwadkyhgktipidgdffsytrhepvgvcgqiipwnfpllmqawklgpalatg
nvvvmkvaeqtpltalyvanlikeagfppgvvnivpgfgptagaaiashedvdkvaftgs
teigrviqvaagssnlkrvtlelggkspniimsdadmdwaveqahfalffnqgqcccags
rtfvqediydefversvaraksrvvgnpfdskteqgpqvdetqfkkilgyintgkqegak
llcgggiaadrgyfiqptvfgdvqdgmtiakeeifgpvmqilkfktieevvgrannstyg
laaavftkdldkanylsqalqagtvwvncydvfgaqspfggykmsgsgrelgeyglqayt
evktvtvkvpqkns
>d1cw3h_ 3.71.1.1.4 Aldehyde reductase (dehydrogenase), ALDH {Human (Homo sapiens), mitochondrial}
avpapnqqpevfcnqifinnewhdavsrktfptvnpstgevicqvaegdkedvdkavkaa
raafqlgspwrrmdashrgrllnrladlierdrtylaaletldngkpyvisylvdldmvl
kclryyagwadkyhgktipidgdffsytrhepvgvcgqiipwnfpllmqawklgpalatg
nvvvmkvaeqtpltalyvanlikeagfppgvvnivpgfgptagaaiashedvdkvaftgs
teigrviqvaagssnlkrvtlelggkspniimsdadmdwaveqahfalffnqgqcccags
rtfvqediydefversvaraksrvvgnpfdskteqgpqvdetqfkkilgyintgkqegak
llcgggiaadrgyfiqptvfgdvqdgmtiakeeifgpvmqilkfktieevvgrannstyg
laaavftkdldkanylsqalqagtvwvncydvfgaqspfggykmsgsgrelgeyglqayt
evktvtvkvpqkns
>d1cw4a_ 3.65.1.1.7 Isocitrate dehydrogenase, ICDH {Escherichia coli}
eskvvvpaqgkkitlqngklnvpenpiipyiegdgigvdvtpamlkvvdaavekaykger
kiswmeiytgekstqvygqdvwlpaetldlireyrvaikgplttpvgggirslnvalrqe
ldlyiclrpvryyqgtpspvkhpeltdmvifrensediyagiewkadsadaekvikflre
emgvkkirfpehcgigikpcseegtkrlvraaieyaiandrdsvtlvhmgnimkftegaf
kdwgyqlareefggelidggpwlkvknpntgkeivikdviadaflqqillrpaeydviac
mnlngdyisdalaaqvggigiapganigdecalfeathgtapkyagqdkvnpgsiilsae
mmlrhmgwteaadlivkgmegainaktvtydferlmdgakllkcsefgdaiienm
>d1cw7a_ 3.65.1.1.7 Isocitrate dehydrogenase, ICDH {Escherichia coli}
eskvvvpaqgkkitlqngklnvpenpiipyiegdgigvdvtpamlkvvdaavekaykger
kiswmeiytgekstqvygqdvwlpaetldlireyrvaikgplttpvgggirslnvalrqe
ldlyiclrpvryyqgtpspvkhpeltdmvifrensediyagiewkadsadaekvikflre
emgvkkirfpehcgigikpcseegtkrlvraaieyaiandrdsvtlvhkgnimkftegaf
kdwgyqlareefggelidggpwlkvknpntgkeivikdviadaflqqillrpaeydviac
mnlngdyisdalaaqvggigiapganigdecalfeathgtapayagqdkvnpgsiilsae
mmlrhmgwteaadlivkgmegainaktvtydferlmdgakllkcsefgdaiienm
>d1cwaa_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
mvnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgf
mcqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictakte
wldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1cwba_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
mvnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgf
mcqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictakte
wldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1cwca_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
mvnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgf
mcqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictakte
wldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1cwdl_ 4.72.1.1.1 p56-lck tyrosine kinase {Human (Homo sapiens)}
gswffknlsrkdaerqllapgnthgsfliresestagsfslsvrdfdqnqgevvkhykir
nldnggfyispritfpglhelvrhytnasdglctrlsr
>d1cwea_ 4.72.1.1.1 p56-lck tyrosine kinase {Human (Homo sapiens)}
gswffknlsrkdaerqllapgnthgsfliresestagsfslsvrdfdqnqgevvkhykir
nldnggfyispritfpglhelvrhytnasdglctrlsr
>d1cwec_ 4.72.1.1.1 p56-lck tyrosine kinase {Human (Homo sapiens)}
gswffknlsrkdaerqllapgnthgsfliresestagsfslsvrdfdqnqgevvkhykir
nldnggfyispritfpglhelvrhytnasdglctrlsr
>d1cwfa_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
mvnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgf
mcqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictakte
wldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1cwha_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
mvnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgf
mcqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictakte
wldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1cwia_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
mvnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgf
mcqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictakte
wldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1cwja_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
mvnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgf
mcqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictakte
wldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1cwka_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
mvnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgf
mcqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictakte
wldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1cwla_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
mvnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgf
mcqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictakte
wldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1cwma_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
mvnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgf
mcqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictakte
wldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1cwn__ 3.1.6.1.5 Aldose reductase (aldehyde reductase) {Porcine (Sus scrofa)}
aascvllhtgqkmpliglgtwksepgqvkaaikyaltvgyrhidcaaiygneleigealt
etvgpgkavpreelfvtsklwntkhhpedvepalrktladlqleyldlylmhwpyaferg
dnpfpknadgtirydathykdtwkalealvakglvralglsnfssrqiddvlsvasvrpa
vlqvechpylaqneliahcqarglevtaysplgssdrawrdpnepvlleepvvqalaeky
nrspaqillrwqvqrkvicipksvtpsripqniqvfdftfspeemkqldalnknlrfivp
mltvdgkrvprdaghplypfndpy
>d1cwoa_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
mvnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgf
mcqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictakte
wldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1cwpa_ 2.9.1.2.9 Cowpea chlorotic mottle virus {Host: cowpea (Vigna unguiculta), (L.)}
kaikawtgysvskwtascaaaeakvtsaitislpnelssernkqlkvgrvllwlgllpsv
sgtvkscvtetqttaaasfqvalavadnskdvvaamypeafkgitleqlaadltiylyss
aaltegdvivhlevehvrptfddsftpvy
>d1cwpb_ 2.9.1.2.9 Cowpea chlorotic mottle virus {Host: cowpea (Vigna unguiculta), (L.)}
vvqpvivepiasgqgkaikawtgysvskwtascaaaeakvtsaitislpnelssernkql
kvgrvllwlgllpsvsgtvkscvtetqttaaasfqvalavadnskdvvaamypeafkgit
leqlaadltiylyssaaltegdvivhlevehvrptfddsftpvy
>d1cwpc_ 2.9.1.2.9 Cowpea chlorotic mottle virus {Host: cowpea (Vigna unguiculta), (L.)}
vvqpvivepiasgqgkaikawtgysvskwtascaaaeakvtsaitislpnelssernkql
kvgrvllwlgllpsvsgtvkscvtetqttaaasfqvalavadnskdvvaamypeafkgit
leqlaadltiylyssaaltegdvivhlevehvrptfddsftpvy
>d1cwqa_ 6.2.1.1.2 Bacteriorhodopsin {Halobacterium salinarium}
aqitgrpewiwlalgtalmglgtlyflvkgmgvsdpdakkfyaittlvpaiaftmylsml
lgygltmvpfggeqnpiywaryadwlfttplllldlallvdadqgtilalvgadgimigt
glvgaltkvysyrfvwwaistaamlyilyvlffgftskaesmrpevastfkvlrnvtvvl
wsaypvvwligsegagivplnietllfmvldvsakvgfglillrsraifgeaeapeps
>d1cwqb_ 6.2.1.1.2 Bacteriorhodopsin {Halobacterium salinarium}
aqitgrpewiwlalgtalmglgtlyflvkgmgvsdpdakkfyaittlvpaiaftmylsml
lgygltmvpfggeqnpiywaryadwlfttplllldlallvdadqgtilalvgadgimigt
glvgaltkvysyrfvwwaistaamlyilyvlffgftskaesmrpevastfkvlrnvtvvl
wsaypvvwligsegagivplnietllfmvldvsakvgfglillrsraifgeaeapeps
>d1cwua_ 3.2.1.2.13 Enoyl-ACP reductase {Oil seed rape (Brassica napus)}
lpidlrgkrafiagiaddngygwavakslaaagaeilvgtwvpalnifetslrrgkfdqs
rvlpdgslmeikkvypldavfdnpedvpedvkankryagssnwtvqeaaecvrqdfgsid
ilvhslgngpevskplletsrkgylaaisassysfvsllshflpimnpggasisltyias
eriipgygggmssakaalesdtrvlafeagrkqnirvntisagplgsraakaigfidtmi
eysynnapiqktltadevgnaaaflvsplasaitgatiyvdnglnsmgvaldspvf
>d1cwub_ 3.2.1.2.13 Enoyl-ACP reductase {Oil seed rape (Brassica napus)}
lpidlrgkrafiagiaddngygwavakslaaagaeilvgtwvpalnifetslrrgkfdqs
rvlpdgslmeikkvypldavfdnpedvpedvkankryagssnwtvqeaaecvrqdfgsid
ilvhslgngpevskplletsrkgylaaisassysfvsllshflpimnpggasisltyias
eriipgygggmssakaalesdtrvlafeagrkqnirvntisagplgsraakaigfidtmi
eysynnapiqktltadevgnaaaflvsplasaitgatiyvdnglnsmgvaldspvf
>d1cwva1 2.1.13.1.2 (503-596) Invasin {(Yersinia pseudotuberculosis)}
ltltaavigdgapangktaitveftvadfegkplagqevvittnngalpnkitektdang
varialtnttdgvtvvtaevegqrqsvdthfvkg
>d1cwva2 2.1.13.1.2 (597-692) Invasin {(Yersinia pseudotuberculosis)}
tiaadkstlaavptsiiadglmastitlelkdtygdpqaganvafdttlgnmgvitdhnd
gtysapltsttlgvatvtvkvdgaafsvpsvtvnft
>d1cwva3 2.1.13.1.2 (693-795) Invasin {(Yersinia pseudotuberculosis)}
adpipdagrssftvstpdiladgtmsstlsfvpvdknghfisgmqglsftqngvpvsisp
iteqpdsytatvvgnsvgdvtitpqvdtlilstlqkkislfpv
>d1cwva4 2.1.13.1.2 (796-886) Invasin {(Yersinia pseudotuberculosis)}
ptltgilvngqnfatdkgfpktifknatfqlqmdndvanntqyewsssftpnvsvndqgq
vtityqtysevavtakskkfpsysvsyrfyp
>d1cwva5 4.139.1.3.2 (887-986) Invasin {(Yersinia pseudotuberculosis)}
nrwiydggrslvssleasrqcqgsdmsavlessratngtrapdgtlwgewgsltayssdw
qsgeywvkktstdfetmnmdtgalqpgpaylafplcalsi
>d1cx0a_ 4.47.7.1.2 Splicesomal U1A protein {Human (Homo sapiens)}
petrpnhtiyinnlnekikkdelkkslhaifsrfgqildilvsrslkxrgqafvifkevs
satnalrsxqgfpfydkpxriqyaktdsdiiakxa
>d1cx2a1 1.90.1.2.4 (74-583) Prostaglandin H2 synthase-1 {Mouse (Mus musculus)}
fltriklllkptpntvhyilthfkgvwnivnnipflrslimkyvltsrsylidspptynv
hygyksweafsnlsyytralppvaddcptpmgvkgnkelpdskevlekvllrrefipdpq
gsnmmfaffaqhfthqffktdhkrgpgftrglghgvdlnhiygetldrqhklrlfkdgkl
kyqviggevypptvkdtqvemiypphipenlqfavgqevfglvpglmmyatiwlrehqrv
cdilkqehpewgdeqlfqtskliligetikiviedyvqhlsgyhfklkfdpellfnqqfq
yqnriasefntlyhwhpllpdtfniedqeysfkqflynnsillehgltqfvesftrqiag
rvaggrnvpiavqavakasidqsremkyqslneyrkrfslkpytsfeeltgekemaaelk
alysdidvmelypallvekprpdaifgetmvelgapfslkglmgnpicspqywkpstfgg
evgfkiintasiqslicnnvkgcpftsfnvq
>d1cx2a2 7.3.11.1.10 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Mouse (Mus musculus)}
anpccsnpcqnrgecmstgfdqykcdctrtgfygencttpe
>d1cx2b1 1.90.1.2.4 (74-583) Prostaglandin H2 synthase-1 {Mouse (Mus musculus)}
fltriklllkptpntvhyilthfkgvwnivnnipflrslimkyvltsrsylidspptynv
hygyksweafsnlsyytralppvaddcptpmgvkgnkelpdskevlekvllrrefipdpq
gsnmmfaffaqhfthqffktdhkrgpgftrglghgvdlnhiygetldrqhklrlfkdgkl
kyqviggevypptvkdtqvemiypphipenlqfavgqevfglvpglmmyatiwlrehqrv
cdilkqehpewgdeqlfqtskliligetikiviedyvqhlsgyhfklkfdpellfnqqfq
yqnriasefntlyhwhpllpdtfniedqeysfkqflynnsillehgltqfvesftrqiag
rvaggrnvpiavqavakasidqsremkyqslneyrkrfslkpytsfeeltgekemaaelk
alysdidvmelypallvekprpdaifgetmvelgapfslkglmgnpicspqywkpstfgg
evgfkiintasiqslicnnvkgcpftsfnvq
>d1cx2b2 7.3.11.1.10 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Mouse (Mus musculus)}
anpccsnpcqnrgecmstgfdqykcdctrtgfygencttpe
>d1cx2c1 1.90.1.2.4 (74-583) Prostaglandin H2 synthase-1 {Mouse (Mus musculus)}
fltriklllkptpntvhyilthfkgvwnivnnipflrslimkyvltsrsylidspptynv
hygyksweafsnlsyytralppvaddcptpmgvkgnkelpdskevlekvllrrefipdpq
gsnmmfaffaqhfthqffktdhkrgpgftrglghgvdlnhiygetldrqhklrlfkdgkl
kyqviggevypptvkdtqvemiypphipenlqfavgqevfglvpglmmyatiwlrehqrv
cdilkqehpewgdeqlfqtskliligetikiviedyvqhlsgyhfklkfdpellfnqqfq
yqnriasefntlyhwhpllpdtfniedqeysfkqflynnsillehgltqfvesftrqiag
rvaggrnvpiavqavakasidqsremkyqslneyrkrfslkpytsfeeltgekemaaelk
alysdidvmelypallvekprpdaifgetmvelgapfslkglmgnpicspqywkpstfgg
evgfkiintasiqslicnnvkgcpftsfnvq
>d1cx2c2 7.3.11.1.10 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Mouse (Mus musculus)}
anpccsnpcqnrgecmstgfdqykcdctrtgfygencttpe
>d1cx2d1 1.90.1.2.4 (74-583) Prostaglandin H2 synthase-1 {Mouse (Mus musculus)}
fltriklllkptpntvhyilthfkgvwnivnnipflrslimkyvltsrsylidspptynv
hygyksweafsnlsyytralppvaddcptpmgvkgnkelpdskevlekvllrrefipdpq
gsnmmfaffaqhfthqffktdhkrgpgftrglghgvdlnhiygetldrqhklrlfkdgkl
kyqviggevypptvkdtqvemiypphipenlqfavgqevfglvpglmmyatiwlrehqrv
cdilkqehpewgdeqlfqtskliligetikiviedyvqhlsgyhfklkfdpellfnqqfq
yqnriasefntlyhwhpllpdtfniedqeysfkqflynnsillehgltqfvesftrqiag
rvaggrnvpiavqavakasidqsremkyqslneyrkrfslkpytsfeeltgekemaaelk
alysdidvmelypallvekprpdaifgetmvelgapfslkglmgnpicspqywkpstfgg
evgfkiintasiqslicnnvkgcpftsfnvq
>d1cx2d2 7.3.11.1.10 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Mouse (Mus musculus)}
anpccsnpcqnrgecmstgfdqykcdctrtgfygencttpe
>d1cx8a1 1.51.2.1.1 (609-760) Transferrin receptor ectodomain, C-terminal domain {Human (Homo sapiens)}
ldyeeynsqllsfvrdlnqyradikemglslqwlysargdffratsrlttdfgnaektdr
fvmkklndrvmrveyhflspyvspkespfrhvfwgsgshtlpallenlklrkqnngafne
tlfrnqlalatwtiqgaanalsgdvwdidnef
>d1cx8a2 3.7.4.1.1 (190-382) Transferrin receptor ectodomain, apical domain {Human (Homo sapiens)}
iqvkdsaqnsviivdkngrlvylvenpggyvayskaatvtgklvhanfgtkkdfedlytp
vngsivivragkitfaekvanaeslnaigvliymdqtkfpivnaelsffghahlgtgdpy
tpgfpsfnhtqfppsrssglpnipvqtisraaaeklfgnmegdcpsdwktdstcrmvtse
sknvkltvsnvlk
>d1cx8a3 3.47.4.5.1 (122-189,383-608) Transferrin receptor ectodomain, protease-like domain {Human (Homo sapiens)}
lywddlkrklsekldstdftstikllnensyvpreagsqkdenlalyvenefrefklskv
wrdqhfvkXeikilnifgvikgfvepdhyvvvgaqrdawgpgaaksgvgtalllklaqmf
sdmvlkdgfqpsrsiifaswsagdfgsvgatewlegylsslhlkaftyinldkavlgtsn
fkvsaspllytliektmqnvkhpvtgqflyqdsnwaskvekltldnaafpflaysgipav
sfcfcedtdypylgttmdtykelieripelnkvaraaaevagqfviklthdveln
>d1cx8b1 1.51.2.1.1 (609-760) Transferrin receptor ectodomain, C-terminal domain {Human (Homo sapiens)}
ldyeeynsqllsfvrdlnqyradikemglslqwlysargdffratsrlttdfgnaektdr
fvmkklndrvmrveyhflspyvspkespfrhvfwgsgshtlpallenlklrkqnngafne
tlfrnqlalatwtiqgaanalsgdvwdidnef
>d1cx8b2 3.7.4.1.1 (190-382) Transferrin receptor ectodomain, apical domain {Human (Homo sapiens)}
iqvkdsaqnsviivdkngrlvylvenpggyvayskaatvtgklvhanfgtkkdfedlytp
vngsivivragkitfaekvanaeslnaigvliymdqtkfpivnaelsffghahlgtgdpy
tpgfpsfnhtqfppsrssglpnipvqtisraaaeklfgnmegdcpsdwktdstcrmvtse
sknvkltvsnvlk
>d1cx8b3 3.47.4.5.1 (122-189,383-608) Transferrin receptor ectodomain, protease-like domain {Human (Homo sapiens)}
lywddlkrklsekldstdftstikllnensyvpreagsqkdenlalyvenefrefklskv
wrdqhfvkXeikilnifgvikgfvepdhyvvvgaqrdawgpgaaksgvgtalllklaqmf
sdmvlkdgfqpsrsiifaswsagdfgsvgatewlegylsslhlkaftyinldkavlgtsn
fkvsaspllytliektmqnvkhpvtgqflyqdsnwaskvekltldnaafpflaysgipav
sfcfcedtdypylgttmdtykelieripelnkvaraaaevagqfviklthdveln
>d1cx8c1 1.51.2.1.1 (609-760) Transferrin receptor ectodomain, C-terminal domain {Human (Homo sapiens)}
ldyeeynsqllsfvrdlnqyradikemglslqwlysargdffratsrlttdfgnaektdr
fvmkklndrvmrveyhflspyvspkespfrhvfwgsgshtlpallenlklrkqnngafne
tlfrnqlalatwtiqgaanalsgdvwdidnef
>d1cx8c2 3.7.4.1.1 (190-382) Transferrin receptor ectodomain, apical domain {Human (Homo sapiens)}
iqvkdsaqnsviivdkngrlvylvenpggyvayskaatvtgklvhanfgtkkdfedlytp
vngsivivragkitfaekvanaeslnaigvliymdqtkfpivnaelsffghahlgtgdpy
tpgfpsfnhtqfppsrssglpnipvqtisraaaeklfgnmegdcpsdwktdstcrmvtse
sknvkltvsnvlk
>d1cx8c3 3.47.4.5.1 (122-189,383-608) Transferrin receptor ectodomain, protease-like domain {Human (Homo sapiens)}
lywddlkrklsekldstdftstikllnensyvpreagsqkdenlalyvenefrefklskv
wrdqhfvkXeikilnifgvikgfvepdhyvvvgaqrdawgpgaaksgvgtalllklaqmf
sdmvlkdgfqpsrsiifaswsagdfgsvgatewlegylsslhlkaftyinldkavlgtsn
fkvsaspllytliektmqnvkhpvtgqflyqdsnwaskvekltldnaafpflaysgipav
sfcfcedtdypylgttmdtykelieripelnkvaraaaevagqfviklthdveln
>d1cx8d1 1.51.2.1.1 (609-760) Transferrin receptor ectodomain, C-terminal domain {Human (Homo sapiens)}
ldyeeynsqllsfvrdlnqyradikemglslqwlysargdffratsrlttdfgnaektdr
fvmkklndrvmrveyhflspyvspkespfrhvfwgsgshtlpallenlklrkqnngafne
tlfrnqlalatwtiqgaanalsgdvwdidnef
>d1cx8d2 3.7.4.1.1 (190-382) Transferrin receptor ectodomain, apical domain {Human (Homo sapiens)}
iqvkdsaqnsviivdkngrlvylvenpggyvayskaatvtgklvhanfgtkkdfedlytp
vngsivivragkitfaekvanaeslnaigvliymdqtkfpivnaelsffghahlgtgdpy
tpgfpsfnhtqfppsrssglpnipvqtisraaaeklfgnmegdcpsdwktdstcrmvtse
sknvkltvsnvlk
>d1cx8d3 3.47.4.5.1 (122-189,383-608) Transferrin receptor ectodomain, protease-like domain {Human (Homo sapiens)}
lywddlkrklsekldstdftstikllnensyvpreagsqkdenlalyvenefrefklskv
wrdqhfvkXeikilnifgvikgfvepdhyvvvgaqrdawgpgaaksgvgtalllklaqmf
sdmvlkdgfqpsrsiifaswsagdfgsvgatewlegylsslhlkaftyinldkavlgtsn
fkvsaspllytliektmqnvkhpvtgqflyqdsnwaskvekltldnaafpflaysgipav
sfcfcedtdypylgttmdtykelieripelnkvaraaaevagqfviklthdveln
>d1cx8e1 1.51.2.1.1 (609-760) Transferrin receptor ectodomain, C-terminal domain {Human (Homo sapiens)}
ldyeeynsqllsfvrdlnqyradikemglslqwlysargdffratsrlttdfgnaektdr
fvmkklndrvmrveyhflspyvspkespfrhvfwgsgshtlpallenlklrkqnngafne
tlfrnqlalatwtiqgaanalsgdvwdidnef
>d1cx8e2 3.7.4.1.1 (190-382) Transferrin receptor ectodomain, apical domain {Human (Homo sapiens)}
iqvkdsaqnsviivdkngrlvylvenpggyvayskaatvtgklvhanfgtkkdfedlytp
vngsivivragkitfaekvanaeslnaigvliymdqtkfpivnaelsffghahlgtgdpy
tpgfpsfnhtqfppsrssglpnipvqtisraaaeklfgnmegdcpsdwktdstcrmvtse
sknvkltvsnvlk
>d1cx8e3 3.47.4.5.1 (122-189,383-608) Transferrin receptor ectodomain, protease-like domain {Human (Homo sapiens)}
lywddlkrklsekldstdftstikllnensyvpreagsqkdenlalyvenefrefklskv
wrdqhfvkXeikilnifgvikgfvepdhyvvvgaqrdawgpgaaksgvgtalllklaqmf
sdmvlkdgfqpsrsiifaswsagdfgsvgatewlegylsslhlkaftyinldkavlgtsn
fkvsaspllytliektmqnvkhpvtgqflyqdsnwaskvekltldnaafpflaysgipav
sfcfcedtdypylgttmdtykelieripelnkvaraaaevagqfviklthdveln
>d1cx8f1 1.51.2.1.1 (609-760) Transferrin receptor ectodomain, C-terminal domain {Human (Homo sapiens)}
ldyeeynsqllsfvrdlnqyradikemglslqwlysargdffratsrlttdfgnaektdr
fvmkklndrvmrveyhflspyvspkespfrhvfwgsgshtlpallenlklrkqnngafne
tlfrnqlalatwtiqgaanalsgdvwdidnef
>d1cx8f2 3.7.4.1.1 (190-382) Transferrin receptor ectodomain, apical domain {Human (Homo sapiens)}
iqvkdsaqnsviivdkngrlvylvenpggyvayskaatvtgklvhanfgtkkdfedlytp
vngsivivragkitfaekvanaeslnaigvliymdqtkfpivnaelsffghahlgtgdpy
tpgfpsfnhtqfppsrssglpnipvqtisraaaeklfgnmegdcpsdwktdstcrmvtse
sknvkltvsnvlk
>d1cx8f3 3.47.4.5.1 (122-189,383-608) Transferrin receptor ectodomain, protease-like domain {Human (Homo sapiens)}
lywddlkrklsekldstdftstikllnensyvpreagsqkdenlalyvenefrefklskv
wrdqhfvkXeikilnifgvikgfvepdhyvvvgaqrdawgpgaaksgvgtalllklaqmf
sdmvlkdgfqpsrsiifaswsagdfgsvgatewlegylsslhlkaftyinldkavlgtsn
fkvsaspllytliektmqnvkhpvtgqflyqdsnwaskvekltldnaafpflaysgipav
sfcfcedtdypylgttmdtykelieripelnkvaraaaevagqfviklthdveln
>d1cx8g1 1.51.2.1.1 (609-760) Transferrin receptor ectodomain, C-terminal domain {Human (Homo sapiens)}
ldyeeynsqllsfvrdlnqyradikemglslqwlysargdffratsrlttdfgnaektdr
fvmkklndrvmrveyhflspyvspkespfrhvfwgsgshtlpallenlklrkqnngafne
tlfrnqlalatwtiqgaanalsgdvwdidnef
>d1cx8g2 3.7.4.1.1 (190-382) Transferrin receptor ectodomain, apical domain {Human (Homo sapiens)}
iqvkdsaqnsviivdkngrlvylvenpggyvayskaatvtgklvhanfgtkkdfedlytp
vngsivivragkitfaekvanaeslnaigvliymdqtkfpivnaelsffghahlgtgdpy
tpgfpsfnhtqfppsrssglpnipvqtisraaaeklfgnmegdcpsdwktdstcrmvtse
sknvkltvsnvlk
>d1cx8g3 3.47.4.5.1 (122-189,383-608) Transferrin receptor ectodomain, protease-like domain {Human (Homo sapiens)}
lywddlkrklsekldstdftstikllnensyvpreagsqkdenlalyvenefrefklskv
wrdqhfvkXeikilnifgvikgfvepdhyvvvgaqrdawgpgaaksgvgtalllklaqmf
sdmvlkdgfqpsrsiifaswsagdfgsvgatewlegylsslhlkaftyinldkavlgtsn
fkvsaspllytliektmqnvkhpvtgqflyqdsnwaskvekltldnaafpflaysgipav
sfcfcedtdypylgttmdtykelieripelnkvaraaaevagqfviklthdveln
>d1cx8h1 1.51.2.1.1 (609-760) Transferrin receptor ectodomain, C-terminal domain {Human (Homo sapiens)}
ldyeeynsqllsfvrdlnqyradikemglslqwlysargdffratsrlttdfgnaektdr
fvmkklndrvmrveyhflspyvspkespfrhvfwgsgshtlpallenlklrkqnngafne
tlfrnqlalatwtiqgaanalsgdvwdidnef
>d1cx8h2 3.7.4.1.1 (190-382) Transferrin receptor ectodomain, apical domain {Human (Homo sapiens)}
iqvkdsaqnsviivdkngrlvylvenpggyvayskaatvtgklvhanfgtkkdfedlytp
vngsivivragkitfaekvanaeslnaigvliymdqtkfpivnaelsffghahlgtgdpy
tpgfpsfnhtqfppsrssglpnipvqtisraaaeklfgnmegdcpsdwktdstcrmvtse
sknvkltvsnvlk
>d1cx8h3 3.47.4.5.1 (122-189,383-608) Transferrin receptor ectodomain, protease-like domain {Human (Homo sapiens)}
lywddlkrklsekldstdftstikllnensyvpreagsqkdenlalyvenefrefklskv
wrdqhfvkXeikilnifgvikgfvepdhyvvvgaqrdawgpgaaksgvgtalllklaqmf
sdmvlkdgfqpsrsiifaswsagdfgsvgatewlegylsslhlkaftyinldkavlgtsn
fkvsaspllytliektmqnvkhpvtgqflyqdsnwaskvekltldnaafpflaysgipav
sfcfcedtdypylgttmdtykelieripelnkvaraaaevagqfviklthdveln
>d1cxa__ 1.3.1.1.14 Cytochrome c2 {Rhodobacter spaeroides}
qegdpeagakafnqcqtchvivddsgttiagrnaktgpnlygvvgrtagtqadfkgygeg
mkeagakglawdeehfvqyvqdptkflkeytgdakakgkmtfklkkeadahniwaylqqv
avrp
>d1cxc__ 1.3.1.1.14 Cytochrome c2 {Rhodobacter spaeroides}
qegdpeagakafnqcqtchvivddsgttiagrnaktgpnlygvvgrtagtqadfkgygeg
mkeagakglawdeehfvqyvqdptkflkeytgdakakgkmtfklkkeadahniwaylqqv
avrp
>d1cxe_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d1cxe_2 2.3.1.1.1 (582-686) Cyclodextrin glycosyltransferase, C-terminal domain {Bacillus circulans}
lsgdqvsvrfvvnnattalgqnvyltgsvselgnwdpakaigpmynqvvyqypnwyydvs
vpagktiefkflkkqgstvtweggsnhtftapssgtatinvnwqp
>d1cxe_3 2.62.1.1.4 (407-495) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqerwinndvliyerkfgsnvavvavnrnlnapasisglvtslpqgsyndvlggllng
ntlsvgsggaasnftlaaggtavwqytaa
>d1cxe_4 3.1.7.1.4 (1-406) Cyclodextrin glycosyltransferase {Bacillus circulans}
apdtsvsnkqnfstdviyqiftdrfsdgnpannptgaafdgtctnlrlycggdwqgiink
indgyltgmgvtaiwisqpveniysiinysgvnntayhgywardfkktnpaygtiadfqn
liaaahaknikviidfapnhtspassdqpsfaengrlydngtllggytndtqnlfhhngg
tdfsttengiyknlydladlnhnnstvdvylkdaikmwldlgidgirmdavkhmpfgwqk
sfmaavnnykpvftfgewflgvnevspenhkfanesgmslldfrfaqkvrqvfrdntdnm
yglkamlegsaadyaqvddqvtfidnhdmerfhasnanrrkleqalaftltsrgvpaiyy
gteqymsggtdpdnraripsfststtayqviqklaplrkcnpaiay
>d1cxf_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d1cxf_2 2.3.1.1.1 (582-686) Cyclodextrin glycosyltransferase, C-terminal domain {Bacillus circulans}
lsgdqvsvrfvvnnattalgqnvyltgsvselgnwdpakaigpmynqvvyqypnwyydvs
vpagktiefkflkkqgstvtweggsnhtftapssgtatinvnwqp
>d1cxf_3 2.62.1.1.4 (407-495) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqerwinndvliyerkfgsnvavvavnrnlnapasisglvtslpqgsyndvlggllng
ntlsvgsggaasnftlaaggtavwqytaa
>d1cxf_4 3.1.7.1.4 (1-406) Cyclodextrin glycosyltransferase {Bacillus circulans}
apdtsvsnkqnfstdviyqiftdrfsdgnpannptgaafdgtctnlrlycggdwqgiink
indgyltgmgvtaiwisqpveniysiinysgvnntayhgywardfkktnpaygtiadfqn
liaaahaknikviidfapnhtspassdqpsfaengrlydngtllggytndtqnlfhhngg
tdfsttengiyknlydladlnhnnstvdvylkdaikmwldlgidgirmnavkhmpfgwqk
sfmaavnnykpvftfgqwflgvnevspenhkfanesgmslldfrfaqkvrqvfrdntdnm
yglkamlegsaadyaqvddqvtfidnhdmerfhasnanrrkleqalaftltsrgvpaiyy
gteqymsggtdpdnraripsfststtayqviqklaplrkcnpaiay
>d1cxh_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d1cxh_2 2.3.1.1.1 (582-686) Cyclodextrin glycosyltransferase, C-terminal domain {Bacillus circulans}
lsgdqvsvrfvvnnattalgqnvyltgsvselgnwdpakaigpmynqvvyqypnwyydvs
vpagktiefkflkkqgstvtweggsnhtftapssgtatinvnwqp
>d1cxh_3 2.62.1.1.4 (407-495) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqerwinndvliyerkfgsnvavvavnrnlnapasisglvtslpqgsyndvlggllng
ntlsvgsggaasnftlaaggtavwqytaa
>d1cxh_4 3.1.7.1.4 (1-406) Cyclodextrin glycosyltransferase {Bacillus circulans}
apdtsvsnkqnfstdviyqiftdrfsdgnpannptgaafdgtctnlrlycggdwqgiink
indgyltgmgvtaiwisqpveniysiinysgvnntayhgywardfkktnpaygtiadfqn
liaaahaknikviidfapnhtspassdqpsfaengrlydngtllggytndtqnlfhhngg
tdfsttengiyknlydladlnhnnstvdvylkdaikmwldlgidgirmdavkhmpfgwqk
sfmaavnnykpvftfgewflgvnevspenhkfanesgmslldfrfaqkvrqvfrdntdnm
yglkamlegsaadyaqvddqvtfidnhdmerfhasnanrrkleqalaftltsrgvpaiyy
gteqymsggtdpdnraripsfststtayqviqklaplrkcnpaiay
>d1cxi_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d1cxi_2 2.3.1.1.1 (582-686) Cyclodextrin glycosyltransferase, C-terminal domain {Bacillus circulans}
lsgdqvsvrfvvnnattalgqnvyltgsvselgnwdpakaigpmynqvvyqypnwyydvs
vpagktiefkflkkqgstvtweggsnhtftapssgtatinvnwqp
>d1cxi_3 2.62.1.1.4 (407-495) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqerwinndvliyerkfgsnvavvavnrnlnapasisglvtslpqgsyndvlggllng
ntlsvgsggaasnftlaaggtavwqytaa
>d1cxi_4 3.1.7.1.4 (1-406) Cyclodextrin glycosyltransferase {Bacillus circulans}
apdtsvsnkqnfstdviyqiftdrfsdgnpannptgaafdgtctnlrlycggdwqgiink
indgyltgmgvtaiwisqpveniysiinysgvnntayhgywardfkktnpaygtiadfqn
liaaahaknikviidfapnhtspassdqpsfaengrlydngtllggytndtqnlfhhngg
tdfsttengiyknlydladlnhnnstvdvylkdaikmwldlgidgirmdavkhmpfgwqk
sfmaavnnykpvftfgewflgvnevspenhkfanesgmslldfrfaqkvrqvfrdntdnm
yglkamlegsaadyaqvddqvtfidnhdmerfhasnanrrkleqalaftltsrgvpaiyy
gteqymsggtdpdnraripsfststtayqviqklaplrkcnpaiay
>d1cxka1 2.1.1.5.4 (497-583) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
atptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipav
aggnynikvanaagtasnvydnfevls
>d1cxka2 2.3.1.1.1 (584-686) Cyclodextrin glycosyltransferase, C-terminal domain {Bacillus circulans}
gdqvsvrfvvnnattalgqnvyltgsvselgnwdpakaigpmynqvvyqypnwyydvsvp
agktiefkflkkqgstvtweggsnhtftapssgtatinvnwqp
>d1cxka3 2.62.1.1.4 (407-496) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqerwinndvliyerkfgsnvavvavnrnlnapasisglvtslpqgsyndvlggllng
ntlsvgsggaasnftlaaggtavwqytaat
>d1cxka4 3.1.7.1.4 (1-406) Cyclodextrin glycosyltransferase {Bacillus circulans}
apdtsvsnkqnfstdviyqiftdrfsdgnpannptgaafdgtctnlrlycggdwqgiink
indgyltgmgvtaiwisqpveniysiinysgvnntayhgywardfkktnpaygtiadfqn
liaaahaknikviidfapnhtspassdqpsfaengrlydngtllggytndtqnlfhhngg
tdfsttengiyknlydladlnhnnstvdvylkdaikmwldlgidgirmnavkhmpfgwqk
sfmaavnnykpvftfgqwflgvnevspenhkfanesgmslldfrfaqkvrqvfrdntdnm
yglkamlegsaadyaqvddqvtfidnhdmerfhasnanrrkleqalaftltsrgvpaiyy
gteqymsggtdpdnraripsfststtayqviqklaplrkcnpaiay
>d1cxla1 2.1.1.5.4 (497-583) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
atptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipav
aggnynikvanaagtasnvydnfevls
>d1cxla2 2.3.1.1.1 (584-686) Cyclodextrin glycosyltransferase, C-terminal domain {Bacillus circulans}
gdqvsvrfvvnnattalgqnvyltgsvselgnwdpakaigpmynqvvyqypnwyydvsvp
agktiefkflkkqgstvtweggsnhtftapssgtatinvnwqp
>d1cxla3 2.62.1.1.4 (407-496) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqerwinndvliyerkfgsnvavvavnrnlnapasisglvtslpqgsyndvlggllng
ntlsvgsggaasnftlaaggtavwqytaat
>d1cxla4 3.1.7.1.4 (1-406) Cyclodextrin glycosyltransferase {Bacillus circulans}
apdtsvsnkqnfstdviyqiftdrfsdgnpannptgaafdgtctnlrlycggdwqgiink
indgyltgmgvtaiwisqpveniysiinysgvnntayhgywardfkktnpaygtiadfqn
liaaahaknikviidfapnhtspassdqpsfaengrlydngtllggytndtqnlfhhngg
tdfsttengiyknlydladlnhnnstvdvylkdaikmwldlgidgirmdavkhmpfgwqk
sfmaavnnykpvftfgqwflgvnevspenhkfanesgmslldfrfaqkvrqvfrdntdnm
yglkamlegsaadyaqvddqvtfidnhdmerfhasnanrrkleqalaftltsrgvpaiyy
gteqymsggtdpdnraripsfststtayqviqklaplrksnpaiay
>d1cxn__ 7.7.1.1.2 gamma-Cardiotoxin {Snake (Naja nigricollis)}
lkcnqlippfwktcpkgknlcykmtmraapmvpvkrgcidvcpkssllikymccntdkcn
>d1cxo__ 7.7.1.1.2 gamma-Cardiotoxin {Snake (Naja nigricollis)}
lkcnqlippfwktcpkgknlcykmtmraapmvpvkrgcidvcpkssllikymccntdkcn
>d1cxqa_ 3.46.3.2.1 ASV integrase, catalytic domain {Avian sarcoma virus, Rous sarcoma virus, Schmidt-Ruppin strain B}
grglgplqiwqtdftleprmaprswlavtvdtassaivvtqhgrvtsvaaqhhwataiav
lgrpkaiktdngscftskstrewlarwgiahttgipgnsqgqamveranrllkdkirvla
egdgfmkriptskqgellakamyalnh
>d1cxra_ 7.13.1.1.1 Crambin {Abyssinian cabbage (Crambe abyssinica)}
ttccpsivarsnfnvcrlpgtseaicatytgciiipgatcpgdyan
>d1cxsa1 2.46.2.2.1 (626-780) Dimethylsulfoxide reductase (DMSO reductase) {Rhodobacter sphaeroides}
erlggagakyplhvvashpksrlhsqlngtslrdlyavaghepclinpadaaargiadgd
vlrvfndrgqilvgakvsdavmpgaiqiyeggwydpldpseegtldkygdvnvlsldvgt
sklaqgncgqtiladvekyagapvtvtvfdtpkga
>d1cxsa2 3.70.1.1.1 (1-625) Dimethylsulfoxide reductase (DMSO reductase) {Rhodobacter sphaeroides}
eglangevmsgchwgvfkarvengravafepwdkdpapshqlpgvldsiysptrikypmv
rreflekgvnadrstrgngdfvrvtwdealdlvarelkrvqesygptgtfggsygwkspg
rlhncqvlmrralnlaggfvnssgdystaaaqiimphvmgtlevyeqqtawpvvventdl
mvfwaadpmktneigwvipdhgayagmkalkekgtrvicinpvrtetadyfgadvvsprp
qtdvalmlgmahtlysedlhdkdflencttgfdlfaayltgesdgtpktaewaaeicglp
aeqirelarsfvagrtmlaagwsiqrmhhgeqahwmlvtlasmigqiglpgggfglsyhy
snggsptsdgpalggisdggkavegaawlsesgatsipcarvvdmllnpggefqfngata
typdvklaywaggnpfahhqdrnrmlkawekletfivqdfqwtatarhadivlpattsye
rndiesvgdysnrailamkkvvdplyearsdydifaalaerlgkgaeftegrdemgwiss
fyeaavkqaefknvampsfedfwsegivefpiteganfvryadfredplfnplgtpsgli
eiyskniekmgyddcpahptwmepa
>d1cxta1 2.46.2.2.1 (626-780) Dimethylsulfoxide reductase (DMSO reductase) {Rhodobacter sphaeroides}
erlggagakyplhvvashpksrlhsqlngtslrdlyavaghepclinpadaaargiadgd
vlrvfndrgqilvgakvsdavmpgaiqiyeggwydpldpseegtldkygdvnvlsldvgt
sklaqgncgqtiladvekyagapvtvtvfdtpkga
>d1cxta2 3.70.1.1.1 (1-625) Dimethylsulfoxide reductase (DMSO reductase) {Rhodobacter sphaeroides}
eglangevmsgchwgvfkarvengravafepwdkdpapshqlpgvldsiysptrikypmv
rreflekgvnadrstrgngdfvrvtwdealdlvarelkrvqesygptgtfggsygwkspg
rlhncqvlmrralnlaggfvnssgdystaaaqiimphvmgtlevyeqqtawpvvventdl
mvfwaadpmktneigwvipdhgayagmkalkekgtrvicinpvrtetadyfgadvvsprp
qtdvalmlgmahtlysedlhdkdflencttgfdlfaayltgesdgtpktaewaaeicglp
aeqirelarsfvagrtmlaagwsiqrmhhgeqahwmlvtlasmigqiglpgggfglsyhy
snggsptsdgpalggisdggkavegaawlsesgatsipcarvvdmllnpggefqfngata
typdvklaywaggnpfahhqdrnrmlkawekletfivqdfqwtatarhadivlpattsye
rndiesvgdysnrailamkkvvdplyearsdydifaalaerlgkgaeftegrdemgwiss
fyeaavkqaefknvampsfedfwsegivefpiteganfvryadfredplfnplgtpsgli
eiyskniekmgyddcpahptwmepa
>d1cxua_ 3.46.3.2.1 ASV integrase, catalytic domain {Avian sarcoma virus, Rous sarcoma virus, Schmidt-Ruppin strain B}
gplqiwqtdftleprmaprswlavtvdtassaivvtqhgrvtsvaaqhhwataiavlgrp
kaiktdngscftskstrewlarwgiahttgipgnsqgqamveranrllkdkirvlaegdg
fmkriptskqgellakamyalnh
>d1cxxa1 7.33.1.3.2 (117-144) Cysteine-rich (intestinal) protein, CRP, CRIP {Japanese quail (Coturnix coturnix japonica), CRP2}
aekcsacgdsvyaaekvigagkpwhknc
>d1cxxa2 7.33.1.3.2 (145-175) Cysteine-rich (intestinal) protein, CRP, CRIP {Japanese quail (Coturnix coturnix japonica), CRP2}
frcakcgkslesttltekegeiyckgcyakn
>d1cxya_ 4.94.1.1.3 Cytochrome b558 {Ectothiorhodospira vacuolata |A|}
tlpvftleqvaehhspddcwmaihgkvydltpyvpnhpgpagmmlvwcgqesteawetks
ygephsslaarllqryligtl
>d1cxza_ 3.30.1.6.8 RhoA {Human (Homo sapiens)}
smaairkklvivgdvacgktcllivfskdqfpevyvptvfenyvadievdgkqvelalwd
tagqedydrlrplsypdtdvilmcfsidspdslenipekwtpevkhfcpnvpiilvgnkk
dlrndehtrrelakmkqepvkpeegrdmanrigafgymecsaktkdgvrevfematraal
qa
>d1cxzb_ 1.2.3.1.1 Effector domain of the protein kinase pkn/prk1 {Human (Homo sapiens)}
wslleqlglagadlaapgvqqqlelererlrreirkelklkegaenlrrattdlgrslgp
velllrgssrrldllhqqlqelhahv
>d1cy5a_ 1.76.1.1.6 Apoptotic protease activating factor 1, APAF-1 {Human (Homo sapiens)}
mdakarncllqhrealekdiktsyimdhmisdgfltiseeekvrneptqqqraamlikmi
lkkdndsyvsfynallhegykdlaallhdgipv
>d1cyc__ 1.3.1.1.11 Mitochondrial cytochrome c {Bonito (Katsuwonus pelamis)}
gdvakgkktfvqkcaqchtvenggkhkvgpnlwglfgrktgqaegysytdankskgivwn
entlmeylenpkkyipgtkmifagikkkgerqdlvaylksats
>d1cyda_ 3.2.1.2.4 Carbonyl reductase {Mouse (Mus musculus)}
lnfsglralvtgagkgigrdtvkalhasgakvvavtrtnsdlvslakecpgiepvcvdlg
dwdatekalggigpvdllvnnaalvimqpflevtkeafdrsfsvnlrsvfqvsqmvardm
inrgvpgsivnvssmvahvtfpnlitysstkgamtmltkamamelgphkirvnsvnptvv
ltdmgkkvsadpefarklkerhplrkfaevedvvnsilfllsdrsastsgggilvdagyl
as
>d1cydb_ 3.2.1.2.4 Carbonyl reductase {Mouse (Mus musculus)}
lnfsglralvtgagkgigrdtvkalhasgakvvavtrtnsdlvslakecpgiepvcvdlg
dwdatekalggigpvdllvnnaalvimqpflevtkeafdrsfsvnlrsvfqvsqmvardm
inrgvpgsivnvssmvahvtfpnlitysstkgamtmltkamamelgphkirvnsvnptvv
ltdmgkkvsadpefarklkerhplrkfaevedvvnsilfllsdrsastsgggilvdagyl
as
>d1cydc_ 3.2.1.2.4 Carbonyl reductase {Mouse (Mus musculus)}
lnfsglralvtgagkgigrdtvkalhasgakvvavtrtnsdlvslakecpgiepvcvdlg
dwdatekalggigpvdllvnnaalvimqpflevtkeafdrsfsvnlrsvfqvsqmvardm
inrgvpgsivnvssmvahvtfpnlitysstkgamtmltkamamelgphkirvnsvnptvv
ltdmgkkvsadpefarklkerhplrkfaevedvvnsilfllsdrsastsgggilvdagyl
as
>d1cydd_ 3.2.1.2.4 Carbonyl reductase {Mouse (Mus musculus)}
lnfsglralvtgagkgigrdtvkalhasgakvvavtrtnsdlvslakecpgiepvcvdlg
dwdatekalggigpvdllvnnaalvimqpflevtkeafdrsfsvnlrsvfqvsqmvardm
inrgvpgsivnvssmvahvtfpnlitysstkgamtmltkamamelgphkirvnsvnptvv
ltdmgkkvsadpefarklkerhplrkfaevedvvnsilfllsdrsastsgggilvdagyl
as
>d1cye__ 3.16.2.1.1 CheY protein {Escherichia coli}
rsdkelkflvvddfstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnm
pnmdglellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleekl
nkifeklgm
>d1cyf__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
mittplvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwd
khdntggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqe
mqgpkipwragrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalg
kthlknsgyegpwgcannvftnefylnllnedwklekndanneqwdsksgymmlptdysl
iqdpkylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1cyg_1 2.1.1.5.5 (492-574) Cyclodextrin glycosyltransferase, domain E {Bacillus stearothermophilus}
estpiighvgpmmgqvghqvtidgegfgtntgtvkfgttaanvvswsnnqivvavpnvsp
gkynitvqsssgqtsaaydnfev
>d1cyg_2 2.3.1.1.2 (575-680) Cyclodextrin glycosyltransferase, C-terminal domain {Bacillus stearothermophilus}
ltndqvsvrfvvnnattnlgqniyivgnvyelgnwdtskaigpmfnqvvysyptwyidvs
vpegktiefkfikkdsqgnvtwesgsnhvyttptnttgkiivdwqn
>d1cyg_3 2.62.1.1.5 (403-491) Cyclodextrin glycosyltransferase {Bacillus stearothermophilus}
gdteqrwingdvyvyerqfgkdvvlvavnrssssnysitglftalpagtytdqlgglldg
ntiqvgsngsvnafdlgpgevgvwaysat
>d1cyg_4 3.1.7.1.5 (1-402) Cyclodextrin glycosyltransferase {Bacillus stearothermophilus}
agnlnkvnftsdvvyqivvdrfvdgntsnnpsgalfssgctnlrkycggdwqgiinkind
gyltdmgvtaiwisqpvenvfsvmndasgsasyhgywardfkkpnpffgtlsdfqrlvda
ahakgikviidfapnhtspasetnpsymengrlydngtllggytndanmyfhhnggttfs
sledgiyrnlfdladlnhqnpvidrylkdavkmwidmgidgirmdavkhmpfgwqkslmd
eidnyrpvftfgewflsenevdannhyfanesgmslldfrfgqklrqvlrnnsdnwygfn
qmiqdtasaydevldqvtfidnhdmdrfmidggdprkvdmalavlltsrgvpniyygteq
ymtgngdpnnrkmmssfnkntrayqviqklsslrrnnpalay
>d1cyi__ 1.3.1.1.3 Cytochrome c6 (synonym: cytochrome c553) {Chlamydomonas reinhardtii}
adlalgaqvfngncaachmggrnsvmpektldkaaleqyldggfkvesiiyqvengkgam
pawadrlseeeiqavaeyvfkqatdaawk
>d1cyj__ 1.3.1.1.3 Cytochrome c6 (synonym: cytochrome c553) {Chlamydomonas reinhardtii}
adlalgaqvfngncaachmggrnsvmpektldkaaleqyldggfkvesiiyqvengkgam
pawadrlseeeiqavaeyvfkqatdaawky
>d1cyl__ 1.27.1.2.3 Interleukin-4 (IL-4) {Human (Homo sapiens)}
hkcditlqeiiktlnslteqktlcteltvtdifaaskntteketfcraatvlrqfyshhe
kdtrclgataqqfhrhkqlirflkrldrnlwglaglnscpvkeanqstlenflerlktim
rekyskcss
>d1cyna_ 2.55.1.1.2 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant B}
gpkvtvkvyfdlrigdedvgrvifglfgktvpktvdnfvalatgekgfgyknskfhrvik
dfmiqggdftrgdgtggksiygerfpdenfklkhygpgwvsmanagkdtngsqffittvk
tawldgkhvvfgkvlegmevvrkvestktdsrdkplkdviiadcgkievekpfaiake
>d1cyo__ 4.94.1.1.1 Cytochrome b5 {Bovine (Bos taurus)}
skavkyytleeiqkhnnskstwlilhykvydltkfleehpggeevlreqaggdatenfed
vghstdarelsktfiigelhpddrskit
>d1cyu__ 4.15.1.2.2 Cystatin A (stefin A) {Human (Homo sapiens)}
mipgglseakpatpeiqeivdkvkpqleektnetygkleavqyktqvvagtnyyikvrag
dnkylhlkvfkslpgqnedlvltgyqvdknkddeltgf
>d1cyv__ 4.15.1.2.2 Cystatin A (stefin A) {Human (Homo sapiens)}
mipgglseakpatpeiqeivdkvkpqleektnetygkleavqyktqvvagtnyyikvrag
dnkylhlkvfkslpgqnedlvltgyqvdknkddeltgf
>d1cyw__ 2.5.1.2.1 Quinol oxidase (CYOA) {Escherichia coli}
kpitievvsmdwkwffiypeqgiatvneiafpantpvyfkvtsnsvmnsffiprlgsqiy
amagmqtrlhlianepgtydgisasysgpgfsgmkfkaiatpdraafdqwvakakqspnt
msdmaafeklaapseynqveyfsnvkpdlfadvinkfma
>d1cyx__ 2.5.1.2.1 Quinol oxidase (CYOA) {Escherichia coli}
kpitievvsmdwkwffiypeqgiatvneiafpantpvyfkvtsnsvmhsffiprlgsqiy
amagmqtrlhlianepgtydgicaeicgpghsgmkfkaiatpdraafdqwvakakqspnt
msdmaafeklaapseynqveyfsnvkpdlfadvinkfm
>d1cz4a1 2.46.2.3.2 (1-91) N-terminal domain of VAT-N, VAT-Nn {Thermoplasma acidophilum}
mesnngiilrvaeanstdpgmsrvrldessrrlldaeigdvveiekvrktvgrvyrarpe
denkgivridsvmrnncgasigdkvkvrkvr
>d1cz4a2 4.26.1.1.2 (92-185) C-terminal domain of VAT-N, VAT-Nc {Thermoplasma acidophilum}
teiakkvtlapiirkdqrlkfgegieeyvqralirrpmleqdnisvpgltlagqtgllfk
vvktlpskvpveigeetkieireepasevleegg
>d1cz5a1 2.46.2.3.2 (1-91) N-terminal domain of VAT-N, VAT-Nn {Thermoplasma acidophilum}
mesnngiilrvaeanstdpgmsrvrldessrrlldaeigdvveiekvrktvgrvyrarpe
denkgivridsvmrnncgasigdkvkvrkvr
>d1cz5a2 4.26.1.1.2 (92-185) C-terminal domain of VAT-N, VAT-Nc {Thermoplasma acidophilum}
teiakkvtlapiirkdqrlkfgegieeyvqralirrpmleqdnisvpgltlagqtgllfk
vvktlpskvpveigeetkieireepasevleegg
>d1cz9a_ 3.46.3.2.1 ASV integrase, catalytic domain {Avian sarcoma virus, Rous sarcoma virus, Schmidt-Ruppin strain B}
qiwqtnftleprmaprswlavtvdtassaivvtqhgrvtsvaaqhhwataiavlgrpkai
ktdngscftskstrewlarwgiahttgipgnsqgqamveranrllkdkirvlaegdgfmk
riptskqgellakamyaln
>d1czba_ 3.46.3.2.1 ASV integrase, catalytic domain {Avian sarcoma virus, Rous sarcoma virus, Schmidt-Ruppin strain B}
grglgplqiwqtdftleprmaprswlavtvdtassaivvtqhgrvtsvaaqhhwataiav
lgrpkaiktdngscftskstrewlarwgiahttggqamveranrllkdkirvlaegdgfm
kriptskqgellakamyalnh
>d1czie_ 2.44.1.2.15 Chymosin (synonim: renin) {Bovine (Bos taurus)}
gevasvpltnyldsqyfgkiylgtppqeftvlfdtgssdfwvpsiycksnacknhqrfdp
rksstfqnlgkplsihygtgsmqgilgydtvtvsnivdiqqtvglstqepgdvftyaefd
gilgmaypslaseysipvfdnmmnrhlvaqdlfsvymdrngqesmltlgaidpsyytgsl
hwvpvtvqqywqftvdsvtisgvvvaceggcqaildtgtsklvgpssdilniqqaigatq
nqygefdidcdnlsymptvvfeingkmypltpsaytsqdqgfctsgfqsenhsqkwilgd
vfireyysvfdrannlvglakai
>d1czj__ 1.126.1.1.1 Cytochrome c3 {Desulfovibrio desulfuricans, different strains}
tfeipesvtmspkqfegytpkkgdvtfnhashmdiacqqchhtvpdtytiescmtegchd
nikerteissvyrtfhttkdsekscvgchrelkrqgpsdaplacnschvq
>d1czm__ 2.65.1.1.1 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme I}
aspdwgyddkngpeqwsklypiangnnqspvdiktsetkhdtslkpisvsynpatakeii
nvghsfhvnfedndnrsvlkggpfsdsyrlfqfhfhwgstnehgsehtvdgvkysaelhv
ahwnsakysslaeaaskadglavigvlmkvgeanpklqkvldalqaiktkgkrapftnfd
pstllpssldfwtypgslthpplyesvtwiickesisvsseqlaqfrsllsnvegdnavp
mqhnnrptqplkgrtvrasf
>d1d0ga_ 2.20.1.1.5 Apoptosis-2 ligand, apo2l/trail {Human (Homo sapiens)}
pqrvaahitgtrgrsntlsspnsknekalgrkinswessrsghsflsnlhlrngelvihe
kgfyyiysqtyfrfqeeikentkndkqmvqyiykytsypdpillmksarnscwskdaeyg
lysiyqggifelkendrifvsvtnehlidmdheasffgaflvg
>d1d0gb_ 2.20.1.1.5 Apoptosis-2 ligand, apo2l/trail {Human (Homo sapiens)}
pqrvaahitgtrgrsntlsspnsknekalgrkinswessrsghsflsnlhlrngelvihe
kgfyyiysqtyfrfqeeikentkndkqmvqyiykytsypdpillmksarnscwskdaeyg
lysiyqggifelkendrifvsvtnehlidmdheasffgaflvg
>d1d0gd_ 2.20.1.1.5 Apoptosis-2 ligand, apo2l/trail {Human (Homo sapiens)}
pqrvaahitgtrgrsntlsspnsknekalgrkinswessrsghsflsnlhlrngelvihe
kgfyyiysqtyfrfqeeikentkndkqmvqyiykytsypdpillmksarnscwskdaeyg
lysiyqggifelkendrifvsvtnehlidmdheasffgaflvg
>d1d0gr1 7.24.1.1.2 (21-61) Death receptor-5 (dr5) fragment {Human (Homo sapiens)}
sspseglcppghhisedgrdcisckygqdysthwndllfcl
>d1d0gr2 7.24.1.1.2 (62-101) Death receptor-5 (dr5) fragment {Human (Homo sapiens)}
rctrcdsgevelspctttrntvcqceegtfreedspemcr
>d1d0gr3 7.24.1.1.2 (102-128) Death receptor-5 (dr5) fragment {Human (Homo sapiens)}
kcrtgcprgmvkvgdctpwsdiecvhk
>d1d0gs1 7.24.1.1.2 (21-61) Death receptor-5 (dr5) fragment {Human (Homo sapiens)}
sspseglcppghhisedgrdcisckygqdysthwndllfcl
>d1d0gs2 7.24.1.1.2 (62-101) Death receptor-5 (dr5) fragment {Human (Homo sapiens)}
rctrcdsgevelspctttrntvcqceegtfreedspemcr
>d1d0gs3 7.24.1.1.2 (102-130) Death receptor-5 (dr5) fragment {Human (Homo sapiens)}
kcrtgcprgmvkvgdctpwsdiecvhkes
>d1d0gt1 7.24.1.1.2 (21-61) Death receptor-5 (dr5) fragment {Human (Homo sapiens)}
sspseglcppghhisedgrdcisckygqdysthwndllfcl
>d1d0gt2 7.24.1.1.2 (62-101) Death receptor-5 (dr5) fragment {Human (Homo sapiens)}
rctrcdsgevelspctttrntvcqceegtfreedspemcr
>d1d0gt3 7.24.1.1.2 (102-130) Death receptor-5 (dr5) fragment {Human (Homo sapiens)}
kcrtgcprgmvkvgdctpwsdiecvhkes
>d1d0na1 4.85.1.1.3 (27-152) Gelsolin {Horse (Equus caballus)}
vehpeflkagkepglqiwrvekfdlvpvppnlygdfftgdayvilktvqlrngilqydlh
ywlgnecsqdesgaaaiftvqlddylngravqhrevqgfesatflgyfksglkykkggva
sgfkhv
>d1d0na2 4.85.1.1.3 (153-262) Gelsolin {Horse (Equus caballus)}
vpnevvvqrllqvkgrrvvratevpvswesfnngdcfildlgnniyqwcgsksnrferlk
atqvskgirdnersgraqvsvfeegaepeamlqvlgpkptlpeatedtvk
>d1d0na3 4.85.1.1.3 (263-383) Gelsolin {Horse (Equus caballus)}
edaanrklaklykvsngagpmvvslvadenpfaqgalrsedcfildhgkdgkifvwkgkq
anmeerkaalktasdfiskmdypkqtqvsvlpeggetplfrqffknwrdpdqteglglay
l
>d1d0na4 4.85.1.1.3 (384-532) Gelsolin {Horse (Equus caballus)}
sshiahvervpfdaatlhtstamaaqhgmdddgtgqkqiwrvegsnkvpvdpatygqfyg
gdsyiilynyrhgsrqgqiiynwqgaqstqdevaasailtaqldeelggtpvqsrvvqgk
epahlmslfggkpmivykggtsreggqta
>d1d0na5 4.85.1.1.3 (533-628) Gelsolin {Horse (Equus caballus)}
pastrlfqvrasssgatraveiipkagalnsndafvlktpsaaylwvgagaseaektgaq
ellrvlraqpvqvaegsepdsfwealggkatyrtsp
>d1d0na6 4.85.1.1.3 (629-755) Gelsolin {Horse (Equus caballus)}
rlkdkkmdahpprlfacsnkigrfvieevpgefmqedlatddvmlldtwdqvfvwvgkds
qdeektealtsakryidtdpahrdrrtpitvvkqgfeppsfvgwflgwddsywsvdpldr
alaelaa
>d1d0nb1 4.85.1.1.3 (27-152) Gelsolin {Horse (Equus caballus)}
vehpeflkagkepglqiwrvekfdlvpvppnlygdfftgdayvilktvqlrngilqydlh
ywlgnecsqdesgaaaiftvqlddylngravqhrevqgfesatflgyfksglkykkggva
sgfkhv
>d1d0nb2 4.85.1.1.3 (153-262) Gelsolin {Horse (Equus caballus)}
vpnevvvqrllqvkgrrvvratevpvswesfnngdcfildlgnniyqwcgsksnrferlk
atqvskgirdnersgraqvsvfeegaepeamlqvlgpkptlpeatedtvk
>d1d0nb3 4.85.1.1.3 (263-383) Gelsolin {Horse (Equus caballus)}
edaanrklaklykvsngagpmvvslvadenpfaqgalrsedcfildhgkdgkifvwkgkq
anmeerkaalktasdfiskmdypkqtqvsvlpeggetplfrqffknwrdpdqteglglay
l
>d1d0nb4 4.85.1.1.3 (384-532) Gelsolin {Horse (Equus caballus)}
sshiahvervpfdaatlhtstamaaqhgmdddgtgqkqiwrvegsnkvpvdpatygqfyg
gdsyiilynyrhgsrqgqiiynwqgaqstqdevaasailtaqldeelggtpvqsrvvqgk
epahlmslfggkpmivykggtsreggqta
>d1d0nb5 4.85.1.1.3 (533-628) Gelsolin {Horse (Equus caballus)}
pastrlfqvrasssgatraveiipkagalnsndafvlktpsaaylwvgagaseaektgaq
ellrvlraqpvqvaegsepdsfwealggkatyrtsp
>d1d0nb6 4.85.1.1.3 (629-755) Gelsolin {Horse (Equus caballus)}
rlkdkkmdahpprlfacsnkigrfvieevpgefmqedlatddvmlldtwdqvfvwvgkds
qdeektealtsakryidtdpahrdrrtpitvvkqgfeppsfvgwflgwddsywsvdpldr
alaelaa
>d1d1la_ 1.36.1.2.5 cro lambda repressor {Bacteriophage lambda (Escherichia coli)}
meqritlkdyamrfgqtktakdlgvyqsainkaihagrkifltinadgsvyaeevkpwps
n
>d1d1ma_ 1.36.1.2.5 cro lambda repressor {Bacteriophage lambda (Escherichia coli)}
meqritlkdyamrfgqtktakdlgvyqsainkaihagrkifltinadgsvyaeevkdgev
kpwps
>d1d1mb_ 1.36.1.2.5 cro lambda repressor {Bacteriophage lambda (Escherichia coli)}
meqritlkdyamrfgqtktakdlgvyqsainkaihagrkifltinadgsvyaeevkdgev
kpwps
>d1d1ra_ 4.49.1.1.2 YciH {Escherichia coli}
kgdgvvriqrqtsgrkgkgvclitgvdlddaeltklaaelkkkcgcggavkdgvieiqgd
krdllkslleakgmkvklaggle
>d1d1sa1 2.31.1.2.2 (1-174,325-374) Alcohol dehydrogenase {Human (Homo sapiens)}
gtagkvikckaavlweqkqpfsieeievappktkevrikilatgicrtddhvikgtmvsk
fpvivgheatgivesigegvttvkpgdkviplflpqcrecnacrnpdgnlcirsditgrg
vladgttrftckgkpvhhfmntstfteytvvdessvakiddaappekvcligcXrddvpk
lvteflakkfdldqlithvlpfkkisegfellnsgqsirtvltf
>d1d1sa2 3.2.1.1.2 (175-324) Alcohol dehydrogenase {Human (Homo sapiens), different isozymes}
gfstgygaavktgkvkpgstcvvfglggvglsvimgcksagasriigidlnkdkfekama
vgatecispkdstkpisevlsemtgnnvgytfevighletmidalaschmnygtsvvvgv
ppsakmltydpmllftgrtwkgcvfgglks
>d1d1sb1 2.31.1.2.2 (1-174,325-374) Alcohol dehydrogenase {Human (Homo sapiens)}
gtagkvikckaavlweqkqpfsieeievappktkevrikilatgicrtddhvikgtmvsk
fpvivgheatgivesigegvttvkpgdkviplflpqcrecnacrnpdgnlcirsditgrg
vladgttrftckgkpvhhfmntstfteytvvdessvakiddaappekvcligcXrddvpk
lvteflakkfdldqlithvlpfkkisegfellnsgqsirtvltf
>d1d1sb2 3.2.1.1.2 (175-324) Alcohol dehydrogenase {Human (Homo sapiens), different isozymes}
gfstgygaavktgkvkpgstcvvfglggvglsvimgcksagasriigidlnkdkfekama
vgatecispkdstkpisevlsemtgnnvgytfevighletmidalaschmnygtsvvvgv
ppsakmltydpmllftgrtwkgcvfgglks
>d1d1sc1 2.31.1.2.2 (1-174,325-374) Alcohol dehydrogenase {Human (Homo sapiens)}
gtagkvikckaavlweqkqpfsieeievappktkevrikilatgicrtddhvikgtmvsk
fpvivgheatgivesigegvttvkpgdkviplflpqcrecnacrnpdgnlcirsditgrg
vladgttrftckgkpvhhfmntstfteytvvdessvakiddaappekvcligcXrddvpk
lvteflakkfdldqlithvlpfkkisegfellnsgqsirtvltf
>d1d1sc2 3.2.1.1.2 (175-324) Alcohol dehydrogenase {Human (Homo sapiens), different isozymes}
gfstgygaavktgkvkpgstcvvfglggvglsvimgcksagasriigidlnkdkfekama
vgatecispkdstkpisevlsemtgnnvgytfevighletmidalaschmnygtsvvvgv
ppsakmltydpmllftgrtwkgcvfgglks
>d1d1sd1 2.31.1.2.2 (1-174,325-374) Alcohol dehydrogenase {Human (Homo sapiens)}
gtagkvikckaavlweqkqpfsieeievappktkevrikilatgicrtddhvikgtmvsk
fpvivgheatgivesigegvttvkpgdkviplflpqcrecnacrnpdgnlcirsditgrg
vladgttrftckgkpvhhfmntstfteytvvdessvakiddaappekvcligcXrddvpk
lvteflakkfdldqlithvlpfkkisegfellnsgqsirtvltf
>d1d1sd2 3.2.1.1.2 (175-324) Alcohol dehydrogenase {Human (Homo sapiens), different isozymes}
gfstgygaavktgkvkpgstcvvfglggvglsvimgcksagasriigidlnkdkfekama
vgatecispkdstkpisevlsemtgnnvgytfevighletmidalaschmnygtsvvvgv
ppsakmltydpmllftgrtwkgcvfgglks
>d1d1ta1 2.31.1.2.2 (1-174,325-374) Alcohol dehydrogenase {Human (Homo sapiens)}
gtagkvikckaavlweqkqpfsieeievappktkevrikilatgicrtddhvikgtmvsk
fpvivgheatgivesigegvttvkpgdkviplflpqcrecnacrnpdgnlcirsditgrg
vladgttrftckgkpvhhflntstfteytvvdessvakiddaappekvcligcXrddvpk
lvteflakkfdldqlithvlpfkkisegfellnsgqsirtvltf
>d1d1ta2 3.2.1.1.2 (175-324) Alcohol dehydrogenase {Human (Homo sapiens), different isozymes}
gfstgygaavktgkvkpgstcvvfglggvglsvimgcksagasriigidlnkdkfekama
vgatecispkdstkpisevlsemtgnnvgytfevighletmidalaschmnygtsvvvgv
ppsakmltydpmllftgrtwkgcvfgglks
>d1d1tb1 2.31.1.2.2 (1-174,325-374) Alcohol dehydrogenase {Human (Homo sapiens)}
gtagkvikckaavlweqkqpfsieeievappktkevrikilatgicrtddhvikgtmvsk
fpvivgheatgivesigegvttvkpgdkviplflpqcrecnacrnpdgnlcirsditgrg
vladgttrftckgkpvhhflntstfteytvvdessvakiddaappekvcligcXrddvpk
lvteflakkfdldqlithvlpfkkisegfellnsgqsirtvltf
>d1d1tb2 3.2.1.1.2 (175-324) Alcohol dehydrogenase {Human (Homo sapiens), different isozymes}
gfstgygaavktgkvkpgstcvvfglggvglsvimgcksagasriigidlnkdkfekama
vgatecispkdstkpisevlsemtgnnvgytfevighletmidalaschmnygtsvvvgv
ppsakmltydpmllftgrtwkgcvfgglks
>d1d1tc1 2.31.1.2.2 (1-174,325-374) Alcohol dehydrogenase {Human (Homo sapiens)}
gtagkvikckaavlweqkqpfsieeievappktkevrikilatgicrtddhvikgtmvsk
fpvivgheatgivesigegvttvkpgdkviplflpqcrecnacrnpdgnlcirsditgrg
vladgttrftckgkpvhhflntstfteytvvdessvakiddaappekvcligcXrddvpk
lvteflakkfdldqlithvlpfkkisegfellnsgqsirtvltf
>d1d1tc2 3.2.1.1.2 (175-324) Alcohol dehydrogenase {Human (Homo sapiens), different isozymes}
gfstgygaavktgkvkpgstcvvfglggvglsvimgcksagasriigidlnkdkfekama
vgatecispkdstkpisevlsemtgnnvgytfevighletmidalaschmnygtsvvvgv
ppsakmltydpmllftgrtwkgcvfgglks
>d1d1td1 2.31.1.2.2 (1-174,325-374) Alcohol dehydrogenase {Human (Homo sapiens)}
gtagkvikckaavlweqkqpfsieeievappktkevrikilatgicrtddhvikgtmvsk
fpvivgheatgivesigegvttvkpgdkviplflpqcrecnacrnpdgnlcirsditgrg
vladgttrftckgkpvhhflntstfteytvvdessvakiddaappekvcligcXrddvpk
lvteflakkfdldqlithvlpfkkisegfellnsgqsirtvltf
>d1d1td2 3.2.1.1.2 (175-324) Alcohol dehydrogenase {Human (Homo sapiens), different isozymes}
gfstgygaavktgkvkpgstcvvfglggvglsvimgcksagasriigidlnkdkfekama
vgatecispkdstkpisevlsemtgnnvgytfevighletmidalaschmnygtsvvvgv
ppsakmltydpmllftgrtwkgcvfgglks
>d1d1za_ 4.72.1.1.21 The Xlp protein Sap {Human (Homo sapiens)}
vavyhgkisretgeklllatgldgsyllrdsesvpgvyclcvlyhgyiytyrvsqtetgs
wsaetapgvhkryfrkiknlisafqkpdqgiviplqypvek
>d1d1zb_ 4.72.1.1.21 The Xlp protein Sap {Human (Homo sapiens)}
vavyhgkisretgeklllatgldgsyllrdsesvpgvyclcvlyhgyiytyrvsqtetgs
wsaetapgvhkryfrkiknlisafqkpdqgiviplqypvek
>d1d1zc_ 4.72.1.1.21 The Xlp protein Sap {Human (Homo sapiens)}
vavyhgkisretgeklllatgldgsyllrdsesvpgvyclcvlyhgyiytyrvsqtetgs
wsaetapgvhkryfrkiknlisafqkpdqgiviplqypvek
>d1d1zd_ 4.72.1.1.21 The Xlp protein Sap {Human (Homo sapiens)}
vavyhgkisretgeklllatgldgsyllrdsesvpgvyclcvlyhgyiytyrvsqtetgs
wsaetapgvhkryfrkiknlisafqkpdqgiviplqypvek
>d1d2ca_ 3.56.1.2.1 Glycine <i>N</i>-methyltransferase {Rat (Rattus norvegicus)}
vdsvyrtrslgvaaegipdqyadgeaarvwqlyigdtrsrtaeykawllgllrqhgchrv
ldvacgtgvdsimlveegfsvtsvdasdkmlkyalkerwnrrkepafdkwvieeanwltl
dkdvpagdgfdaviclgnsfahlpdskgdqsehrlalkniasmvrpggllvidhrnydyi
lstgcappgkniyyksdltkdittsvltvnnkahmvtldytvqvpgagrdgapgfskfrl
syyphclasftelvqeafggrcqhsvlgdfkpyrpgqayvpcyfihvlkktg
>d1d2cb_ 3.56.1.2.1 Glycine <i>N</i>-methyltransferase {Rat (Rattus norvegicus)}
vdsvyrtrslgvaaegipdqyadgeaarvwqlyigdtrsrtaeykawllgllrqhgchrv
ldvacgtgvdsimlveegfsvtsvdasdkmlkyalkerwnrrkepafdkwvieeanwltl
dkdvpagdgfdaviclgnsfahlpdskgdqsehrlalkniasmvrpggllvidhrnydyi
lstgcappgkniyyksdltkdittsvltvnnkahmvtldytvqvpgagrdgapgfskfrl
syyphclasftelvqeafggrcqhsvlgdfkpyrpgqayvpcyfihvlkktg
>d1d2ea1 2.38.3.1.4 (251-348) Elongation factor Tu (EF-Tu), domain 2 {Bovine (Bos taurus), mitochondrial}
trdlekpfllpvesvysipgrgtvvtgtlergilkkgdeceflghsknirtvvtgiemfh
ksldraeagdnlgalvrglkredlrrglvmakpgsiqp
>d1d2ea2 2.39.1.1.4 (349-451) Elongation factor Tu (EF-Tu), C-terminal domain {Bovine (Bos taurus), mitochondrial}
hqkveaqvyiltkeeggrhkpfvshfmpvmfsltwdmacriilppgkelampgedlkltl
ilrqpmilekgqrftlrdgnrtigtglvtdtpamteedknikw
>d1d2ea3 3.30.1.6.17 (55-250) Elongation factor Tu (EF-Tu), N-terminal (G) domain {Bovine (Bos taurus), mitochondrial}
kphvnvgtighvdhgkttltaaitkilaegggakfkkyeeidnapeerargitinaahve
ystaarhyahtdcpghadyvknmitgtapldgcilvvaandgpmpqtrehlllarqigve
hvvvyvnkadavqdsemvelveleirelltefgykgeetpiivgsalcaleqrdpelglk
svqklldavdtyipvp
>d1d2eb1 2.38.3.1.4 (251-348) Elongation factor Tu (EF-Tu), domain 2 {Bovine (Bos taurus), mitochondrial}
trdlekpfllpvesvysipgrgtvvtgtlergilkkgdeceflghsknirtvvtgiemfh
ksldraeagdnlgalvrglkredlrrglvmakpgsiqp
>d1d2eb2 2.39.1.1.4 (349-451) Elongation factor Tu (EF-Tu), C-terminal domain {Bovine (Bos taurus), mitochondrial}
hqkveaqvyiltkeeggrhkpfvshfmpvmfsltwdmacriilppgkelampgedlkltl
ilrqpmilekgqrftlrdgnrtigtglvtdtpamteedknikw
>d1d2eb3 3.30.1.6.17 (55-250) Elongation factor Tu (EF-Tu), N-terminal (G) domain {Bovine (Bos taurus), mitochondrial}
kphvnvgtighvdhgkttltaaitkilaegggakfkkyeeidnapeerargitinaahve
ystaarhyahtdcpghadyvknmitgtapldgcilvvaandgpmpqtrehlllarqigve
hvvvyvnkadavqdsemvelveleirelltefgykgeetpiivgsalcaleqrdpelglk
svqklldavdtyipvp
>d1d2ec1 2.38.3.1.4 (251-348) Elongation factor Tu (EF-Tu), domain 2 {Bovine (Bos taurus), mitochondrial}
trdlekpfllpvesvysipgrgtvvtgtlergilkkgdeceflghsknirtvvtgiemfh
ksldraeagdnlgalvrglkredlrrglvmakpgsiqp
>d1d2ec2 2.39.1.1.4 (349-451) Elongation factor Tu (EF-Tu), C-terminal domain {Bovine (Bos taurus), mitochondrial}
hqkveaqvyiltkeeggrhkpfvshfmpvmfsltwdmacriilppgkelampgedlkltl
ilrqpmilekgqrftlrdgnrtigtglvtdtpamteedknikw
>d1d2ec3 3.30.1.6.17 (55-250) Elongation factor Tu (EF-Tu), N-terminal (G) domain {Bovine (Bos taurus), mitochondrial}
kphvnvgtighvdhgkttltaaitkilaegggakfkkyeeidnapeerargitinaahve
ystaarhyahtdcpghadyvknmitgtapldgcilvvaandgpmpqtrehlllarqigve
hvvvyvnkadavqdsemvelveleirelltefgykgeetpiivgsalcaleqrdpelglk
svqklldavdtyipvp
>d1d2ed1 2.38.3.1.4 (251-348) Elongation factor Tu (EF-Tu), domain 2 {Bovine (Bos taurus), mitochondrial}
trdlekpfllpvesvysipgrgtvvtgtlergilkkgdeceflghsknirtvvtgiemfh
ksldraeagdnlgalvrglkredlrrglvmakpgsiqp
>d1d2ed2 2.39.1.1.4 (349-451) Elongation factor Tu (EF-Tu), C-terminal domain {Bovine (Bos taurus), mitochondrial}
hqkveaqvyiltkeeggrhkpfvshfmpvmfsltwdmacriilppgkelampgedlkltl
ilrqpmilekgqrftlrdgnrtigtglvtdtpamteedknikw
>d1d2ed3 3.30.1.6.17 (55-250) Elongation factor Tu (EF-Tu), N-terminal (G) domain {Bovine (Bos taurus), mitochondrial}
kphvnvgtighvdhgkttltaaitkilaegggakfkkyeeidnapeerargitinaahve
ystaarhyahtdcpghadyvknmitgtapldgcilvvaandgpmpqtrehlllarqigve
hvvvyvnkadavqdsemvelveleirelltefgykgeetpiivgsalcaleqrdpelglk
svqklldavdtyipvp
>d1d2ga_ 3.56.1.2.1 Glycine <i>N</i>-methyltransferase {Rat (Rattus norvegicus)}
vdsvyrtrslgvaaegipdqyadgeaarvwqlyigdtrsrtaeykawllgllrqhgchrv
ldvacgtgvdsimlveegfsvtsvdasdkmlkyalkerwnrrkepafdkwvieeanwltl
dkdvpagdgfdaviclgnsfahlpdskgdqsehrlalkniasmvrpggllvidhknydyi
lstgcappgkniyyksdltkdittsvltvnnkahmvtldytvqvpgagrdgapgfskfrl
syyphclasftelvqeafggrcqhsvlgdfkpyrpgqayvpcyfihvlkktg
>d1d2gb_ 3.56.1.2.1 Glycine <i>N</i>-methyltransferase {Rat (Rattus norvegicus)}
vdsvyrtrslgvaaegipdqyadgeaarvwqlyigdtrsrtaeykawllgllrqhgchrv
ldvacgtgvdsimlveegfsvtsvdasdkmlkyalkerwnrrkepafdkwvieeanwltl
dkdvpagdgfdaviclgnsfahlpdskgdqsehrlalkniasmvrpggllvidhknydyi
lstgcappgkniyyksdltkdittsvltvnnkahmvtldytvqvpgagrdgapgfskfrl
syyphclasftelvqeafggrcqhsvlgdfkpyrpgqayvpcyfihvlkktg
>d1d2ha_ 3.56.1.2.1 Glycine <i>N</i>-methyltransferase {Rat (Rattus norvegicus)}
taeykawllgllrqhgchrvldvacgtgvdsimlveegfsvtsvdasdkmlkyalkerwn
rrkepafdkwvieeanwltldkdvpagdgfdaviclgnsfahlpdskgdqsehrlalkni
asmvrpggllvidhknydyilstgcappgkniyyksdltkdittsvltvnnkahmvtldy
tvqvpgagrdgapgfskfrlsyyphclasftelvqeafggrcqhsvlgdfkpyrpgqayv
pcyfihvlkktg
>d1d2hb_ 3.56.1.2.1 Glycine <i>N</i>-methyltransferase {Rat (Rattus norvegicus)}
taeykawllgllrqhgchrvldvacgtgvdsimlveegfsvtsvdasdkmlkyalkerwn
rrkepafdkwvieeanwltldkdvpagdgfdaviclgnsfahlpdskgdqsehrlalkni
asmvrpggllvidhknydyilstgcappgkniyyksdltkdittsvltvnnkahmvtldy
tvqvpgagrdgapgfskfrlsyyphclasftelvqeafggrcqhsvlgdfkpyrpgqayv
pcyfihvlkktg
>d1d2hc_ 3.56.1.2.1 Glycine <i>N</i>-methyltransferase {Rat (Rattus norvegicus)}
taeykawllgllrqhgchrvldvacgtgvdsimlveegfsvtsvdasdkmlkyalkerwn
rrkepafdkwvieeanwltldkdvpagdgfdaviclgnsfahlpdskgdqsehrlalkni
asmvrpggllvidhknydyilstgcappgkniyyksdltkdittsvltvnnkahmvtldy
tvqvpgagrdgapgfskfrlsyyphclasftelvqeafggrcqhsvlgdfkpyrpgqayv
pcyfihvlkktg
>d1d2hd_ 3.56.1.2.1 Glycine <i>N</i>-methyltransferase {Rat (Rattus norvegicus)}
taeykawllgllrqhgchrvldvacgtgvdsimlveegfsvtsvdasdkmlkyalkerwn
rrkepafdkwvieeanwltldkdvpagdgfdaviclgnsfahlpdskgdqsehrlalkni
asmvrpggllvidhknydyilstgcappgkniyyksdltkdittsvltvnnkahmvtldy
tvqvpgagrdgapgfskfrlsyyphclasftelvqeafggrcqhsvlgdfkpyrpgqayv
pcyfihvlkktg
>d1d2na_ 3.30.1.10.4 Hexamerization domain of N-ethylmalemide-sensitive fusion (NESF) protein {Chinese hamster (Cricetulus griseus)}
edyasyimngiikwgdpvtrvlddgellvqqtknsdrtplvsvllegpphsgktalaaki
aeesnfpfikicspdkmigfsetakcqamkkifddayksqlscvvvddierlldyvpigp
rfsnlvlqallvllkkappqgrklliigttsrkdvlqememlnafsttihvpniatgeql
lealellgnfkdkerttiaqqvkgkkvwigikkllmliemslqmdpeyrvrkflallree
gaspld
>d1d2wa_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytmgighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1d2ya_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkamgrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1d3fa_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvmtk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1d3ja_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaekmfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1d3ma_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnakmkpvydsmdavrraaminmvfqmgetgvagftnsmrm
mqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1d3na_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
nifexlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitkd
eaeklfnqdvdaavrgilrnakxkpvydsxdavrraaxinxvfqxgetgvagftnsxrxx
qqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1d3wa_ 4.47.1.2.1 Ferredoxin {Azotobacter vinelandii}
afvvtdncikckytecvevcpvdcfyegpnflvihpdecidcalcepecpaqaifsedev
pedmqefiqlnaelaevwpnitekkdplpdaedwdgvkgklqhler
>d1d3za_ 4.13.2.1.1 Ubiquitin {Human (Homo sapiens)}
mqifvktltgktitlevepsdtienvkakiqdkegippdqqrlifagkqledgrtlsdyn
iqkestlhlvlrlrgg
>d1d4aa_ 3.16.4.3.3 NAD(P)H:quinone reductase {Human (Homo sapiens)}
vgrralivlahsertsfnyamkeaaaaalkkkgwevvesdlyamnfnpiisrkditgklk
dpanfqypaesvlaykeghlspdivaeqkkleaadlvifqfplqwfgvpailkgwfervf
igefaytyaamydkgpfrskkavlsittggsgsmyslqgihgdmnvilwpiqsgilhfcg
fqvlepqltysightpadariqilegwkkrleniwdetplyfapsslfdlnfqagflmkk
evqdeeknkkfglsvghhlgksiptdnqikark
>d1d4ab_ 3.16.4.3.3 NAD(P)H:quinone reductase {Human (Homo sapiens)}
vgrralivlahsertsfnyamkeaaaaalkkkgwevvesdlyamnfnpiisrkditgklk
dpanfqypaesvlaykeghlspdivaeqkkleaadlvifqfplqwfgvpailkgwfervf
igefaytyaamydkgpfrskkavlsittggsgsmyslqgihgdmnvilwpiqsgilhfcg
fqvlepqltysightpadariqilegwkkrleniwdetplyfapsslfdlnfqagflmkk
evqdeeknkkfglsvghhlgksiptdnqikark
>d1d4ac_ 3.16.4.3.3 NAD(P)H:quinone reductase {Human (Homo sapiens)}
vgrralivlahsertsfnyamkeaaaaalkkkgwevvesdlyamnfnpiisrkditgklk
dpanfqypaesvlaykeghlspdivaeqkkleaadlvifqfplqwfgvpailkgwfervf
igefaytyaamydkgpfrskkavlsittggsgsmyslqgihgdmnvilwpiqsgilhfcg
fqvlepqltysightpadariqilegwkkrleniwdetplyfapsslfdlnfqagflmkk
evqdeeknkkfglsvghhlgksiptdnqikark
>d1d4ad_ 3.16.4.3.3 NAD(P)H:quinone reductase {Human (Homo sapiens)}
vgrralivlahsertsfnyamkeaaaaalkkkgwevvesdlyamnfnpiisrkditgklk
dpanfqypaesvlaykeghlspdivaeqkkleaadlvifqfplqwfgvpailkgwfervf
igefaytyaamydkgpfrskkavlsittggsgsmyslqgihgdmnvilwpiqsgilhfcg
fqvlepqltysightpadariqilegwkkrleniwdetplyfapsslfdlnfqagflmkk
evqdeeknkkfglsvghhlgksiptdnqikark
>e1d4p.1a 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
eadcglrplfekksledkterellesyi
>e1d4p.1b 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqf
>d1d4sa_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpfnvigrnlltqigctlnf
>d1d4sb_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpfnvigrnlltqigctlnf
>d1d4ta_ 4.72.1.1.21 The Xlp protein Sap {Human (Homo sapiens)}
mdavavyhgkisretgeklllatgldgsyllrdsesvpgvyclcvlyhgyiytyrvsqte
tgswsaetapgvhkryfrkiknlisafqkpdqgiviplqypvek
>d1d4ua1 1.6.1.2.1 (37-111) DNA repair factor XPA DNA- and RPA-binding domain, C-terminal subdomain {Human (Homo sapiens)}
dkhklitkteakqeyllkdcdlekrepplkfivkknphhsqwgdmklylklqivkrslev
wgsqealeeakevrq
>d1d4ua2 7.33.1.5.1 (1-36) DNA repair factor XPA DNA- and RPA-binding domain, N-terminal subdomain {Human (Homo sapiens)}
mefdyviceecgkefmdsylmdhfdlptcddcrdad
>d1d4wa_ 4.72.1.1.21 The Xlp protein Sap {Human (Homo sapiens)}
mdavavyhgkisretgeklllatgldgsyllrdsesvpgvyclcvlyhgyiytyrvsqte
tgswsaetapgvhkryfrkiknlisafqkpdqgiviplqypvek
>d1d4wb_ 4.72.1.1.21 The Xlp protein Sap {Human (Homo sapiens)}
avavyhgkisretgeklllatgldgsyllrdsesvpgvyclcvlyhgyiytyrvsqtetg
swsaetapgvhkryfrkiknlisafqkpdqgiviplqypvek
>d1d4ya_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwkrplvtikiggqlkealldtgaddtvieemslpgrwkpkmiggiggfikvrqyd
qiiieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1d4yb_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwkrplvtikiggqlkealldtgaddtvieemslpgrwkpkmiggiggfikvrqyd
qiiieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1d4za_ 3.16.2.1.1 CheY protein {Escherichia coli}
adkelkflvvddfstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmp
nmdglellktiradgamsalpvlmvtaeakkenviaaaqagasgyvvkpftpatleekln
kifeklgm
>e1d5d.1b 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
nycnqmmksrnltkdrckpvntfvhesladvqavcsqknvackngqtncyqsystmsitd
cretgsskypncaykttqankhiivacegnpyvpvhfdasv
>e1d5e.1b 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
nycnqmmksrnltkdrckpvntfvhesladvqavcsqknvackngqtncyqsystmsitd
cretgsskypncaykttqankhiivacegnpyvpvhfdasv
>e1d5h.1b 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
nycnqmmksrnltkdrckpvntfvhesladvqavcsqknvackngqtncyqsystmsitd
cretgsskypncaykttqankhiivacegnpyvpvhfdasv
>d1d66a1 7.32.1.1.1 (8-48) Gal4 {Baker's yeast (Saccharomyces cerevisiae)}
eqacdicrlkklkcskekpkcakclknnwecryspktkrsp
>d1d66b1 7.32.1.1.1 (8-48) Gal4 {Baker's yeast (Saccharomyces cerevisiae)}
eqacdicrlkklkcskekpkcakclknnwecryspktkrsp
>d1d6oa_ 4.23.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1d6ob_ 4.23.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1d7ha_ 4.23.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1d7hb_ 4.23.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1d7ia_ 4.23.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1d7ib_ 4.23.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1d7ja_ 4.23.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1d7jb_ 4.23.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1daaa_ 5.13.1.1.1 D-amino acid aminotransferase {Bacillus strain YM-1}
gytlwndqivkdeevkidkedrgyqfgdgvyevvkvyngemftvnehidrlyasaekiri
tipytkdkfhqllhelveknelntghiyfqvtrgtsprahqfpentvkpviigytkenpr
plenlekgvkatfvedirwlrcdikslnllgavlakqeahekgcyeailhrnntvtegss
snvfgikdgilythpannmilkgitrdvviacaneinmpvkeipftthealkmdelfvts
ttseitpvieidgklirdgkvgewtrklqkqfetkip
>d1daab_ 5.13.1.1.1 D-amino acid aminotransferase {Bacillus strain YM-1}
gytlwndqivkdeevkidkedrgyqfgdgvyevvkvyngemftvnehidrlyasaekiri
tipytkdkfhqllhelveknelntghiyfqvtrgtsprahqfpentvkpviigytkenpr
plenlekgvkatfvedirwlrcdikslnllgavlakqeahekgcyeailhrnntvtegss
snvfgikdgilythpannmilkgitrdvviacaneinmpvkeipftthealkmdelfvts
ttseitpvieidgklirdgkvgewtrklqkqfetkip
>d1dad__ 3.30.1.8.1 Dethiobiotin synthetase {Escherichia coli}
skryfvtgtdtevgktvascallqaakaagyrtagykpvasgsektpeglrnsdalalqr
nsslqldyatvnpytfaeptsphiisaqegrpieslvmsaglraleqqadwvlvegaggw
ftplsdtftfadwvtqeqlpvilvvgvklgcinhamltaqviqhagltlagwvandvtpp
gkrhaeymttltrmipapllgeipwlaenpenaatgkyinlall
>d1dae__ 3.30.1.8.1 Dethiobiotin synthetase {Escherichia coli}
skryfvtgtdtevgktvascallqaakaagyrtagykpvasgsektpeglrnsdalalqr
nsslqldyatvnpytfaeptsphiisaqegrpieslvmsaglraleqqadwvlvegaggw
ftplsdtftfadwvtqeqlpvilvvgvklgcinhamltaqviqhagltlagwvandvtpp
gkrhaeymttltrmipapllgeipwlaenpenaatgkyinlall
>d1daf__ 3.30.1.8.1 Dethiobiotin synthetase {Escherichia coli}
skryfvtgtdtevgktvascallqaakaagyrtagykpvasgsektpeglrnsdalalqr
nsslqldyatvnpytfaeptsphiisaqegrpieslvmsaglraleqqadwvlvegaggw
ftplsdtftfadwvtqeqlpvilvvgvklgcinhamltaqviqhagltlagwvandvtpp
gkrhaeymttltrmipapllgeipwlaenpenaatgkyinlall
>d1dag__ 3.30.1.8.1 Dethiobiotin synthetase {Escherichia coli}
skryfvtgtdtevgktvascallqaakaagyrtagykpvasgsektpeglrnsdalalqr
nsslqldyatvnpytfaeptsphiisaqegrpieslvmsaglraleqqadwvlvegaggw
ftplsdtftfadwvtqeqlpvilvvgvklgcinhamltaqviqhagltlagwvandvtpp
gkrhaeymttltrmipapllgeipwlaenpenaatgkyinlall
>d1dah__ 3.30.1.8.1 Dethiobiotin synthetase {Escherichia coli}
skryfvtgtdtevgktvascallqaakaagyrtagykpvasgsektpeglrnsdalalqr
nsslqldyatvnpytfaeptsphiisaqegrpieslvmsaglraleqqadwvlvegaggw
ftplsdtftfadwvtqeqlpvilvvgvklgcinhamltaqviqhagltlagwvandvtpp
gkrhaeymttltrmipapllgeipwlaenpenaatgkyinlall
>d1dai__ 3.30.1.8.1 Dethiobiotin synthetase {Escherichia coli}
skryfvtgtdtevgktvascallqaakaagyrtagykpvasgsektpeglrnsdalalqr
nsslqldyatvnpytfaeptsphiisaqegrpieslvmsaglraleqqadwvlvegaggw
ftplsdtftfadwvtqeqlpvilvvgvklgcinhamltaqviqhagltlagwvandvtpp
gkrhaeymttltrmipapllgeipwlaenpenaatgkyinlall
>d1daj__ 3.61.1.1.6 Dihydrofolate reductases, eukaryotic type {Fungus (Pneumocystis carinii)}
mnqqksltlivalttsygigrsnslpwklkkeisyfkrvtsfvptfdsfesmnvvlmgrk
twesiplqfrplkgrinvvitrnesldlgngihsaksldhalellyrtygsessvqinri
fviggaqlykaamdhpkldrimatiiykdihcdvffplkfrdkewssvwkkekhsdlesw
vgtkvphgkinedgfdyefemwtrdl
>d1daka_ 3.30.1.8.1 Dethiobiotin synthetase {Escherichia coli}
skryfvtgtdtevgktvascallqaakaagyrtagykpvasgsektpeglrnsdalalqr
nsslqldyatvnpytfaeptsphiisaqegrpieslvmsaglraleqqadwvlvegaggw
ftplsdtftfadwvtqeqlpvilvvgvklgcinhamltaqviqhagltlagwvandvtpp
gkrhaeymttltrmipapllgeipwlaenpenaatgkyinlall
>d1dama_ 3.30.1.8.1 Dethiobiotin synthetase {Escherichia coli}
skryfvtgtdtevgktvascallqaakaagyrtagykpvasgsektpeglrnsdalalqr
nsslqldyatvnpytfaeptsphiisaqegrpieslvmsaglraleqqadwvlvegaggw
ftplsdtftfadwvtqeqlpvilvvgvklgcinhamltaqviqhagltlagwvandvtpp
gkrhaeymttltrmipapllgeipwlaenpenaatgkyinlall
>e1dan.1t 2.1.2.1.1 Extracellular region of human tissue factor {Human (Homo sapiens)}
tvaaynltwkstnfktilewepkpvnqvytvqistksgdwkskcfyttdtecdltdeivk
dvkqtylarvfsypa
>d1danh_ 2.41.1.2.21 Coagulation factor VIIa {Human (Homo sapiens)}
ivggkvcpkgecpwqvlllvngaqlcggtlintiwvvsaahcfdkiknwrnliavlgehd
lsehdgdeqsrrvaqviipstyvpgttnhdiallrlhqpvvltdhvvplclpertfsert
lafvrfslvsgwgqlldrgatalelmvlnvprlmtqdclqqsrkvgdspniteymfcagy
sdgskdsckgdsggphathyrgtwyltgivswgqgcatvghfgvytrvsqyiewlqklmr
seprpgvllrapfp
>d1danl1 7.3.11.1.3 (47-86) Coagulation factor VIIa {Human (Homo sapiens)}
gdqcasspcqnggsckdqlqsyicfclpafegrncethkd
>d1danl2 7.3.11.1.3 (87-142) Coagulation factor VIIa {Human (Homo sapiens)}
dqlicvnenggceqycsdhtgtkrscrchegyslladgvsctptveypcgkipile
>d1danu1 2.1.2.1.1 (107-210) Extracellular region of human tissue factor {Human (Homo sapiens)}
nlgqptiqsfeqvgtkvnvtvedertlvrrnntflslrdvfgkdliytlyywkssssgkk
taktntneflidvdkgenycfsvqavipsrtvnrkstdspvecm
>d1daoa1 3.4.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1daoa2 4.14.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1daob1 3.4.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1daob2 4.14.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1daoc1 3.4.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1daoc2 4.14.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1daod1 3.4.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1daod2 4.14.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1daoe1 3.4.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1daoe2 4.14.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1daof1 3.4.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1daof2 4.14.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1daog1 3.4.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1daog2 4.14.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1daoh1 3.4.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1daoh2 4.14.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1dapa1 3.2.1.3.12 (1-118,269-320) Diaminopimelic acid dehydrogenase (DAPDH) {Corynebacterium glutamicum}
mtnirvaivgygnlgrsvekliakqpdmdlvgifsrratldtktpvfdvadvdkhaddvd
vlflcmgsatdipeqapkfaqfactvdtydnhrdiprhrqvmneaataagnvalvstgXr
npdftassqiafgraahrmkqqgqsgaftvlevapyllspenlddliardv
>d1dapa2 4.61.1.2.1 (119-268) Diaminopimelic acid dehydrogenase (DAPDH) {Corynebacterium glutamicum}
wdpgmfsinrvyaaavlaehqqhtfwgpglsqghsdalrripgvqkavqytlpsedalek
arrgeagdltgkqthkrqcfvvadaadheriendirtmpdyfvgyevevnfideatfdse
htgmphgghvittgdtggfnhtveyilkld
>d1dapb1 3.2.1.3.12 (1-118,269-320) Diaminopimelic acid dehydrogenase (DAPDH) {Corynebacterium glutamicum}
mtnirvaivgygnlgrsvekliakqpdmdlvgifsrratldtktpvfdvadvdkhaddvd
vlflcmgsatdipeqapkfaqfactvdtydnhrdiprhrqvmneaataagnvalvstgXr
npdftassqiafgraahrmkqqgqsgaftvlevapyllspenlddliardv
>d1dapb2 4.61.1.2.1 (119-268) Diaminopimelic acid dehydrogenase (DAPDH) {Corynebacterium glutamicum}
wdpgmfsinrvyaaavlaehqqhtfwgpglsqghsdalrripgvqkavqytlpsedalek
arrgeagdltgkqthkrqcfvvadaadheriendirtmpdyfvgyevevnfideatfdse
htgmphgghvittgdtggfnhtveyilkld
>d1dar_1 2.38.3.1.5 (283-400) Elongation factor G (EF-G), domain II {Thermus thermophilus}
pldippikgttpegevveihpdpngplaalafkimadpyvgrltfirvysgtltsgsyvy
nttkgrkervarllrmhanhreeveelkagdlgavvglketitgdtlvgedaprvile
>d1dar_2 3.30.1.6.18 (1-282) Elongation factor G (EF-G), N-terminal (G) domain {Thermus thermophilus}
mavkveydlkrlrnigiaahidagktttterilyytgrihkigevhegaatmdfmeqere
rgititaavttcfwkdhriniidtpghvdftieversmrvldgaivvfdssqgvepqset
vwrqaekykvpriafankmdktgadlwlvirtmqerlgarpvvmqlpigredtfsgiidv
lrmkaytygndlgtdireipipeeyldqareyheklvevaadfdenimlkylegeeptee
elvaairkgtidlkitpvflgsalknkgvqllldavvdylps
>d1dar_3 4.12.1.1.1 (476-599) Elongation factor G (EF-G), domain IV {Thermus thermophilus}
vgkpqvayretitkpvdvegkfirqtggrgqyghvkikveplprgsgfefvnaivggvip
keyipavqkgieeamqsgpligfpvvdikvtlydgsyhevdssemafkiagsmaikeavq
kgdp
>d1dar_4 4.47.11.1.1 (600-689) Elongation factor G (EF-G), domain V {Thermus thermophilus}
vilepimrvevttpeeymgdvigdlnarrgqilgmeprgnaqvirafvplaemfgyatdl
rsktqgrgsfvmffdhyqevpkqvqeklik
>d1dat__ 1.26.1.1.5 (Apo)ferritin {Horse (Equus caballus), L chain}
ssqirqnysteveaavnrlvnlylrasytylslgfyfdrddvalegvchffrelaeekre
gaerllkmqnqrggralfqdlqkpsqdewgttpdamkaaivlekslnqalldlhalgsaq
adphlcdfleshfldeevklikkmgdhltniqrlvgsqaglgeylferltlkhd
>d1dax__ 4.47.1.4.2 Ferredoxin I {Sulfate-reducing bacteria (Desulfovibrio africanus)}
arkfyvdqdeciacescveiapgafamdpeiekayvkdvegasqeeveeamdtcpvqcih
wede
>d1dbah1 2.1.1.1.18 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
qiqlvqsgpelkkpgetvkisckasgyaftnygvnwvkeapgkelkwmgwiniytgepty
vddfkgrfafsletsastayleinnlknedtatyfctrgdyvnwyfdvwgagttvtvs
>d1dbah2 2.1.1.2.28 (113-228) Immunoglobulin (constant domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
sakttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqs
dlytlsssvtvpssprpsetvtcnvahpasstkvdkkivpr
>d1dbal1 2.1.1.1.18 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
dvvmtqiplslpvnlgdqasiscrssqslihsngntylhwylqkpgqspkllmykvsnrf
ygvpdrfsgsgsgtdftlkisrveaedlgiyfcsqsshvpptfgggtkleik
>d1dbal2 2.1.1.2.28 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1dbbh1 2.1.1.1.18 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
qiqlvqsgpelkkpgetvkisckasgyaftnygvnwvkeapgkelkwmgwiniytgepty
vddfkgrfafsletsastayleinnlknedtatyfctrgdyvnwyfdvwgagttvtvs
>d1dbbh2 2.1.1.2.28 (113-228) Immunoglobulin (constant domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
sakttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqs
dlytlsssvtvpssprpsetvtcnvahpasstkvdkkivpr
>d1dbbl1 2.1.1.1.18 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
dvvmtqiplslpvnlgdqasiscrssqslihsngntylhwylqkpgqspkllmykvsnrf
ygvpdrfsgsgsgtdftlkisrveaedlgiyfcsqsshvpptfgggtkleik
>d1dbbl2 2.1.1.2.28 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1dbh_1 1.84.1.1.1 (198-404) Son of sevenless-1 (sos-1) {Human (Homo sapiens)}
eqtyydlvkafmaeirqyirelnliikvfrepfvsnsklfsandvenifsrivdihelsv
kllghiedtvemtdegsphplvgscfedlaeelafdpyesyardilrpgfhdrflsqlsk
pgaalylqsigegfkeavqyvlprlllapvyhclhyfellkqleeksedqedkeclkqai
tallnvqsgmekicskslakrrlsesa
>d1dbh_2 2.49.1.1.8 (418-550) Son of sevenless-1 (sos-1) {Human (Homo sapiens)}
eqtyydlvkafmaeirqyirelnliikvfrepfvsnsklfsandvenifsrivdihelsv
kllghiedtvemtdegsphplvgscfedlaeelafdpyesyardilrpgfhdrflsqlsk
pgaalylqsigegfkeavqyvlprlllapvyhclhyfellkqleeksedqedkeclkqai
tallnvqsgmekicskslakrrlsesacrfysqqmkgkqlaikkmneiqknidgwegkdi
gqccnefimegtltrvgakherhiflfdglmiccksnhgqprlpgasnaeyrlkekffmr
kvqindkddtneykhafeiilkdensvifsaksaeeknnwmaalislqyrstl
>d1dbjh1 2.1.1.1.18 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
qiqlvqsgpelkkpgetvkisckasgyaftnygvnwvkeapgkelkwmgwiniytgepty
vddfkgrfafsletsastayleinnlknedtatyfctrgdyvnwyfdvwgagttvtvs
>d1dbjh2 2.1.1.2.28 (113-228) Immunoglobulin (constant domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
sakttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqs
dlytlsssvtvpssprpsetvtcnvahpasstkvdkkivpr
>d1dbjl1 2.1.1.1.18 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
dvvmtqiplslpvnlgdqasiscrssqslihsngntylhwylqkpgqspkllmykvsnrf
ygvpdrfsgsgsgtdftlkisrveaedlgiyfcsqsshvpptfgggtkleik
>d1dbjl2 2.1.1.2.28 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1dbkh1 2.1.1.1.18 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
qiqlvqsgpelkkpgetvkisckasgyaftnygvnwvkeapgkelkwmgwiniytgepty
vddfkgrfafsletsastayleinnlknedtatyfctrgdyvnwyfdvwgagttvtvs
>d1dbkh2 2.1.1.2.28 (113-228) Immunoglobulin (constant domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
sakttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqs
dlytlsssvtvpssprpsetvtcnvahpasstkvdkkivpr
>d1dbkl1 2.1.1.1.18 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
dvvmtqiplslpvnlgdqasiscrssqslihsngntylhwylqkpgqspkllmykvsnrf
ygvpdrfsgsgsgtdftlkisrveaedlgiyfcsqsshvpptfgggtkleik
>d1dbkl2 2.1.1.2.28 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1dbmh1 2.1.1.1.18 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
qiqlvqsgpelkkpgetvkisckasgyaftnygvnwvkeapgkelkwmgwiniytgepty
vddfkgrfafsletsastayleinnlknedtatyfctrgdyvnwyfdvwgagttvtvs
>d1dbmh2 2.1.1.2.28 (113-228) Immunoglobulin (constant domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
sakttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqs
dlytlsssvtvpssprpsetvtcnvahpasstkvdkkivpr
>d1dbml1 2.1.1.1.18 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
dvvmtqiplslpvnlgdqasiscrssqslihsngntylhwylqkpgqspkllmykvsnrf
ygvpdrfsgsgsgtdftlkisrveaedlgiyfcsqsshvpptfgggtkleik
>d1dbml2 2.1.1.2.28 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1dbp__ 3.83.1.1.1 D-ribose-binding protein {Escherichia coli, strain k-12}
kdtialvvstlnnpffvslkdgaqkeadklgynlvvldsqnnpakelanvqdltvrgtki
llinptdsdavdnavkmanqanipvitldrqatkgevvshiasdnvlggkiagdyiakka
gegakvielqgiagtsaarergegfqqavaahkfnvlasqpadfdrikglnvmqnlltah
pdvqavfaqndemalgalralqtagksdvmvvgfdgtpdgekavndgklaatiaqlpdqi
gakgvetadkvlkgekvqakypvdlklvvkq
>d1dbqa_ 3.83.1.1.7 Purine repressor (PurR), C-terminal domain {Escherichia coli}
ksigllatsseaayfaeiieavekncfqkgytlilgnawnnlekqraylsmmaqkrvdgl
lvmcseypepllamleeyrhipmvvmdwgeakadftdavidnafeggymagrylierghr
eigvipgplerntgagrlagfmkameeamikvpeswivqgdfepesgyramqqilsqphr
ptavfcggdimamgalcaademglrvpqdvsligydnvrnaryftpalttihqpkdslge
tafnmlldrivnkreepqsievhprlierrsvadgpfrdyrr
>d1dbqb_ 3.83.1.1.7 Purine repressor (PurR), C-terminal domain {Escherichia coli}
ksigllatsseaayfaeiieavekncfqkgytlilgnawnnlekqraylsmmaqkrvdgl
lvmcseypepllamleeyrhipmvvmdwgeakadftdavidnafeggymagrylierghr
eigvipgplerntgagrlagfmkameeamikvpeswivqgdfepesgyramqqilsqphr
ptavfcggdimamgalcaademglrvpqdvsligydnvrnaryftpalttihqpkdslge
tafnmlldrivnkreepqsievhprlierrsvadgpfrdyrr
>d1dbra_ 3.51.1.1.3 Hypoxantine-guanine-xanthine PRTase (HGPRTase) {Toxoplasma gondii}
askpiedygkgkgriepmyipdntfynaddflvpphckpyidkillpgglvkdrveklay
dihrtyfgeelhiicilkgsrgffnllidylatiqkysgressvppffehyvrlksyqnd
nstgqltvlsddlsifrdkhvlivedivdtgftltefgerlkavgpksmriatlvekrtd
rsnslkgdfvgfsiedvwivgccydfnemfrdfdhvavlsdaarkkfekv
>d1dbrb_ 3.51.1.1.3 Hypoxantine-guanine-xanthine PRTase (HGPRTase) {Toxoplasma gondii}
askpiedygkgkgriepmyipdntfynaddflvpphckpyidkillpgglvkdrveklay
dihrtyfgeelhiicilkgsrgffnllidylatiqkysgressvppffehyvrlksyqnd
nstgqltvlsddlsifrdkhvlivedivdtgftltefgerlkavgpksmriatlvekrtd
rsnslkgdfvgfsiedvwivgccydfnemfrdfdhvavlsdaarkkfekv
>d1dbrc_ 3.51.1.1.3 Hypoxantine-guanine-xanthine PRTase (HGPRTase) {Toxoplasma gondii}
iedygkgkgriepmyipdntfynaddflvpphckpyidkillpgglvkdrveklaydihr
tyfgeelhiicilkgsrgffnllidylatiqkysgressvppffehyvrlksyqndnstg
qltvlsddlsifrdkhvlivedivdtgftltefgerlkavgpksmriatlvekrtdrsns
lkgdfvgfsiedvwivgccydfnemfrdfdhvavlsdaarkkfekv
>d1dbrd_ 3.51.1.1.3 Hypoxantine-guanine-xanthine PRTase (HGPRTase) {Toxoplasma gondii}
iedygkgkgriepmyipdntfynaddflvpphckpyidkillpgglvkdrveklaydihr
tyfgeelhiicilkgsrgffnllidylatiqkysgressvppffehyvrlksyqndnstg
qltvlsddlsifrdkhvlivedivdtgftltefgerlkavgpksmriatlvekrtdrsns
lkgdfvgfsiedvwivgccydfnemfrdfdhvavlsdaarkkfekv
>d1dbs__ 3.30.1.8.1 Dethiobiotin synthetase {Escherichia coli}
skryfvtgtdtevgktvascallqaakaagyrtagykpvasgsektpeglrnsdalalqr
nsslqldyatvnpytfaeptsphiisaqegrpieslvmsaglraleqqadwvlvegaggw
ftplsdtftfadwvtqeqlpvilvvgvklgcinhamltaqviqhagltlagwvandvtpp
gkrhaeymttltrmipapllgeipwlaenpenaatgkyinlall
>d1dbvo1 3.2.1.3.2 (0-148,313-333) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Bacillus stearothermophilus, nca 1503}
avkvgingfgrigrnvfraalknpdievvavngltdantlahllkydsvhgrldaevsvn
gnnlvvngkeiivkaerdpenlawgeigvdivvestgrftkredaakhleagakkviisa
pakneditivmgvnqdkydpkahhvisnasXnetgyshrvvdlaayiaskgl
>d1dbvo2 4.61.1.1.2 (149-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Bacillus stearothermophilus, nca 1503}
cttnclapfakvlheqfgivrgmmttvhsytndqrildashkdlrraraaaesiiptttg
aakavalvlpelkgklngmamrvptpnvsvvdlvaelekevtveevnaalkaaaegelkg
ilayseeplvsrdyngstvsstidalstmvidgkmvkvvswyd
>d1dbvp1 3.2.1.3.2 (0-148,313-333) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Bacillus stearothermophilus, nca 1503}
avkvgingfgrigrnvfraalknpdievvavngltdantlahllkydsvhgrldaevsvn
gnnlvvngkeiivkaerdpenlawgeigvdivvestgrftkredaakhleagakkviisa
pakneditivmgvnqdkydpkahhvisnasXnetgyshrvvdlaayiaskgl
>d1dbvp2 4.61.1.1.2 (149-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Bacillus stearothermophilus, nca 1503}
cttnclapfakvlheqfgivrgmmttvhsytndqrildashkdlrraraaaesiiptttg
aakavalvlpelkgklngmamrvptpnvsvvdlvaelekevtveevnaalkaaaegelkg
ilayseeplvsrdyngstvsstidalstmvidgkmvkvvswyd
>d1dbvq1 3.2.1.3.2 (0-148,313-333) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Bacillus stearothermophilus, nca 1503}
avkvgingfgrigrnvfraalknpdievvavngltdantlahllkydsvhgrldaevsvn
gnnlvvngkeiivkaerdpenlawgeigvdivvestgrftkredaakhleagakkviisa
pakneditivmgvnqdkydpkahhvisnasXnetgyshrvvdlaayiaskgl
>d1dbvq2 4.61.1.1.2 (149-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Bacillus stearothermophilus, nca 1503}
cttnclapfakvlheqfgivrgmmttvhsytndqrildashkdlrraraaaesiiptttg
aakavalvlpelkgklngmamrvptpnvsvvdlvaelekevtveevnaalkaaaegelkg
ilayseeplvsrdyngstvsstidalstmvidgkmvkvvswyd
>d1dbvr1 3.2.1.3.2 (0-148,313-333) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Bacillus stearothermophilus, nca 1503}
avkvgingfgrigrnvfraalknpdievvavngltdantlahllkydsvhgrldaevsvn
gnnlvvngkeiivkaerdpenlawgeigvdivvestgrftkredaakhleagakkviisa
pakneditivmgvnqdkydpkahhvisnasXnetgyshrvvdlaayiaskgl
>d1dbvr2 4.61.1.1.2 (149-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Bacillus stearothermophilus, nca 1503}
cttnclapfakvlheqfgivrgmmttvhsytndqrildashkdlrraraaaesiiptttg
aakavalvlpelkgklngmamrvptpnvsvvdlvaelekevtveevnaalkaaaegelkg
ilayseeplvsrdyngstvsstidalstmvidgkmvkvvswyd
>d1dca__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslctppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1dcb__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslctppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1dcc__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpfgaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1dcda_ 7.35.4.2.1 Desulforedoxin {Desulfovibrio gigas}
anegdvykcelcgqvvkvleegggtlvccgedmvkq
>d1dcdb_ 7.35.4.2.1 Desulforedoxin {Desulfovibrio gigas}
anegdvykcelcgqvvkvleegggtlvccgedmvkq
>d1dcha_ 4.56.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dchb_ 4.56.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dchc_ 4.56.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dchd_ 4.56.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dche_ 4.56.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dchf_ 4.56.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dchg_ 4.56.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dchh_ 4.56.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcia_ 3.11.1.2.3 Dienoyl-CoA isomerase {Rat (Rattus norvegicus)}
ayesiqvtsaqkhvlhvqlnrpekrnamnrafwrelvecfqkiskdsdcravvvsgagkm
ftsgidlmdmasdilqppgddvariawylrdlisryqktftviekcpkpviaaihggcig
ggvdlisacdiryctqdaffqvkevdvglaadvgtlqrlpkvignrslvneltftarkmm
adealdsglvsrvfpdkdvmlnaafalaadisskspvavqgskinliysrdhsvdesldy
matwnmsmlqtqdiiksvqaamekkdsksitfskl
>d1dcib_ 3.11.1.2.3 Dienoyl-CoA isomerase {Rat (Rattus norvegicus)}
ayesiqvtsaqkhvlhvqlnrpekrnamnrafwrelvecfqkiskdsdcravvvsgagkm
ftsgidlmdmasdilqppgddvariawylrdlisryqktftviekcpkpviaaihggcig
ggvdlisacdiryctqdaffqvkevdvglaadvgtlqrlpkvignrslvneltftarkmm
adealdsglvsrvfpdkdvmlnaafalaadisskspvavqgskinliysrdhsvdesldy
matwnmsmlqtqdiiksvqaamekkdsksitfskl
>d1dcic_ 3.11.1.2.3 Dienoyl-CoA isomerase {Rat (Rattus norvegicus)}
ayesiqvtsaqkhvlhvqlnrpekrnamnrafwrelvecfqkiskdsdcravvvsgagkm
ftsgidlmdmasdilqppgddvariawylrdlisryqktftviekcpkpviaaihggcig
ggvdlisacdiryctqdaffqvkevdvglaadvgtlqrlpkvignrslvneltftarkmm
adealdsglvsrvfpdkdvmlnaafalaadisskspvavqgskinliysrdhsvdesldy
matwnmsmlqtqdiiksvqaamekkdsksitfskl
>d1dcla1 2.1.1.1.151 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psaltqppsasgslgqsvtisctgtssnvggynyvswyqqhagkapkviiyevnkrpsgv
pdrfsgsksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1dcla2 2.1.1.2.136 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1dclb1 2.1.1.1.151 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psaltqppsasgslgqsvtisctgtssnvggynyvswyqqhagkapkviiyevnkrpsgv
pdrfsgsksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1dclb2 2.1.1.2.136 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1dcna_ 1.117.1.1.5 Argininosuccinate lyase/delta-crystallin {Domestic duck (Anas platyrhynchos), delta-crystallin}
dqrlsevdiqgsmayakalekagiltktelakilsglekiseewskgvfvvkgsdediht
anerrlkeligdiagklntgrsrndqvvtdlklfmknslsiisthllqliktlveraaie
idvilpgytnlqkaqpirwsqfllshavaltrdserlgevkkrinvlplgsgalagnpld
idremlrselefasislnsmdaiserdfvveflsfatllmihlskmaedliiystsefgf
ltlsdafstnpdslelirsksgrvfgrlasilmvlkglpstynkdlqedkeavfdvvdtl
tavlqvatgvistlqiskenmekaltpemlatdlalylvrkgvpfrqahtasgkavhlae
tkgitinnlsledlksispqfssdvsqvfnfvnsveqytalggtakssvttqieqlrelm
kkqk
>d1dcnb_ 1.117.1.1.5 Argininosuccinate lyase/delta-crystallin {Domestic duck (Anas platyrhynchos), delta-crystallin}
dpimaklnssiaydqrlsevdiqgsmayakalekagiltktelakilsglekiseediht
anerrlkeligdiagklntgrsrndqvvtdlklfmknslsiisthllqliktlveraaie
idvilpgytnlqkaqpirwsqfllshavaltrdserlgevkkrinvlplgsgalagnpld
idremlrselefasislnsmdaiserdfvveflsfatllmihlskmaedliiystsefgf
ltlspdslelirsksgrvfgrlasilmvlkglpstynkdlqedkeavfdvvdtltavlqv
atgvistlqiskenmekaltpemlatdlalylvrkgvpfrqahtasgkavhlaetkgiti
nnlsledlksispqfssdvsqvfnfvnsveqytalggtakssvttqieqlrelmkkqk
>d1dcnc_ 1.117.1.1.5 Argininosuccinate lyase/delta-crystallin {Domestic duck (Anas platyrhynchos), delta-crystallin}
tdpimaklnssiaydqrlsevdiqgsmayakalekagiltktelakilsglekiseewsk
gvfvvkgsdedihtanerrlkeligdiagklntgrsrndqvvtdlklfmknslsiisthl
lqliktlveraaieidvilpgytnlqkaqpirwsqfllshavaltrdserlgevkkrinv
lplgsgalagnpldidremlrselefasislnsmdaiserdfvveflsfatllmihlskm
aedliiystsefgfltlsdapdslelirsksgrvfgrlasilmvlkglpstynkdlqedk
eavfdvvdtltavlqvatgvistlqiskenmekaltpemlatdlalylvrkgvpfrqaht
asgkavhlaetkgitinnlsledlksispqfssdvsqvfnfvnsveqytalggtakssvt
tqieqlrelmkkqk
>d1dcnd_ 1.117.1.1.5 Argininosuccinate lyase/delta-crystallin {Domestic duck (Anas platyrhynchos), delta-crystallin}
pimaklnssiaydqrlsevdiqgsmayakalekagiltktelakilsglekiseewskgv
fvvkgsdedihtanerrlkeligdiagklntgrsrndqvvtdlklfmknslsiisthllq
liktlveraaieidvilpgytnlqkaqpirwsqfllshavaltrdserlgevkkrinvlp
lgsgalagnpldidremlrselefasislnsmdaiserdfvveflsfatllmihlskmae
dliiystsefgfltlsdafstnpdslelirsksgrvfgrlasilmvlkglpstynkdlqe
dkeavfdvvdtltavlqvatgvistlqiskenmekaltpemlatdlalylvrkgvpfrqa
htasgkavhlaetkgitinnlsledlksispqfssdvsqvfnfvnsveqytalggtakss
vttqieqlrelmkkqk
>d1dcoa_ 4.56.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcob_ 4.56.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcoc_ 4.56.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcod_ 4.56.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcoe_ 4.56.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcof_ 4.56.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcog_ 4.56.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcoh_ 4.56.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcpa_ 4.56.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcpb_ 4.56.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcpc_ 4.56.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcpd_ 4.56.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcpe_ 4.56.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcpf_ 4.56.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcpg_ 4.56.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcph_ 4.56.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcs__ 2.73.3.1.2 Deacetoxycephalosporin C synthase {Streptomyces clavuligerus}
mdttvptfslaelqqglhqdefrrclrdkglfyltdcgltdtelksakdlvidffehgse
aekravtspvptmrrgftglesestaqitntgsysdysmcysmgtadnlfpsgdferiwt
qyfdrqytasravarevlratgtepdggveafldcepllrfryfpqvpehrsaeeqplrm
aphydlsmvtliqqtpcangfvslqaevggaftdlpyrpdavlvfcgaiatlvtggqvka
prhhvaaprrdqiagssrtssvfflrpnadftfsvplarecgfdvsldgetatfqdwigg
nyvnirrtska
>d1dcta_ 3.56.1.5.3 DNA methylase HaeIII, coenzyme-binding domain {Haemophilus aegyptius}
mnlislfsgaggldlgfqkagfriicaneydksiwktyesnhsaklikgdiskissdefp
kcdgiiggppcqswseggslrgiddprgklfyeyirilkqkkpifflaenvkgmmaqrhn
kavqefiqefdnagydvhiillnandygvaqdrkrvfyigfrkelninylppiphlikpt
fkdviwdlkdnpipaldknktngnkciypnheyfigsystifmsrnrvrqwnepaftvqa
sgrqcqlhpqapvmlkvsknlnkfvegkehlyrrltvrecarvqgfpddfifhyeslndg
ykmignavpvnlayeiaktiksal
>d1dctb_ 3.56.1.5.3 DNA methylase HaeIII, coenzyme-binding domain {Haemophilus aegyptius}
mnlislfsgaggldlgfqkagfriicaneydksiwktyesnhsaklikgdiskissdefp
kcdgiiggppcqswseggslrgiddprgklfyeyirilkqkkpifflaenvkgmmaqrhn
kavqefiqefdnagydvhiillnandygvaqdrkrvfyigfrkelninylppiphlikpt
fkdviwdlkdnpipaldknktngnkciypnheyfigsystifmsrnrvrqwnepaftvqa
sgrqcqlhpqapvmlkvsknlnkfvegkehlyrrltvrecarvqgfpddfifhyeslndg
ykmignavpvnlayeiaktiksal
>d1ddba_ 6.1.4.1.3 Proapoptotic molecule BID {Mouse (Mus musculus)}
mdsevsngsglgakhitdllvfgflqssgctrqelevlgrelpvqayweadledelqtdg
sqasrsfnqgriepdsesqeeiihniarhlaqigdemdhniqptlvrqlaaqfmngslse
edkrnclakaldevktafprdmendkamlimtmllakkvashapsllrdvfhttvnfinq
nlfsyvrnlvrnemd
>d1ddca_ 1.126.1.4.3 Dimeric di-heme split-soret cytochrome c {Desulfovibrio desulfuricans, ATCC 27774}
rfdqvggafgwkphkldpkecaqvaydgywykgfgcgfgafysivglmgekygapynqfp
famleankggisdwgtiygalygaaatfslfwgrkevhpmvnelfrwyevtklpifnpgd
aaqgvkgdlpmsasdsvlchisvskwcyenkieatskqrseragrltadaafkaaeiint
kidqgkdfkstfpmqasvsscgechmtkgndanwakgimdctpchsgtaatqnkfvnh
>d1ddcb_ 1.126.1.4.3 Dimeric di-heme split-soret cytochrome c {Desulfovibrio desulfuricans, ATCC 27774}
rfdqvggafgwkphkldpkecaqvaydgywykgfgcgfgafysivglmgekygapynqfp
famleankggisdwgtiygalygaaatfslfwgrkevhpmvnelfrwyevtklpifnpgd
aaqgvkgdlpmsasdsvlchisvskwcyenkieatskqrseragrltadaafkaaeiint
kidqgkdfkstfpmqasvsscgechmtkgndanwakgimdctpchsgtaatqnkfvnh
>d1ddcc_ 1.126.1.4.3 Dimeric di-heme split-soret cytochrome c {Desulfovibrio desulfuricans, ATCC 27774}
rfdqvggafgwkphkldpkecaqvaydgywykgfgcgfgafysivglmgekygapynqfp
famleankggisdwgtiygalygaaatfslfwgrkevhpmvnelfrwyevtklpifnpgd
aaqgvkgdlpmsasdsvlchisvskwcyenkieatskqrseragrltadaafkaaeiint
kidqgkdfkstfpmqasvsscgechmtkgndanwakgimdctpchsgtaatqnkfvnh
>d1ddcd_ 1.126.1.4.3 Dimeric di-heme split-soret cytochrome c {Desulfovibrio desulfuricans, ATCC 27774}
rfdqvggafgwkphkldpkecaqvaydgywykgfgcgfgafysivglmgekygapynqfp
famleankggisdwgtiygalygaaatfslfwgrkevhpmvnelfrwyevtklpifnpgd
aaqgvkgdlpmsasdsvlchisvskwcyenkieatskqrseragrltadaafkaaeiint
kidqgkdfkstfpmqasvsscgechmtkgndanwakgimdctpchsgtaatqnkfvnh
>d1ddf__ 1.76.1.1.2 Fas {Human (Homo sapiens)}
metvainlsdvdlskyittiagvmtlsqvkgfvrkngvneakideikndnvqdtaeqkvq
llrnwhqlhgkkeaydtlikdlkkanlctlaekiqtiilkditsdsensnfrneiqslvl
ehhhhhh
>d1ddha1 2.1.1.2.17 (182-274) Class I MHC, beta2-microglobulin and alpha-3 domain {Mouse (Mus musculus), H-2DD}
tdppkahvthhrrpegdvtlrcwalgfypaeitltwqlngeeltqemelvetrpagdgtf
qkwasvvvplgkqqkytchveheglpepltlrw
>d1ddha2 4.17.1.1.24 (1-181) MHC class I, alpha-1 and alpha-2 domains {Mouse (Mus musculus), H-2DD}
mshslryfvtavsrpgfgeprymevgyvdntefvrfdsdaenpryeprarwieqegpeyw
eretrrangneqsfrvdlrtalryynqsaggshtlqwmagcdvesdgrllrgywqfaydg
cdyialnedlktwtaadmaaqitrrkweqagaaerdraylegecvewlrrylkngnatll
a
>d1ddhb1 2.1.1.2.17 Class I MHC, beta2-microglobulin and alpha-3 domain {Mouse (Mus musculus), H-2DD}
mqktpqiqvysrhppengkpnilncyvtqfhpphieiqmlkngkkipkvemsdmsfskdw
sfyilahteftptetdtyacrvkhasmaepktvywdrdm
>d1ddna1 1.4.3.19.1 (3-64) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
dlvdttemylrtiyeleeegvtplrariaerleqsgptvsqtvarmerdglvvvasdrsl
qm
>d1ddna2 1.75.1.1.1 (65-120) Diphtheria toxin repressor (DtxR) dimerization domain {Corynebacterium diphtheriae}
tptgrtlatavmrkhrlaerlltdiigldinkvhdeadrwehvmsdeverrlvkvl
>d1ddnb1 1.4.3.19.1 (3-64) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
dlvdttemylrtiyeleeegvtplrariaerleqsgptvsqtvarmerdglvvvasdrsl
qm
>d1ddnb2 1.75.1.1.1 (65-120) Diphtheria toxin repressor (DtxR) dimerization domain {Corynebacterium diphtheriae}
tptgrtlatavmrkhrlaerlltdiigldinkvhdeadrwehvmsdeverrlvkvl
>d1ddnc1 1.4.3.19.1 (3-64) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
dlvdttemylrtiyeleeegvtplrariaerleqsgptvsqtvarmerdglvvvasdrsl
qm
>d1ddnc2 1.75.1.1.1 (65-120) Diphtheria toxin repressor (DtxR) dimerization domain {Corynebacterium diphtheriae}
tptgrtlatavmrkhrlaerlltdiigldinkvhdeadrwehvmsdeverrlvkvl
>d1ddnd1 1.4.3.19.1 (3-64) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
dlvdttemylrtiyeleeegvtplrariaerleqsgptvsqtvarmerdglvvvasdrsl
qm
>d1ddnd2 1.75.1.1.1 (65-120) Diphtheria toxin repressor (DtxR) dimerization domain {Corynebacterium diphtheriae}
tptgrtlatavmrkhrlaerlltdiigldinkvhdeadrwehvmsdeverrlvkvl
>d1ddoa1 3.4.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1ddoa2 4.14.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1ddob1 3.4.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1ddob2 4.14.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1ddoc1 3.4.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1ddoc2 4.14.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1ddod1 3.4.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1ddod2 4.14.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1ddoe1 3.4.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1ddoe2 4.14.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1ddof1 3.4.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1ddof2 4.14.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1ddog1 3.4.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1ddog2 4.14.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1ddoh1 3.4.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1ddoh2 4.14.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1ddra_ 3.61.1.1.1 Dihydrofolate reductase, prokaryotic type {Escherichia coli}
misliaalavdrvigmenampwnlpadlawfkrntlnkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1ddrb_ 3.61.1.1.1 Dihydrofolate reductase, prokaryotic type {Escherichia coli}
misliaalavdrvigmenampwnlpadlawfkrntlnkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1ddsa_ 3.61.1.1.1 Dihydrofolate reductase, prokaryotic type {Escherichia coli}
misliaalavdrvigmenampwnlpadlawfkrntlnkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1ddsb_ 3.61.1.1.1 Dihydrofolate reductase, prokaryotic type {Escherichia coli}
misliaalavdrvigmenampwnlpadlawfkrntlnkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1ddt_1 2.2.1.1.1 (381-535) Diphtheria toxin, C-terminal domain {Corynebacterium diphtheriae}
spghktqpflhdgyavswntvedsiirtgfqgesghdikitaentplpiagvllptipgk
ldvnkskthisvngrkirmrcraidgdvtfcrpkspvyvgngvhanlhvafhrsssekih
sneissdsigvlgyqktvdhtkvnsklslffeiks
>d1ddt_2 4.136.1.1.3 (1-187) Diphtheria toxin, N-terminal domain {Corynebacterium diphtheriae}
gaddvvdssksfvmenfssyhgtkpgyvdsiqkgiqkpksgtqgnydddwkgfystdnky
daagysvdnenplsgkaggvvkvtypgltkvlalkvdnaetikkelglslteplmeqvgt
eefikrfgdgasrvvlslpfaegsssveyinnweqakalsveleinfetrgkrgqdamye
ymaqaca
>d1ddt_3 6.1.2.1.1 (200-380) Diphtheria toxin, middle domain {Corynebacterium diphtheriae}
scinldwdvirdktktkieslkehgpiknkmsespnktvseekakqyleefhqtalehpe
lselktvtgtnpvfaganyaawavnvaqvidsetadnlekttaalsilpgigsvmgiadg
avhhnteeivaqsialsslmvaqaiplvgelvdigfaaynfvesiinlfqvvhnsynrpa
y
>d1ddua_ 4.91.1.1.1 Thymidylate synthase {Escherichia coli}
mkqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihell
wflqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlk
ndpdsrriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfnias
yallvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesif
dyrfedfeiegydphpgikapvai
>d1ddub_ 4.91.1.1.1 Thymidylate synthase {Escherichia coli}
mkqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihell
wflqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlk
ndpdsrriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfnias
yallvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesif
dyrfedfeiegydphpgikapvai
>d1deaa_ 3.28.1.1.1 Glucosamine 6-phosphate deaminase {Escherichia coli}
mrliplttaeqvgkwaarhivnrinafkptadrpfvlglptggtpmttykalvemhkagq
vsfkhvvtfnmdeyvglpkehpesyysfmhrnffdhvdipaeninllngnapdidaecrq
yeekirsygkihlfmggvgndghiafnepasslasrtriktlthdtrvansrffdndvnq
vpkyaltvgvgtlldaeevmilvlgsqkalalqaavegcvnhmwtisclqlhpkaimvcd
epstmelkvktlryfneleaenikgl
>d1deab_ 3.28.1.1.1 Glucosamine 6-phosphate deaminase {Escherichia coli}
mrliplttaeqvgkwaarhivnrinafkptadrpfvlglptggtpmttykalvemhkagq
vsfkhvvtfnmdeyvglpkehpesyysfmhrnffdhvdipaeninllngnapdidaecrq
yeekirsygkihlfmggvgndghiafnepasslasrtriktlthdtrvansrffdndvnq
vpkyaltvgvgtlldaeevmilvlgsqkalalqaavegcvnhmwtisclqlhpkaimvcd
epstmelkvktlryfneleaenikgl
>d1dec__ 7.3.15.2.2 Decorsin {North american leech (Macrobdella decora)}
aprlpqcqgddqekclcnkdecppgqcrfprgdadpyce
>d1def__ 4.137.1.1.1 Peptide deformylase {Escherichia coli}
svlqvlhipderlrkvakpveevnaeiqrivddmfetmyaeegiglaatqvdihqriivi
dvsenrderlvlinpelleksgetgieegclsipeqralvpraekvkiraldrdgkpfel
eadgllaiciqhemdhlvgklfmdyls
>d1deg__ 1.42.1.5.8 Calmodulin {Bovine (Bos taurus)}
teeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngtid
fpefltmmarkmkdtdseeireafrvfdkdgngyisaaelrhvmtnlgekltdeevdemi
reanidgdgqvnyeefvqmmta
>d1deha1 2.31.1.2.2 (1-174,325-374) Alcohol dehydrogenase {Human (Homo sapiens)}
stagkvikckaavlwevkkpfsiedvevappkayevrikmvavgicrtddhvvsgnlvtp
lpvilgheaagivesvgegvttvkpgdkviplftpqcgkcrvcknpesnyclkndlgnpr
gtlqdgtrrftcrgkpihhflgtstfsqytvvdenavakidaasplekvcligcXkegip
klvadfmakkfsldalithvlpfekinegfdllhsgksirtvltf
>d1deha2 3.2.1.1.2 (175-324) Alcohol dehydrogenase {Human (Homo sapiens), different isozymes}
gfstgygsavnvakvtpgstcavfglggvglsavmgckaagaariiavdinkdkfakake
lgatecinpqdykkpiqevlkemtdggvdfsfevigrldtmmasllccheacgtsvivgv
ppasqnlsinpmllltgrtwkgavyggfks
>d1dehb1 2.31.1.2.2 (1-174,325-374) Alcohol dehydrogenase {Human (Homo sapiens)}
stagkvikckaavlwevkkpfsiedvevappkayevrikmvavgicrtddhvvsgnlvtp
lpvilgheaagivesvgegvttvkpgdkviplftpqcgkcrvcknpesnyclkndlgnpr
gtlqdgtrrftcrgkpihhflgtstfsqytvvdenavakidaasplekvcligcXkegip
klvadfmakkfsldalithvlpfekinegfdllhsgksirtvltf
>d1dehb2 3.2.1.1.2 (175-324) Alcohol dehydrogenase {Human (Homo sapiens), different isozymes}
gfstgygsavnvakvtpgstcavfglggvglsavmgckaagaariiavdinkdkfakake
lgatecinpqdykkpiqevlkemtdggvdfsfevigrldtmmasllccheacgtsvivgv
ppasqnlsinpmllltgrtwkgavyggfks
>e1dei.1a 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e1dei.1b 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
fvnqhlcgshlvealylvcgerg
>e1dei.2c 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e1dei.2d 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
fvnqhlcgshlvealylvcgerg
>d1deka_ 3.30.1.1.3 Deoxynucleoside monophosphate kinase {Bacteriophage T4}
mkliflsgvkrsgkdttadfimsnysavkyqlagpikdalayawgvfaantdypxltrke
fegidydretnlnltklevitimeqafcylngkspikgvfvfddegkesvnfvafnkitd
vinniedqwsvrrlmqalgtdlivnnfdrmywvklfaldyldkfnsgydyyivpdtrqdh
emdaaramgatvihvvrpgqksndthiteaglpirdgdlvitndgsleelfskikntlkv
l
>d1dekb_ 3.30.1.1.3 Deoxynucleoside monophosphate kinase {Bacteriophage T4}
mkliflsgvkrsgkdttadfimsnysavkyqlagpikdalayawgvfaantdypxltrke
fegidydretnlnltklevitimeqafcylngkspikgvfvfddegkesvnfvafnkitd
vinniedqwsvrrlmqalgtdlivnnfdrmywvklfaldyldkfnsgydyyivpdtrqdh
emdaaramgatvihvvrpgqksndthiteaglpirdgdlvitndgsleelfskikntlkv
l
>d1dela_ 3.30.1.1.3 Deoxynucleoside monophosphate kinase {Bacteriophage T4}
mkliflsgvkrsgkdttadfimsnysavkyqlagpikdalayawgvfaantdypcltrke
fegidydretnlnltklevitimeqafcylngkspikgvfvfddegkesvnfvafnkitd
vinniedqwsvrrlmqalgtdlivnnfdrmywvklfaldyldkfnsgydyyivpdtrqdh
emdaaramgatvihvvrpgqksndthiteaglpirdgdlvitndgsleelfskikntlkv
l
>d1delb_ 3.30.1.1.3 Deoxynucleoside monophosphate kinase {Bacteriophage T4}
mkliflsgvkrsgkdttadfimsnysavkyqlagpikdalayawgvfaantdypcltrke
fegidydretnlnltklevitimeqafcylngkspikgvfvfddegkesvnfvafnkitd
vinniedqwsvrrlmqalgtdlivnnfdrmywvklfaldyldkfnsgydyyivpdtrqdh
emdaaramgatvihvvrpgqksndthiteaglpirdgdlvitndgsleelfskikntlkv
l
>d1dem__ 7.8.1.1.10 Dendrotoxin I {African elapid snake (Dendroaspis polylepis polylepis)}
qplrklcilhrnpgrcyqkipafyynqkkkqcegftwsgcggnsnrfktieecrrtcirk
>d1den__ 7.8.1.1.10 Dendrotoxin I {African elapid snake (Dendroaspis polylepis polylepis)}
qplrklcilhrnpgrcyqkipafyynqkkkqcegftwsgcggnsnrfktieecrrtcirk
>d1dera1 1.119.1.1.1 (2-136,410-526) GroEL {Escherichia coli}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlpk
>d1dera2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1dera3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1derb1 1.119.1.1.1 (2-136,410-526) GroEL {Escherichia coli}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlpk
>d1derb2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1derb3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1derc1 1.119.1.1.1 (2-136,410-526) GroEL {Escherichia coli}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlpk
>d1derc2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1derc3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1derd1 1.119.1.1.1 (2-136,410-526) GroEL {Escherichia coli}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlpk
>d1derd2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1derd3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1dere1 1.119.1.1.1 (2-136,410-526) GroEL {Escherichia coli}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlpk
>d1dere2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1dere3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1derf1 1.119.1.1.1 (2-136,410-526) GroEL {Escherichia coli}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlpk
>d1derf2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1derf3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1derg1 1.119.1.1.1 (2-136,410-526) GroEL {Escherichia coli}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlpk
>d1derg2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1derg3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1derh1 1.119.1.1.1 (2-136,410-526) GroEL {Escherichia coli}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlpk
>d1derh2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1derh3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1deri1 1.119.1.1.1 (2-136,410-526) GroEL {Escherichia coli}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlpk
>d1deri2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1deri3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1derj1 1.119.1.1.1 (2-136,410-526) GroEL {Escherichia coli}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlpk
>d1derj2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1derj3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1derk1 1.119.1.1.1 (2-136,410-526) GroEL {Escherichia coli}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlpk
>d1derk2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1derk3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1derl1 1.119.1.1.1 (2-136,410-526) GroEL {Escherichia coli}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlpk
>d1derl2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1derl3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1derm1 1.119.1.1.1 (2-136,410-526) GroEL {Escherichia coli}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlpk
>d1derm2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1derm3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1dern1 1.119.1.1.1 (2-136,410-526) GroEL {Escherichia coli}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlpk
>d1dern2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1dern3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1det__ 4.1.1.1.3 RNase T1 {Aspergillus oryzae}
acdytcgsncysssdvstaqaagyqlhedgetvgsnsyphkynnyegfdfsvsspyyewp
ilssgdvysggspgadrvvfnennqlagvithtgasgnnfvect
>d1dfbh1 2.1.1.1.19 (1-126) Immunoglobulin (variable domains of L and H chains) {Fab 3D6 (human), kappa L chain}
evqlvesggglvqpgrslrlscaasgftfndyamhwvrqapgkglewvsgiswdsssigy
adsvkgrftisrdnaknslylqmnslraedmalyycvkgrdyydsggyftvafdiwgqgt
mvtvss
>d1dfbh2 2.1.1.2.29 (127-229) Immunoglobulin (constant domains of L and H chains) {Fab 3D6 (human), kappa L chain}
astkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkvepksc
>d1dfbl1 2.1.1.1.19 (1-106) Immunoglobulin (variable domains of L and H chains) {Fab 3D6 (human), kappa L chain}
diqmtqspstlsasvgdrvtitcrasqsisrwlawyqqkpgkvpklliykasslesgvps
rfsgsgsgteftltisslqpddfatyycqqynsysfgpgtkvdikr
>d1dfbl2 2.1.1.2.29 (107-212) Immunoglobulin (constant domains of L and H chains) {Fab 3D6 (human), kappa L chain}
tvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqds
kdstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1dfd__ 4.47.1.4.2 Ferredoxin I {Sulfate-reducing bacteria (Desulfovibrio africanus)}
arkfyvdqdeciacescveiapgafamdpeiekayvkdvegasqeeveeamdtcpvqcih
wede
>d1dff__ 4.137.1.1.1 Peptide deformylase {Escherichia coli}
svlqvlhipderlrkvakpveevnaeiqrivddmfetmyaeegiglaatqvdihqriivi
dvsenrderlvlinpelleksgetgieegclsipeqralvpraekvkiraldrdgkpfel
eadgllaiciqhemdhlvgklfmdylsplkqqrirqkvekldrl
>d1dfga_ 3.2.1.2.15 Enoyl-ACP reductase {Escherichia coli}
gflsgkrilvtgvasklsiaygiaqamhregaelaftyqndklkgrveefaaqlgsdivl
qcdvaedasidtmfaelgkvwpkfdgfvhsigfapgdqldgdyvnavtregfkiahdiss
ysfvamakacrsmlnpgsalltlsylgaeraipnynvmglakasleanvrymanamgpeg
vrvnaisagpirtlaasgikdfrkmlahceavtpirrtvtiedvgnsaaflcsdlsagis
gevvhvdggfsiaamne
>d1dfgb_ 3.2.1.2.15 Enoyl-ACP reductase {Escherichia coli}
gflsgkrilvtgvasklsiaygiaqamhregaelaftyqndklkgrveefaaqlgsdivl
qcdvaedasidtmfaelgkvwpkfdgfvhsigfapgdqldgdyvnavtregfkiahdiss
ysfvamakacrsmlnpgsalltlsylgaeraipnynvmglakasleanvrymanamgpeg
vrvnaisagpirtlaasgikdfrkmlahceavtpirrtvtiedvgnsaaflcsdlsagis
gevvhvdggfsiaamne
>d1dfha_ 3.2.1.2.15 Enoyl-ACP reductase {Escherichia coli}
gflsgkrilvtgvasklsiaygiaqamhregaelaftyqndklkgrveefaaqlgsdivl
qcdvaedasidtmfaelgkvwpkfdgfvhsigfapgdqldgdyvnavtregfkiahdiss
ysfvamakacrsmlnpgsalltlsylgaeraipnynvmglakasleanvrymanamgpeg
vrvnaisagpirtlaasgikdfrkmlahceavtpirrtvtiedvgnsaaflcsdlsagis
gevvhvdggfsiaamne
>d1dfhb_ 3.2.1.2.15 Enoyl-ACP reductase {Escherichia coli}
gflsgkrilvtgvasklsiaygiaqamhregaelaftyqndklkgrveefaaqlgsdivl
qcdvaedasidtmfaelgkvwpkfdgfvhsigfapgdqldgdyvnavtregfkiahdiss
ysfvamakacrsmlnpgsalltlsylgaeraipnynvmglakasleanvrymanamgpeg
vrvnaisagpirtlaasgikdfrkmlahceavtpirrtvtiedvgnsaaflcsdlsagis
gevvhvdggfsiaamne
>d1dfia_ 3.2.1.2.15 Enoyl-ACP reductase {Escherichia coli}
gflsgkrilvtgvasklsiaygiaqamhregaelaftyqndklkgrveefaaqlgsdivl
qcdvaedasidtmfaelgkvwpkfdgfvhsigfapgdqldgdyvnavtregfkiahdiss
ysfvamakacrsmlnpgsalltlsylgaeraipnynvmglakasleanvrymanamgpeg
vrvnaisagpirtlaasgikdfrkmlahceavtpirrtvtiedvgnsaaflcsdlsagis
gevvhvdggfsiaamne
>d1dfib_ 3.2.1.2.15 Enoyl-ACP reductase {Escherichia coli}
gflsgkrilvtgvasklsiaygiaqamhregaelaftyqndklkgrveefaaqlgsdivl
qcdvaedasidtmfaelgkvwpkfdgfvhsigfapgdqldgdyvnavtregfkiahdiss
ysfvamakacrsmlnpgsalltlsylgaeraipnynvmglakasleanvrymanamgpeg
vrvnaisagpirtlaasgikdfrkmlahceavtpirrtvtiedvgnsaaflcsdlsagis
gevvhvdggfsiaamne
>d1dfic_ 3.2.1.2.15 Enoyl-ACP reductase {Escherichia coli}
gflsgkrilvtgvasklsiaygiaqamhregaelaftyqndklkgrveefaaqlgsdivl
qcdvaedasidtmfaelgkvwpkfdgfvhsigfapgdqldgdyvnavtregfkiahdiss
ysfvamakacrsmlnpgsalltlsylgaeraipnynvmglakasleanvrymanamgpeg
vrvnaisagpirtlaasgikdfrkmlahceavtpirrtvtiedvgnsaaflcsdlsagis
gevvhvdggfsiaamne
>d1dfid_ 3.2.1.2.15 Enoyl-ACP reductase {Escherichia coli}
gflsgkrilvtgvasklsiaygiaqamhregaelaftyqndklkgrveefaaqlgsdivl
qcdvaedasidtmfaelgkvwpkfdgfvhsigfapgdqldgdyvnavtregfkiahdiss
ysfvamakacrsmlnpgsalltlsylgaeraipnynvmglakasleanvrymanamgpeg
vrvnaisagpirtlaasgikdfrkmlahceavtpirrtvtiedvgnsaaflcsdlsagis
gevvhvdggfsiaamne
>d1dfje_ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1dfji_ 3.9.1.1.1 Ribonuclease inhibitor {Pig (Sus scrofa)}
mnldihceqlsdarwtellpllqqyevvrlddcglteehckdigsalranpsltelclrt
nelgdagvhlvlqglqsptckiqklslqncslteagcgvlpstlrslptlrelhlsdnpl
gdaglrllceglldpqchleklqleycrltaasceplasvlratralkeltvsnndigea
garvlgqgladsacqletlrlencgltpanckdlcgivasqaslreldlgsnglgdagia
elcpgllspasrlktlwlwecditasgcrdlcrvlqaketlkelslagnklgdegarllc
esllqpgcqleslwvkscsltaaccqhvslmltqnkhllelqlssnklgdsgiqelcqal
sqpgttlrvlclgdcevtnsgcsslaslllanrslreldlsnncvgdpgvlqllgsleqp
gcaleqlvlydtywteevedrlqalegskpglrvis
>d1dfna_ 7.9.1.1.1 Defensin HNP-3 {Human (Homo sapiens)}
dcycripaciagerrygtciyqgrlwafcc
>d1dfnb_ 7.9.1.1.1 Defensin HNP-3 {Human (Homo sapiens)}
dcycripaciagerrygtciyqgrlwafcc
>d1dfpa_ 2.41.1.2.27 Factor D {Human (Homo sapiens)}
ilggreaeaharpymasvqlngahlcggvlvaeqwvlsaahcledaadgkvqvllgahsl
sqpepskrlydvlravphpdsqpdtidhdllllqlsekatlgpavrplpwqrvdrdvapg
tlcdvagwgivnhagrrpdslqhvllpvldratcnrrthhdgaiterlmcaesnrrdsck
gdsggplvcggvlegvvtsgsrvcgnrkkpgiytrvasyaawidsvla
>d1dfpb_ 2.41.1.2.27 Factor D {Human (Homo sapiens)}
ilggreaeaharpymasvqlngahlcggvlvaeqwvlsaahcledaadgkvqvllgahsl
sqpepskrlydvlravphpdsqpdtidhdllllqlsekatlgpavrplpwqrvdrdvapg
tlcdvagwgivnhagrrpdslqhvllpvldratcnrrthhdgaiterlmcaesnrrdsck
gdsggplvcggvlegvvtsgsrvcgnrkkpgiytrvasyaawidsvla
>d1dfx_1 2.1.12.1.1 (37-125) Desulfoferrodoxin C-terminal domain {Desulfovibrio desulfuricans}
vegstdgamekhvpviekvdggylikvgsvphpmeekhwiewielladgrsytkflkpgd
apeaffaidaskvtareycnlhghwkaen
>d1dfx_2 7.35.4.2.2 (1-36) Desulfoferrodoxin N-terminal domain {Desulfovibrio desulfuricans}
pkhlevykcthcgnivevlhgggaelvccgepmkhm
>d1dgd__ 3.57.1.4.1 Dialkylglycine decarboxylase {Pseudomonas cepacia}
lnddatfwrnarhhlvryggtfepmiierakgsfvydadgraildftsgqmsavlghchp
eivsvigeyagkldhlfsgmlsrpvvdlatrlanitppgldralllstgaesneaairma
klvtgkyeivgfaqswhgmtgaaasatysagrkgvgpaavgsfaipapftyrprfernga
ydylaeldyafdlidrqssgnlaafiaepilssggiielpdgymaalkrkceargmllil
deaqtgvgrtgtmfacqrdgvtpdiltlsktlgaglplaaivtsaaieerahelgylfyt
thvsdplpaavglrvldvvqrdglvaranvmgdrlrrglldlmerfdcigdvrgrglllg
veivkdrrtkepadglgakitrecmnlglsmnivqlpgmggvfriappltvsedeidlgl
sllgqaieral
>d1dge__ 3.57.1.4.1 Dialkylglycine decarboxylase {Pseudomonas cepacia}
lnddatfwrnarhhlvryggtfepmiierakgsfvydadgraildftsgqmsavlghchp
eivsvigeyagkldhlfsgmlsrpvvdlatrlanitppgldralllstgaesneaairma
klvtgkyeivgfaqswhgmtgaaasatysagrkgvgpaavgsfaipapftyrprfernga
ydylaeldyafdlidrqssgnlaafiaepilssggiielpdgymaalkrkceargmllil
deaqtgvgrtgtmfacqrdgvtpdiltlsktlgaglplaaivtsaaieerahelgylfyt
thvsdplpaavglrvldvvqrdglvaranvmgdrlrrglldlmerfdcigdvrgrglllg
veivkdrrtkepadglgakitrecmnlglsmnivqlpgmggvfriappltvsedeidlgl
sllgqaieral
>d1dgla_ 2.26.1.1.14 Lectin {Mucana (Dioclea grandiflora)}
adtivavelnsypntdigdpnyphigidiksirskstarwnmqtgkvgtvhisynsvakr
lsavvsysgsssttvsydvdlnnvlpewvrvglsattglyketntilswsftsklktnsi
adanslhfsfhqfsqnpkdlilqgdaftdsdgnleltkvsssgdpqgnsvgralfyapvh
iweksavvasfdatftflikspdrepadgitffiantdtsipsgsggrllglfpdan
>d1dglb_ 2.26.1.1.14 Lectin {Mucana (Dioclea grandiflora)}
adtivavelnsypntdigdpnyphigidiksirskstarwnmqtgkvgtvhisynsvakr
lsavvsysgsssttvsydvdlnnvlpewvrvglsattglyketntilswsftsklktnsi
adanslhfsfhqfsqnpkdlilqgdaftdsdgnleltkvsssgdpqgnsvgralfyapvh
iweksavvasfdatftflikspdrepadgitffiantdtsipsgsggrllglfpdan
>d1dhfa_ 3.61.1.1.5 Dihydrofolate reductases, eukaryotic type {Human (Homo sapiens)}
lncivavsqnmgigkngdlpwpplrnefryfqrmtttssvegkqnlvimgkktwfsipek
nrplkgrinlvlsrelkeppqgahflsrslddalklteqpelankvdmvwivggssvyke
amnhpghlklfvtrimqdfesdtffpeidlekykllpeypgvlsdvqeekgikykfevye
kn
>d1dhfb_ 3.61.1.1.5 Dihydrofolate reductases, eukaryotic type {Human (Homo sapiens)}
lncivavsqnmgigkngdlpwpplrnefryfqrmtttssvegkqnlvimgkktwfsipek
nrplkgrinlvlsrelkeppqgahflsrslddalklteqpelankvdmvwivggssvyke
amnhpghlklfvtrimqdfesdtffpeidlekykllpeypgvlsdvqeekgikykfevye
kn
>d1dhga_ 7.35.4.2.1 Desulforedoxin {Desulfovibrio gigas}
anegdvykcelcgqvvkvleegggtlvccgedmvkq
>d1dhgb_ 7.35.4.2.1 Desulforedoxin {Desulfovibrio gigas}
anegdvykcelcgqvvkvleegggtlvccgedmvkq
>d1dhia_ 3.61.1.1.1 Dihydrofolate reductase, prokaryotic type {Escherichia coli}
misliaalavdrvigmenampwnlpaslawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1dhib_ 3.61.1.1.1 Dihydrofolate reductase, prokaryotic type {Escherichia coli}
misliaalavdrvigmenampwnlpaslawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1dhja_ 3.61.1.1.1 Dihydrofolate reductase, prokaryotic type {Escherichia coli}
misliaalavdrvigmenampwnlpaslawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvssefhdadaqnshsycfeilerr
>d1dhjb_ 3.61.1.1.1 Dihydrofolate reductase, prokaryotic type {Escherichia coli}
misliaalavdrvigmenampwnlpaslawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvssefhdadaqnshsycfeilerr
>d1dhka1 2.62.1.1.8 (404-496) Animal alpha-amylase {Porcine (Sus scrofa)}
qpfanwwdngsnqvafgrgnrgfivfnnddwqlsstlqtglpggtycdvisgdkvgnsct
gikvyvssdgtaqfsisnsaedpfiaihaeskl
>d1dhka2 3.1.7.1.8 (2-403) Animal alpha-amylase {Porcine (Sus scrofa)}
yapqtqsgrtsivhlfewrwvdialecerylgpkgfggvqvsppnenvvvtnpsrpwwer
yqpvsyklctrsgnenefrdmvtrcnnvgvriyvdavinhmcgsgaaagtgttcgsycnp
gsrefpavpysawdfndgkcktasggiesyndpyqvrdcqlvglldlalekdyvrsmiad
ylnklidigvagfridaskhmwpgdikavldklhnlntnwfpagsrpfifqevidlggea
iqsseyfgngrvtefkygaklgtvvrkwsgekmsylknwgegwgfmpsdralvfvdnhdn
qrghgaggasiltfwdarlykvavgfmlahpygftrvmssyrwarnfvngedvndwigpp
nnngvikevtinadttcgndwvcehrwreirnmvwfrnvvdg
>d1dhkb_ 2.26.1.1.15 Phytohemagglutinin-L, PHA-L, also arcelin {Kidney bean (Phaseolus vulgaris)}
atetsfiidafnktnlilqgdatvssngnlqlsynsydsmsrafysapiqirdsttgnva
sfdtnftmnirthrqansavgldfvlvpvqpeskgdtvtvefdtflsrisidvnnndiks
vpwdvhdydgqnaevritynsstkvfsvslsnpstgksnnvsttvelekevydwvsvgfs
atsgayqwsyethdvlswsfsskf
>d1dhma_ 4.47.8.1.2 Papillomavirus-1 E2 protein {Human papillomavirus-31}
mattpiihlkgdanilkclryrlskykqlyeqvsstwhwtctdgkhknaivtltyistsq
rddflntvkipntvsvstgymti
>d1dhmb_ 4.47.8.1.2 Papillomavirus-1 E2 protein {Human papillomavirus-31}
mattpiihlkgdanilkclryrlskykqlyeqvsstwhwtctdgkhknaivtltyistsq
rddflntvkipntvsvstgymti
>d1dhn__ 4.75.1.3.1 7,8-dihidroneopterin aldolase {Staphylococcus aureus}
mqdtiflkgmrfygyhgalsaeneigqifkvdvtlkvdlseagrtdnvidtvhygevfee
vksimegkavnllehlaerianrinsqynrvmetkvritkenppipghydgvgieivren
k
>d1dhpa_ 3.1.9.1.2 Dihydrodipicolinate synthase {Escherichia coli}
mftgsivaivtpmdekgnvcraslkklidyhvasgtsaivsvgttgesatlnhdehadvv
mmtldladgripviagtganataeaisltqrfndsgivgcltvtpyynrpsqeglyqhfk
aiaehtdlpqilynvpsrtgcdllpetvgrlakvkniigikeatgnltrvnqikelvsdd
fvllsgddasaldfmqlgghgvisvtanvaardmaqmcklaaeghfaearvinqrlmplh
nklfvepnpipvkwackelglvatdtlrlpmtpitdsgretvraalkhagll
>d1dhpb_ 3.1.9.1.2 Dihydrodipicolinate synthase {Escherichia coli}
mftgsivaivtpmdekgnvcraslkklidyhvasgtsaivsvgttgesatlnhdehadvv
mmtldladgripviagtganataeaisltqrfndsgivgcltvtpyynrpsqeglyqhfk
aiaehtdlpqilynvpsrtgcdllpetvgrlakvkniigikeatgnltrvnqikelvsdd
fvllsgddasaldfmqlgghgvisvtanvaardmaqmcklaaeghfaearvinqrlmplh
nklfvepnpipvkwackelglvatdtlrlpmtpitdsgretvraalkhagll
>d1dhr__ 3.2.1.2.6 Dihydropteridin reductase {Rat (Rattus norvegicus)}
earrvlvyggrgalgsrcvqafrarnwwvasidvveneeasasvivkmtdsfteqadqvt
aevgkllgdqkvdailcvaggwaggnakskslfkncdlmwkqsiwtstisshlatkhlke
gglltlagakaaldgtpgmigygmakgavhqlcqslagknsgmpsgaaaiavlpvtldtp
mnrksmpeadfsswtpleflvetfhdwitgnkrpnsgsliqvvttdgkteltpayf
>d1dhs__ 3.25.1.1.1 Deoxyhypusine synthase, DHS {Human (Homo sapiens)}
apagalaavlkhsstlppestqvrgydfnrgvnyralleafgttgfqatnfgravqqvna
miekklepltsctiflgytsnlissgiretirylvqhnmvdvlvttaggveedlikclap
tylgefslrgkelrenginrignllvpnenyckfedwlmpildqmvmeqntegvkwtpsk
miarlgkeinnpesvyywaqknhipvfspaltdgslgdmiffhsyknpglvldivedlrl
intqaifakctgmiilgggvvkhhiananlmrngadyavyintaqefdgsdsgarpdeav
swgkirvdaqpvkvyadaslvfpllvaetfaqkmdafmhekned
>d1dht__ 3.2.1.2.8 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylahskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevf
>d1dhx__ 2.12.2.2.1 Adenovirus type 2 hexon {Host: human (Homo sapiens)}
frnptvapthdvttdrsqrltlrfipvdredtaysykarftlavgdnrvldmastyfdir
gvldrgptfkpysgtaynalapkgapnsceweqtedsgravaedeeeededeeeeeeeqn
ardqatkkthvyaqaplsgetitksglqigsdnaetqakpvyadpsyqpepqigesqwne
adanaaggrvlkkttpmkpcygsyarptnpfggqsvlvpdekgvplpkvdlqffsnttsl
ndrqgnatkpkvvlysedvnmetpdthlsykpgkgdenskamlgqqsmpnrpnyiafrdn
figlmyynstgnmgvlagqasqlnavvdlqdrntelsyqllldsigdrtryfsmwnqavd
sydpdvriienhgtedelpnycfplggigvtdtyqaikangngsgdngdttwtkdetfat
rneigvgnnfameinlnanlwrnflysnialylpdklkynptnveisdnpntydymnkrv
vapglvdcyinlgarwsldymdnvnpfnhhrnaglryrsmllgngryvpfhiqvpqkffa
iknllllpgsytyewnfrkdvnmvlqsslgndlrvdgasikfdsiclyatffpmahntas
tleamlrndtndqsfndylsaanmlypipanatnvpisipsrnwaafrgwaftrlktket
pslgsgydpyytysgsipyldgtfylnhtfkkvaitfdssvswpgndrlltpnefeikrs
vdgegynvaqcnmtkdwflvqmlanynigyqgfyipesykdrmysffrnfqpmsrqvvdd
tkykeyqqvgilhqhnnsgfvgylaptmregqaypanvpypligktavdsitqkkflcdr
tlwripfssnfmsmgaltdlgqnllyansahaldmtfevdpmdeptllyvlfevfdvvrv
hqphrgvietvylrtpfsagnatt
>d1dhy_1 4.27.1.3.1 (1-132) 2,3-Dihydroxybiphenyl dioxygenase (DHDB, BPHC enzyme) {Pseudomonas}
sierlgylgfavkdvpawdhfltksvglmaagsagdaalyradqrawriavqpgelddla
yaglevddaaalermadklrqagvaftrgdealmqqrkvmgllclqdpfglpleiyygpa
eifhepflpsap
>d1dhy_2 4.27.1.3.1 (133-288) 2,3-Dihydroxybiphenyl dioxygenase (DHDB, BPHC enzyme) {Pseudomonas}
vsgfvtgdqgighfvrcvpdtakamafytevlgfvlsdiidiqmgpetsvpahflhcngr
hhtialaafpipkrihhfmlqantiddvgyafdrldaagritsllgrhtndqtlsfyadt
pspmievefgwgprtvdsswtvarhsrtamwghksv
>d1dica_ 2.41.1.2.27 Factor D {Human (Homo sapiens)}
ilggreaeaharpymasvqlngahlcggvlvaeqwvlsaahcledaadgkvqvllgahsl
sqpepskrlydvlravphpdsqpdtidhdllllqlsekatlgpavrplpwqrvdrdvapg
tlcdvagwgivnhagrrpdslqhvllpvldratcnrrthhdgaiterlmcaesnrrdsck
gdsggplvcggvlegvvtsgsrvcgnrkkpgiytrvasyaawidsvla
>d1dida_ 3.1.13.2.5 D-xylose isomerase {Arthrobacter strain b3728}
vqptpadhftfglwtvgwtgadpfgvatrknldpveavhklaelgaygitfhdndlipfd
ateaerekilgdfnqalkdtglkvpmvttnlfshpvfkdggftsndrsirrfalakvlhn
idlaaemgaetfvmwggregseydgskdlaaaldrmregvdtaagyikdkgynlrialep
kpneprgdiflptvghglafieqlehgdivglnpetgheqmaglnfthgiaqalwaeklf
hidlngqrgikydqdlvfghgdltsafftvdllengfpnggpkytgprhfdykpsrtdgy
dgvwdsakanmsmylllkeralafradpevqeamktsgvfelgettlnagesaadlmnds
asfagfdaeaaaernfafirlnqlaiehllgsr
>d1didb_ 3.1.13.2.5 D-xylose isomerase {Arthrobacter strain b3728}
vqptpadhftfglwtvgwtgadpfgvatrknldpveavhklaelgaygitfhdndlipfd
ateaerekilgdfnqalkdtglkvpmvttnlfshpvfkdggftsndrsirrfalakvlhn
idlaaemgaetfvmwggregseydgskdlaaaldrmregvdtaagyikdkgynlrialep
kpneprgdiflptvghglafieqlehgdivglnpetgheqmaglnfthgiaqalwaeklf
hidlngqrgikydqdlvfghgdltsafftvdllengfpnggpkytgprhfdykpsrtdgy
dgvwdsakanmsmylllkeralafradpevqeamktsgvfelgettlnagesaadlmnds
asfagfdaeaaaernfafirlnqlaiehllgsr
>d1diea_ 3.1.13.2.5 D-xylose isomerase {Arthrobacter strain b3728}
vqptpadhftfglwtvgwtgadpfgvatrknldpveavhklaelgaygitfhdndlipfd
ateaerekilgdfnqalkdtglkvpmvttnlfshpvfkdggftsndrsirrfalakvlhn
idlaaemgaetfvmwggregseydgskdlaaaldrmregvdtaagyikdkgynlrialep
kpneprgdiflptvghglafieqlehgdivglnpetgheqmaglnfthgiaqalwaeklf
hidlngqrgikydqdlvfghgdltsafftvdllengfpnggpkytgprhfdykpsrtdgy
dgvwdsakanmsmylllkeralafradpevqeamktsgvfelgettlnagesaadlmnds
asfagfdaeaaaernfafirlnqlaiehllgsr
>d1dieb_ 3.1.13.2.5 D-xylose isomerase {Arthrobacter strain b3728}
vqptpadhftfglwtvgwtgadpfgvatrknldpveavhklaelgaygitfhdndlipfd
ateaerekilgdfnqalkdtglkvpmvttnlfshpvfkdggftsndrsirrfalakvlhn
idlaaemgaetfvmwggregseydgskdlaaaldrmregvdtaagyikdkgynlrialep
kpneprgdiflptvghglafieqlehgdivglnpetgheqmaglnfthgiaqalwaeklf
hidlngqrgikydqdlvfghgdltsafftvdllengfpnggpkytgprhfdykpsrtdgy
dgvwdsakanmsmylllkeralafradpevqeamktsgvfelgettlnagesaadlmnds
asfagfdaeaaaernfafirlnqlaiehllgsr
>d1difa_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1difb_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1dih_1 3.2.1.3.13 (2-130,241-273) Dihydrodipicolinate reductase {Escherichia coli}
hdanirvaiagaggrmgrqliqaalalegvqlgaaleregssllgsdagelagagktgvt
vqssldavkddfdvfidftrpegtlnhlafcrqhgkgmvigttgfdeagkqairdaaadi
aivfaanfsXmtfangavrsalwlsgkesglfdmrdvldlnnl
>d1dih_2 4.61.1.2.2 (131-240) Dihydrodipicolinate reductase {Escherichia coli}
vgvnvmlkllekaakvmgdytdieiieahhrhkvdapsgtalamgeaiahaldkdlkdca
vysreghtgervpgtigfatvragdivgehtamfadigerleithkassr
>d1dik_1 3.1.11.2.1 (510-874) Pyruvate phosphate dikinase, C-terminal domain {Escherichia coli}
ietqeasvsgsferimvwadkfrtlkvrtnadtpedtlnavklgaegiglcrtehmffea
drimkirkmilsdsveareealnelipfqkgdfkamykalegrpmtvryldpplhefvph
teeeqaelaknmgltlaevkakvdelhefnpmmghrgcrlavtypeiakmqtravmeaai
evkeetgidivpeimiplvgekkelkfvkdvvvevaeqvkkekgsdmqyhigtmieipra
altadaiaeeaeffsfgtndltqmtfgfsrddagkfldsyykakiyesdpfarldqtgvg
qlvemavkkgrqtrpglkcgicgehggdpssvefchkvglnyvscspfrvpiarlaaaqa
alnnk
>d1dik_2 3.7.1.1.1 (377-505) Pyruvate phosphate dikinase, central domain {Escherichia coli}
lhptfnpaalkagevigsalpaspgaaagkvyftadeakaahekgervilvrletspedi
egmhaaegiltvrggmtshaavvargmgtccvsgcgeikineeaktfelgghtfaegdyi
sldgstgki
>d1dik_3 4.115.1.5.1 (2-376) Pyruvate phosphate dikinase, N-terminal domain {Escherichia coli}
akwvykfeegnasmrnllggkgcnlaemtilgmpipqgftvtteacteyynsgkqitqei
qdqifeaitwleelngkkfgdtedpllvsvrsaarasmpgmmdtilnlglndvavegfak
ktgnprfaydsyrrfiqmysdvvmevpkshfekiidamkeekgvhfdtdltaddlkelae
kfkavykeamngeefpqepkdqlmgavkavfrswdnpraivyrrmndipgdwgtavnvqt
mvfgnkgetsgtgvaftrnpstgekgiygeylinaqgedvvagvrtpqpitqlendmpdc
ykqfmdlamklekhfrdmqdmeftieegklyflqtrngkrtapaalqiacdlvdegmite
eeavvrieaksldql
>d1dil__ 2.59.1.1.1 Salmonella sialidase {Salmonella typhimurium, strain lt2}
tveksvvfkaegehftdqkgntivgsgsggttkyfripamcttskgtivvfadarhntas
dqsfidtaaarstdggktwnkkiaiyndrvnsklsrvmdptcivaniqgretilvmvgkw
nnndktwgayrdkapdtdwdlvlykstddgvtfskvetnihdivtkngtisamlggvgsg
lqlndgklvfpvqmvrtknittvlntsfiystdgitwslpsgycegfgsenniiefnasl
vnnirnsglrrsfetkdfgktwtefppmdkkvdnrnhgvqgstitipsgnklvaahssaq
nknndytrsdislyahnlysgevkliddfypkvgnasgagysclsyrknvdketlyvvye
angsiefqdlsrhlpviksyn
>d1dim__ 2.59.1.1.1 Salmonella sialidase {Salmonella typhimurium, strain lt2}
tveksvvfkaegehftdqkgntivgsgsggttkyfripamcttskgtivvfadarhntas
dqsfidtaaarstdggktwnkkiaiyndrvnsklsrvmdptcivaniqgretilvmvgkw
nnndktwgayrdkapdtdwdlvlykstddgvtfskvetnihdivtkngtisamlggvgsg
lqlndgklvfpvqmvrtknittvlntsfiystdgitwslpsgycegfgsenniiefnasl
vnnirnsglrrsfetkdfgktwtefppmdkkvdnrnhgvqgstitipsgnklvaahssaq
nknndytrsdislyahnlysgevkliddfypkvgnasgagysclsyrknvdketlyvvye
angsiefqdlsrhlpviksyn
>d1din__ 3.59.1.7.1 Dienelactone hydrolase {Pseudomonas B13}
mltegisiqsydghtfgalvgspakapapviviaqeifgvnafmretvswlvdqgyaavc
pdlyarqapgtaldpqderqreqayklwqafdmeagvgdleaairyarhqpysngkvglv
gyxlggalaflvaakgyvdravgyygvglekqlnkvpevkhpalfhmggqdhfvpapsrq
litegfganpllqvhwyeeaghsfartsssgyvasaaalanertldflaplqs
>d1dira_ 3.2.1.2.6 Dihydropteridin reductase {Rat (Rattus norvegicus)}
earrvlvyggrgalgsrcvqafrarnwwvasidvveneeasasvivkmtdsfteqadqvt
aevgkllgdqkvdailcvaggwaggnakskslfkncdlmwkqsiwtstisshlatkhlke
gglltlagakaaldgtpgmigygmakgavhqlcqslagknsgmpsgaaaiavlpvtldtp
mnrksmpeadfsswtpleflvetfhdwitgnkrpnsgsliqvvttdgkteltpayf
>d1dirb_ 3.2.1.2.6 Dihydropteridin reductase {Rat (Rattus norvegicus)}
earrvlvyggrgalgsrcvqafrarnwwvasidvveneeasasvivkmtdsfteqadqvt
aevgkllgdqkvdailcvaggwaggnakskslfkncdlmwkqsiwtstisshlatkhlke
gglltlagakaaldgtpgmigygmakgavhqlcqslagknsgmpsgaaaiavlpvtldtp
mnrksmpeadfsswtpleflvetfhdwitgnkrpnsgsliqvvttdgkteltpayf
>d1dirc_ 3.2.1.2.6 Dihydropteridin reductase {Rat (Rattus norvegicus)}
earrvlvyggrgalgsrcvqafrarnwwvasidvveneeasasvivkmtdsfteqadqvt
aevgkllgdqkvdailcvaggwaggnakskslfkncdlmwkqsiwtstisshlatkhlke
gglltlagakaaldgtpgmigygmakgavhqlcqslagknsgmpsgaaaiavlpvtldtp
mnrksmpeadfsswtpleflvetfhdwitgnkrpnsgsliqvvttdgkteltpayf
>d1dird_ 3.2.1.2.6 Dihydropteridin reductase {Rat (Rattus norvegicus)}
earrvlvyggrgalgsrcvqafrarnwwvasidvveneeasasvivkmtdsfteqadqvt
aevgkllgdqkvdailcvaggwaggnakskslfkncdlmwkqsiwtstisshlatkhlke
gglltlagakaaldgtpgmigygmakgavhqlcqslagknsgmpsgaaaiavlpvtldtp
mnrksmpeadfsswtpleflvetfhdwitgnkrpnsgsliqvvttdgkteltpayf
>d1dis__ 3.61.1.1.2 Dihydrofolate reductase, prokaryotic type {Lactobacillus casei}
taflwaqdrdgligkdghlpwhlpddlhyfraqtvgkimvvgrrtyesfpkrplpertnv
vlthqedyqaqgavvvhdvaavfayakqhpdqelviaggaqiftafkddvdtllvtrlag
sfegdtkmiplnwddftkvssrtvedtnpalthtyevwqkka
>e1dit.1h 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>e1dit.1l 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
geadcglrplfekksledkterellesyi
>d1diu__ 3.61.1.1.2 Dihydrofolate reductase, prokaryotic type {Lactobacillus casei}
taflwaqdrdgligkdghlpwhlpddlhyfraqtvgkimvvgrrtyesfpkrplpertnv
vlthqedyqaqgavvvhdvaavfayakqhpdqelviaggaqiftafkddvdtllvtrlag
sfegdtkmiplnwddftkvssrtvedtnpalthtyevwqkka
>d1div_1 4.78.1.1.1 (56-149) Ribosomal protein L9 C-domain {Bacillus stearothermophilus}
rqaaeelanakklkeqlekltvtipakageggrlfgsitskqiaeslqaqhglkldkrki
eladairalgytnvpvklhpevtatlkvhvteqk
>d1div_2 4.79.1.1.1 (1-55) Ribosomal protein L9 N-domain {Bacillus stearothermophilus}
mkviflkdvkgkgkkgeiknvadgyannflfkqglaieatpanlkaleaqkqkeq
>d1dja__ 5.3.1.1.6 beta-Lactamase, class A {Staphylococcus aureus}
mkelndlekkynahigvyaldtksgkevkfnsdkrfayastshainsailleqvpynkln
kkvhinkddivayspilekyvgkditlkalieasmtysdntannkiikeiggikkvkqrl
kelgdkvtnpvryeielnyyspkskkdtstpaafgktlnkliangklskenkkflldlml
nnksgdtlikdgvpkdykvadksgqaityasrndvafvypkgqsepivlviftnkdnksd
kpndklisetaksvmkef
>d1djb__ 5.3.1.1.6 beta-Lactamase, class A {Staphylococcus aureus}
kelndlekkynahigvyaldtksgkevkfnsdkrfayaatskainsailleqvpynklnk
kvhinkddivayspilekyvgkditlkalieasmtysdntannkiikeiggikkvkqrlk
elgdkvtnpvryeielnyyspkskkdtstpaafgktlnkliangklskenkkflldlmln
nksgdtlikdgvpkdykvadksgqaityasrndvafvypkgqsepivlviftnkdnksdk
pndklisetaksvmkef
>d1djc__ 5.3.1.1.6 beta-Lactamase, class A {Staphylococcus aureus}
kelndlekkynahigvyaldtksgkevkfnsdkrfayaatskainsailleqvpynklnk
kvhinkddivayspilekyvgkditlkalieasmtysdntannkiikeiggikkvkqrlk
elgdkvtnpvryeielnyyspkskkdtstpaafgktlnkliangklskenkkflldlmln
nksgdtlikdgvpkdykvadksgqaityasrndvafvypkgqsepivlviftnkdnksdk
pndklisetaksvmkef
>d1djga1 1.42.1.7.1 (200-298) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
eietfykmltqraeidrafeeaagsaetlsverlvtflqhqqreeeagpalalslierye
psetakaqrqmtkdgflmyllsadgnafslahrrvyqdm
>d1djga2 2.6.1.1.1 (626-756) PI-specific phospholipase C isozyme D1 (PLC-D1), C-terminal domain {Rat (Rattus norvegicus)}
wrperlrvriisgqqlpkvnknknsivdpkviveihgvgrdtgsrqtavitnngfnprwd
mefefevtvpdlalvrfmvedydssskndfigqstipwnslkqgyrhvhllskngdqhps
atlfvkisiqd
>d1djga3 3.1.16.1.1 (299-625) Phospholipase C isozyme D1 (PLC-D1) {Rat (Rattus norvegicus)}
dqplshylvssshntylledqltgpssteayiralckgcrcleldcwdgpnqepiiyhgy
tftskilfcdvlrairdyafkaspypvilslenhcsleqqrvmarhlrailgpilldqpl
dgvttslpspeqlkgkillkgkklggllpaggengseatdvsdeveaaemedeavrsqvq
hkpkedklklvpelsdmiiycksvhfggfsspgtsgqafyemasfsesralrllqesgng
fvrhnvsclsriypagwrtdssnyspvemwnggcqivalnfqtpgpemdvylgcfqdngg
cgyvlkpaflrdpnttfnsraltqgpw
>d1djgb1 1.42.1.7.1 (158-298) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
nkmnfkelkdflkelniqvddgyarkifrecdhsqtdsledeeietfykmltqraeidra
feeaagsaetlsverlvtflqhqqreeeagpalalslieryepsetakaqrqmtkdgflm
yllsadgnafslahrrvyqdm
>d1djgb2 2.6.1.1.1 (626-756) PI-specific phospholipase C isozyme D1 (PLC-D1), C-terminal domain {Rat (Rattus norvegicus)}
wrperlrvriisgqqlpkvnknknsivdpkviveihgvgrdtgsrqtavitnngfnprwd
mefefevtvpdlalvrfmvedydssskndfigqstipwnslkqgyrhvhllskngdqhps
atlfvkisiqd
>d1djgb3 3.1.16.1.1 (299-625) Phospholipase C isozyme D1 (PLC-D1) {Rat (Rattus norvegicus)}
dqplshylvssshntylledqltgpssteayiralckgcrcleldcwdgpnqepiiyhgy
tftskilfcdvlrairdyafkaspypvilslenhcsleqqrvmarhlrailgpilldqpl
dgvttslpspeqlkgkillkgkklggllpaggengseatdvsdeveaaemedeavrsqvq
hkpkedklklvpelsdmiiycksvhfggfsspgtsgqafyemasfsesralrllqesgng
fvrhnvsclsriypagwrtdssnyspvemwnggcqivalnfqtpgpemdvylgcfqdngg
cgyvlkpaflrdpnttfnsraltqgpw
>d1djha1 1.42.1.7.1 (200-298) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
eietfykmltqraeidrafeeaagsaetlsverlvtflqhqqreeeagpalalslierye
psetakaqrqmtkdgflmyllsadgnafslahrrvyqdm
>d1djha2 2.6.1.1.1 (626-756) PI-specific phospholipase C isozyme D1 (PLC-D1), C-terminal domain {Rat (Rattus norvegicus)}
wrperlrvriisgqqlpkvnknknsivdpkviveihgvgrdtgsrqtavitnngfnprwd
mefefevtvpdlalvrfmvedydssskndfigqstipwnslkqgyrhvhllskngdqhps
atlfvkisiqd
>d1djha3 3.1.16.1.1 (299-625) Phospholipase C isozyme D1 (PLC-D1) {Rat (Rattus norvegicus)}
dqplshylvssshntylledqltgpssteayiralckgcrcleldcwdgpnqepiiyhgy
tftskilfcdvlrairdyafkaspypvilslenhcsleqqrvmarhlrailgpilldqpl
dgvttslpspeqlkgkillkgkklggllpaggengseatdvsdeveaaemedeavrsqvq
hkpkedklklvpelsdmiiycksvhfggfsspgtsgqafyemasfsesralrllqesgng
fvrhnvsclsriypagwrtdssnyspvemwnggcqivalnfqtpgpemdvylgcfqdngg
cgyvlkpaflrdpnttfnsraltqgpw
>d1djhb1 1.42.1.7.1 (158-298) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
nkmnfkelkdflkelniqvddgyarkifrecdhsqtdsledeeietfykmltqraeidra
feeaagsaetlsverlvtflqhqqreeeagpalalslieryepsetakaqrqmtkdgflm
yllsadgnafslahrrvyqdm
>d1djhb2 2.6.1.1.1 (626-756) PI-specific phospholipase C isozyme D1 (PLC-D1), C-terminal domain {Rat (Rattus norvegicus)}
wrperlrvriisgqqlpkvnknknsivdpkviveihgvgrdtgsrqtavitnngfnprwd
mefefevtvpdlalvrfmvedydssskndfigqstipwnslkqgyrhvhllskngdqhps
atlfvkisiqd
>d1djhb3 3.1.16.1.1 (299-625) Phospholipase C isozyme D1 (PLC-D1) {Rat (Rattus norvegicus)}
dqplshylvssshntylledqltgpssteayiralckgcrcleldcwdgpnqepiiyhgy
tftskilfcdvlrairdyafkaspypvilslenhcsleqqrvmarhlrailgpilldqpl
dgvttslpspeqlkgkillkgkklggllpaggengseatdvsdeveaaemedeavrsqvq
hkpkedklklvpelsdmiiycksvhfggfsspgtsgqafyemasfsesralrllqesgng
fvrhnvsclsriypagwrtdssnyspvemwnggcqivalnfqtpgpemdvylgcfqdngg
cgyvlkpaflrdpnttfnsraltqgpw
>d1djia1 1.42.1.7.1 (200-298) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
eietfykmltqraeidrafeeaagsaetlsverlvtflqhqqreeeagpalalslierye
psetakaqrqmtkdgflmyllsadgnafslahrrvyqdm
>d1djia2 2.6.1.1.1 (626-756) PI-specific phospholipase C isozyme D1 (PLC-D1), C-terminal domain {Rat (Rattus norvegicus)}
wrperlrvriisgqqlpkvnknknsivdpkviveihgvgrdtgsrqtavitnngfnprwd
mefefevtvpdlalvrfmvedydssskndfigqstipwnslkqgyrhvhllskngdqhps
atlfvkisiqd
>d1djia3 3.1.16.1.1 (299-625) Phospholipase C isozyme D1 (PLC-D1) {Rat (Rattus norvegicus)}
dqplshylvssshntylledqltgpssteayiralckgcrcleldcwdgpnqepiiyhgy
tftskilfcdvlrairdyafkaspypvilslenhcsleqqrvmarhlrailgpilldqpl
dgvttslpspeqlkgkillkgkklggllpaggengseatdvsdeveaaemedeavrsqvq
hkpkedklklvpelsdmiiycksvhfggfsspgtsgqafyemasfsesralrllqesgng
fvrhnvsclsriypagwrtdssnyspvemwnggcqivalnfqtpgpemdvylgcfqdngg
cgyvlkpaflrdpnttfnsraltqgpw
>d1djib1 1.42.1.7.1 (158-298) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
nkmnfkelkdflkelniqvddgyarkifrecdhsqtdsledeeietfykmltqraeidra
feeaagsaetlsverlvtflqhqqreeeagpalalslieryepsetakaqrqmtkdgflm
yllsadgnafslahrrvyqdm
>d1djib2 2.6.1.1.1 (626-756) PI-specific phospholipase C isozyme D1 (PLC-D1), C-terminal domain {Rat (Rattus norvegicus)}
wrperlrvriisgqqlpkvnknknsivdpkviveihgvgrdtgsrqtavitnngfnprwd
mefefevtvpdlalvrfmvedydssskndfigqstipwnslkqgyrhvhllskngdqhps
atlfvkisiqd
>d1djib3 3.1.16.1.1 (299-625) Phospholipase C isozyme D1 (PLC-D1) {Rat (Rattus norvegicus)}
dqplshylvssshntylledqltgpssteayiralckgcrcleldcwdgpnqepiiyhgy
tftskilfcdvlrairdyafkaspypvilslenhcsleqqrvmarhlrailgpilldqpl
dgvttslpspeqlkgkillkgkklggllpaggengseatdvsdeveaaemedeavrsqvq
hkpkedklklvpelsdmiiycksvhfggfsspgtsgqafyemasfsesralrllqesgng
fvrhnvsclsriypagwrtdssnyspvemwnggcqivalnfqtpgpemdvylgcfqdngg
cgyvlkpaflrdpnttfnsraltqgpw
>d1djwa1 1.42.1.7.1 (200-298) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
eietfykmltqraeidrafeeaagsaetlsverlvtflqhqqreeeagpalalslierye
psetakaqrqmtkdgflmyllsadgnafslahrrvyqdm
>d1djwa2 2.6.1.1.1 (626-756) PI-specific phospholipase C isozyme D1 (PLC-D1), C-terminal domain {Rat (Rattus norvegicus)}
wrperlrvriisgqqlpkvnknknsivdpkviveihgvgrdtgsrqtavitnngfnprwd
mefefevtvpdlalvrfmvedydssskndfigqstipwnslkqgyrhvhllskngdqhps
atlfvkisiqd
>d1djwa3 3.1.16.1.1 (299-625) Phospholipase C isozyme D1 (PLC-D1) {Rat (Rattus norvegicus)}
dqplshylvssshntylledqltgpssteayiralckgcrcleldcwdgpnqepiiyhgy
tftskilfcdvlrairdyafkaspypvilslenhcsleqqrvmarhlrailgpilldqpl
dgvttslpspeqlkgkillkgkklggllpaggengseatdvsdeveaaemedeavrsqvq
hkpkedklklvpelsdmiiycksvhfggfsspgtsgqafyemasfsesralrllqesgng
fvrhnvsclsriypagwrtdssnyspvemwnggcqivalnfqtpgpemdvylgcfqdngg
cgyvlkpaflrdpnttfnsraltqgpw
>d1djwb1 1.42.1.7.1 (158-298) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
nkmnfkelkdflkelniqvddgyarkifrecdhsqtdsledeeietfykmltqraeidra
feeaagsaetlsverlvtflqhqqreeeagpalalslieryepsetakaqrqmtkdgflm
yllsadgnafslahrrvyqdm
>d1djwb2 2.6.1.1.1 (626-756) PI-specific phospholipase C isozyme D1 (PLC-D1), C-terminal domain {Rat (Rattus norvegicus)}
wrperlrvriisgqqlpkvnknknsivdpkviveihgvgrdtgsrqtavitnngfnprwd
mefefevtvpdlalvrfmvedydssskndfigqstipwnslkqgyrhvhllskngdqhps
atlfvkisiqd
>d1djwb3 3.1.16.1.1 (299-625) Phospholipase C isozyme D1 (PLC-D1) {Rat (Rattus norvegicus)}
dqplshylvssshntylledqltgpssteayiralckgcrcleldcwdgpnqepiiyhgy
tftskilfcdvlrairdyafkaspypvilslenhcsleqqrvmarhlrailgpilldqpl
dgvttslpspeqlkgkillkgkklggllpaggengseatdvsdeveaaemedeavrsqvq
hkpkedklklvpelsdmiiycksvhfggfsspgtsgqafyemasfsesralrllqesgng
fvrhnvsclsriypagwrtdssnyspvemwnggcqivalnfqtpgpemdvylgcfqdngg
cgyvlkpaflrdpnttfnsraltqgpw
>d1djxa1 1.42.1.7.1 (200-298) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
eietfykmltqraeidrafeeaagsaetlsverlvtflqhqqreeeagpalalslierye
psetakaqrqmtkdgflmyllsadgnafslahrrvyqdm
>d1djxa2 2.6.1.1.1 (626-756) PI-specific phospholipase C isozyme D1 (PLC-D1), C-terminal domain {Rat (Rattus norvegicus)}
wrperlrvriisgqqlpkvnknknsivdpkviveihgvgrdtgsrqtavitnngfnprwd
mefefevtvpdlalvrfmvedydssskndfigqstipwnslkqgyrhvhllskngdqhps
atlfvkisiqd
>d1djxa3 3.1.16.1.1 (299-625) Phospholipase C isozyme D1 (PLC-D1) {Rat (Rattus norvegicus)}
dqplshylvssshntylledqltgpssteayiralckgcrcleldcwdgpnqepiiyhgy
tftskilfcdvlrairdyafkaspypvilslenhcsleqqrvmarhlrailgpilldqpl
dgvttslpspeqlkgkillkgkklggllpaggengseatdvsdeveaaemedeavrsqvq
hkpkedklklvpelsdmiiycksvhfggfsspgtsgqafyemasfsesralrllqesgng
fvrhnvsclsriypagwrtdssnyspvemwnggcqivalnfqtpgpemdvylgcfqdngg
cgyvlkpaflrdpnttfnsraltqgpw
>d1djxb1 1.42.1.7.1 (158-298) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
nkmnfkelkdflkelniqvddgyarkifrecdhsqtdsledeeietfykmltqraeidra
feeaagsaetlsverlvtflqhqqreeeagpalalslieryepsetakaqrqmtkdgflm
yllsadgnafslahrrvyqdm
>d1djxb2 2.6.1.1.1 (626-756) PI-specific phospholipase C isozyme D1 (PLC-D1), C-terminal domain {Rat (Rattus norvegicus)}
wrperlrvriisgqqlpkvnknknsivdpkviveihgvgrdtgsrqtavitnngfnprwd
mefefevtvpdlalvrfmvedydssskndfigqstipwnslkqgyrhvhllskngdqhps
atlfvkisiqd
>d1djxb3 3.1.16.1.1 (299-625) Phospholipase C isozyme D1 (PLC-D1) {Rat (Rattus norvegicus)}
dqplshylvssshntylledqltgpssteayiralckgcrcleldcwdgpnqepiiyhgy
tftskilfcdvlrairdyafkaspypvilslenhcsleqqrvmarhlrailgpilldqpl
dgvttslpspeqlkgkillkgkklggllpaggengseatdvsdeveaaemedeavrsqvq
hkpkedklklvpelsdmiiycksvhfggfsspgtsgqafyemasfsesralrllqesgng
fvrhnvsclsriypagwrtdssnyspvemwnggcqivalnfqtpgpemdvylgcfqdngg
cgyvlkpaflrdpnttfnsraltqgpw
>d1djya1 1.42.1.7.1 (200-298) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
eietfykmltqraeidrafeeaagsaetlsverlvtflqhqqreeeagpalalslierye
psetakaqrqmtkdgflmyllsadgnafslahrrvyqdm
>d1djya2 2.6.1.1.1 (626-756) PI-specific phospholipase C isozyme D1 (PLC-D1), C-terminal domain {Rat (Rattus norvegicus)}
wrperlrvriisgqqlpkvnknknsivdpkviveihgvgrdtgsrqtavitnngfnprwd
mefefevtvpdlalvrfmvedydssskndfigqstipwnslkqgyrhvhllskngdqhps
atlfvkisiqd
>d1djya3 3.1.16.1.1 (299-625) Phospholipase C isozyme D1 (PLC-D1) {Rat (Rattus norvegicus)}
dqplshylvssshntylledqltgpssteayiralckgcrcleldcwdgpnqepiiyhgy
tftskilfcdvlrairdyafkaspypvilslenhcsleqqrvmarhlrailgpilldqpl
dgvttslpspeqlkgkillkgkklggllpaggengseatdvsdeveaaemedeavrsqvq
hkpkedklklvpelsdmiiycksvhfggfsspgtsgqafyemasfsesralrllqesgng
fvrhnvsclsriypagwrtdssnyspvemwnggcqivalnfqtpgpemdvylgcfqdngg
cgyvlkpaflrdpnttfnsraltqgpw
>d1djyb1 1.42.1.7.1 (158-298) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
nkmnfkelkdflkelniqvddgyarkifrecdhsqtdsledeeietfykmltqraeidra
feeaagsaetlsverlvtflqhqqreeeagpalalslieryepsetakaqrqmtkdgflm
yllsadgnafslahrrvyqdm
>d1djyb2 2.6.1.1.1 (626-756) PI-specific phospholipase C isozyme D1 (PLC-D1), C-terminal domain {Rat (Rattus norvegicus)}
wrperlrvriisgqqlpkvnknknsivdpkviveihgvgrdtgsrqtavitnngfnprwd
mefefevtvpdlalvrfmvedydssskndfigqstipwnslkqgyrhvhllskngdqhps
atlfvkisiqd
>d1djyb3 3.1.16.1.1 (299-625) Phospholipase C isozyme D1 (PLC-D1) {Rat (Rattus norvegicus)}
dqplshylvssshntylledqltgpssteayiralckgcrcleldcwdgpnqepiiyhgy
tftskilfcdvlrairdyafkaspypvilslenhcsleqqrvmarhlrailgpilldqpl
dgvttslpspeqlkgkillkgkklggllpaggengseatdvsdeveaaemedeavrsqvq
hkpkedklklvpelsdmiiycksvhfggfsspgtsgqafyemasfsesralrllqesgng
fvrhnvsclsriypagwrtdssnyspvemwnggcqivalnfqtpgpemdvylgcfqdngg
cgyvlkpaflrdpnttfnsraltqgpw
>d1djza1 1.42.1.7.1 (200-298) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
eietfykmltqraeidrafeeaagsaetlsverlvtflqhqqreeeagpalalslierye
psetakaqrqmtkdgflmyllsadgnafslahrrvyqdm
>d1djza2 2.6.1.1.1 (626-756) PI-specific phospholipase C isozyme D1 (PLC-D1), C-terminal domain {Rat (Rattus norvegicus)}
wrperlrvriisgqqlpkvnknknsivdpkviveihgvgrdtgsrqtavitnngfnprwd
mefefevtvpdlalvrfmvedydssskndfigqstipwnslkqgyrhvhllskngdqhps
atlfvkisiqd
>d1djza3 3.1.16.1.1 (299-625) Phospholipase C isozyme D1 (PLC-D1) {Rat (Rattus norvegicus)}
dqplshylvssshntylledqltgpssteayiralckgcrcleldcwdgpnqepiiyhgy
tftskilfcdvlrairdyafkaspypvilslenhcsleqqrvmarhlrailgpilldqpl
dgvttslpspeqlkgkillkgkklggllpaggengseatdvsdeveaaemedeavrsqvq
hkpkedklklvpelsdmiiycksvhfggfsspgtsgqafyemasfsesralrllqesgng
fvrhnvsclsriypagwrtdssnyspvemwnggcqivalnfqtpgpemdvylgcfqdngg
cgyvlkpaflrdpnttfnsraltqgpw
>d1djzb1 1.42.1.7.1 (158-298) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
nkmnfkelkdflkelniqvddgyarkifrecdhsqtdsledeeietfykmltqraeidra
feeaagsaetlsverlvtflqhqqreeeagpalalslieryepsetakaqrqmtkdgflm
yllsadgnafslahrrvyqdm
>d1djzb2 2.6.1.1.1 (626-756) PI-specific phospholipase C isozyme D1 (PLC-D1), C-terminal domain {Rat (Rattus norvegicus)}
wrperlrvriisgqqlpkvnknknsivdpkviveihgvgrdtgsrqtavitnngfnprwd
mefefevtvpdlalvrfmvedydssskndfigqstipwnslkqgyrhvhllskngdqhps
atlfvkisiqd
>d1djzb3 3.1.16.1.1 (299-625) Phospholipase C isozyme D1 (PLC-D1) {Rat (Rattus norvegicus)}
dqplshylvssshntylledqltgpssteayiralckgcrcleldcwdgpnqepiiyhgy
tftskilfcdvlrairdyafkaspypvilslenhcsleqqrvmarhlrailgpilldqpl
dgvttslpspeqlkgkillkgkklggllpaggengseatdvsdeveaaemedeavrsqvq
hkpkedklklvpelsdmiiycksvhfggfsspgtsgqafyemasfsesralrllqesgng
fvrhnvsclsriypagwrtdssnyspvemwnggcqivalnfqtpgpemdvylgcfqdngg
cgyvlkpaflrdpnttfnsraltqgpw
>d1dka__ 3.57.1.4.1 Dialkylglycine decarboxylase {Pseudomonas cepacia}
lnddatfwrnarhhlvryggtfepmiierakgsfvydadgraildftsgqmsavlghchp
eivsvigeyagkldhlfsemlsrpvvdlatrlanitppgldralllstgaesneaairma
klvtgkyeivgfaqswhgmtgaaasatysagrkgvgpaavgsfaipapftyrprfernga
ydylaeldyafdlidrqssgnlaafiaepilssggiielpdgymaalkrkceargmllil
deaqtgvgrtgtmfacqrdgvtpdiltlsktlgaglplaaivtsaaieerahelgylfyt
thvsdplpaavglrvldvvqrdglvaranvmgdrlrrglldlmerfdcigdvrgrglllg
veivkdrrtkepadglgakitrecmnlglsmnivqlpgmggvfriappltvsedeidlgl
sllgqaieral
>d1dkga1 2.64.1.1.1 (139-197) Head domain of nucleotide exchange factor GrpE {Escherichia coli}
veviaetnvpldpnvhqaiamvesddvapgnvlgimqkgytlngrtiraamvtvakaka
>d1dkgb1 2.64.1.1.1 (139-195) Head domain of nucleotide exchange factor GrpE {Escherichia coli}
veviaetnvpldpnvhqaiamvesddvapgnvlgimqkgytlngrtiraamvtvaka
>d1dkgd_ 3.46.1.1.3 Heat shock protein 70kDa, ATPase fragment {Escherichia coli, gene dnaK}
kiigidlgttnscvaimdgttprvlenaegdrttpsiiaytqdgetlvgqpakrqavtnp
qntlfaikrligrrfqdeevqrdvsimpfkiiaadngdawvevkgqkmappqisaevlkk
mkktaedylgepvteavitvpayfndaqrqatkdagriaglevkriineptaaalaygld
kgtgnrtiavydlgggtfdisiieidevdgektfevlatngdthlggedfdsrlinylve
efkkdqgidlrndplamqrlkeaaekakielssaqqtdvnlpyitadatgpkhmnikvtr
akleslvedlvnrsiellkvalqdaglsvsdiddvilvggqtrmpmvqkkvaeffgkepr
kdvnpdeavaigaavqggvlt
>d1dkj__ 4.2.1.2.5 Lysozyme {Bobwhite quail (Colinus virginianus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfnsqatnrntdgstdygvlqins
rwwcndgktpgsrnlcnipcsallssditatvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1dkka_ 4.2.1.2.5 Lysozyme {Bobwhite quail (Colinus virginianus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfnsqatnrntdgstdygvlqins
rwwcndgktpgsrnlcnipcsallssditatvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1dkkb_ 4.2.1.2.5 Lysozyme {Bobwhite quail (Colinus virginianus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfnsqatnrntdgstdygvlqins
rwwcndgktpgsrnlcnipcsallssditatvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1dksa_ 4.76.1.1.3 CksHs1 {Human (Homo sapiens)}
shkqiyysdkyddeefeyrhvmlpkdiaklvpkthlmsesewrnlgvqqsqgwvhymihe
pephillfrrplpkkp
>d1dksb_ 4.76.1.1.3 CksHs1 {Human (Homo sapiens)}
kqiyysdkyddeefeyrhvmlpkdiaklvpkthlmsesewrnlgvqqsqgwvhymihepe
phillfrrplpkk
>d1dkta_ 4.76.1.1.3 CksHs1 {Human (Homo sapiens)}
qiyysdkyddeefeyrhvmlpkdiaklvpkthlmsesewrnlgvqqsqgwvhymihepep
hillfrrplpkk
>d1dktb_ 4.76.1.1.3 CksHs1 {Human (Homo sapiens)}
qiyysdkyddeefeyrhvmlpkdiaklvpkthlmsesewrnlgvqqsqgwvhymihepep
hillfrrplpk
>d1dkxa_ 5.16.1.1.1 DnaK {Escherichia coli}
vllldvtplslgietmggvmttliaknttiptkhsqvfstaednqsavtihvlqgerkra
adnkslgqfnldginpaprgmpqievtfdidadgilhvsakdknsgkeqkitikassgln
edeiqkmvrdaeanaeadrkfdelvqtrnqgdhllhstrkqveeagdklpaddktaiesa
ltaletalkgedkaaieakmqelaqvsqklmeiaqqqha
>d1dkya_ 5.16.1.1.1 DnaK {Escherichia coli}
vllldvtplslgietmggvmttliaknttiptkhsqvfstaednqsavsihvlqgerkra
adnkslgqfnldginpaprgmpqievtfdidadgilhvsakdknsgkeqkitikassgln
edeiqkmvrdaeanaeadrkfeelvqtrnqgdhllhstrkqveeagdklpaddktaiesa
ltaletalkgedkaaieakmqelaqvsqklm
>d1dkyb_ 5.16.1.1.1 DnaK {Escherichia coli}
vllldvtplslgietmggvmttliaknttiptkhsqvfstaednqsavsihvlqgerkra
adnkslgqfnldginpaprgmpqievtfdidadgilhvsakdknsgkeqkitikassgln
edeiqkmvrdaeanaeadrkfeelvqtrnqgdhllhstrkqveeagdklpaddktaiesa
ltaletalkgedkaaieakmqel
>d1dkza_ 5.16.1.1.1 DnaK {Escherichia coli}
vllldvtplslgietmggvmttliaknttiptkhsqvfstaednqsavsihvlqgerkra
adnkslgqfnldginpaprgmpqievtfdidadgilhvsakdknsgkeqkitikassgln
edeiqkmvrdaeanaeadrkfeelvqtrnqgdhllhstrkqveeagdklpaddktaiesa
ltaletalkgedkaaieakmqelaqvsqklmeiaq
>d1dlaa_ 3.1.6.1.3 Aldose reductase (aldehyde reductase) {Human (Homo sapiens)}
shlvlytgakmpilglgtwksppgkvteavkvaidlgyrhidcahvyqnenevglglqek
lqgqvvkredlfivsklwctdheknlvkgacqttlrdlkldyldlylihwptgfkpgkdp
fpldgdgnvvpdesdfvetweameelvdeglvkaigvsnfnhlqvekilnkpglkykpav
nqievhpyltqeklieyckskgivvtaysplgspdrpwakpedpslledprikaiaakyn
kttaqvlirfpmqrnlivipksvtperiaenfqvfdfelspedmntllsynrnwrvcalm
scashkdypfheey
>d1dlab_ 3.1.6.1.3 Aldose reductase (aldehyde reductase) {Human (Homo sapiens)}
shlvlytgakmpilglgtwksppgkvteavkvaidlgyrhidcahvyqnenevglglqek
lqgqvvkredlfivsklwctdheknlvkgacqttlrdlkldyldlylihwptgfkpgkdp
fpldgdgnvvpdesdfvetweameelvdeglvkaigvsnfnhlqvekilnkpglkykpav
nqievhpyltqeklieyckskgivvtaysplgspdrpwakpedpslledprikaiaakyn
kttaqvlirfpmqrnlivipksvtperiaenfqvfdfelspedmntllsynrnwrvcalm
scashkdypfheey
>d1dlac_ 3.1.6.1.3 Aldose reductase (aldehyde reductase) {Human (Homo sapiens)}
shlvlytgakmpilglgtwksppgkvteavkvaidlgyrhidcahvyqnenevglglqek
lqgqvvkredlfivsklwctdheknlvkgacqttlrdlkldyldlylihwptgfkpgkdp
fpldgdgnvvpdesdfvetweameelvdeglvkaigvsnfnhlqvekilnkpglkykpav
nqievhpyltqeklieyckskgivvtaysplgspdrpwakpedpslledprikaiaakyn
kttaqvlirfpmqrnlivipksvtperiaenfqvfdfelspedmntllsynrnwrvcalm
scashkdypfheey
>d1dlad_ 3.1.6.1.3 Aldose reductase (aldehyde reductase) {Human (Homo sapiens)}
shlvlytgakmpilglgtwksppgkvteavkvaidlgyrhidcahvyqnenevglglqek
lqgqvvkredlfivsklwctdheknlvkgacqttlrdlkldyldlylihwptgfkpgkdp
fpldgdgnvvpdesdfvetweameelvdeglvkaigvsnfnhlqvekilnkpglkykpav
nqievhpyltqeklieyckskgivvtaysplgspdrpwakpedpslledprikaiaakyn
kttaqvlirfpmqrnlivipksvtperiaenfqvfdfelspedmntllsynrnwrvcalm
scashkdypfheey
>d1dlc_1 2.16.1.2.1 (500-644) delta-Endotoxin, C-terminal domain {Bacillus thuringiensis tenebrionis, CRYIIIA (BT13)}
ffnmidskkitqlplvkayklqsgasvvagprftggdiiqctengsaatiyvtpdvsysq
kyrarihyastsqitftlsldgapfnqyyfdktinkgdtltynsfnlasfstpfelsgnn
lqigvtglsagdkvyidkiefipvn
>d1dlc_2 2.68.2.1.1 (290-499) delta-Endotoxin (insectocide), middle domain {Bacillus thuringiensis tenebrionis, CRYIIIA (BT13)}
lypkevkteltrdvltdpivgvnnlrgygttfsnienyirkphlfdylhriqfhtrfqpg
yygndsfnywsgnyvstrpsigsndiitspfygnkssepvqnlefngekvyravantnla
vwpsavysgvtkvefsqyndqtdeastqtydskrnvgavswdsidqlppettdeplekgy
shqlnyvmcflmqgsrgtipvltwthksvd
>d1dlc_3 6.1.3.1.1 (61-289) delta-Endotoxin (insectocide), N-terminal domain {Bacillus thuringiensis tenebrionis, CRYIIIA (BT13)}
ttkdviqkgisvvgdllgvvgfpfggalvsfytnflntiwpsedpwkafmeqvealmdqk
iadyaknkalaelqglqnnvedyvsalsswqknpvssrnphsqgrirelfsqaeshfrns
mpsfaisgyevlflttyaqaanthlfllkdaqiygeewgyekediaefykrqlkltqeyt
dhcvkwynvgldklrgssyeswvnfnryrremtltvldlialfplydvr
>d1dlfh_ 2.1.1.1.136 Immunoglobulin (variable domains of L and H chains) {Anti-dansyl Fv, (mouse), kappa L chain}
evkleesggglvqpggsmklscatsgftfsdawmdwvrqspekglewvaeirnkannhat
yyaesvkgrftisrddskrrvylqmntlraedtgiyyctgiyyhypwfaywgqgtlvtvs
>d1dlfl_ 2.1.1.1.136 Immunoglobulin (variable domains of L and H chains) {Anti-dansyl Fv, (mouse), kappa L chain}
dvvmtqtplslpvslgnqasiscrssqslvhsngntylhwylqkpgqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyfcsqsthvpftfgsgtkleikr
>d1dlha1 2.1.1.2.149 (82-182) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dr1}
itnvppevtvltnspvelrepnvlicfidkftppvvnvtwlrngkpvttgvsetvflpre
dhlfrkfhylpflpstedvydcrvehwgldepllkhwefda
>d1dlha2 4.17.1.1.4 (3-81) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
eehviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgalan
iavdkanleimtkrsnytp
>d1dlhb1 2.1.1.2.149 (93-190) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dr1}
rrvepkvtvypsktqplqhhnllvcsvsgfypgsievrwfrngqeekagvvstgliqngd
wtfqtlvmletvprsgevytcqvehpsvtspltvewra
>d1dlhb2 4.17.1.1.4 (3-92) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
trprflwqlkfechffngtervrllerciynqeesvrfdsdvgeyravtelgrpdaeywn
sqkdlleqrraavdtycrhnygvgesftvq
>d1dlhd1 2.1.1.2.149 (82-182) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dr1}
itnvppevtvltnspvelrepnvlicfidkftppvvnvtwlrngkpvttgvsetvflpre
dhlfrkfhylpflpstedvydcrvehwgldepllkhwefda
>d1dlhd2 4.17.1.1.4 (3-81) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
eehviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgalan
iavdkanleimtkrsnytp
>d1dlhe1 2.1.1.2.149 (93-190) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dr1}
rrvepkvtvypsktqplqhhnllvcsvsgfypgsievrwfrngqeekagvvstgliqngd
wtfqtlvmletvprsgevytcqvehpsvtspltvewra
>d1dlhe2 4.17.1.1.4 (3-92) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
trprflwqlkfechffngtervrllerciynqeesvrfdsdvgeyravtelgrpdaeywn
sqkdlleqrraavdtycrhnygvgesftvq
>d1dloa1 3.46.3.1.4 (430-556) HIV RNase H (Domain of reverse transcriptase) {Human immunodeficiency virus, type 1}
ekepivgaetfyvdgaanretklgkagyvtnkgrqkvvpltnttnqktelqaiylalqds
glevnivtdsqyalgiiqaqpdkseselvnqiieqlikkekvylawvpahkgiggneqvd
klvsagi
>d1dloa2 5.8.1.2.2 (1-429) HIV-1 reverse transcriptase {Human immunodeficiency virus, type 1, HIV-1}
pispietvpvklkpgmdgpkvkqwplteekikalveictemekegkiskigpenpyntpv
faikkkdstkwrklvdfrelnkrtqdfwevqlgiphpaglkkkksvtvldvgdayfsvpl
dedfrkytaftipsinnetpgiryqynvlpqgwkgspaifqssmtkilepfkkqnpdivi
yqymddlyvgsdleigqhrtkieelrqhllrwglttpdkkhqkeppflwmgyelhpdkwt
vqpivlpekdswtvndiqklvgklnwasqiypgikvrqlskllrgtkalteviplteeae
lelaenreilkepvhgvyydpskdliaeiqkqgqgqwtyqiyqepfknlktgkyarmrga
htndvkqlteavqkittesiviwgktpkfklpiqketwetwwteywqatwipewefvntp
plvklwyql
>d1dlob1 5.8.1.2.2 HIV-1 reverse transcriptase {Human immunodeficiency virus, type 1, HIV-1}
pispietvpvklkpgmdgpkvkqwplteekikalveictemekegkiskigpenpyntpv
faikkkdstkwrklvdfrelnkrtqdfwevqlgiphpaglkkkksvtvldvgdayfsvpl
dedfrkytaftipsinnetpgiryqynvlpqgwkgspaifqssmtkilepfkkqnpdivi
yqymddlyvgsdleigqhrtkieelrqhllrwglttpdkkhqkeppflwmgyelhpdkwt
vqpivlpekdswtvndiqklvgklnwasqiypgikvrqlskllrgtkalteviplteeae
lelaenreilkepvhgvyydpskdliaeiqkqgqgqwtyqiyqepfknlktgkyarmrga
htndvkqlteavqkittesiviwgktpkfklpiqketwetwwteywqatwipewefvntp
plvklwy
>d1dlr__ 3.61.1.1.5 Dihydrofolate reductases, eukaryotic type {Human (Homo sapiens)}
vgslncivavsqnmgigkngdfpwpplrnefryfqrmtttssvegkqnlvimgkktwfsi
peknrplkgrinlvlsrelkeppqgahflsrslddalklteqpelankvdmvwivggssv
ykeamnhpghlklfvtrimqdfesdtffpeidlekykllpeypgvlsdvqeekgikykfe
vyeknd
>d1dls__ 3.61.1.1.5 Dihydrofolate reductases, eukaryotic type {Human (Homo sapiens)}
vgslncivavsqnmgigkngdypwpplrnefryfqrmtttssvegkqnlvimgkktwfsi
peknrplkgrinlvlsrelkeppqgahflsrslddalklteqpelankvdmvwivggssv
ykeamnhpghlklfvtrimqdfesdtffpeidlekykllpeypgvlsdvqeekgikykfe
vyeknd
>d1dmaa_ 4.136.1.1.4 Exotoxin A, C-terminal domain {Pseudomonas aeruginosa}
flgdggdvsfstrgtqnwtverllqahrqleergyvfvgyhgtfleaaqsivfggvrars
qdldaiwrgfyiagdpalaygyaqdqepdargrirngallrvyvprsslpgfyrtsltla
apeaageverlighplplrldaitgpeeeggrletilgwplaertvvipsaiptdprnvg
gdldpssipdkeqaisalpdyasqpgkppr
>d1dmab_ 4.136.1.1.4 Exotoxin A, C-terminal domain {Pseudomonas aeruginosa}
flgdggdvsfstrgtqnwtverllqahrqleergyvfvgyhgtfleaaqsivfggvrars
qdldaiwrgfyiagdpalaygyaqdqepdargrirngallrvyvprsslpgfyrtsltla
apeaageverlighplplrldaitgpeeeggrletilgwplaertvvipsaiptdprnvg
gdldpssipdkeqaisalpd
>d1dmb__ 3.84.1.1.6 D-maltodextrin-binding protein, MBP {Escherichia coli}
kieegklviwingdkgynglaevgkkfekdtgikvtvehpdkleekfpqvaatgdgpdii
fwahdrfggyaqsgllaeitpdkafqdklypftwdavryngkliaypiavealsliynkd
llpnppktweeipaldkelkakgksalmfnlqepyftwpliaadggyafkyengkydikd
vgvdnagakagltflvdliknkhmnadtdysiaeaafnkgetamtingpwawsnidtskv
nygvtvlptfkgqpskpfvgvlsaginaaspnkelakeflenylltdegleavnkdkplg
avalksyeeelakdpriaatmenaqkgeimpnipqmsafwyavrtavinaasgrqtvdea
lkdaqtritk
>d1dmc__ 7.38.1.1.4 Metallothionein {Crab (Callinectes sapidus), alpha and beta domains}
spcqkctsgckcatkeecsktctkpcsccpk
>d1dmd__ 7.38.1.1.4 Metallothionein {Crab (Callinectes sapidus), alpha and beta domains}
spcqkctsgckcatkeecsktctkpcsccpk
>d1dme__ 7.38.1.1.4 Metallothionein {Crab (Callinectes sapidus), alpha and beta domains}
pgpccndkcvcqeggckagcqctscrcs
>d1dmf__ 7.38.1.1.4 Metallothionein {Crab (Callinectes sapidus), alpha and beta domains}
pgpccndkcvcqeggckagcqctscrcs
>d1dmo__ 1.42.1.5.11 Calmodulin {African frog (Xenopus laevis)}
adqlteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgn
gtidfpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdee
vdemireanidgdgqvnyeefvqmmtak
>d1dmpa_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieixghkaigtvlvgptpvniigrnlltqigatlnf
>d1dmpb_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieixghkaigtvlvgptpvniigrnlltqigatlnf
>d1dmr_1 2.46.2.2.2 (626-781) Dimethylsulfoxide reductase (DMSO reductase) {Rhodobacter capsulatus}
erldgpgakyplhiaashpfnrlhsqlngtvlregyavqghepclmhpddaaargiadgd
vvrvhndrgqiltgvkvtdavmkgviqiyeggwydpsdvtepgtldkygdvnvlsadigt
sklaqgncgqtvlaevekytgpavtltgfvapkaae
>d1dmr_2 3.70.1.1.2 (3-625) Dimethylsulfoxide reductase (DMSO reductase) {Rhodobacter capsulatus}
langtvmsgshwgvftatvengrataftpwekdphpspmlagvldsiysptrikypmvrr
eflekgvnadrstrgngdfvrvswdqaldlvaaevkrveetygpegvfggsygwkspgrl
hncttllrrmltlaggyvngagdystgaaqvimphvvgtlevyeqqtawpvlaentevmv
fwaadpiktsqigwvipehgaypglealkakgtkvividpvrtktveffgaehitpkpqt
dvaimlgmahtlvaedlydkdfianytsgfdkflpyldgetdstpktaewaegisgvpae
tikelarlfeskrtmlaagwsmqrmhhgeqahwmlvtlasmlgqiglpgggfglsyhysg
ggtpstsgpalagitdggaatkgpewlaasgasvipvarvvdmlenpgaefdfngtrskf
pdvkmaywvggnpfvhhqdrnrmvkawekletfvvhdfqwtptarhadivlpattsyern
dietigdysntgilamkkiveplyearsdydifaavaerlgkgaeftegkdemgwiksfy
ddaakqgkaagvqmpafdafwaegivefpvtdgadfvryasfredpllnplgtptgliei
yskniekmgyddcpahptwmepl
>d1dms_1 2.46.2.2.2 (626-781) Dimethylsulfoxide reductase (DMSO reductase) {Rhodobacter capsulatus}
erldgpgakyplhiaashpfnrlhsqlngtvlregyavqghepclmhpddaaargiadgd
vvrvhndrgqiltgvkvtdavmkgviqiyeggwydpsdvteagtldkygdvnvlsadigt
sklaqgncgqtvlaevekytgpavtltgfvapkaae
>d1dms_2 3.70.1.1.2 (3-625) Dimethylsulfoxide reductase (DMSO reductase) {Rhodobacter capsulatus}
langtvmsgshwgvftatvengrataftpwekdphptpmlegvldsiysptrikypmvrr
eflekgvnadrstrgngdfvrvswdqaldlvaaevkrveetygpqgvfggsygwkspgrl
hncttllrrmltlaggyvngagdystgaaqvimphvvgtlevyeqqtawpvlaentevmv
fwaadpiktsqigwvipehgaypglealkakgtkvividpvrtktveffgadhvtpkpqt
dvaimlgmahtlvaedlydkdfianytsgfdkflpylmgetdstpktaewasdisgvpae
tikelarlfkskrtmlaagwsmqrmhhgeqahwmlvtlasmlgqiglpgggfglsyhysg
ggtpsssgpalsgitdggaatkgpewlaasgasvipvarvvdmlenpgaefdfngtrskf
pdvkmaywvggnpfvhhqdrnrmvkawekletfivhdfqwtptarhadivlpattsyern
dietigdysntgilamkkiveplyearsdydifaavaerlgkgkeftegkdemgwiksfy
ddaakqgkaggvempafdafwaegivefpvtdgadfvryasfredpllnplgtptgliei
yskniekmgyddcpahptwmepl
>d1dmxa_ 2.65.1.1.5 Carbonic anhydrase {Murine (Mus musculus), liver, isozyme V}
gtrqspiniqwkdsvydpqlaplrvsydaascrylwntgyffqvefddscedsgisggpl
gnhyrlkqfhfhwgatdewgsehavdghtypaelhlvhwnstkyenykkasvgenglavi
gvflklgahhqalqklvdvlpevrhkdtqvamgpfdpsclmpacrdywtypgslttppla
esvtwivqktpvevspsqlsmfrtllfsgrgeeedvmvnnyrplqplrdrklrssfr
>d1dmxb_ 2.65.1.1.5 Carbonic anhydrase {Murine (Mus musculus), liver, isozyme V}
gtrqspiniqwkdsvydpqlaplrvsydaascrylwntgyffqvefddscedsgisggpl
gnhyrlkqfhfhwgatdewgsehavdghtypaelhlvhwnstkyenykkasvgenglavi
gvflklgahhqalqklvdvlpevrhkdtqvamgpfdpsclmpacrdywtypgslttppla
esvtwivqktpvevspsqlsmfrtllfsgrgeeedvmvnnyrplqplrdrklrssfr
>d1dmya_ 2.65.1.1.5 Carbonic anhydrase {Murine (Mus musculus), liver, isozyme V}
gtrqspiniqwkdsvydpqlaplrvsydaascrylwntgyffqvefddscedsgisggpl
gnhyrlkqfhfhwgatdewgsehavdghtypaelhlvhwnstkyenykkasvgenglavi
gvflklgahhqalqklvdvlpevrhkdtqvamgpfdpsclmpacrdywtypgslttppla
esvtwivqktpvevspsqlsmfrtllfsgrgeeedvmvnnyrplqplrdrklrssfr
>d1dmyb_ 2.65.1.1.5 Carbonic anhydrase {Murine (Mus musculus), liver, isozyme V}
gtrqspiniqwkdsvydpqlaplrvsydaascrylwntgyffqvefddscedsgisggpl
gnhyrlkqfhfhwgatdewgsehavdghtypaelhlvhwnstkyenykkasvgenglavi
gvflklgahhqalqklvdvlpevrhkdtqvamgpfdpsclmpacrdywtypgslttppla
esvtwivqktpvevspsqlsmfrtllfsgrgeeedvmvnnyrplqplrdrklrssfr
>d1dnaa_ 4.91.1.1.1 Thymidylate synthase {Escherichia coli}
kqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihellw
flqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlkn
dpdsrriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscnvflglpfniasy
allvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesifd
yrfedfeiegydphpgikapvai
>d1dnab_ 4.91.1.1.1 Thymidylate synthase {Escherichia coli}
kqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihellw
flqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlkn
dpdsrriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscnvflglpfniasy
allvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesifd
yrfedfeiegydphpgikapvai
>d1dnc_1 3.3.1.5.1 (18-165,291-363) Glutathione reductase {Human (Homo sapiens)}
vasydylvigggsgglasarraaelgaraavveshklggtcvnvgxvpkkvmwntavhse
fmhdhadygfpscegkfnwrvikekrdayvsrlnaiyqnnltkshieiirghaaftsdpk
ptievsgkkytaphiliatggmpstpheXrvpntkdlslnklgiqtddkghiivdefqnt
nvkgiyavgdvcgkalltpvaiaagrklahrlfeykedskld
>d1dnc_2 3.3.1.5.1 (166-290) Glutathione reductase {Human (Homo sapiens)}
sqipgaslgitsdgffqleelpgrsvivgagyiavemagilsalgsktslmirhdkvlrs
fdsmistncteelenagvevlkfsqvkevkktlsglevsmvtavpgrlpvmtmipdvdcl
lwaig
>d1dnc_3 4.67.1.1.1 (364-478) Glutathione reductase {Human (Homo sapiens)}
ynniptvvfshppigtvgltedeaihkygienvktystsftpmyhavtkrktkcvmkmvc
ankeekvvgihmqglgcdemlqgfavavkmgatkadfdntvaihptsseelvtlr
>d1dnka_ 4.122.1.1.3 Deoxyribonuclease I {Bovine (Bos taurus)}
lkiaafnirtfgetkmsnatlasyivrivrrydivliqevrdshlvavgklldylnqddp
ntyhyvvseplgrnsykerylflfrpnkvsvldtyqyddgcescgndsfsrepavvkfss
hstkvkefaivalhsapsdavaeinslydvyldvqqkwhlndvmlmgdfnadcsyvtssq
wssirlrtsstfqwlipdsadttatstncaydrivvagsllqssvvpgsaapfdfqaayg
lsnemalaisdhypvevtlt
>d1dnpa1 1.95.1.1.1 (201-469) FAD-binding (C-terminal) domain of DNA photolyase {Escherichia coli}
pveekaaiaqlrqfcqngageyeqqrdfpavegtsrlsaslatgglsprqclhrllaeqp
qaldggagsvwlneliwrefyrhlityhpslckhrpfiawtdrvqwqsnpahlqawqegk
tgypivdaamrqlnstgwmhnrlrmitasflvkdllidwregeryfmsqlidgdlaanng
gwqwaastgtdaapyfrifnpttqgekfdhegefirqwlpelrdvpgkvvhepwkwaqka
gvtldypqpivehkearvqtlaayeaark
>d1dnpa2 3.21.1.1.1 (1-200) N-terminal domain of DNA photolyase {Escherichia coli}
tthlvwfrqdlrlhdnlalaaacrnssarvlalyiatprqwathnmsprqaelinaqlng
lqialaekgipllfrevddfvasveivkqvcaensvthlfynyqyevnerardveveral
rnvvcegfddsvilppgavmtgnhemykvftpfknawlkrlregmpecvaapkvrssgsi
epspsitlnyprqsfdtahf
>d1dnpb1 1.95.1.1.1 (201-469) FAD-binding (C-terminal) domain of DNA photolyase {Escherichia coli}
pveekaaiaqlrqfcqngageyeqqrdfpavegtsrlsaslatgglsprqclhrllaeqp
qaldggagsvwlneliwrefyrhlityhpslckhrpfiawtdrvqwqsnpahlqawqegk
tgypivdaamrqlnstgwmhnrlrmitasflvkdllidwregeryfmsqlidgdlaanng
gwqwaastgtdaapyfrifnpttqgekfdhegefirqwlpelrdvpgkvvhepwkwaqka
gvtldypqpivehkearvqtlaayeaark
>d1dnpb2 3.21.1.1.1 (1-200) N-terminal domain of DNA photolyase {Escherichia coli}
tthlvwfrqdlrlhdnlalaaacrnssarvlalyiatprqwathnmsprqaelinaqlng
lqialaekgipllfrevddfvasveivkqvcaensvthlfynyqyevnerardveveral
rnvvcegfddsvilppgavmtgnhemykvftpfknawlkrlregmpecvaapkvrssgsi
epspsitlnyprqsfdtahf
>d1dnv__ 2.9.1.3.2 Galleria mellonella densovirus capsid protein {Wax moth (Galleria mellonella), densovirus}
vyiiprpfsnfgkklstytkshkfmifglannvigptgtgttavnrllttclaeipwqkl
plymnqsefdllppgsrvvecnvkvifrtnriafetsstvtkqatlnqisnvqtaiglnk
lgwginraftafqsdqpmiptattapkyepvtgdtgyrgmiadyygadstndtafgnagn
yphhqvssftflqnyycmyqqtnqgtggwpclaehlqqfdsktvnnqclidvtykpkmgl
iksplnykiigqptvkgtisvgdnlvnmrgavvtnppeatqnvaesthnltrnfpadlfn
iysdieksqvlhkgpwghenpqiqpsvhigiqavpalttgallinssplnswtdsmgyid
vmssctvmeaqpthfpfsteantnpgntiyrinltpnsltsafnglygngatlgn
>d1dob_1 3.3.1.2.4 (1-173,276-394) p-Hydroxybenzoate hydroxylase (PHBH) {Pseudomonas aeruginosa}
mktqvaiigagpsglllgqllhkagidnvilerqtpdyvlgriragvleqgmvdllreag
vdrrmardglvhegveiafagqrrridlkrlsggktvtvygqtevtrdlmeareacgatt
vyqaaevrlhdlqgerpyvtferdgerlrldcdyiagcdgfhgisrqsipaerXmqhgrl
flagdaahivpptgakglnlaasdvstlyrlllkayregrgellerysaiclrriwkaer
fswwmtsvlhrfpdtdafsqriqqteleyylgseaglatiaenyvglpyeeie
>d1dob_2 4.14.1.2.2 (174-275) p-Hydroxybenzoate hydroxylase, PHBH {Pseudomonas aeruginosa}
lkvfervypfgwlglladtppvsheliyanhprgfalcsqrsatrsryfvqvplsekved
wsderfwtelkarlpsevaeklvtgpsleksiaplrsfvvep
>d1doc_1 3.3.1.2.4 (1-173,276-394) p-Hydroxybenzoate hydroxylase (PHBH) {Pseudomonas aeruginosa}
mktqvaiigagpsglllgqllhkagidnvilerqtpdyvlgriragvleqgmvdllreag
vdrrmardglvhegveiafagqrrridlkrlsggktvtvygqtevtrdlmeareacgatt
vyqaaevrlhdlqgerpyvtferdgerlrldcdyiagcdgfhgisrqsipaerXmqhgrl
flagdaahivpptgakglnlaasdvstlyrlllkayregrgellerysaiclrriwkaer
fswwmtsvlhrfpdtdafsqriqqteleyylgseaglatiaenyvglpyeeie
>d1doc_2 4.14.1.2.2 (174-275) p-Hydroxybenzoate hydroxylase, PHBH {Pseudomonas aeruginosa}
lkvfervypfgwlglladtppvsheliyanhprgfalcsqrsatrsryyvqvplsekved
wsderfwtelkarlpsevaeklvtgpsleksiaplrsfvvep
>d1dod_1 3.3.1.2.4 (1-173,276-394) p-Hydroxybenzoate hydroxylase (PHBH) {Pseudomonas aeruginosa}
mktqvaiigagpsglllgqllhkagidnvilerqtpdyvlgriragvleqgmvdllreag
vdrrmardglvhegveiafagqrrridlkrlsggktvtvygqtevtrdlmeareacgatt
vyqaaevrlhdlqgerpyvtferdgerlrldcdyiagcdgfhgisrqsipaerXmqhgrl
flagdaahivpptgakglnlaasdvstlyrlllkayregrgellerysaiclrriwkaer
fswwmtsvlhrfpdtdafsqriqqteleyylgseaglatiaenyvglpyeeie
>d1dod_2 4.14.1.2.2 (174-275) p-Hydroxybenzoate hydroxylase, PHBH {Pseudomonas aeruginosa}
lkvfervypfgwlglladtppvsheliyanhprgfalcsqrsatrsryyvqvplsekved
wsderfwtelkarlpsevaeklvtgpsleksiaplrsfvvep
>d1doe_1 3.3.1.2.4 (1-173,276-394) p-Hydroxybenzoate hydroxylase (PHBH) {Pseudomonas aeruginosa}
mktqvaiigagpsglllgqllhkagidnvilerqtpdyvlgriragvleqgmvdllreag
vdrrmardglvhegveiafagqrrridlkrlsggktvtvygqtevtrdlmeareacgatt
vyqaaevrlhdlqgerpyvtferdgerlrldcdyiagcdgfhgisrqsipaerXmqhgrl
flagdaahivpptgakglnlaasdvstlyrlllkayregrgellerysaiclrriwkaer
fswwmtsvlhrfpdtdafsqriqqteleyylgseaglatiaenyvglpyeeie
>d1doe_2 4.14.1.2.2 (174-275) p-Hydroxybenzoate hydroxylase, PHBH {Pseudomonas aeruginosa}
lkvfervypfgwlglladtppvsheliyanhprgfalcsqrsatrsryyvqvplsekved
wsderfwtelkarlpsevaeklvtgpsleksiaplrsfvvep
>d1dog__ 1.98.1.1.1 Glucoamylase {Aspergillus awamori, variant x100}
atldswlsneatvartailnnigadgawvsgadsgivvaspstdnpdyfytwtrdsglvi
ktlvdlfrngdtdllstiehyissqaiiqgvsnpsgdlssgglgepkfnvdetaytgswg
rpqrdgpalratamigfgqwlldngytsaateivwplvrndlsyvaqywnqtgydlweev
ngssfftiavqhralvegsafatavgsscswcdsqapqilcylqsfwtgsyilanfdssr
sgkdtntllgsihtfdpeagcddstfqpcspralanhkevvdsfrsiytlndglsdseav
avgrypedsyyngnpwflctlaaaeqlydalyqwdkqgsleitdvsldffkalysgaatg
tyssssstyssivsavktfadgfvsivethaasngslseqfdksdgdelsardltwsyaa
lltannrrnsvvppswgetsassvpgtcaatsasgtyssvtvtswpsiva
>d1doi__ 4.13.6.1.8 2Fe-2S ferredoxin {Haloarcula marismortui}
ptveylnyevvddngwdmydddvfgeasdmdlddedygslevnegeyileaaeaqgydwp
fscragacancaaivlegdidmdmqqilsdeevedknvrltcigspdadevkivynakhl
dylqnrvi
>d1doka_ 4.8.1.1.10 Monocyte chemoattractant protein-1 (MCP-1, MCAF) {Human (Homo sapiens)}
mqpdainapvtccynftnrkisvqrlasyrritsskcpkeavifktivakeicadpkqkw
vqdsmdhldkqt
>d1dokb_ 4.8.1.1.10 Monocyte chemoattractant protein-1 (MCP-1, MCAF) {Human (Homo sapiens)}
mqpdainapvtccynftnrkisvqrlasyrritsskcpkeavifktivakeicadpkqkw
vqdsmdhldkqt
>d1dol__ 4.8.1.1.10 Monocyte chemoattractant protein-1 (MCP-1, MCAF) {Human (Homo sapiens)}
mqpdainapvtccynftnrkisvqrlasyrritsskcpkeavifktivakeicadpkqkw
vqdsmdhldkq
>d1doma_ 4.8.1.1.10 Monocyte chemoattractant protein-1 (MCP-1, MCAF) {Human (Homo sapiens)}
qpdainapvtccynftnrkisvqrlasyrritsskcpkeavifktivakeicadpkqkwv
qdsmdhldkqtqtpkt
>d1domb_ 4.8.1.1.10 Monocyte chemoattractant protein-1 (MCP-1, MCAF) {Human (Homo sapiens)}
qpdainapvtccynftnrkisvqrlasyrritsskcpkeavifktivakeicadpkqkwv
qdsmdhldkqtqtpkt
>d1dona_ 4.8.1.1.10 Monocyte chemoattractant protein-1 (MCP-1, MCAF) {Human (Homo sapiens)}
qpdainapvtccynftnrkisvqrlasyrritsskcpkeavifktivakeicadpkqkwv
qdsmdhldkqtqtpkt
>d1donb_ 4.8.1.1.10 Monocyte chemoattractant protein-1 (MCP-1, MCAF) {Human (Homo sapiens)}
qpdainapvtccynftnrkisvqrlasyrritsskcpkeavifktivakeicadpkqkwv
qdsmdhldkqtqtpkt
>d1dora_ 3.1.4.1.1 Dihydroorotate dehydrogenase A {Lactococcus lactis}
mlnttfanakfanpfmnasgvhcmtiedleelkasqagayitksstlekregnplpryvd
lelgsinsmglpnlgfdyyldyvlknqkenaqegpiffsiagmsaaeniamlkkiqesdf
sgitelnlscpnvpgkpqlaydfeatekllkevftfftkplgvklppyfdlvhfdimaei
lnqfpltyvnsvnsignglfidpeaesvvikpkdgfggiggayikptalanvrafytrlk
peiqiigtggietgqdafehllcgatmlqigtalhkegpaifdriikeleeimnqkgyqs
iadfhgklksl
>d1dorb_ 3.1.4.1.1 Dihydroorotate dehydrogenase A {Lactococcus lactis}
mlnttfanakfanpfmnasgvhcmtiedleelkasqagayitksstlekregnplpryvd
lelgsinsmglpnlgfdyyldyvlknqkenaqegpiffsiagmsaaeniamlkkiqesdf
sgitelnlscpnvpgkpqlaydfeatekllkevftfftkplgvklppyfdlvhfdimaei
lnqfpltyvnsvnsignglfidpeaesvvikpkdgfggiggayikptalanvrafytrlk
peiqiigtggietgqdafehllcgatmlqigtalhkegpaifdriikeleeimnqkgyqs
iadfhgklksl
>d1dosa_ 3.1.9.2.1 Fructose-bisphosphate aldolase {Escherichia coli}
skifdfvkpgvitgddvqkvfqvakennfalpavncvgtdsinavletaakvkapvivqf
snggasfiagkgvksdvpqgaailgaisgahhvhqmaehygvpvilhtdhcakkllpwid
glldagekhfaatgkplfsshmidlseeslqenieicskylermskigmtleielgctgg
eedgvdnshmdasalytqpedvdyaytelskisprftiaasfgnvhgvykagnvvltpti
lrdsqeyvskkhnlphnslnfvfhggsgstaqeikdsvsygvvkmnidtdtqwatwegvl
nyykaneaylqgqlgnpkgedqpnkkyydprvwlragqtsmiarlekafqelnaidvl
>d1dosb_ 3.1.9.2.1 Fructose-bisphosphate aldolase {Escherichia coli}
skifdfvkpgvitgddvqkvfqvakennfalpavncvgtdsinavletaakvkapvivqf
snggasfiagkgvksdvpqgaailgaisgahhvhqmaehygvpvilhtdhcakkllpwid
glldagekhfaatgkplfsshmidlseeslqenieicskylermskigmtleielgctgg
eedgvdnshmdasalytqpedvdyaytelskisprftiaasfgnvhgvykagnvvltpti
lrdsqeyvskkhnlphnslnfvfhggsgstaqeikdsvsygvvkmnidtdtqwatwegvl
nyykaneaylqgqlgnpkgedqpnkkyydprvwlragqtsmiarlekafqelnaidvl
>d1dot_1 3.84.1.2.5 (1-334) Ovotransferrin {Duck (Anas platyrhynchos)}
appkttvrwctissaeekkcnslkdhmqqervtlscvqkatyldcikaisnneadaisld
ggqvfeaglapyklkpiaaevyersggsttsyyavavvkkgtdfmikdlrgktschtglg
rsagwnipigtlihrediewegiesgiseqavakffsascvpgatieqklcrqckgdakt
kclrngpysgysgafqclkdgkgdvafvkhttvqenapeekdeyellcldgsrqpvdsyk
tcnwarvaahavvarddskiddiwsflgmqayslgvdttsdfhlfgppgkkdpvlkdllf
kdsaimlkrvpelmdsqlylgfeyysaiqslrkd
>d1dot_2 3.84.1.2.5 (335-686) Ovotransferrin {Duck (Anas platyrhynchos)}
qltvgprenkiqwcavgkdekskcdrwsvvsngevectilddnkdcivkitkgeadaisl
dggfvytagvcglvpvvgesyedetqcskdeeqpayyfavavvkkssaitwnnlqgkksc
htavgrtagwnipmglihnktgscdfddyfsegcapgsppnsrlcklcqgsgenllekcv
asshekyygytgalrclveqgdvafikhstvgenvsgsnkddwakgltrddfellctngk
raktmdyktchlakvpthavvarpekankirellegqeklfglhgtekerfmmfqsqtkd
llfkaltkclvklrqgitykeflgdeyyasvaslntcnpsdllqvctfledk
>d1dox__ 4.13.6.1.4 2Fe-2S ferredoxin {Synechocystis PCC 6803}
asytvklitpdgessiecsddtyildaaeeagldlpyscragacstcagkitagsvdqsd
qsfldddqieagyvltcvayptsdctiethkeedly
>d1doy__ 4.13.6.1.4 2Fe-2S ferredoxin {Synechocystis PCC 6803}
asytvklitpdgessiecsddtyildaaeeagldlpyscragacstcagkitagsvdqsd
qsfldddqieagyvltcvayptsdctiethkeedly
>d1dpb__ 3.35.1.1.3 Dihydrolipoamide acetyltransferase {Azotobacter vinelandii}
ippippvdfakygeieevpmtrlmqigatnlhrswlnvphvtqfesaditeleafrvaqk
avaekagvkltvlplllkacayllkelpdfnsslapsgqalirkkyvhigfavdtpdgll
vpvirnvdqksllqlaaeaaelaekarskklgadamqgacftisslghiggtaftpivna
pevailgvskasmqpvwdgkafqprlmlplslsydcrvingaaaarftkrlgdlladira
ill
>d1dpc__ 3.35.1.1.3 Dihydrolipoamide acetyltransferase {Azotobacter vinelandii}
ippippvdfakygeieevpmtrlmqigatnlhrswlnvphvtqfesaditeleafrvaqk
avaekagvkltvlplllkacayllkelpdfnsslapsgqalirkkyvhigfavdtpdgll
vpvirnvdqksllqlaaeaaelaekarskklgadamqgacftisslghiggtaftpivna
pevailgvskasmqpvwdgkafqprlmlplslsydhrvidgaaaarftkrlgdlladira
ill
>d1dpd__ 3.35.1.1.3 Dihydrolipoamide acetyltransferase {Azotobacter vinelandii}
ippippvdfakygeieevpmtrlmqigatnlhrswlnvphvtqfesaditeleafrvaqk
avaekagvkltvlplllkacayllkelpdfnsslapsgqalirkkyvhigfavdtpdgll
vpvirnvdqksllqlaaeaaelaekarskklgadamqgacftiaslghiggtaftpivna
pevailgvskasmqpvwdgkafqprlmlplslsydhrvingaaaarftkrlgdlladira
ill
>d1dpe__ 3.84.1.1.9 Dipeptide-binding protein {Escherichia coli}
ktlvycsegspegfnpqlfisgttydassvplynrlvefkigttevipglaekwevsedg
ktytfhlrkgvkwhdnkefkptrelnaddvvfsfdrqknaqnpyhkvsggsyeyfegmgl
pelisevkkvddntvqfvltrpeapfladlamdfasilskeyadammkagtpekldlnpi
gtgpfqlqqyqkdsrirykafdgywgtkpqidtlvfsitpdasvryaklqknecqvmpyp
npadiarmkqdksinlmempglnvgylsynvqkkplddvkvrqaltyavnkdaiikavyq
gagvsaknlipptmwgynddvqdytydpekakallkeaglekgfsidlwampvqrpynpn
arrmaemiqadwakvgvqakivtyewgeylkrakdgehqtvmmgwtgdngdpdnffatef
scaaseqgsnyskwcykpfedliqparatddhnkrvelykqaqvvmhdqapaliiahstv
fepvrkevkgyvvdplgkhhfenvsie
>d1dpga1 3.2.1.3.15 (1-181,413-426) Glucose 6-phosphate dehydrogenase, N-terminal domain {Leuconostoc mesenteroides}
vseiktlvtffggtgdlakrklypsvfnlykkgylqkhfaivgtarqalnddefkqlvrd
cikdftddqaqaeafiehfsyrahdvtdaasyavlkeaieeaadkfdidgnrifymsvap
rffgtiakylkseglladtgynrlmiekpfgtsydtaaelqndlenafddnqlfridhyl
gXepyermihdtmngd
>d1dpga2 4.61.1.3.2 (182-412,427-485) Glucose 6-phosphate dehydrogenase {Leuconostoc mesenteroides}
kemvqniaalrfgnpifdaawnkdyiknvqvtlsevlgveeragyydtagalldmiqnht
mqivgwlamekpesftdkdiraaknaafnalkiydeaevnkyfvraqygagdsadfkpyl
eeldvpadsknntfiagelqfdlprwegvpfyvrsgkrlaakqtrvdivfkagtfnfgse
qeaqeavlsiiidpkgaielklnaksvedafntrtidlgwtvsdedkkntpXgsnfadwn
gvsiawkfvdaisavytadkapletyksgsmgpeasdkllaangdawvfkg
>d1dpgb1 3.2.1.3.15 (1-181,413-426) Glucose 6-phosphate dehydrogenase, N-terminal domain {Leuconostoc mesenteroides}
vseiktlvtffggtgdlakrklypsvfnlykkgylqkhfaivgtarqalnddefkqlvrd
cikdftddqaqaeafiehfsyrahdvtdaasyavlkeaieeaadkfdidgnrifymsvap
rffgtiakylkseglladtgynrlmiekpfgtsydtaaelqndlenafddnqlfridhyl
gXepyermihdtmngd
>d1dpgb2 4.61.1.3.2 (182-412,427-485) Glucose 6-phosphate dehydrogenase {Leuconostoc mesenteroides}
kemvqniaalrfgnpifdaawnkdyiknvqvtlsevlgveeragyydtagalldmiqnht
mqivgwlamekpesftdkdiraaknaafnalkiydeaevnkyfvraqygagdsadfkpyl
eeldvpadsknntfiagelqfdlprwegvpfyvrsgkrlaakqtrvdivfkagtfnfgse
qeaqeavlsiiidpkgaielklnaksvedafntrtidlgwtvsdedkkntpXgsnfadwn
gvsiawkfvdaisavytadkapletyksgsmgpeasdkllaangdawvfkg
>e1dph.1a 7.1.1.1.1 Insulin {Bovine (Bos taurus)}
giveqccasvcslyqlenycn
>e1dph.1b 7.1.1.1.1 Insulin {Bovine (Bos taurus)}
fvnqhlcgshlvealylvcgergffytpka
>d1dpi_1 3.46.3.5.1 (326-518) Exonuclease domain of DNA polymerase {Escherichia coli}
sydnyvtildeetlkawiaklekapvfafdtetdsldnisanlvglsfaiepgvaayipv
ahdyldapdqisreralellkplledekalkvgqnlkydrgilanygielrgiafdtmle
syilnsvagrhdmdslaerwlkhktitfeeiagkgknqltfnqialeeagryaaedadvt
lqlhlkmwpdlqk
>d1dpi_2 5.8.1.1.1 (519-928) DNA polymerase I (Klenow fragment) {Escherichia coli}
hkgplnvfeniemplvpvlsrierngvkidpkvlhnhseeltlrlaelekkaheiageef
nlsstkqlqtilfekqgikplkktpggapstseevleelaldyplpkvileyrglaklks
tytdklplminpktgrvhtsyhqavtatgrlsstdpnlqnipvrneegrrirqafiaped
yvivsadysqielrimahlsrdkglltafaegkdihrataaevfglpletvtseqrrsak
ainfgliygmsafglarqlniprkeaqkymdlyferypgvleymertraqakeqgyvetl
dgrrlylpdikssngarraaaeraainapmqgtaadiikramiavdawlqaeqprvrmim
qvhdelvfevhkddvdavakqihqlmenctrldvpllvevgsgenwdqah
>d1dpma_ 3.1.8.3.1 Phosphotriesterase {Pseudomonas diminuta}
arintvrgpitiseagftlthehicgssagflrawpeffgsrkalaekavrglrraraag
vrtivdvstfdigrdvsllaevsraadvhivaatglwfdpplsmrlrsveeltqfflrei
qygiedtgiragiikvattgkatpfqelvlkaaaraslatgvpvtthtaasqrdgeqqaa
ifeseglspsrvcighsddtddlsyltalaargyligldhiphsaiglednasasallgi
rswqtrallikalidqgymkqilvsndwlfgfssyvtnimdvmdrvnpdgmafiplrvip
flrekgvpqetlagitvtnparflsptlr
>d1dpmb_ 3.1.8.3.1 Phosphotriesterase {Pseudomonas diminuta}
arintvrgpitiseagftlthehicgssagflrawpeffgsrkalaekavrglrraraag
vrtivdvstfdigrdvsllaevsraadvhivaatglwfdpplsmrlrsveeltqfflrei
qygiedtgiragiikvattgkatpfqelvlkaaaraslatgvpvtthtaasqrdgeqqaa
ifeseglspsrvcighsddtddlsyltalaargyligldhiphsaiglednasasallgi
rswqtrallikalidqgymkqilvsndwlfgfssyvtnimdvmdrvnpdgmafiplrvip
flrekgvpqetlagitvtnparflsptlr
>d1dpo__ 2.41.1.2.3 Trypsin(ogen) {Rat (Rattus rattus)}
ivggytcqensvpyqvslnsgyhfcggslindqwvvsaahcyksriqvrlgehninvleg
neqfvnaakiikhpnfdrktlnndimliklsspvklnarvatvalpsscapagtqclisg
wgntlssgvnepdllqcldapllpqadceasypgkitdnmvcvgfleggkdscqgdcggp
vvcngelqgivswgygcalpdnpgvytkvcnyvdwiqdtiaan
>d1dppa_ 3.84.1.1.9 Dipeptide-binding protein {Escherichia coli}
ktlvycsegspegfnpqlftsgttydassvplynrlvefkigttevipglaekwevsedg
ktytfhlrkgvkwhdnkefkptrelnaddvvfsfdrqknaqnpyhkvsggsyeyfegmgl
pelisevkkvddntvqfvltrpeapfladlamdfasilskeyadammkagtpekldlnpi
gtgpfqlqqyqkdsrirykafdgywgtkpqidtlvfsitpdasvryaklqknecqvmpyp
npadiarmkqdksinlmempglnvgylsynvqkkplddvkvrqaltyavnkdaiikavyq
gagvsaknlipptmwgynddvqdytydpekakallkeaglekgfsidlwampvqrpynpn
arrmaemiqadwakvgvqakivtyewgeylkrakdgehqtvmmgwtgdngdpdnffatlf
scaaseqgsnyskwcykpfedliqparatddhnkrvelykqaqvvmhdqapaliiahstv
fepvrkevkgyvvdplgkhhfenvsie
>d1dppc_ 3.84.1.1.9 Dipeptide-binding protein {Escherichia coli}
ktlvycsegspegfnpqlftsgttydassvplynrlvefkigttevipglaekwevsedg
ktytfhlrkgvkwhdnkefkptrelnaddvvfsfdrqknaqnpyhkvsggsyeyfegmgl
pelisevkkvddntvqfvltrpeapfladlamdfasilskeyadammkagtpekldlnpi
gtgpfqlqqyqkdsrirykafdgywgtkpqidtlvfsitpdasvryaklqknecqvmpyp
npadiarmkqdksinlmempglnvgylsynvqkkplddvkvrqaltyavnkdaiikavyq
gagvsaknlipptmwgynddvqdytydpekakallkeaglekgfsidlwampvqrpynpn
arrmaemiqadwakvgvqakivtyewgeylkrakdgehqtvmmgwtgdngdpdnffatlf
scaaseqgsnyskwcykpfedliqparatddhnkrvelykqaqvvmhdqapaliiahstv
fepvrkevkgyvvdplgkhhfenvsie
>d1dppe_ 3.84.1.1.9 Dipeptide-binding protein {Escherichia coli}
ktlvycsegspegfnpqlftsgttydassvplynrlvefkigttevipglaekwevsedg
ktytfhlrkgvkwhdnkefkptrelnaddvvfsfdrqknaqnpyhkvsggsyeyfegmgl
pelisevkkvddntvqfvltrpeapfladlamdfasilskeyadammkagtpekldlnpi
gtgpfqlqqyqkdsrirykafdgywgtkpqidtlvfsitpdasvryaklqknecqvmpyp
npadiarmkqdksinlmempglnvgylsynvqkkplddvkvrqaltyavnkdaiikavyq
gagvsaknlipptmwgynddvqdytydpekakallkeaglekgfsidlwampvqrpynpn
arrmaemiqadwakvgvqakivtyewgeylkrakdgehqtvmmgwtgdngdpdnffatlf
scaaseqgsnyskwcykpfedliqparatddhnkrvelykqaqvvmhdqapaliiahstv
fepvrkevkgyvvdplgkhhfenvsie
>d1dppg_ 3.84.1.1.9 Dipeptide-binding protein {Escherichia coli}
ktlvycsegspegfnpqlftsgttydassvplynrlvefkigttevipglaekwevsedg
ktytfhlrkgvkwhdnkefkptrelnaddvvfsfdrqknaqnpyhkvsggsyeyfegmgl
pelisevkkvddntvqfvltrpeapfladlamdfasilskeyadammkagtpekldlnpi
gtgpfqlqqyqkdsrirykafdgywgtkpqidtlvfsitpdasvryaklqknecqvmpyp
npadiarmkqdksinlmempglnvgylsynvqkkplddvkvrqaltyavnkdaiikavyq
gagvsaknlipptmwgynddvqdytydpekakallkeaglekgfsidlwampvqrpynpn
arrmaemiqadwakvgvqakivtyewgeylkrakdgehqtvmmgwtgdngdpdnffatlf
scaaseqgsnyskwcykpfedliqparatddhnkrvelykqaqvvmhdqapaliiahstv
fepvrkevkgyvvdplgkhhfenvsie
>d1dpra1 1.4.3.19.1 (3-64) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
dlvdttemylrtiyeleeegvtplrariaerleqsgptvsqtvarmerdglvvvasdrsl
qm
>d1dpra2 1.75.1.1.1 (65-136) Diphtheria toxin repressor (DtxR) dimerization domain {Corynebacterium diphtheriae}
tptgrtlatavmrkhrlaerlltdiigldinkvhdeacrwehvmsdeverrlvkvlkdvs
rspfgnpipgld
>d1dprb1 1.4.3.19.1 (3-64) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
dlvdttemylrtiyeleeegvtplrariaerleqsgptvsqtvarmerdglvvvasdrsl
qm
>d1dprb2 1.75.1.1.1 (65-136) Diphtheria toxin repressor (DtxR) dimerization domain {Corynebacterium diphtheriae}
tptgrtlatavmrkhrlaerlltdiigldinkvhdeacrwehvmsdeverrlvkvlkdvs
rspfgnpipgld
>d1dpsa_ 1.26.1.1.3 DPS {Escherichia coli}
skatnllytrndvsdsekkatvellnrqviqfidlslitkqahwnmrganfiavhemldg
frtalidhldtmaeravqlggvalgttqvinsktplksypldihnvqdhlkeladryaiv
andvrkaigeakdddtadiltaasrdldkflwfiecnie
>d1dpsb_ 1.26.1.1.3 DPS {Escherichia coli}
llytrndvsdsekkatvellnrqviqfidlslitkqahwnmrganfiavhemldgfrtal
idhldtmaeravqlggvalgttqvinsktplksypldihnvqdhlkeladryaivandvr
kaigeakdddtadiltaasrdldkflwfiecnie
>d1dpsc_ 1.26.1.1.3 DPS {Escherichia coli}
llytrndvsdsekkatvellnrqviqfidlslitkqahwnmrganfiavhemldgfrtal
idhldtmaeravqlggvalgttqvinsktplksypldihnvqdhlkeladryaivandvr
kaigeakdddtadiltaasrdldkflwfiecnie
>d1dpsd_ 1.26.1.1.3 DPS {Escherichia coli}
tnllytrndvsdsekkatvellnrqviqfidlslitkqahwnmrganfiavhemldgfrt
alidhldtmaeravqlggvalgttqvinsktplksypldihnvqdhlkeladryaivand
vrkaigeakdddtadiltaasrdldkflwfiecnie
>d1dpse_ 1.26.1.1.3 DPS {Escherichia coli}
llytrndvsdsekkatvellnrqviqfidlslitkqahwnmrganfiavhemldgfrtal
idhldtmaeravqlggvalgttqvinsktplksypldihnvqdhlkeladryaivandvr
kaigeakdddtadiltaasrdldkflwfiecnie
>d1dpsf_ 1.26.1.1.3 DPS {Escherichia coli}
llytrndvsdsekkatvellnrqviqfidlslitkqahwnmrganfiavhemldgfrtal
idhldtmaeravqlggvalgttqvinsktplksypldihnvqdhlkeladryaivandvr
kaigeakdddtadiltaasrdldkflwfiecnie
>d1dpsg_ 1.26.1.1.3 DPS {Escherichia coli}
llytrndvsdsekkatvellnrqviqfidlslitkqahwnmrganfiavhemldgfrtal
idhldtmaeravqlggvalgttqvinsktplksypldihnvqdhlkeladryaivandvr
kaigeakdddtadiltaasrdldkflwfiecnie
>d1dpsh_ 1.26.1.1.3 DPS {Escherichia coli}
llytrndvsdsekkatvellnrqviqfidlslitkqahwnmrganfiavhemldgfrtal
idhldtmaeravqlggvalgttqvinsktplksypldihnvqdhlkeladryaivandvr
kaigeakdddtadiltaasrdldkflwfiecnie
>d1dpsi_ 1.26.1.1.3 DPS {Escherichia coli}
llytrndvsdsekkatvellnrqviqfidlslitkqahwnmrganfiavhemldgfrtal
idhldtmaeravqlggvalgttqvinsktplksypldihnvqdhlkeladryaivandvr
kaigeakdddtadiltaasrdldkflwfiecnie
>d1dpsj_ 1.26.1.1.3 DPS {Escherichia coli}
llytrndvsdsekkatvellnrqviqfidlslitkqahwnmrganfiavhemldgfrtal
idhldtmaeravqlggvalgttqvinsktplksypldihnvqdhlkeladryaivandvr
kaigeakdddtadiltaasrdldkflwfiecnie
>d1dpsk_ 1.26.1.1.3 DPS {Escherichia coli}
llytrndvsdsekkatvellnrqviqfidlslitkqahwnmrganfiavhemldgfrtal
idhldtmaeravqlggvalgttqvinsktplksypldihnvqdhlkeladryaivandvr
kaigeakdddtadiltaasrdldkflwfiecnie
>d1dpsl_ 1.26.1.1.3 DPS {Escherichia coli}
llytrndvsdsekkatvellnrqviqfidlslitkqahwnmrganfiavhemldgfrtal
idhldtmaeravqlggvalgttqvinsktplksypldihnvqdhlkeladryaivandvr
kaigeakdddtadiltaasrdldkflwfiecnie
>d1dpta_ 4.60.1.3.4 D-dopachrome tautomerase {Human (Homo sapiens)}
pfleldtnlpanrvpaglekrlcaaaasilgkpadrvnvtvrpglamalsgstepcaqls
issigvvgtaednrshsahffefltkelalgqdrilirffpleswqigkigtvmtfl
>d1dptb_ 4.60.1.3.4 D-dopachrome tautomerase {Human (Homo sapiens)}
pfleldtnlpanrvpaglekrlcaaaasilgkpadrvnvtvrpglamalsgstepcaqls
issigvvgtaednrshsahffefltkelalgqdrilirffpleswqigkigtvmtfl
>d1dptc_ 4.60.1.3.4 D-dopachrome tautomerase {Human (Homo sapiens)}
pfleldtnlpanrvpaglekrlcaaaasilgkpadrvnvtvrpglamalsgstepcaqls
issigvvgtaednrshsahffefltkelalgqdrilirffpleswqigkigtvmtfl
>d1dqsa_ 5.18.1.1.1 Dehydroquinate synthase, DHQS {Aspergillus nidulans (Emericella nidulans)}
ptkisilgresiiadfglwrnyvakdlisdcssttyvlvtdtnigsiytpsfeeafrkra
aeitpsprlliynrppgevsksrqtkadiedwmlsqnppcgrdtvvialgggvigdltgf
vastymrgvryvqvpttllamvdssiggktaidtplgknligaiwqptkiyidlefletl
pvrefingmaeviktaaisseeeftaleenaetilkavrrevtpgehrfegteeilkari
lasarhkayvvsaderegglrnllnwghsighaieailtpqilhgecvaigmvkeaelar
hlgilkgvavsrivkclaayglptslkdarirkltagkhcsvdqlmfnmaldkkndgpkk
kivllsaigtpyetrasvvanedirvvl
>d1dqsb_ 5.18.1.1.1 Dehydroquinate synthase, DHQS {Aspergillus nidulans (Emericella nidulans)}
nptkisilgresiiadfglwrnyvakdlisdcssttyvlvtdtnigsiytpsfeeafrkr
aaeitpsprlliynrppgevsksrqtkadiedwmlsqnppcgrdtvvialgggvigdltg
fvastymrgvryvqvpttllamvdssiggktaidtplgknligaiwqptkiyidleflet
lpvrefingmaeviktaaisseeeftaleenaetilkavrrevtpgehrfegteeilkar
ilasarhkayvvsaderegglrnllnwghsighaieailtpqilhgecvaigmvkeaela
rhlgilkgvavsrivkclaayglptslkdarirkltagkhcsvdqlmfnmaldkkndgpk
kkivllsaigtpyetrasvvanedirvvlap
>d1dr1__ 3.61.1.1.4 Dihydrofolate reductases, eukaryotic type {Chicken (Gallus gallus)}
vrslnsivavcqnmgigkdgnlpwpplrneykyfqrmtstshvegkqnavimgkktwfsi
peknrplkdrinivlsrelkeapkgahylskslddalalldspelkskvdmvwivggtav
ykaamekpinhrlfvtrilhefesdtffpeidykdfkllteypgvpadiqeedgiqykfe
vyqksv
>d1dr2__ 3.61.1.1.4 Dihydrofolate reductases, eukaryotic type {Chicken (Gallus gallus)}
vrslnsivavcqnmgigkdgnlpwpplrneykyfqrmtstshvegkqnavimgkktwfsi
peknrplkdrinivlsrelkeapkgahylskslddalalldspelkskvdmvwivggtav
ykaamekpinhrlfvtrilhefesdtffpeidykdfkllteypgvpadiqeedgiqykfe
vyqksv
>d1dr3__ 3.61.1.1.4 Dihydrofolate reductases, eukaryotic type {Chicken (Gallus gallus)}
vrslnsivavcqnmgigkdgnlpwpplrneykyfqrmtstshvegkqnavimgkktwfsi
peknrplkdrinivlsrelkeapkgahylskslddalalldspelkskvdmvwivggtav
ykaamekpinhrlfvtrilhefesdtffpeidykdfkllteypgvpadiqeedgiqykfe
vyqksv
>d1dr4__ 3.61.1.1.4 Dihydrofolate reductases, eukaryotic type {Chicken (Gallus gallus)}
vrslnsivavcqnmgigkdgnlpwpplrneykyfqrmtstshvegkqnavimgkktwfsi
peknrplkdrinivlsrelkeapkgahylskslddalalldspelkskvdmvwivggtav
ykaamekpinhrlfvtrilhefesdtffpeidykdfkllteypgvpadiqeedgiqykfe
vyqksv
>d1dr5__ 3.61.1.1.4 Dihydrofolate reductases, eukaryotic type {Chicken (Gallus gallus)}
vrslnsivavcqnmgigkdgnlpwpplrneykyfqrmtstshvegkqnavimgkktwfsi
peknrplkdrinivlsrelkeapkgahylskslddalalldspelkskvdmvwivggtav
ykaamekpinhrlfvtrilhefesdtffpeidykdfkllteypgvpadiqeedgiqykfe
vyqksv
>d1dr6__ 3.61.1.1.4 Dihydrofolate reductases, eukaryotic type {Chicken (Gallus gallus)}
vrslnsivavcqnmgigkdgnlpwpplrneykyfqrmtstshvegkqnavimgkktwfsi
peknrplkdrinivlsrelkeapkgahylskslddalalldspelkskvdmvwivggtav
ykaamekpinhrlfvtrilhefesdtffpeidykdfkllteypgvpadiqeedgiqykfe
vyqksv
>d1dr7__ 3.61.1.1.4 Dihydrofolate reductases, eukaryotic type {Chicken (Gallus gallus)}
vrslnsivavcqnmgigkdgnlpwpplrneykyfqrmtstshvegkqnavimgkktwfsi
peknrplkdrinivlsrelkeapkgahylskslddalalldspelkskvdmvwivggtav
ykaamekpinhrlfvtrilhefesdtffpeidykdfkllteypgvpadiqeedgiqykfe
vyqksv
>d1draa_ 3.61.1.1.1 Dihydrofolate reductase, prokaryotic type {Escherichia coli}
misliaalavdrvigmenampwnlpaelawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1drab_ 3.61.1.1.1 Dihydrofolate reductase, prokaryotic type {Escherichia coli}
misliaalavdrvigmenampwnlpaelawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1drba_ 3.61.1.1.1 Dihydrofolate reductase, prokaryotic type {Escherichia coli}
misliaalavdrvigmenampwnlpaclawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1drbb_ 3.61.1.1.1 Dihydrofolate reductase, prokaryotic type {Escherichia coli}
misliaalavdrvigmenampwnlpaclawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1dre__ 3.61.1.1.1 Dihydrofolate reductase, prokaryotic type {Escherichia coli}
misliaalavdrvigmenampwnlpadlawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1drf__ 3.61.1.1.5 Dihydrofolate reductases, eukaryotic type {Human (Homo sapiens)}
vgslncivavsqnmgigkngdlpwpplrnefryfqrmtttssvegkqnlvimgkktwfsi
peknrplkgrinlvlsrelkeppqgahflsrslddalklteqpelankvdmvwivggssv
ykeamnhpghlklfvtrimqdfesdtffpeidlekykllpeypgvlsdvqeekgikykfe
vyeknd
>d1drh__ 3.61.1.1.1 Dihydrofolate reductase, prokaryotic type {Escherichia coli}
misliaalavdrvigmenampwnlpadlawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1drj__ 3.83.1.1.1 D-ribose-binding protein {Escherichia coli, strain k-12}
kdtialvvstlnnpffvslkdgaqkeadklgynlvvldsqnnpakelanvqdltvrgtki
llinptdsdavgnavkmanqanipvitldrqatkgevvshiasdnvlggkiagdyiakka
gegakvielqgiartsaarergegfqqavaahkfnvlasqpadfdrikglnvmqnlltah
pdvqavfaqndemalgalralqtagksdvmvvgfdgtpdgekavndgklaatiaqlpdqi
gakgvetadkvlkgekvqakypvdlklvvkq
>d1drk__ 3.83.1.1.1 D-ribose-binding protein {Escherichia coli, strain k-12}
kdtialvvstlnnpffvslkdgaqkeadklgynlvvldsqnnpakelanvqdltvrgtki
llinptdsdavgnavkmanqanipvitldrqatkgevvshiasdnvlggkiagdyiakka
gegakvielqgtaatsaarergegfqqavaahkfnvlasqpadfdrikglnvmqnlltah
pdvqavfaqndemalgalralqtagksdvmvvgfdgtpdgekavndgklaatiaqlpdqi
gakgvetadkvlkgekvqakypvdlklvvkq
>d1dro__ 2.49.1.1.3 beta-spectrin {Fruit fly (Drosophila melanogaster)}
gsgtgageghegyvtrkhewdsttkkasnrswdkvymaakagrisfykdqkgyksnpelt
frgepsydlqnaaieiasdytkkkhvlrvklangalfllqahddtemsqwvtslkaqsds
ta
>d1drs__ 7.7.1.2.1 Dendroaspin {Dendroaspis jamesoni kaimose}
ricynhlgtkppttetcqedscykniwtfdniirrgcgcftprgdmpgpyccesdkcnl
>d1dru_1 3.2.1.3.13 (4-130,241-273) Dihydrodipicolinate reductase {Escherichia coli}
anirvaiagaggrmgrqliqaalalegvqlgaaleregssllgsdagelagagktgvtvq
ssldavkddfdvfidftrpegtlnhlafcrqhgkgmvigttgfdeagkqairdaaadiai
vfaanfsXmtfangavrsalwlsgkesglfdmrdvldlnnl
>d1dru_2 4.61.1.2.2 (131-240) Dihydrodipicolinate reductase {Escherichia coli}
vgvnvmlkllekaakvmgdytdieiieahhrhkvdapsgtalamgeaiahaldkdlkdca
vysreghtgervpgtigfatvragdivgehtamfadigerleithkassr
>d1drv_1 3.2.1.3.13 (4-130,241-273) Dihydrodipicolinate reductase {Escherichia coli}
anirvaiagaggrmgrqliqaalalegvqlgaaleregssllgsdagelagagktgvtvq
ssldavkddfdvfidftrpegtlnhlafcrqhgkgmvigttgfdeagkqairdaaadiai
vfaanfsXmtfangavrsalwlsgkesglfdmrdvldlnnl
>d1drv_2 4.61.1.2.2 (131-240) Dihydrodipicolinate reductase {Escherichia coli}
vgvnvmlkllekaakvmgdytdieiieahhrhkvdapsgtalamgeaiahaldkdlkdca
vysreghtgervpgtigfatvragdivgehtamfadigerleithkassr
>d1drw_1 3.2.1.3.13 (2-130,241-273) Dihydrodipicolinate reductase {Escherichia coli}
hdanirvaiagaggrmgrqliqaalalegvqlgaaleregssllgsdagelagagktgvt
vqssldavkddfdvfidftrpegtlnhlafcrqhgkgmvigttgfdeagkqairdaaadi
aivfaanfsXmtfangavrsalwlsgkesglfdmrdvldlnnl
>d1drw_2 4.61.1.2.2 (131-240) Dihydrodipicolinate reductase {Escherichia coli}
vgvnvmlkllekaakvmgdytdieiieahhrhkvdapsgtalamgeaiahaldkdlkdca
vysreghtgervpgtigfatvragdivgehtamfadigerleithkassr
>d1drza_ 4.47.7.1.2 Splicesomal U1A protein {Human (Homo sapiens)}
petrpnhtiyinnlnekikkdelkkslhaifsrfgqildilvsrslkmrgqafvifkevs
satnalrsmqgfpfydkpmriqyaktdsdiiakmk
>d1dsba1 1.47.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1dsba2 3.38.1.4.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
aqyedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsek
>d1dsbb1 1.47.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1dsbb2 3.38.1.4.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
aqyedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsek
>d1dsfh_ 2.1.1.1.106 Immunoglobulin (variable domains of L and H chains) {Anticancer Fv B1}
qlvesggglvkpggslklscaasgfifsdnymywvrqtpekclewvatisdggtyidysd
svkgrftisrdnaknnlylqmsslrsedtgmyycgrspiyydyapftywgqgtlvtvsa
>d1dsfl_ 2.1.1.1.106 Immunoglobulin (variable domains of L and H chains) {Anticancer Fv B1}
dvvmtqtplslpvslgdqasiscrssqnlvhsdgktylhwflqkpgqsptlliykvsnrf
sgvpdrfsgsgsgtdfilkisrveaedlgvyfcsqsthvpltfgcgtklelk
>d1dsha_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltsky
>d1dshb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1dshc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltsky
>d1dshd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1dsl__ 2.10.1.1.1 gamma-Crystallin {Bovine (Bos taurus), isoform II (B)}
tfrmriyerddfrgqmseitddcpslqdrfhltevhslnvlegswvlyempsyrgrqyll
rpgeyrryldwgamnakvgslrrvmdfy
>d1dsn__ 3.84.1.2.1 Lactoferrin {Human (Homo sapiens)}
rrrsvqwcavsqpeatkcfqwqrnmrrvrgppvscikrdspiqciqaiaenradavtlsg
gfiyeaglapyklrpvaaevygterqprthyyavavvkkggsfqlnelqglkschtglrr
tagwnvpigtlrpflnwtgppepieaavarffsascvpgadkgqfpnlcrlcagtgenkc
afssqepyfsysgafkclrdgagdvafirestvfedlsdeaerdeyellcpdntrkpvdk
fkdchlarvpshavvarsvngkedaiwnllrqaqekfgkdkspkfqlfgspsgqkdllfk
dsaigfsrvpprids
>d1dssg1 3.2.1.3.9 (1-148,313-334) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Lobster (Palinurus versicolor)}
skigingfgrigrlvlraalemgaqvvavndpfialeymvymfkydsthgmfkgevkaed
galvvdgkkitvfnemkpenipwskagaeyivestgvfttiekasahfkggakkviisap
sadapmfvcgvnlekyskdmkvvsnasXnefgysqrvidlikhmqkvdsa
>d1dssg2 4.61.1.1.9 (150-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Lobster (Palinurus versicolor)}
ttnclapvakvlhenfeiveglmttvhavtatqktvdgpsakdwrggrgaaqniipsstg
aakavgkvipeldgkltgmafrvptpnvsvvdltvrlgkecsyddikaamkaasegplqg
vlgyteddvvscdftgdnrssifdakagiqlsktfvkvvswyd
>d1dssr1 3.2.1.3.9 (1-148,313-334) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Lobster (Palinurus versicolor)}
skigingfgrigrlvlraalemgaqvvavndpfialeymvymfkydsthgmfkgevkaed
galvvdgkkitvfnemkpenipwskagaeyivestgvfttiekasahfkggakkviisap
sadapmfvcgvnlekyskdmkvvsnasXnefgysqrvidlikhmqkvdsa
>d1dssr2 4.61.1.1.9 (150-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Lobster (Palinurus versicolor)}
ttnclapvakvlhenfeiveglmttvhavtatqktvdgpsakdwrggrgaaqniipsstg
aakavgkvipeldgkltgmafrvptpnvsvvdltvrlgkecsyddikaamkaasegplqg
vlgyteddvvscdftgdnrssifdakagiqlsktfvkvvswyd
>d1dst__ 2.41.1.2.27 Factor D {Human (Homo sapiens)}
ilggreaeaharpymasvqlngahlcggvlvaeqwvlsaahcledaadgkvqvllgahsl
sqpepskrlydvlravphpdyqpdtidhdllllqlsekatlgpavrplpwqrvdrdvapg
tlcdvagwgivnhagrrpdslqhvllpvldratcnrrthhdgaiterlmcaesnrrdsck
gdsggplvcggvlegvvswgsrvcgnrkkpgiytrvasyaawidsvla
>d1dsua_ 2.41.1.2.27 Factor D {Human (Homo sapiens)}
ilggreaeaharpymasvqlngahlcggvlvaeqwvlsaahcledaadgkvqvllgahsl
sqpepskrlydvlravphpdsqpdtidhdllllqlsekatlgpavrplpwqrvdrdvapg
tlcdvagwgivnhagrrpdslqhvllpvldratcnrrthhdgaiterlmcaesnrrdsck
gdsggplvcggvlegvvtsgsrvcgnrkkpgiytrvasyaawidsvla
>d1dsub_ 2.41.1.2.27 Factor D {Human (Homo sapiens)}
ilggreaeaharpymasvqlngahlcggvlvaeqwvlsaahcledaadgkvqvllgahsl
sqpepskrlydvlravphpdsqpdtidhdllllqlsekatlgpavrplpwqrvdrdvapg
tlcdvagwgivnhagrrpdslqhvllpvldratcnrrthhdgaiterlmcaesnrrdsck
gdsggplvcggvlegvvtsgsrvcgnrkkpgiytrvasyaawidsvla
>d1dtha_ 4.71.1.7.2 Snake venom metalloprotease {Western diamonback rattlesnake (Crotalus atrox), atrolysin C}
qnlpqryielvvvadhrvfmkynsdlntirtrvheivnfingfyrslnihvsltdleiws
nedqiniqsassdtlnafaewretdllnrkshdnaqlltaieldeetlglaplgtmcdpk
lsigivqdhspinllmgvtmahelghnlgmehdgkdclrgaslcimrpgltkgrsyefsd
dsmhyyerflkqykpqcilnkp
>d1dthb_ 4.71.1.7.2 Snake venom metalloprotease {Western diamonback rattlesnake (Crotalus atrox), atrolysin C}
qnlpqryielvvvadhrvfmkynsdlntirtrvheivnfingfyrslnihvsltdleiws
nedqiniqsassdtlnafaewretdllnrkshdnaqlltaieldeetlglaplgtmcdpk
lsigivqdhspinllmgvtmahelghnlgmehdgkdclrgaslcimrpgltkgrsyefsd
dsmhyyerflkqykpqcilnkp
>d1dtk__ 7.8.1.1.9 Dendrotoxin K {Black mamba (Dendroaspis polylepis polylepis)}
aakycklplrigpckrkipsfyykwkakqclpfdysgcggnanrfktieecrrtcvg
>d1dtn_1 3.1.10.2.3 (133-359) Mandelate racemase {Pseudomonas putida}
pvqaydshsldgvklateravtaaelgfravktkigypaldqdlavvrsirqavgddfgi
mvdynqsldvpaaikrsqalqqegvtwieeptlqhdyeghqriqsklnvpvqmgenwlgp
eemfkalsigacrlampdamkiggvtgwirasalaqqfgipmsshlfqeisahllaatpt
ahwlqrldlagsvieptltfeggnavipdlpgvgiiwrekeigkylv
>d1dtn_2 4.44.1.1.5 (3-132) Mandelate racemase {Pseudomonas putida}
evlitglrtravnvplaypvhtavgtvgtaplvlidlatsagvvghsylfaytpvalksl
kqllddmaamivneplapvsleamlakrfclagytglirmaaagidmaawdalgkvhetp
lvkllganar
>d1dtp__ 4.136.1.1.3 Diphtheria toxin, N-terminal domain {Corynebacterium diphtheriae}
gaddvvdssksfvmenfssyhgtkpgyvdsiqkgiqkpksgtqgnydddwkgfystdnky
daagysvdnenplsgkaggvvkvtypgltkvlalkvdnaetikkelglslteplmeqvgt
eefikrfgdgasrvvlslpfaegsssveyinnweqakalsveleinfetrgkrgqdamye
ymaqacagnr
>d1dts__ 3.30.1.8.1 Dethiobiotin synthetase {Escherichia coli}
skryfvtgtdtevgktvascallqaakaagyrtagykpvasgsektpeglrnsdalalqr
nsslqldyatvnpytfaeptsphiisaqegrpieslvmsaglraleqqadwvlvegaggw
ftplsdtftfadwvtqeqlpvilvvgvklgcinhamltaqviqhagltlagwvandvtpp
gkrhaeymttltrmipapllgeipwlaeaatgkyinlall
>d1dtx__ 7.8.1.1.6 alpha-Dendrotoxin {Green mamba (Dendroaspis angusticeps)}
xprrklcilhrnpgrcydkipafyynqkkkqcerfdwsgcggnsnrfktieecrrtcig
>d1duba_ 3.11.1.2.2 Enoyl-CoA hydratase {Rat (Rattus norvegicus)}
anfqyiitekkgknssvgliqlnrpkalnalcnglieelnqaletfeedpavgaivltgg
ekafaagadikemqnrtfqdcysgkflshwdhitrikkpviaavngyalgggcelammcd
iiyagekaqfgqpeillgtipgaggtqrltravgkslamemvltgdrisaqdakqaglvs
kifpvetlveeaiqcaekiannskiivamakesvnaafemtltegnklekklfystfatd
drregmsafvekrkanfkdh
>d1dubb_ 3.11.1.2.2 Enoyl-CoA hydratase {Rat (Rattus norvegicus)}
nfqyiitekkgknssvgliqlnrpkalnalcnglieelnqaletfeedpavgaivltgge
kafaagadikemqnrtfqdcysgkflshwdhitrikkpviaavngyalgggcelammcdi
iyagekaqfgqpeillgtipgaggtqrltravgkslamemvltgdrisaqdakqaglvsk
ifpvetlveeaiqcaekiannskiivamakesvnaafemtltegnklekklfystfatdd
rregmsafvekrkanfkdh
>d1dubc_ 3.11.1.2.2 Enoyl-CoA hydratase {Rat (Rattus norvegicus)}
nfqyiitekkgknssvgliqlnrpkalnalcnglieelnqaletfeedpavgaivltgge
kafaagadikemqnrtfqdcysgkflshwdhitrikkpviaavngyalgggcelammcdi
iyagekaqfgqpeillgtipgaggtqrltravgkslamemvltgdrisaqdakqaglvsk
ifpvetlveeaiqcaekiannskiivamakesvnaafemtltegnklekklfystfatdd
rregmsafvekrkanfkdh
>d1dubd_ 3.11.1.2.2 Enoyl-CoA hydratase {Rat (Rattus norvegicus)}
anfqyiitekkgknssvgliqlnrpkalnalcnglieelnqaletfeedpavgaivltgg
ekafaagadikemqnrtfqdcysgkflshwdhitrikkpviaavngyalgggcelammcd
iiyagekaqfgqpeillgtipgaggtqrltravgkslamemvltgdrisaqdakqaglvs
kifpvetlveeaiqcaekiannskiivamakesvnaafemtltegnklekklfystfatd
drregmsafvekrkanfkdh
>d1dube_ 3.11.1.2.2 Enoyl-CoA hydratase {Rat (Rattus norvegicus)}
anfqyiitekkgknssvgliqlnrpkalnalcnglieelnqaletfeedpavgaivltgg
ekafaagadikemqnrtfqdcysgkflshwdhitrikkpviaavngyalgggcelammcd
iiyagekaqfgqpeillgtipgaggtqrltravgkslamemvltgdrisaqdakqaglvs
kifpvetlveeaiqcaekiannskiivamakesvnaafemtltegnklekklfystfatd
drregmsafvekrkanfkdh
>d1dubf_ 3.11.1.2.2 Enoyl-CoA hydratase {Rat (Rattus norvegicus)}
nfqyiitekkgknssvgliqlnrpkalnalcnglieelnqaletfeedpavgaivltgge
kafaagadikemqnrtfqdcysgkflshwdhitrikkpviaavngyalgggcelammcdi
iyagekaqfgqpeillgtipgaggtqrltravgkslamemvltgdrisaqdakqaglvsk
ifpvetlveeaiqcaekiannskiivamakesvnaafemtltegnklekklfystfatdd
rregmsafvekrkanfkdh
>d1duc__ 2.75.3.1.3 Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) {Equine infectious anemia virus, EIAV}
mlayqgtqikekrdedagfdlcvpydimipvsdtkiiptdvkiqvppnsfgwvtgkssma
kqgllinggiidegytgeiqvictnigksnikliegqkfaqliilqhhsnsrqpwden
>d1dud__ 2.75.3.1.1 Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) {Escherichia coli}
mmkkidvkildprvgkefplptyatsgsagldlraclndavelapgdttlvptglaihia
dpslaammlprsglghkhgivlgnlvglidsdyqgqlmisvwnrgqdsftiqpgeriaqm
ifvpvvqaefnlvedf
>d1dun__ 2.75.3.1.3 Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) {Equine infectious anemia virus, EIAV}
mlayqgtqikekrdedagfdlcvpydimipvsdtkiiptdvkiqvppnsfgwvtgkssma
kqgllinggiidegytgeiqvictnigksnikliegqkfaqliilqhhsnsrqpwdenki
>d1dupa_ 2.75.3.1.1 Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) {Escherichia coli}
mmkkidvkildprvgkefplptyatsgsagldlraclndavelapgdttlvptglaihia
dpslaammlprsglghkhgivlgnlvglidsdyqgqlmisvwnrgqdsftiqpgeriaqm
ifvpvvqaefnlvedf
>d1duta_ 2.75.3.1.2 Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) {Feline immunodeficiency virus, FIV}
miiegdgildkrsedagydllaakeihllpgevkviptgvklmlpkgywgliigkssigs
kgldvlggvidegyrgeigviminvsrksitlmerqkiaqliilpckhevleqgkvv
>d1dutb_ 2.75.3.1.2 Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) {Feline immunodeficiency virus, FIV}
miiegdgildkrsedagydllaakeihllpgevkviptgvklmlpkgywgliigkssigs
kgldvlggvidegyrgeigviminvsrksitlmerqkiaqliilpckhevleqgkvv
>d1dvc__ 4.15.1.2.2 Cystatin A (stefin A) {Human (Homo sapiens)}
mipgglseakpatpeiqeivdkvkpqleektnetygkleavqyktqvvagtnyyikvrag
dnkymhlkvfkslpgqnedlvltgyqvdknkddeltgf
>d1dvd__ 4.15.1.2.2 Cystatin A (stefin A) {Human (Homo sapiens)}
mipgglseakpatpeiqeivdkvkpqleektnetygkleavqyktqvvagtnyyikvrag
dnkymhlkvfkslpgqnedlvltgyqvdknkddeltgf
>d1dvfa_ 2.1.1.1.42 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
divltqspaslsasvgetvtitcrasgnihnylawyqqkqgkspqllvyytttladgvps
rfsgsgsgtqyslkinslqpedfgsyycqhfwstprtfgggtkleik
>d1dvfb_ 2.1.1.1.42 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
qvqlqesgpglvapsqslsitctvsgfsltgygvnwvrqppgkglewlgmiwgdgntdyn
salksrlsiskdnsksqvflkmnslhtddtaryycarerdyrldywgqgttltvss
>d1dvfc_ 2.1.1.1.74 Immunoglobulin (variable domains of L and H chains) {Fv E5.2 (mouse), kappa L chain}
diqltqspsslsaslgdrvtiscrasqdisnylnwyqqkpdgtvklliyytsrlhsgvps
rfsgsgsgtdysltisnleqediatyfcqqgntlpwtfgggtkleik
>d1dvfd_ 2.1.1.1.74 Immunoglobulin (variable domains of L and H chains) {Fv E5.2 (mouse), kappa L chain}
qvqlqqsgtelvksgasvklsctasgfnikdthmnwvkqrpeqglewigridpangniqy
dpkfrgkatitadtssntaylqlsltsedtavyycatkviyyqgrgamdywgqgttltvs
>d1dvh__ 1.3.1.1.2 Cytochrome c6 (synonym: cytochrome c553) {Desulfovibrio vulgaris, different strains}
adgaalykscigchgadgskaamgsakpvkgqgaeelykkmkgyadgsyggerkammtna
vkkysdeelkaladymskl
>d1dvia_ 1.42.1.7.2 Calpain domain VI {Rat (Rattus norvegicus)}
eeerqfrklfvqlagddmevsatelmnilnkvvtrhpdlktdgfgidtsrsmvavmdsdt
tgklgfeefkylwnnikkwqgiykrfdtdrsgtigsnelpgafeaagfhlnqhiysmiir
rysdetgnmdfdnfisclvrldamfrafrsldkngtgqiqvniqewlqltmys
>d1dvib_ 1.42.1.7.2 Calpain domain VI {Rat (Rattus norvegicus)}
eeerqfrklfvqlagddmevsatelmnilnkvvtrhpdlktdgfgidtsrsmvavmdsdt
tgklgfeefkylwnnikkwqgiykrfdtdrsgtigsnelpgafeaagfhlnqhiysmiir
rysdetgnmdfdnfisclvrldamfrafrsldkngtgqiqvniqewlqltmys
>d1dvra1 3.30.1.1.11 (1-130,169-220) Adenylate kinase {Baker's yeast (Saccharomyces cerevisiae)}
ssesirmvligppgagkgtqapnlqerfhaahlatgdmlrsqiakgtqlgleakkimdqg
glvsddimvnmikdeltnnpackngfilvgfprtipqaekldqmlkeqgtplekaielkv
ddellvaritXnadalkkrlaayhaqtepivdfykktgiwagvdasqppatvwadilnkl
gkn
>d1dvra2 7.35.2.1.5 (131-168) Microbial and mitochondrial ADK, insert "zinc finger" domain {Baker's yeast (Saccharomyces cerevisiae)}
grlihpasgrsyhkifnppkedmkddvtgealvqisdd
>d1dvrb1 3.30.1.1.11 (1-130,169-220) Adenylate kinase {Baker's yeast (Saccharomyces cerevisiae)}
ssesirmvligppgagkgtqapnlqerfhaahlatgdmlrsqiakgtqlgleakkimdqg
glvsddimvnmikdeltnnpackngfilvgfprtipqaekldqmlkeqgtplekaielkv
ddellvaritXnadalkkrlaayhaqtepivdfykktgiwagvdasqppatvwadilnkl
gkn
>d1dvrb2 7.35.2.1.5 (131-168) Microbial and mitochondrial ADK, insert "zinc finger" domain {Baker's yeast (Saccharomyces cerevisiae)}
grlihpasgrsyhkifnppkedmkddvtgealvqisdd
>e1dwb.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1dwb.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
eadcglrplfekksledkterellesyid
>e1dwc.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1dwc.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
eadcglrplfekksledkterellesyid
>e1dwd.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1dwd.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
eadcglrplfekksledkterellesyid
>e1dwe.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1dwe.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
eadcglrplfekksledkterellesyi
>d1dxga_ 7.35.4.2.1 Desulforedoxin {Desulfovibrio gigas}
anegdvykcelcgqvvkvleegggtlvccgedmvkq
>d1dxgb_ 7.35.4.2.1 Desulforedoxin {Desulfovibrio gigas}
anegdvykcelcgqvvkvleegggtlvccgedmvkq
>d1dxia_ 3.1.13.2.2 D-xylose isomerase {Streptomyces murinus}
msfqptpedrftfglwtvgwqgrdpfgdatrpaldpvetvqrlaelgaygvtfhdddlip
fgssdtereshikrfrqaldatgmtvpmattnlfthpvfkdggftandrdvrryalrkti
gnidlaaelgaktyvawggregaesggakdvrdaldrmkeafdllgeyvtaqgydlrfai
epkpneprgdillptvghalafierlerpelygvnpevgheqmaglnfphgiaqalwagk
lfhidlngqsgikydqdlrfgagdlraafwlvdlletagyegprhfdfkpprtedfdgvw
asaagcmrnylilkdraaafradpevqealraarldqlaqptaadgldalladraafedf
dvdaaaargmafehldqlamdhllgarg
>d1dxib_ 3.1.13.2.2 D-xylose isomerase {Streptomyces murinus}
msfqptpedrftfglwtvgwqgrdpfgdatrpaldpvetvqrlaelgaygvtfhdddlip
fgssdtereshikrfrqaldatgmtvpmattnlfthpvfkdggftandrdvrryalrkti
gnidlaaelgaktyvawggregaesggakdvrdaldrmkeafdllgeyvtaqgydlrfai
epkpneprgdillptvghalafierlerpelygvnpevgheqmaglnfphgiaqalwagk
lfhidlngqsgikydqdlrfgagdlraafwlvdlletagyegprhfdfkpprtedfdgvw
asaagcmrnylilkdraaafradpevqealraarldqlaqptaadgldalladraafedf
dvdaaaargmafehldqlamdhllgarg
>d1dxta_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1dxtb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mvhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpk
vkahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfg
keftppvqaayqkvvagvanalahkyh
>d1dxtc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1dxtd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mvhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpk
vkahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfg
keftppvqaayqkvvagvanalahkyh
>d1dxua_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1dxub_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1dxuc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1dxud_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1dxva_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1dxvb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
ahltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1dxvc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1dxvd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
ahltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1dxy_1 3.2.1.4.3 (101-330) D-2-hydroxyisocaproate dehydrogenase {Lactobacillus casei}
spaaiaefaltdtlyllrnmgkvqaqlqagdyekagtfigkelgqqtvgvmgtghigqva
iklfkgfgakviaydpypmkgdhpdfdyvsledlfkqsdvidlhvpgieqnthiineaaf
nlmkpgaivintarpnlidtqamlsnlksgklagvgidtyeyetedllnlakhgsfkdpl
wdellgmpnvvlsphiayytetavhnmvyfslqhlvdfltkgetstevtg
>d1dxy_2 3.16.9.1.3 (1-100) D-2-hydroxyisocaproate dehydrogenase {Lactobacillus casei}
mkiiaygarvdeiqyfkqwakdtgntleyhtefldentvewakgfdginslqttpyaagv
fekmhaygikfltirnvgtdnidmtamkqygirlsnvpay
>d1dya__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaadnlaksrwynqtpnrakrvittfrtgtwdayk
>d1dyb__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaagnlaksrwynqtpnrakrvittfrtgtwdayk
>d1dyc__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaainlaksrwynqtpnrakrvittfrtgtwdayk
>d1dyd__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaalnlaksrwynqtpnrakrvittfrtgtwdayk
>d1dye__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaasnlaksrwynqtpnrakrvittfrtgtwdayk
>d1dyf__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaamnlaksrwynqtpnrakrvittfrtgtwdayk
>d1dyg__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaaenlaksrwynqtpnrakrvittfrtgtwdayk
>d1dyha_ 3.61.1.1.1 Dihydrofolate reductase, prokaryotic type {Escherichia coli}
misliaalavdrvigmenampwnlpadlawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1dyhb_ 3.61.1.1.1 Dihydrofolate reductase, prokaryotic type {Escherichia coli}
misliaalavdrvigmenampwnlpadlawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1dyia_ 3.61.1.1.1 Dihydrofolate reductase, prokaryotic type {Escherichia coli}
misliaalavdrvigmenampwnlpadlawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1dyib_ 3.61.1.1.1 Dihydrofolate reductase, prokaryotic type {Escherichia coli}
misliaalavdrvigmenampwnlpadlawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1dyja_ 3.61.1.1.1 Dihydrofolate reductase, prokaryotic type {Escherichia coli}
misliaalavdrvigmenampwnlpadlawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1dyjb_ 3.61.1.1.1 Dihydrofolate reductase, prokaryotic type {Escherichia coli}
misliaalavdrvigmenampwnlpadlawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1dyna_ 2.49.1.1.4 Dynamin {Human (Homo sapiens)}
ilvirkgwltinnigimkggskeywfvltaenlswykddeekekkymlsvdnlklrdvek
gfmsskhifalfnteqrnvykdyrqlelacetqeevdswkasflragvyperv
>d1dynb_ 2.49.1.1.4 Dynamin {Human (Homo sapiens)}
ilvirkgwltinnigimkggskeywfvltaenlswykddeekekkymlsvdnlklrdvek
gfmsskhifalfnteqrnvykdyrqlelacetqeevdswkasflragvyperv
>d1dyr__ 3.61.1.1.6 Dihydrofolate reductases, eukaryotic type {Fungus (Pneumocystis carinii)}
nqqksltlivalttsygigrsnslpwklkkeisyfkrvtsfvptfdsfesmnvvlmgrkt
wesiplqfrplkgrinvvitrnesldlgngihsaksldhalellyrtygsessvqinrif
viggaqlykaamdhpkldrimatiiykdihcdvffplkfrdkewssvwkkekhsdleswv
gtkvphgkinedgfdyefemwtrdl
>d1e2aa_ 1.7.3.1.1 Enzyme IIa from lactose specific PTS, IIa-lac {Lactococcus lactis}
mnreemtllgfeivayagdarskllealkaaengdfakadslvveagsciaeahssqtgm
lareasgeelpysvtmmhgqdhlmttillkdvihhlielykr
>d1e2ab_ 1.7.3.1.1 Enzyme IIa from lactose specific PTS, IIa-lac {Lactococcus lactis}
mnreemtllgfeivayagdarskllealkaaengdfakadslvveagsciaeahssqtgm
lareasgeelpysvtmmhgqdhlmttillkdvihhlielykr
>d1e2ac_ 1.7.3.1.1 Enzyme IIa from lactose specific PTS, IIa-lac {Lactococcus lactis}
mnreemtllgfeivayagdarskllealkaaengdfakadslvveagsciaeahssqtgm
lareasgeelpysvtmmhgqdhlmttillkdvihhlielykr
>d1e2b__ 3.36.2.1.1 Enzyme IIB-cellobiose {Escherichia coli}
mekkhiylfssagmstsllvskmraqaekyevpviieafpetlagekgqnadvvllgpqi
aymlpeiqrllpnkpvevidsllygkvdglgvlkaavaaikkaaan
>d1e2o__ 3.35.1.1.5 Dihydrolipoamide succinyltransferase {Escherichia coli}
arsekrvpmtrlrkrvaerlleaknstamlttfnevnmkpimdlrkqygeafekrhgirl
gfmsfyvkavvealkrypevnasidgddvvyhnyfdvsmavstprglvtpvlrdvdtlgm
adiekkikelavkgrdgkltvedltggnftitnggvfgslmstpiinppqsailgmhaik
drpmavngqveilpmmylalsydhrlidgresvgflvtikelledptrllldv
>d1eaa__ 3.35.1.1.3 Dihydrolipoamide acetyltransferase {Azotobacter vinelandii}
ippippvdfakygeieevpmtrlmqigatnlhrswlnvphvtqfesaditeleafrvaqk
avakkagvkltvlplllkacayllkelpdfnsslapsgqalirkkyvhigfavdtpdgll
vpvirnvdqksllqlaaeaaelaekarskklgadamqgacftisslghiggtaftpivna
pevailgvskasmqpvwdgkafqprlmlplslsydhrvingaaaarftkrlgdlladira
ill
>d1eab__ 3.35.1.1.3 Dihydrolipoamide acetyltransferase {Azotobacter vinelandii}
ippippvdfakygeieevpmtrlmqigatnlhrswlnvphvtqfesaditeleafrvaqk
avakkagvkltvlplllkacayllkelpdfnsslapsgqalirkkyvhigfavdtpdgll
vpvirnvdqksllqlaaeaaelaekarskklgadamqgacftisslghiggtaftpivna
pevailgvskasmqpvwdgkafqprlmlplslsydhrvingaaaarftkrlgdlladira
ill
>d1eac__ 3.35.1.1.3 Dihydrolipoamide acetyltransferase {Azotobacter vinelandii}
ippippvdfakygeieevpmtrlmqigatnlhrswlnvphvtqfesaditeleafrvaqk
avakkagvkltvlplllkacayllkelpdfnsslapsgqalirkkyvhigfavdtpdgll
vpvirnvdqksllqlaaeaaelaekarskklgadamqgacftisslghiggtaftpivna
pevailgvskasmqpvwdgkafqprlmlplslsydhrvingaaaarftkrlgdlladira
ill
>d1ead__ 3.35.1.1.3 Dihydrolipoamide acetyltransferase {Azotobacter vinelandii}
ippippvdfakygeieevpmtrlmqigatnlhrswlnvphvtqfesaditeleafrvaqk
avakkagvkltvlplllkacayllkelpdfnsslapsgqalirkkyvhigfavdtpdgll
vpvirnvdqksllqlaaeaaelaekarskklgadamqgacftisslghiggtaftpivna
pevailgvskasmqpvwdgkafqprlmlplslsydhrvingaaaarftkrlgdlladira
ill
>d1eae__ 3.35.1.1.3 Dihydrolipoamide acetyltransferase {Azotobacter vinelandii}
ippippvdfakygeieevpmtrlmqigatnlhrswlnvphvtqfesaditeleafrvaqk
avakkagvkltvlplllkacayllkelpdfnsslapsgqalirkkyvhigfavdtpdgll
vpvirnvdqksllqlaaeaaelaekarskklgadamqgacftisslghiggtaftpivna
pevailgvskasmqpvwdgkafqprlmlplslsydhrvingaaaarftkrlgdlladira
ill
>d1eaf__ 3.35.1.1.3 Dihydrolipoamide acetyltransferase {Azotobacter vinelandii}
ippippvdfakygeieevpmtrlmqigatnlhrswlnvphvtqfesaditeleafrvaqk
avakkagvkltvlplllkacayllkelpdfnsslapsgqalirkkyvhigfavdtpdgll
vpvirnvdqksllqlaaeaaelaekarskklgadamqgacftisslghiggtaftpivna
pevailgvskasmqpvwdgkafqprlmlplslsydhrvingaaaarftkrlgdlladira
ill
>d1eaga_ 2.44.1.2.5 Acid protease {Yeast (Candida albicans)}
qavpvtlhneqvtyaaditvgsnnqklnvivdtgssdlwvpdvnvdcqvtysdqtadfck
qkgtydpsgssasqdlntpfkigygdgsssqgtlykdtvgfggvsiknqvladvdstsid
qgilgvgyktneaggsydnvpvtlkkqgviaknayslylnspdaatgqiifggvdnakys
gslialpvtsdrelrislgsvevsgktintdnvdvlldsgttitylqqdladqiikafng
kltqdsngnsfyevdcnlsgdvvfnfsknakisvpasefaaslqgddgqpydkcqllfdv
ndanilgdnflrsayivydlddneislaqvkytsassisalt
>d1eah1_ 2.9.1.4.6 Poliovirus {Poliovirus type 2, lansing strain}
annlpdtqssgpahsketpaltavetgatnplvpsdtvqtrhviqkrtrsestvesffar
gacvaiievdndaptkrasklfsvwkitykdtvqlrrklefftysrfdmeftfvvtsnyt
dannghalnqvyqimyippgapipgkwndytwqtssnpsvfytygapparisvpyvgian
ayshfydgfakvplagqastegdslygaaslndfgslavrvvndhnptkltskirvymkp
khvrvwcprppravpyygpgvdykdglaplpgkgltty
>d1eah2_ 2.9.1.4.6 Poliovirus {Poliovirus type 2, lansing strain}
svrvmqltlgnstittqeaansvvaygrwpeyikdseanpvdqptepdvaacrfytldtv
twrkesrgwwwklpdalkdmglfgqnmfyhylgragytvhvqcnaskfhqgalgvfavpe
mclagdstthmftkyenanpgekggefkgsftldtnatnparnfcpvdylfgsgvlagna
fvyphqiinlrtnncatlvlpyvnslsidsmtkhnnwgiailplapldfatessteipit
ltiapmccefnglrnitvprtq
>d1eah3_ 2.9.1.4.6 Poliovirus {Poliovirus type 2, lansing strain}
glpvlntpgsnqyltadnyqspcaipefdvtppidipgevrnmmelaeidtmiplnltnq
rkntmdmyrvelndaahsdtpilclslspasdprlahtmlgeilnyythwagslkftflf
cgsmmatgkllvsyappgaeapksrkeamlgthviwdiglqssctmvvpwisnttyrqti
ndsfteggyismfyqtrvvvplstprkmdilgfvsacndfsvrllrdtthisqea
>d1eaia_ 2.41.1.2.15 Elastase {Porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqndgteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1eaib_ 2.41.1.2.15 Elastase {Porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqndgteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1eaic_ 7.22.1.1.2 Ascaris elastase inhibitor {Pig roundworm (Ascaris suum)}
gqescgpnevwtectgcemkcgpdentpcplmcrrpscecspgrgmrrtndgkcipasqc
p
>d1eaid_ 7.22.1.1.2 Ascaris elastase inhibitor {Pig roundworm (Ascaris suum)}
gqescgpnevwtectgcemkcgpdentpcplmcrrpscecspgrgmrrtndgkcipasqc
p
>d1eal__ 2.53.1.2.14 Ileal lipid binding protein {Pig (Sus scrofa)}
aftgkyeieseknydefmkrlalpsdaidkarnlkiisevkqdgqnftwsqqypgghsit
ntftigkecdietiggkkfkatvqmeggkvvvnspnyhhtaeivdgklvevstvggvsye
rvskkla
>d1eama_ 3.56.1.4.1 Polymerase regulatory subunit VP39 {Vaccinia virus}
mdvvsldkpfmyfeeidneldyepesanevakklpyqgqlklllgelfflsklqrhgild
gatvvyigsapgthirylrdhfynlgviikwmlidgrhhdpilnglrdvtlvtrfvdeey
lrsikkqlhpskiilisdvrskrggnepstadllsnyalqnvmisilnpvasslkwrcpf
pdqwikdfyiphgnkmlqpfapsysaemrllsiytgenmrltrvtksdavnyakkmyyln
kivrnkvvvnfdypnqeydyfhmyfmlrtvycnktfpttkakvlflqqsifrflnip
>d1eapa1 2.1.1.1.51 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab 17E8 (mouse), kappa L chain}
dieltqspsslsaslggkvtitckasqdikkyigwyqhkpgkgprllihytstllpgips
rfrgsgsgrdysfsisnleggdiatyyclqyynlrtfgggtkleik
>d1eapa2 2.1.1.2.59 (108-214) Immunoglobulin (constant domains of L and H chains) {Fab 17E8 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgseraqgvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1eapb1 2.1.1.1.51 (1-124) Immunoglobulin (variable domains of L and H chains) {Fab 17E8 (mouse), kappa L chain}
evqlqesgtelvkpgasvkisckasgyistdhaihwvkqrpeqglewigyispgngdiky
nekfkvkatltadqssstaymqlnsltsedsavyfckrsyygssyvdywgqgttltvss
>d1eapb2 2.1.1.2.59 (125-221) Immunoglobulin (constant domains of L and H chains) {Fab 17E8 (mouse), kappa L chain}
akttppsvyplapgcgdttgssvtlgclvkgyfpesvtvtwnsgglsssvhtfpallqsg
lytmsssvtvpgggwpsatvtcsvahpassttvdkkl
>d1eas__ 2.41.1.2.15 Elastase {Porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1eat__ 2.41.1.2.15 Elastase {Porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1eau__ 2.41.1.2.15 Elastase {Porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1eaya_ 3.16.2.1.1 CheY protein {Escherichia coli}
adkelkflvvddfstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmp
nmdglellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleekln
kifeklgm
>d1eayb_ 3.16.2.1.1 CheY protein {Escherichia coli}
adkelkflvvddfstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmp
nmdglellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleekln
kifeklgm
>d1eayc_ 4.47.21.1.1 CheY-binding domain of CheA {Escherichia coli}
prriilsrlkagevdlleeelghlttltdvvkgadslsailpgdiaedditavlcfviea
dqitfet
>d1eayd_ 4.47.21.1.1 CheY-binding domain of CheA {Escherichia coli}
sprriilsrlkagevdlleeelghlttltdvvkgadslsailpgdiaedditavlcfvie
adqitfetv
>d1ebaa1 2.1.2.1.9 (10-116) Erythropoietin (EPO) receptor {Human (Homo sapiens)}
kfeskaallaargpeellcfterledlvcfweeaasagvgpgnysfsyqledepwklcrl
hqaptargavrfwcslptadtssfvplelrvtaasgapryhrvihin
>d1ebaa2 2.1.2.1.9 (117-224) Erythropoietin (EPO) receptor {Human (Homo sapiens)}
evvlldapvglvarladesghvvlrwlpppetpmtshiryevdvsagngagsvqrveile
grtecvlsnlrgrtrytfavrarmaepsfggfwsawsepvslltpsdl
>d1ebab1 2.1.2.1.9 (10-116) Erythropoietin (EPO) receptor {Human (Homo sapiens)}
kfeskaallaargpeellcfterledlvcfweeaasagvgpgnysfsyqledepwklcrl
hqaptargavrfwcslptadtssfvplelrvtaasgapryhrvihin
>d1ebab2 2.1.2.1.9 (117-220) Erythropoietin (EPO) receptor {Human (Homo sapiens)}
evvlldapvglvarladesghvvlrwlpppetpmtshiryevdvsagngagsvqrveile
grtecvlsnlrgrtrytfavrarmaepsfggfwsawsepvsllt
>d1ebca_ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgyqg
>d1ebda1 3.3.1.5.9 (7-154,272-346) Dihydrolipoamide dehydrogenase {Bacillus stearothermophilus}
aietetlvvgagpggyvaairaaqlgqkvtivekgnlggvclnvgcipskalisashrye
qakhseemgikaenvtidfakvqewkasvvkkltggvegllkgnkveivkgeayfvdant
vrvvngdsaqtytfknaiiatgsrpielXvgrrpntdelgleqigikmtnrglievdqqc
rtsvpnifaigdivpgpalahkasyegkvaaeaiaghpsavdyv
>d1ebda2 3.3.1.5.9 (155-271) Dihydrolipoamide dehydrogenase {Bacillus stearothermophilus}
pnfkfsnrildstgalnlgevpkslvvigggyigielgtayanfgtkvtilegageilsg
fekqmaaiikkrlkkkgvevvtnalakgaeeredgvtvtyeangetktidadyvlvt
>d1ebda3 4.67.1.1.7 (347-461) Dihydrolipoamide dehydrogenase {Bacillus stearothermophilus}
aipavvfsdpecasvgyfeqqakdegidviaakfpfaangralalndtdgflklvvrked
gviigaqiigpnasdmiaelglaieagmtaedialtihahptlgeiameaaeval
>d1ebdb1 3.3.1.5.9 (7-154,272-346) Dihydrolipoamide dehydrogenase {Bacillus stearothermophilus}
aietetlvvgagpggyvaairaaqlgqkvtivekgnlggvclnvgcipskalisashrye
qakhseemgikaenvtidfakvqewkasvvkkltggvegllkgnkveivkgeayfvdant
vrvvngdsaqtytfknaiiatgsrpielXvgrrpntdelgleqigikmtnrglievdqqc
rtsvpnifaigdivpgpalahkasyegkvaaeaiaghpsavdyv
>d1ebdb2 3.3.1.5.9 (155-271) Dihydrolipoamide dehydrogenase {Bacillus stearothermophilus}
pnfkfsnrildstgalnlgevpkslvvigggyigielgtayanfgtkvtilegageilsg
fekqmaaiikkrlkkkgvevvtnalakgaeeredgvtvtyeangetktidadyvlvt
>d1ebdb3 4.67.1.1.7 (347-461) Dihydrolipoamide dehydrogenase {Bacillus stearothermophilus}
aipavvfsdpecasvgyfeqqakdegidviaakfpfaangralalndtdgflklvvrked
gviigaqiigpnasdmiaelglaieagmtaedialtihahptlgeiameaaeval
>d1ebdc_ 1.9.1.1.1 E3-binding domain of dihydrolipoamide acetyltransferase {Bacillus stearothermophilus}
iampsvrkyarekgvdirlvqgtgkngrvlkedidaflagg
>d1ebga1 3.1.10.1.1 (142-436) Enolase {Baker's yeast (Saccharomyces cerevisiae)}
spyvlpvpflnvlnggshaggalalqefmiaptgaktfaealrigsevyhnlksltkkry
gasagnvgdeggvapniqtaeealdlivdaikaaghdgkvkigldcasseffkdgkydld
fknpnsdkskwltgpqladlyhslmkrypivsiedpfaeddweawshffktagiqivadd
ltvtnpkriataiekkaadalllkvnqigtlsesikaaqdsfaagwgvmvshrsgetedt
fiadlvvglrtgqiktgaparserlaklnqllrieeelgdnavfagenfhhgdkl
>d1ebga2 4.44.1.1.1 (1-141) Enolase {Baker's yeast (Saccharomyces cerevisiae)}
avskvyarsvydsrgnptvevelttekgvfrsivpsgastgvhealemrdgdkskwmgkg
vlhavknvndviapafvkanidvkdqkavddflisldgtanksklganailgvslaasra
aaaeknvplykhladlskskt
>d1ebgb1 3.1.10.1.1 (142-436) Enolase {Baker's yeast (Saccharomyces cerevisiae)}
spyvlpvpflnvlnggshaggalalqefmiaptgaktfaealrigsevyhnlksltkkry
gasagnvgdeggvapniqtaeealdlivdaikaaghdgkvkigldcasseffkdgkydld
fknpnsdkskwltgpqladlyhslmkrypivsiedpfaeddweawshffktagiqivadd
ltvtnpkriataiekkaadalllkvnqigtlsesikaaqdsfaagwgvmvshrsgetedt
fiadlvvglrtgqiktgaparserlaklnqllrieeelgdnavfagenfhhgdkl
>d1ebgb2 4.44.1.1.1 (1-141) Enolase {Baker's yeast (Saccharomyces cerevisiae)}
avskvyarsvydsrgnptvevelttekgvfrsivpsgastgvhealemrdgdkskwmgkg
vlhavknvndviapafvkanidvkdqkavddflisldgtanksklganailgvslaasra
aaaeknvplykhladlskskt
>d1ebha1 3.1.10.1.1 (142-436) Enolase {Baker's yeast (Saccharomyces cerevisiae)}
spyvlpvpflnvlnggshaggalalqefmiaptgaktfaealrigsevyhnlksltkkry
gasagnvgdeggvapniqtaeealdlivdaikaaghdgkvkigldcasseffkdgkydld
fknpnsdkskwltgpqladlyhslmkrypivsiedpfaeddweawshffktagiqivadd
ltvtnpkriataiekkaadalllkvnqigtlsesikaaqdsfaagwgvmvshrsgetedt
fiadlvvglrtgqiktgaparserlaklnqllrieeelgdnavfagenfhhgdkl
>d1ebha2 4.44.1.1.1 (1-141) Enolase {Baker's yeast (Saccharomyces cerevisiae)}
avskvyarsvydsrgnptvevelttekgvfrsivpsgastgvhealemrdgdkskwmgkg
vlhavknvndviapafvkanidvkdqkavddflisldgtanksklganailgvslaasra
aaaeknvplykhladlskskt
>d1ebhb1 3.1.10.1.1 (142-436) Enolase {Baker's yeast (Saccharomyces cerevisiae)}
spyvlpvpflnvlnggshaggalalqefmiaptgaktfaealrigsevyhnlksltkkry
gasagnvgdeggvapniqtaeealdlivdaikaaghdgkvkigldcasseffkdgkydld
fknpnsdkskwltgpqladlyhslmkrypivsiedpfaeddweawshffktagiqivadd
ltvtnpkriataiekkaadalllkvnqigtlsesikaaqdsfaagwgvmvshrsgetedt
fiadlvvglrtgqiktgaparserlaklnqllrieeelgdnavfagenfhhgdkl
>d1ebhb2 4.44.1.1.1 (1-141) Enolase {Baker's yeast (Saccharomyces cerevisiae)}
avskvyarsvydsrgnptvevelttekgvfrsivpsgastgvhealemrdgdkskwmgkg
vlhavknvndviapafvkanidvkdqkavddflisldgtanksklganailgvslaasra
aaaeknvplykhladlskskt
>d1ebpa1 2.1.2.1.9 (10-116) Erythropoietin (EPO) receptor {Human (Homo sapiens)}
kfeskaallaargpeellcfterledlvcfweeaasagvgpgnysfsyqledepwklcrl
hqaptargavrfwcslptadtssfvplelrvtaasgapryhrvihin
>d1ebpa2 2.1.2.1.9 (117-220) Erythropoietin (EPO) receptor {Human (Homo sapiens)}
evvlldapvglvarladesghvvlrwlpppetpmtshiryevdvsagngagsvqrveile
grtecvlsnlrgrtrytfavrarmaepsfggfwsawsepvsllt
>d1ebpb1 2.1.2.1.9 (10-116) Erythropoietin (EPO) receptor {Human (Homo sapiens)}
kfeskaallaargpeellcfterledlvcfweeaasagvgpgnysfsyqledepwklcrl
hqaptargavrfwcslptadtssfvplelrvtaasgapryhrvihin
>d1ebpb2 2.1.2.1.9 (117-220) Erythropoietin (EPO) receptor {Human (Homo sapiens)}
evvlldapvglvarladesghvvlrwlpppetpmtshiryevdvsagngagsvqrveile
grtecvlsnlrgrtrytfavrarmaepsfggfwsawsepvsllt
>d1eca__ 1.1.1.1.13 Erythrocruorin {Midge (Chironomous thummi thummi), fraction III}
lsadqistvqasfdkvkgdpvgilyavfkadpsimakftqfagkdlesikgtapfethan
rivgffskiigelpnieadvntfvashkprgvthdqlnnfragfvsymkahtdfagaeaa
wgatldtffgmifskm
>d1ecba1 3.51.1.1.5 (250-481) Glutamine PRPP amidotransferase, C-terminal domain {Escherichia coli}
npclfeyvyfarpdsfidkisvysarvnmgtklgekiarewedldidvvipipetscdia
leiarilgkpyrqgfvknryvgrtfimpgqqlrrksvrrklnanraefrdknvllvddsi
vrgttseqiiemareagakkvylasaapeirfpnvygidmpsateliahgrevdeirqii
gadglifqdlndlidavraenpdiqqfecsvfngvyvtkdvdqgyldfldtl
>d1ecba2 4.124.1.1.3 (1-249) Glutamine PRPP amidotransferase, N-terminal domain {Escherichia coli}
cgivgiagvmpvnqsiydaltvlqhrgqdaagiitidanncfrlrkanglvsdvfearhm
qrlqgnmgighvryptagsssaseaqpfyvnspygitlahngnltnahelrkklfeekrr
hinttsdseillnifaseldnfrhypleadnifaaiaatnrlirgayacvamiighgmva
frdpngirplvlgkrdidenrteymvasesvaldtlgfdflrdvapgeaiyiteegqlft
rqcadnpvs
>d1ecbb1 3.51.1.1.5 (250-478) Glutamine PRPP amidotransferase, C-terminal domain {Escherichia coli}
npclfeyvyfarpdsfidkisvysarvnmgtklgekiarewedldidvvipipetscdia
leiarilgkpyrqgfvknryvgrtfimpgqqlrrksvrrklnanraefrdknvllvddsi
vrgttseqiiemareagakkvylasaapeirfpnvygidmpsateliahgrevdeirqii
gadglifqdlndlidavraenpdiqqfecsvfngvyvtkdvdqgyldfl
>d1ecbb2 4.124.1.1.3 (1-249) Glutamine PRPP amidotransferase, N-terminal domain {Escherichia coli}
cgivgiagvmpvnqsiydaltvlqhrgqdaagiitidanncfrlrkanglvsdvfearhm
qrlqgnmgighvryptagsssaseaqpfyvnspygitlahngnltnahelrkklfeekrr
hinttsdseillnifaseldnfrhypleadnifaaiaatnrlirgayacvamiighgmva
frdpngirplvlgkrdidenrteymvasesvaldtlgfdflrdvapgeaiyiteegqlft
rqcadnpvs
>d1ecbc1 3.51.1.1.5 (250-482) Glutamine PRPP amidotransferase, C-terminal domain {Escherichia coli}
npclfeyvyfarpdsfidkisvysarvnmgtklgekiarewedldidvvipipetscdia
leiarilgkpyrqgfvknryvgrtfimpgqqlrrksvrrklnanraefrdknvllvddsi
vrgttseqiiemareagakkvylasaapeirfpnvygidmpsateliahgrevdeirqii
gadglifqdlndlidavraenpdiqqfecsvfngvyvtkdvdqgyldfldtlr
>d1ecbc2 4.124.1.1.3 (1-249) Glutamine PRPP amidotransferase, N-terminal domain {Escherichia coli}
cgivgiagvmpvnqsiydaltvlqhrgqdaagiitidanncfrlrkanglvsdvfearhm
qrlqgnmgighvryptagsssaseaqpfyvnspygitlahngnltnahelrkklfeekrr
hinttsdseillnifaseldnfrhypleadnifaaiaatnrlirgayacvamiighgmva
frdpngirplvlgkrdidenrteymvasesvaldtlgfdflrdvapgeaiyiteegqlft
rqcadnpvs
>d1ecbd1 3.51.1.1.5 (250-481) Glutamine PRPP amidotransferase, C-terminal domain {Escherichia coli}
npclfeyvyfarpdsfidkisvysarvnmgtklgekiarewedldidvvipipetscdia
leiarilgkpyrqgfvknryvgrtfimpgqqlrrksvrrklnanraefrdknvllvddsi
vrgttseqiiemareagakkvylasaapeirfpnvygidmpsateliahgrevdeirqii
gadglifqdlndlidavraenpdiqqfecsvfngvyvtkdvdqgyldfldtl
>d1ecbd2 4.124.1.1.3 (1-249) Glutamine PRPP amidotransferase, N-terminal domain {Escherichia coli}
cgivgiagvmpvnqsiydaltvlqhrgqdaagiitidanncfrlrkanglvsdvfearhm
qrlqgnmgighvryptagsssaseaqpfyvnspygitlahngnltnahelrkklfeekrr
hinttsdseillnifaseldnfrhypleadnifaaiaatnrlirgayacvamiighgmva
frdpngirplvlgkrdidenrteymvasesvaldtlgfdflrdvapgeaiyiteegqlft
rqcadnpvs
>d1ecca1 3.51.1.1.5 (250-492) Glutamine PRPP amidotransferase, C-terminal domain {Escherichia coli}
npclfeyvyfarpdsfidkisvysarvnmgtklgekiarewedldidvvipipetscdia
leiarilgkpyrqgfvknryvgrtfimpgqqlrrksvrrklnanraefrdknvllvddsi
vrgttseqiiemareagakkvylasaapeirfpnvygidmpsateliahgrevdeirqii
gadglifqdlndlidavraenpdiqqfecsvfngvyvtkdvdqgyldfldtlrnddakav
qrq
>d1ecca2 4.124.1.1.3 (1-249) Glutamine PRPP amidotransferase, N-terminal domain {Escherichia coli}
cgivgiagvmpvnqsiydaltvlqhrgqdaagiitidanncfrlrkanglvsdvfearhm
qrlqgnmgighvryptagsssaseaqpfyvnspygitlahngnltnahelrkklfeekrr
hinttsdseillnifaseldnfrhypleadnifaaiaatnrlirgayacvamiighgmva
frdpngirplvlgkrdidenrteymvasesvaldtlgfdflrdvapgeaiyiteegqlft
rqcadnpvs
>d1eccb1 3.51.1.1.5 (250-492) Glutamine PRPP amidotransferase, C-terminal domain {Escherichia coli}
npclfeyvyfarpdsfidkisvysarvnmgtklgekiarewedldidvvipipetscdia
leiarilgkpyrqgfvknryvgrtfimpgqqlrrksvrrklnanraefrdknvllvddsi
vrgttseqiiemareagakkvylasaapeirfpnvygidmpsateliahgrevdeirqii
gadglifqdlndlidavraenpdiqqfecsvfngvyvtkdvdqgyldfldtlrnddakav
qrq
>d1eccb2 4.124.1.1.3 (1-249) Glutamine PRPP amidotransferase, N-terminal domain {Escherichia coli}
cgivgiagvmpvnqsiydaltvlqhrgqdaagiitidanncfrlrkanglvsdvfearhm
qrlqgnmgighvryptagsssaseaqpfyvnspygitlahngnltnahelrkklfeekrr
hinttsdseillnifaseldnfrhypleadnifaaiaatnrlirgayacvamiighgmva
frdpngirplvlgkrdidenrteymvasesvaldtlgfdflrdvapgeaiyiteegqlft
rqcadnpvs
>d1ecd__ 1.1.1.1.13 Erythrocruorin {Midge (Chironomous thummi thummi), fraction III}
lsadqistvqasfdkvkgdpvgilyavfkadpsimakftqfagkdlesikgtapfethan
rivgffskiigelpnieadvntfvashkprgvthdqlnnfragfvsymkahtdfagaeaa
wgatldtffgmifskm
>d1ecea_ 3.1.7.3.6 Endocellulase E1 {Acidothermus cellulolyticus}
agggywhtsgreildannvpvriaginwfgfetcnyvvhglwsrdyrsmldqikslgynt
irlpysddilkpgtmpnsinfyqmnqdlqgltslqvmdkivayagqiglriildrhrpdc
sgqsalwytssvseatwisdlqalaqrykgnptvvgfdlhnephdpacwgcgdpsidwrl
aaeragnavlsvnpnllifvegvqsyngdsywwggnlqgagqypvvlnvpnrlvysahdy
atsvypqtwfsdptfpnnmpgiwnknwgylfnqniapvwlgefgttlqsttdqtwlktlv
qylrptaqygadsfqwtfwswnpdsgdtggilkddwqtvdtvkdgylapikssifdpv
>d1eceb_ 3.1.7.3.6 Endocellulase E1 {Acidothermus cellulolyticus}
agggywhtsgreildannvpvriaginwfgfetcnyvvhglwsrdyrsmldqikslgynt
irlpysddilkpgtmpnsinfyqmnqdlqgltslqvmdkivayagqiglriildrhrpdc
sgqsalwytssvseatwisdlqalaqrykgnptvvgfdlhnephdpacwgcgdpsidwrl
aaeragnavlsvnpnllifvegvqsyngdsywwggnlqgagqypvvlnvpnrlvysahdy
atsvypqtwfsdptfpnnmpgiwnknwgylfnqniapvwlgefgttlqsttdqtwlktlv
qylrptaqygadsfqwtfwswnpdsgdtggilkddwqtvdtvkdgylapikssifdpv
>d1ecfa1 3.51.1.1.5 (250-492) Glutamine PRPP amidotransferase, C-terminal domain {Escherichia coli}
npclfeyvyfarpdsfidkisvysarvnmgtklgekiarewedldidvvipipetscdia
leiarilgkpyrqgfvknryvgrtfimpgqqlrrksvrrklnanraefrdknvllvddsi
vrgttseqiiemareagakkvylasaapeirfpnvygidmpsateliahgrevdeirqii
gadglifqdlndlidavraenpdiqqfecsvfngvyvtkdvdqgyldfldtlrnddakav
qrq
>d1ecfa2 4.124.1.1.3 (1-249) Glutamine PRPP amidotransferase, N-terminal domain {Escherichia coli}
cgivgiagvmpvnqsiydaltvlqhrgqdaagiitidanncfrlrkanglvsdvfearhm
qrlqgnmgighvryptagsssaseaqpfyvnspygitlahngnltnahelrkklfeekrr
hinttsdseillnifaseldnfrhypleadnifaaiaatnrlirgayacvamiighgmva
frdpngirplvlgkrdidenrteymvasesvaldtlgfdflrdvapgeaiyiteegqlft
rqcadnpvs
>d1ecfb1 3.51.1.1.5 (250-500) Glutamine PRPP amidotransferase, C-terminal domain {Escherichia coli}
npclfeyvyfarpdsfidkisvysarvnmgtklgekiarewedldidvvipipetscdia
leiarilgkpyrqgfvknryvgrtfimpgqqlrrksvrrklnanraefrdknvllvddsi
vrgttseqiiemareagakkvylasaapeirfpnvygidmpsateliahgrevdeirqii
gadglifqdlndlidavraenpdiqqfecsvfngvyvtkdvdqgyldfldtlrnddakav
qrqnevenlem
>d1ecfb2 4.124.1.1.3 (1-249) Glutamine PRPP amidotransferase, N-terminal domain {Escherichia coli}
cgivgiagvmpvnqsiydaltvlqhrgqdaagiitidanncfrlrkanglvsdvfearhm
qrlqgnmgighvryptagsssaseaqpfyvnspygitlahngnltnahelrkklfeekrr
hinttsdseillnifaseldnfrhypleadnifaaiaatnrlirgayacvamiighgmva
frdpngirplvlgkrdidenrteymvasesvaldtlgfdflrdvapgeaiyiteegqlft
rqcadnpvs
>d1ecga1 3.51.1.1.5 (250-492) Glutamine PRPP amidotransferase, C-terminal domain {Escherichia coli}
npclfeyvyfarpdsfidkisvysarvnmgtklgekiarewedldidvvipipetscdia
leiarilgkpyrqgfvknryvgrtfimpgqqlrrksvrrklnanraefrdknvllvddsi
vrgttseqiiemareagakkvylasaapeirfpnvygidmpsateliahgrevdeirqii
gadglifqdlndlidavraenpdiqqfecsvfngvyvtkdvdqgyldfldtlrnddakav
qrq
>d1ecga2 4.124.1.1.3 (1-249) Glutamine PRPP amidotransferase, N-terminal domain {Escherichia coli}
cgivgiagvmpvnqsiydaltvlqhrgqdaagiitidanncfrlrkanglvsdvfearhm
qrlqgnmgighvryptagsssaseaqpfyvnspygitlahngnltnahelrkklfeekrr
hinttsdseillnifaseldnfrhypleadnifaaiaatnrlirgayacvamiighgmva
frdpngirplvlgkrdidenrteymvasesvaldtlgfdflrdvapgeaiyiteegqlft
rqcadnpvs
>d1ecgb1 3.51.1.1.5 (250-500) Glutamine PRPP amidotransferase, C-terminal domain {Escherichia coli}
npclfeyvyfarpdsfidkisvysarvnmgtklgekiarewedldidvvipipetscdia
leiarilgkpyrqgfvknryvgrtfimpgqqlrrksvrrklnanraefrdknvllvddsi
vrgttseqiiemareagakkvylasaapeirfpnvygidmpsateliahgrevdeirqii
gadglifqdlndlidavraenpdiqqfecsvfngvyvtkdvdqgyldfldtlrnddakav
qrqnevenlem
>d1ecgb2 4.124.1.1.3 (1-249) Glutamine PRPP amidotransferase, N-terminal domain {Escherichia coli}
cgivgiagvmpvnqsiydaltvlqhrgqdaagiitidanncfrlrkanglvsdvfearhm
qrlqgnmgighvryptagsssaseaqpfyvnspygitlahngnltnahelrkklfeekrr
hinttsdseillnifaseldnfrhypleadnifaaiaatnrlirgayacvamiighgmva
frdpngirplvlgkrdidenrteymvasesvaldtlgfdflrdvapgeaiyiteegqlft
rqcadnpvs
>d1ecia_ 1.34.1.1.1 Ectatomin, A & B chains {Ant (Ectatomma tuberculatum), venom}
gvipkkiwetvcptvepwakkcsgdiatyikrecgkl
>d1ecib_ 1.34.1.1.1 Ectatomin, A & B chains {Ant (Ectatomma tuberculatum), venom}
wstivklticptlksmakkcegsiatmikkkcdk
>d1ecja1 3.51.1.1.5 (250-492) Glutamine PRPP amidotransferase, C-terminal domain {Escherichia coli}
npclfeyvyfarpdsfidkisvysarvnmgtklgekiarewedldidvvipipetscdia
leiarilgkpyrqgfvknryvgrtfimpgqqlrrksvrrklnanraefrdknvllvddsi
vrgttseqiiemareagakkvylasaapeirfpnvygidmpsateliahgrevdeirqii
gadglifqdlndlidavraenpdiqqfecsvfngvyvtkdvdqgyldfldtlrnddakav
qrq
>d1ecja2 4.124.1.1.3 (1-249) Glutamine PRPP amidotransferase, N-terminal domain {Escherichia coli}
cgivgiagvmpvnqsiydaltvlqhrgqdaagiitidanncfrlrkanglvsdvfearhm
qrlqgnmgighvryptagsssaseaqpfyvnspygitlahngnltnahelrkklfeekrr
hinttsdseillnifaseldnfrhypleadnifaaiaatnrlirgayacvamiighgmva
frdpngirplvlgkrdidenrteymvasesvaldtlgfdflrdvapgeaiyiteegqlft
rqcadnpvs
>d1ecjb1 3.51.1.1.5 (250-492) Glutamine PRPP amidotransferase, C-terminal domain {Escherichia coli}
npclfeyvyfarpdsfidkisvysarvnmgtklgekiarewedldidvvipipetscdia
leiarilgkpyrqgfvknryvgrtfimpgqqlrrksvrrklnanraefrdknvllvddsi
vrgttseqiiemareagakkvylasaapeirfpnvygidmpsateliahgrevdeirqii
gadglifqdlndlidavraenpdiqqfecsvfngvyvtkdvdqgyldfldtlrnddakav
qrq
>d1ecjb2 4.124.1.1.3 (1-249) Glutamine PRPP amidotransferase, N-terminal domain {Escherichia coli}
cgivgiagvmpvnqsiydaltvlqhrgqdaagiitidanncfrlrkanglvsdvfearhm
qrlqgnmgighvryptagsssaseaqpfyvnspygitlahngnltnahelrkklfeekrr
hinttsdseillnifaseldnfrhypleadnifaaiaatnrlirgayacvamiighgmva
frdpngirplvlgkrdidenrteymvasesvaldtlgfdflrdvapgeaiyiteegqlft
rqcadnpvs
>d1ecjc1 3.51.1.1.5 (250-492) Glutamine PRPP amidotransferase, C-terminal domain {Escherichia coli}
npclfeyvyfarpdsfidkisvysarvnmgtklgekiarewedldidvvipipetscdia
leiarilgkpyrqgfvknryvgrtfimpgqqlrrksvrrklnanraefrdknvllvddsi
vrgttseqiiemareagakkvylasaapeirfpnvygidmpsateliahgrevdeirqii
gadglifqdlndlidavraenpdiqqfecsvfngvyvtkdvdqgyldfldtlrnddakav
qrq
>d1ecjc2 4.124.1.1.3 (1-249) Glutamine PRPP amidotransferase, N-terminal domain {Escherichia coli}
cgivgiagvmpvnqsiydaltvlqhrgqdaagiitidanncfrlrkanglvsdvfearhm
qrlqgnmgighvryptagsssaseaqpfyvnspygitlahngnltnahelrkklfeekrr
hinttsdseillnifaseldnfrhypleadnifaaiaatnrlirgayacvamiighgmva
frdpngirplvlgkrdidenrteymvasesvaldtlgfdflrdvapgeaiyiteegqlft
rqcadnpvs
>d1ecjd1 3.51.1.1.5 (250-492) Glutamine PRPP amidotransferase, C-terminal domain {Escherichia coli}
npclfeyvyfarpdsfidkisvysarvnmgtklgekiarewedldidvvipipetscdia
leiarilgkpyrqgfvknryvgrtfimpgqqlrrksvrrklnanraefrdknvllvddsi
vrgttseqiiemareagakkvylasaapeirfpnvygidmpsateliahgrevdeirqii
gadglifqdlndlidavraenpdiqqfecsvfngvyvtkdvdqgyldfldtlrnddakav
qrq
>d1ecjd2 4.124.1.1.3 (1-249) Glutamine PRPP amidotransferase, N-terminal domain {Escherichia coli}
cgivgiagvmpvnqsiydaltvlqhrgqdaagiitidanncfrlrkanglvsdvfearhm
qrlqgnmgighvryptagsssaseaqpfyvnspygitlahngnltnahelrkklfeekrr
hinttsdseillnifaseldnfrhypleadnifaaiaatnrlirgayacvamiighgmva
frdpngirplvlgkrdidenrteymvasesvaldtlgfdflrdvapgeaiyiteegqlft
rqcadnpvs
>d1ecl__ 5.10.1.1.1 DNA topoisomerase I, 67K N-terminal domain {Escherichia coli}
gkalvivespakaktinkylgsdyvvkssvghirdltsgsaakksadststktakkpkkp
dergalvnrmgvdpwhnweahyevlpgkekvvselkqlaekadhiylatdldregeaiaw
hlreviggddarysrvvfneitknairqafnkpgelnidrvnaqqarrfmdrvvgymvsp
llwkkiarglsagrvqsvavrlvverereikafvpeefwevdastttpsgealalqvthq
ndkpfrpvnkeqtqaavsllekarysvleredkpttskpgapfitstlqqaastrlgfgv
kktmmmaqrlyeagyitymrtdstnlsqdavnmvrgyisdnfgkkylpespnqyaskgns
qeaheairpsdvnvmaeslkdmeadaqklyqliwrqfvacqmtpakydsttltvgagdfr
lkargrilrfdgwtkvmpalrkgdedrilpavnkgdaltlveltpaqhftkpparfseas
lvkelekrgigrpstyasiistiqdrgyvrvenrrfyaekmgeivtdrleenfrelmnyd
ftaqmensldqvanheaewkavldhffsdftqqldkaekdpeeggmrpn
>d1ecma_ 1.120.1.1.1 Chorismate mutase domain of P-protein {Escherichia coli}
npllalrekisaldekllallaerrelavevgkakllshrpvrdidrerdllerlitlgk
ahhldahyitrlfqliiedsvltqqallqqh
>d1ecmb_ 1.120.1.1.1 Chorismate mutase domain of P-protein {Escherichia coli}
pllalrekisaldekllallaerrelavevgkakllshrpvrdidrerdllerlitlgka
hhldahyitrlfqliiedsvltqqallqqhlnkin
>d1ecn__ 1.1.1.1.13 Erythrocruorin {Midge (Chironomous thummi thummi), fraction III}
lsadqistvqasfdkvkgdpvgilyavfkadpsimakftqfagkdlesikgtapfethan
rivgffskiigelpnieadvntfvashkprgvthdqlnnfragfvsymkahtdfagaeaa
wgatldtffgmifskm
>d1eco__ 1.1.1.1.13 Erythrocruorin {Midge (Chironomous thummi thummi), fraction III}
lsadqistvqasfdkvkgdpvgilyavfkadpsimakftqfagkdlesikgtapfethan
rivgffskiigelpnieadvntfvashkprgvthdqlnnfragfvsymkahtdfagaeaa
wgatldtffgmifskm
>d1ecpa_ 3.47.1.1.3 Purine nucleoside phosphorylase, PNP {Escherichia coli}
atphinaemgdfadvvlmpgdplrakyiaetfledarevnnvrgmlgftgtykgrkisvm
ghgmgipscsiytkelitdfgvkkiirvgscgavlphvklrdvvigmgactdskvnrirf
kdhdfaaiadfdmvrnavdaakalgidarvgnlfsadlfyspdgemfdvmekygilgvem
eaagiygvaaefgakaltictvsdhirtheqttaaerqttfndmikialesvllgdk
>d1ecpb_ 3.47.1.1.3 Purine nucleoside phosphorylase, PNP {Escherichia coli}
atphinaemgdfadvvlmpgdplrakyiaetfledarevnnvrgmlgftgtykgrkisvm
ghgmgipscsiytkelitdfgvkkiirvgscgavlphvklrdvvigmgactdskvnrirf
kdhdfaaiadfdmvrnavdaakalgidarvgnlfsadlfyspdgemfdvmekygilgvem
eaagiygvaaefgakaltictvsdhirtheqttaaerqttfndmikialesvllgdk
>d1ecpc_ 3.47.1.1.3 Purine nucleoside phosphorylase, PNP {Escherichia coli}
atphinaemgdfadvvlmpgdplrakyiaetfledarevnnvrgmlgftgtykgrkisvm
ghgmgipscsiytkelitdfgvkkiirvgscgavlphvklrdvvigmgactdskvnrirf
kdhdfaaiadfdmvrnavdaakalgidarvgnlfsadlfyspdgemfdvmekygilgvem
eaagiygvaaefgakaltictvsdhirtheqttaaerqttfndmikialesvllgdk
>d1ecpd_ 3.47.1.1.3 Purine nucleoside phosphorylase, PNP {Escherichia coli}
atphinaemgdfadvvlmpgdplrakyiaetfledarevnnvrgmlgftgtykgrkisvm
ghgmgipscsiytkelitdfgvkkiirvgscgavlphvklrdvvigmgactdskvnrirf
kdhdfaaiadfdmvrnavdaakalgidarvgnlfsadlfyspdgemfdvmekygilgvem
eaagiygvaaefgakaltictvsdhirtheqttaaerqttfndmikialesvllgdk
>d1ecpe_ 3.47.1.1.3 Purine nucleoside phosphorylase, PNP {Escherichia coli}
atphinaemgdfadvvlmpgdplrakyiaetfledarevnnvrgmlgftgtykgrkisvm
ghgmgipscsiytkelitdfgvkkiirvgscgavlphvklrdvvigmgactdskvnrirf
kdhdfaaiadfdmvrnavdaakalgidarvgnlfsadlfyspdgemfdvmekygilgvem
eaagiygvaaefgakaltictvsdhirtheqttaaerqttfndmikialesvllgdk
>d1ecpf_ 3.47.1.1.3 Purine nucleoside phosphorylase, PNP {Escherichia coli}
atphinaemgdfadvvlmpgdplrakyiaetfledarevnnvrgmlgftgtykgrkisvm
ghgmgipscsiytkelitdfgvkkiirvgscgavlphvklrdvvigmgactdskvnrirf
kdhdfaaiadfdmvrnavdaakalgidarvgnlfsadlfyspdgemfdvmekygilgvem
eaagiygvaaefgakaltictvsdhirtheqttaaerqttfndmikialesvllgdk
>d1ecra_ 5.2.1.1.1 Replication terminator protein (Tus) {Escherichia coli}
dlvdrlnttfrqmeqelaifaahleqhkllvarvfslpevkkedehnplnrievkqhlgn
daqslalrhfrhlfiqqqsenrsskaavrlpgvlcyqvdnlsqaalvshiqhinklkttf
ehivtveselptaarfewvhrhlpglitlnayrtltvlhdpatlrfgwankhiiknlhrd
evlaqlekslksprsvapwtreewqrklereyqdiaalpqnaklkikrpvkvqpiarvwy
kgdqkqvqhacptplialinrdngagvpdvgellnydadnvqhrykpqaqplrliiprlh
lyvad
>d1ecy__ 2.14.1.1.1 Ecotin, trypsin inhibitor {Escherichia coli}
aesvqplekiapypqaekgmkrqviqltpqedestlkvelligqtlevdcnlhrlggkle
nktlegwgydyyvfdkvsspvstmmacpdgkkekkfvtaylgdagmlrynsklpivvytp
dnvdvkyrvwkaeekidnavvr
>d1ecza_ 2.14.1.1.1 Ecotin, trypsin inhibitor {Escherichia coli}
aesvqplekiapypqaekgmkrqviqltpqedestlkvelligqtlevdcnlhrlggkle
nktlegwgydyyvfdkvsspvstmmacpdgkkekkfvtaylgdagmlrynsklpivvytp
dnvdvkyrvwkaeekidnavvr
>d1eczb_ 2.14.1.1.1 Ecotin, trypsin inhibitor {Escherichia coli}
aesvqplekiapypqaekgmkrqviqltpqedestlkvelligqtlevdcnlhrlggkle
nktlegwgydyyvfdkvsspvstmmacpdgkkekkfvtaylgdagmlrynsklpivvytp
dnvdvkyrvwkaeekidnavvr
>d1edb__ 3.59.1.6.1 Haloalkane dehalogenase {Xanthobacter autotrophicus}
minairtpdqrfsnldqypfspnylddlpgypglrahyldegnsdaedvflclhgeptws
ylyrkmipvfaesgarviapdffgfgksdkpvdeedytfefhrnfllalierldlrnitl
vvqdwggflgltlpmadpsrfkrliimnaclmtdpvtqpafsafvtqpadgftawkydlv
tpsdlrldqfmkrwaptlteaeasayaapfpdtsyqagvrkfpkmvaqrdqacidistea
isfwqndwngqtfmaigmkdkllgpdvmypmkalingcpepleiadaghfvqefgeqvar
ealkhfaete
>d1edd__ 3.59.1.6.1 Haloalkane dehalogenase {Xanthobacter autotrophicus}
minairtpdqrfsnldqypfspnylddlpgypglrahyldegnsdaedvflclhgeptws
ylyrkmipvfaesgarviapdffgfgksdkpvdeedytfefhrnfllalierldlrnitl
vvqdwggflgltlpmadpsrfkrliimnaclmtdpvtqpafsafvtqpadgftawkydlv
tpsdlrldqfmkrwaptlteaeasayaapfpdtsyqagvrkfpkmvaqrdqacidistea
isfwqndwngqtfmaigmkdkllgpdvmypmkalingcpepleiadaghfvqefgeqvar
ealkhfaete
>d1ede__ 3.59.1.6.1 Haloalkane dehalogenase {Xanthobacter autotrophicus}
minairtpdqrfsnldqypfspnylddlpgypglrahyldegnsdaedvflclhgeptws
ylyrkmipvfaesgarviapdffgfgksdkpvdeedytfefhrnfllalierldlrnitl
vvqdwggflgltlpmadpsrfkrliimnaclmtdpvtqpafsafvtqpadgftawkydlv
tpsdlrldqfmkrwaptlteaeasayaapfpdtsyqagvrkfpkmvaqrdqacidistea
isfwqndwngqtfmaigmkdkllgpdvmypmkalingcpepleiadaghfvqefgeqvar
ealkhfaete
>d1edg__ 3.1.7.3.3 Endoglucanase CelA {Clostridium cellulolyticum}
mydaslipnlqipqknipnndgmnfvkglrlgwnlgntfdafngtnitneldyetswsgi
kttkqmidaikqkgfntvripvswhphvsgsdykisdvwmnrvqevvnycidnkmyviln
thhdvdkvkgyfpssqymasskkyitsvwaqiaarfanydehlifegmneprlvghanew
wpeltnsdvvdsincinqlnqdfvntvratggknasrylmcpgyvaspdgatndyfrmpn
disgnnnkiivsvhaycpwnfaglamadggtnawnindskdqsevtwfmdniynkytsrg
ipviigecgavdknnlktrveymsyyvaqakargilcilwdnnnfsgtgelfgffdrrsc
qfkfpeiidgmvkyafglin
>d1edha_ 2.1.6.1.2 E-CADHERIN DOMAINS 1 AND 2 {Mouse (Mus musculus)}
vippiscpenekgefpknlvqiksnrdketkvfysitgqgadkppvgvfiieretgwlkv
tqpldreaiakyilyshavssngeavedpmeivitvtdqndnrpeftqevfegsvaegav
pgtsvmkvsatdadddvntynaaiaytivsqdpelphknmftvnrdtgvisvltsgldre
syptytlvvqaadlqgeglsttakavitvkd
>d1edhb_ 2.1.6.1.2 E-CADHERIN DOMAINS 1 AND 2 {Mouse (Mus musculus)}
vippiscpenekgefpknlvqiksnrdketkvfysitgqgadkppvgvfiieretgwlkv
tqpldreaiakyilyshavssngeavedpmeivitvtdqndnrpeftqevfegsvaegav
pgtsvmkvsatdadddvntynaaiaytivsqdpelphknmftvnrdtgvisvltsgldre
syptytlvvqaadlqgeglsttakavitvkd
>d1edi__ 1.8.1.1.1 Immunoglobulin-binding protein A modules {Staphylococcus aureus}
aqhdeaqqnafyqvlnmpnlnadqrngfiqslkddpsqsanvlgeaqklndsqapk
>d1edj__ 1.8.1.1.1 Immunoglobulin-binding protein A modules {Staphylococcus aureus}
aqhdeaqqnafyqvlnmpnlnadqrngfiqslkddpsqsanvlgeaqklndsqapk
>d1edk__ 1.8.1.1.1 Immunoglobulin-binding protein A modules {Staphylococcus aureus}
aqhdeaqqnafyqvlnmpnlnadqrngfiqslkddpsqsanvlgeaqklndsqapk
>d1edl__ 1.8.1.1.1 Immunoglobulin-binding protein A modules {Staphylococcus aureus}
aqhdeaqqnafyqvlnmpnlnadqrngfiqslkddpsqsanvlgeaqklndsqapk
>d1edmb_ 7.3.11.1.1 Factor IX (IXa) {Human (Homo sapiens)}
vdgdqcesnpclnggsckddinsyecwcpfgfegkncel
>d1edmc_ 7.3.11.1.1 Factor IX (IXa) {Human (Homo sapiens)}
vdgdqcesnpclnggsckddinsyecwcpfgfegkncel
>d1edt__ 3.1.7.5.5 Endo-beta-N-acetylglucosaminidase {Streptomyces plicatus, endoglycosidase H}
kqgptsvayvevnnnsmlnvgkytladgggnafdvavifaaninydtgtktaylhfnenv
qrvldnavtqirplqqqgikvllsvlgnhqgagfanfpsqqaasafakqlsdavakygld
gvdfddeyaeygnngtaqpndssfvhlvtalranmpdkiislynigpaasrlsyggvdvs
dkfdyawnpyygtwqvpgialpkaqlspaaveigrtsrstvadlarrtvdegygvyltyn
ldggdrtadvsaftrelygseavrt
>d1eea__ 3.59.1.1.2 Acetylcholinesterase {Electric eel (Electrophorus electricus)}
sellvntksgkvmgtrvpvlsshisaflgipfaeppvgnmrfrrpepkkpwsgvwnasty
pnncqqyvdeqfpgfsgsemwnpnremsedclylniwvpsprpksttvmvwiygggfysg
sstldvyngkylayteevvlvslsyrvgafgflalhgsqeapgnvglldqrmalqwvhdn
iqffggdpktvtifgesaggasvgmhilspgsrdlfrrailqsgspncpwasvsvaegrr
ravelgrnlncnlnsdeelihclrekkpqelidvewnvlpfdsifrfsfvpvidgeffpt
slesmlnsgnfkktqillgvnkdegsffllygapgfskdseskisredfmsgvklsvpha
ndlgldavtlqytdwmddnngiknrdglddivgdhnvicplmhfvnkytkfgngtylyff
nhrasnlvwpewmgvihgyeiefvfglplvkelnytaeeealsrrimhywatfaktgnpn
ephsqeskwplfttkeqkfidlntepmkvhqrlrvqmcvfwnqflpkllna
>d1eedp_ 2.44.1.2.1 Endothiapepsin {Chestnut blight fungus (Endothia parasitica)}
stgsatttpidslddayitpvqigtpaqtlnldfdtgssdlwvfssettasevdgqtiyt
psksttakllsgatwsisygdgssssgdvytdtvsvggltvtgqavesakkvsssfteds
tidgllglafstlntvsptqqktffdnakasldspvftadlgyhapgtynfgfidttayt
gsitytavstkqgfwewtstgyavgsgtfkstsidgiadtgttllylpatvvsaywaqvs
gakssssvggyvfpcsatlpsftfgvgsarivipgdyidfgpistgssscfggiqssagi
ginifgdvalkaafvvfngattptlgfask
>d1eera_ 1.27.1.2.1 Erythropoietin {Human (Homo sapiens)}
apprlicdsrvlerylleakeaekittgcaehcslnekitvpdtkvnfyawkrmevgqqa
vevwqglallseavlrgqallvkssqpweplqlhvdkavsglrslttllralgaqkeais
nsdaasaaplrtitadtfrklfrvysnflrgklklytgeacrtgdr
>d1eerb1 2.1.2.1.9 (8-116) Erythropoietin (EPO) receptor {Human (Homo sapiens)}
dpkfeskaallaargpeellcfterledlvcfweeaasagvgpgqysfsyqledepwklc
rlhqaptargavrfwcslptadtssfvplelrvtaasgapryhrvihin
>d1eerb2 2.1.2.1.9 (117-220) Erythropoietin (EPO) receptor {Human (Homo sapiens)}
evvlldapvglvarladesghvvlrwlpppetpmtshiryevdvsagqgagsvqrveile
grtecvlsnlrgrtrytfavrarmaepsfggfwsewsepvsllt
>d1eerc1 2.1.2.1.9 (8-116) Erythropoietin (EPO) receptor {Human (Homo sapiens)}
dpkfeskaallaargpeellcfterledlvcfweeaasagvgpgqysfsyqledepwklc
rlhqaptargavrfwcslptadtssfvplelrvtaasgapryhrvihin
>d1eerc2 2.1.2.1.9 (117-220) Erythropoietin (EPO) receptor {Human (Homo sapiens)}
evvlldapvglvarladesghvvlrwlpppetpmtshiryevdvsagqgagsvqrveile
grtecvlsnlrgrtrytfavrarmaepsfggfwsewsepvsllt
>d1efca1 2.38.3.1.1 (205-296) Elongation factor Tu (EF-Tu), domain 2 {Escherichia coli}
aidkpfllpiedvfsisgrgtvvtgrvergiikvgeeveivgiketqkstctgvemfrkl
ldegragenvgvllrgikreeiergqvlakpg
>d1efca2 2.39.1.1.1 (297-393) Elongation factor Tu (EF-Tu), C-terminal domain {Escherichia coli}
tikphtkfesevyilskdeggrhtpffkgyrpqfyfrttdvtgtielpegvemvmpgdni
kmvvtlihpiamddglrfaireggrtvgagvvakvls
>d1efca3 3.30.1.6.14 (8-204) Elongation factor Tu (EF-Tu), N-terminal (G) domain {Escherichia coli}
tkphvnvgtighvdhgkttltaaittvlaktyggaarafdqidnapeekargitintshv
eydtptrhyahvdcpghadyvknmitgaaqmdgailvvaatdgpmpqtrehillgrqvgv
pyiivflnkcdmvddeellelvemevrellsqydfpgddtpivrgsalkalegdaeweak
ilelagfldsyipeper
>d1efcb1 2.38.3.1.1 (205-296) Elongation factor Tu (EF-Tu), domain 2 {Escherichia coli}
aidkpfllpiedvfsisgrgtvvtgrvergiikvgeeveivgiketqkstctgvemfrkl
ldegragenvgvllrgikreeiergqvlakpg
>d1efcb2 2.39.1.1.1 (297-393) Elongation factor Tu (EF-Tu), C-terminal domain {Escherichia coli}
tikphtkfesevyilskdeggrhtpffkgyrpqfyfrttdvtgtielpegvemvmpgdni
kmvvtlihpiamddglrfaireggrtvgagvvakvls
>d1efcb3 3.30.1.6.14 (8-204) Elongation factor Tu (EF-Tu), N-terminal (G) domain {Escherichia coli}
tkphvnvgtighvdhgkttltaaittvlaktyggaarafdqidnapeekargitintshv
eydtptrhyahvdcpghadyvknmitgaaqmdgailvvaatdgpmpqtrehillgrqvgv
pyiivflnkcdmvddeellelvemevrellsqydfpgddtpivrgsalkalegdaeweak
ilelagfldsyipeper
>d1efga1 2.38.3.1.5 (283-403) Elongation factor G (EF-G), domain II {Thermus thermophilus}
pldippikgttpegevveihpdpngplaalafkimadpyvgrltfirvysgtltsgsyvy
nttkgrkervarllrmhanhreeveelkagdlgavvglketitgdtlvgedaprvilesi
e
>d1efga2 3.30.1.6.18 (1-282) Elongation factor G (EF-G), N-terminal (G) domain {Thermus thermophilus}
mavkveydlkrlrnigiaahidagktttterilyytgrihkigevhegaatmdfmeqere
rgititaavttcfwkdhriniidtpghvdftieversmrvldgaivvfdssqgvepqset
vwrqaekykvpriafankmdktgadlwlvirtmqerlgarpvvmqlpigredtfsgiidv
lrmkaytygndlgtdireipipeeyldnareyheklvevaadfdenimlkylegeeptee
elvaairkgtidlkitpvflgsalknkgvqllldavvdylps
>d1efga3 4.12.1.1.1 (477-599) Elongation factor G (EF-G), domain IV {Thermus thermophilus}
gkpqvayretitkpvdvegkfirqtggrgqyghvkikveplprgsgfefvnaivggvipk
eyipavqkgieeamqsgpligfpvvdikvtlydgsyhevdssemafkiagsmaikeavqk
gdp
>d1efga4 4.47.11.1.1 (600-689) Elongation factor G (EF-G), domain V {Thermus thermophilus}
vilepimrvevttpeeymgdvigdlnarrgqilgmeprgnaqvirafvplaemfgyatdl
rsktqgrgsfvmffdhyqevpkqvqeklik
>d1efm__ 3.30.1.6.14 Elongation factor Tu (EF-Tu), N-terminal (G) domain {Escherichia coli}
vnvgtighvdhgkttltaaittvlaktyggaarxxxxxxxxxxxxxxgitintshveydt
ptrhyahvdcpghadyvknmitgaaqmdgailvvaatdgpmpqtrehillgrqvgvpyii
vflnkcdmvddeellelvemevrellsqydfpgddtpivrgsalkalegdaeweakile
>d1efna_ 2.30.2.1.2 Fyn proto-oncogene tyrosine kinase, SH3 domain {Human (Homo sapiens)}
alfvalydyeaiteddlsfhkgekfqilnssegdwwearslttgetgyipsnyvapv
>d1efnb_ 4.80.1.1.1 Regulatory factor Nef {Human immunodeficiency virus, type 1, HIV-1}
rpqvplrpmtykaavdlshflkekggleglihsqrrqdildlwiyhtqgyfpdwqnytpg
pgvrypltfgwcyklvpvepdkveeankgentsllhpvslhgmddperevlewrfdsrla
fhhvarelhpeyf
>d1efnc_ 2.30.2.1.2 Fyn proto-oncogene tyrosine kinase, SH3 domain {Human (Homo sapiens)}
alfvalydyeaiteddlsfhkgekfqilnssegdwwearslttgetgyipsnyvapv
>d1efnd_ 4.80.1.1.1 Regulatory factor Nef {Human immunodeficiency virus, type 1, HIV-1}
rpqvplrpmtykaavdlshflkekggleglihsqrrqdildlwiyhtqgyfpdwqnytpg
pgvrypltfgwcyklvpvepdkveeankgentsllhpvslhgmddperevlewrfdsrla
fhhvarelhpeyf
>d1efpa1 3.23.1.1.2 (2-184) Electron transfer flavoprotein, ETFP {Paracoccus denitrificans}
avlllgevtngalnrdatakavaavkalgdvtvlcagasakaaaeeaakiagvakvlvae
dalyghrlaeptaalivglagdyshiaapattdaknvmprvaalldvmvlsdvsaildad
tferpiyagnaiqvvkskdakkvftirtasfdaageggtapvtetaaaadpglsswvade
vae
>d1efpa2 3.25.1.2.2 (185-308) C-terminal domain of the electron transfer flavoprotein alpha subunit {Paracoccus denitrificans}
sdrpeltsarrvvsggrglgskesfaiieeladklgaavgasraavdsgyapndwqvgqt
gkvvapelyvavgisgaiqhlagmkdskvivainkdeeapifqiadyglvgdlfsvvpel
tgkl
>d1efpb1 3.23.1.1.2 Electron transfer flavoprotein, ETFP {Paracoccus denitrificans}
mkvlvpvkrlidynvkarvksdgsgvdlanvkmsmnpfdeiaveeairlkekgqaeeiia
vsigvkqaaetlrtalamgadrailvvaaddvqqdieplavakilaavaraegteliiag
kqaidndmnatgqmlaailgwaqatfaskveiegakakvtrevdgglqtiavslpavvta
dlrlnepryaslpnimkakkkpldektaadygvdvaprlevvsvrepegrkagikvgsvd
elvgkl
>d1efpc1 3.23.1.1.2 (2-184) Electron transfer flavoprotein, ETFP {Paracoccus denitrificans}
avlllgevtngalnrdatakavaavkalgdvtvlcagasakaaaeeaakiagvakvlvae
dalyghrlaeptaalivglagdyshiaapattdaknvmprvaalldvmvlsdvsaildad
tferpiyagnaiqvvkskdakkvftirtasfdaageggtapvtetaaaadpglsswvade
vae
>d1efpc2 3.25.1.2.2 (185-308) C-terminal domain of the electron transfer flavoprotein alpha subunit {Paracoccus denitrificans}
sdrpeltsarrvvsggrglgskesfaiieeladklgaavgasraavdsgyapndwqvgqt
gkvvapelyvavgisgaiqhlagmkdskvivainkdeeapifqiadyglvgdlfsvvpel
tgkl
>d1efpd1 3.23.1.1.2 Electron transfer flavoprotein, ETFP {Paracoccus denitrificans}
mkvlvpvkrlidynvkarvksdgsgvdlanvkmsmnpfdeiaveeairlkekgqaeeiia
vsigvkqaaetlrtalamgadrailvvaaddvqqdieplavakilaavaraegteliiag
kqaidndmnatgqmlaailgwaqatfaskveiegakakvtrevdgglqtiavslpavvta
dlrlnepryaslpnimkakkkpldektaadygvdvaprlevvsvrepegrkagikvgsvd
elvgkl
>d1efra1 1.70.1.1.1 (380-510) C-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
tramkqvagtmklelaqyrevaafaqfgsdldaatqqllsrgvrltellkqgqyspmaie
eqvaviyagvrgyldklepskitkfenaflshvisqhqallgkirtdgkiseesdaklke
ivtnflagfea
>d1efra2 2.43.1.1.1 (24-94) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
dleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgndklik
egdivkrtgai
>d1efra3 3.30.1.9.2 (95-379) Central domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
vdvpvgeellgrvvdalgnaidgkgpigskarrrvglkapgiiprisvrepmqtgikavd
slvpigrgqreliigdrqtgktsiaidtiinqkrfndgtdekkklyciyvaigqkrstva
qlvkrltdadamkytivvsatasdaaplqylapysgcsmgeyfrdngkhaliiyddlskq
avayrqmslllrrppgreaypgdvfylhsrlleraakmndafgggsltalpvietqagdv
sayiptnvisitdgqifletelfykgirpainvglsvsrvgsaaq
>d1efrb1 1.70.1.1.1 (380-510) C-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
tramkqvagtmklelaqyrevaafaqfgsdldaatqqllsrgvrltellkqgqyspmaie
eqvaviyagvrgyldklepskitkfenaflshvisqhqallgkirtdgkiseesdaklke
ivtnflagfea
>d1efrb2 2.43.1.1.1 (24-94) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
dleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgndklik
egdivkrtgai
>d1efrb3 3.30.1.9.2 (95-379) Central domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
vdvpvgeellgrvvdalgnaidgkgpigskarrrvglkapgiiprisvrepmqtgikavd
slvpigrgqreliigdrqtgktsiaidtiinqkrfndgtdekkklyciyvaigqkrstva
qlvkrltdadamkytivvsatasdaaplqylapysgcsmgeyfrdngkhaliiyddlskq
avayrqmslllrrppgreaypgdvfylhsrlleraakmndafgggsltalpvietqagdv
sayiptnvisitdgqifletelfykgirpainvglsvsrvgsaaq
>d1efrc1 1.70.1.1.1 (380-510) C-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
tramkqvagtmklelaqyrevaafaqfgsdldaatqqllsrgvrltellkqgqyspmaie
eqvaviyagvrgyldklepskitkfenaflshvisqhqallgkirtdgkiseesdaklke
ivtnflagfea
>d1efrc2 2.43.1.1.1 (19-94) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
adtsvdleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgn
dklikegdivkrtgai
>d1efrc3 3.30.1.9.2 (95-379) Central domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
vdvpvgeellgrvvdalgnaidgkgpigskarrrvglkapgiiprisvrepmqtgikavd
slvpigrgqreliigdrqtgktsiaidtiinqkrfndgtdekkklyciyvaigqkrstva
qlvkrltdadamkytivvsatasdaaplqylapysgcsmgeyfrdngkhaliiyddlskq
avayrqmslllrrppgreaypgdvfylhsrlleraakmndafgggsltalpvietqagdv
sayiptnvisitdgqifletelfykgirpainvglsvsrvgsaaq
>d1efrd1 1.70.1.1.1 (358-475) C-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
mdpnivgsehydvargvqkilqdykslqdiiailgmdelseedkltvsrarkiqrflsqp
fqvaevftghlgklvplketikgfqqilageydhlpeqafymvgpieeavakadklae
>d1efrd2 2.43.1.1.1 (9-81) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1efrd3 3.30.1.9.2 (82-357) Central domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
iripvgpetlgrimnvigepidergpiktkqfaaihaeapefvemsveqeilvtgikvvd
llapyakggkiglfggagvgktvlimelinnvakahggysvfagvgertregndlyhemi
esgvinlkdatskvalvygqmneppgararvaltgltvaeyfrdqegqdvllfidnifrf
tqagsevsallgripsavgyqptlatdmgtmqeritttkkgsitsvqaiyvpaddltdpa
pattfahldattvlsraiaelgiypavdpldstsri
>d1efre1 1.70.1.1.1 (358-474) C-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
mdpnivgsehydvargvqkilqdykslqdiiailgmdelseedkltvsrarkiqrflsqp
fqvaevftghlgklvplketikgfqqilageydhlpeqafymvgpieeavakadkla
>d1efre2 2.43.1.1.1 (9-81) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1efre3 3.30.1.9.2 (82-357) Central domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
iripvgpetlgrimnvigepidergpiktkqfaaihaeapefvemsveqeilvtgikvvd
llapyakggkiglfggagvgktvlimelinnvakahggysvfagvgertregndlyhemi
esgvinlkdatskvalvygqmneppgararvaltgltvaeyfrdqegqdvllfidnifrf
tqagsevsallgripsavgyqptlatdmgtmqeritttkkgsitsvqaiyvpaddltdpa
pattfahldattvlsraiaelgiypavdpldstsri
>d1efrf1 1.70.1.1.1 (358-474) C-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
mdpnivgsehydvargvqkilqdykslqdiiailgmdelseedkltvsrarkiqrflsqp
fqvaevftghlgklvplketikgfqqilageydhlpeqafymvgpieeavakadkla
>d1efrf2 2.43.1.1.1 (9-81) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1efrf3 3.30.1.9.2 (82-357) Central domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
iripvgpetlgrimnvigepidergpiktkqfaaihaeapefvemsveqeilvtgikvvd
llapyakggkiglfggagvgktvlimelinnvakahggysvfagvgertregndlyhemi
esgvinlkdatskvalvygqmneppgararvaltgltvaeyfrdqegqdvllfidnifrf
tqagsevsallgripsavgyqptlatdmgtmqeritttkkgsitsvqaiyvpaddltdpa
pattfahldattvlsraiaelgiypavdpldstsri
>d1efrg_ 1.20.1.1.1 ATP syntase (F1-ATPase), gamma subunit {Bovine (Bos taurus)}
atlkditrrlksikniqkitksmkmvaaakyaraerelkparvygvgslalyekadiktp
edkkkhliigvssdrglcgaihssvakqmkseaanlaaagkevkiigvgdkirsilhrth
sdqflvtfkevgrrpptfgdasvialellnsgyefdegsiifnrfrsvisykteekpifs
ldtissaesmsiyddidadvlrnyqeyslaniiyyslkesttseqsarmtamdnasknas
emidkltltfnrtrqavitkelieiisgaaal
>d1eft_1 2.38.3.1.2 (213-312) Elongation factor Tu (EF-Tu), domain 2 {Thermus aquaticus}
pvrdvdkpflmpvedvftitgrgtvatgriergkvkvgdeveivglapetrktvvtgvem
hrktlqegiagdnvglllrgvsreevergqvlakpgsitp
>d1eft_2 2.39.1.1.2 (313-405) Elongation factor Tu (EF-Tu), C-terminal domain {Thermus aquaticus}
htkfeasvyvlkkeeggrhtgffsgyrpqfyfrttdvtgvvrlpqgvemvmpgdnvtftv
elikpvaleeglrfaireggrtvgagvvtkile
>d1eft_3 3.30.1.6.15 (1-212) Elongation factor Tu (EF-Tu), N-terminal (G) domain {Thermus aquaticus}
akgefirtkphvnvgtighvdhgkttltaaltfvtaaenpnvevkdygdidkapeerarg
itintahveyetakrhyshvdcpghadyiknmitgaaqmdgailvvsaadgpmpqtrehi
llarqvgvpyivvfmnkvdmvddpelldlvemevrdllnqyefpgdevpvirgsallale
emhknpktkrgenewvdkiwelldaideyipt
>d1efua1 2.38.3.1.1 (205-296) Elongation factor Tu (EF-Tu), domain 2 {Escherichia coli}
aidkpfllpiedvfsisgrgtvvtgrvergiikvgeeveivgiketqkstctgvemfrkl
ldegragenvgvllrgikreeiergqvlakpg
>d1efua2 2.39.1.1.1 (297-393) Elongation factor Tu (EF-Tu), C-terminal domain {Escherichia coli}
tikphtkfesevyilskdeggrhtpffkgyrpqfyfrttdvtgtielpegvemvmpgdni
kmvvtlihpiamddglrfaireggrtvgagvvakvls
>d1efua3 3.30.1.6.14 (9-204) Elongation factor Tu (EF-Tu), N-terminal (G) domain {Escherichia coli}
kphvnvgtighvdhgkttltaaittvlaktyggaarafdqidnapeekargitintshve
ydtptrhyahvdcpghadyvknmitgaaqmdgailvvaatdgpmpqtrehillgrqvgvp
yiivflnkcdmvddeellelvemevrellsqydfpgddtpivrgsalkalegdaeweaki
lelagfldsyipeper
>d1efub1 4.36.1.1.1 (1-139) Elongation factor Ts (EF-Ts), dimerisation domain {Escherichia coli}
aeitaslvkelrertgagmmdckkalteangdielaienmrksgaikaakkagnvaadgv
iktkidgnygiilevncqtdfvakdagfqafadkvldaavagkitdvevlkaqfeeerva
lvakigeninirrvaaleg
>d1efub2 4.36.1.1.1 (140-282) Elongation factor Ts (EF-Ts), dimerisation domain {Escherichia coli}
dvlgsyqhgarigvlvaakgadeelvkhiamhvaaskpefikpedvsaevvekeyqvqld
iamqsgkpkeiaekmvegrmkkftgevsltgqpfvmepsktvgqllkehnaevtgfirfe
vgegiekvetdfaaevaamskqs
>d1efuc1 2.38.3.1.1 (205-296) Elongation factor Tu (EF-Tu), domain 2 {Escherichia coli}
aidkpfllpiedvfsisgrgtvvtgrvergiikvgeeveivgiketqkstctgvemfrkl
ldegragenvgvllrgikreeiergqvlakpg
>d1efuc2 2.39.1.1.1 (297-393) Elongation factor Tu (EF-Tu), C-terminal domain {Escherichia coli}
tikphtkfesevyilskdeggrhtpffkgyrpqfyfrttdvtgtielpegvemvmpgdni
kmvvtlihpiamddglrfaireggrtvgagvvakvls
>d1efuc3 3.30.1.6.14 (9-204) Elongation factor Tu (EF-Tu), N-terminal (G) domain {Escherichia coli}
kphvnvgtighvdhgkttltaaittvlaktyggaarafdqidnapeekargitintshve
ydtptrhyahvdcpghadyvknmitgaaqmdgailvvaatdgpmpqtrehillgrqvgvp
yiivflnkcdmvddeellelvemevrellsqydfpgddtpivrgsalkalegdaeweaki
lelagfldsyipeper
>d1efud1 4.36.1.1.1 (1-139) Elongation factor Ts (EF-Ts), dimerisation domain {Escherichia coli}
aeitaslvkelrertgagmmdckkalteangdielaienmrksgaikaakkagnvaadgv
iktkidgnygiilevncqtdfvakdagfqafadkvldaavagkitdvevlkaqfeeerva
lvakigeninirrvaaleg
>d1efud2 4.36.1.1.1 (140-282) Elongation factor Ts (EF-Ts), dimerisation domain {Escherichia coli}
dvlgsyqhgarigvlvaakgadeelvkhiamhvaaskpefikpedvsaevvekeyqvqld
iamqsgkpkeiaekmvegrmkkftgevsltgqpfvmepsktvgqllkehnaevtgfirfe
vgegiekvetdfaaevaamskqs
>d1efva1 3.23.1.1.1 (20-207) Electron transfer flavoprotein, ETFP {Human (Homo sapiens)}
qstlviaehandslapitlntitaatrlggevsclvagtkcdkvaqdlckvagiakvlva
qhdvykgllpeeltplilatqkqfnythicagasafgknllprvaaklevapisdiiaik
spdtfvrtiyagnalctvkcdekvkvfsvrgtsfdaaatsggsassekasstspveisew
ldqkltks
>d1efva2 3.25.1.2.1 (208-331) C-terminal domain of the electron transfer flavoprotein alpha subunit {Human (Homo sapiens)}
drpeltgakvvvsggrglksgenfkllydladqlhaavgasraavdagfvpndmqvgqtg
kivapelyiavgisgaiqhlagmkdsktivainkdpeapifqvadygivadlfkvvpemt
eilk
>d1efvb1 3.23.1.1.1 Electron transfer flavoprotein, ETFP {Human (Homo sapiens)}
lrvlvavkrvidyavkirvkpdrtgvvtdgvkhsmnpfceiaveeavrlkekklvkevia
vscgpaqcqetirtalamgadrgihvevppaeaerlgplqvarvlaklaekekvdlvllg
kqaidddcnqtgqmtagfldwpqgtfasqvtlegdklkvereidggletlrlklpavvta
dlrlnepryatlpnimkakkkkievikpgdlgvdltsklsvisvedppqrtagvkvette
dlvaklkeigri
>d1eg1a_ 2.26.1.9.2 Endoglucanase I {Trichoderma reesei}
qpgtstpevhpklttykctksggcvaqdtsvvldwnyrwmhdanynsctvnggvnttlcp
deatcgkncfiegvdyaasgvttsgssltmnqympsssggyssvsprlylldsdgeyvml
klngqelsfdvdlsalpcgengslylsqmdengganqyntaganygsgycdaqcpvqtwr
ngtlntshqgfccnemdilegnsranaltphsctatacdsagcgfnpygsgyksyygpgd
tvdtsktftiitqfntdngspsgnlvsitrkyqqngvdipsaqpggdtisscpsasaygg
latmgkalssgmvlvfsiwndnsqymnwldsgnagpcsstegnpsnilannpnthvvfsn
irwgdigstt
>d1eg1c_ 2.26.1.9.2 Endoglucanase I {Trichoderma reesei}
qpgtstpevhpklttykctksggcvaqdtsvvldwnyrwmhdanynsctvnggvnttlcp
deatcgkncfiegvdyaasgvttsgssltmnqympsssggyssvsprlylldsdgeyvml
klngqelsfdvdlsalpcgengslylsqmdengganqyntaganygsgycdaqcpvqtwr
ngtlntshqgfccnemdilegnsranaltphsctatacdsagcgfnpygsgyksyygpgd
tvdtsktftiitqfntdngspsgnlvsitrkyqqngvdipsaqpggdtisscpsasaygg
latmgkalssgmvlvfsiwndnsqymnwldsgnagpcsstegnpsnilannpnthvvfsn
irwgdigstt
>d1egaa1 3.30.1.6.19 (4-182) GTPase Era N-terminal domain {Escherichia coli}
dksycgfiaivgrpnvgkstllnkllgqkisitsrkaqttrhrivgihtegayqaiyvdt
pglhmeekrainrlmnkaasssigdvelvifvvegtrwtpddemvlnklregkapvilav
nkvdnvqekadllphlqflasqmnfldivpisaetglnvdtiaaivrkhlpeathhfpe
>d1egaa2 4.43.3.1.1 (183-295) GTPase Era C-terminal domain {Escherichia coli}
dyitdrsqrfmaseiireklmrflgaelpysvtveierfvsnerggydinglilveregq
kkmvignkgakiktigiearkdmqemfeapvhlelwvkvksgwadderalrsl
>d1egab1 3.30.1.6.19 (4-182) GTPase Era N-terminal domain {Escherichia coli}
dksycgfiaivgrpnvgkstllnkllgqkisitsrkaqttrhrivgihtegayqaiyvdt
pglhmeekrainrlmnkaasssigdvelvifvvegtrwtpddemvlnklregkapvilav
nkvdnvqekadllphlqflasqmnfldivpisaetglnvdtiaaivrkhlpeathhfpe
>d1egab2 4.43.3.1.1 (183-296) GTPase Era C-terminal domain {Escherichia coli}
dyitdrsqrfmaseiireklmrflgaelpysvtveierfvsnerggydinglilveregq
kkmvignkgakiktigiearkdmqemfeapvhlelwvkvksgwadderalrslg
>d1egca1 1.25.6.1.3 (242-396) Medium chain acyl-CoA dehydrogenase {Human (Homo sapiens)}
gagfkvamgafdkerpvvaagavglaqraldeatkyalerktfgkllvehqaisfmlaem
amkvelarmsyqraawevdsgrrntyyasiakafagdianqlatdavqilggngfnteyp
veklmrdakiyqiyggtsqiqrlivarehidkykn
>d1egca2 5.6.1.1.3 (10-241) Medium chain acyl-CoA dehydrogenase {Human (Homo sapiens)}
lgfsfefteqqkefqatarkfareeiipvaaeydktgeypvplirrawelglmnthipen
cgglglgtfdacliseelaygctgvqtaiegnslgqmpiiiagndqqkkkylgrmteepl
mcaycvtepgagsdvagiktkaekkgdeyiingqkmwitnggkanwyfllarsdpdpkap
ankaftgfiveadtpgiqigrkelnmgqrcsdtrgivfedvkvpkenvligd
>d1egcb1 1.25.6.1.3 (242-396) Medium chain acyl-CoA dehydrogenase {Human (Homo sapiens)}
gagfkvamgafdkerpvvaagavglaqraldeatkyalerktfgkllvehqaisfmlaem
amkvelarmsyqraawevdsgrrntyyasiakafagdianqlatdavqilggngfnteyp
veklmrdakiyqiyggtsqiqrlivarehidkykn
>d1egcb2 5.6.1.1.3 (10-241) Medium chain acyl-CoA dehydrogenase {Human (Homo sapiens)}
lgfsfefteqqkefqatarkfareeiipvaaeydktgeypvplirrawelglmnthipen
cgglglgtfdacliseelaygctgvqtaiegnslgqmpiiiagndqqkkkylgrmteepl
mcaycvtepgagsdvagiktkaekkgdeyiingqkmwitnggkanwyfllarsdpdpkap
ankaftgfiveadtpgiqigrkelnmgqrcsdtrgivfedvkvpkenvligd
>d1egcc1 1.25.6.1.3 (242-396) Medium chain acyl-CoA dehydrogenase {Human (Homo sapiens)}
gagfkvamgafdkerpvvaagavglaqraldeatkyalerktfgkllvehqaisfmlaem
amkvelarmsyqraawevdsgrrntyyasiakafagdianqlatdavqilggngfnteyp
veklmrdakiyqiyggtsqiqrlivarehidkykn
>d1egcc2 5.6.1.1.3 (10-241) Medium chain acyl-CoA dehydrogenase {Human (Homo sapiens)}
lgfsfefteqqkefqatarkfareeiipvaaeydktgeypvplirrawelglmnthipen
cgglglgtfdacliseelaygctgvqtaiegnslgqmpiiiagndqqkkkylgrmteepl
mcaycvtepgagsdvagiktkaekkgdeyiingqkmwitnggkanwyfllarsdpdpkap
ankaftgfiveadtpgiqigrkelnmgqrcsdtrgivfedvkvpkenvligd
>d1egcd1 1.25.6.1.3 (242-396) Medium chain acyl-CoA dehydrogenase {Human (Homo sapiens)}
gagfkvamgafdkerpvvaagavglaqraldeatkyalerktfgkllvehqaisfmlaem
amkvelarmsyqraawevdsgrrntyyasiakafagdianqlatdavqilggngfnteyp
veklmrdakiyqiyggtsqiqrlivarehidkykn
>d1egcd2 5.6.1.1.3 (10-241) Medium chain acyl-CoA dehydrogenase {Human (Homo sapiens)}
lgfsfefteqqkefqatarkfareeiipvaaeydktgeypvplirrawelglmnthipen
cgglglgtfdacliseelaygctgvqtaiegnslgqmpiiiagndqqkkkylgrmteepl
mcaycvtepgagsdvagiktkaekkgdeyiingqkmwitnggkanwyfllarsdpdpkap
ankaftgfiveadtpgiqigrkelnmgqrcsdtrgivfedvkvpkenvligd
>d1egda1 1.25.6.1.3 (242-396) Medium chain acyl-CoA dehydrogenase {Human (Homo sapiens)}
gagfkvamgafdkerpvvaagavglaqraldeatkyalerktfgkllvehqaisfmlaem
amkvelarmsyqraawevdsgrrntyyasiakafagdianqlatdavqilggngfnteyp
veklmrdakiyqiyggtsqiqrlivarehidkykn
>d1egda2 5.6.1.1.3 (10-241) Medium chain acyl-CoA dehydrogenase {Human (Homo sapiens)}
lgfsfefteqqkefqatarkfareeiipvaaeydktgeypvplirrawelglmnthipen
cgglglgtfdacliseelaygctgvqtaiegnslgqmpiiiagndqqkkkylgrmteepl
mcaycvtepgagsdvagiktkaekkgdeyiingqkmwitnggkanwyfllarsdpdpkap
ankaftgfiveadtpgiqigrkelnmgqrcsdtrgivfedvkvpkenvligd
>d1egdb1 1.25.6.1.3 (242-396) Medium chain acyl-CoA dehydrogenase {Human (Homo sapiens)}
gagfkvamgafdkerpvvaagavglaqraldeatkyalerktfgkllvehqaisfmlaem
amkvelarmsyqraawevdsgrrntyyasiakafagdianqlatdavqilggngfnteyp
veklmrdakiyqiyggtsqiqrlivarehidkykn
>d1egdb2 5.6.1.1.3 (10-241) Medium chain acyl-CoA dehydrogenase {Human (Homo sapiens)}
lgfsfefteqqkefqatarkfareeiipvaaeydktgeypvplirrawelglmnthipen
cgglglgtfdacliseelaygctgvqtaiegnslgqmpiiiagndqqkkkylgrmteepl
mcaycvtepgagsdvagiktkaekkgdeyiingqkmwitnggkanwyfllarsdpdpkap
ankaftgfiveadtpgiqigrkelnmgqrcsdtrgivfedvkvpkenvligd
>d1egdc1 1.25.6.1.3 (242-396) Medium chain acyl-CoA dehydrogenase {Human (Homo sapiens)}
gagfkvamgafdkerpvvaagavglaqraldeatkyalerktfgkllvehqaisfmlaem
amkvelarmsyqraawevdsgrrntyyasiakafagdianqlatdavqilggngfnteyp
veklmrdakiyqiyggtsqiqrlivarehidkykn
>d1egdc2 5.6.1.1.3 (10-241) Medium chain acyl-CoA dehydrogenase {Human (Homo sapiens)}
lgfsfefteqqkefqatarkfareeiipvaaeydktgeypvplirrawelglmnthipen
cgglglgtfdacliseelaygctgvqtaiegnslgqmpiiiagndqqkkkylgrmteepl
mcaycvtepgagsdvagiktkaekkgdeyiingqkmwitnggkanwyfllarsdpdpkap
ankaftgfiveadtpgiqigrkelnmgqrcsdtrgivfedvkvpkenvligd
>d1egdd1 1.25.6.1.3 (242-396) Medium chain acyl-CoA dehydrogenase {Human (Homo sapiens)}
gagfkvamgafdkerpvvaagavglaqraldeatkyalerktfgkllvehqaisfmlaem
amkvelarmsyqraawevdsgrrntyyasiakafagdianqlatdavqilggngfnteyp
veklmrdakiyqiyggtsqiqrlivarehidkykn
>d1egdd2 5.6.1.1.3 (10-241) Medium chain acyl-CoA dehydrogenase {Human (Homo sapiens)}
lgfsfefteqqkefqatarkfareeiipvaaeydktgeypvplirrawelglmnthipen
cgglglgtfdacliseelaygctgvqtaiegnslgqmpiiiagndqqkkkylgrmteepl
mcaycvtepgagsdvagiktkaekkgdeyiingqkmwitnggkanwyfllarsdpdpkap
ankaftgfiveadtpgiqigrkelnmgqrcsdtrgivfedvkvpkenvligd
>d1egea1 1.25.6.1.3 (242-396) Medium chain acyl-CoA dehydrogenase {Human (Homo sapiens)}
gagfkvamgafdktrpvvaagavglaqraldeatkyalerktfgkllvehqaisfmlaem
amkvelarmsyqraawevdsgrrntyyasiakafagdianqlatdavqilggngfnteyp
veklmrdakiyqiyegtsqiqrlivarehidkykn
>d1egea2 5.6.1.1.3 (10-241) Medium chain acyl-CoA dehydrogenase {Human (Homo sapiens)}
lgfsfefteqqkefqatarkfareeiipvaaeydktgeypvplirrawelglmnthipen
cgglglgtfdacliseelaygctgvqtaiegnslgqmpiiiagndqqkkkylgrmteepl
mcaycvtepgagsdvagiktkaekkgdeyiingqkmwitnggkanwyfllarsdpdpkap
ankaftgfiveadtpgiqigrkelnmgqrcsdtrgivfedvkvpkenvligd
>d1egeb1 1.25.6.1.3 (242-396) Medium chain acyl-CoA dehydrogenase {Human (Homo sapiens)}
gagfkvamgafdktrpvvaagavglaqraldeatkyalerktfgkllvehqaisfmlaem
amkvelarmsyqraawevdsgrrntyyasiakafagdianqlatdavqilggngfnteyp
veklmrdakiyqiyegtsqiqrlivarehidkykn
>d1egeb2 5.6.1.1.3 (10-241) Medium chain acyl-CoA dehydrogenase {Human (Homo sapiens)}
lgfsfefteqqkefqatarkfareeiipvaaeydktgeypvplirrawelglmnthipen
cgglglgtfdacliseelaygctgvqtaiegnslgqmpiiiagndqqkkkylgrmteepl
mcaycvtepgagsdvagiktkaekkgdeyiingqkmwitnggkanwyfllarsdpdpkap
ankaftgfiveadtpgiqigrkelnmgqrcsdtrgivfedvkvpkenvligd
>d1egec1 1.25.6.1.3 (242-396) Medium chain acyl-CoA dehydrogenase {Human (Homo sapiens)}
gagfkvamgafdktrpvvaagavglaqraldeatkyalerktfgkllvehqaisfmlaem
amkvelarmsyqraawevdsgrrntyyasiakafagdianqlatdavqilggngfnteyp
veklmrdakiyqiyegtsqiqrlivarehidkykn
>d1egec2 5.6.1.1.3 (10-241) Medium chain acyl-CoA dehydrogenase {Human (Homo sapiens)}
lgfsfefteqqkefqatarkfareeiipvaaeydktgeypvplirrawelglmnthipen
cgglglgtfdacliseelaygctgvqtaiegnslgqmpiiiagndqqkkkylgrmteepl
mcaycvtepgagsdvagiktkaekkgdeyiingqkmwitnggkanwyfllarsdpdpkap
ankaftgfiveadtpgiqigrkelnmgqrcsdtrgivfedvkvpkenvligd
>d1eged1 1.25.6.1.3 (242-396) Medium chain acyl-CoA dehydrogenase {Human (Homo sapiens)}
gagfkvamgafdktrpvvaagavglaqraldeatkyalerktfgkllvehqaisfmlaem
amkvelarmsyqraawevdsgrrntyyasiakafagdianqlatdavqilggngfnteyp
veklmrdakiyqiyegtsqiqrlivarehidkykn
>d1eged2 5.6.1.1.3 (10-241) Medium chain acyl-CoA dehydrogenase {Human (Homo sapiens)}
lgfsfefteqqkefqatarkfareeiipvaaeydktgeypvplirrawelglmnthipen
cgglglgtfdacliseelaygctgvqtaiegnslgqmpiiiagndqqkkkylgrmteepl
mcaycvtepgagsdvagiktkaekkgdeyiingqkmwitnggkanwyfllarsdpdpkap
ankaftgfiveadtpgiqigrkelnmgqrcsdtrgivfedvkvpkenvligd
>d1egf__ 7.3.11.1.12 Epidermal growth factor, EGF {Mouse (Mus musculus)}
nsypgcpssydgyclnggvcmhiesldsytcncvigysgdrcqtrdlrwwelr
>d1egl__ 4.33.1.1.1 Eglin C {Leech (Hirudo medicinalis)}
tefgselksfpevvgktvdqareyftlhypqydvyflpegspvtldlrynrvrvfynpgt
nvvnhvphvg
>d1ego__ 3.38.1.1.6 Glutaredoxin {Bacteriophage T4}
mqtvifgrsgcpycvrakdlaeklsnerddfqyqyvdiraegitkedlqqkagkpvetvp
qifvdqqhiggytdfaawvkenlda
>e1egp.1a 4.33.1.1.1 Eglin C {Leech (Hirudo medicinalis)}
lksfpevvgktvdqareyftlhypqynvyflpegspvtl
>e1egp.1b 4.33.1.1.1 Eglin C {Leech (Hirudo medicinalis)}
ynrvrvfynpgtnvvnhvphvg
>d1egr__ 3.38.1.1.6 Glutaredoxin {Bacteriophage T4}
mqtvifgrsgcpycvrakdlaeklsnerddfqyqyvdiraegitkedlqqkagkpvetvp
qifvdqqhiggytdfaawvkenlda
>d1egza_ 3.1.7.3.8 Endoglucanase Cel5a {Erwinia chrysanthemi}
sveplsvngnkiyagekaksfagnslfwsnngwggekfytadtvaslkkdwkssivraam
gvqesggylqdpagnkakvervvdaaiandmyaiigwhshsaennrseairffqemarky
gnkpnviyeiyneplqvswsntikpyaeavisairaidpdnliivgtpswsqnvdeasrd
pinakniaytlhfyagthgeslrnkarqalnngialfvtewgtvnadgnggvnqtetdaw
vtfmrdnnisnanwalndknegastyypdsknltesgkkvksiiqswpyka
>d1egzb_ 3.1.7.3.8 Endoglucanase Cel5a {Erwinia chrysanthemi}
sveplsvngnkiyagekaksfagnslfwsnngwggekfytadtvaslkkdwkssivraam
gvqesggylqdpagnkakvervvdaaiandmyaiigwhshsaennrseairffqemarky
gnkpnviyeiyneplqvswsntikpyaeavisairaidpdnliivgtpswsqnvdeasrd
pinakniaytlhfyagthgeslrnkarqalnngialfvtewgtvnadgnggvnqtetdaw
vtfmrdnnisnanwalndknegastyypdsknltesgkkvksiiqswpyka
>d1egzc_ 3.1.7.3.8 Endoglucanase Cel5a {Erwinia chrysanthemi}
sveplsvngnkiyagekaksfagnslfwsnngwggekfytadtvaslkkdwkssivraam
gvqesggylqdpagnkakvervvdaaiandmyaiigwhshsaennrseairffqemarky
gnkpnviyeiyneplqvswsntikpyaeavisairaidpdnliivgtpswsqnvdeasrd
pinakniaytlhfyagthgeslrnkarqalnngialfvtewgtvnadgnggvnqtetdaw
vtfmrdnnisnanwalndknegastyypdsknltesgkkvksiiqswpyka
>d1eh2__ 1.42.1.6.1 Eps15 {Human (Homo sapiens)}
pwavkpedkakydaifdslspvngflsgdkvkpvllnsklpvdilgrvwelsdidhdgml
drdefavamflvycalekepvpmslppalvppskr
>d1ehc__ 3.16.2.1.1 CheY protein {Escherichia coli}
adkelkflvvdkfstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmp
nmdglellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleekln
kifeklgm
>d1ehs__ 7.2.1.1.1 Heat-stable enterotoxin B {Escherichia coli}
stqsnkkdlcehyrqiakesckkgflgvrdgtagacfgaqimvaakgc
>d1ehya_ 3.59.1.9.1 Epoxide hydrolase {(Agrobacterium radiobacter)}
airrpedfkhyevqlpdvkihyvregagptllllhgwpgfwwewskvigplaehydvivp
dlrgfgdsekpdlndlskysldkaaddqaalldalgiekayvvghdfaaivlhkfirkys
drvikaaifdpiqpdfgpvyfglghvheswysqfhqldmavevvgssrevckkyfkhffd
hwsyrdellteeelevhvdncmkpdnihggfnyyranirpdaalwtdldhtmsdlpvtmi
wglgdtcvpyapliefvpkyysnytmetiedcghflmvekpeiaidriktafr
>d1ehyb_ 3.59.1.9.1 Epoxide hydrolase {(Agrobacterium radiobacter)}
airrpedfkhyevqlpdvkihyvregagptllllhgwpgfwwewskvigplaehydvivp
dlrgfgdsekpdlndlskysldkaaddqaalldalgiekayvvghdfaaivlhkfirkys
drvikaaifdpiqpdfgpvyfglghvheswysqfhqldmavevvgssrevckkyfkhffd
hwsyrdellteeelevhvdncmkpdnihggfnyyranirpdaalwtdldhtmsdlpvtmi
wglgdtcvpyapliefvpkyysnytmetiedcghflmvekpeiaidriktafr
>d1ehyc_ 3.59.1.9.1 Epoxide hydrolase {(Agrobacterium radiobacter)}
airrpedfkhyevqlpdvkihyvregagptllllhgwpgfwwewskvigplaehydvivp
dlrgfgdsekpdlndlskysldkaaddqaalldalgiekayvvghdfaaivlhkfirkys
drvikaaifdpiqpdfgpvyfglghvheswysqfhqldmavevvgssrevckkyfkhffd
hwsyrdellteeelevhvdncmkpdnihggfnyyranirpdaalwtdldhtmsdlpvtmi
wglgdtcvpyapliefvpkyysnytmetiedcghflmvekpeiaidriktafr
>d1ehyd_ 3.59.1.9.1 Epoxide hydrolase {(Agrobacterium radiobacter)}
airrpedfkhyevqlpdvkihyvregagptllllhgwpgfwwewskvigplaehydvivp
dlrgfgdsekpdlndlskysldkaaddqaalldalgiekayvvghdfaaivlhkfirkys
drvikaaifdpiqpdfgpvyfglghvheswysqfhqldmavevvgssrevckkyfkhffd
hwsyrdellteeelevhvdncmkpdnihggfnyyranirpdaalwtdldhtmsdlpvtmi
wglgdtcvpyapliefvpkyysnytmetiedcghflmvekpeiaidriktafr
>d1eia_1 1.29.3.1.1 (148-222) EIAV capsid protein p26 {Equine infectious anemia virus, EIAV}
pkaqnirqgakepypefvdrllsqikseghpqeiskfltdtltiqnaneecrnamrhlrp
edtleekmyacrdig
>d1eia_2 1.72.1.1.2 (16-147) EIAV capsid protein p26 {Equine infectious anemia virus, EIAV}
tprgyttwvntiqtngllneasqnlfgilsvdctseemnafldvvpgqagqkqilldaid
kiaddwdnrhplpnaplvappqgpipmtarfirglgvprerqmepafdqfrqtyrqwiie
amsegikvmigk
>d1eif_1 2.30.7.1.1 (4-73) N-terminal domain of eukaryotic initiation translation factor 5a {Methanococcus jannaschii}
mpgtkqvnvgslkvgqyvmidgvpceivdisvskpgkhggakarvvgigifekvkkefva
ptsskvevpi
>d1eif_2 2.35.4.5.6 (74-133) C-terminal domain of eukaryotic initiation translation factor 5a {Methanococcus jannaschii}
idrrkgqvlaimgdmvqimdlqtyetlelpipegieglepggeveyieavgqykitrvig
>d1eit__ 7.3.6.2.2 mu-Agatoxin-I {Funnel web spider (Agelenopsis aperta)}
ecvpenghcrdwydeccegfycscrqppkcicrnnn
>d1ekbb_ 2.41.1.2.17 Enteropeptidase (enterokinase light chain) {Bovine (Bos taurus)}
ivggsdsregawpwvvalyfddqqvcgaslvsrdwlvsaahcvygrnmepskwkavlglh
masnltspqietrlidqivinphynkrrknndiammhlemkvnytdyiqpiclpeenqvf
ppgricsiagwgaliyqgstadvlqeadvpllsnekcqqqmpeynitenmvcagyeaggv
dscqgdsggplmcqennrwllagvtsfgyqcalpnrpgvyarvprftewiqsflh
>d1ekla_ 2.75.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
anqasvvanqlipintaltlvmmrsevvtpvgipakdiprlvsmqvnravplgttlmpdm
vkgyaa
>d1elaa_ 2.41.1.2.15 Elastase {Porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1elba_ 2.41.1.2.15 Elastase {Porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1elca_ 2.41.1.2.15 Elastase {Porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1elde_ 2.41.1.2.15 Elastase {Porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1elee_ 2.41.1.2.15 Elastase {Porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1elf__ 2.41.1.2.15 Elastase {Porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1elg__ 2.41.1.2.15 Elastase {Porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1elo_1 2.38.3.1.5 (283-399) Elongation factor G (EF-G), domain II {Thermus thermophilus}
pldippikgttpegevveihpdpngplaalafkimadpyvgrltfirvysgtltsgsyvy
nttkgrkervarllrmhanhreeveelkagdlgavvglketitgdtlvgedaprvil
>d1elo_2 3.30.1.6.18 (5-282) Elongation factor G (EF-G), N-terminal (G) domain {Thermus thermophilus}
veydlkrlrnigiaahidagktttterilyytgrihkigevhegaatmdfmeqerergit
itaavttcfwkdhriniidtpghvdftieversmrvldgaivvfdssqgvepqsetvwrq
aekykvpriafankmdktgadlwlvirtmqerlgarpvvmqlpigredtfsgiidvlrmk
aytygndlgtdireipipeeyldqareyheklvevaadfdenimlkylegeepteeelva
airkgtidlkitpvflgsalknkgvqllldavvdylps
>d1elo_3 4.12.1.1.1 (476-599) Elongation factor G (EF-G), domain IV {Thermus thermophilus}
vgkpqvayretitkpvdvegkfirqtggrgqyghvkikveplprgsgfefvnaivggvip
keyipavqkgieeamqsgpligfpvvdikvtlydgsyhevdssemafkiagsmaikeavq
kgdp
>d1elo_4 4.47.11.1.1 (600-689) Elongation factor G (EF-G), domain V {Thermus thermophilus}
vilepimrvevttpeeymgdvigdlnarrgqilgmeprgnaqvirafvplaemfgyatdl
rsktqgrgsfvmffdhyqevpkqvqeklik
>d1elpa1 2.10.1.1.2 (1-85) gamma-Crystallin {Bovine (Bos taurus), isoform IIIb (D)}
gkitfyedrgfqgrhyecssdhsnlqpylgrcnsvrvdsgcwmiyeqpnylgpqyflrrg
dypdyqqwmglndsirscrliphag
>d1elpa2 2.10.1.1.2 (87-174) gamma-Crystallin {Bovine (Bos taurus), isoform IIIb (D)}
shrlrlyeredyrgqmieitedcsslqdrfhfneihslnvlegswvlyelpnyrgrqyll
rpgeyrryhdwgamnakvgslrrvidiy
>d1elpb1 2.10.1.1.2 (1-85) gamma-Crystallin {Bovine (Bos taurus), isoform IIIb (D)}
gkitfyedrgfqgrhyecssdhsnlqpylgrcnsvrvdsgcwmiyeqpnylgpqyflrrg
dypdyqqwmglndsirscrliphag
>d1elpb2 2.10.1.1.2 (87-174) gamma-Crystallin {Bovine (Bos taurus), isoform IIIb (D)}
shrlrlyeredyrgqmieitedcsslqdrfhfneihslnvlegswvlyelpnyrgrqyll
rpgeyrryhdwgamnakvgslrrvidiy
>d1els_1 3.1.10.1.1 (142-436) Enolase {Baker's yeast (Saccharomyces cerevisiae)}
spyvlpvpflnvlnggshaggalalqefmiaptgaktfaealrigsevyhnlksltkkry
gasagnvgdeggvapniqtaeealdlivdaikaaghdgkvkigldcasseffkdgkydld
fknpnsdkskwltgpqladlyhslmkrypivsiedpfaeddweawshffktagiqivadd
ltvtnpkriataiekkaadalllkvnqigtlsesikaaqdsfaagwgvmvshrsgetedt
fiadlvvglrtgqiktgaparserlaklnqllrieeelgdnavfagenfhhgdkl
>d1els_2 4.44.1.1.1 (1-141) Enolase {Baker's yeast (Saccharomyces cerevisiae)}
avskvyarsvydsrgnptvevelttekgvfrsivpsgastgvhealemrdgdkskwmgkg
vlhavknvndviapafvkanidvsdqkavddflisldgtanksklganailgvslaasra
aaaeknvplykhladlskskt
>d1elt__ 2.41.1.2.16 Elastase {Salmon (Salmo salar)}
vvggrvaqpnswpwqislqyksgssyyhtcggslirqgwvmtaahcvdsartwrvvlgeh
nlntnegkeqimtvnsvfihsgwnsddvaggydiallrlntqaslnsavqlaalppsnqi
lpnnnpcyitgwgktstggplsdslkqawlpsvdhatcsssgwwgstvkttmvcagggan
sgcngdsggplncqvngsyyvhgvtsfvsssgcnaskkptvftrvsayiswmngim
>d1elxa_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdaaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1elxb_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdaaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1elya_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdcaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1elyb_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdcaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1elza_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdgaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1elzb_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdgaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1ema__ 4.20.1.1.1 Green fluorescent protein, GFP {Jellyfish (Aequorea victoria)}
skgeelftgvvpilveldgdvnghkfsvsgegegdatygkltlkficttgklpvpwptlv
ttfxvqcfsrypdhxkrhdffksaxpegyvqertiffkddgnyktraevkfegdtlvnri
elkgidfkedgnilghkleynynshnvyixadkqkngikvnfkirhniedgsvqladhyq
qntpigdgpvllpdnhylstqsalskdpnekrdhxvllefvtaagi
>d1emb__ 4.20.1.1.1 Green fluorescent protein, GFP {Jellyfish (Aequorea victoria)}
skgeelftgvvpilveldgdvnghkfsvsgegegdatygkltlkficttgklpvpwptlv
ttfxvqcfsrypdhmkrhdffksampegyvqertiffkddgnyktraevkfegdtlvnri
elkgidfkedgnilghkleynynshnvyimadkqkngikvnfkirhniedgsvqladhyq
qntpigdgpvllpdnhylstqsalskdpnekrdhmvllefvtaagi
>d1emca_ 4.20.1.1.1 Green fluorescent protein, GFP {Jellyfish (Aequorea victoria)}
geelftgvvpilveldgdvnghkfsvsgegegdatygkltlkficttgklpvpwptlvtt
lxvqcfsrypdhmkrhdffksampegyvqertiffkddgnyktraevkfegdtlvnriel
kgidfkedgnilghkleynynshnvyimadkqkngikvnfktrhniedgsvqladhyqqn
tpigdgpvllpdnhylstqsalskdpnekrdhmvllefvtaagit
>d1emcb_ 4.20.1.1.1 Green fluorescent protein, GFP {Jellyfish (Aequorea victoria)}
geelftgvvpilveldgdvnghkfsvsgegegdatygkltlkficttgklpvpwptlvtt
lxvqcfsrypdhmkrhdffksampegyvqertiffkddgnyktraevkfegdtlvnriel
kgidfkedgnilghkleynynshnvyimadkqkngikvnfktrhniedgsvqladhyqqn
tpigdgpvllpdnhylstqsalskdpnekrdhmvllefvtaagit
>d1emcc_ 4.20.1.1.1 Green fluorescent protein, GFP {Jellyfish (Aequorea victoria)}
geelftgvvpilveldgdvnghkfsvsgegegdatygkltlkficttgklpvpwptlvtt
lxvqcfsrypdhmkrhdffksampegyvqertiffkddgnyktraevkfegdtlvnriel
kgidfkedgnilghkleynynshnvyimadkqkngikvnfktrhniedgsvqladhyqqn
tpigdgpvllpdnhylstqsalskdpnekrdhmvllefvtaagith
>d1emcd_ 4.20.1.1.1 Green fluorescent protein, GFP {Jellyfish (Aequorea victoria)}
geelftgvvpilveldgdvnghkfsvsgegegdatygkltlkficttgklpvpwptlvtt
lxvqcfsrypdhmkrhdffksampegyvqertiffkddgnyktraevkfegdtlvnriel
kgidfkedgnilghkleynynshnvyimadkqkngikvnfktrhniedgsvqladhyqqn
tpigdgpvllpdnhylstqsalskdpnekrdhmvllefvtaagit
>d1emd_1 3.2.1.5.3 (1-145) Malate dehydrogenase {Escherichia coli}
mkvavlgaaggigqalalllktqlpsgselslydiapvtpgvavdlshiptavkikgfsg
edatpalegadvvlisagvrrkpgmdrsdlfnvnagivknlvqqvaktcpkacigiitnp
vnttvaiaaevlkkagvydknklfg
>d1emd_2 4.132.1.1.3 (146-312) Malate dehydrogenase {Escherichia coli}
vttldiirsntfvaelkgkqpgevevpvigghsgvtilpllsqvpgvsfteqevadltkr
iqnagtevveakagggsatlsmgqaaarfglslvralqgeqgvvecayvegdgqyarffs
qplllgkngveerksigtlsafeqnalegmldtlkkdialgqefvnk
>d1eme__ 4.20.1.1.1 Green fluorescent protein, GFP {Jellyfish (Aequorea victoria)}
elftgvvpilveldgdvnghkfsvsgegegdatygkltlkficttgklpvpwptlvttlx
vqcfsrypdhmkrhdffksampegyvqertiffkddgnyktraevkfegdtlvnrielkg
idfkedgnilghkleynynshnvyimadkqkngikvnfktrhniedgsvqladhyqqntp
igdgpvllpdnhylstqsalskdpnekrdhmvllefvtaagit
>d1emf__ 4.20.1.1.1 Green fluorescent protein, GFP {Jellyfish (Aequorea victoria)}
elftgvvpilveldgdvnghkfsvsgegegdatygkltlkficttgklpvpwptlvttlx
vqcfsrypdhmkrhdffksampegyvqertiffkddgnyktraevkfegdtlvnrielkg
idfkedgnilghkleynynshnvyimadkqkngikanfkirhniedgsvqladhyqqntp
igdgpvllpdnhylstqsalskdpnekrdhmvllefvtaagit
>d1emga_ 4.20.1.1.1 Green fluorescent protein, GFP {Jellyfish (Aequorea victoria)}
skgeelftgvvpilveldgdvnghkfsvsgegegdatygkltlkficttgklpvpwptlv
ttfxvqcfsrypdhmkrhdffksampegyvqertiffkddgnyktraevkfegdtlvnri
elkgidfkedgnilghkleynynshnvyimadkqkngikvnfkirhniedgsvqladhyq
qntpigdgpvllpdnhylstqsalskdpnekrdhmvllefvtaagi
>d1emk__ 4.20.1.1.1 Green fluorescent protein, GFP {Jellyfish (Aequorea victoria)}
elftgvvpilveldgdvnghkfsvsgegegdatygkltlkficttgklpvpwptlvttlx
vqcfsrypdhmkrhdffksampegyvqertiffkddgnyktraevkfegdtlvnrielkg
idfkedgnilghkleynynshnvyimadkqkngikvnfktrhniedgsvqladhyqqntp
igdgpvllpdnhylstqsalskdpnekrdhmvllefvtaagi
>d1eml__ 4.20.1.1.1 Green fluorescent protein, GFP {Jellyfish (Aequorea victoria)}
lftgvvpilveldgdvnghkfsvsgegegdatygkltlkficttgklpvpwptlvttlxv
qcfsrypdhmkrhdffksampegyvqertiffkddgnyktraevkfegdtlvnrielkgi
dfkedgnilghkleynynshnvyimadkqkngikvnfktrhniedgsvqladhyqqntpi
gdgpvllpdnhylstqsalskdpnekrdhmvllefvtaagi
>d1emm__ 4.20.1.1.1 Green fluorescent protein, GFP {Jellyfish (Aequorea victoria)}
lftgvvpilveldgdvnghkfsvsgegegdatygkltlkficttgklpvpwptlvttlxv
qcfsrypdhmkrhdffksampegyvqertiffkddgnyktraevkfegdtlvnrielkgi
dfkedgnilghkleynynshnvyimadkqkngikvnfkirhniedgsvqladhyqqntpi
gdgpvllpdnhylstqsalskdpnekrdhmvllefvtaagi
>d1emn_1 7.3.11.1.18 (2124-2166) Fibrillin-1 fragment (residues 2124-2205) {Human (Homo sapiens)}
savdmdeckepdvckhgqcintdgsyrcecpfgyilagnecvd
>d1emn_2 7.3.11.1.18 (2167-2205) Fibrillin-1 fragment (residues 2124-2205) {Human (Homo sapiens)}
tdecsvgnpcgngtcknviggfectceegfepgpmmtce
>d1emo_1 7.3.11.1.18 (2124-2166) Fibrillin-1 fragment (residues 2124-2205) {Human (Homo sapiens)}
savdmdeckepdvckhgqcintdgsyrcecpfgyilagnecvd
>d1emo_2 7.3.11.1.18 (2167-2205) Fibrillin-1 fragment (residues 2124-2205) {Human (Homo sapiens)}
tdecsvgnpcgngtcknviggfectceegfepgpmmtce
>d1emy__ 1.1.1.1.10 Myoglobin {Asian elephant (Elephas maximus)}
glsdgewelvlktwgkveadipghgetvfvrlftghpetlekfdkfkhlktegemkased
lkkqgvtvltalggilkkkghheaeiqplaqshatkhkipikylefisdaiihvlqskhp
aefgadaqgamkkalelfrndiaakykelgfqg
>d1ena__ 2.35.1.1.1 Staphylococcal nuclease {Staphylococcus aureus}
lhkepatlikaidgetvklmykgqpmtfrlllvdtpetkhpkkgvekygpeasaftkkmv
enakkievefdkgqrtdkygrglayiyadgkmvnealvrqglakvayvykpnntheqhlr
kseaqakkeklniws
>d1enc__ 2.35.1.1.1 Staphylococcal nuclease {Staphylococcus aureus}
lhkepatlikaidgetvklmykgqpmtfrlllvdtpetkhpkkgvekygpeasaftkkmv
enakkievefdkgqrtdkygrglayiyadgkmvnealvrqglakvayvykpnntheqhlr
kseaqakkeklniws
>d1enh__ 1.4.1.1.1 Engrailed Homeodomain {Drosophila melanogaster}
rprtafsseqlarlkrefnenrylterrrqqlsselglneaqikiwfqnkraki
>d1eni__ 1.18.1.1.1 T4 endonuclease V {bacteriophage T4, (Escherichia coli)}
tqinltlvseladqhlmaeyrelprvfgavrkhvangkrvrdfkisptfilgaghvtffy
dkleflrkrqieliaeclkrgfnikdttvqdisdipqefrgdyipheasiaisqarldek
iaqrptwykyygkaiya
>d1enj__ 1.18.1.1.1 T4 endonuclease V {bacteriophage T4, (Escherichia coli)}
trinltlvseladqhlmaeyrqlprvfgavrkhvangkrvrdfkisptfilgaghvtffy
dkleflrkrqieliaeclkrgfnikdttvqdisdipqefrgdyipheasiaisqarldek
iaqrptwykyygkaiya
>d1enk__ 1.18.1.1.1 T4 endonuclease V {bacteriophage T4, (Escherichia coli)}
trinltlvseladqhlmaeyrdlprvfgavrkhvangkrvrdfkisptfilgaghvtffy
dkleflrkrqieliaeclkrgfnikdttvqdisdipqefrgdyipheasiaisqarldek
iaqrptwykyygkaiya
>d1eno__ 3.2.1.2.13 Enoyl-ACP reductase {Oil seed rape (Brassica napus)}
lpidlrgkrafiagiaddngygwavakslaaagaeilvgtwvpalnifetslrrgkfdqs
rvlpdgslmeikkvypldavfdnpedvpedvkankryagssnwtvqeaaecvrqdfgsid
ilvhslangpevskplletsrkgylaaisassysfvsllshflpimnpggasisltyias
eriipgygggmssakaalesdtrvlafeagrkqnirvntisagplgsraakaigfidtmi
eysynnapiqktltadevgnaaaflvsplasaitgatiyvdnglnsmgvaldspvfk
>d1enp__ 3.2.1.2.13 Enoyl-ACP reductase {Oil seed rape (Brassica napus)}
lpidlrgkrafiagiaddngygwavakslaaagaeilvgtwvpalnifetslrrgkfdqs
rvlpdgslmeikkvypldavfdnpedvpedvkankryagssnwtvqeaaecvrqdfgsid
ilvhslangpevskplletsrkgylaaisassysfvsllshflpimnpggasisltyias
eriipgygggmssakaalesdtrvlafeagrkqnirvntisagplgsraakaigfidtmi
eysynnapiqktltadevgnaaaflvsplasaitgatiyvdnglnsmgvaldspvfk
>d1enqa_ 2.26.1.1.1 Concanavalin A {Jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1enqb_ 2.26.1.1.1 Concanavalin A {Jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1enqc_ 2.26.1.1.1 Concanavalin A {Jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1enqd_ 2.26.1.1.1 Concanavalin A {Jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1enr__ 2.26.1.1.1 Concanavalin A {Jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1ensa_ 2.26.1.1.1 Concanavalin A {Jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1ensb_ 2.26.1.1.1 Concanavalin A {Jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1ente_ 2.44.1.2.1 Endothiapepsin {Chestnut blight fungus (Endothia parasitica)}
stgsatttpidslddayitpvqigtpaqtlnldfdtgssdlwvfssettasevdgqtiyt
psksttakllsgatwsisygdgssssgdvytdtvsvggltvtgqavesakkvsssfteds
tidgllglafstlntvsptqqktffdnakasldspvftadlgyhapgtynfgfidttayt
gsitytavstkqgfwewtstgyavgsgtfkstsidgiadtgttllylpatvvsaywaqvs
gakssssvggyvfpcsatlpsftfgvgsarivipgdyidfgpistgssscfggiqssagi
ginifgdvalkaafvvfngattptlgfask
>d1enxa_ 2.26.1.10.5 Xylanase II {Trichoderma reesei, xynII}
xtiqpgtgynngyfysywndghggvtytngpggqfsvnwsnsgnfvggkgwqpgtknkvi
nfsgsynpngnsylsvygwsrnplieyyivenfgtynpstgatklgevtsdgsvydiyrt
qrvnqpsiigtatfyqywsvrrnhrssgsvntanhfnawaqqgltlgtmdyqivavegyf
ssgsasitvs
>d1enxb_ 2.26.1.10.5 Xylanase II {Trichoderma reesei, xynII}
xtiqpgtgynngyfysywndghggvtytngpggqfsvnwsnsgnfvggkgwqpgtknkvi
nfsgsynpngnsylsvygwsrnplieyyivenfgtynpstgatklgevtsdgsvydiyrt
qrvnqpsiigtatfyqywsvrrnhrssgsvntanhfnawaqqgltlgtmdyqivavegyf
ssgsasitvs
>d1eny__ 3.2.1.2.14 Enoyl-ACP reductase {Mycobacterium tuberculosis, TB, gene InhA}
aglldgkrilvsgiitdssiafhiarvaqeqgaqlvltgfdrlrliqritdrlpakapll
eldvqneehlaslagrvteaigagnkldgvvhsigfmpqtgmginpffdapyadvskgih
isaysyasmakallpimnpggsivgmdfdpsrampaynwmtvaksalesvnrfvareagk
ygvrsnlvaagpirtlamsaivggalgeeagaqiqlleegwdqrapigwnmkdatpvakt
vcallsdwlpattgdiiyadggahtqll
>d1enz__ 3.2.1.2.14 Enoyl-ACP reductase {Mycobacterium tuberculosis, TB, gene InhA}
aglldgkrilvsgiitdssiafhiarvaqeqgaqlvltgfdrlrliqritdrlpakapll
eldvqneehlaslagrvteaigagnkldgvvhaigfmpqtgmginpffdapyadvskgih
isaysyasmakallpimnpggsivgmdfdpsrampaynwmtvaksalesvnrfvareagk
ygvrsnlvaagpirtlamsaivggalgeeagaqiqlleegwdqrapigwnmkdatpvakt
vcallsdwlpattgdiiyadggahtqll
>d1eot__ 4.8.1.1.11 Eotaxin {Human (Homo sapiens)}
gpasvpttccfnlanrkiplqrlesyrritsgkcpqkavifktklakdicadpkkkwvqd
smkyldqksptpkp
>d1epaa_ 2.53.1.1.9 Retinoic acid-binding protein {Rat (Rattus norvegicus), albino}
vkdfdiskflgfwyeiafaskmgtpglahkeekmgamvvelkenllaltttyysedhcvl
ekvtategdgpakfqvtrlsgkkevvveatdyltyaiiditslvagavhrtmklysrsld
dngealynfrkitsdhgfsetdlyilkhdltcvkvlqsaa
>d1epab_ 2.53.1.1.9 Retinoic acid-binding protein {Rat (Rattus norvegicus), albino}
avvkdfdiskflgfwyeiafaskmgtpglahkeekmgamvvelkenllaltttyysedhc
vlekvtategdgpakfqvtrlsgkkevvveatdyltyaiiditslvagavhrtmklysrs
lddngealynfrkitsdhgfsetdlyilkhdltcvkvlqsaaes
>d1epba_ 2.53.1.1.9 Retinoic acid-binding protein {Rat (Rattus norvegicus), albino}
vkdfdiskflgfwyeiafaskmgtpglahkeekmgamvvelkenllaltttyysedhcvl
ekvtategdgpakfqvtrlsgkkevvveatdyltyaiiditslvagavhrtmklysrsld
dngealynfrkitsdhgfsetdlyilkhdltcvkvlqsaa
>d1epbb_ 2.53.1.1.9 Retinoic acid-binding protein {Rat (Rattus norvegicus), albino}
avvkdfdiskflgfwyeiafaskmgtpglahkeekmgamvvelkenllaltttyysedhc
vlekvtategdgpakfqvtrlsgkkevvveatdyltyaiiditslvagavhrtmklysrs
lddngealynfrkitsdhgfsetdlyilkhdltcvkvlqsaaes
>d1epg__ 7.3.11.1.12 Epidermal growth factor, EGF {Mouse (Mus musculus)}
nsypgcpssydgyclnggvcmhiesldsytcncvigysgdrcqtrdlrwwelr
>d1eph__ 7.3.11.1.12 Epidermal growth factor, EGF {Mouse (Mus musculus)}
nsypgcpssydgyclnggvcmhiesldsytcncvigysgdrcqtrdlrwwelr
>d1epi__ 7.3.11.1.12 Epidermal growth factor, EGF {Mouse (Mus musculus)}
nsypgcpssydgyclnggvcmhiesldsytcncvigysgdrcqtrdlrwwelr
>d1epj__ 7.3.11.1.12 Epidermal growth factor, EGF {Mouse (Mus musculus)}
nsypgcpssydgyclnggvcmhiesldsytcncvigysgdrcqtrdlrwwelr
>d1eple_ 2.44.1.2.1 Endothiapepsin {Chestnut blight fungus (Endothia parasitica)}
stgsatttpidslddayitpvqigtpaqtlnldfdtgssdlwvfssettasevdgqtiyt
psksttakllsgatwsisygdgssssgdvytdtvsvggltvtgqavesakkvsssfteds
tidgllglafstlntvsptqqktffdnakasldspvftadlgyhapgtynfgfidttayt
gsitytavstkqgfwewtstgyavgsgtfkstsidgiadtgttllylpatvvsaywaqvs
gakssssvggyvfpcsatlpsftfgvgsarivipgdyidfgpistgssscfggiqssagi
ginifgdvalkaafvvfngattptlgfask
>d1epme_ 2.44.1.2.1 Endothiapepsin {Chestnut blight fungus (Endothia parasitica)}
stgsatttpidslddayitpvqigtpaqtlnldfdtgssdlwvfssettasevdgqtiyt
psksttakllsgatwsisygdgssssgdvytdtvsvggltvtgqavesakkvsssfteds
tidgllglafstlntvsptqqktffdnakasldspvftadlgyhapgtynfgfidttayt
gsitytavstkqgfwewtstgyavgsgtfkstsidgiadtgttllylpatvvsaywaqvs
gakssssvggyvfpcsatlpsftfgvgsarivipgdyidfgpistgssscfggiqssagi
ginifgdvalkaafvvfngattptlgfask
>d1epne_ 2.44.1.2.1 Endothiapepsin {Chestnut blight fungus (Endothia parasitica)}
stgsatttpidslddayitpvqigtpaqtlnldfdtgssdlwvfssettasevdgqtiyt
psksttakllsgatwsisygdgssssgdvytdtvsvggltvtgqavesakkvsssfteds
tidgllglafstlntvsptqqktffdnakasldspvftadlgyhapgtynfgfidttayt
gsitytavstkqgfwewtstgyavgsgtfkstsidgiadtgttllylpatvvsaywaqvs
gakssssvggyvfpcsatlpsftfgvgsarivipgdyidfgpistgssscfggiqssagi
ginifgdvalkaafvvfngattptlgfask
>d1epoe_ 2.44.1.2.1 Endothiapepsin {Chestnut blight fungus (Endothia parasitica)}
stgsatttpidslddayitpvqigtpaqtlnldfdtgssdlwvfssettasevdgqtiyt
psksttakllsgatwsisygdgssssgdvytdtvsvggltvtgqavesakkvsssfteds
tidgllglafstlntvsptqqktffdnakasldspvftadlgyhapgtynfgfidttayt
gsitytavstkqgfwewtstgyavgsgtfkstsidgiadtgttllylpatvvsaywaqvs
gakssssvggyvfpcsatlpsftfgvgsarivipgdyidfgpistgssscfggiqssagi
ginifgdvalkaafvvfngattptlgfask
>d1eppe_ 2.44.1.2.1 Endothiapepsin {Chestnut blight fungus (Endothia parasitica)}
stgsatttpidslddayitpvqigtpaqtlnldfdtgssdlwvfssettasevdgqtiyt
psksttakllsgatwsisygdgssssgdvytdtvsvggltvtgqavesakkvsssfteds
tidgllglafstlntvsptqqktffdnakasldspvftadlgyhapgtynfgfidttayt
gsitytavstkqgfwewtstgyavgsgtfkstsidgiadtgttllylpatvvsaywaqvs
gakssssvggyvfpcsatlpsftfgvgsarivipgdyidfgpistgssscfggiqssagi
ginifgdvalkaafvvfngattptlgfask
>d1epqe_ 2.44.1.2.1 Endothiapepsin {Chestnut blight fungus (Endothia parasitica)}
stgsatttpidslddayitpvqigtpaqtlnldfdtgssdlwvfssettasevdgqtiyt
psksttakllsgatwsisygdgssssgdvytdtvsvggltvtgqavesakkvsssfteds
tidgllglafstlntvsptqqktffdnakasldspvftadlgyhapgtynfgfidttayt
gsitytavstkqgfwewtstgyavgsgtfkstsidgiadtgttllylpatvvsaywaqvs
gakssssvggyvfpcsatlpsftfgvgsarivipgdyidfgpistgssscfggiqssagi
ginifgdvalkaafvvfngattptlgfask
>d1epre_ 2.44.1.2.1 Endothiapepsin {Chestnut blight fungus (Endothia parasitica)}
stgsatttpidslddayitpvqigtpaqtlnldfdtgssdlwvfssettasevdgqtiyt
psksttakllsgatwsisygdgssssgdvytdtvsvggltvtgqavesakkvsssfteds
tidgllglafstlntvsptqqktffdnakasldspvftadlgyhapgtynfgfidttayt
gsitytavstkqgfwewtstgyavgsgtfkstsidgiadtgttllylpatvvsaywaqvs
gakssssvggyvfpcsatlpsftfgvgsarivipgdyidfgpistgssscfggiqssagi
ginifgdvalkaafvvfngattptlgfask
>d1eps__ 4.52.2.1.3 5-enol-pyruvyl shikimate-3-phosphate(EPSP) synthase {Escherichia coli}
mesltlqpiarvdgtinlpgsktvsnralllaalahgktvltnlldsddvrhmlnaltal
gvsytlsadrtrceiignggplhaegalelflgnagtamrplaaalclgsndivltgepr
mkerpighlvdalrlggakityleqenypplrlqggftggnvdvdgsvssqfltallmta
plapedtvirikgdlvskpyiditlnlmktfgveienqhyqqfvvkggqsyqspgtylve
gdassasyflaaaaikggtvkvtgigrnsmqgdirfadvlekmgaticwgddyisctrge
lnaidmdmnhipdaamtiataalfakgttrlrniynwrvketdrlfamatelrkvgaeve
eghdyiritppeklnfaeiatyndhrmamcfslvalsdtpvtildpkctaktfpdyfeql
arisqaa
>e1ept.1a 2.41.1.2.2 Trypsin(ogen) {Porcine (Sus scrofa)}
ivggytcaansipyqvslnsgshfcggslinsqwvvsaahcyk
>e1ept.1b 2.41.1.2.2 Trypsin(ogen) {Porcine (Sus scrofa)}
sriqvrlgehnidvlegneqfinaakiithpnfngntldndimliklsspatlnsrvatv
slprscaaagteclisgwgntk
>e1ept.1c 2.41.1.2.2 Trypsin(ogen) {Porcine (Sus scrofa)}
ssgssypsllqclkapvlsnssckssypgqitgnmicvgflqggkdscqgdsggpvvcng
qlqgivswgygcaqknkpgvytkvcnyvnwiqqtiaan
>d1eqa__ 3.56.1.4.1 Polymerase regulatory subunit VP39 {Vaccinia virus}
mdvvsldkpfmyfeeidneldyepesanevakklpyqgqlklllgelfflsklqrhgild
gatvvyigsapgthirylrdhfynlgviikwmlidgrhhdpilnglrdvtlvtrfvdeey
lrsikkqlhpskiilisdvrskrggnepstadllsnyalqnvmisilnpvasslkwrcpf
pdqwikdfyiphgnkmlqpfapsysaemrllsiytgenmrltrvtksdavnyqkkmyyln
kivrnkvvvnfdypnqeydyfhmyfmlrtvycnktfpttkakvlflqqsifrflnip
>d1equ__ 3.2.1.2.8 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvlevnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylahskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevf
>d1er8e_ 2.44.1.2.1 Endothiapepsin {Chestnut blight fungus (Endothia parasitica)}
stgsatttpidslddayitpvqigtpaqtlnldfdtgssdlwvfssettasevdgqtiyt
psksttakllsgatwsisygdgssssgdvytdtvsvggltvtgqavesakkvsssfteds
tidgllglafstlntvsptqqktffdnakasldspvftadlgyhapgtynfgfidttayt
gsitytavstkqgfwewtstgyavgsgtfkstsidgiadtgttllylpatvvsaywaqvs
gakssssvggyvfpcsatlpsftfgvgsarivipgdyidfgpistgssscfggiqssagi
ginifgdvalkaafvvfngattptlgfask
>d1era__ 7.7.1.1.1 Erabutoxin B (also neurotoxin B) {Sea snake (Laticauda semifasciata)}
ricfnhqssqpqttktcspgesscyhkqwsdfrgtiiergcgcptvkpgiklsccesevc
nn
>d1erb__ 2.53.1.1.1 Retinol binding protein {Bovine (Bos taurus)}
rdcrvssfrvkenfdkarfagtwyamakkdpeglflqdnivaefsvdenghmsatakgrv
rllnnwdvcadmvgtftdtedpakfkmkywgvasflqkgnddhwiidtdyetfavqyscr
llnldgtcadsysfvfardpsgfspevqkivrqrqeelclarqyrliphngycd
>d1erc__ 1.10.1.1.1 ER-1 {Euplotes raikovi}
daceqaaiqcvesaceslctegedrtgcymyiysncppyv
>d1erd__ 1.10.1.1.2 ER-2 {Euplotes raikovi}
dpmtceqamascehtmcgycqgplymtcigittdpecglp
>d1erea_ 1.114.1.1.4 Estrogen receptor alpha {Human (Homo sapiens)}
slalsltadqmvsalldaeppilyseydptrpfseasmmglltnladrelvhminwakrv
pgfvdltlhdqvhllecawleilmiglvwrsmehpgkllfapnllldrnqgkcvegmvei
fdmllatssrfrmmnlqgeefvclksiillnsgvytflsstlksleekdhihrvldkitd
tlihlmakagltlqqqhqrlaqlllilshirhmsnkgmehlysmkcknvvplydllleml
dahr
>d1ereb_ 1.114.1.1.4 Estrogen receptor alpha {Human (Homo sapiens)}
slalsltadqmvsalldaeppilyseydptrpfseasmmglltnladrelvhminwakrv
pgfvdltlhdqvhllecawleilmiglvwrsmehpgkllfapnllldrnqgkcvegmvei
fdmllatssrfrmmnlqgeefvclksiillnsgvytflsstlksleekdhihrvldkitd
tlihlmakagltlqqqhqrlaqlllilshirhmsnkgmehlysmkcknvvplydllleml
dahr
>d1erec_ 1.114.1.1.4 Estrogen receptor alpha {Human (Homo sapiens)}
slalsltadqmvsalldaeppilyseydptrpfseasmmglltnladrelvhminwakrv
pgfvdltlhdqvhllecawleilmiglvwrsmehpgkllfapnllldrnqgkcvegmvei
fdmllatssrfrmmnlqgeefvclksiillnsgvytflsstlksleekdhihrvldkitd
tlihlmakagltlqqqhqrlaqlllilshirhmsnkgmehlysmkcknvvplydllleml
dahr
>d1ered_ 1.114.1.1.4 Estrogen receptor alpha {Human (Homo sapiens)}
slalsltadqmvsalldaeppilyseydptrpfseasmmglltnladrelvhminwakrv
pgfvdltlhdqvhllecawleilmiglvwrsmehpgkllfapnllldrnqgkcvegmvei
fdmllatssrfrmmnlqgeefvclksiillnsgvytflsstlksleekdhihrvldkitd
tlihlmakagltlqqqhqrlaqlllilshirhmsnkgmehlysmkcknvvplydllleml
dahr
>d1eree_ 1.114.1.1.4 Estrogen receptor alpha {Human (Homo sapiens)}
slalsltadqmvsalldaeppilyseydptrpfseasmmglltnladrelvhminwakrv
pgfvdltlhdqvhllecawleilmiglvwrsmehpgkllfapnllldrnqgkcvegmvei
fdmllatssrfrmmnlqgeefvclksiillnsgvytflsstlksleekdhihrvldkitd
tlihlmakagltlqqqhqrlaqlllilshirhmsnkgmehlysmkcknvvplydllleml
dahr
>d1eref_ 1.114.1.1.4 Estrogen receptor alpha {Human (Homo sapiens)}
slalsltadqmvsalldaeppilyseydptrpfseasmmglltnladrelvhminwakrv
pgfvdltlhdqvhllecawleilmiglvwrsmehpgkllfapnllldrnqgkcvegmvei
fdmllatssrfrmmnlqgeefvclksiillnsgvytflsstlksleekdhihrvldkitd
tlihlmakagltlqqqhqrlaqlllilshirhmsnkgmehlysmkcknvvplydllleml
dahr
>d1erg__ 7.7.1.3.1 CD59, extracellular domain {Human (Homo sapiens)}
lqcyncpnptadcktavncssdfdaclitkaglqvynkcwkfehcnfndvttrlrenelt
yycckkdlcn
>d1erh__ 7.7.1.3.1 CD59, extracellular domain {Human (Homo sapiens)}
lqcyncpnptadcktavncssdfdaclitkaglqvynkcwkfehcnfndvttrlrenelt
yycckkdlcn
>d1eria_ 3.43.1.1.1 Restriction endonuclease EcoRI {Escherichia coli}
sqgvigifgdyakahdlavgevsklvkkalsneypqlsfryrdsikkteinealkkidpd
lggtlfvsnssikpdggivevkddygewrvvlvaeakhqgkdiinirngllvgkrgdqdl
maagnaiershkniseianfmlseshfpyvlflegsnfltenisitrpdgrvvnleynsg
ilnrldrltaanygmpinsnlcinkfvnhkdksimlqaasiytqgdgrewdskimfeimf
disttslrvlgrdlfeqltsk
>d1erk__ 4.117.1.1.14 MAP kinase Erk2 {Rat (Rattus norvegicus)}
aaaaaagpemvrgqvfdvgprytnlsyigegaygmvcsaydnlnkvrvaikkispfehqt
ycqrtlreikillrfrheniigindiiraptieqmkdvyivqdlmetdlykllktqhlsn
dhicyflyqilrglkyihsanvlhrdlkpsnlllnttcdlkicdfglarvadpdhdhtgf
lteyvatrwyrapeimlnskgytksidiwsvgcilaemlsnrpifpgkhyldqlnhilgi
lgspsqedlnciinlkarnyllslphknkvpwnrlfpnadskaldlldkmltfnphkrie
veqalahpyleqyydpsdepiaeapfkfdmelddlpkeklkelifeetarfqpgyrs
>d1erp__ 1.10.1.1.3 ER-10 {Euplotes raikovi}
dlceqsalqcneqgchnfcspedkpgclgmvwnpelcp
>d1erra_ 1.114.1.1.4 Estrogen receptor alpha {Human (Homo sapiens)}
alsltadqmvsalldaeppilyseydptrpfseasmmglltnladrelvhminwakrvpg
fvdltlhdqvhllecawleilmiglvwrsmehpgkllfapnllldrnqgkcvegmveifd
mllatssrfrmmnlqgeefvclksiillnsgvytflsstlksleekdhihrvldkitdtl
ihlmakagltlqqqhqrlaqlllilshirhmsnkgmehlysmkcknvvplydlllemlda
h
>d1errb_ 1.114.1.1.4 Estrogen receptor alpha {Human (Homo sapiens)}
lalsltadqmvsalldaeppilyseydptrpfseasmmglltnladrelvhminwakrvp
gfvdltlhdqvhllecawleilmiglvwrsmehpgkllfapnllldrnqgkcvegmveif
dmllatssrfrmmnlqgeefvclksiillnsgvytflsstlksleekdhihrvldkitdt
lihlmakagltlqqqhqrlaqlllilshirhmsnkgmehlysmkcknvvplydlllemld
ahrlha
>d1ert__ 3.38.1.1.4 Thioredoxin {Human (Homo sapiens)}
mvkqiesktafqealdaagdklvvvdfsatwcgpckmikpffhslsekysnviflevdvd
dcqdvasecevkcmptfqffkkgqkvgefsgankekleatinelv
>d1eru__ 3.38.1.1.4 Thioredoxin {Human (Homo sapiens)}
mvkqiesktafqealdaagdklvvvdfsatwcgpckmikpffhslsekysnviflevdvd
dcqdvasecevkcmptfqffkkgqkvgefsgankekleatinelv
>d1erv__ 3.38.1.1.4 Thioredoxin {Human (Homo sapiens)}
mvkqiesktafqealdaagdklvvvdfsatwcgpckmikpffhslsekysnviflevdvd
dcqdvasecevksmptfqffkkgqkvgefsgankekleatinelv
>d1erw__ 3.38.1.1.4 Thioredoxin {Human (Homo sapiens)}
mvkqiesktafqealdaagdklvvvdfsatwsgpskmikpffhslsekysnviflevdvd
dcqdvasecevkcmptfqffkkgqkvgefsgankekleatinelv
>d1ery__ 1.10.1.1.4 ER-11 {Euplotes raikovi}
decanaaaqcsitlcnlycgplieiceltvmqnceppfs
>d1esa__ 2.41.1.2.15 Elastase {Porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1esb__ 2.41.1.2.15 Elastase {Porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
a
>d1esc__ 3.16.8.1.1 Esterase {Streptomyces scabies}
dpvptvffgdsytanfgiapvtnqdsergwcfqakenypavatrsladkgitldvqadvs
cggalihhfwekqelpfgagelppqqdalkqdtqltvgslggntlgfnrilkqcsdelrk
psllpgdpvdgdepaakcgeffgtgdgkqwlddqfervgaeleelldrigyfapdakrvl
vgyprlvpedttkcltaapgqtqlpfadipqdalpvldqiqkrlndamkkaaadggadfv
dlyagtgantacdgadrgigglledsqlellgtkipwyahpndkgrdiqakqvadkieei
ln
>d1esd__ 3.16.8.1.1 Esterase {Streptomyces scabies}
dpvptvffgdsytanfgiapvtnqdsergwcfqakenypavatrsladkgitldvqadvs
cggalihhfwekqelpfgagelppqqdalkqdtqltvgslggntlgfnrilkqcsdelrk
psllpgdpvdgdepaakcgeffgtgdgkqwlddqfervgaeleelldrigyfapdakrvl
vgyprlvpedttkcltaapgqtqlpfadipqdalpvldqiqkrlndamkkaaadggadfv
dlyagtgantacdgadrgigglledsqlellgtkipwyahpndkgrdiqakqvadkieei
ln
>d1ese__ 3.16.8.1.1 Esterase {Streptomyces scabies}
dpvptvffgdsytanfgiapvtnqdsergwcfqakenypavatrsladkgitldvqadvs
cggalihhfwekqelpfgagelppqqdalkqdtqltvgslggntlgfnrilkqcsdelrk
psllpgdpvdgdepaakcgeffgtgdgkqwlddqfervgaeleelldrigyfapdakrvl
vgyprlvpedttkcltaapgqtqlpfadipqdalpvldqiqkrlndamkkaaadggadfv
dlyagtgantacdgadrgigglledsqlellgtkipwyahpndkgrdiqakqvadkieei
ln
>d1esfa1 2.35.2.2.1 (1-120) Staphylococcal enterotoxin A, SEA {Staphylococcus aureus}
sekseeinekdlrkkselqgtalgnlkqiyyynekaktenkeshdqflqhtilfkgfftd
hswyndllvdfdskdivdkykgkkvdlygayygyqcaggtpnktacmyggvtlhdnnrlt
>d1esfa2 4.13.7.1.1 (121-233) Staphylococcal enterotoxin A, SEA {Staphylococcus aureus}
eekkvpinlwldgkqntvpletvktnkknvtvqeldlqarrylqekynlynsdvfdgkvq
rglivfhtstepsvnydlfgaqgqysntllriyrdnktinsenmhidiylyts
>d1esfb1 2.35.2.2.1 (1-120) Staphylococcal enterotoxin A, SEA {Staphylococcus aureus}
sekseeinekdlrkkselqgtalgnlkqiyyynekaktenkeshdqflqhtilfkgfftd
hswyndllvdfdskdivdkykgkkvdlygayygyqcaggtpnktacmyggvtlhdnnrlt
>d1esfb2 4.13.7.1.1 (121-233) Staphylococcal enterotoxin A, SEA {Staphylococcus aureus}
eekkvpinlwldgkqntvpletvktnkknvtvqeldlqarrylqekynlynsdvfdgkvq
rglivfhtstepsvnydlfgaqgqysntllriyrdnktinsenmhidiylyts
>d1esl_1 4.139.1.1.5 (1-118) E-selectin {Human (Homo sapiens)}
wsyntsteamtydeasaycqqrythlvaiqnkeeieylnsilsyspsyywigirkvnnvw
vwvgtqkplteeaknwapgepnnrqkdedcveiyikrekdvgmwndercskkklalcy
>d1esl_2 7.3.11.1.4 (119-157) E-selectin, EGF-domain {Human (Homo sapiens)}
taactntscsghgecvetinnytckcdpgfsglkceqiv
>d1eso__ 2.1.8.1.7 Cu,Zn superoxide dismutase, SOD {Escherichia coli}
asekvemnlvtsqgvgqsigsvtitetdkglefspdlkalppgehgfhihakgscqpatk
dgkasaaesagghldpqntgkhegpegaghlgdlpalvvnndgkatdaviaprlksldei
kdkalmvhvggdnmsdqpkplggggeryacgvik
>d1esp_1 1.68.1.1.3 (157-317) Neutral protease {Bacillus cereus, strain dsm 3101}
iyqnesgalneaisdifgtlvefydnrnpdweigediytpgkagdalrsmsdptkygdpd
hyskrytgssdnggvhtnsgiinkqayllanggthygvtvtgigkdklgaiyyrantqyf
tqsttfsqaragavqaaadlygansaevaavkqsfsavgvn
>d1esp_2 4.71.1.2.3 (1-156) Neutral protease {Bacillus cereus, strain dsm 3101}
vtgtnkvgtgkgvlgdtkslnttlsgssyylqdntrgatiftydaknrstlpgtlwadad
nvfnaaydaaavdahyyagktydyykatfnrnsindagaplkstvhygsnynnafwngsq
mvygdgdgvtftslsggidvighslthavtenssnl
>d1est__ 2.41.1.2.15 Elastase {Porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1eta1_ 2.3.3.1.1 Transthyretin (synonym: prealbumin) {Human (Homo sapiens)}
gptgtgeskcplmvkvldavrgspainvavhvfrkaaddtwepfasgktsesgelhgltt
eeefvegiykveidtksywkalgispfhehaevvftandsgprrytiaallspysystta
vvtnpke
>d1eta2_ 2.3.3.1.1 Transthyretin (synonym: prealbumin) {Human (Homo sapiens)}
gptgtgeskcplmvkvldavrgspainvavhvfrkaaddtwepfasgktsesgelhgltt
eeefvegiykveidtksywkalgispfhehaevvftandsgprrytiaallspysystta
vvtnpke
>d1etb1_ 2.3.3.1.1 Transthyretin (synonym: prealbumin) {Human (Homo sapiens)}
kcplmvkvldavrgspainvavhvfrkaaddtwepfasgktsesgelhgltteeefvegi
ykveidtksywkalgispfhehaevvftandsgprrytiatllspysysttavvtnpk
>d1etb2_ 2.3.3.1.1 Transthyretin (synonym: prealbumin) {Human (Homo sapiens)}
kcplmvkvldavrgspainvavhvfrkaaddtwepfasgktsesgelhgltteeefvegi
ykveidtksywkalgispfhehaevvftandsgprrytiatllspysysttavvtnp
>d1etc__ 1.4.3.16.2 ETS-1 transcription factor, residues 331-440 {Murine (Mus musculus)}
iqlwqfllelltdkscqsfiswtgdgwefklsdpdevarrwgkrknkpkmnyeklsrglr
yyydkniihktagkryvyrfvcdlqsllgytpeelhamldvkpdad
>d1etd__ 1.4.3.16.2 ETS-1 transcription factor, residues 331-440 {Murine (Mus musculus)}
iqlwqfllelltdkscqsfiswtgdgwefklsdpdevarrwgkrknkpkmnyeklsrglr
yyydkniihktagkryvyrfvcdlqsllgytpeelhamldvkpdad
>d1etha1 2.11.1.2.2 (337-448) Pancreatic lipase, C-terminal domain {Pig (Sus scrofa)}
arwrykvsvtlsgkkvtghilvslfgnegnsrqyeiykgtlqpdnthsdefdsdvevgdl
qkvkfiwynvinptlprvgaskitverndgkvydfcsqetvreevlltlnpc
>d1etha2 3.59.1.16.2 (1-336) Pancreatic lipase, N-terminal domain {Pig (Sus scrofa)}
sevcfprlgcfsddapwagivqrplkilpwspkdvdtrfllytnqnqnnyqelvadpsti
tnsnfrmdrktrfiihgfidkgeedwlsnicknlfkvesvncicvdwkggsrtgytqasq
nirivgaevayfvevlksslgyspsnvhvighslgshaageagrrtngtieritgldpae
pcfqgtpelvrldpsdakfvdvihtdaapiipnlgfgmsqtvghldffpnggkqmpgcqk
nilsqivdidgiwegtrdfvacnhlrsykyyadsilnpdgfagfpcdsynvftankcfpc
psegcpqmghyadrfpgktngvsqvfylntgdasnf
>d1ethb1 7.3.10.1.1 (4-44) (Pro)colipase {Pig (Sus scrofa)}
prgiiinldegelclnsaqcksnccqhdtilslsrcalkar
>d1ethb2 7.3.10.1.1 (45-90) (Pro)colipase {Pig (Sus scrofa)}
ensecsaftlygvyykcpcergltcegdkslvgsitntnfgichnv
>d1ethc1 2.11.1.2.2 (337-448) Pancreatic lipase, C-terminal domain {Pig (Sus scrofa)}
arwrykvsvtlsgkkvtghilvslfgnegnsrqyeiykgtlqpdnthsdefdsdvevgdl
qkvkfiwynvinptlprvgaskitverndgkvydfcsqetvreevlltlnpc
>d1ethc2 3.59.1.16.2 (1-336) Pancreatic lipase, N-terminal domain {Pig (Sus scrofa)}
sevcfprlgcfsddapwagivqrplkilpwspkdvdtrfllytnqnqnnyqelvadpsti
tnsnfrmdrktrfiihgfidkgeedwlsnicknlfkvesvncicvdwkggsrtgytqasq
nirivgaevayfvevlksslgyspsnvhvighslgshaageagrrtngtieritgldpae
pcfqgtpelvrldpsdakfvdvihtdaapiipnlgfgmsqtvghldffpnggkqmpgcqk
nilsqivdidgiwegtrdfvacnhlrsykyyadsilnpdgfagfpcdsynvftankcfpc
psegcpqmghyadrfpgktngvsqvfylntgdasnf
>d1ethd1 7.3.10.1.1 (4-44) (Pro)colipase {Pig (Sus scrofa)}
prgiiinldegelclnsaqcksnccqhdtilslsrcalkar
>d1ethd2 7.3.10.1.1 (45-90) (Pro)colipase {Pig (Sus scrofa)}
ensecsaftlygvyykcpcergltcegdkslvgsitntnfgichnv
>d1etja_ 2.5.1.1.23 Azurin {Pseudomonas aeruginosa}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctfpghsal
ekgtltlk
>d1etjb_ 2.5.1.1.23 Azurin {Pseudomonas aeruginosa}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctfpghsal
ekgtltlk
>d1etjc_ 2.5.1.1.23 Azurin {Pseudomonas aeruginosa}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctfpghsal
ekgtltlk
>d1etjd_ 2.5.1.1.23 Azurin {Pseudomonas aeruginosa}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctfpghsal
ekgtltlk
>d1etpa1 1.3.1.3.1 (1-92) Cytochrome c4 {Pseudomonas stutzeri}
agdaeagqgkvavcgachgvdgnspapnfpklagqgeryllkqlqdikagstpgapegvg
rkvlemtgmldplsdqdlediaayfssqkgsv
>d1etpa2 1.3.1.3.1 (93-190) Cytochrome c4 {Pseudomonas stutzeri}
gyadpalakqgeklfrggkldqgmpactgchapngvgndlagfpklggqhaaytakqltd
fregnrtndgdtmimrgvaaklsnkdiealssyiqglh
>d1etpb1 1.3.1.3.1 (1-92) Cytochrome c4 {Pseudomonas stutzeri}
agdaeagqgkvavcgachgvdgnspapnfpklagqgeryllkqlqdikagstpgapegvg
rkvlemtgmldplsdqdlediaayfssqkgsv
>d1etpb2 1.3.1.3.1 (93-190) Cytochrome c4 {Pseudomonas stutzeri}
gyadpalakqgeklfrggkldqgmpactgchapngvgndlagfpklggqhaaytakqltd
fregnrtndgdtmimrgvaaklsnkdiealssyiqglh
>e1etr.1h 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
ivegqdaevglspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftvddll
vrigkhsrtryerkvekismldkiyihprynwkenldrdiallklkrpielsdyihpvcl
pdkqtaakllhagfkgrvtgwgnrretwttsvaevqpsvlqvvnlplverpvckastrir
itdnmfcagykpgegkrgdacegdsggpfvmkspynnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidrlgs
>e1etr.1l 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1ets.1h 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
ivegqdaevglspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftvddll
vrigkhsrtryerkvekismldkiyihprynwkenldrdiallklkrpielsdyihpvcl
pdkqtaakllhagfkgrvtgwgnrretwttsvaevqpsvlqvvnlplverpvckastrir
itdnmfcagykpgegkrgdacegdsggpfvmkspynnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidrlgs
>e1ets.1l 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1ett.1h 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
ivegqdaevglspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftvddll
vrigkhsrtryerkvekismldkiyihprynwkenldrdiallklkrpielsdyihpvcl
pdkqtaakllhagfkgrvtgwgnrretwttsvaevqpsvlqvvnlplverpvckastrir
itdnmfcagykpgegkrgdacegdsggpfvmkspynnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidrlgs
>e1ett.1l 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>d1etu__ 3.30.1.6.14 Elongation factor Tu (EF-Tu), N-terminal (G) domain {Escherichia coli}
fertkphvnvgtighvdhgkttltaaittvlaktyggaaxxxxxxxxxxxxxxxgitint
shveydtptrhyahvdcpghadyvknmitgaaqmdgailvvaatdgpmpqtrehillgrq
vgvpyiivflnkcdmvddeellelvemevrellsqydfpgddtpivrgsalkalegdaew
eakilelagfldsyip
>d1euga_ 3.14.1.1.3 Uracil-DNA glycosylase {Escherichia coli}
ltwhdvlaeekqqpyflntlqtvaserqsgvtiyppqkdvfnafrftelgdvkvvilgqd
pyhgpgqahglafsvrpgiaippsllnmykelentipgftrpnhgyleswarqgvlllnt
vltvragqahshaslgwetftdkvislinqhregvvfllwgshaqkkgaiidkqrhhvlk
aphpsplsahrgffgcnhfvlanqwleqhgetpidwmpvlpaese
>d1euha_ 3.71.1.1.7 Aldehyde reductase (dehydrogenase), ALDH {Streptococcus mutans}
tkqyknyvngewklseneikiyepasgaelgsvpamsteevdyvyasakkaqpawralsy
ieraaylhkvadilmrdkekigailskevakgyksavsevvrtaeiinyaaeeglrmege
vleggsfeaaskkkiavvrrepvglvlaispfnypvnlagskiapaliagnviafkpptq
gsisglllaeafaeaglpagvfntitgrgseigdyivehqavnfinftgstgigerigkm
agmrpimlelggkdsaivledadleltakniiagafgysgqrctavkrvlvmesvadelv
ekirekvlaltignpeddaditplidtksadyveglindandkgatalteikregnlicp
ilfdkvttdmrlaweepfgpvlpiirvtsveeaieisnkseyglqasiftndfprafgia
eqlevgtvhinnktqrgtdnfpflgakksgagiqgvkysieamttvksvvfdik
>d1euhb_ 3.71.1.1.7 Aldehyde reductase (dehydrogenase), ALDH {Streptococcus mutans}
tkqyknyvngewklseneikiyepasgaelgsvpamsteevdyvyasakkaqpawralsy
ieraaylhkvadilmrdkekigailskevakgyksavsevvrtaeiinyaaeeglrmege
vleggsfeaaskkkiavvrrepvglvlaispfnypvnlagskiapaliagnviafkpptq
gsisglllaeafaeaglpagvfntitgrgseigdyivehqavnfinftgstgigerigkm
agmrpimlelggkdsaivledadleltakniiagafgysgqrctavkrvlvmesvadelv
ekirekvlaltignpeddaditplidtksadyveglindandkgatalteikregnlicp
ilfdkvttdmrlaweepfgpvlpiirvtsveeaieisnkseyglqasiftndfprafgia
eqlevgtvhinnktqrgtdnfpflgakksgagiqgvkysieamttvksvvfdik
>d1euhc_ 3.71.1.1.7 Aldehyde reductase (dehydrogenase), ALDH {Streptococcus mutans}
tkqyknyvngewklseneikiyepasgaelgsvpamsteevdyvyasakkaqpawralsy
ieraaylhkvadilmrdkekigailskevakgyksavsevvrtaeiinyaaeeglrmege
vleggsfeaaskkkiavvrrepvglvlaispfnypvnlagskiapaliagnviafkpptq
gsisglllaeafaeaglpagvfntitgrgseigdyivehqavnfinftgstgigerigkm
agmrpimlelggkdsaivledadleltakniiagafgysgqrctavkrvlvmesvadelv
ekirekvlaltignpeddaditplidtksadyveglindandkgatalteikregnlicp
ilfdkvttdmrlaweepfgpvlpiirvtsveeaieisnkseyglqasiftndfprafgia
eqlevgtvhinnktqrgtdnfpflgakksgagiqgvkysieamttvksvvfdik
>d1euhd_ 3.71.1.1.7 Aldehyde reductase (dehydrogenase), ALDH {Streptococcus mutans}
tkqyknyvngewklseneikiyepasgaelgsvpamsteevdyvyasakkaqpawralsy
ieraaylhkvadilmrdkekigailskevakgyksavsevvrtaeiinyaaeeglrmege
vleggsfeaaskkkiavvrrepvglvlaispfnypvnlagskiapaliagnviafkpptq
gsisglllaeafaeaglpagvfntitgrgseigdyivehqavnfinftgstgigerigkm
agmrpimlelggkdsaivledadleltakniiagafgysgqrctavkrvlvmesvadelv
ekirekvlaltignpeddaditplidtksadyveglindandkgatalteikregnlicp
ilfdkvttdmrlaweepfgpvlpiirvtsveeaieisnkseyglqasiftndfprafgia
eqlevgtvhinnktqrgtdnfpflgakksgagiqgvkysieamttvksvvfdik
>d1euia_ 3.14.1.1.3 Uracil-DNA glycosylase {Escherichia coli}
twhdvlaeekqqpyflntlqtvaserqsgvtiyppqkdvfnafrftelgdvkvvilgqdp
yhgpgqahglafsvrpgiaippsllnmykelentipgftrpnhgyleswarqgvlllntv
ltvragqahshaslgwetftdkvislinqhregvvfllwgshaqkkgaiidkqrhhvlka
phpsplsahrgffgcnhfvlanqwleqrgetpidwmpvlpa
>d1euib_ 3.14.1.1.3 Uracil-DNA glycosylase {Escherichia coli}
twhdvlaeekqqpyflntlqtvaserqsgvtiyppqkdvfnafrftelgdvkvvilgqdp
yhgpgqahglafsvrpgiaippsllnmykelentipgftrpnhgyleswarqgvlllntv
ltvragqahshaslgwetftdkvislinqhregvvfllwgshaqkkgaiidkqrhhvlka
phpsplsahrgffgcnhfvlanqwleqrgetpidwmpvlp
>d1euic_ 4.15.4.1.2 Uracil-DNA glycosylase inhibitor protein {Bacteriophage pbs2}
qlviqesilmlpeeveevignkpesdilvhtaydestdenvmlltsdapeykpwalviqd
sngenkikml
>d1euid_ 4.15.4.1.2 Uracil-DNA glycosylase inhibitor protein {Bacteriophage pbs2}
qlviqesilmlpeeveevignkpesdilvhtaydestdenvmlltsdapeykpwalviqd
sngenkikml
>d1eur__ 2.59.1.1.4 Micromonospora sialidase, N-terminal domain {Micromonospora viridifaciens}
geplyteqdlavngregfpnyripaltvtpdgdllasydgrptgidapgpnsilqrrstd
ggrtwgeqqvvsagqttapikgfsdpsylvdretgtifnfhvysqrqgfagsrpgtdpad
pnvlhanvatstdggltwshrtitaditpdpgwrsrfaasgegiqlrygphagrliqqyt
iinaagafqavsvysddhgrtwrageavgvgmdenktvelsdgrvllnsrdsarsgyrkv
avstdgghsygpvtidrdlpdptnnasiirafpdapagsarakvllfsnaasqtsrsqgt
irmscddgqtwpvskvfqpgsmsystltalpdgtygllyepgtgiryanfnlawlggica
p
>d1eus__ 2.59.1.1.4 Micromonospora sialidase, N-terminal domain {Micromonospora viridifaciens}
geplyteqdlavngregfpnyripaltvtpdgdllasydgrptgidapgpnsilqrrstd
ggrtwgeqqvvsagqttapikgfsdpsylvdretgtifnfhvysqrqgfagsrpgtdpad
pnvlhanvatstdggltwshrtitaditpdpgwrsrfaasgegiqlrygphagrliqqyt
iinaagafqavsvysddhgrtwrageavgvgmdenktvelsdgrvllnsrdsarsgyrkv
avstdgghsygpvtidrdlpdptnnasiirafpdapagsarakvllfsnaasqtsrsqgt
irmscddgqtwpvskvfqpgsmsystltalpdgtygllyepgtgiryanfnlawlggi
>d1eut_1 2.1.1.5.15 (403-505) Sialidase, "linker" domain {Micromonospora viridifaciens}
gicapftipdvalepgqqvtvpvavtnqsgiavpkpslqldaspdwqvqgsveplmpgrq
akgqvtitvpagttpgryrvgatlrtsagnasttftvtvglld
>d1eut_2 2.16.1.1.2 (506-647) Sialidase, C-terminal domain {Micromonospora viridifaciens}
qarmsiadvdseetaredgrasnvidgnpstfwhtewsradapgyphrisldlggthtis
glqytrrqnsaneqvadyeiytslngttwdgpvasgrfttslapqravfpardaryirlv
alseqtghkyaavaelevegqr
>d1eut_3 2.59.1.1.4 (47-402) Micromonospora sialidase, N-terminal domain {Micromonospora viridifaciens}
geplyteqdlavngregfpnyripaltvtpdgdllasydgrptgidapgpnsilqrrstd
ggrtwgeqqvvsagqttapikgfsdpsylvdretgtifnfhvysqrqgfagsrpgtdpad
pnvlhanvatstdggltwshrtitaditpdpgwrsrfaasgegiqlrygphagrliqqyt
iinaagafqavsvysddhgrtwrageavgvgmdenktvelsdgrvllnsrdsarsgyrkv
avstdgghsygpvtidrdlpdptnnasiirafpdapagsarakvllfsnaasqtsrsqgt
irmscddgqtwpvskvfqpgsmsystltalpdgtygllyepgtgiryanfnlawlg
>d1euu_1 2.1.1.5.15 (403-505) Sialidase, "linker" domain {Micromonospora viridifaciens}
gicapftipdvalepgqqvtvpvavtnqsgiavpkpslqldaspdwqvqgsveplmpgrq
akgqvtitvpagttpgryrvgatlrtsagnasttftvtvglld
>d1euu_2 2.16.1.1.2 (506-647) Sialidase, C-terminal domain {Micromonospora viridifaciens}
qarmsiadvdseetaredgrasnvidgnpstfwhtewsradapgyphrisldlggthtis
glqytrrqnsaneqvadyeiytslngttwdgpvasgrfttslapqravfpardaryirlv
alseqtghkyaavaelevegqr
>d1euu_3 2.59.1.1.4 (47-402) Micromonospora sialidase, N-terminal domain {Micromonospora viridifaciens}
geplyteqdlavngregfpnyripaltvtpdgdllasydgrptgidapgpnsilqrrstd
ggrtwgeqqvvsagqttapikgfsdpsylvdretgtifnfhvysqrqgfagsrpgtdpad
pnvlhanvatstdggltwshrtitaditpdpgwrsrfaasgegiqlrygphagrliqqyt
iinaagafqavsvysddhgrtwrageavgvgmdenktvelsdgrvllnsrdsarsgyrkv
avstdgghsygpvtidrdlpdptnnasiirafpdapagsarakvllfsnaasqtsrsqgt
irmscddgqtwpvskvfqpgsmsystltalpdgtygllyepgtgiryanfnlawlg
>d1ev11_ 2.9.1.4.15 Echovirus 1 {Host: human (Homo sapiens)}
gdvqnavegamvrvadtvqtsatnservpnltavetghtsqavpgdtmqtrhvinnhvrs
estienflarsacvfyleyktgtkedsnsfnnwvittrrvaqlrrklemftylrfdmeit
vvitssqdqstsqnqnapvlthqimyvppggpipvsvddyswqtstnpsifwtegnapar
msipfisignaysnfydgwshfsqagvygfttlnnmgqlffrhvnkpnpaaitsvariyf
kpkhvrawvprpprlcpyinstnvnfepkpvtevrtniitt
>d1ev12_ 2.9.1.4.15 Echovirus 1 {Host: human (Homo sapiens)}
gysdrvrsitlgnstittqecanvvvgygewpeylsdneataedqptqpdvatcrfytld
svqwengspgwwwkfpdalrdmglfgqnmyyhylgragytihvqcnaskfhqgcilvvcv
peaemgsaqtsgvvnyehiskgeiasrftttttaedhgvqaavwnagmgvgvgnltifph
qwinlrtnnsativmpyvnsvpmdnmyrhhnftlmiipfvpldfsagastyvpitvtvap
mcaeynglrlaghq
>d1ev13_ 2.9.1.4.15 Echovirus 1 {Host: human (Homo sapiens)}
glptmntpgsnqfltsddfqspsampqfdvtpemhipgevrnlmeiaevdsvmpinndsa
akvssmeayrvelstntnagtqvfgfqlnpgaesvmnrtlmgeilnyyahwsgsikitfv
fcgsamttgkfllsyappgagapktrkdamlgthvvwdvglqsscvlcipwisqthyrfv
ekdpytnagfvtcwyqtsvvspasnqpkcymmcmvsacndfsvrmlrdtkfieqtsfyq
>d1eve__ 3.59.1.1.1 Acetylcholinesterase {Electric ray (Torpedo californica)}
dhsellvntksgkvmgtrvpvlsshisaflgipfaeppvgnmrfrrpepkkpwsgvwnas
typnncqqyvdeqfpgfsgsemwnpnremsedclylniwvpsprpksttvmvwiygggfy
sgsstldvyngkylayteevvlvslsyrvgafgflalhgsqeapgnvglldqrmalqwvh
dniqffggdpktvtifgesaggasvgmhilspgsrdlfrrailqsgspncpwasvsvaeg
rrravelgrnlncnlnsdeelihclrekkpqelidvewnvlpfdsifrfsfvpvidgeff
ptslesmlnsgnfkktqillgvnkdegsffllygapgfskdseskisredfmsgvklsvp
handlgldavtlqytdwmddnngiknrdglddivgdhnvicplmhfvnkytkfgngtyly
ffnhrasnlvwpewmgvihgyeiefvfglplvkelnytaeeealsrrimhywatfaktgn
pnephsqeskwplfttkeqkfidlntepmkvhqrlrvqmcvfwnqflpkllnat
>d1evha_ 2.49.1.4.1 Enabled {Mouse (Mus musculus)}
seqsicqaraavmvyddankkwvpaggstgfsrvhiyhhtgnntfrvvgrkiqdhqvvin
caipkglkynqatqtfhqwrdarqvyglnfgskedanvfasammhalevln
>d1exfa_ 2.41.1.1.8 Epidermolytic (exfoliative) toxin A {Staphylococcus aureus}
vsaeeikkheekwnkyygvnafnlpkelfskvdekdrqkypyntignvfvkgqtsatgvl
igkntvltnrhiakfangdpskvsfrpsintddngntetpygeyevkeilqepfgagvdl
alirlkpdqngvslgdkispakigtsndlkdgdkleligypfdhkvnqmhrseielttls
rglryygftvpgnsgsgifnsngelvgihsskvshldrehqinygvgignyvkriinekn
e
>d1exg__ 2.2.2.1.1 Exo-1,4-beta-D-glycanase (cellulase, xylanase) {Cellulomonas fimi}
assgpagcqvlwgvnqwntgftanvtvkntssapvdgwtltfsfpsgqqvtqawsstvtq
sgsavtvrnapwngsipaggtaqfgfngshtgtnaaptafslngtpctvg
>d1exh__ 2.2.2.1.1 Exo-1,4-beta-D-glycanase (cellulase, xylanase) {Cellulomonas fimi}
assgpagcqvlwgvnqwntgftanvtvkntssapvdgwtltfsfpsgqqvtqawsstvtq
sgsavtvrnapwngsipaggtaqfgfngshtgtnaaptafslngtpctvg
>d1exna1 1.61.3.1.3 (186-290) T5 5'-exonuclease {Bacteriophage T5}
vddveqfislkaixgdlgdnirgvegigakrgyniirefgnvldiidqlplpgkqkyiqn
lnaseellfrnlilvdlptycvdaiaavgqdvldkftkdileiae
>d1exna2 3.44.1.2.3 (20-185) T5 5'-exonuclease {Bacteriophage T5}
rnlxivdgtnlgfrfkhnnskkpfassyvstiqslaksysarttivlgdkgksvfrlehl
peykgnrdekyaqrteeekaldeqffeylkdafelckttfptftirgveaddxaayivkl
ighlydhvwlistdgdwdtlltdkvsrfsfttrreyhlrdxyehhn
>d1exnb1 1.61.3.1.3 (186-291) T5 5'-exonuclease {Bacteriophage T5}
vddveqfislkaixgdlgdnirgvegigakrgyniirefgnvldiidqlplpgkqkyiqn
lnaseellfrnlilvdlptycvdaiaavgqdvldkftkdileiaeq
>d1exnb2 3.44.1.2.3 (20-185) T5 5'-exonuclease {Bacteriophage T5}
rnlxivdgtnlgfrfkhnnskkpfassyvstiqslaksysarttivlgdkgksvfrlehl
peykgnrdekyaqrteeekaldeqffeylkdafelckttfptftirgveaddxaayivkl
ighlydhvwlistdgdwdtlltdkvsrfsfttrreyhlrdxyehhn
>d1exp__ 3.1.7.3.4 beta-1,4-glycanase Cex, catalytic domain {Cellulomonas fimi, ATCC 484}
attlkeaadgagrdfgfaldpnrlseaqykaiadsefnlvvaenamkwdatepsqnsfsf
gagdrvasyaadtgkelyghtlvwhsqlpdwaknlngsafesamvnhvtkvadhfegkva
swdvvneafadgggrrqdsafqqklgngyietafraaraadptaklcindynveginaks
nslydlvkdfkargvpldcvgfqshlivgqvpgdfrqnlqrfadlgvdvriteldirmrt
psdatklatqaadykkvvqacmqvtrcqgvtvwgitdkyswvpdvfpgegaalvwdasya
kkpayaavmeaf
>d1exta1 7.24.1.1.1 (13-71) Tumor necrosis factor (TNF) receptor {Human (Homo sapiens)}
svcpqgkyihpqnnsicctkchkgtylyndcpgpgqdtdcrecesgsftasenhlrhcl
>d1exta2 7.24.1.1.1 (72-115) Tumor necrosis factor (TNF) receptor {Human (Homo sapiens)}
scskcrkemgqveissctvdrdtvcgcrknqyrhywsenlfqcf
>d1exta3 7.24.1.1.1 (116-172) Tumor necrosis factor (TNF) receptor {Human (Homo sapiens)}
ncslclngtvhlscqekqntvctchagfflrenecvscsnckkslectklclpqien
>d1extb1 7.24.1.1.1 (11-71) Tumor necrosis factor (TNF) receptor {Human (Homo sapiens)}
mdsvcpqgkyihpqnnsicctkchkgtylyndcpgpgqdtdcrecesgsftasenhlrhc
l
>d1extb2 7.24.1.1.1 (72-115) Tumor necrosis factor (TNF) receptor {Human (Homo sapiens)}
scskcrkemgqveissctvdrdtvcgcrknqyrhywsenlfqcf
>d1extb3 7.24.1.1.1 (116-168) Tumor necrosis factor (TNF) receptor {Human (Homo sapiens)}
ncslclngtvhlscqekqntvctchagfflrenecvscsnckkslectklclp
>d1eza_1 1.61.7.1.1 (22-144) Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain {Escherichia coli}
deividrkkisadqvdqeverflsgrakasaqletiktkagetfgeekeaifeghimlle
deeleqeiialikdkhmtadaaaheviegqasaleelddeylkeraadvrdigkrllrni
lgl
>d1eza_2 3.7.1.2.1 (1-21,145-259) N-terminal domain of enzyme I of the PEP:sugar phosphotransferase system {Escherichia coli}
misgilaspgiafgkalllkeXkiidlsaiqdevilvaadltpsetaqlnlkkvlgfitd
aggrtshtsimarslelpaivgtgsvtsqvknddylildavnnqvyvnptnevidkmrav
qeqvasekaelaklkdr
>d1ezb_1 1.61.7.1.1 (22-144) Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain {Escherichia coli}
deividrkkisadqvdqeverflsgrakasaqletiktkagetfgeekeaifeghimlle
deeleqeiialikdkhmtadaaaheviegqasaleelddeylkeraadvrdigkrllrni
lgl
>d1ezb_2 3.7.1.2.1 (1-21,145-259) N-terminal domain of enzyme I of the PEP:sugar phosphotransferase system {Escherichia coli}
misgilaspgiafgkalllkeXkiidlsaiqdevilvaadltpsetaqlnlkkvlgfitd
aggrtshtsimarslelpaivgtgsvtsqvknddylildavnnqvyvnptnevidkmrav
qeqvasekaelaklkdr
>d1ezc_1 1.61.7.1.1 (22-144) Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain {Escherichia coli}
deividrkkisadqvdqeverflsgrakasaqletiktkagetfgeekeaifeghimlle
deeleqeiialikdkhmtadaaaheviegqasaleelddeylkeraadvrdigkrllrni
lgl
>d1ezc_2 3.7.1.2.1 (1-21,145-259) N-terminal domain of enzyme I of the PEP:sugar phosphotransferase system {Escherichia coli}
misgilaspgiafgkalllkeXkiidlsaiqdevilvaadltpsetaqlnlkkvlgfitd
aggrtshtsimarslelpaivgtgsvtsqvknddylildavnnqvyvnptnevidkmrav
qeqvasekaelaklkdr
>d1ezd_1 1.61.7.1.1 (22-144) Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain {Escherichia coli}
deividrkkisadqvdqeverflsgrakasaqletiktkagetfgeekeaifeghimlle
deeleqeiialikdkhmtadaaaheviegqasaleelddeylkeraadvrdigkrllrni
lgl
>d1ezd_2 3.7.1.2.1 (1-21,145-259) N-terminal domain of enzyme I of the PEP:sugar phosphotransferase system {Escherichia coli}
misgilaspgiafgkalllkeXkiidlsaiqdevilvaadltpsetaqlnlkkvlgfitd
aggrtshtsimarslelpaivgtgsvtsqvknddylildavnnqvyvnptnevidkmrav
qeqvasekaelaklkdr
>d1ezm_1 1.68.1.1.1 (154-298) Elastase {Pseudomonas aeruginosa}
iyrgqsggmneafsdmageaaefymrgkndfligydikkgsgalrymdqpsrdgrsidna
sqyyngidvhhssgvynrafyllanspgwdtrkafevfvdanryywtatsnynsgacgvi
rsaqnrnysaadvtrafstvgvtcp
>d1ezm_2 4.71.1.2.1 (1-153) Elastase {Pseudomonas aeruginosa}
aeaggpggnqkigkytygsdygplivndrcemddgnvitvdmnsstddskttpfrfacpt
ntykqvngaysplndahffggvvfklyrdwfgtsplthklymkvhygrsvenaywdgtam
lfgdgatmfyplvsldvaahevshgfteqnsgl
>d1f13a1 2.1.1.5.14 (5-190) Transglutaminase factor XIII, N-terminal domain {Human (Homo sapiens), blood}
rtafggrravppnnsnaaeddlptvelqgvvprgvnlqeflnvtsvhlfkerwdtnkvdh
htdkyennklivrrgqsfyvqidfsrpydprrdlfrveyvigrypqenkgtyipvpivse
lqsgkwgakivmredrsvrlsiqsspkcivgkfrmyvavwtpygvlrtsrnpetdtyilf
npwced
>d1f13a2 2.1.5.1.1 (516-627) Coagulation factor XIII, two C-terminal domains {Human (Homo sapiens), blood}
snvdmdfevenavlgkdfklsitfrnnshnrytitaylsanitfytgvpkaefkketfdv
tleplsfkkeavliqageymgqlleqaslhffvtarinetrdvlakqkstvl
>d1f13a3 2.1.5.1.1 (628-728) Coagulation factor XIII, two C-terminal domains {Human (Homo sapiens), blood}
tipeiiikvrgtqvvgsdmtvtveftnplketlrnvwvhldgpgvtrpmkkmfreirpns
tvqweevcrpwvsghrkliasmssdslrhvygeldvqiqrr
>d1f13a4 4.3.1.2.1 (191-515) Coagulation factor XIII, catalytic domain {Human (Homo sapiens), blood}
davyldnekereeyvlndigvifygevndiktrswsygqfedgildtclyvmdraqmdls
grgnpikvsrvgsamvnakddegvlvgswdniyaygvppsawtgsvdilleyrssenpvr
ygqcwvfagvfntflrclgiparivtnyfsahdndanlqmdifleedgnvnskltkdsvw
nyhcwneawmtrpdlpvgfggwqavdstpqensdgmyrcgpasvqaikhghvcfqfdapf
vfaevnsdliyitakkdgthvvenvdathigklivtkqiggdgmmditdtykfqegqeee
rlaletalmygakkplntegvmksr
>d1f13b1 2.1.1.5.14 (6-190) Transglutaminase factor XIII, N-terminal domain {Human (Homo sapiens), blood}
tafggrravppnnsnaaeddlptvelqgvvprgvnlqeflnvtsvhlfkerwdtnkvdhh
tdkyennklivrrgqsfyvqidfsrpydprrdlfrveyvigrypqenkgtyipvpivsel
qsgkwgakivmredrsvrlsiqsspkcivgkfrmyvavwtpygvlrtsrnpetdtyilfn
pwced
>d1f13b2 2.1.5.1.1 (516-627) Coagulation factor XIII, two C-terminal domains {Human (Homo sapiens), blood}
snvdmdfevenavlgkdfklsitfrnnshnrytitaylsanitfytgvpkaefkketfdv
tleplsfkkeavliqageymgqlleqaslhffvtarinetrdvlakqkstvl
>d1f13b3 2.1.5.1.1 (628-728) Coagulation factor XIII, two C-terminal domains {Human (Homo sapiens), blood}
tipeiiikvrgtqvvgsdmtvtveftnplketlrnvwvhldgpgvtrpmkkmfreirpns
tvqweevcrpwvsghrkliasmssdslrhvygeldvqiqrr
>d1f13b4 4.3.1.2.1 (191-515) Coagulation factor XIII, catalytic domain {Human (Homo sapiens), blood}
davyldnekereeyvlndigvifygevndiktrswsygqfedgildtclyvmdraqmdls
grgnpikvsrvgsamvnakddegvlvgswdniyaygvppsawtgsvdilleyrssenpvr
ygqcwvfagvfntflrclgiparivtnyfsahdndanlqmdifleedgnvnskltkdsvw
nyhcwneawmtrpdlpvgfggwqavdstpqensdgmyrcgpasvqaikhghvcfqfdapf
vfaevnsdliyitakkdgthvvenvdathigklivtkqiggdgmmditdtykfqegqeee
rlaletalmygakkplntegvmksr
>d1f2g__ 4.47.1.1.1 Ferredoxin II {Desulfovibrio gigas}
pievnddcmaceacveicpdvfemneegdkavvinpdsdldcveeaidscpaeaivrs
>d1f36a_ 1.101.1.1.1 FIS protein {Escherichia coli}
vltvstvnsqdqvtqkplrdsvkqalenyfaqlngqdvndlyelvlaeveqplldmvmqy
trgnqtraalmmginrgtlrkklkkygmn
>d1f36b_ 1.101.1.1.1 FIS protein {Escherichia coli}
vltvstvnsqdqvtqkplrdsvkqalenyfaqlngqdvndlyelvlaeveqplldmvmqy
trgnqtraalmmginrgtlrkklkkygmn
>d1f3g__ 2.74.3.1.2 Glucose-specific factor III (glsIII) {Escherichia coli}
tieiiaplsgeivniedvpdvvfaekivgdgiaikptgnkmvapvdgtigkifetnhafs
iesdsgvelfvhfgidtvelkgegfkriaeegqrvkvgdtviefdlplleekakstltpv
visnmdeikeliklsgsvtvgetpvirikk
>d1f3z__ 2.74.3.1.2 Glucose-specific factor III (glsIII) {Escherichia coli}
tieiiaplsgeivniedvpdvvfaekivgdgiaikptgnkmvapvdgtigkifetnhafs
iesdsgvelfvhfgidtvelkgegfkriaeegqrvkvgdtviefdlplleekakstltpv
visnmdeikeliklsgsvtvgetpvirikk
>d1f58h1 2.1.1.1.127 (1-113) Immunoglobulin (variable domains of L and H chains) {Anti-gp120 (HIV-1) Fab 58.2, (mouse), kappa L chain}
dvqlqqsgpdlvkpsqslsltctvtgysitsgyswhwirqfpgnklewmgyihysagtny
npslksrisitrdtsknqfflqlnsvttedtatyycareeampygnqayyyamdcwgqgt
tvtvss
>d1f58h2 2.1.1.2.125 (114-230) Immunoglobulin (constant domains of L and H chains) {Anti-gp120 (HIV-1) Fab 58.2, (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpssprpsetvtcnvahpasstkvdkkivprdc
>d1f58l1 2.1.1.1.127 (1-107) Immunoglobulin (variable domains of L and H chains) {Anti-gp120 (HIV-1) Fab 58.2, (mouse), kappa L chain}
divltqspaslavslgqratisckasqgvdfdgasfmnwyqqkpgqppkllifaastles
giparfsgrgsgtdftlnihpveeedaatyycqqshedpltfgagtklelk
>d1f58l2 2.1.1.2.125 (108-212) Immunoglobulin (constant domains of L and H chains) {Anti-gp120 (HIV-1) Fab 58.2, (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnra
>d1f7ea_ 7.3.11.1.8 Factor VII, N-terminal domain {Human (Homo sapiens)}
sdgdqcasspcqnggsckdqlqsyicfclpafegrncethkddgsa
>d1f7ma_ 7.3.11.1.8 Factor VII, N-terminal domain {Human (Homo sapiens)}
sdgdqcasspcqnggsckdqlqsyicfclpafegrncethkddgsa
>d1fada_ 1.76.1.1.4 FADD (Mort1) {Mouse (Mus musculus)}
aappgeaylqvafdivcdnvgrdwkrlarelkvseakmdgieekyprslservreslkvw
knaekknasvaglvkalrtcrlnlvadlveeaqes
>d1faga_ 1.100.1.1.2 Cytochrome P450 {Bacillus megaterium}
tikempqpktfgelknlpllntdkpvqalmkiadelgeifkfeapgrvtrylssqrlike
acdesrfdknlsqalkfvrdfagdglftswtheknwkkahnillpsfsqqamkgyhammv
diavqlvqkwerlnadehievpedmtrltldtiglcgfnyrfnsfyrdqphpfitsmvra
ldeamnklqranpddpaydenkrqfqedikvmndlvdkiiadrkasgeqsddllthmlng
kdpetgeplddeniryqiitfliaghettsgllsfalyflvknphvlqkaaeeaarvlvd
pvpsykqvkqlkyvgmvlnealrlwptapafslyakedtvlggeyplekgdelmvlipql
hrdktiwgddveefrperfenpsaipqhafkpfgngqracigqqfalheatlvlgmmlkh
fdfedhtnyeldiketltlkpegfvvkakskkipl
>d1fagb_ 1.100.1.1.2 Cytochrome P450 {Bacillus megaterium}
tikempqpktfgelknlpllntdkpvqalmkiadelgeifkfeapgrvtrylssqrlike
acdesrfdknlsqalkfvrdfagdglftswtheknwkkahnillpsfsqqamkgyhammv
diavqlvqkwerlnadehievpedmtrltldtiglcgfnyrfnsfyrdqphpfitsmvra
ldeamnklqranpddpaydenkrqfqedikvmndlvdkiiadrkasgeqsddllthmlng
kdpetgeplddeniryqiitfliaghettsgllsfalyflvknphvlqkaaeeaarvlvd
pvpsykqvkqlkyvgmvlnealrlwptapafslyakedtvlggeyplekgdelmvlipql
hrdktiwgddveefrperfenpsaipqhafkpfgngqracigqqfalheatlvlgmmlkh
fdfedhtnyeldiketltlkpegfvvkakskkipl
>d1fagc_ 1.100.1.1.2 Cytochrome P450 {Bacillus megaterium}
tikempqpktfgelknlpllntdkpvqalmkiadelgeifkfeapgrvtrylssqrlike
acdesrfdknlsqalkfvrdfagdglftswtheknwkkahnillpsfsqqamkgyhammv
diavqlvqkwerlnadehievpedmtrltldtiglcgfnyrfnsfyrdqphpfitsmvra
ldeamnklqranpddpaydenkrqfqedikvmndlvdkiiadrkasgeqsddllthmlng
kdpetgeplddeniryqiitfliaghettsgllsfalyflvknphvlqkaaeeaarvlvd
pvpsykqvkqlkyvgmvlnealrlwptapafslyakedtvlggeyplekgdelmvlipql
hrdktiwgddveefrperfenpsaipqhafkpfgngqracigqqfalheatlvlgmmlkh
fdfedhtnyeldiketltlkpegfvvkakskkipl
>d1fagd_ 1.100.1.1.2 Cytochrome P450 {Bacillus megaterium}
tikempqpktfgelknlpllntdkpvqalmkiadelgeifkfeapgrvtrylssqrlike
acdesrfdknlsqalkfvrdfagdglftswtheknwkkahnillpsfsqqamkgyhammv
diavqlvqkwerlnadehievpedmtrltldtiglcgfnyrfnsfyrdqphpfitsmvra
ldeamnklqranpddpaydenkrqfqedikvmndlvdkiiadrkasgeqsddllthmlng
kdpetgeplddeniryqiitfliaghettsgllsfalyflvknphvlqkaaeeaarvlvd
pvpsykqvkqlkyvgmvlnealrlwptapafslyakedtvlggeyplekgdelmvlipql
hrdktiwgddveefrperfenpsaipqhafkpfgngqracigqqfalheatlvlgmmlkh
fdfedhtnyeldiketltlkpegfvvkakskkipl
>d1faha_ 1.100.1.1.2 Cytochrome P450 {Bacillus megaterium}
tikempqpktfgelknlpllntdkpvqalmkiadelgeifkfeapgrvtrylssqrlike
acdesrfdknlsqalkfvrdfagdglftswtheknwkkahnillpsfsqqamkgyhammv
diavqlvqkwerlnadehievpedmtrltldtiglcgfnyrfnsfyrdqphpfitsmvra
ldeamnklqranpddpaydenkrqfqedikvmndlvdkiiadrkasgeqsddllthmlng
kdpetgeplddeniryqiitfliagheatsgllsfalyflvknphvlqkaaeeaarvlvd
pvpsykqvkqlkyvgmvlnealrlwptapafslyakedtvlggeyplekgdelmvlipql
hrdktiwgddveefrperfenpsaipqhafkpfgngqracigqqfalheatlvlgmmlkh
fdfedhtnyeldiketltlkpegfvvkakskkipl
>d1fahb_ 1.100.1.1.2 Cytochrome P450 {Bacillus megaterium}
tikempqpktfgelknlpllntdkpvqalmkiadelgeifkfeapgrvtrylssqrlike
acdesrfdknlsqalkfvrdfagdglftswtheknwkkahnillpsfsqqamkgyhammv
diavqlvqkwerlnadehievpedmtrltldtiglcgfnyrfnsfyrdqphpfitsmvra
ldeamnklqranpddpaydenkrqfqedikvmndlvdkiiadrkasgeqsddllthmlng
kdpetgeplddeniryqiitfliagheatsgllsfalyflvknphvlqkaaeeaarvlvd
pvpsykqvkqlkyvgmvlnealrlwptapafslyakedtvlggeyplekgdelmvlipql
hrdktiwgddveefrperfenpsaipqhafkpfgngqracigqqfalheatlvlgmmlkh
fdfedhtnyeldiketltlkpegfvvkakskkipl
>d1faih1 2.1.1.1.24 (1-123) Immunoglobulin (variable domains of L and H chains) {Fab R19.9 (mouse), kappa L chain}
qvqlqqsgaelvragssvkmsckasgytftsygvnwvkqrpgqglewigyinpgkgylsy
nekfkgkttltvdrssstaymqlrsltsedaavyfcarsfyggsdlavyyfdswgqgttl
tvs
>d1faih2 2.1.1.2.33 (124-221) Immunoglobulin (constant domains of L and H chains) {Fab R19.9 (mouse), kappa L chain}
sakttppsvyplapgcgdttgssvtlgclvkgyfpesvtvtwnsgslsssvhtfpallqs
alytmsssvtvpsstwpsqtvtcsvahpassttvdkkl
>d1fail1 2.1.1.1.24 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab R19.9 (mouse), kappa L chain}
diqmtqttsslsaslgdrvtiscrasqdisnylnwyqqkpdgtvklliyytsrlhsgvps
rfsgsgsgtdysltisnlehediatyfcqqgstlprtfgggtkleikr
>d1fail2 2.1.1.2.33 (109-214) Immunoglobulin (constant domains of L and H chains) {Fab R19.9 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1faj__ 2.35.5.1.3 Inorganic pyrophosphatase {Escherichia coli}
sllnvpagkdlpediyvvieipanadpikyeidkesgalfvdrfmstamfypcnygyinh
tlsldgdpvdvlvptpyplqpgsvircrpvgvlkmtdeagedaklvavphsklskeydhi
kdvndlpellkaqiahffehykdlekgkwvkvegwenaeaakaeivasferak
>d1fan__ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnaksaedcmrtcgga
>d1fapa_ 4.23.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1fapb_ 1.25.7.1.1 FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP) {Human (Homo sapiens)}
rvailwhemwhegleeasrlyfgernvkgmfevleplhammergpqtlketsfnqaygrd
lmeaqewcrkymksgnvkdltqawdlyyhvfrris
>d1faq__ 7.41.1.1.2 RAF-1 {Human (Homo sapiens)}
ltthnfarktflklafcdicqkfllngfrcqtcgykfhehcstkvptmcvdw
>d1far__ 7.41.1.1.2 RAF-1 {Human (Homo sapiens)}
ltthnfarktflklafcdicqkfllngfrcqtcgykfhehcstkvptmcvdw
>d1fas__ 7.7.1.1.3 Fasciculin {Green mamba (Dendroaspis angusticeps)}
tmcyshtttsrailtncgenscyrksrrhppkmvlgrgcgcppgddylevkcctspdkcn
y
>d1fata_ 2.26.1.1.15 Phytohemagglutinin-L, PHA-L, also arcelin {Kidney bean (Phaseolus vulgaris)}
sndiyfnfqrfnetnlilqrdasvsssgqlrltnlngngeprvgslgrafysapiqiwdn
ttgtvasfatsftfniqvpnnagpadglafalvpvgsqpkdkggflglfdgsnsnfhtva
vefdtlynkdwdpterhigidvnsirsikttrwdfvngenaevlitydsstnllvaslvy
psqktsfivsdtvdlksvlpewvsvgfsattginkgnvetndvlswsfaskls
>d1fatb_ 2.26.1.1.15 Phytohemagglutinin-L, PHA-L, also arcelin {Kidney bean (Phaseolus vulgaris)}
sndiyfnfqrfnetnlilqrdasvsssgqlrltnlngngeprvgslgrafysapiqiwdn
ttgtvasfatsftfniqvpnnagpadglafalvpvgsqpkdkggflglfdgsnsnfhtva
vefdtlynkdwdpterhigidvnsirsikttrwdfvngenaevlitydsstnllvaslvy
psqktsfivsdtvdlksvlpewvsvgfsattginkgnvetndvlswsfaskls
>d1fatc_ 2.26.1.1.15 Phytohemagglutinin-L, PHA-L, also arcelin {Kidney bean (Phaseolus vulgaris)}
sndiyfnfqrfnetnlilqrdasvsssgqlrltnlngngeprvgslgrafysapiqiwdn
ttgtvasfatsftfniqvpnnagpadglafalvpvgsqpkdkggflglfdgsnsnfhtva
vefdtlynkdwdpterhigidvnsirsikttrwdfvngenaevlitydsstnllvaslvy
psqktsfivsdtvdlksvlpewvsvgfsattginkgnvetndvlswsfaskls
>d1fatd_ 2.26.1.1.15 Phytohemagglutinin-L, PHA-L, also arcelin {Kidney bean (Phaseolus vulgaris)}
sndiyfnfqrfnetnlilqrdasvsssgqlrltnlngngeprvgslgrafysapiqiwdn
ttgtvasfatsftfniqvpnnagpadglafalvpvgsqpkdkggflglfdgsnsnfhtva
vefdtlynkdwdpterhigidvnsirsikttrwdfvngenaevlitydsstnllvaslvy
psqktsfivsdtvdlksvlpewvsvgfsattginkgnvetndvlswsfaskls
>d1faxa_ 2.41.1.2.33 Coagulation factor Xa (Chrismas factor), protease domain {Human (Homo sapiens)}
ivggqeckdgecpwqallineenegfcggtilsefyiltaahclyqakrfkvrvgdrnta
aeeggeavhevevvikhnrftketydfdiavlrlktpitfrmnvapaclperdwaestlm
tqktgivsgfgrthekgrqstrlkmlevpyvdrnscklsssfiitqnmfcagydtkqeda
cqgdsggphvtrfkdtyfvtgivswgegcarkgkygiytkvtaflkwidrsmktr
>d1faxl_ 7.3.11.1.5 Factor X, N-terminal module {Human (Homo sapiens)}
trklcsldngdcdqfcheeqasvvcscargytladngkaciptgpypcgkqtler
>d1fbaa_ 3.1.9.1.4 Fructose-1,6-bisphosphate aldolase {Drosophila melanogaster, strain sevelen (wild type, pupea)}
xttyfnypskelqdelreiaqkivapgkgilaadesgptmgkrlqdigventednrrayr
qllfstdpklaenisgvilfhetlyqkaddgtpfaeilkkkgiilgikvdkgvvplfgse
devttqglddlaarcaqykkdgcdfakwrcvlkigkntpsyqsilenanvlaryasicqs
qrivpivepevlpdgdhdldraqkvtetvlaavykalsdhhvylegtllkpnmvtagqsa
kkntpeeialatvqalrrtvpaavtgvtflsggqseeeatvnlsainnvplirpwaltfs
ygralqasvlrawagkkeniaagqnellkrakangdaaqgkyvagsagagsgslfvanha
y
>d1fbab_ 3.1.9.1.4 Fructose-1,6-bisphosphate aldolase {Drosophila melanogaster, strain sevelen (wild type, pupea)}
xttyfnypskelqdelreiaqkivapgkgilaadesgptmgkrlqdigventednrrayr
qllfstdpklaenisgvilfhetlyqkaddgtpfaeilkkkgiilgikvdkgvvplfgse
devttqglddlaarcaqykkdgcdfakwrcvlkigkntpsyqsilenanvlaryasicqs
qrivpivepevlpdgdhdldraqkvtetvlaavykalsdhhvylegtllkpnmvtagqsa
kkntpeeialatvqalrrtvpaavtgvtflsggqseeeatvnlsainnvplirpwaltfs
ygralqasvlrawagkkeniaagqnellkrakangdaaqgkyvagsagagsgslfvanha
y
>d1fbac_ 3.1.9.1.4 Fructose-1,6-bisphosphate aldolase {Drosophila melanogaster, strain sevelen (wild type, pupea)}
xttyfnypskelqdelreiaqkivapgkgilaadesgptmgkrlqdigventednrrayr
qllfstdpklaenisgvilfhetlyqkaddgtpfaeilkkkgiilgikvdkgvvplfgse
devttqglddlaarcaqykkdgcdfakwrcvlkigkntpsyqsilenanvlaryasicqs
qrivpivepevlpdgdhdldraqkvtetvlaavykalsdhhvylegtllkpnmvtagqsa
kkntpeeialatvqalrrtvpaavtgvtflsggqseeeatvnlsainnvplirpwaltfs
ygralqasvlrawagkkeniaagqnellkrakangdaaqgkyvagsagagsgslfvanha
y
>d1fbad_ 3.1.9.1.4 Fructose-1,6-bisphosphate aldolase {Drosophila melanogaster, strain sevelen (wild type, pupea)}
xttyfnypskelqdelreiaqkivapgkgilaadesgptmgkrlqdigventednrrayr
qllfstdpklaenisgvilfhetlyqkaddgtpfaeilkkkgiilgikvdkgvvplfgse
devttqglddlaarcaqykkdgcdfakwrcvlkigkntpsyqsilenanvlaryasicqs
qrivpivepevlpdgdhdldraqkvtetvlaavykalsdhhvylegtllkpnmvtagqsa
kkntpeeialatvqalrrtvpaavtgvtflsggqseeeatvnlsainnvplirpwaltfs
ygralqasvlrawagkkeniaagqnellkrakangdaaqgkyvagsagagsgslfvanha
y
>d1fbca_ 5.7.1.1.1 Fructose-1,6-bisphosphatase {Pig (Sus scrofa)}
dtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnvt
gdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssni
dclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfml
dpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvg
smvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldiv
ptdihqrapiilgspedvtelleiyqkha
>d1fbcb_ 5.7.1.1.1 Fructose-1,6-bisphosphatase {Pig (Sus scrofa)}
afdtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstn
vtgdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgss
nidclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncf
mldpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygary
vgsmvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavld
ivptdihqrapiilgspedvtelleiyqkha
>d1fbda_ 5.7.1.1.1 Fructose-1,6-bisphosphatase {Pig (Sus scrofa)}
dtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnvt
gdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssni
dclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfml
dpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvg
smvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldiv
ptdihqrapiilgspedvtelleiyqkha
>d1fbdb_ 5.7.1.1.1 Fructose-1,6-bisphosphatase {Pig (Sus scrofa)}
afdtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstn
vtgdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgss
nidclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncf
mldpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygary
vgsmvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavld
ivptdihqrapiilgspedvtelleiyqkha
>d1fbea_ 5.7.1.1.1 Fructose-1,6-bisphosphatase {Pig (Sus scrofa)}
dtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnvt
gdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssni
dclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfml
dpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvg
smvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldiv
ptdihqrapiilgspedvtelleiyqkha
>d1fbeb_ 5.7.1.1.1 Fructose-1,6-bisphosphatase {Pig (Sus scrofa)}
afdtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstn
vtgdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgss
nidclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncf
mldpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygary
vgsmvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavld
ivptdihqrapiilgspedvtelleiyqkha
>d1fbfa_ 5.7.1.1.1 Fructose-1,6-bisphosphatase {Pig (Sus scrofa)}
dtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnvt
gdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssni
dclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfml
dpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvg
smvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldiv
ptdihqrapiilgspedvtelleiyqkha
>d1fbfb_ 5.7.1.1.1 Fructose-1,6-bisphosphatase {Pig (Sus scrofa)}
afdtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstn
vtgdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgss
nidclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncf
mldpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygary
vgsmvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavld
ivptdihqrapiilgspedvtelleiyqkha
>d1fbga_ 5.7.1.1.1 Fructose-1,6-bisphosphatase {Pig (Sus scrofa)}
dtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnvt
gdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssni
dclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfml
dpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvg
smvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldiv
ptdihqrapiilgspedvtelleiyqkha
>d1fbgb_ 5.7.1.1.1 Fructose-1,6-bisphosphatase {Pig (Sus scrofa)}
afdtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstn
vtgdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgss
nidclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncf
mldpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygary
vgsmvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavld
ivptdihqrapiilgspedvtelleiyqkha
>d1fbha_ 5.7.1.1.1 Fructose-1,6-bisphosphatase {Pig (Sus scrofa)}
dtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnvt
gdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssni
dclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfml
dpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvg
smvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldiv
ptdihqrapiilgspedvtelleiyqkha
>d1fbhb_ 5.7.1.1.1 Fructose-1,6-bisphosphatase {Pig (Sus scrofa)}
fdtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnv
tgdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssn
idclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfm
ldpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryv
gsmvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldi
vptdihqrapiilgspedvtelleiyqkha
>d1fbih1 2.1.1.1.53 (1-121) Immunoglobulin (variable domains of L and H chains) {Fab F9.13.7 (mouse), kappa L chain}
qvqlqqpgaelvkpgasvklsckasgytftsywmhwvkqgpgqglewigeidpsdsypny
nekfkgkatltvdkssstaymqlssltsedsavyycaslyyygtsygvldywgqgtsvtv
s
>d1fbih2 2.1.1.2.61 (122-221) Immunoglobulin (constant domains of L and H chains) {Fab F9.13.7 (mouse), kappa L chain}
sakttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqs
dlytlsssvtvpssprpsetvtcnvahpasstkvdkkivp
>d1fbil1 2.1.1.1.53 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab F9.13.7 (mouse), kappa L chain}
diqmtqttsslsaslgdrvtiscrasqdisnylnwyqkkpdgtvklliyytsrlhsgvps
rfsgsgsgtdysltirnleqediatyfcqqgytlpytfgggtkleik
>d1fbil2 2.1.1.2.61 (108-214) Immunoglobulin (constant domains of L and H chains) {Fab F9.13.7 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1fbip1 2.1.1.1.53 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab F9.13.7 (mouse), kappa L chain}
diqmtqttsslsaslgdrvtiscrasqdisnylnwyqkkpdgtvklliyytsrlhsgvps
rfsgsgsgtdysltirnleqediatyfcqqgytlpytfgggtkleik
>d1fbip2 2.1.1.2.61 (108-214) Immunoglobulin (constant domains of L and H chains) {Fab F9.13.7 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1fbiq1 2.1.1.1.53 (1-121) Immunoglobulin (variable domains of L and H chains) {Fab F9.13.7 (mouse), kappa L chain}
qvqlqqpgaelvkpgasvklsckasgytftsywmhwvkqgpgqglewigeidpsdsypny
nekfkgkatltvdkssstaymqlssltsedsavyycaslyyygtsygvldywgqgtsvtv
s
>d1fbiq2 2.1.1.2.61 (122-221) Immunoglobulin (constant domains of L and H chains) {Fab F9.13.7 (mouse), kappa L chain}
sakttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqs
dlytlsssvtvpssprpsetvtcnvahpasstkvdkkivp
>d1fbix_ 4.2.1.2.3 Lysozyme {Guinea fowl (Numida meleagris)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfnsqatnrntdgstdygvlqins
rwwcndgrtpgsrnlcnipcsalqssditatancakkivsdgngmnawvawrkhckgtdv
rvwikgcrl
>d1fbiy_ 4.2.1.2.3 Lysozyme {Guinea fowl (Numida meleagris)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfnsqatnrntdgstdygvlqins
rwwcndgrtpgsrnlcnipcsalqssditatancakkivsdgngmnawvawrkhckgtdv
rvwikgcrl
>d1fbl_1 2.58.1.1.3 (272-466) Collagenase, C-terminal domain {Porcine (Sus scrofa)}
pqtpqvcdskltfdaittlrgelmffkdrfymrtnsfypevelnfisvfwpqvpnglqaa
yeiadrdevrffkgnkywavrgqdvlygypkdihrsfgfpstvknidaavfeedtgktyf
fvahecwrydeykqsmdtgypkmiaeefpgignkvdavfqkdgflyffhgtrqyqfdfkt
kriltlqkanswfnc
>d1fbl_2 4.71.1.9.5 (100-271) Stromelysin-1 (MMP-3) {Porcine (Sus scrofa), fibroblast}
fvltpgnprwenthltyrienytpdlsredvdraiekafqlwsnvspltftkvsegqadi
misfvrgdhrdnspfdgpggnlahafqpgpgiggdahfdederwtknfrdynlyrvaahe
lghslglshstdigalmypnyiytgdvqlsqddidgiqaiygpsenpvqpsg
>d1fbpa_ 5.7.1.1.1 Fructose-1,6-bisphosphatase {Pig (Sus scrofa)}
fdtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnv
tgdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssn
idclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfm
ldpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryv
gsmvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldi
vptdihqrapiilgspedvtelleiyqkha
>d1fbpb_ 5.7.1.1.1 Fructose-1,6-bisphosphatase {Pig (Sus scrofa)}
fdtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnv
tgdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssn
idclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfm
ldpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryv
gsmvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldi
vptdihqrapiilgspedvtelleiyqkha
>d1fbr_1 7.27.1.1.1 (1-46) Fibronectin {Human (Homo sapiens)}
aekcfdhaagtsyvvgetwekpyqgwmmvdctclgegsgritctsr
>d1fbr_2 7.27.1.1.1 (47-93) Fibronectin {Human (Homo sapiens)}
nrcndqdtrtsyrigdtwskkdnrgnllqcictgngrgewkcerhts
>d1fbta_ 3.50.1.4.1 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, phosphatase domain {Rat (Rattus norvegicus)}
rsiylcrhgeselnlrgriggdsglsargkqyayalanfirsqgisslkvwtshxkrtiq
taealgvpyeqwkalneidagvceextyeeiqehypeefalrdqdkyryrypkgesyedl
vqrlepvixelerqenvlvichqavxrcllayfldkssdelpylkcplhtvlkltpvayg
crvesiylnv
>d1fbtb_ 3.50.1.4.1 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, phosphatase domain {Rat (Rattus norvegicus)}
rsiylcrhgeselnlrgriggdsglsargkqyayalanfirsqgisslkvwtshxkrtiq
taealgvpyeqwkalneidagvceextyeeiqehypeefalrdqdkyryrypkgesyedl
vqrlepvixelerqenvlvichqavxrcllayfldkssdelpylkcplhtvlkltpvayg
crvesiylnv
>d1fc1a1 2.1.1.2.139 (238-341) Immunoglobulin (constant domains of L and H chains) {Fc (human) IgG1 class}
psvflfppkpkdtlmisrtpevtcvvvdvshedpqvkfnwyvdgvqvhnaktkpreqqyn
styrvvsvltvlhqnwldgkeykckvsnkalpapiektiskakg
>d1fc1a2 2.1.1.2.139 (342-444) Immunoglobulin (constant domains of L and H chains) {Fc (human) IgG1 class}
qprepqvytlppsreemtknqvsltclvkgfypsdiavewesngqpennykttppvldsd
gsfflyskltvdksrwqqgnvfscsvmhealhnhytqkslsls
>d1fc1b1 2.1.1.2.139 (238-341) Immunoglobulin (constant domains of L and H chains) {Fc (human) IgG1 class}
psvflfppkpkdtlmisrtpevtcvvvdvshedpqvkfnwyvdgvqvhnaktkpreqqyn
styrvvsvltvlhqnwldgkeykckvsnkalpapiektiskakg
>d1fc1b2 2.1.1.2.139 (342-444) Immunoglobulin (constant domains of L and H chains) {Fc (human) IgG1 class}
qprepqvytlppsreemtknqvsltclvkgfypsdiavewesngqpennykttppvldsd
gsfflyskltvdksrwqqgnvfscsvmhealhnhytqkslsls
>d1fc2c_ 1.8.1.1.1 Immunoglobulin-binding protein A modules {Staphylococcus aureus}
fnkeqqnafyeilhlpnlneeqrngfiqslkddpsqsanllaea
>d1fc2d1 2.1.1.2.139 (238-341) Immunoglobulin (constant domains of L and H chains) {Fc (human) IgG1 class}
psvflfppkpkdtlmisrtpevtcvvvdvshedpqvkfnwyvdgvqvhnaktkpreqqyn
styrvvsvltvlhqnwldgkeykckvsnkalpapiektiskakg
>d1fc2d2 2.1.1.2.139 (342-444) Immunoglobulin (constant domains of L and H chains) {Fc (human) IgG1 class}
qprepqvytlppsreemtknqvsltclvkgfypsdiavewesngqpennykttppvldsd
gsfflyskltvdksrwqqgnvfscsvmhealhnhytqkslsls
>d1fca__ 4.47.1.1.3 Ferredoxin II {Closridium acidi-urici}
ayvineaciscgacepecpvdaisqggsryvidadtcidcgacagvcpvdapvqa
>d1fcba1 3.1.4.1.6 (98-511) Flavocytochrome b2, C-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
apgetkediarkeqlksllppldniinlydfeylasqtltkqawayyssgandevthren
hnayhriffkpkilvdvrkvdistdmlgshvdvpfyvsatalcklgnplegekdvargcg
qgvtkvpqmistlascspeeiieaapsdkqiqwyqlyvnsdrkitddlvknveklgvkal
fvtvdapslgqrekdmklkfsntkagpkamkktnveesqgasralskfidpsltwkdiee
lkkktklpivikgvqrtedvikaaeigvsgvvlsnhggrqldfsrapievlaetmpileq
rnlkdklevfvdggvrrgtdvlkalclgakgvglgrpflyanscygrngvekaieilrde
iemsmrllgvtsiaelkpdlldlstlkartvgvpndvlynevyegptltefeda
>d1fcba2 4.94.1.1.4 (1-97) Flavocytochrome b2, N-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
epkldmnkqkispaevakhnkpddcwvvingyvydltrflpnhpggqdvikfnagkdvta
ifeplhapnvidkyiapekklgplqgsmppelvcppy
>d1fcbb1 3.1.4.1.6 Flavocytochrome b2, C-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
getkediarkeqlksllppldniinlydfeylasqtltkqawayyssgandevthrenhn
ayhriffkpkilvdvrkvdistdmlgshvdvpfyvsatalcklgnplegekdvargcgqg
vtkvpqmistlascspeeiieaapsdkqiqwyqlyvnsdrkitddlvknveklgvkalfv
tvdapslgqrekdmklkfsntkagpkamkktnveesqgasralskfidpsltwkdieelk
kktklpivikgvqrtedvikaaeigvsgvvlsnhggrqldfsrapievlaetmpileqrn
lkdklevfvdggvrrgtdvlkalclgakgvglgrpflyanscygrngvekaieilrdeie
msmrllgvtsiaelkpdlldlstlkartvgvpndvlynevyegptltefeda
>d1fcca1 2.1.1.2.139 (238-341) Immunoglobulin (constant domains of L and H chains) {Fc (human) IgG1 class}
psvflfppkpkdtlmisrtpevtcvvvdvshedpqvkfnwyvdgvqvhnaktkpreqqyn
styrvvsvltvlhqnwldgkeykckvsnkalpapiektiskakg
>d1fcca2 2.1.1.2.139 (342-443) Immunoglobulin (constant domains of L and H chains) {Fc (human) IgG1 class}
qprepqvytlppsreemtknqvsltclvkgfypsdiavewesngqpennykttppvldsd
gsfflyskltvdksrwqqgnvfscsvmhealhnhytqkslsl
>d1fccc_ 4.13.1.1.1 Immunoglobulin-binding protein G, different constituent domains {Group G Streptococcus)}
ttyklvingktlkgettteavdaataekvfkqyandngvdgewtyddatktftvte
>d1fcda1 3.3.1.5.11 (1-114,256-327) Flavocytochrome c sulfide dehydrogenase, FCSD, flavin-binding subunit {Purple phototrophic bacterium (Chromatium vinosum)}
agrkvvvvgggtggataakyikladpsievtliepntdyytcylsneviggdrklesikh
gydglrahgiqvvhdsatgidpdkklvktaggaefgydrcvvapgieliydkieXqragk
iaqiagltndagwcpvdiktfessihkgihvigdasianpmpksgysansqgkvaaaavv
vllkgee
>d1fcda2 3.3.1.5.11 (115-255) Flavocytochrome c sulfide dehydrogenase, FCSD, flavin-binding subunit {Purple phototrophic bacterium (Chromatium vinosum)}
gyseeaaaklphawkageqtailrkqledmadggtvviappaapfrcppgpyerasqvay
ylkahkpmskviildssqtfskqsqfskgwerlygfgtenamiewhpgpdsavvkvdgge
mmvetafgdefkadvinlipp
>d1fcda3 4.67.1.1.9 (328-401) Flavocytochrome c sulfide dehydrogenase, FCSD, flavin-binding subunit {Purple phototrophic bacterium (Chromatium vinosum)}
pgtpsylntcysilapaygisvaaiyrpnadgsaiesvpdsggvtpvdapdwvlerevqy
ayswynnivhdtfg
>d1fcdb1 3.3.1.5.11 (1-114,256-327) Flavocytochrome c sulfide dehydrogenase, FCSD, flavin-binding subunit {Purple phototrophic bacterium (Chromatium vinosum)}
agrkvvvvgggtggataakyikladpsievtliepntdyytcylsneviggdrklesikh
gydglrahgiqvvhdsatgidpdkklvktaggaefgydrcvvapgieliydkieXqragk
iaqiagltndagwcpvdiktfessihkgihvigdasianpmpksgysansqgkvaaaavv
vllkgee
>d1fcdb2 3.3.1.5.11 (115-255) Flavocytochrome c sulfide dehydrogenase, FCSD, flavin-binding subunit {Purple phototrophic bacterium (Chromatium vinosum)}
gyseeaaaklphawkageqtailrkqledmadggtvviappaapfrcppgpyerasqvay
ylkahkpmskviildssqtfskqsqfskgwerlygfgtenamiewhpgpdsavvkvdgge
mmvetafgdefkadvinlipp
>d1fcdb3 4.67.1.1.9 (328-401) Flavocytochrome c sulfide dehydrogenase, FCSD, flavin-binding subunit {Purple phototrophic bacterium (Chromatium vinosum)}
pgtpsylntcysilapaygisvaaiyrpnadgsaiesvpdsggvtpvdapdwvlerevqy
ayswynnivhdtfg
>d1fcdc1 1.3.1.3.2 (1-80) Flavocytochrome c sulfide dehydrogenase, FCSD, cytochrome subunit {Purple phototrophic bacterium (Cromatium vinosum)}
eptaemltnncagchgthgnsvgpaspsiaqmdpmvfvevmegfksgeiastimgriakg
ystadfekmagyfkqqtyqp
>d1fcdc2 1.3.1.3.2 (81-174) Flavocytochrome c sulfide dehydrogenase, FCSD, cytochrome subunit {Purple phototrophic bacterium (Cromatium vinosum)}
akqsfdtaladtgaklhdkycekchveggkpladeedyhilagqwtpylqyamsdfreer
rpmekkmasklrellkaegdagldalfafyasqq
>d1fcdd1 1.3.1.3.2 (1-80) Flavocytochrome c sulfide dehydrogenase, FCSD, cytochrome subunit {Purple phototrophic bacterium (Cromatium vinosum)}
eptaemltnncagchgthgnsvgpaspsiaqmdpmvfvevmegfksgeiastimgriakg
ystadfekmagyfkqqtyqp
>d1fcdd2 1.3.1.3.2 (81-174) Flavocytochrome c sulfide dehydrogenase, FCSD, cytochrome subunit {Purple phototrophic bacterium (Cromatium vinosum)}
akqsfdtaladtgaklhdkycekchveggkpladeedyhilagqwtpylqyamsdfreer
rpmekkmasklrellkaegdagldalfafyasqq
>d1fce__ 1.98.1.2.4 Processive endocellulase CelF {Clostridium cellulolyticum}
asspankvyqdrfesmyskikdpangyfseqgipyhsietlmveapdyghvttseamsyy
mwleamhgrfsgdftgfdkswsvteqyliptekdqpntsmsrydankpatyapefqdpsk
ypspldtsqpvgrdpinsqltsaygtsmlygmhwildvdnwygfgaradgtskpsyintf
qrgeqestwetipqpcwdehkfggqygfldlftkdtgtpakqfkytnapdadaravqaty
wadqwakeqgksvstsvgkatkmgdylrysffdkyfrkigqpsqagtgydaahyllswyy
awgggidstwswiigsshnhfgyqnpfaawvlstdanfkpkssngasdwaksldrqlefy
qwlqsaegaiaggatnswngryeavpsgtstfygmgyvenpvyadpgsntwfgmqvwsmq
rvaelyyktgdarakklldkwakwingeikfnadgtfqipstidwegqpdtwnptqgytg
nanlhvkvvnygtdlgcasslantltyyaaksgdetsrqnaqklldamwnnysdskgist
veqrgdyhrfldqevfvpagwtgkmpngdviksgvkfidirskykqdpewqtmvaalqag
qvptqrlhrfwaqsefavangvyailfpd
>d1fcpa_ 6.4.3.3.1 Ferric hydroxamate uptake receptor FhuA {Escherichia coli}
esawgpaatiaarqsatgtktdtpiqkvpqsisvvtaeexalhqpksvkealsytpgvsv
gtrgasntydhliirgfaaegqsqnnylnglklqgnfyndavidpyxleraeixrgpvsv
lygksspggllnxvskrptteplkevqfkagtdslfqtgfdfsdsldddgvysyrltgla
rsanaqqkgseeqryaiapaftwrpddktnftflsyfqnepetgyygwlpkegtveplpn
gkrlptdfnegaknntysrnekxvgysfdhefndtftvrqnlrfaenktsqnsvygygvc
sdpanayskqcaalapadkghylarkyvvddeklqnfsvdtqlqskfatgdidhtlltgv
dfxrxrndinawfgyddsvpllnlynpshhhhhhgsvntdfdfnakdpansgpyrilnkq
kqtgvyvqdqaqwdkvlvtlggrydwadqeslnrvagttdkrddkqftwrggvnylfdng
vtpyfsysesfepssqvgkdgnifapskgkqyevgvkyvpedrpivvtgavynltktnnl
xadpegsffsveggeirargveieakaalsasvnvvgsytytdaeyttdttykgntpaqv
pkhxaslwadytffdgplsgltlgtggrytgssygdpansfkvgsytvvdalvrydlarv
gxagsnvalhvnnlfdreyvascfntygcfwgaerqvvatatfrf
>d1fcs__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkvgvrvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gnfgadaqgamnkalelfrkdiaakykelgyqg
>d1fd2__ 4.47.1.2.1 Ferredoxin {Azotobacter vinelandii}
afvvtdncikckytdcvevapvdcfyegpnflvihpdecidcalcepecpaqaifsedev
pedmqefiqlnaelaevwpnitekkdplpdaedwdgvkgklqhler
>d1fda__ 4.47.1.2.1 Ferredoxin {Azotobacter vinelandii}
afvvtdncikckytdcvevcpvdcfyegpnflvihpdecidcalcepecpaqaifsedev
pedmqefiqlnaelaevwpnitekkdplpdaedwdgvkgklqhler
>d1fdb__ 4.47.1.2.1 Ferredoxin {Azotobacter vinelandii}
afvvtdncikckytdcvevcpvdcfyegpnflvihpdecidcalcepecpaqaifsedev
pedmqefiqlnaelaevwpnitekkdplpdaedwdgvkgklqhler
>d1fdd__ 4.47.1.2.1 Ferredoxin {Azotobacter vinelandii}
afvvtdncikckytncvevcpvdcfyegpnflvihpdecidcalcepecpaqaifsedev
pedmqefiqlnaelaevwpnitekkdplpdaedwdgvkgklqhler
>d1fdha_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1fdhg_ 1.1.1.1.29 Hemoglobin, beta-chain {Human fetus (Homo sapiens), gamma-chain}
xghfteedkatitslwgkvnvedaggetlgrllvvypwtqrffdsfgnlssasaimgnpk
vkahgkkvltslgdaikhlddlkgtfaqlselhcdklhvdpenfkllgnvlvtvlaihfg
keftpevqaswqkmvtgvasalssryh
>d1fdi_1 2.46.2.2.3 (565-715) Formate dehydrogenase H {Escherichia coli}
pidkltdeypmvlstvrevghyscrsmtgncaalaaladepgyaqintedakrlgiedea
lvwvhsrkgkiitraqvsdrpnkgaiymtyqwwigacnelvtenlspitktpeykycavr
vepiadqraaeqyvideynklktrlreaala
>d1fdi_2 3.70.1.1.3 (1-564) Formate dehydrogenase H {Escherichia coli}
mkkvvtvcpycasgckinlvvdngkivraeaaqgktnqgtlclkgyygwdfindtqiltp
rlktpmirrqrggklepvswdealnyvaerlsaikekygpdaiqttgssrgtgnetnyvm
qkfaravigtnnvdccarvxhgpsvaglhqsvgngamsnaineidntdlvfvfgynpads
hpivanhvinakrngakiivcdprkietariadmhialkngsniallnamghviieenly
dkafvasrtegfeeyrkivegytpesveditgvsaseirqaarmyaqaksaailwgmgvt
qfyqgvetvrsltslamltgnlgkphagvnpvrgqnnvqgacdmgalpdtypgyqyvkdp
anrekfakawgveslpahtgyriselphraahgevraayimgedplqtdaelsavrkafe
dlelvivqdifmtktasaadvilpstswgehegvftaadrgfqrffkavepkwdlktdwq
iiseiatrmgypmhynntqeiwdelrhlcpdfygatyekmgelgfiqwpcrdtsdadqgt
sylfkekfdtpnglaqfftcdwva
>d1fdk__ 1.123.1.2.12 Phospholipase A2 {Bovine (Bos taurus), pancreas}
alwqfngmikckipsseplldfnnygcycglggsgtpvddldrccqthdncykqakklds
ckvlvdnpytnnysyscsnneitcssennaceaficncdrnaaicfskvpynkehknldk
knc
>d1fdlh1 2.1.1.1.42 (1-116) Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
qvqlkesgpglvapsqslsitctvsgfsltgygvnwvrqppgkglewlgmiwgdgntdyn
salksrlsiskdnsksqvflkmnslhtddtaryycarerdyrldywgqgttltvss
>d1fdlh2 2.1.1.2.51 (117-218) Immunoglobulin (constant domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
asttppsvfplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpssprpsetvtcnvahpasstkvdkkivprdc
>d1fdll1 2.1.1.1.42 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
diqmtqspaslsasvgetvtitcrasgnihnylawyqqkqgkspqllvyytttladgvps
rfsgsgsgtqyslkinslqpedfgsyycqhfwstprtfgggtkleik
>d1fdll2 2.1.1.2.51 (108-214) Immunoglobulin (constant domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1fdly_ 4.2.1.2.1 Lysozyme {Chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1fdn__ 4.47.1.1.3 Ferredoxin II {Closridium acidi-urici}
ayvineaciscgacepecpvnaissgddryvidadtcidcgacagvcpvdapvqa
>d1fdo_1 2.46.2.2.3 (565-715) Formate dehydrogenase H {Escherichia coli}
pidkltdeypmvlstvrevghyscrsmtgncaalaaladepgyaqintedakrlgiedea
lvwvhsrkgkiitraqvsdrpnkgaiymtyqwwigacnelvtenlspitktpeykycavr
vepiadqraaeqyvideynklktrlreaala
>d1fdo_2 3.70.1.1.3 (1-564) Formate dehydrogenase H {Escherichia coli}
mkkvvtvcpycasgckinlvvdngkivraeaaqgktnqgtlclkgyygwdfindtqiltp
rlktpmirrqrggklepvswdealnyvaerlsaikekygpdaiqttgssrgtgnetnyvm
qkfaravigtnnvdccarvxhgpsvaglhqsvgngamsnaineidntdlvfvfgynpads
hpivanhvinakrngakiivcdprkietariadmhialkngsniallnamghviieenly
dkafvasrtegfeeyrkivegytpesveditgvsaseirqaarmyaqaksaailwgmgvt
qfyqgvetvrsltslamltgnlgkphagvnpvrgqnnvqgacdmgalpdtypgyqyvkdp
anrekfakawgveslpahtgyriselphraahgevraayimgedplqtdaelsavrkafe
dlelvivqdifmtktasaadvilpstswgehegvftaadrgfqrffkavepkwdlktdwq
iiseiatrmgypmhynntqeiwdelrhlcpdfygatyekmgelgfiqwpcrdtsdadqgt
sylfkekfdtpnglaqfftcdwva
>d1fdr_1 2.38.1.1.4 (2-100) Ferredoxin reductase (flavodoxin reductase) {Escherichia coli}
adwvtgkvtkvqnwtdalfsltvhapvlpftagqftklgleidgervqraysyvnspdnp
dlefylvtvpdgklsprlaalkpgdevqvvseaagffvl
>d1fdr_2 3.18.1.1.4 (101-248) Ferredoxin reductase (flavodoxin reductase) {Escherichia coli}
devphcetlwmlatgtaigpylsilrlgkdldrfknlvlvhaaryaadlsylplmqelek
ryegklriqtvvsretaagsltgripaliesgelestiglpmnketshvmlcgnpqmvrd
tqqllketrqmtkhlrrrpghmtaehyw
>d1fds__ 3.2.1.2.8 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylahskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevfgdv
>d1fdt__ 3.2.1.2.8 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylahskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevfg
>d1fdua_ 3.2.1.2.8 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylalskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevfg
>d1fdub_ 3.2.1.2.8 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylalskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevfg
>d1fduc_ 3.2.1.2.8 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylalskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevfg
>d1fdud_ 3.2.1.2.8 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylalskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevfg
>d1fdva_ 3.2.1.2.8 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylalskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevfg
>d1fdvb_ 3.2.1.2.8 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylalskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevfgd
>d1fdvc_ 3.2.1.2.8 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylalskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevfg
>d1fdvd_ 3.2.1.2.8 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylalskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevfgd
>d1fdw__ 3.2.1.2.8 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylaqskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevfg
>d1fdx__ 4.47.1.1.2 Ferredoxin II {Peptococcus aerogenes}
ayvindsciacgackpecpvniiqgsiyaidadscidcgscasvcpvgapnped
>d1fdya_ 3.1.9.1.1 N-acetylneuraminate lyase {Escherichia coli}
nlrgvmaalltpfdqqqaldkaslrrlvqfniqqgidglyvggstgeafvqslsereqvl
eivaeegkgkikliahvgcvttaesqqlaasakrygfdavsavtpfyypfsfeehcdhyr
aiidsadglpmvvynipalsgvkltldqintlvtlpgvgalkqtsgdlyqmeqirrehpd
lvlyngydeifasgllagadggigstynimgwryqgivkalkegdiqtaqklqtecnkvi
dlliktgvfrglktvlhymdvvsvplcrkpfgpvdekylpelkalaqqlmqe
>d1fdyb_ 3.1.9.1.1 N-acetylneuraminate lyase {Escherichia coli}
nlrgvmaalltpfdqqqaldkaslrrlvqfniqqgidglyvggstgeafvqslsereqvl
eivaeegkgkikliahvgcvttaesqqlaasakrygfdavsavtpfyypfsfeehcdhyr
aiidsadglpmvvynipalsgvkltldqintlvtlpgvgalkqtsgdlyqmeqirrehpd
lvlyngydeifasgllagadggigstynimgwryqgivkalkegdiqtaqklqtecnkvi
dlliktgvfrglktvlhymdvvsvplcrkpfgpvdekylpelkalaqqlmq
>d1fdyc_ 3.1.9.1.1 N-acetylneuraminate lyase {Escherichia coli}
nlrgvmaalltpfdqqqaldkaslrrlvqfniqqgidglyvggstgeafvqslsereqvl
eivaeegkgkikliahvgcvttaesqqlaasakrygfdavsavtpfyypfsfeehcdhyr
aiidsadglpmvvynipalsgvkltldqintlvtlpgvgalkqtsgdlyqmeqirrehpd
lvlyngydeifasgllagadggigstynimgwryqgivkalkegdiqtaqklqtecnkvi
dlliktgvfrglktvlhymdvvsvplcrkpfgpvdekylpelkalaqqlmq
>d1fdyd_ 3.1.9.1.1 N-acetylneuraminate lyase {Escherichia coli}
nlrgvmaalltpfdqqqaldkaslrrlvqfniqqgidglyvggstgeafvqslsereqvl
eivaeegkgkikliahvgcvttaesqqlaasakrygfdavsavtpfyypfsfeehcdhyr
aiidsadglpmvvynipalsgvkltldqintlvtlpgvgalkqtsgdlyqmeqirrehpd
lvlyngydeifasgllagadggigstynimgwryqgivkalkegdiqtaqklqtecnkvi
dlliktgvfrglktvlhymdvvsvplcrkpfgpvdekylpelkalaqqlmq
>d1fdza_ 3.1.9.1.1 N-acetylneuraminate lyase {Escherichia coli}
nlrgvmaalltpfdqqqaldkaslrrlvqfniqqgidglyvggstgeafvqslsereqvl
eivaeegkgkikliahvgcvttaesqqlaasakrygfdavsavtpfyypfsfeehcdhyr
aiidsadglpmvvynipalsgvkltldqintlvtlpgvgalkqtsgdlyqmeqirrehpd
lvlyngydeifasgllagadggigstynimgwryqgivkalkegdiqtaqklqtecnkvi
dlliktgvfrglktvlhymdvvsvplcrkpfgpvdekylpelkalaqqlmqe
>d1fdzb_ 3.1.9.1.1 N-acetylneuraminate lyase {Escherichia coli}
nlrgvmaalltpfdqqqaldkaslrrlvqfniqqgidglyvggstgeafvqslsereqvl
eivaeegkgkikliahvgcvttaesqqlaasakrygfdavsavtpfyypfsfeehcdhyr
aiidsadglpmvvynipalsgvkltldqintlvtlpgvgalkqtsgdlyqmeqirrehpd
lvlyngydeifasgllagadggigstynimgwryqgivkalkegdiqtaqklqtecnkvi
dlliktgvfrglktvlhymdvvsvplcrkpfgpvdekylpelkalaqqlmq
>d1fdzc_ 3.1.9.1.1 N-acetylneuraminate lyase {Escherichia coli}
nlrgvmaalltpfdqqqaldkaslrrlvqfniqqgidglyvggstgeafvqslsereqvl
eivaeegkgkikliahvgcvttaesqqlaasakrygfdavsavtpfyypfsfeehcdhyr
aiidsadglpmvvynipalsgvkltldqintlvtlpgvgalkqtsgdlyqmeqirrehpd
lvlyngydeifasgllagadggigstynimgwryqgivkalkegdiqtaqklqtecnkvi
dlliktgvfrglktvlhymdvvsvplcrkpfgpvdekylpelkalaqqlmq
>d1fdzd_ 3.1.9.1.1 N-acetylneuraminate lyase {Escherichia coli}
nlrgvmaalltpfdqqqaldkaslrrlvqfniqqgidglyvggstgeafvqslsereqvl
eivaeegkgkikliahvgcvttaesqqlaasakrygfdavsavtpfyypfsfeehcdhyr
aiidsadglpmvvynipalsgvkltldqintlvtlpgvgalkqtsgdlyqmeqirrehpd
lvlyngydeifasgllagadggigstynimgwryqgivkalkegdiqtaqklqtecnkvi
dlliktgvfrglktvlhymdvvsvplcrkpfgpvdekylpelkalaqqlmqe
>d1feaa1 3.3.1.5.3 (1-169,287-357) Trypanothione reductase {Crithidia fasciculata}
sraydlvvigagsggleagwnaaslhkkrvavidlqkhhgpphyaalggtcvnvgcvpkk
lmvtganymdtiresagfgweldresvrpnwkaliaaknkavsgindsyegmfadteglt
fhqgfgalqdnhtvlvresadpnsavletldteyillatgswpqhlgieXvprsqtlqle
kagvevakngaikvdaysktnvdniyaigdvtdrvmltpvainegaafvdtvfankprat
d
>d1feaa2 3.3.1.5.3 (170-286) Trypanothione reductase {Crithidia fasciculata}
gddlcitsneafyldeapkralcvgggyisiefagifnaykarggqvdlayrgdmilrgf
dselrkqlteqlranginvrthenpakvtknadgtrhvvfesgaeadydvvmlaigr
>d1feaa3 4.67.1.1.3 (358-487) Trypanothione reductase {Crithidia fasciculata}
htkvacavfsippmgvcgyveedaakkydqvavyessftplmhnisgstykkfmvrivtn
hadgevlgvhmlgdsspeiiqsvaiclkmgakisdfyntigvhptsaeelcsmrtpayfy
ekgkrvekid
>d1feab1 3.3.1.5.3 (1-169,287-357) Trypanothione reductase {Crithidia fasciculata}
sraydlvvigagsggleagwnaaslhkkrvavidlqkhhgpphyaalggtcvnvgcvpkk
lmvtganymdtiresagfgweldresvrpnwkaliaaknkavsgindsyegmfadteglt
fhqgfgalqdnhtvlvresadpnsavletldteyillatgswpqhlgieXvprsqtlqle
kagvevakngaikvdaysktnvdniyaigdvtdrvmltpvainegaafvdtvfankprat
d
>d1feab2 3.3.1.5.3 (170-286) Trypanothione reductase {Crithidia fasciculata}
gddlcitsneafyldeapkralcvgggyisiefagifnaykarggqvdlayrgdmilrgf
dselrkqlteqlranginvrthenpakvtknadgtrhvvfesgaeadydvvmlaigr
>d1feab3 4.67.1.1.3 (358-484) Trypanothione reductase {Crithidia fasciculata}
htkvacavfsippmgvcgyveedaakkydqvavyessftplmhnisgstykkfmvrivtn
hadgevlgvhmlgdsspeiiqsvaiclkmgakisdfyntigvhptsaeelcsmrtpayfy
ekgkrve
>d1feac1 3.3.1.5.3 (1-169,287-357) Trypanothione reductase {Crithidia fasciculata}
sraydlvvigagsggleagwnaaslhkkrvavidlqkhhgpphyaalggtcvnvgcvpkk
lmvtganymdtiresagfgweldresvrpnwkaliaaknkavsgindsyegmfadteglt
fhqgfgalqdnhtvlvresadpnsavletldteyillatgswpqhlgieXvprsqtlqle
kagvevakngaikvdaysktnvdniyaigdvtdrvmltpvainegaafvdtvfankprat
d
>d1feac2 3.3.1.5.3 (170-286) Trypanothione reductase {Crithidia fasciculata}
gddlcitsneafyldeapkralcvgggyisiefagifnaykarggqvdlayrgdmilrgf
dselrkqlteqlranginvrthenpakvtknadgtrhvvfesgaeadydvvmlaigr
>d1feac3 4.67.1.1.3 (358-487) Trypanothione reductase {Crithidia fasciculata}
htkvacavfsippmgvcgyveedaakkydqvavyessftplmhnisgstykkfmvrivtn
hadgevlgvhmlgdsspeiiqsvaiclkmgakisdfyntigvhptsaeelcsmrtpayfy
ekgkrvekid
>d1fead1 3.3.1.5.3 (1-169,287-357) Trypanothione reductase {Crithidia fasciculata}
sraydlvvigagsggleagwnaaslhkkrvavidlqkhhgpphyaalggtcvnvgcvpkk
lmvtganymdtiresagfgweldresvrpnwkaliaaknkavsgindsyegmfadteglt
fhqgfgalqdnhtvlvresadpnsavletldteyillatgswpqhlgieXvprsqtlqle
kagvevakngaikvdaysktnvdniyaigdvtdrvmltpvainegaafvdtvfankprat
d
>d1fead2 3.3.1.5.3 (170-286) Trypanothione reductase {Crithidia fasciculata}
gddlcitsneafyldeapkralcvgggyisiefagifnaykarggqvdlayrgdmilrgf
dselrkqlteqlranginvrthenpakvtknadgtrhvvfesgaeadydvvmlaigr
>d1fead3 4.67.1.1.3 (358-484) Trypanothione reductase {Crithidia fasciculata}
htkvacavfsippmgvcgyveedaakkydqvavyessftplmhnisgstykkfmvrivtn
hadgevlgvhmlgdsspeiiqsvaiclkmgakisdfyntigvhptsaeelcsmrtpayfy
ekgkrve
>d1feba1 3.3.1.5.3 (1-169,287-357) Trypanothione reductase {Crithidia fasciculata}
sraydlvvigagsggleagwnaaslhkkrvavidlqkhhgpphyaalggtcvnvgcvpkk
lmvtganymdtiresagfgweldresvrpnwkaliaaknkavsgindsyegmfadteglt
fhqgfgalqdnhtvlvresadpnsavletldteyillatgswpqhlgieXvprsqtlqle
kagvevakngaikvdaysktnvdniyaigdvtdrvmltpvainegaafvdtvfankprat
d
>d1feba2 3.3.1.5.3 (170-286) Trypanothione reductase {Crithidia fasciculata}
gddlcitsneafyldeapkralcvgggyisiefagifnaykarggqvdlayrgdmilrgf
dselrkqlteqlranginvrthenpakvtknadgtrhvvfesgaeadydvvmlaigr
>d1feba3 4.67.1.1.3 (358-487) Trypanothione reductase {Crithidia fasciculata}
htkvacavfsippmgvcgyveedaakkydqvavyessftplmhnisgstykkfmvrivtn
hadgevlgvhmlgdsspeiiqsvaiclkmgakisdfyntigvhptsaeelcsmrtpayfy
ekgkrvekid
>d1febb1 3.3.1.5.3 (1-169,287-357) Trypanothione reductase {Crithidia fasciculata}
sraydlvvigagsggleagwnaaslhkkrvavidlqkhhgpphyaalggtcvnvgcvpkk
lmvtganymdtiresagfgweldresvrpnwkaliaaknkavsgindsyegmfadteglt
fhqgfgalqdnhtvlvresadpnsavletldteyillatgswpqhlgieXvprsqtlqle
kagvevakngaikvdaysktnvdniyaigdvtdrvmltpvainegaafvdtvfankprat
d
>d1febb2 3.3.1.5.3 (170-286) Trypanothione reductase {Crithidia fasciculata}
gddlcitsneafyldeapkralcvgggyisiefagifnaykarggqvdlayrgdmilrgf
dselrkqlteqlranginvrthenpakvtknadgtrhvvfesgaeadydvvmlaigr
>d1febb3 4.67.1.1.3 (358-484) Trypanothione reductase {Crithidia fasciculata}
htkvacavfsippmgvcgyveedaakkydqvavyessftplmhnisgstykkfmvrivtn
hadgevlgvhmlgdsspeiiqsvaiclkmgakisdfyntigvhptsaeelcsmrtpayfy
ekgkrve
>d1feca1 3.3.1.5.3 (1-169,287-357) Trypanothione reductase {Crithidia fasciculata}
sraydlvvigagsggleagwnaaslhkkrvavidlqkhhgpphyaalggtcvnvgcvpkk
lmvtganymdtiresagfgweldresvrpnwkaliaaknkavsgindsyegmfadteglt
fhqgfgalqdnhtvlvresadpnsavletldteyillatgswpqhlgieXvprsqtlqle
kagvevakngaikvdaysktnvdniyaigdvtdrvmltpvainegaafvdtvfankprat
d
>d1feca2 3.3.1.5.3 (170-286) Trypanothione reductase {Crithidia fasciculata}
gddlcitsneafyldeapkralcvgggyisiefagifnaykarggqvdlayrgdmilrgf
dselrkqlteqlranginvrthenpakvtknadgtrhvvfesgaeadydvvmlaigr
>d1feca3 4.67.1.1.3 (358-485) Trypanothione reductase {Crithidia fasciculata}
htkvacavfsippmgvcgyveedaakkydqvavyessftplmhnisgstykkfmvrivtn
hadgevlgvhmlgdsspeiiqsvaiclkmgakisdfyntigvhptsaeelcsmrtpayfy
ekgkrvek
>d1fecb1 3.3.1.5.3 (2-169,287-357) Trypanothione reductase {Crithidia fasciculata}
raydlvvigagsggleagwnaaslhkkrvavidlqkhhgpphyaalggtcvnvgcvpkkl
mvtganymdtiresagfgweldresvrpnwkaliaaknkavsgindsyegmfadtegltf
hqgfgalqdnhtvlvresadpnsavletldteyillatgswpqhlgieXvprsqtlqlek
agvevakngaikvdaysktnvdniyaigdvtdrvmltpvainegaafvdtvfankpratd
>d1fecb2 3.3.1.5.3 (170-286) Trypanothione reductase {Crithidia fasciculata}
gddlcitsneafyldeapkralcvgggyisiefagifnaykarggqvdlayrgdmilrgf
dselrkqlteqlranginvrthenpakvtknadgtrhvvfesgaeadydvvmlaigr
>d1fecb3 4.67.1.1.3 (358-486) Trypanothione reductase {Crithidia fasciculata}
htkvacavfsippmgvcgyveedaakkydqvavyessftplmhnisgstykkfmvrivtn
hadgevlgvhmlgdsspeiiqsvaiclkmgakisdfyntigvhptsaeelcsmrtpayfy
ekgkrveki
>d1feha1 3.86.1.1.1 (210-574) Fe-only hydrogenase, catalytic domain {Clostridium pasteurianum}
hmdrvknalnapekhvivamapsvrasigelfnmgfgvdvtgkiytalrqlgfdkifdin
fgadmtimeeatelvqrienngpfpmftsccpgwvrqaenyypellnnlssakspqqifg
tasktyypsisgldpknvftvtvmpctskkfeadrpqmekdglrdidavittrelakmik
dakipfakledseadpamgeysgagaifgatggvmeaalrsakdfaenaeledieykqvr
glngikeaeveinnnkynvavingasnlfkfmksgminekqyhfievmachggcvngggq
phvnpkdlekvdikkvrasvlynqdehlskrkshentalvkmyqnyfgkpgegraheilh
fkykk
>d1feha2 4.13.6.2.1 (1-126) Fe-only hydrogenase, N-terminal domain {Clostridium pasteurianum}
mktiiingvqfntdedttilkfardnnidisalcflnncnndinkceictvevegtglvt
acdtliedgmiintnsdavnekiksrisqlldihefkcgpcnrrenceflklvikykara
skpflp
>d1feha3 4.47.1.5.1 (127-209) Fe-only hydrogenase, second domain {Clostridium pasteurianum}
kdkteyvdersksltvdrtkcllcgrcvnacgkntetyamkflnkngktiigaedekcfd
dtncllcgqciiacpvaalseks
>d1fel__ 2.53.1.1.1 Retinol binding protein {Bovine (Bos taurus)}
erdcrvssfrvkenfdkarfagtwyamakkdpeglflqdnivaefsvdenghmsatakgr
vrllnnwdvcadmvgtftdtedpakfkmkywgvasflqkgnddhwiidtdyetfavqysc
rllnldgtcadsysfvfardpsgfspevqkivrqrqeelclarqyrliphngycd
>d1fem__ 2.53.1.1.1 Retinol binding protein {Bovine (Bos taurus)}
erdcrvssfrvkenfdkarfagtwyamakkdpeglflqdnivaefsvdenghmsatakgr
vrllnnwdvcadmvgtftdtedpakfkmkywgvasflqkgnddhwiidtdyetfavqysc
rllnldgtcadsysfvfardpsgfspevqkivrqrqeelclarqyrliphngycdgk
>d1fen__ 2.53.1.1.1 Retinol binding protein {Bovine (Bos taurus)}
erdcrvssfrvkenfdkarfagtwyamakkdpeglflqdnivaefsvdenghmsatakgr
vrllnnwdvcadmvgtftdtedpakfkmkywgvasflqkgnddhwiidtdyetfavqysc
rllnldgtcadsysfvfardpsgfspevqkivrqrqeelclarqyrliphngycdgk
>d1fep__ 6.4.3.3.2 Ferric enterobactin receptor FepA {Escherichia coli}
ddtivvtaaeqnlqapgvstitadeirknpvardvskiirtmpgvnltgnstsgqrgnnr
qidirgmgpentlilidgkpvssrnsvrqgwrgerdtrgdtswvppemierievlrgpaa
arygngaaggvvniitkkgsgewhgswdayfnapehkeegatkrtnfsltgplgdefsfr
lygnldktqadawdinqghqsaragtyattlpagregvinkdingvvrwdfaplqslele
agysrqgnlyagdtqntnsdsytrskygdetnrlyrqnyaltwnggwdngvttsnwvqye
htrnsripeglaggtegkfnekatqdfvdidlddvmlhsevnlpidflvnqtltlgtewn
qqrmkdlssntqaltgtntggaidgvsttdrspyskaeifslfaennmeltdstivtpgl
rfdhhsivgnnwspalnisqglgddftlkmgiaraykapslyqtnpnyilyskgqgcyas
aggcylqgnddlkaetsinkeiglefkrdgwlagvtwfrndyrnkieagyvavgqnavgt
dlyqwdnvpkavveglegslnvpvsetvmwtnnitymlksenkttgdrlsiipeytlnst
lswqaredlsmqttftwygkqqpkkynykgqpavgpetkeispysivglsatwdvtknvs
ltggvdnlfdkrlwragnaqttgdlaganyiagagaytynepgrtwymsvnthf
>d1fer__ 4.47.1.2.1 Ferredoxin {Azotobacter vinelandii}
afvvtdncikckytdcvevcpvdcfyegpnflvihpdecidcalcepecpaqaifsedev
pedmqefiqlnaelaevwpnitekkdplpdaedwdgvkgklqhler
>d1ff7a_ 7.3.11.1.8 Factor VII, N-terminal domain {Human (Homo sapiens)}
sdgdqcasspcqnggsckdqlqsyicfclpafegrncethkddgsa
>d1ffa__ 3.16.7.1.1 Cutinase {Fungus (Fusarium solani), subsp. Pisi}
rttrddlingnsascrdvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdaalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1ffb__ 3.16.7.1.1 Cutinase {Fungus (Fusarium solani), subsp. Pisi}
rttrddlingnsascrdvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgddalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1ffc__ 3.16.7.1.1 Cutinase {Fungus (Fusarium solani), subsp. Pisi}
rttrddlingnsascrdvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdlalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1ffd__ 3.16.7.1.1 Cutinase {Fungus (Fusarium solani), subsp. Pisi}
rttrddlingnsascrdvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdwalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1ffe__ 3.16.7.1.1 Cutinase {Fungus (Fusarium solani), subsp. Pisi}
rttrddlingnsascrdvifiyargatetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1ffh_1 1.30.1.1.1 (2-88) Signal sequence recognition protein Ffh {Thermus aquaticus}
fqqlsarlqeaigrlrgrgriteedlkatlreirralmdadvnlevtrdfvervreealg
kqvlesltpaevilatvyealkealgg
>d1ffh_2 3.30.1.8.5 (89-295) GTPase domain of the signal sequence recognition protein Ffh {Thermus aquaticus}
earlpvlkdrnlwflvglqgsgktttaaklalyykgkgrrpllvaadtqrpaareqlrll
gekvgvpvlevmdgespesirrrveekarleardlilvdtagrlqideplmgelarlkev
lgpdevllvldamtgqealsvarafdekvgvtglvltkldgdarggaalsarhvtgkpiy
fagvsekpeglepfyperlagrilgmg
>d1ffma_ 7.3.11.1.8 Factor VII, N-terminal domain {Human (Homo sapiens)}
sdgdqcasspcqnggsckdqlqsyicfclpafegrncethkddgsa
>d1fga__ 2.37.1.1.1 Basic FGF {Human (Homo sapiens)}
pkrlycknggfflrihpdgrvdgvreksdphiklqlqaeergvvsikgvcanrylamked
grllaskcvtdecffferlesnnyntyrsrkytswyvalkrtgqyklgsktgpgqkailf
lpms
>d1fgbd_ 2.35.2.1.3 Cholera toxin {Vibrio cholerae}
tpqnitdlcaeyhntqihtlndkifsyteslagkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1fgbe_ 2.35.2.1.3 Cholera toxin {Vibrio cholerae}
tpqnitdlcaeyhntqihtlndkifsyteslagkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1fgbf_ 2.35.2.1.3 Cholera toxin {Vibrio cholerae}
tpqnitdlcaeyhntqihtlndkifsyteslagkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1fgbg_ 2.35.2.1.3 Cholera toxin {Vibrio cholerae}
tpqnitdlcaeyhntqihtlndkifsyteslagkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1fgbh_ 2.35.2.1.3 Cholera toxin {Vibrio cholerae}
tpqnitdlcaeyhntqihtlndkifsyteslagkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1fgh_1 3.7.2.1.2 (529-754) Aconitase, C-terminal domain {Bovine (Bos taurus)}
vdvsptsqrlqllepfdkwdgkdledlqilikvkgkcttdhisaagpwlkfrghldnisn
nlligainsenrkansvrnavtqefgpvpdtaryykqhgirwvvigdenygegssrehsa
leprflggraiitksfarihetnlkkqgllpltfadpadynkihpvdkltiqglkdfapg
kpltciikhpngtqetillnhtfnetqiewfragsalnrmkelqqk
>d1fgh_2 3.72.1.1.2 (2-528) Aconitase, first 3 domains {Bovine (Bos taurus)}
rakvamshfepheyirydlleknidivrkrlnrpltlsekivyghlddpanqeiergkty
lrlrpdrvamqdataqmamlqfissglpkvavpstihcdhlieaqlggekdlrrakdinq
evynflatagakygvgfwrpgsgiihqiilenyaypgvlligtdshtpnggglggicigv
ggadavdvmagipwelkcpkvigvkltgslsgwtspkdvilkvagiltvkggtgaiveyh
gpgvdsisctgmaticnmgaeigattsvfpynhrmkkylsktgradianladefkdhlvp
dsgchydqlieinlselkphingpftpdlahpvaevgsvaekegwpldirvgligsctns
syedmgrsaavakqalahglkcksqftitpgseqiratierdgyaqvlrdvggivlanac
gpcigqwdrkdikkgekntivtsynrnftgrndanpethafvtspeivtalaiagtlkfn
petdfltgkdgkkfkleapdadelpraefdpgqdtyqhppkdssgqr
>d1fgia_ 4.117.1.2.5 Fibroblast growth factor receptor 1 {Human (Homo sapiens)}
elpedprwelprdrlvlgkplgegafgqvvlaeaigldkdkpnrvtkvavkmlksdatek
dlsdlisememmkmigkhkniinllgactqdgplyviveyaskgnlreylqarrppgley
synpshnpeeqlsskdlvscayqvargmeylaskkcihrdlaarnvlvtednvmkiadfg
lardihhidyykkttngrlpvkwmapealfdriythqsdvwsfgvllweiftlggspypg
vpveelfkllkeghrmdkpsnctnelymmmrdcwhavpsqrptfkqlvedldrivalts
>d1fgib_ 4.117.1.2.5 Fibroblast growth factor receptor 1 {Human (Homo sapiens)}
seyelpedprwelprdrlvlgkplgegafgqvvlaeaigldkdkpnrvtkvavkmlksda
tekdlsdlisememmkmigkhkniinllgactqdgplyviveyaskgnlreylqarrppg
leysynpshnpeeqlsskdlvscayqvargmeylaskkcihrdlaarnvlvtednvmkia
dfglardihhidyykkttngrlpvkwmapealfdriythqsdvwsfgvllweiftlggsp
ypgvpveelfkllkeghrmdkpsnctnelymmmrdcwhavpsqrptfkqlvedldrival
t
>d1fgja_ 1.126.1.4.1 Hydroxylamine oxidoreductase, HAO {Nitrosomonas europaea}
distvpdetydalkldrgkatpketyealvkrykdpahgagkgtmgdywepiaisiymdp
ntfykppvspkevaerkdcvechsdetpvwvrawkrsthanldkirnlksddplyykkgk
leevennlrsmgklgeketlkevgcidchvdvnkkdkadhtkdirmptadtcgtchlref
aereserdtmvwpngqwpagrpshaldytaniettvwatmpqrevaegctmchtnqnkcd
nchtrhefsaaesrkpeacatchsgvdhnnweaytmskhgklaemnrdkwnwevrlkdaf
skggqnaptcaachmeyegeythnitrktrwanypfvpgiaenitsdwsearldswvltc
tqchserfarsyldlmdkgtleglakyqeanaivhkmyedgtltgqktnrpnppepekpg
fgiftqlfwskgnnpaslelkvlemgennlakmhvglahvnpggwtytegwgpmnrayve
iqdeytkmqelsalqarvn
>d1fgjb_ 1.126.1.4.1 Hydroxylamine oxidoreductase, HAO {Nitrosomonas europaea}
distvpdetydalkldrgkatpketyealvkrykdpahgagkgtmgdywepiaisiymdp
ntfykppvspkevaerkdcvechsdetpvwvrawkrsthanldkirnlksddplyykkgk
leevennlrsmgklgeketlkevgcidchvdvnkkdkadhtkdirmptadtcgtchlref
aereserdtmvwpngqwpagrpshaldytaniettvwatmpqrevaegctmchtnqnkcd
nchtrhefsaaesrkpeacatchsgvdhnnweaytmskhgklaemnrdkwnwevrlkdaf
skggqnaptcaachmeyegeythnitrktrwanypfvpgiaenitsdwsearldswvltc
tqchserfarsyldlmdkgtleglakyqeanaivhkmyedgtltgqktnrpnppepekpg
fgiftqlfwskgnnpaslelkvlemgennlakmhvglahvnpggwtytegwgpmnrayve
iqdeytkmqelsalqarvn
>d1fgka_ 4.117.1.2.5 Fibroblast growth factor receptor 1 {Human (Homo sapiens)}
elpedprwelprdrlvlgkplgegafgqvvlaeaigldkdkpnrvtkvavkmlksdatek
dlsdlisememmkmigkhkniinllgactqdgplyviveyaskgnlreylqarrppgley
synpshnpeeqlsskdlvscayqvargmeylaskkcihrdlaarnvlvtednvmkiadfg
lardihhidyykkttngrlpvkwmapealfdriythqsdvwsfgvllweiftlggspypg
vpveelfkllkeghrmdkpsnctnelymmmrdcwhavpsqrptfkqlvedldrivalts
>d1fgkb_ 4.117.1.2.5 Fibroblast growth factor receptor 1 {Human (Homo sapiens)}
seyelpedprwelprdrlvlgkplgegafgqvvlaeaigldkdkpnrvtkvavkmlksda
tekdlsdlisememmkmigkhkniinllgactqdgplyviveyaskgnlreylqarrppg
leysynpshnpeeqlsskdlvscayqvargmeylaskkcihrdlaarnvlvtednvmkia
dfglardihhidyykkttngrlpvkwmapealfdriythqsdvwsfgvllweiftlggsp
ypgvpveelfkllkeghrmdkpsnctnelymmmrdcwhavpsqrptfkqlvedldrival
t
>d1fgla_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
mvnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgf
mcqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictakte
wldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1fgnh1 2.1.1.1.99 (1-117) Immunoglobulin (variable domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
eiqlqqsgaelvrpgalvklsckasgfnikdyymhwvkqrpeqglewiglidpengntiy
dpkfqgkasitadtssntaylqlssltsedtavyycardnsyyfdywgqgttltvss
>d1fgnh2 2.1.1.2.100 (118-214) Immunoglobulin (constant domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpsstwpsetvtcnvahpasstkvdkki
>d1fgnl1 2.1.1.1.99 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
dikmtqspssmyaslgervtitckasqdirkylnwyqqkpwkspktliyyatsladgvps
rfsgsgsgqdysltisslesddtatyyclqhgespytfgggtkleinr
>d1fgnl2 2.1.1.2.100 (109-214) Immunoglobulin (constant domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1fgp__ 2.33.1.1.1 N-terminal domains of the minor coat protein g3p {Bacteriophage fd}
etvesclakphtensftnvwkddktldryanyegclwnatgvvvctgdetqcygtwvpig
laipenaaah
>d1fgs_1 3.49.1.2.1 (297-425) Folylpolyglutamate synthetase, C-terminal domain {Lactobacillus casei}
wparlekisdtplividgahnpdginglitalkqlfsqpitviagiladkdyaamadrlt
aafstvylvpvpgtpralpeagyealhegrlkdswqealaaslndvpdqpivitgslyla
savrqtllg
>d1fgs_2 3.62.2.2.1 (1-296) Folylpolyglutamate synthetase {Lactobacillus casei}
mnytetvayihsfprlaktgdhrriltllhalgnpqqqgryihvtgtngkgsaanaiahv
leasgltvglytspfimrfnerimidhepipdaalvnavafvraalerlqqqqadfnvte
fefitalaywyfrqrqvdvavievgiggdtdstnvitpvvsvltevaldhqkllghtita
iakhkagiikrgipvvtgnlvpdaaavvaakvattgsqwlrfdrdfsvpkaklhgwgqrf
tyedqdgrisdlevplvgdyqqrnmaiaiqtakvyakqtewpltpqnirqglaash
>d1fgvh_ 2.1.1.1.27 Immunoglobulin (variable domains of L and H chains) {Fab H52 (synthetic, humanised version), kappa L chain}
evqlvesggglvqpggslrlscatsgytfteytmhwmrqapgkglewvaginpknggtsy
adsvkgrftisvdkskntlylqmnslraedtavyycarwrglnygfdvryfdvwgqgtlv
tvss
>d1fgvl_ 2.1.1.1.27 Immunoglobulin (variable domains of L and H chains) {Fab H52 (synthetic, humanised version), kappa L chain}
diqmtqspsslsasvgdrvtitcrasqdinnylnwyqqkpgkapklliyytstlesgvps
rfsgsgsgtdytltisslqpedfatyycqqgntlpptfgagtkveik
>d1fha__ 1.26.1.1.4 (Apo)ferritin {Human (Homo sapiens), H chain}
tsqvrqnyhqdseaainrqinlelyasyvylsmsyyfdrddvalknfakyflhqsheere
haeklmklqnqrggriflqdiqkpdcddwesglnamecalhleknvnqsllelhklatdk
ndphlcdfiethylneqvkaikelgdhvtnlrkmgapesglaeylfdkhtlg
>d1fhb__ 1.3.1.1.7 Mitochondrial cytochrome c {Baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrqsgqaegysytdanikk
nvlwdennmseyltnpkkyipgtkaafgglkkekdrndlitylkkase
>d1fhe_1 1.48.1.1.15 (81-214) Glutathione S-transferase {Fasciola hepatica}
lgttpeerarismiegaamdlrigfgrvcynpkfeevkeeyvkelpktlkmwsdflgdrh
yltgssvshvdfmlyetldsirylaphcldefpklkefksriealpkikaymeskrfikw
plngwaasfgagda
>d1fhe_2 3.38.1.5.15 (1-80) Glutathione S-transferase {Fasciola hepatica}
paklgywklrglaqpvrlfleylgeeyeehlygrddrekwmsekfnmgldlpnlpyyidd
kckltqsvaimryiadkhgm
>d1fhi__ 4.11.1.1.2 FHIT (fragile histidine triad protein) {Human (Homo sapiens)}
sfrfgqhlikpsvvflktelsfalvnrkpvvpghvlvcplrpverfhdlrpdevadlfqt
tqrvgtvvekhfhgtsltfsmqdgpeagqtvkhvhvhvlprkagdfhrndsiyeelqkhd
kedfpaswrseeemaaeaaalrvyfq
>d1fhs__ 4.72.1.1.7 Growth factor receptor-bound protein 2 (GRB2) {Human (Homo sapiens)}
giemkphpwffgkiprakaeemlskqrhdgafliresesapgdfslsvkfgndvqhfkvl
rdgagkyflwvvkfnslnelvdyhrstsvsrnqqiflrdieqvpqqptyvqa
>d1fht__ 4.47.7.1.2 Splicesomal U1A protein {Human (Homo sapiens)}
avpetrpnhtiyinnlnekikkdelkkslyaifsqfgqildilvsrslkmrgqafvifke
vssatnalrsmqgfpfydkpmriqyaktdsdiiakmkgtfverdrkrekrkpksqe
>d1fiaa_ 1.101.1.1.1 FIS protein {Escherichia coli}
qkplrdsvkqalknyfaqlngqdvndlyelvlaeveqplldmvmqytrgnqtraalmmgi
nrgtlrkklkkygmn
>d1fiab_ 1.101.1.1.1 FIS protein {Escherichia coli}
kplrdsvkqalknyfaqlngqdvndlyelvlaeveqplldmvmqytrgnqtraalmmgin
rgtlrkklkkygmn
>d1fib__ 4.141.1.1.1 Fibrinogen C-terminal domains {Human (Homo sapiens), beta and gamma}
qihditgkdcqdiankgakqsglyfikplkanqqflvyceidgsgngwtvfqkrldgsvd
fkknwiqykegfghlsptgttefwlgnekihlistqsaipyalrveledwngrtstadya
mfkvgpeadkyrltyayfaggdagdafdgfdfgddpsdkfftshngmqfstwdndndkfe
gncaeqdgsgwwmnkchaghlngvyyqggtyskastpngydngiiwatwktrwysmkktt
mkiipfnrl
>d1fica_ 4.141.1.1.1 Fibrinogen C-terminal domains {Human (Homo sapiens), beta and gamma}
qihditgkdcqdiankgakqsglyfikplkanqqflvyceidgsgngwtvfqkrldgsvd
fkknwiqykegfghlsptgttefwlgnekihlistqsaipyalrveledwngrtstadya
mfkvgpeadkyrltyayfaggdagdafdgfdfgddpsdkfftshngmqfstwdndndkfe
gncaeqdgsgwwmnkchaghlngvyyqggtyskastpngydngiiwatwktrwysmkktt
mkiipfnrltigegqqhhlg
>d1ficb_ 4.141.1.1.1 Fibrinogen C-terminal domains {Human (Homo sapiens), beta and gamma}
vqihditgkdcqdiankgakqsglyfikplkanqqflvyceidgsgngwtvfqkrldgsv
dfkknwiqykegfghlsptgttefwlgnekihlistqsaipyalrveledwngrtstady
amfkvgpeadkyrltyayfaggdagdafdgfdfgddpsdkfftshngmqfstwdndndkf
egncaeqdgsgwwmnkchaghlngvyyqggtyskastpngydngiiwatwktrwysmkkt
tmkiipfnrltigegqqhhlg
>d1fid__ 4.141.1.1.1 Fibrinogen C-terminal domains {Human (Homo sapiens), beta and gamma}
qihditgkdcqdiankgakqsglyfikplkanqqflvyceidgsgngwtvfqkrldgsvd
fkknwiqykegfghlsptgttefwlgnekihlistqsaipyalrveledwngrtstadya
mfkvgpeadkyrltyayfaggdagdafdgfdfgddpsdkfftshngmqfstwdndndkfe
gncaeqdgsgwwmnkchaghlngvyyqggtyskastpngydngiiwatwktrwysmkktt
mkiipfnrltigegqqhhl
>d1fiea1 2.1.1.5.14 (9-190) Transglutaminase factor XIII, N-terminal domain {Human (Homo sapiens), blood}
ggrravppnnsnaaeddlptvelqgvvprgvnlqeflnvtsvhlfkerwdtnkvdhhtdk
yennklivrrgqsfyvqidfsrpydprrdlfrveyvigrypqenkgtyipvpivselqsg
kwgakivmredrsvrlsiqsspkcivgkfrmyvavwtpygvlrtsrnpetdtyilfnpwc
ed
>d1fiea2 2.1.5.1.1 (516-627) Coagulation factor XIII, two C-terminal domains {Human (Homo sapiens), blood}
snvdmdfevenavlgkdfklsitfrnnshnrytitaylsanitfytgvpkaefkketfdv
tleplsfkkeavliqageymgqlleqaslhffvtarinetrdvlakqkstvl
>d1fiea3 2.1.5.1.1 (628-727) Coagulation factor XIII, two C-terminal domains {Human (Homo sapiens), blood}
tipeiiikvrgtqvvgsdmtvtiqftnplketlrnvwvhldgpgvtrpmkkmfreirpns
tvqweevcrpwvsghrkliasmssdslrhvygeldvqiqr
>d1fiea4 4.3.1.2.1 (191-515) Coagulation factor XIII, catalytic domain {Human (Homo sapiens), blood}
davyldnekereeyvlndigvifygevndiktrswsygqfedgildtclyvmdraqmdls
grgnpikvsrvgsamvnakddegvlvgswdniyaygvppsawtgsvdilleyrssenpvr
ygqcwvfagvfntflrclgiparivtnyfsahdndanlqmdifleedgnvnskltkdsvw
nyhcwneawmtrpdlpvgfggwqavdstpqensdgmyrcgpasvqaikhghvcfqfdapf
vfaevnsdliyitakkdgthvvenvdathigklivtkqiggdgmmditdtykfqegqeee
rlaletalmygakkplntegvmksr
>d1fieb1 2.1.1.5.14 (10-190) Transglutaminase factor XIII, N-terminal domain {Human (Homo sapiens), blood}
grravppnnsnaaeddlptvelqgvvprgvnlqeflnvtsvhlfkerwdtnkvdhhtdky
ennklivrrgqsfyvqidfsrpydprrdlfrveyvigrypqenkgtyipvpivselqsgk
wgakivmredrsvrlsiqsspkcivgkfrmyvavwtpygvlrtsrnpetdtyilfnpwce
d
>d1fieb2 2.1.5.1.1 (516-627) Coagulation factor XIII, two C-terminal domains {Human (Homo sapiens), blood}
snvdmdfevenavlgkdfklsitfrnnshnrytitaylsanitfytgvpkaefkketfdv
tleplsfkkeavliqageymgqlleqaslhffvtarinetrdvlakqkstvl
>d1fieb3 2.1.5.1.1 (628-727) Coagulation factor XIII, two C-terminal domains {Human (Homo sapiens), blood}
tipeiiikvrgtqvvgsdmtvtiqftnplketlrnvwvhldgpgvtrpmkkmfreirpns
tvqweevcrpwvsghrkliasmssdslrhvygeldvqiqr
>d1fieb4 4.3.1.2.1 (191-515) Coagulation factor XIII, catalytic domain {Human (Homo sapiens), blood}
davyldnekereeyvlndigvifygevndiktrswsygqfedgildtclyvmdraqmdls
grgnpikvsrvgsamvnakddegvlvgswdniyaygvppsawtgsvdilleyrssenpvr
ygqcwvfagvfntflrclgiparivtnyfsahdndanlqmdifleedgnvnskltkdsvw
nyhcwneawmtrpdlpvgfggwqavdstpqensdgmyrcgpasvqaikhghvcfqfdapf
vfaevnsdliyitakkdgthvvenvdathigklivtkqiggdgmmditdtykfqegqeee
rlaletalmygakkplntegvmksr
>d1figh1 2.1.1.1.40 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab 1F7 (mouse), kappa L chain}
dvqlqqsgpelekpgasvkisckasgfslpghninwivqrngkslewignidpyyggtnf
npkfkgkatltvdkssstlymhltslqsedsavyycarrrdgnygftywgqgtlvtvsa
>d1figh2 2.1.1.2.49 (114-223) Immunoglobulin (constant domains of L and H chains) {Fab 1F7 (mouse), kappa