>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
>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
>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
>d120l__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnsakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d121p__ 3.29.1.4.1 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
>d12ca__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlahwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>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
>d13pka_ 3.74.1.1.5 Phosphoglycerate kinase {(Trypanosoma brucei)}
ekksinecdlkgkkvlirvdfnvpvkngkitndyrirsalptlkkvlteggscvlmshlg
rpkgipmaqagkirstggvpgfqqkatlkpvakrlselllrpvtfapdclnaadvvskms
pgdvvllenvrfykeegskkakdreamakilasygdvyisdafgtahrdsatmtgipkil
gngaagylmekeisyfakvlgnpprplvaivggakvsdkiqlldnmlqridylliggama
ytflkaqgysigkskceesklefarsllkkaedrkvqvilpidhvchtefkavdsplite
dqnipeghmaldigpktiekyvqtigkcksaiwngpmgvfemvpyskgtfaiakamgrgt
hehglmsiigggdsasaaelsgeakrmshvstgggaslellegktlpgvtvlddk
>d13pkb_ 3.74.1.1.5 Phosphoglycerate kinase {(Trypanosoma brucei)}
ekksinecdlkgkkvlirvdfnvpvkngkitndyrirsalptlkkvlteggscvlmshlg
rpkgipmaqagkirstggvpgfqqkatlkpvakrlselllrpvtfapdclnaadvvskms
pgdvvllenvrfykeegskkakdreamakilasygdvyisdafgtahrdsatmtgipkil
gngaagylmekeisyfakvlgnpprplvaivggakvsdkiqlldnmlqridylliggama
ytflkaqgysigkskceesklefarsllkkaedrkvqvilpidhvchtefkavdsplite
dqnipeghmaldigpktiekyvqtigkcksaiwngpmgvfemvpyskgtfaiakamgrgt
hehglmsiigggdsasaaelsgeakrmshvstgggaslellegktlpgvtvlddk
>d13pkc_ 3.74.1.1.5 Phosphoglycerate kinase {(Trypanosoma brucei)}
ekksinecdlkgkkvlirvdfnvpvkngkitndyrirsalptlkkvlteggscvlmshlg
rpkgipmaqagkirstggvpgfqqkatlkpvakrlselllrpvtfapdclnaadvvskms
pgdvvllenvrfykeegskkakdreamakilasygdvyisdafgtahrdsatmtgipkil
gngaagylmekeisyfakvlgnpprplvaivggakvsdkiqlldnmlqridylliggama
ytflkaqgysigkskceesklefarsllkkaedrkvqvilpidhvchtefkavdsplite
dqnipeghmaldigpktiekyvqtigkcksaiwngpmgvfemvpyskgtfaiakamgrgt
hehglmsiigggdsasaaelsgeakrmshvstgggaslellegktlpgvtvlddk
>d13pkd_ 3.74.1.1.5 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
>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__ 1.3.1.1.16 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
>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
>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
>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
>d190l__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigracagaitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>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
>d1a00a_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a00b_ 1.1.1.1.25 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_ 1.1.1.1.25 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_ 1.1.1.1.25 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_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypatqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a02f_ 1.105.2.1.5 C-fos {Human (Homo sapiens)}
rrirrernkmaaaksrnrrreltdtlqaetdqledeksalqteianllkekek
>d1a02j_ 1.105.2.1.6 C-jun {Human (Homo sapiens)}
rkrmrnriaasksrkrkleriarleekvktlkaqnselastanmlreqvaql
>d1a02n1 2.1.1.5.17 (577-678) Transcription factor NFATC, C-terminal domain {Human (Homo sapiens)}
lpmverqdtdsclvyggqqmiltgqnftseskvvftekttdgqqiwemeatvdkdksqpn
mlfveipeyrnkhirtpvkvnfyvingkrkrsqpqhftyhpv
>d1a02n2 2.2.4.1.2 (399-576) Transcription factor NFATC, DNA-binding domain {human (Homo sapiens)}
wplssqsgsyelrievqpkphhrahyetegsrgavkaptgghpvvqlhgymenkplglqi
figtaderilkphafyqvhritgktvtttsyekivgntkvleiplepknnmratidcagi
lklrnadielrkgetdigrkntrvrlvfrvhipessgrivslqtasnpiecsqrsahe
>d1a04a1 1.33.1.2.1 (155-216) Nitrate/nitrite response regulator (NARL), receiver domain {(Escherichia coli)}
qltprerdilkliaqglpnkmiarrlditestvkvhvkhmlkkmklksrveaavwvhqer
if
>d1a04a2 3.14.2.1.4 (5-142) Nitrate/nitrite response regulator (NARL), receiver domain {(Escherichia coli)}
epatilliddhpmlrtgvkqlismapditvvgeasngeqgielaesldpdlilldlnmpg
mngletldklrekslsgrivvfsvsnheedvvtalkrgadgyllkdmepedllkalhqaa
agemvlsealtpvlaasl
>d1a04b1 1.33.1.2.1 (155-216) Nitrate/nitrite response regulator (NARL), receiver domain {(Escherichia coli)}
qltprerdilkliaqglpnkmiarrlditestvkvhvkhmlkkmklksrveaavwvhqer
if
>d1a04b2 3.14.2.1.4 (5-142) Nitrate/nitrite response regulator (NARL), receiver domain {(Escherichia coli)}
epatilliddhpmlrtgvkqlismapditvvgeasngeqgielaesldpdlilldlnmpg
mngletldklrekslsgrivvfsvsnheedvvtalkrgadgyllkdmepedllkalhqaa
agemvlsealtpvlaasl
>d1a05a_ 3.65.1.1.4 3-isopropylmalate dehydrogenase {(Thiobacillus ferrooxidans)}
mkkiaifagdgigpeivaaarqvldavdqaahlglrcteglvggaaldasddplpaaslq
lamaadavilgavggprwdayppakrpeqgllrlrkgldlyanlrpaqifpqlldasplr
pelvrdvdilvvreltgdiyfgqprglevidgkrrgfntmvydedeirriahvafraaqg
rrkqlcsvdkanvlettrlwrevvtevardypdvrlshmyvdnaamqlirapaqfdvllt
gnmfgdilsdeasqltgsigmlpsaslgegramyepihgsapdiagqdkanplatilsva
mmlrhslnaepwaqrveaavqrvldqglrtadiaapgtpvigtkamgaavvnalnlk
>d1a05b_ 3.65.1.1.4 3-isopropylmalate dehydrogenase {(Thiobacillus ferrooxidans)}
mkkiaifagdgigpeivaaarqvldavdqaahlglrcteglvggaaldasddplpaaslq
lamaadavilgavggprwdayppakrpeqgllrlrkgldlyanlrpaqifpqlldasplr
pelvrdvdilvvreltgdiyfgqprglevidgkrrgfntmvydedeirriahvafraaqg
rrkqlcsvdkanvlettrlwrevvtevardypdvrlshmyvdnaamqlirapaqfdvllt
gnmfgdilsdeasqltgsigmlpsaslgegramyepihgsapdiagqdkanplatilsva
mmlrhslnaepwaqrveaavqrvldqglrtadiaapgtpvigtkamgaavvnalnlk
>d1a06__ 5.1.1.1.5 Calmodulin-dependent protein kinase {Rat (Rattus norvegicus)}
wkqaedirdiydfrdvlgtgafsevilaedkrtqklvaikciakkalegkegsmeneiav
lhkikhpnivalddiyesgghlylimqlvsggelfdrivekgfyterdasrlifqvldav
kylhdlgivhrdlkpenllyysldedskimisdfglskmedpgsvlstacgtpgyvapev
laqkpyskavdcwsigviayillcgyppfydendaklfeqilkaeyefdspywddisdsa
kdfirhlmekdpekrftceqalqhpwiagdtaldknihqsvseqikknfakskwkqafna
tavvrhm
>d1a07a_ 4.53.1.1.3 c-src tyrosine kinase {human (Homo sapiens)}
siqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkh
ykirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a07b_ 4.53.1.1.3 c-src tyrosine kinase {human (Homo sapiens)}
iqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkhy
kirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a08a_ 4.53.1.1.3 c-src tyrosine kinase {human (Homo sapiens)}
siqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkh
ykirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a08b_ 4.53.1.1.3 c-src tyrosine kinase {human (Homo sapiens)}
iqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkhy
kirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a09a_ 4.53.1.1.3 c-src tyrosine kinase {human (Homo sapiens)}
dsiqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvk
hykirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a09b_ 4.53.1.1.3 c-src tyrosine kinase {human (Homo sapiens)}
aeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkhyki
rkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a0aa_ 1.36.1.1.5 Pho4 B/HLH domain {Baker's yeast (Saccharomyces cerevisiae)}
mkreshkhaeqarrnrlavalhelaslipaewkqqnvsaapskattveaacryirhlqqn
gst
>d1a0ab_ 1.36.1.1.5 Pho4 B/HLH domain {Baker's yeast (Saccharomyces cerevisiae)}
mkreshkhaeqarrnrlavalhelaslipaewkqqnvsaapskattveaacryirhlqqn
gst
>d1a0b__ 1.24.9.1.1 ArcB HTP {(Escherichia coli)}
ksealldipmleqylelvgpklitdglavfekmmpgyvsvlesnltaqdkkgiveeghki
kgaagsvglrhlqqlgqqiqspdlpawednvgewieemkeewrhdvevlkawvakat
>d1a0ca_ 3.1.12.1.7 D-xylose isomerase {(Clostridium thermosulfurogenes) Thermoanaerobacter thermosulfurigenes}
nkyfenvskikyegpksnnpysfkfynpeevidgktmeehlrfsiaywhtftadgtdqfg
katmqrpwnhytdpmdiakarveaafeffdkinapyfcfhdrdiapegdtlretnknldt
ivamikdylktsktkvlwgtanlfsnprfvhgastscnadvfaysaaqvkkaleitkelg
genyvfwggregyetllntdmefeldnfarflhmavdyakeigfegqfliepkpkeptkh
qydfdvanvlaflrkydldkyfkvnieanhatlafhdfqhelryaringvlgsidantgd
mllgwdtdqfptdirmttlamyevikmggfdkgglnfdakvrrasfepedlflghiagmd
afakgfkvayklvkdrvfdkfieeryasykdgigadivsgkadfrslekyalersqivnk
sgrqellesilnqylfa
>d1a0cb_ 3.1.12.1.7 D-xylose isomerase {(Clostridium thermosulfurogenes) Thermoanaerobacter thermosulfurigenes}
nkyfenvskikyegpksnnpysfkfynpeevidgktmeehlrfsiaywhtftadgtdqfg
katmqrpwnhytdpmdiakarveaafeffdkinapyfcfhdrdiapegdtlretnknldt
ivamikdylktsktkvlwgtanlfsnprfvhgastscnadvfaysaaqvkkaleitkelg
genyvfwggregyetllntdmefeldnfarflhmavdyakeigfegqfliepkpkeptkh
qydfdvanvlaflrkydldkyfkvnieanhatlafhdfqhelryaringvlgsidantgd
mllgwdtdqfptdirmttlamyevikmggfdkgglnfdakvrrasfepedlflghiagmd
afakgfkvayklvkdrvfdkfieeryasykdgigadivsgkadfrslekyalersqivnk
sgrqellesilnqylfa
>d1a0cc_ 3.1.12.1.7 D-xylose isomerase {(Clostridium thermosulfurogenes) Thermoanaerobacter thermosulfurigenes}
nkyfenvskikyegpksnnpysfkfynpeevidgktmeehlrfsiaywhtftadgtdqfg
katmqrpwnhytdpmdiakarveaafeffdkinapyfcfhdrdiapegdtlretnknldt
ivamikdylktsktkvlwgtanlfsnprfvhgastscnadvfaysaaqvkkaleitkelg
genyvfwggregyetllntdmefeldnfarflhmavdyakeigfegqfliepkpkeptkh
qydfdvanvlaflrkydldkyfkvnieanhatlafhdfqhelryaringvlgsidantgd
mllgwdtdqfptdirmttlamyevikmggfdkgglnfdakvrrasfepedlflghiagmd
afakgfkvayklvkdrvfdkfieeryasykdgigadivsgkadfrslekyalersqivnk
sgrqellesilnqylfa
>d1a0cd_ 3.1.12.1.7 D-xylose isomerase {(Clostridium thermosulfurogenes) Thermoanaerobacter thermosulfurigenes}
nkyfenvskikyegpksnnpysfkfynpeevidgktmeehlrfsiaywhtftadgtdqfg
katmqrpwnhytdpmdiakarveaafeffdkinapyfcfhdrdiapegdtlretnknldt
ivamikdylktsktkvlwgtanlfsnprfvhgastscnadvfaysaaqvkkaleitkelg
genyvfwggregyetllntdmefeldnfarflhmavdyakeigfegqfliepkpkeptkh
qydfdvanvlaflrkydldkyfkvnieanhatlafhdfqhelryaringvlgsidantgd
mllgwdtdqfptdirmttlamyevikmggfdkgglnfdakvrrasfepedlflghiagmd
afakgfkvayklvkdrvfdkfieeryasykdgigadivsgkadfrslekyalersqivnk
sgrqellesilnqylfa
>d1a0da_ 3.1.12.1.8 D-xylose isomerase {(Bacillus stearothermophilus)}
pyfdnistiayegpasknplafkfynpeekvgdktmeehlrfsvaywhtftgdgsdpfga
gnmirpwnkysgmdlakarveaafeffeklnipffcfhdvdiapegetlketyknldiiv
dmieeymktsktkllwntanlfthprfvhgaatscnadvfayaaakvkkgleiakrlgae
nyvfwggregyetllntdmkleldnlarflhmavdyakeigfdgqfliepkpkeptkhqy
dfdvatalaflqtyglkdyfkfnieanhatlaghtfehelrvarihgmlgsvdanqgdml
lgwdtdefptdlysttlamyeilkngglgrgglnfdakvrrgsfepedlfyahiagmdsf
avglkvahrliedrvfdefieeryksytegigreivegtadfhkleahalqlgeiqnqsg
rqerlktllnqyllevc
>d1a0db_ 3.1.12.1.8 D-xylose isomerase {(Bacillus stearothermophilus)}
pyfdnistiayegpasknplafkfynpeekvgdktmeehlrfsvaywhtftgdgsdpfga
gnmirpwnkysgmdlakarveaafeffeklnipffcfhdvdiapegetlketyknldiiv
dmieeymktsktkllwntanlfthprfvhgaatscnadvfayaaakvkkgleiakrlgae
nyvfwggregyetllntdmkleldnlarflhmavdyakeigfdgqfliepkpkeptkhqy
dfdvatalaflqtyglkdyfkfnieanhatlaghtfehelrvarihgmlgsvdanqgdml
lgwdtdefptdlysttlamyeilkngglgrgglnfdakvrrgsfepedlfyahiagmdsf
avglkvahrliedrvfdefieeryksytegigreivegtadfhkleahalqlgeiqnqsg
rqerlktllnqyllevc
>d1a0dc_ 3.1.12.1.8 D-xylose isomerase {(Bacillus stearothermophilus)}
pyfdnistiayegpasknplafkfynpeekvgdktmeehlrfsvaywhtftgdgsdpfga
gnmirpwnkysgmdlakarveaafeffeklnipffcfhdvdiapegetlketyknldiiv
dmieeymktsktkllwntanlfthprfvhgaatscnadvfayaaakvkkgleiakrlgae
nyvfwggregyetllntdmkleldnlarflhmavdyakeigfdgqfliepkpkeptkhqy
dfdvatalaflqtyglkdyfkfnieanhatlaghtfehelrvarihgmlgsvdanqgdml
lgwdtdefptdlysttlamyeilkngglgrgglnfdakvrrgsfepedlfyahiagmdsf
avglkvahrliedrvfdefieeryksytegigreivegtadfhkleahalqlgeiqnqsg
rqerlktllnqyllevc
>d1a0dd_ 3.1.12.1.8 D-xylose isomerase {(Bacillus stearothermophilus)}
pyfdnistiayegpasknplafkfynpeekvgdktmeehlrfsvaywhtftgdgsdpfga
gnmirpwnkysgmdlakarveaafeffeklnipffcfhdvdiapegetlketyknldiiv
dmieeymktsktkllwntanlfthprfvhgaatscnadvfayaaakvkkgleiakrlgae
nyvfwggregyetllntdmkleldnlarflhmavdyakeigfdgqfliepkpkeptkhqy
dfdvatalaflqtyglkdyfkfnieanhatlaghtfehelrvarihgmlgsvdanqgdml
lgwdtdefptdlysttlamyeilkngglgrgglnfdakvrrgsfepedlfyahiagmdsf
avglkvahrliedrvfdefieeryksytegigreivegtadfhkleahalqlgeiqnqsg
rqerlktllnqyllevc
>d1a0ea_ 3.1.12.1.9 D-xylose isomerase {(Thermotoga neapolitana)}
aeffpeipkvqfegkestnplafkfydpeeiidgkplkdhlkfsvafwhtfvnegrdpfg
dptadrpwnrytdpmdkafarvdalfefceklnieyfcfhdrdiapegktlretnkildk
vverikermkdsnvkllwgtanlfshprymhgaattcsadvfayaaaqvkkaleitkelg
gegyvfwggregyetllntdlgfelenlarflrmavdyakrigftgqfliepkpkeptkh
qydfdvatayaflkshgldeyfkfnieanhatlaghtfqhelrmarilgklgsidanqgd
lllgwdtdqfptnvydttlamyevikaggftkgglnfdakvrrasykvedlfighiagmd
tfalgfkvayklvkdgvldkfieekyrsfregigrdivegkvdfekleeyiidketielp
sgkqeyleslinsyivktilelr
>d1a0ed_ 3.1.12.1.9 D-xylose isomerase {(Thermotoga neapolitana)}
aeffpeipkvqfegkestnplafkfydpeeiidgkplkdhlkfsvafwhtfvnegrdpfg
dptadrpwnrytdpmdkafarvdalfefceklnieyfcfhdrdiapegktlretnkildk
vverikermkdsnvkllwgtanlfshprymhgaattcsadvfayaaaqvkkaleitkelg
gegyvfwggregyetllntdlgfelenlarflrmavdyakrigftgqfliepkpkeptkh
qydfdvatayaflkshgldeyfkfnieanhatlaghtfqhelrmarilgklgsidanqgd
lllgwdtdqfptnvydttlamyevikaggftkgglnfdakvrrasykvedlfighiagmd
tfalgfkvayklvkdgvldkfieekyrsfregigrdivegkvdfekleeyiidketielp
sgkqeyleslinsyivktilelr
>d1a0ga_ 5.14.1.1.1 D-amino acid aminotransferase {(Bacillus sp.) strain YM-1}
gytlwndqivkdeevkidkedrgyqfgdgvyevvkvyngemftvnehidrlyasaekiri
tipytkdkfhqllhelveknelntghiyfqvtrgtsprahqfpentvkpviigytkenpr
plenlekgvkatfvedirwlrcdikslnllgavlakqeahekgcyeailhrnntvtegss
snvfgikdgilythpannmiakgitrdvviacaneinmpvkeipftthealkmdelfvts
ttseitpvieidgklirdgkvgewtrklqkqfetkipkpl
>d1a0gb_ 5.14.1.1.1 D-amino acid aminotransferase {(Bacillus sp.) strain YM-1}
gytlwndqivkdeevkidkedrgyqfgdgvyevvkvyngemftvnehidrlyasaekiri
tipytkdkfhqllhelveknelntghiyfqvtrgtsprahqfpentvkpviigytkenpr
plenlekgvkatfvedirwlrcdikslnllgavlakqeahekgcyeailhrnntvtegss
snvfgikdgilythpannmiakgitrdvviacaneinmpvkeipftthealkmdelfvts
ttseitpvieidgklirdgkvgewtrklqkqfetkipkplhi
>d1a0ha1 7.13.1.1.5 (164-270) meizothrombin domain {Bovine (Bos taurus)}
splletcvpdrgreyrgrlavtthgsrclawsseqakalskdqdfnpavplaenfcrnpd
gdeegawcyvadqpgdfeycdlnyceepvdgdlgdrlgedpdpdaaieg
>d1a0hd1 7.13.1.1.5 (164-270) meizothrombin domain {Bovine (Bos taurus)}
splletcvpdrgreyrgrlavtthgsrclawsseqakalskdqdfnpavplaenfcrnpd
gdeegawcyvadqpgdfeycdlnyceepvdgdlgdrlgedpdpdaaieg
>d1a0i_1 2.29.4.6.2 (241-315) ATP-dependent DNA ligase {(Bacteriophage T7)}
peneadgiiqglvwgtkglanegkvigfevllesgrlvnatnisralmdeftetvkeatl
sqwgffspygigdnd
>d1a0i_2 4.89.2.1.1 (2-240) ATP-dependent DNA ligase, N-terminal domain {(Bacteriophage T7)}
vniktnpfkavsfvesaikkaldnagyliaeikydgvrgnicvdntansywlsrvsktip
alehlngfdvrwkrllnddrcfykdgfmldgelmvkgvdfntgsgllrtkwtdtknqefh
eelfvepirkkdkvpfklhtghlhiklyailplhivesgedcdvmtllmqehvknmlpll
qeyfpeiewqaaesyevydmvelqqlyeqkraegheglivkdpmciykrgkksgwwkmk
>d1a0k__ 4.63.1.1.6 Profilin (actin-binding protein) {Mouse-ear cress (Arabidopsis thaliana)}
swqsyvddhlmcdvegnhltaaailgqdgsvwaqsakfpqlkpqeidgikkdfeepgfla
ptglflggekymviqgeqgavirgkkgpggvtikktnqalvfgfydepmtggqcnlvver
lgdyliesel
>d1a0nb_ 2.24.2.1.2 Fyn proto-oncogene tyrosine kinase, SH3 domain {human (Homo sapiens)}
vtlfvalydyearteddlsfhkgekfqilnssegdwwearslttgetgyipsnyvapv
>d1a0p__ 4.101.1.1.3 Recombinase XerD {(Escherichia coli)}
qdlarieqfldalwleknlaentlnayrrdlsmmvewlhhrgltlataqsddlqallaer
leggykatssarllsavrrlfqylyrekfreddpsahlaspklpqrlpkdlseaqverll
qaplidqplelrdkamlevlyatglrvselvgltmsdislrqgvvrvigkgnkerlvplg
eeavywletylehgrpwllngvsidvlfpsqraqqmtrqtfwhrikhyavlagidsekls
phvlrhafathllnhgadlrvvqmllghsdlsttqiythvaterlrqlhq
>d1a0sp_ 6.7.1.2.3 Sucrose-specific porin {Enterobacterium (Salmonella typhimurium)}
sgfefhgyarsgvimndsgastksgayitpagetggaigrlgnqadtyvemnlehkqtld
ngattrfkvmvadgqtsyndwtastsdlnvrqafvelgnlptfagpfkgstlwagkrfdr
dnfdihwidsdvvflagtgggiydvkwndglrsnfslygrnfgdiddssnsvqnyiltmn
hfagplqmmvsglrakdnderkdsngnlakgdaantgvhallglhndsfyglrdgsskta
llyghglgaevkgigsdgalrpgadtwriasygttplsenwsvapamlaqrskdryadgd
syqwatfnlrliqainqnfalayegsyqymdlkpegyndrqavngsfykltfaptfkvgs
igdffsrpeirfytswmdwskklnnyasddalgsdgfnsggewsfgvqmetwf
>d1a0sq_ 6.7.1.2.3 Sucrose-specific porin {Enterobacterium (Salmonella typhimurium)}
sgfefhgyarsgvimndsgastksgayitpagetggaigrlgnqadtyvemnlehkqtld
ngattrfkvmvadgqtsyndwtastsdlnvrqafvelgnlptfagpfkgstlwagkrfdr
dnfdihwidsdvvflagtgggiydvkwndglrsnfslygrnfgdiddssnsvqnyiltmn
hfagplqmmvsglrakdnderkdsngnlakgdaantgvhallglhndsfyglrdgsskta
llyghglgaevkgigsdgalrpgadtwriasygttplsenwsvapamlaqrskdryadgd
syqwatfnlrliqainqnfalayegsyqymdlkpegyndrqavngsfykltfaptfkvgs
igdffsrpeirfytswmdwskklnnyasddalgsdgfnsggewsfgvqmetwf
>d1a0sr_ 6.7.1.2.3 Sucrose-specific porin {Enterobacterium (Salmonella typhimurium)}
sgfefhgyarsgvimndsgastksgayitpagetggaigrlgnqadtyvemnlehkqtld
ngattrfkvmvadgqtsyndwtastsdlnvrqafvelgnlptfagpfkgstlwagkrfdr
dnfdihwidsdvvflagtgggiydvkwndglrsnfslygrnfgdiddssnsvqnyiltmn
hfagplqmmvsglrakdnderkdsngnlakgdaantgvhallglhndsfyglrdgsskta
llyghglgaevkgigsdgalrpgadtwriasygttplsenwsvapamlaqrskdryadgd
syqwatfnlrliqainqnfalayegsyqymdlkpegyndrqavngsfykltfaptfkvgs
igdffsrpeirfytswmdwskklnnyasddalgsdgfnsggewsfgvqmetwf
>d1a0tp_ 6.7.1.2.3 Sucrose-specific porin {Enterobacterium (Salmonella typhimurium)}
sgfefhgyarsgvimndsgastksgayitpagetggaigrlgnqadtyvemnlehkqtld
ngattrfkvmvadgqtsyndwtastsdlnvrqafvelgnlptfagpfkgstlwagkrfdr
dnfdihwidsdvvflagtgggiydvkwndglrsnfslygrnfgdiddssnsvqnyiltmn
hfagplqmmvsglrakdnderkdsngnlakgdaantgvhallglhndsfyglrdgsskta
llyghglgaevkgigsdgalrpgadtwriasygttplsenwsvapamlaqrskdryadgd
syqwatfnlrliqainqnfalayegsyqymdlkpegyndrqavngsfykltfaptfkvgs
igdffsrpeirfytswmdwskklnnyasddalgsdgfnsggewsfgvqmetwf
>d1a0tq_ 6.7.1.2.3 Sucrose-specific porin {Enterobacterium (Salmonella typhimurium)}
sgfefhgyarsgvimndsgastksgayitpagetggaigrlgnqadtyvemnlehkqtld
ngattrfkvmvadgqtsyndwtastsdlnvrqafvelgnlptfagpfkgstlwagkrfdr
dnfdihwidsdvvflagtgggiydvkwndglrsnfslygrnfgdiddssnsvqnyiltmn
hfagplqmmvsglrakdnderkdsngnlakgdaantgvhallglhndsfyglrdgsskta
llyghglgaevkgigsdgalrpgadtwriasygttplsenwsvapamlaqrskdryadgd
syqwatfnlrliqainqnfalayegsyqymdlkpegyndrqavngsfykltfaptfkvgs
igdffsrpeirfytswmdwskklnnyasddalgsdgfnsggewsfgvqmetwf
>d1a0tr_ 6.7.1.2.3 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_ 1.1.1.1.25 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_ 1.1.1.1.25 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_ 1.1.1.1.25 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_ 1.1.1.1.25 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_ 1.1.1.1.25 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_ 1.1.1.1.25 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_ 1.1.1.1.25 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_ 1.1.1.1.25 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_ 1.1.1.1.25 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_ 1.1.1.1.25 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_ 1.1.1.1.25 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_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a14h_ 2.1.1.1.58 Immunoglobulin (variable domains of L and H chains) {Fab NC10 (mouse), kappa L chain}
qvqlqqsgaelvkpgasvrmsckasgytftnynmywvkqspgqglewigifypgngdtsy
nqkfkdkatltadkssntaymqlssltsedsavyycarsggsyrydggfdywgqgttvtv
>d1a14l_ 2.1.1.1.58 Immunoglobulin (variable domains of L and H chains) {Fab NC10 (mouse), kappa L chain}
dieltqttsslsaslgdrvtiscrasqdisnylnwyqqnpdgtvklliyytsnlhsevps
rfsgsgsgtdysltisnleqediatyfcqqdftlpftfgggtaa
>d1a14n_ 2.50.1.1.2 Influenza neuraminidase {(influenza virus A), different strains}
rdfnnltkglctinswhiygkdnavrigedsdvlvtrepyvscdpdecrfyalsqgttir
gkhsngtihdrsqyraliswplsspptvynsrvecigwsstschdgktrmsicisgpnnn
asaviwynrrpvteintwarnilrtqesecvchngvcpvvftdgsatgpaetriyyfkeg
kilkweplagtakhieecscygeraeitctcrdnwqgsnrpviridpvamthtsqyicsp
vltdnprpndptvgkcndpypgnnnngvkgfsyldgvntwlgrtisiasrsgyemlkvpn
altddkskptqgqtivlntdwsgysgsfmdywaegecyracfyvelirgrpkedkvwwts
nsivsmcssteflgqwdwpdgakieyfl
>d1a17__ 1.91.8.1.1 Protein phosphatase 5 {Human (Homo sapiens)}
ppadgalkraeelktqandyfkakdyenaikfysqaielnpsnaiyygnrslaylrtecy
gyalgdatraieldkkyikgyyrraasnmalgkfraalrdyetvvkvkphdkdakmkyqe
cnkivkqkaferaiagdehkrsvvdsldiesmtiedeys
>d1a18__ 2.45.1.2.3 Adipocyte lipid-binding protein, ALBP {mouse (Mus musculus)}
cdafvgtwklvssenfddymkevgvgfatrkvagmakpnmiisvngdlvtirsestfknt
eisfklgvefdeitaddrkvksiitldggalvqvqkwdgksttikrkrdgdklvvexvmk
gvtstrvyera
>d1a19a_ 3.6.1.1.1 Barstar (barnase inhibitor) {(Bacillus amyloliquefaciens)}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdcltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegaditiils
>d1a19b_ 3.6.1.1.1 Barstar (barnase inhibitor) {(Bacillus amyloliquefaciens)}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdcltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegaditiils
>d1a1aa_ 4.53.1.1.3 c-src tyrosine kinase {human (Homo sapiens)}
dsiqaeewyfgkitrreserlllnaenprgtflvresettkgayslsvsdfdnakglnvk
hykirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a1ab_ 4.53.1.1.3 c-src tyrosine kinase {human (Homo sapiens)}
aeewyfgkitrreserlllnaenprgtflvresettkgayslsvsdfdnakglnvkhyki
rkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a1ba_ 4.53.1.1.3 c-src tyrosine kinase {human (Homo sapiens)}
siqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkh
ykirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a1bb_ 4.53.1.1.3 c-src tyrosine kinase {human (Homo sapiens)}
iqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkhy
kirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a1ca_ 4.53.1.1.3 c-src tyrosine kinase {human (Homo sapiens)}
siqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkh
ykirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a1cb_ 4.53.1.1.3 c-src tyrosine kinase {human (Homo sapiens)}
iqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkhy
kirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a1ea_ 4.53.1.1.3 c-src tyrosine kinase {human (Homo sapiens)}
iqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkhy
kirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a1eb_ 4.53.1.1.3 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 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain {(human HLA-B53)}
adppkthvthhpvsdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrwep
>d1a1ma2 4.15.1.1.13 (1-181) MHC class I, alpha-1 and alpha-2 domains {(human HLA-B53)}
gshsmryfytamsrpgrgeprfiavgyvddtqfvrfdsdaasprteprppwieqegpeyw
drntqifktntqtyrenlrialryynqseagshiiqrmygcdlgpdgrllrghdqsaydg
kdyialnedlsswtaadtaaqitqrkweaarvaeqlrayleglcvewlrrylengketlq
r
>d1a1na1 2.1.1.2.10 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain {(human HLA-B*3501)}
adppkthvthhpvsdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrwep
>d1a1na2 4.15.1.1.14 (1-181) MHC class I, alpha-1 and alpha-2 domains {(human HLA-B*3501)}
gshsmryfytamsrpgrgeprfiavgyvddtqfvrfdsdaasprteprppwieqegpeyw
drntqifktntqtyreslrnlrgyynqseagshiiqrmygcdlgpdgrllrghdqsaydg
kdyialnedlsswtaadtaaqitqrkweaarvaeqlrayleglcvewlrrylengketlq
r
>d1a1oa1 2.1.1.2.9 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain {(human HLA-B53)}
adppkthvthhpvsdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrwep
>d1a1oa2 4.15.1.1.13 (1-181) MHC class I, alpha-1 and alpha-2 domains {(human HLA-B53)}
gshsmryfytamsrpgrgeprfiavgyvddtqfvrfdsdaasprteprppwieqegpeyw
drntqifktntqtyrenlrialryynqseagshiiqrmygcdlgpdgrllrghdqsaydg
kdyialnedlsswtaadtaaqitqrkweaarvaeqlrayleglcvewlrrylengketlq
r
>e1a1q.1a 2.35.1.3.3 NS3 protease {(Human hepatitis C virus) Bk strain}
pitaysqqtrgllgciitsltgrdknqvegevqvvstatqsflatcvngvcwtvyhgags
ktlagpkgpitqmytnvdqdlvgwqappgarsltpctcgssdlylvtrhadvipvrrrgd
srgsllsprpvsylkgssggpllcpsghavgifraavctrgvakavdfvpvesmettmrs
pvf
>e1a1q.1b 2.35.1.3.3 NS3 protease {(Human hepatitis C virus) Bk strain}
pitaysqqtrgllgciitsltgrdknqvegevqvvstatqsflatcvngvcwtvyhgags
ktlagpkgpitqmytnvdqdlvgwqappgarsltpctcgssdlylvtrhadvipvrrrgd
srgsllsprpvsylkgssggpllcpsghavgifraavctrgvakavdfvpvesmettm
>e1a1q.1c 2.35.1.3.3 NS3 protease {(Human hepatitis C virus) Bk strain}
pitaysqqtrgllgciitsltgrdknqvegevqvvstatqsflatcvngvcwtvyhgags
ktlagpkgpitqmytnvdqdlvgwqappgarsltpctcgssdlylvtrhadvipvrrrgd
srgsllsprpvsylkgssggpllcpsghavgifraavctrgvakavdfvpvesmettm
>e1a1r.1a 2.35.1.3.3 NS3 protease {(Human hepatitis C virus) Bk strain}
vegevqivstatqtflatcingvcwtvyhgagtrtiaspkgpviqmytnvdqdlvgwpap
qgsrsltpctcgssdlylvtrhadvipvrrrgdsrgsllsprpisylkgssggpllcptg
havglfraavctrgvakavdfipvenlettmr
>e1a1r.2b 2.35.1.3.3 NS3 protease {(Human hepatitis C virus) Bk strain}
pitayaqqtrgllgciitsltgrdknqvegevqivstatqtflatcingvcwtvyhgagt
rtiaspkgpviqmytnvdqdlvgwpapqgsrsltpctcgssdlylvtrhadvipvrrrgd
srgsllsprpisylkgssggpllcptghavglfraavctrgvakavdfipvenlettmr
>e1a1r.2d 2.35.1.3.3 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-1 nucleocapsid {human immunodeficiency virus type 1 (Mn isolate)}
mqkgnfrnqrktvkcfncgkeghiakncraprkkgcwkcgkeghqmkdcterqan
>d1a1ua_ 1.49.1.1.1 p53 tetramerization domain {human (Homo sapiens)}
eyftlqirgrerfekireynealelkdaq
>d1a1uc_ 1.49.1.1.1 p53 tetramerization domain {human (Homo sapiens)}
eyftlqirgrerfekireynealelkdaq
>d1a1x__ 2.48.1.1.2 MTCP-1 {Human (Homo sapiens)}
agedvgappdhlwvhqegiyrdeyqrtwvavveeetsflrarvqqiqvplgdaarpshll
tsqlplmwqlypeerymdnnsrlwqiqhhlmvrgvqelllkllpdd
>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_ 1.26.1.1.6 Growth hormone, somatotropin {human (Homo sapiens)}
fptiplsrlfdnamlrahrlhqlafdtyqefeeayipkeqkysflqnpqtslcfsesipt
psnreetqqksnlellrisllliqswlepvqflrsvfanslvygasdsnvydllkdleer
iqtlmgrlegqifkqtyskfdtdallknygllycfrkdmdkvetflrivqcrsvegscgf
>d1a22b1 2.1.2.1.7 (233-328) Growth hormone receptor {human (Homo sapiens)}
pkftkcrsperetfschwtdevhhgtknlgpiqlfytrrntqewtqewkecpdyvsagen
scyfnssftsiwipycikltsnggtvdekcfsvdei
>d1a22b2 2.1.2.1.7 (329-437) Growth hormone receptor {human (Homo sapiens)}
vqpdppialnwtllnvsltgihadiqvrweaprnadiqkgwmvleyelqykevnetkwkm
mdpilttsvpvyslkvdkeyevrvrskqrnsgnygefsevlyvtlpqms
>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 1.39.1.1.1 (662-796) A domain of poly(ADP-ribose) polymerase {Chicken (Gallus gallus)}
ksklakpiqdlikmifdvesmkkamvefeidlqkmplgklskrqiqsaysilnevqqavs
dggsesqildlsnrfytliphdfgmkkppllsnleyiqakvqmldnlldievaysllrgg
nedgdkdpidinyek
>d1a26_2 4.103.1.2.1 (797-1012) Poly(ADP-ribose) polymerase, C-terminal domain {Chicken (Gallus gallus)}
lrtdikvvdkdseeakiikqyvknthaathnaydlkvveifrieregesqrykpfkqlhn
rqllwhgsrttnfagilsqglriappeapvtgymfgkgiyfadmvsksanychtsqadpi
glillgevalgnmyelknashitklpkgkhsvkglgktapdptatttldgvevplgngis
tgindtcllyneyivydvaqvnlkyllklkfnykts
>d1a27__ 3.22.1.2.3 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylahskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevfg
>d1a28a_ 1.95.1.1.3 Progesterone receptor {Human (Homo sapiens)}
qlipplinllmsiepdviyaghdntkpdtssslltslnqlgerqllsvvkwskslpgfrn
lhiddqitliqyswmslmvfglgwrsykhvsgqmlyfapdlilneqrmkessfyslcltm
wqipqefvklqvsqeeflcmkvllllntipleglrsqtqfeemrssyirelikaiglrqk
gvvsssqrfyqltklldnlhdlvkqlhlyclntfiqsralsvefpemmseviaaqlpkil
agmvkpllfhk
>d1a28b_ 1.95.1.1.3 Progesterone receptor {Human (Homo sapiens)}
lipplinllmsiepdviyaghdntkpdtssslltslnqlgerqllsvvkwskslpgfrnl
hiddqitliqyswmslmvfglgwrsykhvsgqmlyfapdlilneqrmkessfyslcltmw
qipqefvklqvsqeeflcmkvllllntipleglrsqtqfeemrssyirelikaiglrqkg
vvsssqrfyqltklldnlhdlvkqlhlyclntfiqsralsvefpemmseviaaqlpkila
gmvkpllfh
>d1a2b__ 3.29.1.4.7 RhoA {Human (Homo sapiens)}
irkklvivgdvacgktcllivfskdqfpevyvptvfenyvadievdgkqvelalwdtagq
edydrlrplsypdtdvilmcfsidspdslenipekwtpevkhfcpnvpiilvgnkkdlrn
dehtrrelakmkqepvkpeegrdmanrigafgymecsaktkdgvrevfematraalqa
>e1a2c.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>e1a2c.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>d1a2da_ 2.45.1.2.3 Adipocyte lipid-binding protein, ALBP {mouse (Mus musculus)}
cdafvgtwklvssenfddymkevgvgfatrkvagmakpnmiisvngdlvtirsestfknt
eisfklgvefdeitaddrkvksiitldggalvqvqkwdgksttikrkrdgdklvvexvmk
gvtstrvyera
>d1a2db_ 2.45.1.2.3 Adipocyte lipid-binding protein, ALBP {mouse (Mus musculus)}
cdafvgtwklvssenfddymkevgvgfatrkvagmakpnmiisvngdlvtirsestfknt
eisfklgvefdeitaddrkvksiitldggalvqvqkwdgksttikrkrdgdklvvexvmk
gvtstrvyera
>d1a2i__ 1.107.1.1.2 Cytochrome c3 {(Desulfovibrio vulgaris)}
apkapadglkmeatkqpvvfnhsthksvkcgdchhpvngkedyrkcgtagchdsmdkkdk
sakgyyhvmhdkntkfkscvgchvevagadaakkkdltgckkskche
>d1a2ka_ 4.13.3.2.1 Nuclear transport factor-2 (NTF2) {Rat (Rattus norvegicus)}
kpiweqigssfiqhyyqlfdndrtqlgaiyidascltwegqqfqgkaaiveklsslpfqk
iqhsitaqdhqptpdsciismvvgqlkadedpimgfhqmfllknindawvctndmfrlal
hnfg
>d1a2kb_ 4.13.3.2.1 Nuclear transport factor-2 (NTF2) {Rat (Rattus norvegicus)}
kpiweqigssfiqhyyqlfdndrtqlgaiyidascltwegqqfqgkaaiveklsslpfqk
iqhsitaqdhqptpdsciismvvgqlkadedpimgfhqmfllknindawvctndmfrlal
hnfg
>d1a2kc_ 3.29.1.4.5 Ran {Dog (Canis familiaris)}
qvqfklvlvgdggtgkttfvkrhltgefekkyvatlgvevhplvfhtnrgpikfnvwdta
gqekfgglrdgyyiqaqcaiimfdvtsrvtyknvpnwhrdlvrvcenipivlcgnkvdik
drkvkaksivfhrkknlqyydisaksnynfekpflwlarkligdpnlefvampalappev
vmdpalaaqyehdlev
>d1a2kd_ 3.29.1.4.5 Ran {Dog (Canis familiaris)}
qvqfklvlvgdggtgkttfvkrhltgefekkyvatlgvevhplvfhtnrgpikfnvwdta
gqekfgglrdgyyiqaqcaiimfdvtsrvtyknvpnwhrdlvrvcenipivlcgnkvdik
drkvkaksivfhrkknlqyydisaksnynfekpflwlarkligdpnlefvampalappev
vmdpalaaqyehdlevaqt
>d1a2ke_ 3.29.1.4.5 Ran {Dog (Canis familiaris)}
qvqfklvlvgdggtgkttfvkrhltgefekkyvatlgvevhplvfhtnrgpikfnvwdta
gqekfgglrdgyyiqaqcaiimfdvtsrvtyknvpnwhrdlvrvcenipivlcgnkvdik
drkvkaksivfhrkknlqyydisaksnynfekpflwlarkligdpnlefvampalappev
vmdpalaaqyehdlevaqttalpde
>d1a2la1 1.42.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {(Escherichia coli)}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1a2la2 3.38.1.3.1 (3-64,129-188) Disulphide-bond formation facilitator (DSBA) {(Escherichia coli)}
yedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyhvn
fmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvkyl
sek
>d1a2lb1 1.42.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {(Escherichia coli)}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1a2lb2 3.38.1.3.1 (3-64,129-188) Disulphide-bond formation facilitator (DSBA) {(Escherichia coli)}
yedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyhvn
fmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvkyl
sek
>d1a2ma1 1.42.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {(Escherichia coli)}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1a2ma2 3.38.1.3.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) {(Escherichia coli)}
aqyedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsek
>d1a2mb1 1.42.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {(Escherichia coli)}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1a2mb2 3.38.1.3.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) {(Escherichia coli)}
aqyedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsek
>d1a2n__ 4.36.2.1.1 UDP-N-acetylglucosamine enolpyruvyl transferase (EPT, MurA, MurZ) {(Escherichia coli)}
mdkfrvqgptklqgevtisgaknaalpilfaallaeepveiqnvpklkdvdtsmkllsql
gakverngsvhidardvnvfcapydlvktmrasiwalgplvarfgqgqvslpggatigar
pvdlhisgleqlgatikleegyvkasvdgrlkgahivmdkvsvgatvtimcaatlaegtt
iienaarepeivdtanflitlgakisgqgtdriviegverlgggvyrvlpdrietgtflv
aaaisrgkiicrnaqpdtldavlaklrdagadievgedwisldmhgkrpkavnvrtaphp
afptdmqaqftllnlvaegtgfitetvfenrfmhvpelsrmgahaeiesntvichgvekl
sgaqvmatdlrasaslvlagciaegttvvdriyhidrgyeriedklralganiervkg
>d1a2oa1 3.14.2.1.7 (1-140) Methylesterase CheB, N-terminal domain {(Salmonella typhimurium)}
mskirvlsvddsalmrqimteiinshsdmemvatapdplvardlikkfnpdvltldvemp
rmdgldfleklmrlrpmpvvmvssltgkgsevtlralelgaidfvtkpqlgiregmlays
emiaekvrtaarariaahkp
>d1a2oa2 3.31.1.1.1 (141-347) Methylesterase CheB, C-terminal domain {(Salmonella typhimurium)}
maapttlkagpllssekliaigastggteairhvlqplplsspaviitqhmppgftrsfa
erlnklcqisvkeaedgervlpghayiapgdkhmelarsganyqikihdgppvnrhrpsv
dvlfhsvakhagrnavgviltgmgndgaagmlamyqagawtiaqneascvvfgmpreain
mggvsevvdlsqvsqqmlakisagqai
>d1a2ob1 3.14.2.1.7 (1-140) Methylesterase CheB, N-terminal domain {(Salmonella typhimurium)}
mskirvlsvddsalmrqimteiinshsdmemvatapdplvardlikkfnpdvltldvemp
rmdgldfleklmrlrpmpvvmvssltgkgsevtlralelgaidfvtkpqlgiregmlays
emiaekvrtaarariaahkp
>d1a2ob2 3.31.1.1.1 (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__ 3.33.1.1.6 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__ 2.29.1.1.1 Staphylococcal nuclease {(Staphylococcal aureus)}
lhkepatlikaidgdtxklmykgqpmtfrlllvdtpetkhpkkgvekygpeasaftkkmv
enakkievefdkgqrtdkygrglayiyadgkmvnealvrqglakvayvykpnntheqhlr
kseaqakkeklniws
>d1a2u__ 2.29.1.1.1 Staphylococcal nuclease {(Staphylococcal aureus)}
lhkepatlikaidgdtxklmykgqpmtfrlllvdtpetkhpkkgvekygpeasaftkkmv
enakkievefdkgqrtdkygrglayiyadgkmvnealvrqglakvayvykpnntheqhlr
kseaqakkeklniws
>d1a2va1 2.22.2.1.4 (237-672) Copper amine oxidase, domain 3 (catalytic) {Yeast (Hansenula polymorpha)}
peappinvtqpegvsfkmtgnvmewsnfkfhigfnyregivlsdvsyndhgnvrpifhri
slsemivpygspefphqrkhaldigeygagymtnplslgcdckgvihyldahfsdragdp
itvknavciheeddgllfkhsdfrdnfatslvtratklvvsqiftaanxeyclywvfmqd
gairldirltgilntyilgddeeagpwgtrvypnvnahnhqhlfslridpridgdgnsaa
acdaksspyplgspenmygnafysekttfktvkdsltnyesatgrswdifnpnkvnpysg
kppsyklvstqcppllakegslvakrapwashsvnvvpykdnrlypsgdhvpqwsgdgvr
gmrewigdgsenidntdilffhtfgithfpapedfplmpaepitlmlrprhfftenpgld
iqpsyamttseakrav
>d1a2va2 4.13.2.1.4 (18-115) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
parpahpldplstaeikaatntvksyfagkkisfntvtlreparkayiqwkeqggplppr
layyvileagkpgvkeglvdlaslsvietraletvqpi
>d1a2va3 4.13.2.1.4 (116-236) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
ltvedlcsteevirndpavieqcvlsgipanemhkvycdpwtigyderwgtgkrlqqalv
yyrsdeddsqyshpldfcpivdteekkvifidipnrrrkvskhkhanfypkhmiekvgam
r
>d1a2vb1 2.22.2.1.4 (237-672) Copper amine oxidase, domain 3 (catalytic) {Yeast (Hansenula polymorpha)}
peappinvtqpegvsfkmtgnvmewsnfkfhigfnyregivlsdvsyndhgnvrpifhri
slsemivpygspefphqrkhaldigeygagymtnplslgcdckgvihyldahfsdragdp
itvknavciheeddgllfkhsdfrdnfatslvtratklvvsqiftaanxeyclywvfmqd
gairldirltgilntyilgddeeagpwgtrvypnvnahnhqhlfslridpridgdgnsaa
acdaksspyplgspenmygnafysekttfktvkdsltnyesatgrswdifnpnkvnpysg
kppsyklvstqcppllakegslvakrapwashsvnvvpykdnrlypsgdhvpqwsgdgvr
gmrewigdgsenidntdilffhtfgithfpapedfplmpaepitlmlrprhfftenpgld
iqpsyamttseakrav
>d1a2vb2 4.13.2.1.4 (18-115) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
parpahpldplstaeikaatntvksyfagkkisfntvtlreparkayiqwkeqggplppr
layyvileagkpgvkeglvdlaslsvietraletvqpi
>d1a2vb3 4.13.2.1.4 (116-236) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
ltvedlcsteevirndpavieqcvlsgipanemhkvycdpwtigyderwgtgkrlqqalv
yyrsdeddsqyshpldfcpivdteekkvifidipnrrrkvskhkhanfypkhmiekvgam
r
>d1a2vc1 2.22.2.1.4 (237-672) Copper amine oxidase, domain 3 (catalytic) {Yeast (Hansenula polymorpha)}
peappinvtqpegvsfkmtgnvmewsnfkfhigfnyregivlsdvsyndhgnvrpifhri
slsemivpygspefphqrkhaldigeygagymtnplslgcdckgvihyldahfsdragdp
itvknavciheeddgllfkhsdfrdnfatslvtratklvvsqiftaanxeyclywvfmqd
gairldirltgilntyilgddeeagpwgtrvypnvnahnhqhlfslridpridgdgnsaa
acdaksspyplgspenmygnafysekttfktvkdsltnyesatgrswdifnpnkvnpysg
kppsyklvstqcppllakegslvakrapwashsvnvvpykdnrlypsgdhvpqwsgdgvr
gmrewigdgsenidntdilffhtfgithfpapedfplmpaepitlmlrprhfftenpgld
iqpsyamttseakrav
>d1a2vc2 4.13.2.1.4 (18-115) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
parpahpldplstaeikaatntvksyfagkkisfntvtlreparkayiqwkeqggplppr
layyvileagkpgvkeglvdlaslsvietraletvqpi
>d1a2vc3 4.13.2.1.4 (116-236) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
ltvedlcsteevirndpavieqcvlsgipanemhkvycdpwtigyderwgtgkrlqqalv
yyrsdeddsqyshpldfcpivdteekkvifidipnrrrkvskhkhanfypkhmiekvgam
r
>d1a2vd1 2.22.2.1.4 (237-672) Copper amine oxidase, domain 3 (catalytic) {Yeast (Hansenula polymorpha)}
peappinvtqpegvsfkmtgnvmewsnfkfhigfnyregivlsdvsyndhgnvrpifhri
slsemivpygspefphqrkhaldigeygagymtnplslgcdckgvihyldahfsdragdp
itvknavciheeddgllfkhsdfrdnfatslvtratklvvsqiftaanxeyclywvfmqd
gairldirltgilntyilgddeeagpwgtrvypnvnahnhqhlfslridpridgdgnsaa
acdaksspyplgspenmygnafysekttfktvkdsltnyesatgrswdifnpnkvnpysg
kppsyklvstqcppllakegslvakrapwashsvnvvpykdnrlypsgdhvpqwsgdgvr
gmrewigdgsenidntdilffhtfgithfpapedfplmpaepitlmlrprhfftenpgld
iqpsyamttseakrav
>d1a2vd2 4.13.2.1.4 (18-115) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
parpahpldplstaeikaatntvksyfagkkisfntvtlreparkayiqwkeqggplppr
layyvileagkpgvkeglvdlaslsvietraletvqpi
>d1a2vd3 4.13.2.1.4 (116-236) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
ltvedlcsteevirndpavieqcvlsgipanemhkvycdpwtigyderwgtgkrlqqalv
yyrsdeddsqyshpldfcpivdteekkvifidipnrrrkvskhkhanfypkhmiekvgam
r
>d1a2ve1 2.22.2.1.4 (237-672) Copper amine oxidase, domain 3 (catalytic) {Yeast (Hansenula polymorpha)}
peappinvtqpegvsfkmtgnvmewsnfkfhigfnyregivlsdvsyndhgnvrpifhri
slsemivpygspefphqrkhaldigeygagymtnplslgcdckgvihyldahfsdragdp
itvknavciheeddgllfkhsdfrdnfatslvtratklvvsqiftaanxeyclywvfmqd
gairldirltgilntyilgddeeagpwgtrvypnvnahnhqhlfslridpridgdgnsaa
acdaksspyplgspenmygnafysekttfktvkdsltnyesatgrswdifnpnkvnpysg
kppsyklvstqcppllakegslvakrapwashsvnvvpykdnrlypsgdhvpqwsgdgvr
gmrewigdgsenidntdilffhtfgithfpapedfplmpaepitlmlrprhfftenpgld
iqpsyamttseakrav
>d1a2ve2 4.13.2.1.4 (18-115) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
parpahpldplstaeikaatntvksyfagkkisfntvtlreparkayiqwkeqggplppr
layyvileagkpgvkeglvdlaslsvietraletvqpi
>d1a2ve3 4.13.2.1.4 (116-236) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
ltvedlcsteevirndpavieqcvlsgipanemhkvycdpwtigyderwgtgkrlqqalv
yyrsdeddsqyshpldfcpivdteekkvifidipnrrrkvskhkhanfypkhmiekvgam
r
>d1a2vf1 2.22.2.1.4 (237-672) Copper amine oxidase, domain 3 (catalytic) {Yeast (Hansenula polymorpha)}
peappinvtqpegvsfkmtgnvmewsnfkfhigfnyregivlsdvsyndhgnvrpifhri
slsemivpygspefphqrkhaldigeygagymtnplslgcdckgvihyldahfsdragdp
itvknavciheeddgllfkhsdfrdnfatslvtratklvvsqiftaanxeyclywvfmqd
gairldirltgilntyilgddeeagpwgtrvypnvnahnhqhlfslridpridgdgnsaa
acdaksspyplgspenmygnafysekttfktvkdsltnyesatgrswdifnpnkvnpysg
kppsyklvstqcppllakegslvakrapwashsvnvvpykdnrlypsgdhvpqwsgdgvr
gmrewigdgsenidntdilffhtfgithfpapedfplmpaepitlmlrprhfftenpgld
iqpsyamttseakrav
>d1a2vf2 4.13.2.1.4 (18-115) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
parpahpldplstaeikaatntvksyfagkkisfntvtlreparkayiqwkeqggplppr
layyvileagkpgvkeglvdlaslsvietraletvqpi
>d1a2vf3 4.13.2.1.4 (116-236) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
ltvedlcsteevirndpavieqcvlsgipanemhkvycdpwtigyderwgtgkrlqqalv
yyrsdeddsqyshpldfcpivdteekkvifidipnrrrkvskhkhanfypkhmiekvgam
r
>d1a2wa_ 4.4.1.1.1 Ribonuclease A (also ribonuclease B, S) {bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1a2wb_ 4.4.1.1.1 Ribonuclease A (also ribonuclease B, S) {bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1a2xa_ 1.37.1.5.3 Troponin C {Rabbit (Oryctolagus cuniculus)}
dqqaearsylseemiaefkaafdmfdadgggdisvkelgtvmrmlgqtptkeeldaiiee
vdedgsgtidfeeflvmmvrqmkedakgkseeelaecfrifdrnadgyidaeelaeifra
sgehvtdeeieslmkdgdknndgridfdeflkmmegvq
>d1a2ya_ 2.1.1.1.39 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
divltqspaslsasvgetvtitcrasgnihnylawyqqkqgkspqllvyytttladgvps
rfsgsgsgtqyslkinslqpedfgsyycqhfwstprtfgggtkleik
>d1a2yb_ 2.1.1.1.39 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_ 3.58.3.1.1 Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase) {(Thermococcus litoralis)}
mkkvlitgfepfggdsknpteqiakyfdrkqignamvygrvlpvsvkratielkryleei
kpeivinlglaptysnitveriavniidaripdndgyqpidekieedaplaymatlpvra
itktlrdngipatisysagtylcnyvmfktlhfskiegyplkagfihvpytpdqvvnkff
llgkntpsmcleaeikaielavkvsldylekdrddikipl
>d1a2zb_ 3.58.3.1.1 Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase) {(Thermococcus litoralis)}
mkkvlitgfepfggdsknpteqiakyfdrkqignamvygrvlpvsvkratielkryleei
kpeivinlglaptysnitveriavniidaripdndgyqpidekieedaplaymatlpvra
itktlrdngipatisysagtylcnyvmfktlhfskiegyplkagfihvpytpdqvvnkff
llgkntpsmcleaeikaielavkvsldylekdrddikipl
>d1a2zc_ 3.58.3.1.1 Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase) {(Thermococcus litoralis)}
mkkvlitgfepfggdsknpteqiakyfdrkqignamvygrvlpvsvkratielkryleei
kpeivinlglaptysnitveriavniidaripdndgyqpidekieedaplaymatlpvra
itktlrdngipatisysagtylcnyvmfktlhfskiegyplkagfihvpytpdqvvnkff
llgkntpsmcleaeikaielavkvsldylekdrddikipl
>d1a2zd_ 3.58.3.1.1 Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase) {(Thermococcus litoralis)}
mkkvlitgfepfggdsknpteqiakyfdrkqignamvygrvlpvsvkratielkryleei
kpeivinlglaptysnitveriavniidaripdndgyqpidekieedaplaymatlpvra
itktlrdngipatisysagtylcnyvmfktlhfskiegyplkagfihvpytpdqvvnkff
llgkntpsmcleaeikaielavkvsldylekdrddikipl
>d1a30a_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwkrplvtikiggqlkealldtgaddtvieemslpgrwkpkmiggiggfikvrqyd
qiiieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1a30b_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwkrplvtikiggqlkealldtgaddtvieemslpgrwkpkmiggiggfikvrqyd
qiiieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1a32__ 1.15.1.2.1 Ribosomal protein S15 {(Bacillus stearothermophilus)}
ltqerkreiieqfkvhendtgspevqiailteqinnlnehlrvhkkdhhsrrgllkmvgk
rrrllaylrnkdvaryreiveklgl
>d1a34a_ 2.8.1.2.2 STMV coat protein {(Satellite tobacco mosaic virus)}
tgdnsnvvtmiragsypkvnptptwvraipfevsvqsgiafkvpvgslfsanfrtdsfts
vtvmsvrawtqltppvneysfvrlkplfktgdsteefegrasnintrasvgyriptnlrq
ntvaadnvcevrsncrqvalvisccfn
>e1a3b.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqf
>e1a3b.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
adcglrplfekksledkterellesyi
>d1a3d__ 1.103.1.2.2 Snake phospholipase A2 {indian cobra (Naja naja naja)}
nlyqfknmikctvpsrswwdfadygcycgrggsgtpvddldrccqvhdncyneaekisgc
wpyfktysyecsqgtltckgdnnacaasvcdcdrlaaicfagapyndnnynidlkarcq
>e1a3e.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqf
>e1a3e.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
adcglrplfekksledkterellesyi
>d1a3fa_ 1.103.1.2.2 Snake phospholipase A2 {indian cobra (Naja naja naja)}
nlyqfknmikctvpsrswwdfadygcycgrggsgtpvddldrccqvhdncyneaekisgc
wpyfktysyecsqgtltckgdnnacaasvcdcdrlaaicfagapyndnnynidlkarcq
>d1a3fb_ 1.103.1.2.2 Snake phospholipase A2 {indian cobra (Naja naja naja)}
nlyqfknmikctvpsrswwdfadygcycgrggsgtpvddldrccqvhdncyneaekisgc
wpyfktysyecsqgtltckgdnnacaasvcdcdrlaaicfagapyndnnynidlkarcq
>d1a3fc_ 1.103.1.2.2 Snake phospholipase A2 {indian cobra (Naja naja naja)}
nlyqfknmikctvpsrswwdfadygcycgrggsgtpvddldrccqvhdncyneaekisgc
wpyfktysyecsqgtltckgdnnacaasvcdcdrlaaicfagapyndnnynidlkarcq
>d1a3ga_ 5.14.1.1.2 Branched-chain amino acid aminotransferase {(Escherichia coli)}
kadyiwfngemvrwedakvhvmshalhygtsvfegircydshkgpvvfrhrehmqrlhds
akiyrfpvsqsidelmeacrdvirknnltsayirplifvgdvgmgvnppagystdviiaa
fpwgaylgaealeqgidamvsswnraapntiptaakaggnylssllvgsearrhgyqegi
aldvngyisegagenlfevkdgvlftppftssalpgitrdaiiklakelgievreqvlsr
eslyladevfmsgtaaeitpvrsvdgiqvgegrcgpvtkriqqaffglftgetedkwgwl
dqvnq
>d1a3gb_ 5.14.1.1.2 Branched-chain amino acid aminotransferase {(Escherichia coli)}
kadyiwfngemvrwedakvhvmshalhygtsvfegircydshkgpvvfrhrehmqrlhds
akiyrfpvsqsidelmeacrdvirknnltsayirplifvgdvgmgvnppagystdviiaa
fpwgaylgaealeqgidamvsswnraapntiptaakaggnylssllvgsearrhgyqegi
aldvngyisegagenlfevkdgvlftppftssalpgitrdaiiklakelgievreqvlsr
eslyladevfmsgtaaeitpvrsvdgiqvgegrcgpvtkriqqaffglftgetedkwgwl
dqvnq
>d1a3gc_ 5.14.1.1.2 Branched-chain amino acid aminotransferase {(Escherichia coli)}
kadyiwfngemvrwedakvhvmshalhygtsvfegircydshkgpvvfrhrehmqrlhds
akiyrfpvsqsidelmeacrdvirknnltsayirplifvgdvgmgvnppagystdviiaa
fpwgaylgaealeqgidamvsswnraapntiptaakaggnylssllvgsearrhgyqegi
aldvngyisegagenlfevkdgvlftppftssalpgitrdaiiklakelgievreqvlsr
eslyladevfmsgtaaeitpvrsvdgiqvgegrcgpvtkriqqaffglftgetedkwgwl
dqvnq
>d1a3k__ 2.21.1.3.5 Galectin-3 CRD {Human (Homo sapiens)}
livpynlplpggvvprmlitilgtvkpnanrialdfqrgndvafhfnprfnennrrvivc
ntkldnnwgreerqsvfpfesgkpfkiqvlvepdhfkvavndahllqynhrvkklneisk
lgisgdidltsasytmi
>d1a3na_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a3nb_ 1.1.1.1.25 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_ 1.1.1.1.25 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_ 1.1.1.1.25 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_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
hltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkvk
ahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgke
ftppvqaayqkvvagvanalahkyh
>d1a3qa1 2.1.1.5.19 (227-327) p50 subunit of NF-kappa B transcription factor, C-terminal domain {mouse (Mus musculus)}
nlkisrmdktagsvrggdevyllcdkvqkddievrfyeddengwqafgdfsptdvhkqya
ivfrtppyhkmkierpvtvflqlkrkrggdvsdskqftyyp
>d1a3qa2 2.2.4.1.4 (37-226) p50 subunit of NF-kappa B (NFKB), N-terminal domain {mouse (Mus musculus)}
gpylviveqpkqrgfrfrygcegpshgglpgassekgrktyptvkicnyegpakievdlv
thsdpprahahslvgkqcselgicavsvgpkdmtaqfnnlgvlhvtkknmmgtmiqklqr
qrlrsrpqglteaeqreleqeakelkkvmdlsivrlrfsaflrslplkpvisqpihdsks
pgas
>d1a3qb1 2.1.1.5.19 (227-327) p50 subunit of NF-kappa B transcription factor, C-terminal domain {mouse (Mus musculus)}
nlkisrmdktagsvrggdevyllcdkvqkddievrfyeddengwqafgdfsptdvhkqya
ivfrtppyhkmkierpvtvflqlkrkrggdvsdskqftyyp
>d1a3qb2 2.2.4.1.4 (37-226) p50 subunit of NF-kappa B (NFKB), N-terminal domain {mouse (Mus musculus)}
gpylviveqpkqrgfrfrygcegpshgglpgassekgrktyptvkicnyegpakievdlv
thsdpprahahslvgkqcselgicavsvgpkdmtaqfnnlgvlhvtkknmmgtmiqklqr
qrlrsrpqglteaeqreleqeakelkkvmdlsivrlrfsaflrslplkpvisqpihdsks
pgas
>d1a3rh1 2.1.1.1.12 (2-119) Immunoglobulin (variable domains of L and H chains) {Fab 8F5 (mouse), kappa L chain}
vqlqqsgaelvrpgasvklscttsgfnikdiyihwvkqrpeqglewigrldpangytkyd
pkfqgkatitvdtssntaylhlssltsedtavyycdgyysyydmdywgpgtsvtvssakt
tap
>d1a3rh2 2.1.1.2.21 (120-218) Immunoglobulin (constant domains of L and H chains) {Fab 8F5 (mouse), kappa L chain}
svyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsdlytlss
svtvtsstwpsqsitcnvahpasstk
>d1a3rl1 2.1.1.1.12 (1-114) Immunoglobulin (variable domains of L and H chains) {Fab 8F5 (mouse), kappa L chain}
divmtqspssltvttgekvtmtckssqsllnsrtqknyltwyqqkpgqspklliywastr
esgvpdrftgsgsgtdftlsisgvqaedlavyycqnnynypltfgagtklelkradaapt
>d1a3rl2 2.1.1.2.21 (115-214) Immunoglobulin (constant domains of L and H chains) {Fab 8F5 (mouse), kappa L chain}
vsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqdskdstys
msstltltkdeyerhnsytceathktstspivksfnrnec
>d1a3s__ 4.16.1.1.4 Ubiquitin conjugating enzyme {human/mouse (Homo sapiens/Mus musculus) ubc9}
msgialsrlaqerkawrkdhpfgfvavptknpdgtmnlmnwecaipgkkgtpwegglfkl
rmlfkddypssppkckfepplfhpnvypsgtvclsileedkdwrpaitikqillgiqell
nepniqdpaqaeaytiycqnrveyekrvraqakkfaps
>d1a3t__ 2.29.1.1.1 Staphylococcal nuclease {(Staphylococcal aureus)}
lhkepatlikaidgdtxklmykgqpmtfrlllvdtpetkhpkkgvekygpeasaftkkmv
enakkievefdkgqrtdkygrglayiyadgkmvnealvrqglakvayvykpnntheqhlr
kseaqakkeklniws
>d1a3u__ 2.29.1.1.1 Staphylococcal nuclease {(Staphylococcal aureus)}
lhkepatlikaidgdtxklmykgqpmtfrlllvdtpetkhpkkgvekygpeasaftkkmv
enakkievefdkgqrtdkygrglayiyadgkmvnealvrqglakvayvykpnntheqhlr
kseaqakkeklniws
>d1a3v__ 2.29.1.1.1 Staphylococcal nuclease {(Staphylococcal aureus)}
lhkepatlikaidgdtxklmykgqpmtfrlllvdtpetkhpkkgvekygpeasaftkkmv
enakkievefdkgqrtdkygrglayiyadgkmvnealvrqglakvayvykpnntheqhlr
kseaqakkeklniws
>d1a3wa1 2.44.1.1.3 (88-188) Pyruvate kinase {Baker's yeast (Saccharomyces cerevisiae)}
peirtgtttndvdypippnhemifttddkyakacddkimyvdyknitkvisagriiyvdd
gvlsfqvlevvddktlkvkalnagkicshkgvnlpgtdvdl
>d1a3wa2 3.1.9.1.3 (2-87,189-366) Pyruvate kinase, N-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
srlerltslnvvagsdlrrtsiigtigpktnnpetlvalrkaglnivrmnfshgsyeyhk
svidnarkseelypgrplaialdtkgXpalsekdkedlrfgvkngvhmvfasfirtandv
ltirevlgeqgkdvkiivkienqqgvnnfdeilkvtdgvmvargdlgieipapevlavqk
kliaksnlagkpvicatqmlesmtynprptraevsdvgnaildgadcvmlsgetakgnyp
inavttmaetaviaeqaiaylpnyd
>d1a3wa3 3.40.1.1.3 (367-500) Pyruvate kinase, C-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
dmrnctpkptsttetvaasavaavfeqkakaiivlstsgttprlvskyrpncpiilvtrc
praarfshlyrgvfpfvfekepvsdwtddvearinfgiekakefgilkkgdtyvsiqgfk
agaghsntlqvstv
>d1a3wb1 2.44.1.1.3 (88-188) Pyruvate kinase {Baker's yeast (Saccharomyces cerevisiae)}
peirtgtttndvdypippnhemifttddkyakacddkimyvdyknitkvisagriiyvdd
gvlsfqvlevvddktlkvkalnagkicshkgvnlpgtdvdl
>d1a3wb2 3.1.9.1.3 (2-87,189-366) Pyruvate kinase, N-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
srlerltslnvvagsdlrrtsiigtigpktnnpetlvalrkaglnivrmnfshgsyeyhk
svidnarkseelypgrplaialdtkgXpalsekdkedlrfgvkngvhmvfasfirtandv
ltirevlgeqgkdvkiivkienqqgvnnfdeilkvtdgvmvargdlgieipapevlavqk
kliaksnlagkpvicatqmlesmtynprptraevsdvgnaildgadcvmlsgetakgnyp
inavttmaetaviaeqaiaylpnyd
>d1a3wb3 3.40.1.1.3 (367-500) Pyruvate kinase, C-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
dmrnctpkptsttetvaasavaavfeqkakaiivlstsgttprlvskyrpncpiilvtrc
praarfshlyrgvfpfvfekepvsdwtddvearinfgiekakefgilkkgdtyvsiqgfk
agaghsntlqvstv
>d1a3xa1 2.44.1.1.3 (88-188) Pyruvate kinase {Baker's yeast (Saccharomyces cerevisiae)}
peirtgtttndvdypippnhemifttddkyakacddkimyvdyknitkvisagriiyvdd
gvlsfqvlevvddktlkvkalnagkicshkgvnlpgtdvdl
>d1a3xa2 3.1.9.1.3 (2-87,189-366) Pyruvate kinase, N-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
srlerltslnvvagsdlrrtsiigtigpktnnpetlvalrkaglnivrmnfshgsyeyhk
svidnarkseelypgrplaialdtkgXpalsekdkedlrfgvkngvhmvfasfirtandv
ltirevlgeqgkdvkiivkienqqgvnnfdeilkvtdgvmvargdlgieipapevlavqk
kliaksnlagkpvicatqmlesmtynprptraevsdvgnaildgadcvmlsgetakgnyp
inavttmaetaviaeqaiaylpnyd
>d1a3xa3 3.40.1.1.3 (367-500) Pyruvate kinase, C-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
dmrnctpkptsttetvaasavaavfeqkakaiivlstsgttprlvskyrpncpiilvtrc
praarfshlyrgvfpfvfekepvsdwtddvearinfgiekakefgilkkgdtyvsiqgfk
agaghsntlqvstv
>d1a3xb1 2.44.1.1.3 (88-188) Pyruvate kinase {Baker's yeast (Saccharomyces cerevisiae)}
peirtgtttndvdypippnhemifttddkyakacddkimyvdyknitkvisagriiyvdd
gvlsfqvlevvddktlkvkalnagkicshkgvnlpgtdvdl
>d1a3xb2 3.1.9.1.3 (2-87,189-366) Pyruvate kinase, N-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
srlerltslnvvagsdlrrtsiigtigpktnnpetlvalrkaglnivrmnfshgsyeyhk
svidnarkseelypgrplaialdtkgXpalsekdkedlrfgvkngvhmvfasfirtandv
ltirevlgeqgkdvkiivkienqqgvnnfdeilkvtdgvmvargdlgieipapevlavqk
kliaksnlagkpvicatqmlesmtynprptraevsdvgnaildgadcvmlsgetakgnyp
inavttmaetaviaeqaiaylpnyd
>d1a3xb3 3.40.1.1.3 (367-500) Pyruvate kinase, C-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
dmrnctpkptsttetvaasavaavfeqkakaiivlstsgttprlvskyrpncpiilvtrc
praarfshlyrgvfpfvfekepvsdwtddvearinfgiekakefgilkkgdtyvsiqgfk
agaghsntlqvstv
>d1a45_1 2.9.1.1.4 (1-84) gamma-Crystallin {bovine (Bos taurus) isoform F}
gkitfyedrgfqgrhyecssdhsnlqpyfsrcnsirvdsgcwmlyeqpnfqgpqyflrrg
dypdyqqwmglndsirscrlipht
>d1a45_2 2.9.1.1.4 (86-174) gamma-Crystallin {bovine (Bos taurus) isoform F}
gshrlriyeredyrgqmveitedcsslhdrfhfseihsfnvlegwwvlyemtnyrgrqyl
lrpgdyrryhdwgatnarvgslrravdfy
>e1a46.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1a46.1l 2.35.1.2.10 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 2.53.1.1.5 (383-495) Cyclodextrin glycosyltransferase {(Thermoanaerobacterium thermosulfurigenes) EM1}
tsttaynvikklaplrksnpaiaygttqqrwinndvyiyerkfgnnvalvainrnlstsy
nitglytalpagtytdvlggllngnsisvasdgsvtpftlsagevavwqyvss
>d1a47_4 3.1.1.1.5 (1-382) Cyclodextrin glycosyltransferase {(Thermoanaerobacterium thermosulfurigenes) EM1}
asdtavsnvvnystdviyqivtdrfvdgntsnnptgdlydpthtslkkyfggdwqgiink
indgyltgmgvtaiwisqpveniyavlpdstfggstsyhgywardfkrtnpyfgsftdfq
nlintahahnikviidfapnhtspasetdptyaengrlydngtllggytndtngyfhhyg
gtdfssyedgiyrnlfdladlnqqnstidsylksaikvwldmgidgirldavkhmpfgwq
knfmdsilsyrpvftfgewflgtneidvnntyfanesgmslldfrfsqkvrqvfrdntdt
mygldsmiqstasdynfindmvtfidnhdmdrfynggstrpveqalaftltsrgvpaiyy
gteqymtgngdpynrammtsfn
>d1a4aa_ 2.5.1.1.15 Azurin {(Alcaligenes denitrificans)}
aqceatiesndamqydlkemvvdksckqftvhlkhvgkmaksamghnwvltkeadkegva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
hkgtlklsn
>d1a4ab_ 2.5.1.1.15 Azurin {(Alcaligenes denitrificans)}
aqceatiesndamqydlkemvvdksckqftvhlkhvgkmaksamghnwvltkeadkegva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
hkgtlklsn
>d1a4ba_ 2.5.1.1.15 Azurin {(Alcaligenes denitrificans)}
aqceatiesndamqydlkemvvdksckqftvhlkhvgkmaksamghnwvltkeadkegva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
hkgtlklsn
>d1a4bb_ 2.5.1.1.15 Azurin {(Alcaligenes denitrificans)}
aqceatiesndamqydlkemvvdksckqftvhlkhvgkmaksamghnwvltkeadkegva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
hkgtlklsn
>d1a4ca_ 2.5.1.1.15 Azurin {(Alcaligenes denitrificans)}
aqceatiesndamqydlkemvvdksckqftvhlkhvgkmaksamghnwvltkeadkegva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
hkgtlklsn
>d1a4cb_ 2.5.1.1.15 Azurin {(Alcaligenes denitrificans)}
aqceatiesndamqydlkemvvdksckqftvhlkhvgkmaksamghnwvltkeadkegva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
hkgtlklsn
>d1a4cc_ 2.5.1.1.15 Azurin {(Alcaligenes denitrificans)}
aqceatiesndamqydlkemvvdksckqftvhlkhvgkmaksamghnwvltkeadkegva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
hkgtlklsn
>d1a4cd_ 2.5.1.1.15 Azurin {(Alcaligenes denitrificans)}
aqceatiesndamqydlkemvvdksckqftvhlkhvgkmaksamghnwvltkeadkegva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
hkgtlklsn
>d1a4fa_ 1.1.1.1.21 Hemoglobin, alpha-chain {Bar-headed goose (Anser indicus)}
vlsaadktnvkgvfskisghaeeygaetlermftaypqtktyfphfdlqhgsaqikahgk
kvvaalveavnhiddiagalsklsdlhaqklrvdpvnfkflghcflvvvaihhpsaltae
vhasldkflcavgtvltakyr
>d1a4fb_ 1.1.1.1.32 Hemoglobin, beta-chain {Bar-headed goose (Anser indicus)}
vhwsaeekqlitglwgkvnvadcgaealarllivypwtqrffssfgnlssptailgnpmv
rahgkkvltsfgdavknldnikntfaqlselhcdklhvdpenfrllgdiliivlaahfak
eftpdcqaawqklvrvvahalarkyh
>d1a4ja1 2.1.1.1.99 (1-112) Immunoglobulin (variable domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
elvmtqtplslpvslgdqasiscrssqslvhsngntylhwylqkpgqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyfcsqsthvpptfgggtkleik
>d1a4ja2 2.1.1.2.99 (113-217) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
rtvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqd
skdstyslsstltlskadyekhkvyacevthqglsspvtksfnrg
>d1a4jb1 2.1.1.1.99 (1-119) Immunoglobulin (variable domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
qvqllesgpelkkpgetvkisckasgytftnygmnwvkqapgkglkwmgwintytgepty
addfkgrfafsletsastaylqinnlknedtatyfcvqaerlrrtfdywgagttvtvss
>d1a4jb2 2.1.1.2.99 (120-217) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
astkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkv
>d1a4jh1 2.1.1.1.99 (1-119) Immunoglobulin (variable domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
qvqllesgpelkkpgetvkisckasgytftnygmnwvkqapgkglkwmgwintytgepty
addfkgrfafsletsastaylqinnlknedtatyfcvqaerlrrtfdywgagttvtvss
>d1a4jh2 2.1.1.2.99 (120-217) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
astkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkv
>d1a4jl1 2.1.1.1.99 (1-112) Immunoglobulin (variable domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
elvmtqtplslpvslgdqasiscrssqslvhsngntylhwylqkpgqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyfcsqsthvpptfgggtkleik
>d1a4jl2 2.1.1.2.99 (113-217) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
rtvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqd
skdstyslsstltlskadyekhkvyacevthqglsspvtksfnrg
>d1a4ka1 2.1.1.1.99 (1-112) Immunoglobulin (variable domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
elvmtqtplslpvslgdqasiscrssqsllhsngntylhwylqkpgqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyfcsqvthvpptfgggtkleikrtvaa
>d1a4ka2 2.1.1.2.99 (113-211) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
psvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqdskdst
yslsstltlskadyekhkvyacevthqglsspvtksfnr
>d1a4kb1 2.1.1.1.99 (1-119) Immunoglobulin (variable domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
qvqllesgpelkkpgetvkisckasgytftnygmnwvkqapgkglkwmgwintytgepty
addfkgrfafsletsastaylqinnlknedtatyfcvqaerlrrtfdywgagttvtvssa
stkgp
>d1a4kb2 2.1.1.2.99 (120-213) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
svfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqssglysls
svvtvpssslgtqtyicnvnhkpsntkvdkkvep
>d1a4kh1 2.1.1.1.99 (1-119) Immunoglobulin (variable domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
qvqllesgpelkkpgetvkisckasgytftnygmnwvkqapgkglkwmgwintytgepty
addfkgrfafsletsastaylqinnlknedtatyfcvqaerlrrtfdywgagttvtvssa
stkgp
>d1a4kh2 2.1.1.2.99 (120-211) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
svfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqssglysls
svvtvpssslgtqtyicnvnhkpsntkvdkkv
>d1a4kl1 2.1.1.1.99 (1-112) Immunoglobulin (variable domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
elvmtqtplslpvslgdqasiscrssqsllhsngntylhwylqkpgqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyfcsqvthvpptfgggtkleikrtvaa
>d1a4kl2 2.1.1.2.99 (113-212) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
psvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqdskdst
yslsstltlskadyekhkvyacevthqglsspvtksfnrg
>d1a4pa_ 1.37.1.2.5 Calcyclin (S100) {Human (Homo sapiens), P11 s100a10}
psqmehametmmftfhkfagdkgyltkedlrvlmekefpgflenqkdplavdkimkdldq
crdgkvgfqsffsliagltiacndyfvvhmkq
>d1a4pb_ 1.37.1.2.5 Calcyclin (S100) {Human (Homo sapiens), P11 s100a10}
psqmehametmmftfhkfagdkgyltkedlrvlmekefpgflenqkdplavdkimkdldq
crdgkvgfqsffsliagltiacndyfvvhmk
>d1a4sa_ 3.70.1.1.3 Aldehyde reductase (dehydrogenase) {Baltic cod (Gadus callarias)}
aqlvdsmpsastgsvvvtddlnywggrrikskdgattepvfepatgrvlcqmvpcgaeev
dqavqsaqaaylkwskmagiersrvmleaariirerrdniaklevinngktiteaeydid
aawqcieyyaglaptlsgqhiqlpggafaytrreplgvcagilawnypfmiaawkcapal
acgnavvfkpspmtpvtgvilaeifheagvpvglvnvvqggaetgsllchhpnvakvsft
gsvptgkkvmemsaktvkhvtlelggkspllifkdcelenavrgalmanfltqgqvctng
trvfvqreimpqfleevvkrtkaivvgdplltetrmggliskpqldkvlgfvaqakkega
rvlcggepltpsdpklkngyfmspcvldncrddmtcvkeeifgpvmsvlpfdteeevlqr
annttfglasgvftrdisrahrvaanleagtcyintysispvevpfggykmsgfgrengq
atvdyysqlktvivemgdvdslf
>d1a4sb_ 3.70.1.1.3 Aldehyde reductase (dehydrogenase) {Baltic cod (Gadus callarias)}
aqlvdsmpsastgsvvvtddlnywggrrikskdgattepvfepatgrvlcqmvpcgaeev
dqavqsaqaaylkwskmagiersrvmleaariirerrdniaklevinngktiteaeydid
aawqcieyyaglaptlsgqhiqlpggafaytrreplgvcagilawnypfmiaawkcapal
acgnavvfkpspmtpvtgvilaeifheagvpvglvnvvqggaetgsllchhpnvakvsft
gsvptgkkvmemsaktvkhvtlelggkspllifkdcelenavrgalmanfltqgqvctng
trvfvqreimpqfleevvkrtkaivvgdplltetrmggliskpqldkvlgfvaqakkega
rvlcggepltpsdpklkngyfmspcvldncrddmtcvkeeifgpvmsvlpfdteeevlqr
annttfglasgvftrdisrahrvaanleagtcyintysispvevpfggykmsgfgrengq
atvdyysqlktvivemgdvdslf
>d1a4sc_ 3.70.1.1.3 Aldehyde reductase (dehydrogenase) {Baltic cod (Gadus callarias)}
aqlvdsmpsastgsvvvtddlnywggrrikskdgattepvfepatgrvlcqmvpcgaeev
dqavqsaqaaylkwskmagiersrvmleaariirerrdniaklevinngktiteaeydid
aawqcieyyaglaptlsgqhiqlpggafaytrreplgvcagilawnypfmiaawkcapal
acgnavvfkpspmtpvtgvilaeifheagvpvglvnvvqggaetgsllchhpnvakvsft
gsvptgkkvmemsaktvkhvtlelggkspllifkdcelenavrgalmanfltqgqvctng
trvfvqreimpqfleevvkrtkaivvgdplltetrmggliskpqldkvlgfvaqakkega
rvlcggepltpsdpklkngyfmspcvldncrddmtcvkeeifgpvmsvlpfdteeevlqr
annttfglasgvftrdisrahrvaanleagtcyintysispvevpfggykmsgfgrengq
atvdyysqlktvivemgdvdslf
>d1a4sd_ 3.70.1.1.3 Aldehyde reductase (dehydrogenase) {Baltic cod (Gadus callarias)}
aqlvdsmpsastgsvvvtddlnywggrrikskdgattepvfepatgrvlcqmvpcgaeev
dqavqsaqaaylkwskmagiersrvmleaariirerrdniaklevinngktiteaeydid
aawqcieyyaglaptlsgqhiqlpggafaytrreplgvcagilawnypfmiaawkcapal
acgnavvfkpspmtpvtgvilaeifheagvpvglvnvvqggaetgsllchhpnvakvsft
gsvptgkkvmemsaktvkhvtlelggkspllifkdcelenavrgalmanfltqgqvctng
trvfvqreimpqfleevvkrtkaivvgdplltetrmggliskpqldkvlgfvaqakkega
rvlcggepltpsdpklkngyfmspcvldncrddmtcvkeeifgpvmsvlpfdteeevlqr
annttfglasgvftrdisrahrvaanleagtcyintysispvevpfggykmsgfgrengq
atvdyysqlktvivemgdvdslf
>e1a4w.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidq
>e1a4w.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
dcglrplfekksledkterellesyi
>d1a4za_ 3.70.1.1.2 Aldehyde reductase (dehydrogenase) {bovine (Bos taurus) mitochondria}
vptpnqqpevlynqifinnewhdavskktfptvnpstgdvichvaegdkadvdravkaar
aafqlgspwrrmdasergrllnrladlierdrtylaaletldngkpyiisylvdldmvlk
clryyagwadkyhgktipidgdyfsytrhepvgvcgqiipwnfpllmqawklgpalatgn
vvvmkvaeqtpltalyvanlikeagfppgvvnvipgfgptagaaiashedvdkvaftgst
evghliqvaagksnlkrvtleiggkspniimsdadmdwaveqahfalffnqgqcccagsr
tfvqediyaefversvaraksrvvgnpfdsrteqgpqvdetqfkkvlgyiksgkeeglkl
lcgggaaadrgyfiqptvfgdlqdgmtiakeeifgpvmqilkfksmeevvgrannskygl
aaavftkdldkanylsqalqagtvwvncydvfgaqspfggyklsgsgrelgeyglqayte
vktvtvrvpqkns
>d1a4zb_ 3.70.1.1.2 Aldehyde reductase (dehydrogenase) {bovine (Bos taurus) mitochondria}
vptpnqqpevlynqifinnewhdavskktfptvnpstgdvichvaegdkadvdravkaar
aafqlgspwrrmdasergrllnrladlierdrtylaaletldngkpyiisylvdldmvlk
clryyagwadkyhgktipidgdyfsytrhepvgvcgqiipwnfpllmqawklgpalatgn
vvvmkvaeqtpltalyvanlikeagfppgvvnvipgfgptagaaiashedvdkvaftgst
evghliqvaagksnlkrvtleiggkspniimsdadmdwaveqahfalffnqgqcccagsr
tfvqediyaefversvaraksrvvgnpfdsrteqgpqvdetqfkkvlgyiksgkeeglkl
lcgggaaadrgyfiqptvfgdlqdgmtiakeeifgpvmqilkfksmeevvgrannskygl
aaavftkdldkanylsqalqagtvwvncydvfgaqspfggyklsgsgrelgeyglqayte
vktvtvrvpqkns
>d1a4zc_ 3.70.1.1.2 Aldehyde reductase (dehydrogenase) {bovine (Bos taurus) mitochondria}
vptpnqqpevlynqifinnewhdavskktfptvnpstgdvichvaegdkadvdravkaar
aafqlgspwrrmdasergrllnrladlierdrtylaaletldngkpyiisylvdldmvlk
clryyagwadkyhgktipidgdyfsytrhepvgvcgqiipwnfpllmqawklgpalatgn
vvvmkvaeqtpltalyvanlikeagfppgvvnvipgfgptagaaiashedvdkvaftgst
evghliqvaagksnlkrvtleiggkspniimsdadmdwaveqahfalffnqgqcccagsr
tfvqediyaefversvaraksrvvgnpfdsrteqgpqvdetqfkkvlgyiksgkeeglkl
lcgggaaadrgyfiqptvfgdlqdgmtiakeeifgpvmqilkfksmeevvgrannskygl
aaavftkdldkanylsqalqagtvwvncydvfgaqspfggyklsgsgrelgeyglqayte
vktvtvrvpqkns
>d1a4zd_ 3.70.1.1.2 Aldehyde reductase (dehydrogenase) {bovine (Bos taurus) mitochondria}
vptpnqqpevlynqifinnewhdavskktfptvnpstgdvichvaegdkadvdravkaar
aafqlgspwrrmdasergrllnrladlierdrtylaaletldngkpyiisylvdldmvlk
clryyagwadkyhgktipidgdyfsytrhepvgvcgqiipwnfpllmqawklgpalatgn
vvvmkvaeqtpltalyvanlikeagfppgvvnvipgfgptagaaiashedvdkvaftgst
evghliqvaagksnlkrvtleiggkspniimsdadmdwaveqahfalffnqgqcccagsr
tfvqediyaefversvaraksrvvgnpfdsrteqgpqvdetqfkkvlgyiksgkeeglkl
lcgggaaadrgyfiqptvfgdlqdgmtiakeeifgpvmqilkfksmeevvgrannskygl
aaavftkdldkanylsqalqagtvwvncydvfgaqspfggyklsgsgrelgeyglqayte
vktvtvrvpqkns
>d1a57__ 2.45.1.2.2 Intestinal fatty acid binding protein {rat (Rattus rattus)}
afdgtwkvdrnenysgahdnlkltitqegnkftvkessnfrnidvvfelgvdfaysladg
teltgtwtmegnklvgkfkrvdngkeliavreisgneliqtytyegveakrifkke
>d1a58__ 2.47.1.1.4 Cyclophilin B {Nematode (Brugia malayi)}
mskkdrrrvfldvtidgnlagrivmelyndiaprtcnnflmlctgmagtgkisgkplhyk
gstfhrviknfmiqggdftkgdgtggesiyggmfddeefvmkhdepfvvsmankgpntng
sqffitttpaphlnnihvvfgkvvsgqevvtkieylktnsknrpladvvilncgelv
>d1a5aa_ 3.1.8.1.5 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_ 3.1.8.1.5 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_ 3.1.3.1.6 Fructose-1,6-bisphosphate aldolase {(Plasmodium falciparum)}
lpadvaeelattaqklvqagkgilaadestqtikkrfdniklentienrasyrdllfgtk
glgkfisgailfeetlfqkneagvpmvnllhneniipgikvdkglvnipctdeekstqgl
dglaerckeyykagarfakwrtvlvidtakgkptdlsihetawglaryasicqqnrlvpi
vepeiladgphsievcavvtqkvlscvfkalqengvllegallkpnmvtagyectakttt
qdvgfltvrtlrrtvppalpgvvflsggqseeeasvnlnsinalgphpwaltfsygralq
asvlntwqgkkenvakarevllqraeanslatygkykggagg
>d1a5cb_ 3.1.3.1.6 Fructose-1,6-bisphosphate aldolase {(Plasmodium falciparum)}
lpadvaeelattaqklvqagkgilaadestqtikkrfdniklentienrasyrdllfgtk
glgkfisgailfeetlfqkneagvpmvnllhneniipgikvdkglvnipctdeekstqgl
dglaerckeyykagarfakwrtvlvidtakgkptdlsihetawglaryasicqqnrlvpi
vepeiladgphsievcavvtqkvlscvfkalqengvllegallkpnmvtagyectakttt
qdvgfltvrtlrrtvppalpgvvflsggqseeeasvnlnsinalgphpwaltfsygralq
asvlntwqgkkenvakarevllqraeanslatygkykggagg
>d1a5da1 2.9.1.1.6 (1-84) beta-Crystallin {Rat (Rattus norvegicus) isoform E}
gkitfyedrgfqgrhyecstdhsnlqpyfsrcnsvrvdsgcwmlyeqpnftgcqyflrrg
dypdyqqwmgfsdsvrscrliphs
>d1a5da2 2.9.1.1.6 (85-174) beta-Crystallin {Rat (Rattus norvegicus) isoform E}
sshririyeredyrgqmveitddcphlqdrfhfsdfhsfhvmegywvlyempnyrgrqyl
lrpgeyrryhdwgamnarvgslrrimdfy
>d1a5db1 2.9.1.1.6 (1-84) beta-Crystallin {Rat (Rattus norvegicus) isoform E}
gkitfyedrgfqgrhyecstdhsnlqpyfsrcnsvrvdsgcwmlyeqpnftgcqyflrrg
dypdyqqwmgfsdsvrscrliphs
>d1a5db2 2.9.1.1.6 (85-174) beta-Crystallin {Rat (Rattus norvegicus) isoform E}
sshririyeredyrgqmveitddcphlqdrfhfsdfhsfhvmegywvlyempnyrgrqyl
lrpgeyrryhdwgamnarvgslrrimdfy
>e1a5g.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1a5g.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
adcglrplfekksledkterellesyi
>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_ 4.6.1.1.1 Urease, gamma-subunit {(Klebsiella aerogenes)}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1a5kb_ 2.66.2.1.1 Urease, beta-subunit {(Klebsiella aerogenes)}
mipgeyhvkpgqialntgratcrvvvenhgdrpiqvgshyhfaevnpalkfdrqqaagyr
lnipagtavrfepgqkrevelvafaghravfgfrgevmgpl
>d1a5kc1 2.69.1.1.1 (2-129,423-475) alpha-Subunit of urease, composite domain {(Klebsiella aerogenes)}
snisrqayadmfgptvgdkvrladtelwieveddlttygeevkfgggkvirdgmgqgqml
aadcvdlvltnalivdhwgivkadigvkdgrifaigkagnpdiqpnvtipigaateviaa
egkivtagXsievgkladlvvwspaffgvkpatvikggmiaiapmgdinasiptpqpvhy
rp
>d1a5kc2 3.1.2.2.1 (130-422,476-567) alpha-subunit of urease, catalytic domain {(Klebsiella aerogenes)}
gidthihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagvigleihedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvchhldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf
>d1a5la_ 4.6.1.1.1 Urease, gamma-subunit {(Klebsiella aerogenes)}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1a5lb_ 2.66.2.1.1 Urease, beta-subunit {(Klebsiella aerogenes)}
mipgeyhvkpgqialntgratcrvvvenhgdrpiqvgshyhfaevnpalkfdrqqaagyr
lnipagtavrfepgqkrevelvafaghravfgfrgevmgpl
>d1a5lc1 2.69.1.1.1 (2-129,423-475) alpha-Subunit of urease, composite domain {(Klebsiella aerogenes)}
snisrqayadmfgptvgdkvrladtelwieveddlttygeevkfgggkvirdgmgqgqml
aadcvdlvltnalivdhwgivkadigvkdgrifaigkagnpdiqpnvtipigaateviaa
egkivtagXsievgkladlvvwspaffgvkpatvikggmiaiapmgdinasiptpqpvhy
rp
>d1a5lc2 3.1.2.2.1 (130-422,476-567) alpha-subunit of urease, catalytic domain {(Klebsiella aerogenes)}
gidthihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagviglcihedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvahhldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf
>d1a5ma_ 4.6.1.1.1 Urease, gamma-subunit {(Klebsiella aerogenes)}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1a5mb_ 2.66.2.1.1 Urease, beta-subunit {(Klebsiella aerogenes)}
mipgeyhvkpgqialntgratcrvvvenhgdrpiqvgshyhfaevnpalkfdrqqaagyr
lnipagtavrfepgqkrevelvafaghravfgfrgevmgpl
>d1a5mc1 2.69.1.1.1 (2-129,423-475) alpha-Subunit of urease, composite domain {(Klebsiella aerogenes)}
snisrqayadmfgptvgdkvrladtelwieveddlttygeevkfgggkvirdgmgqgqml
aadcvdlvltnalivdhwgivkadigvkdgrifaigkagnpdiqpnvtipigaateviaa
egkivtagXsievgkladlvvwspaffgvkpatvikggmiaiapmgdinasiptpqpvhy
rp
>d1a5mc2 3.1.2.2.1 (130-422,476-567) alpha-subunit of urease, catalytic domain {(Klebsiella aerogenes)}
gidthihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagviglaihedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvchhldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf
>d1a5na_ 4.6.1.1.1 Urease, gamma-subunit {(Klebsiella aerogenes)}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1a5nb_ 2.66.2.1.1 Urease, beta-subunit {(Klebsiella aerogenes)}
mipgeyhvkpgqialntgratcrvvvenhgdrpiqvgshyhfaevnpalkfdrqqaagyr
lnipagtavrfepgqkrevelvafaghravfgfrgevmgpl
>d1a5nc1 2.69.1.1.1 (2-129,423-475) alpha-Subunit of urease, composite domain {(Klebsiella aerogenes)}
snisrqayadmfgptvgdkvrladtelwieveddlttygeevkfgggkvirdgmgqgqml
aadcvdlvltnalivdhwgivkadigvkdgrifaigkagnpdiqpnvtipigaateviaa
egkivtagXsievgkladlvvwspaffgvkpatvikggmiaiapmgdinasiptpqpvhy
rp
>d1a5nc2 3.1.2.2.1 (130-422,476-567) alpha-subunit of urease, catalytic domain {(Klebsiella aerogenes)}
gidthihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagviglaihedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvchhldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf
>d1a5oa_ 4.6.1.1.1 Urease, gamma-subunit {(Klebsiella aerogenes)}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1a5ob_ 2.66.2.1.1 Urease, beta-subunit {(Klebsiella aerogenes)}
mipgeyhvkpgqialntgratcrvvvenhgdrpiqvgshyhfaevnpalkfdrqqaagyr
lnipagtavrfepgqkrevelvafaghravfgfrgevmgpl
>d1a5oc1 2.69.1.1.1 (2-129,423-475) alpha-Subunit of urease, composite domain {(Klebsiella aerogenes)}
snisrqayadmfgptvgdkvrladtelwieveddlttygeevkfgggkvirdgmgqgqml
aadcvdlvltnalivdhwgivkadigvkdgrifaigkagnpdiqpnvtipigaateviaa
egkivtagXsievgkladlvvwspaffgvkpatvikggmiaiapmgdinasiptpqpvhy
rp
>d1a5oc2 3.1.2.2.1 (130-422,476-567) alpha-subunit of urease, catalytic domain {(Klebsiella aerogenes)}
gidthihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagviglcihedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvchhldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf
>d1a5p__ 4.4.1.1.1 Ribonuclease A (also ribonuclease B, S) {bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrakpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypnaaykttqankhiivacegnpyvpvhf
dasv
>d1a5q__ 4.4.1.1.1 Ribonuclease A (also ribonuclease B, S) {bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskyancaykttqankhiivacegnpyvpvhf
dasv
>d1a5t_1 1.93.1.1.1 (167-330) delta prime subunit of DNA polymerase III, C-terminal domain {(Escherichia coli)}
ppeqyavtwlsrevtmsqdallaalrlsagspgaalalfqgdnwqaretlcqalaysvps
gdwysllaalnheqaparlhwlatllmdalkrhhgaaqvtnvdvpglvaelanhlspsrl
qailgdvchireqlmsvtginrellitdlllriehylqpgvvlp
>d1a5t_2 3.29.1.8.3 (1-166) delta prime subunit of DNA polymerase III, N-terminal domain {(Escherichia coli)}
mrwypwlrpdfeklvasyqagrghhalliqalpgmgddaliyalsryllcqqpqghkscg
hcrgcqlmqagthpdyytlapekgkntlgvdavrevteklneharlggakvvwvtdaall
tdaaanallktleeppaetwfflatreperllatlrsrcrlhylap
>d1a5v__ 3.47.3.2.1 ASV integrase, catalytic domain {Avian sarcoma virus (Rous sarcoma virus), Schmidt-Ruppin strain B}
glgplqiwqtdftleprmaprswlavtvdtassaivvtqhgrvtsvaaqhhwataiavlg
rpkaiktdngscftskstrewlarwgiahttgipgnsqgqamveranrllkdkirvlaeg
dgfmkriptskqgellakamyalnhf
>d1a5w__ 3.47.3.2.1 ASV integrase, catalytic domain {Avian sarcoma virus (Rous sarcoma virus), Schmidt-Ruppin strain B}
glgplqiwqtdftleprmaprswlavtvdtassaivvtqhgrvtsvaaqhhwataiavlg
rpkaiktdngscftskstrewlarwgiahttgipgnsqgqamveranrllkdkirvlaeg
dgfmkriptskqgellakamyalnhf
>d1a5x__ 3.47.3.2.1 ASV integrase, catalytic domain {Avian sarcoma virus (Rous sarcoma virus), Schmidt-Ruppin strain B}
glgplqiwqtdftleprmaprswlavtvdtassaivvtqhgrvtsvaaqhhwataiavlg
rpkaiktdngscftskstrewlarwgiahttgipgnsqgqamveranrllkdkirvlaeg
dgfmkriptskqgellakamyalnhf
>d1a5y__ 3.37.1.2.1 Tyrosine phosphatase {Human (Homo sapiens) 1B}
emekefeqidksgswaaiyqdirheasdfpcrvaklpknknrnryrdvspfdhsriklhq
edndyinaslikmeeaqrsyiltqgplpntcghfwemvweqksrgvvmlnrvmekgslkc
aqywpqkeekemifedtnlkltlisediksyytvrqlelenlttqetreilhfhyttwpd
fgvpespasflnflfkvresgslspehgpvvvhxsagigrsgtfcladtclllmdkrkdp
ssvdikkvlldmrkfrmgliataeqlrfsylaviegakfimgds
>e1a61.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1a61.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
adcglrplfekksledkterellesyi
>d1a62__ 2.29.4.5.5 Rho termination factor, N-terminal, RNA-binding domain {(Escherichia coli)}
nltelkntpvselitlgenxglenlarxrkqdiifailkqhaksgedifgdgvleilqdg
fgflrsadssylagpddiyvspsqirrfnlrtgdtisgkirppkegeryfallkvnevnf
dkpe
>d1a63__ 2.29.4.5.5 Rho termination factor, N-terminal, RNA-binding domain {(Escherichia coli)}
mnltelkntpvselitlgenmglenlarmrkqdiifailkqhaksgedifgdgvleilqd
gfgflrsadssylagpddiyvspsqirrfnlrtgdtisgkirppkegeryfallkvnevn
fdkpenarnk
>d1a64a_ 2.1.1.1.6 CD2 {rat (Rattus rattus)}
gtvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlki
knltrddsgtynvtvystngtrildkaldlrile
>d1a64b_ 2.1.1.1.6 CD2 {rat (Rattus rattus)}
gtvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlki
knltrddsgtynvtvystngtrildkaldlrile
>d1a66a_ 2.2.4.1.2 Transcription factor NFATC, DNA-binding domain {human (Homo sapiens)}
mkdwqlpshsgpyelrievqpkshhraryetegsrgavkasagghpivqlhgyleneplm
lqlfigtaddrllrphafyqvhritgktvsttsheailsntkvleipllpensmravidc
agilklrnsdielrkgetdigrkntrvrlvfrvhvpqpsgrtlslqvasnpiecsqrs
>d1a67__ 4.13.1.2.1 Cystatin {chicken (Gallus gallus)}
gapvpvdendeglqralqfamaeynrasndkyssrvvrvisakrqlvsgikyilqveigr
ttcpkssgdlqscefhdepemakyttctfvvysipwlnqiklleskcq
>d1a68__ 4.24.1.1.1 Tetramerization domain of the shaker potassium channel {California sea hare (Aplysia californica)}
ervvinvsglrfetqlktlnqfpdtllgnpqkrnryydplrneyffdrnrpsfdailyfy
qsggrlrrpvnvpldvfseeikfyelg
>d1a6aa1 2.1.1.2.115 (82-180) Class II MHC, C-terminal domains of alpha and beta chains {(human hla-dr3)}
itnvppevtvltnspvelrepnvlicfidkftppvvnvtwlrngkpvttgvsetvflpre
dhlfrkfhylpflpstedvydcrvehwgldepllkhwef
>d1a6aa2 4.15.1.1.4 (5-81) MHC class II, N-terminal domains of alpha and beta chains {(human hla-dr3)}
hviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgalania
vdkanleimtkrsnytp
>d1a6ab1 2.1.1.2.115 (93-191) Class II MHC, C-terminal domains of alpha and beta chains {(human hla-dr3)}
rrvhpkvtvypsktqplqhhnllvcsvsgfypgsievrwfrngqeektgvvstglihngd
wtfqtlvmletvprsgevytcqvehpsvtspltvewrar
>d1a6ab2 4.15.1.1.4 (5-92) MHC class II, N-terminal domains of alpha and beta chains {(human hla-dr3)}
prfleystsechffngtervryldryfhnqeenvrfdsdvgefravtelgrpdaeywnsq
kdlleqkrgrvdnycrhnygvvesftvq
>d1a6ca1 2.8.1.2.6 (1-176) TRSV capsid protein {(tobacco ringspot virus)}
avtvvpdptccgtlsfkvpkdakkgkhlgtfdirqaimdygglhsqewcakgivnptftv
rmhaprnafaglsiactfddykridlpalgnecppsemfelptkvfmlkdadvhewqfny
geltghglcnwanvatqptlyffvastnqvtmaadwqcivtmhvdmgpvidrfeln
>d1a6ca2 2.8.1.2.6 (177-348) TRSV capsid protein {(tobacco ringspot virus)}
ptmtwpiqlgdtfaidryyeakeikldgstsmlsisynfggpvkhskkhaisysravmsr
nlgwsgtisgsvksvsslfctasfvifpweceapptlrqvlwgphqimhgdgqfeiaikt
rlhsaatteegfgrlgilplsgpiapdahvgsyefivhintwrpdsqvhppm
>d1a6ca3 2.8.1.2.6 (349-513) TRSV capsid protein {(tobacco ringspot virus)}
fssselynwftltnlkpdantgvvnfdipgyihdfaskdatvtlasnplswlvaatgwhy
gevdlciswsrskqaqaqegsvsittnyrdwgaywqgqariydlrrteaeipiflgsyag
atpsgalgkqnyvrisivnakdivalrvclrpksikfwgrsatlf
>d1a6ja_ 4.65.1.1.1 Nitrogen regulatory bacterial protein IIa-ntr {(Escherichia coli)}
lqlssvlnrectrsrvhcqskkraleiiselaakqlslppqvvfeailtrekmgstgign
giaiphgkleedtlravgvfvqletpiafdaidnqpvdllfallvpadqtkthlhtlslv
akrladkticrrlraaqsdeelyqiitdte
>d1a6jb_ 4.65.1.1.1 Nitrogen regulatory bacterial protein IIa-ntr {(Escherichia coli)}
mtnndttlqlssvlnrectrsrvhcqskkraleiiselaakqlslppqvvfeailtrekm
gstgigngiaiphgkleedtlravgvfvqletpiafdaidnqpvdllfallvpadqtkth
lhtlslvakrladkticrrlraaqsdeelyqiitdte
>d1a6l__ 4.34.1.2.1 Ferredoxin {(Azotobacter vinelandii )}
afvvtdncikckycdcvevcpvdcfyegpnflvihpdecidcalcepecpaqaifsedev
pedmqefiqlnaelaevwpnitekkdplpdaedwdgvkgklqhler
>d1a6o__ 5.1.1.1.14 Protein kiase CK2, alpha subunit {Maize (Zea mays)}
skarvyadvnvlrpkeywdyealtvqwgeqddyevvrkvgrgkysevfeginvnnnekci
ikilkpvkkkkikreikilqnlcggpnivklldivrdqhsktpslifeyvnntdfkvlyp
tltdydiryyiyellkaldychsqgimhrdvkphnvmidhelrklrlidwglaefyhpgk
eynvrvasryfkgpellvdlqdydysldmwslgcmfagmifrkepffyghdnhdqlvkia
kvlgtdglnvylnkyrieldpqlealvgrhsrkpwlkfmnadnqhlvspeaidfldkllr
ydhqerltaleamthpyfqqvraaens
>d1a6pa_ 2.1.1.1.6 CD2 {rat (Rattus rattus)}
gtvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlki
knltrddsgtynvtvystngtrildkaldlrile
>d1a6pb_ 2.1.1.1.6 CD2 {rat (Rattus rattus)}
gtvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlki
knltrddsgtynvtvystngtrildkaldlrile
>d1a6q__ 4.98.1.1.1 Protein serine/threonine phosphatase 2C {Human (Homo sapiens)}
gafldkpkmekhnaqgqgnglryglssmqgwrvemedahtaviglpsgleswsffavydg
hagsqvakyccehlldhitnnqdfkgsagapsvenvkngirtgfleidehmrvmsekkhg
adrsgstavgvlispqhtyfincgdsrgllcrnrkvhfftqdhkpsnplekeriqnaggs
vmiqrvngslavsralgdfdykcvhgkgpteqlvspepevhdierseeddqfiilacdgi
wdvmgneelcdfvrsrlevtddlekvcnevvdtclykgsrdnmsvilicfpnapkvspea
vkkeaeldkylecrveeiikkqgegvpdlvhvmrtlasenipslppggelaskrnvieav
ynrlnpy
>d1a6ta1 2.1.1.1.102 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab Mab1-IA (mouse), kappa L chain}
qsvlsqspailsaspgekvimtcspsssvsymqwyqqkpgsspkpwiystsnlasgvpgr
fsgggsgtsfsltisgveaedaatyycqqysshpltfgggtklelk
>d1a6ta2 2.1.1.2.101 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab Mab1-IA (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1a6tb1 2.1.1.1.102 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab Mab1-IA (mouse), kappa L chain}
evqlqqsgpdlvkpgasvkisckasgysfstyymhwvkqshgkslewigrvdpdnggtsf
nqkfkgkailtvdkssstaymelgsltsedsavyycarrddyyfdfwgqgtsltvss
>d1a6tb2 2.1.1.2.101 (114-213) Immunoglobulin (constant domains of L and H chains) {Fab Mab1-IA (mouse), kappa L chain}
akttppsvyplapvcggttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsg
lytlsssvtvtsstwpsqtitcnvahpasstkvdkkiepr
>d1a6tc1 2.1.1.1.102 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab Mab1-IA (mouse), kappa L chain}
qsvlsqspailsaspgekvimtcspsssvsymqwyqqkpgsspkpwiystsnlasgvpgr
fsgggsgtsfsltisgveaedaatyycqqysshpltfgggtklelk
>d1a6tc2 2.1.1.2.101 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab Mab1-IA (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1a6td1 2.1.1.1.102 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab Mab1-IA (mouse), kappa L chain}
evqlqqsgpdlvkpgasvkisckasgysfstyymhwvkqshgkslewigrvdpdnggtsf
nqkfkgkailtvdkssstaymelgsltsedsavyycarrddyyfdfwgqgtsltvss
>d1a6td2 2.1.1.2.101 (114-213) Immunoglobulin (constant domains of L and H chains) {Fab Mab1-IA (mouse), kappa L chain}
akttppsvyplapvcggttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsg
lytlsssvtvtsstwpsqtitcnvahpasstkvdkkiepr
>d1a6uh_ 2.1.1.1.103 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
qvqlqqpgaelvkpgasvklsckasgytftsywmhwvkqrpgrglewigridpnsggtky
nekfkskatltvdkpsstaymqlssltsedsavyycarydyygssyfdywgqgttvtvss
>d1a6ul_ 2.1.1.1.103 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
avvtqesalttspgetvtltcrsstgavttsnyanwvqekpdhlftgliggtnnrapgvp
arfsgslignkaaltitgaqtedeaiyfcalwysnhwvfgggtkltvl
>d1a6vh_ 2.1.1.1.103 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
qvqlqqpgaelvkpgasvklsckasgytftsywmhwvkqrpgrglewigridpnsggtky
nekfkskatltvdkpsstaymqlssltsedsavyycarydyygssyfdywgqgttvtv
>d1a6vi_ 2.1.1.1.103 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
qvqlqqpgaelvkpgasvklsckasgytftsywmhwvkqrpgrglewigridpnsggtky
nekfkskatltvdkpsstaymqlssltsedsavyycarydyygssyfdywgqgttvtvs
>d1a6vj_ 2.1.1.1.103 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
qvqlqqpgaelvkpgasvklsckasgytftsywmhwvkqrpgrglewigridpnsggtky
nekfkskatltvdkpsstaymqlssltsedsavyycarydyygssyfdywgqgttvtvss
>d1a6vl_ 2.1.1.1.103 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
qavvtqesalttspgetvtltcrsstgavttsnyanwvqekpdhlftgliggtnnrapgv
parfsgslignkaaltitgaqtedeaiyfcalwysnhwvfgggtkltvle
>d1a6vm_ 2.1.1.1.103 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
qavvtqesalttspgetvtltcrsstgavttsnyanwvqekpdhlftgliggtnnrapgv
parfsgslignkaaltitgaqtedeaiyfcalwysnhwvfgggtkltvl
>d1a6vn_ 2.1.1.1.103 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
qavvtqesalttspgetvtltcrsstgavttsnyanwvqekpdhlftgliggtnnrapgv
parfsgslignkaaltitgaqtedeaiyfcalwysnhwvfgggtkltvl
>d1a6wh_ 2.1.1.1.103 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
qvqlqqpgaelvkpgasvklsckasgytftsywmhwvkqrpgrglewigridpnsggtky
nekfkskatltvdkpsstaymqlssltsedsavyycarydyygssyfdywgqgttvtvss
>d1a6wl_ 2.1.1.1.103 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
avvtqesalttspgetvtltcrsstgavttsnyanwvqekpdhlftgliggtnnrapgvp
arfsgslignkaaltitgaqtedeaiyfcalwysnhwvfgggtkltvle
>d1a71a1 2.25.1.2.1 (1-174,325-374) Alcohol dehydrogenase {horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplwtpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1a71a2 3.22.1.1.1 (175-324) Alcohol dehydrogenase {horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggaglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1a71b1 2.25.1.2.1 (1-174,325-374) Alcohol dehydrogenase {horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplwtpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1a71b2 3.22.1.1.1 (175-324) Alcohol dehydrogenase {horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggaglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1a72_1 2.25.1.2.1 (1-174,325-374) Alcohol dehydrogenase {horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplwtpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1a72_2 3.22.1.1.1 (175-324) Alcohol dehydrogenase {horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggaglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1a74a_ 4.107.1.1.1 Intron-encoded homing endonuclease I-PpoI {Slime mold (Physarum polycephalum)}
altnaqilavidsweetvgqfpvithhvplggglqgtlhcyeiplaapygvgfakngptr
wqykrtinqvvhrwgshtvpfllepdningktctashlchntrchnplhlcweslddnkg
rnwcpgpnggcvhavvclrqgplygpgatvagpqqrgshfvv
>d1a74b_ 4.107.1.1.1 Intron-encoded homing endonuclease I-PpoI {Slime mold (Physarum polycephalum)}
altnaqilavidsweetvgqfpvithhvplggglqgtlhcyeiplaapygvgfakngptr
wqykrtinqvvhrwgshtvpfllepdningktctashlchntrchnplhlcweslddnkg
rnwcpgpnggcvhavvclrqgplygpgatvagpqqrgshfvv
>d1a75a_ 1.37.1.4.5 Parvalbumin {Whiting (Merlangius merlangus)}
agiladadcaaavkaceaadsfsykaffakcglsgksaddikkafvfidqdksgfieede
lklflqvfkagaraltdaetkaflkagdsdgdgaigveewvalvka
>d1a75b_ 1.37.1.4.5 Parvalbumin {Whiting (Merlangius merlangus)}
afagiladadcaaavkaceaadsfsykaffakcglsgksaddikkafvfidqdksgfiee
delklflqvfkagaraltdaetkaflkagdsdgdgaigveewvalvka
>d1a7ba_ 2.1.1.1.6 CD2 {rat (Rattus rattus)}
tvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlkik
nltrddsgtynvtvystngtrildkaldlrile
>d1a7bb_ 2.1.1.1.6 CD2 {rat (Rattus rattus)}
tvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlkik
nltrddsgtynvtvystngtrildkaldlrile
>d1a7bc_ 2.1.1.1.6 CD2 {rat (Rattus rattus)}
tvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlkik
nltrddsgtynvtvystngtrildkaldlrile
>d1a7bd_ 2.1.1.1.6 CD2 {rat (Rattus rattus)}
tvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlkik
nltrddsgtynvtvystngtrildkaldlrile
>e1a7f.1a 7.1.1.1.2 Insulin {human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1a7f.1b 7.1.1.1.2 Insulin {human (Homo sapiens)}
fvnqhlcgshlvealelvcgerggfytpk
>d1a7ha_ 2.9.1.1.3 gamma-Crystallin {bovine (Bos taurus) isoform S}
mykiqifekgdfngqmhettedcpsimeqfhmrevhsckvlegawifyelpnyrgrqyll
dkkeyrkpvdwgaaspavqsfrrive
>d1a7hb_ 2.9.1.1.3 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__ 3.29.1.2.1 Phosphoribulokinase {(Rhodobacter sphaeroides)}
skkhpiisvtgssgagtstvkhtfdqifrregvkavsiegdafhrfnradmkaeldrrya
agdatfshfsyeanelkelervfreygetgqgrtrtyvhddaeaartgvapgnftdwrdf
dsdshllfyeglhgavvnsevniagladlkigvvpvinlewiqkihrdratrgytteavt
dvilrrmhayvhcivpqfsqtdinfqrvpvvdtsnpfiarwiptadesvvvirfrnprgi
dfpyltsmihgswmsransivvpgnkldlamqliltplidrvvreskv
>d1a7ka1 3.22.1.3.6 (1-165,335-358) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Leishmania mexicana)}
apikvgingfgrigrmvfqaicdqgligteidvvavvdmstnaeyfayqmkhdtvhgrpk
ytveavksspsvetadvlvvnghrikcvkaqrnpadlpwgklgvdyviestglftdklka
eghikggakkvvisapasggaktivmgvnqheyspashhvvsnasXnewayshrvvdlvr
ymaakdaass
>d1a7ka2 4.42.1.1.6 (166-334) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Leishmania mexicana)}
cttnclapivhvltkenfgietglmttihsytatqktvdgvslkdwrggraaavniipst
tgaakavgmvipstkgkltgmsfrvptpdvsvvdltfratrdtsiqeidkaikkaaqtym
kgilgftdeelvsadfindnrssvydskatlqnnlpgekrffkvvswyd
>d1a7kb1 3.22.1.3.6 (1-165,335-358) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Leishmania mexicana)}
apikvgingfgrigrmvfqaicdqgligteidvvavvdmstnaeyfayqmkhdtvhgrpk
ytveavksspsvetadvlvvnghrikcvkaqrnpadlpwgklgvdyviestglftdklka
eghikggakkvvisapasggaktivmgvnqheyspashhvvsnasXnewayshrvvdlvr
ymaakdaass
>d1a7kb2 4.42.1.1.6 (166-334) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Leishmania mexicana)}
cttnclapivhvltkenfgietglmttihsytatqktvdgvslkdwrggraaavniipst
tgaakavgmvipstkgkltgmsfrvptpdvsvvdltfratrdtsiqeidkaikkaaqtym
kgilgftdeelvsadfindnrssvydskatlqnnlpgekrffkvvswyd
>d1a7kc1 3.22.1.3.6 (1-165,335-358) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Leishmania mexicana)}
apikvgingfgrigrmvfqaicdqgligteidvvavvdmstnaeyfayqmkhdtvhgrpk
ytveavksspsvetadvlvvnghrikcvkaqrnpadlpwgklgvdyviestglftdklka
eghikggakkvvisapasggaktivmgvnqheyspashhvvsnasXnewayshrvvdlvr
ymaakdaass
>d1a7kc2 4.42.1.1.6 (166-334) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Leishmania mexicana)}
cttnclapivhvltkenfgietglmttihsytatqktvdgvslkdwrggraaavniipst
tgaakavgmvipstkgkltgmsfrvptpdvsvvdltfratrdtsiqeidkaikkaaqtym
kgilgftdeelvsadfindnrssvydskatlqnnlpgekrffkvvswyd
>d1a7kd1 3.22.1.3.6 (1-165,335-358) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Leishmania mexicana)}
apikvgingfgrigrmvfqaicdqgligteidvvavvdmstnaeyfayqmkhdtvhgrpk
ytveavksspsvetadvlvvnghrikcvkaqrnpadlpwgklgvdyviestglftdklka
eghikggakkvvisapasggaktivmgvnqheyspashhvvsnasXnewayshrvvdlvr
ymaakdaass
>d1a7kd2 4.42.1.1.6 (166-334) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Leishmania mexicana)}
cttnclapivhvltkenfgietglmttihsytatqktvdgvslkdwrggraaavniipst
tgaakavgmvipstkgkltgmsfrvptpdvsvvdltfratrdtsiqeidkaikkaaqtym
kgilgftdeelvsadfindnrssvydskatlqnnlpgekrffkvvswyd
>d1a7la_ 3.82.1.1.6 D-maltodextrin-binding protein {(Escherichia coli)}
egklviwingdkgynglaevgkkfekdtgikvtvehpdkleekfpqvaatgdgpdiifwa
hdrfggyaqsgllaeitpdkafqdklypftwdavryngkliaypiavealsliynkdllp
nppktweeipaldkelkakgksalmfnlqepyftwpliaadggyafkyengkydikdvgv
dnagakagltflvdliknkhmnadtdysiaeaafnkgetamtingpwawsnidtskvnyg
vtvlptfkgqpskpfvgvlsaginaaspnkelakeflenylltdegleavnkdkplgava
lksyeeelakdpriaatmenaqkgeimpnipqmsafwyavrtavinaasgrqtvdealkd
gsqdprvrglyfpaggsecc
>d1a7lb_ 3.82.1.1.6 D-maltodextrin-binding protein {(Escherichia coli)}
egklviwingdkgynglaevgkkfekdtgikvtvehpdkleekfpqvaatgdgpdiifwa
hdrfggyaqsgllaeitpdkafqdklypftwdavryngkliaypiavealsliynkdllp
nppktweeipaldkelkakgksalmfnlqepyftwpliaadggyafkyengkydikdvgv
dnagakagltflvdliknkhmnadtdysiaeaafnkgetamtingpwawsnidtskvnyg
vtvlptfkgqpskpfvgvlsaginaaspnkelakeflenylltdegleavnkdkplgava
lksyeeelakdpriaatmenaqkgeimpnipqmsafwyavrtavinaasgrqtvdealkd
gsqdprvrglyf
>d1a7lc_ 3.82.1.1.6 D-maltodextrin-binding protein {(Escherichia coli)}
egklviwingdkgynglaevgkkfekdtgikvtvehpdkleekfpqvaatgdgpdiifwa
hdrfggyaqsgllaeitpdkafqdklypftwdavryngkliaypiavealsliynkdllp
nppktweeipaldkelkakgksalmfnlqepyftwpliaadggyafkyengkydikdvgv
dnagakagltflvdliknkhmnadtdysiaeaafnkgetamtingpwawsnidtskvnyg
vtvlptfkgqpskpfvgvlsaginaaspnkelakeflenylltdegleavnkdkplgava
lksyeeelakdpriaatmenaqkgeimpnipqmsafwyavrtavinaasgrqtvdealkd
gs
>d1a7nh_ 2.1.1.1.39 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
qvqlqesgpglvapsqslsitctvsgfsltgygvnwvrqppgkglewlgmiwgdgntdyn
salksrlsiskdnsksqvflkmnslhtddtaryycarerdyrldywgqgttvtvss
>d1a7nl_ 2.1.1.1.39 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
divltqspaslsasvgetvtitcrasgnihnylawyqqkqgkspqllvyytttladgvps
rfsgsgsgtqyslkinslqpddfgsyycqhfwstprtfgggtkleik
>d1a7oh_ 2.1.1.1.39 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
qvqlqesgpglvapsqslsitctvsgfsltgygvnwvrqppgkglewlgmiwgdgntdyn
salksrlsiskdnsksqvflkmnslhtddtaryycarerdyrldywgqgttvtvss
>d1a7ol_ 2.1.1.1.39 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
divltqspaslsasvgetvtitcrasgnihnylawyqqkqgkspqllvyytttladgvps
rfsgsgsgtqyslkinslqpddfgsyycqhfwstptfgggtkleik
>d1a7ph_ 2.1.1.1.39 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
qvqlqesgpglvapsqslsitctvsgfsltgygvnwvrqppgkglewlgmiwgdgntdyn
salksrlsiskdnsksqvflkmnslhtddtaryycarerdyrldywgqgttvtvss
>d1a7pl_ 2.1.1.1.39 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
divltqspaslsasvgetvtitcrasgnihnylawyqqkqgkspqllvyytttladgvps
rfsgsgsgtqyslkinslqpddfgsyycqhfwstsrtfgggtkleik
>d1a7qh_ 2.1.1.1.39 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
qvqlqesgpglvapsqslsitctvsgfsltgygvnwvrqlpgkglewlgmiwgdgntayn
salksrlsiskdnsksqvflemdslhtddtaryycarerdyrldywgqgttvtvss
>d1a7ql_ 2.1.1.1.39 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
divltqspaslsasvgetvtitcraggnthnylawyqqkqgkspqllvyytttlaagvps
rfsgsgsgtqyslkinslqpddfgsyycqhfwstprsfgggtklei
>d1a7rh_ 2.1.1.1.39 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
qvqlqesgpglvapsqslsitctvsgfsltgygvnwvrqppgkglewlgmiwgdgntdyn
salksrlsiskdnsksqvflkmnslhtddtaryycarerdyrldywgqgttltvss
>d1a7rl_ 2.1.1.1.39 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
divltqspaslsasvgetvtitcrasgnihnylawyqqkqgkspqllvyytttladgvps
rfsgsgsgtqyslkinslqpddfgsyycqhfwstprtfgggtkleik
>d1a7ta_ 4.97.1.1.2 Zn metallo-beta-lactamase {(Bacteroides fragilis)}
svkisddisitqlsdkvytyvslaeiegwgmvpsngmivinnhqaalldtpindaqteml
vnwvtdslhakvttfipnhwhgdcigglgylqrkgvqsyanqmtidlakekglpvpehgf
tdsltvsldgmplqcyylggghatdnivvwlptenilfggcmlkdnqttsignisdadvt
awpktldkvkakfpsaryvvpghgnyggteliehtkqivnqyiests
>d1a7tb_ 4.97.1.1.2 Zn metallo-beta-lactamase {(Bacteroides fragilis)}
svkisddisitqlsdkvytyvslaeiegwgmvpsngmivinnhqaalldtpindaqteml
vnwvtdslhakvttfipnhwhgdcigglgylqrkgvqsyanqmtidlakekglpvpehgf
tdsltvsldgmplqcyylggghatdnivvwlptenilfggcmlkdnqttsignisdadvt
awpktldkvkakfpsaryvvpghgnyggteliehtkqivnqyiests
>d1a7ua_ 3.56.1.5.3 Chloroperoxidase T {(Streptomyces aureofaciens)}
pfitvgqenstsidlyyedhgagqpvvlihgfplsghswerqsaalldagyrvitydrrg
fgqssqpttgydydtfaadlntvletldlqdavlvgfsmgtgevaryvssygtariakva
flaslepfllktddnpdgaapkeffdgivaavkadryafytgffndfynldenlgtrise
eavrnswntaasggffaaaaapttwytdfradipridvpalilhgtgdrtlpientarvf
hkalpsaeyvevegaphgllwthaeevntallaflak
>d1a7ub_ 3.56.1.5.3 Chloroperoxidase T {(Streptomyces aureofaciens)}
pfitvgqenstsidlyyedhgagqpvvlihgfplsghswerqsaalldagyrvitydrrg
fgqssqpttgydydtfaadlntvletldlqdavlvgfsmgtgevaryvssygtariakva
flaslepfllktddnpdgaapkeffdgivaavkadryafytgffndfynldenlgtrise
eavrnswntaasggffaaaaapttwytdfradipridvpalilhgtgdrtlpientarvf
hkalpsaeyvevegaphgllwthaeevntallaflak
>d1a7va_ 1.24.3.2.7 Cytochrome c' {(Rhodopseudomonas palustris)}
qtdviaqrkailkqmgeatkpiaamlkgeakfdqavvqkslaaiaddskklpalfpadsk
tggdtaalpkiwedkakfddlfaklaaaataaqgtikdeaslkaniggvlgnckschddf
rakks
>d1a7vb_ 1.24.3.2.7 Cytochrome c' {(Rhodopseudomonas palustris)}
qtdviaqrkailkqmgeatkpiaamlkgeakfdqavvqkslaaiaddskklpalfpadsk
tggdtaalpkiwedkakfddlfaklaaaataaqgtikdeaslkaniggvlgnckschddf
rakks
>d1a7xa_ 4.19.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1a7xb_ 4.19.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1a8a__ 1.55.1.1.6 Annexin V {Rat (Rattus norvegicus)}
alrgtvtdfsgfdgradaevlrkamkglgtdedsilnlltarsnaqrqqiaeefktlfgr
dlvndmkseltgkfeklivalmkpsrlydayelkhalkgagtdekvlteiiasrtpeelr
aikqayeeeygsnleddvvgdtsgyyqrmlvvllqanrdpdtaiddaqveldaqalfqag
elkwgtdeekfitilgtrsvshlrrvfdkymtisgfqieetidretsgnlenlllavvks
irsipaylaetlyyamkgagtddhtlirvivsrseidlfnirkefrknfatslysmikgd
tsgdykkallllcggedd
>d1a8b__ 1.55.1.1.6 Annexin V {Rat (Rattus norvegicus)}
alrgtvtdfsgfdgradaevlrkamkglgtdedsilnlltarsnaqrqqiaeefktlfgr
dlvndmkseltgkfeklivalmkpsrlydayelkhalkgagtdekvlteiiasrtpeelr
aikqayeeeygsnleddvvgdtsgyyqrmlvvllqanrdpdtaiddaqveldaqalfqag
elkwgtdeekfitilgtrsvshlrrvfdkymtisgfqieetidretsgnlenlllavvks
irsipaylaetlyyamkgagtddhtlirvivsrseidlfnirkefrknfatslysmikgd
tsgdykkallllcggedd
>d1a8e__ 3.82.1.2.6 Transferrin {human (Homo sapiens)}
dktvrwcavseheatkcqsfrdhmksvipsdgpsvacvkkasyldciraiaaneadavtl
daglvydaylapnnlkpvvaefygskedpqtfyyavavvkkdsgfqmnqlrgkkschtgl
grsagwnipigllycdlpeprkplekavanffsgscapcadgtdfpqlcqlcpgcgcstl
nqyfgysgafkclkdgagdvafvkhstifenlankadrdqyellcldntrkpvdeykdch
laqvpshtvvarsmggkedliwellnqaqehfgkdkskefqlfssphgkdllfkdsahgf
lkvpprmdakmylgyeyvtairnlregtc
>d1a8f__ 3.82.1.2.6 Transferrin {human (Homo sapiens)}
dktvrwcavseheatkcqsfrdhmksvipsdgpsvacvkkasyldciraiaaneadavtl
daglvydaylapnnlkpvvaefygskedpqtfyyavavvkkdsgfqmnqlrgkkschtgl
grsagwnipigllycdlpeprkplekavanffsgscapcadgtdfpqlcqlcpgcgcstl
nqyfgysgafkclkdgagdvafvkhstifenlankadrdqyellcldntrkpvdeykdch
laqvpshtvvarsmggkedliwellnqaqehfgkdkskefqlfssphgkdllfkdsahgf
lkvpprmdakmylgyeyvtairnlregtc
>d1a8ga_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemnlpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1a8gb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemnlpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1a8i__ 3.76.1.2.1 Glycogen phosphorylase {rabbit (Oryctolagus cuniculus)}
qekrkqisvrglagvenvtelkknfnrhlhftlvkdrnvatprdyyfalahtvrdhlvgr
wirtqqhyyekdpkriyylslefymgrtlqntmvnlalenacdeatyqlgldmeeleeie
edaglgngglgrlaacfldsmatlglaaygygiryefgifnqkicggwqmeeaddwlryg
npwekarpeftlpvhfygrvehtsqgakwvdtqvvlampydtpvpgyrnnvvntmrlwsa
kapndfnlkdfnvggyiqavldrnlaenisrvlypndnffegkelrlkqeyfvvaatlqd
iirrfksskfgcrdpvrtnfdafpdkvaiqlndthpslaipelmrvlvdlerldwdkawe
vtvktcaytnhtvipealerwpvhlletllprhlqiiyeinqrflnrvaaafpgdvdrlr
rmslveegavkrinmahlciagshavngvarihseilkktifkdfyelephkfqnktngi
tprrwlvlcnpglaeiiaerigeeyisdldqlrkllsyvddeafirdvakvkqenklkfa
aylereykvhinpnslfdvqvkriheykrqllnclhvitlynrikkepnkfvvprtvmig
gkaapgyhmakmiiklitaigdvvnhdpvvgdrlrviflenyrvslaekvipaadlseqi
stagteasgtgnmxfmlngaltigtmdganvemaeeageenffifgmrvedvdrldqrgy
naqeyydripelrqiieqlssgffspkqpdlfkdivnmlmhhdrfkvfadyeeyvkcqer
vsalyknprewtrmvirniatsgkfssdrtiaqyareiwgvepsrqrlp
>d1a8jh1 2.1.1.1.117 (2-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
saltqppsasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvp
drfsgsksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1a8jh2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1a8jl1 2.1.1.1.117 (2-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
saltqppsasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvp
drfsgsksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1a8jl2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1a8ma_ 2.17.1.1.2 Tumor necrosis factor (TNF) {human (Homo sapiens)}
rtpsdkpvahvvanpqaegqlqwlndranallangvelrdnqlvvpseglyliysqvlfk
gqgcpsthvllthtisriavsyqtkvnllsaikspcqretpegaeakpwyepiylggvfq
lekgdrlsaeinrpdyldfaesgqvyfgiial
>d1a8mb_ 2.17.1.1.2 Tumor necrosis factor (TNF) {human (Homo sapiens)}
rtpsdkpvahvvanpqaegqlqwlndranallangvelrdnqlvvpseglyliysqvlfk
gqgcpsthvllthtisriavsyqtkvnllsaikspcqretpegaeakpwyepiylggvfq
lekgdrlsaeinrpdyldfaesgqvyfgiial
>d1a8mc_ 2.17.1.1.2 Tumor necrosis factor (TNF) {human (Homo sapiens)}
rtpsdkpvahvvanpqaegqlqwlndranallangvelrdnqlvvpseglyliysqvlfk
gqgcpsthvllthtisriavsyqtkvnllsaikspcqretpegaeakpwyepiylggvfq
lekgdrlsaeinrpdyldfaesgqvyfgiial
>d1a8p_1 2.32.1.1.4 (2-100) Ferredoxin reductase (flavodoxin reductase) {(Azotobacter vinelandii)}
snlnvervlsvhhwndtlfsfkttrnpslrfengqfvmiglevdgrplmraysiaspnye
ehleffsikvqngpltsrlqhlkegdelmvsrkptgtlv
>d1a8p_2 3.16.1.1.4 (101-258) Ferredoxin reductase (flavodoxin reductase) {(Azotobacter vinelandii)}
tsdllpgkhlymlstgtglapfmsliqdpevyerfekvvlihgvrqvnelayqqfitehl
pqseyfgeavkekliyyptvtresfhnqgrltdlmrsgklfediglppinpqddramicg
spsmldescevldgfglkisprmgepgdylierafvek
>d1a8q__ 3.56.1.5.2 Bromoperoxidase A1 {(Streptomyces aureofaciens)}
picttrdgveifykdwgqgrpvvfihgwplngdawqdqlkavvdagyrgiahdrrghghs
tpvwdgydfdtfaddlndlltdldlrdvtlvahsmgggelaryvgrhgtgrlrsavllsa
ippvmiksdknpdgvpdevfdalkngvltersqfwkdtaegffsanrpgnkvtqgnkdaf
wymamaqtieggvrcvdafgytdftedlkkfdiptlvvhgdddqvvpidatgrksaqiip
naelkvyegsshgiamvpgdkekfnrdlleflnk
>d1a8s__ 3.56.1.5.4 Chloroperoxidase F {(Pseudomonas fluorescens)}
ttfttrdgtqiyykdwgsgqpivfshgwplnadswesqmiflaaqgyrviahdrrghgrs
sqpwsgndmdtyaddlaqliehldlrdavlfgfstgggevaryigrhgtarvakaglisa
vpplmlkteanpgglpmevfdgirqasladrsqlykdlasgpffgfnqpgakssagmvdw
fwlqgmaaghknaydcikafsetdftedlkkidvptlvvhgdadqvvpieasgiasaalv
kgstlkiysgaphgltdthkdqlnadllafikg
>d1a8ua_ 3.56.1.5.3 Chloroperoxidase T {(Streptomyces aureofaciens)}
pfitvgqenstsidlyyedhgagqpvvlihgfplsghswerqsaalldagyrvitydrrg
fgqssqpttgydydtfaadlntvletldlqdavlvgfsmgtgevaryvssygtariakva
flaslepfllktddnpdgaapkeffdgivaavkadryafytgffndfynldenlgtrise
eavrnswntaasggffaaaaapttwytdfradipridvpalilhgtgdrtlpientarvf
hkalpsaeyvevegaphgllwthaeevntallaflak
>d1a8ub_ 3.56.1.5.3 Chloroperoxidase T {(Streptomyces aureofaciens)}
pfitvgqenstsidlyyedhgagqpvvlihgfplsghswerqsaalldagyrvitydrrg
fgqssqpttgydydtfaadlntvletldlqdavlvgfsmgtgevaryvssygtariakva
flaslepfllktddnpdgaapkeffdgivaavkadryafytgffndfynldenlgtrise
eavrnswntaasggffaaaaapttwytdfradipridvpalilhgtgdrtlpientarvf
hkalpsaeyvevegaphgllwthaeevntallaflak
>d1a8z__ 2.5.1.1.20 Rusticyanin {(Thiobacillus ferooxidans)}
ldtswkeatlpqvkamlqkdtgkvsgdtvtysgktvhvvaaavlpgfpfpsfevhdkknp
tldipagatvdvtfintnkgfghsfditqktppfavmpvidpivagtgfspvpkdgkfgy
tnftwhptagtyyyvcqipghaatgmfgkivvk
>d1a90__ 4.13.1.2.1 Cystatin {chicken (Gallus gallus)}
gapvpvdendeglqralqfaiaeynrasndkyssrvvrvisakrqlvsgikyilqveigr
ttcpkssgdlqscefhdepelakyttctfvvysipwlnqiklleskcq
>d1a91__ 6.5.1.1.6 Subunit C of the F1F0 ATP synthase {(Escherichia coli)}
menlnmdllymaaavmmglaaigaaigigilggkflegaarqpdlipllrtqffivmglv
daipmiavglglyvmfava
>d1a98a_ 3.49.1.1.1 Xantine-guanine PRTase (XPRTase) {(Escherichia coli)}
ekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvaiss
ydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrplv
ddyvvdipqdtwieqpwdmgvvfvppisgr
>d1a98b_ 3.49.1.1.1 Xantine-guanine PRTase (XPRTase) {(Escherichia coli)}
ekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvaiss
ydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrplv
ddyvvdipqdtwieqpwdmgvvfvppis
>d1a9da1 2.1.1.2.15 (182-274) Class I MHC, beta2-microglobulin and alpha-3 domain {mouse (Mus musculus) H-2DB}
tdspkahvthhprskgevtlrcwalgfypaditltwqlngeeltqdmelvetrpagdgtf
qkwasvvvplgkeqnytcrvyheglpepltlrw
>d1a9da2 4.15.1.1.19 (2-181) MHC class I, alpha-1 and alpha-2 domains {mouse (Mus musculus) H-2DB}
phsmryfetavsrpgleepryisvgyvdnkefvrfdsdaenpryeprapwmeqegpeywe
retqkakgqeqwfrvslrnllgyynqsaggshtlqqmsgcdlgsdwrllrgylqfayegr
dyialnedlktwtaadmaaqitrrkweqsgaaehykaylegecvewlhrylkngnatllr
>d1a9ka1 2.1.1.2.5 (182-270) Class I MHC, beta2-microglobulin and alpha-3 domain {human (Homo sapiens) hla-a2.1}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrdgedqtqdtelvetrpagdgtf
qkwaavvvpsgqeqrytchvqheglpkpl
>d1a9ka2 4.15.1.1.9 (1-181) MHC class I, alpha-1 and alpha-2 domains {(human hla-a2.1)}
gshsmryfftsvsrpgrgeprfiavgyvddtqfvrfdsdaasqrmeprapwieqegpeyw
dgetrkvkahsqthrvdlgtlrgyynqseagshtvqrmygcdvgsdwrflrgyhqyaydg
kdyialkedlrswtaadmaaqttkhkweaahvaeqlraylegtcvewlrrylengketlq
r
>d1a9kd1 2.1.1.2.5 (182-270) Class I MHC, beta2-microglobulin and alpha-3 domain {human (Homo sapiens) hla-a2.1}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrdgedqtqdtelvetrpagdgtf
qkwaavvvpsgqeqrytchvqheglpkpl
>d1a9kd2 4.15.1.1.9 (1-181) MHC class I, alpha-1 and alpha-2 domains {(human hla-a2.1)}
gshsmryfftsvsrpgrgeprfiavgyvddtqfvrfdsdaasqrmeprapwieqegpeyw
dgetrkvkahsqthrvdlgtlrgyynqseagshtvqrmygcdvgsdwrflrgyhqyaydg
kdyialkedlrswtaadmaaqttkhkweaahvaeqlraylegtcvewlrrylengketlq
r
>d1a9ma_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmihgiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1a9mb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmihgiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1a9o__ 3.58.1.1.2 Purine nucleoside phosphorylase, PNP {Bovine (Bos taurus)}
mqngytyedyqdtakwllshteqrpqvavicgsglgglvnkltqaqtfdyseipnfpest
vpghagrlvfgilngracvmmqgrfhmyegypfwkvtfpvrvfrllgvetlvvtnaaggl
npnfevgdimlirdhinlpgfsgenplrgpneerfgvrfpamsdaydrdmrqkahstwkq
mgeqrelqegtyvmlggpnfetvaecrllrnlgadavgmstvpevivarhcglrvfgfsl
itnkvimdtesqgkanheevleagkqaaqkleqfvsllmasipvsghtg
>d1a9p__ 3.58.1.1.2 Purine nucleoside phosphorylase, PNP {Bovine (Bos taurus)}
mqngytyedyqdtakwllshteqrpqvavicgsglgglvnkltqaqtfdyseipnfpest
vpghagrlvfgilngracvmmqgrfhmyegypfwkvtfpvrvfrllgvetlvvtnaaggl
npnfevgdimlirdhinlpgfsgenplrgpneerfgvrfpamsdaydrdmrqkahstwkq
mgeqrelqegtyvmlggpnfetvaecrllrnlgadavgmstvpevivarhcglrvfgfsl
itnkvimdtesqgkanheevleagkqaaqkleqfvsllmasipvsghtg
>d1a9q__ 3.58.1.1.2 Purine nucleoside phosphorylase, PNP {Bovine (Bos taurus)}
mqngytyedyqdtakwllshteqrpqvavicgsglgglvnkltqaqtfdyseipnfpest
vpghagrlvfgilngracvmmqgrfhmyegypfwkvtfpvrvfrllgvetlvvtnaaggl
npnfevgdimlirdhinlpgfsgenplrgpneerfgvrfpamsdaydrdmrqkahstwkq
mgeqrelqegtyvmlggpnfetvaecrllrnlgadavgmstvpevivarhcglrvfgfsl
itnkvimdtesqgkanheevleagkqaaqkleqfvsllmasi
>d1a9r__ 3.58.1.1.2 Purine nucleoside phosphorylase, PNP {Bovine (Bos taurus)}
mqngytyedyqdtakwllshteqrpqvavicgsglgglvnkltqaqtfdyseipnfpest
vpghagrlvfgilngracvmmqgrfhmyegypfwkvtfpvrvfrllgvetlvvtnaaggl
npnfevgdimlirdhinlpgfsgenplrgpneerfgvrfpamsdaydrdmrqkahstwkq
mgeqrelqegtyvmlggpnfetvaecrllrnlgadavgmstvpevivarhcglrvfgfsl
itnkvimdtesqgkanheevleagkqaaqkleqfvsllmasi
>d1a9s__ 3.58.1.1.2 Purine nucleoside phosphorylase, PNP {Bovine (Bos taurus)}
mqngytyedyqdtakwllshteqrpqvavicgsglgglvnkltqaqtfdyseipnfpest
vpghagrlvfgilngracvmmqgrfhmyegypfwkvtfpvrvfrllgvetlvvtnaaggl
npnfevgdimlirdhinlpgfsgenplrgpneerfgvrfpamsdaydrdmrqkahstwkq
mgeqrelqegtyvmlggpnfetvaecrllrnlgadavgmstvpevivarhcglrvfgfsl
itnkvimdtesqgkanheevleagkqaaqkleqfvsllmasi
>d1a9t__ 3.58.1.1.2 Purine nucleoside phosphorylase, PNP {Bovine (Bos taurus)}
mangytyedyqdtakwllshteqrpqvavicgsglgglvnkltqaqtfdyseipnfpest
vpghagrlvfgilngracvmmqgrfhmyegypfwkvtfpvrvfrllgvetlvvtnaaggl
npnfevgdimlirdhinlpgfsgenplrgpneerfgvrfpamsdaydrdmrqkahstwkq
mgeqrelqegtyvmlggpnfetvaecrllrnlgadavgmstvpevivarhcglrvfgfsl
itnkvimdtesqgkanheevleagkqaaqkleqfvsllmasipv
>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_ 1.1.1.1.27 Hemoglobin, beta-chain {human (Homo sapiens) embryonic gower II}
vhftaeekaavtslwskmnveeaggealgrllvvypwtqrffdsfgnlsspsailgnpkv
kahgkkvltsfgdaiknmdnlkpafaklselhcdklhvdpenfkllgnvmviilathfgk
eftpevqaawqklvsavaialahky
>d1a9wf_ 1.1.1.1.27 Hemoglobin, beta-chain {human (Homo sapiens) embryonic gower II}
vhftaeekaavtslwskmnveeaggealgrllvvypwtqrffdsfgnlsspsailgnpkv
kahgkkvltsfgdaiknmdnlkpafaklselhcdklhvdpenfkllgnvmviilathfgk
eftpevqaawqklvsavaialahky
>d1aa0__ 6.4.1.1.1 Fibritin {(Bacteriophage T4)}
vsglnnavqnlqveignnsagikgqvvalntlvngtnpngstveergltnsikanetnia
svtqevntakgnisslqgdvqalqeagyipeaprdgqayvrkdgewvllstfl
>d1aa1b1 3.1.10.1.2 (148-463) Ribulose 1,5-bisphosphate carboxylase-oxygenase {spinach (Spinacia oleracea)}
fqgpphgiqverdklnkygrpllgctikpklglsaknygravyeclrggldftxddenvn
sqpfmrwrdrflfcaealykaqaetgeikghylnatagtcedmmkravfarelgvpivmh
dyltggftanttlshycrdnglllhihramhavidrqknhgmhfrvlakalrlsggdhih
sgtvvgklegerditlgfvdllrddytekdrsrgiyftqswvstpgvlpvasggihvwhm
palteifgddsvlqfgggtlghpwgnapgavanrvaleacvqarnegrdlaregntiire
atkwspelaaacevwk
>d1aa1b2 4.34.10.1.2 (21-147) Ribulose 1,5-bisphosphate carboxylase-oxygenase {spinach (Spinacia oleracea)}
kltyytpeyetldtdilaafrvspqpgvppeeagaavaaesstgtwttvwtdgltnldry
kgrcyhiepvageenqyicyvaypldlfeegsvtnmftsivgnvfgfkalralrledlri
pvayvkt
>d1aa1c_ 4.38.1.1.2 Ribulose 1,5-bisphosphate carboxylase-oxygenase {spinach (Spinacia oleracea)}
mqvwpilnlkkyetlsylpplttdqlarqvdyllnnkwvpclefetdhgfvyrehhnspg
yydgrywtmwklpmfgctdpaqvlneleeckkeypnafiriigfdsnrevqcisfiaykp
agy
>d1aa1e1 3.1.10.1.2 (148-463) Ribulose 1,5-bisphosphate carboxylase-oxygenase {spinach (Spinacia oleracea)}
fqgpphgiqverdklnkygrpllgctikpklglsaknygravyeclrggldftxddenvn
sqpfmrwrdrflfcaealykaqaetgeikghylnatagtcedmmkravfarelgvpivmh
dyltggftanttlshycrdnglllhihramhavidrqknhgmhfrvlakalrlsggdhih
sgtvvgklegerditlgfvdllrddytekdrsrgiyftqswvstpgvlpvasggihvwhm
palteifgddsvlqfgggtlghpwgnapgavanrvaleacvqarnegrdlaregntiire
atkwspelaaacevwk
>d1aa1e2 4.34.10.1.2 (21-147) Ribulose 1,5-bisphosphate carboxylase-oxygenase {spinach (Spinacia oleracea)}
kltyytpeyetldtdilaafrvspqpgvppeeagaavaaesstgtwttvwtdgltnldry
kgrcyhiepvageenqyicyvaypldlfeegsvtnmftsivgnvfgfkalralrledlri
pvayvkt
>d1aa1f_ 4.38.1.1.2 Ribulose 1,5-bisphosphate carboxylase-oxygenase {spinach (Spinacia oleracea)}
mqvwpilnlkkyetlsylpplttdqlarqvdyllnnkwvpclefetdhgfvyrehhnspg
yydgrywtmwklpmfgctdpaqvlneleeckkeypnafiriigfdsnrevqcisfiaykp
agy
>d1aa1h1 3.1.10.1.2 (148-463) Ribulose 1,5-bisphosphate carboxylase-oxygenase {spinach (Spinacia oleracea)}
fqgpphgiqverdklnkygrpllgctikpklglsaknygravyeclrggldftxddenvn
sqpfmrwrdrflfcaealykaqaetgeikghylnatagtcedmmkravfarelgvpivmh
dyltggftanttlshycrdnglllhihramhavidrqknhgmhfrvlakalrlsggdhih
sgtvvgklegerditlgfvdllrddytekdrsrgiyftqswvstpgvlpvasggihvwhm
palteifgddsvlqfgggtlghpwgnapgavanrvaleacvqarnegrdlaregntiire
atkwspelaaacevwk
>d1aa1h2 4.34.10.1.2 (21-147) Ribulose 1,5-bisphosphate carboxylase-oxygenase {spinach (Spinacia oleracea)}
kltyytpeyetldtdilaafrvspqpgvppeeagaavaaesstgtwttvwtdgltnldry
kgrcyhiepvageenqyicyvaypldlfeegsvtnmftsivgnvfgfkalralrledlri
pvayvkt
>d1aa1i_ 4.38.1.1.2 Ribulose 1,5-bisphosphate carboxylase-oxygenase {spinach (Spinacia oleracea)}
mqvwpilnlkkyetlsylpplttdqlarqvdyllnnkwvpclefetdhgfvyrehhnspg
yydgrywtmwklpmfgctdpaqvlneleeckkeypnafiriigfdsnrevqcisfiaykp
agy
>d1aa1l1 3.1.10.1.2 (148-463) Ribulose 1,5-bisphosphate carboxylase-oxygenase {spinach (Spinacia oleracea)}
fqgpphgiqverdklnkygrpllgctikpklglsaknygravyeclrggldftxddenvn
sqpfmrwrdrflfcaealykaqaetgeikghylnatagtcedmmkravfarelgvpivmh
dyltggftanttlshycrdnglllhihramhavidrqknhgmhfrvlakalrlsggdhih
sgtvvgklegerditlgfvdllrddytekdrsrgiyftqswvstpgvlpvasggihvwhm
palteifgddsvlqfgggtlghpwgnapgavanrvaleacvqarnegrdlaregntiire
atkwspelaaacevwk
>d1aa1l2 4.34.10.1.2 (21-147) Ribulose 1,5-bisphosphate carboxylase-oxygenase {spinach (Spinacia oleracea)}
kltyytpeyetldtdilaafrvspqpgvppeeagaavaaesstgtwttvwtdgltnldry
kgrcyhiepvageenqyicyvaypldlfeegsvtnmftsivgnvfgfkalralrledlri
pvayvkt
>d1aa1s_ 4.38.1.1.2 Ribulose 1,5-bisphosphate carboxylase-oxygenase {spinach (Spinacia oleracea)}
mqvwpilnlkkyetlsylpplttdqlarqvdyllnnkwvpclefetdhgfvyrehhnspg
yydgrywtmwklpmfgctdpaqvlneleeckkeypnafiriigfdsnrevqcisfiaykp
agy
>d1aa2__ 1.38.1.1.1 beta-spectrin {Human (Homo sapiens)}
ksakdalllwcqmktagypnvnihnfttswrdgmafnalihkhrpdlidfdklkksnahy
nlqnafnlaeqhlgltklldpedisvdhpdeksiityvvtyyhyfskm
>d1aa3__ 4.28.1.1.1 RecA protein, C-terminal domain {(Escherichia coli)}
infygelvdlgvkekliekagawysykgekigqgkanatawlkdnpetakeiekkvrell
lsn
>d1aa4__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1aa6_1 2.39.2.2.3 (565-715) Formate dehydrogenase H {(Escherichia coli)}
pidkltdeypmvlstvrevghyscrsmtgncaalaaladepgyaqintedakrlgiedea
lvwvhsrkgkiitraqvsdrpnkgaiymtyqwwigacnelvtenlspitktpeykycavr
vepiadqraaeqyvideynklktrlreaala
>d1aa6_2 3.69.1.1.3 (1-564) Formate dehydrogenase H {(Escherichia coli)}
mkkvvtvcpycasgckinlvvdngkivraeaaqgktnqgtlclkgyygwdfindtqiltp
rlktpmirrqrggklepvswdealnyvaerlsaikekygpdaiqttgssrgtgnetnyvm
qkfaravigtnnvdccarvxhgpsvaglhqsvgngamsnaineidntdlvfvfgynpads
hpivanhvinakrngakiivcdprkietariadmhialkngsniallnamghviieenly
dkafvasrtegfeeyrkivegytpesveditgvsaseirqaarmyaqaksaailwgmgvt
qfyqgvetvrsltslamltgnlgkphagvnpvrgqnnvqgacdmgalpdtypgyqyvkdp
anrekfakawgveslpahtgyriselphraahgevraayimgedplqtdaelsavrkafe
dlelvivqdifmtktasaadvilpstswgehegvftaadrgfqrffkavepkwdlktdwq
iiseiatrmgypmhynntqeiwdelrhlcpdfygatyekmgelgfiqwpcrdtsdadqgt
sylfkekfdtpnglaqfftcdwva
>d1aa7a_ 1.73.1.1.1 Influenza virus matrix protein M1 {(Influenza virus)}
mslltevetyvlsiipsgplkaeiaqrledvfagkntdlevlmewlktrpilspltkgil
gfvftltvpserglqrrrfvqnalngngdpnnmdkavklyrklkreitfhgakeislsys
agalascmgliynrmgavttevafglvcatceqiadsq
>d1aa7b_ 1.73.1.1.1 Influenza virus matrix protein M1 {(Influenza virus)}
slltevetyvlsiipsgplkaeiaqrledvfagkntdlevlmewlktrpilspltkgilg
fvftltvpserglqrrrfvqnalngngdpnnmdkavklyrklkreitfhgakeislsysa
galascmgliynrmgavttevafglvcatceqiadsq
>d1aa8a1 3.21.1.2.1 (1-194,288-340) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernll
>d1aa8a2 4.12.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1aa8b1 3.21.1.2.1 (1-194,288-340) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernll
>d1aa8b2 4.12.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1aa9__ 3.29.1.4.1 cH-p21 Ras protein {human (Homo sapiens)}
mteyklvvvgaggvgksaltiqliqnhfvdeydptiedsyrkqvvidgetclldildtag
qeeysamrdqymrtgegflcvfainntksfedihqyreqikrvkdsddvpmvlvgnkcdl
aartvesrqaqdlarsygipyietsaktrqgvedafytlvreirqhklrkl
>d1aab__ 1.21.1.1.1 HMG1, fragments 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-1 nucleocapsid {human immunodeficiency virus type 1 (Mn isolate)}
mqrgnfrnqrkiikcfncgkeghiakncraprkrgcwkcgkeghqmkdcterqan
>d1aaj__ 2.5.1.1.1 Amicyanin {(Paracoccus denitrificans)}
dkatipsespfaaaevadgaivvdiakmkyetpelhvkvgdtvtwinreamphnvhfvag
vlgeaalkgpmmkkeqaysltfteagtydyhctphpfmrgkvvve
>d1aala_ 7.7.1.1.1 Pancreatic trypsin inhibitor {bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglvqtfvyggcrakrnnfksaedamrtcgga
>d1aalb_ 7.7.1.1.1 Pancreatic trypsin inhibitor {bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglvqtfvyggcrakrnnfksaedamrtcgg
>d1aam__ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaaidanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aan__ 2.5.1.1.1 Amicyanin {(Paracoccus denitrificans)}
dkatipsespfaaaevadgaivvdiakmkyetpelhvkvgdtvtwinreamphnvhfvag
vlgeaalkgpmmkkeqaysltfteagtydyhctphpfmrgkvvve
>d1aapa_ 7.7.1.1.4 Alzheimer's amyloid B-protein precursor, APPI {human (Homo sapiens)}
vrevcseqaetgpcramisrwyfdvtegkcapffyggcggnrnnfdteeycmavcg
>d1aapb_ 7.7.1.1.4 Alzheimer's amyloid B-protein precursor, APPI {human (Homo sapiens)}
vrevcseqaetgpcramisrwyfdvtegkcapffyggcggnrnnfdteeycmavcg
>d1aaqa_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qiiieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1aaqb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qiiieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1aara_ 4.11.2.1.1 Ubiquitin {human (Homo sapiens)}
mqifvktltgktitlevepsdtienvkakiqdkegippdqqrlifagkqledgrtlsdyn
iqkestlhlvlrlrgg
>d1aarb_ 4.11.2.1.1 Ubiquitin {human (Homo sapiens)}
mqifvktltgktitlevepsdtienvkakiqdkegippdqqrlifagkqledgrtlsdyn
iqkestlhlvlrlrgg
>d1aat__ 3.54.1.1.2 Aspartate aminotransferase {chicken (Gallus gallus), cytosolic form}
aasifaavprappvavfkltadfredgdsrkvnlgvgayrtdegqpwvlpvvrkveqlia
gngslnheylpilglpefranasrialgddspaiaqkrvgsvqglggtgalrigaeflrr
wyngnnntatpvyvssptwenhnsvfmdagfkdirtyrywdaakrgldlqgllsdmekap
efsifilhacahnptgtdptpdewkqiaavmkrrclfpffdsayqgfasgnlekdawavr
yfvsegfelfcaqsfsknfglynervgnlsvvgkdednvqrvlsqmekivrttwsnppsq
garivattltspqlfaewkdnvktmadrvllmrselrsrleslgtpgtwnhitdqigmfs
ftglnpkqveymikekhiylmasgrinmcglttknldyvaksiheavtkiq
>d1aaw__ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aax__ 3.37.1.2.1 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_ 3.38.1.1.5 Glutaredoxin {(bacteriophage t4)}
mfkvygydsnihkcvycdnakrlltvkkqpfefinimpekgvfddekiaelltklgrdtq
igltmpqvfapdgshiggfdqlreyfk
>d1aazb_ 3.38.1.1.5 Glutaredoxin {(bacteriophage t4)}
mfkvygydsnihkcvycdnakrlltvkkqpfefinimpekgvfddekiaelltklgrdtq
igltmpqvfapdgshiggfdqlreyfk
>d1ab0__ 2.45.1.2.3 Adipocyte lipid-binding protein, ALBP {mouse (Mus musculus)}
gdafvgtwklvssenfddymkevgvgfatrkdagmakpnmiisvngdlvtirsesthknt
eisfklgvefdeitaddrkvksiitldggalvqvqkwdgksttikrkrdgdklvvecvmk
gvtstrvyera
>d1ab1__ 7.12.1.1.1 Crambin {abyssinian cabbage (Crambe abyssinica)}
ttccpsivarsnfnvcrlpgtseaicatytgciiipgatcpgdyan
>d1ab2__ 4.53.1.1.12 Proto-oncogen tyrosine kinase {Human (Homo sapiens)}
gsgnslekhswyhgpvsrnaaeyllssgingsflvresesspgqrsislryegrvyhyri
ntasdgklyvssesrfntlaelvhhhstvadglittlhypapkrgihrd
>d1ab3__ 1.15.1.2.2 Ribosomal protein S15 {(Thermus thermophilus)}
pitkeekqkviqefarfpgdtgstevqvalltlrinrlsehlkvhkkdhhshrgllmmvg
qrrrllrylqredperyralieklgirg
>d1ab5a_ 3.14.2.1.1 CheY protein {(Escherichia coli)}
elkflvvddnstmrritrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmpnmd
glellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleeklnkif
eklgm
>d1ab5b_ 3.14.2.1.1 CheY protein {(Escherichia coli)}
elkflvvddnstmrritrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmpnmd
glellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleeklnkif
eklgm
>d1ab6a_ 3.14.2.1.1 CheY protein {(Escherichia coli)}
elkflvvddnstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmpnmd
glellktiradgamsalpvlmttaeakkeniiaaaqagasgyvvkpftaatleeklnkif
eklgm
>d1ab6b_ 3.14.2.1.1 CheY protein {(Escherichia coli)}
elkflvvddnstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmpnmd
glellktiradgamsalpvlmttaeakkeniiaaaqagasgyvvkpftaatleeklnkif
eklgm
>d1ab7__ 3.6.1.1.1 Barstar (barnase inhibitor) {(Bacillus amyloliquefaciens)}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdaltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegaditiils
>d1ab8a_ 4.34.22.1.1 Type II adenylyl cyclase C2 domain {rat (Rattus norvegicus)}
lyhqsydcvcvmfasipdfkefytesdvnkegleclrllneiiadfddllskpkfsgvek
iktigstymaatglsaipsqehaqeperqymhigtmvefayalvgkldainkhsfndfkl
rvginhgpviagvigaqkpqydiwgntvnvasrmdstgvldkiqvteetslilqtlgytc
tcrgiinvkgkgdlktyfvn
>d1ab8b_ 4.34.22.1.1 Type II adenylyl cyclase C2 domain {rat (Rattus norvegicus)}
eelyhqsydcvcvmfasipdfkefytesdvnkegleclrllneiiadfddllskpkfsgv
ekiktigstymaatglsaipsqehaqeperqymhigtmvefayalvgkldainkhsfndf
klrvginhgpviagvigaqkpqydiwgntvnvasrmdstgvldkiqvteetslilqtlgy
tctcrgiinvkgkgdlktyfvn
>e1ab9.1b 2.35.1.2.7 (alpha, gamma-)chymotrypsin(ogen) {bovine (Bos taurus)}
ivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgvttsdvvvagefdqgs
ssekiqklkiakvfknskynsltinnditllklstaasfsqtvsavclpsasddfaagtt
cvttgwgltry
>e1ab9.1c 2.35.1.2.7 (alpha, gamma-)chymotrypsin(ogen) {bovine (Bos taurus)}
ntpdrlqqaslpllsntnckkywgtkikdamicagasgvsscmgdsggplvckkngawtl
vgivswgsstcststpgvyarvtalvnwvqqtlaan
>d1aba__ 3.38.1.1.5 Glutaredoxin {(bacteriophage t4)}
mfkvygydsnihkcgpcdnakrlltvkkqpfefinimpekgvfddekiaelltklgrdtq
igltmpqvfapdgshiggfdqlreyfk
>d1abba_ 3.76.1.2.1 Glycogen phosphorylase {rabbit (Oryctolagus cuniculus)}
rkqisvrglagvenvtelkknfnrhlhftlvkdrnvatprdyyfalahtvrdhlvgrwir
tqqhyyekdpkriyylslefymgrtlqntmvnlalenacdeatyqlgldmeeleeieeda
glgngglgrlaacfldsmatlglaaygygiryefgifnqkicggwqmeeaddwlrygnpw
ekarpeftlpvhfygrvehtsqgakwvdtqvvlampydtpvpgyrnnvvntmrlwsakap
ndfnlkdfnvggyiqavldrnlaenisrvlypndnffegkelrlkqeyfvvaatlqdiir
rfksskfgcrdpvrtnfdafpdkvaiqlndthpslaipelmrvlvdlerldwdkawevtv
ktcaytnhtvipealerwpvhlletllprhlqiiyeinqrflnrvaaafpgdvdrlrrms
lveegavkrinmahlciagshavngvarihseilkktifkdfyelephkfqnktngitpr
rwlvlcnpglaeiiaerigeeyisdldqlrkllsyvddeafirdvakvkqenklkfaayl
ereykvhinpnslfdvqvkriheykrqllnclhvitlynrikkepnkfvvprtvmiggka
apgyhmakmiiklitaigdvvnhdpvvgdrlrviflenyrvslaekvipaadlseqista
gteasgtgnmkfmlngaltigtmdganvemaeeageenffifgmrvedvdrldqrgynaq
eyydripelrqiieqlssgffspkqpdlfkdivnmlmhhdrfkvfadyeeyvkcqervsa
lyknprewtrmvirniatsgkfssdrtiaqyareiwgvepsrqrlpap
>d1abbb_ 3.76.1.2.1 Glycogen phosphorylase {rabbit (Oryctolagus cuniculus)}
rkqisvrglagvenvtelkknfnrhlhftlvkdrnvatprdyyfalahtvrdhlvgrwir
tqqhyyekdpkriyylslefymgrtlqntmvnlalenacdeatyqlgldmeeleeieeda
glgngglgrlaacfldsmatlglaaygygiryefgifnqkicggwqmeeaddwlrygnpw
ekarpeftlpvhfygrvehtsqgakwvdtqvvlampydtpvpgyrnnvvntmrlwsakap
ndfnlkdfnvggyiqavldrnlaenisrvlypndnffegkelrlkqeyfvvaatlqdiir
rfksskfgcrdpvrtnfdafpdkvaiqlndthpslaipelmrvlvdlerldwdkawevtv
ktcaytnhtvipealerwpvhlletllprhlqiiyeinqrflnrvaaafpgdvdrlrrms
lveegavkrinmahlciagshavngvarihseilkktifkdfyelephkfqnktngitpr
rwlvlcnpglaeiiaerigeeyisdldqlrkllsyvddeafirdvakvkqenklkfaayl
ereykvhinpnslfdvqvkriheykrqllnclhvitlynrikkepnkfvvprtvmiggka
apgyhmakmiiklitaigdvvnhdpvvgdrlrviflenyrvslaekvipaadlseqista
gteasgtgnmkfmlngaltigtmdganvemaeeageenffifgmrvedvdrldqrgynaq
eyydripelrqiieqlssgffspkqpdlfkdivnmlmhhdrfkvfadyeeyvkcqervsa
lyknprewtrmvirniatsgkfssdrtiaqyareiwgvepsrqrlpap
>d1abbc_ 3.76.1.2.1 Glycogen phosphorylase {rabbit (Oryctolagus cuniculus)}
rkqisvrglagvenvtelkknfnrhlhftlvkdrnvatprdyyfalahtvrdhlvgrwir
tqqhyyekdpkriyylslefymgrtlqntmvnlalenacdeatyqlgldmeeleeieeda
glgngglgrlaacfldsmatlglaaygygiryefgifnqkicggwqmeeaddwlrygnpw
ekarpeftlpvhfygrvehtsqgakwvdtqvvlampydtpvpgyrnnvvntmrlwsakap
ndfnlkdfnvggyiqavldrnlaenisrvlypndnffegkelrlkqeyfvvaatlqdiir
rfksskfgcrdpvrtnfdafpdkvaiqlndthpslaipelmrvlvdlerldwdkawevtv
ktcaytnhtvipealerwpvhlletllprhlqiiyeinqrflnrvaaafpgdvdrlrrms
lveegavkrinmahlciagshavngvarihseilkktifkdfyelephkfqnktngitpr
rwlvlcnpglaeiiaerigeeyisdldqlrkllsyvddeafirdvakvkqenklkfaayl
ereykvhinpnslfdvqvkriheykrqllnclhvitlynrikkepnkfvvprtvmiggka
apgyhmakmiiklitaigdvvnhdpvvgdrlrviflenyrvslaekvipaadlseqista
gteasgtgnmkfmlngaltigtmdganvemaeeageenffifgmrvedvdrldqrgynaq
eyydripelrqiieqlssgffspkqpdlfkdivnmlmhhdrfkvfadyeeyvkcqervsa
lyknprewtrmvirniatsgkfssdrtiaqyareiwgvepsrqrlpap
>d1abbd_ 3.76.1.2.1 Glycogen phosphorylase {rabbit (Oryctolagus cuniculus)}
rkqisvrglagvenvtelkknfnrhlhftlvkdrnvatprdyyfalahtvrdhlvgrwir
tqqhyyekdpkriyylslefymgrtlqntmvnlalenacdeatyqlgldmeeleeieeda
glgngglgrlaacfldsmatlglaaygygiryefgifnqkicggwqmeeaddwlrygnpw
ekarpeftlpvhfygrvehtsqgakwvdtqvvlampydtpvpgyrnnvvntmrlwsakap
ndfnlkdfnvggyiqavldrnlaenisrvlypndnffegkelrlkqeyfvvaatlqdiir
rfksskfgcrdpvrtnfdafpdkvaiqlndthpslaipelmrvlvdlerldwdkawevtv
ktcaytnhtvipealerwpvhlletllprhlqiiyeinqrflnrvaaafpgdvdrlrrms
lveegavkrinmahlciagshavngvarihseilkktifkdfyelephkfqnktngitpr
rwlvlcnpglaeiiaerigeeyisdldqlrkllsyvddeafirdvakvkqenklkfaayl
ereykvhinpnslfdvqvkriheykrqllnclhvitlynrikkepnkfvvprtvmiggka
apgyhmakmiiklitaigdvvnhdpvvgdrlrviflenyrvslaekvipaadlseqista
gteasgtgnmkfmlngaltigtmdganvemaeeageenffifgmrvedvdrldqrgynaq
eyydripelrqiieqlssgffspkqpdlfkdivnmlmhhdrfkvfadyeeyvkcqervsa
lyknprewtrmvirniatsgkfssdrtiaqyareiwgvepsrqrlpap
>d1abe__ 3.81.1.1.2 L-arabinose-binding protein {(Escherichia coli)}
nlklgflvkqpeepwfqtewkfadkagkdlgfevikiavpdgektlnaidslaasgakgf
victpdpklgsaivakargydmkviavddqfvnakgkpmdtvplvmmaatkigerqgqel
ykemqkrgwdvkesavmaitaneldtarrrttgsmdalkaagfpekqiyqvptksndipg
afdaansmlvqhpevkhwlivgmndstvlggvrategqgfkaadiigigingvdavsels
kaqatgfygsllpspdvhgykssemlynwvakdveppkftevtdvvlitrdnfkeelekk
glggk
>d1abf__ 3.81.1.1.2 L-arabinose-binding protein {(Escherichia coli)}
nlklgflvkqpeepwfqtewkfadkagkdlgfevikiavpdgektlnaidslaasgakgf
victpdpklgsaivakargydmkviavddqfvnakgkpmdtvplvmmaatkigerqgqel
ykemqkrgwdvkesavmaitaneldtarrrttgsmdalkaagfpekqiyqvptksndipg
afdaansmlvqhpevkhwlivgmndstvlggvrategqgfkaadiigigingvdavsels
kaqatgfygsllpspdvhgykssemlynwvakdveppkftevtdvvlitrdnfkeelekk
glggk
>e1abi.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>e1abi.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
sgeadcglrplfekksledkterellesyidgr
>e1abj.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1abj.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
adcglrplfekksledkterellesyi
>d1abma1 1.2.4.1.4 (1-83) Mn superoxide dismutase (SOD) {human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaayvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1abma2 4.26.1.1.3 (84-198) Mn superoxide dismutase (SOD) {human (Homo sapiens)}
ngggepkgelleaikrdfgsfdkfkekltaasvgvqgsgwgwlgfnkerghlqiaacpnq
dplqgttglipllgidvwehayylqyknvrpdylkaiwnvinwenvterymackk
>d1abmb1 1.2.4.1.4 (1-83) Mn superoxide dismutase (SOD) {human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaayvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1abmb2 4.26.1.1.3 (84-198) Mn superoxide dismutase (SOD) {human (Homo sapiens)}
ngggepkgelleaikrdfgsfdkfkekltaasvgvqgsgwgwlgfnkerghlqiaacpnq
dplqgttglipllgidvwehayylqyknvrpdylkaiwnvinwenvterymackk
>d1abn__ 3.1.5.1.2 Aldose reductase (aldehyde reductase) {human (Homo sapiens)}
srlllnngakmpilglgtwksppgqvteavkvaidvgyrhidcahvyqnenevgvaiqek
lreqvvkreelfivsklwctyhekglvkgacqktlsdlkldyldlylihwptgfkpgkef
fpldesgnvvpsdtnildtwaameelvdeglvkaigisnfnhlqvemilnkpglkykpav
nqiechpyltqekliqycqskgivvtaysplgspdrpwakpedpslledprikaiaakhn
kttaqvlirfpmqrnlvvipksvtperiaenfkvfdfelssqdmttllsynrnwrvsall
sctshkdypfheef
>d1aboa_ 2.24.2.1.4 Abl tyrosine kinase, SH3 domain {Mouse (Mus musculus)}
nlfvalydfvasgdntlsitkgeklrvlgynhngewceaqtkngqgwvpsnyitpvns
>d1abob_ 2.24.2.1.4 Abl tyrosine kinase, SH3 domain {Mouse (Mus musculus)}
nlfvalydfvasgdntlsitkgeklrvlgynhngewceaqtkngqgwvpsnyitpvns
>d1abq__ 2.24.2.1.4 Abl tyrosine kinase, SH3 domain {Mouse (Mus musculus)}
lfvalydfvasgdntlsitkgeklrvlgynhngewceaqtkngqgwvpsnyitpvn
>d1abra_ 4.102.1.1.4 Abrin A-chain {(Abrus precatorius)}
edrpikfstegatsqsykqfiealrerlrgglihdipvlpdpttlqernryitvelsnsd
tesievgidvtnayvvayragtqsyflrdapssasdylftgtdqhslpfygtygdlerwa
hqsrqqiplglqalthgisffrsggndneekartliviiqmvaeaarfryisnrvrvsiq
tgtafqpdaamislennwdnlsrgvqesvqdtfpnqvtltnirnepvivdslshptvavl
almlfvcnppn
>d1abrb1 2.31.2.1.2 (1-140) Plant cytotoxin B-chain (lectin) {(Abrus precatorius); Abrin}
ivekskicssryeptvriggrdgmcvdvydngyhngnriimwkckdrleenqlwtlksdk
tirsngkclttygyapgsyvmiydctsavaeatyweiwdngtiinpksalvlsaesssmg
gtltvqtneylmrqgwrtgn
>d1abrb2 2.31.2.1.2 (141-267) Plant cytotoxin B-chain (lectin) {(Abrus precatorius); Abrin}
ntspfvtsisgysdlcmqaqgsnvwmadcdsnkkeqqwalytdgsirsvqntnncltskd
hkqgstillmgcsngwasqrwvfkndgsiyslyddmvmdvkgsdpslkqiilwpytgkpn
qiwltlf
>d1abs__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1abta_ 7.6.1.1.10 Bungarotoxin {alpha-bungarotoxin: (Bungarus multicinctus)}
ivchttatspisavtcppgenlcyrkmwcdafcssrgkvvelgcaatcpskkpyeevtcc
stdkcnphpkqrpg
>d1abv__ 1.60.1.1.1 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_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgkvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1abwd_ 1.1.1.1.25 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_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgkvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1abyd_ 1.1.1.1.25 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 1.42.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {(Escherichia coli)}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1ac1a2 3.38.1.3.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) {(Escherichia coli)}
aqyedgkqyttlekpvagapqvleffsffcplcyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsek
>d1ac1b1 1.42.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {(Escherichia coli)}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1ac1b2 3.38.1.3.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) {(Escherichia coli)}
aqyedgkqyttlekpvagapqvleffsffcplcyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsek
>d1ac4__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1ac5__ 3.56.1.2.3 Serine carboxypeptidase II {yeast (Saccharomyces cerevisiae), kex1(delta)p}
lpsseeykvayellpglsevpdpsnipqmhaghiplrsedadeqdssdleyffwkftnnd
sngnvdrpliiwlnggpgcssmdgalvesgpfrvnsdgklylnegswiskgdllfidqpt
gtgfsveqnkdegkidknkfdedledvtkhfmdflenyfkifpedltrkiilsgesyagq
yipffanailnhnkfskidgdtydlkalligngwidpntqslsylpfamekklidesnpn
fkhltnahencqnlinsastdeaahfsyqecenilnlllsytressqkgtadclnmynfn
lkdsypscgmnwpkdisfvskffstpgvidslhldsdkidhwkectnsvgtklsnpiskp
sihllpgllesgieivlfngdkdlicnnkgvldtidnlkwggikgfsddavsfdwihksk
stddseefsgyvkydrnltfvsvynashmvpfdkslvsrgivdiysndvmiidnngknvm
itt
>d1ac6a_ 2.1.1.1.120 T-cell antigen receptor {human (Homo sapiens), alpha-chain}
dsvtqtegqvalseedfltihcnysasgypalfwyvqypgegpqflfrasrdkekgssrg
featynkeatsfhlqkasvqesdsavyycalsggnnkltfgagtkltikp
>d1ac6b_ 2.1.1.1.120 T-cell antigen receptor {human (Homo sapiens), alpha-chain}
dsvtqtegqvalseedfltihcnysasgypalfwyvqypgegpqflfrasrdkekgssrg
featynkeatsfhlqkasvqesdsavyycalsggnnkltfgagtkltikp
>d1ac8__ 1.72.1.1.3 Cytochrome c peroxidase {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_ 2.35.1.2.7 (alpha, gamma-)chymotrypsin(ogen) {bovine (Bos taurus)}
cgvpaiqpvlsglsrivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgv
ttsdvvvagefdqgsssekiqklkiakvfknskynsltinnditllklstaasfsqtvsa
vclpsasddfaagttcvttgwgltrytnantpdrlqqaslpllsntnckkywgtkikdam
icagasgvsscmgdsggplvckkngawtlvgivswgsstcststpgvyarvtalvnwvqq
tlaan
>d1acbi_ 4.22.1.1.1 Eglin C {leech (Hirudo medicinalis)}
ksfpevvgktvdqareyftlhypqydvyflpegspvtldlrynrvrvfynpgtnvvnhvp
hvg
>d1acc__ 6.12.1.1.1 Anthrax protective antigen {Anthrax bacillus (Bacillus anthracis)}
sssqgllgyyfsdlnfqapmvvtssttgdlsipsselenipsenqyfqsaiwsgfikvkk
sdeytfatsadnhvtmwvddqevinkasnsnkirlekgrlyqikiqyqrenptekgldfk
lywtdsqnkkevissdnlqlpelkqkssnsrkkrstsagptvpdrdndgipdslevegyt
vdvknkrtflspwisnihekkgltkyksspekwstasdpysdfekvtgridknvspearh
plvaaypivhvdmeniilsknedqstqntdsetrtiskntstsrthtsevhgnaevhasf
fdiggsvsagfsnsnsstvaidhslslagertwaetmglntadtarlnaniryvntgtap
iynvlpttslvlgknqtlatikakenqlsqilapnnyypsknlapialnaqddfsstpit
mnynqflelektkqlrldtdqvygniatynfengrvrvdtgsnwsevlpqiqettariif
ngkdlnlverriaavnpsdplettkpdmtlkealkiafgfnepngnlqyqgkditefdfn
fdqqtsqniknqlaelnatniytvldkiklnakmnilirdkrfhydrnniavgadesvvk
eahrevinssteglllnidkdirkilsgyiveiedteglkevindrydmlnisslrqdgk
tfidfkkyndklplyisnpnykvnvyavtkentiinpsengdtstngikkilifskkgye
ig
>d1acd__ 2.45.1.2.3 Adipocyte lipid-binding protein, ALBP {mouse (Mus musculus)}
gdafvgtwklvssenfddymkevgvgfatrkdagmakpnmiisvngdlvtirsesthknt
eisfklgvefdeitaddrkvksiitldggalvqvqkwdgksttikrkrdgdklvvexvmk
gvtstrvyera
>d1acf__ 4.63.1.1.3 Profilin (actin-binding protein) {(Acanthamoeba castellanii)}
swqtyvdtnlvgtgavtqaailgldgntwatsagfavtpaqgttlagafnnadairaggf
dlagvhyvtlraddrsiygkkgssgvitvktskailvgvynekiqpgtaanvvekladyl
igqgf
>d1aci__ 1.4.4.1.1 Ribosomal protein L11, the C-terminal domain {(Bacillus stearothermophilus)}
mtfitktppaavllkkaagiesgsgepnrnkvatikrdkvreiaelkmpdlnaasieaam
rmiegtarsmgivved
>d1acj__ 3.56.1.1.1 Acetylcholinesterase {Electric ray (Torpedo californica)}
sellvntksgkvmgtrvpvlsshisaflgipfaeppvgnmrfrrpepkkpwsgvwnasty
pnncqqyvdeqfpgfsgsemwnpnremsedclylniwvpsprpksttvmvwiygggfysg
sstldvyngkylayteevvlvslsyrvgafgflalhgsqeapgnvglldqrmalqwvhdn
iqffggdpktvtifgesaggasvgmhilspgsrdlfrrailqsgspncpwasvsvaegrr
ravelgrnlncnlnsdeelihclrekkpqelidvewnvlpfdsifrfsfvpvidgeffpt
slesmlnsgnfkktqillgvnkdegsffllygapgfskdseskisredfmsgvklsvpha
ndlgldavtlqytdwmddnngiknrdglddivgdhnvicplmhfvnkytkfgngtylyff
nhrasnlvwpewmgvihgyeiefvfglplvkelnytaeeealsrrimhywatfaktgnpn
ephsqeskwplfttkeqkfidlntepmkvhqrlrvqmcvfwnqflpkllnat
>d1acl__ 3.56.1.1.1 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 4.34.2.1.1 (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 4.34.2.1.1 (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 3.5.2.1.2 (529-754) Aconitase, C-terminal domain {bovine (Bos taurus)}
vdvsptsqrlqllepfdkwdgkdledlqilikvkgkcttdhisaagpwlkfrghldnisn
nlligainsenrkansvrnavtqefgpvpdtaryykqhgirwvvigdenygegssrehsa
leprflggraiitksfarihetnlkkqgllpltfadpadynkihpvdkltiqglkdfapg
kpltciikhpngtqetillnhtfnetqiewfragsalnrmkelqqk
>d1aco_2 3.71.1.1.2 (2-528) Aconitase, first 3 domains {bovine (Bos taurus)}
rakvamshfepheyirydlleknidivrkrlnrpltlsekivyghlddpanqeiergkty
lrlrpdrvamqdataqmamlqfissglpkvavpstihcdhlieaqlggekdlrrakdinq
evynflatagakygvgfwrpgsgiihqiilenyaypgvlligtdshtpnggglggicigv
ggadavdvmagipwelkcpkvigvkltgslsgwtspkdvilkvagiltvkggtgaiveyh
gpgvdsisctgmaticnmgaeigattsvfpynhrmkkylsktgradianladefkdhlvp
dsgchydqlieinlselkphingpftpdlahpvaevgsvaekegwpldirvgligsctns
syedmgrsaavakqalahglkcksqftitpgseqiratierdgyaqvlrdvggivlanac
gpcigqwdrkdikkgekntivtsynrnftgrndanpethafvtspeivtalaiagtlkfn
petdfltgkdgkkfkleapdadelpraefdpgqdtyqhppkdssgqr
>d1acp__ 1.27.1.1.1 Acyl carrier protein {(Escherichia coli)}
stieervkkiigeqlgvkqeevtnnasfvedlgadsldtvelvmaleeefdteipdeeae
kittvqaaidyinghqa
>d1acva1 1.42.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {(Escherichia coli)}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1acva2 3.38.1.3.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) {(Escherichia coli)}
aqyedgkqyttlekpvagapqvleffsffcpscyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsek
>d1acvb1 1.42.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {(Escherichia coli)}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1acvb2 3.38.1.3.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) {(Escherichia coli)}
aqyedgkqyttlekpvagapqvleffsffcpscyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsek
>d1acw__ 7.3.6.2.11 Toxin analog P01 {(Androctonus mauretanicus mauretanicus)}
vscedcpehcstqkaqakcdndkcvcepi
>d1acx__ 2.1.6.1.3 Actinoxanthin {(Actinomyces globisporus), number 1131}
apafsvspasgasdgqsvsvsvaaagetyyiaqcapvggqdacnpatatsfttdasgaas
fsftvrksyagqtpsgtpvgsvdcatdacnlgagnsglnlghvaltfg
>d1acyh1 2.1.1.1.28 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab 59.1 (mouse), kappa L chain}
qvklqesgpavikpsqslsltcivsgfsitrtnycwhwirqapgkglewmgricyegsiy
yspsiksrstisrdtslnkffiqlisvtnedtamyycsrenhmyetyfdvwgqgttvtvs
>d1acyh2 2.1.1.2.36 (113-226) Immunoglobulin (constant domains of L and H chains) {Fab 59.1 (mouse), kappa L chain}
sakttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqs
dlytlsssvtvpssprpsetvtcnvahpasstkvdkkivpr
>d1acyl1 2.1.1.1.28 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab 59.1 (mouse), kappa L chain}
divmtqspaslvvslgqratiscrasesvdsygksfmhwyqqkpgqppkvliyiasnles
gvparfsgsgsrtdftltidpveaddaatyycqqnnedpptfgagtklemrr
>d1acyl2 2.1.1.2.36 (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 2.1.1.1.76 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab A5B7 (engineered human construct), kappa L chain}
qtvltqspsslsvsvgdrvtitcrasssvtyihwyqqkpglapksliyatsnlasgvpsr
fsgsgsgtdytftisslqpediatyycqhwsskpptfgqgtkvevkr
>d1ad0a2 2.1.1.2.79 (108-213) Immunoglobulin (constant domains of L and H chains) {Fab A5B7 (engineered human construct), kappa L chain}
tvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqds
kdstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1ad0b1 2.1.1.1.76 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab A5B7 (engineered human construct), kappa L chain}
evqllesggglvqpggslrlscatsgftftdyymnwvrqapgkglewlgfignkangytt
eysasvkgrftisrdkskstlylqmntlqaedsaiyyctrdrglrfyfdywgqgtlvtvs
s
>d1ad0b2 2.1.1.2.79 (114-211) Immunoglobulin (constant domains of L and H chains) {Fab A5B7 (engineered human construct), kappa L chain}
astkgpsvfplapcsrstsestaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtktytcnvdhkpsntkvdkrve
>d1ad0c1 2.1.1.1.76 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab A5B7 (engineered human construct), kappa L chain}
qtvltqspsslsvsvgdrvtitcrasssvtyihwyqqkpglapksliyatsnlasgvpsr
fsgsgsgtdytftisslqpediatyycqhwsskpptfgqgtkvevkr
>d1ad0c2 2.1.1.2.79 (108-213) Immunoglobulin (constant domains of L and H chains) {Fab A5B7 (engineered human construct), kappa L chain}
tvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqds
kdstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1ad0d1 2.1.1.1.76 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab A5B7 (engineered human construct), kappa L chain}
evqllesggglvqpggslrlscatsgftftdyymnwvrqapgkglewlgfignkangytt
eysasvkgrftisrdkskstlylqmntlqaedsaiyyctrdrglrfyfdywgqgtlvtvs
s
>d1ad0d2 2.1.1.2.79 (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_ 3.70.1.1.1 Aldehyde reductase (dehydrogenase) {rat (Rattus norvegicus)}
sisdtvkrareafnsgktrslqfriqqlealqrminenlksisgalasdlgknewtsyye
evahvleeldttikelpdwaedepvaktrqtqqddlyihseplgvvlvigawnypfnlti
qpmvgavaagnavilkpsevsghmadllatlipqymdqnlylvvkggvpettellkerfd
himytgstavgkivmaaaakhltpvtlelggkspcyvdkdcdldvacrriawgkfmnsgq
tcvapdyilcdpsiqnqiveklkkslkdfygedakqsrdygriindrhfqrvkglidnqk
vahggtwdqssryiaptilvdvdpqspvmqeeifgpvmpivcvrsleeaiqfinqrekpl
alyvfsnnekvikkmiaetssggvtandvivhitvptlpfggvgnsgmgayhgkksfetf
shrrsclvksllneeahkaryppspa
>d1ad3b_ 3.70.1.1.1 Aldehyde reductase (dehydrogenase) {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 2.24.2.1.10 (82-145) Hemapoetic cell kinase Hck {human (Homo sapiens)}
ediivvalydyeaihhedlsfqkgdqmvvleesgewwkarslatrkegyipsnyvarvds
let
>d1ad5a2 4.53.1.1.8 (146-248) Hemopoetic cell kinase Hck {human (Homo sapiens)}
eewffkgisrkdaerqllapgnmlgsfmirdsettkgsyslsvrdydprqgdtvkhykir
tldnggfyisprstfstlqelvdhykkgndglcqklsvpcmss
>d1ad5a3 5.1.1.2.1 (249-531) Haemopoetic cell kinase Hck {human (Homo sapiens)}
kpqkpwekdaweipreslklekklgagqfgevwmatynkhtkvavktmkpgsmsveafla
eanvmktlqhdklvklhavvtkepiyiitefmakgslldflksdegskqplpklidfsaq
iaegmafieqrnyihrdlraanilvsaslvckiadfglarvgakfpikwtapeainfgsf
tiksdvwsfgillmeivtygripypgmsnpeviralergyrmprpencpeelynimmrcw
knrpeerptfeyiqsvlddfytatesqxqqqp
>d1ad5b1 2.24.2.1.10 (82-145) Hemapoetic cell kinase Hck {human (Homo sapiens)}
ediivvalydyeaihhedlsfqkgdqmvvleesgewwkarslatrkegyipsnyvarvds
let
>d1ad5b2 4.53.1.1.8 (146-248) Hemopoetic cell kinase Hck {human (Homo sapiens)}
eewffkgisrkdaerqllapgnmlgsfmirdsettkgsyslsvrdydprqgdtvkhykir
tldnggfyisprstfstlqelvdhykkgndglcqklsvpcmss
>d1ad5b3 5.1.1.2.1 (249-531) Haemopoetic cell kinase Hck {human (Homo sapiens)}
kpqkpwekdaweipreslklekklgagqfgevwmatynkhtkvavktmkpgsmsveafla
eanvmktlqhdklvklhavvtkepiyiitefmakgslldflksdegskqplpklidfsaq
iaegmafieqrnyihrdlraanilvsaslvckiadfglarvgakfpikwtapeainfgsf
tiksdvwsfgillmeivtygripypgmsnpeviralergyrmprpencpeelynimmrcw
knrpeerptfeyiqsvlddfytatesqxqqqp
>e1ad8.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqf
>e1ad8.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
eadcglrplfekksledkterellesyi
>d1ad9a1 2.1.1.1.94 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab CTM01 (human consruct), kappa L chain}
diqmtqspstlsasvgdrvtitcrssksllhsngdtflywfqqkpgkapkllmyrmsnla
sgvpsrfsgsgsgteftltisslqpddfatyycmqhleypftfgqgtkvevkr
>d1ad9a2 2.1.1.2.94 (108-213) Immunoglobulin (constant domains of L and H chains) {Fab CTM01 (human construct), kappa L chain}
tvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqds
kdstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1ad9b1 2.1.1.1.94 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab CTM01 (human consruct), kappa L chain}
eiqlvqsgaevkkpgssvkvsckasgytftdyyinwmrqapgqglewigwidpgsgntky
nekfkgratltvdtstntaymelsslrsedtafyfcarekttyyyamdywgqgtlvtvss
>d1ad9b2 2.1.1.2.94 (114-212) Immunoglobulin (constant domains of L and H chains) {Fab CTM01 (human construct), kappa L chain}
astkgpsvfplapcsrstsestaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtktytcnvdhkpsntkvdkrve
>d1ad9h1 2.1.1.1.94 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab CTM01 (human consruct), kappa L chain}
eiqlvqsgaevkkpgssvkvsckasgytftdyyinwmrqapgqglewigwidpgsgntky
nekfkgratltvdtstntaymelsslrsedtafyfcarekttyyyamdywgqgtlvtvss
>d1ad9h2 2.1.1.2.94 (114-212) Immunoglobulin (constant domains of L and H chains) {Fab CTM01 (human construct), kappa L chain}
astkgpsvfplapcsrstsestaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtktytcnvdhkpsntkvdkrve
>d1ad9l1 2.1.1.1.94 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab CTM01 (human consruct), kappa L chain}
diqmtqspstlsasvgdrvtitcrssksllhsngdtflywfqqkpgkapkllmyrmsnla
sgvpsrfsgsgsgteftltisslqpddfatyycmqhleypftfgqgtkvevkr
>d1ad9l2 2.1.1.2.94 (108-213) Immunoglobulin (constant domains of L and H chains) {Fab CTM01 (human construct), kappa L chain}
tvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqds
kdstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1adba1 2.25.1.2.1 (1-174,325-374) Alcohol dehydrogenase {horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1adba2 3.22.1.1.1 (175-324) Alcohol dehydrogenase {horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1adbb1 2.25.1.2.1 (1-174,325-374) Alcohol dehydrogenase {horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1adbb2 3.22.1.1.1 (175-324) Alcohol dehydrogenase {horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1adca1 2.25.1.2.1 (1-174,325-374) Alcohol dehydrogenase {horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1adca2 3.22.1.1.1 (175-324) Alcohol dehydrogenase {horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1adcb1 2.25.1.2.1 (1-174,325-374) Alcohol dehydrogenase {horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1adcb2 3.22.1.1.1 (175-324) Alcohol dehydrogenase {horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1add__ 3.1.2.1.1 Adenosine deaminase {mouse (Mus musculus)}
tpafnkpkvelhvhldgaikpetilyfgkkrgialpadtveelrniigmdkplslpgfla
kfdyympviagcreaikriayefvemkakegvvyvevrysphllanskvdpmpwnqtegd
vtpddvvdlvnqglqegeqafgikvrsilccmrhqpswslevlelckkynqktvvamdla
gdetiegsslfpghveayegavkngihrtvhagevgspevvreavdilktervghgyhti
edealynrllkenmhfevcpwssyltgawdpktthavvrfkndkanyslntddplifkst
ldtdyqmtkkdmgfteeefkrlninaakssflpeeekkellerlyreyq
>d1adea_ 3.29.1.6.2 Adenylosuccinate synthetase (gene purA product) {(Escherichia coli)}
gnnvvvlgtqwgdegkgkivdllterakyvvryqgghnaghtlvingektvlhlipsgil
renvtsiigngvvlspaalmkemkeledrgipvrerlllseacplildyhvaldnareka
rgakaigttgrgigpayedkvarrglrvgdlfdketfaeklkevmeyhnfqlvnyykaea
vdyqkvlddtmavadiltsmvvdvsdlldqarqrgdfvmfegaqgtlldidhgtypyvts
snttaggvatgsglgpryvdyvlgilkaystrvgagpfptelfdetgeflckqgnefgat
tgrrrrtgwldtvavrravqlnslsgfcltkldvldglkevklcvayrmpdgrevtttpl
aaddwkgvepiyetmpgwsestfgvkdrsglpqaalnyikrieeltgvpidiistgpdrt
etmilrdpfda
>d1adeb_ 3.29.1.6.2 Adenylosuccinate synthetase (gene purA product) {(Escherichia coli)}
gnnvvvlgtqwgdegkgkivdllterakyvvryqgghnaghtlvingektvlhlipsgil
renvtsiigngvvlspaalmkemkeledrgipvrerlllseacplildyhvaldnareka
rgakaigttgrgigpayedkvarrglrvgdlfdketfaeklkevmeyhnfqlvnyykaea
vdyqkvlddtmavadiltsmvvdvsdlldqarqrgdfvmfegaqgtlldidhgtypyvts
snttaggvatgsglgpryvdyvlgilkaystrvgagpfptelfdetgeflckqgnefgat
tgrrrrtgwldtvavrravqlnslsgfcltkldvldglkevklcvayrmpdgrevtttpl
aaddwkgvepiyetmpgwsestfgvkdrsglpqaalnyikrieeltgvpidiistgpdrt
etmilrdpfda
>d1adf_1 2.25.1.2.1 (1-174,325-374) Alcohol dehydrogenase {horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1adf_2 3.22.1.1.1 (175-324) Alcohol dehydrogenase {horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1adg_1 2.25.1.2.1 (1-174,325-374) Alcohol dehydrogenase {horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1adg_2 3.22.1.1.1 (175-324) Alcohol dehydrogenase {horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1adia_ 3.29.1.6.2 Adenylosuccinate synthetase (gene purA product) {(Escherichia coli)}
gnnvvvlgtqwgdegkgkivdllterakyvvryqgghnaghtlvingektvlhlipsgil
renvtsiigngvvlspaalmkemkeledrgipvrerlllseacplildyhvaldnareka
rgakaigttgrgigpayedkvarrglrvgdlfdketfaeklkevmeyhnfqlvnyykaea
vdyqkvlddtmavadiltsmvvdvsdlldqarqrgdfvmfegaqgtlldidhgtypyvts
snttaggvatgsglgpryvdyvlgilkaystrvgagpfptelfdetgeflckqgnefgat
tgrrrrtgwldtvavrravqlnslsgfcltkldvldglkevklcvayrmpdgrevtttpl
aaddwkgvepiyetmpgwsestfgvkdrsglpqaalnyikrieeltgvpidiistgpdrt
etmilrdpfda
>d1adib_ 3.29.1.6.2 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 4.61.1.1.4 (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 4.61.1.1.4 (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 4.61.1.1.4 (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 4.61.1.1.4 (2-325) Histidyl-tRNA synthetase (HisRS) {(Thermus thermophilus)}
taravrgtkdlfgkelrmhqrivatarkvleaagalelvtpifeetqvfekgvgaatdiv
rkemftfqdrggrsltlrpegtaamvraylehgmkvwpqpvrlwmagpmfraerpqkgry
rqfhqvnyealgsenpildaeavvllyeclkelglrrlkvklssvgdpedrarynaylre
vlsphrealsedskerleenpmrildskserdqallkelgvrpmldflgeearahlkeve
rhlerlsvpyelepalvrgldyyvrtafevhheeigaqsalggggrydglsellggprvp
gvgfafgvervalaleaegfglpe
>d1adl__ 2.45.1.2.3 Adipocyte lipid-binding protein, ALBP {mouse (Mus musculus)}
cdafvgtwklvssenfddymkevgvgfatrkvagmakpnmiisvngdlvtirsestfknt
eisfklgvefdeitaddrkvksiitldggalvqvqkwdgksttikrkrdgdklvvecvmk
gvtstrvyera
>d1adn__ 7.39.1.1.1 Ada DNA repair protein, N-terminal domain (N-Ada 10) {(Escherichia coli)}
mkkatcltddqrwqsvlardpnadgefvfavrttgifcrpscrarhalrenvsfyanase
alaagfrpckrcqpdkanprqhrldkithacr
>d1adoa_ 3.1.3.1.5 Fructose-1,6-bisphosphate aldolase {Rabbit (Oryctolagus cuniculus)}
phshpaltpeqkkelsdiahrivapgkgilaadestgsiakrlqsigtenteenrrfyrq
llltaddrvnpciggvilfhetlyqkaddgrpfpqvikskggvvgikvdkgvvplagtng
etttqgldglsercaqykkdgadfakwrcvlkigehtpsalaimenanvlaryasicqqn
givpivepeilpdgdhdlkrcqyvtekvlaavykalsdhhiylegtllkpnmvtpghact
qkysheeiamatvtalrrtvppavtgvtflsggqseeeasinlnainkcpllkpwaltfs
ygralqasalkawggkkenlkaaqeeyvkralanslacqgkytssgqagaaaseslfisn
hay
>d1adob_ 3.1.3.1.5 Fructose-1,6-bisphosphate aldolase {Rabbit (Oryctolagus cuniculus)}
phshpaltpeqkkelsdiahrivapgkgilaadestgsiakrlqsigtenteenrrfyrq
llltaddrvnpciggvilfhetlyqkaddgrpfpqvikskggvvgikvdkgvvplagtng
etttqgldglsercaqykkdgadfakwrcvlkigehtpsalaimenanvlaryasicqqn
givpivepeilpdgdhdlkrcqyvtekvlaavykalsdhhiylegtllkpnmvtpghact
qkysheeiamatvtalrrtvppavtgvtflsggqseeeasinlnainkcpllkpwaltfs
ygralqasalkawggkkenlkaaqeeyvkralanslacqgkytssgqagaaaseslfisn
hay
>d1adoc_ 3.1.3.1.5 Fructose-1,6-bisphosphate aldolase {Rabbit (Oryctolagus cuniculus)}
phshpaltpeqkkelsdiahrivapgkgilaadestgsiakrlqsigtenteenrrfyrq
llltaddrvnpciggvilfhetlyqkaddgrpfpqvikskggvvgikvdkgvvplagtng
etttqgldglsercaqykkdgadfakwrcvlkigehtpsalaimenanvlaryasicqqn
givpivepeilpdgdhdlkrcqyvtekvlaavykalsdhhiylegtllkpnmvtpghact
qkysheeiamatvtalrrtvppavtgvtflsggqseeeasinlnainkcpllkpwaltfs
ygralqasalkawggkkenlkaaqeeyvkralanslacqgkytssgqagaaaseslfisn
hay
>d1adod_ 3.1.3.1.5 Fructose-1,6-bisphosphate aldolase {Rabbit (Oryctolagus cuniculus)}
phshpaltpeqkkelsdiahrivapgkgilaadestgsiakrlqsigtenteenrrfyrq
llltaddrvnpciggvilfhetlyqkaddgrpfpqvikskggvvgikvdkgvvplagtng
etttqgldglsercaqykkdgadfakwrcvlkigehtpsalaimenanvlaryasicqqn
givpivepeilpdgdhdlkrcqyvtekvlaavykalsdhhiylegtllkpnmvtpghact
qkysheeiamatvtalrrtvppavtgvtflsggqseeeasinlnainkcpllkpwaltfs
ygralqasalkawggkkenlkaaqeeyvkralanslacqgkytssgqagaaaseslfisn
hay
>d1adr__ 1.32.1.2.4 p22 C2 repressor, DNA-binding domain {(Salmonella )bacteriophage P22}
mntqlmgerirarrkklkirqaalgkmvgvsnvaisqwersetepngenllalskalqcs
pdyllkgdlsqtnvay
>d1ads__ 3.1.5.1.2 Aldose reductase (aldehyde reductase) {human (Homo sapiens)}
asrlllnngakmpilglgtwksppgqvteavkvaidvgyrhidcahvyqnenevgvaiqe
klreqvvkreelfivsklwctyhekglvkgacqktlsdlkldyldlylihwptgfkpgke
ffpldesgnvvpsdtnildtwaameelvdeglvkaigisnfnhlqvemilnkpglkykpa
vnqiechpyltqekliqycqskgivvtaysplgspdrpwakpedpslledprikaiaakh
nkttaqvlirfpmqrnlvvipksvtperiaenfkvfdfelssqdmttllsynrnwrvcal
lsctshkdypfheef
>d1adt_1 1.50.1.1.1 (176-265) A domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
pivsawekgmeaaralmdkyhvdndlkanfkllpdqvealaavcktwlneehrglqltft
snktfvtmmgrflqaylqsfaevtykhhep
>d1adt_2 7.41.1.1.1 (266-385) The first Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
tgcalwlhrcaeiegelkclhgsiminkehviemdvtsengqralkeqsskakivknrwg
rnvvqisntdarccvhdaacpanqfsgkscgmffsegakaqvafkqikafmqalypnaqt
>d1adt_3 7.41.1.1.2 (386-529) The second Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
ghghllmplrcecnskpghapflgrqlpkltpfalsnaedldadlisdksvlasvhhpal
ivfqccnpvyrnsraqgggpncdfkisapdllnalvmvrslwsenftelprmvvpqfkws
tkhqyrnvslpvahsdarqnpfdf
>d1adua1 1.50.1.1.1 (180-265) A domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
awekgmeaaralmdkyhvdndlkanfkllpdqvealaavcktwlneehrglqltftsnkt
fvtmmgrflqaylqsfaevtykhhep
>d1adua2 7.41.1.1.1 (266-385) The first Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
tgcalwlhrcaeiegelkclhgsiminkehviemdvtsengqralkeqsskakivknrwg
rnvvqisntdarccvhdaacpanqfsgkscgmffsegakaqvafkqikafmqalypnaqt
>d1adua3 7.41.1.1.2 (386-529) The second Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
ghghllmplrcecnskpghapflgrqlpkltpfalsnaedldadlisdksvlasvhhpal
ivfqccnpvyrnsraqgggpncdfkisapdllnalvmvrslwsenftelprmvvpefkws
tkhqyrnvslpvahsdarqnpfdf
>d1adub1 1.50.1.1.1 (180-265) A domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
awekgmeaaralmdkyhvdndlkanfkllpdqvealaavcktwlneehrglqltftsnkt
fvtmmgrflqaylqsfaevtykhhep
>d1adub2 7.41.1.1.1 (266-385) The first Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
tgcalwlhrcaeiegelkclhgsiminkehviemdvtsengqralkeqsskakivknrwg
rnvvqisntdarccvhdaacpanqfsgkscgmffsegakaqvafkqikafmqalypnaqt
>d1adub3 7.41.1.1.2 (386-529) The second Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
ghghllmplrcecnskpghapflgrqlpkltpfalsnaedldadlisdksvlasvhhpal
ivfqccnpvyrnsraqgggpncdfkisapdllnalvmvrslwsenftelprmvvpefkws
tkhqyrnvslpvahsdarqnpfdf
>d1adva1 1.50.1.1.1 (180-265) A domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
awekgmeaaralmdkyhvdndlkanfkllpdqvealaavcktwlneehrglqltftsnkt
fvtmmgrflqaylqsfaevtykhhep
>d1adva2 7.41.1.1.1 (266-385) The first Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
tgcalwlhrcaeiegelkclhgsiminkehviemdvtsengqralkeqsskakivknrwg
rnvvqisntdarccvhdaacpanqfsgkscgmffsegakaqvafkqikafmqalypnaqt
>d1adva3 7.41.1.1.2 (386-529) The second Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
ghghllmplrcecnskpghapflgrqlpkltpfalsnaedldadlisdksvlasvhhpal
ivfqccnpvyrnsraqgggpncdfkisapdllnalvmvrslwsenftelprmvvpefkws
tkhqyrnvslpvahsdarqnpfdf
>d1advb1 1.50.1.1.1 (180-265) A domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
awekgmeaaralmdkyhvdndlkanfkllpdqvealaavcktwlneehrglqltftsnkt
fvtmmgrflqaylqsfaevtykhhep
>d1advb2 7.41.1.1.1 (266-385) The first Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
tgcalwlhrcaeiegelkclhgsiminkehviemdvtsengqralkeqsskakivknrwg
rnvvqisntdarccvhdaacpanqfsgkscgmffsegakaqvafkqikafmqalypnaqt
>d1advb3 7.41.1.1.2 (386-529) The second Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
ghghllmplrcecnskpghapflgrqlpkltpfalsnaedldadlisdksvlasvhhpal
ivfqccnpvyrnsraqgggpncdfkisapdllnalvmvrslwsenftelprmvvpefkws
tkhqyrnvslpvahsdarqnpfdf
>d1adwa_ 2.5.1.1.13 Pseudoazurin {(Thiosphaera pantotropha)}
athevhmlnkgesgamvfepafvraepgdvinfvptdkshnveaikeilpegvesfkski
nesytltvtepglygvkctphfgmgmvglvqvgdapenldaaktakmpkkarermdaela
qvn
>d1adwb_ 2.5.1.1.13 Pseudoazurin {(Thiosphaera pantotropha)}
athevhmlnkgesgamvfepafvraepgdvinfvptdkshnveaikeilpegvesfkski
nesytltvtepglygvkctphfgmgmvglvqvgdapenldaaktakmpkkarermdaela
qvn
>d1adx__ 7.3.9.1.16 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 4.61.1.1.4 (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 4.61.1.1.4 (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 4.61.1.1.4 (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 4.61.1.1.4 (2-325) Histidyl-tRNA synthetase (HisRS) {(Thermus thermophilus)}
taravrgtkdlfgkelrmhqrivatarkvleaagalelvtpifeetqvfekgvgaatdiv
rkemftfqdrggrsltlrpegtaamvraylehgmkvwpqpvrlwmagpmfraerpqkgry
rqfhqvnyealgsenpildaeavvllyeclkelglrrlkvklssvgdpedrarynaylre
vlsphrealsedskerleenpmrildskserdqallkelgvrpmldflgeearahlkeve
rhlerlsvpyelepalvrgldyyvrtafevhheeigaqsalggggrydglsellggprvp
gvgfafgvervalaleaegfglpe
>d1adz__ 7.7.1.1.3 Tissue factor pathway inhibitor {Human (Homo sapiens)}
dykddddklkpdfcfleedpgicrgyitryfynnqtkqcerfkyggclgnmnnfetleec
knicedgpngf
>d1ae2__ 2.29.4.8.1 Gene V protein {(Bacteriophage f1)}
mikveikpsqaqfttrsgvsrqgkpyslneqrcyvdlgneypvlvkitldegqpayapgl
ytvhlssfkvgqfgslmidrlrlvpa
>d1ae3__ 2.29.4.8.1 Gene V protein {(Bacteriophage f1)}
mikveikpsqaqfttrsgvsrqgkpyslneqlcyvdlgneypvlvkitldegqpayapgl
ytvhlssfkvgqfgslmidrlclvpa
>d1ae4__ 3.1.5.1.4 Aldose reductase (aldehyde reductase) {porcine (Sus scrofa)}
aascvllhtgqkmpliglgtwksepgqvkaaikyaltvgyrhidcaaiygneleigealt
etvgpgkavpreelfvtsklwntkhhpedvepalrktladlqleyldlylmhwpyaferg
dnpfpknadgtirydathykdtwkalealvakglvralglsnfssrqiddvlsvasvrpa
vlqvechpylaqneliahcqarglevtaysplgssdrawrdpnepvlleepvvqalaeky
nrspaqillrwqvqrkvicipksvtpsripqniqvfdftfspeemkqldalnknlrfivp
mltvdgkrvprdaghplypfndpy
>d1ae5__ 2.35.1.2.16 Heparin binding protein, HBP {Human (Homo sapiens)}
ivggrkarprqfpflasiqnqgrhfcggaliharfvmtaascfqsqnpgvstvvlgaydl
rrrerqsrqtfsissmsengydpqqnlndlmllqldreanltssvtilplplqnatveag
trcqvagwgsqrsggrlsrfprfvnvtvtpedqcrpnnvctgvltrrggicngdggtplv
ceglahgvasfslgpcgrgpdfftrvalfrdwidgvlnnpgpgpa
>d1ae6h1 2.1.1.1.93 (1-114) Immunoglobulin (variable domains of L and H chains) {Fab CTM01 (mouse), kappa L chain}
qiqlqqsgpelvkpgasvkisckasgytftdyyinwmkqkpgqglewigwidpgsgntky
nekfkgkatltvdtssstaymqlssltsedtavyfcarekttyyyamdywgqgtsvtvsa
a
>d1ae6h2 2.1.1.2.93 (115-211) Immunoglobulin (constant domains of L and H chains) {Fab CTM01 (mouse), kappa L chain}
kttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsdl
ytlsssvtvpssprpsetvtcnvahpasstkvdkkiv
>d1ae6l1 2.1.1.1.93 (1-106) Immunoglobulin (variable domains of L and H chains) {Fab CTM01 (mouse), kappa L chain}
divmtqaapsvpvtpgeslsiscrssksllhsngdtflywflqrpgqspqlliyrmsnla
sgvpdrfsgsgsgtaftlrvsrveaedvgvyycmqhleypftfgagtklel
>d1ae6l2 2.1.1.2.93 (107-213) Immunoglobulin (constant domains of L and H chains) {Fab CTM01 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1ae7__ 1.103.1.2.6 Snake phospholipase A2 {mainland tiger snake (Notechis scutatus scutatus) notexin}
nlvqfsyliqcanhgkrptwhymdygcycgaggsgtpvdeldrcckihddcydeagkkgc
fpkmsaydyycgengpycrnikkkclrfvcdcdveaafcfakapynnanwnidtkkrcq
>e1ae8.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>e1ae8.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>d1ae9a_ 4.101.1.1.2 Integrase (Int) {(Bacteriophage lambda)}
rsrltadeylkiyqaaesspcwlrlamelavvtgqrvgdlcemkwsdivdgylyveqskt
gvkiaiptalhidalgismketldkckeilggetiiastrreplssgtvsryfmrarkas
glsfegdpptfhelrslsarlyekqisdkfaqhllghksdtmasqfrddrgrewdkiei
>d1ae9b_ 4.101.1.1.2 Integrase (Int) {(Bacteriophage lambda)}
rsrltadeylkiyqaaesspcwlrlamelavvtgqrvgdlcemkwsdivdgylyveqskt
gvkiaiptalhidalgismketldkckeilggetiiastrreplssgtvsryfmrarkas
glsfegdpptfhelrslsarlyekqisdkfaqhllghksdtmasqfrddrgrewdkiei
>d1aeb__ 1.72.1.1.3 Cytochrome c peroxidase {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__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aee__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aef__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aeg__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aeh__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aeia_ 1.55.1.1.8 Annexin XII {hydra (Hydra attenuata)}
vvqgtvkphasfnsredaetlrkamkgigtdeksithilatrsnaqrqqiktdyttlfgk
hledelkselsgnyeaaalallrkpdeflaeqlhaamkglgtdenalidilctqsnaqih
aikaafkllykedlekeiisetsgnfqrllvsmlqggrkedepvnaahaaedaaaiyqag
egqigtdesrfnavlatrsypqlhqifheyskisnktilqaienefsgdikngllaivks
venrfayfaerlhhamkglgtsdktlirilvsrseidlaniketfqamygkslyefiadd
csgdykdlllqitgh
>d1aeib_ 1.55.1.1.8 Annexin XII {hydra (Hydra attenuata)}
vvqgtvkphasfnsredaetlrkamkgigtdeksithilatrsnaqrqqiktdyttlfgk
hledelkselsgnyeaaalallrkpdeflaeqlhaamkglgtdenalidilctqsnaqih
aikaafkllykedlekeiisetsgnfqrllvsmlqggrkedepvnaahaaedaaaiyqag
egqigtdesrfnavlatrsypqlhqifheyskisnktilqaienefsgdikngllaivks
venrfayfaerlhhamkglgtsdktlirilvsrseidlaniketfqamygkslyefiadd
csgdykdlllqitgh
>d1aeic_ 1.55.1.1.8 Annexin XII {hydra (Hydra attenuata)}
vvqgtvkphasfnsredaetlrkamkgigtdeksithilatrsnaqrqqiktdyttlfgk
hledelkselsgnyeaaalallrkpdeflaeqlhaamkglgtdenalidilctqsnaqih
aikaafkllykedlekeiisetsgnfqrllvsmlqggrkedepvnaahaaedaaaiyqag
egqigtdesrfnavlatrsypqlhqifheyskisnktilqaienefsgdikngllaivks
venrfayfaerlhhamkglgtsdktlirilvsrseidlaniketfqamygkslyefiadd
csgdykdlllqitgh
>d1aeid_ 1.55.1.1.8 Annexin XII {hydra (Hydra attenuata)}
vvqgtvkphasfnsredaetlrkamkgigtdeksithilatrsnaqrqqiktdyttlfgk
hledelkselsgnyeaaalallrkpdeflaeqlhaamkglgtdenalidilctqsnaqih
aikaafkllykedlekeiisetsgnfqrllvsmlqggrkedepvnaahaaedaaaiyqag
egqigtdesrfnavlatrsypqlhqifheyskisnktilqaienefsgdikngllaivks
venrfayfaerlhhamkglgtsdktlirilvsrseidlaniketfqamygkslyefiadd
csgdykdlllqitgh
>d1aeie_ 1.55.1.1.8 Annexin XII {hydra (Hydra attenuata)}
vvqgtvkphasfnsredaetlrkamkgigtdeksithilatrsnaqrqqiktdyttlfgk
hledelkselsgnyeaaalallrkpdeflaeqlhaamkglgtdenalidilctqsnaqih
aikaafkllykedlekeiisetsgnfqrllvsmlqggrkedepvnaahaaedaaaiyqag
egqigtdesrfnavlatrsypqlhqifheyskisnktilqaienefsgdikngllaivks
venrfayfaerlhhamkglgtsdktlirilvsrseidlaniketfqamygkslyefiadd
csgdykdlllqitgh
>d1aeif_ 1.55.1.1.8 Annexin XII {hydra (Hydra attenuata)}
vvqgtvkphasfnsredaetlrkamkgigtdeksithilatrsnaqrqqiktdyttlfgk
hledelkselsgnyeaaalallrkpdeflaeqlhaamkglgtdenalidilctqsnaqih
aikaafkllykedlekeiisetsgnfqrllvsmlqggrkedepvnaahaaedaaaiyqag
egqigtdesrfnavlatrsypqlhqifheyskisnktilqaienefsgdikngllaivks
venrfayfaerlhhamkglgtsdktlirilvsrseidlaniketfqamygkslyefiadd
csgdykdlllqitgh
>d1aej__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aek__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1ael__ 2.45.1.2.2 Intestinal fatty acid binding protein {rat (Rattus rattus)}
afdgtwkvdrnenyekfmekmginvvkrklgahdnlkltitqegnkftvkessnfrnidv
vfelgvdfaysladgteltgtwtmegnklvgkfkrvdngkeliavreisgneliqtytye
gveakrifkke
>d1aem__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aen__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aeo__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aep__ 1.53.1.1.1 Apolipophorin-III {african locust (Locusta migratoria)}
niaeavqqlnhtivnaahelhetlglptpdealnllteqanafktkiaevttslkqeaek
hqgsvaeqlnafarnlnnsihdaatslnlqdqlnslqsaltnvghqwqdiatktqasaqe
awapvqsalqeaaektkeaaanlqnsiqsavqk
>d1aeq__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aera_ 4.103.1.1.4 Exotoxin A, C-terminal domain {(Pseudomonas aeruginosa)}
aflgdggdvsfstrgtqnwtverllqahrqleergyvfvgyhgtfleaaqsivfggvraa
iwrgfyiagdpalaygyaqdqepdargrirngallrvyvprsslpgfyrtsltlaapeaa
geverlighplplrldaitgpeeeggrletilgwplaertvvipsaiptdprnvggdldp
ssipdkeqaisalpdyasqpgkppr
>d1aerb_ 4.103.1.1.4 Exotoxin A, C-terminal domain {(Pseudomonas aeruginosa)}
flgdggdvsfstrgtqnwtverllqahrqleergyvfvgyhgtfleaaqsivfggvrars
qdldaiwrgfyiagdpalaygyaqdqepdrgrirngallrvyvprsslpgfyrtsltlaa
peaageverlighplplrldaitgprletilgwplaertvvipsaiptdprnvggdldps
sipdkeqaisalpdy
>d1aes__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aet__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aeu__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aev__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aew__ 1.25.1.1.4 (Apo)ferritin {horse (Equus caballus), L chain}
sqirqnysteveaavnrlvnlylrasytylslgfyfdrddvalegvchffrelaeekreg
aerllkmqnqrggralfqdlqkpsqdewgttpdamkaaivlekslnqalldlhalgsaqa
dphlcdfleshfldeevklikkmgdhltniqrlvgsqaglgeylferltl
>d1aex__ 2.29.1.1.1 Staphylococcal nuclease {(Staphylococcal aureus)}
lhkepatlikaidgdtxklmykgqpmtfrlllvdtpetkhpkkgvekygpeasaftkkmv
enakkievefdkgqrtdkygrglayiyadgkmvnealvrqglakvayvykpnntheqhlr
kseaqakkeklniws
>d1aey__ 2.24.2.1.8 alpha-Spectrin, SH3 domain {chicken (Gallus gallus)}
gkelvlalydyqeksprevtmkkgdiltllnstnkdwwkvevndrqgfvpaayvkkld
>d1af0a1 2.61.1.1.2 (247-471) Metalloprotease, C-terminal domain {(Serratia marcescens)}
ganlstrtgdtvygfnsntgrdflsttsnsqkvifaawdaggndtfdfsgytanqrinln
eksfsdvgglkgnvsiaagvtienaiggsgndvivgnaannvlkggagndvlfggggade
lwggagkdifvfsaasdsapgasdwirdfqkgidkidlsffdkeansssfihfvdhfsgt
ageallsynassnvtdlsvnigghqapdflvkivgqvdvatdfiv
>d1af0a2 4.52.1.6.2 (4-239) Metallo protease, catalytic (N-terminal) domain {(Serratia marcescens)}
tgydavddllhyhergngiqingkdsfsneqaglfitrenqtwngykvfgqpvkltfsfp
dykfsstnvagdtglskfsaeqqqqaklslqswadvanitftevaagqkanitfgnysqd
rpghydygtqayaflpntiwqgqdlggqtwynvnqsnvkhpatedygrqtftheighalg
lshpgdynagegdptyndvtyaedtrqfslmsywsetntggdngghyaaapllddi
>d1af2a1 3.84.1.1.1 (1-150) Cytidine deaminase {(Escherichia coli)}
mhprfqtafaqladnlqsalepiladkyfpalltgeqvsslksatgldedalafallpla
aacartplsnfnvgaiargvsgtwyfganmefigatmqqtvhaeqsaishawlsgekala
aitvnytpcghcrqfmnelnsgldlrihlp
>d1af2a2 3.84.1.1.1 (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__ 4.55.2.1.1 DNA endonuclease I-CreI {(Chlamydomonas reinhardtii)}
kynkefllylagfvdgdgsiiaqikpnqsykfkhqlsltfqvtqktqrrwflgklvdeig
vgyvrdrgsvsdyilseikplhnfltqlqpflklkqkqanlvlkiieqlplevctwvdqi
aalnds
>d1af6a_ 6.7.1.2.1 Maltoporin (also LamB protein) {(Escherichia coli)}
vdfhgyarsgigwtgsggeqqcfqttgaqskyrlgnecetyaelklgqevwkegdksfyf
dtnvaysvaqqndweatdpafreanvqgknliewlpgstiwagkrfyqrhdvhmidfyyw
disgpgaglenidvgfgklslaatrsseaggsssfasnniydytnetandvfdvrlaqme
inpggtlelgvdygranlrdnyrlvdgaskdgwlftaehtqsvlkgfnkfvvqyatdsmt
sqgkglsqgsgvafdnekfayninnnghmlrildhgaismgdnwdmmyvgmyqdinwdnd
ngtkwwtvgirpmykwtpimstvmeigydnvesqrtgdknnqykitlaqqwqagdsiwsr
pairvfatyakwdekwgydytgnadnnanfgkavpadfnggsfgrgdsdewtfgaqmeiw
w
>d1af6b_ 6.7.1.2.1 Maltoporin (also LamB protein) {(Escherichia coli)}
vdfhgyarsgigwtgsggeqqcfqttgaqskyrlgnecetyaelklgqevwkegdksfyf
dtnvaysvaqqndweatdpafreanvqgknliewlpgstiwagkrfyqrhdvhmidfyyw
disgpgaglenidvgfgklslaatrsseaggsssfasnniydytnetandvfdvrlaqme
inpggtlelgvdygranlrdnyrlvdgaskdgwlftaehtqsvlkgfnkfvvqyatdsmt
sqgkglsqgsgvafdnekfayninnnghmlrildhgaismgdnwdmmyvgmyqdinwdnd
ngtkwwtvgirpmykwtpimstvmeigydnvesqrtgdknnqykitlaqqwqagdsiwsr
pairvfatyakwdekwgydytgnadnnanfgkavpadfnggsfgrgdsdewtfgaqmeiw
w
>d1af6c_ 6.7.1.2.1 Maltoporin (also LamB protein) {(Escherichia coli)}
vdfhgyarsgigwtgsggeqqcfqttgaqskyrlgnecetyaelklgqevwkegdksfyf
dtnvaysvaqqndweatdpafreanvqgknliewlpgstiwagkrfyqrhdvhmidfyyw
disgpgaglenidvgfgklslaatrsseaggsssfasnniydytnetandvfdvrlaqme
inpggtlelgvdygranlrdnyrlvdgaskdgwlftaehtqsvlkgfnkfvvqyatdsmt
sqgkglsqgsgvafdnekfayninnnghmlrildhgaismgdnwdmmyvgmyqdinwdnd
ngtkwwtvgirpmykwtpimstvmeigydnvesqrtgdknnqykitlaqqwqagdsiwsr
pairvfatyakwdekwgydytgnadnnanfgkavpadfnggsfgrgdsdewtfgaqmeiw
w
>d1af7__ 3.53.1.3.1 Chemotaxis receptor methyltransferase CheR {(Salmonella typhimurium)}
svllqmtqrlalsdahfrricqliyqragivladhkrdmvynrlvrrlralglddfgryl
smleanqnsaewqafinalttnltaffreahhfpilaeharrrhgeyrvwsaaastgeep
ysiaitladalgmapgrwkvfasdidtevlekarsgiyrlselktlspqqlqryfmrgtg
pheglvrvrqelanyvefssvnllekqynvpgpfdaifcrnvmiyfdkttqedilrrfvp
llkpdgllfaghsenfsnlvrefslrgqtvyals
>d1af8__ 1.27.1.1.2 Actinorhodin polyketide synthase acyl carrier protein, ACT ACP {(Streptomyces coelicolor) A3(2)}
matllttddlrralvecagetdgtdlsgdfldlrfedigydslalmetaarlesrygvsi
pddvagrvdtprelldlingalaeaa
>d1af9_1 2.21.1.5.1 (875-1110) Tetanus neurotoxin, the second last domain {(Clostridium tetani)}
edidvilkkstilnldinndiisdisgfnssvitypdaqlvpgingkaihlvnnessevi
vhkamdieyndmfnnftvsfwlrvpkvsashleqygtneysiissmkkhslsigsgwsvs
lkgnnliwtlkdsagevrqitfrdlpdkfnaylankwvfititndrlssanlyingvlmg
saeitglgairednnitlkldrcnnnnqyvsidkfrifckalnpkeieklytsyls
>d1af9_2 2.31.4.2.1 (1111-1315) Tetanus neurotoxin, C-terminal domain {(Clostridium tetani)}
itflrdfwgnplrydteyylipvassskdvqlknitdymyltnapsytngklniyyrrly
nglkfiikrytpnneidsfvksgdfiklyvsynnnehivgypkdgnafnnldrilrvgyn
apgiplykkmeavklrdlktysvqlklyddknaslglvgthngqigndpnrdiliasnwy
fnhlkdkilgcdwyfvptdegwtnd
>d1afa11 1.105.1.1.1 (73-104) Mannose-binding protein A {rat (Rattus rattus)}
aievklanmeaeintlkskleltnklhafsmg
>d1afa12 4.105.1.1.5 (105-226) Mannose-binding protein A, lectin domain {rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvtivdnglwndiscqashtavcef
pa
>d1afa21 1.105.1.1.1 (73-104) Mannose-binding protein A {rat (Rattus rattus)}
aievklanmeaeintlkskleltnklhafsmg
>d1afa22 4.105.1.1.5 (105-226) Mannose-binding protein A, lectin domain {rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvtivdnglwndiscqashtavcef
pa
>d1afa31 1.105.1.1.1 (73-104) Mannose-binding protein A {rat (Rattus rattus)}
aievklanmeaeintlkskleltnklhafsmg
>d1afa32 4.105.1.1.5 (105-226) Mannose-binding protein A, lectin domain {rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvtivdnglwndiscqashtavcef
pa
>d1afb11 1.105.1.1.1 (73-104) Mannose-binding protein A {rat (Rattus rattus)}
aievklanmeaeintlkskleltnklhafsmg
>d1afb12 4.105.1.1.5 (105-221) Mannose-binding protein A, lectin domain {rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvtivdnglwndiscqashtav
>d1afb21 1.105.1.1.1 (73-104) Mannose-binding protein A {rat (Rattus rattus)}
aievklanmeaeintlkskleltnklhafsmg
>d1afb22 4.105.1.1.5 (105-221) Mannose-binding protein A, lectin domain {rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvtivdnglwndiscqashtav
>d1afb31 1.105.1.1.1 (73-104) Mannose-binding protein A {rat (Rattus rattus)}
aievklanmeaeintlkskleltnklhafsmg
>d1afb32 4.105.1.1.5 (105-226) Mannose-binding protein A, lectin domain {rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvtivdnglwndiscqashtavcef
pa
>d1afca_ 2.31.1.1.2 Acidic FGF {bovine (Bos taurus)}
kpkllycsnggyflrilpdgtvdgtkdrsdqhiqlqlaaesigevyikstetgqflamdt
dgllygsqtpneeclflerleenhyntyiskkhaekhwfvglkkngrsklgprthfgqka
ilflplp
>d1afcb_ 2.31.1.1.2 Acidic FGF {bovine (Bos taurus)}
kpkllycsnggyflrilpdgtvdgtkdrsdqhiqlqlaaesigevyikstetgqflamdt
dgllygsqtpneeclflerleenhyntyiskkhaekhwfvglkkngrsklgprthfgqka
ilflplp
>d1afcc_ 2.31.1.1.2 Acidic FGF {bovine (Bos taurus)}
kpkllycsnggyflrilpdgtvdgtkdrsdqhiqlqlaaesigevyikstetgqflamdt
dgllygsqtpneeclflerleenhyntyiskkhaekhwfvglkkngrsklgprthfgqka
ilflplp
>d1afcd_ 2.31.1.1.2 Acidic FGF {bovine (Bos taurus)}
kpkllycsnggyflrilpdgtvdgtkdrsdqhiqlqlaaesigevyikstetgqflamdt
dgllygsqtpneeclflerleenhyntyiskkhaekhwfvglkkngrsklgprthfgqka
ilflplp
>d1afce_ 2.31.1.1.2 Acidic FGF {bovine (Bos taurus)}
kpkllycsnggyflrilpdgtvdgtkdrsdqhiqlqlaaesigevyikstetgqflamdt
dgllygsqtpneeclflerleenhyntyiskkhaekhwfvglkkngrsklgprthfgqka
ilflplp
>d1afcf_ 2.31.1.1.2 Acidic FGF {bovine (Bos taurus)}
kpkllycsnggyflrilpdgtvdgtkdrsdqhiqlqlaaesigevyikstetgqflamdt
dgllygsqtpneeclflerleenhyntyiskkhaekhwfvglkkngrsklgprthfgqka
ilflplp
>d1afcg_ 2.31.1.1.2 Acidic FGF {bovine (Bos taurus)}
kpkllycsnggyflrilpdgtvdgtkdrsdqhiqlqlaaesigevyikstetgqflamdt
dgllygsqtpneeclflerleenhyntyiskkhaekhwfvglkkngrsklgprthfgqka
ilflplp
>d1afch_ 2.31.1.1.2 Acidic FGF {bovine (Bos taurus)}
kpkllycsnggyflrilpdgtvdgtkdrsdqhiqlqlaaesigevyikstetgqflamdt
dgllygsqtpneeclflerleenhyntyiskkhaekhwfvglkkngrsklgprthfgqka
ilflplp
>d1afd11 1.105.1.1.1 (73-104) Mannose-binding protein A {rat (Rattus rattus)}
aievklanmeaeintlkskleltnklhafsmg
>d1afd12 4.105.1.1.5 (105-221) Mannose-binding protein A, lectin domain {rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvtivdnglwndiscqashtav
>d1afd21 1.105.1.1.1 (73-104) Mannose-binding protein A {rat (Rattus rattus)}
aievklanmeaeintlkskleltnklhafsmg
>d1afd22 4.105.1.1.5 (105-221) Mannose-binding protein A, lectin domain {rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvtivdnglwndiscqashtav
>d1afd31 1.105.1.1.1 (73-104) Mannose-binding protein A {rat (Rattus rattus)}
aievklanmeaeintlkskleltnklhafsmg
>d1afd32 4.105.1.1.5 (105-226) Mannose-binding protein A, lectin domain {rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvtivdnglwndiscqashtavcef
pa
>e1afe.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>e1afe.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>d1afh__ 1.47.1.1.4 plant non-specific lipid-transfer protein (ns-LTP) {maize (Zea mays)}
aiscgqvasaiapcisyargqgsgpsagccsgvrslnnaarttadrraacnclknaaagv
sglnagnaasipskcgvsipytiststdcsrvn
>d1afi__ 4.34.15.1.1 Mercuric ion binding protein MerP {(Shigella flexneri)}
atqtvtlavpgmtcaacpitvkkalskvegvskvdvgfekreavvtfddtkasvqkltka
tadagypssvkq
>d1afj__ 4.34.15.1.1 Mercuric ion binding protein MerP {(Shigella flexneri)}
atqtvtlavpgmtcaacpitvkkalskvegvskvdvgfekreavvtfddtkasvqkltka
tadagypssvkq
>d1afka_ 4.4.1.1.1 Ribonuclease A (also ribonuclease B, S) {bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1afkb_ 4.4.1.1.1 Ribonuclease A (also ribonuclease B, S) {bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1afla_ 4.4.1.1.1 Ribonuclease A (also ribonuclease B, S) {bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1aflb_ 4.4.1.1.1 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 2.35.1.2.7 (alpha, gamma-)chymotrypsin(ogen) {bovine (Bos taurus)}
ivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgvttsdvvvagefdqgs
ssekiqklkiakvfknskynsltinnditllklstaasfsqtvsavclpsasddfaagtt
cvttgwgltry
>e1afq.1c 2.35.1.2.7 (alpha, gamma-)chymotrypsin(ogen) {bovine (Bos taurus)}
ntpdrlqqaslpllsntnckkywgtkikdamicagasgvsscmgdsggplvckkngawtl
vgivswgsstcststpgvyarvtalvnwvqqtlaan
>d1afra_ 1.25.1.2.5 delta 9-stearoyl-acyl carrier protein desaturase {Castor bean (Ricinus communis)}
mpprevhvqvthsmppqkieifksldnwaeenilvhlkpvekcwqpqdflpdpasdgfde
qvrelrerakeipddyfvvlvgdmiteealptyqtmlntldgvrdetgasptswaiwtra
wtaeenrhgdllnkylylsgrvdmrqiektiqyligsgmdprtenspylgfiytsfqera
tfishgntarqakehgdiklaqicgtiaadekrhetaytkiveklfeidpdgtvlafadm
mrkkismpahlmydgrddnlfdhfsavaqrlgvytakdyadileflvgrwkvdkltglsa
egqkaqdyvcrlpprirrleeraqgrakeaptmpfswifdrqvkl
>d1afrb_ 1.25.1.2.5 delta 9-stearoyl-acyl carrier protein desaturase {Castor bean (Ricinus communis)}
mpprevhvqvthsmppqkieifksldnwaeenilvhlkpvekcwqpqdflpdpasdgfde
qvrelrerakeipddyfvvlvgdmiteealptyqtmlntldgvrdetgasptswaiwtra
wtaeenrhgdllnkylylsgrvdmrqiektiqyligsgmdprtenspylgfiytsfqera
tfishgntarqakehgdiklaqicgtiaadekrhetaytkiveklfeidpdgtvlafadm
mrkkismpahlmydgrddnlfdhfsavaqrlgvytakdyadileflvgrwkvdkltglsa
egqkaqdyvcrlpprirrleeraqgrakeaptmpfswifdrqvkl
>d1afrc_ 1.25.1.2.5 delta 9-stearoyl-acyl carrier protein desaturase {Castor bean (Ricinus communis)}
mpprevhvqvthsmppqkieifksldnwaeenilvhlkpvekcwqpqdflpdpasdgfde
qvrelrerakeipddyfvvlvgdmiteealptyqtmlntldgvrdetgasptswaiwtra
wtaeenrhgdllnkylylsgrvdmrqiektiqyligsgmdprtenspylgfiytsfqera
tfishgntarqakehgdiklaqicgtiaadekrhetaytkiveklfeidpdgtvlafadm
mrkkismpahlmydgrddnlfdhfsavaqrlgvytakdyadileflvgrwkvdkltglsa
egqkaqdyvcrlpprirrleeraqgrakeaptmpfswifdrqvkl
>d1afrd_ 1.25.1.2.5 delta 9-stearoyl-acyl carrier protein desaturase {Castor bean (Ricinus communis)}
mpprevhvqvthsmppqkieifksldnwaeenilvhlkpvekcwqpqdflpdpasdgfde
qvrelrerakeipddyfvvlvgdmiteealptyqtmlntldgvrdetgasptswaiwtra
wtaeenrhgdllnkylylsgrvdmrqiektiqyligsgmdprtenspylgfiytsfqera
tfishgntarqakehgdiklaqicgtiaadekrhetaytkiveklfeidpdgtvlafadm
mrkkismpahlmydgrddnlfdhfsavaqrlgvytakdyadileflvgrwkvdkltglsa
egqkaqdyvcrlpprirrleeraqgrakeaptmpfswifdrqvkl
>d1afre_ 1.25.1.2.5 delta 9-stearoyl-acyl carrier protein desaturase {Castor bean (Ricinus communis)}
mpprevhvqvthsmppqkieifksldnwaeenilvhlkpvekcwqpqdflpdpasdgfde
qvrelrerakeipddyfvvlvgdmiteealptyqtmlntldgvrdetgasptswaiwtra
wtaeenrhgdllnkylylsgrvdmrqiektiqyligsgmdprtenspylgfiytsfqera
tfishgntarqakehgdiklaqicgtiaadekrhetaytkiveklfeidpdgtvlafadm
mrkkismpahlmydgrddnlfdhfsavaqrlgvytakdyadileflvgrwkvdkltglsa
egqkaqdyvcrlpprirrleeraqgrakeaptmpfswifdrqvkl
>d1afrf_ 1.25.1.2.5 delta 9-stearoyl-acyl carrier protein desaturase {Castor bean (Ricinus communis)}
mpprevhvqvthsmppqkieifksldnwaeenilvhlkpvekcwqpqdflpdpasdgfde
qvrelrerakeipddyfvvlvgdmiteealptyqtmlntldgvrdetgasptswaiwtra
wtaeenrhgdllnkylylsgrvdmrqiektiqyligsgmdprtenspylgfiytsfqera
tfishgntarqakehgdiklaqicgtiaadekrhetaytkiveklfeidpdgtvlafadm
mrkkismpahlmydgrddnlfdhfsavaqrlgvytakdyadileflvgrwkvdkltglsa
egqkaqdyvcrlpprirrleeraqgrakeaptmpfswifdrqvkl
>d1afsa_ 3.1.5.1.5 3-alpha-hydroxysteroid dehydrogenase {rat (Rattus norvegicus) sprague-dawley strain}
mdsislrvalndgnfipvlgfgttvpekvakdevikatkiaidngfrhfdsaylyeveee
vgqairskiedgtvkredifytsklwstfhrpelvrtclektlkstqldyvdlyiihfpm
alqpgdiffprdehgkllfetvdicdtweamekckdaglaksigvsnfncrqlerilnkp
glkykpvcnqvechlylnqskmldyckskdiilvsyctlgssrdktwvdqkspvllddpv
lcaiakkykqtpalvalryqlqrgvvplirsfnakrikeltqvfefqlasedmkaldgln
rnfrynnakyfddhpnhpf
>d1afsb_ 3.1.5.1.5 3-alpha-hydroxysteroid dehydrogenase {rat (Rattus norvegicus) sprague-dawley strain}
mdsislrvalndgnfipvlgfgttvpekvakdevikatkiaidngfrhfdsaylyeveee
vgqairskiedgtvkredifytsklwstfhrpelvrtclektlkstqldyvdlyiihfpm
alqpgdiffprdehgkllfetvdicdtweamekckdaglaksigvsnfncrqlerilnkp
glkykpvcnqvechlylnqskmldyckskdiilvsyctlgssrdktwvdqkspvllddpv
lcaiakkykqtpalvalryqlqrgvvplirsfnakrikeltqvfefqlasedmkaldgln
rnfrynnakyfddhpnhpf
>d1afua_ 4.4.1.1.1 Ribonuclease A (also ribonuclease B, S) {bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1afub_ 4.4.1.1.1 Ribonuclease A (also ribonuclease B, S) {bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1afva_ 1.61.1.1.1 HIV-1 capsid protein, N-terminal core domain {Human immunodeficiency virus type 1 (HIV-1)}
pivqnlqgqmvhqaisprtlnawvkvveekafspevipmfsalsegatpqdlntmlntvg
ghqaamqmlketineeaaewdrlhpvhagpiapgqmreprgsdiagttstlqeqigwmth
nppipvgeiykrwiilglnkivrmysptsil
>d1afvb_ 1.61.1.1.1 HIV-1 capsid protein, N-terminal core domain {Human immunodeficiency virus type 1 (HIV-1)}
pivqnlqgqmvhqaisprtlnawvkvveekafspevipmfsalsegatpqdlntmlntvg
ghqaamqmlketineeaaewdrlhpvhagpiapgqmreprgsdiagttstlqeqigwmth
nppipvgeiykrwiilglnkivrmysptsil
>d1afvh1 2.1.1.1.78 (1-120) Immunoglobulin (variable domains of L and H chains) {Fab 25.3 (mouse), kappa L chain}
qvqlqqpgsvlvrpgasvklsckasgytftsswihwakqrpgqglewigeihpnsgntny
nekfkgkatltvdtssstayvdlssltsedsavyycarwrygspyyfdywgqgttltvss
>d1afvh2 2.1.1.2.81 (121-220) Immunoglobulin (constant domains of L and H chains) {Fab 25.3 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpsstwpsetvtcnvahpasstkvdkkivpk
>d1afvk1 2.1.1.1.78 (1-120) Immunoglobulin (variable domains of L and H chains) {Fab 25.3 (mouse), kappa L chain}
qvqlqqpgsvlvrpgasvklsckasgytftsswihwakqrpgqglewigeihpnsgntny
nekfkgkatltvdtssstayvdlssltsedsavyycarwrygspyyfdywgqgttltvss
>d1afvk2 2.1.1.2.81 (121-220) Immunoglobulin (constant domains of L and H chains) {Fab 25.3 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpsstwpsetvtcnvahpasstkvdkkivpk
>d1afvl1 2.1.1.1.78 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab 25.3 (mouse), kappa L chain}
divltqspaslavslgqratiscrasesvdnygisfmnwfqqkpgqppklliyaasnlgs
gvparfsgsgsgtdfslnihpmeeedtamyfcqqskevpltfgagtkvelkr
>d1afvl2 2.1.1.2.81 (113-217) Immunoglobulin (constant domains of L and H chains) {Fab 25.3 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrne
>d1afvm1 2.1.1.1.78 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab 25.3 (mouse), kappa L chain}
divltqspaslavslgqratiscrasesvdnygisfmnwfqqkpgqppklliyaasnlgs
gvparfsgsgsgtdfslnihpmeeedtamyfcqqskevpltfgagtkvelkr
>d1afvm2 2.1.1.2.81 (113-217) Immunoglobulin (constant domains of L and H chains) {Fab 25.3 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrne
>d1afwa1 3.83.1.1.1 (25-293) Thiolase {yeast (Saccharomyces serevisiae)}
knsllekrpedvvivaanrsaigkgfkgafkdvntdyllynflnefigrfpeplradlnl
ieevacgnvlnvgagatehraaclasgipystpfvalnrqcssgltavndiankikvgqi
diglalgvesmtnnyknvnplgmisseelqknreakkclipmgitnenvaanfkisrkdq
defaansyqkaykakneglfedeilpiklpdgsicqsdegprpnvtaeslssirpafikd
rgtttagnasqvsdgvagvllarrsvanq
>d1afwa2 3.83.1.1.1 (294-417) Thiolase {yeast (Saccharomyces serevisiae)}
lnlpvlgryidfqtvgvppeimgvgpayaipkvleatglqvqdidifeineafaaqalyc
ihklgidlnkvnprggaialghplgctgarqvatilrelkkdqigvvsmcigtgmgaaai
fike
>d1afwb1 3.83.1.1.1 (25-293) Thiolase {yeast (Saccharomyces serevisiae)}
knsllekrpedvvivaanrsaigkgfkgafkdvntdyllynflnefigrfpeplradlnl
ieevacgnvlnvgagatehraaclasgipystpfvalnrqcssgltavndiankikvgqi
diglalgvesmtnnyknvnplgmisseelqknreakkclipmgitnenvaanfkisrkdq
defaansyqkaykakneglfedeilpiklpdgsicqsdegprpnvtaeslssirpafikd
rgtttagnasqvsdgvagvllarrsvanq
>d1afwb2 3.83.1.1.1 (294-417) Thiolase {yeast (Saccharomyces serevisiae)}
lnlpvlgryidfqtvgvppeimgvgpayaipkvleatglqvqdidifeineafaaqalyc
ihklgidlnkvnprggaialghplgctgarqvatilrelkkdqigvvsmcigtgmgaaai
fike
>d1ag0a_ 2.5.1.1.17 Azurin {(Pseudomonas aeruginosa)}
aaecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgv
vtdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffdtfpghsa
lmkgtltlk
>d1ag0b_ 2.5.1.1.17 Azurin {(Pseudomonas aeruginosa)}
aaecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgv
vtdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffdtfpghsa
lmkgtltlk
>d1ag1o_ 3.1.11.1.4 Triosephosphate isomerase {(Trypanosoma brucei brucei)}
skpqpiaaanwkcngsqqslselidlfnstsinhdvqcvvastfvhlamtkerlshpkfv
iaaqnaiaksgaftgevslpilkdfgvnwivlghserrayygetneivadkvaaavasgf
mviacigetlqeresgrtavvvltqiaaiakklkkadwakvviayepvwaigtgkvatpq
qaqeahalirswvsskigadvagelrilyggsvngknartlyqqrdvngflvggaslkpe
fvdiikatq
>d1ag1t_ 3.1.11.1.4 Triosephosphate isomerase {(Trypanosoma brucei brucei)}
skpqpiaaanwkcngsqqslselidlfnstsinhdvqcvvastfvhlamtkerlshpkfv
iaaqnaiaksgaftgevslpilkdfgvnwivlghserrayygetneivadkvaaavasgf
mviacigetlqeresgrtavvvltqiaaiakklkkadwakvviayepvwaigtgkvatpq
qaqeahalirswvsskigadvagelrilyggsvngknartlyqqrdvngflvggaslkpe
fvdiikatq
>d1ag2__ 4.5.1.1.1 Prion protein domain {mouse (Mus musculus)}
glggymlgsamsrpmihfgndwedryyrenmyrypnqvyyrpvdqysnqnnfvhdcvnit
ikqhtvttttkgenftetdvkmmervveqmcvtqyqkesqayy
>d1ag4__ 2.9.1.2.2 Spherulin 3a (S3a) {Slime mold (Physarum polycephalum)}
msvckgvsgnpakgevflykhvnfqgdswkvtgnvydfrsvsglndvvssvkvgpntkaf
ifkddrfngnfirleessqvtdlttrnlndaissiivatfesa
>d1ag7__ 7.3.5.1.2 Conotoxin {Synthetic (Conus geographus) GS}
acsgrgsrcxxqccmglrcgrgnpqkcigahxdv
>d1ag8a_ 3.70.1.1.2 Aldehyde reductase (dehydrogenase) {bovine (Bos taurus) mitochondria}
vptpnqqpevlynqifinnewhdavskktfptvnpstgdvichvaegdkadvdravkaar
aafqlgspwrrmdasergrllnrladlierdrtylaaletldngkpyiisylvdldmvlk
clryyagwadkyhgktipidgdyfsytrhepvgvcgqiipwnfpllmqawklgpalatgn
vvvmkvaeqtpltalyvanlikeagfppgvvnvipgfgptagaaiashedvdkvaftgst
evghliqvaagksnlkrvtleiggkspniimsdadmdwaveqahfalffnqgqcccagsr
tfvqediyaefversvaraksrvvgnpfdsrteqgpqvdetqfkkvlgyiksgkeeglkl
lcgggaaadrgyfiqptvfgdlqdgmtiakeeifgpvmqilkfksmeevvgrannskygl
aaavftkdldkanylsqalqagtvwvncydvfgaqspfggyklsgsgrelgeyglqayte
vktvtvrvpqkns
>d1ag8b_ 3.70.1.1.2 Aldehyde reductase (dehydrogenase) {bovine (Bos taurus) mitochondria}
vptpnqqpevlynqifinnewhdavskktfptvnpstgdvichvaegdkadvdravkaar
aafqlgspwrrmdasergrllnrladlierdrtylaaletldngkpyiisylvdldmvlk
clryyagwadkyhgktipidgdyfsytrhepvgvcgqiipwnfpllmqawklgpalatgn
vvvmkvaeqtpltalyvanlikeagfppgvvnvipgfgptagaaiashedvdkvaftgst
evghliqvaagksnlkrvtleiggkspniimsdadmdwaveqahfalffnqgqcccagsr
tfvqediyaefversvaraksrvvgnpfdsrteqgpqvdetqfkkvlgyiksgkeeglkl
lcgggaaadrgyfiqptvfgdlqdgmtiakeeifgpvmqilkfksmeevvgrannskygl
aaavftkdldkanylsqalqagtvwvncydvfgaqspfggyklsgsgrelgeyglqayte
vktvtvrvpqkns
>d1ag8c_ 3.70.1.1.2 Aldehyde reductase (dehydrogenase) {bovine (Bos taurus) mitochondria}
vptpnqqpevlynqifinnewhdavskktfptvnpstgdvichvaegdkadvdravkaar
aafqlgspwrrmdasergrllnrladlierdrtylaaletldngkpyiisylvdldmvlk
clryyagwadkyhgktipidgdyfsytrhepvgvcgqiipwnfpllmqawklgpalatgn
vvvmkvaeqtpltalyvanlikeagfppgvvnvipgfgptagaaiashedvdkvaftgst
evghliqvaagksnlkrvtleiggkspniimsdadmdwaveqahfalffnqgqcccagsr
tfvqediyaefversvaraksrvvgnpfdsrteqgpqvdetqfkkvlgyiksgkeeglkl
lcgggaaadrgyfiqptvfgdlqdgmtiakeeifgpvmqilkfksmeevvgrannskygl
aaavftkdldkanylsqalqagtvwvncydvfgaqspfggyklsgsgrelgeyglqayte
vktvtvrvpqkns
>d1ag8d_ 3.70.1.1.2 Aldehyde reductase (dehydrogenase) {bovine (Bos taurus) mitochondria}
vptpnqqpevlynqifinnewhdavskktfptvnpstgdvichvaegdkadvdravkaar
aafqlgspwrrmdasergrllnrladlierdrtylaaletldngkpyiisylvdldmvlk
clryyagwadkyhgktipidgdyfsytrhepvgvcgqiipwnfpllmqawklgpalatgn
vvvmkvaeqtpltalyvanlikeagfppgvvnvipgfgptagaaiashedvdkvaftgst
evghliqvaagksnlkrvtleiggkspniimsdadmdwaveqahfalffnqgqcccagsr
tfvqediyaefversvaraksrvvgnpfdsrteqgpqvdetqfkkvlgyiksgkeeglkl
lcgggaaadrgyfiqptvfgdlqdgmtiakeeifgpvmqilkfksmeevvgrannskygl
aaavftkdldkanylsqalqagtvwvncydvfgaqspfggyklsgsgrelgeyglqayte
vktvtvrvpqkns
>d1ag9a_ 3.14.4.1.5 Flavodoxin {(Escherichia coli)}
aitgiffgsdtgnteniakmiqkqlgkdvadvhdiaksskedleaydilllgiptwyyge
aqcdwddffptleeidfngklvalfgcgdqedyaeyfcdalgtirdiieprgativghwp
tagyhfeaskgladddhfvglaidedrqpeltaervekwvkqiseelhldeilna
>d1ag9b_ 3.14.4.1.5 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 4.15.1.1.12 (1-181) MHC class I, alpha-1 and alpha-2 domains {(human hla-b0801)}
gshsmryfdtamsrpgrgeprfisvgyvddtqfvrfdsdaaspreeprapwieqegpeyw
drntqifktntqtdreslrnlrgyynqseagshtlqsmygcdvgpdgrllrghnqyaydg
kdyialnedlrswtaadtaaqitqrkweaarvaeqdraylegtcvewlrrylengkdtle
r
>d1agca1 2.1.1.2.8 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain {(human hla-b0801)}
adppkthvthhpisdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrwep
>d1agca2 4.15.1.1.12 (1-181) MHC class I, alpha-1 and alpha-2 domains {(human hla-b0801)}
gshsmryfdtamsrpgrgeprfisvgyvddtqfvrfdsdaaspreeprapwieqegpeyw
drntqifktntqtdreslrnlrgyynqseagshtlqsmygcdvgpdgrllrghnqyaydg
kdyialnedlrswtaadtaaqitqrkweaarvaeqdraylegtcvewlrrylengkdtle
r
>d1agda1 2.1.1.2.8 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain {(human hla-b0801)}
adppkthvthhpisdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrwep
>d1agda2 4.15.1.1.12 (1-181) MHC class I, alpha-1 and alpha-2 domains {(human hla-b0801)}
gshsmryfdtamsrpgrgeprfisvgyvddtqfvrfdsdaaspreeprapwieqegpeyw
drntqifktntqtdreslrnlrgyynqseagshtlqsmygcdvgpdgrllrghnqyaydg
kdyialnedlrswtaadtaaqitqrkweaarvaeqdraylegtcvewlrrylengkdtle
r
>d1agea1 2.1.1.2.8 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain {(human hla-b0801)}
adppkthvthhpisdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrwep
>d1agea2 4.15.1.1.12 (1-181) MHC class I, alpha-1 and alpha-2 domains {(human hla-b0801)}
gshsmryfdtamsrpgrgeprfisvgyvddtqfvrfdsdaaspreeprapwieqegpeyw
drntqifktntqtdreslrnlrgyynqseagshtlqsmygcdvgpdgrllrghnqyaydg
kdyialnedlrswtaadtaaqitqrkweaarvaeqdraylegtcvewlrrylengkdtle
r
>d1agfa1 2.1.1.2.8 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain {(human hla-b0801)}
adppkthvthhpisdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrwep
>d1agfa2 4.15.1.1.12 (1-181) MHC class I, alpha-1 and alpha-2 domains {(human hla-b0801)}
gshsmryfdtamsrpgrgeprfisvgyvddtqfvrfdsdaaspreeprapwieqegpeyw
drntqifktntqtdreslrnlrgyynqseagshtlqsmygcdvgpdgrllrghnqyaydg
kdyialnedlrswtaadtaaqitqrkweaarvaeqdraylegtcvewlrrylengkdtle
r
>d1agg__ 7.3.5.2.1 omega-Agatoxin IV, IVa, IVb {funnel web spider (Agelenopsis aperta)}
ednciaedygkctwggtkccrgrpcrcsmigtncectprlimeglsfa
>d1agi__ 4.4.1.1.5 Angiogenin {Bovine (Bos taurus)}
aqddyryihfltqhydakpkgrndeycfnmmknrrltrpckdrntfihgnkndikaiced
rngqpyrgdlrisksefqitickhkggssrppcrygatedsrvivvgcenglpvhfdesf
itprh
>d1agja_ 2.35.1.1.8 Epidermolytic toxin A {(Staphylococcus aureus)}
evsaeeikkheekwnkyygvnafnlpkelfskvdekdrqkypyntignvfvkgqtsatgv
ligkntvltnrhiakfangdpskvsfrpsintddngntetpygeyevkeilqepfgagvd
lalirlkpdqngvslgdkispakigtsndlkdgdkleligypfdhkvnqmhrseielttl
srglryygftvpgnsgsgifnsngelvgihsskvshldrehqinygvgignyvkriinek
ne
>d1agjb_ 2.35.1.1.8 Epidermolytic toxin A {(Staphylococcus aureus)}
evsaeeikkheekwnkyygvnafnlpkelfskvdekdrqkypyntignvfvkgqtsatgv
ligkntvltnrhiakfangdpskvsfrpsintddngntetpygeyevkeilqepfgagvd
lalirlkpdqngvslgdkispakigtsndlkdgdkleligypfdhkvnqmhrseielttl
srglryygftvpgnsgsgifnsngelvgihsskvshldrehqinygvgignyvkriinek
ne
>d1agm__ 1.81.1.1.1 Glucoamylase {(Aspergillus awamori), variant x100}
atldswlsneatvartailnnigadgawvsgadsgivvaspstdnpdyfytwtrdsglvi
ktlvdlfrngdtdllstiehyissqaiiqgvsnpsgdlssgglgepkfnvdetaytgswg
rpqrdgpalratamigfgqwlldngytsaateivwplvrndlsyvaqywnqtgydlweev
ngssfftiavqhralvegsafatavgsscswcdsqapqilcylqsfwtgsyilanfdssr
sgkdtntllgsihtfdpeagcddstfqpcspralanhkevvdsfrsiytlndglsdseav
avgrypedsyyngnpwflctlaaaeqlydalyqwdkqgsleitdvsldffkalysgaatg
tyssssstyssivsavktfadgfvsivethaasngslseqfdksdgdelsardltwsyaa
lltannrrnsvvppswgetsassvpgtcaatsasgtyssvtvtswpsiva
>d1agna1 2.25.1.2.2 (1-174,325-374) Alcohol dehydrogenase {human (Homo sapiens)}
gtagkvikckaavlweqkqpfsieeievappktkevrikilatgicrtddhvikgtmvsk
fpvivgheatgivesigegvttvkpgdkviplflpqcrecnacrnpdgnlcirsditgrg
vladgttrftckgkpvhhfmntstfteytvvdessvakiddaappekvcligcXrddvpk
lvteflakkfdldqlithvlpfkkisegfellnsgqsirtvltf
>d1agna2 3.22.1.1.2 (175-324) Alcohol dehydrogenase {human (Homo sapiens), different isozymes}
gfstgygaavktgkvkpgstcvvfglggvglsvimgcksagasriigidlnkdkfekama
vgatecispkdstkpisevlsemtgnnvgytfevighletmidalaschmnygtsvvvgv
ppsakmltydpmllftgrtwkgcvfgglks
>d1agnb1 2.25.1.2.2 (1-174,325-374) Alcohol dehydrogenase {human (Homo sapiens)}
gtagkvikckaavlweqkqpfsieeievappktkevrikilatgicrtddhvikgtmvsk
fpvivgheatgivesigegvttvkpgdkviplflpqcrecnacrnpdgnlcirsditgrg
vladgttrftckgkpvhhfmntstfteytvvdessvakiddaappekvcligcXrddvpk
lvteflakkfdldqlithvlpfkkisegfellnsgqsirtvltf
>d1agnb2 3.22.1.1.2 (175-324) Alcohol dehydrogenase {human (Homo sapiens), different isozymes}
gfstgygaavktgkvkpgstcvvfglggvglsvimgcksagasriigidlnkdkfekama
vgatecispkdstkpisevlsemtgnnvgytfevighletmidalaschmnygtsvvvgv
ppsakmltydpmllftgrtwkgcvfgglks
>d1agnc1 2.25.1.2.2 (1-174,325-374) Alcohol dehydrogenase {human (Homo sapiens)}
gtagkvikckaavlweqkqpfsieeievappktkevrikilatgicrtddhvikgtmvsk
fpvivgheatgivesigegvttvkpgdkviplflpqcrecnacrnpdgnlcirsditgrg
vladgttrftckgkpvhhfmntstfteytvvdessvakiddaappekvcligcXrddvpk
lvteflakkfdldqlithvlpfkkisegfellnsgqsirtvltf
>d1agnc2 3.22.1.1.2 (175-324) Alcohol dehydrogenase {human (Homo sapiens), different isozymes}
gfstgygaavktgkvkpgstcvvfglggvglsvimgcksagasriigidlnkdkfekama
vgatecispkdstkpisevlsemtgnnvgytfevighletmidalaschmnygtsvvvgv
ppsakmltydpmllftgrtwkgcvfgglks
>d1agnd1 2.25.1.2.2 (1-174,325-374) Alcohol dehydrogenase {human (Homo sapiens)}
gtagkvikckaavlweqkqpfsieeievappktkevrikilatgicrtddhvikgtmvsk
fpvivgheatgivesigegvttvkpgdkviplflpqcrecnacrnpdgnlcirsditgrg
vladgttrftckgkpvhhfmntstfteytvvdessvakiddaappekvcligcXrddvpk
lvteflakkfdldqlithvlpfkkisegfellnsgqsirtvltf
>d1agnd2 3.22.1.1.2 (175-324) Alcohol dehydrogenase {human (Homo sapiens), different isozymes}
gfstgygaavktgkvkpgstcvvfglggvglsvimgcksagasriigidlnkdkfekama
vgatecispkdstkpisevlsemtgnnvgytfevighletmidalaschmnygtsvvvgv
ppsakmltydpmllftgrtwkgcvfgglks
>d1agp__ 3.29.1.4.1 cH-p21 Ras protein {human (Homo sapiens)}
mteyklvvvgadgvgksaltiqliqnhfvdeydptiedsyrkqvvidgetclldildtag
qeeysamrdqymrtgegflcvfainntksfedihqyreqikrvkdsddvpmvlvgnkcdl
aartvesrqaqdlarsygipyietsaktrqgvedafytlvreirqh
>d1agqa_ 7.16.1.3.1 Glial cell-derived neurotrophic factor {rat (Rattus norvegicus)}
nrgcvltaihlnvtdlglgyetkeelifrycsgsceaaetmydkilknlsrsrrltsdkv
gqaccrpvafdddlsflddslvyhilrkhsakrcgci
>d1agqb_ 7.16.1.3.1 Glial cell-derived neurotrophic factor {rat (Rattus norvegicus)}
knrgcvltaihlnvtdlglgyetkeelifrycsgsceaaetmydkilknlsrsrrltsdk
vgqaccrpvafdddlsflddslvyhilrkhsakrcgci
>d1agqc_ 7.16.1.3.1 Glial cell-derived neurotrophic factor {rat (Rattus norvegicus)}
gcvltaihlnvtdlglgyetkeelifrycsgsceaaetmydkilknlsrsrrltsdkvgq
accrpvafdddlsflddslvyhilrkhsakrcgci
>d1agqd_ 7.16.1.3.1 Glial cell-derived neurotrophic factor {rat (Rattus norvegicus)}
gcvltaihlnvtdlglgyetkeelifrycsgsceaaetmydkilknlsrsrrltsdkvgq
accrpvafdddlsflddslvyhilrkhsakrcgci
>d1agra1 1.56.1.1.2 (61-181) Transducin (alpha subunit), insertion domain {rat (Rattus rattus)}
yseeeckqykavvysntiqsiiaiiramgrlkidfgdaaraddarqlfvlagaaeegfmt
aelagvikrlwkdsgvqacfnrsreyqlndsaayylndldriaqpnyiptqqdvlrtrvk
t
>d1agra2 3.29.1.4.12 (5-60,182-354) Transducin (alpha subunit) {rat (Rattus rattus)}
lsaedkaaverskmidrnlredgekaarevkllllgagesgkstivkqmkiiheagXtgi
vethftfkdlhfkmfdvggqrserkkwihcfegvtaiifcvalsdydlvlaedeemnrmh
esmklfdsicnnkwftdtsiilflnkkdlfeekikksplticypeyagsntyeeaaayiq
cqfedlnkrkdtkeiythftcatdtknvqfvfdavtdviiknnlkdcglf
>d1agrd1 1.56.1.1.2 (61-181) Transducin (alpha subunit), insertion domain {rat (Rattus rattus)}
yseeeckqykavvysntiqsiiaiiramgrlkidfgdaaraddarqlfvlagaaeegfmt
aelagvikrlwkdsgvqacfnrsreyqlndsaayylndldriaqpnyiptqqdvlrtrvk
t
>d1agrd2 3.29.1.4.12 (11-60,182-354) Transducin (alpha subunit) {rat (Rattus rattus)}
aaverskmidrnlredgekaarevkllllgagesgkstivkqmkiiheagXtgivethft
fkdlhfkmfdvggqrserkkwihcfegvtaiifcvalsdydlvlaedeemnrmhesmklf
dsicnnkwftdtsiilflnkkdlfeekikksplticypeyagsntyeeaaayiqcqfedl
nkrkdtkeiythftcatdtknvqfvfdavtdviiknnlkdcglf
>d1agre_ 1.70.1.1.1 Regulator of G-protein signalling 4, RGS4 {rat (Rattus norvegicus)}
vsqeevkkwaeslenlinhecglaafkaflkseyseenidfwisceeykkikspsklspk
akkiynefisvqatkevnldsctreetsrnmleptitcfdeaqkkifnlmekdsyrrflk
srfyldlt
>d1agrh_ 1.70.1.1.1 Regulator of G-protein signalling 4, RGS4 {rat (Rattus norvegicus)}
aeslenlinhecglaafkaflkseyseenidfwisceeykkikspsklspkakkiynefi
svqatkevnldsctreetsrnmleptitcfdeaqkkifnlmekdsyrrflksrfyl
>d1agsa1 1.43.1.1.8 (80-221) Glutathione S-transferase {human (Homo sapiens), class alpha}
lyrkdikekalidmyiegiadlgemilllpftqpeeqdaklalikekiknryfpafekvl
kshgqdylvgnklsradihlvellyyveeldsslissfpllkalktrisnlptvkkflqp
gsprkppmdeksleearkifrf
>d1agsa2 3.38.1.4.8 (1-79) Glutathione S-transferase {human (Homo sapiens) class alpha}
aekpklhyfnargrmestrwllaaagvefeekfiksaedldklrndgylmfqqvpmveid
gmklvqtrailnyiaskyn
>d1agsb1 1.43.1.1.8 (80-221) Glutathione S-transferase {human (Homo sapiens), class alpha}
lyrkdikekalidmyiegiadlgemilllpftqpeeqdaklalikekiknryfpafekvl
kshgqdylvgnklsradihlvellyyveeldsslissfpllkalktrisnlptvkkflqp
gsprkppmdeksleearkifrf
>d1agsb2 3.38.1.4.8 (1-79) Glutathione S-transferase {human (Homo sapiens) class alpha}
aekpklhyfnargrmestrwllaaagvefeekfiksaedldklrndgylmfqqvpmveid
gmklvqtrailnyiaskyn
>d1agt__ 7.3.6.2.6 Agitoxin {scorpion (Leiurus quinquestriatus hebraeus)}
gvpinvsctgspqcikpckdagmrfgkcmnrkchctpk
>d1agwa_ 5.1.1.2.5 Fibroblast growth factor receptor 1 {human (Homo sapiens)}
elpedprwelprdrlvlgkplgegafgqvvlaeaigldkdkpnrvtkvavkmlksdatek
dlsdlisememmkmigkhkniinllgactqdgplyviveyaskgnlreylqarrppgley
synpshnpeeqlsskdlvscayqvargmeylaskkcihrdlaarnvlvtednvmkiadfg
lardihhidyykkttngrlpvkwmapealfdriythqsdvwsfgvllweiftlggspypg
vpveelfkllkeghrmdkpsnctnelymmmrdcwhavpsqrptfkqlvedldrivalts
>d1agwb_ 5.1.1.2.5 Fibroblast growth factor receptor 1 {human (Homo sapiens)}
seyelpedprwelprdrlvlgkplgegafgqvvlaeaigldkdkpnrvtkvavkmlksda
tekdlsdlisememmkmigkhkniinllgactqdgplyviveyaskgnlreylqarrppg
leysynpshnpeeqlsskdlvscayqvargmeylaskkcihrdlaarnvlvtednvmkia
dfglardihhidyykkttngrlpvkwmapealfdriythqsdvwsfgvllweiftlggsp
ypgvpveelfkllkeghrmdkpsnctnelymmmrdcwhavpsqrptfkqlvedldrival
t
>d1agx__ 3.77.1.1.3 Glutaminase-asparaginase {(Acinetobacter glutaminasificans)}
knnvvivatggtiagagasstnsatysaakvpvdalikavpqvndlanitgiqalqvase
sitdkellslarqvndlvkkpsvngvvithgtdtmeetafflnlvvhtdkpivlvgsmrp
stalsadgplnlysavalassneaknkgvmvlmndsifaardvtkginihthafvsqwga
lgtlvegkpywfrssvkkhtnnsefniekiqgdalpgvqivygsdnmmpdayqafakagv
kaiihagtgngsmanylvpevrklhdeqglqivrssrvaqgfvlrnaeqpddkygwiaah
dlnpqkarllmalaltktndakeiqnmfwny
>d1agy__ 3.14.7.1.1 Cutinase {fungus (Fusarium solani, subsp. pisi)}
rttrddlingnsascrdvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1ah0__ 3.1.5.1.4 Aldose reductase (aldehyde reductase) {porcine (Sus scrofa)}
ashlvlytgakmpilglgtwksppgkvteavkvaidlgyrhidcahvyqnenevglglqe
klqgqvvkredlfivsklwctdheknlvkgacqttlrdlkldyldlylihwptgfkpgkd
pfpldgdgnvvpdesdfvetweameelvdeglvkaigvsnfnhlqvekilnkpglkykpa
vnqievhpyltqeklieyckskgivvtaysplgspdrpwakpedpslledprikaiaaky
nkttaqvlirfpmqrnlivipksvtperiaenfqvfdfelspedmntllsynrnwrvcal
mscashkdypfheey
>d1ah1__ 2.1.1.1.124 Immunoreceptor CTLA-4 (CD152), N-terminal fragment {Human (Homo sapiens)}
amhvaqpavvlassrgiasfvceyaspgkatevrvtvlrqadsqvtevcaatymmgnelt
flddsictgtssgnqvnltiqglramdtglyickvelmypppyylgigngtqiyvidpep
cpdsdqepk
>d1ah2__ 3.33.1.1.10 Serine protease PB92 {(Bacillus alcalophylus)}
aqsvpwgisrvqapaahnrgltgsgvkvavldtgisthpdlnirggasfvpgepstqdgn
ghgthvagtiaalnnsigvlgvapnaelyavkvlgasgsgsvssiaqglewagnngmhva
nlslgspspsatleqavnsatsrgvlvvaasgnsgagsisyparyanamavgatdqnnnr
asfsqygagldivapgvnvqstypgstyaslngtsmatphvagaaalvkqknpswsnvqi
rnhlkntatslgstnlygsglvnaeaatr
>d1ah3__ 3.1.5.1.4 Aldose reductase (aldehyde reductase) {porcine (Sus scrofa)}
shlvlytgakmpilglgtwksppgkvteavkvaidlgyrhidcahvyqnenevglglqek
lqgqvvkredlfivsklwctdheknlvkgacqttlrdlkldyldlylihwptgfkpgkdp
fpldgdgnvvpdesdfvetweameelvdeglvkaigvsnfnhlqvekilnkpglkykpav
nqievhpyltqeklieyckskgivvtaysplgspdrpwakpedpslledprikaiaakyn
kttaqvlirfpmqrnlivipksvtperiaenfqvfdfelspedmntllsynrnwrvcalm
scashkdypfheey
>d1ah4__ 3.1.5.1.4 Aldose reductase (aldehyde reductase) {porcine (Sus scrofa)}
shlvlytgakmpilglgtwksppgkvteavkvaidlgyrhidcahvyqnenevglglqek
lqgqvvkredlfivsklwctdheknlvkgacqttlrdlkldyldlylihwptgfkpgkdp
fpldgdgnvvpdesdfvetweameelvdeglvkaigvsnfnhlqvekilnkpglkykpav
nqievhpyltqeklieyckskgivvtaysplgspdrpwakpedpslledprikaiaakyn
kttaqvlirfpmqrnlivipksvtperiaenfqvfdfelspedmntllsynrnwrvcalm
scashkdypfheey
>d1ah5_1 3.82.1.1.2 (3-219) Porphobilinogen deaminase (hydroxymethylbilane synthase), N-terminal domain {(Escherichia coli)}
dnvlriatrqsplalwqahyvkdklxashpglvvelvpxvtrgdvildtplakvggkglf
vkelevallenradiavhsxkdvpvefpqglglvticeredprdafvsnnydsldalpag
sivgtsslrrqcqlaerrpdliirslrgnvgtrlskldngeydaiilavaglkrlglesr
iraalppeislpavgqgavgiecrlddsrtrellaal
>d1ah5_2 4.29.2.1.1 (220-313) Porphobilinogen deaminase (hydroxymethylbilane synthase), C-terminal domain {(Escherichia coli)}
nhhetalrvtaeraxntrleggcqvpigsyaelidgeiwlralvgapdgsqiirgerrga
pqdaeqxgislaeellnngareilaevyngdapa
>d1ah6__ 4.72.1.1.1 HSP90 {yeast (Saccharomyces cerevisiae)}
asetfefqaeitqlmsliintvysnkeiflrelisnasdaldkirykslsdpkqletepd
lfiritpkpeqkvleirdsgigmtkaelinnlgtiaksgtkafmealsagadvsmigqfg
vgfyslflvadrvqvisksnddeqyiwesnaggsftvtldevnerigrgtilrlflkddq
leyleekrikevikrhsefvaypiqlvvtkeve
>d1ah7__ 1.96.1.1.1 Bacterial phosholipase C {(Bacillus cereus)}
wsaedkhkegvnshlwivnraidimsrnttlvkqdrvaqlnewrtelengiyaadyenpy
ydnstfashfydpdngktyipfakqaketgakyfklagesyknkdmkqaffylglslhyl
gdvnqpmhaanftnlsypqgfhskyenfvdtikdnykvtdgngywnwkgtnpeewihgaa
vvakqdysgivndntkdwfvkaavsqeyadkwraevtpmtgkrlmdaqrvtagyiqlwfd
tygdr
>d1ah8a_ 4.72.1.1.1 HSP90 {yeast (Saccharomyces cerevisiae)}
asetfefqaeitqlmsliintvysnkeiflrelisnasdaldkirykslsdpkqletepd
lfiritpkpeqkvleirdsgigmtkaelinnlgtiaksgtkafmealsagadvsmigqfg
vgfyslflvadrvqvisksnddeqyiwesnaggsftvtldevnerigrgtilrlflkddq
leyleekrikevikrhsefvaypiqlvvtkeveke
>d1ah8b_ 4.72.1.1.1 HSP90 {yeast (Saccharomyces cerevisiae)}
asetfefqaeitqlmsliintvysnkeiflrelisnasdaldkirykslsdpkqletepd
lfiritpkpeqkvleirdsgigmtkaelinnlgtiaksgtkafmealsagadvsmigqfg
vgfyslflvadrvqvisksnddeqyiwesnaggsftvtldevnerigrgtilrlflkddq
leyleekrikevikrhsefvaypiqlvvtkevekevpi
>d1ah9__ 2.29.4.5.4 Translational initiation factor 1, IF1 {(Escherichia coli)}
akedniemqgtvletlpntmfrvelenghvvtahisgkmrknyiriltgdkvtveltpyd
lskgrivfrsr
>d1aha__ 4.102.1.1.3 alpha-Momorcharin (momordin) {bitter melon (Momordica charantia)}
dvsfrlsgadprsygmfikdlrnalpfrekvyniplllpsvsgagryllmhlfnydgkti
tvavdvtnvyimgyladttsyffnepaaelasqyvfrdarrkitlpysgnyerlqiaagk
prekipiglpaldsaistllhydstaaagallvliqttaeaarfkyieqqiqerayrdev
pslatislenswsglskqiqlaqgnngifrtpivlvdnkgnrvqitnvtskvvtsniqll
lntrni
>d1ahb__ 4.102.1.1.3 alpha-Momorcharin (momordin) {bitter melon (Momordica charantia)}
dvsfrlsgadprsygmfikdlrnalpfrekvyniplllpsvsgagryllmhlfnydgkti
tvavdvtnvyimgyladttsyffnepaaelasqyvfrdarrkitlpysgnyerlqiaagk
prekipiglpaldsaistllhydstaaagallvliqttaeaarfkyieqqiqerayrdev
pslatislenswsglskqiqlaqgnngifrtpivlvdnkgnrvqitnvtskvvtsniqll
lntrni
>d1ahc__ 4.102.1.1.3 alpha-Momorcharin (momordin) {bitter melon (Momordica charantia)}
dvsfrlsgadprsygmfikdlrnalpfrekvyniplllpsvsgagryllmhlfnydgkti
tvavdvtnvyimgyladttsyffnepaaelasqyvfrdarrkitlpysgnyerlqiaagk
prekipiglpaldsaistllhydstaaagallvliqttaeaarfkyieqqiqerayrdev
pslatislenswsglskqiqlaqgnngifrtpivlvdnkgnrvqitnvtskvvtsniqll
lntrni
>d1ahdp_ 1.4.1.1.10 antennapedia Homeodomain {(Drosophila melanogaster)}
mrkrgrqtytryqtlelekefhfnryltrrrrieiahalslterqikiwfqnrrmkwkke
nktkgepg
>d1ahea_ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgiglyydetgkipvltsvkkaeqyllene
ttklylgidgipefgrctqellfgkgsalindkrartaqtpggsgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanyssppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aheb_ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgiglyydetgkipvltsvkkaeqyllene
ttklylgidgipefgrctqellfgkgsalindkrartaqtpggsgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanyssppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ahfa_ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgiglyydetgkipvltsvkkaeqyllene
ttklylgidgipefgrctqellfgkgsalindkrartaqtpggsgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanyssppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ahfb_ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgiglyydetgkipvltsvkkaeqyllene
ttklylgidgipefgrctqellfgkgsalindkrartaqtpggsgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanyssppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ahga_ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgiglyydetgkipvltsvkkaeqyllene
ttklylgidgipefgrctqellfgkgsalindkrartaqtpggsgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanyssppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ahgb_ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgiglyydetgkipvltsvkkaeqyllene
ttklylgidgipefgrctqellfgkgsalindkrartaqtpggsgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanyssppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ahha_ 3.22.1.2.4 7-alpha-hydroxysteroid dehydrogenase {(Escherichia coli)}
mfnsdnlrldgkcaiitgagagigkeiaitfatagasvvvsdinadaanhvvdeiqqlgg
qafacrcditseqelsaladfaisklgkvdilvnnaggggpkpfdmpmadfrrayelnvf
sffhlsqlvapemekngggviltitsmaaenkninmtsyasskaaashlvrnmafdlgek
nirvngiapgailtdalksvitpeieqkmlqhtpirrlgqpqdianaalflcspaaswvs
gqiltvsgggvqe
>d1ahhb_ 3.22.1.2.4 7-alpha-hydroxysteroid dehydrogenase {(Escherichia coli)}
mfnsdnlrldgkcaiitgagagigkeiaitfatagasvvvsdinadaanhvvdeiqqlgg
qafacrcditseqelsaladfaisklgkvdilvnnaggggpkpfdmpmadfrrayelnvf
sffhlsqlvapemekngggviltitsmaaenkninmtsyasskaaashlvrnmafdlgek
nirvngiapgailtdalksvitpeieqkmlqhtpirrlgqpqdianaalflcspaaswvs
gqiltvsgggvqe
>d1ahia_ 3.22.1.2.4 7-alpha-hydroxysteroid dehydrogenase {(Escherichia coli)}
mfnsdnlrldgkcaiitgagagigkeiaitfatagasvvvsdinadaanhvvdeiqqlgg
qafacrcditseqelsaladfaisklgkvdilvnnaggggpkpfdmpmadfrrayelnvf
sffhlsqlvapemekngggviltitsmaaenkninmtsyasskaaashlvrnmafdlgek
nirvngiapgailtdalksvitpeieqkmlqhtpirrlgqpqdianaalflcspaaswvs
gqiltvsgggvqeln
>d1ahib_ 3.22.1.2.4 7-alpha-hydroxysteroid dehydrogenase {(Escherichia coli)}
mfnsdnlrldgkcaiitgagagigkeiaitfatagasvvvsdinadaanhvvdeiqqlgg
qafacrcditseqelsaladfaisklgkvdilvnnaggggpkpfdmpmadfrrayelnvf
sffhlsqlvapemekngggviltitsmaaenkninmtsyasskaaashlvrnmafdlgek
nirvngiapgailtdalksvitpeieqkmlqhtpirrlgqpqdianaalflcspaaswvs
gqiltvsgggvqeln
>d1ahja_ 4.92.1.1.1 Nitrile hydratase alpha chain {(Rhodococcus sp. r312)}
enaapaqaavsdrawalfraldgkglvpdgyvegwkktfeedfsprrgaelvarawtdpe
frqllltdgtaavaqygylgpqgeyivavedtptlknvivcslcsctawpilglpptwyk
sfeyrarvvreprkvlsemgteiasdieirvydttaetrymvlpqrpagtegwsqeqlqe
ivtkdcligvaipqvptv
>d1ahjb_ 2.24.6.1.1 Nitrile hydratase beta chain {(Rhodococcus sp. r312)}
mdgvhdlagvqgfgkvphtvdadigptfhaewehlpyslmfagvaelgafsvdevryvve
rmeprhymmtpyyeryvigvatlmvekgiltqdeleslaggpfplsrpsesegrpapvet
ttfevgqrvrvrdeyvpghirmpaycrgrvgtishrttekwpfpdaighgrndageepty
hvkfaaeelfgsdtdggsvvvdlfegylepaa
>d1ahjc_ 4.92.1.1.1 Nitrile hydratase alpha chain {(Rhodococcus sp. r312)}
enaapaqaavsdrawalfraldgkglvpdgyvegwkktfeedfsprrgaelvarawtdpe
frqllltdgtaavaqygylgpqgeyivavedtptlknvivcslcsctawpilglpptwyk
sfeyrarvvreprkvlsemgteiasdieirvydttaetrymvlpqrpagtegwsqeqlqe
ivtkdcligvaipqvptv
>d1ahjd_ 2.24.6.1.1 Nitrile hydratase beta chain {(Rhodococcus sp. r312)}
mdgvhdlagvqgfgkvphtvdadigptfhaewehlpyslmfagvaelgafsvdevryvve
rmeprhymmtpyyeryvigvatlmvekgiltqdeleslaggpfplsrpsesegrpapvet
ttfevgqrvrvrdeyvpghirmpaycrgrvgtishrttekwpfpdaighgrndageepty
hvkfaaeelfgsdtdggsvvvdlfegylepaa
>d1ahje_ 4.92.1.1.1 Nitrile hydratase alpha chain {(Rhodococcus sp. r312)}
enaapaqaavsdrawalfraldgkglvpdgyvegwkktfeedfsprrgaelvarawtdpe
frqllltdgtaavaqygylgpqgeyivavedtptlknvivcslcsctawpilglpptwyk
sfeyrarvvreprkvlsemgteiasdieirvydttaetrymvlpqrpagtegwsqeqlqe
ivtkdcligvaipqvptv
>d1ahjf_ 2.24.6.1.1 Nitrile hydratase beta chain {(Rhodococcus sp. r312)}
mdgvhdlagvqgfgkvphtvdadigptfhaewehlpyslmfagvaelgafsvdevryvve
rmeprhymmtpyyeryvigvatlmvekgiltqdeleslaggpfplsrpsesegrpapvet
ttfevgqrvrvrdeyvpghirmpaycrgrvgtishrttekwpfpdaighgrndageepty
hvkfaaeelfgsdtdggsvvvdlfegylepaa
>d1ahjg_ 4.92.1.1.1 Nitrile hydratase alpha chain {(Rhodococcus sp. r312)}
enaapaqaavsdrawalfraldgkglvpdgyvegwkktfeedfsprrgaelvarawtdpe
frqllltdgtaavaqygylgpqgeyivavedtptlknvivcslcsctawpilglpptwyk
sfeyrarvvreprkvlsemgteiasdieirvydttaetrymvlpqrpagtegwsqeqlqe
ivtkdcligvaipqvptv
>d1ahjh_ 2.24.6.1.1 Nitrile hydratase beta chain {(Rhodococcus sp. r312)}
mdgvhdlagvqgfgkvphtvdadigptfhaewehlpyslmfagvaelgafsvdevryvve
rmeprhymmtpyyeryvigvatlmvekgiltqdeleslaggpfplsrpsesegrpapvet
ttfevgqrvrvrdeyvpghirmpaycrgrvgtishrttekwpfpdaighgrndageepty
hvkfaaeelfgsdtdggsvvvdlfegylepaa
>d1ahk__ 2.1.1.5.20 Major mite allergen Der f 2 {House-dust mite (Dermatophagoides farinae)}
dqvdvkdcanneikkvmvdgchgsdpciihrgkpftlealfdanqntktakieikasldg
leidvpgidtnachfvkcplvkgqqydikytwnvpkiapksenvvvtvkligdngvlaca
iathgkird
>d1ahl__ 7.8.1.1.6 Anthopleurin-A {Giant green sea anemone (Anthopleura xanthogrammica)}
gvsclcdsdgpsvrgntlsgtlwlypsgcpsgwhnckahgptigwcckq
>d1ahm__ 2.1.1.5.20 Major mite allergen Der f 2 {House-dust mite (Dermatophagoides farinae)}
dqvdvkdcanneikkvmvdgchgsdpciihrgkpftlealfdanqntktakieikasldg
leidvpgidtnachfvkcplvkgqqydikytwnvpkiapksenvvvtvkligdngvlaca
iathgkird
>d1ahn__ 3.14.4.1.5 Flavodoxin {(Escherichia coli)}
aitgiffgsdtgnteniakmiqkqlgkdvadvhdiaksskedleaydilllgiptwyyge
aqcdwddffptleeidfngklvalfgcgdqedyaeyfcdalgtirdiieprgativghwp
tagyhfeaskgladddhfvglaidedrqpeltaervekwvkqiseelhl
>d1aho__ 7.3.6.1.4 scorpion toxin {(Androctonus australius hector), toxin II}
vkdgyivddvnctyfcgrnaycneectklkgesgycqwaspygnacycyklpdhvrtkgp
grch
>d1ahpa_ 3.76.1.2.3 Maltodextrin phosphorylase (MALP) {(Escherichia coli)}
sqpifndkqfqealsrqwqryglnsaaemtprqwwlavsealaemlraqpfakpvanqrh
vnyismefligrltgnnllnlgwyqdvqdslkaydinltdlleeeidpalgagglgrlaa
cfldsmatvgqsatgyglnyqyglfrqsfvdgkqveapddwhrsnypwfrhnealdvqvg
iggavtkdgrwepeftitgqawdlpvvgyrngvaqplrlwqathahpfdltkfndgdflr
aeqqginaekltkvlypndnhtagkklrlmqqyfqcacsvadilrrhhlagrelhelady
eviqlndthptiaipellrvlidehqmswddawaitsktfaytnhtlmpealerwdvklv
kgllprhmqiineintrfktlvektwpgdekvwaklavvhdkqvhmanlcvvggfavngv
aalhsdlvvkdlfpeyhqlwpnkfhnvtngitprrwikqcnpalaalldkslqkewandl
dqlinlvkladdakfrdlyrvikqankvrlaefvkvrtgidinpqaifdiqikrlheykr
qhlnllrilalykeirenpqadrvprvflfgakaapgyylakniifainkvadvinndpl
vgdklkvvflpdycvsaaeklipaadiseqistagkeasgtgnmklalngaltvgtldga
nveiaekvgeenififghtvkqvkailakgydpvkwrkkdkvldavlkelesgkysdgdk
hafdqmlhsigkqggdpylvmadfaayveaqkqvdvlyrdqeawtraailntarcgmfss
drsirdyqariwqaar
>d1ahpb_ 3.76.1.2.3 Maltodextrin phosphorylase (MALP) {(Escherichia coli)}
sqpifndkqfqealsrqwqryglnsaaemtprqwwlavsealaemlraqpfakpvanqrh
vnyismefligrltgnnllnlgwyqdvqdslkaydinltdlleeeidpalgagglgrlaa
cfldsmatvgqsatgyglnyqyglfrqsfvdgkqveapddwhrsnypwfrhnealdvqvg
iggavtkdgrwepeftitgqawdlpvvgyrngvaqplrlwqathahpfdltkfndgdflr
aeqqginaekltkvlypndnhtagkklrlmqqyfqcacsvadilrrhhlagrelhelady
eviqlndthptiaipellrvlidehqmswddawaitsktfaytnhtlmpealerwdvklv
kgllprhmqiineintrfktlvektwpgdekvwaklavvhdkqvhmanlcvvggfavngv
aalhsdlvvkdlfpeyhqlwpnkfhnvtngitprrwikqcnpalaalldkslqkewandl
dqlinlvkladdakfrdlyrvikqankvrlaefvkvrtgidinpqaifdiqikrlheykr
qhlnllrilalykeirenpqadrvprvflfgakaapgyylakniifainkvadvinndpl
vgdklkvvflpdycvsaaeklipaadiseqistagkeasgtgnmklalngaltvgtldga
nveiaekvgeenififghtvkqvkailakgydpvkwrkkdkvldavlkelesgkysdgdk
hafdqmlhsigkqggdpylvmadfaayveaqkqvdvlyrdqeawtraailntarcgmfss
drsirdyqariwqaar
>d1ahq__ 4.62.1.2.2 Actophorin {amoeba (Acanthamoeba castellanii)}
giavsddcvqkfnelklghqhryvtfkmnasntevvvehvggpnatyedfksqlperdcr
yaifdyefqvdggqrnkitfilwapdsapikskmmytstkdsikkklvgiqvevqatdaa
eisedavserakk
>d1ahr__ 1.37.1.5.10 Calmodulin {chicken (gallus gallus)}
adqlteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgn
gtidfpefltmmarkmkdseeeireafrvfdkdgngfisaaelrhvmtnlgekltdeevd
emireadidgdgqvnyeefvtmmtsk
>d1ahsa_ 2.14.1.1.2 Virus coat protein vp7 (BTV-10 vp7), central (top) domain {(African horse sickness virus)}
tgpyagavevqqsgryyvpqgrtrggyinsniaevcmdagaagqvnallaprrgdavmiy
fvwrplrifcdpqgaslesapgtfvtvdgvnvaagdvvawntiapvnvgnpgarrsilqf
evlwyt
>d1ahsb_ 2.14.1.1.2 Virus coat protein vp7 (BTV-10 vp7), central (top) domain {(African horse sickness virus)}
tgpyagavevqqsgryyvpqgrtrggyinsniaevcmdagaagqvnallaprrgdavmiy
fvwrplrifcdpqgaslesapgtfvtvdgvnvaagdvvawntiapvnvgnpgarrsilqf
evlwyt
>d1ahsc_ 2.14.1.1.2 Virus coat protein vp7 (BTV-10 vp7), central (top) domain {(African horse sickness virus)}
tgpyagavevqqsgryyvpqgrtrggyinsniaevcmdagaagqvnallaprrgdavmiy
fvwrplrifcdpqgaslesapgtfvtvdgvnvaagdvvawntiapvnvgnpgarrsilqf
evlwyt
>e1aht.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1aht.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
eadcglrplfekksledkterellesyi
>d1ahua1 4.34.23.1.1 (274-560) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
rgyqsylitlpkdgdlkqavdiirplrlgmalqnvptirhilldaavlgdkrsyssrtep
lsdeeldkiakqlnlgrwnfygalygpepirrvlwetikdafsaipgvkfyfpedtpens
vlrvrdktmqgiptydelkwidwlpngahlffspiakvsgedammqyavtkkrcqeagld
figtftvgmremhhivcivfnkkdliqkrkvqwlmrtliddcaangwgeyrthlafmdqi
metynwnnssflrfnevlknavdpngiiapgksgvwpsqyshvtwkl
>d1ahua2 4.90.1.1.1 (6-273) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
efrpltlppklslsdfnefiqdiirivgsenvevisskdqivdgsymkpththdphhvmd
qdyflasaivaprnvadvqsivglankfsfplwpisigrnsgyggaaprvsgsvvldmgk
nmnrvlevnvegaycvvepgvtyhdlhnyleannlrdklwldvpdlgggsvlgnavergv
gytpygdhwmmhsgmevvlangellrtgmgalpdpkrpetmglkpedqpwskiahlfpyg
fgpyidglfsqsnmgivtkigiwlmpnp
>d1ahub1 4.34.23.1.1 (274-560) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
rgyqsylitlpkdgdlkqavdiirplrlgmalqnvptirhilldaavlgdkrsyssrtep
lsdeeldkiakqlnlgrwnfygalygpepirrvlwetikdafsaipgvkfyfpedtpens
vlrvrdktmqgiptydelkwidwlpngahlffspiakvsgedammqyavtkkrcqeagld
figtftvgmremhhivcivfnkkdliqkrkvqwlmrtliddcaangwgeyrthlafmdqi
metynwnnssflrfnevlknavdpngiiapgksgvwpsqyshvtwkl
>d1ahub2 4.90.1.1.1 (6-273) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
efrpltlppklslsdfnefiqdiirivgsenvevisskdqivdgsymkpththdphhvmd
qdyflasaivaprnvadvqsivglankfsfplwpisigrnsgyggaaprvsgsvvldmgk
nmnrvlevnvegaycvvepgvtyhdlhnyleannlrdklwldvpdlgggsvlgnavergv
gytpygdhwmmhsgmevvlangellrtgmgalpdpkrpetmglkpedqpwskiahlfpyg
fgpyidglfsqsnmgivtkigiwlmpnp
>d1ahva1 4.34.23.1.1 (274-560) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
rgyqsylitlpkdgdlkqavdiirplrlgmalqnvptirhilldaavlgdkrsyssrtep
lsdeeldkiakqlnlgrwnfygalygpepirrvlwetikdafsaipgvkfyfpedtpens
vlrvrdktmqgiptydelkwidwlpngahlffspiakvsgedammqyavtkkrcqeagld
figtftvgmremhhivcivfnkkdliqkrkvqwlmrtliddcaangwgeyrthlafmdqi
metynwnnssflrfnevlknavdpngiiapgksgvwpsqyshvtwkl
>d1ahva2 4.90.1.1.1 (6-273) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
efrpltlppklslsdfnefiqdiirivgsenvevisskdqivdgsymkpththdphhvmd
qdyflasaivaprnvadvqsivglankfsfplwpisigrnsgyggaaprvsgsvvldmgk
nmnrvlevnvegaycvvepgvtyhdlhnyleannlrdklwldvpdlgggsvlgnavergv
gytpygdhwmmhsgmevvlangellrtgmgalpdpkrpetmglkpedqpwskiahlfpyg
fgpyidglfsqsnmgivtkigiwlmpnp
>d1ahvb1 4.34.23.1.1 (274-560) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
rgyqsylitlpkdgdlkqavdiirplrlgmalqnvptirhilldaavlgdkrsyssrtep
lsdeeldkiakqlnlgrwnfygalygpepirrvlwetikdafsaipgvkfyfpedtpens
vlrvrdktmqgiptydelkwidwlpngahlffspiakvsgedammqyavtkkrcqeagld
figtftvgmremhhivcivfnkkdliqkrkvqwlmrtliddcaangwgeyrthlafmdqi
metynwnnssflrfnevlknavdpngiiapgksgvwpsqyshvtwkl
>d1ahvb2 4.90.1.1.1 (6-273) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
efrpltlppklslsdfnefiqdiirivgsenvevisskdqivdgsymkpththdphhvmd
qdyflasaivaprnvadvqsivglankfsfplwpisigrnsgyggaaprvsgsvvldmgk
nmnrvlevnvegaycvvepgvtyhdlhnyleannlrdklwldvpdlgggsvlgnavergv
gytpygdhwmmhsgmevvlangellrtgmgalpdpkrpetmglkpedqpwskiahlfpyg
fgpyidglfsqsnmgivtkigiwlmpnp
>d1ahwa1 2.1.1.1.95 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
dikmtqspssmyaslgervtitckasqdirkylnwyqqkpwkspktliyyatsladgvps
rfsgsgsgqdysltisslesddtatyyclqhgespytfgggtkleinr
>d1ahwa2 2.1.1.2.95 (109-214) Immunoglobulin (constant domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1ahwb1 2.1.1.1.95 (1-117) Immunoglobulin (variable domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
eiqlqqsgaelvrpgalvklsckasgfnikdyymhwvkqrpeqglewiglidpengntiy
dpkfqgkasitadtssntaylqlssltsedtavyycardnsyyfdywgqgttltvss
>d1ahwb2 2.1.1.2.95 (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 2.1.1.1.95 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
dikmtqspssmyaslgervtitckasqdirkylnwyqqkpwkspktliyyatsladgvps
rfsgsgsgqdysltisslesddtatyyclqhgespytfgggtkleinr
>d1ahwd2 2.1.1.2.95 (109-214) Immunoglobulin (constant domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1ahwe1 2.1.1.1.95 (1-117) Immunoglobulin (variable domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
eiqlqqsgaelvrpgalvklsckasgfnikdyymhwvkqrpeqglewiglidpengntiy
dpkfqgkasitadtssntaylqlssltsedtavyycardnsyyfdywgqgttltvss
>d1ahwe2 2.1.1.2.95 (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_ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgiglyydetgkipvltsvkkaeqyllene
ttklylgidgipefgrctqellfgkgsalindkrartaqtpggsgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanyssppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ahxb_ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgiglyydetgkipvltsvkkaeqyllene
ttklylgidgipefgrctqellfgkgsalindkrartaqtpggsgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanyssppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ahya_ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgiglyydetgkipvltsvkkaeqyllene
ttklylgidgipefgrctqellfgkgsalindkrartaqtpggsgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanyssppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ahyb_ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgiglyydetgkipvltsvkkaeqyllene
ttklylgidgipefgrctqellfgkgsalindkrartaqtpggsgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanyssppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ahza1 4.34.23.1.1 (274-560) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
rgyqsylitlpkdgdlkqavdiirplrlgmalqnvptirhilldaavlgdkrsyssrtep
lsdeeldkiakqlnlgrwnfygalygpepirrvlwetikdafsaipgvkfyfpedtpens
vlrvrdktmqgiptydelkwidwlpngahlffspiakvsgedammqyavtkkrcqeagld
figtftvgmremhhivcivfnkkdliqkrkvqwlmrtliddcaangwgeyrthlafmdqi
metynwnnssflrfnevlknavdpngiiapgksgvwpsqyshvtwkl
>d1ahza2 4.90.1.1.1 (6-273) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
efrpltlppklslsdfnefiqdiirivgsenvevisskdqivdgsymkpththdphhvmd
qdyflasaivaprnvadvqsivglankfsfplwpisigrnsgyggaaprvsgsvvldmgk
nmnrvlevnvegaycvvepgvtyhdlhnyleannlrdklwldvpdlgggsvlgnavergv
gytpygdhwmmhsgmevvlangellrtgmgalpdpkrpetmglkpedqpwskiahlfpyg
fgpyidglfsqsnmgivtkigiwlmpnp
>d1ahzb1 4.34.23.1.1 (274-560) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
rgyqsylitlpkdgdlkqavdiirplrlgmalqnvptirhilldaavlgdkrsyssrtep
lsdeeldkiakqlnlgrwnfygalygpepirrvlwetikdafsaipgvkfyfpedtpens
vlrvrdktmqgiptydelkwidwlpngahlffspiakvsgedammqyavtkkrcqeagld
figtftvgmremhhivcivfnkkdliqkrkvqwlmrtliddcaangwgeyrthlafmdqi
metynwnnssflrfnevlknavdpngiiapgksgvwpsqyshvtwkl
>d1ahzb2 4.90.1.1.1 (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 2.1.1.1.28 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab 59.1 (mouse), kappa L chain}
qvklqesgpavikpsqslsltcivsgfsitrtnycwhwirqapgkglewmgricyegsiy
yspsiksrstisrdtslnkffiqlisvtnedtamyycsrenhmyetyfdvwgqgttvtvs
>d1ai1h2 2.1.1.2.36 (113-226) Immunoglobulin (constant domains of L and H chains) {Fab 59.1 (mouse), kappa L chain}
sakttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqs
dlytlsssvtvpssprpsetvtcnvahpasstkvdkkivpr
>d1ai1l1 2.1.1.1.28 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab 59.1 (mouse), kappa L chain}
divmtqspaslvvslgqratiscrasesvdsygksfmhwyqqkpgqppkvliyiasnles
gvparfsgsgsrtdftltidpveaddaatyycqqnnedpptfgagtklemrr
>d1ai1l2 2.1.1.2.36 (109-211) Immunoglobulin (constant domains of L and H chains) {Fab 59.1 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1ai2__ 3.65.1.1.5 Isocitrate dehydrogenase {(Escherichia coli)}
skvvvpaqgkkitlqngklnvpenpiipyiegdgigvdvtpamlkvvdaavekaykgerk
iswmeiytgekstqvygqdvwlpaetldlireyrvaikgplttpvgggirslnvalrqel
dlyiclrpvryyqgtpspvkhpeltdmvifrensediyagiewkadsadaekvikflree
mgvkkirfpehcgigikpcseegtkrlvraaieyaiandrdsvtlvhkgnimkftegafk
dwgyqlareefggelidggpwlkvknpntgkeivikdviadaflqqillrpaeydviacm
nlngdyisdalaaqvggigiapganigdecalfeathgtapkyagqdkvnpgsiilsaem
mlrhmgwteaadlivkgmegainaktvtydferlmdgakllkcsefgdaiienm
>d1ai3__ 3.65.1.1.5 Isocitrate dehydrogenase {(Escherichia coli)}
skvvvpaqgkkitlqngklnvpenpiipyiegdgigvdvtpamlkvvdaavekaykgerk
iswmeiytgekstqvygqdvwlpaetldlireyrvaikgplttpvgggirslnvalrqel
dlyiclrpvryyqgtpspvkhpeltdmvifrensediyagiewkadsadaekvikflree
mgvkkirfpehcgigikpcseegtkrlvraaieyaiandrdsvtlvhkgnimkftegafk
dwgyqlareefggelidggpwlkvknpntgkeivikdviadaflqqillrpaeydviacm
nlngdyisdalaaqvggigiapganigdecalfeathgtapkyagqdkvnpgsiilsaem
mlrhmgwteaadlivkgmegainaktvtydferlmdgakllkcsefgdaiienm
>e1ai4.1a 4.95.1.2.1 Penicillin acylase, catalytic domain {(Escherichia coli)}
ssseikivrdeygmphiyandtwhlfygygyvvaqdrlfqmemarrstqgtvaevlgkdf
vkfdkdirrnywpdairaqiaalspedmsilqgyadgmnawidkvntnpetllpkqfntf
gftpkrwepfdvamifvgtmanrfsdstseidnlalltalkdkygvsqgmavfnqlkwlv
npsapttiavqesnyplkfnqqnsqt
>e1ai4.1b 4.95.1.2.1 Penicillin acylase, catalytic domain {(Escherichia coli)}
snmwvigkskaqdakaimvngpqfgwyapaytygiglhgagydvtgntpfaypglvfghn
gviswgstagfgddvdifaerlsaekpgyylhngkwvkmlsreetitvkngqaetftvwr
tvhgnilqtdqttqtayaksrawdgkevasllawthqmkaknwqqwtqqaakqaltinwy
yadvngnigyvhtgaypdrqsghdprlpvpgtgkwdwkgllpfemnpkvynpqsgyianw
nnspqkdypasdlfaflwggadrvteidrlleqkprltadqawdvirqtsrqdlnlrlfl
ptlqaatsgltqsdprrqlvetltrwdginllnddgktwqqpgsailnvwltsmlkrtvv
aavpmpfdkwysasgyettqdgptgslnisvgakilyeavqgdkspipqavdlfagkpqq
evvlaaledtwetlskrygnnvsnwktpamaltfrannffgvpqaaaeetrhqaeyqnrg
tendmivfspttsdrpvlawdvvapgqsgfiapdgtvdkhyedqlkmyenfgrkslwltk
qdveahkesqevlhvqr
>e1ai5.1a 4.95.1.2.1 Penicillin acylase, catalytic domain {(Escherichia coli)}
ssseikivrdeygmphiyandtwhlfygygyvvaqdrlfqmemarrstqgtvaevlgkdf
vkfdkdirrnywpdairaqiaalspedmsilqgyadgmnawidkvntnpetllpkqfntf
gftpkrwepfdvamifvgtmanrfsdstseidnlalltalkdkygvsqgmavfnqlkwlv
npsapttiavqesnyplkfnqqnsqt
>e1ai5.1b 4.95.1.2.1 Penicillin acylase, catalytic domain {(Escherichia coli)}
snmwvigkskaqdakaimvngpqfgwyapaytygiglhgagydvtgntpfaypglvfghn
gviswgstagfgddvdifaerlsaekpgyylhngkwvkmlsreetitvkngqaetftvwr
tvhgnilqtdqttqtayaksrawdgkevasllawthqmkaknwqqwtqqaakqaltinwy
yadvngnigyvhtgaypdrqsghdprlpvpgtgkwdwkgllpfemnpkvynpqsgyianw
nnspqkdypasdlfaflwggadrvteidrlleqkprltadqawdvirqtsrqdlnlrlfl
ptlqaatsgltqsdprrqlvetltrwdginllnddgktwqqpgsailnvwltsmlkrtvv
aavpmpfdkwysasgyettqdgptgslnisvgakilyeavqgdkspipqavdlfagkpqq
evvlaaledtwetlskrygnnvsnwktpamaltfrannffgvpqaaaeetrhqaeyqnrg
tendmivfspttsdrpvlawdvvapgqsgfiapdgtvdkhyedqlkmyenfgrkslwltk
qdveahkesqevlhvqr
>e1ai6.1a 4.95.1.2.1 Penicillin acylase, catalytic domain {(Escherichia coli)}
ssseikivrdeygmphiyandtwhlfygygyvvaqdrlfqmemarrstqgtvaevlgkdf
vkfdkdirrnywpdairaqiaalspedmsilqgyadgmnawidkvntnpetllpkqfntf
gftpkrwepfdvamifvgtmanrfsdstseidnlalltalkdkygvsqgmavfnqlkwlv
npsapttiavqesny
>e1ai6.1b 4.95.1.2.1 Penicillin acylase, catalytic domain {(Escherichia coli)}
snmwvigkskaqdakaimvngpqfgwyapaytygiglhgagydvtgntpfaypglvfghn
gviswgstagfgddvdifaerlsaekpgyylhngkwvkmlsreetitvkngqaetftvwr
tvhgnilqtdqttqtayaksrawdgkevasllawthqmkaknwqqwtqqaakqaltinwy
yadvngnigyvhtgaypdrqsghdprlpvpgtgkwdwkgllpfemnpkvynpqsgyianw
nnspqkdypasdlfaflwggadrvteidrlleqkprltadqawdvirqtsrqdlnlrlfl
ptlqaatsgltqsdprrqlvetltrwdginllnddgktwqqpgsailnvwltsmlkrtvv
aavpmpfdkwysasgyettqdgptgslnisvgakilyeavqgdkspipqavdlfagkpqq
evvlaaledtwetlskrygnnvsnwktpamaltfrannffgvpqaaaeetrhqaeyqnrg
tendmivfspttsdrpvlawdvvapgqsgfiapdgtvdkhyedqlkmyenfgrkslwltk
qdveahkesqevlhvqr
>e1ai7.1a 4.95.1.2.1 Penicillin acylase, catalytic domain {(Escherichia coli)}
ssseikivrdeygmphiyandtwhlfygygyvvaqdrlfqmemarrstqgtvaevlgkdf
vkfdkdirrnywpdairaqiaalspedmsilqgyadgmnawidkvntnpetllpkqfntf
gftpkrwepfdvamifvgtmanrfsdstseidnlalltalkdkygvsqgmavfnqlkwlv
npsapttiavqesnyplkfnqqnsqt
>e1ai7.1b 4.95.1.2.1 Penicillin acylase, catalytic domain {(Escherichia coli)}
snmwvigkskaqdakaimvngpqfgwyapaytygiglhgagydvtgntpfaypglvfghn
gviswgstagfgddvdifaerlsaekpgyylhngkwvkmlsreetitvkngqaetftvwr
tvhgnilqtdqttqtayaksrawdgkevasllawthqmkaknwqqwtqqaakqaltinwy
yadvngnigyvhtgaypdrqsghdprlpvpgtgkwdwkgllpfemnpkvynpqsgyianw
nnspqkdypasdlfaflwggadrvteidrlleqkprltadqawdvirqtsrqdlnlrlfl
ptlqaatsgltqsdprrqlvetltrwdginllnddgktwqqpgsailnvwltsmlkrtvv
aavpmpfdkwysasgyettqdgptgslnisvgakilyeavqgdkspipqavdlfagkpqq
evvlaaledtwetlskrygnnvsnwktpamaltfrannffgvpqaaaeetrhqaeyqnrg
tendmivfspttsdrpvlawdvvapgqsgfiapdgtvdkhyedqlkmyenfgrkslwltk
qdveahkesqevlhvqr
>e1ai8.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqf
>e1ai8.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
adcglrplfekksledkterellesyi
>d1ai9a_ 3.60.1.1.7 Dihydrofolate reductases, eukaryotic type {yeast (Candida albicans)}
mlkpnvaiivaalkpalgigykgkmpwrlrkeiryfkdvttrttkpntrnavimgrktwe
sipqkfrplpdrlniilsrsyeneiiddniihassiesslnlvsdvervfiiggaeiyne
linnslvshlliteiehpspesiemdtflkfpleswtkqpkselqkfvgdtvleddikeg
dftynytlwtrk
>d1ai9b_ 3.60.1.1.7 Dihydrofolate reductases, eukaryotic type {yeast (Candida albicans)}
mlkpnvaiivaalkpalgigykgkmpwrlrkeiryfkdvttrttkpntrnavimgrktwe
sipqkfrplpdrlniilsrsyeneiiddniihassiesslnlvsdvervfiiggaeiyne
linnslvshlliteiehpspesiemdtflkfpleswtkqpkselqkfvgdtvleddikeg
dftynytlwtrk
>d1aiaa_ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assyshnfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aiab_ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assyshnfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aiba_ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assyshnfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aibb_ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assyshnfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aica_ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assyshnfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aicb_ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assyshnfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aida_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtiriggqlkealldtgaddtvleemnlpgkwkpkmiggiggfikvrqyd
qipveicghkaigtvlvgptpvniigrnlltqigctlnf
>d1aidb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtiriggqlkealldtgaddtvleemnlpgkwkpkmiggiggfikvrqyd
qipveicghkaigtvlvgptpvniigrnlltqigctlnf
>d1aie__ 1.49.1.1.1 p53 tetramerization domain {human (Homo sapiens)}
eyftlqirgrerfemfrelnealelkdaqag
>d1aifa1 2.1.1.1.62 (1-109) Immunoglobulin (variable domains of L and H chains) {Fab 409.5.3 (mouse), kappa L chain}
diqltqspafmaaspgekvtitcsvsssisssnlhwyqqksetspkpwiygtsnlasgvp
vrfsgsgsgtsysltissmeaedaatyycqqwnsypytfgggtkleikr
>d1aifa2 2.1.1.2.66 (110-215) Immunoglobulin (constant domains of L and H chains) {Fab 409.5.3 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1aifb1 2.1.1.1.62 (1-121) Immunoglobulin (variable domains of L and H chains) {Fab 409.5.3 (mouse), kappa L chain}
evklqesggglvqpggsmklscvasgftfnnywmswvrqspekglewvaeirlnsdnfat
hyaesvkgkfiisrddsksrlylqmnslraedtgiyycvlrplfyyavdywgqgtsvtvs
s
>d1aifb2 2.1.1.2.66 (122-218) Immunoglobulin (constant domains of L and H chains) {Fab 409.5.3 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpstwrpsetvtcnvahpasstkvdkki
>d1aifh1 2.1.1.1.62 (1-121) Immunoglobulin (variable domains of L and H chains) {Fab 409.5.3 (mouse), kappa L chain}
evklqesggglvqpggsmklscvasgftfnnywmswvrqspekglewvaeirlnsdnfat
hyaesvkgkfiisrddsksrlylqmnslraedtgiyycvlrplfyyavdywgqgtsvtvs
s
>d1aifh2 2.1.1.2.66 (122-218) Immunoglobulin (constant domains of L and H chains) {Fab 409.5.3 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpstwrpsetvtcnvahpasstkvdkki
>d1aifl1 2.1.1.1.62 (1-109) Immunoglobulin (variable domains of L and H chains) {Fab 409.5.3 (mouse), kappa L chain}
diqltqspafmaaspgekvtitcsvsssisssnlhwyqqksetspkpwiygtsnlasgvp
vrfsgsgsgtsysltissmeaedaatyycqqwnsypytfgggtkleikr
>d1aifl2 2.1.1.2.66 (110-215) Immunoglobulin (constant domains of L and H chains) {Fab 409.5.3 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1aigh1 2.30.1.1.2 (36-258) Photosynthetic reaction centre {(Rhodobacter sphaeroides)}
mregyplenedgtpaanqgpfplpkpktfilphgrgtltvpgpesedrpialartavseg
fphaptgdpmkdgvgpaswvarrdlpeldghghnkikpmkaaagfhvsagknpiglpvrg
cdleiagkvvdiwvdipeqmarflevelkdgstrllpmqmvkvqsnrvhvnalssdlfag
iptiksptevtlleedkicgyvagglmyaapkrksvvaamlae
>d1aigh2 6.5.1.1.2 (11-35) Photosynthetic reaction centre, L-, M- and H-chains {(rhodobacter sphaeroides )}
dlaslaiysfwiflagliyylqten
>d1aigp1 2.30.1.1.2 (36-258) Photosynthetic reaction centre {(Rhodobacter sphaeroides)}
mregyplenedgtpaanqgpfplpkpktfilphgrgtltvpgpesedrpialartavseg
fphaptgdpmkdgvgpaswvarrdlpeldghghnkikpmkaaagfhvsagknpiglpvrg
cdleiagkvvdiwvdipeqmarflevelkdgstrllpmqmvkvqsnrvhvnalssdlfag
iptiksptevtlleedkicgyvagglmyaapkrksvvaamlae
>d1aigp2 6.5.1.1.2 (11-35) Photosynthetic reaction centre, L-, M- and H-chains {(rhodobacter sphaeroides )}
dlaslaiysfwiflagliyylqten
>d1aiha_ 4.101.1.1.1 Integrase {(Bacteriophage HP1)}
etelaflyerdiyrllaecdnsrnpdlglivriclatgarwseaetltqsqvmpykitft
ntkskknrtvpisdelfdmlpkkrgrlfndayesfenavlraeielpkgqlthvlrhtfa
shfmmnggnilvlkeilghstiemtmryahfapshlesavkfnplsnpaq
>d1aihb_ 4.101.1.1.1 Integrase {(Bacteriophage HP1)}
elaflyerdiyrllaecdnsrnpdlglivriclatgarwseaetltqsqvmpykitftnt
kskknrtvpisdelfdmlpkkrgrlfndayesfenavlraeielpkgqlthvlrhtfash
fmmnggnilvlkeilghstiemtmryahfapshlesavkfnplsnpaq
>d1aihc_ 4.101.1.1.1 Integrase {(Bacteriophage HP1)}
elaflyerdiyrllaecdnsrnpdlglivriclatgarwseaetltqsqvmpykitftnt
kskknrtvpisdelfdmlpkkrgrlfndayesfenavlraeielpkgqlthvlrhtfash
fmmnggnilvlkeilghstiemtmryahfapshlesavkfnplsnpaq
>d1aihd_ 4.101.1.1.1 Integrase {(Bacteriophage HP1)}
etelaflyerdiyrllaecdnsrnpdlglivriclatgarwseaetltqsqvmpykitft
ntkskknrtvpisdelfdmlpkkrgrlfndayesfenavlraeielpkgqlthvlrhtfa
shfmmnggnilvlkeilghstiemtmryahfapshlesavkfnplsnpaq
>d1aii__ 1.55.1.1.2 Annexin III {human (Homo sapiens)}
asiwvghrgtvrdypdfspsvdaeaiqkairgigtdekmlisiltersnaqrqlivkeyq
aaygkelkddlkgdlsghfehlmvalvtppavfdakqlkksmkgagtnedalieilttrt
srqmkdisqayytvykkslgddissetsgdfrkalltladgrrdeslkvdehlakqdaqi
lykagenrwgtdedkfteilclrsfpqlkltfdeyrnisqkdivdsikgelsghfedlll
aivncvrntpaflaerlhralkgigtdeftlnrimvsrseidlldirtefkkhygyslys
aiksdtsgdyeitllkicggdd
>d1aijh1 2.30.1.1.2 (36-256) Photosynthetic reaction centre {(Rhodobacter sphaeroides)}
mregyplenedgtpaanqgpfplpkpktfilphgrgtltvpgpesedrpialartavseg
fphaptgdpmkdgvgpaswvarrdlpeldghghnkikpmkaaagfhvsagknpiglpvrg
cdleiagkvvdiwvdipeqmarflevelkdgstrllpmqmvkvqsnrvhvnalssdlfag
iptiksptevtlleedkicgyvagglmyaapkrksvvaaml
>d1aijh2 6.5.1.1.2 (11-35) Photosynthetic reaction centre, L-, M- and H-chains {(rhodobacter sphaeroides )}
dlaslaiysfwiflagliyylqten
>d1aijt1 2.30.1.1.2 (36-256) Photosynthetic reaction centre {(Rhodobacter sphaeroides)}
mregyplenedgtpaanqgpfplpkpktfilphgrgtltvpgpesedrpialartavseg
fphaptgdpmkdgvgpaswvarrdlpeldghghnkikpmkaaagfhvsagknpiglpvrg
cdleiagkvvdiwvdipeqmarflevelkdgstrllpmqmvkvqsnrvhvnalssdlfag
iptiksptevtlleedkicgyvagglmyaapkrksvvaaml
>d1aijt2 6.5.1.1.2 (11-35) Photosynthetic reaction centre, L-, M- and H-chains {(rhodobacter sphaeroides )}
dlaslaiysfwiflagliyylqten
>e1aik.1c 6.2.2.1.1 HIV-1 gp41 protease-resistant core {(human immunodeficiency virus type 1)}
wmewdreinnytslihslieesqnqqekneqell
>e1aik.1n 6.2.2.1.1 HIV-1 gp41 protease-resistant core {(human immunodeficiency virus type 1)}
sgivqqqnnllraieaqqhllqltvwgikqlqaril
>d1ail__ 1.15.1.1.1 N-terminal, RNA-binding domain of nonstructural protein NS1 {(Influenza A virus)}
mdsntvssfqvdcflwhvrkqvvdqelgdapfldrlrrdqkslrgrgstlglnieaathv
gkqivekilk
>d1aim__ 4.3.1.1.10 Cruzain {(Trypanosoma cruzi)}
apaavdwrargavtavkdqgqcgscwafsaignvecqwflaghpltnlseqmlvscdktd
sgcsgglmnnafewivqenngavytedsypyasgegisppcttsghtvgatitghvelpq
deaqiaawlavngpvavavdasswmtytggvmtscvsealdhgvllvgyndsaavpywii
knswttqwgeegyiriakgsnqclvkeeassavvg
>d1ain__ 1.55.1.1.1 Annexin I {human (Homo sapiens)}
gsavspyptfnpssdvaalhkaimvkgvdeatiidiltkrnnaqrqqikaaylqetgkpl
detlkkaltghleevvlallktpaqfdadelraamkglgtdedtlieilasrtnkeirdi
nrvyreelkrdlakditsdtsgdfrnallslakgdrsedfgvnedladsdaralyeager
rkgtdvnvfntilttrsypqlrrvfqkytkyskhdmnkvldlelkgdiekcltaivkcat
skpaffaeklhqamkgvgtrhkalirimvsrseidmndikafyqkmygislcqaildetk
gdyekilvalcggn
>d1aipa1 2.32.3.1.3 (213-312) Elongation factor Tu (EF-Tu), domain 2 {(Thermus thermophilus)}
pvrdvdkpflmpvedvftitgrgtvatgriergkvkvgdeveivglapetrrtvvtgvem
hrktlqegiagdnvgvllrgvsreevergqvlakpgsitp
>d1aipa2 2.33.1.1.3 (313-405) Elongation factor Tu (EF-Tu), the C-terminal domain {(Thermus thermophilus)}
htkfeasvyvlkkeeggrhtgffsgyrpqfyfrttdvtgvvqlppgvemvmpgdnvtftv
elikpvaleeglrfaireggrtvgagvvtkile
>d1aipa3 3.29.1.4.15 (9-212) Elongation factor Tu (EF-Tu), the N-terminal (G) domain {(Thermus thermophilus)}
kphvnvgtighvdhgkttltaaltyvtaaenpnvevkdygdidkapeerargitintahv
eyetakrhyshvdcpghadyiknmitgaaqmdgailvvsaadgpmpqtrehillarqvgv
pyivvfmnkvdmvddpelldlvemevrdllnqyefpgdevpvirgsallaleqmhrnpkt
rrgenewvdkiwelldaideyipt
>d1aipb1 2.32.3.1.3 (213-312) Elongation factor Tu (EF-Tu), domain 2 {(Thermus thermophilus)}
pvrdvdkpflmpvedvftitgrgtvatgriergkvkvgdeveivglapetrrtvvtgvem
hrktlqegiagdnvgvllrgvsreevergqvlakpgsitp
>d1aipb2 2.33.1.1.3 (313-405) Elongation factor Tu (EF-Tu), the C-terminal domain {(Thermus thermophilus)}
htkfeasvyvlkkeeggrhtgffsgyrpqfyfrttdvtgvvqlppgvemvmpgdnvtftv
elikpvaleeglrfaireggrtvgagvvtkile
>d1aipb3 3.29.1.4.15 (9-212) Elongation factor Tu (EF-Tu), the N-terminal (G) domain {(Thermus thermophilus)}
kphvnvgtighvdhgkttltaaltyvtaaenpnvevkdygdidkapeerargitintahv
eyetakrhyshvdcpghadyiknmitgaaqmdgailvvsaadgpmpqtrehillarqvgv
pyivvfmnkvdmvddpelldlvemevrdllnqyefpgdevpvirgsallaleqmhrnpkt
rrgenewvdkiwelldaideyipt
>d1aipc_ 4.25.1.1.2 Elongation factor Ts (EF-Ts), dimerisation domain {(Thermus termophilus)}
sqmelikklreatgagmmdvkraledagwdeekavqllrergamkaakkadrearegiig
hyihhnqrvgvlvelncetdfvarnelfqnlakdlamhiammnpryvsaeeipaeeleke
rqiyiqaalnegkpqqiaekiaegrlkkyleevvlleqpfvkddkvkvkeliqqaiakig
enivvrrfcrfelga
>d1aipd_ 4.25.1.1.2 Elongation factor Ts (EF-Ts), dimerisation domain {(Thermus termophilus)}
sqmelikklreatgagmmdvkraledagwdeekavqllrergamkaakkadrearegiig
hyihhnqrvgvlvelncetdfvarnelfqnlakdlamhiammnpryvsaeeipaeeleke
rqiyiqaalnegkpqqiaekiaegrlkkyleevvlleqpfvkddkvkvkeliqqaiakig
enivvrrfcrfelga
>d1aipe1 2.32.3.1.3 (213-312) Elongation factor Tu (EF-Tu), domain 2 {(Thermus thermophilus)}
pvrdvdkpflmpvedvftitgrgtvatgriergkvkvgdeveivglapetrrtvvtgvem
hrktlqegiagdnvgvllrgvsreevergqvlakpgsitp
>d1aipe2 2.33.1.1.3 (313-405) Elongation factor Tu (EF-Tu), the C-terminal domain {(Thermus thermophilus)}
htkfeasvyvlkkeeggrhtgffsgyrpqfyfrttdvtgvvqlppgvemvmpgdnvtftv
elikpvaleeglrfaireggrtvgagvvtkile
>d1aipe3 3.29.1.4.15 (9-212) Elongation factor Tu (EF-Tu), the N-terminal (G) domain {(Thermus thermophilus)}
kphvnvgtighvdhgkttltaaltyvtaaenpnvevkdygdidkapeerargitintahv
eyetakrhyshvdcpghadyiknmitgaaqmdgailvvsaadgpmpqtrehillarqvgv
pyivvfmnkvdmvddpelldlvemevrdllnqyefpgdevpvirgsallaleqmhrnpkt
rrgenewvdkiwelldaideyipt
>d1aipf1 2.32.3.1.3 (213-312) Elongation factor Tu (EF-Tu), domain 2 {(Thermus thermophilus)}
pvrdvdkpflmpvedvftitgrgtvatgriergkvkvgdeveivglapetrrtvvtgvem
hrktlqegiagdnvgvllrgvsreevergqvlakpgsitp
>d1aipf2 2.33.1.1.3 (313-405) Elongation factor Tu (EF-Tu), the C-terminal domain {(Thermus thermophilus)}
htkfeasvyvlkkeeggrhtgffsgyrpqfyfrttdvtgvvqlppgvemvmpgdnvtftv
elikpvaleeglrfaireggrtvgagvvtkile
>d1aipf3 3.29.1.4.15 (9-212) Elongation factor Tu (EF-Tu), the N-terminal (G) domain {(Thermus thermophilus)}
kphvnvgtighvdhgkttltaaltyvtaaenpnvevkdygdidkapeerargitintahv
eyetakrhyshvdcpghadyiknmitgaaqmdgailvvsaadgpmpqtrehillarqvgv
pyivvfmnkvdmvddpelldlvemevrdllnqyefpgdevpvirgsallaleqmhrnpkt
rrgenewvdkiwelldaideyipt
>d1aipg_ 4.25.1.1.2 Elongation factor Ts (EF-Ts), dimerisation domain {(Thermus termophilus)}
sqmelikklreatgagmmdvkraledagwdeekavqllrergamkaakkadrearegiig
hyihhnqrvgvlvelncetdfvarnelfqnlakdlamhiammnpryvsaeeipaeeleke
rqiyiqaalnegkpqqiaekiaegrlkkyleevvlleqpfvkddkvkvkeliqqaiakig
enivvrrfcrfelga
>d1aiph_ 4.25.1.1.2 Elongation factor Ts (EF-Ts), dimerisation domain {(Thermus termophilus)}
qmelikklreatgagmmdvkraledagwdeekavqllrergamkaakkadrearegiigh
yihhnqrvgvlvelncetdfvarnelfqnlakdlamhiammnpryvsaeeipaeeleker
qiyiqaalnegkpqqiaekiaegrlkkyleevvlleqpfvkddkvkvkeliqqaiakige
nivvrrfcrfelga
>d1aiqa_ 4.67.1.1.1 Thymidylate synthase {(Escherichia coli)}
kqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihellw
flqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlkn
dpdseriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfniasy
allvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesifd
yrfedfeiegydphpgikapvai
>d1aiqb_ 4.67.1.1.1 Thymidylate synthase {(Escherichia coli)}
kqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihellw
flqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlkn
dpdseriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfniasy
allvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesifd
yrfedfeiegydphpgikapvai
>d1air__ 2.62.1.1.1 Pectate lyase {(Erwinia chrysanthemi) type C}
atdtggyaataggnvtgavsktatsmqdivniidaarldangkkvkggayplvitytgne
dslinaaaanicgqwskdprgveikeftkgitiigangssanfgiwikkssdvvvqnmri
gylpggakdgdmirvddspnvwvdhnelfaanhecdgtpdndttfesavdikgasntvtv
synyihgvkkvgldgssssdtgrnityhhnyyndvnarlplqrgglvhaynnlytnitgs
glnvrqngqaliennwfekainpvtsrydgknfgtwvlkgnnitkpadfstysitwtadt
kpyvnadswtstgtfptvaynyspvsaqcvkdklpgyagvgknlatltstac
>d1aisa1 4.79.1.1.4 (1-92) TATA-box binding protein (TBP), C-terminal domain {(Pyrococcus woesei)}
mvdmskvklrienivasvdlfaqldlekvldlcpnskynpeefpgiichlddpkvallif
ssgklvvtgaksvqdieravaklaqklksigv
>d1aisa2 4.79.1.1.4 (93-181) TATA-box binding protein (TBP), C-terminal domain {(Pyrococcus woesei)}
kfkrapqidvqnmvfsgdigrefnldvvaltlpnceyepeqfpgviyrvkepksvillfs
sgkivcsgakseadaweavrkllreldky
>d1aisb1 1.63.1.2.2 (1108-1205) Transcription factor IIB (TFIIB), the core domain {(Pyrococcus woesei)}
nlafalseldritaqlklprhveeeaarlyreavrkglirgrsiesvmaacvyaacrllk
vprtldeiadiarvdkkeigrsyrfiarnlnltpkklf
>d1aisb2 1.63.1.2.2 (1206-1300) Transcription factor IIB (TFIIB), the core domain {(Pyrococcus woesei)}
vkptdyvnkfadelglsekvrrraieildeaykrgltsgkspaglvaaalyiasllegek
rtqrevaevarvtevtvrnrykelveklkikvpia
>d1aiu__ 3.38.1.1.4 Thioredoxin {human (Homo sapiens)}
mvkqiesktafqealdaagdklvvvdfsatwcgpckmikpffhslsekysnviflevdvn
dcqdvasecevkcmptfqffkkgqkvgefsgankekleatinelv
>d1aiv_1 3.82.1.2.4 (1-334) Ovotransferrin {Chicken (Gallus gallus)}
appksvirwctisspeekkcnnlrdltqqerisltcvqkatyldcikaianneadaisld
ggqafeaglapyklkpiaaevyehtegsttsyyavavvkkgteftvndlqgktschtglg
rsagwnipigtllhrgaiewegiesgsveqavakffsascvpgatieqklcrqckgdpkt
kcarnapysgysgafhclkdgkgdvafvkhttvnenapdqkdeyellcldgsrqpvdnyk
tcnwarvaahavvarddnkvediwsflskaqsdfgvdtksdfhlfgppgkkdpvlkdllf
kdsaimlkrvpslmdsqlylgfeyysaiqsmrkd
>d1aiv_2 3.82.1.2.4 (335-686) Ovotransferrin {Chicken (Gallus gallus)}
qltpsprenriqwcavgkdekskcdrwsvvsngdvectvvdetkdciikimkgeadaval
dgglvytagvcglvpvmaeryddesqcsktderpasyfavavarkdsnvnwnnlkgkksc
htavgrtagwvipmglihnrtgtcnfdeyfsegcapgsppnsrlcqlcqgsggippekcv
asshekyfgytgalrclvekgdvafiqhstveentggknkadwaknlqmddfellctdgr
ranvmdyrecnlaevpthavvvrpekankirdllerqekrfgvngsekskfmmfesqnkd
llfkdltkclfkvregttykeflgdkfytvisslktcnpsdilqmcsflegk
>d1aiw__ 2.54.1.1.1 Cellulose-binding domain of the endoglucanase Z {(Erwinia chrysanthemi)}
mgdcananvypnwvskdwaggqpthneagqsivykgnlytanwytasvpgsdsswtqvgs
cn
>e1aix.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqf
>e1aix.1l 2.35.1.2.10 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_ 2.5.1.1.15 Azurin {(Alcaligenes denitrificans)}
aqceatiesndamqynlkemvvdksckqftvhlkhvgkmakvamghnwvltkeadkqgva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
mkgtlklsn
>d1aizb_ 2.5.1.1.15 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__ 1.37.1.5.1 Troponin C {chicken (Gallus gallus)}
adiykaaveqlteeqknefkaafdifvlgaedgsistkelgkvmrmlgqnptpeelqemi
devdedgsgtvdfdeflvmmvrsmkddskgkteeelsdlfrmfdknadgyidleelkiml
qatgetiteddieelmkdgdknndgridydeflefmkgve
>d1aj5a_ 1.37.1.6.2 Calpain domain VI {Rat (Rattus norvegicus)}
eeerqfrklfvqlagddmevsatelmnilnkvvtrhpdlktdgfgidtcrsmvavmdsdt
tgklgfeefkylwnnikkwqgiykrfdtdrsgtigsnelpgafeaagfhlnqhiysmiir
rysdetgnmdfdnfisclvrldamfrafrsldkngtgqiqvniqewlqltmys
>d1aj5b_ 1.37.1.6.2 Calpain domain VI {Rat (Rattus norvegicus)}
eeerqfrklfvqlagddmevsatelmnilnkvvtrhpdlktdgfgidtcrsmvavmdsdt
tgklgfeefkylwnnikkwqgiykrfdtdrsgtigsnelpgafeaagfhlnqhiysmiir
rysdetgnmdfdnfisclvrldamfrafrsldkngtgqiqvniqewlqltmys
>d1aj6__ 4.72.1.2.1 DNA gyrase B, N-terminal domain {(Escherichia coli)}
vlkgldavrkrpgmyigdtddgtglhhmvfevvdnaidealaghckeiivtihadnsvsv
qddgrgiptgihpeegvsaaevimtvlhaggkfddnsykvsgglhgvgvsvvnalsqkle
lviqhegkihrqiyehgvpqaplavtgetektgtmvrfwpsletftnvtefeyeilakrl
relsflnsgvsirlrdkrdgkedhfh
>d1aj7h1 2.1.1.1.64 (1-114) Immunoglobulin (variable domains of L and H chains) {Fab 48G7 (mouse/human), kappa L chain}
qvqlqqsgaelvkpgasvklsctasgfnikdtymhwvkqrpeqglewigridpangntky
dpkfqgkatitadtssntaylqlssltsedtavyycasyygiywgqgttltvssa
>d1aj7h2 2.1.1.2.68 (115-216) Immunoglobulin (constant domains of L and H chains) {Fab 48G7 (mouse/human), kappa L chain}
stkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqssg
lyslssvvtvpssslgtqtyicnvnhkpsntkvdkkvepksc
>d1aj7l1 2.1.1.1.64 (1-109) Immunoglobulin (variable domains of L and H chains) {Fab 48G7 (mouse/human), kappa L chain}
diqmtqspsslsaslgervsltcrasqeisgylswlqqkpdgtikrliyaastldsgvpk
rfsgsrsgsdysltisslesedfadyyclqyasyprtfgggtkveikrt
>d1aj7l2 2.1.1.2.68 (110-214) Immunoglobulin (constant domains of L and H chains) {Fab 48G7 (mouse/human), kappa L chain}
vaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqdsk
dstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1aj8a_ 1.82.1.1.3 Citrate synthase {(Pyrococcus furiosus)}
lakgledvyidqtnicyidgkegklyyrgysveelaelstfeevvyllwwgklpslsele
nfkkelaksrglpkevieimealpknthpmgalrtiisylgniddsgdipvtpeevyrig
isvtakiptivanwyrikngleyvppkeklshaanflymlhgeeppkewekamdvalily
aeheinastlavmtvgstlsdyysailagigalkgpihggaveeaikqfmeigspekvee
wffkalqqkrkimgaghrvyktydprarifkkyasklgdkklfeiaerlerlveeylskk
gisinvdywsglvfygmkipielyttifamgriagwtahlaeyvshnriirprlqyvgei
gkkylpielrr
>d1aj8b_ 1.82.1.1.3 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_ 1.1.1.1.25 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__ 3.29.1.4.10 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__ 7.11.1.1.1 Ligand-binding domain of low-density lipoprotein receptor {human (Homo sapiens)}
pcsafefhclsgecihsswrcdggpdckdksdeenca
>d1ajka_ 2.21.1.2.3 Bacillus 1-3,1-4-beta-glucanase {(Bacillus macerans)}
ntgivssfftytgpahgtqwdeidieflgkdttkvqfnyytngvgghekvislgfdaskg
fhtyafdwqpgyikwyvdgvlkhtatanipstpgkimmnlwngtgvddwlgsynganply
aeydwvkytsnqtggsffepfnsynsgtwekadgysnggvfnctwrannvnftndgklkl
gltssaynkfdcaeyrstniygyglyevsmkpak
>d1ajkb_ 2.21.1.2.3 Bacillus 1-3,1-4-beta-glucanase {(Bacillus macerans)}
ntgivssfftytgpahgtqwdeidieflgkdttkvqfnyytngvgghekvislgfdaskg
fhtyafdwqpgyikwyvdgvlkhtatanipstpgkimmnlwngtgvddwlgsynganply
aeydwvkytsnqtggsffepfnsynsgtwekadgysnggvfnctwrannvnftndgklkl
gltssaynkfdcaeyrstniygyglyevsmkpak
>d1ajm__ 4.67.1.1.1 Thymidylate synthase {(Escherichia coli)}
kqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihellw
flqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlkn
dpdseriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfniasy
allvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesifd
yrfedfeiegydphpgikapvai
>e1ajn.1a 4.95.1.2.1 Penicillin acylase, catalytic domain {(Escherichia coli)}
ssseikivrdeygmphiyandtwhlfygygyvvaqdrlfqmemarrstqgtvaevlgkdf
vkfdkdirrnywpdairaqiaalspedmsilqgyadgmnawidkvntnpetllpkqfntf
gftpkrwepfdvamifvgtmanrfsdstseidnlalltalkdkygvsqgmavfnqlkwlv
npsapttiavqesnyplkfnqqnsqt
>e1ajn.1b 4.95.1.2.1 Penicillin acylase, catalytic domain {(Escherichia coli)}
snmwvigkskaqdakaimvngpqfgwyapaytygiglhgagydvtgntpfaypglvfghn
gviswgstagfgddvdifaerlsaekpgyylhngkwvkmlsreetitvkngqaetftvwr
tvhgnilqtdqttqtayaksrawdgkevasllawthqmkaknwqqwtqqaakqaltinwy
yadvngnigyvhtgaypdrqsghdprlpvpgtgkwdwkgllpfemnpkvynpqsgyianw
nnspqkdypasdlfaflwggadrvteidrlleqkprltadqawdvirqtsrqdlnlrlfl
ptlqaatsgltqsdprrqlvetltrwdginllnddgktwqqpgsailnvwltsmlkrtvv
aavpmpfdkwysasgyettqdgptgslnisvgakilyeavqgdkspipqavdlfagkpqq
evvlaaledtwetlskrygnnvsnwktpamaltfrannffgvpqaaaeetrhqaeyqnrg
tendmivfspttsdrpvlawdvvapgqsgfiapdgtvdkhyedqlkmyenfgrkslwltk
qdveahkesqevlhvqr
>d1ajoa_ 2.21.1.2.3 Bacillus 1-3,1-4-beta-glucanase {(Bacillus macerans)}
ghekvislgfdaskgfhtyafdwqpgyikwyvdgvlkhtatanipstpgkimmnlwngtg
vddwlgsynganplyaeydwvkytsnqtggsffepfnsynsgtwekadgysnggvfnctw
rannvnftndgklklgltssaynkfdcaeyrstniygyglyevsmkpakntgivssffty
tgpahgtqwdeidieflgkdttkvqfnyytng
>d1ajob_ 2.21.1.2.3 Bacillus 1-3,1-4-beta-glucanase {(Bacillus macerans)}
vgghekvislgfdaskgfhtyafdwqpgyikwyvdgvlkhtatanipstpgkimmnlwng
tgvddwlgsynganplyaeydwvkytsnqtggsffepfnsynsgtwekadgysnggvfnc
twrannvnftndgklklgltssaynkfdcaeyrstniygyglyevsmkpakntgivssff
tytgpahgtqwdeidieflgkdttkvqfnyytng
>e1ajp.1a 4.95.1.2.1 Penicillin acylase, catalytic domain {(Escherichia coli)}
ssseikivrdeygmphiyandtwhlfygygyvvaqdrlfqmemarrstqgtvaevlgkdf
vkfdkdirrnywpdairaqiaalspedmsilqgyadgmnawidkvntnpetllpkqfntf
gftpkrwepfdvamifvgtmanrfsdstseidnlalltalkdkygvsqgmavfnqlkwlv
npsapttiavqesnyplkfnqqnsqt
>e1ajp.1b 4.95.1.2.1 Penicillin acylase, catalytic domain {(Escherichia coli)}
snmwvigkskaqdakaimvngpqfgwyapaytygiglhgagydvtgntpfaypglvfghn
gviswgstagfgddvdifaerlsaekpgyylhngkwvkmlsreetitvkngqaetftvwr
tvhgnilqtdqttqtayaksrawdgkevasllawthqmkaknwqqwtqqaakqaltinwy
yadvngnigyvhtgaypdrqsghdprlpvpgtgkwdwkgllpfemnpkvynpqsgyianw
nnspqkdypasdlfaflwggadrvteidrlleqkprltadqawdvirqtsrqdlnlrlfl
ptlqaatsgltqsdprrqlvetltrwdginllnddgktwqqpgsailnvwltsmlkrtvv
aavpmpfdkwysasgyettqdgptgslnisvgakilyeavqgdkspipqavdlfagkpqq
evvlaaledtwetlskrygnnvsnwktpamaltfrannffgvpqaaaeetrhqaeyqnrg
tendmivfspttsdrpvlawdvvapgqsgfiapdgtvdkhyedqlkmyenfgrkslwltk
qdveahkesqevlhvqr
>e1ajq.1a 4.95.1.2.1 Penicillin acylase, catalytic domain {(Escherichia coli)}
ssseikivrdeygmphiyandtwhlfygygyvvaqdrlfqmemarrstqgtvaevlgkdf
vkfdkdirrnywpdairaqiaalspedmsilqgyadgmnawidkvntnpetllpkqfntf
gftpkrwepfdvamifvgtmanrfsdstseidnlalltalkdkygvsqgmavfnqlkwlv
npsapttiavqesnyplkfnqqnsqt
>e1ajq.1b 4.95.1.2.1 Penicillin acylase, catalytic domain {(Escherichia coli)}
snmwvigkskaqdakaimvngpqfgwyapaytygiglhgagydvtgntpfaypglvfghn
gviswgstagfgddvdifaerlsaekpgyylhngkwvkmlsreetitvkngqaetftvwr
tvhgnilqtdqttqtayaksrawdgkevasllawthqmkaknwqqwtqqaakqaltinwy
yadvngnigyvhtgaypdrqsghdprlpvpgtgkwdwkgllpfemnpkvynpqsgyianw
nnspqkdypasdlfaflwggadrvteidrlleqkprltadqawdvirqtsrqdlnlrlfl
ptlqaatsgltqsdprrqlvetltrwdginllnddgktwqqpgsailnvwltsmlkrtvv
aavpmpfdkwysasgyettqdgptgslnisvgakilyeavqgdkspipqavdlfagkpqq
evvlaaledtwetlskrygnnvsnwktpamaltfrannffgvpqaaaeetrhqaeyqnrg
tendmivfspttsdrpvlawdvvapgqsgfiapdgtvdkhyedqlkmyenfgrkslwltk
qdveahkesqevlhvqr
>d1ajra_ 3.54.1.1.3 Aspartate aminotransferase {pig (sus scrofa), cytosolic form}
appsvfaevpqaqpvlvfkliadfredpdprkvnlgvgayrtddcqpwvlpvvrkveqri
annsslnheylpilglaefrtcasrlalgddspalqekrvggvqslggtgalrigaefla
rwyngtnnkdtpvyvssptwenhngvfttagfkdirsyrywdtekrgldlqgflsdlena
pefsifvlhacahnptgtdptpeqwkqiasvmkrrflfpffdsayqgfasgnlekdawai
ryfvsegfelfcaqsfsxnfglynervgnltvvakepdsilrvlsqmqkivrvtwsnppa
qgarivartlsdpelfhewtgnvktmadrilsmrselrarlealktpgtwnhitdqigmf
sftglnpkqveylinqkhiyllpsgrinmcglttknldyvatsiheavtkiq
>d1ajrb_ 3.54.1.1.3 Aspartate aminotransferase {pig (sus scrofa), cytosolic form}
appsvfaevpqaqpvlvfkliadfredpdprkvnlgvgayrtddcqpwvlpvvrkveqri
annsslnheylpilglaefrtcasrlalgddspalqekrvggvqslggtgalrigaefla
rwyngtnnkdtpvyvssptwenhngvfttagfkdirsyrywdtekrgldlqgflsdlena
pefsifvlhacahnptgtdptpeqwkqiasvmkrrflfpffdsayqgfasgnlekdawai
ryfvsegfelfcaqsfsxnfglynervgnltvvakepdsilrvlsqmqkivrvtwsnppa
qgarivartlsdpelfhewtgnvktmadrilsmrselrarlealktpgtwnhitdqigmf
sftglnpkqveylinqkhiyllpsgrinmcglttknldyvatsiheavtkiq
>d1ajsa_ 3.54.1.1.3 Aspartate aminotransferase {pig (sus scrofa), cytosolic form}
appsvfaevpqaqpvlvfkliadfredpdprkvnlgvgayrtddcqpwvlpvvrkveqri
annsslnheylpilglaefrtcasrlalgddspalqekrvggvqslggtgalrigaefla
rwyngtnnkdtpvyvssptwenhngvfttagfkdirsyrywdtekrgldlqgflsdlena
pefsifvlhacahnptgtdptpeqwkqiasvmkrrflfpffdsayqgfasgnlekdawai
ryfvsegfelfcaqsfsknfglynervgnltvvakepdsilrvlsqmqkivrvtwsnppa
qgarivartlsdpelfhewtgnvktmadrilsmrselrarlealktpgtwnhitdqigmf
sftglnpkqveylinqkhiyllpsgrinmcglttknldyvatsiheavtkiq
>d1ajsb_ 3.54.1.1.3 Aspartate aminotransferase {pig (sus scrofa), cytosolic form}
appsvfaevpqaqpvlvfkliadfredpdprkvnlgvgayrtddcqpwvlpvvrkveqri
annsslnheylpilglaefrtcasrlalgddspalqekrvggvqslggtgalrigaefla
rwyngtnnkdtpvyvssptwenhngvfttagfkdirsyrywdtekrgldlqgflsdlena
pefsifvlhacahnptgtdptpeqwkqiasvmkrrflfpffdsayqgfasgnlekdawai
ryfvsegfelfcaqsfsxnfglynervgnltvvakepdsilrvlsqmqkivrvtwsnppa
qgarivartlsdpelfhewtgnvktmadrilsmrselrarlealktpgtwnhitdqigmf
sftglnpkqveylinqkhiyllpsgrinmcglttknldyvatsiheavtkiq
>d1ajva_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1ajvb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1ajw__ 2.1.1.5.16 Rho GDP-dissociation inhibitor 1, RhoGDI {Bovine (Bos taurus)}
avsadpnvpnvvvtrltlvcstapgpleldltgdlesfkkqsfvlkegveyrikisfrvn
reivsgmkyiqhtyrkgvkidktdymvgsygpraeeyefltpmeeapkgmlargsyniks
rftdddrtdhlswewnltikkewkd
>d1ajxa_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1ajxb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1ajya1 1.105.2.1.4 (67-100) PUT3 {Yeast (Saccharomyces cerevisiae)}
kkivvstkylqqlqkdlndkteennrlkalller
>d1ajya2 7.32.1.1.3 (30-66) PUT3 {Yeast (Saccharomyces cerevisiae)}
msvaclscrkrhikcpggnpcqkcvtsnaiceyleps
>d1ajyb1 1.105.2.1.4 (67-100) PUT3 {Yeast (Saccharomyces cerevisiae)}
kkivvstkylqqlqkdlndkteennrlkalller
>d1ajyb2 7.32.1.1.3 (30-66) PUT3 {Yeast (Saccharomyces cerevisiae)}
msvaclscrkrhikcpggnpcqkcvtsnaiceyleps
>d1ajz__ 3.1.19.1.1 Dihydropteroate synthetase {(Escherichia coli)}
mklfaqgtsldlshphvmgilnvtpdsfsdggthnslidavkhanlminagatiidvgge
strpgaaevsveeelqrvipvveaiaqrfevwisvdtskpeviresakvgahiindirsl
sepgaleaaaetglpvclmhmqgnpktmqeapkyddvfaevnryfieqiarceqagiake
kllldpgfgfgknlshnysllarlaefhhfnlpllvgmsrksmigqllnvgpserlsgsl
acaviaamqgahiirvhdvketveamrvveatlsakenkrye
>d1ak0__ 1.96.1.2.1 P1 nuclease {(Penicillium citrinum)}
wgalghatvayvaqhyvspeaaswaqgilgsssssylasiaswadeyrltsagkwsaslh
fidaednpptncnvdyerdcgssgcsisaianytqrvsdsslssenhaealrflvhfigd
mtqplhdeayavggnkinvtfdgyhdnlhsdwdtympqkligghalsdaeswaktlvqni
esgnytaqaigwikgdnisepittatrwasdanalvctvvmphgaaalqtgdlyptyyds
vidtielqiakggyrlanwineih
>d1ak1__ 3.80.1.1.1 Ferrochelatase {(Bacillus subtilis)}
rkkmgllvmaygtpykeedieryythirrgrkpepemlqdlkdryeaiggisplaqiteq
qahnleqhlneiqdeitfkayiglkhiepfiedavaemhkdgiteavsivlaphfstfsv
qsynkrakeeaeklggltitsveswydepkfvtywvdrvketyasmpederenamlivsa
hslpekikefgdpypdqlhesakliaegagvseyavgwqsegntpdpwlgpdvqdltrdl
feqkgyqafvyvpvgfvadhlevlydndyeckvvtddigasyyrpempnakpefidalat
vvlkklgr
>d1ak2__ 3.29.1.1.7 Adenylate kinase {bovine (Bos taurus) izozymes}
pkgvravllgppgagkgtqapklaknfcvchlatgdmlramvasgselgkklkatmdagk
lvsdemvlelieknletppckngflldgfprtvrqaemlddlmekrkekldsviefsipd
sllirritgrlihpqsgrsyheefnppkepmkdditgeplirrsddnkkalkirleayht
qttplveyyskrgihsaidasqtpdvvfasilaafskats
>d1ak4a_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
mvnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgf
mcqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictakte
wldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1ak4b_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
nptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfmc
qggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktewl
dgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1ak4c_ 1.61.1.1.1 HIV-1 capsid protein, N-terminal core domain {Human immunodeficiency virus type 1 (HIV-1)}
pivqnlqgqmvhqaisprtlnawvkvveekafspevipmfsalsegatpqdlntmlntvg
ghqaamqmlketineeaaewdrlhpvhagpiapgqmreprgsdiagttstlqeqigwmth
nppipvgeiykrwiilglnkivrmy
>d1ak4d_ 1.61.1.1.1 HIV-1 capsid protein, N-terminal core domain {Human immunodeficiency virus type 1 (HIV-1)}
pivqnlqgqmvhqaisprtlnawvkvveekafspevipmfsalsegatpqdlntmlntvg
ghqaamqmlketineeaaewdrlhpvhagpiapgqmreprgsdiagttstlqeqigwmth
nppipvgeiykrwiilglnkivrmy
>d1ak5__ 3.1.5.2.1 Inosine monophosphate dehydrogenase (IMPDH) {(Tritrichomonas foetus)}
akyynepchtfneyllipglstvdcipsnvnlstplvkfqkgqqseinlkiplvsaimqs
vsgekmaialareggisfifgsqsiesqaamvhavknfkagfvvsdsnvkpdqtfadvla
isqrtthntvavtddgtphgvllglvtqrdypidltqtetkvsdmmtpfsklvtahqdtk
lseankiiwekklnalpiidddqhlryivfrkdydrsqvchnelvdsqkrylvgagintr
dfrervpalveagadvlcidssdgfsewqkitigwirekygdkvkvgagnivdgegfryl
adagadfikigigggsicitreqkgigrgqatavidvvaernkyfeetgiyipvcsdggi
vydyhmtlalamgadfimlgryfarfeesptrkvtingsvmkeywgegssrarnwqrydl
ggkqklsfeegvdsyvpyagklkdnveaslnkvkstmcncgaltipqlqskakitlvssv
si
>d1ak6__ 4.62.1.2.3 Destrin {Human (Homo sapiens)/pig (Sus scrofa)}
tmitpssgnsasgvqvadevcrifydmkvrkcstpeeikkrkkavifclsadkkciivee
gkeilvgdvgvtitdpfkhfvgmlpekdcryalydasfetkesrkeelmfflwapelapl
kskmiyasskdaikkkfqgikhecqangpedlnraciaeklggslivafegcpv
>d1ak7__ 4.62.1.2.3 Destrin {Human (Homo sapiens)/pig (Sus scrofa)}
tmitpssgnsasgvqvadevcrifydmkvrkcstpeeikkrkkavifclsadkkciivee
gkeilvgdvgvtitdpfkhfvgmlpekdcryalydasfetkesrkeelmfflwapelapl
kskmiyasskdaikkkfqgikhecqangpedlnraciaeklggslivafegcpv
>d1ak8__ 1.37.1.5.8 Calmodulin {bovine (Bos taurus)}
madqlteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadg
ngtidfpefltmmark
>d1ak9__ 3.33.1.1.6 Subtilisin Novo/BPN' {(Bacillus amyloliquefaciens)}
aqsvpygvsqikapalhsqgycgsnvkvavidsgidsshpdlkvaggasfvpsetnpfqd
nnshgthvagtvaalnnsigvlgvapcaslyavkvlgadgsgqyswiingiewaiannmd
vinmslggpsgsaalkaavdkavasgvvvvaaagnegtsgssstvgypakypsviavgav
dssnqrasfssvgpeldvmapgvsiqstlpgnkygaksgtsmasphvagaaalilskhpn
wtntqvrsslentttklgdsfyygkglinvqaaaq
>d1akaa_ 3.54.1.1.1 Aspartate aminotransferase {chicken (Gallus gallus) mitochondria}
sswwshvemgppdpilgvteafkrdtnskkmnlgvgayrddngkpyvlncvrkaeamiaa
kkmdkeylpiagladftrasaelalgenseafksgryvtvqgisgtgslrvganflqrff
kfsrdvylpkpswgnhtpifrdaglqlqayryydpktcsldftgamediskipeksiill
hacahnptgvdprqeqwkelasvvkkrnllayfdmayqgfasgdinrdawalrhfieqgi
dvvlsqsyahnmglygeragaftvicrdaeeakrvesqlkilirpmysnppmngariasl
ilntpelrkewlvevkgmadriismrtqlvsnlkkegsshnwqhitdqigmfcftglkpe
qverltkefsiymtkdgrisvagvassnvgylahaihqvtk
>d1akab_ 3.54.1.1.1 Aspartate aminotransferase {chicken (Gallus gallus) mitochondria}
sswwshvemgppdpilgvteafkrdtnskkmnlgvgayrddngkpyvlncvrkaeamiaa
kkmdkeylpiagladftrasaelalgenseafksgryvtvqgisgtgslrvganflqrff
kfsrdvylpkpswgnhtpifrdaglqlqayryydpktcsldftgamediskipeksiill
hacahnptgvdprqeqwkelasvvkkrnllayfdmayqgfasgdinrdawalrhfieqgi
dvvlsqsyahnmglygeragaftvicrdaeeakrvesqlkilirpmysnppmngariasl
ilntpelrkewlvevkgmadriismrtqlvsnlkkegsshnwqhitdqigmfcftglkpe
qverltkefsiymtkdgrisvagvassnvgylahaihqvtk
>d1akba_ 3.54.1.1.1 Aspartate aminotransferase {chicken (Gallus gallus) mitochondria}
sswwshvemgppdpilgvteafkrdtnskkmnlgvgayrddngkpyvlncvrkaeamiaa
kkmdkeylpiagladftrasaelalgenseafksgryvtvqgisgtgslrvganflqrff
kfsrdvylpkpswgnhtpifrdaglqlqayryydpktcsldftgamediskipeksiill
hacahnptgvdprqeqwkelasvvkkrnllayfdmayqgfasgdinrdawalrhfieqgi
dvvlsqsyahnmglygeragaftvicrdaeeakrvesqlkilirpmysnppmngariasl
ilntpelrkewlvevkgmadriismrtqlvsnlkkegsshnwqhitdqigmfcftglkpe
qverltkefsiymtkdgrisvagvassnvgylahaihqvtk
>d1akca_ 3.54.1.1.1 Aspartate aminotransferase {chicken (Gallus gallus) mitochondria}
sswwshvemgppdpilgvteafkrdtnskkmnlgvgayrddngkpyvlncvrkaeamiaa
kkmdkeylpiagladftrasaelalgenseafksgryvtvqgisgtgslrvganflqrff
kfsrdvylpkpswgnhtpifrdaglqlqayryydpktcsldftgamediskipeksiill
hacahnptgvdprqeqwkelasvvkkrnllayfdmayqgfasgdinrdawalrhfieqgi
dvvlsqsyahnmglygeragaftvicrdaeeakrvesqlkilirpmysnppmngariasl
ilntpelrkewlvevkgmadriismrtqlvsnlkkegsshnwqhitdqigmfcftglkpe
qverltkefsiymtkdgrisvagvassnvgylahaihqvtk
>d1akd__ 1.83.1.1.1 Cytochrome P450 {(Pseudomonas putida)}
nlaplpphvpehlvfdfdmynpsnlsagvqeawavlqesnvpdlvwtrcngghwiatrgq
lireayedyrhfssecpfipreageaydfiptsmdppeqrqfralanqvvgmpvvdklen
riqelacslieslrpqgqcnftedyaepfpirifmllaglpeediphlkyltdqmtrpdg
smtfaeakealydylipiieqrrqkpgtdaisivangqvngrpitsdeakrmcglllvgg
ldtvvnflsfsmeflakspehrqeliqrperipaaceellrrfslvadgriltsdyefhg
vqlkkgdqillpqmlsglderenacpmhvdfsrqkvshttfghgshlclgqhlarreiiv
tlkewltripdfsiapgaqiqhksgivsgvqalplvwdpattkav
>d1akea1 3.29.1.1.9 (1-121,157-214) Adenylate kinase {(Escherichia coli)}
mriillgapgagkgtqaqfimekygipqistgdmlraavksgselgkqakdimdagklvt
delvialvkeriaqedcrngflldgfprtipqadamkeaginvdyvlefdvpdelivdri
vXkddqeetvrkrlveyhqmtapligyyskeaeagntkyakvdgtkpvaevradlekilg
>d1akea2 7.35.2.1.2 (122-156) Bacterial ADK, insert zinc finger domain {(Escherichia coli)}
grrvhapsgrvyhvkfnppkvegkddvtgeelttr
>d1akeb1 3.29.1.1.9 (1-121,157-214) Adenylate kinase {(Escherichia coli)}
mriillgapgagkgtqaqfimekygipqistgdmlraavksgselgkqakdimdagklvt
delvialvkeriaqedcrngflldgfprtipqadamkeaginvdyvlefdvpdelivdri
vXkddqeetvrkrlveyhqmtapligyyskeaeagntkyakvdgtkpvaevradlekilg
>d1akeb2 7.35.2.1.2 (122-156) Bacterial 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 4.15.1.1.8 (1-181) MHC class I, alpha-1 and alpha-2 domains {(human hla-a0201)}
gshsmryfftsvsrpgrgeprfiavgyvddtqfvrfdsdaasqrmeprapwieqegpeyw
dgetrkvkahsqthrvdlgtlrgyynqseagshtvqrmygcdvgsdwrflrgyhqyaydg
kdyialkedlrswtaadmaaqttkhkweaahvaeqlraylegtcvewlrrylengketlq
r
>d1akjd_ 2.1.1.1.2 CD8 {human (Homo sapiens)}
sqfrvspldrtwnlgetvelkcqvllsnptsgcswlfqprgaaasptfllylsqnkpkaa
egldtqrfsgkrlgdtfvltlsdfrrenegyyfcsalsnsimyfshfvpvflpa
>d1akje_ 2.1.1.1.2 CD8 {human (Homo sapiens)}
sqfrvspldrtwnlgetvelkcqvllsnptsgcswlfqprgaaasptfllylsqnkpkaa
egldtqrfsgkrlgdtfvltlsdfrrenegyyfcsalsnsimyfshfvpvflpa
>d1akk__ 1.3.1.1.7 Mitochondrial cytochrome c {horse (Equus caballus)}
gdvekgkkifvqkcaqchtvekggkhktgpnlhglfgrktgqapgftytdanknkgitwk
eetlmeylenpkkyipgtkmifagikkkteredliaylkkatne
>d1akl_1 2.61.1.1.1 (247-470) Metalloprotease, C-terminal domain {(Pseudomonas aeruginosa) (alkaline protease)}
ganlttrtgdtvygfnsnterdfysatssssklvfsvwdaggndtldfsgfsqnqkinln
ekalsdvgglkgnvsiaagvtvenaiggsgsdlligndvanvlkggagndilygglgadq
lwggagadtfvygdiaessaaapdtlrdfvsgqdkidlsgldafvngglvlqyvdafagk
agqailsydaaskagslaidfsgdahadfainligqatqadivv
>d1akl_2 4.52.1.6.1 (1-239) Metallo protease, catalytic (N-terminal) domain {(Pseudomonas aeruginosa) alkaline protease}
grsdaytqvdnflhayarggdelvnghpsytvdqaaeqilreqaswqkapgdsvltlsys
fltkpndffntpwkyvsdiyslgkfsafsaqqqaqaklslqswsdvtnihfvdagqgdqg
dltfgnfsssvggaafaflpdvpdalkgqswylinssysanvnpangnygrqtltheigh
tlglshpgdynagegdptyadatyaedtraysvmsyweeqntgqdfkgayssapllddi
>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__ 3.56.1.1.4 Bile-salt activated lipase {Bovine (Bos taurus)}
aklgsvyteggfvegvnkklslfgdsidifkgipfaaapkalekperhpgwqgtlkaksf
kkrclqatltqdstygnedclylniwvpqgrkevshdlpvmiwiyggaflmgasqganfl
snylydgeeiatrgnvivvtfnyrvgplgflstgdsnlpgnyglwdqhmaiawvkrniea
fggdpdnitlfgesaggasvslqtlspynkglikraisqsgvglcpwaiqqdplfwakri
aekvgcpvddtskmagclkitdpraltlayklplgsteypklhylsfvpvidgdfipddp
vnlyanaadvdyiagtndmdghlfvgmdvpainsnkqdvteedfyklvsgltvtkglrga
natyevytepwaqdssqetrkktmvdletdilfliptkiavaqhkshaksantytylfsq
psrmpiypkwmgadhaddlqyvfgkpfatplgyraqdrtvskamiaywtnfartgdpntg
hstvpanwdpytleddnyleinkqmdsnsmklhlrtnylqfwtqtyqalptvtsagasll
ppednsq
>d1ako__ 4.93.1.1.1 DNA-repair enzyme exonuclease III {(Escherichia coli)}
mkfvsfninglrarphqleaivekhqpdviglqetkvhddmfpleevaklgynvfyhgqk
ghygvalltketpiavrrgfpgddeeaqrriimaeipsllgnvtvingyfpqgesrdhpi
kfpakaqfyqnlqnyletelkrdnpvlimgdmnisptdldigigeenrkrwlrtgkcsfl
peerewmdrlmswglvdtfrhanpqtadrfswfdyrskgfddnrglridlllasqplaec
cvetgidyeirsmekpsdhapvwatfrr
>d1akp__ 2.1.6.1.4 Kedarcidin (apo form) {(Actimomycete strain L585-6)}
asaavsvspatgladgatvtvsasgfatstsatalqcailadgrgacnvaefhdfslsgg
egttsvvvrrsftgyvmpdgpevgavdcdtapggceivvggntgeygnaaisfg
>d1akr__ 3.14.4.1.2 Flavodoxin {(Desulfovibrio vulgaris)}
pkalivygsttgnteytaetiareladagyevdsrdaasveagglfegfdlvllgcstwa
ddsielqddfiplfdsleetgaqgrkvacfgcgdssyeyfcgavdaieeklknlgaeivq
dglridgdpraarddivgwahdvrgai
>e1aks.1a 2.35.1.2.2 Trypsin(ogen) {porcine (Sus scrofa)}
ivggytcaansipyqvslnsgshfcggslinsqwvvsaahcyksriqvrlgehnidvleg
neqfinaakiithpnfngntldndimliklsspatlnsrvatvslprscaaagteclisg
wgntk
>e1aks.1b 2.35.1.2.2 Trypsin(ogen) {porcine (Sus scrofa)}
ssgssypsllqclkapvlsnssckssypgqitgnmicvgflqggkdscqgdsggpvvcng
qlqgivswgygcaqknkpgvytkvcnyvnwiqqtiaan
>d1akt__ 3.14.4.1.2 Flavodoxin {(Desulfovibrio vulgaris)}
pkalivygsttgnteytaetiareladagyevdsrdaasveagglfegfdlvllgcstwn
ddsielqddfiplfdsleetgaqgrkvacfgcgdssyeyfcgavdaieeklknlgaeivq
dglridgdpraarddivgwahdvrgai
>d1akw__ 3.14.4.1.2 Flavodoxin {(Desulfovibrio vulgaris)}
pkalivygsttgnteytaetiareladagyevdsrdaasveagglfegfdlvllgcstwl
ddsielqddfiplfdsleetgaqgrkvacfgcgdssyeyfcgavdaieeklknlgaeivq
dglridgdpraarddivgwahdvrgai
>d1aky__ 3.29.1.1.8 Adenylate kinase {baker's yeast (Saccharomyces cerevisiae)}
esirmvligppgagkgtqapnlqerfhaahlatgdmlrsqiakgtqlgleakkimdqggl
vsddimvnmikdeltnnpackngfildgfprtipqaekldqmlkeqgtplekaielkvdd
ellvaritgrlihpasgrsyhkifnppkedmkddvtgealvqrsddnadalkkrlaayha
qtepivdfykktgiwagvdasqppatvwadilnklgkn
>d1akz__ 3.12.1.1.1 Uracil-DNA glycosylase {Human (Homo sapiens)}
meffgeswkkhlsgefgkpyfiklmgfvaeerkhytvyppphqvftwtqmcdikdvkvvi
lgqdpyhgpnqahglcfsvqrpvppppsleniykelstdiedfvhpghgdlsgwakqgvl
llnavltvrahqanshkergweqftdavvswlnqnsnglvfllwgsyaqkkgsaidrkrh
hvlqtahpsplsvyrgffgcrhfsktnellqksgkkpidwkel
>d1al01_ 1.69.1.1.1 Scaffolding protein gpD of bacteriophage procapsid {(Bacteriophage phi-x174)}
eqsvrfqtalasikliqasavldlteddfdfltsnkvwiatdrsrarrcveacvygtldf
vgyprfpapvefiaaviayyvhpvniqtaclimegaefteniingverpvkaaelfaftl
rvragntdvltdaeenvrqklra
>d1al02_ 1.69.1.1.1 Scaffolding protein gpD of bacteriophage procapsid {(Bacteriophage phi-x174)}
eqsvrfqtalasikliqasavldlteddfdfltsnkvwiatdrsrarrcveacvygtldf
vgyprfpapvefiaaviayyvhpvniqtaclimegaefteniingverpvkaaelfaftl
rvragntdvltda
>d1al03_ 1.69.1.1.1 Scaffolding protein gpD of bacteriophage procapsid {(Bacteriophage phi-x174)}
teqsvrfqtalasikliqasavldlteddfdfltsnkvwiatdrsrarrcveacvygtld
fvgyprfpapvefiaaviayyvhpvniqtaclimegaefteniingverpvkaaelfaft
lrvragntdvltdaeenvrq
>d1al04_ 1.69.1.1.1 Scaffolding protein gpD of bacteriophage procapsid {(Bacteriophage phi-x174)}
qsvrfqtalasikliqasavldlteddfdfltsnkvwiatdrsrarrcveacvygtldfv
gyprfpapvefiaaviayyvhpvniqtaclimegaefteniingverpvkaaelfaftlr
vragntdvltdaeenvrqklraegvm
>d1al0f_ 2.8.1.1.1 Bacteriophage capsid proteins {(bacteriophage phiX174)}
qtgaermphdlshlgflagqigrlitisttpviagdsfemdavgalrlsplrrglaidst
vdiftfyvphrhvygeqwikfmkdgvnatplptvnttgyidhaaflgtinpdtnkipkhl
fqgylniynnyfkapwmpdrteanpnelnqddarygfrcchlkniwtaplppetelsrqm
ttsttsidimglqaayanlhtdqerdyfmqryrdvissfggktsydadnrpllvmrsnlw
asgydvdgtdqtslgqfsgrvqqtykhsvprffvpehgtmftlalvrfpptatkeiqyln
akgaltytdiagdpvlygnlppreismkdvfrsgdsskkfkiaegqwyryapsyvspayh
llegfpfiqeppsgdlqervlirhhdydqcfqsvqllqwnsqvkfnvtvyrnlpttrd
>d1al0g_ 2.8.1.1.1 Bacteriophage capsid proteins {(bacteriophage phiX174)}
mfqtfisrhnsnffsdklvltsvtpassapvlqtpkatsstlyfdsltvnagnggflhci
qmdtsvnaanqvvsvgadiafdadpkffaclvrfesssvpttlptaydvyplngrhdggy
ytvkdcvtidvlprtpgnnvyvgfmvwsnftatkcrglvslnqvikeiiclqplk
>d1al21_ 2.8.1.4.3 Poliovirus {poliovirus (type 1, mahoney strain)}
aatsrdalpnteasgpthskeipaltavetgatnplvpsdtvqtrhvvqhrsrsessies
ffargacvtimtvdnpasttnkdklfavwkitykdtvqlrrklefftysrfdmeltfvvt
anftetnnghalnqvyqimyippgapvpekwddytwqtssnpsifytygtaparisvpyv
gisnayshfydgfskvplkdqsaalgdslygaaslndfgilavrvvndhnptkvtskirv
ylkpkhirvwcprppravayygpgvdykdgtltplstkdltty
>d1al22_ 2.8.1.4.3 Poliovirus {poliovirus (type 1, mahoney strain)}
eacgysdrvlqltlgnstittqeaansvvaygrwpeylrdseanpvdqptepdvaacrfy
tldtvswtkesrgwwwklpdalrdmglfgqnmyyhylgrsgytvhvqcnaskfhqgalgv
favpemclagdsntttmhtsyqnanpgekggtftgtftpdnnqtsparrfcpvdyllgng
tllgnafvfphqiinlrtnncatlvlpyvnslsidsmvkhnnwgiailplaplnfasess
peipitltiapmccefnglrnitlprlq
>d1al23_ 2.8.1.4.3 Poliovirus {poliovirus (type 1, mahoney strain)}
glpvmntpgsnqyltadnfqspcalpefdvtppidipgevknmmelaeidtmipfdlsat
kkntmemyrvrlsdkphtddpilclslspasdprlshtmlgeilnyythwagslkftflf
cgsmmatgkllvsyappgadppkkrkeamlgthviwdiglqssctmvvpwisnttyrqti
ddsfteggyisvfyqtrivvplstpremdilgfvsacndfsvrllrdtthieqka
>d1al3__ 3.82.1.1.14 Cofactor-binding fragment of CysB {(Klebsiella aerogenes)}
twpdkgslyvatthtqaryalpgvikgfieryprvslhmhqgsptqiaeavskgnadfai
atealhlyddlvmlpcyhwnrsivvtpehplatkgsvsieelaqyplvtytfgftgrsel
dtafnragltprivftatdadviktyvrlglgvgviasmavdpvsdpdlvkldangifsh
sttkigfrrstflrsymydfiqrfaphltrdvvdtavalrsnedieamfkdiklpek
>d1al6__ 1.82.1.1.1 Citrate synthase {chicken (Gallus gallus)}
stnlkdvlaslipkeqariktfrqqhgntavgqitvdmsyggmrgmkgliyetsvldpde
girfrgfsipecqkllpkagggeeplpeglfwllvtgqiptpeqvswvskewakraalps
hvvtmldnfptnlhpmsqlsaaitalnsesnfarayaeginrtkywefvyedamdliakl
pcvaakiyrnlyragssigaidskldwshnftnmlgytdpqftelmrlyltihsdheggn
vsahtshlvgsalsdpylsfaaamnglagplhglanqevllwlsqlqkdlgadasdeklr
dyiwntlnsgrvvpgyghavlrktdprytcqrefalkhlpsdpmfklvaqlykivpnvll
eqgkaknpwpnvdahsgvllqyygmtemnyytvlfgvsralgvlaqliwsralgfplerp
ksmstagleklsagg
>d1al7__ 3.1.7.1.3 Glycolate oxidase {spinach (Spinacia oleracea)}
meitnvneyeaiakqklpkmvydyyasgaedqwtlaenrnafsrilfrprilidvtnidm
tttilgfkismpimiaptamqkmahpegeyataraasaagtimtlsswatssveevastg
pgirffqlyvykdrnvvaqlvrraeragfkaialtvdtprlgrreadiknrfvlppfltl
knfegidlgkmdkandsglssyvagqidrslswkdvawlqtitslpilvkgvitaedarl
avqhgaagiivsnhgarqldyvpatimaleevvkaaqgripvfldggvrrgtdvfkalal
gaagvfigrpvvfslaaegeagvkkvlqmmrdefeltmalsgcrslkeisrshiaadwd
>d1al8__ 3.1.7.1.3 Glycolate oxidase {spinach (Spinacia oleracea)}
meitnvneyeaiakqklpkmvydyyasgaedqwtlaenrnafsrilfrprilidvtnidm
tttilgfkismpimiaptamqkmahpegeyataraasaagtimtlsswatssveevastg
pgirffqlyvykdrnvvaqlvrraeragfkaialtvdtprlgrreadiknrfvlppfltl
knfegidlgkmdkandsglssyvagqidrslswkdvawlqtitslpilvkgvitaedarl
avqhgaagiivsnhgarqldyvpatimaleevvkaaqgripvfldggvrrgtdvfkalal
gaagvfigrpvvfslaaegeagvkkvlqmmrdefeltmalsgcrslkeisrshiaadwd
>d1ala__ 1.55.1.1.4 Annexin V {chicken (Gallus gallus)}
kytrgtvtafspfdaradaealrkamkgmgtdeetilkiltsrnnaqrqeiasafktlfg
rdlvddlkseltgkfetlmvslmrparifdahalkhaikgagtnekvlteilasrtpaev
qnikqvymqeyeanledkitgetsghfqrllvvllqanrdpdgrveealvekdaqvlfra
gelkwgtdeetfitilgtrsvshlrrvfdkymtisgfqieetidretsgdleklllavvk
cirsvpayfaetlyysmkgagtdddtlirvmvsrseidlldirhefrknfakslyqmiqk
dtsgdyrkallllcgg
>d1alb__ 2.45.1.2.3 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__ 3.1.3.1.3 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 3.84.1.1.1 (1-150) Cytidine deaminase {(Escherichia coli)}
mhprfqtafaqladnlqsalepiladkyfpalltgeqvsslksatgldedalafallpla
aacartplsnfnvgaiargvsgtwyfganmefigatmqqtvhaeqsaishawlsgekala
aitvnytpcghcrqfmnelnsgldlrihlp
>d1aln_2 3.84.1.1.1 (151-294) Cytidine deaminase {(Escherichia coli)}
greahalrdylpdafgpkdleiktllmdeqdhgyaltgdalsqaaiaaanrshmpysksp
sgvaleckdgrifsgsyaenaafnptlpplqgalillnlkgydypdiqravlaekadapl
iqwdatsatlkalgchsidrvlla
>d1alo_1 1.52.1.1.1 (81-193) Aldehyde oxidoreductase, domain 2 {(Desulfovibrio gigas)}
qpenlhplqkawvlhggaqcgfcspgfivsakglldtnadpsredvrdwfqkhrnacrct
gykplvdavmdaaavingkkpetdlefkmpadgriwgskyprptavakvtgtl
>d1alo_2 4.11.5.1.9 (1-80) Aldehyde oxidoreductase, N-terminal domain {(Desulfovibrio gigas)}
miqkvitvngieqnlfvdaeallsdvlrqqlgltgvkvgceqgqcgacsvildgkvvrac
vtkmkrvadgaqittiegvg
>d1alo_3 4.23.1.1.1 (194-310) Aldehyde oxidoreductase, domain 3 {(Desulfovibrio gigas)}
dygadlglkmpagtlhlamvqakvshanikgidtsealtmpgvhsvithkdvkgknritg
litfptnkgdgwdrpilcdekvfqygdcialvcadseanaraaaekvkvdleelpay
>d1alo_4 4.82.1.1.1 (311-442) Aldehyde oxidoreductase, molybdemum cofactor-binding domain {(Desulfovibrio gigas)}
msgpaaaaedaieihpgtpnvyfeqpivkgedtgpifasadvtvegdfyvgrqphmpiep
dvafaymgddgkcyihsksigvhlhlymiapgvglepdqlvlvanpmggtfgykfsptse
alvavaamatgr
>d1alo_5 4.82.1.1.1 (443-557) Aldehyde oxidoreductase, molybdemum cofactor-binding domain {(Desulfovibrio gigas)}
pvhlrynyqqqqqytgkrspwemnvkfaakkdgtllamesdwlvdhgpysefgdlltlrg
aqfigagynipnirglgrtvatnhvwgsafrgygapqsmfaseclmdmlaeklgm
>d1alo_6 4.82.1.1.1 (558-735) Aldehyde oxidoreductase, molybdemum cofactor-binding domain {(Desulfovibrio gigas)}
dplelryknayrpgdtnptgqepevfslpdmidqlrpkyqaalekaqkestathkkgvgi
sigvygsgldgpdaseawaelnadgtitvhtawedhgqgadigcvgtahealrpmgvape
kikftwpntattpnsgpsggsreqvmtgnairvacenllkacekpgggyytydelkaa
>d1alo_7 4.82.1.1.1 (736-907) Aldehyde oxidoreductase, molybdemum cofactor-binding domain {(Desulfovibrio gigas)}
dkptkitgnwtasgathcdavtglgkpfvvymygvfmaevtvdvatgqttvdgmtlmadl
gslcnqlatdgqiygglaqgiglalsedfedikkhatlvgagfpfikqipdkldivyvnh
prpdgpfgasgvgelpltsphaaiinaiksatgvriyrlpaypekvlealka
>d1alq__ 5.4.1.1.3 beta-Lactamase, class A {(Staphylococcus aureus)}
sepivlviftnkdnksdkpndklisetaksvmkefaagsknaakelndlekkynahigvy
aldtksgkevkfnsdkrfayastskainsailleqvpynklnkkvhinkddivayspile
kyvgkditlkalieasmtysdntannkiikeiggikkvkqrlkelgdkvtnpvryeieln
yyspkskkdtstpaafgktlnkliangklskenkkflldlmlnnksgdtlikdgvpkdyk
vadksgqaityasrndvafvypk
>d1alu__ 1.26.1.1.4 Interleukin-6 {Human (Homo sapiens)}
ltsseridkqiryildgisalrketcnksnmcesskealaennlnlpkmaekdgcfqsgf
neetclvkiitgllefevyleylqnrfesseeqaravqmstkvliqflqkkaknldaitt
pdpttnaslltklqaqnqwlqdmtthlilrsfkeflqsslralrqm
>d1alva_ 1.37.1.6.3 Calpain domain VI {Pig (Sus scrofa)}
eevrqfrrlfaqlagddmevsatelmnilnkvvtrhpdlktdgfgidtcrsmvavmdsdt
tgklgfeefkylwnnikkwqaiykqfdvdrsgtigsselpgafeaagfhlnehlysmiir
rysdeggnmdfdnfisclvrldamfrafksldkdgtgqiqvniqewlqltmys
>d1alvb_ 1.37.1.6.3 Calpain domain VI {Pig (Sus scrofa)}
eevrqfrrlfaqlagddmevsatelmnilnkvvtrhpdlktdgfgidtcrsmvavmdsdt
tgklgfeefkylwnnikkwqaiykqfdvdrsgtigsselpgafeaagfhlnehlysmiir
rysdeggnmdfdnfisclvrldamfrafksldkdgtgqiqvniqewlqltmys
>d1alwa_ 1.37.1.6.3 Calpain domain VI {Pig (Sus scrofa)}
eevrqfrrlfaqlagddmevsatelmnilnkvvtrhpdlktdgfgidtcrsmvavmdsdt
tgklgfeefkylwnnikkwqaiykqfdvdrsgtigsselpgafeaagfhlnehlysmiir
rysdeggnmdfdnfisclvrldamfrafksldkdgtgqiqvniqewlqltmys
>d1alwb_ 1.37.1.6.3 Calpain domain VI {Pig (Sus scrofa)}
eevrqfrrlfaqlagddmevsatelmnilnkvvtrhpdlktdgfgidtcrsmvavmdsdt
tgklgfeefkylwnnikkwqaiykqfdvdrsgtigsselpgafeaagfhlnehlysmiir
rysdeggnmdfdnfisclvrldamfrafksldkdgtgqiqvniqewlqltmys
>d1aly__ 2.17.1.1.1 Extracellular domain of CD40 ligand {human (Homo sapiens)}
gdqnpqiaahviseasskttsvlqwaekgyytmsnnlvtlengkqltvkrqglyyiyaqv
tfcsnreassqapfiaslclkspgrferillraanthssakpcgqqsihlggvfelqpga
svfvnvtdpsqvshgtgftsfgllkl
>d1am1__ 4.72.1.1.1 HSP90 {yeast (Saccharomyces cerevisiae)}
asetfefqaeitqlmsliintvysnkeiflrelisnasdaldkirykslsdpkqletepd
lfiritpkpeqkvleirdsgigmtkaelinnlgtiaksgtkafmealsagadvsmigqfg
vgfyslflvadrvqvisksnddeqyiwesnaggsftvtldevnerigrgtilrlflkddq
leyleekrikevikrhsefvaypiqlvvtkeve
>d1am2__ 2.67.1.2.2 GyrA intein {(Mycobacterium xenopi)}
asitgdalvalpegesvriadivpgarpnsdnaidlkvldrhgnpvladrlfhsgehpvy
avrtveglrvtgtanhpllclvdvagvptllwklideikpgdyaviqrsafsvdcagfar
gkpefapttytvgvpglvrfleahhrdpdakaiadeltdgrfyyakvasvtdagvqpvys
lrvdtadhafitngfvshn
>d1am3__ 1.27.3.1.1 HIV capsid C-terminal domain {Human immunodeficiency virus type 1 (HIV-1)}
mdirqgpkepfrdyvdrfyktlraeqasqevknwmtetllvqnanpdcktilkalgpgat
leemmtacqg
>d1am4a_ 1.90.1.1.1 p50 RhoGAP domain {human (Homo sapiens)}
prpplpnqqfgvslqhlqeknpeqepipivlretvaylqahalttegifrrsantqvvre
vqqkynmglpvdfdqynelhlpavilktflrelpeplltfdlyphvvgflnidesqrvpa
tlqvlqtlpeenyqvlrfltaflvqisahsdqnkmtntnlavvfgpnllwakdaaitlka
inpintftkflldhqgelf
>d1am4b_ 1.90.1.1.1 p50 RhoGAP domain {human (Homo sapiens)}
prpplpnqqfgvslqhlqeknpeqepipivlretvaylqahalttegifrrsantqvvre
vqqkynmglpvdfdqynelhlpavilktflrelpeplltfdlyphvvgflnidesqrvpa
tlqvlqtlpeenyqvlrfltaflvqisahsdqnkmtntnlavvfgpnllwakdaaitlka
inpintftkflldhqgelf
>d1am4c_ 1.90.1.1.1 p50 RhoGAP domain {human (Homo sapiens)}
prpplpnqqfgvslqhlqeknpeqepipivlretvaylqahalttegifrrsantqvvre
vqqkynmglpvdfdqynelhlpavilktflrelpeplltfdlyphvvgflnidesqrvpa
tlqvlqtlpeenyqvlrfltaflvqisahsdqnkmtntnlavvfgpnllwakdaaitlka
inpintftkflldhqgelf
>d1am4d_ 3.29.1.4.10 CDC42 {Human (Homo sapiens)}
pqtikcvvvgdgavgktcllisyttnkfpseyvptvfdnyavtvmiggepytlglfdtag
qedydrlrplsypqtdvflvcfsvvspssfenvkekwvpeithhcpktpfllvgtqidlr
ddpstieklaknkqkpitpetaeklardlkavkyvecsaltqrglknvfdeailaal
>d1am4e_ 3.29.1.4.10 CDC42 {Human (Homo sapiens)}
pqtikcvvvgdgavgktcllisyttnkfpseyvptvfdnyavtvmiggepytlglfdtag
qedydrlrplsypqtdvflvcfsvvspssfenvkekwvpeithhcpktpfllvgtqidlr
ddpstieklaknkqkpitpetaeklardlkavkyvecsaltqrglknvfdeailaal
>d1am4f_ 3.29.1.4.10 CDC42 {Human (Homo sapiens)}
pqtikcvvvgdgavgktcllisyttnkfpseyvptvfdnyavtvmiggepytlglfdtag
qedydrlrplsypqtdvflvcfsvvspssfenvkekwvpeithhcpktpfllvgtqidlr
ddpstieklaknkqkpitpetaeklardlkavkyvecsaltqrglknvfdeailaal
>d1am5__ 2.38.1.2.10 Pepsin(ogen) {Atlantic cod (Gadus morhua)}
rvteqmkneadteyygvisigtppesfkvifdtgssnlwvssshcsaqacsnhnkfkprq
sstyvetgktvdltygtggmrgilgqdtvsvgggsdpnqelgesqtepgpfqaaapfdgi
lglaypsiaaagavpvfdnmgsqslvekdlfsfylsgggangsevmlggvdnshytgsih
wipvtaekywqvaldgitvngqtaacegcqaivdtgtskivapvsalanimkdigasenq
gemmgncasvqslpditftingvkqplppsayiegdqafctsglgssgvpsntselwifg
dvflrnyytiydrtnnkvgfapaa
>d1am6__ 2.56.1.1.2 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_ 1.36.1.1.6 SREBP-1a {Human (Homo sapiens)}
qsrgekrtahnaiekryrssindkiielkdlvvgteaklnksavlrkaidyirflqhsnq
klkqenlslrtavhkskslk
>d1am9b_ 1.36.1.1.6 SREBP-1a {Human (Homo sapiens)}
srgekrtahnaiekryrssindkiielkdlvvgteaklnksavlrkaidyirflqhsnqk
lkqenlslrtavhks
>d1am9c_ 1.36.1.1.6 SREBP-1a {Human (Homo sapiens)}
qsrgekrtahnaiekryrssindkiielkdlvvgteaklnksavlrkaidyirflqhsnq
klkqenlslrtavhkskslkdl
>d1am9d_ 1.36.1.1.6 SREBP-1a {Human (Homo sapiens)}
qsrgekrtahnaiekryrssindkiielkdlvvgteaklnksavlrkaidyirflqhsnq
klkqenlslrtavhks
>d1ama__ 3.54.1.1.1 Aspartate aminotransferase {chicken (Gallus gallus) mitochondria}
sswwshvemgppdpilgvteafkrdtnskkmnlgvgayrddngkpyvlncvrkaeamiaa
kkmdkeylpiagladftrasaelalgenseafksgryvtvqgisgtgslrvganflqrff
kfsrdvylpkpswgnhtpifrdaglqlqayryydpktcsldftgamediskipeksiill
hacahnptgvdprqeqwkelasvvkkrnllayfdmayqgfasgdinrdawalrhfieqgi
dvvlsqsyaknmglygeragaftvicrdaeeakrvesqlkilirpmysnppmngariasl
ilntpelrkewlvevkgmadriismrtqlvsnlkkegsshnwqhitdqigmfcftglkpe
qverltkefsiymtkdgrisvagvassnvgylahaihqvtk
>d1ame__ 2.66.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus)}
anqasvvanqlipintaltlvmmrsevvtpvgipaediprlvsmqvnravplgttlmpdm
vkgyaa
>d1amf__ 3.82.1.1.13 Molybdate-binding protein, ModA {(Escherichia coli)}
gkitvfaaasltnamqdiatqfkkekgvdvvssfassstlarqieagapadlfisadqkw
mdyavdkkaidtatrqtllgnslvvvapkasvqkdftidsktnwtsllnggrlavgdpeh
vpagiyakealqklgawdtlspklapaedvrgalalverneaplgivygsdavaskgvkv
vatfpedshkkveypvavveghnnatvkafydylkgpqaaeifkrygftik
>d1amha_ 2.35.1.2.3 Trypsin(ogen) {rat (Rattus rattus)}
ivggytcqensvpyqvslnsgyhfcggslindqwvvsaahcyksriqvrlgehninvleg
neqfvnaakiikhpnfdrktlnndimliklsspvklnarvatvalpsscapagtqclisg
wgntlssgvnepdllqcldapllpqadceasypgkitdnmvcvgfleggksscqgdsggp
vvcngelqgivswgygcalpdnpgvytkvcnyvdwiqdtiaan
>d1amhb_ 2.35.1.2.3 Trypsin(ogen) {rat (Rattus rattus)}
ivggytcqensvpyqvslnsgyhfcggslindqwvvsaahcyksriqvrlgehninvleg
neqfvnaakiikhpnfdrktlnndimliklsspvklnarvatvalpsscapagtqclisg
wgntlssgvnepdllqcldapllpqadceasypgkitdnmvcvgfleggksscqgdsggp
vvcngelqgivswgygcalpdnpgvytkvcnyvdwiqdtiaan
>d1ami_1 3.5.2.1.2 (529-754) Aconitase, C-terminal domain {bovine (Bos taurus)}
vdvsptsqrlqllepfdkwdgkdledlqilikvkgkcttdhisaagpwlkfrghldnisn
nlligainsenrkansvrnavtqefgpvpdtaryykqhgirwvvigdenygegssrehsa
leprflggraiitksfarihetnlkkqgllpltfadpadynkihpvdkltiqglkdfapg
kpltciikhpngtqetillnhtfnetqiewfragsalnrmkelqqk
>d1ami_2 3.71.1.1.2 (2-528) Aconitase, first 3 domains {bovine (Bos taurus)}
rakvamshfepheyirydlleknidivrkrlnrpltlsekivyghlddpanqeiergkty
lrlrpdrvamqdataqmamlqfissglpkvavpstihcdhlieaqlggekdlrrakdinq
evynflatagakygvgfwrpgsgiihqiilenyaypgvlligtdshtpnggglggicigv
ggadavdvmagipwelkcpkvigvkltgslsgwtspkdvilkvagiltvkggtgaiveyh
gpgvdsisctgmaticnmgaeigattsvfpynhrmkkylsktgradianladefkdhlvp
dsgchydqlieinlselkphingpftpdlahpvaevgsvaekegwpldirvgligsctns
syedmgrsaavakqalahglkcksqftitpgseqiratierdgyaqvlrdvggivlanac
gpcigqwdrkdikkgekntivtsynrnftgrndanpethafvtspeivtalaiagtlkfn
petdfltgkdgkkfkleapdadelpraefdpgqdtyqhppkdssgqr
>d1amj_1 3.5.2.1.2 (529-754) Aconitase, C-terminal domain {bovine (Bos taurus)}
vdvsptsqrlqllepfdkwdgkdledlqilikvkgkcttdhisaagpwlkfrghldnisn
nlligainsenrkansvrnavtqefgpvpdtaryykqhgirwvvigdenygegssrehsa
leprflggraiitksfarihetnlkkqgllpltfadpadynkihpvdkltiqglkdfapg
kpltciikhpngtqetillnhtfnetqiewfragsalnrmkelqqk
>d1amj_2 3.71.1.1.2 (2-528) Aconitase, first 3 domains {bovine (Bos taurus)}
rakvamshfepheyirydlleknidivrkrlnrpltlsekivyghlddpanqeiergkty
lrlrpdrvamqdataqmamlqfissglpkvavpstihcdhlieaqlggekdlrrakdinq
evynflatagakygvgfwrpgsgiihqiilenyaypgvlligtdshtpnggglggicigv
ggadavdvmagipwelkcpkvigvkltgslsgwtspkdvilkvagiltvkggtgaiveyh
gpgvdsisctgmaticnmgaeigattsvfpynhrmkkylsktgradianladefkdhlvp
dsgchydqlieinlselkphingpftpdlahpvaevgsvaekegwpldirvgligsctns
syedmgrsaavakqalahglkcksqftitpgseqiratierdgyaqvlrdvggivlanac
gpcigqwdrkdikkgekntivtsynrnftgrndanpethafvtspeivtalaiagtlkfn
petdfltgkdgkkfkleapdadelpraefdpgqdtyqhppkdssgqr
>d1amk__ 3.1.11.1.10 Triosephosphate isomerase {(Leishmania mexicana)}
sakpqpiaaanwkcngttasieklvqvfnehtishdvqcvvaptfvhiplvqaklrnpky
visaenaiaksgaftgevsmpilkdigvhwvilghserrtyygetdeivaqkvseackqg
fmviacigetlqqreanqtakvvlsqtsaiaakltkdawnqvvlayepvwaigtgkvatp
eqaqevhlllrkwvsenigtdvaaklrilyggsvnaanaatlyakpdingflvggaslkp
efrdiidatr
>d1amm_1 2.9.1.1.1 (1-85) gamma-Crystallin {bovine (Bos taurus) isoform II (B)}
gkitfyedrgfqghcyecssdcpnlqpyfsrcnsirvdsgcwmlyerpnyqghqyflrrg
dypdyqqwmgfndsirscrlipqht
>d1amm_2 2.9.1.1.1 (86-174) gamma-Crystallin {bovine (Bos taurus) isoform II (B)}
gtfrmriyerddfrgqmseitddcpslqdrfhltevhslnvlegswvlyempsyrgrqyl
lrpgeyrryldwgamnakvgslrrvmdfy
>d1amn__ 3.56.1.1.1 Acetylcholinesterase {Electric ray (Torpedo californica)}
sellvntksgkvmgtrvpvlsshisaflgipfaeppvgnmrfrrpepkkpwsgvwnasty
pnncqqyvdeqfpgfsgsemwnpnremsedclylniwvpsprpksttvmvwiygggfysg
sstldvyngkylayteevvlvslsyrvgafgflalhgsqeapgnvglldqrmalqwvhdn
iqffggdpktvtifgesaggasvgmhilspgsrdlfrrailqsgspncpwasvsvaegrr
ravelgrnlncnlnsdeelihclrekkpqelidvewnvlpfdsifrfsfvpvidgeffpt
slesmlnsgnfkktqillgvnkdegsffllygapgfskdseskisredfmsgvklsvpha
ndlgldavtlqytdwmddnngiknrdglddivgdhnvicplmhfvnkytkfgngtylyff
nhrasnlvwpewmgvihgyeiefvfglplvkelnytaeeealsrrimhywatfaktgnpn
eskwplfttkeqkfidlntepmkvhqrlrvqmcvfwnqflpkllna
>d1amoa1 2.32.1.4.1 (243-518) NADPH-cytochrome p450 reductase {Rat (Rattus norvegicus)}
rqyelvvhedmdvakvytgemgrlksyenqkppfdaknpflaavtanrklnqgterhlmh
leldisdskiryesgdhvavypandsalvnqigeilgadldvimslnnldeesnkkhpfp
cpttyrtaltyylditnpprtnvlyelaqyasepseqehlhkmasssgegkelylswvve
arrhilailqdypslrppidhlcellprlqaryysiassskvhpnsvhicavaveyeaks
grvnkgvatswlrakepagenggralvpmfvrksqf
>d1amoa2 3.14.4.2.1 (64-235) NADPH-cytochrome p450 reductase, N-terminal domain {Rat (Rattus norvegicus)}
vkessfvekmkktgrniivfygsqtgtaeefanrlskdahrygmrgmsadpeeydladls
slpeidkslvvfcmatygegdptdnaqdfydwlqetdvdltgvkfavfglgnktyehfna
mgkyvdqrleqlgaqrifelglgdddgnleedfitwreqfwpavceffgvea
>d1amoa3 3.16.1.3.1 (519-678) NADPH-cytochrome p450 reductase {Rat (Rattus norvegicus)}
rlpfksttpvimvgpgtgiapfmgfiqerawlreqgkevgetllyygcrrsdedylyree
larfhkdgaltqlnvafsreqahkvyvqhllkrdrehlwkliheggahiyvcgdarnmak
dvqntfydivaefgpmehtqavdyvkklmtkgrysldvws
>d1amob1 2.32.1.4.1 (243-518) NADPH-cytochrome p450 reductase {Rat (Rattus norvegicus)}
rqyelvvhedmdvakvytgemgrlksyenqkppfdaknpflaavtanrklnqgterhlmh
leldisdskiryesgdhvavypandsalvnqigeilgadldvimslnnldeesnkkhpfp
cpttyrtaltyylditnpprtnvlyelaqyasepseqehlhkmasssgegkelylswvve
arrhilailqdypslrppidhlcellprlqaryysiassskvhpnsvhicavaveyeaks
grvnkgvatswlrakepagenggralvpmfvrksqf
>d1amob2 3.14.4.2.1 (64-235) NADPH-cytochrome p450 reductase, N-terminal domain {Rat (Rattus norvegicus)}
vkessfvekmkktgrniivfygsqtgtaeefanrlskdahrygmrgmsadpeeydladls
slpeidkslvvfcmatygegdptdnaqdfydwlqetdvdltgvkfavfglgnktyehfna
mgkyvdqrleqlgaqrifelglgdddgnleedfitwreqfwpavceffgvea
>d1amob3 3.16.1.3.1 (519-678) NADPH-cytochrome p450 reductase {Rat (Rattus norvegicus)}
rlpfksttpvimvgpgtgiapfmgfiqerawlreqgkevgetllyygcrrsdedylyree
larfhkdgaltqlnvafsreqahkvyvqhllkrdrehlwkliheggahiyvcgdarnmak
dvqntfydivaefgpmehtqavdyvkklmtkgrysldvws
>d1amp__ 3.58.4.4.1 Aminopeptidase {(Aeromonas proteolytica)}
mppitqqatvtawlpqvdasqitgtisslesftnrfytttsgaqasdwiasewqalsasl
pnasvkqvshsgynqksvvmtitgseapdewivigghldstigshtneqsvapgadddas
giaavtevirvlsennfqpkrsiafmayaaeevglrgsqdlanqyksegknvvsalqldm
tnykgsaqdvvfitdytdsnftqyltqlmdeylpsltygfdtcgyacsdhaswhnagypa
ampfeskfndynprihttqdtlansdptgshakkftqlglayaiemgsatg
>d1amq__ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1amr__ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ams__ 3.54.1.1.4 Aspartate aminotransferase {(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
>d1amv__ 3.76.1.2.1 Glycogen phosphorylase {rabbit (Oryctolagus cuniculus)}
svrglagvenvtelkknfnrhlhftlvkdrnvatprdyyfalahtvrdhlvgrwirtqqh
yyekdpkriyylslefymgrtlqntmvnlalenacdeatyqlgldmeeleeieedaglgn
gglgrlaacfldsmatlglaaygygiryefgifnqkicggwqmeeaddwlrygnpwekar
peftlpvhfygrvehtsqgakwvdtqvvlampydtpvpgyrnnvvntmrlwsakapndfn
lkdfnvggyiqavldrnlaenisrvlypndnffegkelrlkqeyfvvaatlqdiirrfks
skfgcrdpvrtnfdafpdkvaiqlndthpslaipelmrvlvdlerldwdkawevtvktca
ytnhtvlpealerwpvhlletllprhlqiiyeinqrflnrvaaafpgdvdrlrrmslvee
gavkrinmahlciagshavngvarihseilkktifkdfyelephkfqnktngitprrwlv
lcnpglaeiiaerigeeyisdldqlrkllsyvddeafirdvakvkqenklkfaaylerey
kvhinpnslfdvqvkriheykrqllnclhvitlynrikkepnkfvvprtvmiggkaapgy
hmakmiiklitaigdvvnhdpvvgdrlrviflenyrvslaekvipaadlseqistagtea
sgtgnmkfmlngaltigtmdganvemaeeageenffifgmrvedvdrldqrgynaqeyyd
ripelrqiieqlssgffspkqpdlfkdivnmlmhhdrfkvfadyeeyvkcqervsalykn
prewtrmvirniatsgkfssdrtiaqyareiwgvepsrqrlpapdekip
>d1amw__ 4.72.1.1.1 HSP90 {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 2.53.1.1.11 (347-403) plant alpha-amylase {Barley (Hordeum vulgare) seeds, AMY2 isozyme}
hnesklqiieadadlylaeidgkvivklgprydvgnlipggfkvaahgndyavweki
>d1amy_2 3.1.1.1.11 (1-346) Plant alpha-amylase {Barley (Hordeum vulgare) seeds, AMY2 isozyme}
qvlfqgfnweswkhnggwynflmgkvddiaaagithvwlppasqsvaeqgympgrlydld
askygnkaqlksligalhgkgvkaiadivinhrtaehkdgrgiycifeggtpdarldwgp
hmicrddrpyadgtgnpdtgadfgaapdidhlnlrvqkelvewlnwlkadigfdgwrfdf
akgysadvakiyidrsepsfavaeiwtslayggdgkpnlnqdqhrqelvnwvdkvggkgp
attfdfttkgilnvavegelwrlrgtdgkapgmigwwpakavtfvdnhdtgstqhmwpfp
sdrvmqgyayilthpgtpcifydhffdwglkeeidrlvsvrtrhgi
>d1amz__ 1.82.1.1.1 Citrate synthase {chicken (Gallus gallus)}
stnlkdvlaslipkeqariktfrqqhgntavgqitvdmsyggmrgmkgliyetsvldpde
girfrgfsipecqkllpkagggeeplpeglfwllvtgqiptpeqvswvskewakraalps
hvvtmldnfptnlhpmsqlsaaitalnsesnfarayaeginrtkywefvyedamdliakl
pcvaakiyrnlyragssigaidskldwshnftnmlgytdpqftelmrlyltihsdheggn
vsahtshlvgsalsdpylsfaaamnglagplhglanqevllwlsqlqkdlgadasdeklr
dyiwntlnsgrvvpgyghavlrktdprytcqrefalkhlpsdpmfklvaqlykivpnvll
eqgkaknpwpnvdahsgvllqyygmtemnyytvlfgvsralgvlaqliwsralgfplerp
ksmstagleklsagg
>d1an1e_ 2.35.1.2.3 Trypsin(ogen) {rat (Rattus rattus)}
ivggytcaansipyqvslnsgshfcggslinsqwvvsaahcyksriqvrlgehnidvleg
neqfinaakiithpnfngntldndimliklsspatlxsrvatvslprscaaagteclisg
wgntkssgssypsllqclkapvlsdssckssypgqitgnmicvgfleggkdscqgdsggp
vvcngqlqgivswgygcaqknkpgvytkvcnyvnwiqqtiaan
>d1an1i_ 7.14.1.1.10 leech derived tryptase inhibitor (LDTI-C) {Medicinal leech (Hirudo medicinalis)}
kvcacpkilkpvcgsdgrtyansciarcngvsiksegscp
>d1an2a_ 1.36.1.1.2 Max protein {mouse (Mus musculus)}
adkrahhnalerkrrdhikdsfhslrdsvpslqgekasraqildkateyiqymrrknhth
qqdiddlkrqnalleqqvralekars
>d1an2c_ 1.36.1.1.2 Max protein {mouse (Mus musculus)}
adkrahhnalerkrrdhikdsfhslrdsvpslqgekasraqildkateyiqymrrknhth
qqdiddlkrqnalleqqvralekars
>d1an4a_ 1.36.1.1.4 Usf B/HLH domain {human (Homo sapiens)}
mdekrraqhneverrrrdkinnwivqlskiipdssmestksgqskggilskasdyiqelr
qsnhr
>d1an4b_ 1.36.1.1.4 Usf B/HLH domain {human (Homo sapiens)}
mdekrraqhneverrrrdkinnwivqlskiipdssmestksgqskggilskasdyiqelr
qsnhr
>d1an5a_ 4.67.1.1.1 Thymidylate synthase {(Escherichia coli)}
mkqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihell
wflqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlk
ndpdsrriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfnias
yallvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesif
dyrfedfeiegydphpgikapvai
>d1an5b_ 4.67.1.1.1 Thymidylate synthase {(Escherichia coli)}
mkqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihell
wflqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlk
ndpdsrriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfnias
yallvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesif
dyrfedfeiegydphpgikapvai
>d1an7a_ 4.86.1.1.2 Ribosomal protein S8 {(Thermus thermophilus)}
tdpiadmltrirnatrvykestdvpasrfkeeilrilaregfikgyervdvdgkpylrvy
lkygprrqgpdprpeqvihhirriskpgrrvyvgvkeiprvrrglgiailstskgvltdr
earklgvggelicevw
>d1an7b_ 4.86.1.1.2 Ribosomal protein S8 {(Thermus thermophilus)}
tdpiadmltrirnatrvykestdvpasrfkeeilrilaregfikgyervdvdgkpylrvy
lkygprrqgpdprpeqvihhirriskpgrrvyvgvkeiprvrrglgiailstskgvltdr
earklgvggelicevw
>d1an8_1 2.29.2.2.6 (3-95) Streptococcal superantigen Spe-C {(Streptococcus pyogenes)}
kkdisnvksdllyaytitpydykdcrvnfstthtlnidtqkyrgkdyyissemsyeasqk
fkrddhvdvfglfyilnshtgeyiyggitpaqn
>d1an8_2 4.11.6.1.6 (96-208) Streptococcal superantigen Spe-C {(Streptococcus pyogenes)}
nkvnhkllgnlfisgesqqnlnnkiilekdivtfqeidfkirkylmdnykiydatspyvs
grieigtkdgkheqidlfdspnegtrsdifakykdnriinmknfshfdiylek
>d1an9a1 3.21.1.2.1 (1-194,288-340) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernll
>d1an9a2 4.12.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1an9b1 3.21.1.2.1 (1-194,288-340) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernll
>d1an9b2 4.12.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1anb__ 2.35.1.2.3 Trypsin(ogen) {rat (Rattus rattus)}
ivggytcqensvpyqvslnsgyhfcggslindqwvvsaahcyksriqvrlgehninvleg
neqfvnaakiikhpnfdrktlnndimliklsspvklnarvatvalpsscapagtqclisg
wgntlssgvnepdllqcldapllpqadceasypgkitdnmvcvgfleggkdscqgdsggp
vvcngelqgivewgygcalpdnpgvytkvcnyvdwiqdtiaan
>d1anc__ 2.35.1.2.3 Trypsin(ogen) {rat (Rattus rattus)}
ivggytcqensvpyqvslnsgyhfcggslindqwvvsaahcyksriqvrlgehninvleg
neqfvnaakiikhpnfdrktlnndimliklsspvklnarvatvalpsscapagtqclisg
wgntlssgvnepdllqcldapllpqadceasypgkitdnmvcvgfleggkdscqgdsggp
vvcngelqgivkwgygcalpdnpgvytkvcnyvdwiqdtiaan
>d1and__ 2.35.1.2.3 Trypsin(ogen) {rat (Rattus rattus)}
ivggytcqensvpyqvslnsgyhfcggslindqwvvsaahcyksriqvrlgehninvleg
neqfvnaakiikhpnfdhktlnndimliklsspvklnarvatvalpsscapagtqclisg
wgntlssgvnepdllqcldapllpqadceasypgkitdnmvcvgfleggkdscqgdsggp
vvcngelqgivswgygcalpdnpgvytkvcnyvdwiqdtiaan
>d1ane__ 2.35.1.2.3 Trypsin(ogen) {rat (Rattus rattus)}
ivggytcqensvpyqvslnsgyhfcggslindqwvvsaahcyksriqvrlgehninvleg
neqfvnaakiikhpnfdrktlnndimliklsspvklnarvatvalpsscapagtqclisg
wgntlssgvnepdllqcldapllpqadceasypgkitdnmvcvgfleggkdscqgdsggp
vvcngelqgivswgygcalpdnpgvytkvcnyvdwiqdtiaan
>d1anf__ 3.82.1.1.6 D-maltodextrin-binding protein {(Escherichia coli)}
kieegklviwingdkgynglaevgkkfekdtgikvtvehpdkleekfpqvaatgdgpdii
fwahdrfggyaqsgllaeitpdkafqdklypftwdavryngkliaypiavealsliynkd
llpnppktweeipaldkelkakgksalmfnlqepyftwpliaadggyafkyengkydikd
vgvdnagakagltflvdliknkhmnadtdysiaeaafnkgetamtingpwawsnidtskv
nygvtvlptfkgqpskpfvgvlsaginaaspnkelakeflenylltdegleavnkdkplg
avalksyeeelakdpriaatmenaqkgeimpnipqmsafwyavrtavinaasgrqtvdea
lkdaqtritk
>d1ang__ 4.4.1.1.4 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 3.29.1.1.9 (1-121,157-214) Adenylate kinase {(Escherichia coli)}
mriillgapgagkgtqaqfimekygipqistgdmlraavksgselgkqakdimdagklvt
delvialvkeriaqedcrngflldgfprtipqadamkeaginvdyvlefdvpdelivdri
vXkddqeetvrkrlveyhqmtapligyyskeaeagntkyakvdgtkpvaevradlekilg
>d1anka2 7.35.2.1.2 (122-156) Bacterial ADK, insert zinc finger domain {(Escherichia coli)}
grrvhapsgrvyhvkfnppkvegkddvtgeelttr
>d1ankb1 3.29.1.1.9 (1-121,157-214) Adenylate kinase {(Escherichia coli)}
mriillgapgagkgtqaqfimekygipqistgdmlraavksgselgkqakdimdagklvt
delvialvkeriaqedcrngflldgfprtipqadamkeaginvdyvlefdvpdelivdri
vXkddqeetvrkrlveyhqmtapligyyskeaeagntkyakvdgtkpvaevradlekilg
>d1ankb2 7.35.2.1.2 (122-156) Bacterial ADK, insert zinc finger domain {(Escherichia coli)}
grrvhapsgrvyhvkfnppkvegkddvtgeelttr
>d1ann__ 1.55.1.1.3 Annexin IV {bovine (Bos taurus)}
ggtvkaasgfnaaedaqtlrkamkglgtdedaiinvlayrstaqrqeirtaykttigrdl
mddlkselsgnfeqvilgmmtptvlydvqelrkamkgagtdegclieilasrtpeeirri
nqtyqlqygrsleddirsdtsfmfqrvlvslsaggrdesnylddalmrqdaqdlyeagek
kwgtdevkfltvlcsrnrnhllhvfdeykriaqkdieqsiksetsgsfedallaivkcmr
nksayfaerlyksmkglgtdddtlirvmvsraeidmldiranfkrlygkslysfikgdts
gdyrkvllilcggdd
>d1ans__ 7.10.1.1.1 Neurotoxin III (ATX III) {Sea anemone (Anemonia sulcata)}
rsccpcywggcpwgqncypegcsgpkv
>d1anti_ 5.2.1.1.6 Antithrombin {human (Homo sapiens)}
rdipmnpmciyrspekkatedegseqkipeatnrrvwelskansrfattfyqhladsknd
ndniflsplsistafamtklgacndtlqqlmevfkfdtisektsdqihfffaklncrlyr
kankssklvsanrlfgdksltfnetyqdiselvygaklqpldfkenaeqsraainkwvsn
ktegritdvipseaineltvlvlvntiyfkglwkskfspentrkelfykadgescsasmm
yqegkfryrrvaegtqvlelpfkgdditmvlilpkpekslakvekeltpevlqewldele
emmlvvhmprfriedgfslkeqlqdmglvdlfspeksklpgivaegrddlyvsdafhkaf
levneegseaaastavviagrslnpnrvtfkanrpflvfirevplntiifmgrvanpcvk
>d1antl_ 5.2.1.1.6 Antithrombin {human (Homo sapiens)}
dipmnpmciyrspekkatedegseqkipeatnrrvwelskansrfattfyqhladskndn
dniflsplsistafamtklgacndtlqqlmevfkfdtisektsdqihfffaklncrlyrk
ankssklvsanrlfgdksltfnetyqdiselvygaklqpldfkenaeqsraainkwvsnk
tegritdvipseaineltvlvlvntiyfkglwkskfspentrkelfykadgescsasmmy
qegkfryrrvaegtqvlelpfkgdditmvlilpkpekslakvekeltpevlqewldelee
mmlvvhmprfriedgfslkeqlqdmglvdlfspeksklpgivaegrddlyvsdafhkafl
evneegseaaastavviagrslnpnrvtfkanrpflvfirevplntiifmgrvanpcvk
>d1anu__ 2.2.2.2.3 Cohesin-2 domain of the cellulosome {(Clostridium thermocellum)}
vvveigkvtgsvgttveipvyfrgvpskgiancdfvfrydpnvleiigidpgdiivdpnp
tksfdtaiypdrkiivflfaedsgtgayaitkdgvfakiratvkssapgyitfdevggfa
dndlveqkvsfidggvnv
>d1anv_1 1.50.1.1.1 (179-265) A domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
sawekgmeaaralmdkyhvdndlkanfkllpdqvealaavcktwlneehrglqltftsnk
tfvtmmgrflqaylqsfaevtykhhep
>d1anv_2 7.41.1.1.1 (266-385) The first Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
tgcalwlhrcaeiegelkclhgsiminkehviemdvtsengqralkeqsskakivknrwg
rnvvqisntdarccvhdaacpanqfsgkscgmffsegakaqvafkqikafmqalypnaqt
>d1anv_3 7.41.1.1.2 (386-529) The second Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
ghghllmplrcecnskpghapflgrqlpkltpfalsnaedldadlisdksvlasvhhpal
ivfqccnpvyrnsraqgggpncdfkisapdllnalvmvrslwsenftelprmvvpefkws
tkhqyrnvslpvahsdarqnpfdf
>d1anwa_ 1.55.1.1.5 Annexin V {human (Homo sapiens)}
aqvlrgtvtdfpgfderadaetlrkamkglgtdeesiltlltsrsnaqrqeisaafktlf
grdllddlkseltgkfeklivalmkpsrlydayelkhalkgagtnekvlteiiasrtpee
lraikqvyeeeygssleddvvgdtsgyyqrmlvvllqanrdpdagideaqveqdaqalfq
agelkwgtdeekfitifgtrsvshlrkvfdkymtisgfqieetidretsgnleqlllavv
ksirsipaylaetlyyamkgagtddhtlirvmvsrseidlfnirkefrknfatslysmik
gdtsgdykkallllcgedd
>d1anwb_ 1.55.1.1.5 Annexin V {human (Homo sapiens)}
aqvlrgtvtdfpgfderadaetlrkamkglgtdeesiltlltsrsnaqrqeisaafktlf
grdllddlkseltgkfeklivalmkpsrlydayelkhalkgagtnekvlteiiasrtpee
lraikqvyeeeygssleddvvgdtsgyyqrmlvvllqanrdpdagideaqveqdaqalfq
agelkwgtdeekfitifgtrsvshlrkvfdkymtisgfqieetidretsgnleqlllavv
ksirsipaylaetlyyamkgagtddhtlirvmvsrseidlfnirkefrknfatslysmik
gdtsgdykkallllcgedd
>d1anxa_ 1.55.1.1.5 Annexin V {human (Homo sapiens)}
qvlrgtvtdfpgfderadaetlrkamkglgtdeesiltlltsrsnaqrqeisaafktlfg
rdllddlkseltgkfeklivalmkpsrlydayelkhalkgagtnekvlteiiasrtpeel
raikqvyeeeygssleddvvgdtsgyyqrmlvvllqanrdpdagideaqveqdaqalfqa
gelkwgtdeekfitifgtrsvshlrkvfdkymtisgfqieetidretsgnleqlllavvk
sirsipaylaetlyyamkgagtddhtlirvmvsrseidlfnirkefrknfatslysmikg
dtsgdykkallllcge
>d1anxb_ 1.55.1.1.5 Annexin V {human (Homo sapiens)}
qvlrgtvtdfpgfderadaetlrkamkglgtdeesiltlltsrsnaqrqeisaafktlfg
rdllddlkseltgkfeklivalmkpsrlydayelkhalkgagtnekvlteiiasrtpeel
raikqvyeeeygssleddvvgdtsgyyqrmlvvllqanrdpdagideaqveqdaqalfqa
gelkwgtdeekfitifgtrsvshlrkvfdkymtisgfqieetidretsgnleqlllavvk
sirsipaylaetlyyamkgagtddhtlirvmvsrseidlfnirkefrknfatslysmikg
dtsgdykkallllcge
>d1anxc_ 1.55.1.1.5 Annexin V {human (Homo sapiens)}
qvlrgtvtdfpgfderadaetlrkamkglgtdeesiltlltsrsnaqrqeisaafktlfg
rdllddlkseltgkfeklivalmkpsrlydayelkhalkgagtnekvlteiiasrtpeel
raikqvyeeeygssleddvvgdtsgyyqrmlvvllqanrdpdagideaqveqdaqalfqa
gelkwgtdeekfitifgtrsvshlrkvfdkymtisgfqieetidretsgnleqlllavvk
sirsipaylaetlyyamkgagtddhtlirvmvsrseidlfnirkefrknfatslysmikg
dtsgdykkallllcge
>d1ao0a1 3.49.1.1.4 (235-459) Glutamine PRPP amidotransferase, C-terminal domain {(Bacillus subtilis)}
icsmeyiyfsrpdsnidginvhsarknlgkmlaqesaveadvvtgvpdssisaaigyaea
tgipyelgliknryvgrtfiqpsqalreqgvrmklsavrgvvegkrvvmvddsivrgtts
rrivtmlreagatevhvkissppiahpcfygidtstheeliasshsveeirqeigadtls
flsvegllkgigrkyddsncgqclacftgkypteiyqdtvlphvk
>d1ao0a2 4.95.1.1.2 (1-234) Glutamine PRPP amidotransferase, N-terminal domain {(Bacillus subtilis)}
cgvfgiwgheeapqityyglhslqhrgqegagivatdgekltahkgqglitevfqngels
kvkgkgaighvryataggggyenvqpllfrsqnngslalahngnlvnatqlkqqlenqgs
ifqtssdtevlahlikrsghftlkdqiknslsmlkgayaflimtetemivaldpnglrpl
sigmmgdayvvasetcafdvvgatylrevepgemliindegmkserfsmninrs
>d1ao0b1 3.49.1.1.4 (235-459) Glutamine PRPP amidotransferase, C-terminal domain {(Bacillus subtilis)}
icsmeyiyfsrpdsnidginvhsarknlgkmlaqesaveadvvtgvpdssisaaigyaea
tgipyelgliknryvgrtfiqpsqalreqgvrmklsavrgvvegkrvvmvddsivrgtts
rrivtmlreagatevhvkissppiahpcfygidtstheeliasshsveeirqeigadtls
flsvegllkgigrkyddsncgqclacftgkypteiyqdtvlphvk
>d1ao0b2 4.95.1.1.2 (1-234) Glutamine PRPP amidotransferase, N-terminal domain {(Bacillus subtilis)}
cgvfgiwgheeapqityyglhslqhrgqegagivatdgekltahkgqglitevfqngels
kvkgkgaighvryataggggyenvqpllfrsqnngslalahngnlvnatqlkqqlenqgs
ifqtssdtevlahlikrsghftlkdqiknslsmlkgayaflimtetemivaldpnglrpl
sigmmgdayvvasetcafdvvgatylrevepgemliindegmkserfsmninrs
>d1ao0c1 3.49.1.1.4 (235-459) Glutamine PRPP amidotransferase, C-terminal domain {(Bacillus subtilis)}
icsmeyiyfsrpdsnidginvhsarknlgkmlaqesaveadvvtgvpdssisaaigyaea
tgipyelgliknryvgrtfiqpsqalreqgvrmklsavrgvvegkrvvmvddsivrgtts
rrivtmlreagatevhvkissppiahpcfygidtstheeliasshsveeirqeigadtls
flsvegllkgigrkyddsncgqclacftgkypteiyqdtvlphvk
>d1ao0c2 4.95.1.1.2 (1-234) Glutamine PRPP amidotransferase, N-terminal domain {(Bacillus subtilis)}
cgvfgiwgheeapqityyglhslqhrgqegagivatdgekltahkgqglitevfqngels
kvkgkgaighvryataggggyenvqpllfrsqnngslalahngnlvnatqlkqqlenqgs
ifqtssdtevlahlikrsghftlkdqiknslsmlkgayaflimtetemivaldpnglrpl
sigmmgdayvvasetcafdvvgatylrevepgemliindegmkserfsmninrs
>d1ao0d1 3.49.1.1.4 (235-459) Glutamine PRPP amidotransferase, C-terminal domain {(Bacillus subtilis)}
icsmeyiyfsrpdsnidginvhsarknlgkmlaqesaveadvvtgvpdssisaaigyaea
tgipyelgliknryvgrtfiqpsqalreqgvrmklsavrgvvegkrvvmvddsivrgtts
rrivtmlreagatevhvkissppiahpcfygidtstheeliasshsveeirqeigadtls
flsvegllkgigrkyddsncgqclacftgkypteiyqdtvlphvk
>d1ao0d2 4.95.1.1.2 (1-234) Glutamine PRPP amidotransferase, N-terminal domain {(Bacillus subtilis)}
cgvfgiwgheeapqityyglhslqhrgqegagivatdgekltahkgqglitevfqngels
kvkgkgaighvryataggggyenvqpllfrsqnngslalahngnlvnatqlkqqlenqgs
ifqtssdtevlahlikrsghftlkdqiknslsmlkgayaflimtetemivaldpnglrpl
sigmmgdayvvasetcafdvvgatylrevepgemliindegmkserfsmninrs
>d1ao3a_ 3.50.1.1.2 von Willebrand factor A3 domain {Human (Homo sapiens)}
csqpldvillldgsssfpasyfdemksfakafiskanigprltqvsvlqygsittidvpw
nvvpekahllslvdvmqreggpsqigdalgfavryltsemhgarpgaskavvilvtdvsv
dsvdaaadaarsnrvtvfpigigdrydaaqlrilagpagdsnvvklqriedlptmvtlgn
sflhklc
>d1ao3b_ 3.50.1.1.2 von Willebrand factor A3 domain {Human (Homo sapiens)}
csqpldvillldgsssfpasyfdemksfakafiskanigprltqvsvlqygsittidvpw
nvvpekahllslvdvmqreggpsqigdalgfavryltsemhgarpgaskavvilvtdvsv
dsvdaaadaarsnrvtvfpigigdrydaaqlrilagpagdsnvvklqriedlptmvtlgn
sflhklc
>d1ao5a_ 2.35.1.2.25 Kallikrein-13 {mouse (Mus musculus)}
vvggfnceknsqpwqvavyyqkehicggvlldrnwvltaahcyvdqyevwlgknklfqee
psaqhrlvsksfphpgfnmsllmlqtippgadfsddlmllrlskpaditdvvkpialptk
epkpgskclasgwgsitptrwqkpddlqcvfitllpnencakvylqkvtdvmlcagemgg
gkdtcrddsggplicdgilqgttsygpvpcgkpgvpaiytnlikfnswikdtmmkna
>d1ao5b_ 2.35.1.2.25 Kallikrein-13 {mouse (Mus musculus)}
vvggfnceknsqpwqvavyyqkehicggvlldrnwvltaahcyvdqyevwlgknklfqee
psaqhrlvsksfphpgfnmsllmlqtippgadfsddlmllrlskpaditdvvkpialptk
epkpgskclasgwgsitptrwqkpddlqcvfitllpnencakvylqkvtdvmlcagemgg
gkdtcrddsggplicdgilqgttsygpvpcgkpgvpaiytnlikfnswikdtmmkna
>d1ao6a1 1.97.1.1.1 (5-196) Serum albumin {Human (Homo sapiens)}
sevahrfkdlgeenfkalvliafaqylqqcpfedhvklvnevtefaktcvadesaencdk
slhtlfgdklctvatlretygemadccakqepernecflqhkddnpnlprlvrpevdvmc
tafhdneetflkkylyeiarrhpyfyapellffakrykaafteccqaadkaacllpklde
lrdegkassakq
>d1ao6a2 1.97.1.1.1 (197-388) Serum albumin {Human (Homo sapiens)}
rlkcaslqkfgerafkawavarlsqrfpkaefaevsklvtdltkvhtecchgdllecadd
radlakyicenqdsissklkeccekpllekshciaevendempadlpslaadfveskdvc
knyaeakdvflgmflyeyarrhpdysvvlllrlaktyettlekccaaadphecyakvfde
fkplveepqnli
>d1ao6a3 1.97.1.1.1 (389-582) Serum albumin {Human (Homo sapiens)}
kqncelfeqlgeykfqnallvrytkkvpqvstptlvevsrnlgkvgskcckhpeakrmpc
aedylsvvlnqlcvlhektpvsdrvtkccteslvnrrpcfsalevdetyvpkefnaetft
fhadictlsekerqikkqtalvelvkhkpkatkeqlkavmddfaafvekcckaddketcf
aeegkklvaasqaa
>d1ao6b1 1.97.1.1.1 (5-196) Serum albumin {Human (Homo sapiens)}
sevahrfkdlgeenfkalvliafaqylqqcpfedhvklvnevtefaktcvadesaencdk
slhtlfgdklctvatlretygemadccakqepernecflqhkddnpnlprlvrpevdvmc
tafhdneetflkkylyeiarrhpyfyapellffakrykaafteccqaadkaacllpklde
lrdegkassakq
>d1ao6b2 1.97.1.1.1 (197-388) Serum albumin {Human (Homo sapiens)}
rlkcaslqkfgerafkawavarlsqrfpkaefaevsklvtdltkvhtecchgdllecadd
radlakyicenqdsissklkeccekpllekshciaevendempadlpslaadfveskdvc
knyaeakdvflgmflyeyarrhpdysvvlllrlaktyettlekccaaadphecyakvfde
fkplveepqnli
>d1ao6b3 1.97.1.1.1 (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 4.15.1.1.8 (1-181) MHC class I, alpha-1 and alpha-2 domains {(human hla-a0201)}
gshsmryfftsvsrpgrgeprfiavgyvddtqfvrfdsdaasqrmeprapwieqegpeyw
dgetrkvkahsqthrvdlgtlrgyynqseagshtvqrmygcdvgsdwrflrgyhqyaydg
kdyialkedlrswtaadmaaqttkhkweaahvaeqlraylegtcvewlrrylengketlq
r
>d1ao7d_ 2.1.1.1.120 T-cell antigen receptor {human (Homo sapiens), alpha-chain}
keveqnsgplsvpegaiaslnctysdrgsqsffwyrqysgkspelimsiysngdkedgrf
taqlnkasqyvsllirdsqpsdsatylcavttdswgklqfgagtqvvvtpdiqnp
>d1ao7e1 2.1.1.1.122 (3-118) T-cell antigen receptor {human (Homo sapiens), beta-chain}
gvtqtpkfqvlktgqsmtlqcaqdmnheymswyrqdpgmglrlihysvgagitdqgevpn
gynvsrsttedfplrllsaapsqtsvyfcasrpglaggrpeqyfgpgtrltvted
>d1ao7e2 2.1.1.2.112 (119-246) T-cell antigen receptor {human (Homo sapiens), beta-chain}
lknvfppevavfepseaeishtqkatlvclatgfypdhvelswwvngkevhsgvstdpqp
lkeqpalndsryalssrlrvsatfwqnprnhfrcqvqfyglsendewtqdrakpvtqivs
aeawgrad
>d1ao8__ 3.60.1.1.2 Dihydrofolate reductase, prokaryotic type {(Lactobacillus casei)}
taflwaqdrdgligkdghlpwhlpddlhyfraqtvgkimvvgrrtyesfpkrplpertnv
vlthqedyqaqgavvvhdvaavfayakqhpdqelviaggaqiftafkddvdtllvtrlag
sfegdtkmiplnwddftkvssrtvedtnpalthtyevwqkka
>d1aoa_1 1.38.1.1.2 (121-251) N-terminal actin-crosslinking domain from fimbrin {Human (Homo sapiens)}
yseeekyafvnwinkalendpdcrhvipmnpntddlfkavgdgivlckminlsvpdtide
rainkkkltpfiiqenlnlalnsasaigchvvnigaedlragkphlvlgllwqiikiglf
adielsrneal
>d1aoa_2 1.38.1.1.2 (260-375) N-terminal actin-crosslinking domain from fimbrin {Human (Homo sapiens)}
tleelmklspeelllrwanfhlensgwqkinnfsadikdskayfhllnqiapkgqkegep
ridinmsgfnetddlkraesmlqqadklgcrqfvtpadvvsgnpklnlafvanlfn
>d1aob__ 4.67.1.1.1 Thymidylate synthase {(Escherichia coli)}
mkqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihell
wflqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlk
ndpdsrriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfnias
yallvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesif
dyrfedfeiegydphpgikapvai
>d1aoca_ 7.16.1.5.1 Coagulogen {japanese horseshoe crab (Tachypleus tridentatus)}
adtnapiclcdepgvlgrtqivtteikdkiekaveavaqesgvsgrgfsifshhpvfrec
gkyecrtvrpehsrcynfppfthfksecpvstrdcepvfgytvagefrvivqapragfrq
cvwqhkcrfgsnscgyngrctqqrsvvrlvtynlekdgflcesfrtccgcpcrsf
>d1aocb_ 7.16.1.5.1 Coagulogen {japanese horseshoe crab (Tachypleus tridentatus)}
adtnapiclcdepgvlgrtqivtteikdkiekaveavaqesgvsgrgfsifshhpvfrec
gkyecrtvrpehsrcynfppfthfksecpvstrdcepvfgytvagefrvivqapragfrq
cvwqhkcrfgsnscgyngrctqqrsvvrlvtynlekdgflcesfrtccgcpcrsf
>d1aod__ 3.1.15.2.2 Phosphatidylinositol-specific phospholipase C {(Listeria monocytogenes)}
vttkqwmsalpdttnlaalsipgthdtmsyngditwtltkplaqtqtmslyqqleagiry
idirakdnlniyhgpiflnaslsgvletitqflkknpketiimrlkdeqnsndsfdyriq
pliniykdyfyttprtdtsnkiptlkdvrgkilllsenhtkkplvinsrkfgmqfgapnq
viqddyngpsvktkfkeivqtayqaskadnklflnhisatsltftprqyaaalnnkveqf
vlnltsekvrglgilimdfpekqtikniiknnkf
>d1aoea_ 3.60.1.1.7 Dihydrofolate reductases, eukaryotic type {yeast (Candida albicans)}
mlkpnvaiivaalkpalgigykgkmpwrlrkeiryfkdvttrttkpntrnavimgrktwe
sipqkfrplpdrlniilsrsyeneiiddniihassiesslnlvsdvervfiiggaeiyne
linnslvshlliteiehpspesiemdtflkfpleswtkqpkselqkfvgdtvleddikeg
dftynytlwtrk
>d1aoeb_ 3.60.1.1.7 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 2.52.2.1.1 (134-567) C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase {(Triosphaera 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 2.52.2.1.1 (134-567) C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase {(Triosphaera pantotropha)}
ppefgmkemreswkvhvapedrptqqmndwdlenlfsvtlrdagqialidgstyeiktvl
dtgyavhisrlsasgrylfvigrdgkvnmidlwmkepttvaeikigsearsietskmegw
edkyaiagaywppqyvimdgetlepkkiqstrgmtydeqeyhpeprvaailashyrpefi
vnvketgkillvdytdlnnlktteisaerflhdggldgshryfitaanarnklvvidtke
gklvaiedtggqtphpgrganfvhptfgpvwatshmgddsvaligtdpeghpdnawkild
sfpalgggslfikthpnsqylyvdatlnpeaeisgsvavfdikamtgdgsdpefktlpia
ewagitegqprvvqgefnkdgtevwfsvwngkdqesalvvvddktlelkhvikderlvtp
tgkfnvyntmtdty
>d1aoga1 3.4.1.4.4 (3-169,287-357) Trypanothione reductase {(Trypanosoma cruzi)}
skifdlvvigagsggleaawnaatlykkrvavidvqmvhgppffsalggtcvnvgcvpkk
lmvtgaqymehlresagfgwefdrttlraewknliavkdeavlninksydemfrdtegle
fflgwgslesknvvnvresadpasavkerletehillasgswphmpnXgrsprtkdlqlq
nagvmiknggvqvdeysrtnvsniyaigdvtnrvmltpvaineaaalvdtvfgttprkt
>d1aoga2 3.4.1.4.4 (170-286) Trypanothione reductase {(Trypanosoma cruzi)}
ipgiehcissneafylpepprrvltvgggfisvefagifnaykpkdgqvtlcyrgemilr
gfdhtlreeltkqltangiqiltkenpakvelnadgsksvtfesgkkmdfdlvmmai
>d1aoga3 4.48.1.1.4 (358-487) Trypanothione reductase {(Trypanosoma cruzi)}
dhtrvasavfsippigtcglieevaskryevvavylssftplmhkvsgskyktfvakiit
nhsdgtvlgvhllgdnapeiiqgigiclklnakisdfyntigvhptsaeelcsmrtpsyy
yvkgekmekp
>d1aogb1 3.4.1.4.4 (5-169,287-357) Trypanothione reductase {(Trypanosoma cruzi)}
ifdlvvigagsggleaawnaatlykkrvavidvqmvhgppffsalggtcvnvgcvpkklm
vtgaqymehlresagfgwefdrttlraewknliavkdeavlninksydemfrdtegleff
lgwgslesknvvnvresadpasavkerletehillasgswphmpnXgrsprtkdlqlqna
gvmiknggvqvdeysrtnvsniyaigdvtnrvmltpvaineaaalvdtvfgttprkt
>d1aogb2 3.4.1.4.4 (170-286) Trypanothione reductase {(Trypanosoma cruzi)}
ipgiehcissneafylpepprrvltvgggfisvefagifnaykpkdgqvtlcyrgemilr
gfdhtlreeltkqltangiqiltkenpakvelnadgsksvtfesgkkmdfdlvmmai
>d1aogb3 4.48.1.1.4 (358-487) Trypanothione reductase {(Trypanosoma cruzi)}
dhtrvasavfsippigtcglieevaskryevvavylssftplmhkvsgskyktfvakiit
nhsdgtvlgvhllgdnapeiiqgigiclklnakisdfyntigvhptsaeelcsmrtpsyy
yvkgekmekp
>d1aoha_ 2.2.2.2.4 Cohesin domain from the scaffolding protein CipA {(Clostridium thermocellum)}
avrikvdtvnakpgdtvripvrfsgipskgiancdfvysydpnvleiieiepgelivdpn
ptksfdtavypdrkmivflfaedsgtgayaitedgvfativakvksgapnglsvikfvev
ggfanndlveqktqffdggvnvg
>d1aohb_ 2.2.2.2.4 Cohesin domain from the scaffolding protein CipA {(Clostridium thermocellum)}
tdldavrikvdtvnakpgdtvripvrfsgipskgiancdfvysydpnvleiieiepgeli
vdpnptksfdtavypdrkmivflfaedsgtgayaitedgvfativakvksgapnglsvik
fvevggfanndlveqktqffdggvnvg
>d1aoja_ 2.24.2.1.24 EPS8 SH3 domain {Mouse (Mus musculus)}
kkyakskydfvarnsselsvmkddvleilddrrqwwkvrnasgdsgfvpnnildimrtpe
>d1aojb_ 2.24.2.1.24 EPS8 SH3 domain {Mouse (Mus musculus)}
kkyakskydfvarnsselsvmkddvleilddrrqwwkvrnasgdsgfvpnnildimrtpe
>d1aoka_ 1.103.1.2.9 Snake phospholipase A2 {Sand viper (Vipera ammodytes) vipoxin}
nlfqfgdmilqktgkeavhsyaiygcycgwggqgraqdatdrccfaqdccygrvndcnpk
tatytysrengdivcgdddlclravcecdraaaiclgenvntydknyeyysishcteese
qc
>d1aokb_ 1.103.1.2.9 Snake phospholipase A2 {Sand viper (Vipera ammodytes) vipoxin}
nlfqfakmingklgafsvwnyisygcycgwggqgtpkdatdrccfvhdccygrvrgcnpk
laiyyysfkkgnivcgknngclrdicecdrvaancfhqnkntynanykflsssrcrqtge
kc
>d1aol__ 2.15.1.1.1 F-MuLV receptor-binding domain {(Friend murine leukemia virus), F-MuLV}
qvynitwevtngdretvwaisgnhplwtwwpvltpdlcmlalsgpphwgleyqapysspp
gppccsgssgssagcsrdcdepltsltprcntawnrlkldqvthkssegfyvcpgshrpr
eakscggpdsfycaswgcettgrvywkpssswdyitvdnnlttsqavqvckdnkwcnpla
iqftnagkqvtswttghywglrlyvsgrdpgltfgirlryqnlgprvp
>d1aoma1 2.52.2.1.1 (129-567) C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase {(Triosphaera pantotropha)}
ldpaappefgmkemreswkvhvapedrptqqmndwdlenlfsvtlrdagqialidgstye
iktvldtgyavhisrlsasgrylfvigrdgkvnmidlwmkepttvaeikigsearsiets
kmegwedkyaiagaywppqyvimdgetlepkkiqstrgmtydeqeyhpeprvaailashy
rpefivnvketgkillvdytdlnnlktteisaerflhdggldgshryfitaanarnklvv
idtkegklvaiedtggqtphpgrganfvhptfgpvwatshmgddsvaligtdpeghpdna
wkildsfpalgggslfikthpnsqylyvdatlnpeaeisgsvavfdikamtgdgsdpefk
tlpiaewagitegqprvvqgefnkdgtevwfsvwngkdqesalvvvddktlelkhvikde
rlvtptgkfnvyntmtdty
>d1aomb1 1.3.1.2.1 (26-133) N-terminal (heme c) domain of cytochrome cd1-nitrite reductase {(Thiosphaera pantotropha)}
epsldnlaqqdvaapgapegvtalsdaqyneankiyfercagchgvlrkgatgkaltpdl
trdlgfdylqsfityaspagmpnwgtsgelsaeqvdlmanyllldpaa
>d1aomb2 2.52.2.1.1 (134-567) C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase {(Triosphaera pantotropha)}
ppefgmkemreswkvhvapedrptqqmndwdlenlfsvtlrdagqialidgstyeiktvl
dtgyavhisrlsasgrylfvigrdgkvnmidlwmkepttvaeikigsearsietskmegw
edkyaiagaywppqyvimdgetlepkkiqstrgmtydeqeyhpeprvaailashyrpefi
vnvketgkillvdytdlnnlktteisaerflhdggldgshryfitaanarnklvvidtke
gklvaiedtggqtphpgrganfvhptfgpvwatshmgddsvaligtdpeghpdnawkild
sfpalgggslfikthpnsqylyvdatlnpeaeisgsvavfdikamtgdgsdpefktlpia
ewagitegqprvvqgefnkdgtevwfsvwngkdqesalvvvddktlelkhvikderlvtp
tgkfnvyntmtdty
>d1aona1 1.100.1.1.1 (2-136,410-525) GroEL, the ATPase domain {(Escherichia coli)}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aona2 3.5.4.1.1 (191-366) GroEL {(Escherichia coli)}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aona3 4.33.1.1.1 (137-190,367-409) The intermediate domain of GroEL {(Escherichia coli)}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonb1 1.100.1.1.1 (2-136,410-525) GroEL, the ATPase domain {(Escherichia coli)}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aonb2 3.5.4.1.1 (191-366) GroEL {(Escherichia coli)}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aonb3 4.33.1.1.1 (137-190,367-409) The intermediate domain of GroEL {(Escherichia coli)}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonc1 1.100.1.1.1 (2-136,410-525) GroEL, the ATPase domain {(Escherichia coli)}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aonc2 3.5.4.1.1 (191-366) GroEL {(Escherichia coli)}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aonc3 4.33.1.1.1 (137-190,367-409) The intermediate domain of GroEL {(Escherichia coli)}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aond1 1.100.1.1.1 (2-136,410-525) GroEL, the ATPase domain {(Escherichia coli)}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aond2 3.5.4.1.1 (191-366) GroEL {(Escherichia coli)}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aond3 4.33.1.1.1 (137-190,367-409) The intermediate domain of GroEL {(Escherichia coli)}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aone1 1.100.1.1.1 (2-136,410-525) GroEL, the ATPase domain {(Escherichia coli)}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aone2 3.5.4.1.1 (191-366) GroEL {(Escherichia coli)}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aone3 4.33.1.1.1 (137-190,367-409) The intermediate domain of GroEL {(Escherichia coli)}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonf1 1.100.1.1.1 (2-136,410-525) GroEL, the ATPase domain {(Escherichia coli)}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aonf2 3.5.4.1.1 (191-366) GroEL {(Escherichia coli)}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aonf3 4.33.1.1.1 (137-190,367-409) The intermediate domain of GroEL {(Escherichia coli)}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aong1 1.100.1.1.1 (2-136,410-525) GroEL, the ATPase domain {(Escherichia coli)}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aong2 3.5.4.1.1 (191-366) GroEL {(Escherichia coli)}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aong3 4.33.1.1.1 (137-190,367-409) The intermediate domain of GroEL {(Escherichia coli)}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonh1 1.100.1.1.1 (2-136,410-525) GroEL, the ATPase domain {(Escherichia coli)}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aonh2 3.5.4.1.1 (191-366) GroEL {(Escherichia coli)}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aonh3 4.33.1.1.1 (137-190,367-409) The intermediate domain of GroEL {(Escherichia coli)}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aoni1 1.100.1.1.1 (2-136,410-525) GroEL, the ATPase domain {(Escherichia coli)}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aoni2 3.5.4.1.1 (191-366) GroEL {(Escherichia coli)}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aoni3 4.33.1.1.1 (137-190,367-409) The intermediate domain of GroEL {(Escherichia coli)}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonj1 1.100.1.1.1 (2-136,410-525) GroEL, the ATPase domain {(Escherichia coli)}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aonj2 3.5.4.1.1 (191-366) GroEL {(Escherichia coli)}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aonj3 4.33.1.1.1 (137-190,367-409) The intermediate domain of GroEL {(Escherichia coli)}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonk1 1.100.1.1.1 (2-136,410-525) GroEL, the ATPase domain {(Escherichia coli)}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aonk2 3.5.4.1.1 (191-366) GroEL {(Escherichia coli)}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aonk3 4.33.1.1.1 (137-190,367-409) The intermediate domain of GroEL {(Escherichia coli)}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonl1 1.100.1.1.1 (2-136,410-525) GroEL, the ATPase domain {(Escherichia coli)}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aonl2 3.5.4.1.1 (191-366) GroEL {(Escherichia coli)}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aonl3 4.33.1.1.1 (137-190,367-409) The intermediate domain of GroEL {(Escherichia coli)}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonm1 1.100.1.1.1 (2-136,410-525) GroEL, the ATPase domain {(Escherichia coli)}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aonm2 3.5.4.1.1 (191-366) GroEL {(Escherichia coli)}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aonm3 4.33.1.1.1 (137-190,367-409) The intermediate domain of GroEL {(Escherichia coli)}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonn1 1.100.1.1.1 (2-136,410-525) GroEL, the ATPase domain {(Escherichia coli)}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aonn2 3.5.4.1.1 (191-366) GroEL {(Escherichia coli)}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aonn3 4.33.1.1.1 (137-190,367-409) The intermediate domain of GroEL {(Escherichia coli)}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aono_ 2.25.1.1.1 Chaperonin-10 (GroES) {(Escherichia coli)}
mnirplhdrvivkrkevetksaggivltgsaaakstrgevlavgngrilengevkpldvk
vgdivifndgygvksekidneevlimsesdilaivea
>d1aonp_ 2.25.1.1.1 Chaperonin-10 (GroES) {(Escherichia coli)}
mnirplhdrvivkrkevetksaggivltgsaaakstrgevlavgngrilengevkpldvk
vgdivifndgygvksekidneevlimsesdilaivea
>d1aonq_ 2.25.1.1.1 Chaperonin-10 (GroES) {(Escherichia coli)}
mnirplhdrvivkrkevetksaggivltgsaaakstrgevlavgngrilengevkpldvk
vgdivifndgygvksekidneevlimsesdilaivea
>d1aonr_ 2.25.1.1.1 Chaperonin-10 (GroES) {(Escherichia coli)}
mnirplhdrvivkrkevetksaggivltgsaaakstrgevlavgngrilengevkpldvk
vgdivifndgygvksekidneevlimsesdilaivea
>d1aons_ 2.25.1.1.1 Chaperonin-10 (GroES) {(Escherichia coli)}
mnirplhdrvivkrkevetksaggivltgsaaakstrgevlavgngrilengevkpldvk
vgdivifndgygvksekidneevlimsesdilaivea
>d1aont_ 2.25.1.1.1 Chaperonin-10 (GroES) {(Escherichia coli)}
mnirplhdrvivkrkevetksaggivltgsaaakstrgevlavgngrilengevkpldvk
vgdivifndgygvksekidneevlimsesdilaivea
>d1aonu_ 2.25.1.1.1 Chaperonin-10 (GroES) {(Escherichia coli)}
mnirplhdrvivkrkevetksaggivltgsaaakstrgevlavgngrilengevkpldvk
vgdivifndgygvksekidneevlimsesdilaivea
>d1aoo__ 7.38.1.1.5 Metallothionein {Baker's yeast (Saccharomyces cerevisiae)}
qneghecqcqcgscknneqcqkscscptgcnsddkcpcgn
>d1aop_1 4.34.24.1.1 (82-145) Sulfite reductase, domains 1 and 3 {(Escherichia coli)}
lrcrlpggvittkqwqaidkfagentiygsirltnrqtfqfhgilkknvkpvhqmlhsvg
ldal
>d1aop_2 4.34.24.1.1 (346-425) Sulfite reductase, domains 1 and 3 {(Escherichia coli)}
igwvkgiddnwhltlfiengrildyparplktglleiakihkgdfritanqnliiagvpe
sekakiekiakesglmnavt
>d1aop_3 4.83.1.1.1 (149-345) Sulfite reductase hemoprotein (SiRHP), domains 2 and 4 {(Escherichia coli)}
ndmnrnvlctsnpyesqlhaeayewakkisehllprtrayaeiwldqekvattdeepilg
qtylprkfkttvvippqndidlhandmnfvaiaengklvgfnllvggglsiehgnkktya
rtasefgylplehtlavaeavvttqrdwgnrtdrknaktkytlervgvetfkaeverrag
ikfepirpyeftgrgdr
>d1aop_4 4.83.1.1.1 (426-570) Sulfite reductase hemoprotein (SiRHP), domains 2 and 4 {(Escherichia coli)}
pqrensmacvsfptcplamaeaerflpsfidnidnlmakhgvsdehivmrvtgcpngcgr
amlaevglvgkapgrynlhlggnrigtriprmykenitepeilasldeligrwakereag
egfgdftvragiirpvldpardlwd
>d1aoqa1 1.3.1.2.1 (36-133) N-terminal (heme c) domain of cytochrome cd1-nitrite reductase {(Thiosphaera pantotropha)}
dvaapgapegvtalsdaqyneankiyfercagchgvlrkgatgkaltpdltrdlgfdylq
sfityaspagmpnwgtsgelsaeqvdlmanyllldpaa
>d1aoqa2 2.52.2.1.1 (134-567) C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase {(Triosphaera pantotropha)}
ppefgmkemreswkvhvapedrptqqmndwdlenlfsvtlrdagqialidgstyeiktvl
dtgyavhisrlsasgrylfvigrdgkvnmidlwmkepttvaeikigsearsietskmegw
edkyaiagaywppqyvimdgetlepkkiqstrgmtydeqeyhpeprvaailashyrpefi
vnvketgkillvdytdlnnlktteisaerflhdggldgshryfitaanarnklvvidtke
gklvaiedtggqtphpgrganfvhptfgpvwatshmgddsvaligtdpeghpdnawkild
sfpalgggslfikthpnsqylyvdatlnpeaeisgsvavfdikamtgdgsdpefktlpia
ewagitegqprvvqgefnkdgtevwfsvwngkdqesalvvvddktlelkhvikderlvtp
tgkfnvyntmtdty
>d1aoqb1 1.3.1.2.1 (26-133) N-terminal (heme c) domain of cytochrome cd1-nitrite reductase {(Thiosphaera pantotropha)}
epsldnlaqqdvaapgapegvtalsdaqyneankiyfercagchgvlrkgatgkaltpdl
trdlgfdylqsfityaspagmpnwgtsgelsaeqvdlmanyllldpaa
>d1aoqb2 2.52.2.1.1 (134-567) C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase {(Triosphaera pantotropha)}
ppefgmkemreswkvhvapedrptqqmndwdlenlfsvtlrdagqialidgstyeiktvl
dtgyavhisrlsasgrylfvigrdgkvnmidlwmkepttvaeikigsearsietskmegw
edkyaiagaywppqyvimdgetlepkkiqstrgmtydeqeyhpeprvaailashyrpefi
vnvketgkillvdytdlnnlktteisaerflhdggldgshryfitaanarnklvvidtke
gklvaiedtggqtphpgrganfvhptfgpvwatshmgddsvaligtdpeghpdnawkild
sfpalgggslfikthpnsqylyvdatlnpeaeisgsvavfdikamtgdgsdpefktlpia
ewagitegqprvvqgefnkdgtevwfsvwngkdqesalvvvddktlelkhvikderlvtp
tgkfnvyntmtdty
>d1aora1 1.86.1.1.1 (211-605) Aldehyde ferredoxin oxidoreductase, C-terminal domains {(Pyrococcus furiosis)}
iadkqkfmlvvrekvnklrndpvaggglpkygtavlvniinenglypvknfqtgvypyay
eqsgeamaakylvrnkpcyacpigcgrvnrlptvgetegpeyesvwalganlgindlasi
ieanhmcdelgldtistggtlatamelyekghikdeelgdappfrwgntevlhyyiekia
kregfgdklaegsyrlaesyghpelsmtvkklelpaydprgaeghglgyatnnrggchik
nymispeilgypykmdphdvsddkikmlilfqdltalidsaglclfttfglgaddyrdll
naalgwdfttedylkigeriwnaerlfnlkagldparddtlpkrfleepmpegpnkghtv
rlkemlpryyklrgwtedgkipkekleelgiaefy
>d1aora2 4.94.1.1.1 (1-210) Aldehyde ferredoxin oxidoreductase, N-terminal domains {(Pyrococcus furiosis)}
mygnwgrfirvnlstgdikveeydeelakkwlgsrglaiylllkemdptvdplspenkli
iaagpltgtsaptggrynvvtkspltgfitmansggyfgaelkfagydaivvegkaekpv
yiyikdehieirdashiwgkkvseteatirkevgsekvkiasigpagenlvkfaaimndg
hraagrggvgavmgsknlkaiavegsktvp
>d1aorb1 1.86.1.1.1 (211-605) Aldehyde ferredoxin oxidoreductase, C-terminal domains {(Pyrococcus furiosis)}
iadkqkfmlvvrekvnklrndpvaggglpkygtavlvniinenglypvknfqtgvypyay
eqsgeamaakylvrnkpcyacpigcgrvnrlptvgetegpeyesvwalganlgindlasi
ieanhmcdelgldtistggtlatamelyekghikdeelgdappfrwgntevlhyyiekia
kregfgdklaegsyrlaesyghpelsmtvkklelpaydprgaeghglgyatnnrggchik
nymispeilgypykmdphdvsddkikmlilfqdltalidsaglclfttfglgaddyrdll
naalgwdfttedylkigeriwnaerlfnlkagldparddtlpkrfleepmpegpnkghtv
rlkemlpryyklrgwtedgkipkekleelgiaefy
>d1aorb2 4.94.1.1.1 (1-210) Aldehyde ferredoxin oxidoreductase, N-terminal domains {(Pyrococcus furiosis)}
mygnwgrfirvnlstgdikveeydeelakkwlgsrglaiylllkemdptvdplspenkli
iaagpltgtsaptggrynvvtkspltgfitmansggyfgaelkfagydaivvegkaekpv
yiyikdehieirdashiwgkkvseteatirkevgsekvkiasigpagenlvkfaaimndg
hraagrggvgavmgsknlkaiavegsktvp
>d1aosa_ 1.98.1.3.1 Argininosuccinate lyase {Human (Homo sapiens)}
imekfnasiaydrhlwevdvqgskaysrglekaglltkaemdqilhgldkvaeewaqgtf
klnsndedihtanerrlkeligatagklhtgrsrndqvvtdlrlwmrqtcstlsgllwel
irtmvdraeaerdvlfpgythlqraqpirwshwilshavaltrdserllevrkrinvlpl
gsgaiagnplgvdrellraelnfgaitlnsmdatserdfvaeflfwrslcmthlsrmaed
lilyctkefsfvqlsdaystgsslmpqkknpdslelirskagrvfgrcagllmtlkglps
tynkdlqedkeavfevsdtmsavlqvatgvistlqihqenmgqalspdmlatdlayylvr
kgmpfrqaheasgkavfmaetkgvalnqlslqelqtisplfsgdvicvwdyrhsveqyga
lggtarssvdwqirqvrallqaq
>d1aosb_ 1.98.1.3.1 Argininosuccinate lyase {Human (Homo sapiens)}
imekfnasiaydrhlwevdvqgskaysrglekaglltkaemdqilhgldkvaeewaqgtf
klnsndedihtanerrlkeligatagklhtgrsrndqvvtdlrlwmrqtcstlsgllwel
irtmvdraeaerdvlfpgythlqraqpirwshwilshavaltrdserllevrkrinvlpl
gsgaiagnplgvdrellraelnfgaitlnsmdatserdfvaeflfwrslcmthlsrmaed
lilyctkefsfvqlsdaystgsslmpqkknpdslelirskagrvfgrcagllmtlkglps
tynkdlqedkeavfevsdtmsavlqvatgvistlqihqenmgqalspdmlatdlayylvr
kgmpfrqaheasgkavfmaetkgvalnqlslqelqtisplfsgdvicvwdyrhsveqyga
lggtarssvdwqirqvrallqaq
>d1aotf_ 4.53.1.1.5 Tyrosine kinase Fyn {Human (Homo sapiens)}
siqaeewyfgklgrkdaerqllsfgnprgtfliresettkgayslsirdwddmkgdhvkh
ykirkldnggyyittraqfetlqqlvqhyseraaglssrlvvpshk
>d1aouf_ 4.53.1.1.5 Tyrosine kinase Fyn {Human (Homo sapiens)}
siqaeewyfgklgrkdaerqllsfgnprgtfliresettkgayslsirdwddmkgdhvkh
ykirkldnggyyittraqfetlqqlvqhyseraaglssrlvvpshk
>d1aov_1 3.82.1.2.3 (1-334) Ovotransferrin {Duck (Anas platyrhynchos)}
appkttvrwctissaeekkcnslkdhmqqervtlscvqkatyldcikaisnneadaisld
ggqvfeaglapyklkpiaaevyersggsttsyyavavvkkgtdfmikdlrgktschtglg
rsagwnipigtlihrediewegiesgiseqavakffsascvpgatieqklcrqckgdakt
kclrngpysgysgafqclkdgkgdvafvkhttvqenapeekdeyellcldgsrqpvdsyk
tcnwarvaahavvarddskiddiwsflgmqayslgvdttsdfhlfgppgkkdpvlkdllf
kdsaimlkrvpelmdsqlylgfeyysaiqslrkd
>d1aov_2 3.82.1.2.3 (335-686) Ovotransferrin {Duck (Anas platyrhynchos)}
qltvgprenkiqwcavgkdekskcdrwsvvsngevectilddnkdcivkitkgeadaisl
dggfvytagvcglvpvvgesyedetqcskdeeqpayyfavavvkkssaitwnnlqgkksc
htavgrtagwnipmglihnktgscdfddyfsegcapgsppnsrlcklcqgsgenllekcv
asshekyygytgalrclveqgdvafikhstvgenvsgsnkddwakgltrddfellctngk
raktmdyktchlakvpthavvarpekankirellegqeklfglhgtekerfmmfqsqtkd
llfkaltkclvklrqgitykeflgdeyyasvaslntcnpsdllqvctfledk
>d1aow__ 1.55.1.1.3 Annexin IV {bovine (Bos taurus)}
asgfnaaedaqtlrkamkglgtdedaiinvlayrstaqrqeirtaykttigrdlmddlks
elsgnfeqvilgmmtptvlydvqevrkamkgagtdegclieilasrtpeeirrinqtyql
qygrsleddirsdtsfmfqrvlvslsaggrdesnylddalmrqdaqdlyeagekkwgtde
vkfltvlcsrnrnhllhvfdeykriaqkdieqsiksetsgsfedallaivkcmrnksayf
aerlyksmkglgtdddtlirvmvsraeidmldiranfkrlygkslysfikgdtsgdyrkv
llilcggdd
>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__ 4.7.2.2.1 Modifier protein 1 (also HP1) {Mouse (Mus musculus)}
hmveevleeeeeeyvvekvldrrvvkgkveyllkwkgfsdedntwepeenldcpdliaef
lqsqktahetdks
>d1ap2a_ 2.1.1.1.87 Immunoglobulin (variable domains of L and H chains) {scFv c219}
divmtqspssltvtagekvtmsckssqsllnsgnqknyltwyqqkpgqppklliywastr
esgvpdrftgsgsgtdftltissvqaedlavyycqndysypltfgagtklep
>d1ap2b_ 2.1.1.1.87 Immunoglobulin (variable domains of L and H chains) {scFv c219}
evqlqqsgaelvrpgasvklsctasgfnikddfmhwvkqrpeqglewigridpandntky
apkfqdkatiiadtssntaylqlssltsedtavyycarrevysyyspldvwgagttvtvp
>d1ap2c_ 2.1.1.1.87 Immunoglobulin (variable domains of L and H chains) {scFv c219}
divmtqspssltvtagekvtmsckssqsllnsgnqknyltwyqqkpgqppklliywastr
esgvpdrftgsgsgtdftltissvqaedlavyycqndysypltfgagtklepg
>d1ap2d_ 2.1.1.1.87 Immunoglobulin (variable domains of L and H chains) {scFv c219}
evqlqqsgaelvrpgasvklsctasgfnikddfmhwvkqrpeqglewigridpandntky
apkfqdkatiiadtssntaylqlssltsedtavyycarrevysyyspldvwgagttvtvp
sgs
>d1ap4__ 1.37.1.5.4 Troponin C {Human (Homo sapiens), cardiac isoform}
mddiykaaveqlteeqknefkaafdifvlgaedgcistkelgkvmrmlgqnptpeelqem
idevdedgsgtvdfdeflvmmvrcmkdds
>d1ap5a1 1.2.4.1.4 (1-83) Mn superoxide dismutase (SOD) {human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaafvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1ap5a2 4.26.1.1.3 (84-198) Mn superoxide dismutase (SOD) {human (Homo sapiens)}
ngggepkgelleaikrdfgsfdkfkekltaasvgvqgsgwgwlgfnkerghlqiaacpnq
dplqgttglipllgidvwehayylqyknvrpdylkaiwnvinwenvterymackk
>d1ap5b1 1.2.4.1.4 (1-83) Mn superoxide dismutase (SOD) {human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaafvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1ap5b2 4.26.1.1.3 (84-198) Mn superoxide dismutase (SOD) {human (Homo sapiens)}
ngggepkgelleaikrdfgsfdkfkekltaasvgvqgsgwgwlgfnkerghlqiaacpnq
dplqgttglipllgidvwehayylqyknvrpdylkaiwnvinwenvterymackk
>d1ap6a1 1.2.4.1.4 (1-83) Mn superoxide dismutase (SOD) {human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaafvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1ap6a2 4.26.1.1.3 (84-198) Mn superoxide dismutase (SOD) {human (Homo sapiens)}
ngggepkgelleaikrdfgsfdkfkekltaasvgvqgsgwgwlgfnkerghlqiaacpnq
dplqgttglipllgidvwehayylqyknvrpdylkaiwnvinwenvterymackk
>d1ap6b1 1.2.4.1.4 (1-83) Mn superoxide dismutase (SOD) {human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaafvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1ap6b2 4.26.1.1.3 (84-198) Mn superoxide dismutase (SOD) {human (Homo sapiens)}
ngggepkgelleaikrdfgsfdkfkekltaasvgvqgsgwgwlgfnkerghlqiaacpnq
dplqgttglipllgidvwehayylqyknvrpdylkaiwnvinwenvterymackk
>d1ap8__ 4.47.1.1.1 Translation initiation factor eIF4e {Baker's yeast (Saccharomyces cerevisiae)}
msveevskkfeenvsvddttatpktvlsdsahfdvkhplntkwtlwytkpavdkseswsd
llrpvtsfqtveefwaiiqnipephelplksdyhvfrndvrpewedeanakggkwsfqlr
gkgadidelwlrtllavigetideddsqingvvlsirkggnkfalwtksedkepllrigg
kfkqvlkltddghleffphssangrhpqpsitl
>d1apa__ 4.102.1.1.5 Pokeweed antiviral protein alpha {pokeweed (Phytolacca americana)}
intitfdvgnatinkyatfmksihnqakdptlkcygipmlpntnltpkyllvtlqdsslk
titlmlkrnnlyvmgyadtyngkcryhifkdisntterndvmttlcpnpssrvgkninyd
ssypalekkvgrprsqvqlgiqilnsgigkiygvdsftekteaefllvaiqmvseaarfk
yienqvktnfnrafypnakvlnleeswgkistaihnakngaltsplelknangskwivlr
vddiepdvgllkyvngtcqat
>d1apb__ 3.81.1.1.2 L-arabinose-binding protein {(Escherichia coli)}
nlklgflvkqpeepwfqtewkfadkagkdlgfevikiavpdgektlnaidslaasgakgf
victpdpklgsaivakargydmkviavddqfvnakgkpmdtvplvmmaatkigerqgqel
ykemqkrgwdvkesavmaitaneldtarrrttgsmdalkaagfpekqiyqvptksndipg
afdaansmlvqhpevkhwlivgmndstvlggvrategqgfkaadiigigingvdavsels
kaqatgfygsllgspdvhgykssemlynwvakdveppkftevtdvvlitrdnfkeelekk
glggk
>d1apc__ 1.24.3.1.1 Cytochrome b562 {(Escherichia coli)}
adlednmetlndnlkviekadnaaqvkdaltkmraaaldaqkatppkledkspdspemkd
frhgfdilvgqiddalklanegkvkeaqaaaeqlkttrnayhqkyr
>d1apf__ 7.8.1.1.7 Anthopleurin-B {Giant green sea anemone (Anthopleura xanthogrammica)}
gvpclcdsdgprprgntlsgilwfypsgcpsgwhnckahgpnigwcckk
>d1apga_ 4.102.1.1.6 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_ 5.1.1.1.4 cAMP-dependent PK, catalytic subunit {mouse (Mus musculus)}
seqesvkeflakakedflkkwetpsqntaqldqfdriktlgtgsfgrvmlvkhkesgnhy
amkildkqkvvklkqiehtlnekrilqavnfpflvklefsfkdnsnlymvmeyvaggemf
shlrrigrfaepharfyaaqivltfeylhsldliyrdlkpenllidqqgyiqvtdfgfak
rvkgrtwtlcgtpeylapeiilskgynkavdwwalgvliyemaagyppffadqpiqiyek
ivsgkvrfpshfssdlkdllrnllqvdltkrfgnlkngvndiknhkwfattdwiaiyqrk
veapfipkfkgpgdtsnfddyeeeeirvsinekcgkeftef
>d1apna_ 2.21.1.1.1 Concanavalin A {jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1apnb_ 2.21.1.1.1 Concanavalin A {jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1apo__ 7.3.9.1.6 Factor X, N-terminal module {bovine (Bos taurus)}
kdgdqceghpclnqghckdgigdytctcaegfegkncefstr
>d1apq__ 7.3.9.1.18 Complement protease C1R {human (Homo sapiens)}
avdldecasrsksgeedpqpqcqhlchnyvggyfcscrpgyelqedrhscqae
>d1aps__ 4.34.11.1.2 Acylphosphatase {horse (Equus caballus)}
starplksvdyevfgrvqgvcfrmyaedearkigvvgwvkntskgtvtgqvqgpeekvns
mkswlskvgspssridrtnfsnektiskleysnfsvry
>d1apte_ 2.38.1.2.2 Acid protease {fungus (Penicillium janthinellum)}
aasgvatntptandeeyitpvtiggttlnlnfdtgsadlwvfstelpasqqsghsvynps
atgkelsgytwsisygdgssasgnvftdsvtvggvtahgqavqaaqqisaqfqqdtnndg
llglafssintvqpqsqttffdtvksslaqplfavalkhqqpgvydfgfidsskytgslt
ytgvdnsqgfwsfnvdsytagsqsgdgfsgiadtgttllllddsvvsqyysqvsgaqqds
naggyvfdcstnlpdfsvsisgytatvpgslinygpsgdgstclggiqsnsgigfsifgd
iflksqyvvfdsdgpqlgfapqa
>d1apue_ 2.38.1.2.2 Acid protease {fungus (Penicillium janthinellum)}
aasgvatntptandeeyitpvtiggttlnlnfdtgsadlwvfstelpasqqsghsvynps
atgkelsgytwsisygdgssasgnvftdsvtvggvtahgqavqaaqqisaqfqqdtnndg
llglafssintvqpqsqttffdtvksslaqplfavalkhqqpgvydfgfidsskytgslt
ytgvdnsqgfwsfnvdsytagsqsgdgfsgiadtgttllllddsvvsqyysqvsgaqqds
naggyvfdcstnlpdfsvsisgytatvpgslinygpsgdgstclggiqsnsgigfsifgd
iflksqyvvfdsdgpqlgfapqa
>d1apve_ 2.38.1.2.2 Acid protease {fungus (Penicillium janthinellum)}
aasgvatntptandeeyitpvtiggttlnlnfdtgsadlwvfstelpasqqsghsvynps
atgkelsgytwsisygdgssasgnvftdsvtvggvtahgqavqaaqqisaqfqqdtnndg
llglafssintvqpqsqttffdtvksslaqplfavalkhqqpgvydfgfidsskytgslt
ytgvdnsqgfwsfnvdsytagsqsgdgfsgiadtgttllllddsvvsqyysqvsgaqqds
naggyvfdcstnlpdfsvsisgytatvpgslinygpsgdgstclggiqsnsgigfsifgd
iflksqyvvfdsdgpqlgfapqa
>d1apwe_ 2.38.1.2.2 Acid protease {fungus (Penicillium janthinellum)}
aasgvatntptandeeyitpvtiggttlnlnfdtgsadlwvfstelpasqqsghsvynps
atgkelsgytwsisygdgssasgnvftdsvtvggvtahgqavqaaqqisaqfqqdtnndg
llglafssintvqpqsqttffdtvksslaqplfavalkhqqpgvydfgfidsskytgslt
ytgvdnsqgfwsfnvdsytagsqsgdgfsgiadtgttllllddsvvsqyysqvsgaqqds
naggyvfdcstnlpdfsvsisgytatvpgslinygpsgdgstclggiqsnsgigfsifgd
iflksqyvvfdsdgpqlgfapqa
>d1apxa_ 1.72.1.1.5 Ascorbate peroxidase {Pea (Pisum sativum)}
gksyptvspdyqkaiekakrklrgfiaekkcaplilrlawhsagtfdsktktggpfgtik
hqaelahganngldiavrllepikeqfpivsyadfyqlagvvaveitggpevpfhpgred
kpepppegrlpdatkgsdhlrdvfgkamglsdqdivalsgghtigaahkersgfegpwts
nplifdnsyftelltgekdgllqlpsdkalltdsvfrplvekyaadedvffadyaeahlk
lselgfaea
>d1apxb_ 1.72.1.1.5 Ascorbate peroxidase {Pea (Pisum sativum)}
gksyptvspdyqkaiekakrklrgfiaekkcaplilrlawhsagtfdsktktggpfgtik
hqaelahganngldiavrllepikeqfpivsyadfyqlagvvaveitggpevpfhpgred
kpepppegrlpdatkgsdhlrdvfgkamglsdqdivalsgghtigaahkersgfegpwts
nplifdnsyftelltgekdgllqlpsdkalltdsvfrplvekyaadedvffadyaeahlk
lselgfaea
>d1apxc_ 1.72.1.1.5 Ascorbate peroxidase {Pea (Pisum sativum)}
gksyptvspdyqkaiekakrklrgfiaekkcaplilrlawhsagtfdsktktggpfgtik
hqaelahganngldiavrllepikeqfpivsyadfyqlagvvaveitggpevpfhpgred
kpepppegrlpdatkgsdhlrdvfgkamglsdqdivalsgghtigaahkersgfegpwts
nplifdnsyftelltgekdgllqlpsdkalltdsvfrplvekyaadedvffadyaeahlk
lselgfaea
>d1apxd_ 1.72.1.1.5 Ascorbate peroxidase {Pea (Pisum sativum)}
gksyptvspdyqkaiekakrklrgfiaekkcaplilrlawhsagtfdsktktggpfgtik
hqaelahganngldiavrllepikeqfpivsyadfyqlagvvaveitggpevpfhpgred
kpepppegrlpdatkgsdhlrdvfgkamglsdqdivalsgghtigaahkersgfegpwts
nplifdnsyftelltgekdgllqlpsdkalltdsvfrplvekyaadedvffadyaeahlk
lselgfaea
>e1apy.1a 4.95.1.4.1 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Human (Homo sapiens)}
splplvvntwpfknateaawralasggsaldavesgcamcereqcdgsvgfggspdelge
ttldamimdgttmdvgavgdlrriknaigvarkvlehtthtllvgesattfaqsmgfine
dlstsasqalhsdwlarncqpnywrnvipdpskycgpykpp
>e1apy.1b 4.95.1.4.1 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Human (Homo sapiens)}
tigmvvihktghiaagtstngikfkihgrvgdspipgagayaddtagaaaatgngdilmr
flpsyqaveymrrgedptiacqkvisriqkhfpeffgavicanvtgsygaacnklstftq
fsfmvynseknqpteekvdci
>e1apy.2c 4.95.1.4.1 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Human (Homo sapiens)}
splplvvntwpfknateaawralasggsaldavesgcamcereqcdgsvgfggspdelge
ttldamimdgttmdvgavgdlrriknaigvarkvlehtthtllvgesattfaqsmgfine
dlstsasqalhsdwlarncqpnywrnvipdpskycgpykpp
>e1apy.2d 4.95.1.4.1 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Human (Homo sapiens)}
tigmvvihktghiaagtstngikfkihgrvgdspipgagayaddtagaaaatgngdilmr
flpsyqaveymrrgedptiacqkvisriqkhfpeffgavicanvtgsygaacnklstftq
fsfmvynseknqpteekvdci
>e1apz.1a 4.95.1.4.1 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Human (Homo sapiens)}
splplvvntwpfknateaawralasggsaldavesgcamcereqcdgsvgfggspdelge
ttldamimdgttmdvgavgdlrriknaigvarkvlehtthtllvgesattfaqsmgfine
dlstsasqalhsdwlarncqpnywrnvipdpskycgpykpp
>e1apz.1b 4.95.1.4.1 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Human (Homo sapiens)}
tigmvvihktghiaagtstngikfkihgrvgdspipgagayaddtagaaaatgngdilmr
flpsyqaveymrrgedptiacqkvisriqkhfpeffgavicanvtgsygaacnklstftq
fsfmvynseknqpteekvdci
>e1apz.2c 4.95.1.4.1 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Human (Homo sapiens)}
splplvvntwpfknateaawralasggsaldavesgcamcereqcdgsvgfggspdelge
ttldamimdgttmdvgavgdlrriknaigvarkvlehtthtllvgesattfaqsmgfine
dlstsasqalhsdwlarncqpnywrnvipdpskycgpykpp
>e1apz.2d 4.95.1.4.1 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Human (Homo sapiens)}
tigmvvihktghiaagtstngikfkihgrvgdspipgagayaddtagaaaatgngdilmr
flpsyqaveymrrgedptiacqkvisriqkhfpeffgavicanvtgsygaacnklstftq
fsfmvynseknqpteekvdci
>d1aq0a_ 3.1.1.3.7 plant beta-glucanases {barley (Hordeum vulgare) 1,3-1,4-beta-glucanase}
igvcygmsannlpaastvvsmfksngiksmrlyapnqaalqavggtginvvvgapndvls
nlaaspaaaaswvksniqaypkvsfryvcvgnevaggatrnlvpamknvhgalvaaglgh
ikvttsvsqailgvfsppsagsftgeaaafmgpvvqflartnaplmaniypylawaynps
amdmgyalfnasgtvvrdgaygyqnlfdttvdafytamgkhggssvklvvsesgwpsggg
taatpanarfynqhlinhvgrgtprhpgaietyifamfnenqkdsgveqnwglfypnmqh
vypinf
>d1aq0b_ 3.1.1.3.7 plant beta-glucanases {barley (Hordeum vulgare) 1,3-1,4-beta-glucanase}
igvcygmsannlpaastvvsmfksngiksmrlyapnqaalqavggtginvvvgapndvls
nlaaspaaaaswvksniqaypkvsfryvcvgnevaggatrnlvpamknvhgalvaaglgh
ikvttsvsqailgvfsppsagsftgeaaafmgpvvqflartnaplmaniypylawaynps
amdmgyalfnasgtvvrdgaygyqnlfdttvdafytamgkhggssvklvvsesgwpsggg
taatpanarfynqhlinhvgrgtprhpgaietyifamfnenqkdsgveqnwglfypnmqh
vypinf
>d1aq1__ 5.1.1.1.1 Cyclin-dependent PK {Human (Homo sapiens)}
menfqkvekigegtygvvykarnkltgevvalkkirldtetegvpstaireisllkelnh
pnivklldvihtenklylvfeflhqdlkkfmdasaltgiplpliksylfqllqglafchs
hrvlhrdlkpqnllintegaikladfglarafgvpvrtythevvtlwyrapeillgckyy
stavdiwslgcifaemvtrralfpgdseidqlfrifrtlgtpdevvwpgvtsmpdykpsf
pkwarqdfskvvppldedgrsllsqmlhydpnkrisakaalahpffqdvtkpvphlrl
>d1aq3a_ 4.46.1.1.1 MS2 virus coat protein {(bacteriophage MS2)}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvtcsvrqssaqnrkysi
kvevpkvatqtvggvelpvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1aq3b_ 4.46.1.1.1 MS2 virus coat protein {(bacteriophage MS2)}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvtcsvrqssaqnrkysi
kvevpkvatqtvggvelpvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1aq3c_ 4.46.1.1.1 MS2 virus coat protein {(bacteriophage MS2)}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvtcsvrqssaqnrkysi
kvevpkvatqtvggvelpvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1aq4a_ 4.46.1.1.1 MS2 virus coat protein {(bacteriophage MS2)}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvacsvrqssaqnrkyti
kvevpkvatqtvggvelpvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1aq4b_ 4.46.1.1.1 MS2 virus coat protein {(bacteriophage MS2)}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvacsvrqssaqnrkyti
kvevpkvatqtvggvelpvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1aq4c_ 4.46.1.1.1 MS2 virus coat protein {(bacteriophage MS2)}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvacsvrqssaqnrkyti
kvevpkvatqtvggvelpvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1aq5a_ 1.105.5.1.1 Chicken cartilage matrix protein {Chicken (Gallus gallus)}
gshmeedpcecksivkfqtkveelintlqqkleavakriealenkii
>d1aq5b_ 1.105.5.1.1 Chicken cartilage matrix protein {Chicken (Gallus gallus)}
gshmeedpcecksivkfqtkveelintlqqkleavakriealenkii
>d1aq5c_ 1.105.5.1.1 Chicken cartilage matrix protein {Chicken (Gallus gallus)}
gshmeedpcecksivkfqtkveelintlqqkleavakriealenkii
>d1aq6a_ 5.18.1.1.2 L-2-Haloacid dehalogenase {(Xanthobacter autotrophicus)}
mikavvfdaygtlfdvqsvadateraypgrgeyitqvwrqkqleyswlralmgryadfwg
vtrealaytlgtlglepdesfladmaqaynrltpypdaaqclaelaplkrailsngapdm
lqalvanagltdsfdavisvdakrvfkphpdsyalveevlgvtpaevlfvssngfdvgga
knfgfsvarvarlsqealarelvsgtiapltmfkalrmreetyaeapdfvvpalgdlprl
vrgma
>d1aq6b_ 5.18.1.1.2 L-2-Haloacid dehalogenase {(Xanthobacter autotrophicus)}
mikavvfdaygtlfdvqsvadateraypgrgeyitqvwrqkqleyswlralmgryadfwg
vtrealaytlgtlglepdesfladmaqaynrltpypdaaqclaelaplkrailsngapdm
lqalvanagltdsfdavisvdakrvfkphpdsyalveevlgvtpaevlfvssngfdvgga
knfgfsvarvarlsqealarelvsgtiapltmfkalrmreetyaeapdfvvpalgdlprl
vrgma
>d1aq7__ 2.35.1.2.1 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__ 4.70.1.1.2 Cytochrome b5 {rat (Rattus norvegicus)}
kyytleeiqkhkdskstwvilhhkvydltkfleehpggeevlreqaggdatenfedvghs
tdarelsktyiigelhpddrskia
>d1aqb__ 2.45.1.1.2 Retinol binding protein {Pig (Sus scrofa domesticus)}
erdcrvssfrvkenfdkarfsgtwyamakkdpeglflqdnivaefsvdenghmsatakgr
vrllnnwdvcadmvgtftdtedpakfkmkywgvasflqkgnddhwiidtdydtyavqysc
rlqnldgtcadsysfvfardphgfspevqkivrqrqeelclarqyriithngycd
>d1aqca_ 2.41.1.2.1 X11 {Human (Homo sapiens)}
edlidgiifaanylgstqllsdktpsknvrxxqaqeavsrikxaqklaksrkkapegesq
pxtevdlfiltqrikvlnadtqetxxdhplrtisyiadignivvlxarrriprsnsqenv
eashpsqdgkrqykxichvfesedaqliaqsigqafsvayqeflr
>d1aqcb_ 2.41.1.2.1 X11 {Human (Homo sapiens)}
iifaanylgstqllsdktpsknvrxxqaqeavsrikxaqklaksrkkapegesqpxtevd
lfiltqrikvlnadtqetxxdhplrtisyiadignivvlxarrriprsnsqenveashps
qdgkrqykxichvfesedaqliaqsigqafsvayqeflranginp
>d1aqda1 2.1.1.2.114 (82-181) Class II MHC, C-terminal domains of alpha and beta chains {(human hla-dr1)}
itnvppevtvltnspvelrepnvlicfidkftppvvnvtwlrngkpvttgvsetvflpre
dhlfrkfhylpflpstedvydcrvehwgldepllkhwefd
>d1aqda2 4.15.1.1.3 (3-81) MHC class II, N-terminal domains of alpha and beta chains {(human hla-dr1)}
eehviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgalan
iavdkanleimtkrsnytp
>d1aqdb1 2.1.1.2.114 (93-190) Class II MHC, C-terminal domains of alpha and beta chains {(human hla-dr1)}
rrvepkvtvypsktqplqhhnllvcsvsgfypgsievrwfrngqeekagvvstgliqngd
wtfqtlvmletvprsgevytcqvehpsvtspltvewra
>d1aqdb2 4.15.1.1.3 (4-92) MHC class II, N-terminal domains of alpha and beta chains {(human hla-dr1)}
rprflwqlkfechffngtervrllerciynqeesvrfdsdvgeyravtelgrpdaeywns
qkdlleqrraavdtycrhnygvgesftvq
>d1aqdd1 2.1.1.2.114 (82-179) Class II MHC, C-terminal domains of alpha and beta chains {(human hla-dr1)}
itnvppevtvltnspvelrepnvlicfidkftppvvnvtwlrngkpvttgvsetvflpre
dhlfrkfhylpflpstedvydcrvehwgldepllkhwe
>d1aqdd2 4.15.1.1.3 (3-81) MHC class II, N-terminal domains of alpha and beta chains {(human hla-dr1)}
eehviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgalan
iavdkanleimtkrsnytp
>d1aqde1 2.1.1.2.114 (93-190) Class II MHC, C-terminal domains of alpha and beta chains {(human hla-dr1)}
rrvepkvtvypsktqplqhhnllvcsvsgfypgsievrwfrngqeekagvvstgliqngd
wtfqtlvmletvprsgevytcqvehpsvtspltvewra
>d1aqde2 4.15.1.1.3 (4-92) MHC class II, N-terminal domains of alpha and beta chains {(human hla-dr1)}
rprflwqlkfechffngtervrllerciynqeesvrfdsdvgeyravtelgrpdaeywns
qkdlleqrraavdtycrhnygvgesftvq
>d1aqdg1 2.1.1.2.114 (82-179) Class II MHC, C-terminal domains of alpha and beta chains {(human hla-dr1)}
itnvppevtvltnspvelrepnvlicfidkftppvvnvtwlrngkpvttgvsetvflpre
dhlfrkfhylpflpstedvydcrvehwgldepllkhwe
>d1aqdg2 4.15.1.1.3 (3-81) MHC class II, N-terminal domains of alpha and beta chains {(human hla-dr1)}
eehviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgalan
iavdkanleimtkrsnytp
>d1aqdh1 2.1.1.2.114 (93-190) Class II MHC, C-terminal domains of alpha and beta chains {(human hla-dr1)}
rrvepkvtvypsktqplqhhnllvcsvsgfypgsievrwfrngqeekagvvstgliqngd
wtfqtlvmletvprsgevytcqvehpsvtspltvewra
>d1aqdh2 4.15.1.1.3 (4-92) MHC class II, N-terminal domains of alpha and beta chains {(human hla-dr1)}
rprflwqlkfechffngtervrllerciynqeesvrfdsdvgeyravtelgrpdaeywns
qkdlleqrraavdtycrhnygvgesftvq
>d1aqdj1 2.1.1.2.114 (82-179) Class II MHC, C-terminal domains of alpha and beta chains {(human hla-dr1)}
itnvppevtvltnspvelrepnvlicfidkftppvvnvtwlrngkpvttgvsetvflpre
dhlfrkfhylpflpstedvydcrvehwgldepllkhwe
>d1aqdj2 4.15.1.1.3 (3-81) MHC class II, N-terminal domains of alpha and beta chains {(human hla-dr1)}
eehviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgalan
iavdkanleimtkrsnytp
>d1aqdk1 2.1.1.2.114 (93-190) Class II MHC, C-terminal domains of alpha and beta chains {(human hla-dr1)}
rrvepkvtvypsktqplqhhnllvcsvsgfypgsievrwfrngqeekagvvstgliqngd
wtfqtlvmletvprsgevytcqvehpsvtspltvewra
>d1aqdk2 4.15.1.1.3 (4-92) MHC class II, N-terminal domains of alpha and beta chains {(human hla-dr1)}
rprflwqlkfechffngtervrllerciynqeesvrfdsdvgeyravtelgrpdaeywns
qkdlleqrraavdtycrhnygvgesftvq
>d1aqe__ 1.107.1.1.1 Cytochrome c3 {(Desulfovibrio desulfuricans), different strains}
tfeipesvtmspkqfegytpkkgdvtfnhashmdiacqqchhtvpdtytiescmtegchd
nikerteissvertfhttkdsekscvgchrelkrqgpsdaplacnschvq
>d1aqia_ 3.53.1.5.2 DNA methylase TaqI, coenzyme-binding domain {(Thermus aquaticus)}
vetppevvdfmvslaeaprggrvlepacahgpflrafreahgtgyrfvgveidpkaldlp
pwaegiladfllwepgeafdlilgnppygivgeaskypihvfkavkdlykkafstwkgky
nlygaflekavrllkpggvlvfvvpatwlvledfallreflaregktsvyylgevfpqkk
vsavvirfqksgkglslwdtqesesgftpilwaeyphwegeiirfeteetrkleisgmpl
gdlfhirfaarspefkkhpavrkepgpglvpvltgrnlkpgwvdyeknhsglwmpkerak
elrdfyatphlvvahtkgtrvvaawderaypwreefhllpkegvrldpstlvqwlnseam
qkhvrtlyrdfvphltlrmlerlpvrreygfht
>d1aqib_ 3.53.1.5.2 DNA methylase TaqI, coenzyme-binding domain {(Thermus aquaticus)}
vetppevvdfmvslaeaprggrvlepacahgpflrafreahgtgyrfvgveidpkaldlp
pwaegiladfllwepgeafdlilgnppygivgeaskypihvfkavkdlykkafstwkgky
nlygaflekavrllkpggvlvfvvpatwlvledfallreflaregktsvyylgevfpqkk
vsavvirfqksgkglslwdtqesesgftpilwaeyphwegeiirfeteetrkleisgmpl
gdlfhirfaarspefkkhpavrkepgpglvpvltgrnlkpgwvdyeknhsglwmpkerak
elrdfyatphlvvahtkgtrvvaawderaypwreefhllpkegvrldpstlvqwlnseam
qkhvrtlyrdfvphltlrmlerlpvrreygfht
>d1aqja_ 3.53.1.5.2 DNA methylase TaqI, coenzyme-binding domain {(Thermus aquaticus)}
vetppevvdfmvslaeaprggrvlepacahgpflrafreahgtgyrfvgveidpkaldlp
pwaegiladfllwepgeafdlilgnppygivgeaskypihvfkavkdlykkafstwkgky
nlygaflekavrllkpggvlvfvvpatwlvledfallreflaregktsvyylgevfpqkk
vsavvirfqksgkglslwdtqesesgftpilwaeyphwegeiirfeteetrkleisgmpl
gdlfhirfaarspefkkhpavrkepgpglvpvltgrnlkpgwvdyeknhsglwmpkerak
elrdfyatphlvvahtkgtrvvaawderaypwreefhllpkegvrldpsslvqwlnseam
qkhvrtlyrdfvphltlrmlerlpvrreygfht
>d1aqjb_ 3.53.1.5.2 DNA methylase TaqI, coenzyme-binding domain {(Thermus aquaticus)}
vetppevvdfmvslaeaprggrvlepacahgpflrafreahgtgyrfvgveidpkaldlp
pwaegiladfllwepgeafdlilgnppygivgeaskypihvfkavkdlykkafstwkgky
nlygaflekavrllkpggvlvfvvpatwlvledfallreflaregktsvyylgevfpqkk
vsavvirfqksgkglslwdtqesesgftpilwaeyphwegeiirfeteetrkleisgmpl
gdlfhirfaarspefkkhpavrkepgpglvpvltgrnlkpgwvdyeknhsglwmpkerak
elrdfyatphlvvahtkgtrvvaawderaypwreefhllpkegvrldpsslvqwlnseam
qkhvrtlyrdfvphltlrmlerlpvrreygfht
>d1aqkh1 2.1.1.1.90 (2-123) Immunoglobulin (variable domains of L and H chains) {Fab B7-15A2 (human), lambda L chain}
vqlvesgggvvqpgrslrlscaasgftfnnyaihwvrqapgkglewvafisydgsknyya
dsvkgrftisrdnskntlflqmnslrpedtaiyycarvlfqqlvlyapfdiwgqgtmvtv
ss
>d1aqkh2 2.1.1.2.91 (124-226) Immunoglobulin (constant domains of L and H chains) {Fab B7-15A2 (human), lambda L chain}
astkgpsvfplapsskstsggtaalgclvkdyfpqpvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkvepksc
>d1aqkl1 2.1.1.1.90 (2-111) Immunoglobulin (variable domains of L and H chains) {Fab B7-15A2 (human), lambda L chain}
nvltqppsvsgapgqrvtisctgsnsnigagftvhwyqhlpgtapkllifantnrpsgvp
drfsgsksgtsaslaitglqaedeadyycqsydsslsarfgggtrltvlg
>d1aqkl2 2.1.1.2.91 (112-216) Immunoglobulin (constant domains of L and H chains) {Fab B7-15A2 (human), lambda L chain}
qpkaapsvtlfppsseelqankatlvclisdfypgavtvawkadsspvnagvettkpskq
snnkyaassylsltpeqwkshksyscqvthegstvektvapaecs
>d1aqn__ 3.33.1.1.6 Subtilisin Novo/BPN' {(Bacillus amyloliquefaciens)}
aqsvpygvsqikapalhsqgycgsnvkvavidsgidsshpdlkvaggasfvpsetnpfqd
nnshgthvagtvaalnnsigvlgvapcaslyavkvlgadgsgqyswiingiewaiannmd
vinmslggpsgsaalkaavdkavasgvvvvaaagnegtsgssstvgypakypsviavgav
dssnqrasfssvgpeldvmapgvsicstlpgnkygaksgtsmasphvagaaalilskhpn
wtntqvrsslentttklgdsfyygkglinvqaaaq
>d1aqp__ 4.4.1.1.1 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__ 2.70.1.1.1 Epsilon subunit of F1F0-ATP synthase {(Escherichia coli)}
styhldvvsaeqqmfsglvekiqvtgsegelgiypghaplltaikpgmirivkqhgheef
iylsggilevqpgnvtvladtairgqdldearameakrkaeehissshgdvdyaqasael
akaiaqlrvieltkk
>d1aqva1 1.43.1.1.4 (77-209) Glutathione S-transferase {human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d1aqva2 3.38.1.4.4 (1-76) Glutathione S-transferase {human (Homo sapiens) class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d1aqvb1 1.43.1.1.4 (77-209) Glutathione S-transferase {human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d1aqvb2 3.38.1.4.4 (1-76) Glutathione S-transferase {human (Homo sapiens) class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d1aqwa1 1.43.1.1.4 (77-207) Glutathione S-transferase {human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingng
>d1aqwa2 3.38.1.4.4 (1-76) Glutathione S-transferase {human (Homo sapiens) class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d1aqwb1 1.43.1.1.4 (77-207) Glutathione S-transferase {human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingng
>d1aqwb2 3.38.1.4.4 (1-76) Glutathione S-transferase {human (Homo sapiens) class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d1aqwc1 1.43.1.1.4 (77-207) Glutathione S-transferase {human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingng
>d1aqwc2 3.38.1.4.4 (1-76) Glutathione S-transferase {human (Homo sapiens) class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d1aqwd1 1.43.1.1.4 (77-207) Glutathione S-transferase {human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingng
>d1aqwd2 3.38.1.4.4 (1-76) Glutathione S-transferase {human (Homo sapiens) class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d1aqxa1 1.43.1.1.4 (77-207) Glutathione S-transferase {human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingng
>d1aqxa2 3.38.1.4.4 (2-76) Glutathione S-transferase {human (Homo sapiens) class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d1aqxb1 1.43.1.1.4 (77-207) Glutathione S-transferase {human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingng
>d1aqxb2 3.38.1.4.4 (2-76) Glutathione S-transferase {human (Homo sapiens) class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d1aqxc1 1.43.1.1.4 (77-207) Glutathione S-transferase {human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingng
>d1aqxc2 3.38.1.4.4 (2-76) Glutathione S-transferase {human (Homo sapiens) class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d1aqxd1 1.43.1.1.4 (77-207) Glutathione S-transferase {human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingng
>d1aqxd2 3.38.1.4.4 (2-76) Glutathione S-transferase {human (Homo sapiens) class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d1aqza_ 4.1.1.1.9 Ribotoxin restrictocin {Fungus (Aspergilus restrictus)}
atwtcinqqlnpktnkwedkrllysqakaesnshhaplsdgktgssyphwftngydgngk
likgrtpikfgkadcdrppkhsqngmgkddhyllefptfpdghdykfdskkpkenpgpar
viytypnkvfcgivahqrgnqgdlrlcsh
>d1aqzb_ 4.1.1.1.9 Ribotoxin restrictocin {Fungus (Aspergilus restrictus)}
atwtcinqqlnpktnkwedkrllysqakaesnshhaplsdgktgssyphwftngydgngk
likgrtpikfgkadcdrppkhsqngmgkddhyllefptfpdghdykfdskkpkenpgpar
viytypnkvfcgivahqrgnqgdlrlcsh
>d1ar0a_ 4.13.3.2.1 Nuclear transport factor-2 (NTF2) {Rat (Rattus norvegicus)}
gdkpiweqigssfiqhyyqlfdndrtqlgaiyidascltwkgqqfqgkaaiveklsslpf
qkiqhsitaqdhqptpdsciismvvgqlkadedpimgfhqmfllknindawvctndmfrl
alhnf
>d1ar0b_ 4.13.3.2.1 Nuclear transport factor-2 (NTF2) {Rat (Rattus norvegicus)}
kpiweqigssfiqhyyqlfdndrtqlgaiyidascltwkgqqfqgkaaiveklsslpfqk
iqhsitaqdhqptpdsciismvvgqlkadedpimgfhqmfllknindawvctndmfrlal
h
>d1ar1b1 2.5.1.2.3 (108-252) Cytochrome c oxidase {(Paracoccus denitrificans)}
ndpdlvikaighqwywsyeypndgvafdalmlekealadagysedeyllatdnpvvvpvg
kkvlvqvtatdvihawtipafavkqdavpgriaqlwfsvdqegvyfgqcselcginhaym
pivvkavsqekyeawlagakeefaa
>d1ar1b2 6.5.1.1.4 (1-107) Cytochrome c oxidase {(Paracoccus denitrificans)}
qdvlgdlpvigkpvnggmnfqpassplahdqqwldhfvlyiitavtifvcllllicivrf
nrranpvparfthntpieviwtlvpvlilvaigafslpilfrsqemp
>d1ar1c_ 2.1.1.1.92 Immunoglobulin (variable domains of L and H chains) {Fv against Paracoccus denitrificans cytochrome c oxidase (mouse), kappa L chain}
evklqesggdlvqpggslklscaasgftfssytmswvrqtpekrlewvasinngggrtyy
pdtvkgrftisrdnakntlylqmsslksedtamyycvrheyyyamdywgqgttvtvss
>d1ar1d_ 2.1.1.1.92 Immunoglobulin (variable domains of L and H chains) {Fv against Paracoccus denitrificans cytochrome c oxidase (mouse), kappa L chain}
dieltqtpvslsasvgetvtitcraseniysylawyqqkqgkspqflvynaktlgegvps
rfsgsgsgtqfslkinsllpedfgsyycqhhygtppltfgggtkleik
>d1ar2__ 2.1.1.1.109 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (kappa) dimer REI (human)}
tpdiqmtqspsslsasvgdrvtitvqasqdiikhlnwyqqtpgkapklliyeasnlqagv
psrfsgsgsgtdytftisslqpediatyycqqyqslpytfgqgtklqit
>d1ar3_1 3.5.2.1.1 (529-754) Aconitase, C-terminal domain {pig (Sus scrofa)}
vdvsptsqrlqllepfdkwdgkdledlqilikvkgkcttdhisaagpwlkfrghldnisn
nlligainienrkansvrnavtqefgpvpdtaryykqhgirwvvigdenygegasrehsa
leprhlggraiitksfarihetnlkkqgllpltfadpadynkihpvdkltiqglkdfapg
kplkciikhpngtqetillnhtfnetqiewfragsalnrmkelqqk
>d1ar3_2 3.71.1.1.1 (2-528) Aconitase, first 3 domains {pig (Sus scrofa)}
rakvamshfepheyirydlleknidivrkrlnrpltlsekivyghlddpanqeiergkty
lrlrpdrvamqdataqmamlqfissglpkvavpstihcdhlieaqlggekdlrrakdinq
evynflatagakygvgfwrpgsgiihqiilenyaypgvlligtdshtpnggglggicigv
ggadavdvmagipwelkcpkvigvkltgslsgwtspkdvilkvagiltvkggtgaiveyh
gpgvdsisctgmaticnmgaeigattsvfpynhrmkkylsktgradianladefkdhlvp
dpgchydqvieinlselkphingpftpdlahpvaevgsvaekegwpldirvgligsctns
syedmgrsaavakqalahglkcksqftitpgseqiratierdgyaqvlrdvggivlanac
gpcigqwdrkdikkgekntivtsynrnftgrndanpethafvtspeivtalaiagtlkfn
petdfltgkdgkkfkleapdadelpraefdpgqdtyqhppkdssgqr
>d1ar4a1 1.2.4.1.7 (1-86) Cambialistic superoxide dismutase {(Propionibacterium freudenreichii)}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1ar4a2 4.26.1.1.7 (87-201) Cambialistic superoxide dismutase {(Propionibacterium freudenreichii) shermani}
saperptdelgaaideffgsfdnmkaqftaaatgiqgsgwaslvwdplgkrintlqfydh
qnnlpagsipllqldmwehafylqyknvkgdyvkswwnvvnwddvalrfsearva
>d1ar4b1 1.2.4.1.7 (1-86) Cambialistic superoxide dismutase {(Propionibacterium freudenreichii)}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1ar4b2 4.26.1.1.7 (87-201) Cambialistic superoxide dismutase {(Propionibacterium freudenreichii) shermani}
saperptdelgaaideffgsfdnmkaqftaaatgiqgsgwaslvwdplgkrintlqfydh
qnnlpagsipllqldmwehafylqyknvkgdyvkswwnvvnwddvalrfsearva
>d1ar5a1 1.2.4.1.7 (1-86) Cambialistic superoxide dismutase {(Propionibacterium freudenreichii)}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1ar5a2 4.26.1.1.7 (87-201) Cambialistic superoxide dismutase {(Propionibacterium freudenreichii) shermani}
saperptdelgaaideffgsfdnmkaqftaaatgiqgsgwaslvwdplgkrintlqfydh
qnnlpagsipllqldmwehafylqyknvkgdyvkswwnvvnwddvalrfsearva
>d1ar5b1 1.2.4.1.7 (1-86) Cambialistic superoxide dismutase {(Propionibacterium freudenreichii)}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1ar5b2 4.26.1.1.7 (87-201) Cambialistic superoxide dismutase {(Propionibacterium freudenreichii) shermani}
saperptdelgaaideffgsfdnmkaqftaaatgiqgsgwaslvwdplgkrintlqfydh
qnnlpagsipllqldmwehafylqyknvkgdyvkswwnvvnwddvalrfsearva
>d1ar61_ 2.8.1.4.3 Poliovirus {poliovirus (type 1, mahoney strain)}
aatsrdalpnteasgpthskeipaltavetgatnplvpsdtvqtrhvvqhrsrsessies
ffargacvtimtvdnsasttnkdklfavwkitykdtvqlrrklefftysrfdmeltfvvt
anftetnnghalnqvyqimyippgapvpekwddytwqtssnpsifytygtaparisvpyv
gisnayshfydgfskvplkdqsaalgdslygaaslndfgilavrvvndhnptkvtskirv
ylkpkhirvwcprppravayygpgvdykdgtltplstkdltty
>d1ar62_ 2.8.1.4.3 Poliovirus {poliovirus (type 1, mahoney strain)}
eacgysdrvlqltlgnstittqeaansvvaygrwpeylrdseanpvdqptepdvaacrfy
tldtvswtkesrgwwwklpdalrdmglfgqnmyyhylgrsgytvhvqcnaskfhqgalgv
favpemclagdsntttmhtsyqnanpgekggtftgtftpdnnqtsparrfcpvdyllgng
tllgnafvfphqiinlrtnncatlvlpyvnslsidsmvkhnnwgiailplaplnfasess
peipitltiapmccefnglrnitlprlq
>d1ar63_ 2.8.1.4.3 Poliovirus {poliovirus (type 1, mahoney strain)}
glpvmntpgsnqyltadnfqspcalpefdvtppidipgevknmmelaeidtmipfdlsat
kkntmemyrvrlsdkphtddpilclslspasdprlshtmlgeilnyythwagslkftflf
cgsmmatgkllvsyappgadppkkrkeamlgthviwdiglqssctmvvpwisnttyrqti
ddsfteggyisvfyqtrivvplstpremdilgfvsacndfsvrllrdtthieqka
>d1ar71_ 2.8.1.4.3 Poliovirus {poliovirus (type 1, mahoney strain)}
aatsrdalpnteasgpthskeipaltavetgatnplvpsdtvqtrhvvqhrsrsessies
ffargacvtimtvdnsasttnkdklfavwkitykdtvqlrrklefftysrfdmeltfvvt
anftetnnghalnqvyqimyvppgapvpekwddytwqtssnpsifytygtaparisvpyv
gisnayshfydgfskvplkdqsaalgdslygaaslndfgilavrvvndhnptkvtskirv
ylkpkhirvwcprppravayygpgvdykdgtltplstkdltty
>d1ar72_ 2.8.1.4.3 Poliovirus {poliovirus (type 1, mahoney strain)}
eacgysdrvlqltlgnstittqeaansvvaygrwpeylrdseanpvdqptepdvaacrfy
tldtvswtkesrgwwwklpdalrdmglfgqnmyyhylgrsgytvhvqcnaskfhqgalgv
favpemclagdsntttmytsyqnanpgekggtftgtftpdnnqtsparrfcpvdyllgng
tllgnafvfphqiinlrtnncatlvlpyvnslsidsmvkhnnwgiailplaplnfasess
peipitltiapmccefnglrnitlprlq
>d1ar73_ 2.8.1.4.3 Poliovirus {poliovirus (type 1, mahoney strain)}
glpvmntpgsnqyltadnfqspcalpefdvtppidipgevknmmelaeidtmipfdlsat
kkntmemyrvrlsdkphtddpilclslspasdprlshtmlgeilnyythwagslkftflf
cgsmmatgkllvsyappgadppkkrkeamlgthviwdiglqssctmvvpwisnttyrqti
ddsfteggyisvfyqtrivvplstpremdilgfvsacndfsvrllrdtthieqka
>d1ar81_ 2.8.1.4.3 Poliovirus {poliovirus (type 1, mahoney strain)}
aatsrdalpnteasgpthskeipaltavetgatnplvpsdtvqtrhvvqhrsrsessies
ffargacvtimtvdnsasttnkdklfavwkitykdtvqlrrklefftysrfdmeltfvvt
anftetnnghalnqvyqimyvppgapvpekwddytwqtssnpsifytygtaparisvpyv
gisnayshfydgfskvplkdqsaalgdslygaaslndfgilavrvvndhnptkvtskirv
ylkpkhirvwcprppravayygpgvdykdgtltplstkdltty
>d1ar82_ 2.8.1.4.3 Poliovirus {poliovirus (type 1, mahoney strain)}
eacgysdrvlqltlgnstittqeaansvvaygrwpeylrdseanpvdqptepdvaacrfy
tldtvswtkesrgwwwklpdalrdmglfgqnmyyhylgrsgytvhvqcnaskfhqgalgv
favpemclagdsntttmhtsyqnanpgekggtftgtftpdnnqtsparrfcpvdyllgng
tllgnafvfphqiinlrtnncatlvlpyvnslsidsmvkhnnwgiailplaplnfasess
peipitltiapmccefnglrnitlprlq
>d1ar83_ 2.8.1.4.3 Poliovirus {poliovirus (type 1, mahoney strain)}
glpvmntpgsnqyltadnfqspcalpefdvtppidipgevknmmelaeidtmipfdlsat
kkntmemyrvrlsdkphtddpilclslspasdprlshtmlgeilnyythwagslkftflf
cgsmmatgkllvsyappgadppkkrkeamlgthviwdiglqssctmvvpwisnttyrqti
ddsfteggyisvfyqtrivvplstpremdilgfvsacndfsvrllrdtthieqka
>d1ar91_ 2.8.1.4.3 Poliovirus {poliovirus (type 1, mahoney strain)}
aatsrdalpnteasgpthskeipaltavetgatnplvpsdtvqtrhvvqhrsrsessies
ffargacvtimtvdnpasttnkdklfavwkitykdtvqlrrklefftysrfdmeltfvvt
anftetnnghalnqvyqimyvppgapvpekwddytwqtssnpsifytygtaparisvpyv
gisnayshfydgfskvplkdqsaalgdslygaaslndfgilavrvvndhnptkvtskirv
ylkpkhirvwcprppravayygpgvdykdgtltplstkdltty
>d1ar92_ 2.8.1.4.3 Poliovirus {poliovirus (type 1, mahoney strain)}
eacgysdrvlqltlgnstittqeaansvvaygrwpeylrdseanpvdqptepdvaacrfy
tldtvswtkesrgwwwklpdalrdmglfgqnmyyhylgrsgytvhvqcnaskfhqgalgv
favpemclagdsntttmytsyqnanpgekggtftgtftpdnnqtsparrfcpvdyllgng
tllgnafvfphqiinlrtnncatlvlpyvnslsidsmvkhnnwgiailplaplnfasess
peipitltiapmccefnglrnitlprlq
>d1ar93_ 2.8.1.4.3 Poliovirus {poliovirus (type 1, mahoney strain)}
glpvmntpgsnqyltadnfqspcalpefdvtppidipgevknmmelaeidtmipfdlsat
kkntmemyrvrlsdkphtddpilclslspasdprlshtmlgeilnyythwagslkftflf
cgsmmatgkllvsyappgadppkkrkeamlgthviwdiglqssctmvvpwisnttyrqti
ddsfteggyisvfyqtrivvplstpremdilgfvsacndfsvrllrdtthieqka
>d1arb__ 2.35.1.1.1 Achromobacter protease {(Achromobacter lyticus), strain m497-1}
gvsgscnidvvcpegdgrrdiiravgaysksgtlactgslvnntandrkmyfltahhcgm
gtastaasivvywnyqnstcrapntpasgangdgsmsqtqsgstvkatyatsdftlleln
naanpafnlfwagwdrrdqnypgaiaihhpnvaekrisnstsptsfvawgggagtthlnv
qwqpsggvtepgssgspiyspekrvlgqlhggpsscsatgtnrsdqygrvftswtgggaa
asrlsdwldpastgaqfidglds
>d1arc__ 2.35.1.1.1 Achromobacter protease {(Achromobacter lyticus), strain m497-1}
gvsgscnidvvcpegdgrrdiiravgaysksgtlactgslvnntandrkmyfltahhcgm
gtastaasivvywnyqnstcrapntpasgangdgsmsqtqsgstvkatyatsdftlleln
naanpafnlfwagwdrrdqnypgaiaihhpnvaekrisnstsptsfvawgggagtthlnv
qwqpsggvtepgssgspiyspekrvlgqlhggpsscsatgtnrsdqygrvftswtgggaa
asrlsdwldpastgaqfidglds
>d1ard__ 7.31.1.1.4 ADR1 {synthetic based on yeast (Saccharomyces cerevisiae)}
rsfvcevctrafarqehlkrhyrshtnek
>d1are__ 7.31.1.1.4 ADR1 {synthetic based on yeast (Saccharomyces cerevisiae)}
rsfvcevctrafarqealkrhyrshtnek
>d1arf__ 7.31.1.1.4 ADR1 {synthetic based on yeast (Saccharomyces cerevisiae)}
rsfvcevctrafarqeylkrhyrshtnek
>d1arga_ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1argb_ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1arha_ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfarqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgavnvagmtpdnmaplceaivavl
>d1arhb_ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfarqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgavnvagmtpdnmaplceaivavl
>d1aria_ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpshpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1arib_ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpshpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ark__ 2.24.2.1.3 Sh3 domain from nebulin {Human (Homo sapiens)}
tagkiframydymaadadevsfkdgdaiinvqaidegwmygtvqrtgrtgmlpanyveai
>d1arl__ 3.58.4.1.1 Carboxypeptidase A {bovine (Bos taurus)}
arstntfnyatyhtldeiydfmdllvaehpqlvsklqigrsyegrpiyvlkfstggsnrp
aiwidlgihsrewitqatgvwfakkftedygqdpsftaildsmdifleivtnpdgfafth
sqnrlwrktrsvtssslcvgvdanrnwdagfgkagassspcsetyhgkyansevevksiv
dfvkdhgnfkaflsihsysqlllypygyttqsipdktelnqvaksavaalkslygtsyky
gsiittiyqasggsidwsynqgikysftfelrdtgrygfllpasqiiptaqetwlgvlti
mehtvnn
>d1arm__ 3.58.4.1.1 Carboxypeptidase A {bovine (Bos taurus)}
arstntfnyatyhtldeiydfmdllvaehpqlvsklqigrsyegrpiyvlkfstggsnrp
aiwidlgihsrewitqatgvwfakkftedygqdpsftaildsmdifleivtnpdgfafth
sqnrlwrktrsvtssslcvgvdanrnwdagfgkagassspcsetyhgkyansevevksiv
dfvkdhgnfkaflsihsysqlllypygyttqsipdktelnqvaksavaalkslygtsyky
gsiittiyqasggsidwsynqgikysftfelrdtgrygfllpasqiiptaqetwlgvlti
mehtvnn
>d1arn__ 2.5.1.1.16 Azurin {(Alcaligenes xylosoxidans xylosoxidans) NCIMB (11015), different isoforms}
aqceatvesndamqynvkeivvdksckqftmhlkhvgkmakvamghnlvltkdadkqava
tdgmgaglaqdyvkagdtrviahtkvigggesdsvtfdvskiaagenyayfcsfpghwam
mkgtlklgs
>d1arp__ 1.72.1.1.2 Peroxidase {(Arthromyces ramous)}
svtcpggqstsnsqccvwfdvlddlqtnfyqgskcespvrkilrivfhdaigfspaltaa
gqfggggadgsiiahsnielafpanggltdtiealravginhgvsfgdliqfatavgmsn
cpgsprlefltgrsnssqpsppslipgpgntvtaildrmgdagfspdevvdllaahslas
qeglnsaifrspldstpqvfdtqfyietllkgttqpgpslgfaeelspfpgefrmrsdal
lardsrtacrwqsmtssnevmgqryraamakmsvlgfdrnaltdcsdvipsavsnnaapv
ipggltvddievscpsepfpeiatasgplpslapap
>d1arqa_ 1.41.1.1.1 Arc repressor {(Salmonella )bacteriophage P22}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1arqb_ 1.41.1.1.1 Arc repressor {(Salmonella )bacteriophage P22}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1arra_ 1.41.1.1.1 Arc repressor {(Salmonella )bacteriophage P22}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1arrb_ 1.41.1.1.1 Arc repressor {(Salmonella )bacteriophage P22}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1ars__ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1art__ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aru__ 1.72.1.1.2 Peroxidase {(Arthromyces ramous)}
svtcpggqstsnsqccvwfdvlddlqtnfyqgskcespvrkilrivfhdaigfspaltaa
gqfggggadgsiiahsnielafpanggltdtiealravginhgvsfgdliqfatavgmsn
cpgsprlefltgrsnssqpsppslipgpgntvtaildrmgdagfspdevvdllaahslas
qeglnsaifrspldstpqvfdtqfyietllkgttqpgpslgfaeelspfpgefrmrsdal
lardsrtacrwqsmtssnevmgqryraamakmsvlgfdrnaltdcsdvipsavsnnaapv
ipggltvddievscpsepfpeiatasgplpslapap
>d1arv__ 1.72.1.1.2 Peroxidase {(Arthromyces ramous)}
svtcpggqstsnsqccvwfdvlddlqtnfyqgskcespvrkilrivfhdaigfspaltaa
gqfggggadgsiiahsnielafpanggltdtiealravginhgvsfgdliqfatavgmsn
cpgsprlefltgrsnssqpsppslipgpgntvtaildrmgdagfspdevvdllaahslas
qeglnsaifrspldstpqvfdtqfyietllkgttqpgpslgfaeelspfpgefrmrsdal
lardsrtacrwqsmtssnevmgqryraamakmsvlgfdrnaltdcsdvipsavsnnaapv
ipggltvddievscpsepfpeiatasgplpslapap
>d1arw__ 1.72.1.1.2 Peroxidase {(Arthromyces ramous)}
svtcpggqstsnsqccvwfdvlddlqtnfyqgskcespvrkilrivfhdaigfspaltaa
gqfggggadgsiiahsnielafpanggltdtiealravginhgvsfgdliqfatavgmsn
cpgsprlefltgrsnssqpsppslipgpgntvtaildrmgdagfspdevvdllaahslas
qeglnsaifrspldstpqvfdtqfyietllkgttqpgpslgfaeelspfpgefrmrsdal
lardsrtacrwqsmtssnevmgqryraamakmsvlgfdrnaltdcsdvipsavsnnaapv
ipggltvddievscpsepfpeiatasgplpslapap
>d1arx__ 1.72.1.1.2 Peroxidase {(Arthromyces ramous)}
svtcpggqstsnsqccvwfdvlddlqtnfyqgskcespvrkilrivfhdaigfspaltaa
gqfggggadgsiiahsnielafpanggltdtiealravginhgvsfgdliqfatavgmsn
cpgsprlefltgrsnssqpsppslipgpgntvtaildrmgdagfspdevvdllaahslas
qeglnsaifrspldstpqvfdtqfyietllkgttqpgpslgfaeelspfpgefrmrsdal
lardsrtacrwqsmtssnevmgqryraamakmsvlgfdrnaltdcsdvipsavsnnaapv
ipggltvddievscpsepfpeiatasgplpslapap
>d1ary__ 1.72.1.1.2 Peroxidase {(Arthromyces ramous)}
svtcpggqstsnsqccvwfdvlddlqtnfyqgskcespvrkilrivfhdaigfspaltaa
gqfggggadgsiiahsnielafpanggltdtiealravginhgvsfgdliqfatavgmsn
cpgsprlefltgrsnssqpsppslipgpgntvtaildrmgdagfspdevvdllaahslas
qeglnsaifrspldstpqvfdtqfyietllkgttqpgpslgfaeelspfpgefrmrsdal
lardsrtacrwqsmtssnevmgqryraamakmsvlgfdrnaltdcsdvipsavsnnaapv
ipggltvddievscpsepfpeiatasgplpslapap
>d1as0_1 1.56.1.1.2 (61-181) Transducin (alpha subunit), insertion domain {rat (Rattus rattus)}
yseeeckqykavvysntiqsiiaiiramgrlkidfgdaaraddarqlfvlagaaeegfmt
aelagvikrlwkdsgvqacfnrsreyqlndsaayylndldriaqpnyiptqqdvlrtrvk
t
>d1as0_2 3.29.1.4.12 (32-60,182-344) Transducin (alpha subunit) {rat (Rattus rattus)}
revkllllgavesgkstivkqmkiiheagXtgivethftfkdlhfkmfdvggqrserkkw
ihcfegvtaiifcvalsdydlvlaedeemnrmhesmklfdsicnnkwftdtsiilflnkk
dlfeekikksplticypeyagsntyeeaaayiqcqfedlnkrkdtkeiythftcatdtkn
vqfvfdavtdvii
>d1as2_1 1.56.1.1.2 (61-181) Transducin (alpha subunit), insertion domain {rat (Rattus rattus)}
yseeeckqykavvysntiqsiiaiiramgrlkidfgdaaraddarqlfvlagaaeegfmt
aelagvikrlwkdsgvqacfnrsreyqlndsaayylndldriaqpnyiptqqdvlrtrvk
t
>d1as2_2 3.29.1.4.12 (32-60,182-346) Transducin (alpha subunit) {rat (Rattus rattus)}
revkllllgavesgkstivkqmkiiheagXtgivethftfkdlhfkmfdvggqrserkkw
ihcfegvtaiifcvalsdydlvlaedeemnrmhesmklfdsicnnkwftdtsiilflnkk
dlfeekikksplticypeyagsntyeeaaayiqcqfedlnkrkdtkeiythftcatdtkn
vqfvfdavtdviikn
>d1as3_1 1.56.1.1.2 (61-181) Transducin (alpha subunit), insertion domain {rat (Rattus rattus)}
yseeeckqykavvysntiqsiiaiiramgrlkidfgdaaraddarqlfvlagaaeegfmt
aelagvikrlwkdsgvqacfnrsreyqlndsaayylndldriaqpnyiptqqdvlrtrvk
t
>d1as3_2 3.29.1.4.12 (32-60,182-348) Transducin (alpha subunit) {rat (Rattus rattus)}
revkllllgavesgkstivkqmkiiheagXtgivethftfkdlhfkmfdvggqrserkkw
ihcfegvtaiifcvalsdydlvlaedeemnrmhesmklfdsicnnkwftdtsiilflnkk
dlfeekikksplticypeyagsntyeeaaayiqcqfedlnkrkdtkeiythftcatdtkn
vqfvfdavtdviiknnl
>e1as4.1a 5.2.1.1.3 Antichymotrypsin, alpha-1 {human (Homo sapiens)}
glasanvdfafslykqlvlkapdknvifsplsistalaflslgahnttlteilkglkfnl
tetseaeihqsfqhllrtlnqssdelqlsmgnamfvkeqlslldrftedakrlygseafa
tdfqdsaaakklindyvkngtrgkitdlikdldsqtmmvlvnyiffkakwempfdpqdth
qsrfylskkkwvmvpmmslhhltipyfrdeelsctvvelkytgnasalfilpdqdkmeev
eamllpetlkrwrdslefreigelylpkfsisrdynlndillqlgieeaftskadlsgit
garnlavsqvvhkavldvfeegteasratavkitll
>e1as4.1b 5.2.1.1.3 Antichymotrypsin, alpha-1 {human (Homo sapiens)}
gtivrfnrpflmiivptdtqniffmskvtnpkq
>d1as6a1 2.5.1.3.2 (9-166) Nitrite reductase, NIR {(Alcaligenes faecalis), strain s-6}
iaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhamafngtv
pgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilrfkatk
pgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>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 (9-166) Nitrite reductase, NIR {(Alcaligenes faecalis), strain s-6}
iaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhamafngtv
pgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilrfkatk
pgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>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 (9-166) Nitrite reductase, NIR {(Alcaligenes faecalis), strain s-6}
iaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhamafngtv
pgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilrfkatk
pgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>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 (9-166) Nitrite reductase, NIR {(Alcaligenes faecalis), strain s-6}
iaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhamafngtv
pgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilrfkatk
pgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>d1as7a2 2.5.1.3.2 (167-339) Nitrite reductase, NIR {(Alcaligenes faecalis), strain s-6}
gkaltydkiyyvgeqdfyvprdengkykkyeapgdayedtvkvmrtltpthvvfngavga
ltgdkamtaavgekvlivhsqanrdtrphligghgdyvwatgkfntppdvdqetwfipgg
aagaafytfqqpgiyayvnhnlieafelgaaahfkvtgewnddlmtsvlapsg
>d1as7b1 2.5.1.3.2 (9-166) Nitrite reductase, NIR {(Alcaligenes faecalis), strain s-6}
iaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhamafngtv
pgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilrfkatk
pgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>d1as7b2 2.5.1.3.2 (167-339) Nitrite reductase, NIR {(Alcaligenes faecalis), strain s-6}
gkaltydkiyyvgeqdfyvprdengkykkyeapgdayedtvkvmrtltpthvvfngavga
ltgdkamtaavgekvlivhsqanrdtrphligghgdyvwatgkfntppdvdqetwfipgg
aagaafytfqqpgiyayvnhnlieafelgaaahfkvtgewnddlmtsvlapsg
>d1as7c1 2.5.1.3.2 (9-166) Nitrite reductase, NIR {(Alcaligenes faecalis), strain s-6}
iaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhamafngtv
pgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilrfkatk
pgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>d1as7c2 2.5.1.3.2 (167-339) Nitrite reductase, NIR {(Alcaligenes faecalis), strain s-6}
gkaltydkiyyvgeqdfyvprdengkykkyeapgdayedtvkvmrtltpthvvfngavga
ltgdkamtaavgekvlivhsqanrdtrphligghgdyvwatgkfntppdvdqetwfipgg
aagaafytfqqpgiyayvnhnlieafelgaaahfkvtgewnddlmtsvlapsg
>d1as8a1 2.5.1.3.2 (9-166) Nitrite reductase, NIR {(Alcaligenes faecalis), strain s-6}
iaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhamafngtv
pgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilrfkatk
pgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>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 (9-166) Nitrite reductase, NIR {(Alcaligenes faecalis), strain s-6}
iaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhamafngtv
pgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilrfkatk
pgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>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 (9-166) Nitrite reductase, NIR {(Alcaligenes faecalis), strain s-6}
iaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhamafngtv
pgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilrfkatk
pgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>d1as8c2 2.5.1.3.2 (167-339) Nitrite reductase, NIR {(Alcaligenes faecalis), strain s-6}
gkaltydkiyyvgeqdfyvprdengkykkyeapgdayedtvkvmrtltpthvvfngavga
ltgdkamtaavgekvlivhsqanrdtrphligghgdyvwatgkfntppdvdqetwfipgg
aagaafytfqqpgiyayvnhnlieafelgaaahfkvtgewnddlmtsvlapsg
>d1as9_1 3.5.2.1.1 (529-754) Aconitase, C-terminal domain {pig (Sus scrofa)}
vdvsptsqrlqllepfdkwdgkdledlqilikvkgkcttdhisaagpwlkfrghldnisn
nlligainienrkansvrnavtqefgpvpdtaryykqhgirwvvigdenygegasrehsa
leprhlggraiitksfarihetnlkkqgllpltfadpadynkihpvdkltiqglkdfapg
kplkciikhpngtqetillnhtfnetqiewfragsalnrmkelqqk
>d1as9_2 3.71.1.1.1 (2-528) Aconitase, first 3 domains {pig (Sus scrofa)}
rakvamshfepheyirydlleknidivrkrlnrpltlsekivyghlddpanqeiergkty
lrlrpdrvamqdataqmamlqfissglpkvavpstihcdhlieaqlggekdlrrakdinq
evynflatagakygvgfwrpgsgiihqiilenyaypgvlligtdshtpnggglggicigv
ggadavdvmagipwelkcpkvigvkltgslsgwtspkdvilkvagiltvkggtgaiveyh
gpgvdsisctgmaticnmgaeigattsvfpynhrmkkylsktgradianladefkdhlvp
dpgchydqvieinlselkphingpftpdlahpvaevgsvaekegwpldirvgligsctns
syedmgrsaavakqalahglkcksqftitpgseqiratierdgyaqvlrdvggivlanac
gpcigqwdrkdikkgekntivtsynrnftgrndanpethafvtspeivtalaiagtlkfn
petdfltgkdgkkfkleapdadelpraefdpgqdtyqhppkdssgqr
>d1asa__ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1asb__ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfafayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1asc__ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfafayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1asd__ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ase__ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1asf__ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfafqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1asg__ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfafqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ash__ 1.1.1.1.37 Ascaris hemoglobin, domain 1 {pig roundworm (Ascaris suum)}
anktrelcmkslehakvdtsnearqdgidlykhmfenypplrkyfksreeytaedvqndp
ffakqgqkillachvlcatyddretfnaytrelldrhardhvhmppevwtdfwklfeeyl
gkkttldeptkqawheigrefakeink
>d1asj1_ 2.8.1.4.3 Poliovirus {poliovirus (type 1, mahoney strain)}
aatsrdalpnteasgpthskeipaltavetgatnplvpsdtvqtrhvvqhrsrsessies
ffargacvtimtvdnpasttnkdklfavwkitykdtvqlrrklefftysrfdmeltfvvt
anftetnnghalnqvyqimyvppgapvpekwddytwqtssnpsifytygtaparisvpyv
gisnayshfydgfskvplkdqsaalgdslygaaslndfgilavrvvndhnptkvtskirv
ylkpkhirvwcprppravayygpgvdykdgtltplstkdltty
>d1asj2_ 2.8.1.4.3 Poliovirus {poliovirus (type 1, mahoney strain)}
eacgysdrvlqltlgnstittqeaansvvaygrwpeylrdseanpvdqptepdvaacrfy
tldtvswtkesrgwwwklpdalrdmglfgqnmyyhylgrsgytvhvqcnaskfhqgalgv
favpemclagdsntttmhtsyqnanpgekggtftgtftpdnnqtsparrfcpvdyllgng
tllgnafvfphqiinlrtnncatlvlpyvnslsidsmvkhnnwgiailplaplnfasess
peipitltiapmccefnglrnitlprlq
>d1asj3_ 2.8.1.4.3 Poliovirus {poliovirus (type 1, mahoney strain)}
glpvmntpgsnqyltadnfqspcalpefdvtppidipgevknmmelaeidtmipfdlsat
kkntmemyrvrlsdkphtddpilclslspasdprlshtmlgeilnyythwagslkftflf
cgsmmatgkllvsyappgadppkkrkeamlgthviwdiglqssctmvvpwisnttyrqti
ddsfteggyisvfyqtrivvplstpremdilgfvsacndfsvrllrdtthieqka
>d1aska_ 4.13.3.2.1 Nuclear transport factor-2 (NTF2) {Rat (Rattus norvegicus)}
gdkpiweqigssfiqhyyqlfdndrtqlgaiyidascltwegqqfqgkaaiveklsslpf
qkiqasitaqdhqptpdsciismvvgqlkadedpimgfhqmfllknindawvctndmfrl
alhnf
>d1askb_ 4.13.3.2.1 Nuclear transport factor-2 (NTF2) {Rat (Rattus norvegicus)}
kpiweqigssfiqhyyqlfdndrtqlgaiyidascltwegqqfqgkaaiveklsslpfqk
iqasitaqdhqptpdsciismvvgqlkadedpimgfhqmfllknindawvctndmfrlal
>d1asla_ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aslb_ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1asma_ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1asmb_ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1asna_ 3.54.1.1.4 Aspartate aminotransferase {(Escherichia coli)}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1asnb_ 3.54.1.1.4 Aspartate aminotransferase {(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__ 3.5.4.2.1 Thermosome {(Thermoplasma acidophilum)}
msgividkekvhskmpdvvknakialidsaleikkteieakvqisdpskiqdflnqetnt
fkqmvekikksganvvlcqkgiddvaqhylakegiyavrrvkksdmeklakatgakivtd
lddltpsvlgeaetveerkigddrmtfvmgck
>d1ast__ 4.52.1.4.1 Astacin {The european fresh water crayfish (Astacus astacus L.)}
aailgdeylwsggvipytfagvsgadqsailsgmqeleektcirfvprttesdyveifts
gsgcwsyvgrisgaqqvslqangcvyhgtiihelmhaigfyhehtrmdrdnyvtinyqnv
dpsmtsnfdidtysryvgedyqyysimhygkysfsiqwgvletivplqngidltdpydka
hmlqtdanqinnlytnecsl
>d1asu__ 3.47.3.2.1 ASV integrase, catalytic domain {Avian sarcoma virus (Rous sarcoma virus), Schmidt-Ruppin strain B}
plreprglgplqiwqtdftleprmaprswlavtvdtassaivvtqhgrvtsvaaqhhwat
aiavlgrpkaiktdngscftskstrewlarwgiahttgipgnsqgqamveranrllkdki
rvlaegdgfmkriptskqgellakamyalnhfergentktnl
>d1asv__ 3.47.3.2.1 ASV integrase, catalytic domain {Avian sarcoma virus (Rous sarcoma virus), Schmidt-Ruppin strain B}
glgplqiwqtdftleprmaprswlavtvdtassaivvtqhgrvtsvaaqhhwataiavlg
rpkaiktdngscftskstrewlarwgiahttgipgnsqgqamveranrllkdkirvlaeg
dgfmkriptskqgellakamyalnhf
>d1asw__ 3.47.3.2.1 ASV integrase, catalytic domain {Avian sarcoma virus (Rous sarcoma virus), Schmidt-Ruppin strain B}
reprglgplqiwqtdftleprxaprswlavtvdtassaivvtqhgrvtsvaaqhhwatai
avlgrpkaiktdngscftskstrewlarwgiahttgipgnsqgqaxveranrllkdkirv
laegdgfxkriptskqgellakaxyalnhfer
>d1asx__ 3.5.4.2.1 Thermosome {(Thermoplasma acidophilum)}
msgividkekvhskmpdvvknakialidsaleikkteieakvqisdpskiqdflnqetnt
fkqmvekikksganvvlcqkgiddvaqhylakegiyavrrvkksdmeklakatgakivtd
lddltpsvlgeaetveerkigddrmtfvmgck
>d1asya1 2.29.4.1.1 (68-204) Aspartyl-tRNA synthetase (AspRS) {Yeast (Saccharomyces cerevisiae)}
edtakdnygklpliqsrdsdrtgqkrvkfvdldeakdsdkevlfrarvhntrqqgatlaf
ltlrqqasliqglvkankegtisknmvkwagslnlesivlvrgivkkvdepiksatvqnl
eihitkiytisetpeal
>d1asya2 4.61.1.1.6 (205-557) Aspartyl-tRNA synthetase (AspRS) {Yeast (Saccharomyces serevisiae)}
pilledasrseaeaeaaglpvvnldtrldyrvidlrtvtnqaifriqagvcelfreylat
kkftevhtpkllgapseggssvfevtyfkgkaylaqspqfnkqqlivadfervyeigpvf
raensnthrhmteftgldmemafeehyhevldtlselfvfifselpkrfaheielvrkqy
pveefklpkdgkmvrltykegiemlraagkeigdfedlstenekflgklvrdkydtdfyi
ldkfpleirpfytmpdpanpkysnsydffmrgeeilsgaqrihdhallqermkahglspe
dpglkdycdgfsygcpphagggiglervvmfyldlknirraslfprdpkrlrp
>d1asyb1 2.29.4.1.1 (68-204) Aspartyl-tRNA synthetase (AspRS) {Yeast (Saccharomyces cerevisiae)}
edtakdnygklpliqsrdsdrtgqkrvkfvdldeakdsdkevlfrarvhntrqqgatlaf
ltlrqqasliqglvkankegtisknmvkwagslnlesivlvrgivkkvdepiksatvqnl
eihitkiytisetpeal
>d1asyb2 4.61.1.1.6 (205-557) Aspartyl-tRNA synthetase (AspRS) {Yeast (Saccharomyces serevisiae)}
pilledasrseaeaeaaglpvvnldtrldyrvidlrtvtnqaifriqagvcelfreylat
kkftevhtpkllgapseggssvfevtyfkgkaylaqspqfnkqqlivadfervyeigpvf
raensnthrhmteftgldmemafeehyhevldtlselfvfifselpkrfaheielvrkqy
pveefklpkdgkmvrltykegiemlraagkeigdfedlstenekflgklvrdkydtdfyi
ldkfpleirpfytmpdpanpkysnsydffmrgeeilsgaqrihdhallqermkahglspe
dpglkdycdgfsygcpphagggiglervvmfyldlknirraslfprdpkrlrp
>d1asza1 2.29.4.1.1 (68-204) Aspartyl-tRNA synthetase (AspRS) {Yeast (Saccharomyces cerevisiae)}
edtakdnygklpliqsrdsdrtgqkrvkfvdldeakdsdkevlfrarvhntrqqgatlaf
ltlrqqasliqglvkankegtisknmvkwagslnlesivlvrgivkkvdepiksatvqnl
eihitkiytisetpeal
>d1asza2 4.61.1.1.6 (205-557) Aspartyl-tRNA synthetase (AspRS) {Yeast (Saccharomyces serevisiae)}
pilledasrseaeaeaaglpvvnldtrldyrvidlrtvtnqaifriqagvcelfreylat
kkftevhtpkllgapseggssvfevtyfkgkaylaqspqfnkqqlivadfervyeigpvf
raensnthrhmteftgldmemafeehyhevldtlselfvfifselpkrfaheielvrkqy
pveefklpkdgkmvrltykegiemlraagkeigdfedlstenekflgklvrdkydtdfyi
ldkfpleirpfytmpdpanpkysnsydffmrgeeilsgaqrihdhallqermkahglspe
dpglkdycdgfsygcpphagggiglervvmfyldlknirraslfprdpkrlrp
>d1aszb1 2.29.4.1.1 (68-204) Aspartyl-tRNA synthetase (AspRS) {Yeast (Saccharomyces cerevisiae)}
edtakdnygklpliqsrdsdrtgqkrvkfvdldeakdsdkevlfrarvhntrqqgatlaf
ltlrqqasliqglvkankegtisknmvkwagslnlesivlvrgivkkvdepiksatvqnl
eihitkiytisetpeal
>d1aszb2 4.61.1.1.6 (205-557) Aspartyl-tRNA synthetase (AspRS) {Yeast (Saccharomyces serevisiae)}
pilledasrseaeaeaaglpvvnldtrldyrvidlrtvtnqaifriqagvcelfreylat
kkftevhtpkllgapseggssvfevtyfkgkaylaqspqfnkqqlivadfervyeigpvf
raensnthrhmteftgldmemafeehyhevldtlselfvfifselpkrfaheielvrkqy
pveefklpkdgkmvrltykegiemlraagkeigdfedlstenekflgklvrdkydtdfyi
ldkfpleirpfytmpdpanpkysnsydffmrgeeilsgaqrihdhallqermkahglspe
dpglkdycdgfsygcpphagggiglervvmfyldlknirraslfprdpkrlrp
>d1at0__ 2.67.1.1.1 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 4.34.2.1.1 (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 4.34.2.1.1 (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
>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
>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
>d1atha_ 5.2.1.1.6 Antithrombin {human (Homo sapiens)}
ictakprdipmnpmciyrspekkatedegseqkipeatnrrvwelskansrfattfyqhl
adskndndniflsplsistafamtklgacndtlqqlmevfkfdtisektsdqihfffakl
ncrlyrkankssklvsanrlfgdksltfnetyqdiselvygaklqpldfkenaeqsraai
nkwvsnktegritdvipseaineltvlvlvntiyfkglwkskfspentrkelfykadges
csasmmyqegkfryrrvaegtqvlelpfkgdditmvlilpkpekslakvekeltpevlqe
wldeleemmlvvhmprfriedgfslkeqlqdmglvdlfspeksklpgivaegrddlyvsd
afhkaflevneegseaaastavviagrslnpnrvtfkanrpflvfirevplntiifmgrv
anpcv
>d1athb_ 5.2.1.1.6 Antithrombin {human (Homo sapiens)}
pmciarspekkatedegseqkipeatnrrvwelskansrfattfyqhladskndndnifl
splsistafamtklgacndtlqqlmevfkfdtisektsdqihfffaklncrlyrkankss
klvsanrlfgdksltfnetyqdiselvygaklqpldfkenaeqsraainkwvsnktegri
tdvipseaineltvlvlvntiyfkglwkskfspentrkelfykadgescsasmmyqegkf
ryrrvaegtqvlelpfkgdditmvlilpkpekslakvekeltpevlqewldeleemmlvv
hmprfriedgfslkeqlqdmglvdlfspeksklpgivaegrddlyvsdafhkaflevnee
gseaaastavviagrslnpnrvtfkanrpflvfirevplntiifmgrvanpc
>d1atia1 3.42.1.1.3 (395-505) Glycyl-tRNA synthetase (GlyRS), C-terminal domain {(Thermus thermophilus)}
qlapikvaviplvknrpeiteyakrlkarllalglgrvlyedtgnigkayrrhdevgtpf
avtvdydtigqskdgttrlkdtvtvrdrdtmeqirlhvdelegflrerlrw
>d1atia2 4.61.1.1.5 (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 4.61.1.1.5 (1-394) Glycyl-tRNA synthetase (GlyRS) {(Thermus thermophilus)}
aassldelvalckrrgfifqsseiygglqgvydygplgvelknnlkqawwrrnvyerddm
egldasvlthrlvlhysgheatfadpmvdnritkkryrldhllkeqpeevlkrlyramev
eeenlhalvqammqaperaggamtaagvldpasgepgdwtppryfnmmfqdlrgprggrg
llaylrpetaqgifvnfknvldatsrklgfgiaqigkafrneitprnfifrvrefeqmei
eyfvrpgedeywhrywveerlkwwqemglsrenlvpyqqppessahyakatvdilyrfph
gslelegiaqrtdfdlgshtkdqealgitarvlrnehstqrlayrdpetgkwfvpyviep
sagvdrgvlallaeaftreelpngeerivlklkp
>d1atja_ 1.72.1.1.6 Peroxidase {Horseradish (Armoracia rusticana)}
qltptfydnscpnvsnivrdtivnelrsdpriaasilrlhfhdcfvngcdasilldntts
frtekdafgnansargfpvidrmkaavesacprtvscadlltiaaqqsvtlaggpswrvp
lgrrdslqafldlananlpapfftlpqlkdsfrnvglnrssdlvalsgghtfgknqcrfi
mdrlynfsntglpdptlnttylqtlrglcplngnlsalvdfdlrtptifdnkyyvnleeq
kgliqsdqelfsspnatdtiplvrsfanstqtffnafveamdrmgnitpltgtqgqirln
crvvns
>d1atjb_ 1.72.1.1.6 Peroxidase {Horseradish (Armoracia rusticana)}
qltptfydnscpnvsnivrdtivnelrsdpriaasilrlhfhdcfvngcdasilldntts
frtekdafgnansargfpvidrmkaavesacprtvscadlltiaaqqsvtlaggpswrvp
lgrrdslqafldlananlpapfftlpqlkdsfrnvglnrssdlvalsgghtfgknqcrfi
mdrlynfsntglpdptlnttylqtlrglcplngnlsalvdfdlrtptifdnkyyvnleeq
kgliqsdqelfsspnatdtiplvrsfanstqtffnafveamdrmgnitpltgtqgqirln
crvvns
>d1atjc_ 1.72.1.1.6 Peroxidase {Horseradish (Armoracia rusticana)}
qltptfydnscpnvsnivrdtivnelrsdpriaasilrlhfhdcfvngcdasilldntts
frtekdafgnansargfpvidrmkaavesacprtvscadlltiaaqqsvtlaggpswrvp
lgrrdslqafldlananlpapfftlpqlkdsfrnvglnrssdlvalsgghtfgknqcrfi
mdrlynfsntglpdptlnttylqtlrglcplngnlsalvdfdlrtptifdnkyyvnleeq
kgliqsdqelfsspnatdtiplvrsfanstqtffnafveamdrmgnitpltgtqgqirln
crvvns
>d1atjd_ 1.72.1.1.6 Peroxidase {Horseradish (Armoracia rusticana)}
qltptfydnscpnvsnivrdtivnelrsdpriaasilrlhfhdcfvngcdasilldntts
frtekdafgnansargfpvidrmkaavesacprtvscadlltiaaqqsvtlaggpswrvp
lgrrdslqafldlananlpapfftlpqlkdsfrnvglnrssdlvalsgghtfgknqcrfi
mdrlynfsntglpdptlnttylqtlrglcplngnlsalvdfdlrtptifdnkyyvnleeq
kgliqsdqelfsspnatdtiplvrsfanstqtffnafveamdrmgnitpltgtqgqirln
crvvns
>d1atje_ 1.72.1.1.6 Peroxidase {Horseradish (Armoracia rusticana)}
qltptfydnscpnvsnivrdtivnelrsdpriaasilrlhfhdcfvngcdasilldntts
frtekdafgnansargfpvidrmkaavesacprtvscadlltiaaqqsvtlaggpswrvp
lgrrdslqafldlananlpapfftlpqlkdsfrnvglnrssdlvalsgghtfgknqcrfi
mdrlynfsntglpdptlnttylqtlrglcplngnlsalvdfdlrtptifdnkyyvnleeq
kgliqsdqelfsspnatdtiplvrsfanstqtffnafveamdrmgnitpltgtqgqirln
crvvns
>d1atjf_ 1.72.1.1.6 Peroxidase {Horseradish (Armoracia rusticana)}
qltptfydnscpnvsnivrdtivnelrsdpriaasilrlhfhdcfvngcdasilldntts
frtekdafgnansargfpvidrmkaavesacprtvscadlltiaaqqsvtlaggpswrvp
lgrrdslqafldlananlpapfftlpqlkdsfrnvglnrssdlvalsgghtfgknqcrfi
mdrlynfsntglpdptlnttylqtlrglcplngnlsalvdfdlrtptifdnkyyvnleeq
kgliqsdqelfsspnatdtiplvrsfanstqtffnafveamdrmgnitpltgtqgqirln
crvvns
>d1atk__ 4.3.1.1.12 Cathepsin K {Human (Homo sapiens)}
apdsvdyrkkgyvtpvknqgqcgscwafssvgalegqlkkktgkllnlspqnlvdcvsen
dgcgggymtnafqyvqknrgidsedaypyvgqeescmynptgkaakcrgyreipegneka
lkravarvgpvsvaidasltsfqfyskgvyydescnsdnlnhavlavgygiqkgnkhwii
knswgenwgnkgyilmarnknnacgianlasfpkm
>d1atla_ 4.52.1.5.2 Snake venom metalloprotease {Atrolysin C: Western diamonback rattlesnake (Crotalus atrox)}
lpqryielvvvadhrvfmkynsdlntirtrvheivnfingfyrslnihvsltdleiwsne
dqiniqsassdtlnafaewretdllnrkshdnaqlltaieldeetlglaplgtmcdpkls
igivqdhspinllmgvtmahelghnlgmehdgkdclrgaslcimrpgltkgrsyefsdds
mhyyerflkqykpqcilnkp
>d1atlb_ 4.52.1.5.2 Snake venom metalloprotease {Atrolysin C: Western diamonback rattlesnake (Crotalus atrox)}
lpqryielvvvadhrvfmkynsdlntirtrvheivnfingfyrslnihvsltdleiwsne
dqiniqsassdtlnafaewretdllnrkshdnaqlltaieldeetlglaplgtmcdpkls
igivqdhspinllmgvtmahelghnlgmehdgkdclrgaslcimrpgltkgrsyefsdds
mhyyerflkqykpqcilnkp
>d1atna1 3.47.1.1.3 (1-146) Actin {bovine (Bos taurus) pancreas}
dedettalvcdngsglvkagfagddapravfpsivgrprhqgvmvgmgqkdsyvgdeaqs
krgiltlkypiehgiitnwddmekiwhhtfynelrvapeehptllteaplnpkanrekmt
qimfetfnvpamyvaiqavlslyasg
>d1atna2 3.47.1.1.3 (147-372) Actin {bovine (Bos taurus) pancreas}
rttgivldsgdgvthnvpiyegyalphaimrldlagrdltdylmkiltergysfvttaer
eivrdikeklcyvaldfenemataassssleksyelpdgqvitignerfrcpetlfqpsf
igmesagihettynsimkcdidirkdlyannvmsggttmypgiadrmqkeitalapstmk
ikiiapperkysvwiggsilaslstfqqmwitkqeydeagpsivhr
>d1atnd_ 4.93.1.1.2 Deoxyribonuclease I {bovine (Bos taurus)}
lkiaafnirtfgetkmsnatlasyivrivrrydivliqevrdshlvavgklldylnqddp
ntyhyvvseplgrnsykerylflfrpnkvsvldtyqyddgcgncgndsfsrepavvkfss
hstkvkefaivalhsapsdavaeinslydvyldvqqkwhlndvmlmgdfnadcsyvtssq
wssirlrtsstfqwlipdsadttatstncaydrivvagsllqssvvpgsaapfdfqaayg
lsnemalaisdhypvevtlt
>d1atpe_ 5.1.1.1.4 cAMP-dependent PK, catalytic subunit {mouse (Mus musculus)}
vkeflakakedflkkwetpsqntaqldqfdriktlgtgsfgrvmlvkhkesgnhyamkil
dkqkvvklkqiehtlnekrilqavnfpflvklefsfkdnsnlymvmeyvaggemfshlrr
igrfsepharfyaaqivltfeylhsldliyrdlkpenllidqqgyiqvtdfgfakrvkgr
twtlcgtpeylapeiilskgynkavdwwalgvliyemaagyppffadqpiqiyekivsgk
vrfpshfssdlkdllrnllqvdltkrfgnlkngvndiknhkwfattdwiaiyqrkveapf
ipkfkgpgdtsnfddyeeeeirvsinekcgkeftef
>d1atq_1 3.5.2.1.1 (529-754) Aconitase, C-terminal domain {pig (Sus scrofa)}
vdvsptsqrlqllepfdkwdgkdledlqilikvkgkcttdhisaagpwlkfrghldnisn
nlligainienrkansvrnavtqefgpvpdtaryykqhgirwvvigdenygegssqehsa
leprhlggraiitksfarihetnlkkqgllpltfadpadynkihpvdkltiqglkdfapg
kplkciikhpngtqetillnhtfnetqiewfragsalnrmkelqqk
>d1atq_2 3.71.1.1.1 (2-528) Aconitase, first 3 domains {pig (Sus scrofa)}
rakvamshfepheyirydlleknidivrkrlnrpltlsekivyghlddpanqeiergkty
lrlrpdrvamqdataqmamlqfissglpkvavpstihcdhlieaqlggekdlrrakdinq
evynflatagakygvgfwrpgsgiihqiilenyaypgvlligtdshtpnggglggicigv
ggadavdvmagipwelkcpkvigvkltgslsgwtspkdvilkvagiltvkggtgaiveyh
gpgvdsisctgmaticnmgaeigattsvfpynhrmkkylsktgradianladefkdhlvp
dpgchydqvieinlselkphingpftpdlahpvaevgsvaekegwpldirvgligsctns
syedmgrsaavakqalahglkcksqftitpgseqiratierdgyaqvlrdvggivlanac
gpcigqwdrkdikkgekntivtsynrnftgrndanpethafvtspeivtalaiagtlkfn
petdfltgkdgkkfkleapdadelpraefdpgqdtyqhppkdssgqr
>d1atr_1 3.47.1.1.1 (2-188) Heat shock protein 70kDa, ATPase fragment {bovine (Bos taurus)}
skgpavgidlgttyscvgvfqhgkveiiandqgnrttpsyvaftdterligdaaknqvam
nptntvfdakrligrrfddavvqsdmkhwpfmvvndagrpkvqveykgetksfypeevss
mvltkmkeiaeaylgktvtnavvtvpayfndsqrqatkdagtiaglnvlriineptaaai
aygldkk
>d1atr_2 3.47.1.1.1 (189-384) Heat shock protein 70kDa, ATPase fragment {bovine (Bos taurus)}
vgaernvlifdlgggvfdvsiltiedgifevkstagdthlggedfdnrmvnhfiaefkrk
hkkdisenkravrrlrtacerakrtlssstqasieidslyegidfytsitrarfeelnad
lfrgtldpvekalrdakldksqihdivlvggstripkiqkllqdffngkelnksinpdea
vaygaavqaailsgdk
>d1ats_1 3.47.1.1.1 (2-188) Heat shock protein 70kDa, ATPase fragment {bovine (Bos taurus)}
skgpavgidlgttyscvgvfqhgkveiiandqgnrttpsyvaftdterligdaaknqvam
nptntvfdakrligrrfddavvqsdmkhwpfmvvndagrpkvqveykgetksfypeevss
mvltkmkeiaeaylgktvtnavvtvpayfndsqrqatkdagtiaglnvlriineptaaai
aygldkk
>d1ats_2 3.47.1.1.1 (189-383) Heat shock protein 70kDa, ATPase fragment {bovine (Bos taurus)}
vgaernvlifdlgggefdvsiltiedgifevkstagdthlggedfdnrmvnhfiaefkrk
hkkdisenkravrrlrtacerakrtlssstqasieidslyegidfytsitrarfeelnad
lfrgtldpvekalrdakldksqihdivlvggstripkiqkllqdffngkelnksinpdea
vaygaavqaailsgd
>d1atta_ 5.2.1.1.5 Antithrombin {bovine (Bos Taurus)}
vedvctakprdipvnpmciyrategqgseqkipgatnrrvwelskanshfatafyqhlad
sknnndniflsplsistafamtklgacnntltqlmevfkfdtisektsdqihfffaklnc
rlyrkanksselvsanrlfgdksitfnetyqdisevvygaklqpldfkgnaeqsrltinq
wisnktegritdvippqaineftvlvlvntiyfkglwkskfspentrkelfykadgescs
vlmmyqeskfryrrvaestqvlelpfkgdditmvlilpklektlakveqeltpdmlqewl
deltetllvvhmprfriedsfsvkeqlqdmgledlfspeksrlpgivaegrsdlyvsdaf
hkaflevneegseaaastvisiagrslrvtfkanrpflvlirevalntiifmgrvanpcv
d
>d1attb_ 5.2.1.1.5 Antithrombin {bovine (Bos Taurus)}
kprdipvnpmciyrssqkipgatnrrvwelskanshfatafyqhladsknnndniflspl
sistafamtklgacnntltqlmevfkfdtisektsdqihfffaklncrlyrkanksselv
sanrlfgdksitfnetyqdisevvygaklqpldfkgnaeqsrltinqwisnktegritdv
ippqaineftvlvlvntiyfkglwkskfspentrkelfykadgescsvlmmyqeskfryr
rvaestqvlelpfkgdditmvlilpklektlakveqeltpdmlqewldeltetllvvhmp
rfriedsfsvkeqlqdmgledlfspeksrlpgivaegrsdlyvsdafhkaflevneegse
aaastvisiagrslnsdrvtfkanrpflvlirevalntiifmgrvanpcvd
>d1atu__ 5.2.1.1.4 Antitrypsin, alpha-1 {human (Homo sapiens)}
ptfnkitpnlaefafslyrqlahqsnstnilfspvsiaaafamlslgakgdthdeilegl
nfnlteipeaqihegfqellrtlnqpdsqlqlttgnglflseglklvdkfledvkklyhs
eaftvnfgdteeakkqindyvekgtqgkivdlvkeldrdtvfalvnyiffkgkwerpfev
kdteeedfhvdqvttvkvpmmkrlgmfniqhckklsswvllmkylgnataifflpdegkl
qhlenelthdiitkflenedrrsaslhlpklsitgtydlksvlgqlgitkvfsngadlsg
vteeaplklskavhkavltidekgteaagamfleaipmsippevkfnkpfvfliieqntk
aplfmgrvvnptqk
>d1atx__ 7.8.1.1.5 Sea anemone toxin IA {sea anemone (Anemonia sulcata)}
gaaclcksdgpntrgnsmsgtiwvfgcpsgwnncegraiigycckq
>d1atza_ 3.50.1.1.2 von Willebrand factor A3 domain {Human (Homo sapiens)}
qpldvillldgsssfpasyfdemksfakafiskanigprltqvsvlqygsittidvpwnv
vpekahllslvdvmqreggpsqigdalgfavryltsemhgarpgaskavvilvtdvsvds
vdaaadaarsnrvtvfpigigdrydaaqlrilagpagdsnvvklqriedlptmvtlgnsf
lhkl
>d1atzb_ 3.50.1.1.2 von Willebrand factor A3 domain {Human (Homo sapiens)}
dcsqpldvillldgsssfpasyfdemksfakafiskanigprltqvsvlqygsittidvp
wnvvpekahllslvdvmqreggpsqigdalgfavryltsemhgarpgaskavvilvtdvs
vdsvdaaadaarsnrvtvfpigigdrydaaqlrilagpagdsnvvklqriedlptmvtlg
nsflhklcs
>d1au1a_ 1.26.1.3.3 Interferon-beta {Human (Homo sapiens)}
msynllgflqrssnfqcqkllwqlngrleyclkdrmnfdipeeikqlqqfqkedaaltiy
emlqnifaifrqdssstgwnetivenllanvyhqinhlktvleeklekedftrgklmssl
hlkryygrilhylkakeyshcawtivrveilrnfyfinrltgylrn
>d1au1b_ 1.26.1.3.3 Interferon-beta {Human (Homo sapiens)}
msynllgflqrssnfqcqkllwqlngrleyclkdrmnfdipeeikqlqqfqkedaaltiy
emlqnifaifrqdssstgwnetivenllanvyhqinhlktvleeklekedftrgklmssl
hlkryygrilhylkakeyshcawtivrveilrnfyfinrltgylrn
>d1au7a1 1.4.1.1.6 (103-160) Pit-1 POU homeodomain {Rat (Rattus norvegicus)}
krrttisiaakdalerhfgehskpssqeimrmaeelnlekevvrvwfcnrrqrekrvk
>d1au7a2 1.32.1.1.2 (5-74) Pit-1 {Rat (Rattus norvegicus)}
gmraleqfanefkvrriklgytqtnvgealaavhgsefsqtticrfenlqlsfknacklk
ailskwleea
>d1au7b1 1.4.1.1.6 (103-160) Pit-1 POU homeodomain {Rat (Rattus norvegicus)}
krrttisiaakdalerhfgehskpssqeimrmaeelnlekevvrvwfcnrrqrekrvk
>d1au7b2 1.32.1.1.2 (5-74) Pit-1 {Rat (Rattus norvegicus)}
gmraleqfanefkvrriklgytqtnvgealaavhgsefsqtticrfenlqlsfknacklk
ailskwleea
>d1au9__ 3.33.1.1.6 Subtilisin Novo/BPN' {(Bacillus amyloliquefaciens)}
aqsvpygvsqikapalhsqgycgsnvkvavidsgidsshpdlkvaggasfvpsetnpfqd
nnshgthvagtvaalnnsigvlgvapcaslyavkvlgadgsgqyswiingiewaiannmd
vinmslggpsgsaalkaavdkavasgvvvvaaagnegtsgssstvgypakypsviavgav
dssnqrasfssvgpeldvmapgvsicstlpgnkygaksgtsmasphvagaaalilskhpn
wtntqvrsslentttklgdsfyygkglinvqaaaq
>d1aua_1 1.5.2.1.1 (4-96) N-terminal domain of phosphatidylinositol transfer protein sec14p {Baker's yeast (Saccharomyces cerevisiae)}
qqekeflesypqncppdalpgtpgnldsaqekalaelrklledagfierlddstllrflr
arkfdvqlakemfencekwrkdygtdtilqdfh
>d1aua_2 3.8.1.1.1 (97-299) C-terminal domain of phosphatidylinositol transfer protein sec14p {Baker's yeast (Saccharomyces cerevisiae)}
ydekpliakfypqyyhktdkdgrpvyfeelgavnlhemnkvtseermlknlvweyesvvq
yrlpacsraaghlvetsctimdlkgisissaysvmsyvreasyisqnyypermgkfyiin
apfgfstafrlfkpfldpvtvskifilgssyqkellkqipaenlpvkfggksevdeskgg
lylsdigpwrdpkyigpegeape
>d1auc__ 3.38.1.1.4 Thioredoxin {human (Homo sapiens)}
mvkqiesktafqealdaagdklvvvdfsatwcgpckmikpffhslsekysnviflevdvd
dcqdvasecevkcmptfqffkkgqkvgefsgankekleatinelv
>d1auda_ 4.34.7.1.2 U1A protein {human (Homo sapiens)}
avpetrpnhtiyinnlnekikkdelkkslhaifsrfgqildilvsrslkmrgqafvifke
vssatnalrsmqgfpfydkpmriqyaktdsdiiakmkgtfv
>d1auia_ 4.99.1.2.3 Protein phosphatase-2B (PP-2B, calcineurin A subunit) {Human (Homo sapiens)}
tdrvvkavpfppshrltakevfdndgkprvdilkahlmkegrleesvalriitegasilr
qeknlldidapvtvcgdihgqffdlmklfevggspantrylflgdyvdrgyfsiecvlyl
walkilypktlfllrgnhecrhlteyftfkqeckikyservydacmdafdclplaalmnq
qflcvhgglspeintlddirkldrfkeppaygpmcdilwsdpledfgnektqehfthntv
rgcsyfysypavceflqhnnllsilraheaqdagyrmyrksqttgfpslitifsapnyld
vynnkaavlkyennvmnirqfncsphpywlpnfmdvftwslpfvgekvtemlvnvlnics
ddelgseedgfdgataaarkevirnkiraigkmarvfsvlreesesvltlkgltptgmlp
sgvlsggkqtlqsatveaieadeaikgfspqhkitsfeeakgldrinermppr
>d1auib_ 1.37.1.5.19 Calcineurin regulatory subunit (B-chain) {Human (Homo sapiens)}
syplemcshfdadeikrlgkrfkkldldnsgslsveefmslpelqqnplvqrvidifdtd
gngevdfkefiegvsqfsvkgdkeqklrfafriydmdkdgyisngelfqvlkmmvgnnlk
dtqlqqivdktiinadkdgdgrisfeefcavvggldihkkmvvdv
>d1auk__ 3.64.1.2.1 Arylsulfatase A {Human (Homo sapiens)}
rppnivlifaddlgygdlgcyghpssttpnldqlaagglrftdfyvpvslxtpsraallt
grlpvrmgmypgvlvpssrgglpleevtvaevlaargyltgmagkwhlgvgpegaflpph
qgfhrflgipyshdqgpcqnltcfppatpcdggcdqglvpipllanlsveaqppwlpgle
arymafahdlmadaqrqdrpfflyyashhthypqfsgqsfaersgrgpfgdslmeldaav
gtlmtaigdlglleetlviftadngpetmrmsrggcsgllrcgkgttyeggvrepalafw
pghiapgvthelassldllptlaalagaplpnvtldgfdlsplllgtgksprqslffyps
ypdevrgvfavrtgkykahfftqgsahsdttadpachasssltaheppllydlskdpgen
ynllggvagatpevlqalkqlqllkaqldaavtfgpsqvargedpalqicchpgctprpa
cchcp
>d1aum__ 1.27.3.1.1 HIV capsid C-terminal domain {Human immunodeficiency virus type 1 (HIV-1)}
ldirqgpkepfrdyvdrfyktlraeqasqevknwmtetllvqnanpdcktilkalgpgat
leemmtacqg
>d1aun__ 2.19.1.1.1 Pathogenesis-related protein 5d {Common tobacco (Nicotiana tabacum)}
sgvfevhnncpytvwaaatpvgggrrlergqswwfwappgtkmariwgrtncnfdgagrg
wcqtgdcggvleckgwgkppntlaeyalnqfsnldfwdisvidgfnipmsfgptkpgpgk
chgiqctaningecpgslrvpggcnnpcttfggqqycctqgpcgptelsrwfkqrcpday
sypqddptstftctswttdykvmfcpyg
>d1auoa_ 3.56.1.7.1 Carboxylesterase {(Pseudomonas fluorescens)}
mteplilqpakpadacviwlhglgadrydfmpvaealqesllttrfvlpqaptrpvting
gyempswydikamsparsisleelevsakmvtdlieaqkrtgidasriflagfsqggavv
fhtafinwqgplggvialstyaptfgdelelsasqqripalclhgqyddvvqnamgrsaf
ehlksrgvtvtwqeypmghevlpqeihdigawlaarlg
>d1auob_ 3.56.1.7.1 Carboxylesterase {(Pseudomonas fluorescens)}
mteplilqpakpadacviwlhglgadrydfmpvaealqesllttrfvlpqaptrpvting
gyempswydikamsparsisleelevsakmvtdlieaqkrtgidasriflagfsqggavv
fhtafinwqgplggvialstyaptfgdelelsasqqripalclhgqyddvvqnamgrsaf
ehlksrgvtvtwqeypmghevlpqeihdigawlaarlg
>d1aup_1 3.22.1.7.1 (205-449) Glutamate dehydrogenase, C-terminal domain {(Clostridium symbiosum)}
rpeatgygsvyyveavmkhendtlvgktvalagfgnvawgaakklaelgakavtlsgpdg
yiydpegitteekinymlemrasgrnkvqdyadkfgvqffpgekpwgqkvdiimpcatqn
dvdleqakkivannvkyyievanmpttnealrflmqqpnmvvapskavnaggvlvvgfem
sqnserlswtaeevdsklhqvmtdihdgsaaaaeryglgynlvaganivgfqkiadamma
qgiaw
>d1aup_2 3.61.1.1.1 (1-192) Glutamate dehydrogenase, N-terminal domain {(Clostridium symbiosum)}
skyvdrviaevekkyadepefvqtveevlsslgpvvdahpeyeevallermvipervief
rvpweddngkvhvntgyrvqfngaigpylgglrfapsvnlsimkflgfeqafkdslttlp
mggakggsdfdpngksdrevmrfcqafmtelyrhigpdidvpagdlgvgareigymygqy
rkivggfyngvl
>d1aura_ 3.56.1.7.1 Carboxylesterase {(Pseudomonas fluorescens)}
mteplilqpakpadacviwlhglgadrydfmpvaealqesllttrfvlpqaptrpvting
gyempswydikamsparsisleelevsakmvtdlieaqkrtgidasriflagfsqggavv
fhtafinwqgplggvialstyaptfgdelelsasqqripalclhgqyddvvqnamgrsaf
ehlksrgvtvtwqeypmghevlpqeihdigawlaarlg
>d1aurb_ 3.56.1.7.1 Carboxylesterase {(Pseudomonas fluorescens)}
mteplilqpakpadacviwlhglgadrydfmpvaealqesllttrfvlpqaptrpvting
gyempswydikamsparsisleelevsakmvtdlieaqkrtgidasriflagfsqggavv
fhtafinwqgplggvialstyaptfgdelelsasqqripalclhgqyddvvqnamgrsaf
ehlksrgvtvtwqeypmghevlpqeihdigawlaarlg
>d1ausl1 3.1.10.1.2 (148-463) Ribulose 1,5-bisphosphate carboxylase-oxygenase {spinach (Spinacia oleracea)}
fqgpphgiqverdklnkygrpllgctikpklglsaknygravyeclrggldftkddenvn
sqpfmrwrdrflfcaealykaqaetgeikghylnatagtcedmmkravfarelgvpivmh
dyltggftanttlshycrdnglllhihramhavidrqknhgmhfrvlakalrlsggdhih
sgtvvgklegerditlgfvdllrddytekdrsrgiyftqswvstpgvlpvasggihvwhm
palteifgddsvlqfgggtlghpwgnapgavanrvaleacvqarnegrdlaregntiire
atkwspelaaacevwk
>d1ausl2 4.34.10.1.2 (20-147) Ribulose 1,5-bisphosphate carboxylase-oxygenase {spinach (Spinacia oleracea)}
ykltyytpeyetldtdilaafrvspqpgvppeeagaavaaesstgtwttvwtdgltnldr
ykgrcyhiepvageenqyicyvaypldlfeegsvtnmftsivgnvfgfkalralrledlr
ipvayvkt
>d1auss_ 4.38.1.1.2 Ribulose 1,5-bisphosphate carboxylase-oxygenase {spinach (Spinacia oleracea)}
mqvwpilnlkkyetlsylpplttdqlarqvdyllnnkwvpclefetdhgfvyrehhnspg
yydgrywtmwklpmfgctdpaqvlneleeckkeypnafiriigfdsnrevqcisfiaykp
agy
>d1autc_ 2.35.1.2.28 Activated protein c (autoprothrombin IIa) {human (Homo sapiens)}
lidgkmtrrgdspwqvvlldskkklacgavlihpswvltaahcmdeskkllvrlgeydlr
rwekweldldikevfvhpnysksttdndiallhlaqpatlsqtivpiclpdsglaereln
qagqetlvtgwgyhssrekeakrnrtfvlnfikipvvphnecsevmsnmvsenmlcagil
gdrqdacegdsggpmvasfhgtwflvglvswgegcgllhnygvytkvsryldwihghird
>d1autl1 7.3.9.1.7 (49-96) Activated protein c (autoprothrombin IIa) {human (Homo sapiens)}
qclvlplehpcaslccghgtcixgigsfscdcrsgwegrfcqrevsfl
>d1autl2 7.3.9.1.7 (97-146) Activated protein c (autoprothrombin IIa) {human (Homo sapiens)}
ncsldnggcthycleevgwrrcscapgyklgddllqchpavkfpcgrpwk
>d1auua_ 2.25.2.1.1 SacY {(Bacillus subtilis)}
mkikrilnhnaivvkdqneekillgagiafnkkkndivdpskiektfirkdtpdy
>d1auub_ 2.25.2.1.1 SacY {(Bacillus subtilis)}
mkikrilnhnaivvkdqneekillgagiafnkkkndivdpskiektfirkdtpdy
>d1auva1 3.23.1.4.1 (112-213) Synapsin Ia domain {Bovine (Bos taurus)}
aarvllvidephtdwakyfkgkkihgeidikveqaefsdlnlvahanggfsvdxevlrng
vkvvrslkpdfvlirqhafsxarngdyrslviglqyagipsi
>d1auva2 4.89.1.3.1 (214-417) Synapsin Ia, C-terminal domain {Bovine (Bos taurus)}
nslhsvynfcdkpwvfaqxvrlhkklgteefplinqtfypnhkexlssttypvvvkxgha
hsgxgkvkvdnqhdfqdiasvvaltktyattepfidakydvriqkigqnykayxrtsvsg
nwktntgsaxleqiaxsdryklwvdtcseifggldicavealhgkdgrdhiievvgssxp
ligdhqdedkqlivelvvnkxaqa
>d1auvb1 3.23.1.4.1 (112-213) Synapsin Ia domain {Bovine (Bos taurus)}
aarvllvidephtdwakyfkgkkihgeidikveqaefsdlnlvahanggfsvdxevlrng
vkvvrslkpdfvlirqhafsxarngdyrslviglqyagipsi
>d1auvb2 4.89.1.3.1 (214-417) Synapsin Ia, C-terminal domain {Bovine (Bos taurus)}
nslhsvynfcdkpwvfaqxvrlhkklgteefplinqtfypnhkexlssttypvvvkxgha
hsgxgkvkvdnqhdfqdiasvvaltktyattepfidakydvriqkigqnykayxrtsvsg
nwktntgsaxleqiaxsdryklwvdtcseifggldicavealhgkdgrdhiievvgssxp
ligdhqdedkqlivelvvnkxaqa
>e1auw.1a 1.98.1.3.2 delta-crystallin {Domestic duck (Anas platyrhynchos)}
tdpimeklnssiaydqrlsevdiqgsmayakalekagiltktelekilsglekiseewsk
gvfvvkqsdedintanerrlkeligdiagklhtgrsrndqvvtdlklfmknslsiisthl
lqliktlveraaieidvilpgythlqkaqpirwsqfllshavaltrdserlgevkkrinv
lplgsgalagnpldidremlrselefasislnsmdaiserdfvveflsfatllmihlskm
aedliiystsefgfltdsdafstgsslmpqkknpdslelirskagrvfgrlasilmvlkg
lpstynkdlqedkeavfdvvdtltavlqvatgvistlqiskenmekaltpemlatdlaly
lvrkgvpfrqahtasgkavhlaetkgitinklsledlksispqfssdvsqvfnfvnsveq
ytalggtakssvttqieqlrelmkkqk
>e1auw.1b 1.98.1.3.2 delta-crystallin {Domestic duck (Anas platyrhynchos)}
tdpimeklnssiaydqrlsevdiqgsmayakalekagiltktelekilsglekiseewsk
gvfvvkqsdedintanerrlkeligdiagklhtgrsrndqvvtdlklfmknslsiisthl
lqliktlveraaieidvilpgythlqkaqpirwsqfllshavaltrdserlgevkkrinv
lplgsgalagnpldidremlrselefasislnsmdaiserdfvveflsfatllmihlskm
aedliiystsefgfltdsdafstgsslmpqkknpdslelirskagrvfgrlasilmvlkg
lpstynkdlqedkeavfdvvdtltavlqvatgvistlqiskenmekaltpemlatdlaly
lvrkgvpfrqahtasgkavhlaetkgitinklsledlksispqfssdvsqvfnfvnsveq
ytalggtakssvttqieqlrelmkkqk
>e1auw.1c 1.98.1.3.2 delta-crystallin {Domestic duck (Anas platyrhynchos)}
tdpimeklnssiaydqrlsevdiqgsmayakalekagiltktelekilsglekiseewsk
gvfvvkqsdedintanerrlkeligdiagklhtgrsrndqvvtdlklfmknslsiisthl
lqliktlveraaieidvilpgythlqkaqpirwsqfllshavaltrdserlgevkkrinv
lplgsgalagnpldidremlrselefasislnsmdaiserdfvveflsfatllmihlskm
aedliiystsefgfltdsdafstgsslmpqkknpdslelirskagrvfgrlasilmvlkg
lpstynkdlqedkeavfdvvdtltavlqvatgvistlqiskenmekaltpemlatdlaly
lvrkgvpfrqahtasgkavhlaetkgitinklsledlksispqfssdvsqvfnfvnsveq
ytalggtakssvttqieqlrelmkkqk
>e1auw.1d 1.98.1.3.2 delta-crystallin {Domestic duck (Anas platyrhynchos)}
tdpimeklnssiaydqrlsevdiqgsmayakalekagiltktelekilsglekiseewsk
gvfvvkqsdedintanerrlkeligdiagklhtgrsrndqvvtdlklfmknslsiisthl
lqliktlveraaieidvilpgythlqkaqpirwsqfllshavaltrdserlgevkkrinv
lplgsgalagnpldidremlrselefasislnsmdaiserdfvveflsfatllmihlskm
aedliiystsefgfltdsdafstgsslmpqkknpdslelirskagrvfgrlasilmvlkg
lpstynkdlqedkeavfdvvdtltavlqvatgvistlqiskenmekaltpemlatdlaly
lvrkgvpfrqahtasgkavhlaetkgitinklsledlksispqfssdvsqvfnfvnsveq
ytalggtakssvttqieqlrelmkkqk
>d1auxa1 3.23.1.4.1 (112-213) Synapsin Ia domain {Bovine (Bos taurus)}
aarvllvidephtdwakyfkgkkihgeidikveqaefsdlnlvahanggfsvdmevlrng
vkvvrslkpdfvlirqhafsmarngdyrslviglqyagipsi
>d1auxa2 4.89.1.3.1 (214-417) Synapsin Ia, C-terminal domain {Bovine (Bos taurus)}
nslhsvynfcdkpwvfaqmvrlhkklgteefplinqtfypnhkemlssttypvvvkmgha
hsgmgkvkvdnqhdfqdiasvvaltktyattepfidakydvriqkigqnykaymrtsvsg
nwktntgsamleqiamsdryklwvdtcseifggldicavealhgkdgrdhiievvgssmp
ligdhqdedkqlivelvvnkmaqa
>d1auxb1 3.23.1.4.1 (112-213) Synapsin Ia domain {Bovine (Bos taurus)}
aarvllvidephtdwakyfkgkkihgeidikveqaefsdlnlvahanggfsvdmevlrng
vkvvrslkpdfvlirqhafsmarngdyrslviglqyagipsi
>d1auxb2 4.89.1.3.1 (214-417) Synapsin Ia, C-terminal domain {Bovine (Bos taurus)}
nslhsvynfcdkpwvfaqmvrlhkklgteefplinqtfypnhkemlssttypvvvkmgha
hsgmgkvkvdnqhdfqdiasvvaltktyattepfidakydvriqkigqnykaymrtsvsg
nwktntgsamleqiamsdryklwvdtcseifggldicavealhgkdgrdhiievvgssmp
ligdhqdedkqlivelvvnkmaqa
>d1auya_ 2.8.1.2.11 TYMV coat protein {(Turnip yellow mosaic virus)}
spltikqpfqsevlfagtkdaeasltianidsvstlttfyrhasleslwvtihptlqapt
fpttvgvcwvpaqspvtpaqitktyggqifciggaiqtlsplivkcplemmqprvkdsiq
yldspkllisitaqptappastciitvsgtlsmhsplitdtst
>d1auyb_ 2.8.1.2.11 TYMV coat protein {(Turnip yellow mosaic virus)}
meidkelapqdrtvtvatvlpavpgpspltikqpfqsevlfagtkdaeasltianidsvs
tlttfyrhasleslwvtihptlqaptfpttvgvcwvpaqspvtpaqitktyggqifcigg
aiqtlsplivkcplemmqprvkdsiqyldspkllisitaqptappastciitvsgtlsmh
splitdtst
>d1auyc_ 2.8.1.2.11 TYMV coat protein {(Turnip yellow mosaic virus)}
meidkelapqdrtvtvatvlpavpgpspltikqpfqsevlfagtkdaeasltianidsvs
tlttfyrhasleslwvtihptlqaptfpttvgvcwvpaqspvtpaqitktyggqifcigg
aiqtlsplivkcplemmqprvkdsiqyldspkllisitaqptappastciitvsgtlsmh
splitdtst
>d1auz__ 3.8.2.1.1 SpoIIaa {(Bacillus subtilis)}
slgidmnvkesvlcirltgeldhhtaetlkqkvtqslekddirhivlnledlsfmdssgl
gvilgrykqikqiggemvvcaispavkrlfdmsglfkiirfeqseqqalltlgvas
>d1av1a_ 1.105.11.1.1 Apolipoprotein A-i {Human (Homo sapiens)}
mlklldnwdsvtstfsklreqlgpvtqefwdnleketeglrqemskdleevkakvqpyld
dfqkkwqeemelyrqkveplraelqegarqklhelqeklsplgeemrdrarahvdalrth
lapysdelrqrlaarlealkenggarlaeyhakatehlstlsekakpaledlrqgllpvl
esfkvsflsaleeytkklntq
>d1av1b_ 1.105.11.1.1 Apolipoprotein A-i {Human (Homo sapiens)}
mlklldnwdsvtstfsklreqlgpvtqefwdnleketeglrqemskdleevkakvqpyld
dfqkkwqeemelyrqkveplraelqegarqklhelqeklsplgeemrdrarahvdalrth
lapysdelrqrlaarlealkenggarlaeyhakatehlstlsekakpaledlrqgllpvl
esfkvsflsaleeytkklntq
>d1av1c_ 1.105.11.1.1 Apolipoprotein A-i {Human (Homo sapiens)}
mlklldnwdsvtstfsklreqlgpvtqefwdnleketeglrqemskdleevkakvqpyld
dfqkkwqeemelyrqkveplraelqegarqklhelqeklsplgeemrdrarahvdalrth
lapysdelrqrlaarlealkenggarlaeyhakatehlstlsekakpaledlrqgllpvl
esfkvsflsaleeytkklntq
>d1av1d_ 1.105.11.1.1 Apolipoprotein A-i {Human (Homo sapiens)}
mlklldnwdsvtstfsklreqlgpvtqefwdnleketeglrqemskdleevkakvqpyld
dfqkkwqeemelyrqkveplraelqegarqklhelqeklsplgeemrdrarahvdalrth
lapysdelrqrlaarlealkenggarlaeyhakatehlstlsekakpaledlrqgllpvl
esfkvsflsaleeytkklntq
>d1av4_1 2.22.2.1.3 (212-628) Copper amine oxidase, domain 3 (catalytic) {(Arthrobacter globiformis)}
plrttqkpisitqpegpsftvtggnhiewekwsldvgfdvregvvlhniafrdgdrlrpi
inrasiaemvvpygdpspirswqnyfdtgeylvgqyanslelgcdclgditylspvisda
fgnpreirngicmheedwgilakhsdlwsginytrrnrrmvisffttignxdygfywyly
ldgtiefeakatgvvftsafpeggsdnisqlapglgapfhqhifsarldmaidgftnrve
eedvvrqtmgpgnergnafsrkrtvltreseavreadartgrtwiisnpesknrlnepvg
yklhahnqptlladpgssiarraafatkdlwvtryadderyptgdfvnqhsggaglpsyi
aqdrdidgqdivvwhtfglthfprvedwpimpvdtvgfklrpegffdrspvldvpan
>d1av4_2 4.13.2.1.3 (9-96) Copper amine oxidase, domains 1 and 2 {(Arthrobacter globiformis)}
aspfrlasageisevqgilrtagllgpekriaylgvldpargagseaedrrfrvfihdvs
garpqevtvsvtngtvisaveldtaatg
>d1av4_3 4.13.2.1.3 (97-211) Copper amine oxidase, domains 1 and 2 {(Arthrobacter globiformis)}
elpvleeefevveqllatderwlkalaarnldvskvrvaplsagvfeyaeergrrilrgl
afvqdfpedsawahpvdglvayvdvvskevtrvidtgvfpvpaehgnytdpeltg
>d1av5a_ 4.9.1.1.3 Protein kinase C inhibitor-1, PKCI-1 {human (Homo sapiens)}
ggdtifgkiirkeipakiifeddrclafhdispqapthflvipkkhisqisvaedddesl
lghlmivgkkcaadlglnkgyrmvvnegsdggqsvyhvhlhvlggrqmhwppg
>d1av5b_ 4.9.1.1.3 Protein kinase C inhibitor-1, PKCI-1 {human (Homo sapiens)}
ggdtifgkiirkeipakiifeddrclafhdispqapthflvipkkhisqisvaedddesl
lghlmivgkkcaadlglnkgyrmvvnegsdggqsvyhvhlhvlggrqmhwppg
>d1av6a_ 3.53.1.4.1 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
>d1avc__ 1.55.1.1.7 Annexin VI {Bovine (Bos taurus)}
yrgsirdfpdfnpsqdaetlynamkgfgsdkeaiinlitsrsnkqrqeicqnykslygkd
liadlkyeltgkferlivglmrppayadakeikdaisgigtdekclieilasrtneqihq
lvaaykdayerdleaditgdtsghfrkmlvvllqgtreeddvvsedlvqqdvqdlyeage
lkwgtdeaqfiyilgnrskqhlrlvfdeylkttgkpieasirgelsgdfeklmlavvkci
rstaeyfaerlfkamkglgtrdntlirimvsrseldmldireifrtkyekslysmikndt
sgeykktllklcggdddaagqffpeaaqvayqmwelsavarvelkgtvrpagdfnpdada
kalrkamkglgtdedtiidiithrsnaqrqqirqtfkshfgrdlmadlkselsgdlarli
lglmmppahydakqlkkamegagtdekalieilatrtnaeiqainkaykedyhktledal
ssdtsghfkrilislatgnreeggedreraredaqvaaeileiadttsgdkssletrfmm
ilctrsypdlrrvfqefvkmtnydvehtikkemsgdvrdvfvaivqsvknkplffadkly
ksmkgagteektltrimvsrseidllnirrefiekydkslhqaiegdtsghflkallaic
gg
>d1avda_ 2.46.1.1.2 Avidin {Chicken (Gallus gallus)}
kcsltgkwtndlgsnmtigavnsrgeftgtyttavtatsneikesplhgtentinkrtqp
tfgftvnwkfsesttvftgqcfidrngkevlktmwllrssvndigddwkatrvginiftr
lrt
>d1avdb_ 2.46.1.1.2 Avidin {Chicken (Gallus gallus)}
rkcsltgkwtndlgsnmtigavnsrgeftgtyttavtatsneikesplhgtentinkrtq
ptfgftvnwkfsesttvftgqcfidrngkevlktmwllrssvndigddwkatrvginift
rlrt
>d1avea_ 2.46.1.1.2 Avidin {Chicken (Gallus gallus)}
kcsltgkwtndlgsnmtigavnsrgeftgtyttavtatsneikesplhgtentinkrtqp
tfgftvnwkfsesttvftgqcfidrngkevlktmwllrssvndigddwkatrvginiftr
lrt
>d1aveb_ 2.46.1.1.2 Avidin {Chicken (Gallus gallus)}
kcsltgkwtndlgsnmtigavnsrgeftgtyttavtatsneikesplhgtentinkrtqp
tfgftvnwkfsesttvftgqcfidrngkevlktmwllrssvndigddwkatrvginiftr
lrt
>e1avf.1a 2.38.1.2.9 Pepsin(ogen) {human (Homo sapiens) progastricsin (pepsinogen C)}
vtyepmaymdaayfgeisigtppqnflvlfdtgssnlwvpsvycqsqactshsrfnpses
stystngqtfslqygsgsltgffgydtltvqsiqvpnqefglsenepgtnfvyaqfdgim
glaypalsvdeattamqgmvqegaltspvfsvylsnqqgssggavvfggvdsslytgqiy
wapvtqelywqigieefliggqasgwcsegcqaivdtgtslltvpqqymsallqatgaqe
deygqflvncnsiqnlpsltfiingvefplppssyilsnngyctvgveptylssqngqpl
wilgdvflrsyysvydlgnnrvgfataa
>e1avf.1p 2.38.1.2.9 Pepsin(ogen) {human (Homo sapiens) progastricsin (pepsinogen C)}
avvkvplkkfksiretmkekg
>e1avf.2j 2.38.1.2.9 Pepsin(ogen) {human (Homo sapiens) progastricsin (pepsinogen C)}
vtyepmaymdaayfgeisigtppqnflvlfdtgssnlwvpsvycqsqactshsrfnpses
stystngqtfslqygsgsltgffgydtltvqsiqvpnqefglsenepgtnfvyaqfdgim
glaypalsvdeattamqgmvqegaltspvfsvylsnqqgssggavvfggvdsslytgqiy
wapvtqelywqigieefliggqasgwcsegcqaivdtgtslltvpqqymsallqatgaqe
deygqflvncnsiqnlpsltfiingvefplppssyilsnngyctvgveptylssqngqpl
wilgdvflrsyysvydlgnnrvgfataa
>e1avf.2q 2.38.1.2.9 Pepsin(ogen) {human (Homo sapiens) progastricsin (pepsinogen C)}
avvkvplkkfksiretmkekgl
>d1avha_ 1.55.1.1.5 Annexin V {human (Homo sapiens)}
qvlrgtvtdfpgfderadaetlrkamkglgtdeesiltlltsrsnaqrqeisaafktlfg
rdllddlkseltgkfeklivalmkpsrlydayelkhalkgagtnekvlteiiasrtpeel
raikqvyeeeygssleddvvgdtsgyyqrmlvvllqanrdpdagideaqveqdaqalfqa
gelkwgtdeekfitifgtrsvshlrkvfdkymtisgfqieetidretsgnleqlllavvk
sirsipaylaetlyyamkgagtddhtlirvmvsrseidlfnirkefrknfatslysmikg
dtsgdykkallllcgedd
>d1avhb_ 1.55.1.1.5 Annexin V {human (Homo sapiens)}
qvlrgtvtdfpgfderadaetlrkamkglgtdeesiltlltsrsnaqrqeisaafktlfg
rdllddlkseltgkfeklivalmkpsrlydayelkhalkgagtnekvlteiiasrtpeel
raikqvyeeeygssleddvvgdtsgyyqrmlvvllqanrdpdagideaqveqdaqalfqa
gelkwgtdeekfitifgtrsvshlrkvfdkymtisgfqieetidretsgnleqlllavvk
sirsipaylaetlyyamkgagtddhtlirvmvsrseidlfnirkefrknfatslysmikg
dtsgdykkallllcgedd
>d1avk_1 2.22.2.1.3 (212-628) Copper amine oxidase, domain 3 (catalytic) {(Arthrobacter globiformis)}
plrttqkpisitqpegpsftvtggnhiewekwsldvgfdvregvvlhniafrdgdrlrpi
inrasiaemvvpygdpspirswqnyfdtgeylvgqyanslelgcdclgditylspvisda
fgnpreirngicmheedwgilakhsdlwsginytrrnrrmvisffttignydygfywyly
ldgtiefeakatgvvftsafpeggsdnisqlapglgapfhqhifsarldmaidgftnrve
eedvvrqtmgpgnergnafsrkrtvltreseavreadartgrtwiisnpesknrlnepvg
yklhahnqptlladpgssiarraafatkdlwvtryadderyptgdfvnqhsggaglpsyi
aqdrdidgqdivvwhtfglthfprvedwpimpvdtvgfklrpegffdrspvldvpan
>d1avk_2 4.13.2.1.3 (9-96) Copper amine oxidase, domains 1 and 2 {(Arthrobacter globiformis)}
aspfrlasageisevqgilrtagllgpekriaylgvldpargagseaedrrfrvfihdvs
garpqevtvsvtngtvisaveldtaatg
>d1avk_3 4.13.2.1.3 (97-211) Copper amine oxidase, domains 1 and 2 {(Arthrobacter globiformis)}
elpvleeefevveqllatderwlkalaarnldvskvrvaplsagvfeyaeergrrilrgl
afvqdfpedsawahpvdglvayvdvvskevtrvidtgvfpvpaehgnytdpeltg
>d1avl_1 2.22.2.1.3 (212-628) Copper amine oxidase, domain 3 (catalytic) {(Arthrobacter globiformis)}
plrttqkpisitqpegpsftvtggnhiewekwsldvgfdvregvvlhniafrdgdrlrpi
inrasiaemvvpygdpspirswqnyfdtgeylvgqyanslelgcdclgditylspvisda
fgnpreirngicmheedwgilakhsdlwsginytrrnrrmvisffttignxdygfywyly
ldgtiefeakatgvvftsafpeggsdnisqlapglgapfhqhifsarldmaidgftnrve
eedvvrqtmgpgnergnafsrkrtvltreseavreadartgrtwiisnpesknrlnepvg
yklhahnqptlladpgssiarraafatkdlwvtryadderyptgdfvnqhsggaglpsyi
aqdrdidgqdivvwhtfglthfprvedwpimpvdtvgfklrpegffdrspvldvpan
>d1avl_2 4.13.2.1.3 (9-96) Copper amine oxidase, domains 1 and 2 {(Arthrobacter globiformis)}
aspfrlasageisevqgilrtagllgpekriaylgvldpargagseaedrrfrvfihdvs
garpqevtvsvtngtvisaveldtaatg
>d1avl_3 4.13.2.1.3 (97-211) Copper amine oxidase, domains 1 and 2 {(Arthrobacter globiformis)}
elpvleeefevveqllatderwlkalaarnldvskvrvaplsagvfeyaeergrrilrgl
afvqdfpedsawahpvdglvayvdvvskevtrvidtgvfpvpaehgnytdpeltg
>d1avma1 1.2.4.1.7 (1-86) Cambialistic superoxide dismutase {(Propionibacterium freudenreichii)}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1avma2 4.26.1.1.7 (87-201) Cambialistic superoxide dismutase {(Propionibacterium freudenreichii) shermani}
saperptdelgaaideffgsfdnmkaqftaaatgiqgsgwaslvwdplgkrintlqfydh
qnnlpagsipllqldmwehafylqyknvkgdyvkswwnvvnwddvalrfsearva
>d1avmb1 1.2.4.1.7 (1-86) Cambialistic superoxide dismutase {(Propionibacterium freudenreichii)}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1avmb2 4.26.1.1.7 (87-201) Cambialistic superoxide dismutase {(Propionibacterium freudenreichii) shermani}
saperptdelgaaideffgsfdnmkaqftaaatgiqgsgwaslvwdplgkrintlqfydh
qnnlpagsipllqldmwehafylqyknvkgdyvkswwnvvnwddvalrfsearva
>d1avn__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasfk
>e1avo.1a 1.24.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
lrvqpeaqakvdvfredlctktenllgsyfpkkiseldaflkepalneanlsnlkapldi
>e1avo.1b 1.24.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
avncnekivvllqrlkpeikdvieqlnlvttwlqlqipriedgnnfgvavqekvfelmts
lhtklegfhtqiskyfsergdavtkaakqphvgdyrqlvheldeaeyrdirlmvmeirna
yavlydiilknfeklkkprg
>e1avo.2c 1.24.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
lrvqpeaqakvdvfredlctktenllgsyfpkkiseldaflkepalneanlsnlkapldi
>e1avo.2d 1.24.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
avncnekivvllqrlkpeikdvieqlnlvttwlqlqipriedgnnfgvavqekvfelmts
lhtklegfhtqiskyfsergdavtkaakqphvgdyrqlvheldeaeyrdirlmvmeirna
yavlydiilknfeklkkprg
>e1avo.3e 1.24.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
lrvqpeaqakvdvfredlctktenllgsyfpkkiseldaflkepalneanlsnlkapldi
>e1avo.3f 1.24.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
avncnekivvllqrlkpeikdvieqlnlvttwlqlqipriedgnnfgvavqekvfelmts
lhtklegfhtqiskyfsergdavtkaakqphvgdyrqlvheldeaeyrdirlmvmeirna
yavlydiilknfeklkkprg
>e1avo.4g 1.24.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
lrvqpeaqakvdvfredlctktenllgsyfpkkiseldaflkepalneanlsnlkapldi
>e1avo.4h 1.24.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
avncnekivvllqrlkpeikdvieqlnlvttwlqlqipriedgnnfgvavqekvfelmts
lhtklegfhtqiskyfsergdavtkaakqphvgdyrqlvheldeaeyrdirlmvmeirna
yavlydiilknfeklkkprg
>e1avo.5i 1.24.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
lrvqpeaqakvdvfredlctktenllgsyfpkkiseldaflkepalneanlsnlkapldi
>e1avo.5j 1.24.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
avncnekivvllqrlkpeikdvieqlnlvttwlqlqipriedgnnfgvavqekvfelmts
lhtklegfhtqiskyfsergdavtkaakqphvgdyrqlvheldeaeyrdirlmvmeirna
yavlydiilknfeklkkprg
>e1avo.6k 1.24.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
lrvqpeaqakvdvfredlctktenllgsyfpkkiseldaflkepalneanlsnlkapldi
>e1avo.6l 1.24.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
avncnekivvllqrlkpeikdvieqlnlvttwlqlqipriedgnnfgvavqekvfelmts
lhtklegfhtqiskyfsergdavtkaakqphvgdyrqlvheldeaeyrdirlmvmeirna
yavlydiilknfeklkkprg
>e1avo.7m 1.24.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
lrvqpeaqakvdvfredlctktenllgsyfpkkiseldaflkepalneanlsnlkapldi
>e1avo.7n 1.24.8.1.1 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 {Lambda (Bacteriophage lambda)}
shmtpdiilqrtgidvraveqgddawhklrlgvitasevhnviakprsgkkwpdmkmsyf
htllaevctgvapevnakalawgkqyendartlfeftsgvnvtespiiyrdesmrtacsp
dglcsdgnglelkcpftsrdfmkfrlggfeaiksaymaqvqysmwvtrknawyfanydpr
mkreglhyvvierdekymasfdeivpefiekmdealaeigfvfgeqwr
>d1avqb_ 3.43.1.7.1 lambda exonuclease {Lambda (Bacteriophage lambda)}
shmtpdiilqrtgidvraveqgddawhklrlgvitasevhnviakprsgkkwpdmkmsyf
htllaevctgvapevnakalawgkqyendartlfeftsgvnvtespiiyrdesmrtacsp
dglcsdgnglelkcpftsrdfmkfrlggfeaiksaymaqvqysmwvtrknawyfanydpr
mkreglhyvvierdekymasfdeivpefiekmdealaeigfvfgeqwr
>d1avqc_ 3.43.1.7.1 lambda exonuclease {Lambda (Bacteriophage lambda)}
tpdiilqrtgidvraveqgddawhklrlgvitasevhnviakprsgkkwpdmkmsyfhtl
laevctgvapevnakalawgkqyendartlfeftsgvnvtespiiyrdesmrtacspdgl
csdgnglelkcpftsrdfmkfrlggfeaiksaymaqvqysmwvtrknawyfanydprmkr
eglhyvvierdekymasfdeivpefiekmdealaeigfvfgeqwr
>d1avr__ 1.55.1.1.5 Annexin V {human (Homo sapiens)}
qvlrgtvtdfpgfderadaetlrkamkglgtdeesiltlltsrsnaqrqeisaafktlfg
rdllddlkseltgkfeklivalmkpsrlydayelkhalkgagtnekvlteiiasrtpeel
raikqvyeeeygssleddvvgdtsgyyqrmlvvllqanrdpdagideaqveqdaqalfqa
gelkwgtdeekfitifgtrsvshlrkvfdkymtisgfqieetidretsgnleqlllavvk
sirsipaylaetlyyamkgagtddhtlirvmvsrseidlfnirkefrknfatslysmikg
dtsgdykkallllcged
>d1avsa_ 1.37.1.5.1 Troponin C {chicken (Gallus gallus)}
qaearaflseemiaefkaafdmfdadgggdistkelgtvmrmlgqnptkeeldaiieevd
edgsgtidfeeflvmmvrqmk
>d1avsb_ 1.37.1.5.1 Troponin C {chicken (Gallus gallus)}
qqaearaflseemiaefkaafdmfdadgggdistkelgtvmrmlgqnptkeeldaiieev
dedgsgtidfeeflvmmvrqmk
>d1avt__ 3.33.1.1.2 Subtilisin Carlsberg {(Bacillus licheniformis)}
aqtvpygiplikadkvqaqgfkganvkvavldtgiqashpdlnvvggasfvageayntdg
nghgthvagtvaaldnttgvlgvapsvslyavkvlnssgsgsysgivsgiewattngmdv
inmslggasgstamkqavdnayargvvvvaaagnsgnsgstntigypakydsviavgavd
snsnrasfssvgaelevmapgagvystyptntyatlngtxmasphvagaaalilskhpnl
sasqvrnrlsstatylgssfyygkglinveaaaq
>d1avv__ 4.59.1.1.1 Regulatory factor Nef {(Human immunodeficiency virus type 1), HIV-1}
vplrpmtykaavdlshflkekggleglihsqrrqdildlwiyhtqgyfpdwqnytpgpgv
rypltfgwcyklvpvepdkveeankgentsllhpvslhgmddperevlewrfdsrlafhh
varelhpeyf
>d1avya_ 6.4.1.1.1 Fibritin {(Bacteriophage T4)}
tnkikaietdiasvrqevntakgnisslqgdvqalqeagyipeaprdgqayvrkdgewvl
lstflspa
>d1avyb_ 6.4.1.1.1 Fibritin {(Bacteriophage T4)}
vrqevntakgnisslqgdvqalqeagyipeaprdgqayvrkdgewvllstflsp
>d1avyc_ 6.4.1.1.1 Fibritin {(Bacteriophage T4)}
ltnkikaietdiasvrqevntakgnisslqgdvqalqeagyipeaprdgqayvrkdgewv
llstflsp
>d1avza_ 4.59.1.1.1 Regulatory factor Nef {(Human immunodeficiency virus type 1), HIV-1}
vplrpmtykaavdlshflkekggleglihsqrrqdildlwiyhtqgyfpdwqnytpgpgv
rypltfgwcyklvpvepdkveeankgentsllhpvslhgmddperevlewrfdsrlafhh
varelhpeyf
>d1avzb_ 4.59.1.1.1 Regulatory factor Nef {(Human immunodeficiency virus type 1), HIV-1}
tpqvplrpmtykaavdlshflkekggleglihsqrrqdildlwiyhtqgyfpdwqnytpg
pgvrypltfgwcyklvpvepdkveeankgentsllhpvslhgmddperevlewrfdsrla
fhhvarelhpeyf
>d1avzc_ 2.24.2.1.2 Fyn proto-oncogene tyrosine kinase, SH3 domain {human (Homo sapiens)}
tlfvalydyearteddlsfhkgekfqilnssegdwwearslttgetgyipsnyvapv
>d1aw0__ 4.34.15.1.3 Menkes copper-transporting ATPase {Human (Homo sapiens)}
ltqetvinidgmtcnscvqsiegviskkpgvksirvslansngtveydplltspetlrga
iedmgfdatlsd
>d1aw1a_ 3.1.11.1.8 Triosephosphate isomerase {(Vibrio marinus)}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeaka
>d1aw1b_ 3.1.11.1.8 Triosephosphate isomerase {(Vibrio marinus)}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeak
>d1aw1d_ 3.1.11.1.8 Triosephosphate isomerase {(Vibrio marinus)}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeaka
>d1aw1e_ 3.1.11.1.8 Triosephosphate isomerase {(Vibrio marinus)}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeak
>d1aw1g_ 3.1.11.1.8 Triosephosphate isomerase {(Vibrio marinus)}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeaka
>d1aw1h_ 3.1.11.1.8 Triosephosphate isomerase {(Vibrio marinus)}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeak
>d1aw1j_ 3.1.11.1.8 Triosephosphate isomerase {(Vibrio marinus)}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeaka
>d1aw1k_ 3.1.11.1.8 Triosephosphate isomerase {(Vibrio marinus)}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeak
>d1aw2a_ 3.1.11.1.8 Triosephosphate isomerase {(Vibrio marinus)}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeaka
>d1aw2b_ 3.1.11.1.8 Triosephosphate isomerase {(Vibrio marinus)}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeak
>d1aw2d_ 3.1.11.1.8 Triosephosphate isomerase {(Vibrio marinus)}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeaka
>d1aw2e_ 3.1.11.1.8 Triosephosphate isomerase {(Vibrio marinus)}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeak
>d1aw2g_ 3.1.11.1.8 Triosephosphate isomerase {(Vibrio marinus)}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeaka
>d1aw2h_ 3.1.11.1.8 Triosephosphate isomerase {(Vibrio marinus)}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeak
>d1aw2j_ 3.1.11.1.8 Triosephosphate isomerase {(Vibrio marinus)}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeaka
>d1aw2k_ 3.1.11.1.8 Triosephosphate isomerase {(Vibrio marinus)}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeak
>d1aw3__ 4.70.1.1.2 Cytochrome b5 {rat (Rattus norvegicus)}
dkdvkyytleeiqkhkdskstwvilhhkvydltkfleehpggeevlreqaggdatenfed
vghstdarelsktyiigelhpddrskiakpsetl
>d1aw6__ 7.32.1.1.1 Gal4 {yeast (Saccharomyces cerevisiae)}
mkllssieqacdicrlkklkcskekpkcakclknnwecryspk
>e1aw8.1a 2.39.2.1.1 Pyruvoyl dependent aspartate decarboxylase, ADC {(Escherichia coli)}
mirtmlqgklhrvkvthadlhyeg
>e1aw8.1b 2.39.2.1.1 Pyruvoyl dependent aspartate decarboxylase, ADC {(Escherichia coli)}
caidqdfldaagileneaidiwnvtngkrfstyaiaaergsriisvngaaahcasvgdiv
iiasfvtmpdeeartwrpnvayfegdnemk
>e1aw8.2d 2.39.2.1.1 Pyruvoyl dependent aspartate decarboxylase, ADC {(Escherichia coli)}
mirtmlqgklhrvkvthadlhyeg
>e1aw8.2e 2.39.2.1.1 Pyruvoyl dependent aspartate decarboxylase, ADC {(Escherichia coli)}
caidqdfldaagileneaidiwnvtngkrfstyaiaaergsriisvngaaahcasvgdiv
iiasfvtmpdeeartwrpnvayfegdnemk
>d1awba_ 5.8.1.2.1 Inositol monophosphatase {human (Homo sapiens)}
wqecmdyavtlarqagevvceaiknemnvmlksspvdlvtatdqkvekmlissikekyps
hsfigeesvaageksiltdnptwiidpidgttnfvhrfpfvavsigfavnkkiefgvvys
cvegkmytarkgkgafcngqklqvsqqeditksllvtelgssrtpetvrmvlsnmeklfc
ipvhgirsvgtaavnmclvatggadayyemgihcwdvagagiivteaggvlmdvtggpfd
lmsrrviaannrilaeriakeiqviplqrdde
>d1awbb_ 5.8.1.2.1 Inositol monophosphatase {human (Homo sapiens)}
wqecmdyavtlarqagevvceaiknemnvmlksspvdlvtatdqkvekmlissikekyps
hsfigeesvaageksiltdnptwiidpidgttnfvhrfpfvavsigfavnkkiefgvvys
cvegkmytarkgkgafcngqklqvsqqeditksllvtelgssrtpetvrmvlsnmeklfc
ipvhgirsvgtaavnmclvatggadayyemgihcwdvagagiivteaggvlmdvtggpfd
lmsrrviaannrilaeriakeiqviplqrdde
>d1awca_ 1.4.3.12.5 GA binding protein (GABP) alpha {Mouse (Mus musculus)}
iqlwqfllelltdkdardciswvgdegefklnqpelvaqkwgqrknkptmnyeklsralr
yyydgdmickvqgkrfvykfvcdlktligysaaelnrlvieceqkklarm
>d1awcb_ 1.91.3.1.2 GA bindinig protein (GABP) beta 1 {Mouse (Mus musculus)}
dlgkklleaaragqddevrilmangapfttdwlgtsplhlaaqyghfsttevllragvsr
dartkvdrtplhmaaseghanivevllkhgadvnakdmlkmtalhwatehnhqevvelli
kygadvhtqskfcktafdisidngnedlaeilq
>d1awd__ 4.11.5.1.6 2Fe-2S ferredoxin {(Chlorella fusca)}
ykvtlktpsgeetiecpedtyildaaeeagldlpyscragacsscagkvesgevdqsdqs
flddaqmgkgfvltcvayptsdvtilthqeaaly
>d1awe__ 2.41.1.1.8 Son of sevenless 1 (sos1) {Human (Homo sapiens)}
mneiqknidgwegkdigqccnefimegtltrvgakherhiflfdglmiccksnhgqprlp
gasnaeyrlkekffmrkvqindkddtneykhafeiilkdensvifsaksaeeknnwmaal
islqyrstle
>d1awj__ 2.24.2.1.9 IL-2 inducible T-cell (Itc) kinase {Mouse (Mus musculus)}
kkplpptpednrrsfqepeetlvialydyqtndpqelalrcdeeyylldsseihwwrvqd
knghegyapssylveks
>d1awo__ 2.24.2.1.5 Abl tyrosine kinase, SH3 domain {Human (Homo sapiens)}
slfvalydfvasgdntlsitkgeklrvlgynhngewceaqtkngqgwvpsnyitpvs
>d1awqa_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awra_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awrb_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awrc_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awrd_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awre_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awrf_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awsa_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfx
cqggdftrhngtggksiygekfedenfilkhtgpgilsxanagpntngsqffictaktew
ldgkhvvfgkvkegxniveaxerfgsrngktskkitiadcgqle
>d1awta_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfx
cqggdftrhngtggksiygekfedenfilkhtgpgilsxanagpntngsqffictaktew
ldgkhvvfgkvkegxniveaxerfgsrngktskkitiadcgqle
>d1awtb_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfx
cqggdftrhngtggksiygekfedenfilkhtgpgilsxanagpntngsqffictaktew
ldgkhvvfgkvkegxniveaxerfgsrngktskkitiadcgqle
>d1awtc_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfx
cqggdftrhngtggksiygekfedenfilkhtgpgilsxanagpntngsqffictaktew
ldgkhvvfgkvkegxniveaxerfgsrngktskkitiadcgqle
>d1awtd_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfx
cqggdftrhngtggksiygekfedenfilkhtgpgilsxanagpntngsqffictaktew
ldgkhvvfgkvkegxniveaxerfgsrngktskkitiadcgqle
>d1awte_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfx
cqggdftrhngtggksiygekfedenfilkhtgpgilsxanagpntngsqffictaktew
ldgkhvvfgkvkegxniveaxerfgsrngktskkitiadcgqle
>d1awtf_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfx
cqggdftrhngtggksiygekfedenfilkhtgpgilsxanagpntngsqffictaktew
ldgkhvvfgkvkegxniveaxerfgsrngktskkitiadcgqle
>d1awua_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awva_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awvb_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awvc_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awvd_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awve_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awvf_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1aww__ 2.24.2.1.13 Bruton's tyrosine kinase {Human (Homo sapiens)}
gsmstselkkvvalydympmnandlqlrkgdeyfileesnlpwwrardkngqegyipsny
vteaeds
>d1awx__ 2.24.2.1.13 Bruton's tyrosine kinase {Human (Homo sapiens)}
gsmstselkkvvalydympmnandlqlrkgdeyfileesnlpwwrardkngqegyipsny
vteaeds
>d1awz__ 4.4.1.1.4 Angiogenin {Human (Homo sapiens)}
qdnsrythfltqhydakpqgrddrycesimrrrgltspckdintfihgnkrsikaicenk
ngnphrenlriskssfqvttcklhggspwppcqyratagfrnvvvacenglpvhldqsif
rrp
>d1ax0__ 2.21.1.1.6 Lectin {coral tree (Erythrina corallodendron)}
vetisfsfsefepgndnltlqgaalitqsgvlqltkinqngmpawdstgrtlyakpvhiw
dmttgtvasfetrfsfsieqpytrplpadglvffmgptkskpaqgygylgifnnskqdns
yqtlgvefdtfsnpwdppqvphigidvnsirsiktqpfqldngqvanvvikydasskilh
avlvypssgaiytiaeivdvkqvlpewvdvglsgatgaqrdaaethdvyswsfqaslpe
>d1ax1__ 2.21.1.1.6 Lectin {coral tree (Erythrina corallodendron)}
vetisfsfsefepgndnltlqgaalitqsgvlqltkinqngmpawdstgrtlyakpvhiw
dmttgtvasfetrfsfsieqpytrplpadglvffmgptkskpaqgygylgifnnskqdns
yqtlgvefdtfsnpwdppqvphigidvnsirsiktqpfqldngqvanvvikydasskilh
avlvypssgaiytiaeivdvkqvlpewvdvglsgatgaqrdaaethdvyswsfqaslpe
>d1ax2__ 2.21.1.1.6 Lectin {coral tree (Erythrina corallodendron)}
vetisfsfsefepgndnltlqgaalitqsgvlqltkinqngmpawdstgrtlyakpvhiw
dmttgtvasfetrfsfsieqpytrplpadglvffmgptkskpaqgygylgifnnskqdns
yqtlgvefdtfsnpwdppqvphigidvnsirsiktqpfqldngqvanvvikydasskilh
avlvypssgaiytiaeivdvkqvlpewvdvglsgatgaqrdaaethdvyswsfqaslpe
>d1ax3__ 2.65.3.1.1 Glucose permease IIa domain, IIa-glc {(Bacillus subtilis)}
miaeplqneigeevfvspitgeihpitdvpdqvfsgkmmgdgfailpsegivvspvrgki
lnvfptkhaiglqsdggreilihfgidtvslkgegftsfvsegdrvepgqkllevdldav
kpnvpslmtpivftnlaegetvsikasgsvnreqedivkiek
>d1ax4a_ 3.54.1.2.2 Tryptophan indol-lyase (tryptophanase) {(Proteus vulgaris)}
akrivepfrikmvekirvpsreereaalkeagynpfllpssavyidlltdsgtnamsdhq
waamitgdeayagsrnyydlkdkakelfnydyiipahqgrgaenilfpvllkykqkegka
knpvfisnfhfdttaahvelngckainivtekafdsetyddwkgdfdikklkeniaqhga
dnivaivstvtcnsaggqpvsmsnlkevyeiakqhgifvvmdsarfcenayfikardpky
knatikevifdmykyadaltmsakxdpllnigglvairdneeiftlarqrcvpmegfvty
gglagrdmaamvqgleegteeeylhyrigqvkylgdrlreagipiqyptgghavfvdckk
lvpqipgdqfpaqavinalylesgvraveigsfllgrdpatgeqkhadmefmrltiarrv
ytndhmdyiadaliglkekfatlkglefeyeppvlrhftarlkpi
>d1ax4b_ 3.54.1.2.2 Tryptophan indol-lyase (tryptophanase) {(Proteus vulgaris)}
akrivepfrikmvekirvpsreereaalkeagynpfllpssavyidlltdsgtnamsdhq
waamitgdeayagsrnyydlkdkakelfnydyiipahqgrgaenilfpvllkykqkegka
knpvfisnfhfdttaahvelngckainivtekafdsetyddwkgdfdikklkeniaqhga
dnivaivstvtcnsaggqpvsmsnlkevyeiakqhgifvvmdsarfcenayfikardpky
knatikevifdmykyadaltmsakxdpllnigglvairdneeiftlarqrcvpmegfvty
gglagrdmaamvqgleegteeeylhyrigqvkylgdrlreagipiqyptgghavfvdckk
lvpqipgdqfpaqavinalylesgvraveigsfllgrdpatgeqkhadmefmrltiarrv
ytndhmdyiadaliglkekfatlkglefeyeppvlrhftarlkpi
>d1ax4c_ 3.54.1.2.2 Tryptophan indol-lyase (tryptophanase) {(Proteus vulgaris)}
akrivepfrikmvekirvpsreereaalkeagynpfllpssavyidlltdsgtnamsdhq
waamitgdeayagsrnyydlkdkakelfnydyiipahqgrgaenilfpvllkykqkegka
knpvfisnfhfdttaahvelngckainivtekafdsetyddwkgdfdikklkeniaqhga
dnivaivstvtcnsaggqpvsmsnlkevyeiakqhgifvvmdsarfcenayfikardpky
knatikevifdmykyadaltmsakxdpllnigglvairdneeiftlarqrcvpmegfvty
gglagrdmaamvqgleegteeeylhyrigqvkylgdrlreagipiqyptgghavfvdckk
lvpqipgdqfpaqavinalylesgvraveigsfllgrdpatgeqkhadmefmrltiarrv
ytndhmdyiadaliglkekfatlkglefeyeppvlrhftarlkpi
>d1ax4d_ 3.54.1.2.2 Tryptophan indol-lyase (tryptophanase) {(Proteus vulgaris)}
akrivepfrikmvekirvpsreereaalkeagynpfllpssavyidlltdsgtnamsdhq
waamitgdeayagsrnyydlkdkakelfnydyiipahqgrgaenilfpvllkykqkegka
knpvfisnfhfdttaahvelngckainivtekafdsetyddwkgdfdikklkeniaqhga
dnivaivstvtcnsaggqpvsmsnlkevyeiakqhgifvvmdsarfcenayfikardpky
knatikevifdmykyadaltmsakxdpllnigglvairdneeiftlarqrcvpmegfvty
gglagrdmaamvqgleegteeeylhyrigqvkylgdrlreagipiqyptgghavfvdckk
lvpqipgdqfpaqavinalylesgvraveigsfllgrdpatgeqkhadmefmrltiarrv
ytndhmdyiadaliglkekfatlkglefeyeppvlrhftarlkpi
>d1ax9__ 3.56.1.1.1 Acetylcholinesterase {Electric ray (Torpedo californica)}
sellvntksgkvmgtrvpvlsshisaflgipfaeppvgnmrfrrpepkkpwsgvwnasty
pnncqqyvdeqfpgfsgsemwnpnremsedclylniwvpsprpksttvmvwiygggfysg
sstldvyngkylayteevvlvslsyrvgafgflalhgsqeapgnvglldqrmalqwvhdn
iqffggdpktvtifgesaggasvgmhilspgsrdlfrrailqsgspncpwasvsvaegrr
ravelgrnlncnlnsdeelihclrekkpqelidvewnvlpfdsifrfsfvpvidgeffpt
slesmlnsgnfkktqillgvnkdegsffllygapgfskdseskisredfmsgvklsvpha
ndlgldavtlqytdwmddnngiknrdglddivgdhnvicplmhfvnkytkfgngtylyff
nhrasnlvwpewmgvihgyeiefvfglplvkelnytaeeealsrrimhywatfaktgnpn
ephsqeskwplfttkeqkfidlntepmkvhqrlrvqmcvfwnqflpkllnat
>d1axaa_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgsddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1axab_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgsddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1axca1 4.81.1.2.2 (1-126) Prolifirating cell nuclear antigen (PCNA) {Human (Homo sapiens)}
mfearlvqgsilkkvlealkdlineacwdisssgvnlqsmdsshvslvqltlrsegfdty
rcdrnlamgvnltsmskilkcagnediitlraednadtlalvfeapnqekvsdyemklmd
ldveql
>d1axca2 4.81.1.2.2 (127-255) Prolifirating cell nuclear antigen (PCNA) {Human (Homo sapiens)}
gipeqeyscvvkmpsgefaricrdlshigdavviscakdgvkfsasgelgngniklsqts
nvdkeeeavtiemnepvqltfalrylnfftkatplsstvtlsmsadvplvveykiadmgh
lkyylapki
>d1axcc1 4.81.1.2.2 (1-126) Prolifirating cell nuclear antigen (PCNA) {Human (Homo sapiens)}
mfearlvqgsilkkvlealkdlineacwdisssgvnlqsmdsshvslvqltlrsegfdty
rcdrnlamgvnltsmskilkcagnediitlraednadtlalvfeapnqekvsdyemklmd
ldveql
>d1axcc2 4.81.1.2.2 (127-255) Prolifirating cell nuclear antigen (PCNA) {Human (Homo sapiens)}
gipeqeyscvvkmpsgefaricrdlshigdavviscakdgvkfsasgelgngniklsqts
nvdkeeeavtiemnepvqltfalrylnfftkatplsstvtlsmsadvplvveykiadmgh
lkyylapki
>d1axce1 4.81.1.2.2 (1-126) Prolifirating cell nuclear antigen (PCNA) {Human (Homo sapiens)}
mfearlvqgsilkkvlealkdlineacwdisssgvnlqsmdsshvslvqltlrsegfdty
rcdrnlamgvnltsmskilkcagnediitlraednadtlalvfeapnqekvsdyemklmd
ldveql
>d1axce2 4.81.1.2.2 (127-255) Prolifirating cell nuclear antigen (PCNA) {Human (Homo sapiens)}
gipeqeyscvvkmpsgefaricrdlshigdavviscakdgvkfsasgelgngniklsqts
nvdkeeeavtiemnepvqltfalrylnfftkatplsstvtlsmsadvplvveykiadmgh
lkyylapki
>d1axea1 2.25.1.2.2 (1-174,325-374) Alcohol dehydrogenase {human (Homo sapiens)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplwtpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1axea2 3.22.1.1.2 (175-324) Alcohol dehydrogenase {human (Homo sapiens), different isozymes}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1axeb1 2.25.1.2.2 (1-174,325-374) Alcohol dehydrogenase {human (Homo sapiens)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplwtpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1axeb2 3.22.1.1.2 (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_ 1.1.1.1.25 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_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahky
>d1axga1 2.25.1.2.2 (1-174,325-374) Alcohol dehydrogenase {human (Homo sapiens)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1axga2 3.22.1.1.2 (175-324) Alcohol dehydrogenase {human (Homo sapiens), different isozymes}
gfstgygsavkvakvtqgstcavfglggaglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1axgb1 2.25.1.2.2 (1-174,325-374) Alcohol dehydrogenase {human (Homo sapiens)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1axgb2 3.22.1.1.2 (175-324) Alcohol dehydrogenase {human (Homo sapiens), different isozymes}
gfstgygsavkvakvtqgstcavfglggaglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1axgc1 2.25.1.2.2 (1-174,325-374) Alcohol dehydrogenase {human (Homo sapiens)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1axgc2 3.22.1.1.2 (175-324) Alcohol dehydrogenase {human (Homo sapiens), different isozymes}
gfstgygsavkvakvtqgstcavfglggaglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1axgd1 2.25.1.2.2 (1-174,325-374) Alcohol dehydrogenase {human (Homo sapiens)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1axgd2 3.22.1.1.2 (175-324) Alcohol dehydrogenase {human (Homo sapiens), different isozymes}
gfstgygsavkvakvtqgstcavfglggaglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1axh__ 7.3.5.2.3 Atracotoxin-hVI (versutoxin) {australian funnel-web spider (Hadronyche versuta)}
sptcipsgqpcpynenccsqsctfkenengntvkrcd
>d1axia_ 1.26.1.1.6 Growth hormone, somatotropin {human (Homo sapiens)}
tiplsrlfdnamlrahrlhqlafdtyqefeeayipkeqkysflqnpqtslcfsesiptps
nreetqqksnlellrisllliqswlepvqflrsvfanslvygasdsnvydllkdleeriq
tlmgrltdgsprtgqifkqtyskfdtnshnddallknygllycfrrdmtyvatylrivqc
rsvegscgf
>d1axib1 2.1.2.1.7 (32-130) Growth hormone receptor {human (Homo sapiens)}
epkftkcrsperetfschwtdevhhgtknegpiqlfytrrntqewtqewkecpdyvsage
nscyfnssftsiaipycikltsnggtvdekcfsvdeivq
>d1axib2 2.1.2.1.7 (131-236) Growth hormone receptor {human (Homo sapiens)}
pdppialnwtllnvsltgihadiqvrweaprnadiqkgwmvleyelqykevnetkwkmmd
pilttsvpvyslkvdkeyevrvrskqrnsgnygefsevlyvtlpqm
>d1axj__ 2.32.1.5.1 FMN-binding protein {(Desulfovibrio vulgaris) strain Miyazaki F}
mlpgtffevlknegvvaiatqgedgphlvntwnsylkvldgnrivvpvggmhkteanvar
dervlmtlgsrkvagrngpgtgflirgsaafrtdgpefeaiarfkwaraalvitvvsaeq
tl
>d1axma_ 2.31.1.1.3 Acidic FGF {human (Homo sapiens)}
kkpkllycsngghflrilpdgtvdgtrdrsdqhiqlqlsaesvgevyikstetgqylaxd
tdgllygsqtpneeclflerleenhyntyiskkhaeknwfvglkkngsckrgprthygqk
ailflplpvs
>d1axmb_ 2.31.1.1.3 Acidic FGF {human (Homo sapiens)}
pkllycsngghflrilpdgtvdgtrdrsdqhiqlqlsaesvgevyikstetgqylaxdtd
gllygsqtpneeclflerleenhyntyiskkhaeknwfvglkkngsckrgprthygqkai
lflplpv
>d1axmc_ 2.31.1.1.3 Acidic FGF {human (Homo sapiens)}
kpkllycsngghflrilpdgtvdgtrdrsdqhiqlqlsaesvgevyikstetgqylaxdt
dgllygsqtpneeclflerleenhyntyiskkhaeknwfvglkkngsckrgprthygqka
ilflplpv
>d1axmd_ 2.31.1.1.3 Acidic FGF {human (Homo sapiens)}
pkllycsngghflrilpdgtvdgtrdrsdqhiqlqlsaesvgevyikstetgqylaxdtd
gllygsqtpneeclflerleenhyntyiskkhaeknwfvglkkngsckrgprthygqkai
lflplpv
>d1axme_ 2.31.1.1.3 Acidic FGF {human (Homo sapiens)}
kpkllycsngghflrilpdgtvdgtrdrsdqhiqlqlsaesvgevyikstetgqylaxdt
dgllygsqtpneeclflerleenhyntyiskkhaeknwfvglkkngsckrgprthygqka
ilflplpvs
>d1axmf_ 2.31.1.1.3 Acidic FGF {human (Homo sapiens)}
kpkllycsngghflrilpdgtvdgtrdrsdqhiqlqlsaesvgevyikstetgqylaxdt
dgllygsqtpneeclflerleenhyntyiskkhaeknwfvglkkngsckrgprthygqka
ilflplpvs
>d1axn__ 1.55.1.1.2 Annexin III {human (Homo sapiens)}
sasiwvghrgtvrdypdfspsvdaeaiqkairgigtdekmlisiltersnaqrqlivkey
qaaygkelkddlkgdlsghfehlmvalvtppavfdakqlkksmkgagtnedalieilttr
tsrqmkdisqayytvykkslgddissetsgdfrkalltladgrrdeslkvdehlakqdaq
ilykagenrwgtdedkfteilclrsfpqlkltfdeyrnisqkdivdsikgelsghfedll
laivncvrntpaflaerlhralkgigtdeftlnrimvsrseidlldirtefkkhygysly
saiksdtsgdyeitllkicggdd
>d1axq__ 4.34.1.2.1 Ferredoxin {(Azotobacter vinelandii )}
afvvtdncikckytdcvevcpvdcfyegpnflvihpdecidcalcepecpaqaifsedev
pedmqefiqlnaelaevwpnitekkdplpdaedwdgvkgklqhler
>d1axr__ 3.76.1.2.1 Glycogen phosphorylase {rabbit (Oryctolagus cuniculus)}
svrglagvenvtelkknfnrhlhftlvkdrnvatprdyyfalahtvrdhlvgrwirtqqh
yyekdpkriyylslefymgrtlqntmvnlalenacdeatyqlgldmeeleeieedaglgn
gglgrlaacfldsmatlglaaygygiryefgifnqkicggwqmeeaddwlrygnpwekar
peftlpvhfygrvehtsqgakwvdtqvvlampydtpvpgyrnnvvntmrlwsakapndfn
lkdfnvggyiqavldrnlaenisrvlypndnffegkelrlkqeyfvvaatlqdiirrfks
skfgcrdpvrtnfdafpdkvaiqlndthpslaipelmrvlvdlerldwdkawevtvktca
ytnhtvlpealerwpvhlletllprhlqiiyeinqrflnrvaaafpgdvdrlrrmslvee
gavkrinmahlciagshavngvarihseilkktifkdfyelephkfqnktngitprrwlv
lcnpglaeiiaerigeeyisdldqlrkllsyvddeafirdvakvkqenklkfaaylerey
kvhinpnslfdvqvkriheykrqllnclhvitlynrikkepnkfvvprtvmiggkaapgy
hmakmiiklitaigdvvnhdpvvgdrlrviflenyrvslaekvipaadlseqistagtea
sgtgnmkfmlngaltigtmdganvemaeeageenffifgmrvedvdrldqrgynaqeyyd
ripelrqiieqlssgffspkqpdlfkdivnmlmhhdrfkvfadyeeyvkcqervsalykn
prewtrmvirniatsgkfssdrtiaqyareiwgvepsrqrlpapdekip
>d1axsa1 2.1.1.1.91 (1-107) Immunoglobulin (variable domains of L and H chains) {oxy-cope catalytic Fab, chimeric (mouse V domains/human C1 domains)}
elvltqspssmyaslgervtitckasqdinsylnwfqqkpgkspktliyrtnrlvdgvps
rfsgsgsgqdysltissleyedmgiyyclqydefpytfgsgtkleik
>d1axsa2 2.1.1.2.92 (108-211) Immunoglobulin (constant domains of L and H chains) {oxy-cope catalytic Fab, chimeric (mouse V domains/human C1 domains)}
rtvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqd
skdstyslsstltlskadyekhkvyacevthqglsspvtksfnr
>d1axsb1 2.1.1.1.91 (1-113) Immunoglobulin (variable domains of L and H chains) {oxy-cope catalytic Fab, chimeric (mouse V domains/human C1 domains)}
qvqllesgaelmkpgasvkisckatgytfssfwiewvkqrpghglewigeilpgsggthy
nekfkgkatftadkssntaymqlssltsedsavyycarghsyyfydgdywgqgtsvtvss
>d1axsb2 2.1.1.2.92 (114-214) Immunoglobulin (constant domains of L and H chains) {oxy-cope catalytic Fab, chimeric (mouse V domains/human C1 domains)}
astkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkvepk
>d1axsh1 2.1.1.1.91 (1-113) Immunoglobulin (variable domains of L and H chains) {oxy-cope catalytic Fab, chimeric (mouse V domains/human C1 domains)}
qvqllesgaelmkpgasvkisckatgytfssfwiewvkqrpghglewigeilpgsggthy
nekfkgkatftadkssntaymqlssltsedsavyycarghsyyfydgdywgqgtsvtvss
>d1axsh2 2.1.1.2.92 (114-214) Immunoglobulin (constant domains of L and H chains) {oxy-cope catalytic Fab, chimeric (mouse V domains/human C1 domains)}
astkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkvepk
>d1axsl1 2.1.1.1.91 (1-107) Immunoglobulin (variable domains of L and H chains) {oxy-cope catalytic Fab, chimeric (mouse V domains/human C1 domains)}
elvltqspssmyaslgervtitckasqdinsylnwfqqkpgkspktliyrtnrlvdgvps
rfsgsgsgqdysltissleyedmgiyyclqydefpytfgsgtkleik
>d1axsl2 2.1.1.2.92 (108-211) Immunoglobulin (constant domains of L and H chains) {oxy-cope catalytic Fab, chimeric (mouse V domains/human C1 domains)}
rtvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqd
skdstyslsstltlskadyekhkvyacevthqglsspvtksfnr
>d1axx__ 4.70.1.1.2 Cytochrome b5 {rat (Rattus norvegicus)}
dkdvkyytleeiqkhkdskstwvilhhkvydltkfleehpggeevlreqaggdatenfed
vghstdarelsktyiigelhpddrskiakpsetl
>d1axy__ 2.21.1.1.6 Lectin {coral tree (Erythrina corallodendron)}
vetisfsfsefepgndnltlqgaalitqsgvlqltkinqngmpawdstgrtlyakpvhiw
dmttgtvasfetrfsfsieqpytrplpadglvffmgptkskpaqgygylgifnnskqdns
yqtlgvefdtfsnpwdppqvphigidvnsirsiktqpfqldngqvanvvikydasskilh
avlvypssgaiytiaeivdvkqvlpewvdvglsgatgaqrdaaethdvyswsfqaslpe
>d1axz__ 2.21.1.1.6 Lectin {coral tree (Erythrina corallodendron)}
vetisfsfsefepgndnltlqgaalitqsgvlqltkinqngmpawdstgrtlyakpvhiw
dmttgtvasfetrfsfsieqpytrplpadglvffmgptkskpaqgygylgifnnskqdns
yqtlgvefdtfsnpwdppqvphigidvnsirsiktqpfqldngqvanvvikydasskilh
avlvypssgaiytiaeivdvkqvlpewvdvglsgatgaqrdaaethdvyswsfqaslpe
>d1ay0a1 3.28.1.2.1 (3-337) Transketolase {baker's yeast (Saccharomyces cerevisiae)}
qftdidklavstirilavdtvskansghpgaplgmapaahvlwsqmrmnptnpdwinrdr
fvlsnghavallysmlhltgydlsiedlkqfrqlgsrtpghpefelpgvevttgplgqgi
snavgmamaqanlaatynkpgftlsdnytyvflgdgclqegisseasslaghlklgnlia
iyddnkitidgatsisfdedvakryeaygwevlyvengnedlagiakaiaqaklskdkpt
likmtttigygslhagshsvagaplkaddvkqlkskfgfnpdksfvvpqevydhyqktil
kpgveannkwnklfseyqkkfpelgaelarrlsgq
>d1ay0a2 3.28.1.2.1 (338-534) Transketolase {baker's yeast (Saccharomyces cerevisiae)}
lpanwesklptytakdsavatrklsetvledvynqlpeliggsadltpsnltrwkealdf
qppssgsgnysgryirygirehamgaimngisafganykpyggtflnfvsyaagavrlsa
lsghpviwvathdsigvgedgpthqpietlahfrslpniqvwrpadgnevsaayknsles
khtpsiialsrqnlpql
>d1ay0a3 3.39.1.1.1 (535-680) Transketolase, C-terminal domain {baker's yeast (Saccharomyces cerevisiae)}
egssiesaskggyvlqdvanpdiilvatgsevslsveaaktlaaknikarvvslpdfftf
dkqpleyrlsvlpdnvpimsvevlattcwgkyahqsfgidrfgasgkapevfkffgftpe
gvaeraqktiafykgdklisplkkaf
>d1ay0b1 3.28.1.2.1 (3-337) Transketolase {baker's yeast (Saccharomyces cerevisiae)}
qftdidklavstirilavdtvskansghpgaplgmapaahvlwsqmrmnptnpdwinrdr
fvlsnghavallysmlhltgydlsiedlkqfrqlgsrtpghpefelpgvevttgplgqgi
snavgmamaqanlaatynkpgftlsdnytyvflgdgclqegisseasslaghlklgnlia
iyddnkitidgatsisfdedvakryeaygwevlyvengnedlagiakaiaqaklskdkpt
likmtttigygslhagshsvagaplkaddvkqlkskfgfnpdksfvvpqevydhyqktil
kpgveannkwnklfseyqkkfpelgaelarrlsgq
>d1ay0b2 3.28.1.2.1 (338-534) Transketolase {baker's yeast (Saccharomyces cerevisiae)}
lpanwesklptytakdsavatrklsetvledvynqlpeliggsadltpsnltrwkealdf
qppssgsgnysgryirygirehamgaimngisafganykpyggtflnfvsyaagavrlsa
lsghpviwvathdsigvgedgpthqpietlahfrslpniqvwrpadgnevsaayknsles
khtpsiialsrqnlpql
>d1ay0b3 3.39.1.1.1 (535-680) Transketolase, C-terminal domain {baker's yeast (Saccharomyces cerevisiae)}
egssiesaskggyvlqdvanpdiilvatgsevslsveaaktlaaknikarvvslpdfftf
dkqpleyrlsvlpdnvpimsvevlattcwgkyahqsfgidrfgasgkapevfkffgftpe
gvaeraqktiafykgdklisplkkaf
>d1ay1h1 2.1.1.1.100 (1-115) Immunoglobulin (variable domains of L and H chains) {Fab TP7 (mouse), kappa L chain}
evqlqesgpglvkpyqslslsctvtgysitsdyawnwirqfpgnklewmgyitysgttdy
npslksrisitrdtsknqfflqlnsvttedtatyycaryyygywyfdvwgqgttltvss
>d1ay1h2 2.1.1.2.100 (116-209) Immunoglobulin (constant domains of L and H chains) {Fab TP7 (mouse), kappa L chain}
akttapsvyplapvssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsdlytlss
svtvtsstwpsqsitcnvahpasstkvdkkiepr
>d1ay1l1 2.1.1.1.100 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab TP7 (mouse), kappa L chain}
diqmtqspaimsaspgekvtmtcsasssvsymywyqqkpgssprlliydstnlasgvpvr
fsgsgsgtsysltisrmeaedaatyycqqwstypltfgagtklelk
>d1ay1l2 2.1.1.2.100 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab TP7 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1ay2__ 4.18.1.1.1 Pilin {Gc (Neisseria gonorrhoeae)}
ftlielmiviaivgilaavalpayqdytaraqvseaillaegqksavteyylnhgkwpen
ntsagvasppsdikgkyvkevevkngvvtatmlssgvnneikgkklslwarrengsvkwf
cgqpvtrtdddtvadakdgkeidtkhlpstcrdnfdak
>e1ay6.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>e1ay6.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
geadcglrplfekksledkterellesyi
>d1ay9a_ 2.24.1.2.1 UmuD' {(Escherichia coli)}
dyveqridlnqlliqhpsatyfvkasgdsmidggisdgdllivdsaitashgdiviaavd
geftvkklqlrptvqlipmnsayspitissedtldvfgvvihvvkamr
>d1ay9b_ 2.24.1.2.1 UmuD' {(Escherichia coli)}
dyveqridlnqlliqhpsatyfvkasgdsmidggisdgdllivdsaitashgdiviaavd
geftvkklqlrptvqlipmnsayspitissedtldvfgvvihvvkamr
>d1ayaa_ 4.53.1.1.6 Tyrosine phosphatase Syp {mouse (Mus musculus)}
mrrwfhpnitgveaenllltrgvdgsflarpsksnpgdftlsvrrngavthikiqntgdy
ydlyggekfatlaelvqyymehhgqlkekngdvielkypln
>d1ayab_ 4.53.1.1.6 Tyrosine phosphatase Syp {mouse (Mus musculus)}
mrrwfhpnitgveaenllltrgvdgsflarpsksnpgdftlsvrrngavthikiqntgdy
ydlyggekfatlaelvqyymehhgqlkekngdvielkypln
>d1ayba_ 4.53.1.1.6 Tyrosine phosphatase Syp {mouse (Mus musculus)}
rrwfhpnitgveaenllltrgvdgsflarpsksnpgdftlsvrrngavthikiqntgdyy
dlyggekfatlaelvqyymehhgqlkekngdvielkypln
>d1ayca_ 4.53.1.1.6 Tyrosine phosphatase Syp {mouse (Mus musculus)}
rrwfhpnitgveaenllltrgvdgsflarpsksnpgdftlsvrrngavthikiqntgdyy
dlyggekfatlaelvqyymehhgqlkekngdvielkypln
>d1ayd__ 4.53.1.1.6 Tyrosine phosphatase Syp {mouse (Mus musculus)}
mrrwfhpnitgveaenllltrgvdgsflarpsksnpgdftlsvrrngavthikiqntgdy
ydlyggekfatlaelvqyymehhgqlkekngdvielkypln
>d1ayi__ 1.27.2.1.1 ImmE7 protein {(Escherichia coli)}
melknsisdyteaefvqllkeiekenvaatddvldvllehfvkitehpdgtdliyypsdn
rddspegivkeikewraangkpgfkq
>d1ayj__ 7.3.6.4.3 Antifungal protein 1 (RS-AFP1) {Radish (Raphanus sativus l.)}
klcerpsgtwsgvcgnnnacknqcinlekarhgscnyvfpahkcicyfpc
>d1ayk__ 4.52.1.7.1 Fibroblast collagenase {human (Homo sapiens)}
vltegnprweqthltyrienytpdlpradvdhaiekafqlwsnvtpltftkvsegqadim
isfvrgdhrdnspfdgpggnlahafqpgpgiggdahfdederwtnnfreynlhrvaahel
ghslglshstdigalmypsytfsgdvqlaqddidgiqaiygrsqnpvqp
>d1ayl__ 3.79.1.1.1 Phosphoenolpyruvate carboxykinase (ATP-oxaloacetate carboxy-liase) {(Escherichia coli)}
mrvnngltpqeleaygisdvhdivynpsydllyqeeldpsltgyergvltnlgavavdtg
iftgrspkdkyivrddttrdtfwwadkgkgkndnkplspetwqhlkglvtrqlsgkrlfv
vdafcganpdtrlsvrfitevawqahfvknmfirpsdeelagfkpdfivmngakctnpqw
keqglnsenfvafnltermqliggtwyggemkkgmfsmmnyllplkgiasmhcsanvgek
gdvavffglsgtgkttlstdpkrrligddehgwdddgvfnfeggcyaktiklskeaepei
ynairrdallenvtvredgtidfddgsktentrvsypiyhidnivkpvskaghatkvifl
tadafgvlppvsrltadqtqyhflsgftaklagtergiteptptfsacfgaaflslhptq
yaevlvkrmqaagaqaylvntgwngtgkrisikdtraiidailngsldnaetftlpmfnl
aiptelpgvdtkildprntyaspeqwqekaetlaklfidnfdkytdtpagaalvaagpkl
>d1aym1_ 2.8.1.4.8 Rhinovirus coat protein {Human (Homo sapiens) rhinovirus 16}
npveryvdevlnevlvvpninqshpttsnaapvldaaetghtnkiqpedtietryvqssq
tldemsvesflgrsgcihesvldivdnyndqsftkwninlqemaqirrkfemftyarfds
eitmvpsvaakdghighivmqymyvppgapipttrddyawqsgtnasvfwqhgqpfprfs
lpflsiasayymfydgydgdtyksrygtvvtndmgtlcsrivtseqlhkvkvvtriyhka
khtkawcprppravqyshthttnyklssevhndvairprtnlttv
>d1aym2_ 2.8.1.4.8 Rhinovirus coat protein {Human (Homo sapiens) rhinovirus 16}
sdriiqitrgdstitsqdvanavvgygvwphyltpqdataidkptqpdtssnrfytldsk
mwnstskgwwwklpdalkdmgifgenmfyhflgrsgytvhvqcnaskfhqgtllvvmipe
hqlatvnkgnvnagykythpgeagrevgtqvenekqpsddnwlnfdgtllgnllifphqf
inlrsnnsatlivpyvnavpmdsmvrhnnwslviipvcqlqsnnisnivpitvsispmca
efsgaraktvvq
>d1aym3_ 2.8.1.4.8 Rhinovirus coat protein {Human (Homo sapiens) rhinovirus 16}
glpvyvtpgsgqfmttddmqspcalpwyhptkeifipgevknliemcqvdtlipinstqs
nignvsmytvtlspqtklaeeifaikvdiashplattligeiasyfthwtgslrfsfmfc
gtanttlkvllaytppgigkprsrkeamlgthvvwdvglqstvslvvpwisasqyrfttp
dtyssagyitcwyqtnfvvppntpntaemlcfvsgckdfclrmardtdlhkqtgpitq
>d1ayn1_ 2.8.1.4.8 Rhinovirus coat protein {Human (Homo sapiens) rhinovirus 16}
npveryvdevlnevlvvpninqshpttsnaapvldaaetghtnkiqpedtietryvqssq
tldemsvesflgrsgcihesvldivdnyndqsftkwninlqemaqirrkfemftyarfds
eitmvpsvaakdghighivmqymyvppgapipttrddyawqsgtnasvfwqhgqpfprfs
lpflsiasayymfydgydgdtyksrygtvvtndmgtlcsrivtseqlhkvkvvtriyhka
khtkawcprppravqyshthttnyklssevhndvairprtnlttv
>d1ayn2_ 2.8.1.4.8 Rhinovirus coat protein {Human (Homo sapiens) rhinovirus 16}
sdriiqitrgdstitsqdvanavvgygvwphyltpqdataidkptqpdtssnrfytldsk
mwnstskgwwwklpdalkdmgifgenmfyhflgrsgytvhvqcnaskfhqgtllvvmipe
hqlatvnkgnvnagykythpgeagrevgtqvenekqpsddnwlnfdgtllgnllifphqf
inlrsnnsatlivpyvnavpmdsmvrhnnwslviipvcqlqsnnisnivpitvsispmca
efsgaraktvvq
>d1ayn3_ 2.8.1.4.8 Rhinovirus coat protein {Human (Homo sapiens) rhinovirus 16}
glpvyvtpgsgqfmttddmqspcalpwyhptkeifipgevknliemcqvdtlipinstqs
nignvsmytvtlspqtklaeeifaikvdiashplattligeiasyfthwtgslrfsfmfc
gtanttlkvllaytppgigkprsrkeamlgthvvwdvglqstvslvvpwisasqyrfttp
dtyssagyitcwyqtnfvvppntpntaemlcfvsgckdfclrmardtdlhkqtgpitq
>d1aypa_ 1.103.1.2.10 Phospholipase A2 {human (Homo sapiens) synovial fluid}
nlvnfhrmiklttgkeaalsygfygchcgvggrgspkdatdrccvthdccykrlekrgcg
tkflsykfsnsgsritcakqdscrsqlcecdkaaatcfarnkttynkkyqyysnkhcrgs
tprc
>d1aypb_ 1.103.1.2.10 Phospholipase A2 {human (Homo sapiens) synovial fluid}
nlvnfhrmiklttgkeaalsygfygchcgvggrgspkdatdrccvthdccykrlekrgcg
tkflsykfsnsgsritcakqdscrsqlcecdkaaatcfarnkttynkkyqyysnkhcrgs
tprc
>d1aypc_ 1.103.1.2.10 Phospholipase A2 {human (Homo sapiens) synovial fluid}
nlvnfhrmiklttgkeaalsygfygchcgvggrgspkdatdrccvthdccykrlekrgcg
tkflsykfsnsgsritcakqdscrsqlcecdkaaatcfarnkttynkkyqyysnkhcrgs
tprc
>d1aypd_ 1.103.1.2.10 Phospholipase A2 {human (Homo sapiens) synovial fluid}
nlvnfhrmiklttgkeaalsygfygchcgvggrgspkdatdrccvthdccykrlekrgcg
tkflsykfsnsgsritcakqdscrsqlcecdkaaatcfarnkttynkkyqyysnkhcrgs
tprc
>d1aype_ 1.103.1.2.10 Phospholipase A2 {human (Homo sapiens) synovial fluid}
nlvnfhrmiklttgkeaalsygfygchcgvggrgspkdatdrccvthdccykrlekrgcg
tkflsykfsnsgsritcakqdscrsqlcecdkaaatcfarnkttynkkyqyysnkhcrgs
tprc
>d1aypf_ 1.103.1.2.10 Phospholipase A2 {human (Homo sapiens) synovial fluid}
nlvnfhrmiklttgkeaalsygfygchcgvggrgspkdatdrccvthdccykrlekrgcg
tkflsykfsnsgsritcakqdscrsqlcecdkaaatcfarnkttynkkyqyysnkhcrgs
tprc
>d1ayx__ 1.81.1.1.2 Glucoamylase {Yeast (Saccharomycopsis fibuligera)}
aypsfeaysnykvdrtdletfldkqkevslyyllqniaypegqfnngvpgtviaspstsn
pdyyyqwtrdsaitfltvlselednnfnttlakaveyyintsynlqrtsnpsgsfddenh
kglgepkfntdgsaytgawgrpqndgpalrayaisrylndvnslnegklvltdsgdinfs
stediykniikpdleyvigywdstgfdlweenqgrhfftslvqqkalayavdiaksfddg
dfantlsstastlesylsgsdggfvntdvnhivenpdllqqnsrqgldsatyigpllthd
igessstpfdvdneyvlqsyylllednkdrysvnsaysagaaigrypedvyngdgssegn
pwflatayaaqvpyklaydaksasnditinkinydffnkyivdlstinsayqssdsvtik
sgsdefntvadnlvtfgdsflqvildhinddgslneqlnrytgystgaysltwssgalle
airlrnkvkala
>e1ayy.1a 4.95.1.4.2 Glycosylasparaginase (aspartylglucosaminidase, AGA) {(Flavobacterium meningosepticum)}
tnkpivlstwnfglhanveawkvlskggkaldavekgvrlveddptersvgyggrpdrdg
rvtldacimdenynigsvacmehiknpisvaravmektphvmlvgdgalefalsqgfkke
nlltaesekewkewlkts
>e1ayy.1b 4.95.1.4.2 Glycosylasparaginase (aspartylglucosaminidase, AGA) {(Flavobacterium meningosepticum)}
tigmialdaqgnlsgacttsgmaykmhgrvgdspiigaglfvdneigaatatghgeevir
tvgthlvvelmnqgrtpqqackeaverivkivnrrgknlkdiqvgfialnkkgeygayci
qdgfnfavhdqkgnrletpgfal
>e1ayy.2c 4.95.1.4.2 Glycosylasparaginase (aspartylglucosaminidase, AGA) {(Flavobacterium meningosepticum)}
tnkpivlstwnfglhanveawkvlskggkaldavekgvrlveddptersvgyggrpdrdg
rvtldacimdenynigsvacmehiknpisvaravmektphvmlvgdgalefalsqgfkke
nlltaesekewkewlktsqy
>e1ayy.2d 4.95.1.4.2 Glycosylasparaginase (aspartylglucosaminidase, AGA) {(Flavobacterium meningosepticum)}
tigmialdaqgnlsgacttsgmaykmhgrvgdspiigaglfvdneigaatatghgeevir
tvgthlvvelmnqgrtpqqackeaverivkivnrrgknlkdiqvgfialnkkgeygayci
qdgfnfavhdqkgnrletpgfalk
>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__ 3.1.5.1.2 Aldose reductase (aldehyde reductase) {human (Homo sapiens)}
srlllnngakmpilglgtwksppgqvteavkvaidvgyrhidcahvyqnenevgvaiqek
lreqvvkreelfivsklwctyhekglvkgacqktlsdlkldyldlylihwptgfkpgkef
fpldesgnvvpsdtnildtwaameelvdeglvkaigisnfnhlqvemilnkpglkykpav
nqiechpyltqekliqycqskgivvtaysplgspdrpyakpedpslledprikaiaakhn
kttaqvlirfpmqrnlvvipksvtperiaenfkvfdfelssqdmttllsynrnwrvaall
sctshkdypfheef
>d1az2__ 3.1.5.1.2 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__ 2.38.1.1.6 Simian immunodeficiency virus (SIV) protease {simian immunodeficiency virus (Mac251 isolate)}
pqfhlwkrpvvtahiegqpvevlldtgaddsivtgielgphytpkivggiggfintkeyk
nvevevlgkrikgtimtgdtpinifgrnlltalgmslnf
>d1az6__ 7.3.7.1.1 Cellobiohydrolase I {ct-cbh I from (Trichoderma reesei)}
tqshagqcggigysgptvcasgttcqvlnpyysqcl
>d1azba_ 2.5.1.1.15 Azurin {(Alcaligenes denitrificans)}
aqceatiesndamqynlkemvvdksckqftvhlkhvgkmakvamghnwvltkeadkqgva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
mkgtlklsn
>d1azbb_ 2.5.1.1.15 Azurin {(Alcaligenes denitrificans)}
aqceatiesndamqynlkemvvdksckqftvhlkhvgkmakvamghnwvltkeadkqgva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
mkgtlklsn
>d1azca_ 2.5.1.1.15 Azurin {(Alcaligenes denitrificans)}
aqceatiesndamqynlkemvvdksckqftvhlkhvgkmakvamghnwvltkeadkqgva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
mkgtlklsn
>d1azcb_ 2.5.1.1.15 Azurin {(Alcaligenes denitrificans)}
aqceatiesndamqynlkemvvdksckqftvhlkhvgkmakvamghnwvltkeadkqgva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
mkgtlklsn
>d1azda_ 2.21.1.1.2 Concanavalin A {Brazilian jackbean (Canavalia brasiliensis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvgkr
lsavvsypngdsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtegnlrltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1azdb_ 2.21.1.1.2 Concanavalin A {Brazilian jackbean (Canavalia brasiliensis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvgkr
lsavvsypngdsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtegnlrltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1azdc_ 2.21.1.1.2 Concanavalin A {Brazilian jackbean (Canavalia brasiliensis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvgkr
lsavvsypngdsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtegnlrltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1azdd_ 2.21.1.1.2 Concanavalin A {Brazilian jackbean (Canavalia brasiliensis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvgkr
lsavvsypngdsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtegnlrltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1azf__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1azgb_ 2.24.2.1.2 Fyn proto-oncogene tyrosine kinase, SH3 domain {human (Homo sapiens)}
vtlfvalydyearteddlsfhkgekfqilnssegdwwearslttgetgyipsnyvapv
>d1azh__ 7.3.7.1.1 Cellobiohydrolase I {ct-cbh I from (Trichoderma reesei)}
tqshagqcggigysgptvcasgttcqvlnpyysqcl
>d1azi__ 1.1.1.1.8 Myoglobin {horse (Equus caballus)}
glsdgewqqvlnvwgkveadiaghgqevlirlftghpetlekfdkfkhlkteaemkased
lkkhgtvvltalggilkkkghheaelkplaqshatkhkipikylefisdaiihvlhskhp
gdfgadaqgamtkalelfrndiaakykelgfqg
>d1azj__ 7.3.7.1.1 Cellobiohydrolase I {ct-cbh I from (Trichoderma reesei)}
tqshygqcggigysgptvcasgttcqvlnpaysqcl
>d1azk__ 7.3.7.1.1 Cellobiohydrolase I {ct-cbh I from (Trichoderma reesei)}
tqshygqcggigysgptvcasgttcqvlnpyasqcl
>d1azl__ 3.14.4.1.2 Flavodoxin {(Desulfovibrio vulgaris)}
pkalivygsttgnteytaetiareladagyevdsrdaasveagglfegfdlvllgcstwv
ddsielqddfiplfdsleetgaqgrkvacfgcgdssyeyfcgavdaieeklknlgaeivq
dglridgdpraarddivgwahdvrgai
>d1azm__ 2.56.1.1.1 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme I}
pdwgyddkngpeqwsklypiangnnqspvdiktsetkhdtslkpisvsynpatakeiinv
ghsfhvnfedndnrsvlkggpfsdsyrlfqfhfhwgstnehgsehtvdgvkysaelhvah
wnsakysslaeaaskadglavigvlmkvgeanpklqkvldalqaiktkgkrapftnfdps
tllpssldfwtypgslthpplyesvtwiickesisvsseqlaqfrsllsnvegdnavpmq
hnnrptqplkgrtvrasf
>d1azna_ 2.5.1.1.17 Azurin {(Pseudomonas aeruginosa)}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctapghsal
mkgtltlk
>d1aznb_ 2.5.1.1.17 Azurin {(Pseudomonas aeruginosa)}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctapghsal
mkgtltlk
>d1aznc_ 2.5.1.1.17 Azurin {(Pseudomonas aeruginosa)}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctapghsal
mkgtltlk
>d1aznd_ 2.5.1.1.17 Azurin {(Pseudomonas aeruginosa)}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctapghsal
mkgtltlk
>d1azo__ 3.43.1.8.1 DNA mismatch repair protein MutH from {(Escherichia coli)}
prpllsppeteeqllaqaqqlsgytlgelaalvglvtpenlkrdkgwigvlleiwlgasa
gskpeqdfaalgvelktipvdslgrplettfvcvapltgnsgvtwetshvrhklkrvlwi
pvegeasiplaqrrvgspllwspneeedrqlredweelxdxivlgqveritarhgeylqi
rpkaanakalteaigargeriltlprgfylkknftsallarhfliq
>d1azra_ 2.5.1.1.17 Azurin {(Pseudomonas aeruginosa)}
aqcsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghdwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctfpghsal
mkgtltlk
>d1azrb_ 2.5.1.1.17 Azurin {(Pseudomonas aeruginosa)}
aqcsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghdwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctfpghsal
mkgtltlk
>d1azrc_ 2.5.1.1.17 Azurin {(Pseudomonas aeruginosa)}
aqcsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghdwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctfpghsal
mkgtltlk
>d1azrd_ 2.5.1.1.17 Azurin {(Pseudomonas aeruginosa)}
aqcsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghdwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctfpghsal
mkgtltlk
>d1azsa_ 4.34.22.1.2 Adenylyl cyclase VC1, domain C1a {Dog (Canis familiaris)}
dmmfhkiyiqkhdnvsilfadiegftslasqctaqelvmtlnelfarfdklaaenhclri
kilgdcyycvsglpearadhahccvemgmdmieaislvremtgvnvnmrvgihsgrvhcg
vlglrkwqfdvwsndvtlanhmeaggkagrihitkatlsylngdyevepgcggernaylk
ehsietflil
>d1azsb_ 4.34.22.1.3 Adenylyl cyclase IIC1, domain C2a {Rat (Rattus norvegicus)}
hqsydcvcvmfasipdfkefytesdvnkegleclrllneiiadfddllskpkfsgvekik
tigstymaatglsaipsqehaqeperqymhigtmvefayalvgkldainkhsfndfklrv
ginhgpviagvigaqkpqydiwgntvnvasrmdstgvldkiqvteetslilqtlgytctc
rgiinvkgkgdlktyfvnt
>d1azsc1 1.56.1.1.1 (86-201) Transducin (alpha subunit), insertion domain {bovine (Bos taurus)}
gfngdgekatkvqdiknnlkeaietivaamsnlvppvelanpenqfrvdyilsvmnvpdf
dfppefyehakalwedegvracyersneyqlidcaqyfldkidvikqddyvpsdqdllrc
r
>d1azsc2 3.29.1.4.11 (36-66,202-393) Transducin (alpha subunit) {bovine (Bos taurus)}
vyrathrllllgagesgkstivkqmrilhvnXvltsgifetkfqvdkvnfhmfdvggqrd
errkwiqcfndvtaiifvvasssynmvirednqtnrlqealnlfksiwnnrwlrtisvil
flnkqdllaekvlagkskiedyfpefaryttpedatpepgedprvtrakyfirdeflris
tasgdgrhycyphftcavdtenirrvfndcrdiiqrmhlrqyel
>d1azta1 1.56.1.1.1 (88-201) Transducin (alpha subunit), insertion domain {bovine (Bos taurus)}
katkvqdiknnlkeaietivaamsnlvppvelanpenqfrvdyilsvmnvpdfdfppefy
ehakalwedegvracyersneyqlidcaqyfldkidvikqddyvpsdqdllrcr
>d1azta2 3.29.1.4.11 (35-65,202-391) Transducin (alpha subunit) {bovine (Bos taurus)}
qvyrathrllllgagesgkstivkqmrilhvXvltsgifetkfqvdkvnfhmfdvggqrd
errkwiqcfndvtaiifvvasssynmvirednqtnrlqealnlfksiwnnrwlrtisvil
flnkqdllaekvlagkskiedyfpefaryttpedatpepgedprvtrakyfirdeflris
tasgdgrhycyphftcavdtenirrvfndcrdiiqrmhlrqy
>d1aztb1 1.56.1.1.1 (88-201) Transducin (alpha subunit), insertion domain {bovine (Bos taurus)}
katkvqdiknnlkeaietivaamsnlvppvelanpenqfrvdyilsvmnvpdfdfppefy
ehakalwedegvracyersneyqlidcaqyfldkidvikqddyvpsdqdllrcr
>d1aztb2 3.29.1.4.11 (35-66,202-391) Transducin (alpha subunit) {bovine (Bos taurus)}
qvyrathrllllgagesgkstivkqmrilhvnXvltsgifetkfqvdkvnfhmfdvggqr
derrkwiqcfndvtaiifvvasssynmvirednqtnrlqealnlfksiwnnrwlrtisvi
lflnkqdllaekvlagkskiedyfpefaryttpedatpepgedprvtrakyfirdeflri
stasgdgrhycyphftcavdtenirrvfndcrdiiqrmhlrqy
>d1azu__ 2.5.1.1.17 Azurin {(Pseudomonas aeruginosa)}
csvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvvtd
gmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctfpghsalmk
gtltlk
>d1azva_ 2.1.7.1.2 Cu,Zn superoxide dismutase, SOD {human (Homo sapiens)}
atkavcvlkgdgpvqgiinfeqkesngpvkvwgsikrlteglhgfhvhefgdntagctsa
gphfnplsrkhggpkdeerhvgdlgnvtadkdgvadvsiedsvislsgdhciigrtlvvh
ekaddlgkggneestktgnagsrlacgvigiaq
>d1azvb_ 2.1.7.1.2 Cu,Zn superoxide dismutase, SOD {human (Homo sapiens)}
atkavcvlkgdgpvqgiinfeqkesngpvkvwgsikrlteglhgfhvhefgdntagctsa
gphfnplsrkhggpkdeerhvgdlgnvtadkdgvadvsiedsvislsgdhciigrtlvvh
ekaddlgkggneestktgnagsrlacgvigiaq
>d1azza_ 2.35.1.2.8 Crab collagenase {Atlantic sand fiddler crab (Uca pugilator)}
ivggveavpnswphqaalfiddmyfcggslispewiltaahcmdgagfvdvvlgahnire
deatqvtiqstdftvhenynsfvisndiavirlpvpvtltaaiatvglpstdvgvgtvvt
ptgwglpsdsalgisdvlrqvdvpimsnadcdavygivtdgnicidstggkgtcngdsgg
plnyngltygitsfgaaagceagypdaftrvtyfldwiqtqtgitp
>d1azzb_ 2.35.1.2.8 Crab collagenase {Atlantic sand fiddler crab (Uca pugilator)}
ivggveavpnswphqaalfiddmyfcggslispewiltaahcmdgagfvdvvlgahnire
deatqvtiqstdftvhenynsfvisndiavirlpvpvtltaaiatvglpstdvgvgtvvt
ptgwglpsdsalgisdvlrqvdvpimsnadcdavygivtdgnicidstggkgtcngdsgg
plnyngltygitsfgaaagceagypdaftrvtyfldwiqtqtgitp
>d1azzc_ 2.12.1.1.1 Ecotin, trypsin inhibitor {(Escherichia coli)}
plekiapypqaekgmkrqviqltpqedestlkvelligqtlevdcnlhrlggklenktle
gwgydyyvfdkvsspvstmmacpdgkkekkfvtaylgdagmlrynsklpivvytpdnvdv
kyrvwkaeekidnavvr
>d1azzd_ 2.12.1.1.1 Ecotin, trypsin inhibitor {(Escherichia coli)}
qplekiapypqaekgmkrqviqltpqedestlkvelligqtlevdcnlhrlggklenktl
egwgydyyvfdkvsspvstmmacpdgkkekkfvtaylgdagmlrynsklpivvytpdnvd
vkyrvwkaeekidnavvr
>d1b5a__ 4.70.1.1.2 Cytochrome b5 {rat (Rattus norvegicus)}
dkdvkyytleeiqkhkdskstwvilhhkvydltkfleehpggeevlreqaggdatenfed
vghstdarelsktyiigelhpddrskiakpsetl
>d1b5b__ 4.70.1.1.2 Cytochrome b5 {rat (Rattus norvegicus)}
dkdvkyytleeiqkhkdskstwvilhhkvydltkfleehpggeevlreqaggdatenfed
vghstdarelsktyiigelhpddrskiakpsetl
>e1b5g.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1b5g.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
eadcglrplfekksledkterellesyid
>d1b5m__ 4.70.1.1.2 Cytochrome b5 {rat (Rattus norvegicus)}
avtyyrleevakrntaeetwmvihgrvyditrflsehpggeevlleqagadatesfedvg
hspdaremlkqyyigdvhpndlkp
>d1ba0_1 3.47.1.1.1 (4-188) Heat shock protein 70kDa, ATPase fragment {bovine (Bos taurus)}
gpavgidlgttyscvgvfqhgkveiiandqgnrttpsyvaftdterligdaaknqvamnp
tntvfdakrligrrfddavvqsdmkhwpfmvvndagrpkvqveykgetksfypeevssmv
ltkmkeiaeaylgktvtnavvtvpayfndsqrqatkdagtiaglnvlriineptaaaiay
gldkk
>d1ba0_2 3.47.1.1.1 (189-381) Heat shock protein 70kDa, ATPase fragment {bovine (Bos taurus)}
vgaernvlifdlgggtfkvsiltiedgifevkstagdthlggedfdnrmvnhfiaefkrk
hkkdisenkravrrlrtacerakrtlssstqasieidslyegidfytsitrarfeelnad
lfrgtldpvekalrdakldksqihdivlvggstripkiqkllqdffngkelnksinpdea
vaygaavqaails
>d1ba1_1 3.47.1.1.1 (4-188) Heat shock protein 70kDa, ATPase fragment {bovine (Bos taurus)}
gpavgidlgttyskvgvfqhgkveiiandqgnrttpsyvaftdterligdaaknqvamnp
tntvfdakrligrrfddavvqsdmkhwpfmvvndagrpkvqveykgetksfypeevssmv
ltkmkeiaeaylgktvtnavvtvpayfndsqrqatkdagtiaglnvlriineptaaaiay
gldkk
>d1ba1_2 3.47.1.1.1 (189-381) Heat shock protein 70kDa, ATPase fragment {bovine (Bos taurus)}
vgaernvlifdlgggtfdvsiltiedgifevkstagdthlggedfdnrmvnhfiaefkrk
hkkdisenkravrrlrtacerakrtlssstqasieidslyegidfytsitrarfeelnad
lfrgtldpvekalrdakldksqihdivlvggstripkiqkllqdffngkelnksinpdea
vaygaavqaails
>d1ba2a_ 3.81.1.1.1 D-ribose-binding protein {(Escherichia coli), strain k-12}
kdtialvvstlnnpffvslkdgaqkeadklgynlvvldsqnnpakelanvqdltvrgtki
llinptrsdavgnavkmanqanipvitldrqatkgevvshiasdnvlggkiagdyiakka
gegakvielqgiagtsaarergegfqqavaahkfnvlasqpadfdrikglnvmqnlltah
pdvqavfaqndemalgalralqtagksdvmvvgfdgtpdgekavndgklaatiaqlpdqi
gakgvetadkvlkgekvqakypvdlklvvkq
>d1ba2b_ 3.81.1.1.1 D-ribose-binding protein {(Escherichia coli), strain k-12}
kdtialvvstlnnpffvslkdgaqkeadklgynlvvldsqnnpakelanvqdltvrgtki
llinptrsdavgnavkmanqanipvitldrqatkgevvshiasdnvlggkiagdyiakka
gegakvielqgiagtsaarergegfqqavaahkfnvlasqpadfdrikglnvmqnlltah
pdvqavfaqndemalgalralqtagksdvmvvgfdgtpdgekavndgklaatiaqlpdqi
gakgvetadkvlkgekvqakypvdlklvvkq
>d1ba7a_ 2.31.4.1.4 Soybean trypsin inhibitor {Soybean (Glycine max)}
dfvldnegnplenggtyyilsditafggiraaptgnercpltvvqsrneldkgigtiiss
pyrirfiaeghplslkfdsfavimlcvgiptewsvvedlpegpavkigenkdamdgwfrl
ervsddefnnyklvfcpqqaeddkcgdigisidhddgtrrlvvsknkplvvqfqkl
>d1ba7b_ 2.31.4.1.4 Soybean trypsin inhibitor {Soybean (Glycine max)}
dfvldnegnplenggtyyilsditafggiraaptgnercpltvvqsrneldkgigtiiss
pyrirfiaeghplslkfdsfavimlcvgiptewsvvedlpegpavkigenkdamdgwfrl
ervsddefnnyklvfcpqqaeddkcgdigisidhddgtrrlvvsknkplvvqfqkl
>d1baba_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
xmelspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkgh
gkkvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeft
pavhasldkflasvstvltskyr
>d1babb_ 1.1.1.1.25 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_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1bafh1 2.1.1.1.11 (1-115) Immunoglobulin (variable domains of L and H chains) {Fab ANO2 (mouse), kappa L chain}
dvqlqesgpglvkpsqsqsltctvtgysitsdyawnwirqfpgnklewmgymsysgstry
npslrsrisitrdtsknqfflqlksvttedtatyfcargwplaywgqgtqvsvse
>d1bafh2 2.1.1.2.20 (116-217) Immunoglobulin (constant domains of L and H chains) {Fab ANO2 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpssprpsetvtcnvahpasstkvdkkivprdc
>d1bafl1 2.1.1.1.11 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab ANO2 (mouse), kappa L chain}
qivltqspaimsaspgekvtmtcsasssvyymywyqqkpgssprlliydtsnlasgvpvr
fsgsgsgtsysltisrmeaedaatyycqqwssyppitfgvgtklelkr
>d1bafl2 2.1.1.2.20 (109-214) Immunoglobulin (constant domains of L and H chains) {Fab ANO2 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1bah__ 7.3.6.2.4 Charybdotoxin {scorpion (Leiurus quinquestriatus hebraeus)}
ftnvscttskexwsvcqrlhntsrgkcmnkkxrcys
>d1bak__ 2.41.1.1.9 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__ 3.81.1.1.2 L-arabinose-binding protein {(Escherichia coli)}
nlklgflvkqpeepwfqtewkfadkagkdlgfevikiavpdgektlnaidslaasgakgf
victpdpklgsaivakargydmkviavddqfvnakgkpmdtvplvmmaatkigerqgqel
ykemqkrgwdvkesavmaitaneldtarrrttgsmdalkaagfpekqiyqvptksndipg
afdaansmlvqhpevkhwlivgmndstvlggvrategqgfkaadiigigingvdavsels
kaqatgfygsllgspdvhgykssemlynwvakdveppkftevtdvvlitrdnfkeelekk
glggk
>d1bara_ 2.31.1.1.2 Acidic FGF {bovine (Bos taurus)}
pkllycsnggyflrilpdgtvdgtkdrsdqhiqlqlaaesigevyikstetgqflamdtd
gllygsqtpneeclflerleengyntyiskkhaekhwfvglkkngrsklgprthfgqkai
lflplpv
>d1barb_ 2.31.1.1.2 Acidic FGF {bovine (Bos taurus)}
fnlplgnykkpkllycsnggyflrilpdgtvdgtkdrsdqhiqlqlaaesigevyikste
tgqflamdtdgllygsqtpneeclflerleengyntyiskkhaekhwfvglkkngrsklg
prthfgqkailflplpvs
>d1bas__ 2.31.1.1.1 Basic FGF {human (Homo sapiens)}
dpkrlycknggfflrihpdgrvdgvreksdphiklqlqaeergvvsikgvsanrylamke
dgrllasksvtdecffferlesnnyntyrsrkytswyvalkrtgqyklgsktgpgqkail
flpms
>d1bava_ 3.58.4.1.1 Carboxypeptidase A {bovine (Bos taurus)}
arstntfnyatyhtldeiydfmdllvaqhpelvsklqigrsyegrpiyvlkfstggsnrp
aiwidlgihsrewitqatgvwfakkftenygqnpsftaildsmdifleivtnpngfafth
senrlwrktrsvtssslcvgvdanrnwdagfgkagassspcsetyhgkyansevevksiv
dfvknhgnfkaflsihsysqlllypygyttqsipdktelnqvaksavaalkslygtsyky
gsiittiyqasggsidwsynqgikysftfelrdtgrygfllpasqiiptaqetwlgvlti
mehtvnn
>d1bavb_ 3.58.4.1.1 Carboxypeptidase A {bovine (Bos taurus)}
arstntfnyatyhtldeiydfmdllvaqhpelvsklqigrsyegrpiyvlkfstggsnrp
aiwidlgihsrewitqatgvwfakkftenygqnpsftaildsmdifleivtnpngfafth
senrlwrktrsvtssslcvgvdanrnwdagfgkagassspcsetyhgkyansevevksiv
dfvknhgnfkaflsihsysqlllypygyttqsipdktelnqvaksavaalkslygtsyky
gsiittiyqasggsidwsynqgikysftfelrdtgrygfllpasqiiptaqetwlgvlti
mehtvnn
>d1bavc_ 3.58.4.1.1 Carboxypeptidase A {bovine (Bos taurus)}
arstntfnyatyhtldeiydfmdllvaqhpelvsklqigrsyegrpiyvlkfstggsnrp
aiwidlgihsrewitqatgvwfakkftenygqnpsftaildsmdifleivtnpngfafth
senrlwrktrsvtssslcvgvdanrnwdagfgkagassspcsetyhgkyansevevksiv
dfvknhgnfkaflsihsysqlllypygyttqsipdktelnqvaksavaalkslygtsyky
gsiittiyqasggsidwsynqgikysftfelrdtgrygfllpasqiiptaqetwlgvlti
mehtvnn
>d1bavd_ 3.58.4.1.1 Carboxypeptidase A {bovine (Bos taurus)}
arstntfnyatyhtldeiydfmdllvaqhpelvsklqigrsyegrpiyvlkfstggsnrp
aiwidlgihsrewitqatgvwfakkftenygqnpsftaildsmdifleivtnpngfafth
senrlwrktrsvtssslcvgvdanrnwdagfgkagassspcsetyhgkyansevevksiv
dfvknhgnfkaflsihsysqlllypygyttqsipdktelnqvaksavaalkslygtsyky
gsiittiyqasggsidwsynqgikysftfelrdtgrygfllpasqiiptaqetwlgvlti
mehtvnn
>d1bax__ 1.62.1.3.1 Mason-pfizer monkey virus matrix protein {MPMV (Simian mason-pfizer virus)}
mgqelsqheryveqlkqalktrgvkvkyadllkffdfvkdtcpwfpqegtidikrwrrvg
dcfqdyyntfgpekvpvtafsywnlikelidkke
>d1baya1 1.43.1.1.2 (79-209) Glutathione S-transferase {mouse (Mus musculus)}
ygknqreaaqmdmvndgvedlrgkyvtliytnyengkndyvkalpghlkpfetllsqnqg
gkafivgdqisfadynlldlllihqvlapgcldnfpllsayvarlsarpkikaflsspeh
vnrpingngkq
>d1baya2 3.38.1.4.2 (1-78) Glutathione S-transferase {mouse (Mus musculus) class pi}
ppytivyfpvrgrceamrmlladqgqswkeevvtidtwmqglkptclygqlpkfedgdlt
lyqsnailrhlgrslgl
>d1bayb1 1.43.1.1.2 (79-209) Glutathione S-transferase {mouse (Mus musculus)}
ygknqreaaqmdmvndgvedlrgkyvtliytnyengkndyvkalpghlkpfetllsqnqg
gkafivgdqisfadynlldlllihqvlapgcldnfpllsayvarlsarpkikaflsspeh
vnrpingngkq
>d1bayb2 3.38.1.4.2 (1-78) Glutathione S-transferase {mouse (Mus musculus) class pi}
ppytivyfpvrgrceamrmlladqgqswkeevvtidtwmqglkptclygqlpkfedgdlt
lyqsnailrhlgrslgl
>d1baza_ 1.41.1.1.1 Arc repressor {(Salmonella )bacteriophage P22}
skmpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1bazb_ 1.41.1.1.1 Arc repressor {(Salmonella )bacteriophage P22}
kmpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfk
>d1bazc_ 1.41.1.1.1 Arc repressor {(Salmonella )bacteriophage P22}
mpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegrig
>d1bazd_ 1.41.1.1.1 Arc repressor {(Salmonella )bacteriophage P22}
mpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfk
>d1bb9__ 2.24.2.1.23 Amphiphysin 2 {Rat (Rattus norvegicus)}
ttgrldlppgfmfkvqaqhdytatdtdelqlkagdvvlvipfqnpeeqdegwlmgvkesd
wnqhkelekcrgvfpenftervq
>d1bbba_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1bbbb_ 1.1.1.1.25 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_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1bbc__ 1.103.1.2.10 Phospholipase A2 {human (Homo sapiens) synovial fluid}
nlvnfhrmiklttgkeaalsygfygchcgvggrgspkdatdrccvthdccykrlekrgcg
tkflsykfsnsgsritcakqdscrsqlcecdkaaatcfarnkttynkkyqyysnkhcrgs
tprc
>d1bbdh1 2.1.1.1.12 (1-119) Immunoglobulin (variable domains of L and H chains) {Fab 8F5 (mouse), kappa L chain}
evqlqqsgaelvrpgasvklscttsgfnikdiyihwvkqrpeqglewigrldpangytky
dpkfqgkatitvdtssntaylhlssltsedtavyycdgyysyydmdywgpgtsvtvssa
>d1bbdh2 2.1.1.2.21 (120-218) Immunoglobulin (constant domains of L and H chains) {Fab 8F5 (mouse), kappa L chain}
kttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsdl
ytlsssvtvtsstwpsqsitcnvahpasstkvdkkiepr
>d1bbdl1 2.1.1.1.12 (1-114) Immunoglobulin (variable domains of L and H chains) {Fab 8F5 (mouse), kappa L chain}
divmtqspssltvttgekvtmtckssqsllnsrtqknyltwyqqkpgqspklliywastr
esgvpdrftgsgsgtdftlsisgvqaedlavyycqnnynypltfgagtklelkr
>d1bbdl2 2.1.1.2.21 (115-219) Immunoglobulin (constant domains of L and H chains) {Fab 8F5 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrne
>d1bbg__ 7.5.1.1.1 Amb  V allergen {Giant ragweed (Ambrosia trifida) pollen}
ddglcyegtncgkvgkyccspigkycvcydskaicnknct
>d1bbha_ 1.24.3.2.2 Cytochrome c' {(Chromatium vinosum)}
aglspeeqietrqagyefmgwnmgkikanlegeynaaqveaaanviaaiansgmgalygp
gtdknvgdvktrvkpeffqnmedvgkiarefvgaantlaevaatgeaeavktafgdvgaa
ckschekyrak
>d1bbhb_ 1.24.3.2.2 Cytochrome c' {(Chromatium vinosum)}
aglspeeqietrqagyefmgwnmgkikanlegeynaaqveaaanviaaiansgmgalygp
gtdknvgdvktrvkpeffqnmedvgkiarefvgaantlaevaatgeaeavktafgdvgaa
ckschekyrak
>d1bbi__ 7.3.11.1.1 Bowman-Birk inhibitor {soybean (Glycine max)}
ddesskpccdqcactksnppqcrcsdmrlnschsackscicalsypaqcfcvditdfcye
pckpseddken
>d1bbjh1 2.1.1.1.13 (1-115) Immunoglobulin (variable domains of L and H chains) {Fab B72.3 (mouse/human chimera), kappa L chain}
xvqlqqsdaelvkpgasvkisckasgytftdhaihwakqkpeqglewigyispgnddiky
nekfkgkatltadkssstaymqlnsltsedsavyfckrsyyghwgqgttltvssa
>d1bbjh2 2.1.1.2.22 (116-212) Immunoglobulin (constant domains of L and H chains) {Fab B72.3 (mouse/human chimera), kappa L chain}
stkgpsvfplapcsrstsestaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqssg
lyslssvvtvpssslgtktytcnvdhkpsntkvdkrv
>d1bbjl1 2.1.1.1.13 (1-109) Immunoglobulin (variable domains of L and H chains) {Fab B72.3 (mouse/human chimera), kappa L chain}
diqmtqspaslsvsvgetvtitcraseniysnlawyqqkqgkspqllvyaatnladgvps
rfsgsgsgtqyslkinslqsedfgsyycqhfwgtpytfgggtrleikra
>d1bbjl2 2.1.1.2.22 (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__ 1.26.1.2.2 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_ 2.45.1.1.7 Bilin-binding protein {cabbage butterfly (Pieris brassicae)}
nvyhdgacpevkpvdnfdwsnyhgkwwevakypnsvekygkcgwaeytpegksvkvsnyh
vihgkeyfiegtaypvgdskigkiyhkltyggvtkenvfnvlstdnknyiigyyckyded
kkghqdfvwvlsrskvltgeaktavenyligspvvdsqklvysdfseaackvn
>d1bbpb_ 2.45.1.1.7 Bilin-binding protein {cabbage butterfly (Pieris brassicae)}
nvyhdgacpevkpvdnfdwsnyhgkwwevakypnsvekygkcgwaeytpegksvkvsnyh
vihgkeyfiegtaypvgdskigkiyhkltyggvtkenvfnvlstdnknyiigyyckyded
kkghqdfvwvlsrskvltgeaktavenyligspvvdsqklvysdfseaackvn
>d1bbpc_ 2.45.1.1.7 Bilin-binding protein {cabbage butterfly (Pieris brassicae)}
nvyhdgacpevkpvdnfdwsnyhgkwwevakypnsvekygkcgwaeytpegksvkvsnyh
vihgkeyfiegtaypvgdskigkiyhkltyggvtkenvfnvlstdnknyiigyyckyded
kkghqdfvwvlsrskvltgeaktavenyligspvvdsqklvysdfseaackvn
>d1bbpd_ 2.45.1.1.7 Bilin-binding protein {cabbage butterfly (Pieris brassicae)}
nvyhdgacpevkpvdnfdwsnyhgkwwevakypnsvekygkcgwaeytpegksvkvsnyh
vihgkeyfiegtaypvgdskigkiyhkltyggvtkenvfnvlstdnknyiigyyckyded
kkghqdfvwvlsrskvltgeaktavenyligspvvdsqklvysdfseaackvn
>e1bbr.1e 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
svaevqpsvlqvvnlplverpvckastriritdnmfcagykpgegkrgdacegdsggpfv
mkspynnrwyqmgivswgegcdrdgkygfythvfrlkkwiqkvidrlgs
>e1bbr.1h 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
ivegqdaevglspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftvddll
vrigkhsrtryerkvekismldkiyihprynwkenldrdiallklkrpielsdyihpvcl
pdkqtaakllhagfkgrvtgwgnrretwtt
>e1bbr.1l 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1bbr.2j 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1bbr.2k 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
ivegqdaevglspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftvddll
vrigkhsrtryerkvekismldkiyihprynwkenldrdiallklkrpielsdyihpvcl
pdkqtaakllhagfkgrvtgwgnrretwttsvaevqpsvlqvvnlplverpvckastrir
itdnmfcagykpgegkrgdacegdsggpfvmkspynnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidrlgs
>e1bbr.3m 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1bbr.3n 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
ivegqdaevglspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftvddll
vrigkhsrtryerkvekismldkiyihprynwkenldrdiallklkrpielsdyihpvcl
pdkqtaakllhagfkgrvtgwgnrretwttsvaevqpsvlqvvnlplverpvckastrir
itdnmfcagykpgegkrgdacegdsggpfvmkspynnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidrlgs
>d1bbs__ 2.38.1.2.14 Chymosin (synonim: renin) {human (Homo sapiens)}
ttssviltnymdtqyygeigigtppqtfkvvfdtgssnvwvpsskcsrlytacvyhklfd
asdsssykhngteltlrystgtvsgflsqdiitvggitvtqmfgevtempalpfmlaefd
gvvgmgfieqaigrvtpifdniisqgvlkedvfsfyynrdsensqslggqivlggsdpqh
yegnfhyinliktgvwqiqmkgvsvgsstllcedgclalvdtgasyisgstssieklmea
lgakkrlfdyvvkcnegptlpdisfhlggkeytltsadyvfqesysskklctlaihamdi
ppptgptwalgatfirkfytefdrrnnrigfalar
>d1bbt1_ 2.8.1.4.2 Foot-and-mouth desease virus {foot-and-mouth disease virus (Strain bfs, 1860)}
ttsagesadpvtttvenyggetqiqrrqhtdvsfimdrfvkvtpqnqinildlmqvpsht
lvggllrastyyfsdleiavkhegdltwvpngapekaldnttnptayhkapltrlalpyt
aphrvlatvyngecrysrnavpnlrgdlqvlaqkvartlptsfnygaikatrvtellyrm
kraetycprpllaihptearhkqkivap
>d1bbt2_ 2.8.1.4.2 Foot-and-mouth desease virus {foot-and-mouth disease virus (Strain bfs, 1860)}
lledrilttrnghttsttqssvgvtygyataedfvsgpntsgletrvvqaerffkthlfd
wvtsdsfgrchllelptdhkgvygsltdsyaymrngwdvevtavgnqfnggcllvamvpe
lcsiqkrelyqltlfphqfinprtnmtahitvpfvgvnrydqykvhkpwtlvvmvvaplt
vntegapqikvyaniaptnvhvagefpske
>d1bbt3_ 2.8.1.4.2 Foot-and-mouth desease virus {foot-and-mouth disease virus (Strain bfs, 1860)}
gifpvacsdgygglvttdpktadpvygkvfnpprnqlpgrftnlldvaeacptflrfegg
vpyvttktdsdrvlaqfdmslaakhmsntflaglaqyytqysgtinlhfmftgptdakar
ymvayappgmeppktpeaaahcihaewdtglnskftfsipylsaadytytasdvaettnv
qgwvclfqithgkadgdalvvlasagkdfelrlpvdarae
>d1bc6__ 4.34.1.2.2 Ferredoxin {(Bacillus schlegelii)}
ayvitepcigtkdascvevcpvdcihegedqyyidpdvcidcgaceavcpvsaiyhedfv
peewksyiqknrdffkk
>d1bcd__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
hhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnn
ghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvh
wntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprg
llpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvd
nwrpaqplknrqikasfk
>d1bcfa_ 1.25.1.1.2 Bacterioferritin (cytochrome b1) {(Escherichia coli)}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bcfb_ 1.25.1.1.2 Bacterioferritin (cytochrome b1) {(Escherichia coli)}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bch11 1.105.1.1.1 (73-104) Mannose-binding protein A {rat (Rattus rattus)}
aievklanmeaeintlkskleltnklhafsmg
>d1bch12 4.105.1.1.5 (105-221) Mannose-binding protein A, lectin domain {rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvhivdnglwndiscqashtav
>d1bch21 1.105.1.1.1 (73-104) Mannose-binding protein A {rat (Rattus rattus)}
aievklanmeaeintlkskleltnklhafsmg
>d1bch22 4.105.1.1.5 (105-221) Mannose-binding protein A, lectin domain {rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvhivdnglwndiscqashtav
>d1bch31 1.105.1.1.1 (73-104) Mannose-binding protein A {rat (Rattus rattus)}
aievklanmeaeintlkskleltnklhafsmg
>d1bch32 4.105.1.1.5 (105-221) Mannose-binding protein A, lectin domain {rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvhivdnglwndiscqashtav
>d1bcj11 1.105.1.1.1 (73-104) Mannose-binding protein A {rat (Rattus rattus)}
aievklanmeaeintlkskleltnklhafsmg
>d1bcj12 4.105.1.1.5 (105-221) Mannose-binding protein A, lectin domain {rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktvaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvhivdnglwndiscqashtav
>d1bcj21 1.105.1.1.1 (73-104) Mannose-binding protein A {rat (Rattus rattus)}
aievklanmeaeintlkskleltnklhafsmg
>d1bcj22 4.105.1.1.5 (105-221) Mannose-binding protein A, lectin domain {rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktvaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvhivdnglwndiscqashtav
>d1bcj31 1.105.1.1.1 (73-104) Mannose-binding protein A {rat (Rattus rattus)}
aievklanmeaeintlkskleltnklhafsmg
>d1bcj32 4.105.1.1.5 (105-221) Mannose-binding protein A, lectin domain {rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktvaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvhivdnglwndiscqashtav
>d1bcma1 2.36.1.1.1 (481-560) Mu transposase, C-terminal domain {(Bacteriophage mu)}
teeqkrmlllpaeavnvsrkgeftlkvggslkgaknvyynmalmnagvkkvvvrfdpqql
hstvycytldgrficeaecl
>d1bcma2 3.47.3.3.1 (257-480) Mu transposase, core domain {(Bacteriophage mu)}
vehldamqwingdgylhnvfvrwfngdvirpktwfwqdvktrkilgwrcdvsenidsirl
sfmdvvtrygipedfhitidntrgaankwltggapnryrfkvkeddpkglfllmgakmhw
tsvvagkgwgqakpverafgvggleeyvdkhpalagaytgpnpqakpdnygdravdaelf
lktlaegvamfnartgretemcggklsfddvfereyartivrkp
>d1bcmb1 2.36.1.1.1 (481-560) Mu transposase, C-terminal domain {(Bacteriophage mu)}
teeqkrmlllpaeavnvsrkgeftlkvggslkgaknvyynmalmnagvkkvvvrfdpqql
hstvycytldgrficeaecl
>d1bcmb2 3.47.3.3.1 (258-480) Mu transposase, core domain {(Bacteriophage mu)}
ehldamqwingdgylhnvfvrwfngdvirpktwfwqdvktrkilgwrcdvsenidsirls
fmdvvtrygipedfhitidntrgaankwltggapnryrfkvkeddpkglfllmgakmhwt
svvagkgwgqakpverafgvggleeyvdkhpalagaytgpnpqakpdnygdravdaelfl
ktlaegvamfnartgretemcggklsfddvfereyartivrkp
>d1bcn__ 1.26.1.2.2 Interleukin-4 (IL-4) {human (Homo sapiens)}
eaeahkcditlqeiiktlnslteqktlcteltvtdifaaskdtteketfcraatvlrqfy
shhekdtrclgataqqfhrhkqlirflkrldrnlwglaglnscpvkeadqstlenflerl
ktimrekyskcss
>d1bco_1 2.36.1.1.1 (481-560) Mu transposase, C-terminal domain {(Bacteriophage mu)}
teeqkrmlllpaeavnvsrkgeftlkvggslkgaknvyynmalmnagvkkvvvrfdpqql
hstvycytldgrficeaecl
>d1bco_2 3.47.3.3.1 (258-480) Mu transposase, core domain {(Bacteriophage mu)}
ehldamqwingdgylhnvfvrwfngdvirpktwfwqdvktrkilgwrcdvsenidsirls
fmdvvtrygipedfhitidntrgaankwltggapnryrfkvkeddpkglfllmgakmhwt
svvagkgwgqakpverafgvggleeyvdkhpalagaytgpnpqakpdnygdravdaelfl
ktlaegvamfnartgretemcggklsfddvfereyartivrkp
>d1bcpa_ 4.103.1.1.5 Pertussis toxin, S1 subunit {(Bordetella pertussis)}
dppatvyrydsrppedvfqngftawgnndnvlehltgrscqvgssnsafvstsssrryte
vylehrmqeaveaeragrgtghfigyiyevradnnfygaassyfeyvdtygdnagrilag
alatyqseylahrrippenirrvtrvyhngitgetttteysnaryvsqqtranpnpytsr
rsvasivgtlvrmapvvgacmarqaesseamaawserageamvlvyyesiaysf
>d1bcpb1 2.29.2.1.6 (88-199) Pertussis toxin S2/S3 subunits, C-terminal domain {(Bordetella pertussis)}
imttrntgqpatdhyysnvtatrllsstnsrlcavfvrsgqpvigactspydgkywsmys
rlrkmlyliyvagisvrvhvskeeqyydyedatfetyaltgisicnpgsslc
>d1bcpb2 4.105.1.2.1 (3-87) Pertussis toxin, S2/S3 subunits, N-terminal domain {(Bordetella pertussis)}
pgivippqeqitqhgspygrcanktraltvaelrgsgdlqeylrhvtrgwsifalydgty
lggeyggvikdgtpggafdlkttfc
>d1bcpc1 2.29.2.1.6 (88-199) Pertussis toxin S2/S3 subunits, C-terminal domain {(Bordetella pertussis)}
ittiyktgqpaadhyyskvtatrllastnsrlcavfvrdgqsvigacaspyegryrdmyd
alrrllymiymsglavrvhvskeeqyydyedatfqtyaltgislcnpaasic
>d1bcpc2 4.105.1.2.1 (4-87) Pertussis toxin, S2/S3 subunits, N-terminal domain {(Bordetella pertussis)}
givippkalftqqggaygrcpngtraltvaelrgnaelqtylrqitpgwsiyglydgtyl
gqayggiikdappgagfiyretfc
>d1bcpd_ 2.29.2.1.7 Pertussis toxin S4 subunit {(Bordetella pertussis)}
dvpyvlvktnmvvtsvamkpyevtptrmlvcgiaaklgaaasspdahvpfcfgkdlkrpg
sspmevmlravfmqqrplrmflgpkqltfegkpalelirmvecsgkqdcp
>d1bcpe_ 2.29.2.1.7 Pertussis toxin S4 subunit {(Bordetella pertussis)}
dvpyvlvktnmvvtsvamkpyevtptrmlvcgiaaklgaaasspdahvpfcfgkdlkrpg
sspmevmlravfmqqrplrmflgpkqltfegkpalelirmvecsgkqdcp
>d1bcpf_ 2.29.2.1.8 Pertussis toxin S5 subunit {(Bordetella pertussis)}
lpthlyknftvqelalklkgknqefcltafmsgrslvraclsdaghehdtwfdtmlgfai
sayalksrialtvedspypgtpgdllelqicplngyce
>d1bcpg_ 4.103.1.1.5 Pertussis toxin, S1 subunit {(Bordetella pertussis)}
dppatvyrydsrppedvfqngftawgnndnvlehltgrscqvgssnsafvstsssrryte
vylehrmqeaveaeragrgtghfigyiyevradnnfygaassyfeyvdtygdnagrilag
alatyqseylahrrippenirrvtrvyhngitgetttteysnaryvsqqtranpnpytsr
rsvasivgtlvrmapvvgacmarqaesseamaawserageamvlvyyesiaysf
>d1bcph1 2.29.2.1.6 (88-199) Pertussis toxin S2/S3 subunits, C-terminal domain {(Bordetella pertussis)}
imttrntgqpatdhyysnvtatrllsstnsrlcavfvrsgqpvigactspydgkywsmys
rlrkmlyliyvagisvrvhvskeeqyydyedatfetyaltgisicnpgsslc
>d1bcph2 4.105.1.2.1 (3-87) Pertussis toxin, S2/S3 subunits, N-terminal domain {(Bordetella pertussis)}
pgivippqeqitqhgspygrcanktraltvaelrgsgdlqeylrhvtrgwsifalydgty
lggeyggvikdgtpggafdlkttfc
>d1bcpi1 2.29.2.1.6 (88-199) Pertussis toxin S2/S3 subunits, C-terminal domain {(Bordetella pertussis)}
ittiyktgqpaadhyyskvtatrllastnsrlcavfvrdgqsvigacaspyegryrdmyd
alrrllymiymsglavrvhvskeeqyydyedatfqtyaltgislcnpaasic
>d1bcpi2 4.105.1.2.1 (4-87) Pertussis toxin, S2/S3 subunits, N-terminal domain {(Bordetella pertussis)}
givippkalftqqggaygrcpngtraltvaelrgnaelqtylrqitpgwsiyglydgtyl
gqayggiikdappgagfiyretfc
>d1bcpj_ 2.29.2.1.7 Pertussis toxin S4 subunit {(Bordetella pertussis)}
dvpyvlvktnmvvtsvamkpyevtptrmlvcgiaaklgaaasspdahvpfcfgkdlkrpg
sspmevmlravfmqqrplrmflgpkqltfegkpalelirmvecsgkqdcp
>d1bcpk_ 2.29.2.1.7 Pertussis toxin S4 subunit {(Bordetella pertussis)}
dvpyvlvktnmvvtsvamkpyevtptrmlvcgiaaklgaaasspdahvpfcfgkdlkrpg
sspmevmlravfmqqrplrmflgpkqltfegkpalelirmvecsgkqdcp
>d1bcpl_ 2.29.2.1.8 Pertussis toxin S5 subunit {(Bordetella pertussis)}
lpthlyknftvqelalklkgknqefcltafmsgrslvraclsdaghehdtwfdtmlgfai
sayalksrialtvedspypgtpgdllelqicplngyce
>e1bcr.1a 3.56.1.2.1 Serine carboxypeptidase II {wheat (Triticum vulgaris)}
haadriarlpgqpavdfdmysgyitvdegagrslfyllqeapedaqpaplvlwlnggpgc
ssvaygaseelgafrvkprgaglvlneyrwnkvanvlfldspagvgfsytntssdiytsg
dnrtahdsyaflakwferfphykyrdfyiagesyaghyvpelsqlvhrsknpvinlkgfm
vgngliddyhdyvgtfefwwnhgivsddtyrrlkeaclhdsfihpspacdaatdvataeq
gnidmyslytpvcn
>e1bcr.1b 3.56.1.2.1 Serine carboxypeptidase II {wheat (Triticum vulgaris)}
sydpcterystayynrrdvqmalhanvtgamnytwatcsdtinthwhdaprsmlpiyrel
iaaglriwvfsgdtdavvpltatrysigalglptttswypwyddqevggwsqvykgltlv
svrgaghevplhrprqalvlfqyflqgkpmpg
>e1bcs.1a 3.56.1.2.1 Serine carboxypeptidase II {wheat (Triticum vulgaris)}
haadriarlpgqpavdfdmysgyitvdegagrslfyllqeapedaqpaplvlwlnggpgc
ssvaygaseelgafrvkprgaglvlneyrwnkvanvlfldspagvgfsytntssdiytsg
dnrtahdsyaflakwferfphykyrdfyiagesyaghyvpelsqlvhrsknpvinlkgfm
vgngliddyhdyvgtfefwwnhgivsddtyrrlkeaclhdsfihpspacdaatdvataeq
gnidmyslytpvcni
>e1bcs.1b 3.56.1.2.1 Serine carboxypeptidase II {wheat (Triticum vulgaris)}
sydpcterystayynrrdvqmalhanvtgamnytwatcsdtinthwhdaprsmlpiyrel
iaaglriwvfsgdtdavvpltatrysigalglptttswypwyddqevggwsqvykgltlv
svrgaghevplhrprqalvlfqyflqgkpmpgq
>d1bcx__ 2.21.1.9.1 Xylanase II {(Bacillus circulans)}
astdywqnwtdgggivnavngsggnysvnwsntgnfvvgkgwttgspfrtinynagvwap
ngngyltlygwtrsplieyyvvdswgtyrptgtykgtvksdggtydiytttrynapsidg
drttftqywsvrqskrptgsnatitftnhvnawkshgmnlgsnwayqvmatcgyqssgss
nvtvw
>d1bd6__ 4.34.1.2.2 Ferredoxin {(Bacillus schlegelii)}
ayvitepcigtkdascvevcpvdcihegedqyyidpdvcidcgaceavcpvsaiyhedfv
peewksyiqknrdffkk
>d1bdb__ 3.22.1.2.6 Cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase {(Pseudomonas sp.) 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
>d1bdha1 1.32.1.3.1 (3-58) Purine repressor (PurR), N-terminal domain {(Escherichia coli)}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslavnh
>d1bdha2 3.81.1.1.6 (59-340) Purine repressor (PurR), C-terminal domain {(Escherichia coli)}
tksigllatsseaayfaeiieavekncfqkgytlilgnawnnlekqraylsmmaqkrvdg
llvmcseypepllamleeyrhipmvvmdwgeakadftdavidnafeggymagryliergh
reigvipgplerntgagrlagfmkameeamikvpeswivqgdfepesgyramqqilsqph
rptavfcggdimamgalcaademglrvpqdvsligydnvrnaryftpalttihqpkdslg
etafnmlldrivnkreepqsievhprlierrsvadgpfrdyr
>d1bdia1 1.32.1.3.1 (3-58) Purine repressor (PurR), N-terminal domain {(Escherichia coli)}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkvnh
>d1bdia2 3.81.1.1.6 (59-340) Purine repressor (PurR), C-terminal domain {(Escherichia coli)}
tksigllatsseaayfaeiieavekncfqkgytlilgnawnnlekqraylsmmaqkrvdg
llvmcseypepllamleeyrhipmvvmdwgeakadftdavidnafeggymagryliergh
reigvipgplerntgagrlagfmkameeamikvpeswivqgdfepesgyramqqilsqph
rptavfcggdimamgalcaademglrvpqdvsligydnvrnaryftpalttihqpkdslg
etafnmlldrivnkreepqsievhprlierrsvadgpfrdyr
>d1bdma1 3.22.1.5.3 (1-154) Malate dehydrogenase {(Thermus flavus)}
kapvrvavtgaagqigysllfriaagemlgkdqpvilqlleipqamkalegvvmeledca
fpllagleatddpdvafkdadyallvgaaprkagmerrdllqvngkifteqgralaevak
kdvkvlvvgnpantnaliayknapglnprnftam
>d1bdma2 4.100.1.1.3 (155-332) Malate dehydrogenase {(Thermus flavus)}
trldhnrakaqlakktgtgvdrirrmtvwgnhssimfpdlfhaevdgrpalelvdmewye
kvfiptvaqrgaaiiqargassaasaanaaiehirdwalgtpegdwvsmavpsqgeygip
egivysfpvtakdgayrvvegleinefarkrmeitaqelldemeqvkalgli
>d1bdmb1 3.22.1.5.3 (1-154) Malate dehydrogenase {(Thermus flavus)}
kapvrvavtgaagqigysllfriaagemlgkdqpvilqlleipqamkalegvvmeledca
fpllagleatddpdvafkdadyallvgaaprkagmerrdllqvngkifteqgralaevak
kdvkvlvvgnpantnaliayknapglnprnftam
>d1bdmb2 4.100.1.1.3 (155-332) Malate dehydrogenase {(Thermus flavus)}
trldhnrakaqlakktgtgvdrirrmtvwgnhssimfpdlfhaevdgrpalelvdmewye
kvfiptvaqrgaaiiqargassaasaanaaiehirdwalgtpegdwvsmavpsqgeygip
egivysfpvtakdgayrvvegleinefarkrmeitaqelldemeqvkalgli
>d1bdo__ 2.65.1.1.1 biotinyl domain of acetyl-CoA carboxylase {(Escherichia coli)}
eisghivrspmvgtfyrtpspdakafievgqkvnvgdtlciveamkmmnqieadksgtvk
ailvesgqpvefdeplvvie
>d1bdp_1 3.47.3.4.3 (297-492) Exonuclease domain of DNA polymerase {(Bacillus stearothermophilus) newly identified strain as yet unnamed}
akmaftladrvteemladkaalvlevveenyhdapivgiavvnehgrfflrpetaladpq
fvawlgdetkkksmfdskraavalkwkgielcgvsfdlllaaylldpaqgvddvraaakm
kqyeavrpdeavygkgakravpdepvlaehlvrkaaaiwelerpfldelrrneqdrllve
leqplssilaemefag
>d1bdp_2 5.9.1.1.3 (493-876) DNA polymerase I (Klenow fragment) {(Bacillus stearothermophilus) newly identified strain as yet unnamed}
vkvdtkrleqmgkelreklgtveqriyelagqefninspkqlgvilfeklqlpvlkktkt
gystsadvleklapyheivenilhyrqlgklqstyiegllkvvrpdtkkvhtifnqaltq
tgrlsstepnlqnipirleegrkirqafvpsesdwlifaadysqielrvlahiaeddnlm
eafrrdldihtktamdifqvsedevtpnmrrqakavnfgivygisdyglaqnlnisrkea
aefieryfesfpgvkrymenivqeakqkgyvttllhrrrylpditsrnfnvrsfaermam
ntpiqgsaadiikkamidlnarlkeerlqarlllqvhdelileapkeemerlcrlvpevm
eqavtlrvplkvdyhygstwydak
>d1bds__ 7.8.1.1.3 BDs-I defensin {sea anemone (Anemonia sulcata)}
aapcfcsgkpgrgdlwilrgtcpggygytsncykwpniccyph
>d1bdu__ 4.67.1.1.1 Thymidylate synthase {(Escherichia coli)}
mkqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihell
wflqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlk
ndpdsrriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfnias
yallvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesif
dyrfedfeiegydphpgikapvai
>d1beba_ 2.45.1.1.6 beta-Lactoglobulin {Bovine (Bos taurus)}
qtmkgldiqkvagtwyslamaasdislldaqsaplrvyveelkptpegdleillqkweng
ecaqkkiiaektkipavfkidalnenkvlvldtdykkyllfcmensaepeqslvcqclvr
tpevddealekfdkalkalpmhirlsfnptqleeqc
>d1bebb_ 2.45.1.1.6 beta-Lactoglobulin {Bovine (Bos taurus)}
qtmkgldiqkvagtwyslamaasdislldaqsaplrvyveelkptpegdleillqkweng
ecaqkkiiaektkipavfkidalnenkvlvldtdykkyllfcmensaepeqslvcqclvr
tpevddealekfdkalkalpmhirlsfnptqleeqc
>d1bec_1 2.1.1.1.121 (3-117) T-cell antigen receptor {Mouse (Mus musculus), beta-chain}
avtqsprnkvavtggkvtlscqqtnnhnnmywyrqdtghglrlihysygagstekgdipd
gykasrpsqeqfslilelatpsqtsvyfcasgggrgsyaeqffgpgtrltvle
>d1bec_2 2.1.1.2.111 (118-246) T-cell antigen receptor {Mouse (Mus musculus), beta-chain}
dlrqvtppkvslfepskaeiankqkatlvclargffpdhvelswwvngkevhsgvstdpq
aykesnysyclssrlrvsatfwhnprnhfrcqvqfhglseedkwpegspkpvtqnisaea
wgrad
>d1bed_1 1.42.1.1.2 (63-126) Disulphide-bond formation facilitator (DSBA), insertion domain {(Vibrio cholerae)}
gnmgqamskayatmialevedkmvpvmfnrihtlrkppkdeqelrqifldegidaakfda
ayng
>d1bed_2 3.38.1.3.2 (1-62,127-181) Disulphide-bond formation facilitator (DSBA) {(Vibrio cholerae)}
aqfkegehyqvlktpassspvvseffsfycphcntfepiiaqlkqqlpegakfqknhvsf
mgXfavdsmvrrfdkqfqdsgltgvpavvvnnrylvqgqsvksldeyfdlvnylltlk
>d1beg__ 1.104.1.1.1 beta-cryptogein {(Phytophthora cryptogea)}
tactatqqtaayktlvsilsdasfnqcstdsgysmltakalpttaqyklmcastacntmi
kkivtlnppncdltvptsglvlnvysyangfsnkcssl
>d1bel__ 4.4.1.1.1 Ribonuclease A (also ribonuclease B, S) {bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>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__ 1.104.1.1.1 beta-cryptogein {(Phytophthora cryptogea)}
tactatqqtaayktlvsilsdasfnqcstdsgysmltakalpttaqyklmcastacntmi
kkivtlnppncdltvptsglvlnvysyangfsnkcssl
>d1bera1 1.4.3.4.1 (138-207) Catabolite gene activator protein (CAP), C-terminal domain {(Escherichia coli)}
dvtgriaqtllnlakqpdamthpdgmqikitrqeigqivgcsretvgrilkmledqnlis
ahgktivvyg
>d1bera2 2.64.4.1.1 (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 2.64.4.1.1 (9-137) Catabolite gene activator protein, N-terminal domain, {(Escherichia coli)}
ptlewflshchihkypskstlihqgekaetlyyivkgsvavlikdeegkemilsylnqgd
figelglfeegqersawvraktacevaeisykkfrqliqvnpdilmrlsaqmarrlqvts
ekvgnlafl
>d1bet__ 7.16.1.3.3 beta-Nerve growth factor {mouse (Mus musculus)}
gefsvcdsvsvwvgdkttatdikgkevtvlaevninnsvfrqyffetkcrasnpvesgcr
gidskhwnsycttthtfvkalttdekqaawrfiridtacvcvlsrka
>d1bfb__ 2.31.1.1.1 Basic FGF {human (Homo sapiens)}
pkrlycknggfflrihpdgrvdgvreksdphiklqlqaeergvvsikgvsanrylamked
grllasksvtdecffferlesnnyntyrsrkytswyvalkrtgqyklgsktgpgqkailf
lpms
>d1bfc__ 2.31.1.1.1 Basic FGF {human (Homo sapiens)}
pkrlycknggfflrihpdgrvdgvreksdphiklqlqaeergvvsikgvsanrylamked
grllasksvtdecffferlesnnyntyrsrkytswyvalkrtgqyklgsktgpgqkailf
lpms
>d1bfd_1 3.24.1.3.4 (182-341) Benzoylformate decarboxylase {(Pseudomonas putida)}
svrlndqdldilvkalnsasnpaivlgpdvdaananadcvmlaerlkapvwvapsaprcp
fptrhpcfrglmpagiaaisqlleghdvvlvigapvfryhqydpgqylkpgtrlisvtcd
pleaarapmgdaivadigamasalanlveessrqlptaap
>d1bfd_2 3.28.1.1.4 (2-181) Benzoylformate decarboxylase {(Pseudomonas putida)}
asvhgttyellrrqgidtvfgnpgsnelpflkdfpedfryilalqeacvvgiadgyaqas
rkpafinlhsaagtgnamgalsnawnshsplivtagqqtramigvealltnvdaanlprp
lvkwsyepasaaevphamsraihmasmapqgpvylsvpyddwdkdadpqshhlfdrhvss
>d1bfd_3 3.28.1.1.4 (342-524) Benzoylformate decarboxylase {(Pseudomonas putida)}
epakvdqdagrlhpetvfdtlndmapenaiylneststtaqmwqrlnmrnpgsyyfcaag
glgfalpaaigvqlaeperqviavigdgsanysisalwtaaqyniptifvimnngtygal
rwfagvleaenvpgldvpgidfralakgygvqalkadnleqlkgslqealsakgpvliev
stv
>d1bff__ 2.31.1.1.1 Basic FGF {human (Homo sapiens)}
kdpkrlycknggfflrihpdgrvdgvreksdphiklqlqaeergvvsikgvcanrylamk
edgrllaskcvtdecffferlesnnyntyrsrkytswyvalkrtgqyklgsktgpgqkai
lflpmsaks
>d1bfg__ 2.31.1.1.1 Basic FGF {human (Homo sapiens)}
dpkrlycknggfflrihpdgrvdgvreksdphiklqlqaeergvvsikgvsanrylamke
dgrllasksvtdecffferlesnnyntyrsrkytswyvalkrtgqyklgsktgpgqkail
flpmsa
>d1bfi__ 4.53.1.1.11 Phosphatidylinositol 3-kinase, p85-alpha subunit {human (Homo sapiens)}
edlphhdektwnvgssnrnkaenllrgkrdgtflvresskqgcyacsvvvdgevkhcvin
ktatgygfaepynlysslkelvlhyqhtslvqhndslnvtlaypvyaqqrr
>d1bfj__ 4.53.1.1.11 Phosphatidylinositol 3-kinase, p85-alpha subunit {human (Homo sapiens)}
edlphhdektwnvgssnrnkaenllrgkrdgtflvresskqgcyacsvvvdgevkhcvin
ktatgygfaepynlysslkelvlhyqhtslvqhndslnvtlaypvyaqqrr
>d1bfma_ 1.22.1.2.1 Histone B {(Methanothermus fervidus)}
melpiapigriikdagaervsddaritlakileemgrdiaseaiklarhagrktikaedi
elavrrfkk
>d1bfmb_ 1.22.1.2.1 Histone B {(Methanothermus fervidus)}
melpiapigriikdagaervsddaritlakileemgrdiaseaiklarhagrktikaedi
elavrrfkk
>d1bfp__ 4.17.1.1.1 Green fluorescent protein {Jellyfish (Aequorea victoria)}
mskgeelftgvvpilveldgdvnghkfsvsgegegdatygkltlkficttgklpvpwptl
vttfxvqcfsrypdhmkrhdffksampegyvqertiffkddgnyktraevkfegdtlvnr
ielkgidfkedgnilghkleynfnshnvyimadkqkngikvnfkirhniedgsvqladhy
qqntpigdgpvllpdnhylstqsalskdpnekrdhmvllefvtaagi
>d1bfra_ 1.25.1.1.2 Bacterioferritin (cytochrome b1) {(Escherichia coli)}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrb_ 1.25.1.1.2 Bacterioferritin (cytochrome b1) {(Escherichia coli)}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrc_ 1.25.1.1.2 Bacterioferritin (cytochrome b1) {(Escherichia coli)}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrd_ 1.25.1.1.2 Bacterioferritin (cytochrome b1) {(Escherichia coli)}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfre_ 1.25.1.1.2 Bacterioferritin (cytochrome b1) {(Escherichia coli)}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrf_ 1.25.1.1.2 Bacterioferritin (cytochrome b1) {(Escherichia coli)}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrg_ 1.25.1.1.2 Bacterioferritin (cytochrome b1) {(Escherichia coli)}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrh_ 1.25.1.1.2 Bacterioferritin (cytochrome b1) {(Escherichia coli)}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfri_ 1.25.1.1.2 Bacterioferritin (cytochrome b1) {(Escherichia coli)}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrj_ 1.25.1.1.2 Bacterioferritin (cytochrome b1) {(Escherichia coli)}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrk_ 1.25.1.1.2 Bacterioferritin (cytochrome b1) {(Escherichia coli)}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrl_ 1.25.1.1.2 Bacterioferritin (cytochrome b1) {(Escherichia coli)}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrm_ 1.25.1.1.2 Bacterioferritin (cytochrome b1) {(Escherichia coli)}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrn_ 1.25.1.1.2 Bacterioferritin (cytochrome b1) {(Escherichia coli)}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfro_ 1.25.1.1.2 Bacterioferritin (cytochrome b1) {(Escherichia coli)}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrp_ 1.25.1.1.2 Bacterioferritin (cytochrome b1) {(Escherichia coli)}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrq_ 1.25.1.1.2 Bacterioferritin (cytochrome b1) {(Escherichia coli)}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrr_ 1.25.1.1.2 Bacterioferritin (cytochrome b1) {(Escherichia coli)}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrs_ 1.25.1.1.2 Bacterioferritin (cytochrome b1) {(Escherichia coli)}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrt_ 1.25.1.1.2 Bacterioferritin (cytochrome b1) {(Escherichia coli)}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfru_ 1.25.1.1.2 Bacterioferritin (cytochrome b1) {(Escherichia coli)}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrv_ 1.25.1.1.2 Bacterioferritin (cytochrome b1) {(Escherichia coli)}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrw_ 1.25.1.1.2 Bacterioferritin (cytochrome b1) {(Escherichia coli)}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrx_ 1.25.1.1.2 Bacterioferritin (cytochrome b1) {(Escherichia coli)}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfs__ 2.1.1.5.19 p50 subunit of NF-kappa B transcription factor, C-terminal domain {mouse (Mus musculus)}
asnlkivrmdrtagcvtggeeiyllcdkvqkddiqirfyeeeenggvwegfgdfsptdvh
rqfaivfktpkykdvnitkpasvfvqlrrksdletsepkpflyype
>d1bfta_ 2.1.1.5.19 p50 subunit of NF-kappa B transcription factor, C-terminal domain {mouse (Mus musculus)}
taelkicrvnrnsgsclggdeifllcdkvqkedievyftgpgweargsfsqadvhrqvai
vfrtppyadpslqapvrvsmqlrrpsdrelsepmefqylpd
>d1bftb_ 2.1.1.5.19 p50 subunit of NF-kappa B transcription factor, C-terminal domain {mouse (Mus musculus)}
taelkicrvnrnsgsclggdeifllcdkvqkedievyftgpgweargsfsqadvhrqvai
vfrtppyadpslqapvrvsmqlrrpsdrelsepmefqylpd
>d1bfvh_ 2.1.1.1.84 Immunoglobulin (variable domains of L and H chains) {Fv 4155 (mouse), kappa L chain}
qvqlqesggglvnlggsmtlscvasgftfntyymswvrqtpektlelvaainsdgepiyy
pdtlkgrvtisrdnakktlylqmsslnfedtalyycarlnyavygmdywgqgttvtvss
>d1bfvl_ 2.1.1.1.84 Immunoglobulin (variable domains of L and H chains) {Fv 4155 (mouse), kappa L chain}
dieltqsppslpvslgdqvsiscrssqslvsnnrrnylhwylqkpgqspklviykvsnrf
sgvpdrfsgsgsgtdftlkisrvaaedlglyfcsqsshvpltfgsgtkleikr
>d1bgaa_ 3.1.1.4.4 Beta-glucosidase A {(Bacillus polymyxa)}
tifqfpqdfmwgtataayqiegayqedgrglsiwdtfahtpgkvfngdngnvacdsyhry
eedirlmkelgirtyrfsvswprifpngdgevnqegldyyhrvvdllndngiepfctlyh
wdlpqalqdaggwgnrrtiqafvqfaetmfrefhgkiqhwltfnepwciaflsnmlgvha
pgltnlqtaidvghhllvahglsvrrfrelgtsgqigiapnvswavpystseedkaacar
tislhsdwflqpiyqgsypqflvdwfaeqgatvpiqdgdmdiigepidmiginyysmsvn
rfnpeagflqseeinmglpvtdigwpvesrglyevlhylqkygnidiyitengacindev
vngkvqddrrisymqqhlvqvhrtihdglhvkgymawslldnfewaegynmrfgmihvdf
rtqvrtpkesyywyrnvvsnnwletrr
>d1bgab_ 3.1.1.4.4 Beta-glucosidase A {(Bacillus polymyxa)}
tifqfpqdfmwgtataayqiegayqedgrglsiwdtfahtpgkvfngdngnvacdsyhry
eedirlmkelgirtyrfsvswprifpngdgevnqegldyyhrvvdllndngiepfctlyh
wdlpqalqdaggwgnrrtiqafvqfaetmfrefhgkiqhwltfnepwciaflsnmlgvha
pgltnlqtaidvghhllvahglsvrrfrelgtsgqigiapnvswavpystseedkaacar
tislhsdwflqpiyqgsypqflvdwfaeqgatvpiqdgdmdiigepidmiginyysmsvn
rfnpeagflqseeinmglpvtdigwpvesrglyevlhylqkygnidiyitengacindev
vngkvqddrrisymqqhlvqvhrtihdglhvkgymawslldnfewaegynmrfgmihvdf
rtqvrtpkesyywyrnvvsnnwletrr
>d1bgac_ 3.1.1.4.4 Beta-glucosidase A {(Bacillus polymyxa)}
tifqfpqdfmwgtataayqiegayqedgrglsiwdtfahtpgkvfngdngnvacdsyhry
eedirlmkelgirtyrfsvswprifpngdgevnqegldyyhrvvdllndngiepfctlyh
wdlpqalqdaggwgnrrtiqafvqfaetmfrefhgkiqhwltfnepwciaflsnmlgvha
pgltnlqtaidvghhllvahglsvrrfrelgtsgqigiapnvswavpystseedkaacar
tislhsdwflqpiyqgsypqflvdwfaeqgatvpiqdgdmdiigepidmiginyysmsvn
rfnpeagflqseeinmglpvtdigwpvesrglyevlhylqkygnidiyitengacindev
vngkvqddrrisymqqhlvqvhrtihdglhvkgymawslldnfewaegynmrfgmihvdf
rtqvrtpkesyywyrnvvsnnwletrr
>d1bgad_ 3.1.1.4.4 Beta-glucosidase A {(Bacillus polymyxa)}
tifqfpqdfmwgtataayqiegayqedgrglsiwdtfahtpgkvfngdngnvacdsyhry
eedirlmkelgirtyrfsvswprifpngdgevnqegldyyhrvvdllndngiepfctlyh
wdlpqalqdaggwgnrrtiqafvqfaetmfrefhgkiqhwltfnepwciaflsnmlgvha
pgltnlqtaidvghhllvahglsvrrfrelgtsgqigiapnvswavpystseedkaacar
tislhsdwflqpiyqgsypqflvdwfaeqgatvpiqdgdmdiigepidmiginyysmsvn
rfnpeagflqseeinmglpvtdigwpvesrglyevlhylqkygnidiyitengacindev
vngkvqddrrisymqqhlvqvhrtihdglhvkgymawslldnfewaegynmrfgmihvdf
rtqvrtpkesyywyrnvvsnnwletrr
>d1bgc__ 1.26.1.1.2 Granulocyte-colony stimulating factor (G-CSF) {Bovine (Bos taurus)}
slpqsfllkcleqvrkiqadgaelqerlcaahklchpeelmllrhslgipqaplsscssq
slqlrgclnqlhgglflyqgllqalagispelaptldtlqldvtdfatniwlqmedlgaa
pavqptqgamptftsafqrraggvlvasqlhrflelayrglryla
>d1bgd__ 1.26.1.1.3 Granulocyte-colony stimulating factor (G-CSF) {canine (Canis familiaris)}
lpqsfllkcleqmrkvqadgtalqetlcathqlchpeelvllghalgipqpplsscssqa
lqlmgclrqlhsglflyqgllqalagispelaptldtlqldttdfainiwqqmedlgmap
avpptqgtmpaftsafqrraggvlvasnlqsflelayralrhfa
>d1bgea_ 1.26.1.1.3 Granulocyte-colony stimulating factor (G-CSF) {canine (Canis familiaris)}
plpqsfllkcleqmrkvqadgtalqetlcathqlchpeelvllghalgipqpplsscssq
alqlmgclrqlhsglflyqgllqalagispelaptldtlqldttdfainiwqqmedlgma
pavpptqgtmpaftsafqrraggvlvasnlqsflelayralrhfak
>d1bgeb_ 1.26.1.1.3 Granulocyte-colony stimulating factor (G-CSF) {canine (Canis familiaris)}
plpqsfllkcleqmrkvqadgtalqetlcathqlchpeelvllghalgipqpplsscssq
alqlmgclrqlhsglflyqgllqalagispelaptldtlqldttdfainiwqqmedlgma
pavpptqgtmpaftsafqrraggvlvasnlqsflelayralrhfa
>d1bgga_ 3.1.1.4.4 Beta-glucosidase A {(Bacillus polymyxa)}
tifqfpqdfmwgtataayqiegayqedgrglsiwdtfahtpgkvfngdngnvacdsyhry
eedirlmkelgirtyrfsvswprifpngdgevnqegldyyhrvvdllndngiepfctlyh
wdlpqalqdaggwgnrrtiqafvqfaetmfrefhgkiqhwltfnepwciaflsnmlgvha
pgltnlqtaidvghhllvahglsvrrfrelgtsgqigiapnvswavpystseedkaacar
tislhsdwflqpiyqgsypqflvdwfaeqgatvpiqdgdmdiigepidmiginyysmsvn
rfnpeagflqseeinmglpvtdigwpvesrglyevlhylqkygnidiyitengacindev
vngkvqddrrisymqqhlvqvhrtihdglhvkgymawslldnfewaegynmrfgmihvdf
rtqvrtpkesyywyrnvvsnnwletrr
>d1bggb_ 3.1.1.4.4 Beta-glucosidase A {(Bacillus polymyxa)}
tifqfpqdfmwgtataayqiegayqedgrglsiwdtfahtpgkvfngdngnvacdsyhry
eedirlmkelgirtyrfsvswprifpngdgevnqegldyyhrvvdllndngiepfctlyh
wdlpqalqdaggwgnrrtiqafvqfaetmfrefhgkiqhwltfnepwciaflsnmlgvha
pgltnlqtaidvghhllvahglsvrrfrelgtsgqigiapnvswavpystseedkaacar
tislhsdwflqpiyqgsypqflvdwfaeqgatvpiqdgdmdiigepidmiginyysmsvn
rfnpeagflqseeinmglpvtdigwpvesrglyevlhylqkygnidiyitengacindev
vngkvqddrrisymqqhlvqvhrtihdglhvkgymawslldnfewaegynmrfgmihvdf
rtqvrtpkesyywyrnvvsnnwletrr
>d1bggc_ 3.1.1.4.4 Beta-glucosidase A {(Bacillus polymyxa)}
tifqfpqdfmwgtataayqiegayqedgrglsiwdtfahtpgkvfngdngnvacdsyhry
eedirlmkelgirtyrfsvswprifpngdgevnqegldyyhrvvdllndngiepfctlyh
wdlpqalqdaggwgnrrtiqafvqfaetmfrefhgkiqhwltfnepwciaflsnmlgvha
pgltnlqtaidvghhllvahglsvrrfrelgtsgqigiapnvswavpystseedkaacar
tislhsdwflqpiyqgsypqflvdwfaeqgatvpiqdgdmdiigepidmiginyysmsvn
rfnpeagflqseeinmglpvtdigwpvesrglyevlhylqkygnidiyitengacindev
vngkvqddrrisymqqhlvqvhrtihdglhvkgymawslldnfewaegynmrfgmihvdf
rtqvrtpkesyywyrnvvsnnwletrr
>d1bggd_ 3.1.1.4.4 Beta-glucosidase A {(Bacillus polymyxa)}
tifqfpqdfmwgtataayqiegayqedgrglsiwdtfahtpgkvfngdngnvacdsyhry
eedirlmkelgirtyrfsvswprifpngdgevnqegldyyhrvvdllndngiepfctlyh
wdlpqalqdaggwgnrrtiqafvqfaetmfrefhgkiqhwltfnepwciaflsnmlgvha
pgltnlqtaidvghhllvahglsvrrfrelgtsgqigiapnvswavpystseedkaacar
tislhsdwflqpiyqgsypqflvdwfaeqgatvpiqdgdmdiigepidmiginyysmsvn
rfnpeagflqseeinmglpvtdigwpvesrglyevlhylqkygnidiyitengacindev
vngkvqddrrisymqqhlvqvhrtihdglhvkgymawslldnfewaegynmrfgmihvdf
rtqvrtpkesyywyrnvvsnnwletrr
>d1bgk__ 7.18.1.1.1 Sea anemone toxin k {sea anemone (Bunodosoma granulifera), BGK}
vcrdwfketacrhakslgncrtsqkyrancaktcelc
>d1bgla1 2.1.3.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgla2 2.1.3.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgla3 2.13.1.3.1 (3-219) beta-Galactosidase {(Escherichia coli)}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgla4 2.22.1.1.1 (731-1023) beta-Galactosidase, domain 5 {(Escherichia coli)}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgla5 3.1.1.3.8 (334-625) beta-Galactosidase, domain 3 {(Escherichia coli)}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bglb1 2.1.3.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bglb2 2.1.3.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bglb3 2.13.1.3.1 (3-219) beta-Galactosidase {(Escherichia coli)}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bglb4 2.22.1.1.1 (731-1023) beta-Galactosidase, domain 5 {(Escherichia coli)}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bglb5 3.1.1.3.8 (443-625) beta-Galactosidase, domain 3 {(Escherichia coli)}
mvqrdrnhpsviiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpm
yarvdedqpfpavpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprl
qggfvwdwvdqslikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakh
qqq
>d1bglc1 2.1.3.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bglc2 2.1.3.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bglc3 2.13.1.3.1 (3-219) beta-Galactosidase {(Escherichia coli)}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bglc4 2.22.1.1.1 (731-1023) beta-Galactosidase, domain 5 {(Escherichia coli)}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bglc5 3.1.1.3.8 (334-625) beta-Galactosidase, domain 3 {(Escherichia coli)}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgld1 2.1.3.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgld2 2.1.3.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgld3 2.13.1.3.1 (3-219) beta-Galactosidase {(Escherichia coli)}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgld4 2.22.1.1.1 (731-1023) beta-Galactosidase, domain 5 {(Escherichia coli)}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgld5 3.1.1.3.8 (334-625) beta-Galactosidase, domain 3 {(Escherichia coli)}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgle1 2.1.3.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgle2 2.1.3.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgle3 2.13.1.3.1 (3-219) beta-Galactosidase {(Escherichia coli)}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgle4 2.22.1.1.1 (731-1023) beta-Galactosidase, domain 5 {(Escherichia coli)}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgle5 3.1.1.3.8 (334-625) beta-Galactosidase, domain 3 {(Escherichia coli)}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bglf1 2.1.3.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bglf2 2.1.3.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bglf3 2.13.1.3.1 (3-219) beta-Galactosidase {(Escherichia coli)}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bglf4 2.22.1.1.1 (731-1023) beta-Galactosidase, domain 5 {(Escherichia coli)}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bglf5 3.1.1.3.8 (443-625) beta-Galactosidase, domain 3 {(Escherichia coli)}
mvqrdrnhpsviiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpm
yarvdedqpfpavpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprl
qggfvwdwvdqslikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakh
qqq
>d1bglg1 2.1.3.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bglg2 2.1.3.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bglg3 2.13.1.3.1 (3-219) beta-Galactosidase {(Escherichia coli)}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bglg4 2.22.1.1.1 (731-1023) beta-Galactosidase, domain 5 {(Escherichia coli)}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bglg5 3.1.1.3.8 (334-625) beta-Galactosidase, domain 3 {(Escherichia coli)}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bglh1 2.1.3.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bglh2 2.1.3.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bglh3 2.13.1.3.1 (3-219) beta-Galactosidase {(Escherichia coli)}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bglh4 2.22.1.1.1 (731-1023) beta-Galactosidase, domain 5 {(Escherichia coli)}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bglh5 3.1.1.3.8 (334-625) beta-Galactosidase, domain 3 {(Escherichia coli)}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgmi1 2.1.3.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgmi2 2.1.3.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgmi3 2.13.1.3.1 (3-219) beta-Galactosidase {(Escherichia coli)}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgmi4 2.22.1.1.1 (731-1023) beta-Galactosidase, domain 5 {(Escherichia coli)}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgmi5 3.1.1.3.8 (334-625) beta-Galactosidase, domain 3 {(Escherichia coli)}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgmj1 2.1.3.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgmj2 2.1.3.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgmj3 2.13.1.3.1 (3-219) beta-Galactosidase {(Escherichia coli)}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgmj4 2.22.1.1.1 (731-1023) beta-Galactosidase, domain 5 {(Escherichia coli)}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgmj5 3.1.1.3.8 (443-625) beta-Galactosidase, domain 3 {(Escherichia coli)}
mvqrdrnhpsviiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpm
yarvdedqpfpavpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprl
qggfvwdwvdqslikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakh
qqq
>d1bgmk1 2.1.3.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgmk2 2.1.3.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgmk3 2.13.1.3.1 (3-219) beta-Galactosidase {(Escherichia coli)}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgmk4 2.22.1.1.1 (731-1023) beta-Galactosidase, domain 5 {(Escherichia coli)}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgmk5 3.1.1.3.8 (334-625) beta-Galactosidase, domain 3 {(Escherichia coli)}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgml1 2.1.3.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgml2 2.1.3.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgml3 2.13.1.3.1 (3-219) beta-Galactosidase {(Escherichia coli)}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgml4 2.22.1.1.1 (731-1023) beta-Galactosidase, domain 5 {(Escherichia coli)}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgml5 3.1.1.3.8 (334-625) beta-Galactosidase, domain 3 {(Escherichia coli)}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgmm1 2.1.3.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgmm2 2.1.3.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgmm3 2.13.1.3.1 (3-219) beta-Galactosidase {(Escherichia coli)}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgmm4 2.22.1.1.1 (731-1023) beta-Galactosidase, domain 5 {(Escherichia coli)}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgmm5 3.1.1.3.8 (334-625) beta-Galactosidase, domain 3 {(Escherichia coli)}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgmn1 2.1.3.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgmn2 2.1.3.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgmn3 2.13.1.3.1 (3-219) beta-Galactosidase {(Escherichia coli)}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgmn4 2.22.1.1.1 (731-1023) beta-Galactosidase, domain 5 {(Escherichia coli)}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgmn5 3.1.1.3.8 (443-625) beta-Galactosidase, domain 3 {(Escherichia coli)}
mvqrdrnhpsviiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpm
yarvdedqpfpavpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprl
qggfvwdwvdqslikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakh
qqq
>d1bgmo1 2.1.3.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgmo2 2.1.3.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgmo3 2.13.1.3.1 (3-219) beta-Galactosidase {(Escherichia coli)}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgmo4 2.22.1.1.1 (731-1023) beta-Galactosidase, domain 5 {(Escherichia coli)}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgmo5 3.1.1.3.8 (334-625) beta-Galactosidase, domain 3 {(Escherichia coli)}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgmp1 2.1.3.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgmp2 2.1.3.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {(Escherichia coli)}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgmp3 2.13.1.3.1 (3-219) beta-Galactosidase {(Escherichia coli)}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgmp4 2.22.1.1.1 (731-1023) beta-Galactosidase, domain 5 {(Escherichia coli)}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgmp5 3.1.1.3.8 (334-625) beta-Galactosidase, domain 3 {(Escherichia coli)}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgp__ 1.72.1.1.8 Peroxidase 1 {Barley (Hordeum vulgare) grain}
aeppvapglsfdfywqtcpraesivrefvqeavrkdiglaagllrlhfhdcfvqgcdasv
lldgsatgpgeqqappnltlrpsafkavndirdrlerecrgavvscsdilalaardsvvv
sggpdyrvplgrrdsrsfastqdvlsdlpgpssnvqsllallgrlgldatdlvtisgght
iglahcssfedrlfprpdptisptflsrlkrtcpakgtdrrtvldvrtpnvfdnkyyidl
vnreglfvsdqdlftnaitrpiverfaqsqqdffeqfgvsigkmgqmrvrtsdqgevrrn
csvrnpgpg
>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_ 3.6.1.1.1 Barstar (barnase inhibitor) {(Bacillus amyloliquefaciens)}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdaltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegaditiils
>d1bgsf_ 3.6.1.1.1 Barstar (barnase inhibitor) {(Bacillus amyloliquefaciens)}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdaltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegaditiils
>d1bgsg_ 3.6.1.1.1 Barstar (barnase inhibitor) {(Bacillus amyloliquefaciens)}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdaltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegaditiils
>d1bgt__ 3.76.1.1.1 beta-Glucosyltransferase (DNA-modifying) {Bacteriophage T4}
mkiaiinmgnnvinfktvpssetiylfkvisemglnvdiislkngvytksfdevdvndyd
rlivvnssinffggkpnlailsaqkfmakykskiyylftdirlpfsqswpnvknrpwayl
yteeellikspikvisqginldiakaahkkvdnviefeyfpieqykihmndfqlskptkk
tldviyggsfrsgqreskmveflfdtglnieffgnarekqfknpkypwtkapvftgkipm
nmvseknsqaiaaliigdknyndnfitlrvwetmasdavmlideefdtkhriindarfyv
nnraelidrvnelkhsdvlrkemlsiqhdilnktrakkaewqdafkkaidl
>d1bgu__ 3.76.1.1.1 beta-Glucosyltransferase (DNA-modifying) {Bacteriophage T4}
mkiaiinmgnnvinfktvpssetiylfkvisemglnvdiislkngvytksfdevdvndyd
rlivvnssinffggkpnlailsaqkfmakykskiyylftdirlpfsqswpnvknrpwayl
yteeellikspikvisqginldiakaahkkvdnviefeyfpieqykihmndfqlskptkk
tldviyggsfrsgqreskmveflfdtglnieffgnarekqfknpkypwtkapvftgkipm
nmvseknsqaiaaliigdknyndnfitlrvwetmasdavmlideefdtkhriindarfyv
nnraelidrvnelkhsdvlrkemlsiqhdilnktrakkaewqdafkkaidl
>d1bgw__ 5.13.1.1.1 DNA topoisomerase II, the C-terminal fragment (residues 410-1202) {(Saccharomyces cerevisiae)}
rksritnypkledankagtkegykctlvltegdsalslavaglavvgrdyygcyplrgkm
lnvreasadqilknaeiqaikkimglqhrkkyedtkslryghlmimtdqdhdgshikgli
inflessflglldiqgfllefitpiikvsitkptkntiafynmpdyekwreeeshkftwk
qkyykglgtslaqevreyfsnldrhlkifhslqgndkdyidlafskkkaddrkewlrqye
pgtvldptlkeipisdfinkelilfsladnirsipnvldgfkpgqrkvlygcfkknlkse
lkvaqlapyvsectayhhgeqslaqtiiglaqnfvgsnniylllpngafgtratggkdaa
aaryiytelnkltrkifhpaddplykyiqedektvepewylpilpmilvngaegigtgws
tyippfnpleiiknirhlmndeeleqmhpwfrgwtgtieeieplryrmygrieqigdnvl
eitelpartwtstikeylllglsgndkikpwikdmeeqhddnikfiitlspeemaktrki
gfyerfklispislmnmvafdphgkikkynsvneilsefyyvrleyyqkrkdhmserlqw
evekysfqvkfikmiiekeltvtnkprnaiiqelenlgfprfnkegkpyygspndeiaeq
indvkgatsdeedeesshedtenvingpeelygtyeyllgmriwsltkeryqkllkqkqe
ketelenllklsakdiwntdlkafevgyqeflqrdaear
>d1bhga1 2.1.3.1.2 (226-328) beta-Glucuronidase {human (Homo sapiens)}
tyidditvttsveqdsglvnyqisvkgsnlfklevrlldaenkvvangtgtqgqlkvpgv
slwwpylmherpaylyslevqltaqtslgpvsdfytlpvgirt
>d1bhga2 2.13.1.3.2 (22-225) beta-Glucuronidase {human (Homo sapiens)}
glqggmlypqespsreckeldglwsfradfsdnrrrgfeeqwyrrplwesgptvdmpvps
sfndisqdwrlrhfvgwvwyerevilperwtqdlrtrvvlrigsahsyaivwvngvdtle
heggylpfeadisnlvqvgplpsrlritiainntltpttlppgtiqyltdtskypkgyfv
qntyfdffnyaglqrsvllyttpt
>d1bhga3 3.1.1.3.9 (329-632) beta-Glucuronidase, domain 3 {human (Homo sapiens)}
vavtksqflingkpfyfhgvnkhedadirgkgfdwpllvkdfnllrwlganafrtshypy
aeevmqmcdrygivvidecpgvglalpqffnnvslhhhmqvmeevvrrdknhpavvmwsv
anepashlesagyylkmviahtksldpsrpvtfvsnsnyaadkgapyvdviclnsyyswy
hdyghleliqlqlatqfenwykkyqkpiiqseygaetiagfhqdpplmfteeyqkslleq
yhlgldqkrrkyvvgeliwnfadfmteqsptrvlgnkkgiftrqrqpksaafllrerywk
iane
>d1bhgb1 2.1.3.1.2 (226-328) beta-Glucuronidase {human (Homo sapiens)}
tyidditvttsveqdsglvnyqisvkgsnlfklevrlldaenkvvangtgtqgqlkvpgv
slwwpylmherpaylyslevqltaqtslgpvsdfytlpvgirt
>d1bhgb2 2.13.1.3.2 (22-225) beta-Glucuronidase {human (Homo sapiens)}
glqggmlypqespsreckeldglwsfradfsdnrrrgfeeqwyrrplwesgptvdmpvps
sfndisqdwrlrhfvgwvwyerevilperwtqdlrtrvvlrigsahsyaivwvngvdtle
heggylpfeadisnlvqvgplpsrlritiainntltpttlppgtiqyltdtskypkgyfv
qntyfdffnyaglqrsvllyttpt
>d1bhgb3 3.1.1.3.9 (329-632) beta-Glucuronidase, domain 3 {human (Homo sapiens)}
vavtksqflingkpfyfhgvnkhedadirgkgfdwpllvkdfnllrwlganafrtshypy
aeevmqmcdrygivvidecpgvglalpqffnnvslhhhmqvmeevvrrdknhpavvmwsv
anepashlesagyylkmviahtksldpsrpvtfvsnsnyaadkgapyvdviclnsyyswy
hdyghleliqlqlatqfenwykkyqkpiiqseygaetiagfhqdpplmfteeyqkslleq
yhlgldqkrrkyvvgeliwnfadfmteqsptrvlgnkkgiftrqrqpksaafllrerywk
iane
>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
>d1bhp__ 7.12.1.1.2 beta-Purothionin {Wheat (Triticum aestivum)}
kscckstlgrncynlcrargaqklcanvcrckltsglscpkdfpk
>d1bhs__ 3.22.1.2.3 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylahskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevf
>d1bi6h1 7.3.10.1.1 (8-31) Bromelain inhibitor VI (cysteine protease inhibitor) {Pineapple (Ananas comosus)}
tdtysdcpgfcktckaefgkyicl
>d1bia_1 1.4.3.1.1 (1-63) Biotin repressor, N-terminal domain {(Escherichia coli)}
mkdntvplkliallangefhsgeqlgetlgmsraainkhiqtlrdwgvdvftvpgkgysl
pep
>d1bia_2 2.24.1.1.1 (271-317) Biotin repressor/biotin holoenzyme synthetase, C-terminal domain {(Escherichia coli)}
finrpvkliigdkeifgisrgidkqgallleqdgiikpwmggeislr
>d1bia_3 4.61.1.2.1 (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 2.24.1.1.1 (271-317) Biotin repressor/biotin holoenzyme synthetase, C-terminal domain {(Escherichia coli)}
finrpvkliigdkeifgisrgidkqgallleqdgiikpwmggeislr
>d1bib_3 4.61.1.2.1 (64-270) Biotin repressor/biotin holoenzyme synthetase, catalytic (central) domain {(Escherichia coli)}
iqllnakqilgqldggsvavlpvidstnqylldrigelksgdaciaeyqqagrgrrgrkw
fspfganlylsmfwrleqgpaaaiglslvigivmaevlrklgadkvrvkwpndlylqdrk
lagilveltgktgdaaqivigaginmamrrveesvvnqgwitlqeaginldrntlaamli
relraalelfeqeglapylsrwekldn
>d1bic__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
hhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnn
ghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvh
wntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprg
llpesldywtypgslthppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvd
nwrpaqplknrqikasfk
>d1bid__ 4.67.1.1.1 Thymidylate synthase {(Escherichia coli)}
mkqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihell
wflqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlk
ndpdsrriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfnias
yallvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesif
dyrfedfeiegydphpgikapvai
>d1bif_1 3.29.1.3.1 (37-249) 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, kinase domain {Rat (Rattus norvegicus)}
cptlivmvglpargktyiskkltrylnfigvptrefnvgqyrrdmvktyksfefflpdne
eglkirkqcalaalndvrkflseegghvavfdatnttrerramifnfgeqngyktffves
icvdpeviaanivqvklgspdyvnrdsdeatedfmrriecyensyesldeeqdrdlsyik
imdvgqsyvvnrvadhiqsrivyylmnihvtpr
>d1bif_2 3.48.1.4.1 (250-468) 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, phosphatase domain {Rat (Rattus norvegicus)}
siylcrhgeselnlkgriggdpglsprgrefskhlaqfisdqnikdlkvftsqmkrtiqt
aealsvpyeqfkvlneidagvceemtyeeiqdhyplefalrdqdkyryrypkgesyedlv
qrlepvimelerqenvlvichqavmrcllayfldkaaeelpylkcplhtvlkltpvaygc
kvesiflnvaavnthrdrpqnvdisrpseealvtvpahq
>d1bila_ 2.38.1.2.14 Chymosin (synonim: renin) {human (Homo sapiens)}
gnttssviltnymdtqyygeigigtppqtfkvvfdtgssnvwvpsskcsrlytacvyhkl
fdasdsssykhngteltlrystgtvsgflsqdiitvggitvtqmfgevtempalpfmlae
fdgvvgmgfieqaigrvtpifdniisqgvlkedvfsfyynrdsensqslggqivlggsdp
qhyegnfhyinliktgvwqiqmkgvsvgsstllcedgclalvdtgasyisgstssieklm
ealgakkrlfdyvvkcnegptlpdisfhlggkeytltsadyvfqesysskklctlaiham
dippptgptwalgatfirkfytefdrrnnrigfalar
>d1bilb_ 2.38.1.2.14 Chymosin (synonim: renin) {human (Homo sapiens)}
gnttssviltnymdtqyygeigigtppqtfkvvfdtgssnvwvpsskcsrlytacvyhkl
fdasdsssykhngteltlrystgtvsgflsqdiitvggitvtqmfgevtempalpfmlae
fdgvvgmgfieqaigrvtpifdniisqgvlkedvfsfyynrdsensqslggqivlggsdp
qhyegnfhyinliktgvwqiqmkgvsvgsstllcedgclalvdtgasyisgstssieklm
ealgakkrlfdyvvkcnegptlpdisfhlggkeytltsadyvfqesysskklctlaiham
dippptgptwalgatfirkfytefdrrnnrigfalar
>d1bima_ 2.38.1.2.14 Chymosin (synonim: renin) {human (Homo sapiens)}
gnttssviltnymdtqyygeigigtppqtfkvvfdtgssnvwvpsskcsrlytacvyhkl
fdasdsssykhngteltlrystgtvsgflsqdiitvggitvtqmfgevtempalpfmlae
fdgvvgmgfieqaigrvtpifdniisqgvlkedvfsfyynrdsensqslggqivlggsdp
qhyegnfhyinliktgvwqiqmkgvsvgsstllcedgclalvdtgasyisgstssieklm
ealgakkrlfdyvvkcnegptlpdisfhlggkeytltsadyvfqesysskklctlaiham
dippptgptwalgatfirkfytefdrrnnrigfalar
>d1bimb_ 2.38.1.2.14 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
>d1bip__ 1.47.1.2.2 Trypsin/alpha-amylase inhibitor RBI {Ragi (Elucine coracana gaertneri) seeds}
svgtscipgmaiphnpldscrwyvstrtcgvgprlatqemkarccrqleaipaycrceav
rilmdgvvtssgqhegrllqdlpgcprqvqrafapklvtevecnlatihggpfclsllga
ge
>d1bira_ 4.1.1.1.3 RNase T1 {(Aspergillus oryzae)}
acdytcgsncysssdvstaqaagyklhedgetvgsnsyphkynnyegfdfsvsspyyewp
ilssgdvysggspgadrvvfnennqlagvithtgasgnnavect
>d1birb_ 4.1.1.1.3 RNase T1 {(Aspergillus oryzae)}
acdytcgsncysssdvstaqaagyklhedgetvgsnsyphkynnyegfdfsvsspyyewp
ilssgdvysggspgadrvvfnennqlagvithtgasgnnavect
>d1bit__ 2.35.1.2.5 Trypsin(ogen) {north atlantic salmon (Salmo salar)}
ivggyeckaysqahqvslnsgyhfcggslvnenwvvsaahcyksrvevrlgehnikvteg
seqfisssrvirhpnyssynidndimliklskpatlntyvqpvalptscapagtmctvsg
wgntmsstadsnklqclnipilsysdcnnsypgmitnamfcagyleggkdscqgdsggpv
vcngelqgvvswgygcaepgnpgvyakvcifndwltstmasy
>d1bje__ 1.1.1.1.8 Myoglobin {horse (Equus caballus)}
glsdgewqqvlnvwgkveadiaghgqevlirlftghpetlekfdkfkhlkteaemkased
lkktgtvvltalggilkkkghheaelkplaqshatkhkipikylefisdaiihvlhskhp
gdfgadaqgamtkalelfrndiaakykelgfqg
>d1bji__ 2.50.1.1.2 Influenza neuraminidase {(influenza virus A), different strains}
rdfnnltkglctinswhiygkdnavrigedsdvlvtrepyvscdpdecrfyalsqgttir
gkhsngtihdrsqyraliswplsspptvynsrvecigwsstschdgktrmsicisgpnnn
asaviwynrrpvteintwarnilrtqesecvchngvcpvvftdgsatgpaetriyyfkeg
kilkweplagtakhieecscygeraeitctcrdnwqgsnrpviridpvamthtsqyicsp
vltdnprpndptvgkcndpypgnnnngvkgfsyldgvntwlgrtisiasrsgyemlkvpn
altddkskptqgqtivlntdwsgysgsfmdywaegecyracfyvelirgrpkedkvwwts
nsivsmcssteflgqwdwpdgakieyfl
>d1bjma_ 2.1.1.1.111 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (lambda) dimer LOC (human)}
xsvltqppsasgtpgqrvtiscsgsssnigensvtwyqhlsgtapklliyednsrasgvs
drfsasksgtsaslaisglqpedetdyycaawddsldvavfgtgtkvtvlgqpkanptvt
lfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskqsnnkyaass
ylsltpeqwkshrsyscqvthegstvektvaptecs
>d1bjmb_ 2.1.1.1.111 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (lambda) dimer LOC (human)}
xsvltqppsasgtpgqrvtiscsgsssnigensvtwyqhlsgtapklliyednsrasgvs
drfsasksgtsaslaisglqpedetdyycaawddsldvavfgtgtkvtvlgqpkanptvt
lfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskqsnnkyaass
ylsltpeqwkshrsyscqvthegstvektvaptecs
>d1bk4__ 5.8.1.1.3 Fructose-1,6-bisphosphatase {Rabbit (Oryctolagus cuniculus)}
fdtdistmtrfvmeegrkaggtgemtqllnslctavkaistavrkagiahlygiagstnv
tgdqvkkldvlsndlvmnmlkssfatcvlvseedknaiivepekrgkyvvcfdpldgssn
idclvsigtifgiyrkkstdepstkdalqpgrnlvaagyalygsatmlvlaggsgvnsfm
ldpaigefilvdknvkikkkgniyslnegyakdfdpavteyiqkkkfppdnsspygaryv
gsmvadvhrtlvyggiflypankkspdgklrllyecnpmafimekaggmattgkeaildi
vptdihqrapvilgspddvqefleiykkhavk
>d1bka_1 3.82.1.2.1 (4-334) Lactoferrin {human (Homo sapiens)}
rsvqwcavsqpeatkcfqwqrnmrkvrgppvscikrdspiqciqaiaenradavtldggf
iyeaglapyklrpvaaevygterqprthyyavavvkkggsfqlnelqglkschtglrrta
gwnvpigtlrpflnwtgppepieaavarffsascvpgadkgqfpnlcrlcagtgenkcaf
ssqepyfsysgafkclrdgagdvafirestvfedlsdeaerdeyellcpdntrkpvdkfk
dchlarvpshavvarsvngkedaiwnllrqaqekfgkdkspkfqlfgspsgqkdllfkds
aigfsrvppridsglylgsgyftaiqnlrks
>d1bka_2 3.82.1.2.1 (335-691) Lactoferrin {human (Homo sapiens)}
eeevaarrarvvwcavgeqelrkcnqwsglsegsvtcssasttedcialvlkgeadamsl
dggyvytagkcglvpvlaenyksqqssdpdpncvdrpvegylavavvrrsdtsltwnsvk
gkkschtavdrtagwnipmgllfnqtgsckfdeyfsqscapgsdprsnlcalcigdeqge
nkcvpnsneryygytgafrclaenagdvafvkdvtvlqntdgnnneawakdlkladfall
cldgkrkpvtearschlamapnhavvsrmdkverlkqvllhqqakfgrngsdcpdkfclf
qsetknllfndnteclarlhgkttyekylgpqyvagitnlkkcstsplleaceflrk
>d1bkf__ 4.19.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdknkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatgvpgiipphatlvfdvellkle
>d1bkl__ 4.53.1.1.2 v-src tyrosine kinase {rous sarcoma virus (Schmidt-ruppin strain a)}
eewyfgkitrreseslllnpenprgtflvresettkgayclsvsdfdnakglnvkhykir
kldsggfyitsrtqfsslqqlvayyskhadglchrltnvcptskefivtd
>d1bkm__ 4.53.1.1.2 v-src tyrosine kinase {rous sarcoma virus (Schmidt-ruppin strain a)}
eewyfgkitrresealllnpenprgtflvresettkgayclsvsdfdnakglnvkhykir
kldsggfyitsrtqfsslqqlvayyskhadglchrltnvcpt
>d1bkw_1 3.4.1.2.2 (1-173,276-391) p-Hydroxybenzoate hydroxylase (PHBH) {(Pseudomonas fluorescens)}
mktqvaiigagpsglllgqllhkagidnvilerqtpdyvlgriragvleqgmvdllreag
vdrrmardglvhegveiafagqrrridlkrlsggktvtvygqtevtrdlmeareacgatt
vyqaaevrlhdlqgerpyvtferdgerlrldcdyiagcdgfhgisrqsipaerXmqhgrl
flagdaahivpptgakglnlaasdvstlyrlllkayregrgellerysaiclrriwkaer
fswwmtsvlhrfpdtdafsqriqqteleyylgseaglatiaenyvglpye
>d1bkw_2 4.12.1.2.1 (174-275) p-Hydroxybenzoate hydroxylase {(Pseudomonas fluorescens)}
lkvfervypfgwlglladtppvsheliyanhprgfalcsqrsatrsryyvqvpltekved
wsderfwtelkarlpaevaeklvtgpsleksiaplrsfvvep
>d1bkxa_ 5.1.1.1.4 cAMP-dependent PK, catalytic subunit {mouse (Mus musculus)}
qesvkeflakakedflkkwetpsqntaqldqfdriktlgtgsfgrvmlvkhkesgnhyam
kildkqkvvklkqiehtlnekrilqavnfpflvklefsfkdnsnlymvmeyvaggemfsh
lrrigrfsepharfyaaqivltfeylhsldliyrdlkpenllidqqgyiqvtdfgfakrv
kgrtwxlcgtpeylapeiilskgynkavdwwalgvliyemaagyppffadqpiqiyekiv
sgkvrfpshfssdlkdllrnllqvdltkrfgnlkngvndiknhkwfattdwiaiyqrkve
apfipkfkgpgdtsnfddyeeeeirvxinekcgkeftef
>d1bla__ 2.31.1.1.1 Basic FGF {human (Homo sapiens)}
maegeittlpalpedggsgafppghfkdpkrlycknggfflrihpdgrvdgvreksdphi
klqlqaeergvvsikgvsanrylamkedgrllasksvtdecffferlesnnyntyrsrky
tswyvalkrtgqyklgsktgpgqkailflpmsaks
>d1blba1 2.9.1.1.5 (-6-85) beta-Crystallin {bovine (Bos taurus)}
apqplnpkiiifeqenfqghshelngpcpnlketgvekagsvlvqagpwvgyeqanckge
qfvfekgeyprwdswtssrrtdslsslrpikvds
>d1blba2 2.9.1.1.5 (86-175) beta-Crystallin {bovine (Bos taurus)}
qehkitlyenpnftgkkmevidddvpsfhahgyqekvssvrvqsgtwvgyqypgyrglqy
llekgdykdsgdfgapqpqvqsvrrirdmqw
>d1blbb1 2.9.1.1.5 (-2-85) beta-Crystallin {bovine (Bos taurus)}
lnpkiiifeqenfqghshelngpcpnlketgvekagsvlvqagpwvgyeqanckgeqfvf
ekgeyprwdswtssrrtdslsslrpikvds
>d1blbb2 2.9.1.1.5 (86-175) beta-Crystallin {bovine (Bos taurus)}
qehkitlyenpnftgkkmevidddvpsfhahgyqekvssvrvqsgtwvgyqypgyrglqy
llekgdykdsgdfgapqpqvqsvrrirdmqw
>d1blbc1 2.9.1.1.5 (-8-85) beta-Crystallin {bovine (Bos taurus)}
agkpqplnpkiiifeqenfqghshelngpcpnlketgvekagsvlvqagpwvgyeqanck
geqfvfekgeyprwdswtssrrtdslsslrpikvds
>d1blbc2 2.9.1.1.5 (86-175) beta-Crystallin {bovine (Bos taurus)}
qehkitlyenpnftgkkmevidddvpsfhahgyqekvssvrvqsgtwvgyqypgyrglqy
llekgdykdsgdfgapqpqvqsvrrirdmqw
>d1blbd1 2.9.1.1.5 (-4-85) beta-Crystallin {bovine (Bos taurus)}
qplnpkiiifeqenfqghshelngpcpnlketgvekagsvlvqagpwvgyeqanckgeqf
vfekgeyprwdswtssrrtdslsslrpikvds
>d1blbd2 2.9.1.1.5 (86-175) beta-Crystallin {bovine (Bos taurus)}
qehkitlyenpnftgkkmevidddvpsfhahgyqekvssvrvqsgtwvgyqypgyrglqy
llekgdykdsgdfgapqpqvqsvrrirdmqw
>d1blc__ 5.4.1.1.3 beta-Lactamase, class A {(Staphylococcus aureus)}
kelndlekkynahigvyaldtksgkevkfnsdkrfayastskainsailleqvpynklnk
kvhinkddivayspilekyvgkditlkalieasmtysdntannkiikeiggikkvkqrlk
elgdkvtnpvryeielnyyspkskkdtstpaafgktlnkliangklskenkkflldlmln
nksgdtlikdgvpkdykvadksgqaityasrndvafvypkgqsepivlviftnkdnksdk
pndklisetaksvmkef
>d1bld__ 2.31.1.1.1 Basic FGF {human (Homo sapiens)}
maegeittlpalpedggsgafppghfkdpkrlycknggfflrihpdgrvdgvreksdphi
klqlqaeergvvsikgvsanrylamkedgrllasksvtdecffferlesnnyntyrsrky
tswyvalkrtgqyklgsktgpgqkailflpmsaks
>d1ble__ 3.30.1.1.1 Fructose permease, subunit IIb {(Bacillus subtilis)}
mnivlariddrfihgqiltrwikvhaadriivvsddiaqdemrktlilsvapsnvkasav
svskmakafhspryegvtamllfenpsdivslieagvpiktvnvggmrfenhrrqitksv
svteqdikafetlsdkgvklelrqlpsdasedfvqilrnvt
>d1blf_1 3.82.1.2.2 (5-333) Lactoferrin {Bovine (Bos taurus)}
nvrwctisqpewfkcrrwqwrmkklgapsitcvrrafaleciraiaekkadavtldggmv
feagrdpyklrpvaaeiygtkespqthyyavavvkkgsnfqldqlqgrkschtglgrsag
wiipmgilrpylswtesleplqgavakffsascvpcidrqaypnlcqlckgegenqcacs
srepyfgysgafkclqdgagdvafvkettvfenlpekadrdqyellclnnsrapvdafke
chlaqvpshavvarsvdgkedliwkllskaqekfgknksrsfqlfgsppgqrdllfkdsa
lgflripskvdsalylgsrylttlknlre
>d1blf_2 3.82.1.2.2 (334-689) Lactoferrin {Bovine (Bos taurus)}
taeevkarytrvvwcavgpeeqkkcqqwsqqsgqnvtcatasttddcivlvlkgeadaln
ldggyiytagkcglvpvlaenrksskhssldcvlrptegylavavvkkanegltwnslkd
kkschtavdrtagwnipmglivnqtgscafdeffsqscapgadpksrlcalcagddqgld
kcvpnskekyygytgafrclaedvgdvafvkndtvwentngestadwaknlnredfrllc
ldgtrkpvteaqschlavapnhavvsrsdraahvkqvllhqqalfgkngkncpdkfclfk
setknllfndnteclaklggrptyeeylgteyvtaianlkkcstsplleacafltr
>d1blh__ 5.4.1.1.3 beta-Lactamase, class A {(Staphylococcus aureus)}
kelndlekkynahigvyaldtksgkevkfnsdkrfayastskainsailleqvpynklnk
kvhinkddivayspilekyvgkditlkalieasmtysdntannkiikeiggikkvkqrlk
elgdkvtnpvryeielnyyspkskkdtstpaafgktlnkliangklskenkkflldlmln
nksgdtlikdgvpkdykvadksgqaityasrndvafvypkgqsepivlviftnkdnksdk
pndklisetaksvmkef
>d1blj__ 4.53.1.1.15 P55 Blk protein tyrosine kinase {mouse (Mus musculus)}
gsvapvetlevekwffrtisrkdaerqllapmnkagsfliresesnkgafslsvkdittq
gevvkhykirsldnggyyispritfptlqalvqhyskkgdglcqkltlpcvnla
>d1blk__ 4.53.1.1.15 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 3.58.4.3.1 (160-484) Leucine aminopeptidase, C-terminal domain {bovine (Bos taurus)}
fasgqnlarrlmetpanemtptkfaeiveenlksasiktdvfirpkswieeqemgsflsv
akgseeppvfleihykgspnasepplvfvgkgitfdsggisikaaanmdlmradmggaat
icsaivsaakldlpinivglaplcenmpsgkankpgdvvrarngktiqvdntdaegrlil
adalcyahtfnpkviinaatltgamdialgsgatgvftnsswlwnklfeasietgdrvwr
mplfehytrqvidcqladvnnigkyrsagactaaaflkefvthpkwahldiagvmtnkde
vpylrkgmagrptrtlieflfrfsq
>d1blp__ 5.4.1.1.3 beta-Lactamase, class A {(Staphylococcus aureus)}
kelndlekkynahigvyaldtksgkevkfnsdkrfayastskainsailleqvpynklnk
kvhinkddivayspilekyvgkditlkalieasmtysdntannkiikeiggikkvkqrlk
elgdkvtnpvryeielnyyspkskkntstpaafgktlnkliangklskenkkflldlmln
nksgdtlikdgvpkdykvadksgqaityasrndvafvypkgqsepivlviftnkdnksdk
pndklisetaksvmkef
>d1blsa_ 5.4.1.1.6 beta-Lactamase, class C {Cephalosporinase (Enterobacter cloacae P99)}
pvsekqlaevvantitplmkaqsvpgmavaviyqgkphyytfgkadiaankpvtpqtlfe
lgsisktftgvlggdaiargeislddavtrywpqltgkqwqgirmldlatytagglplqv
pdevtdnasllrfyqnwqpqwkpgttrlyanasiglfgalavkpsgmpyeqamttrvlkp
lkldhtwinvpkaeeahyawgyrdgkavrvspgmldaqaygvktnvqdmanwvmanmape
nvadaslkqgialaqsrywrigsmyqglgwemlnwpveantvvegsdskvalaplpvaev
nppappvkaswvhktgstggfgsyvafipekqigivmlantsypnparveaayhileal
>d1blsb_ 5.4.1.1.6 beta-Lactamase, class C {Cephalosporinase (Enterobacter cloacae P99)}
pvsekqlaevvantitplmkaqsvpgmavaviyqgkphyytfgkadiaankpvtpqtlfe
lgsisktftgvlggdaiargeislddavtrywpqltgkqwqgirmldlatytagglplqv
pdevtdnasllrfyqnwqpqwkpgttrlyanasiglfgalavkpsgmpyeqamttrvlkp
lkldhtwinvpkaeeahyawgyrdgkavrvspgmldaqaygvktnvqdmanwvmanmape
nvadaslkqgialaqsrywrigsmyqglgwemlnwpveantvvegsdskvalaplpvaev
nppappvkaswvhktgstggfgsyvafipekqigivmlantsypnparveaayhileal
>d1blu__ 4.34.1.1.5 Ferredoxin II {(Cromatium vinosum)}
almitdecincdvcepecpngaisqgdetyviepslctecvghyetsqcvevcpvdciik
dpsheetedelrakyeritg
>d1bmaa_ 2.35.1.2.14 Elastase {porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1bmc__ 4.97.1.1.1 Zn metallo-beta-lactamase {(Bacillus cereus)}
tviknetgtisisqlnknvwvhtelgsfngeavpsnglvlntskglvlvdsswddkltke
liemvekkfqkrvtdviithahadriggiktlkergikahstaltaelakkngyeeplgd
lqtvtnlkfgnmkvetfypgkghtednivvwlpqynilvggclvkstsakdlgnvadayv
newstsienvlkryrninavvpghgevgdkglllhtldllk
>d1bmda1 3.22.1.5.3 (1-154) Malate dehydrogenase {(Thermus flavus)}
kapvrvavtgaagqigysllfriaagemlgkdqpvilqlleipqamkalegvvmeledca
fpllagleatddpdvafkdadyallvgaaprkagmerrdllqvngkifteqgralaevak
kdvkvlvvgnpantnaliayknapglnprnftam
>d1bmda2 4.100.1.1.3 (155-332) Malate dehydrogenase {(Thermus flavus)}
trldhnrakaqlakktgtgvdrirrmtvwgnhsstmfpdlfhaevdgrpalelvdmewye
kvfiptvaqrgaaiiqargassaasaanaaiehirdwalgtpegdwvsmavpsqgeygip
egivysfpvtakdgayrvvegleinefarkrmeitaqelldemeqvkalgli
>d1bmdb1 3.22.1.5.3 (1-154) Malate dehydrogenase {(Thermus flavus)}
kapvrvavtgaagqigysllfriaagemlgkdqpvilqlleipqamkalegvvmeledca
fpllagleatddpdvafkdadyallvgaaprkagmerrdllqvngkifteqgralaevak
kdvkvlvvgnpantnaliayknapglnprnftam
>d1bmdb2 4.100.1.1.3 (155-332) Malate dehydrogenase {(Thermus flavus)}
trldhnrakaqlakktgtgvdrirrmtvwgnhsstmfpdlfhaevdgrpalelvdmewye
kvfiptvaqrgaaiiqargassaasaanaaiehirdwalgtpegdwvsmavpsqgeygip
egivysfpvtakdgayrvvegleinefarkrmeitaqelldemeqvkalgli
>d1bme__ 4.97.1.1.1 Zn metallo-beta-lactamase {(Bacillus cereus)}
tviknetgtisisqlnknvwvhtelgsfngeavpsnglvlntskglvlvdsswddkltke
liemvekkfqkrvtdviithahadriggiktlkergikahstaltaelakkngyeeplgd
lqtvtnlkfgnmkvetfypgkghtednivvwlpqynilvggclvkstsakdlgnvadayv
newstsienvlkryrninavvpghgevgdkglllhtldllk
>d1bmfa1 1.59.1.1.1 (380-510) The C-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
tramkqvagtmklelaqyrevaafaqfgsdldaatqqllsrgvrltellkqgqyspmaie
eqvaviyagvrgyldklepskitkfenaflshvisqhqallgkirtdgkiseesdaklke
ivtnflagfea
>d1bmfa2 2.37.1.1.1 (24-94) The N-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
dleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgndklik
egdivkrtgai
>d1bmfa3 3.29.1.7.2 (95-379) central domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
vdvpvgeellgrvvdalgnaidgkgpigskarrrvglkapgiiprisvrepmqtgikavd
slvpigrgqreliigdrqtgktsiaidtiinqkrfndgtdekkklyciyvaigqkrstva
qlvkrltdadamkytivvsatasdaaplqylapysgcsmgeyfrdngkhaliiyddlskq
avayrqmslllrrppgreaypgdvfylhsrlleraakmndafgggsltalpvietqagdv
sayiptnvisitdgqifletelfykgirpainvglsvsrvgsaaq
>d1bmfb1 1.59.1.1.1 (380-510) The C-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
tramkqvagtmklelaqyrevaafaqfgsdldaatqqllsrgvrltellkqgqyspmaie
eqvaviyagvrgyldklepskitkfenaflshvisqhqallgkirtdgkiseesdaklke
ivtnflagfea
>d1bmfb2 2.37.1.1.1 (24-94) The N-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
dleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgndklik
egdivkrtgai
>d1bmfb3 3.29.1.7.2 (95-379) central domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
vdvpvgeellgrvvdalgnaidgkgpigskarrrvglkapgiiprisvrepmqtgikavd
slvpigrgqreliigdrqtgktsiaidtiinqkrfndgtdekkklyciyvaigqkrstva
qlvkrltdadamkytivvsatasdaaplqylapysgcsmgeyfrdngkhaliiyddlskq
avayrqmslllrrppgreaypgdvfylhsrlleraakmndafgggsltalpvietqagdv
sayiptnvisitdgqifletelfykgirpainvglsvsrvgsaaq
>d1bmfc1 1.59.1.1.1 (380-510) The C-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
tramkqvagtmklelaqyrevaafaqfgsdldaatqqllsrgvrltellkqgqyspmaie
eqvaviyagvrgyldklepskitkfenaflshvisqhqallgkirtdgkiseesdaklke
ivtnflagfea
>d1bmfc2 2.37.1.1.1 (19-94) The N-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
adtsvdleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgn
dklikegdivkrtgai
>d1bmfc3 3.29.1.7.2 (95-379) central domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
vdvpvgeellgrvvdalgnaidgkgpigskarrrvglkapgiiprisvrepmqtgikavd
slvpigrgqreliigdrqtgktsiaidtiinqkrfndgtdekkklyciyvaigqkrstva
qlvkrltdadamkytivvsatasdaaplqylapysgcsmgeyfrdngkhaliiyddlskq
avayrqmslllrrppgreaypgdvfylhsrlleraakmndafgggsltalpvietqagdv
sayiptnvisitdgqifletelfykgirpainvglsvsrvgsaaq
>d1bmfd1 1.59.1.1.1 (358-475) The C-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
mdpnivgsehydvargvqkilqdykslqdiiailgmdelseedkltvsrarkiqrflsqp
fqvaevftghlgklvplketikgfqqilageydhlpeqafymvgpieeavakadklae
>d1bmfd2 2.37.1.1.1 (9-81) The N-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1bmfd3 3.29.1.7.2 (82-357) central domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
iripvgpetlgrimnvigepidergpiktkqfaaihaeapefvemsveqeilvtgikvvd
llapyakggkiglfggagvgktvlimelinnvakahggysvfagvgertregndlyhemi
esgvinlkdatskvalvygqmneppgararvaltgltvaeyfrdqegqdvllfidnifrf
tqagsevsallgripsavgyqptlatdmgtmqeritttkkgsitsvqaiyvpaddltdpa
pattfahldattvlsraiaelgiypavdpldstsri
>d1bmfe1 1.59.1.1.1 (358-474) The C-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
mdpnivgsehydvargvqkilqdykslqdiiailgmdelseedkltvsrarkiqrflsqp
fqvaevftghlgklvplketikgfqqilageydhlpeqafymvgpieeavakadkla
>d1bmfe2 2.37.1.1.1 (9-81) The N-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1bmfe3 3.29.1.7.2 (82-357) central domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
iripvgpetlgrimnvigepidergpiktkqfaaihaeapefvemsveqeilvtgikvvd
llapyakggkiglfggagvgktvlimelinnvakahggysvfagvgertregndlyhemi
esgvinlkdatskvalvygqmneppgararvaltgltvaeyfrdqegqdvllfidnifrf
tqagsevsallgripsavgyqptlatdmgtmqeritttkkgsitsvqaiyvpaddltdpa
pattfahldattvlsraiaelgiypavdpldstsri
>d1bmff1 1.59.1.1.1 (358-474) The C-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
mdpnivgsehydvargvqkilqdykslqdiiailgmdelseedkltvsrarkiqrflsqp
fqvaevftghlgklvplketikgfqqilageydhlpeqafymvgpieeavakadkla
>d1bmff2 2.37.1.1.1 (9-81) The N-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1bmff3 3.29.1.7.2 (82-357) central domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
iripvgpetlgrimnvigepidergpiktkqfaaihaeapefvemsveqeilvtgikvvd
llapyakggkiglfggagvgktvlimelinnvakahggysvfagvgertregndlyhemi
esgvinlkdatskvalvygqmneppgararvaltgltvaeyfrdqegqdvllfidnifrf
tqagsevsallgripsavgyqptlatdmgtmqeritttkkgsitsvqaiyvpaddltdpa
pattfahldattvlsraiaelgiypavdpldstsri
>d1bmfg_ 1.19.1.1.1 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_ 4.97.1.1.2 Zn metallo-beta-lactamase {(Bacteroides fragilis)}
svkisddisitqlsdkvytyvslaeiegwgmvpsngmivinnhqaalldtpindaqteml
vnwvtdslhakvttfipnhwhgdcigglgylqrkgvqsyanqmtidlakekglpvpehgf
tdsltvsldgmplqcyylggghatdnivvwlptenilfggcmlkdnqatsignisdadvt
awpktldkvkakfpsaryvvpghgdyggteliehtkqivnqyiestsk
>d1bmib_ 4.97.1.1.2 Zn metallo-beta-lactamase {(Bacteroides fragilis)}
ksvkisddisitqlsdkvytyvslaeiegwgmvpsngmivinnhqaalldtpindaqtem
lvnwvtdslhakvttfipnhwhgdcigglgylqrkgvqsyanqmtidlakekglpvpehg
ftdsltvsldgmplqcyylggghatdnivvwlptenilfggcmlkdnqatsignisdadv
tawpktldkvkakfpsaryvvpghgdyggteliehtkqivnqyiestskp
>e1bmm.1h 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1bmm.1l 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
geadcglrplfekksledkterellesy
>e1bmn.1h 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqf
>e1bmn.1l 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
adcglrplfekksledkterellesy
>d1bmoa1 1.37.1.3.1 (136-286) The C-terminal (EC) domain of BM-40/SPARC/osteonectin {human (Homo sapiens)}
ppcldseltefplrmrdwlknvlvtlyerdednnlltekqklrvkkihenekrleagdhp
vellardfeknynmyifpvhwqfgqldqhpidgylshtelaplraplipmehcttrffet
cdldndkyialdewagcfgikqkdidkdlvi
>d1bmoa2 7.3.9.3.1 (54-77) A domain of BM-40/SPARC/osteonectin {human (Homo sapiens)}
pcqnhhckhgkvceldenntpmcv
>d1bmoa3 7.14.1.1.7 (78-135) A domain of BM-40/SPARC/osteonectin {human (Homo sapiens)}
cqdptscpapigefekvcsndnktfdsschffatkctlegtkkghklhldyigpckyi
>d1bmob1 1.37.1.3.1 (136-286) The C-terminal (EC) domain of BM-40/SPARC/osteonectin {human (Homo sapiens)}
ppcldseltefplrmrdwlknvlvtlyerdednnlltekqklrvkkihenekrleagdhp
vellardfeknynmyifpvhwqfgqldqhpidgylshtelaplraplipmehcttrffet
cdldndkyialdewagcfgikqkdidkdlvi
>d1bmob2 7.3.9.3.1 (54-77) A domain of BM-40/SPARC/osteonectin {human (Homo sapiens)}
pcqnhhckhgkvceldenntpmcv
>d1bmob3 7.14.1.1.7 (78-135) A domain of BM-40/SPARC/osteonectin {human (Homo sapiens)}
cqdptscpapigefekvcsndnktfdsschffatkctlegtkkghklhldyigpckyi
>d1bmp__ 7.16.1.2.4 bone morphogenetic protein-7 {human (Homo sapiens)}
qackkhelyvsfrdlgwqdwiiapegyaayycegecafplnsymnatnhaivqtlvhfin
petvpkpccaptqlnaisvlyfddssnvilkkyrnmvvracgch
>d1bmsa_ 4.46.1.1.1 MS2 virus coat protein {(bacteriophage MS2)}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvtcsvrqssaqnrkyti
kvevpkvatqtvggvelnvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1bmsb_ 4.46.1.1.1 MS2 virus coat protein {(bacteriophage MS2)}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvtcsvrqssaqnrkyti
kvevpkvatqtvggvelnvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1bmsc_ 4.46.1.1.1 MS2 virus coat protein {(bacteriophage MS2)}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvtcsvrqssaqnrkyti
kvevpkvatqtvggvelnvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1bmta1 1.44.1.1.1 (651-740) Methionine synthase domain {(Escherichia coli)}
qaewrswevnkrleyslvkgitefieqdteearqqatrpieviegplmdgmnvvgdlfge
gkmflpqvvksarvmkqavaylepfieask
>d1bmta2 3.14.5.1.1 (741-896) Methionine synthase, C-terminal domain {(Escherichia coli)}
eqgktngkmviatvkgdvhdigknivgvvlqcnnyeivdlgvmvpaekilrtakevnadl
iglsglitpsldemvnvakemerqgftiplliggattskahtavkieqnysgptvyvqna
srtvgvvaallsdtqrddfvartrkeyetvriqhgr
>d1bmtb1 1.44.1.1.1 (651-740) Methionine synthase domain {(Escherichia coli)}
qaewrswevnkrleyslvkgitefieqdteearqqatrpieviegplmdgmnvvgdlfge
gkmflpqvvksarvmkqavaylepfieask
>d1bmtb2 3.14.5.1.1 (741-896) Methionine synthase, C-terminal domain {(Escherichia coli)}
eqgktngkmviatvkgdvhdigknivgvvlqcnnyeivdlgvmvpaekilrtakevnadl
iglsglitpsldemvnvakemerqgftiplliggattskahtavkieqnysgptvyvqna
srtvgvvaallsdtqrddfvartrkeyetvriqhgr
>d1bmv1_ 2.8.1.2.5 BPMV coat protein {(Bean pod mottle virus)}
sisqqtvwnqmatvrtplnfdsskqsfcqfsvdllgggisvdktgdwitlvqnspisnll
rvaawkkgclmvkvvmsgnaavkrsdwaslvqvfltnsnstehfdacrwtksephsweli
fpievcgpnngfemwssewanqtswhlsflvdnpkqsttfdvllgisqnfeiagntlmpa
fsvpq
>d1bmv2_ 2.8.1.2.5 BPMV coat protein {(Bean pod mottle virus)}
metnlfklslddvetpkgsmldlkisqskialpkntvggtilrsdllanfltegnfrasv
dlqrthrikgmikmvatvgipentgialacamnssirgrassdiyticsqdcelwnpact
kamtmsfnpnpcsdawsleflkrtgfhcdiicvtgwtatpmqdvqvtidwfissqecvpr
tycvlnpqnpfvlnrwmgkltfpqgtsrsvkrmplsigggagaksailmnmpnavlsmwr
yfvgdlvfevskmtspyikctvsffiafgnladdtinfeafphklvqfgeiqekvvlkfs
qeefltawstqvrpattlladgcpylyamvhdssvstipgdfvigvkltiienmcaygln
pgisgsrllgtipq
>d1bn21_ 2.7.1.1.1 Neurophysin II {bovine (Bos taurus)}
amsdlelrqclpcgpggkgrcfgpsiccgdelgcfvgtaealrcqeenylpspcqsgqkp
cgsggrcaaagiccndescvtepecr
>d1bn22_ 2.7.1.1.1 Neurophysin II {bovine (Bos taurus)}
amsdlelrqclpcgpggkgrcfgpsiccgdelgcfvgtaealrcqeenylpspcqsgqkp
cgsggrcaaagiccndescvtepecr
>d1bn23_ 2.7.1.1.1 Neurophysin II {bovine (Bos taurus)}
amsdlelrqclpcgpggkgrcfgpsiccgdelgcfvgtaealrcqeenylpspcqsgqkp
cgsggrcaaagiccndescvtepecr
>d1bn24_ 2.7.1.1.1 Neurophysin II {bovine (Bos taurus)}
amsdlelrqclpcgpggkgrcfgpsiccgdelgcfvgtaealrcqeenylpspcqsgqkp
cgsggrcaaagiccndescvtepecr
>d1bnb__ 7.8.1.1.2 Beta-defensin 12 {Bovine (Bos taurus)}
aplscgrnggvcipircpvpmrqigtcfgrpvkccrsw
>d1bnca1 2.65.2.1.1 (331-446) Biotin carboxylase subunit of acetyl-CoA carboxylase, C-terminal domain {(Escherichia coli)}
rghavecrinaedpntflpspgkitrfhapggfgvrweshiyagytvppyydsmigklic
ygenrdvaiarmknalqeliidgiktnvdlqirimndenfqhggtnihylekklgl
>d1bnca2 3.23.1.1.1 (1-114) Biotin carboxylase (BC) subunit of acetyl-CoA carboxylase {(Escherichia coli)}
mldkivianrgeialrilrackelgiktvavhssadrdlkhvlladetvcigpapsvksy
lnipaiisaaeitgavaihpgygflsenanfaeqversgfifigpkaetirlmg
>d1bnca3 4.89.1.2.1 (115-330) Biotin carboxylase subunit of acetyl-CoA carboxylase {(Escherichia coli)}
dkvsaiaamkkagvpcvpgsdgplgddmdknraiakrigypviikasgggggrgmrvvrg
daelaqsismtraeakaafsndmvymekylenprhveiqvladgqgnaiylaerdcsmqr
rhqkvveeapapgitpelrryigercakacvdigyrgagtfeflfengefyfiemntriq
vehpvtemitgvdlikeqlriaagqplsikqeevhv
>d1bncb1 2.65.2.1.1 (331-448) Biotin carboxylase subunit of acetyl-CoA carboxylase, C-terminal domain {(Escherichia coli)}
rghavecrinaedpntflpspgkitrfhapggfgvrweshiyagytvppyydsmigklic
ygenrdvaiarmknalqeliidgiktnvdlqirimndenfqhggtnihylekklglqe
>d1bncb2 3.23.1.1.1 (1-114) Biotin carboxylase (BC) subunit of acetyl-CoA carboxylase {(Escherichia coli)}
mldkivianrgeialrilrackelgiktvavhssadrdlkhvlladetvcigpapsvksy
lnipaiisaaeitgavaihpgygflsenanfaeqversgfifigpkaetirlmg
>d1bncb3 4.89.1.2.1 (115-330) Biotin carboxylase subunit of acetyl-CoA carboxylase {(Escherichia coli)}
dkvsaiaamkkagvpcvpgsdgplgddmdknraiakrigypviikasgggggrgmrvvrg
daelaqsismtraeakaafsndmvymekylenprhveiqvladgqgnaiylaerdcsmqr
rhqkvveeapapgitpelrryigercakacvdigyrgagtfeflfengefyfiemntriq
vehpvtemitgvdlikeqlriaagqplsikqeevhv
>d1bnda_ 7.16.1.3.2 Brain-derived neurotrophic factor/neurotrophin 3 heterodimer, BDNF/NT3 {Human (Homo sapiens)}
gqlsvcdsisewvtaadkktavdmsggtvtvlekvpvskgqlkqyfyetkcnpmgytkeg
crgidkrhwnsqcrttqsyvraltmdskkrigwrfiridtscvctltik
>d1bndb_ 7.16.1.3.2 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
>d1bno__ 1.48.1.1.2 DNA polymerase beta, N-terminal (8 kD)-domain {rat (Rattus norvegicus)}
mskrkapqetlnggitdmlvelanfeknvsqaihkynayrkaasviakyphkiksgaeak
klpgvgtkiaekideflatgklrklek
>d1bnp__ 1.48.1.1.2 DNA polymerase beta, N-terminal (8 kD)-domain {rat (Rattus norvegicus)}
mskrkapqetlnggitdmlvelanfeknvsqaihkynayrkaasviakyphkiksgaeak
klpgvgtkiaekideflatgklrklek
>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
>d1boc__ 1.37.1.1.1 Calbindin D9K {bovine (Bos taurus)}
mkspeelkgifekyadkegdgnqlskeelklllqtefpsllkgmstldelfeeldkngdg
evsfeefqvlvkkisq
>d1bod__ 1.37.1.1.1 Calbindin D9K {bovine (Bos taurus)}
mkspeelkgifekydkegdgqlskeelklllqtefpsllkgmstldelfeeldkngdgev
sfeefqvlvkkisq
>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
>d1bor__ 7.37.1.1.3 The acute promyelocytic leukaemia proto-onkoprotein PML {Human (Homo sapiens)}
eeefqflrcqqcqaeakcpkllpclhtlcsgcleasgmqcpicqapwplgadtpal
>d1bova_ 2.29.2.1.4 Verotoxin-1 {(Escherichia coli)}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bovb_ 2.29.2.1.4 Verotoxin-1 {(Escherichia coli)}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bovc_ 2.29.2.1.4 Verotoxin-1 {(Escherichia coli)}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bovd_ 2.29.2.1.4 Verotoxin-1 {(Escherichia coli)}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bove_ 2.29.2.1.4 Verotoxin-1 {(Escherichia coli)}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>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
>d1bp1_1 4.44.1.1.1 (1-217) Bactericidal permeability-increasing protein, BPI {human (Homo sapiens)}
vnpgvvvrisqkgldyasqqgtaalqkelkrikipdysdsfkikhlgkghysfysmdire
fqlpssqismvpnvglkfsisnanikisgkwkaqkrflkmsgnfdlsiegmsisadlklg
snptsgkptitcsscsshinsvhvhiskskvgwliqlfhkkiesalrnkmnsqvcekvtn
svssklqpyfqtlpvmtkidsvaginyglvappatta
>d1bp1_2 4.44.1.1.1 (218-456) Bactericidal permeability-increasing protein, BPI {human (Homo sapiens)}
etldvqmkgefysenhhnpppfappvmefpaahdrmvylglsdyffntaglvyqeagvlk
mtlrddmipkeskfrlttkffgtflpevakkfpnmkiqihvsastpphlsvqptgltfyp
avdvqafavlpnsalaslfligmhttgsmevsaesnrlvgelkldrlllelkhsnigpfp
vellqdimnyivpilvlprvneklqkgfplptparvqlynvvlqphqnfllfgadvvyk
>d1bp2__ 1.103.1.2.11 Phospholipase A2 {bovine (Bos taurus l.) pancreas}
alwqfngmikckipsseplldfnnygcycglggsgtpvddldrccqthdncykqakklds
ckvlvdnpytnnysyscsnneitcssennaceaficncdrnaaicfskvpynkehknldk
knc
>d1bpb__ 5.10.1.1.2 DNA polymerase beta, catalytic (31 kD) fragment {rat (Rattus norvegicus)}
ddtsssinfltrvtgigpsaarklvdegiktledlrknedklnhhqriglkyfedfekri
preemlqmqdivlnevkkldpeyiatvcgsfrrgaessgdmdvllthpnftsesskqpkl
lhrvveqlqkvrfitdtlskgetkfmgvcqlpsendeneyphrridirlipkdqyycgvl
yftgsdifnknmrahalekgftineytirplgvtgvageplpvdseqdifdyiqwryrep
kdrse
>d1bpd_1 1.48.1.1.2 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {rat (Rattus norvegicus)}
etlnggitdmlvelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d1bpd_2 5.10.1.1.2 (92-335) DNA polymerase beta, catalytic (31 kD) fragment {rat (Rattus norvegicus)}
dtsssinfltrvtgigpsaarklvdegiktledlrknedklnhhqriglkyfedfekrip
reemlqmqdivlnevkkldpeyiatvcgsfrrgaessgdmdvllthpnftsesskqpkll
hrvveqlqkvrfitdtlskgetkfmgvcqlpsendeneyphrridirlipkdqyycgvly
ftgsdifnknmrahalekgftineytirplgvtgvageplpvdseqdifdyiqwryrepk
drse
>d1bpe_1 5.10.1.1.2 (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__ 7.7.1.1.1 Pancreatic trypsin inhibitor {bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d1bplb1 2.53.1.1.1 (374-482) Bacterial alpha-Amylase (BLA) {(Bacillus licheniformis)}
qreipalkhkiepilkarkqyaygaqhdyfdhhdivgwtregdssvansglaalitdgpg
gakrmyvgrqnagetwhditgnrsepvvinsegwgefhvnggsvsiyvq
>d1bpm_1 3.41.1.1.1 (1-159) Leucine aminopeptidase, N-terminal domain {bovine (Bos taurus)}
tkglvlgiyskekeedepqftsagenfnklvsgklreilnisgpplkagktrtfyglhed
fpsvvvvglgkktagideqenwhegkeniraavaagcrqiqdleipsvevdpcgdaqaaa
egavlglyeyddlkqkrkvvvsaklhgsedqeawqrgvl
>d1bpm_2 3.58.4.3.1 (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 3.58.4.3.1 (160-484) Leucine aminopeptidase, C-terminal domain {bovine (Bos taurus)}
fasgqnlarrlmetpanemtptkfaeiveenlksasiktdvfirpkswieeqemgsflsv
akgseeppvfleihykgspnasepplvfvgkgitfdsggisikaaanmdlmradmggaat
icsaivsaakldlpinivglaplcenmpsgkankpgdvvrarngktiqvdntdaegrlil
adalcyahtfnpkviinaatltgamdialgsgatgvftnsswlwnklfeasietgdrvwr
mplfehytrqvidcqladvnnigkyrsagactaaaflkefvthpkwahldiagvmtnkde
vpylrkgmagrptrtlieflfrfsq
>d1bpq__ 1.103.1.2.11 Phospholipase A2 {bovine (Bos taurus l.) pancreas}
alwqfngmikckipsseplldfnnygcycglggsgtpvddldrccqthdncykqamklds
ckvlvdnpytnnysyscsnneitcssennaceaficncdrnaaicfskvpynkehknldk
knc
>d1bpt__ 7.7.1.1.1 Pancreatic trypsin inhibitor {bovine (Bos taurus)}
rpdfcleppytgpckariiryfanakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bpxa1 1.48.1.1.1 (5-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
kapqetlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpg
vgtkiaekideflatgklrklekirqd
>d1bpxa2 5.10.1.1.1 (92-335) DNA polymerase beta, catalytic (31 kD) fragment {Human (Homo sapiens)}
dtsssinfltrvsgigpsaarkfvdegiktledlrknedklnhhqriglkyfgdfekrip
reemlqmqdivlnevkkvdseyiatvcgsfrrgaessgdmdvllthpsftsestkqpkll
hqvveqlqkvhfitdtlskgetkfmgvcqlpskndekeyphrridirlipkdqyycgvly
ftgsdifnknmrahalekgftineytirplgvtgvageplpvdsekdifdyiqwkyrepk
drse
>d1bpya1 1.48.1.1.1 (10-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
tlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtki
aekideflatgklrklekirqd
>d1bpya2 5.10.1.1.1 (92-335) DNA polymerase beta, catalytic (31 kD) fragment {Human (Homo sapiens)}
dtsssinfltrvsgigpsaarkfvdegiktledlrknedklnhhqriglkyfgdfekrip
reemlqmqdivlnevkkvdseyiatvcgsfrrgaessgdmdvllthpsftsestkqpkll
hqvveqlqkvhfitdtlskgetkfmgvcqlpskndekeyphrridirlipkdqyycgvly
ftgsdifnknmrahalekgftineytirplgvtgvageplpvdsekdifdyiqwkyrepk
drse
>d1bpza1 1.48.1.1.1 (5-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
kapqetlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpg
vgtkiaekideflatgklrklekirqd
>d1bpza2 5.10.1.1.1 (92-335) DNA polymerase beta, catalytic (31 kD) fragment {Human (Homo sapiens)}
dtsssinfltrvsgigpsaarkfvdegiktledlrknedklnhhqriglkyfgdfekrip
reemlqmqdivlnevkkvdseyiatvcgsfrrgaessgdmdvllthpsftsestkqpkll
hqvveqlqkvhfitdtlskgetkfmgvcqlpskndekeyphrridirlipkdqyycgvly
ftgsdifnknmrahalekgftineytirplgvtgvageplpvdsekdifdyiqwkyrepk
drse
>d1bqlh1 2.1.1.1.41 (2-116) Immunoglobulin (variable domains of L and H chains) {Fab HyHEL-5 (mouse), kappa L chain}
vqlqqsgaelmkpgasvkisckasgytfsdywiewvkqrpghglewigeilpgsgstnyh
erfkgkatftadtssstaymqlnsltsedsgvyyclhgnydfdgwgqgttltvss
>d1bqlh2 2.1.1.2.48 (117-215) Immunoglobulin (constant domains of L and H chains) {Fab HyHEL-5 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpssprpsetvtcnvahpasstkvdkkivp
>d1bqll1 2.1.1.1.41 (1-106) Immunoglobulin (variable domains of L and H chains) {Fab HyHEL-5 (mouse), kappa L chain}
divltqspaimsaspgekvtmtcsasssvnymywyqqksgtspkrwiydtsklasgvpvr
fsgsgsgtsysltissmetedaatyycqqwgrnptfgggtkleikr
>d1bqll2 2.1.1.2.48 (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
>d1bra__ 2.35.1.2.3 Trypsin(ogen) {rat (Rattus rattus)}
ivggytcqensvpyqvslnsgyhfcggslindqwvvsaahcyksriqvrlgehninvleg
neqfvnaakiikhpnfdrktlnndimliklsspvklnarvatvalpsscapagtqclisg
wgntlssgvnepdllqcldapllpqadceasypgkitdnmvcvgfleggkgscqgdsggp
vvcngelqgivswgygcalpdnpdvytkvcnyvdwiqdtiaan
>d1brbe_ 2.35.1.2.3 Trypsin(ogen) {rat (Rattus rattus)}
ivggytcqensvpyqvslnsgyhfcggslindqwvvsaahcyksriqvrlgehninvleg
neqfvnaakiikhpnfdrktlnndimliklsspvklnarvatvalpsscapagtqclisg
wgntlssgvnepdllqcldapllpqadceasypgkitdnmvcvgfleggkgscqgdsggp
vvcngelqgivswgygcalpdnpdvytkvcnyvdwiqdtiaan
>d1brbi_ 7.7.1.1.1 Pancreatic trypsin inhibitor {bovine (Bos taurus)}
ageppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrta
>d1brce_ 2.35.1.2.3 Trypsin(ogen) {rat (Rattus rattus)}
ivggytcqensvpyqvslnsgyhfcggslindqwvvsaahcyksriqvrlgehninvleg
neqfvnaakiikhpnfdrktlnndimliklsspvklnarvatvalpsscapagtqclisg
wgntlssgvnepdllqcldapllpqadceasypgkitdnmvcvgfleggkgscqgdsggp
vvcngelqgivswgygcalpdnpdvytkvcnyvdwiqdtiaan
>d1brci_ 7.7.1.1.4 Alzheimer's amyloid B-protein precursor, APPI {human (Homo sapiens)}
vrevcseqaetgpcramisrwyfdvtegkcapffyggcggnrnnfdteeycmavcg
>d1brd__ 6.5.1.1.5 Bacteriorhodopsin {(Halobacterium halobium)}
pewiwlalgtalmglgtlyflvkgmgvsdpdakkfyaittlvpaiaftmylsmllgyglt
mvpfggeqnpiywaryadwlfttplllldlallvdadqgtilalvgadgimigtglvgal
tkvysyrfvwwaistaamlyilyvlffgftskaesmrpevastfkvlrnvtvvlwsaypv
vwligsegagivplnietllfmvldvsakvgfglillrs
>d1brea_ 2.1.1.1.113 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (kappa) dimer BRE (human)}
diqmtqspsslsasvgdrvtitcqasqdisdyliwyqqklgkapnlliydastletgvps
rfsgsgsgteytftisslqpediatyycqqyddlpytfgqgtkveik
>d1breb_ 2.1.1.1.113 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (kappa) dimer BRE (human)}
diqmtqspsslsasvgdrvtitcqasqdisdyliwyqqklgkapnlliydastletgvps
rfsgsgsgteytftisslqpediatyycqqyddlpytfgqgtkveik
>d1brec_ 2.1.1.1.113 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (kappa) dimer BRE (human)}
diqmtqspsslsasvgdrvtitcqasqdisdyliwyqqklgkapnlliydastletgvps
rfsgsgsgteytftisslqpediatyycqqyddlpytfgqgtkveik
>d1bred_ 2.1.1.1.113 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (kappa) dimer BRE (human)}
diqmtqspsslsasvgdrvtitcqasqdisdyliwyqqklgkapnlliydastletgvps
rfsgsgsgteytftisslqpediatyycqqyddlpytfgqgtkveik
>d1bree_ 2.1.1.1.113 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (kappa) dimer BRE (human)}
diqmtqspsslsasvgdrvtitcqasqdisdyliwyqqklgkapnlliydastletgvps
rfsgsgsgteytftisslqpediatyycqqyddlpytfgqgtkveik
>d1bref_ 2.1.1.1.113 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (kappa) dimer BRE (human)}
diqmtqspsslsasvgdrvtitcqasqdisdyliwyqqklgkapnlliydastletgvps
rfsgsgsgteytftisslqpediatyycqqyddlpytfgqgtkveik
>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_ 3.1.13.1.1 Bacterial luciferase (alkanal monooxygenase) {(Vibrio harveyi)}
mkfgnflltyqppelsqtevmkrlvnlgkasegcgfdtvwllehhftefgllgnpyvaaa
hllgatetlnvgtaaivlptahpvrqaedvnlldqmskgrfrfgicrglydkdfrvfgtd
mdnsralmdcwydlmkegfnegyiaadnehikfpkiqlnpsaytqggapvyvvaesastt
ewaaerglpmilswiinthekkaqldlynevatehgydvtkidhclsyitsvdhdsnrak
dicrnflghwydsyvnatkifddsdqtkgydfnkgqwrdfvlkghkdtnrridysyeinp
vgtpeeciaiiqqdidatgidniccgfeangseeeiiasmklfqsdvmpylkekq
>d1brlb_ 3.1.13.1.1 Bacterial luciferase (alkanal monooxygenase) {(Vibrio harveyi)}
mkfglfflnfmnskrssdqvieemldtahyvdqlkfdtlavyenhfsnngvvgapltvag
fllgmtknakvaslnhvitthhpvrvaeeaclldqmsegrfafgfsdceksadmrffnrp
tdsqfqlfsechkiindafttgychpnndfysfpkisvnphafteggpaqfvnatskevv
ewaaklglplvfrwddsnaqrkeyaglyhevaqahgvdvsqvrhkltllvnqnvdgeaar
aearvyleefvresysntdfeqkmgellsenaigtyeestqaarvaieccgaadllmsfe
smedkaqqravidvvnani
>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_ 3.56.1.5.1 Bromoperoxidase A2 {(Streptomyces aureofaciens)}
pfitvgqenstsidlyyedhgtgqpvvlihgfplsghswerqsaalldagyrvitydrrg
fgqssqpttgydydtfaadlntvletldlqdavlvgfsmgtgevaryvssygtariakva
flaslepfllktddnpdgaapqeffdgivaavkadryafytgffndfynldenlgtrise
eavrnswntaasggffaaaaapttwytdfradipridvpalilhgtgdrtlpientarvf
hkalpsaeyvevegaphgllwthaeevntallaflak
>d1brob_ 3.56.1.5.1 Bromoperoxidase A2 {(Streptomyces aureofaciens)}
pfitvgqenstsidlyyedhgtgqpvvlihgfplsghswerqsaalldagyrvitydrrg
fgqssqpttgydydtfaadlntvletldlqdavlvgfsmgtgevaryvssygtariakva
flaslepfllktddnpdgaapqeffdgivaavkadryafytgffndfynldenlgtrise
eavrnswntaasggffaaaaapttwytdfradipridvpalilhgtgdrtlpientarvf
hkalpsaeyvevegaphgllwthaeevntallaflak
>d1brp__ 2.45.1.1.3 Retinol binding protein {human (Homo sapiens)}
erdcrvssfrvkenfdkarfsgtwyamakkdpeglflqdnivaefsvdetgqmsatakgr
vrllnnwdvcadmvgtftdtedpakfkmkywgvasflqkgnddhwivdtdydtyavqysc
rllnldgtcadsysfvfsrdpnglppeaqkivrqrqeelclarqyrlivhngycd
>d1brq__ 2.45.1.1.3 Retinol binding protein {human (Homo sapiens)}
erdcrvssfrvkenfdkarfsgtwyamakkdpeglflqdnivaefsvdetgqmsatakgr
vrllnnwdvcadmvgtftdtedpakfkmkywgvasflqkgnddhwivdtdydtyavqysc
rllnldgtcadsysfvfsrdpnglppeaqkivrqrqeelclarqyrlivhngycd
>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_ 3.6.1.1.1 Barstar (barnase inhibitor) {(Bacillus amyloliquefaciens)}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdaltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegaditiils
>d1brse_ 3.6.1.1.1 Barstar (barnase inhibitor) {(Bacillus amyloliquefaciens)}
kavingeqirsisdlhqtlkkelalpeyygenldalwdaltgwveyplvlewrqfeqskq
ltengaesvlqvfreakaegaditiils
>d1brsf_ 3.6.1.1.1 Barstar (barnase inhibitor) {(Bacillus amyloliquefaciens)}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdaltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegaditiils
>d1brt__ 3.56.1.5.1 Bromoperoxidase A2 {(Streptomyces aureofaciens)}
pfitvgqenstsidlyyedhgtgqpvvlihgfplsghswerqsaalldagyrvitydrrg
fgqssqpttgydydtfaadlntvletldlqdavlvgfstgtgevaryvssygtariakva
flaslepfllktddnpdgaapqeffdgivaavkadryafytgffndfynldenlgtrise
eavrnswntaasggffaaaaapttwytdfradipridvpalilhgtgdrtlpientarvf
hkalpsaeyvevegaphgllwthaeevntallaflak
>d1bryy_ 4.102.1.1.2 Bryodin {Red briony (Bryonia dioica)}
dvsfrlsgatttsygvfiknlrealpyerkvynipllrssisgsgrytllhltnyadeti
svavdvtnvyimgylagdvsyffneasateaakfvfkdakkkvtlpysgnyerlqtaagk
ireniplglpaldsaittlyyytassaasallvliqstaesarykfieqqigkrvdktfl
pslatislennwsalskqiqiastnngqfespvvlidgnnqrvsitnasarvvtsniall
lnrnnia
>d1bryz_ 4.102.1.1.2 Bryodin {Red briony (Bryonia dioica)}
dvsfrlsgatttsygvfiknlrealpyerkvynipllrssisgsgrytllhltnyadeti
svavdvtnvyimgylagdvsyffneasateaakfvfkdakkkvtlpysgnyerlqtaagk
ireniplglpaldsaittlyyytassaasallvliqstaesarykfieqqigkrvdktfl
pslatislennwsalskqiqiastnngqfespvvlidgnnqrvsitnasarvvtsniall
lnrnnia
>d1brz__ 7.3.6.4.4 Brazzein {J'oublie (Pentadiplandra brazzeana)}
dkckkvyenypvskcqlanqcnydckldkharsgecfydekrnlqcicdycey
>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
>d1bsla_ 3.1.13.1.1 Bacterial luciferase (alkanal monooxygenase) {(Vibrio harveyi)}
mkfglfflnfmnskrssdqvieemldtahyvdqlkfdtlavyenhfsnngvvgapltvag
fllgmtknakvaslnhvitthhpvrvaeeaclldqmsegrfafgfsdceksadmrffnrp
tdsqfqlfsechkiindafttgychpnndfysfpkisvnphafteggpaqfvnatskevv
ewaaklglplvfrwddsnaqrkeyaglyhevaqahgvdvsqvrhkltllvnqnvdgeaar
aearvyleefvresysntdfeqkmgellsenaigtyeestqaarvaieccgaadllmsfe
smedkaqqravidvvnanivkyh
>d1bslb_ 3.1.13.1.1 Bacterial luciferase (alkanal monooxygenase) {(Vibrio harveyi)}
mkfglfflnfmnskrssdqvieemldtahyvdqlkfdtlavyenhfsnngvvgapltvag
fllgmtknakvaslnhvitthhpvrvaeeaclldqmsegrfafgfsdceksadmrffnrp
tdsqfqlfsechkiindafttgychpnndfysfpkisvnphafteggpaqfvnatskevv
ewaaklglplvfrwddsnaqrkeyaglyhevaqahgvdvsqvrhkltllvnqnvdgeaar
aearvyleefvresysntdfeqkmgellsenaigtyeestqaarvaieccgaadllmsfe
smedkaqqravidvvnanivkyhs
>d1bsra_ 4.4.1.1.3 Seminal ribonucleasease {bovine (Bos taurus)}
kesaaakferqhmdsgnspssssnycnlmmccrkmtqgkckpvntfvhesladvkavcsq
kkvtckngqtncyqskstmritdcretgsskypncaykttqvekhiivacggkpsvpvhf
dasv
>d1bsrb_ 4.4.1.1.3 Seminal ribonucleasease {bovine (Bos taurus)}
kesaaakferqhmdsgnspssssnycnlmmccrkmtqgkckpvntfvhesladvkavcsq
kkvtckngqtncyqskstmritdcretgsskypncaykttqvekhiivacggkpsvpvhf
dasv
>d1bta__ 3.6.1.1.1 Barstar (barnase inhibitor) {(Bacillus amyloliquefaciens)}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdcltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegcditiils
>d1btb__ 3.6.1.1.1 Barstar (barnase inhibitor) {(Bacillus amyloliquefaciens)}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdcltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegcditiils
>d1btc__ 3.1.1.2.1 beta-Amylase {soybean (Glycine max)}
snmllnyvpvyvmlplgvvnvdnvfedpdglkeqllqlraagvdgvmvdvwwgiielkgp
kqydwrayrslfqlvqecgltlqaimsfhqcggnvgdivnipipqwvldigesnhdifyt
nrsgtrnkeyltvgvdnepifhgrtaieiysdymksfrenmsdflesgliidievglgpa
gelrypsypqsqgwefprigefqcydkylkadfkaavaraghpewelpddagkyndvpes
tgffksngtyvtekgkffltwysnkllnhgdqildeankaflgckvklaikvsgihwwyk
venhaaeltagyynlndrdgyrpiarmlsrhhailnftclemrdseqpsdaksgpqelvq
qvlsggwredirvagenalprydataynqiilnakpqgvnnngppklsmfgvtylrlsdd
llqksnfnifkkfvlkmhadqdycanpqkynhaitplkpsapkipievlleatkptlpfp
wlpetdmkvdg
>d1btga_ 7.16.1.3.3 beta-Nerve growth factor {mouse (Mus musculus)}
gefsvcdsvsvwvgdkttatdikgkevtvlaevninnsvfrqyffetkcrasnpvesgcr
gidskhwnsycttthtfvkalttdekqaawrfiridtacvcvlsrkat
>d1btgb_ 7.16.1.3.3 beta-Nerve growth factor {mouse (Mus musculus)}
gefsvcdsvsvwvgdkttatdikgkevtvlaevninnsvfrqyffetkcrasnpvesgcr
gidskhwnsycttthtfvkalttdekqaawrfiridtacvcvlsrkatr
>d1btgc_ 7.16.1.3.3 beta-Nerve growth factor {mouse (Mus musculus)}
gefsvcdsvsvwvgdkttatdikgkevtvlaevninnsvfrqyffetkcrasnpvesgcr
gidskhwnsycttthtfvkalttdekqaawrfiridtacvcvlsrkatr
>e1bth.1h 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwttnvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacqgdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvi
>e1bth.1l 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
geadcglrplfekksledkterellesyidg
>e1bth.2j 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
geadcglrplfekksledkterellesyidg
>e1bth.2k 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwttnvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacqgdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvi
>d1bthp_ 7.7.1.1.1 Pancreatic trypsin inhibitor {bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d1bthq_ 7.7.1.1.1 Pancreatic trypsin inhibitor {bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d1bti__ 7.7.1.1.1 Pancreatic trypsin inhibitor {bovine (Bos taurus)}
rpdfcleppytgpckariiryaynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d1btka_ 2.41.1.1.5 Bruton's tyrosine kinase {Human (Homo sapiens)}
aavilesiflkrsqqkkktsplnfkkclflltvhklsyyeydfergrrgskkgsidveki
tcvetvvpeknppperqiprrgeessemeqisiierfpypfqvvydegplyvfspteelr
krwihqlknvirynsdlvqkyhpcfwidgqylccsqtaknamgcqilen
>d1btkb_ 2.41.1.1.5 Bruton's tyrosine kinase {Human (Homo sapiens)}
aavilesiflkrsqqkkktsplnfkkclflltvhklsyyeydfergrrgskkgsidveki
tcvetvvpeknppperqiprrgeessemeqisiierfpypfqvvydegplyvfspteelr
krwihqlknvirynsdlvqkyhpcfwidgqylccsqtaknamgcqilen
>d1btl__ 5.4.1.1.2 beta-Lactamase TEM-1 {(Escherichia coli)}
hpetlvkvkdaedqlgarvgyieldlnsgkilesfrpeerfpmmstfkvllcgavlsrid
agqeqlgrrihysqndlveyspvtekhltdgmtvrelcsaaitmsdntaanlllttiggp
keltaflhnmgdhvtrldrwepelneaipnderdttmpvamattlrklltgelltlasrq
qlidwmeadkvagpllrsalpagwfiadksgagergsrgiiaalgpdgkpsrivviyttg
sqatmdernrqiaeigaslikhw
>d1btma_ 3.1.11.1.7 Triosephosphate isomerase {(Bacillus stearothermophilus)}
rkpiiagnwkmhktlaeavqfvedvkghvppadevisvvcapflfldrlvqaadgtdlki
gaqtmhfadqgaytgevspvmlkdlgvtyvilghserrqmfaetdetvnkkvlaaftrgl
ipiiccgesleereagqtnavvasqvekalagltpeqvkqaviayepiwaigtgksstpe
dansvcghirsvvsrlfgpeaaeairiqyggsvkpdnirdflaqqqidgplvggaslepa
sflqlveagrh
>d1btmb_ 3.1.11.1.7 Triosephosphate isomerase {(Bacillus stearothermophilus)}
rkpiiagnwkmhktlaeavqfvedvkghvppadevisvvcapflfldrlvqaadgtdlki
gaqtmhfadqgaytgevspvmlkdlgvtyvilghserrqmfaetdetvnkkvlaaftrgl
ipiiccgesleereagqtnavvasqvekalagltpeqvkqaviayepiwaigtgksstpe
dansvcghirsvvsrlfgpeaaeairiqyggsvkpdnirdflaqqqidgplvggaslepa
sflqlveagrh
>d1btn__ 2.41.1.1.2 beta-spectrin {mouse (Mus musculus) brain}
megflnrkheweahnkkassrswhnvycvinnqemgfykdaksaasgipyhsevpvslke
aicevaldykkkkhvfklrlsdgneylfqakddeemntwiqaissa
>d1btoa1 2.25.1.2.1 (1-174,325-374) Alcohol dehydrogenase {horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1btoa2 3.22.1.1.1 (175-324) Alcohol dehydrogenase {horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1btob1 2.25.1.2.1 (1-174,325-374) Alcohol dehydrogenase {horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1btob2 3.22.1.1.1 (175-324) Alcohol dehydrogenase {horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1btoc1 2.25.1.2.1 (1-174,325-374) Alcohol dehydrogenase {horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1btoc2 3.22.1.1.1 (175-324) Alcohol dehydrogenase {horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1btod1 2.25.1.2.1 (1-174,325-374) Alcohol dehydrogenase {horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1btod2 3.22.1.1.1 (175-324) Alcohol dehydrogenase {horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1btp__ 2.35.1.2.1 Trypsin(ogen) {bovine (Bos taurus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1btv__ 4.79.3.1.1 Major birch pollen allergen Bet v 1 {white birch (Betula verrucosa)}
gvfnyetettsvipaarlfkafildgdnlfpkvapqaissveniegnggpgtikkisfpe
glpfkyvkdrvdevdhtnfkynysvieggpigdtlekisneikivatpdggsilkisnky
htkgdhevkaeqvkaskemgetllravesyllahsdayn
>d1btwa_ 2.35.1.2.1 Trypsin(ogen) {bovine (Bos taurus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1btxa_ 2.35.1.2.1 Trypsin(ogen) {bovine (Bos taurus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1bty__ 2.35.1.2.1 Trypsin(ogen) {bovine (Bos taurus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1btza_ 2.35.1.2.1 Trypsin(ogen) {bovine (Bos taurus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1buca1 1.24.6.1.1 (233-383) Butyryl-CoA dehydrogenase {(Megasphaera elsdenii)}
gkgfkiammtldggrigvaaqalgiaeaaladaveyskqrvqfgkplckfqsisfkladm
kmqieaarnlvykaackkqegkpftvdaaiakrvasdvamrvtteavqifggygyseeyp
varhmrdakitqiyegtnevqlmvtggallr
>d1buca2 5.7.1.1.1 (1-232) Butyryl-CoA dehydrogenase {(Megasphaera elsdenii)}
mdfnltdiqqdflklahdfgekklaptvterdhkgiydkelidellslgitgayfeekyg
gsgddggdvlsyilaveelakydagvaitlsatvslcanpiwqfgteaqkekflvplveg
tklgafgltepnagtdasgqqtiatknddgtytlngskifitnggaadiyivfamtdksk
gnhgitafiledgtpgftygkkedkmgihtsqtmelvfqdvkvpaenmlgee
>d1bucb1 1.24.6.1.1 (233-383) Butyryl-CoA dehydrogenase {(Megasphaera elsdenii)}
gkgfkiammtldggrigvaaqalgiaeaaladaveyskqrvqfgkplckfqsisfkladm
kmqieaarnlvykaackkqegkpftvdaaiakrvasdvamrvtteavqifggygyseeyp
varhmrdakitqiyegtnevqlmvtggallr
>d1bucb2 5.7.1.1.1 (1-232) Butyryl-CoA dehydrogenase {(Megasphaera elsdenii)}
mdfnltdiqqdflklahdfgekklaptvterdhkgiydkelidellslgitgayfeekyg
gsgddggdvlsyilaveelakydagvaitlsatvslcanpiwqfgteaqkekflvplveg
tklgafgltepnagtdasgqqtiatknddgtytlngskifitnggaadiyivfamtdksk
gnhgitafiledgtpgftygkkedkmgihtsqtmelvfqdvkvpaenmlgee
>d1buna_ 1.103.1.2.13 beta2-bungarotoxin, phospholipase A2 chain {Many-banded krait (elapid) (Bungarus multicinctus)}
nlinfmemirytipcektwgeyadygcycgaggsgrpidaldrccyvhdncygdaekkhk
cnpktqsysykltkrtiicygaagtcarivcdcdrtaalcfgnseyieghknidtarfcq
>d1bunb_ 7.7.1.1.6 beta2-bungarotoxin, neurotoxin chain {Many-banded krait (elapid) (Bungarus multicinctus)}
rkrhpdcdkppdtkicqtvvrafyykpsakrcvqfryggcngngnhfksdhlcrcecley
r
>d1bura1 3.1.10.1.2 (148-475) Ribulose 1,5-bisphosphate carboxylase-oxygenase {spinach (Spinacia oleracea)}
fqgpphgiqverdklnkygrpllgctikpklglsaknygravyeclrggldftxddenvn
sqpfmrwrdrflfcaealykaqaetgeikghylnatagtcedmmkravfarelgvpivmh
dyltggftanttlshycrdnglllhihramhavidrqknhgmhfrvlakalrlsggdhih
sgtvvgklegerditlgfvdllrddytekdrsrgiyftqswvstpgvlpvasggihvwhm
palteifgddsvlqfgggtlghpwgnapgavanrvaleacvqarnegrdlaregntiire
atkwspelaaacevwkeikfefpamdtv
>d1bura2 4.34.10.1.2 (12-147) Ribulose 1,5-bisphosphate carboxylase-oxygenase {spinach (Spinacia oleracea)}
efkagvkdykltyytpeyetldtdilaafrvspqpgvppeeagaavaaesstgtwttvwt
dgltnldrykgrcyhiepvageenqyicyvaypldlfeegsvtnmftsivgnvfgfkalr
alrledlripvayvkt
>d1burb1 3.1.10.1.2 (148-475) Ribulose 1,5-bisphosphate carboxylase-oxygenase {spinach (Spinacia oleracea)}
fqgpphgiqverdklnkygrpllgctikpklglsaknygravyeclrggldftxddenvn
sqpfmrwrdrflfcaealykaqaetgeikghylnatagtcedmmkravfarelgvpivmh
dyltggftanttlshycrdnglllhihramhavidrqknhgmhfrvlakalrlsggdhih
sgtvvgklegerditlgfvdllrddytekdrsrgiyftqswvstpgvlpvasggihvwhm
palteifgddsvlqfgggtlghpwgnapgavanrvaleacvqarnegrdlaregntiire
atkwspelaaacevwkeikfefpamdtv
>d1burb2 4.34.10.1.2 (12-147) Ribulose 1,5-bisphosphate carboxylase-oxygenase {spinach (Spinacia oleracea)}
efkagvkdykltyytpeyetldtdilaafrvspqpgvppeeagaavaaesstgtwttvwt
dgltnldrykgrcyhiepvageenqyicyvaypldlfeegsvtnmftsivgnvfgfkalr
alrledlripvayvkt
>d1burc1 3.1.10.1.2 (148-475) Ribulose 1,5-bisphosphate carboxylase-oxygenase {spinach (Spinacia oleracea)}
fqgpphgiqverdklnkygrpllgctikpklglsaknygravyeclrggldftxddenvn
sqpfmrwrdrflfcaealykaqaetgeikghylnatagtcedmmkravfarelgvpivmh
dyltggftanttlshycrdnglllhihramhavidrqknhgmhfrvlakalrlsggdhih
sgtvvgklegerditlgfvdllrddytekdrsrgiyftqswvstpgvlpvasggihvwhm
palteifgddsvlqfgggtlghpwgnapgavanrvaleacvqarnegrdlaregntiire
atkwspelaaacevwkeikfefpamdtv
>d1burc2 4.34.10.1.2 (12-147) Ribulose 1,5-bisphosphate carboxylase-oxygenase {spinach (Spinacia oleracea)}
efkagvkdykltyytpeyetldtdilaafrvspqpgvppeeagaavaaesstgtwttvwt
dgltnldrykgrcyhiepvageenqyicyvaypldlfeegsvtnmftsivgnvfgfkalr
alrledlripvayvkt
>d1burd1 3.1.10.1.2 (148-475) Ribulose 1,5-bisphosphate carboxylase-oxygenase {spinach (Spinacia oleracea)}
fqgpphgiqverdklnkygrpllgctikpklglsaknygravyeclrggldftxddenvn
sqpfmrwrdrflfcaealykaqaetgeikghylnatagtcedmmkravfarelgvpivmh
dyltggftanttlshycrdnglllhihramhavidrqknhgmhfrvlakalrlsggdhih
sgtvvgklegerditlgfvdllrddytekdrsrgiyftqswvstpgvlpvasggihvwhm
palteifgddsvlqfgggtlghpwgnapgavanrvaleacvqarnegrdlaregntiire
atkwspelaaacevwkeikfefpamdtv
>d1burd2 4.34.10.1.2 (12-147) Ribulose 1,5-bisphosphate carboxylase-oxygenase {spinach (Spinacia oleracea)}
efkagvkdykltyytpeyetldtdilaafrvspqpgvppeeagaavaaesstgtwttvwt
dgltnldrykgrcyhiepvageenqyicyvaypldlfeegsvtnmftsivgnvfgfkalr
alrledlripvayvkt
>d1burs_ 4.38.1.1.2 Ribulose 1,5-bisphosphate carboxylase-oxygenase {spinach (Spinacia oleracea)}
mqvwpilgmkkyetlsylppltteqllaevnyllvnnwipclefevkdgfvyrehlkspg
yydgrywtmwklpmfgctdpaqvlneleeckkaypdafiriigfdnkrqvqcisfiaykp
agy
>d1burt_ 4.38.1.1.2 Ribulose 1,5-bisphosphate carboxylase-oxygenase {spinach (Spinacia oleracea)}
mqvwpilgmkkyetlsylppltteqllaevnyllvnnwipclefevkdgfvyrehhkspg
yydgrywtmwklpmfgctdpaqvlneleeckkaypdafiriigfdnkrqvqcisfiaykp
agy
>d1buru_ 4.38.1.1.2 Ribulose 1,5-bisphosphate carboxylase-oxygenase {spinach (Spinacia oleracea)}
mqvwpilgmkkyetlsylppltteqllaevnyllvnnwipclefevkdgfvyrehlkspg
yydgrywtmwklpmfgctdpaqvlneleeckkaypdafiriigfdnkrqvqcisfiaykp
agy
>d1burv_ 4.38.1.1.2 Ribulose 1,5-bisphosphate carboxylase-oxygenase {spinach (Spinacia oleracea)}
mqvwpilgmkkyetlsylppltteqllaevnyllvnnwipclefevkdgfvyrehhkspg
yydgrywtmwklpmfgctdpaqvlneleeckkaypdafiriigfdnkrqvqcisfiaykp
agy
>d1bus__ 7.14.1.1.8 Seminal plasma inhibitor IIa {bovine (Bos taurus)}
xgaqvdcaefkdpkvyctresnphcgsngetygnkcafckavmksggkinlkhrgkc
>d1buz__ 3.8.2.1.1 SpoIIaa {(Bacillus subtilis)}
slgidmnvkesvlcirltgeldhhtaetlkqkvtqslekddirhivlnledlsfmdssgl
gvilgrykqikqiggemvvcaispavkrlfdmsglfkiirfeqseqqalltlgvas
>d1bv1__ 4.79.3.1.1 Major birch pollen allergen Bet v 1 {white birch (Betula verrucosa)}
gvfnyetettsvipaarlfkafildgdnlfpkvapqaissveniegnggpgtikkisfpe
glpfkyvkdrvdevdhtnfkynysvieggpigdtlekisneikivatpdggsilkisnky
htkgdhevkaeqvkaskemgetllravesyllahsdayn
>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_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigatlnf
>d1bveb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigatlnf
>d1bvga_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigatlnf
>d1bvgb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigatlnf
>d1bvh__ 3.36.1.1.1 Tyrosine phosphatase {bovine (Bos taurus)}
aeqvtksvlfvclgnicrspiaeavfrklvtdqnisdnwvidsgavsdwnvgrspdprav
sclrnhgintahkarqvtkedfvtfdyilcmdesnlrdlnrksnqvkncrakiellgsyd
pqkqliiedpyygndadfetvyqqcvrccraflekvr
>d1bvp11 1.89.1.1.1 (1-120,255-349) Bluetongue virus coat protein vp7 (BTV-10 vp7), alpha-helical domain {(Bluetongue virus)}
mdtiaaraltvmracatlqearivleanvmeilgiainryngltlrgvtmrptslaqrne
mffmcldmmlsaaginvgpispdytqhmatigvlatpeipftteaaneiarvtgetstwg
Xktlnqypaltaeifnvysfrdhtwhglrtailnrttlpnmlppifppndrdsiltllll
stladvytvlrpefaihgvnpmpgpltraiaraayv
>d1bvp12 2.14.1.1.1 (121-254) Virus coat protein vp7 (BTV-10 vp7), central (top) domain {(Bluetongue virus)}
parqpygffleteetfqpgrwfmraaqavtavvcgpdmiqvslnagargdvqqifqgrnd
pmmiylvwrrienfamaqgnsqqtqagvtvsvggvdmragriiawdgqaalhvhnptqqn
amvqiqvvfyismd
>d1bvp21 1.89.1.1.1 (1-120,255-349) Bluetongue virus coat protein vp7 (BTV-10 vp7), alpha-helical domain {(Bluetongue virus)}
mdtiaaraltvmracatlqearivleanvmeilgiainryngltlrgvtmrptslaqrne
mffmcldmmlsaaginvgpispdytqhmatigvlatpeipftteaaneiarvtgetstwg
Xktlnqypaltaeifnvysfrdhtwhglrtailnrttlpnmlppifppndrdsiltllll
stladvytvlrpefaihgvnpmpgpltraiaraayv
>d1bvp22 2.14.1.1.1 (121-254) Virus coat protein vp7 (BTV-10 vp7), central (top) domain {(Bluetongue virus)}
parqpygffleteetfqpgrwfmraaqavtavvcgpdmiqvslnagargdvqqifqgrnd
pmmiylvwrrienfamaqgnsqqtqagvtvsvggvdmragriiawdgqaalhvhnptqqn
amvqiqvvfyismd
>d1bvp31 1.89.1.1.1 (1-120,255-349) Bluetongue virus coat protein vp7 (BTV-10 vp7), alpha-helical domain {(Bluetongue virus)}
mdtiaaraltvmracatlqearivleanvmeilgiainryngltlrgvtmrptslaqrne
mffmcldmmlsaaginvgpispdytqhmatigvlatpeipftteaaneiarvtgetstwg
Xktlnqypaltaeifnvysfrdhtwhglrtailnrttlpnmlppifppndrdsiltllll
stladvytvlrpefaihgvnpmpgpltraiaraayv
>d1bvp32 2.14.1.1.1 (121-254) Virus coat protein vp7 (BTV-10 vp7), central (top) domain {(Bluetongue virus)}
parqpygffleteetfqpgrwfmraaqavtavvcgpdmiqvslnagargdvqqifqgrnd
pmmiylvwrrienfamaqgnsqqtqagvtvsvggvdmragriiawdgqaalhvhnptqqn
amvqiqvvfyismd
>d1bvp41 1.89.1.1.1 (1-120,255-349) Bluetongue virus coat protein vp7 (BTV-10 vp7), alpha-helical domain {(Bluetongue virus)}
mdtiaaraltvmracatlqearivleanvmeilgiainryngltlrgvtmrptslaqrne
mffmcldmmlsaaginvgpispdytqhmatigvlatpeipftteaaneiarvtgetstwg
Xktlnqypaltaeifnvysfrdhtwhglrtailnrttlpnmlppifppndrdsiltllll
stladvytvlrpefaihgvnpmpgpltraiaraayv
>d1bvp42 2.14.1.1.1 (121-254) Virus coat protein vp7 (BTV-10 vp7), central (top) domain {(Bluetongue virus)}
parqpygffleteetfqpgrwfmraaqavtavvcgpdmiqvslnagargdvqqifqgrnd
pmmiylvwrrienfamaqgnsqqtqagvtvsvggvdmragriiawdgqaalhvhnptqqn
amvqiqvvfyismd
>d1bvp51 1.89.1.1.1 (1-120,255-349) Bluetongue virus coat protein vp7 (BTV-10 vp7), alpha-helical domain {(Bluetongue virus)}
mdtiaaraltvmracatlqearivleanvmeilgiainryngltlrgvtmrptslaqrne
mffmcldmmlsaaginvgpispdytqhmatigvlatpeipftteaaneiarvtgetstwg
Xktlnqypaltaeifnvysfrdhtwhglrtailnrttlpnmlppifppndrdsiltllll
stladvytvlrpefaihgvnpmpgpltraiaraayv
>d1bvp52 2.14.1.1.1 (121-254) Virus coat protein vp7 (BTV-10 vp7), central (top) domain {(Bluetongue virus)}
parqpygffleteetfqpgrwfmraaqavtavvcgpdmiqvslnagargdvqqifqgrnd
pmmiylvwrrienfamaqgnsqqtqagvtvsvggvdmragriiawdgqaalhvhnptqqn
amvqiqvvfyismd
>d1bvp61 1.89.1.1.1 (1-120,255-349) Bluetongue virus coat protein vp7 (BTV-10 vp7), alpha-helical domain {(Bluetongue virus)}
mdtiaaraltvmracatlqearivleanvmeilgiainryngltlrgvtmrptslaqrne
mffmcldmmlsaaginvgpispdytqhmatigvlatpeipftteaaneiarvtgetstwg
Xktlnqypaltaeifnvysfrdhtwhglrtailnrttlpnmlppifppndrdsiltllll
stladvytvlrpefaihgvnpmpgpltraiaraayv
>d1bvp62 2.14.1.1.1 (121-254) Virus coat protein vp7 (BTV-10 vp7), central (top) domain {(Bluetongue virus)}
parqpygffleteetfqpgrwfmraaqavtavvcgpdmiqvslnagargdvqqifqgrnd
pmmiylvwrrienfamaqgnsqqtqagvtvsvggvdmragriiawdgqaalhvhnptqqn
amvqiqvvfyismd
>d1bw3__ 2.39.1.2.1 Barwin {barley (Hordeum vulgare)}
eqandvratyhyyrpaqnnwdlgapavsaycatwdaskplswrskygwtafcgpagprgq
aacgkclrvtnpatgaqitarivdqcanggldldwdtvftkidtngigyqqghlnvnyqf
vdcrd
>d1bw4__ 2.39.1.2.1 Barwin {barley (Hordeum vulgare)}
eqandvratyhyyrpaqnnwdlgapavsaycatwdaskplswrskygwtafcgpagprgq
aacgkclrvtnpatgaqitarivdqcanggldldwdtvftkidtngigyqqghlnvnyqf
vdcrd
>d1bxla_ 6.1.4.1.1 Apoptosis regulator Bcl-xL {Human (Homo sapiens)}
msmamsqsnrelvvdflsyklsqkgyswsqfsdveenrteapegteseavkqalreagde
felryrrafsdltsqlhitpgtayqsfeqvvnelfrdgvnwgrivaffsfggalcvesvd
kemqvlvsriaawmatylndhlepwiqenggwdtfvelygnnaaaesrkgqerlehhhhh
h
>d1bya__ 3.1.1.2.1 beta-Amylase {soybean (Glycine max)}
snmllnyvpvyvmlplgvvnvdnvfedpdglkeqllqlraagvdgvmvdvwwgiielkgp
kqydwrayrslfqlvqecgltlqaimsfhqcggnvgdivnipipqwvldigesnhdifyt
nrsgtrnkeyltvgvdnepifhgrtaieiysdymksfrenmsdflesgliidievglgpa
gelrypsypqsqgwefprigefqcydkylkadfkaavaraghpewelpddagkyndvpes
tgffksngtyvtekgkffltwysnkllnhgdqildeankaflgckvklaikvsgihwwyk
venhaaeltagyynlndrdgyrpiarmlsrhhailnftclemrdseqpsdaksgpqelvq
qvlsggwredirvagenalprydataynqiilnakpqgvnnngppklsmfgvtylrlsdd
llqksnfnifkkfvlkmhadqdycanpqkynhaitplkpsapkipievlleatkptlpfp
wlpetdmkvdg
>d1byb__ 3.1.1.2.1 beta-Amylase {soybean (Glycine max)}
snmllnyvpvyvmlplgvvnvdnvfedpdglkeqllqlraagvdgvmvdvwwgiielkgp
kqydwrayrslfqlvqecgltlqaimsfhqcggnvgdivnipipqwvldigesnhdifyt
nrsgtrnkeyltvgvdnepifhgrtaieiysdymksfrenmsdflesgliidievglgpa
gelrypsypqsqgwefprigefqcydkylkadfkaavaraghpewelpddagkyndvpes
tgffksngtyvtekgkffltwysnkllnhgdqildeankaflgckvklaikvsgihwwyk
venhaaeltagyynlndrdgyrpiarmlsrhhailnftclemrdseqpsdaksgpqelvq
qvlsggwredirvagenalprydataynqiilnakpqgvnnngppklsmfgvtylrlsdd
llqksnfnifkkfvlkmhadqdycanpqkynhaitplkpsapkipievlleatkptlpfp
wlpetdmkvdg
>d1byc__ 3.1.1.2.1 beta-Amylase {soybean (Glycine max)}
snmllnyvpvyvmlplgvvnvdnvfedpdglkeqllqlraagvdgvmvdvwwgiielkgp
kqydwrayrslfqlvqecgltlqaimsfhqcggnvgdivnipipqwvldigesnhdifyt
nrsgtrnkeyltvgvdnepifhgrtaieiysdymksfrenmsdflesgliidievglgpa
gelrypsypqsqgwefprigefqcydkylkadfkaavaraghpewelpddagkyndvpes
tgffksngtyvtekgkffltwysnkllnhgdqildeankaflgckvklaikvsgihwwyk
venhaaeltagyynlndrdgyrpiarmlsrhhailnftclemrdseqpsdaksgpqelvq
qvlsggwredirvagenalprydataynqiilnakpqgvnnngppklsmfgvtylrlsdd
llqksnfnifkkfvlkmhadqdycanpqkynhaitplkpsapkipievlleatkptlpfp
wlpetdmkvdg
>d1byd__ 3.1.1.2.1 beta-Amylase {soybean (Glycine max)}
snmllnyvpvyvmlplgvvnvdnvfedpdglkeqllqlraagvdgvmvdvwwgiielkgp
kqydwrayrslfqlvqecgltlqaimsfhqcggnvgdivnipipqwvldigesnhdifyt
nrsgtrnkeyltvgvdnepifhgrtaieiysdymksfrenmsdflesgliidievglgpa
gelrypsypqsqgwefprigefqcydkylkadfkaavaraghpewelpddagkyndvpes
tgffksngtyvtekgkffltwysnkllnhgdqildeankaflgckvklaikvsgihwwyk
venhaaeltagyynlndrdgyrpiarmlsrhhailnftclemrdseqpsdaksgpqelvq
qvlsggwredirvagenalprydataynqiilnakpqgvnnngppklsmfgvtylrlsdd
llqksnfnifkkfvlkmhadqdycanpqkynhaitplkpsapkipievlleatkptlpfp
wlpetdmkvdg
>d1byh__ 2.21.1.2.2 Bacillus 1-3,1-4-beta-glucanase {hybrid protein: residues 1-16 from (Bacillus amyloliquefaciens) and (Bacillus macerans)}
qtggsffepfnsynsgtwekadgysnggvfnctwrannvnftndgklklgltssaynkfd
caeyrstniygyglyevsmkpakntgivssfftytgpahgtqwdeidieflgkdttkvqf
nyytngvgghekvislgfdaskgfhtyafdwqpgyikwyvdgvlkhtatanipstpgkim
mnlwngtgvddwlgsynganplyaeydwvkytsn
>d1bzm__ 2.56.1.1.1 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme I}
aspdwgyddkngpeqwsklypiangnnqspvdiktsetkhdtslkpisvsynpatakeii
nvghsfhvnfedndnrsvlkggpfsdsyrlfqfhfhwgstnehgsehtvdgvkysaelhv
ahwnsakysslaeaaskadglavigvlmkvgeanpklqkvldalqaiktkgkrapftnfd
pstllpssldfwtypgslthpplyesvtwiickesisvsseqlaqfrsllsnvegdnavp
mqhnnrptqplkgrtvrasf
>d1c2ra_ 1.3.1.1.12 Cytochrome c2 {(Rhodobacter capsulatus)}
gdaakgekefnkcktchsiiapdgteivkgaktgpnlygvvgrtagtypefkykdsival
gasgfawteediatyvkdpgaflkeklddkkaktgmafklakggedvaaylasvvk
>d1c2rb_ 1.3.1.1.12 Cytochrome c2 {(Rhodobacter capsulatus)}
gdaakgekefnkcktchsiiapdgteivkgaktgpnlygvvgrtagtypefkykdsival
gasgfawteediatyvkdpgaflkeklddkkaktgmafklakggedvaaylasvvk
>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__ 1.45.1.1.2 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
>e1ca0.1b 2.35.1.2.7 (alpha, gamma-)chymotrypsin(ogen) {bovine (Bos taurus)}
ivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgvttsdvvvagefdqgs
ssekiqklkiakvfknskynsltinnditllklstaasfsqtvsavclpsasddfaagtt
cvttgwgltry
>e1ca0.1c 2.35.1.2.7 (alpha, gamma-)chymotrypsin(ogen) {bovine (Bos taurus)}
antpdrlqqaslpllsntnckkywgtkikdamicagasgvsscmgdsggplvckkngawt
lvgivswgsstcststpgvyarvtalvnwvqqtlaan
>e1ca0.2g 2.35.1.2.7 (alpha, gamma-)chymotrypsin(ogen) {bovine (Bos taurus)}
ivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgvttsdvvvagefdqgs
ssekiqklkiakvfknskynsltinnditllklstaasfsqtvsavclpsasddfaagtt
cvttgwgltry
>e1ca0.2h 2.35.1.2.7 (alpha, gamma-)chymotrypsin(ogen) {bovine (Bos taurus)}
antpdrlqqaslpllsntnckkywgtkikdamicagasgvsscmgdsggplvckkngawt
lvgivswgsstcststpgvyarvtalvnwvqqtlaan
>d1ca0d_ 7.7.1.1.4 Alzheimer's amyloid B-protein precursor, APPI {human (Homo sapiens)}
evcseqaetgpcramisrwyfdvtegkcapffyggcggnrnnfdteeycmavcg
>d1ca0i_ 7.7.1.1.4 Alzheimer's amyloid B-protein precursor, APPI {human (Homo sapiens)}
evcseqaetgpcramisrwyfdvtegkcapffyggcggnrnnfdteeycmavcg
>d1ca2__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasf
>d1ca3__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1caa__ 7.35.4.1.5 Rubredoxin {(Pyrococcus furiosus)}
akwvckicgyiydedagdpdngispgtkfeelpddwvcpicgapksefekled
>d1cad__ 7.35.4.1.5 Rubredoxin {(Pyrococcus furiosus)}
akwvckicgyiydedagdpdngispgtkfeelpddwvcpicgapksefekled
>d1cah__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
hhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnn
ghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvh
wntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprg
llpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvd
nwrpaqplknrqikasfk
>d1cai__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
hhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnn
ghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsahtvdkkkyaaelhlvh
wntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprg
llpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvd
nwrpaqplknrqikasfk
>d1caj__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
hhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnn
ghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsdhtvdkkkyaaelhlvh
wntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprg
llpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvd
nwrpaqplknrqikasfk
>d1cak__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
hhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnn
ghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsqhtvdkkkyaaelhlvh
wntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprg
llpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvd
nwrpaqplknrqikasfk
>d1cal__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
hhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnn
ghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvh
wntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprg
llpesldywtypgslatppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvd
nwrpaqplknrqikasfk
>d1cam__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
hhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnn
ghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvh
wntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprg
llpesldywtypgslatppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvd
nwrpaqplknrqikasfk
>d1can__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
xshhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslril
nnghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhl
vhwntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdp
rgllpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelm
vdnwrpaqplknrqikasfk
>d1cao__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
xshhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslril
nnghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhl
vhwntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdp
rgllpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelm
vdnwrpaqplknrqikasfk
>d1caua_ 2.64.1.1.2 Canavalin 7S vicilin {jack bean plant (Canavalia ensiformis)}
aqnnpylfrsnkfltlfknqhgslrllqrfnedteklenlrdyrvleycskpntlllphh
sdsdllvlvlegqailvlvnpdgrdtykldqgdaikiqagtpfylinpdnnqnlrilkfa
itfrrpgtvedfflsstkrlpsylsafsknfleasydspydeieqtllqeeqegvivkmp
k
>d1caub_ 2.64.1.1.2 Canavalin 7S vicilin {jack bean plant (Canavalia ensiformis)}
tlssqdkpfnlrsrdpiysnnygklyeitpeknsqlrdldillnclqmnegalfvphyns
ratvilvanegraevelvgleqqqqqglesmqlrryaatlsegdiivipssfpvalkaas
dlnmvgigvnaennernflaghkenvirqiprqvsdltfpgsgeeveellenqkesyfvd
gqpr
>d1cava_ 2.64.1.1.2 Canavalin 7S vicilin {jack bean plant (Canavalia ensiformis)}
aqnnpylfrsnkfltlfknqhgslrllqrfnedteklenlrdyrvleycskpntlllphh
sdsdllvlvlegqailvlvnpdgrdtykldqgdaikiqagtpfylinpdnnqnlrilkfa
itfrrpgtvedfflsstkrlpsylsafsknfleasydspydeieqtllqeeqegvivkmp
k
>d1cavb_ 2.64.1.1.2 Canavalin 7S vicilin {jack bean plant (Canavalia ensiformis)}
tlssqdkpfnlrsrdpiysnnygklyeitpeknsqlrdldillnclqmnegalfvphyns
ratvilvanegraevelvgleqqqqqglesmqlrryaatlsegdiivipssfpvalkaas
dlnmvgigvnaennernflaghkenvirqiprqvsdltfpgsgeeveellenqkesyfvd
gqpr
>d1cawa_ 2.64.1.1.2 Canavalin 7S vicilin {jack bean plant (Canavalia ensiformis)}
aqnnpylfrsnkfltlfknqhgslrllqrfnedteklenlrdyrvleycskpntlllphh
sdsdllvlvlegqailvlvnpdgrdtykldqgdaikiqagtpfylinpdnnqnlrilkfa
itfrrpgtvedfflsstkrlpsylsafsknfleasydspydeieqtllqeeqegvivkmp
k
>d1cawb_ 2.64.1.1.2 Canavalin 7S vicilin {jack bean plant (Canavalia ensiformis)}
tlssqdkpfnlrsrdpiysnnygklyeitpeknsqlrdldillnclqmnegalfvphyns
ratvilvanegraevelvgleqqqqqglesmqlrryaatlsegdiivipssfpvalkaas
dlnmvgigvnaennernflaghkenvirqiprqvsdltfpgsgeeveellenqkesyfvd
gqpr
>d1caxa_ 2.64.1.1.2 Canavalin 7S vicilin {jack bean plant (Canavalia ensiformis)}
aqnnpylfrsnkfltlfknqhgslrllqrfnedteklenlrdyrvleycskpntlllphh
sdsdllvlvlegqailvlvnpdgrdtykldqgdaikiqagtpfylinpdnnqnlrilkfa
itfrrpgtvedfflsstkrlpsylsafsknfleasydspydeieqtllqeeqegvivkmp
k
>d1caxb_ 2.64.1.1.2 Canavalin 7S vicilin {jack bean plant (Canavalia ensiformis)}
tlssqdkpfnlrsrdpiysnnygklyeitpeknsqlrdldillnclqmnegalfvphyns
ratvilvanegraevelvgleqqqqqglesmqlrryaatlsegdiivipssfpvalkaas
dlnmvgigvnaennernflaghkenvirqiprqvsdltfpgsgeeveellenqkesyfvd
gqpr
>d1caxc_ 2.64.1.1.2 Canavalin 7S vicilin {jack bean plant (Canavalia ensiformis)}
aqnnpylfrsnkfltlfknqhgslrllqrfnedteklenlrdyrvleycskpntlllphh
sdsdllvlvlegqailvlvnpdgrdtykldqgdaikiqagtpfylinpdnnqnlrilkfa
itfrrpgtvedfflsstkrlpsylsafsknfleasydspydeieqtllqeeqegvivkmp
k
>d1caxd_ 2.64.1.1.2 Canavalin 7S vicilin {jack bean plant (Canavalia ensiformis)}
tlssqdkpfnlrsrdpiysnnygklyeitpeknsqlrdldillnclqmnegalfvphyns
ratvilvanegraevelvgleqqqqqglesmqlrryaatlsegdiivipssfpvalkaas
dlnmvgigvnaennernflaghkenvirqiprqvsdltfpgsgeeveellenqkesyfvd
gqpr
>d1caxe_ 2.64.1.1.2 Canavalin 7S vicilin {jack bean plant (Canavalia ensiformis)}
aqnnpylfrsnkfltlfknqhgslrllqrfnedteklenlrdyrvleycskpntlllphh
sdsdllvlvlegqailvlvnpdgrdtykldqgdaikiqagtpfylinpdnnqnlrilkfa
itfrrpgtvedfflsstkrlpsylsafsknfleasydspydeieqtllqeeqegvivkmp
k
>d1caxf_ 2.64.1.1.2 Canavalin 7S vicilin {jack bean plant (Canavalia ensiformis)}
tlssqdkpfnlrsrdpiysnnygklyeitpeknsqlrdldillnclqmnegalfvphyns
ratvilvanegraevelvgleqqqqqglesmqlrryaatlsegdiivipssfpvalkaas
dlnmvgigvnaennernflaghkenvirqiprqvsdltfpgsgeeveellenqkesyfvd
gqpr
>d1cay__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
hhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnn
ghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvh
wntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprg
llpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvd
nwrpaqplknrqikasfk
>d1caz__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
hhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnn
ghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsqhtvdkkkyaaelhlvh
wntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprg
llpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvd
nwrpaqplknrqikasfk
>d1cb1__ 1.37.1.1.2 Calbindin D9K {porcine (Sus scrofa)}
saqkspaelksifekyaakegdpnqlskeelkqliqaefpsllkgprtlddlfqeldkng
dgevsfeefqvlvkkisq
>d1cb2a_ 3.2.1.1.2 Cellobiohydrolase II {(Trichoderma reesei)}
tatysgnpfvgvtpwanayyasevsslaipsltgamataaaavakvpsfmwldtldktpl
meqtladirtanknggnyagqfvvfdlpdrdcaalasngeysiadggvakyknyidtirq
ivveysdirtllviepdslanlvtnlgtpkcanaqsaylecinyavtqlnlpnvamylda
ghagwlgwpanqdpaaqlfanvyknasspralrglatnvanyngwnitsppsytqgnavy
neklyihaigpllanhgwsnaffitdqgrsgkqptgqqqwgdwcnvigtgfgirpsantg
dslldsfvwvkpggecdgtsdssaprfdshcalpdalqpapqagawfqayfvqlltnanp
sfl
>d1cb2b_ 3.2.1.1.2 Cellobiohydrolase II {(Trichoderma reesei)}
tatysgnpfvgvtpwanayyasevsslaipsltgamataaaavakvpsfmwldtldktpl
meqtladirtanknggnyagqfvvfdlpdrdcaalasngeysiadggvakyknyidtirq
ivveysdirtllviepdslanlvtnlgtpkcanaqsaylecinyavtqlnlpnvamylda
ghagwlgwpanqdpaaqlfanvyknasspralrglatnvanyngwnitsppsytqgnavy
neklyihaigpllanhgwsnaffitdqgrsgkqptgqqqwgdwcnvigtgfgirpsantg
dslldsfvwvkpggecdgtsdssaprfdshcalpdalqpapqagawfqayfvqlltnanp
sfl
>d1cbg__ 3.1.1.4.2 Cyanogenic beta glucosidase {Creeping white clover (Trfolium repens)}
fkplpisfddfsdlnrscfapgfvfgtassafqyegaafedgkgpsiwdtfthkypekik
drtngdvaideyhrykedigimkdmnldayrfsiswprvlpkgklsggvnreginyynnl
inevlangmqpyvtlfhwdvpqaledeyrgflgrnivddfrdyaelcfkefgdrvkhwit
lnepwgvsmnayaygtfapgrcsdwlklnctggdsgrepylaahyqllahaaaarlyktk
yqasqngiigitlvshwfepaskekadvdaakrgldfmlgwfmhpltkgrypesmrylvr
krlpkfsteeskeltgsfdflglnyyssyyaakapripnarpaiqtdslinatfehngkp
lgpmaasswlciypqgirklllyvknhynnpviyitengrnefndptlslqeslldtpri
dyyyrhlyyvltaigdgvnvkgyfawslfdnmewdsgytvrfglvfvdfknnlkrhpkls
ahwfksflkk
>d1cbh__ 7.3.7.1.1 Cellobiohydrolase I {ct-cbh I from (Trichoderma reesei)}
tqshygqcggigysgptvcasgttcqvlnpyysqcl
>d1cbia_ 2.45.1.2.7 Cellular retinoic-acid-binding protein (CRABP) {bovine/murine (identical sequences) (Bos taurus/Mus musculus) CRABP-I}
pnfagtwkmrssenfdellkalgvnamlrkvavaaaskphveirqdgdqfyiktsttvrt
teinfkvgegfeeetvdgrkcrslptwenenkihctqtllegdgpktywtrelandelil
tfgaddvvctriyvre
>d1cbib_ 2.45.1.2.7 Cellular retinoic-acid-binding protein (CRABP) {bovine/murine (identical sequences) (Bos taurus/Mus musculus) CRABP-I}
pnfagtwkmrssenfdellkalgvnamlrkvavaaaskphveirqdgdqfyiktsttvrt
teinfkvgegfeeetvdgrkcrslptwenenkihctqtllegdgpktywtrelandelil
tfgaddvvctriyvre
>d1cbla_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1cblb_ 1.1.1.1.25 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_ 1.1.1.1.25 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_ 1.1.1.1.25 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_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1cbn__ 7.12.1.1.1 Crambin {abyssinian cabbage (Crambe abyssinica)}
ttccpsivarsnfnvcrlpgtpealcatytgciiipgatcpgdyan
>d1cbq__ 2.45.1.2.6 Cellular retinoic-acid-binding protein (CRABP) {Human (Homo sapiens) CRABP-II}
pnfsgnwkiirsenfeellkvlgvnvmlrkiavaaaskpaveikqegdtfyiktsttvrt
teinfkvgeefeeqtvdgrpckslvkwesenkmvceqkllkgegpktswtreltndgeli
ltmtaddvvctrvyvre
>d1cbra_ 2.45.1.2.7 Cellular retinoic-acid-binding protein (CRABP) {bovine/murine (identical sequences) (Bos taurus/Mus musculus) CRABP-I}
pnfagtwkmrssenfdellkalgvnamlrkvavaaaskphveirqdgdqfyiktsttvrt
teinfkvgegfeeetvdgrkcrslptwenenkihctqtllegdgpktywtrelandelil
tfgaddvvctriyvre
>d1cbrb_ 2.45.1.2.7 Cellular retinoic-acid-binding protein (CRABP) {bovine/murine (identical sequences) (Bos taurus/Mus musculus) CRABP-I}
pnfagtwkmrssenfdellkalgvnamlrkvavaaaskphveirqdgdqfyiktsttvrt
teinfkvgegfeeetvdgrkcrslptwenenkihctqtllegdgpktywtrelandelil
tfgaddvvctriyvre
>d1cbs__ 2.45.1.2.6 Cellular retinoic-acid-binding protein (CRABP) {Human (Homo sapiens) CRABP-II}
pnfsgnwkiirsenfeellkvlgvnvmlrkiavaaaskpaveikqegdtfyiktsttvrt
teinfkvgeefeeqtvdgrpckslvkwesenkmvceqkllkgegpktswtreltndgeli
ltmtaddvvctrvyvre
>d1cbvh1 2.1.1.1.31 (1-122) Immunoglobulin (variable domains of L and H chains) {Fab BV04-01 (mouse), kappa L chain}
evqpvetggglvqpkgslklscaasgfsfntnamnwvrqapgkglewvarirsksnnyat
yyadsvkdrftisrddsqnmlylqmnnlktedtamyycvrdqtgtawfaywgqgtlvtvs
aa
>d1cbvh2 2.1.1.2.39 (123-219) Immunoglobulin (constant domains of L and H chains) {Fab BV04-01 (mouse), kappa L chain}
kttppsvyplapgcgdttgssvtlgclvkgyfpesvtvtwnsgslsssvhtfpallqsgl
ytmsssvtvpsstwpsqtvtcsvahpassttvdkkle
>d1cbvl1 2.1.1.1.31 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab BV04-01 (mouse), kappa L chain}
dvvmtqtplslpvslgdqasiscrssqslvhsngntylhwylqkpgqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyfcsqsthvpltfgagtklelk
>d1cbvl2 2.1.1.2.39 (113-219) Immunoglobulin (constant domains of L and H chains) {Fab BV04-01 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>e1cbw.1b 2.35.1.2.7 (alpha, gamma-)chymotrypsin(ogen) {bovine (Bos taurus)}
ivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgvttsdvvvagefdqgs
ssekiqklkiakvfknskynsltinnditllklstaasfsqtvsavclpsasddfaagtt
cvttgwgltry
>e1cbw.1c 2.35.1.2.7 (alpha, gamma-)chymotrypsin(ogen) {bovine (Bos taurus)}
antpdrlqqaslpllsntnckkywgtkikdamicagasgvsscmgdsggplvckkngawt
lvgivswgsstcststpgvyarvtalvnwvqqtlaan
>e1cbw.2g 2.35.1.2.7 (alpha, gamma-)chymotrypsin(ogen) {bovine (Bos taurus)}
ivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgvttsdvvvagefdqgs
ssekiqklkiakvfknskynsltinnditllklstaasfsqtvsavclpsasddfaagtt
cvttgwgltry
>e1cbw.2h 2.35.1.2.7 (alpha, gamma-)chymotrypsin(ogen) {bovine (Bos taurus)}
antpdrlqqaslpllsntnckkywgtkikdamicagasgvsscmgdsggplvckkngawt
lvgivswgsstcststpgvyarvtalvnwvqqtlaan
>d1cbwd_ 7.7.1.1.1 Pancreatic trypsin inhibitor {bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d1cbwi_ 7.7.1.1.1 Pancreatic trypsin inhibitor {bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d1cbx__ 3.58.4.1.1 Carboxypeptidase A {bovine (Bos taurus)}
arstntfnyatyhtldeiydfmdllvaehpqlvsklqigrsyegrpiyvlkfstggsnrp
aiwidlgihsrewitqatgvwfakkftenygqnpsftaildsmdifleivtnpngfafth
senrlwrktrsvtssslcvgvdanrnwdagfgkagassspcsetyhgkyansevevksiv
dfvknhgnfkaflsihsysqlllypygyttqsipdktelnqvaksavaalkslygtsyky
gsiittiyqasggsidwsynqgikysftfelrdtgrygfllpasqiiptaqetwlgvlti
mehtvnn
>d1cby__ 4.60.1.1.1 Mosquitocidal delta-endotoxin CytB {(Bacillus thuringiensis), strain Kyushuensis}
csapiirkpfkhivltvpssdldnfntvfyvqpqyinqalhlanafqgaidplnlnfnfe
kalqiangipnsaivktlnqsviqqtveisvmveqlkkiiqevlglvinstsfwnsveat
ikgtftnldtqideawifwhslsahntsyyynilfsiqnedtgavmavlplafevsvdve
kqkvlfftikdsaryevkmkaltlvqalhssnapivdifnvnnynly
>d1cc5__ 1.3.1.1.17 Cytochrome c5 {(Azotobacter vinelandii)}
gggarsgddvvakycnachgtgllnapkvgdsaawktradakggldgllaqslsglnamp
pkgtcadcsddelkaaigkmsgl
>d1cca__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpwgaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1ccb__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpwgaannvftnefylnllnedwklekndanneqwdsksgymmlpteysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1ccc__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpwgaannvftnefylnllnedwklekndanneqwdsksgymmlptaysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1ccd__ 1.80.1.1.2 Clara cell 17kDa protein {rat (Rattus rattus)}
ssdicpgflqvlealllgsesnyeaalkpfnpasdlqnagtqlkrlvdtlpqetrinivk
ltekiltsplceqdlrv
>d1cce__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgagalgkthlk
nsgyegpwgaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1ccf__ 7.3.9.1.6 Factor X, N-terminal module {bovine (Bos taurus)}
kdgdqceghpclnqghckdgigdytctcaegfegkncefstr
>d1ccg__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgagalgkthlk
nsgyegpwgaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1cch__ 1.3.1.1.18 Cytochrome c551 {(Pseudomonas stutzeri)}
qdgealfkskpcaachsvdtkmvgpalkevaaknagvegaadtlalhikngsqgvwgpip
mppnpvteeeakilaewvlslk
>d1cci__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpwgaannvftnegylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1ccj__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpwgaannvftnegylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1ccm__ 7.12.1.1.1 Crambin {abyssinian cabbage (Crambe abyssinica)}
ttccpsivarsnfnvcrlpgtpealcatytgciiipgatcpgdyan
>d1ccn__ 7.12.1.1.1 Crambin {abyssinian cabbage (Crambe abyssinica)}
ttccpsivarsnfnvcrlpgtpealcatytgciiipgatcpgdyan
>d1ccp__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
tplvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhd
ntggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqg
pkipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkth
lknsgyegpwgaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqd
pkylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1ccr__ 1.3.1.1.8 Mitochondrial cytochrome c {rice embryos (Oryza sativa l)}
xasfseappgnpkagekifktkcaqchtvdkgaghkqgpnlnglfgrqsgttpgysysta
dknmaviweentlydyllnpkkyipgtkmvfpglkkpqeradlisylkeats
>d1ccs__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgsldtppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1cct__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgsletppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1ccu__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslhtppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1cd1a1 2.1.1.2.113 (186-279) CD1, beta2-microglobulin and alpha-3 domain {Mouse (Mus musculus)}
qekpvawlssvpssahghrqlvchvsgfypkpvwvmwmrgdqeqqgthrgdflpnadetw
ylqatldveageeaglacrvkhsslggqdiilyw
>d1cd1a2 4.15.1.1.2 (7-185) CD1, alpha-1 and alpha-2 domains {Mouse (Mus musculus)}
nytfrclqmssfanrswsrtdsvvwlgdlqthrwsndsatisftkpwsqgklsnqqwekl
qhmfqvyrvsftrdiqelvkmmspkedypieiqlsagcemypgnasesflhvafqgkyvv
rfwgtswqtvpgapswldlpikvlnadqgtsatvqmllndtcplfvrglleagksdlek
>d1cd1c1 2.1.1.2.113 (186-279) CD1, beta2-microglobulin and alpha-3 domain {Mouse (Mus musculus)}
qekpvawlssvpssahghrqlvchvsgfypkpvwvmwmrgdqeqqgthrgdflpnadetw
ylqatldveageeaglacrvkhsslggqdiilyw
>d1cd1c2 4.15.1.1.2 (7-185) CD1, alpha-1 and alpha-2 domains {Mouse (Mus musculus)}
nytfrclqmssfanrswsrtdsvvwlgdlqthrwsndsatisftkpwsqgklsnqqwekl
qhmfqvyrvsftrdiqelvkmmspkedypieiqlsagcemypgnasesflhvafqgkyvv
rfwgtswqtvpgapswldlpikvlnadqgtsatvqmllndtcplfvrglleagksdlek
>d1cd8__ 2.1.1.1.2 CD8 {human (Homo sapiens)}
sqfrvspldrtwnlgetvelkcqvllsnptsgcswlfqprgaaasptfllylsqnkpkaa
egldtqrfsgkrlgdtfvltlsdfrrenegyyfcsalsnsimyfshfvpvflpa
>d1cdb__ 2.1.1.1.5 CD2 {human (Homo sapiens)}
keitnaletwgalgqdinldipsfqmsddiddikwektsdkkkiaqfrkeketfkekdty
klfkngtlkikhlktddqdiykvsiydtkgknvlekifdlkiqer
>d1cdca_ 2.1.1.1.6 CD2 {rat (Rattus rattus)}
gtvwgalghginlnipnfqmtddidevrwergstlvaefkrkmkpflksgafeilangdl
kiknltrddsgtynvtvystngtrildkaldlrile
>d1cdcb_ 2.1.1.1.6 CD2 {rat (Rattus rattus)}
gtvwgalghginlnipnfqmtddidevrwergstlvaefkrkmkpflksgafeilangdl
kiknltrddsgtynvtvystngtrildkaldlrile
>d1cdda_ 3.52.1.1.1 Glycinamide ribonucleotide transformylase {(Escherichia coli), k12 strain tx635, with plasmid pjs167}
mnivvlisgngsnlqaiidacktnkikgtvravfsnkadafglerarqagiathtliasa
fdsreaydreliheidmyapdvvvlagfmrilspafvshyagrllnihpsllpkypglht
hrqalengdeehgtsvhfvtdeldggpvilqakvpvfagdsedditarvqtqehaiyplv
iswfadgrlkmhenaawldgqrlppqgyaade
>d1cddb_ 3.52.1.1.1 Glycinamide ribonucleotide transformylase {(Escherichia coli), k12 strain tx635, with plasmid pjs167}
mnivvlisgngsnlqaiidacktnkikgtvravfsnkadafglerarqagiathtliasa
fdsreaydreliheidmyapdvvvlagfmrilspafvshyagrllnihpsllpkypglht
hrqalengdeehgtsvhfvtdeldggpvilqakvpvfagdsedditarvqtqehaiyplv
iswfadgrlkmhenaawldgqrlppqgyaade
>d1cde__ 3.52.1.1.1 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)}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d1cdg_2 2.3.1.1.1 (582-686) Cyclodextrin glycosyltransferase, C-terminal domain {(Bacillus circulans)}
lsgdqvsvrfvvnnattalgqnvyltgsvselgnwdpakaigpmynqvvyqypnwyydvs
vpagktiefkflkkqgstvtweggsnhtftapssgtatinvnwqp
>d1cdg_3 2.53.1.1.2 (383-495) Cyclodextrin glycosyltransferase {(Bacillus circulans)}
tsttayqviqklaplrkcnpaiaygstqerwinndvliyerkfgsnvavvavnrnlnapa
sisglvtslpqgsyndvlggllngntlsvgsggaasnftlaaggtavwqytaa
>d1cdg_4 3.1.1.1.2 (1-382) Cyclodextrin glycosyltransferase {(Bacillus circulans)}
apdtsvsnkqnfstdviyqiftdrfsdgnpannptgaafdgtctnlrlycggdwqgiink
indgyltgmgvtaiwisqpveniysiinysgvnntayhgywardfkktnpaygtiadfqn
liaaahaknikviidfapnhtspassdqpsfaengrlydngtllggytndtqnlfhhngg
tdfsttengiyknlydladlnhnnstvdvylkdaikmwldlgidgirmdavkhmpfgwqk
sfmaavnnykpvftfgewflgvnevspenhkfanesgmslldfrfaqkvrqvfrdntdnm
yglkamlegsaadyaqvddqvtfidnhdmerfhasnanrrkleqalaftltsrgvpaiyy
gteqymsggtdpdnraripsfs
>d1cdh_1 2.1.1.1.3 (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 2.1.1.1.3 (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 2.1.1.1.3 (1-97) CD4 {human (Homo sapiens)}
kkvvlgkkgdtveltctasqkksiqfhwknsnqikilgnqgsfltkgpsklndradsrrs
lwdqgnfpliiknlkiedsdtyicevedqkeevqllv
>d1cdj_2 2.1.1.3.4 (98-178) CD4 {human (Homo sapiens)}
fgltansdthllqgqsltltlesppgsspsvqcrsprgkniqggktlsvsqlelqdsgtw
tctvlqnqkkvefkidivvla
>d1cdka_ 5.1.1.1.2 cAMP-dependent PK, catalytic subunit {pig (Sus scrofa)}
kgseqesvkeflakakedflkkwenpaqntahldqferiktlgtgsfgrvmlvkhketgn
hfamkildkqkvvklkqiehtlnekrilqavnfpflvkleysfkdnsnlymvmeyvpgge
mfshlrrigrfsepharfyaaqivltfeylhsldliyrdlkpenllidqqgyiqvtdfgf
akrvkgrtwtlcgtpeylapeiilskgynkavdwwalgvliyemaagyppffadqpiqiy
ekivsgkvrfpshfssdlkdllrnllqvdltkrfgnlkdgvndiknhkwfattdwiaiyq
rkveapfipkfkgpgdtsnfddyeeeeirvsinekcgkefsef
>d1cdkb_ 5.1.1.1.2 cAMP-dependent PK, catalytic subunit {pig (Sus scrofa)}
kgseqesvkeflakakedflkkwenpaqntahldqferiktlgtgsfgrvmlvkhketgn
hfamkildkqkvvklkqiehtlnekrilqavnfpflvkleysfkdnsnlymvmeyvpgge
mfshlrrigrfsepharfyaaqivltfeylhsldliyrdlkpenllidqqgyiqvtdfgf
akrvkgrtwtlcgtpeylapeiilskgynkavdwwalgvliyemaagyppffadqpiqiy
ekivsgkvrfpshfssdlkdllrnllqvdltkrfgnlkdgvndiknhkwfattdwiaiyq
rkveapfipkfkgpgdtsnfddyeeeeirvsinekcgkefsef
>d1cdla_ 1.37.1.5.8 Calmodulin {bovine (Bos taurus)}
teeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngtid
fpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevdem
ireadidgdgqvnyeefvqmmt
>d1cdlb_ 1.37.1.5.8 Calmodulin {bovine (Bos taurus)}
teeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngtid
fpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevdem
ireadidgdgqvnyeefvqmmt
>d1cdlc_ 1.37.1.5.8 Calmodulin {bovine (Bos taurus)}
teeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngtid
fpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevdem
ireadidgdgqvnyeefvqmmt
>d1cdld_ 1.37.1.5.8 Calmodulin {bovine (Bos taurus)}
teeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngtid
fpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevdem
ireadidgdgqvnyeefvqmmt
>d1cdma_ 1.37.1.5.8 Calmodulin {bovine (Bos taurus)}
lteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngti
dfpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevde
mireadidgdgqvnyeefvqmmt
>d1cdn__ 1.37.1.1.1 Calbindin D9K {bovine (Bos taurus)}
kspeelkgifekyaakegdpnqlskeelklllqtefpsllkggstldelfeeldkngdge
vsfeefqvlvkkisq
>d1cdoa1 2.25.1.2.1 (1-175,325-374) Alcohol dehydrogenase {horse (Equus caballus)}
atvgkvikckaavaweankplvieeievdvphaneirikiiatgvchtdlyhlfegkhkd
gfpvvlghegagivesvgpgvtefqpgekviplfisqcgecrfcqspktnqcvkgwanes
pdvmspketrftckgrkvlqflgtstfsqytvvnqiavakidpsapldtvcllgcXkdgv
pkmvkayldkkvkldefithrmplesvndaidlmkhgkcirtvlsl
>d1cdoa2 3.22.1.1.1 (176-324) Alcohol dehydrogenase {horse (Equus caballus)}
gvstgfgaavntakvepgstcavfglgavglaavmgchsagakriiavdlnpdkfekakv
fgatdfvnpndhsepisqvlskmtnggvdfslecvgnvgvmrnalesclkgwgvsvlvgw
tdlhdvatrpiqliagrtwkgsmfggfkg
>d1cdob1 2.25.1.2.1 (1-175,325-374) Alcohol dehydrogenase {horse (Equus caballus)}
atvgkvikckaavaweankplvieeievdvphaneirikiiatgvchtdlyhlfegkhkd
gfpvvlghegagivesvgpgvtefqpgekviplfisqcgecrfcqspktnqcvkgwanes
pdvmspketrftckgrkvlqflgtstfsqytvvnqiavakidpsapldtvcllgcXkdgv
pkmvkayldkkvkldefithrmplesvndaidlmkhgkcirtvlsl
>d1cdob2 3.22.1.1.1 (176-324) Alcohol dehydrogenase {horse (Equus caballus)}
gvstgfgaavntakvepgstcavfglgavglaavmgchsagakriiavdlnpdkfekakv
fgatdfvnpndhsepisqvlskmtnggvdfslecvgnvgvmrnalesclkgwgvsvlvgw
tdlhdvatrpiqliagrtwkgsmfggfkg
>d1cdp__ 1.37.1.4.2 Parvalbumin {carp (Cyprinus carpio)}
xafagvlndadiaaaleackaadsfnhkaffakvgltsksaddvkkafaiidqdksgfie
edelklflqnfkadaraltdgetktflkagdsdgdgkigvdeftalvka
>d1cdq__ 7.6.1.3.1 CD59, extracellular domain {human (Homo sapiens)}
lqcyncpnptadcktavncssdfdaclitkaglqvynkcwkfehcnfndvttrlrenelt
yycckkdlcnfneqlen
>d1cdr__ 7.6.1.3.1 CD59, extracellular domain {human (Homo sapiens)}
lqcyncpnptadcktavncssdfdaclitkaglqvynkcwkfehcnfndvttrlrenelt
yycckkdlcnfneqlen
>d1cds__ 7.6.1.3.1 CD59, extracellular domain {human (Homo sapiens)}
lqcyncpnptadcktavncssdfdaclitkaglqvynkcwkfehcnfndvttrlrenelt
yycckkdlcnfneqlen
>d1cdta_ 7.6.1.1.6 Cardiotoxin V {taiwan cobra (Naja naja atra)}
lkcnklipiayktcpegknlcykmmlaskkmvpvkrgcinvcpknsalvkyvccstdrcn
>d1cdtb_ 7.6.1.1.6 Cardiotoxin V {taiwan cobra (Naja naja atra)}
lkcnklipiayktcpegknlcykmmlaskkmvpvkrgcinvcpknsalvkyvccstdrcn
>d1cdu_1 2.1.1.1.3 (1-97) CD4 {human (Homo sapiens)}
kkvvlgkkgdtveltctasqkksiqfhwknsnqikilgnqgsvltkgpsklndradsrrs
lwdqgnfpliiknlkiedsdtyicevedqkeevqllv
>d1cdu_2 2.1.1.3.4 (98-178) CD4 {human (Homo sapiens)}
fgltansdthllqgqsltltlesppgsspsvqcrsprgkniqggktlsvsqlelqdsgtw
tctvlqnqkkvefkidivvla
>d1cdwa_ 4.79.1.1.1 TATA-box binding protein (TBP), C-terminal domain {Human (Homo sapiens)}
sgivpqlqnivstvnlgckldlktialrarnaeynpkrfaavimrireprttalifssgk
mvctgakseensrlaarkyarvvqklgfpakfldfkiqnmvgscdvkfpirleglvlthq
qfssyepelfpgliyrmikprivllifvsgkvvltgakvraeiyeafeniypilkgfrk
>d1cdy_1 2.1.1.1.3 (1-97) CD4 {human (Homo sapiens)}
kkvvlgkkgdtveltctasqkksiqfhwknsnqikilgnqgsfltkspsklndradsrrs
lwdqgnfpliiknlkiedsdtyicevedqkeevqllv
>d1cdy_2 2.1.1.3.4 (98-178) CD4 {human (Homo sapiens)}
fgltansdthllqgqsltltlesppgsspsvqcrsprgkniqggktlsvsqlelqdsgtw
tctvlqnqkkvefkidivvla
>d1ceaa_ 7.13.1.1.3 Plasminogen kringles {human (Homo sapiens)}
ecktgngknyrgtmsktkngitcqkwsstsphrprfspathpsegleenycrnpdndpqg
pwcyttdpekrydycdilec
>d1ceab_ 7.13.1.1.3 Plasminogen kringles {human (Homo sapiens)}
ecktgngknyrgtmsktkngitcqkwsstsphrprfspathpsegleenycrnpdndpqg
pwcyttdpekrydycdilec
>d1ceba_ 7.13.1.1.3 Plasminogen kringles {human (Homo sapiens)}
ecktgngknyrgtmsktkngitcqkwsstsphrprfspathpsegleenycrnpdndpqg
pwcyttdpekrydycdilec
>d1cebb_ 7.13.1.1.3 Plasminogen kringles {human (Homo sapiens)}
ecktgngknyrgtmsktkngitcqkwsstsphrprfspathpsegleenycrnpdndpqg
pwcyttdpekrydycdilec
>d1cec__ 3.1.1.3.4 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
>d1cef__ 5.4.1.1.1 D-ala carboxypeptidase/transpeptidase {(streptomyces R61)}
adlpapddtglqavlhtalsqgapgamvrvddngtihqlsegvadratgraitttdrfrv
gsvtksfsavvllqlvdegkldldasvntylpgllpddritvrqvmshrsglydytndmf
aqtvpgfesvrnkvfsyqdlitlslkhgvtnapgaaysysntnfvvagmliekltghsva
teyqnriftplnltdtfyvhpdtvipgthangyltpdeaggalvdsteqtvswaqsagav
isstqdldtffsalmsgqlmsaaqlaqmqqwttvnstqgyglglrrrdlscgisvyghtg
tvqgyytyafaskdgkrsvtalantsnnvnvlntmartlesafcgkp
>d1ceg__ 5.4.1.1.1 D-ala carboxypeptidase/transpeptidase {(streptomyces R61)}
adlpapddtglqavlhtalsqgapgamvrvddngtihqlsegvadratgraitttdrfrv
gsvtksfsavvllqlvdegkldldasvntylpgllpddritvrqvmshrsglydytndmf
aqtvpgfesvrnkvfsyqdlitlslkhgvtnapgaaysysntnfvvagmliekltghsva
teyqnriftplnltdtfyvhpdtvipgthangyltpdeaggalvdsteqtvswaqsagav
isstqdldtffsalmsgqlmsaaqlaqmqqwttvnstqgyglglrrrdlscgisvyghtg
tvqgyytyafaskdgkrsvtalantsnnvnvlntmartlesafcgkp
>d1ceh__ 1.103.1.2.11 Phospholipase A2 {bovine (Bos taurus l.) pancreas}
alwqfngmikckipsseplldfnnygcycglggsgtpvddldrccqthdncykqakklds
ckvlvdnpytnnysyscsnneitcssennaceaficncnrnaaicfskvpynkehknldk
knc
>d1cei__ 1.27.2.1.1 ImmE7 protein {(Escherichia coli)}
lknsisdyteaefvqllkeiekenvaatddvldvllehfvkitehpdgtdliyypsdnrd
dspegivkeikewraangkpgfkqg
>d1cela_ 2.21.1.8.1 Cellobiohydrolase I (cellulase) {(Trichoderma reesei)}
xsactlqsethppltwqkcssggtctqqtgsvvidanwrwthatnsstncydgntwsstl
cpdnetcaknccldgaayastygvttsgnslsigfvtqsaqknvgarlylmasdttyqef
tllgnefsfdvdvsqlpcglngalyfvsmdadggvskyptntagakygtgycdsqcprdl
kfingqanvegwepssnnantgigghgsccsemdiweansisealtphpcttvgqeiceg
dgcggtysdnryggtcdpdgcdwnpyrlgntsfygpgssftldttkkltvvtqfetsgai
nryyvqngvtfqqpnaelgsysgnelnddyctaeeaefggssfsdkggltqfkkatsggm
vlvmslwddyyanmlwldstyptnetsstpgavrgscstssgvpaqvesqspnakvtfsn
ikfgpigstgnpsg
>d1celb_ 2.21.1.8.1 Cellobiohydrolase I (cellulase) {(Trichoderma reesei)}
xsactlqsethppltwqkcssggtctqqtgsvvidanwrwthatnsstncydgntwsstl
cpdnetcaknccldgaayastygvttsgnslsigfvtqsaqknvgarlylmasdttyqef
tllgnefsfdvdvsqlpcglngalyfvsmdadggvskyptntagakygtgycdsqcprdl
kfingqanvegwepssnnantgigghgsccsemdiweansisealtphpcttvgqeiceg
dgcggtysdnryggtcdpdgcdwnpyrlgntsfygpgssftldttkkltvvtqfetsgai
nryyvqngvtfqqpnaelgsysgnelnddyctaeeaefggssfsdkggltqfkkatsggm
vlvmslwddyyanmlwldstyptnetsstpgavrgscstssgvpaqvesqspnakvtfsn
ikfgpigstgnpsg
>d1cem__ 1.81.1.2.1 CelA cellulase {(Clostridium thermocellum)}
agvpfntkypygptsiadnqsevtamlkaewedwkskritsngaggykrvqrdastnydt
vsegmgyglllavcfneqalfddlyryvkshfngnglmhwhidannnvtshdggdgaatd
adedialalifadkqwgssgainygqeartlinnlynhcvehgsyvlkpgdrwggssvtn
psyfapawykvyaqytgdtrwnqvadkcyqiveevkkynngtglvpdwctasgtpasgqs
ydykydatrygwrtavdyswfgdqrakancdmltkffardgakgivdgytiqgskisnnh
nasfigpvaaasmtgydlnfakelyretvavkdseyygyygnslrlltllyitgnfpnpl
sdl
>d1cen__ 3.1.1.3.4 Endoglucanase CelC {(Clostridium thermocellum)}
mvsfkaginlggwisqyqvfskehfdtfitekdietiaeagfdhvrlpfdypiiesddnv
geykedglsyidrclewckkynlglvldmhhapgyrfqdfktstlfedpnqqkrfvdiwr
flakryinerehiafellnqvvepdstrwnklmlecikaireidstmwlyiggnnynspd
elknladidddyivynfhfynpfffthqkahwsesamaynrtvkypgqyegieefvknnp
kysfmmelnnlklnkellrkdlkpaiefrekkkcklycgefgviaiadlesrikwhedyi
slleeydiggavwnykkmdfeiynedrkpvsqelvnilar
>d1ceo__ 3.1.1.3.4 Endoglucanase CelC {(Clostridium thermocellum)}
mvsfkaginlggwisqyqvfskehfdtfitekdietiaeagfdhvrlpfdypiiesddnv
geykedglsyidrclewckkynlglvldmhhapgyrfqdfktstlfedpnqqkrfvdiwr
flakryinerehiafellnqvvepdstrwnklmlecikaireidstmwlyiggnnynspd
elknladidddyivynfhfynpfffthqkahwsesamaynrtvkypgqyegieefvknnp
kysfmmelnnlklnkellrkdlkpaiefrekkkcklycgefgviaiadlesrikwhedyi
slleeydiggavwnykkmdfeiynedrkpvsqelvnilar
>d1cero1 3.22.1.3.3 (1-148,313-333) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Thermus aquaticus)}
mkvgingfgrigrqvfrilhsrgvevalindltdnktlahllkydsiyhrfpgevayddq
ylyvdgkairatavkdpkeipwaeagvgvviestgvftdadkakahleggakkviitapa
kgeditivmgvnheaydpsrhhiisnasXnewgyanrvadlvelvlrkgv
>d1cero2 4.42.1.1.3 (149-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Thermus aquaticus)}
cttnslapvmkvleeafgvekalmttvhsytndqrlldlphkdlrraraaainiiptttg
aakatalvlpslkgrfdgmalrvptatgsisditallkrevtaeevnaalkaaaegplkg
ilaytedeivlqdivmdphssivdakltkalgnmvkvfawyd
>d1cerp1 3.22.1.3.3 (1-148,313-333) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Thermus aquaticus)}
mkvgingfgrigrqvfrilhsrgvevalindltdnktlahllkydsiyhrfpgevayddq
ylyvdgkairatavkdpkeipwaeagvgvviestgvftdadkakahleggakkviitapa
kgeditivmgvnheaydpsrhhiisnasXnewgyanrvadlvelvlrkgv
>d1cerp2 4.42.1.1.3 (149-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Thermus aquaticus)}
cttnslapvmkvleeafgvekalmttvhsytndqrlldlphkdlrraraaainiiptttg
aakatalvlpslkgrfdgmalrvptatgsisditallkrevtaeevnaalkaaaegplkg
ilaytedeivlqdivmdphssivdakltkalgnmvkvfawyd
>d1cerq1 3.22.1.3.3 (1-148,313-333) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Thermus aquaticus)}
mkvgingfgrigrqvfrilhsrgvevalindltdnktlahllkydsiyhrfpgevayddq
ylyvdgkairatavkdpkeipwaeagvgvviestgvftdadkakahleggakkviitapa
kgeditivmgvnheaydpsrhhiisnasXnewgyanrvadlvelvlrkgv
>d1cerq2 4.42.1.1.3 (149-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Thermus aquaticus)}
cttnslapvmkvleeafgvekalmttvhsytndqrlldlphkdlrraraaainiiptttg
aakatalvlpslkgrfdgmalrvptatgsisditallkrevtaeevnaalkaaaegplkg
ilaytedeivlqdivmdphssivdakltkalgnmvkvfawyd
>d1cerr1 3.22.1.3.3 (1-148,313-333) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Thermus aquaticus)}
mkvgingfgrigrqvfrilhsrgvevalindltdnktlahllkydsiyhrfpgevayddq
ylyvdgkairatavkdpkeipwaeagvgvviestgvftdadkakahleggakkviitapa
kgeditivmgvnheaydpsrhhiisnasXnewgyanrvadlvelvlrkgv
>d1cerr2 4.42.1.1.3 (149-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Thermus aquaticus)}
cttnslapvmkvleeafgvekalmttvhsytndqrlldlphkdlrraraaainiiptttg
aakatalvlpslkgrfdgmalrvptatgsisditallkrevtaeevnaalkaaaegplkg
ilaytedeivlqdivmdphssivdakltkalgnmvkvfawyd
>d1cesa_ 2.21.1.1.1 Concanavalin A {jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1cesb_ 2.21.1.1.1 Concanavalin A {jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1cewi_ 4.13.1.2.1 Cystatin {chicken (Gallus gallus)}
gapvpvdendeglqralqfamaeynrasndkyssrvvrvisakrqlvsgikyilqveigr
ttcpkssgdlqscefhdepemakyttctfvvysipwlnqiklleskcq
>d1cex__ 3.14.7.1.1 Cutinase {fungus (Fusarium solani, subsp. pisi)}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1cey__ 3.14.2.1.2 CheY protein {(Salmonella typhimurium)}
adkelkflvvddfstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmp
nmdglellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleekln
kifeklgm
>d1cfaa_ 1.45.1.1.1 C5a anaphylotoxin {human (Homo sapiens)}
mlqkkieeiaakykhsvvkkccydgasvnndetceqraarislgprcikafteccvvasq
lranishkdmc
>d1cfb_1 2.1.2.1.6 (610-709) Neuroglian, the two amino proximal Fn3 repeats {(Drosophila melanogaster)}
ivqdvpnapkltgitcqadkaeihweqqgdnrspilhytiqfntsftpaswdaayekvpn
tdssfvvqmspwanytfrviafnkigasppsahsdscttq
>d1cfb_2 2.1.2.1.6 (710-814) Neuroglian, the two amino proximal Fn3 repeats {(Drosophila melanogaster)}
pdvpfknpdnvvgqgtepnnlviswtpmpeiehnapnfhyyvswkrdipaaawennnifd
wrqnniviadqptfvkylikvvaindrgesnvaaeevvgysgedr
>d1cfc__ 1.37.1.5.11 Calmodulin {African frog (Xenopus laevis)}
adqlteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgn
gtidfpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdee
vdemireadidgdgqvnyeefvqmmtak
>d1cfd__ 1.37.1.5.11 Calmodulin {African frog (Xenopus laevis)}
adqlteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgn
gtidfpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdee
vdemireadidgdgqvnyeefvqmmtak
>d1cfe__ 4.64.1.1.1 P14a {Tomato (Lycopersicon esculentum)}
qnspqdylavhndaraqvgvgpmswdanlasraqnyansragdcnlihsgagenlakggg
dftgraavqlwvserpsynyatnqcvggkkcrhytqvvwrnsvrlgcgrarcnngwwfis
cnydpvgnwigqrpy
>d1cfh__ 7.28.1.1.3 Coagulation factor IX (IXa) {human (Homo sapiens)}
ynsgkleefvqgnlerecmeekcsfeearevfenterttefwkqyvd
>d1cfpa_ 1.37.1.2.3 Calcyclin (S100) {bovine (bos taurus)}
mselekavvalidvfhqysgregdkhklkkselkelinnelshfleeikeqevvdkvmet
ldsdgdgecdfqefmafvamittacheffehe
>d1cfpb_ 1.37.1.2.3 Calcyclin (S100) {bovine (bos taurus)}
mselekavvalidvfhqysgregdkhklkkselkelinnelshfleeikeqevvdkvmet
ldsdgdgecdfqefmafvamittacheffehe
>d1cfr__ 3.43.1.5.1 Restriction endonuclease Cfr10I {(Citrobacter freundii)}
mdiisksgegnkytinsaiafvayashidinttefskvlsglrdfindeairlggkisdg
sfnkcngdwyewligiraiefflesetnfivvkmpnatsfdvmsiyksclsefiydlrsk
lslnnvnlitsnpdfsiidirgrreelksmlkdisfsnislstiseidnlyknfidyael
ehiksflsvkttfrpdrrlqlahegslmkalythlqtrtwtinptgiryyaaatsignad
viglktvathsitdvkslpqsavdeifkinsvldvdsclshil
>d1cfvh_ 2.1.1.1.84 Immunoglobulin (variable domains of L and H chains) {Fv 4155 (mouse), kappa L chain}
qvqlqesggglvnlggsmtlscvasgftfntyymswvrqtpektlelvaainsdgepiyy
pdtlkgrvtisrdnakktlylqmsslnfedtalyycarlnyavygmdywgqgttvtvss
>d1cfvl_ 2.1.1.1.84 Immunoglobulin (variable domains of L and H chains) {Fv 4155 (mouse), kappa L chain}
dieltqsppslpvslgdqvsiscrssqslvsnnrrnylhwylqkpgqspklviykvsnrf
sgvpdrfsgsgsgtdftlkisrvaaedlglyfcsqsshvpltfgsgtkleikr
>d1cfya_ 4.62.1.2.1 yeast cofilin, monoclinic crystal form {baker's yeast (saccharomyces cerevisiae)}
vavadesltafndlklgkkykfilfglndakteivvketstdpsydafleklpendclya
iydfeyeingnegkrskivfftwspdtapvrskmvyasskdalrralngvstdvqgtdfs
evsydsvlervsr
>d1cfyb_ 4.62.1.2.1 yeast cofilin, monoclinic crystal form {baker's yeast (saccharomyces cerevisiae)}
vavadesltafndlklgkkykfilfglndakteivvketstdpsydafleklpendclya
iydfeyeingnegkrskivfftwspdtapvrskmvyasskdalrralngvstdvqgtdfs
evsydsvlervsr
>d1cg2a1 3.58.4.4.3 (26-213,327-414) Carboxypeptidase G2, catalytic domain {(Pseudomonas sp.) strain rs-16}
qkrdnvlfqaatdeqpaviktleklvnietgtgdaegiaaagnfleaelknlgftvtrsk
saglvvgdnivgkikgrggknlllmshmdtvylkgilakapfrvegdkaygpgiaddkgg
navilhtlkllkeygvrdygtitvlfntdeekgsfgsrdliqeeakladyvlsfeptsag
deklslgtXfnageggkklvdkavayykeaggtlgveertgggtdaayaalsgkpviesl
glpgfgyhsdkaeyvdisaiprrlymaarlimdlgag
>d1cg2a2 4.34.17.1.1 (214-326) PR Carboxypeptidase G2, dimerisation domain {(Pseudomonas sp.) strain rs-16}
sgiayvqvnitgkashagaapelgvnalveasdlvlrtmniddkaknlrfnwtiakagnv
sniipasatlnadvryarnedfdaamktleeraqqkklpeadvkvivtrgrpa
>d1cg2b1 3.58.4.4.3 (26-213,327-414) Carboxypeptidase G2, catalytic domain {(Pseudomonas sp.) strain rs-16}
qkrdnvlfqaatdeqpaviktleklvnietgtgdaegiaaagnfleaelknlgftvtrsk
saglvvgdnivgkikgrggknlllmshmdtvylkgilakapfrvegdkaygpgiaddkgg
navilhtlkllkeygvrdygtitvlfntdeekgsfgsrdliqeeakladyvlsfeptsag
deklslgtXfnageggkklvdkavayykeaggtlgveertgggtdaayaalsgkpviesl
glpgfgyhsdkaeyvdisaiprrlymaarlimdlgag
>d1cg2b2 4.34.17.1.1 (214-326) PR Carboxypeptidase G2, dimerisation domain {(Pseudomonas sp.) strain rs-16}
sgiayvqvnitgkashagaapelgvnalveasdlvlrtmniddkaknlrfnwtiakagnv
sniipasatlnadvryarnedfdaamktleeraqqkklpeadvkvivtrgrpa
>d1cg2c1 3.58.4.4.3 (26-213,327-414) Carboxypeptidase G2, catalytic domain {(Pseudomonas sp.) strain rs-16}
qkrdnvlfqaatdeqpaviktleklvnietgtgdaegiaaagnfleaelknlgftvtrsk
saglvvgdnivgkikgrggknlllmshmdtvylkgilakapfrvegdkaygpgiaddkgg
navilhtlkllkeygvrdygtitvlfntdeekgsfgsrdliqeeakladyvlsfeptsag
deklslgtXfnageggkklvdkavayykeaggtlgveertgggtdaayaalsgkpviesl
glpgfgyhsdkaeyvdisaiprrlymaarlimdlgag
>d1cg2c2 4.34.17.1.1 (214-326) PR Carboxypeptidase G2, dimerisation domain {(Pseudomonas sp.) strain rs-16}
sgiayvqvnitgkashagaapelgvnalveasdlvlrtmniddkaknlrfnwtiakagnv
sniipasatlnadvryarnedfdaamktleeraqqkklpeadvkvivtrgrpa
>d1cg2d1 3.58.4.4.3 (26-213,327-414) Carboxypeptidase G2, catalytic domain {(Pseudomonas sp.) strain rs-16}
qkrdnvlfqaatdeqpaviktleklvnietgtgdaegiaaagnfleaelknlgftvtrsk
saglvvgdnivgkikgrggknlllmshmdtvylkgilakapfrvegdkaygpgiaddkgg
navilhtlkllkeygvrdygtitvlfntdeekgsfgsrdliqeeakladyvlsfeptsag
deklslgtXfnageggkklvdkavayykeaggtlgveertgggtdaayaalsgkpviesl
glpgfgyhsdkaeyvdisaiprrlymaarlimdlgag
>d1cg2d2 4.34.17.1.1 (214-326) PR Carboxypeptidase G2, dimerisation domain {(Pseudomonas sp.) strain rs-16}
sgiayvqvnitgkashagaapelgvnalveasdlvlrtmniddkaknlrfnwtiakagnv
sniipasatlnadvryarnedfdaamktleeraqqkklpeadvkvivtrgrpa
>d1cge__ 4.52.1.7.1 Fibroblast collagenase {human (Homo sapiens)}
ltegnprweqthlryrienytpdlpradvdhaiekafqlwsnvtpltftkvsegqadimi
sfvrgdhrdnspfdgpggnlahafqpgpgiggdahfdederwtnnfreynlhrvaahelg
hslglshstdigalmypsytfsgdvqlaqddidgiqaiygrs
>d1cgfa_ 4.52.1.7.1 Fibroblast collagenase {human (Homo sapiens)}
ltegnprweqthlryrienytpdlpradvdhaiekafqlwsnvtpltftkvsegqadimi
sfvrgdhrdnspfdgpggnlahafqpgpgiggdahfdederwtnnfreynlhrvaahelg
hslglshstdigalmypsytfsgdvqlaqddidgiqaiygrs
>d1cgfb_ 4.52.1.7.1 Fibroblast collagenase {human (Homo sapiens)}
ltegnprweqthlryrienytpdlpradvdhaiekafqlwsnvtpltftkvsegqadimi
sfvrgdhrdnspfdgpggnlahafqpgpgiggdahfdederwtnnfreynlhrvaahelg
hslglshstdigalmypsytfsgdvqlaqddidgiqaiygrs
>d1cgha_ 2.35.1.2.17 Cathepsin G {human (homo sapiens)}
iiggresrphsrpymaylqiqspagqsrcggflvredfvltaahcwgsninvtlgahniq
rrentqqhitarrairhpqynqrtiqndimllqlsrrvrrnrnvnpvalpraqeglrpgt
lctvagwgrvsmrrgtdtlrevqlrvqrdrqclrifgsydprrqicvgdrrerkaafkgd
sggpllcnnvahgivsygkssgvppevftrvssflpwirttmrs
>d1cgie_ 2.35.1.2.7 (alpha, gamma-)chymotrypsin(ogen) {bovine (Bos taurus)}
cgvpaiqpvlsglsrivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgv
ttsdvvvagefdqgsssekiqklkiakvfknskynsltinnditllklstaasfsqtvsa
vclpsasddfaagttcvttgwgltrytnantpdrlqqaslpllsntnckkywgtkikdam
icagasgvsscmgdsggplvckkngawtlvgivswgsstcststpgvyarvtalvnwvqq
tlaan
>d1cgii_ 7.14.1.1.4 Secretory trypsin inhibitor {human (Homo sapiens)}
dslgreakcynelngctyeyrpvcgtdgdtypnecvlcfenrkrqtsiliqksgpc
>d1cgje_ 2.35.1.2.7 (alpha, gamma-)chymotrypsin(ogen) {bovine (Bos taurus)}
cgvpaiqpvlsglsrivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgv
ttsdvvvagefdqgsssekiqklkiakvfknskynsltinnditllklstaasfsqtvsa
vclpsasddfaagttcvttgwgltrytnantpdrlqqaslpllsntnckkywgtkikdam
icagasgvsscmgdsggplvckkngawtlvgivswgsstcststpgvyarvtalvnwvqq
tlaan
>d1cgji_ 7.14.1.1.4 Secretory trypsin inhibitor {human (Homo sapiens)}
dslgreakcynelngctleyrpvcgtdgdtypnecvlcfenrkrqtsiliqksgpc
>d1cgla_ 4.52.1.7.1 Fibroblast collagenase {human (Homo sapiens)}
vltegnprweqthlryrienytpdlpradvdhaiekafqlwsdvtpltftkvsegqadim
isfvrgdhrdnspfdgpggnlahafdpgpgiggdahfdederwtnnfreynlhrvaahel
ghslglshstdigalmypsytfsgdvqlaqddidgiqaiygrsqnpvq
>d1cglb_ 4.52.1.7.1 Fibroblast collagenase {human (Homo sapiens)}
nprweqthlryrienytpdlpradvdhaiekafqlwsdvtpltftkvsegqadimisfvr
gdhrdnspfdgpggnlahafdpgpgiggdahfdederwtnnfreynlhrvaahelghslg
lshstdigalmypsytfsgdvqlaqddidgiqaiygrsqn
>d1cgme_ 1.24.5.1.2 Cucumber green mottle mosaic virus {cucumber green mottle mosaic virus, watermelon strain}
xaynpitpskliafsasyvpvrtllnflvasqgtafqtqagrdsfreslsalpssvvdin
srfpdagfyaflngpvlrpifvsllsstdtrnrvievvdpsnpttaeslnavkrtddast
aaraeidnliesiskgfdvydrasfeaafsvvwseattska
>d1cgn__ 1.24.3.2.3 Cytochrome c' {(Alcaligenes denitrificans)}
xfakpedavkyrqsaltlmashfgrmapvvkgqapydaaqikanvevlktltalpwaafg
agteggdarpeiwsdaagfkqkqqafqdnivklsaaadagdldklraafgdvgasckach
dsyrk
>d1cgo__ 1.24.3.2.4 Cytochrome c' {(Alcaligenes sp.)}
xfakpedavkyrqsaltlmashfgrmtpvvkgqapydaaqikanvevlktltalpwaafg
pgteggdarpeiwsdaasfkqkqqafqdnivklsaaadagdldklraafgdvgasckach
dayrk
>d1cgpa1 1.4.3.4.1 (138-205) Catabolite gene activator protein (CAP), C-terminal domain {(Escherichia coli)}
dvtgriaqtllnlakqpdamthpdgmqikitrqeigqivgcsretvgrilkmledqnlis
ahgktivv
>d1cgpa2 2.64.4.1.1 (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 2.64.4.1.1 (9-137) Catabolite gene activator protein, N-terminal domain, {(Escherichia coli)}
ptlewflshchihkypskstlihqgekaetlyyivkgsvavlikdeegkemilsylnqgd
figelglfeegqersawvraktacevaeisykkfrqliqvnpdilmrlsaqmarrlqvts
ekvgnlafl
>d1cgsh1 2.1.1.1.36 (1-117) Immunoglobulin (variable domains of L and H chains) {Fab, anti-sweetener (mouse), kappa L chain}
rvqllesgaelmkpgasvqisckatgytfseywiewvkerpghglewigeilpgsgrtny
rekfkgkatftadtssntaymqlssltsedsavyyctrgyssmdywgqgtsvtvsaa
>d1cgsh2 2.1.1.2.44 (118-214) Immunoglobulin (constant domains of L and H chains) {Fab, anti-sweetener (mouse), kappa L chain}
kttppsvyplapgcgdttgssvtlgclvkgyfpesvtvtwnsgslsssvhtfpallqsgl
ytmsssvtvpsstwpsqtvtcsvahpassttvdkkle
>d1cgsl1 2.1.1.1.36 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab, anti-sweetener (mouse), kappa L chain}
elvmtqsplslpvslgdqasiscrpsqslvhsngntylhwylqkpgqspklliyrvsnrf
sgvpdrfsgsgsgtaftlkisrveaedlgvyfcsqgthvpytfgggtklelk
>d1cgsl2 2.1.1.2.44 (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)}
ettptighvgpvmgkpgnvvtidgrgfgstkgtvyfgttavtgaaitswedtqikvtips
vaagnyavkvaasgvnsnaynnfti
>d1cgt_2 2.3.1.1.1 (580-684) Cyclodextrin glycosyltransferase, C-terminal domain {(Bacillus circulans)}
ltgdqvtvrfvvnnasttlgqnlyltgnvaelgnwstgstaigpafnqvihqyptwyydv
svpagkqlefkffkkngstitwesgsnhtfttpasgtatvtvnwq
>d1cgt_3 2.53.1.1.2 (383-494) Cyclodextrin glycosyltransferase {(Bacillus circulans)}
ksttafnvisklaplrksnpaiaygstqqrwinndvyvyerkfgksvavvavnrnlstsa
sitglstslptgsytdvlggvlngnnitstngsinnftlaagatavwqytta
>d1cgt_4 3.1.1.1.2 (1-382) Cyclodextrin glycosyltransferase {(Bacillus circulans)}
dpdtavtnkqsfstdviyqvftdrfldgnpsnnptgaaydatcsnlklycggdwqglink
indnyfsdlgvtalwisqpvenifatinysgvtntayhgywardfkktnpyfgtmadfqn
littahakgikividfapnhtspametdtsfaengrlydngtlvggytndtngyfhhngg
sdfsslengiyknlydladfnhnnatidkyfkdaiklwldmgvdgirvdavkhmplgwqk
swmssiyahkpvftfgewflgsaasdadntdfanksgmslldfrfnsavrnvfrdntsnm
yaldsminstatdynqvndqvtfidnhdmdrfktsavnnrrleqalaftltsrgvpaiyy
gteqyltgngdpdnrakmpsfs
>d1cgu_1 2.1.1.5.4 (495-579) Cyclodextrin glycosyltransferase, domain E {(Bacillus circulans)}
ettptighvgpvmgkpgnvvtidgrgfgstkgtvyfgttavtgaaitswedtqikvtips
vaagnyavkvaasgvnsnaynnfti
>d1cgu_2 2.3.1.1.1 (580-684) Cyclodextrin glycosyltransferase, C-terminal domain {(Bacillus circulans)}
ltgdqvtvrfvvnnasttlgqnlyltgnvaelgnwstgstaigpafnqvihqyptwyydv
svpagkqlefkffkkngstitwesgsnhtfttpasgtatvtvnwq
>d1cgu_3 2.53.1.1.2 (383-494) Cyclodextrin glycosyltransferase {(Bacillus circulans)}
ksttafnvisklaplrksnpaiaygstqqrwinndvyvyerkfgksvavvavnrnlstsa
sitglstslptgsytdvlggvlngnnitstngsinnftlaagatavwqytta
>d1cgu_4 3.1.1.1.2 (1-382) Cyclodextrin glycosyltransferase {(Bacillus circulans)}
dpdtavtnkqsfstdviyqvftdrfldgnpsnnptgaaydatcsnlklycggdwqglink
indnyfsdlgvtalwisqpvenifatinysgvtntayhgywardfkktnpyfgtmadfqn
littahakgikividfapnhtspametdtsfaengrlydngtlvggytndtngyfhhngg
sdfsslengiyknlydladfnhnnatidkyfkdaiklwldmgvdgirvaavkhmplgwqk
swmssiyahkpvftfgewflgsaasdadntdfanksgmslldfrfnsavrnvfrdntsnm
yaldsminstatdynqvndqvtfidnhdmdrfktsavnnrrleqalaftltsrgvpaiyy
gteqyltgngdpdnrakmpsfs
>d1cgv_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {(Bacillus circulans)}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d1cgv_2 2.3.1.1.1 (582-686) Cyclodextrin glycosyltransferase, C-terminal domain {(Bacillus circulans)}
lsgdqvsvrfvvnnattalgqnvyltgsvselgnwdpakaigpmynqvvyqypnwyydvs
vpagktiefkflkkqgstvtweggsnhtftapssgtatinvnwqp
>d1cgv_3 2.53.1.1.2 (383-495) Cyclodextrin glycosyltransferase {(Bacillus circulans)}
tsttayqviqklaplrkcnpaiaygstqerwinndvliyerkfgsnvavvavnrnlnapa
sisglvtslpqgsyndvlggllngntlsvgsggaasnftlaaggtavwqytaa
>d1cgv_4 3.1.1.1.2 (1-382) Cyclodextrin glycosyltransferase {(Bacillus circulans)}
apdtsvsnkqnfstdviyqiftdrfsdgnpannptgaafdgtctnlrlycggdwqgiink
indgyltgmgvtaiwisqpveniysiinysgvnntayhgywardfkktnpaygtiadfqn
liaaahaknikviidfapnhtspassdqpsfaengrlydngtllggytndtqnlfhhngg
tdfsttengiyknlfdladlnhnnstvdvylkdaikmwldlgidgirmdavkhmpfgwqk
sfmaavnnykpvftfgewflgvnevspenhkfanesgmslldfrfaqkvrqvfrdntdnm
yglkamlegsaadyaqvddqvtfidnhdmerfhasnanrrkleqalaftltsrgvpaiyy
gteqymsggtdpdnraripsfs
>d1cgw_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {(Bacillus circulans)}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d1cgw_2 2.3.1.1.1 (582-686) Cyclodextrin glycosyltransferase, C-terminal domain {(Bacillus circulans)}
lsgdqvsvrfvvnnattalgqnvyltgsvselgnwdpakaigpmynqvvyqypnwyydvs
vpagktiefkflkkqgstvtweggsnhtftapssgtatinvnwqp
>d1cgw_3 2.53.1.1.2 (383-495) Cyclodextrin glycosyltransferase {(Bacillus circulans)}
tsttayqviqklaplrkcnpaiaygstqerwinndvliyerkfgsnvavvavnrnlnapa
sisglvtslpqgsyndvlggllngntlsvgsggaasnftlaaggtavwqytaa
>d1cgw_4 3.1.1.1.2 (1-382) Cyclodextrin glycosyltransferase {(Bacillus circulans)}
apdtsvsnkqnfstdviyqiftdrfsdgnpannptgaafdgtctnlrlycggdwqgiink
indgyltgmgvtaiwisqpveniysiinysgvnntayhgywardfkktnpaygtiadfqn
liaaahaknikviidfapnhtspassdqpsfaengrlydngtllggytndtqnlfhhngg
tdfsttengiyknlgdladlnhnnstvdvylkdaikmwldlgidgirmdavkhmpfgwqk
sfmaavnnykpvftfgewflgvnevspenhkfanesgmslldfrfaqkvrqvfrdntdnm
yglkamlegsaadyaqvddqvtfidnhdmerfhasnanrrkleqalaftltsrgvpaiyy
gteqymsggtdpdnraripsfs
>d1cgx_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {(Bacillus circulans)}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d1cgx_2 2.3.1.1.1 (582-686) Cyclodextrin glycosyltransferase, C-terminal domain {(Bacillus circulans)}
lsgdqvsvrfvvnnattalgqnvyltgsvselgnwdpakaigpmynqvvyqypnwyydvs
vpagktiefkflkkqgstvtweggsnhtftapssgtatinvnwqp
>d1cgx_3 2.53.1.1.2 (383-495) Cyclodextrin glycosyltransferase {(Bacillus circulans)}
tsttayqviqklaplrkcnpaiaygstqerwinndvliyerkfgsnvavvavnrnlnapa
sisglvtslpqgsyndvlggllngntlsvgsggaasnftlaaggtavwqytaa
>d1cgx_4 3.1.1.1.2 (1-382) Cyclodextrin glycosyltransferase {(Bacillus circulans)}
apdtsvsnkqnfstdviyqiftdrfsdgnpannptgaafdgtctnlrlycggdwqgiink
indgyltgmgvtaiwisqpveniysiinysgvnntayhgywardfkktnpaygtiadfqn
liaaahaknikviidfapnhtspassdqpsfaengrlydngtllggytndtqnlfhhngg
tdfsttengiyknlldladlnhnnstvdvylkdaikmwldlgidgirmdavkhmpfgwqk
sfmaavnnykpvftfgewflgvnevspenhkfanesgmslldfrfaqkvrqvfrdntdnm
yglkamlegsaadyaqvddqvtfidnhdmerfhasnanrrkleqalaftltsrgvpaiyy
gteqymsggtdpdnraripsfs
>d1cgy_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {(Bacillus circulans)}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d1cgy_2 2.3.1.1.1 (582-686) Cyclodextrin glycosyltransferase, C-terminal domain {(Bacillus circulans)}
lsgdqvsvrfvvnnattalgqnvyltgsvselgnwdpakaigpmynqvvyqypnwyydvs
vpagktiefkflkkqgstvtweggsnhtftapssgtatinvnwqp
>d1cgy_3 2.53.1.1.2 (383-495) Cyclodextrin glycosyltransferase {(Bacillus circulans)}
tsttayqviqklaplrkcnpaiaygstqerwinndvliyerkfgsnvavvavnrnlnapa
sisglvtslpqgsyndvlggllngntlsvgsggaasnftlaaggtavwqytaa
>d1cgy_4 3.1.1.1.2 (1-382) Cyclodextrin glycosyltransferase {(Bacillus circulans)}
apdtsvsnkqnfstdviyqiftdrfsdgnpannptgaafdgtctnlrlycggdwqgiink
indgyltgmgvtaiwisqpveniysiinysgvnntayhgywardfkktnpaygtiadfqn
liaaahaknikviidfapnhtspassdqpsfaengrlydngtllggytndtqnlfhhngg
tdfsttengiyknlwdladlnhnnstvdvylkdaikmwldlgidgirmdavkhmpfgwqk
sfmaavnnykpvftfgewflgvnevspenhkfanesgmslldfrfaqkvrqvfrdntdnm
yglkamlegsaadyaqvddqvtfidnhdmerfhasnanrrkleqalaftltsrgvpaiyy
gteqymsggtdpdnraripsfs
>d1chc__ 7.37.1.1.2 Immediate early protein, IEEHV {(equine herpes virus-1 )}
matvaercpicledpsnysmalpclhafcyvcitrwirqnptcplckvpvesvvhtiesd
sefgdqli
>d1chd__ 3.31.1.1.1 Methylesterase CheB, C-terminal domain {(Salmonella typhimurium)}
llssekliaigastggteairhvlqplplsspaviitqhmppgftrsfaerlnklcqisv
keaedgervlpghayiapgdkhmelarsganyqikihdgppvnrhrpsvdvlfhsvakha
grnavgviltgmgndgaagmlamyqagawtiaqneascvvfgmpreainmggvsevvdls
qvsqqmlakisagqairi
>d1chg__ 2.35.1.2.7 (alpha, gamma-)chymotrypsin(ogen) {bovine (Bos taurus)}
cgvpaiqpvlsglsrivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgv
ttsdvvvagefdqgsssekiqklkiakvfknskynsltinnditllklstaasfsqtvsa
vclpsasddfaagttcvttgwgltrytnantpdrlqqaslpllsntnckkywgtkikdam
icagasgvsscmgdsggplvckkngawtlvgivswgsstcststpgvyarvtalvnwvqq
tlaan
>d1chh__ 1.3.1.1.6 Mitochondrial cytochrome c {baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdanikk
nvlwdennmseyltnpkkyipgtkmaygglkkekdrndlitylkkate
>d1chi__ 1.3.1.1.6 Mitochondrial cytochrome c {baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdanikk
nvlwdennmseyltnpkkyipgtkmayggakkekdrndlitylkkate
>d1chj__ 1.3.1.1.6 Mitochondrial cytochrome c {baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdanikk
nvlwdennmseyltnpkkyipgtkmafggakkekdrndlitylkkate
>d1chka_ 4.2.1.7.1 Endochitosanase {(Streptomyces sp.)}
agaglddphkkeiamelvssaenssldwkaqykyiedigdgrgytggiigfcsgtgdmle
lvqhytdlepgnilakylpalkkvngsashsglgtpftkdwataakdtvfqqaqnderdr
vyfdpavsqakadglralgqfayydaivmhgpgndptsfggirktamkkartpaqggdet
tylngfldarkaamlteaahddtsrvdteqrvflkagnldlnpplkwktygdpyvins
>d1chkb_ 4.2.1.7.1 Endochitosanase {(Streptomyces sp.)}
agaglddphkkeiamelvssaenssldwkaqykyiedigdgrgytggiigfcsgtgdmle
lvqhytdlepgnilakylpalkkvngsashsglgtpftkdwataakdtvfqqaqnderdr
vyfdpavsqakadglralgqfayydaivmhgpgndptsfggirktamkkartpaqggdet
tylngfldarkaamlteaahddtsrvdteqrvflkagnldlnpplkwktygdpyvins
>d1chl__ 7.3.6.2.7 Chlorootoxin {scorpion (Leiurus quinquestriatus) venom}
mcmpcfttdhqmarkcddccggkgrgkcygpqclcr
>d1chma1 3.47.2.1.1 (2-156) Creatinase, N-terminal domain {(Pseudomonas putida)}
qmpktlrirngdkvrstfsaqeyanrqarlrahlaaenidaaiftsyhninyysdflycs
fgrpyalvvteddvisisanidggqpwrrtvgtdnivytdwqrdnyfaaiqqalpkarri
giehdhlnlqnrdklaarypdaelvdvaaacmrmr
>d1chma2 4.77.1.1.1 (157-402) Creatinase, catalytic (C-terminal) domain {(Pseudomonas putida)}
miksaeehvmirhgariadiggaavvealgdqvpeyevalhatqamvraiadtfedvelm
dtwtwfqsgintdgahnpvttrkvnkgdilslncfpmiagyytalertlfldhcsddhlr
lwqvnvevheaglklikpgarcsdiarelneiflkhdvlqyrtfgyghsfgtlshyygre
aglelredidtvlepgmvvsmepmimlpeglpgaggyrehdilivnengaenitkfpygp
ekniir
>d1chmb1 3.47.2.1.1 (2-156) Creatinase, N-terminal domain {(Pseudomonas putida)}
qmpktlrirngdkvrstfsaqeyanrqarlrahlaaenidaaiftsyhninyysdflycs
fgrpyalvvteddvisisanidggqpwrrtvgtdnivytdwqrdnyfaaiqqalpkarri
giehdhlnlqnrdklaarypdaelvdvaaacmrmr
>d1chmb2 4.77.1.1.1 (157-402) Creatinase, catalytic (C-terminal) domain {(Pseudomonas putida)}
miksaeehvmirhgariadiggaavvealgdqvpeyevalhatqamvraiadtfedvelm
dtwtwfqsgintdgahnpvttrkvnkgdilslncfpmiagyytalertlfldhcsddhlr
lwqvnvevheaglklikpgarcsdiarelneiflkhdvlqyrtfgyghsfgtlshyygre
aglelredidtvlepgmvvsmepmimlpeglpgaggyrehdilivnengaenitkfpygp
ekniir
>d1chn__ 3.14.2.1.1 CheY protein {(Escherichia coli)}
kelkflvvddfstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmpnm
dglellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleeklnki
feklgm
>d1choe_ 2.35.1.2.7 (alpha, gamma-)chymotrypsin(ogen) {bovine (Bos taurus)}
cgvpaiqpvlsglxxivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgv
ttsdvvvagefdqgsssekiqklkiakvfknskynsltinnditllklstaasfsqtvsa
vclpsasddfaagttcvttgwgltryxxantpdrlqqaslpllsntnckkywgtkikdam
icagasgvsscmgdsggplvckkngawtlvgivswgsstcststpgvyarvtalvnwvqq
tlaan
>d1choi_ 7.14.1.1.1 Ovomucoid III domain {turkey (Meleagris gallopavo)}
vsvdcseypkpactleyrplcgsdnktygnkcnfcnavvesngtltlshfgkc
>d1chpd_ 2.29.2.1.3 Cholera toxin {(Vibrio cholerae)}
tpqnitdlcaeyhntqihtlndkifsytesladkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1chpe_ 2.29.2.1.3 Cholera toxin {(Vibrio cholerae)}
tpqnitdlcaeyhntqihtlndkifsytesladkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1chpf_ 2.29.2.1.3 Cholera toxin {(Vibrio cholerae)}
tpqnitdlcaeyhntqihtlndkifsytesladkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1chpg_ 2.29.2.1.3 Cholera toxin {(Vibrio cholerae)}
tpqnitdlcaeyhntqihtlndkifsytesladkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1chph_ 2.29.2.1.3 Cholera toxin {(Vibrio cholerae)}
tpqnitdlcaeyhntqihtlndkifsytesladkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1chqd_ 2.29.2.1.3 Cholera toxin {(Vibrio cholerae)}
tpqnitdlcaeyhntqihtlndkifsyteslagkdemaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1chqe_ 2.29.2.1.3 Cholera toxin {(Vibrio cholerae)}
tpqnitdlcaeyhntqihtlndkifsyteslagkdemaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1chqf_ 2.29.2.1.3 Cholera toxin {(Vibrio cholerae)}
tpqnitdlcaeyhntqihtlndkifsyteslagkdemaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1chqg_ 2.29.2.1.3 Cholera toxin {(Vibrio cholerae)}
tpqnitdlcaeyhntqihtlndkifsyteslagkdemaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1chqh_ 2.29.2.1.3 Cholera toxin {(Vibrio cholerae)}
tpqnitdlcaeyhntqihtlndkifsyteslagkdemaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1chra1 3.1.6.2.3 (127-370) Chlormuconate cycloisomerase {(Alcaligenes eutrophus)}
plrsaipiawtlasgdtkrdldsavemierrrhnrfkvklgfrspqddlihmealsnslg
skaylrvdvnqawdeqvasvyipelealgvelieqpvgrentqalrrlsdnnrvaimade
slstlasafdlardrsvdvfslklcnmggvsatqkiaavaeasgiasyggtmldstigts
valqlystvpslpfgceligpfvladtlshepleirdyelqvptgvghgmtldedkvrqy
arvs
>d1chra2 4.32.1.1.5 (1-126) Chlormuconate cycloisomerase {(Alcaligenes eutrophus)}
mkidaieavivdvptkrpiqmsittvhqqsyvivrvyseglvgvgeggsvggpvwsaeca
etikiiverylaphllgtdafnvsgalqtmaravtgnasakaavemalldlkaralgvsi
aellgg
>d1chrb1 3.1.6.2.3 (127-370) Chlormuconate cycloisomerase {(Alcaligenes eutrophus)}
plrsaipiawtlasgdtkrdldsavemierrrhnrfkvklgfrspqddlihmealsnslg
skaylrvdvnqawdeqvasvyipelealgvelieqpvgrentqalrrlsdnnrvaimade
slstlasafdlardrsvdvfslklcnmggvsatqkiaavaeasgiasyggtmldstigts
valqlystvpslpfgceligpfvladtlshepleirdyelqvptgvghgmtldedkvrqy
arvs
>d1chrb2 4.32.1.1.5 (1-126) Chlormuconate cycloisomerase {(Alcaligenes eutrophus)}
mkidaieavivdvptkrpiqmsittvhqqsyvivrvyseglvgvgeggsvggpvwsaeca
etikiiverylaphllgtdafnvsgalqtmaravtgnasakaavemalldlkaralgvsi
aellgg
>d1cia__ 3.35.1.1.1 Chloramphenicol acetyltransferase {(Escherichia coli)}
mnytkfdvknwvrrehfefyrhrlpcgfsltskidittlkkslddsaykfypvmiyliaq
avnqfdelrmaikddelivwdsvdpqftvfhqetetfsalscpyssdidqfmvnylsvme
ryksdtklfpqgvtpenhlnisalpwvnfdsfnlnvanftdyfapiitmakyqqegdrll
lplsvqvhqavcdgfhvarfinrlqelcnsklk
>d1cid_1 2.1.1.1.4 (1-105) CD4 {rat (Rattus rattus)}
tsitayksegesaefsfplnlgeeslqgelrwkaekapssqswitfslknqkvsvqksts
npkfqlsetlpltlqipqvslqfagsgnltltldrgilyqevnlv
>d1cid_2 2.1.1.3.5 (106-177) CD4 {rat (Rattus rattus)}
vmkvtqpdsntltcevmgptspkmrlilkqenqearvsrqekviqvqapeagvwqcllse
geevkmdskiqv
>d1cie__ 1.3.1.1.6 Mitochondrial cytochrome c {baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdaiikk
nvlwdennmseyltnpkkyipgtkmasgglkkekdrndlitylkkaae
>d1cif__ 1.3.1.1.6 Mitochondrial cytochrome c {baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgahsgqaegysytdanikk
nvlwdennmseyltnpkkyipgtkmasgglkkekdrndlitylkkaae
>d1cig__ 1.3.1.1.6 Mitochondrial cytochrome c {baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgahsgqaegysytdaiikk
nvlwdennmseyltnpkkyipgtkmafgglkkekdrndlitylkkaae
>d1cih__ 1.3.1.1.6 Mitochondrial cytochrome c {baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgahsgqaegysytdaiikk
nvlwdennmseyltnpkkyipgtkmasgglkkekdrndlitylkkaae
>d1cii_1 1.105.9.1.1 (23-450) Colicin Ia, N-terminal domain {(Escherichia coli)}
eimavdiyvnpprvdvfhgtppawssfgnktiwggnewvddsptrsdiekrdkeitaykn
tlsaqqkenenkrteagkrlsaaiaarekdentlktlragnadaaditrqefrllqaelr
eygfrteiagydalrlhtesrmlfadadslrisprearslieqaekrqkdaqnadkkaad
mlaeyerrkgildtrlseleknggaalavldaqqarllgqqtrndraisearnklssvte
slntarnaltraeqqltqqkntpdgktivspekfpgrsstndsivvsgdprfagtikitt
savidnranlnyllshsgldykrnilndrnpvvtedvegdkkiynaevaewdklrqrlld
arnkitsaesavnsarnnlsartneqkhandalnallkekenirnqlsginqkiaeekrk
qdelkatk
>d1cii_2 6.1.1.1.2 (451-624) Colicin Ia {(Escherichia coli)}
dainftteflksvsekygakaeqlaremagqakgkkirnveealktyekyradinkkina
kdraaiaaalesvklsdissnlnrfsrglgyagkftsladwitefgkavrtenwrplfvk
tetiiagnaatalvalvfsiltgsalgiigygllmavtgalideslvekankfw
>d1cil__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasf
>d1cim__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasf
>d1cin__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasf
>e1ciq.1a 4.22.1.1.2 Chymotrypsin inhibitor CI-2 {barley (Hordeum vulgare), hiproly strain}
ktewpelvgksveeakkvilqdkpeaqiivlpvgtiv
>e1ciq.1b 4.22.1.1.2 Chymotrypsin inhibitor CI-2 {barley (Hordeum vulgare), hiproly strain}
eyridrvrlfvdkldniaqvprvg
>e1cir.1a 4.22.1.1.2 Chymotrypsin inhibitor CI-2 {barley (Hordeum vulgare), hiproly strain}
mktewpelvgksveeakkvilqdkpeaqiivlpvgtivt
>e1cir.1b 4.22.1.1.2 Chymotrypsin inhibitor CI-2 {barley (Hordeum vulgare), hiproly strain}
eyridrvrlfvdkldniaqvprvg
>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 2.53.1.1.5 (383-495) Cyclodextrin glycosyltransferase {(Thermoanaerobacterium thermosulfurigenes) EM1}
tsttaynvikklaplrksnpaiaygttqqrwinndvyiyerkfgnnvalvainrnlstsy
nitglytalpagtytdvlggllngnsisvasdgsvtpftlsagevavwqyvss
>d1ciu_4 3.1.1.1.5 (1-382) Cyclodextrin glycosyltransferase {(Thermoanaerobacterium thermosulfurigenes) EM1}
asdtavsnvvnystdviyqivtdrfvdgntsnnptgdlydpthtslkkyfggdwqgiink
indgyltgmgvtaiwisqpveniyavlpdstfggstsyhgywardfkrtnpyfgsftdfq
nlintahahnikviidfapnhtspasetdptyaengrlydngtllggytndtngyfhhyg
gtdfssyedgiyrnlfdladlnqqnstidsylksaikvwldmgidgirldavkhmpfgwq
knfmdsilsyrpvftfgewflgtneidvnntyfanesgmslldfrfsqkvrqvfrdntdt
mygldsmiqstasdynfindmvtfidnhdmdrfynggstrpveqalaftltsrgvpaiyy
gteqymtgngdpynrammtsfn
>d1ciy_1 2.13.1.2.2 (462-609) delta-Endotoxin, C-terminal domain {(Bacillus thuringiensis), CRYIA (A)}
nniipssqitqipltkstnlgsgtsvvkgpgftggdilrrtspgqistlrvnitaplsqr
yrvriryasttnlqfhtsidgrpinqgnfsatmssgsnlqsgsfrtvgfttpfnfsngss
vftlsahvfnsgnevyidriefvpaevt
>d1ciy_2 2.59.2.1.2 (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
>d1cjl__ 4.3.1.1.11 (Pro)cathepsin L {Human (Homo sapiens)}
dhsleaqwtkwkamhnrlygmneegwrravweknmkmielhnqeyregkhsftmamnafg
dmtseefrqvmnglqnrkprkgkvfqeplfyeaprsvdwrekgyvtpvknqgqcgsswaf
satgalegqmfrktgrlislseqnlvdcsgpegnegcngglmdyafqyvqdnggldsees
ypyeateesckynpkysvandagfvdipkqekalmkavatvgpisvaidaghesflfyke
giyfepdcssedmdhgvlvvgygfestesdgnkywlvknswgeewgmggyvkmakdrrnh
cgiasaasyptv
>d1cjpa_ 2.21.1.1.1 Concanavalin A {jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1cjpb_ 2.21.1.1.1 Concanavalin A {jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1cjpc_ 2.21.1.1.1 Concanavalin A {jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1cjpd_ 2.21.1.1.1 Concanavalin A {jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1ckaa_ 2.24.2.1.1 C-Crk, N-terminal SH3 domain {mouse (Mus musculus)}
aeyvralfdfngndeedlpfkkgdilrirdkpeeqwwnaedsegkrgmipvpyveky
>d1ckba_ 2.24.2.1.1 C-Crk, N-terminal SH3 domain {mouse (Mus musculus)}
aeyvralfdfngndeedlpfkkgdilrirdkpeeqwwnaedsegkrgmipvpyveky
>d1ckia_ 5.1.1.1.12 Casein kinase-1, CK1 {rat (Rattus norvegicus)}
melrvgnryrlgrkigsgsfgdiylgtdiaageevaiklecvktkhpqlhieskiykmmq
ggvgiptirwcgaegdynvmvmellgpsledlfnfcsrkfslktvllladqmisrieyih
sknfihrdvkpdnflmglgkkgnlvyiidfglakkyrdarthqhipyrenknltgtarya
sinthlgieqsrrddleslgyvlmyfnlgslpwqglkaatkrqkyerisekkmstpievl
ckgypsefatylnfcrslrfddkpdysylrqlfrnlfhrqgfsydyvfdwnmlkfgasr
>d1ckib_ 5.1.1.1.12 Casein kinase-1, CK1 {rat (Rattus norvegicus)}
melrvgnryrlgrkigsgsfgdiylgtdiaageevaiklecvktkhpqlhieskiykmmq
ggvgiptirwcgaegdynvmvmellgpsledlfnfcsrkfslktvllladqmisrieyih
sknfihrdvkpdnflmglgkkgnlvyiidfglakkyrdarthqhipyrenknltgtarya
sinthlgieqsrrddleslgyvlmyfnlgslpwqglkaatkrqkyerisekkmstpievl
ckgypsefatylnfcrslrfddkpdysylrqlfrnlfhrqgfsydyvfdwnml
>d1ckja_ 5.1.1.1.12 Casein kinase-1, CK1 {rat (Rattus norvegicus)}
melrvgnryrlgrkigsgsfgdiylgtdiaageevaiklecvktkhpqlhieskiykmmq
ggvgiptirwcgaegdynvmvmellgpsledlfnfcsrkfslktvllladqmisrieyih
sknfihrdvkpdnflmglgkkgnlvyiidfglakkyrdarthqhipyrenknltgtarya
sinthlgieqsrrddleslgyvlmyfnlgslpwqglkaatkrqkyerisekkmstpievl
ckgypsefatylnfcrslrfddkpdysylrqlfrnlfhrqgfsydyvfdwnmlkfg
>d1ckjb_ 5.1.1.1.12 Casein kinase-1, CK1 {rat (Rattus norvegicus)}
melrvgnryrlgrkigsgsfgdiylgtdiaageevaiklecvktkhpqlhieskiykmmq
ggvgiptirwcgaegdynvmvmellgpsledlfnfcsrkfslktvllladqmisrieyih
sknfihrdvkpdnflmglgkkgnlvyiidfglakkyrdarthqhipyrenknltgtarya
sinthlgieqsrrddleslgyvlmyfnlgslpwqglkaatkrqkyerisekkmstpievl
ckgypsefatylnfcrslrfddkpdysylrqlfrnlfhrqgfsydyvfdwnml
>d1ckma1 2.29.4.6.1 (239-327) RNA guanylyltransferase (mRNA capping enzyme) {(Chlorella virus PBCV-1)}
thhtidfiimsedgtigifdpnlrknvpvgkldgyynkgsivecgfadgtwkyiqgrsdk
nqandrltyektllnieenitidelldlf
>d1ckma2 4.89.2.2.1 (11-238) RNA guanylyltransferase (mRNA capping enzyme), N-terminal domain {(Chlorella virus PBCV-1)}
nitteravltlnglqiklhkvvgesrddivakmkdlamddhkfprlpgpnpvsierkdfe
klkqnkyvvsektdgirfmmfftrvfgfkvctiidramtvyllpfkniprvlfqgsifdg
elcvdivekkfafvlfdavvvsgvtvsqmdlasrffamkrslkefknvpedpailrykew
iplehptiikdhlkkanaiyhtdgliimsvdepviygrnfnlfklkpg
>d1ckmb1 2.29.4.6.1 (239-327) RNA guanylyltransferase (mRNA capping enzyme) {(Chlorella virus PBCV-1)}
thhtidfiimsedgtigifdpnlrknvpvgkldgyynkgsivecgfadgtwkyiqgrsdk
nqandrltyektllnieenitidelldlf
>d1ckmb2 4.89.2.2.1 (11-238) RNA guanylyltransferase (mRNA capping enzyme), N-terminal domain {(Chlorella virus PBCV-1)}
nitteravltlnglqiklhkvvgesrddivakmkdlamddhkfprlpgpnpvsierkdfe
klkqnkyvvsektdgirfmmfftrvfgfkvctiidramtvyllpfkniprvlfqgsifdg
elcvdivekkfafvlfdavvvsgvtvsqmdlasrffamkrslkefknvpedpailrykew
iplehptiikdhlkkanaiyhtdgliimsvdepviygrnfnlfklkpg
>d1ckna1 2.29.4.6.1 (239-327) RNA guanylyltransferase (mRNA capping enzyme) {(Chlorella virus PBCV-1)}
thhtidfiimsedgtigifdpnlrknvpvgkldgyynkgsivecgfadgtwkyiqgrsdk
nqandrltyektllnieenitidelldlf
>d1ckna2 4.89.2.2.1 (11-238) RNA guanylyltransferase (mRNA capping enzyme), N-terminal domain {(Chlorella virus PBCV-1)}
nitteravltlnglqiklhkvvgesrddivakmkdlamddhkfprlpgpnpvsierkdfe
klkqnkyvvsektdgirfmmfftrvfgfkvctiidramtvyllpfkniprvlfqgsifdg
elcvdivekkfafvlfdavvvsgvtvsqmdlasrffamkrslkefknvpedpailrykew
iplehptiikdhlkkanaiyhtdgliimsvdepviygrnfnlfklkpg
>d1cknb1 2.29.4.6.1 (239-327) RNA guanylyltransferase (mRNA capping enzyme) {(Chlorella virus PBCV-1)}
thhtidfiimsedgtigifdpnlrknvpvgkldgyynkgsivecgfadgtwkyiqgrsdk
nqandrltyektllnieenitidelldlf
>d1cknb2 4.89.2.2.1 (11-238) RNA guanylyltransferase (mRNA capping enzyme), N-terminal domain {(Chlorella virus PBCV-1)}
nitteravltlnglqiklhkvvgesrddivakmkdlamddhkfprlpgpnpvsierkdfe
klkqnkyvvsextdgirfmmfftrvfgfkvctiidramtvyllpfkniprvlfqgsifdg
elcvdivekkfafvlfdavvvsgvtvsqmdlasrffamkrslkefknvpedpailrykew
iplehptiikdhlkkanaiyhtdgliimsvdepviygrnfnlfklkpg
>d1cko_1 2.29.4.6.1 (239-327) RNA guanylyltransferase (mRNA capping enzyme) {(Chlorella virus PBCV-1)}
thhtidfiimsedgtigifdpnlrknvpvgkldgyynkgsivecgfadgtwkyiqgrsdk
nqandrltyektllnieenitidelldlf
>d1cko_2 4.89.2.2.1 (11-238) RNA guanylyltransferase (mRNA capping enzyme), N-terminal domain {(Chlorella virus PBCV-1)}
nitteravltlnglqiklhkvvgesrddivakmkdlamddhkfprlpgpnpvsierkdfe
klkqnkyvvsektdgirfmmfftrvfgfkvctiidramtvyllpfkniprvlfqgsifdg
elcvdivekkfafvlfdavvvsgvtvsqmdlasrffamkrslkefknvpedpailrykew
iplehptiikdhlkkanaiyhtdgliimsvdepviygrnfnlfklkpg
>d1cksa_ 4.57.1.1.2 CksHs2 {Human (Homo sapiens)}
ahkqiyysdkyfdehyeyrhvmlprelskqvpkthlmseeewrrlgvqqslgwvhymihe
pephillfrrplpk
>d1cksb_ 4.57.1.1.2 CksHs2 {Human (Homo sapiens)}
ahkqiyysdkyfdehyeyrhvmlprelskqvpkthlmseeewrrlgvqqslgwvhymihe
pephillfrrplpkdqqk
>d1cksc_ 4.57.1.1.2 CksHs2 {Human (Homo sapiens)}
ahkqiyysdkyfdehyeyrhvmlprelskqvpkthlmseeewrrlgvqqslgwvhymihe
pephillfrrplpkdqqk
>d1cla__ 3.35.1.1.1 Chloramphenicol acetyltransferase {(Escherichia coli)}
mnytkfdvknwvrrehfefyrhrlpcgfsltskidittlkkslddsaykfypvmiyliaq
avnqfdelrmaikddelivwdsvdpqftvfhqetetfsalscpyssdidqfmvnylsvme
ryksdtklfpqgvtpenhlniaalpwvnfdsfnlnvanftdyfapiitmakyqqegdrll
lplsvqvhhavcdgfhvarfinrlqelcnsklk
>d1clb__ 1.37.1.1.1 Calbindin D9K {bovine (Bos taurus)}
kspeelkgifekyaakegdpnqlskeelklllqtefpsllkggstldelfeeldkngdge
vsfeefqvlvkkisq
>d1clc_1 1.81.1.2.3 (135-575) CelD cellulase {(Clostridium thermocellum)}
amnvyedafktamlgmyllrcgtsvsatyngihyshgpchtndayldyingqhtkkdstk
gwhdagdynkyvvnagitvgsmflawehfkdqlepvaleipeknnsipdfldelkyeidw
iltmqypdgsgrvahkvstrnfggfimpenehderffvpwssaatadfvamtamaarifr
pydpqyaekcinaakvsyeflknnpanvfanqsgfstgeyatvsdaddrlwaaaemwetl
gdeeylrdfenraaqfskkieadfdwdnvanlgmftyllserpgknpalvqsikdsllst
adsivrtsqnhgygrtlgttyywgcngtvvrqtmilqvankispnndyvnaaldaishvf
grnyynrsyvtglginppmnphdrrsgadgiwepwpgylvgggwpgpkdwvdiqdsyqtn
eiainwnaaliyalagfvnyn
>d1clc_2 2.1.1.5.10 (35-134) CelD cellulase, N-terminal domain {(Clostridium thermocellum)}
ietkvsaakitenyqfdsrirlnsigfipnhskkatiaancstfyvvkedgtivytgtat
smfdndtketvyiadfssvneegtyylavpgvgksvnfki
>d1cld__ 7.32.1.1.5 CD2-Lac9 {Yeast (Kluyveromyces lactis)}
qacdacrkkkwkcsktvptctnclkynldcvys
>d1clea_ 3.56.1.9.9 type-B carboxylesterase/lipase {(Candida cylindracea), cholesterol esterase}
aptaklangdtitglnaiineaflgipfaeppvgnlrfkdpvpysgslngqkftsygpsc
mqqnpegtfeenlgktaldlvmqskvfqavlpqsedcltinvvrppgtkaganlpvmlwi
fgggfeigsptifppaqmvtksvlmgkpiihvavnyrvaswgflagddikaegsgnaglk
dqrlgmqwvadniagfggdpskvtifgesagsmsvlchliwndgdntykgkplfragimq
sgamvpsdpvdgtygneiydlfvssagcgsasdklaclrsassdtlldatnntpgflays
slrlsylprpdgknitddmyklvrdgkyasvpviigdqndegtvfglsslnvttnaqara
yfkqsfihasdaeidtlmaaypqditqgspfdtgifnaitpqfkrisavlgdlafiharr
yflnhfqggtkysflskqlsglpimgtfhandivwqdyllgsgsviynnafiafatdldp
ntagllvnwpkytsssqsgnnlmminalglytgkdnfrtagydalmtnpssffv
>d1cleb_ 3.56.1.9.9 type-B carboxylesterase/lipase {(Candida cylindracea), cholesterol esterase}
aptaklangdtitglnaiineaflgipfaeppvgnlrfkdpvpysgslngqkftsygpsc
mqqnpegtfeenlgktaldlvmqskvfqavlpqsedcltinvvrppgtkaganlpvmlwi
fgggfeigsptifppaqmvtksvlmgkpiihvavnyrvaswgflagddikaegsgnaglk
dqrlgmqwvadniagfggdpskvtifgesagsmsvlchliwndgdntykgkplfragimq
sgamvpsdpvdgtygneiydlfvssagcgsasdklaclrsassdtlldatnntpgflays
slrlsylprpdgknitddmyklvrdgkyasvpviigdqndegtvfglsslnvttnaqara
yfkqsfihasdaeidtlmaaypqditqgspfdtgifnaitpqfkrisavlgdlafiharr
yflnhfqggtkysflskqlsglpimgtfhandivwqdyllgsgsviynnafiafatdldp
ntagllvnwpkytsssqsgnnlmminalglytgkdnfrtagydalmtnpssffv
>d1clf__ 4.34.1.1.4 Ferredoxin II {(Closridium pasteurianum)}
aykiadscvscgacasecpvnaisqgdsifvidadtcidcgncanvcpvgapvqe
>d1clh__ 2.47.1.1.5 Cyclophilin {(Escherichia coli)}
akgdphvllttsagnieleldkqkapvsvqnfvdyvnsgfynnttfhrvipgfmiqgggf
teqmqqkkpnppikneadnglrntrgtiamartadkdsatsqffinvadnafldhgqrdf
gyavfgkvvkgmdvadkisqvpthdvgpyqnvpskpvvilsakvlp
>d1cll__ 1.37.1.5.7 Calmodulin {human (Homo sapiens)}
lteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngti
dfpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevde
mireadidgdgqvnyeefvqmmta
>d1clm__ 1.37.1.5.13 Calmodulin {(Paramecium tetraurelia)}
lteeqiaefkeafalfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngti
dfpeflslmarkmkeqdseeelieafkvfdrdgnglisaaelrhvmtnlgekltddevde
mireadidgdghinyeefvrmmvs
>d1cloh1 2.1.1.1.75 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab A5B7 (mouse), kappa L chain}
evklvesggglvqpggslrlscatsgftftdyymnwvrqppgkalewlgfignkangytt
eysasvkgrftisrdksqsilylqmntlraedsatyyctrdrglrfyfdywgqgttltvs
s
>d1cloh2 2.1.1.2.78 (114-214) Immunoglobulin (constant domains of L and H chains) {Fab A5B7 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpssprpsetvtcnvahpasstkvdkkivprd
>d1clol1 2.1.1.1.75 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab A5B7 (mouse), kappa L chain}
qtvlsqspailsaspgekvtmtcrasssvtyihwyqqkpgsspkswiyatsnlasgvpar
fsgsgsgtsysltisrveaedaatyycqhwsskpptfgggtkleik
>d1clol2 2.1.1.2.78 (108-214) Immunoglobulin (constant domains of L and H chains) {Fab A5B7 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1clpa_ 1.103.1.2.14 Myotoxin II {Terciopelo (Bothrops asper)}
slfelgkmilqetgknpaksygaygcncgvlgrgkpkdatdrccyvhkccykkltgcnpk
kdrysyswkdktivcgennsclkelcecdkavaiclrenlntynkkyryylkplckkada
c
>d1clpb_ 1.103.1.2.14 Myotoxin II {Terciopelo (Bothrops asper)}
slfelgkmilqetgknpaksygaygcncgvlgrgkpkdatdrccyvhkccykkltgcnpk
kdrysyswkdktivcgennsclkelcecdkavaiclrenlntynkkyryylkplckkada
c
>d1clsa_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1clsb_ 1.1.1.1.25 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_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1clxa_ 3.1.1.3.11 Xylanase A, catalytic core {(Pseudomonas fluorescens)}
glasladfpigvavaasggnadiftssarqnivraefnqitaenimkmsymysgsnfsft
nsdrlvswaaqngqtvhghalvwhpsyqlpnwasdsnanfrqdfarhidtvaahfagqvk
swdvvnealfdsaddpdgrgsangyrqsvfyrqfggpeyideafrraraadptaelyynd
fnteengakttalvnlvqrllnngvpidgvgfqmhvmndypsianirqamqkivalsptl
kikiteldvrlnnpydgnssndytnrndcavscagldrqkarykeivqaylevvppgrrg
gitvwgiadpdswlythqnlpdwpllfndnlqpkpayqgvveals
>d1clxb_ 3.1.1.3.11 Xylanase A, catalytic core {(Pseudomonas fluorescens)}
glasladfpigvavaasggnadiftssarqnivraefnqitaenimkmsymysgsnfsft
nsdrlvswaaqngqtvhghalvwhpsyqlpnwasdsnanfrqdfarhidtvaahfagqvk
swdvvnealfdsaddpdgrgsangyrqsvfyrqfggpeyideafrraraadptaelyynd
fnteengakttalvnlvqrllnngvpidgvgfqmhvmndypsianirqamqkivalsptl
kikiteldvrlnnpydgnssndytnrndcavscagldrqkarykeivqaylevvppgrrg
gitvwgiadpdswlythqnlpdwpllfndnlqpkpayqgvveals
>d1clxc_ 3.1.1.3.11 Xylanase A, catalytic core {(Pseudomonas fluorescens)}
glasladfpigvavaasggnadiftssarqnivraefnqitaenimkmsymysgsnfsft
nsdrlvswaaqngqtvhghalvwhpsyqlpnwasdsnanfrqdfarhidtvaahfagqvk
swdvvnealfdsaddpdgrgsangyrqsvfyrqfggpeyideafrraraadptaelyynd
fnteengakttalvnlvqrllnngvpidgvgfqmhvmndypsianirqamqkivalsptl
kikiteldvrlnnpydgnssndytnrndcavscagldrqkarykeivqaylevvppgrrg
gitvwgiadpdswlythqnlpdwpllfndnlqpkpayqgvveals
>d1clxd_ 3.1.1.3.11 Xylanase A, catalytic core {(Pseudomonas fluorescens)}
glasladfpigvavaasggnadiftssarqnivraefnqitaenimkmsymysgsnfsft
nsdrlvswaaqngqtvhghalvwhpsyqlpnwasdsnanfrqdfarhidtvaahfagqvk
swdvvnealfdsaddpdgrgsangyrqsvfyrqfggpeyideafrraraadptaelyynd
fnteengakttalvnlvqrllnngvpidgvgfqmhvmndypsianirqamqkivalsptl
kikiteldvrlnnpydgnssndytnrndcavscagldrqkarykeivqaylevvppgrrg
gitvwgiadpdswlythqnlpdwpllfndnlqpkpayqgvveals
>d1clyh1 2.1.1.1.68 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab CBR96 (mouse/human), kappa L chain}
evnlvesggglvqpggslkvscvtsgftfsdyymywvrqtpekrlewvayisqggditdy
pdtvkgrftisrdnaknslylqmsrlksedtamyycarglddgawfaywgqgtlvtvsv
>d1clyh2 2.1.1.2.72 (114-227) Immunoglobulin (constant domains of L and H chains) {Fab CBR96 (mouse/human), kappa L chain}
astkgpsvfplapsskstsggtaalgclvkdyfpqpvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkrvep
>d1clyl1 2.1.1.1.68 (3-108) Immunoglobulin (variable domains of L and H chains) {Fab CBR96 (mouse/human), kappa L chain}
lmtqipvslpvslgdqasiscrssqiivhnngntylewylqkpgqspqlliykvsnrfsg
vpdrfsgsgsgtdftlkisrveaedlgvyycfqgshvpftfgsgtkleikr
>d1clyl2 2.1.1.2.72 (109-214) Immunoglobulin (constant domains of L and H chains) {Fab CBR96 (mouse/human), kappa L chain}
tvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqds
kdstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1clzh1 2.1.1.1.69 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab MBR96 (mouse), kappa L chain}
evnlvesggglvqpggslkvscvtsgftfsdyymywvrqtpekrlewvayisqggditdy
pdtvkgrftisrdnaknslylqmsrlksedtamyycarglddgawfaywgqgtlvtvsv
>d1clzh2 2.1.1.2.73 (115-231) Immunoglobulin (constant domains of L and H chains) {Fab MBR96 (mouse), kappa L chain}
tttapsvyplvpgcsdtsgssvtlgclvkgyfpepvtvkwnygalssgvrtvssvlqsgf
yslsslvtvpsstwpsqtvicnvahpasktelikriepr
>d1clzl1 2.1.1.1.69 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab MBR96 (mouse), kappa L chain}
dvlmtqipvslpvslgdqasiscrssqiivhnngntylewylqkpgqspqlliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyycfqgshvpftfgsgtkleikr
>d1clzl2 2.1.1.2.73 (109-214) Immunoglobulin (constant domains of L and H chains) {Fab MBR96 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1cm1a_ 1.37.1.5.8 Calmodulin {bovine (Bos taurus)}
lteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngti
dfpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevde
mireadidgdgqvnyeefvqmmt
>d1cm4a_ 1.37.1.5.8 Calmodulin {bovine (Bos taurus)}
lteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngti
dfpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevde
mireadidgdgqvnyeefvqmmt
>d1cm4c_ 1.37.1.5.8 Calmodulin {bovine (Bos taurus)}
lteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngti
dfpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevde
mireadidgdgqvnyeefvqmmt
>d1cm4e_ 1.37.1.5.8 Calmodulin {bovine (Bos taurus)}
lteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngti
dfpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevde
mireadidgdgqvnyeefvqmmt
>d1cm4g_ 1.37.1.5.8 Calmodulin {bovine (Bos taurus)}
lteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngti
dfpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevde
mireadidgdgqvnyeefvqmmt
>d1cmaa_ 1.41.1.2.1 Met repressor {(Escherichia coli)}
aewsgeyispyaehgkkseqvkkitvsiplkvlkiltdertrrqvnnlrhatnsellcea
flhaftgqplpddadlrkersdeipeaakeimremginpetwey
>d1cmab_ 1.41.1.2.1 Met repressor {(Escherichia coli)}
aewsgeyispyaehgkkseqvkkitvsiplkvlkiltdertrrqvnnlrhatnsellcea
flhaftgqplpddadlrkersdeipeaakeimremginpetwey
>d1cmba_ 1.41.1.2.1 Met repressor {(Escherichia coli)}
aewsgeyispyaehgkkseqvkkitvsiplkvlkiltdertrrqvnnlrhatnsellcea
flhaftgqplpddadlrkersdeipeaakeimremginpetwey
>d1cmbb_ 1.41.1.2.1 Met repressor {(Escherichia coli)}
aewsgeyispyaehgkkseqvkkitvsiplkvlkiltdertrrqvnnlrhatnsellcea
flhaftgqplpddadlrkersdeipeaakeimremginpetwey
>d1cmca_ 1.41.1.2.1 Met repressor {(Escherichia coli)}
aewsgeyispyaehgkkseqvkkitvsiplkvlkiltdertrrqvnnlrhatnsellcea
flhaftgqplpddadlrkersdeipeaakeimremginpetwey
>d1cmcb_ 1.41.1.2.1 Met repressor {(Escherichia coli)}
aewsgeyispyaehgkkseqvkkitvsiplkvlkiltdertrrqvnnlrhatnsellcea
flhaftgqplpddadlrkersdeipeaakeimremginpetwey
>d1cmf__ 1.37.1.5.8 Calmodulin {bovine (Bos taurus)}
mkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevdemireadidgdgq
vnyeefvqmmtak
>d1cmg__ 1.37.1.5.8 Calmodulin {bovine (Bos taurus)}
mkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevdemireadidgdgq
vnyeefvqmmtak
>d1cmke_ 5.1.1.1.2 cAMP-dependent PK, catalytic subunit {pig (Sus scrofa)}
gnaaaakkgseqesvkeflakakedflkkwenpaqntahldqferiktlgtgsfgrvmlv
khketgnhfamkildkqkvvklkqiehtlnekrilqavnfpflvkleysfkdnsnlymvm
eyvpggemfshlrrigrfsepharfyaaqivltfeylhsldliyrdlkpenllidqqgyi
qvtdfgfakrvkgrtwtlcgtpeylapeiilskgynkavdwwalgvliyemaagyppffa
dqpiqiyekivsgkvrfpshfssdlkdllrnllqvdltkrfgnlkdgvndiknhkwfatt
dwiaiyqrkveapfipkfkgpgdtsnfddyeeeeirvsinekcgkefsef
>d1cmp__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1cmq__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1cmr__ 7.3.6.2.4 Charybdotoxin {scorpion (Leiurus quinquestriatus hebraeus)}
cttskecwsvcqrlhntskgwcdhrgcices
>d1cms__ 2.38.1.2.13 Chymosin (synonim: renin) {bovine (Bos taurus)}
gevasvpltnyldsqyfgkiylgtppqeftvlfdtgssdfwvpsiycksnacknhqrfdp
rksstfqnlgkplsihygtgsmqgilgydtvtvsnivdiqqtvglstqepgdvftyaefd
gilgmaypslaseysipvfdnmmnrhlvaqdlfsvymdrngqesmltlgaidpsyytgsl
hwvpvtvqqywqftvdsvtisgvvvaceggcqaildtgtsklvgpssdilniqqaigatq
nqygefdidcdnlsymptvvfeingkmypltpsaytsqdqgfctsgfqsenhsqkwilgd
vfireyysvfdrannlvglakai
>d1cmt__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1cmu__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptnysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1cmva_ 2.43.1.1.1 Human cytomegalovirus protease {(Human cytomegalovirus), hCMV}
apvyvggflarydqspdeaelllprdvvehwlhaqgqgqpslsvalplninhddtavvgh
vaamqsvrdglfclgcvtsprfleivrrasekselvsrgpvsplqpdkvveflsgsyagl
slssrrcddaeaptslsgsettpfkhvalcsvgrrrgtlavygrdpewvtqrfpdltaad
rdglraqwqrcgstavdasgdpfrsdsygllgnsvdalyirerlpklrydkqlvgvtere
syvka
>d1cmvb_ 2.43.1.1.1 Human cytomegalovirus protease {(Human cytomegalovirus), hCMV}
vapvyvggflarydqspdeaelllprdvvehwlhaqgqgqpslsvalplninhddtavvg
hvaamqsvrdglfclgcvtsprfleivrrasekselvsrgpvsplqpdkvveflsgsyag
lslssrrcddaeaptslsgsettpfkhvalcsvgrrrgtlavygrdpewvtqrfpdltaa
drdglraqwqrcgstavdasgdpfrsdsygllgnsvdalyirerlpklrydkqlvgvter
esyvka
>d1cmya_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1cmyb_ 1.1.1.1.25 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_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvypenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1cn1a_ 2.21.1.1.1 Concanavalin A {jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqdgkvgtahiiynsvdkr
lsavvsypnadatsvsydvdlndvlpewvrvglsastglyketntilswsftsklksnst
hqtdalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspegssvgralfyapvh
iwessaatvsfeatfaflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1cn1b_ 2.21.1.1.1 Concanavalin A {jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqdgkvgtahiiynsvdkr
lsavvsypnadatsvsydvdlndvlpewvrvglsastglyketntilswsftsklksnst
hqtdalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspegssvgralfyapvh
iwessaatvsfeatfaflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1cnb__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfcfhwgsldgqgsehtvdkkkyaaelhlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1cnc__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfcfhwgsldgqgsehtvdkkkyaaelhlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1cne_1 2.32.1.1.5 (11-124) Nitrate reductase core domain {corn (Zea mays)}
grihcrlvakkelsrdvrlfrfslpspdqvlglpigkhifvcatiegklcmraytptsmv
deighfdllvkvyfknehpkfpngglmtqyldslpvgsyidvkgplghveytgr
>d1cne_2 3.16.1.1.5 (125-270) Nitrate reductase {corn (Zea mays)}
gsfvingkqrnarrlamicggsgitpmyqiiqavlrdqpedhtemhlvyanrteddillr
deldrwaaeypdrlkvwyvidqvkrpeegwkysvgfvteavlrehvpeggddtlalasgp
ppmiqfaispnlekmkydmansfvvf
>d1cnf_1 2.32.1.1.5 (11-124) Nitrate reductase core domain {corn (Zea mays)}
grihcrlvakkelsrdvrlfrfslpspdqvlglpigkhifvcatiegklcmraytptsmv
deighfdllvkvyfknehpkfpngglmtqyldslpvgsyidvkgplghveytgr
>d1cnf_2 3.16.1.1.5 (125-270) Nitrate reductase {corn (Zea mays)}
gsfvingkqrnarrlamicggsgitpmyqiiqavlrdqpedhtemhlvyanrteddillr
deldrwaaeypdrlkvwyvidqvkrpeegwkysvgfvteavlrehvpeggddtlalacgp
ppmiqfaispnlekmkydmansfvvf
>d1cng__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaalhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasfk
>d1cnh__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliefhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasfk
>d1cni__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliafhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasfk
>d1cnj__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrlinfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasfk
>d1cnk__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrlilfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasfk
>d1cnpa_ 1.37.1.2.1 Calcyclin (S100) {Rabbit (Oryctolagus cuniculus)}
maspldqaiglligifhkysgkegdkhtlskkelkeliqkeltigsklqdaeivklmddl
drnkdqevnfqeyitflgalamiynealkg
>d1cnpb_ 1.37.1.2.1 Calcyclin (S100) {Rabbit (Oryctolagus cuniculus)}
maspldqaiglligifhkysgkegdkhtlskkelkeliqkeltigsklqdaeivklmddl
drnkdqevnfqeyitflgalamiynealkg
>d1cnr__ 7.12.1.1.1 Crambin {abyssinian cabbage (Crambe abyssinica)}
ttccpsivarsnfnvcrlpgtpealcatytgciiipgatcpgdyan
>d1cnsa_ 4.2.1.1.1 Barley endochitinase {pearled barley (Hordeum vulgare l.)}
svssivsraqfdrmllhrndgacqakgfytydafvaaaaafsgfgttgsadvqkrevaaf
laqtshettggwatapdgafawgycfkqergassdyctpsaqwpcapgkryygrgpiqls
hnynygpagraigvdllanpdlvatdatvsfktamwfwmtaqppkpsshavivgqwspsg
adraagrvpgfgvitniinggiecghgqdsrvadrigfykrycdilgvgygnnldcysqr
pfa
>d1cnsb_ 4.2.1.1.1 Barley endochitinase {pearled barley (Hordeum vulgare l.)}
svssivsraqfdrmllhrndgacqakgfytydafvaaaaafsgfgttgsadvqkrevaaf
laqtshettggwatapdgafawgycfkqergassdyctpsaqwpcapgkryygrgpiqls
hnynygpagraigvdllanpdlvatdatvsfktamwfwmtaqppkpsshavivgqwspsg
adraagrvpgfgvitniinggiecghgqdsrvadrigfykrycdilgvgygnnldcysqr
pfa
>d1cnt1_ 1.26.1.1.7 Ciliary neurotrophic factor (CNTF) {Human (Homo sapiens)}
phrrdlcsrsiwlarkirsdltaltesyvkhqglnkninldsadgmpvastdqwseltea
erlqenlqayrtfhvllarlledqqvhftptegdfhqaihtlllqvaafayqieelmill
eykiprneadgmpinvgdgglfekklwglkvlqelsqwtvrsihdlrfisshqtgip
>d1cnt2_ 1.26.1.1.7 Ciliary neurotrophic factor (CNTF) {Human (Homo sapiens)}
hrrdlcsrsiwlarkirsdltaltesyvkhqglnkninldsadgmpvastdqwselteae
rlqenlqayrtfhvllarlledqqvhftptegdfhqaihtlllqvaafayqieelmille
ykiprneadgmpinvgdgglfekklwglkvlqelsqwtvrsihdlrfisshqtgip
>d1cnt3_ 1.26.1.1.7 Ciliary neurotrophic factor (CNTF) {Human (Homo sapiens)}
phrrdlcsrsiwlarkirsdltaltesyvkhqglnkninldsadgmpvastdqwseltea
erlqenlqayrtfhvllarlledqqvhftptegdfhqaihtlllqvaafayqieelmill
eykiprneadgmpinvgdgglfekklwglkvlqelsqwtvrsihdlrfissh
>d1cnt4_ 1.26.1.1.7 Ciliary neurotrophic factor (CNTF) {Human (Homo sapiens)}
hrrdlcsrsiwlarkirsdltaltesyvkhqglnkninldsadgmpvastdqwselteae
rlqenlqayrtfhvllarlledqqvhftptegdfhqaihtlllqvaafayqieelmille
ykiprneadgmpinvgdgglfekklwglkvlqelsqwtvrsihdlrfis
>d1cnv__ 3.1.1.5.3 Seed storage protein {jack bean (Canavalia ensiformis), Concanavalin B}
dissteiavywgqredgllrdtcktnnykivfisfldkfgceirkpelelegvcgpsvgn
pcsflesqikecqrmgvkvflalggpkgtysacsadyakdlaeylhtyflserregplgk
valdgihfdiqkpvdelnwdnlleelyqikdvyqstfllsaapgclspdeyldnaiqtrh
fdyifvrfyndrscqystgniqrirnawlswtksvyprdknlflelpasqatapgggyip
psaligqvlpylpdlqtryagialwnrqadketgystniiryl
>d1cnw__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasf
>d1cnx__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasf
>d1cny__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasf
>d1coai_ 4.22.1.1.2 Chymotrypsin inhibitor CI-2 {barley (Hordeum vulgare), hiproly strain}
mktewpelvgksveeakkvilqdkpeaqiivlpvgtivtmeyridrvrlfvdkldnvaev
prvg
>d1coba_ 2.1.7.1.1 Cu,Zn superoxide dismutase, SOD {bovine (Bos taurus)}
atkavcvlkgdgpvqgtihfeakgdtvvvtgsitgltegdhgfhvhqfgdntqgctsagp
hfnplskkhggpkdeerhvgdlgnvtadkngvaivdivdplislsgeysiigrtmvvhek
pddlgrggneestktgnagsrlacgvigiak
>d1cobb_ 2.1.7.1.1 Cu,Zn superoxide dismutase, SOD {bovine (Bos taurus)}
atkavcvlkgdgpvqgtihfeakgdtvvvtgsitgltegdhgfhvhqfgdntqgctsagp
hfnplskkhggpkdeerhvgdlgnvtadkngvaivdivdplislsgeysiigrtmvvhek
pddlgrggneestktgnagsrlacgvigiak
>d1cod__ 7.6.1.1.18 Cobrotoxin II {taiwan cobra (Naja naja atra)}
lechnqqssqtptttgcsggetncykkrwrdhrgyrtergcgcpsvkngieinccttdrc
nn
>d1coe__ 7.6.1.1.18 Cobrotoxin II {taiwan cobra (Naja naja atra)}
lechnqqssqtptttgcsggetncykkrwrdhrgyrtergcgcpsvkngieinccttdrc
nn
>d1cof__ 4.62.1.2.1 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_ 1.1.1.1.25 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_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>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_ 4.40.1.1.1 Chorismate mutase {(Bacillus subtilis)}
mirgirgattverdteeeilqktkqllekiieenhtkpedvvqmllsatpdlhavfpaka
vrelsgwqyvpvtcmqemdvtgglkkcirvmmtvqtdvpqdqirhvylekavvl
>d1comb_ 4.40.1.1.1 Chorismate mutase {(Bacillus subtilis)}
mirgirgattverdteeeilqktkqllekiieenhtkpedvvqmllsatpdlhavfpaka
vrelsgwqyvpvtcmqemdvtgglkkcirvmmtvqtdvpqdqirhvylekavvlrpdl
>d1comc_ 4.40.1.1.1 Chorismate mutase {(Bacillus subtilis)}
mirgirgattverdteeeilqktkqllekiieenhtkpedvvqmllsatpdlhavfpaka
vrelsgwqyvpvtcmqemdvtgglkkcirvmmtvqtdvpqdqirhvylekavvlrpdls
>d1comd_ 4.40.1.1.1 Chorismate mutase {(Bacillus subtilis)}
mirgirgattverdteeeilqktkqllekiieenhtkpedvvqmllsatpdlhavfpaka
vrelsgwqyvpvtcmqemdvtgglkkcirvmmtvqtdvpqdqirhvylekavvl
>d1come_ 4.40.1.1.1 Chorismate mutase {(Bacillus subtilis)}
mirgirgattverdteeeilqktkqllekiieenhtkpedvvqmllsatpdlhavfpaka
vrelsgwqyvpvtcmqemdvtgglkkcirvmmtvqtdvpqdqirhvylekavvlrpdl
>d1comf_ 4.40.1.1.1 Chorismate mutase {(Bacillus subtilis)}
mirgirgattverdteeeilqktkqllekiieenhtkpedvvqmllsatpdlhavfpaka
vrelsgwqyvpvtcmqemdvtgglkkcirvmmtvqtdvpqdqirhvylekavvlrpd
>d1comg_ 4.40.1.1.1 Chorismate mutase {(Bacillus subtilis)}
mirgirgattverdteeeilqktkqllekiieenhtkpedvvqmllsatpdlhavfpaka
vrelsgwqyvpvtcmqemdvtgglkkcirvmmtvqtdvpqdqirhvylekavvl
>d1comh_ 4.40.1.1.1 Chorismate mutase {(Bacillus subtilis)}
mirgirgattverdteeeilqktkqllekiieenhtkpedvvqmllsatpdlhavfpaka
vrelsgwqyvpvtcmqemdvtgglkkcirvmmtvqtdvpqdqirhvylekavvl
>d1comi_ 4.40.1.1.1 Chorismate mutase {(Bacillus subtilis)}
mirgirgattverdteeeilqktkqllekiieenhtkpedvvqmllsatpdlhavfpaka
vrelsgwqyvpvtcmqemdvtgglkkcirvmmtvqtdvpqdqirhvylekavvl
>d1comj_ 4.40.1.1.1 Chorismate mutase {(Bacillus subtilis)}
mirgirgattverdteeeilqktkqllekiieenhtkpedvvqmllsatpdlhavfpaka
vrelsgwqyvpvtcmqemdvtgglkkcirvmmtvqtdvpqdqirhvylekavvl
>d1comk_ 4.40.1.1.1 Chorismate mutase {(Bacillus subtilis)}
mirgirgattverdteeeilqktkqllekiieenhtkpedvvqmllsatpdlhavfpaka
vrelsgwqyvpvtcmqemdvtgglkkcirvmmtvqtdvpqdqirhvylekavvlrp
>d1coml_ 4.40.1.1.1 Chorismate mutase {(Bacillus subtilis)}
mirgirgattverdteeeilqktkqllekiieenhtkpedvvqmllsatpdlhavfpaka
vrelsgwqyvpvtcmqemdvtgglkkcirvmmtvqtdvpqdqirhvylekavvl
>d1cona_ 2.21.1.1.1 Concanavalin A {jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1coo__ 1.34.1.1.1 the C-terminal domain of RNA polymerase alpha subunit {(Escherichia coli)}
fdpillrpvddleltvrsanclkaeaihyigdlvqrtevellktpnlgkkslteikdvla
srglslgmrlenwppasiade
>d1copd_ 1.32.1.2.5 cro lambda repressor {(Escherichia coli) bacteriophage Lambda}
meqritlkdyamrfgqtktakdlgvyqsainkaihagrkifltinadgsvyaeevkpfps
nkktta
>d1cope_ 1.32.1.2.5 cro lambda repressor {(Escherichia coli) bacteriophage Lambda}
meqritlkdyamrfgqtktakdlgvyqsainkaihagrkifltinadgsvyaeevkpfps
nkktta
>d1cor__ 1.3.1.1.18 Cytochrome c551 {(Pseudomonas stutzeri)}
xdgealfkskpcaachsidaklvgpafkevaakyagqdgaadllaghikngsqgvwgpip
mppnpvteeeakilaewilsqk
>d1cot__ 1.3.1.1.16 Cytochrome c2 {(Paracoccus denitrificans)}
dgdaakgekefnkckachmiqapdgtdiikggktgpnlygvvgrkiaseegfkygegile
vaeknpdltwteadlieyvtdpkpwlvkmtddkgaktkmtfkmgknqadvvaflaqnspd
a
>d1cov1_ 2.8.1.4.12 Coxsackievirus B3 {Host: human (Homo sapiens)}
rvadtvgtgptnseaipaltaaetghtsqvvpsdtmqtrhvknyhsrsestienflcrsa
cvyfteyensgakryaewvitprqaaqlrrklefftyvrfdleltfvitstqqpsttqnq
daqilthqimyvppggpvpdkvdsyvwqtstnpsvfwtegnapprmsvpflsignaysnf
ydgwsefsrngvygintlnnmgtlyarhvnagstgpikstiriyfkpkhvkawiprpprl
cqyekaknvnfqpsgvtttrqsittmtnt
>d1cov2_ 2.8.1.4.12 Coxsackievirus B3 {Host: human (Homo sapiens)}
gysdrvrsitlgnstittqecanvvvgygvwpdylkdseataedqptqpdvatcrfytld
svqwqktspgwwwklpdalsnlglfgqnmqyhylgrtgytihvqcnaskfhqgcllvvcv
peaemgcatlnntpssaellggdtakefadkpvasgsnklvqrvvynagmgvgvgnltif
phqwinlrtnnsativmpytnsvpmdnmfrhnnvtlmvipfvpldycpgsttyvpitvti
apmcaeynglrlaghq
>d1cov3_ 2.8.1.4.12 Coxsackievirus B3 {Host: human (Homo sapiens)}
glptmntpgscqfltsddfqspsampqydvtpemripgevknlmeiaevdsvvpvqnvge
kvnsmeayqipvrsnegsgtqvfgfplqpgyssvfsrtllgeilnyythwsgsikltfmf
cgsamatgkfllaysppgagaptkrvdamlgthvvwdvglqsscvlcipwisqthyryva
sdeytaggfitcwyqtnivvpadaqsscyimcfvsacndfsvrllkdtpfisqenffq
>d1cowa1 1.59.1.1.1 (380-510) The C-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
tramkqvagtmklelaqyrevaafaqfgsdldaatqqllsrgvrltellkqgqyspmaie
eqvaviyagvrgyldklepskitkfenaflshvisqhqallgkirtdgkiseesdaklke
ivtnflagfea
>d1cowa2 2.37.1.1.1 (24-94) The N-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
dleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgndklik
egdivkrtgai
>d1cowa3 3.29.1.7.2 (95-379) central domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
vdvpvgeellgrvvdalgnaidgkgpigskarrrvglkapgiiprisvrepmqtgikavd
slvpigrgqreliigdrqtgktsiaidtiinqkrfndgtdekkklyciyvaigqkrstva
qlvkrltdadamkytivvsatasdaaplqylapysgcsmgeyfrdngkhaliiyddlskq
avayrqmslllrrppgreaypgdvfylhsrlleraakmndafgggsltalpvietqagdv
sayiptnvisitdgqifletelfykgirpainvglsvsrvgsaaq
>d1cowb1 1.59.1.1.1 (380-510) The C-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
tramkqvagtmklelaqyrevaafaqfgsdldaatqqllsrgvrltellkqgqyspmaie
eqvaviyagvrgyldklepskitkfenaflshvisqhqallgkirtdgkiseesdaklke
ivtnflagfea
>d1cowb2 2.37.1.1.1 (24-94) The N-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
dleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgndklik
egdivkrtgai
>d1cowb3 3.29.1.7.2 (95-379) central domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
vdvpvgeellgrvvdalgnaidgkgpigskarrrvglkapgiiprisvrepmqtgikavd
slvpigrgqreliigdrqtgktsiaidtiinqkrfndgtdekkklyciyvaigqkrstva
qlvkrltdadamkytivvsatasdaaplqylapysgcsmgeyfrdngkhaliiyddlskq
avayrqmslllrrppgreaypgdvfylhsrlleraakmndafgggsltalpvietqagdv
sayiptnvisitdgqifletelfykgirpainvglsvsrvgsaaq
>d1cowc1 1.59.1.1.1 (380-510) The C-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
tramkqvagtmklelaqyrevaafaqfgsdldaatqqllsrgvrltellkqgqyspmaie
eqvaviyagvrgyldklepskitkfenaflshvisqhqallgkirtdgkiseesdaklke
ivtnflagfea
>d1cowc2 2.37.1.1.1 (19-94) The N-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
adtsvdleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgn
dklikegdivkrtgai
>d1cowc3 3.29.1.7.2 (95-379) central domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
vdvpvgeellgrvvdalgnaidgkgpigskarrrvglkapgiiprisvrepmqtgikavd
slvpigrgqreliigdrqtgktsiaidtiinqkrfndgtdekkklyciyvaigqkrstva
qlvkrltdadamkytivvsatasdaaplqylapysgcsmgeyfrdngkhaliiyddlskq
avayrqmslllrrppgreaypgdvfylhsrlleraakmndafgggsltalpvietqagdv
sayiptnvisitdgqifletelfykgirpainvglsvsrvgsaaq
>d1cowd1 1.59.1.1.1 (358-475) The C-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
mdpnivgsehydvargvqkilqdykslqdiiailgmdelseedkltvsrarkiqrflsqp
fqvaevftghlgklvplketikgfqqilageydhlpeqafymvgpieeavakadklae
>d1cowd2 2.37.1.1.1 (9-81) The N-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1cowd3 3.29.1.7.2 (82-357) central domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
iripvgpetlgrimnvigepidergpiktkqfaaihaeapefvemsveqeilvtgikvvd
llapyakggkiglfggagvgktvlimelinnvakahggysvfagvgertregndlyhemi
esgvinlkdatskvalvygqmneppgararvaltgltvaeyfrdqegqdvllfidnifrf
tqagsevsallgripsavgyqptlatdmgtmqeritttkkgsitsvqaiyvpaddltdpa
pattfahldattvlsraiaelgiypavdpldstsri
>d1cowe1 1.59.1.1.1 (358-474) The C-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
mdpnivgsehydvargvqkilqdykslqdiiailgmdelseedkltvsrarkiqrflsqp
fqvaevftghlgklvplketikgfqqilageydhlpeqafymvgpieeavakadkla
>d1cowe2 2.37.1.1.1 (9-81) The N-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1cowe3 3.29.1.7.2 (82-357) central domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
iripvgpetlgrimnvigepidergpiktkqfaaihaeapefvemsveqeilvtgikvvd
llapyakggkiglfggagvgktvlimelinnvakahggysvfagvgertregndlyhemi
esgvinlkdatskvalvygqmneppgararvaltgltvaeyfrdqegqdvllfidnifrf
tqagsevsallgripsavgyqptlatdmgtmqeritttkkgsitsvqaiyvpaddltdpa
pattfahldattvlsraiaelgiypavdpldstsri
>d1cowf1 1.59.1.1.1 (358-474) The C-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
mdpnivgsehydvargvqkilqdykslqdiiailgmdelseedkltvsrarkiqrflsqp
fqvaevftghlgklvplketikgfqqilageydhlpeqafymvgpieeavakadkla
>d1cowf2 2.37.1.1.1 (9-81) The N-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1cowf3 3.29.1.7.2 (82-357) central domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
iripvgpetlgrimnvigepidergpiktkqfaaihaeapefvemsveqeilvtgikvvd
llapyakggkiglfggagvgktvlimelinnvakahggysvfagvgertregndlyhemi
esgvinlkdatskvalvygqmneppgararvaltgltvaeyfrdqegqdvllfidnifrf
tqagsevsallgripsavgyqptlatdmgtmqeritttkkgsitsvqaiyvpaddltdpa
pattfahldattvlsraiaelgiypavdpldstsri
>d1cowg_ 1.19.1.1.1 ATP syntase (F1-ATPase), gamma subunit {Bovine (Bos taurus)}
atlkditrrlksikniqkitksmkmvaaakyaraerelkparvygvgslalyekadiktp
edkkkhliigvssdrglcgaihssvakqmkseaanlaaagkevkiigvgdkirsilhrth
sdqflvtfkevgrrpptfgdasvialellnsgyefdegsiifnrfrsvisykteekpifs
ldtissaesmsiyddidadvlrnyqeyslaniiyyslkesttseqsarmtamdnasknas
emidkltltfnrtrqavitkelieiisgaaal
>d1coy_1 3.4.1.2.1 (4-318) Cholesterol oxidase {(Brevibacterium sterolicum)}
rtladgdrvpalvigsgyggavaalrltqagiptqivemgrswdtpgsdgkifcgmlnpd
krsmwladktdqpvsnfmgfginksidryvgvldserfsgikvyqgrgvgggslvnggma
vtpkrnyfeeilpsvdsnemynkyfprantglgvnnidqawfestewykfartgrktaqr
sgfttafvpnvydfeymkkeaagqvtksglggeviygnnagkksldktylaqaaatgklt
ittlhrvtkvapatgsgysvtmeqideqgnvvatkvvtadrvffaagsvgtskllvsmka
qghlpnlssqvgegw
>d1coy_2 4.12.1.1.1 (319-450) Cholesterol oxidase {(Brevibacterium sterolicum)}
gnngnimvgranhmwdatgskqatiptmgidnwadptapifaeiaplpagletyvslyla
itknperarfqfnsgtgkvdltwaqsqnqkgidmakkvfdkinqkegtiyrtdlfgvyyk
twgddftyhplg
>d1cp3a_ 3.11.1.1.1 Apopain {Human (Homo sapiens)}
nsykmdypemglciiinnknfhkstgmtsrsgtdvdaanlretfrnlkyevrnkndltre
eivelmrdvskedhskrssfvcvllshgeegiifgtngpvdlkkitnffrgdrcrsltgk
pklfiiqacrgteldcgietdsgvdddmachkipvdadflyaystapgyyswrnskdgsw
fiqslcamlkqyadklefmhiltrvnrkvatefesfsfdatfhakkqipcivsmltkely
fyh
>d1cp3b_ 3.11.1.1.1 Apopain {Human (Homo sapiens)}
nsykmdypemglciiinnknfhkstgmtsrsgtdvdaanlretfrnlkyevrnkndltre
eivelmrdvskedhskrssfvcvllshgeegiifgtngpvdlkkitnffrgdrcrsltgk
pklfiiqacrgteldcgietdsgvdddmachkipvdadflyaystapgyyswrnskdgsw
fiqslcamlkqyadklefmhiltrvnrkvatefesfsfdatfhakkqipcivsmltkely
fyh
>d1cp4__ 1.83.1.1.1 Cytochrome P450 {(Pseudomonas putida)}
nlaplpphvpehlvfdfdmynpsnlsagvqeawavlqesnvpdlvwtrcngghwiatrgq
lireayedyrhfssecpfipreageaydfiptsmdppeqrqfralanqvvgmpvvdklen
riqelacslieslrpqgqcnftedyaepfpirifmllaglpeediphlkyltdqmtrpdg
smtfaeakealydylipiieqrrqkpgtdaisivangqvngrpitsdeakrmcglllvgg
ldtvvnflsfsmeflakspehrqelierperipaaceellrrfslvadgriltsdyefhg
vqlkkgdqillpqmlsglderenacpmhvdfsrqkvshttfghgshlclgqhlarreiiv
tlkewltripdfsiapgaqiqhksgivsgvqalplvwdpattkav
>d1cpb__ 3.58.4.1.4 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__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1cpe__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1cpf__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1cpg__ 1.72.1.1.3 Cytochrome c peroxidase {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_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtiriggqlkealldtgaddtvleemnlpgkwkpkmiggiggfikvrqyd
qipveixghkaigtvlvgptpvniigrnlltqigxtlnf
>d1cpib_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtiriggqlkealldtgaddtvleemnlpgkwkpkmiggiggfikvrqyd
qipveixghkaigtvlvgptpvniigrnlltqigxtlnf
>d1cpja_ 4.3.1.1.6 (Pro)cathepsin B {Rat (Rattus norvegicus)}
lpesfdareqwsncptiaqirdqgscgscwafgaveamsdricihtngrvnvevsaedll
tccgiqcgdgcnggypsgawnfwtrkglvsggvynshigclpytippcehhvngarppct
gegdtpkcnkmceagystsykedkhygytsysvsdsekeimaeiykngpvegaftvfsdf
ltyksgvykheagdvmgghairilgwgiengvpywlvanswnadwgdngffkilrgenhc
gieseivagiprt
>d1cpjb_ 4.3.1.1.6 (Pro)cathepsin B {Rat (Rattus norvegicus)}
lpesfdareqwsncptiaqirdqgscgscwafgaveamsdricihtngrvnvevsaedll
tccgiqcgdgcnggypsgawnfwtrkglvsggvynshigclpytippcehhvngarppct
gegdtpkcnkmceagystsykedkhygytsysvsdsekeimaeiykngpvegaftvfsdf
ltyksgvykheagdvmgghairilgwgiengvpywlvanswnadwgdngffkilrgenhc
gieseivagiprt
>d1cpm__ 2.21.1.2.3 Bacillus 1-3,1-4-beta-glucanase {(Bacillus macerans)}
fdcaeyrstniygyglyevsmkpakntgivssfftytgpahgtqwdeidieflgkdttkv
qfnyytngvgghekvislgfdaskgfhtyafdwqpgyikwyvdgvlkhtatanipstpgk
immnlwngtgvddwlgsynganplyaeydwvkytsnqtggsffepfnsynsgtwekadgy
snggvfnctwrannvnftndgklklgltssayna
>d1cpn__ 2.21.1.2.3 Bacillus 1-3,1-4-beta-glucanase {(Bacillus macerans)}
fdcaeyrstniygyglyevsmkpakntgivssfftytgpahgtqwdeidieflgkdttkv
qfnyytngvgghekvislgfdaskgfhtyafdwqpgyikwyvdgvlkhtatanipstpgk
immnlwngtgvddwlgsynganplyaeydwvkytsngsvfwepksyfnpstwekadgysn
ggvfnctwrannvnftndgklklgltss
>d1cpo_1 1.37.2.1.1 (1-119) Cloroperoxidase {Fungus (Caldariomyces fumago)}
epgsgigypydnntlpyvapgptdsrapcpalnalanhgyiphdgraisretlqnaflnh
mgiansvielaltnafvvceyvtgsdcgdslvnltllaephafehdhsfsrkdykqgva
>d1cpo_2 1.37.2.1.1 (120-298) Cloroperoxidase {Fungus (Caldariomyces fumago)}
nsndfidnrnfdaetfqtsldvvagkthfdyadmneirlqreslsneldfpgwfteskpi
qnvesgfifalvsdfnlpdndenplvridwwkywftnesfpyhlgwhppspareiefvts
assavlaasvtstpsslpsgaigpgaeavplsfastmtpfllatnapyyaqdptlgpnd
>d1cpq__ 1.24.3.2.6 Cytochrome c' {(Rhodobacter capsulatus)}
adtkevleareayfkslggsmkamtgvakafdaeaakveaaklekilatdvaplfpagts
stdlpgqteakaaiwanmddfgakgkamheaggaviaaanagdgaafgaalqklggtcka
chddyreed
>d1cpr__ 1.24.3.2.6 Cytochrome c' {(Rhodobacter capsulatus)}
adtkevleareayfkslggsmkamtgvakafdaeaakveaaklekilatdvaplfpagts
stdlpgqteakaaiwanmddfgakgkamhdaggaviaaanagdgaafgaalqklggtcka
chddyreed
>d1cps__ 3.58.4.1.1 Carboxypeptidase A {bovine (Bos taurus)}
arstntfnyatyhtldeiydfmdllvaehpqlvsklqigrsyegrpiyvlkfstggsnrp
aiwidlgihsrewitqatgvwfakkftenygqnpsftaildsmdifleivtnpngfafth
senrlwrktrsvtssslcvgvdanrnwdagfgkagassspcsetyhgkyansevevksiv
dfvknhgnfkaflsihsysqlllypygyttqsipdktelnqvaksavaalkslygtsyky
gsiittiyqasggsidwsynqgikysftfelrdtgrygfllpasqiiptaqetwlgvlti
mehtvnn
>d1cpt__ 1.83.1.1.5 Cytochrome P450-TERP {(Pseudomonas sp.)}
mdaratipehiartvilpqgyaddeviypafkwlrdeqplamahiegydpmwiatkhadv
mqigkqpglfsnaegseilydqnneafmrsisggcphvidsltsmdppthtayrgltlnw
fqpasirkleenirriaqasvqrlldfdgecdfmtdcalyyplhvvmtalgvpeddeplm
lkltqdffgveaarrfhetiatfydyfngftvdrrscpkddvmsllanskldgnyiddky
inayyvaiataghdttssssggaiiglsrnpeqlalaksdpaliprlvdeavrwtapvks
fmrtaladtevrgqnikrgdrimlsypsanrdeevfsnpdefditrfpnrhlgfgwgahm
clgqhlaklemkiffeellpklksvelsgpprlvatnfvggpknvpirftka
>d1cpy__ 3.56.1.2.2 Serine carboxypeptidase II {yeast (Saccharomyces cerevisiae)}
kikdpkilgidpnvtqytgyldvededkhfffwtfesrndpakdpvilwlnggpgcsslt
glffalgpssigpdlkpignpyswnsnatvifldqpvnvgfsysgssgvsntvaagkdvy
nflelffdqfpeyvnkgqdfhiagasyaghyipvfaseilshkdrnfnltsvligngltd
pltqynyyepmacgeggepsvlpseecsamedslerclgliescydsqsvwscvpatiyc
nnaqlapyqrtgrnvydirkdceggnlcyptlqdiddylnqdyvkeavgaevdhyescnf
dinrnflfagdwmkpyhtavtdllnqdlpilvyagdkdficnwlgnkawtdvlpwkydee
fasqkvrnwtasitdevagevksykhftylrvfngghmvpfdvpenalsmvnewihggfs
l
>d1cqa__ 4.63.1.1.5 Profilin (actin-binding protein) {Birch (Betula verrucosa)}
swqtyvdehlmcdidgqgeelaasaivghdgsvwaqsssfpqfkpqeitgimkdfeepgh
laptglhlggikymviqgeagavirgkkgsggitikktgqalvfgiyeepvtpgqcnmvv
erlgdylidqgl
>d1cqga_ 3.38.1.1.4 Thioredoxin {human (Homo sapiens)}
mvkqiesktafqealdaagdklvvvdfsatwcgpakmikpffhslsekysnviflevdvd
daqdvaseaevkatptfqffkkgqkvgefsgankekleatinelv
>d1cqha_ 3.38.1.1.4 Thioredoxin {human (Homo sapiens)}
mvkqiesktafqealdaagdklvvvdfsatwcgpakmikpffhslsekysnviflevdvd
daqdvaseaevkatptfqffkkgqkvgefsgankekleatinelv
>d1cra__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
xshhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslril
nnghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhl
vhwntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdp
rgllpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelm
vdnwrpaqplknrqikasfk
>d1crb__ 2.45.1.2.8 Cellular retinol-binding protein II (CRBP) {rat (Rattus rattus)}
pvdfngywkmlsnenfeeylraldvnvalrkianllkpdkeivqdgdhmiirtlstfrny
imdfqvgkefeedltgiddrkcmttvswdgdklqcvqkgekegrgwtqwiegdelhlemr
aegvtckqvfkkvh
>d1crca_ 1.3.1.1.7 Mitochondrial cytochrome c {horse (Equus caballus)}
xgdvekgkkifvqkcaqchtvekggkhktgpnlhglfgrktgqapgftytdanknkgitw
keetlmeylenpkkyipgtkmifagikkkteredliaylkkatne
>d1crcb_ 1.3.1.1.7 Mitochondrial cytochrome c {horse (Equus caballus)}
xgdvekgkkifvqkcaqchtvekggkhktgpnlhglfgrktgqapgftytdanknkgitw
keetlmeylenpkkyipgtkmifagikkkteredliaylkkatne
>d1cre__ 7.6.1.1.15 Cardiotoxin II {taiwan cobra (Naja naja atra)}
lkcnklvplfyktcpagknlcykmfmvsnltvpvkrgcidvcpknsalvkyvccntdrcn
>d1crf__ 7.6.1.1.15 Cardiotoxin II {taiwan cobra (Naja naja atra)}
lkcnklvplfyktcpagknlcykmfmvsnltvpvkrgcidvcpknsalvkyvccntdrcn
>d1crg__ 1.3.1.1.6 Mitochondrial cytochrome c {baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdaiikk
nvlwdennmseyltnpkkyipgtkmafgglkkekdrndlitylkkate
>d1crh__ 1.3.1.1.6 Mitochondrial cytochrome c {baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdaiikk
nvlwdennmseyltnpkkyipgtkmafgglkkekdrndlitylkkace
>d1cri__ 1.3.1.1.6 Mitochondrial cytochrome c {baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdaiikk
nvlwdennmsefltnpkkyipgtkmafgglkkekdrndlitylkkate
>d1crj__ 1.3.1.1.6 Mitochondrial cytochrome c {baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdaiikk
nvlwdennmsefltnpkkyipgtkmafgglkkekdrndlitylkkate
>d1crka1 1.68.1.1.1 (1-98) Creatine kinase, N-terminal domain {chicken (Gallus gallus) mitochondria}
tvhekrklfppsadypdlrkhnncmaecltpaiyaklrdkltpngysldqciqtgvdnpg
hpfiktvgmvagdeesyevfaeifdpvikarhngydpr
>d1crka2 4.78.1.2.1 (99-380) Creatine kinase, C-terminal domain {chicken (Gallus gallus) mitochondria}
tmkhhtdldaskithgqfderyvlssrvrtgrsirglslppacsraerrevenvvvtala
glkgdlsgkyysltnmserdqqqliddhflfdkpvsplltcagmardwpdargiwhnndk
tflvwineedhtrvismekggnmkrvferfcrglkeverlikergwefmwnerlgyvltc
psnlgtglragvhvklprlskdprfpkilenlrlqkrgtggvdtaavadvydisnldrmg
rsevelvqividgvnylvdcekklekgqdikvppplpqfgrk
>d1crkb1 1.68.1.1.1 (1-98) Creatine kinase, N-terminal domain {chicken (Gallus gallus) mitochondria}
tvhekrklfppsadypdlrkhnncmaecltpaiyaklrdkltpngysldqciqtgvdnpg
hpfiktvgmvagdeesyevfaeifdpvikarhngydpr
>d1crkb2 4.78.1.2.1 (99-380) Creatine kinase, C-terminal domain {chicken (Gallus gallus) mitochondria}
tmkhhtdldaskithgqfderyvlssrvrtgrsirglslppacsraerrevenvvvtala
glkgdlsgkyysltnmserdqqqliddhflfdkpvsplltcagmardwpdargiwhnndk
tflvwineedhtrvismekggnmkrvferfcrglkeverlikergwefmwnerlgyvltc
psnlgtglragvhvklprlskdprfpkilenlrlqkrgtggvdtaavadvydisnldrmg
rsevelvqividgvnylvdcekklekgqdikvppplpqfgrk
>d1crkc1 1.68.1.1.1 (1-98) Creatine kinase, N-terminal domain {chicken (Gallus gallus) mitochondria}
tvhekrklfppsadypdlrkhnncmaecltpaiyaklrdkltpngysldqciqtgvdnpg
hpfiktvgmvagdeesyevfaeifdpvikarhngydpr
>d1crkc2 4.78.1.2.1 (99-380) Creatine kinase, C-terminal domain {chicken (Gallus gallus) mitochondria}
tmkhhtdldaskithgqfderyvlssrvrtgrsirglslppacsraerrevenvvvtala
glkgdlsgkyysltnmserdqqqliddhflfdkpvsplltcagmardwpdargiwhnndk
tflvwineedhtrvismekggnmkrvferfcrglkeverlikergwefmwnerlgyvltc
psnlgtglragvhvklprlskdprfpkilenlrlqkrgtggvdtaavadvydisnldrmg
rsevelvqividgvnylvdcekklekgqdikvppplpqfgrk
>d1crkd1 1.68.1.1.1 (1-98) Creatine kinase, N-terminal domain {chicken (Gallus gallus) mitochondria}
tvhekrklfppsadypdlrkhnncmaecltpaiyaklrdkltpngysldqciqtgvdnpg
hpfiktvgmvagdeesyevfaeifdpvikarhngydpr
>d1crkd2 4.78.1.2.1 (99-380) Creatine kinase, C-terminal domain {chicken (Gallus gallus) mitochondria}
tmkhhtdldaskithgqfderyvlssrvrtgrsirglslppacsraerrevenvvvtala
glkgdlsgkyysltnmserdqqqliddhflfdkpvsplltcagmardwpdargiwhnndk
tflvwineedhtrvismekggnmkrvferfcrglkeverlikergwefmwnerlgyvltc
psnlgtglragvhvklprlskdprfpkilenlrlqkrgtggvdtaavadvydisnldrmg
rsevelvqividgvnylvdcekklekgqdikvppplpqfgrk
>d1crl__ 3.56.1.9.8 type-B carboxylesterase/lipase {fungus (Candida rugosa, formerly cylindracea)}
aptatlangdtitglnaiineaflgipfaeppvgnlrfkdpvpysgsldgqkftsygpsc
mqqnpegtyeenlpkaaldlvmqskvfeavspssedcltinvvrppgtkaganlpvmlwi
fgggfevggtstfppaqmitksiamgkpiihvsvnyrvsswgflagdeikaegsanaglk
dqrlgmqwvadniaafggdptkvtifgesagsmsvmchilwndgdntykgkplfragimq
sgamvpsdavdgiygneifdllasnagcgsasdklaclrgvssdtledatnntpgflays
slrlsylprpdgvnitddmyalvregkyanipviigdqndegtffgtsslnvttdaqare
yfkqsfvhasdaeidtlmtaypgditqgspfdtgilnaltpqfkrisavlgdlgftlarr
yflnhytggtkysflskqlsglpvlgtfhsndivfqdyllgsgsliynnafiafatdldp
ntagllvkwpeytsssqsgnnlmminalglytgkdnfrtagydalfsnppsffv
>d1crm__ 2.56.1.1.1 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme I}
wgyddkngpeqwsklypiangnnqspvdiktsetkhdtslkpisvsynpatakeiinvgh
sfhvnfednqdrsvlkggpfsdsyrlfqfhfhwgstnehgsehtvdgvkysaelhvahwn
sakysslaeaaskadglavigvlmkvgeanpklqkvldalqaiktkgkrapftnfdpstl
lpssldfwtypgslthpplyesvtwiickesisvsseqlaqfrsllsnvegdnavpmqhn
nrptqplkgrtvrasf
>d1crn__ 7.12.1.1.1 Crambin {abyssinian cabbage (Crambe abyssinica)}
ttccpsivarsnfnvcrlpgtpeaicatytgciiipgatcpgdyan
>d1crp__ 3.29.1.4.1 cH-p21 Ras protein {human (Homo sapiens)}
mteyklvvvgaggvgksaltiqliqnhfvdeydptiedsyrkqvvidgetclldildtag
qeeysamrdqymrtgegflcvfainntksfedihqyreqikrvkdsddvpmvlvgnkcdl
aartvesrqaqdlarsygipyietsaktrqgvedafytlvreirqh
>d1crq__ 3.29.1.4.1 cH-p21 Ras protein {human (Homo sapiens)}
mteyklvvvgaggvgksaltiqliqnhfvdeydptiedsyrkqvvidgetclldildtag
qeeysamrdqymrtgegflcvfainntksfedihqyreqikrvkdsddvpmvlvgnkcdl
aartvesrqaqdlarsygipyietsaktrqgvedafytlvreirqh
>d1crr__ 3.29.1.4.1 cH-p21 Ras protein {human (Homo sapiens)}
mteyklvvvgaggvgksaltiqliqnhfvdeydptiedsyrkqvvidgetclldildtag
qeeysamrdqymrtgegflcvfainntksfedihqyreqikrvkdsddvpmvlvgnkcdl
aartvesrqaqdlarsygipyietsaktrqgvedafytlvreirqh
>d1cry__ 1.3.1.1.14 Cytochrome c2 {(Rhodopseudomonas viridis)}
qdaasgeqvfkqclvchsigpgaknkvgpvlnglfgrhsgtiegfaysdanknsgitwte
evfreyirdpkakipgtkmifagvkdeqkvsdliayikqfnadgskk
>e1csb.1a 4.3.1.1.5 (Pro)cathepsin B {Human (Homo sapiens)}
lpasfdareqwpqcptikeirdqgscgscwafgaveaisdricihtn
>e1csb.1b 4.3.1.1.5 (Pro)cathepsin B {Human (Homo sapiens)}
vsvevsaedlltccgsmcgdgcnggypaeawnfwtrkglvsgglyeshvgcrpysippce
hhvngsrppctgegdtpkcskicepgysptykqdkhygynsysvsnsekdimaeiykngp
vegafsvysdfllyksgvyqhvtgemmgghairilgwgvengtpywlvanswntdwgdng
ffkilrgqdhcgiesevvagiprtd
>e1csb.2d 4.3.1.1.5 (Pro)cathepsin B {Human (Homo sapiens)}
lpasfdareqwpqcptikeirdqgscgscwafgaveaisdricihtn
>e1csb.2e 4.3.1.1.5 (Pro)cathepsin B {Human (Homo sapiens)}
vsvevsaedlltccgsmcgdgcnggypaeawnfwtrkglvsgglyeshvgcrpysippce
hhvngsrppctgegdtpkcskicepgysptykqdkhygynsysvsnsekdimaeiykngp
vegafsvysdfllyksgvyqhvtgemmgghairilgwgvengtpywlvanswntdwgdng
ffkilrgqdhcgiesevvagiprtd
>d1csc__ 1.82.1.1.1 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_ 4.22.1.1.1 Eglin C {leech (Hirudo medicinalis)}
ksfpevvgktvdqareyftlhypqynvyflpegspvtldlrynrvrvfynpgtnvvnhvp
hvg
>d1csga_ 1.26.1.2.1 Granulocyte-macrophage colony-stimulating factor (GM-CSF) {human (Homo sapiens)}
spspstqpwehvnaiqearrllnlsrdtaaemnetvevisemfdlqeptclqtrlelykq
glrgsltklkgpltmmashykqhcpptpetscatqiitfesfkenlkdfllvipfdcwep
>d1csgb_ 1.26.1.2.1 Granulocyte-macrophage colony-stimulating factor (GM-CSF) {human (Homo sapiens)}
spspstqpwehvnaiqearrllnlsrdtaaemnetvevisemfdlqeptclqtrlelykq
glrgsltklkgpltmmashykqhcpptpetscatqiitfesfkenlkdfllvipfdcwep
>d1csh__ 1.82.1.1.1 Citrate synthase {chicken (Gallus gallus)}
stnlkdvlaslipkeqariktfrqqhgntavgqitvdmsyggmrgmkgliyetsvldpde
girfrgfsipecqkllpkagggeeplpeglfwllvtgqiptpeqvswvskewakraalps
hvvtmldnfptnlhpmsqlsaaitalnsesnfarayaeginrtkywefvyedamdliakl
pcvaakiyrnlyragssigaidskldwshnftnmlgytdpqftelmrlyltihsdheggn
vsahtshlvgsalsdpylsfaaamnglagplhglanqevllwlsqlqkdlgadasdeklr
dyiwntlnsgrvvpgyghavlrktdprytcqrefalkhlpsdpmfklvaqlykivpnvll
eqgkaknpwpnvdahsgvllqyygmtemnyytvlfgvsralgvlaqliwsralgfplerp
ksmstagleklsagg
>d1csi__ 1.82.1.1.1 Citrate synthase {chicken (Gallus gallus)}
stnlkdvlaslipkeqariktfrqqhgntavgqitvdmsyggmrgmkgliyetsvldpde
girfrgfsipecqkllpkagggeeplpeglfwllvtgqiptpeqvswvskewakraalps
hvvtmldnfptnlhpmsqlsaaitalnsesnfarayaeginrtkywefvyedamdliakl
pcvaakiyrnlyragssigaidskldwshnftnmlgytdpqftelmrlyltihsdheggn
vsahtshlvgsalsdpylsfaaamnglagplhglanqevllwlsqlqkdlgadasdeklr
dyiwntlnsgrvvpgyghavlrktdprytcqrefalkhlpsdpmfklvaqlykivpnvll
eqgkaknpwpnvdahsgvllqyygmtemnyytvlfgvsralgvlaqliwsralgfplerp
ksmstagleklsagg
>d1cska_ 2.24.2.1.19 Src kinase, SH3 domain {human (Homo sapiens)}
gteciakynfhgtaeqdlpfckgdvltivavtkdpnwykaknkvgregiipanyvqkr
>d1cskb_ 2.24.2.1.19 Src kinase, SH3 domain {human (Homo sapiens)}
gteciakynfhgtaeqdlpfckgdvltivavtkdpnwykaknkvgregiipanyvqkr
>d1cskc_ 2.24.2.1.19 Src kinase, SH3 domain {human (Homo sapiens)}
gteciakynfhgtaeqdlpfckgdvltivavtkdpnwykaknkvgregiipanyvqkr
>d1cskd_ 2.24.2.1.19 Src kinase, SH3 domain {human (Homo sapiens)}
gteciakynfhgtaeqdlpfckgdvltivavtkdpnwykaknkvgregiipanyvqkr
>d1csma_ 1.101.1.2.1 Allosteric chorismate mutase {(Saccharomyces cerevisiae)}
mdftkpetvlnlqnirdelvrmedsiifkfiershfatcpsvyeanhpgleipnfkgsfl
dwalsnleiahsrirrfespdetpffpdkiqksflpsinypqilapyapevnyndkikkv
yiekiipliskrdgddknnfgsvatrdieclqslsrrihfgkfvaeakfqsdiplytkli
kskdvegimknitnsaveekilerltkkaevygvdptnesgerriipeylvkiykeivip
itkeveveyllrrlee
>d1csmb_ 1.101.1.2.1 Allosteric chorismate mutase {(Saccharomyces cerevisiae)}
mdftkpetvlnlqnirdelvrmedsiifkfiershfatcpsvyeanhpgleipnfkgsfl
dwalsnleiahsrirrfespdetpffpdkiqksflpsinypqilapyapevnyndkikkv
yiekiipliskrdgddknnfgsvatrdieclqslsrrihfgkfvaeakfqsdiplytkli
kskdvegimknitnsaveekilerltkkaevygvdptnesgerriipeylvkiykeivip
itkeveveyllrrlee
>d1csn__ 5.1.1.1.13 Casein kinase-1, CK1 {(Schizosaccharomyces pombe)}
nvvgvhykvgrrigegsfgvifegtnllnnqqvaikfeprrsdapqlrdeyrtykllagc
tgipnvyyfgqeglhnvlvidllgpsledlldlcgrkfsvktvamaakqmlarvqsihek
slvyrdikpdnfligrpnsknanmiyvvdfgmvkfyrdpvtkqhipyrekknlsgtarym
sinthlgreqsrrddlealghvfmyflrgslpwqglkaatnkqkyerigekkqstplrel
cagfpeefykymhyarnlafdatpdydylqglfskvlerlnttedenfdwnll
>d1csp__ 2.29.4.5.2 Major cold shock protein {(Bacillus subtilis)}
mlegkvkwfnsekgfgfievegqddvfvhfsaiqgegfktleegqavsfeivegnrgpqa
anvtkea
>d1csq__ 2.29.4.5.2 Major cold shock protein {(Bacillus subtilis)}
mlegkvkwfnsekgfgfievegqddvfvhfsaiqgegfktleegqavsfeivegnrgpqa
anvtkea
>d1csr__ 1.82.1.1.1 Citrate synthase {chicken (Gallus gallus)}
stnlkdvlaslipkeqariktfrqqhgntavgqitvdmsyggmrgmkgliyetsvldpde
girfrgfsipecqkllpkagggeeplpeglfwllvtgqiptpeqvswvskewakraalps
hvvtmldnfptnlhpmsqlsaaitalnsesnfarayaeginrtkywefvyedamdliakl
pcvaakiyrnlyragssigaidskldwshnftnmlgytdpqftelmrlyltihsdheggn
vsahtshlvgsalsdpylsfaaamnglagplhglanqevllwlsqlqkdlgadasdeklr
dyiwntlnsgrvvpgyghavlrktdprytcqrefalkhlpsdpmfklvaqlykivpnvll
eqgkaknpwpnvdahsgvllqyygmtemnyytvlfgvsralgvlaqliwsralgfplerp
ksmstagleklsagg
>d1css__ 1.82.1.1.1 Citrate synthase {chicken (Gallus gallus)}
stnlkdvlaslipkeqariktfrqqhgntavgqitvdmsyggmrgmkgliyetsvldpde
girfrgfsipecqkllpkagggeeplpeglfwllvtgqiptpeqvswvskewakraalps
hvvtmldnfptnlhpmsqlsaaitalnsesnfarayaeginrtkywefvyedamdliakl
pcvaakiyrnlyragssigaidskldwshnftnmlgytdpqftelmrlyltihsdheggn
vsahtshlvgsalsdpylsfaaamnglagplhglanqevllwlsqlqkdlgadasdeklr
dyiwntlnsgrvvpgyghavlrktdprytcqrefalkhlpsdpmfklvaqlykivpnvll
eqgkaknpwpnvdahsgvllqyygmtemnyytvlfgvsralgvlaqliwsralgfplerp
ksmstagleklsagg
>d1csu__ 1.3.1.1.6 Mitochondrial cytochrome c {baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdanikk
nvlwdennmseyltnpkkyipgtkmafggckkekdrndlitylkkate
>d1csv__ 1.3.1.1.6 Mitochondrial cytochrome c {baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdanikk
nvlwdennmseyltnpkkyipgtkmafggfkkekdrndlitylkkate
>d1csw__ 1.3.1.1.6 Mitochondrial cytochrome c {baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdanikk
nvlwdennmseyltnpkkyipgtkmafggmkkekdrndlitylkkate
>d1csx__ 1.3.1.1.6 Mitochondrial cytochrome c {baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdanikk
nvlwdennmseyltnpkkyipgtkmafgglkkekdrndsitylkkate
>d1csya_ 4.53.1.1.13 Syk tyrosine kinase {Human (Homo sapiens)}
gsrrasvgshekmpwfhgkisreeseqivligsktngkflirardnngsyalcllhegkv
lhyridkdktgklsipegkkfdtlwqlvehysykadgllrvltvpcqkigtq
>d1csza_ 4.53.1.1.13 Syk tyrosine kinase {Human (Homo sapiens)}
gsrrasvgshekmpwfhgkisreeseqivligsktngkflirardnngsyalcllhegkv
lhyridkdktgklsipegkkfdtlwqlvehysykadgllrvltvpcqkigtq
>d1ct1d_ 2.29.2.1.3 Cholera toxin {(Vibrio cholerae)}
tpqnitdlcaeyhntqihtlndkifsyteslarkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1ct1e_ 2.29.2.1.3 Cholera toxin {(Vibrio cholerae)}
tpqnitdlcaeyhntqihtlndkifsyteslarkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1ct1f_ 2.29.2.1.3 Cholera toxin {(Vibrio cholerae)}
tpqnitdlcaeyhntqihtlndkifsyteslarkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1ct1g_ 2.29.2.1.3 Cholera toxin {(Vibrio cholerae)}
tpqnitdlcaeyhntqihtlndkifsyteslarkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1ct1h_ 2.29.2.1.3 Cholera toxin {(Vibrio cholerae)}
tpqnitdlcaeyhntqihtlndkifsyteslarkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1ctaa_ 1.37.1.5.1 Troponin C {chicken (Gallus gallus)}
xkseeelanafrifdknadgyidieelgeilratg
>d1ctab_ 1.37.1.5.1 Troponin C {chicken (Gallus gallus)}
xkseeelanafrifdknadgyidieelgeilratg
>d1ctda_ 1.37.1.5.1 Troponin C {chicken (Gallus gallus)}
xkseeelanafrifdknadgyidieelgeilratg
>d1ctdb_ 1.37.1.5.1 Troponin C {chicken (Gallus gallus)}
xkseeelanafrifdknadgyidieelgeilratg
>d1ctea_ 4.3.1.1.6 (Pro)cathepsin B {Rat (Rattus norvegicus)}
lpesfdareqwsncptiaqirdqgscgscwafgaveamsdricihtngrvnvevsaedll
tccgiqcgdgcnggypsgawnfwtrkglvsggvynshigclpytippcehhvngarppct
gegdtpkcnkmceagystsykedkhygytsysvsdsekeimaeiykngpvegaftvfsdf
ltyksgvykheagdvmgghairilgwgiengvpywlvanswnadwgdngffkilrgenhc
gieseivagiprt
>d1cteb_ 4.3.1.1.6 (Pro)cathepsin B {Rat (Rattus norvegicus)}
lpesfdareqwsncptiaqirdqgscgscwafgaveamsdricihtngrvnvevsaedll
tccgiqcgdgcnggypsgawnfwtrkglvsggvynshigclpytippcehhvngarppct
gegdtpkcnkmceagystsykedkhygytsysvsdsekeimaeiykngpvegaftvfsdf
ltyksgvykheagdvmgghairilgwgiengvpywlvanswnadwgdngffkilrgenhc
gieseivagiprt
>d1ctf__ 4.27.1.1.1 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 2.2.5.1.1 (1-167,231-250) Cytochrome f, large domain {turnip (Brassica rapa)}
ypifaqqnyenpreatgrivcanchlaskpvdievpqavlpdtvfeavvkipydmqlkqv
langkkgalnvgavlilpegfelappdrispemkekignlsfqnyrpnkknilvigpvpg
qkyseitfpilapdpatnkdvhflkypiyvggnrgrgqiypdgsksnXpnvggfgqgdae
ivlqdplr
>d1ctm_2 2.65.2.2.1 (168-230) Cytochrome f, small domain {turnip (Brassica rapa)}
ntvynataggiiskilrkekggyeitivdasnerqvidiiprglellvsegesikldqpl
tsn
>d1ctn_1 2.1.1.5.11 (24-132) Chitinase A, N-terminal domain {(Serratia marcescens)}
aapgkptiawgntkfaivevdqaataynnlvkvknaadvsvswnlwngdtgttakillng
keawsgpstgssgtanfkvnkggryqmqvalcnadgctasdateivvad
>d1ctn_2 3.1.1.5.6 (133-441,516-561) Chitinase A, central domain {(Serratia marcescens)}
tdgshlaplkeplleknkpykqnsgkvvgsyfvewgvygrnftvdkipaqnlthllygfi
picggngindslkeiegsfqalqrscqgredfkisihdpfaalqkaqkgvtawddpykgn
fgqlmalkqahpdlkilpsiggwtlsdpfffmgdkvkrdrfvgsvkeflqtwkffdgvdi
dwefpggkganpnlgspqdgetyvllmkelramldqlstetgrkyeltsaisagkdkidk
vaynvaqnsmdhiflmsydfygafdlknlghqtalnapawkpdtayttvngvnallaqgv
kpgkivvgtXddarsvqakgkyvldkqlgglfsweidadngdilnsmnaslgnsag
>d1ctn_3 4.19.3.1.1 (442-515) Chitinase A, insertion domain {(Serratia marcescens)}
amygrgwtgvngyqnnipftgtatgpvkgtwengivdyrqiagqfmsgewqytydataea
pyvfkpstgdlitf
>d1cto__ 2.1.2.1.10 Granulocyte colony-stimulating factor (GC-SF) receptor {mouse (Mus musculus)}
gssleppmlqaldigpdvvshqpgclwlswkpwkpseymeqecelryqpqlkganwtlvf
hlpsskdqfelcglhqapvytlqmrcirsslpgfwspwspglqlrptmk
>d1ctpe_ 5.1.1.1.2 cAMP-dependent PK, catalytic subunit {pig (Sus scrofa)}
kkgseqesvkeflakakedflkkwenpaqntahldqferiktlgtgsfgrvmlvkhketg
nhfamkildkqkvvklkqiehtlnekrilqavnfpflvkleysfkdnsnlymvmeyvpgg
emfshlrrigrfsepharfyaaqivltfeylhsldliyrdlkpenllidqqgyiqvtdfg
fakrvkgrtwtlcgtpeylapeiilskgynkavdwwalgvliyemaagyppffadqpiqi
yekivsgkvrfpshfssdlkdllrnllqvdltkrfgnlkngvndiknhkwfattdwiaiy
qrkveapfipkfkgpgdtsnfddyeeeeirvsinekcgkefsef
>d1ctr__ 1.37.1.5.7 Calmodulin {human (Homo sapiens)}
adqlteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgn
gtidfpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdee
vdemireadidgdgqvnyeefvqmmta
>d1cts__ 1.82.1.1.2 Citrate synthase {pig (Sus scrofa)}
asstnlkdiladlipkeqariktfrqqhgntvvgqitvdmmyggmrgmkglvyetsvldp
degirfrgysipecqkmlpkakggeeplpeglfwllvtgqipteeqvswlskewakraal
pshvvtmldnfptnlhpmsqlsaaitalnsesnfarayaegihrtkyweliyedcmdlia
klpcvaakiyrnlyregssigaidskldwshnftnmlgytdaqftelmrlyltihsdheg
gnvsahtshlvgsalsdpylsfaaamnglagplhglanqevlvwltqlqkevgkdvsdek
lrdyiwntlnsgrvvpgyghavlrktdprytcqrefalkhlphdpmfklvaqlykivpnv
lleqgkaknpwpnvdahsgvllqyygmtemnyytvlfgvsralgvlaqliwsralgfple
rpksmstdgliklvdsk
>d1ctt_1 3.84.1.1.1 (1-150) Cytidine deaminase {(Escherichia coli)}
mhprfqtafaqladnlqsalepiladkyfpalltgeqvsslksatgldedalafallpla
aacartplsnfnvgaiargvsgtwyfganmefigatmqqtvhaeqsaishawlsgekala
aitvnytpcghcrqfmnelnsgldlrihlp
>d1ctt_2 3.84.1.1.1 (151-294) Cytidine deaminase {(Escherichia coli)}
greahalrdylpdafgpkdleiktllmdeqdhgyaltgdalsqaaiaaanrshmpysksp
sgvaleckdgrifsgsyaenaafnptlpplqgalillnlkgydypdiqravlaekadapl
iqwdatsatlkalgchsidrvlla
>d1ctu_1 3.84.1.1.1 (1-150) Cytidine deaminase {(Escherichia coli)}
mhprfqtafaqladnlqsalepiladkyfpalltgeqvsslksatgldedalafallpla
aacartplsnfnvgaiargvsgtwyfganmefigatmqqtvhaeqsaishawlsgekala
aitvnytpcghcrqfmnelnsgldlrihlp
>d1ctu_2 3.84.1.1.1 (151-294) Cytidine deaminase {(Escherichia coli)}
greahalrdylpdafgpkdleiktllmdeqdhgyaltgdalsqaaiaaanrshmpysksp
sgvaleckdgrifsgsyaenaafnptlpplqgalillnlkgydypdiqravlaekadapl
iqwdatsatlkalgchsidrvlla
>d1ctx__ 7.6.1.1.7 alpha-Cobratoxin {cobra (Naja naja siamensis)}
ircfitpditskdcpnghvcytktwcdafcsirgkrvdlgcaatcptvktgvdiqccstd
ncnpfptrkrp
>d1cty__ 1.3.1.1.6 Mitochondrial cytochrome c {baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdanikk
nvlwdennmsefltnpkkyipgtkmafgglkkekdrndlitylkkate
>d1ctz__ 1.3.1.1.6 Mitochondrial cytochrome c {baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdanikk
nvlwdennmsefltnpkkyipgtkmafgglkkekdrndlitylkkate
>d1cua__ 3.14.7.1.1 Cutinase {fungus (Fusarium solani, subsp. pisi)}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcktgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1cub__ 3.14.7.1.1 Cutinase {fungus (Fusarium solani, subsp. pisi)}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcktgdlvctgslivaaphlaygpdae
gpapefliekvravrgs
>d1cuc__ 3.14.7.1.1 Cutinase {fungus (Fusarium solani, subsp. pisi)}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcktgdlvctgslivaaphlaygpdae
gpapefliekvravrgs
>d1cuda_ 3.14.7.1.1 Cutinase {fungus (Fusarium solani, subsp. pisi)}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcktgdlvctgslivaaphlaygpdae
gpapefliekvravrgs
>d1cudb_ 3.14.7.1.1 Cutinase {fungus (Fusarium solani, subsp. pisi)}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcktgdlvctgslivaaphlaygpdae
gpapefliekvravrgs
>d1cudc_ 3.14.7.1.1 Cutinase {fungus (Fusarium solani, subsp. pisi)}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcktgdlvctgslivaaphlaygpdae
gpapefliekvravrgs
>d1cue__ 3.14.7.1.1 Cutinase {fungus (Fusarium solani, subsp. pisi)}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggyslgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1cuf__ 3.14.7.1.1 Cutinase {fungus (Fusarium solani, subsp. pisi)}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnlgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1cug__ 3.14.7.1.1 Cutinase {fungus (Fusarium solani, subsp. pisi)}
ettrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcktgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1cuh__ 3.14.7.1.1 Cutinase {fungus (Fusarium solani, subsp. pisi)}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdae
gpapefliekvravrgs
>d1cui__ 3.14.7.1.1 Cutinase {fungus (Fusarium solani, subsp. pisi)}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggyaqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1cuj__ 3.14.7.1.1 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 1.64.1.1.1 (65-142) DNA helicase RuvA subunit, the middle domain {(Escherichia coli)}
nkqertlfkeliktngvgpklalailsgmsaqqfvnavereevgalvklpgigkktaerl
ivemkdrfkglhgdlftp
>d1cuk_3 2.29.4.2.1 (1-64) DNA helicase RuvA subunit, N-terminal domain {(Escherichia coli)}
migrlrgiiiekqpplvlievggvgyevhmpmtcfyelpeagqeaivfthfvvredaqll
ygfn
>d1cuma_ 4.51.1.1.2 Flavin reductase P (NADPH:FMN oxidoreductase) {(Vibrio harveyi)}
nntietilahrsirkftavpitdeqrqtiiqaglaassssmlqvvsivrvtdsekrnela
qfagnqayvesaaeflvfcidyqrhatinpdvqadfteltligavdsgimaqncllaaes
mglggvyigglrnsaaqvdellglpensavlfgmclghpdqnpevkprlpahvvvhenqy
qelnlddiqsydqtmqayyasrtsnqklstwsqevtgklagesrphilpylnskglakr
>d1cumb_ 4.51.1.1.2 Flavin reductase P (NADPH:FMN oxidoreductase) {(Vibrio harveyi)}
nntietilahrsirkftavpitdeqrqtiiqaglaassssmlqvvsivrvtdsekrnela
qfagnqayvesaaeflvfcidyqrhatinpdvqadfteltligavdsgimaqncllaaes
mglggvyigglrnsaaqvdellglpensavlfgmclghpdqnpevkprlpahvvvhenqy
qelnlddiqsydqtmqayyasrtsnqklstwsqevtgklagesrphilpylnskglakr
>d1cur__ 2.5.1.1.20 Rusticyanin {(Thiobacillus ferooxidans)}
gtldttwkeatlpqvkamlekdtgkvsgdtvtysgktvhvvaaavlpgfpfpsfevhdkk
nptleipagatvdvtfintnkgfghsfditkkgppyavmpvidpivagtgfspvpkdgkf
gytdftwhptagtyyyvcqipghaatgmfgkivvk
>d1cus__ 3.14.7.1.1 Cutinase {fungus (Fusarium solani, subsp. pisi)}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1cuu__ 3.14.7.1.1 Cutinase {fungus (Fusarium solani, subsp. pisi)}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpcpefliekvravrgs
>d1cuv__ 3.14.7.1.1 Cutinase {fungus (Fusarium solani, subsp. pisi)}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnflprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1cuwa_ 3.14.7.1.1 Cutinase {fungus (Fusarium solani, subsp. pisi)}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratladnflprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgsliilaphfaygpdar
gpapefliekvravrgs
>d1cuwb_ 3.14.7.1.1 Cutinase {fungus (Fusarium solani, subsp. pisi)}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratladnflprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgsliilaphfaygpdar
gpapefliekvravrgs
>d1cux__ 3.14.7.1.1 Cutinase {fungus (Fusarium solani, subsp. pisi)}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatyiaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1cuy__ 3.14.7.1.1 Cutinase {fungus (Fusarium solani, subsp. pisi)}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphfaygpdar
gpapefliekvravrgs
>d1cuz__ 3.14.7.1.1 Cutinase {fungus (Fusarium solani, subsp. pisi)}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratggdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgsgivaaphlaygpdar
gpapefliekvravrg
>d1cva__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslvtppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1cvb__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslvtppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1cvc__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfdfhwgsldgqgsehtvdkkkyaaelhlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1cvd__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelclvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1cve__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaeldlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1cvf__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfafhwgsldgqgsehtvdkkkyaaelhlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1cvh__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfhfcwgsldgqgsehtvdkkkyaaelhlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1cvl__ 3.56.1.10.3 Bacterial lipase {(chromobacterium viscosum)}
adtyaatrypvilvhglagtdkfanvvdywygiqsdlqshgakvyvanlsgfqsddgpng
rgeqllayvkqvlaatgatkvnlighsqggltsryvaavapqlvasvttigtphrgsefa
dfvqdvlktdptglsstviaafvnvfgtlvssshntdqdalaalrtlttaqtatynrnfp
saglgapgscqtgaatetvggsqhllyswggtaiqptstvlgvtgatdtstgtldvanvt
dpstlallatgavminrasgqndglvsrcsslfgqvistsyhwnhldeinqllgvrgana
edpvavirthvnrlklqgv
>d1cvna_ 2.21.1.1.1 Concanavalin A {jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1cvnb_ 2.21.1.1.1 Concanavalin A {jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1cvnc_ 2.21.1.1.1 Concanavalin A {jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1cvnd_ 2.21.1.1.1 Concanavalin A {jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1cvo__ 7.6.1.1.6 Cardiotoxin V {taiwan cobra (Naja naja atra)}
lkchntqlpfiyktcpegknlcfkatlkkfplkfpvkrgcadncpknsallkyvccstdk
cn
>d1cwaa_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
mvnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgf
mcqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictakte
wldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1cwba_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
mvnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgf
mcqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictakte
wldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1cwca_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
mvnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgf
mcqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictakte
wldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1cwdl_ 4.53.1.1.1 p56-lck tyrosine kinase {human (Homo sapiens)}
gswffknlsrkdaerqllapgnthgsfliresestagsfslsvrdfdqnqgevvkhykir
nldnggfyispritfpglhelvrhytnasdglctrlsr
>d1cwea_ 4.53.1.1.1 p56-lck tyrosine kinase {human (Homo sapiens)}
gswffknlsrkdaerqllapgnthgsfliresestagsfslsvrdfdqnqgevvkhykir
nldnggfyispritfpglhelvrhytnasdglctrlsr
>d1cwec_ 4.53.1.1.1 p56-lck tyrosine kinase {human (Homo sapiens)}
gswffknlsrkdaerqllapgnthgsfliresestagsfslsvrdfdqnqgevvkhykir
nldnggfyispritfpglhelvrhytnasdglctrlsr
>d1cwfa_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
mvnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgf
mcqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictakte
wldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1cwha_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
mvnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgf
mcqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictakte
wldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1cwka_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
mvnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgf
mcqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictakte
wldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1cwla_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
mvnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgf
mcqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictakte
wldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1cwma_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
mvnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgf
mcqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictakte
wldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1cwn__ 3.1.5.1.4 Aldose reductase (aldehyde reductase) {porcine (Sus scrofa)}
aascvllhtgqkmpliglgtwksepgqvkaaikyaltvgyrhidcaaiygneleigealt
etvgpgkavpreelfvtsklwntkhhpedvepalrktladlqleyldlylmhwpyaferg
dnpfpknadgtirydathykdtwkalealvakglvralglsnfssrqiddvlsvasvrpa
vlqvechpylaqneliahcqarglevtaysplgssdrawrdpnepvlleepvvqalaeky
nrspaqillrwqvqrkvicipksvtpsripqniqvfdftfspeemkqldalnknlrfivp
mltvdgkrvprdaghplypfndpy
>d1cwpa_ 2.8.1.2.9 Cowpea chlorotic mottle virus {host: cowpea (Vigna unguiculta) (L.)}
kaikawtgysvskwtascaaaeakvtsaitislpnelssernkqlkvgrvllwlgllpsv
sgtvkscvtetqttaaasfqvalavadnskdvvaamypeafkgitleqlaadltiylyss
aaltegdvivhlevehvrptfddsftpvy
>d1cwpb_ 2.8.1.2.9 Cowpea chlorotic mottle virus {host: cowpea (Vigna unguiculta) (L.)}
vvqpvivepiasgqgkaikawtgysvskwtascaaaeakvtsaitislpnelssernkql
kvgrvllwlgllpsvsgtvkscvtetqttaaasfqvalavadnskdvvaamypeafkgit
leqlaadltiylyssaaltegdvivhlevehvrptfddsftpvy
>d1cwpc_ 2.8.1.2.9 Cowpea chlorotic mottle virus {host: cowpea (Vigna unguiculta) (L.)}
vvqpvivepiasgqgkaikawtgysvskwtascaaaeakvtsaitislpnelssernkql
kvgrvllwlgllpsvsgtvkscvtetqttaaasfqvalavadnskdvvaamypeafkgit
leqlaadltiylyssaaltegdvivhlevehvrptfddsftpvy
>d1cx2a1 1.72.1.2.4 (74-583) Prostaglandin H2 synthase-1 {Mouse (Mus musculus)}
fltriklllkptpntvhyilthfkgvwnivnnipflrslimkyvltsrsylidspptynv
hygyksweafsnlsyytralppvaddcptpmgvkgnkelpdskevlekvllrrefipdpq
gsnmmfaffaqhfthqffktdhkrgpgftrglghgvdlnhiygetldrqhklrlfkdgkl
kyqviggevypptvkdtqvemiypphipenlqfavgqevfglvpglmmyatiwlrehqrv
cdilkqehpewgdeqlfqtskliligetikiviedyvqhlsgyhfklkfdpellfnqqfq
yqnriasefntlyhwhpllpdtfniedqeysfkqflynnsillehgltqfvesftrqiag
rvaggrnvpiavqavakasidqsremkyqslneyrkrfslkpytsfeeltgekemaaelk
alysdidvmelypallvekprpdaifgetmvelgapfslkglmgnpicspqywkpstfgg
evgfkiintasiqslicnnvkgcpftsfnvq
>d1cx2a2 7.3.9.1.9 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Mouse (Mus musculus)}
anpccsnpcqnrgecmstgfdqykcdctrtgfygencttpe
>d1cx2b1 1.72.1.2.4 (74-583) Prostaglandin H2 synthase-1 {Mouse (Mus musculus)}
fltriklllkptpntvhyilthfkgvwnivnnipflrslimkyvltsrsylidspptynv
hygyksweafsnlsyytralppvaddcptpmgvkgnkelpdskevlekvllrrefipdpq
gsnmmfaffaqhfthqffktdhkrgpgftrglghgvdlnhiygetldrqhklrlfkdgkl
kyqviggevypptvkdtqvemiypphipenlqfavgqevfglvpglmmyatiwlrehqrv
cdilkqehpewgdeqlfqtskliligetikiviedyvqhlsgyhfklkfdpellfnqqfq
yqnriasefntlyhwhpllpdtfniedqeysfkqflynnsillehgltqfvesftrqiag
rvaggrnvpiavqavakasidqsremkyqslneyrkrfslkpytsfeeltgekemaaelk
alysdidvmelypallvekprpdaifgetmvelgapfslkglmgnpicspqywkpstfgg
evgfkiintasiqslicnnvkgcpftsfnvq
>d1cx2b2 7.3.9.1.9 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Mouse (Mus musculus)}
anpccsnpcqnrgecmstgfdqykcdctrtgfygencttpe
>d1cx2c1 1.72.1.2.4 (74-583) Prostaglandin H2 synthase-1 {Mouse (Mus musculus)}
fltriklllkptpntvhyilthfkgvwnivnnipflrslimkyvltsrsylidspptynv
hygyksweafsnlsyytralppvaddcptpmgvkgnkelpdskevlekvllrrefipdpq
gsnmmfaffaqhfthqffktdhkrgpgftrglghgvdlnhiygetldrqhklrlfkdgkl
kyqviggevypptvkdtqvemiypphipenlqfavgqevfglvpglmmyatiwlrehqrv
cdilkqehpewgdeqlfqtskliligetikiviedyvqhlsgyhfklkfdpellfnqqfq
yqnriasefntlyhwhpllpdtfniedqeysfkqflynnsillehgltqfvesftrqiag
rvaggrnvpiavqavakasidqsremkyqslneyrkrfslkpytsfeeltgekemaaelk
alysdidvmelypallvekprpdaifgetmvelgapfslkglmgnpicspqywkpstfgg
evgfkiintasiqslicnnvkgcpftsfnvq
>d1cx2c2 7.3.9.1.9 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Mouse (Mus musculus)}
anpccsnpcqnrgecmstgfdqykcdctrtgfygencttpe
>d1cx2d1 1.72.1.2.4 (74-583) Prostaglandin H2 synthase-1 {Mouse (Mus musculus)}
fltriklllkptpntvhyilthfkgvwnivnnipflrslimkyvltsrsylidspptynv
hygyksweafsnlsyytralppvaddcptpmgvkgnkelpdskevlekvllrrefipdpq
gsnmmfaffaqhfthqffktdhkrgpgftrglghgvdlnhiygetldrqhklrlfkdgkl
kyqviggevypptvkdtqvemiypphipenlqfavgqevfglvpglmmyatiwlrehqrv
cdilkqehpewgdeqlfqtskliligetikiviedyvqhlsgyhfklkfdpellfnqqfq
yqnriasefntlyhwhpllpdtfniedqeysfkqflynnsillehgltqfvesftrqiag
rvaggrnvpiavqavakasidqsremkyqslneyrkrfslkpytsfeeltgekemaaelk
alysdidvmelypallvekprpdaifgetmvelgapfslkglmgnpicspqywkpstfgg
evgfkiintasiqslicnnvkgcpftsfnvq
>d1cx2d2 7.3.9.1.9 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Mouse (Mus musculus)}
anpccsnpcqnrgecmstgfdqykcdctrtgfygencttpe
>d1cxa__ 1.3.1.1.13 Cytochrome c2 {(Rhodobacter spaeroides)}
qegdpeagakafnqcqtchvivddsgttiagrnaktgpnlygvvgrtagtqadfkgygeg
mkeagakglawdeehfvqyvqdptkflkeytgdakakgkmtfklkkeadahniwaylqqv
avrp
>d1cxc__ 1.3.1.1.13 Cytochrome c2 {(Rhodobacter spaeroides)}
qegdpeagakafnqcqtchvivddsgttiagrnaktgpnlygvvgrtagtqadfkgygeg
mkeagakglawdeehfvqyvqdptkflkeytgdakakgkmtfklkkeadahniwaylqqv
avrp
>d1cxe_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {(Bacillus circulans)}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d1cxe_2 2.3.1.1.1 (582-686) Cyclodextrin glycosyltransferase, C-terminal domain {(Bacillus circulans)}
lsgdqvsvrfvvnnattalgqnvyltgsvselgnwdpakaigpmynqvvyqypnwyydvs
vpagktiefkflkkqgstvtweggsnhtftapssgtatinvnwqp
>d1cxe_3 2.53.1.1.2 (383-495) Cyclodextrin glycosyltransferase {(Bacillus circulans)}
tsttayqviqklaplrkcnpaiaygstqerwinndvliyerkfgsnvavvavnrnlnapa
sisglvtslpqgsyndvlggllngntlsvgsggaasnftlaaggtavwqytaa
>d1cxe_4 3.1.1.1.2 (1-382) Cyclodextrin glycosyltransferase {(Bacillus circulans)}
apdtsvsnkqnfstdviyqiftdrfsdgnpannptgaafdgtctnlrlycggdwqgiink
indgyltgmgvtaiwisqpveniysiinysgvnntayhgywardfkktnpaygtiadfqn
liaaahaknikviidfapnhtspassdqpsfaengrlydngtllggytndtqnlfhhngg
tdfsttengiyknlydladlnhnnstvdvylkdaikmwldlgidgirmdavkhmpfgwqk
sfmaavnnykpvftfgewflgvnevspenhkfanesgmslldfrfaqkvrqvfrdntdnm
yglkamlegsaadyaqvddqvtfidnhdmerfhasnanrrkleqalaftltsrgvpaiyy
gteqymsggtdpdnraripsfs
>d1cxf_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {(Bacillus circulans)}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d1cxf_2 2.3.1.1.1 (582-686) Cyclodextrin glycosyltransferase, C-terminal domain {(Bacillus circulans)}
lsgdqvsvrfvvnnattalgqnvyltgsvselgnwdpakaigpmynqvvyqypnwyydvs
vpagktiefkflkkqgstvtweggsnhtftapssgtatinvnwqp
>d1cxf_3 2.53.1.1.2 (383-495) Cyclodextrin glycosyltransferase {(Bacillus circulans)}
tsttayqviqklaplrkcnpaiaygstqerwinndvliyerkfgsnvavvavnrnlnapa
sisglvtslpqgsyndvlggllngntlsvgsggaasnftlaaggtavwqytaa
>d1cxf_4 3.1.1.1.2 (1-382) Cyclodextrin glycosyltransferase {(Bacillus circulans)}
apdtsvsnkqnfstdviyqiftdrfsdgnpannptgaafdgtctnlrlycggdwqgiink
indgyltgmgvtaiwisqpveniysiinysgvnntayhgywardfkktnpaygtiadfqn
liaaahaknikviidfapnhtspassdqpsfaengrlydngtllggytndtqnlfhhngg
tdfsttengiyknlydladlnhnnstvdvylkdaikmwldlgidgirmnavkhmpfgwqk
sfmaavnnykpvftfgqwflgvnevspenhkfanesgmslldfrfaqkvrqvfrdntdnm
yglkamlegsaadyaqvddqvtfidnhdmerfhasnanrrkleqalaftltsrgvpaiyy
gteqymsggtdpdnraripsfs
>d1cxg_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {(Bacillus circulans)}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d1cxg_2 2.3.1.1.1 (582-686) Cyclodextrin glycosyltransferase, C-terminal domain {(Bacillus circulans)}
lsgdqvsvrfvvnnattalgqnvyltgsvselgnwdpakaigpmynqvvyqypnwyydvs
vpagktiefkflkkqgstvtweggsnhtftapssgtatinvnwqp
>d1cxg_3 2.53.1.1.2 (383-495) Cyclodextrin glycosyltransferase {(Bacillus circulans)}
tsttayqviqklaplrkcnpaiaygstqerwinndvliyerkfgsnvavvavnrnlnapa
sisglvtslpqgsyndvlggllngntlsvgsggaasnftlaaggtavwqytaa
>d1cxg_4 3.1.1.1.2 (1-382) Cyclodextrin glycosyltransferase {(Bacillus circulans)}
apdtsvsnkqnfstdviyqiftdrfsdgnpannptgaafdgtctnlrlycggdwqgiink
indgyltgmgvtaiwisqpveniysiinysgvnntayhgywardfkktnpaygtiadfqn
liaaahaknikviidfapnhtspassdqpsfaengrlydngtllggytndtqnlfhhngg
tdfsttengiyknlydladlnhnnstvdvylkdaikmwldlgidgirmdavkhmpfgwqk
sfmaavnnykpvftfgewflgvnevspenhkfanesgmslldfrfaqkvrqvfrdntdnm
yglkamlegsaadyaqvddqvtfidnhdmerfhasnanrrkleqalaftltsrgvpaiyy
gteqymsggtdpdnraripsfs
>d1cxh_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {(Bacillus circulans)}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d1cxh_2 2.3.1.1.1 (582-686) Cyclodextrin glycosyltransferase, C-terminal domain {(Bacillus circulans)}
lsgdqvsvrfvvnnattalgqnvyltgsvselgnwdpakaigpmynqvvyqypnwyydvs
vpagktiefkflkkqgstvtweggsnhtftapssgtatinvnwqp
>d1cxh_3 2.53.1.1.2 (383-495) Cyclodextrin glycosyltransferase {(Bacillus circulans)}
tsttayqviqklaplrkcnpaiaygstqerwinndvliyerkfgsnvavvavnrnlnapa
sisglvtslpqgsyndvlggllngntlsvgsggaasnftlaaggtavwqytaa
>d1cxh_4 3.1.1.1.2 (1-382) Cyclodextrin glycosyltransferase {(Bacillus circulans)}
apdtsvsnkqnfstdviyqiftdrfsdgnpannptgaafdgtctnlrlycggdwqgiink
indgyltgmgvtaiwisqpveniysiinysgvnntayhgywardfkktnpaygtiadfqn
liaaahaknikviidfapnhtspassdqpsfaengrlydngtllggytndtqnlfhhngg
tdfsttengiyknlydladlnhnnstvdvylkdaikmwldlgidgirmdavkhmpfgwqk
sfmaavnnykpvftfgewflgvnevspenhkfanesgmslldfrfaqkvrqvfrdntdnm
yglkamlegsaadyaqvddqvtfidnhdmerfhasnanrrkleqalaftltsrgvpaiyy
gteqymsggtdpdnraripsfs
>d1cxi_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {(Bacillus circulans)}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d1cxi_2 2.3.1.1.1 (582-686) Cyclodextrin glycosyltransferase, C-terminal domain {(Bacillus circulans)}
lsgdqvsvrfvvnnattalgqnvyltgsvselgnwdpakaigpmynqvvyqypnwyydvs
vpagktiefkflkkqgstvtweggsnhtftapssgtatinvnwqp
>d1cxi_3 2.53.1.1.2 (383-495) Cyclodextrin glycosyltransferase {(Bacillus circulans)}
tsttayqviqklaplrkcnpaiaygstqerwinndvliyerkfgsnvavvavnrnlnapa
sisglvtslpqgsyndvlggllngntlsvgsggaasnftlaaggtavwqytaa
>d1cxi_4 3.1.1.1.2 (1-382) Cyclodextrin glycosyltransferase {(Bacillus circulans)}
apdtsvsnkqnfstdviyqiftdrfsdgnpannptgaafdgtctnlrlycggdwqgiink
indgyltgmgvtaiwisqpveniysiinysgvnntayhgywardfkktnpaygtiadfqn
liaaahaknikviidfapnhtspassdqpsfaengrlydngtllggytndtqnlfhhngg
tdfsttengiyknlydladlnhnnstvdvylkdaikmwldlgidgirmdavkhmpfgwqk
sfmaavnnykpvftfgewflgvnevspenhkfanesgmslldfrfaqkvrqvfrdntdnm
yglkamlegsaadyaqvddqvtfidnhdmerfhasnanrrkleqalaftltsrgvpaiyy
gteqymsggtdpdnraripsfs
>d1cxn__ 7.6.1.1.2 gamma-Cardiotoxin {snake (Naja nigricollis)}
lkcnqlippfwktcpkgknlcykmtmraapmvpvkrgcidvcpkssllikymccntdkcn
>d1cxo__ 7.6.1.1.2 gamma-Cardiotoxin {snake (Naja nigricollis)}
lkcnqlippfwktcpkgknlcykmtmraapmvpvkrgcidvcpkssllikymccntdkcn
>d1cxsa1 2.39.2.2.1 (626-780) Dimethylsulfoxide reductase (DMSO reductase) {(Rhodobacter sphaeroides)}
erlggagakyplhvvashpksrlhsqlngtslrdlyavaghepclinpadaaargiadgd
vlrvfndrgqilvgakvsdavmpgaiqiyeggwydpldpseegtldkygdvnvlsldvgt
sklaqgncgqtiladvekyagapvtvtvfdtpkga
>d1cxsa2 3.69.1.1.1 (1-625) Dimethylsulfoxide reductase (DMSO reductase) {(Rhodobacter sphaeroides)}
eglangevmsgchwgvfkarvengravafepwdkdpapshqlpgvldsiysptrikypmv
rreflekgvnadrstrgngdfvrvtwdealdlvarelkrvqesygptgtfggsygwkspg
rlhncqvlmrralnlaggfvnssgdystaaaqiimphvmgtlevyeqqtawpvvventdl
mvfwaadpmktneigwvipdhgayagmkalkekgtrvicinpvrtetadyfgadvvsprp
qtdvalmlgmahtlysedlhdkdflencttgfdlfaayltgesdgtpktaewaaeicglp
aeqirelarsfvagrtmlaagwsiqrmhhgeqahwmlvtlasmigqiglpgggfglsyhy
snggsptsdgpalggisdggkavegaawlsesgatsipcarvvdmllnpggefqfngata
typdvklaywaggnpfahhqdrnrmlkawekletfivqdfqwtatarhadivlpattsye
rndiesvgdysnrailamkkvvdplyearsdydifaalaerlgkgaeftegrdemgwiss
fyeaavkqaefknvampsfedfwsegivefpiteganfvryadfredplfnplgtpsgli
eiyskniekmgyddcpahptwmepa
>d1cxta1 2.39.2.2.1 (626-780) Dimethylsulfoxide reductase (DMSO reductase) {(Rhodobacter sphaeroides)}
erlggagakyplhvvashpksrlhsqlngtslrdlyavaghepclinpadaaargiadgd
vlrvfndrgqilvgakvsdavmpgaiqiyeggwydpldpseegtldkygdvnvlsldvgt
sklaqgncgqtiladvekyagapvtvtvfdtpkga
>d1cxta2 3.69.1.1.1 (1-625) Dimethylsulfoxide reductase (DMSO reductase) {(Rhodobacter sphaeroides)}
eglangevmsgchwgvfkarvengravafepwdkdpapshqlpgvldsiysptrikypmv
rreflekgvnadrstrgngdfvrvtwdealdlvarelkrvqesygptgtfggsygwkspg
rlhncqvlmrralnlaggfvnssgdystaaaqiimphvmgtlevyeqqtawpvvventdl
mvfwaadpmktneigwvipdhgayagmkalkekgtrvicinpvrtetadyfgadvvsprp
qtdvalmlgmahtlysedlhdkdflencttgfdlfaayltgesdgtpktaewaaeicglp
aeqirelarsfvagrtmlaagwsiqrmhhgeqahwmlvtlasmigqiglpgggfglsyhy
snggsptsdgpalggisdggkavegaawlsesgatsipcarvvdmllnpggefqfngata
typdvklaywaggnpfahhqdrnrmlkawekletfivqdfqwtatarhadivlpattsye
rndiesvgdysnrailamkkvvdplyearsdydifaalaerlgkgaeftegrdemgwiss
fyeaavkqaefknvampsfedfwsegivefpiteganfvryadfredplfnplgtpsgli
eiyskniekmgyddcpahptwmepa
>d1cyc__ 1.3.1.1.10 Mitochondrial cytochrome c {bonito (Katsuwonus pelamis, linnaeus)}
gdvakgkktfvqkcaqchtvenggkhkvgpnlwglfgrktgqaegysytdankskgivwn
entlmeylenpkkyipgtkmifagikkkgerqdlvaylksats
>d1cyda_ 3.22.1.2.2 Carbonyl reductase {Mouse (Mus musculus)}
lnfsglralvtgagkgigrdtvkalhasgakvvavtrtnsdlvslakecpgiepvcvdlg
dwdatekalggigpvdllvnnaalvimqpflevtkeafdrsfsvnlrsvfqvsqmvardm
inrgvpgsivnvssmvahvtfpnlitysstkgamtmltkamamelgphkirvnsvnptvv
ltdmgkkvsadpefarklkerhplrkfaevedvvnsilfllsdrsastsgggilvdagyl
as
>d1cydb_ 3.22.1.2.2 Carbonyl reductase {Mouse (Mus musculus)}
lnfsglralvtgagkgigrdtvkalhasgakvvavtrtnsdlvslakecpgiepvcvdlg
dwdatekalggigpvdllvnnaalvimqpflevtkeafdrsfsvnlrsvfqvsqmvardm
inrgvpgsivnvssmvahvtfpnlitysstkgamtmltkamamelgphkirvnsvnptvv
ltdmgkkvsadpefarklkerhplrkfaevedvvnsilfllsdrsastsgggilvdagyl
as
>d1cydc_ 3.22.1.2.2 Carbonyl reductase {Mouse (Mus musculus)}
lnfsglralvtgagkgigrdtvkalhasgakvvavtrtnsdlvslakecpgiepvcvdlg
dwdatekalggigpvdllvnnaalvimqpflevtkeafdrsfsvnlrsvfqvsqmvardm
inrgvpgsivnvssmvahvtfpnlitysstkgamtmltkamamelgphkirvnsvnptvv
ltdmgkkvsadpefarklkerhplrkfaevedvvnsilfllsdrsastsgggilvdagyl
as
>d1cydd_ 3.22.1.2.2 Carbonyl reductase {Mouse (Mus musculus)}
lnfsglralvtgagkgigrdtvkalhasgakvvavtrtnsdlvslakecpgiepvcvdlg
dwdatekalggigpvdllvnnaalvimqpflevtkeafdrsfsvnlrsvfqvsqmvardm
inrgvpgsivnvssmvahvtfpnlitysstkgamtmltkamamelgphkirvnsvnptvv
ltdmgkkvsadpefarklkerhplrkfaevedvvnsilfllsdrsastsgggilvdagyl
as
>d1cye__ 3.14.2.1.1 CheY protein {(Escherichia coli)}
rsdkelkflvvddfstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnm
pnmdglellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleekl
nkifeklgm
>d1cyf__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
mittplvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwd
khdntggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqe
mqgpkipwragrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalg
kthlknsgyegpwgcannvftnefylnllnedwklekndanneqwdsksgymmlptdysl
iqdpkylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1cyg_1 2.1.1.5.5 (492-574) Cyclodextrin glycosyltransferase, domain E {(Bacillus stearothermophylus)}
estpiighvgpmmgqvghqvtidgegfgtntgtvkfgttaanvvswsnnqivvavpnvsp
gkynitvqsssgqtsaaydnfev
>d1cyg_2 2.3.1.1.2 (575-680) Cyclodextrin glycosyltransferase, C-terminal domain {(Bacillus stearothermophilus)}
ltndqvsvrfvvnnattnlgqniyivgnvyelgnwdtskaigpmfnqvvysyptwyidvs
vpegktiefkfikkdsqgnvtwesgsnhvyttptnttgkiivdwqn
>d1cyg_3 2.53.1.1.3 (379-491) Cyclodextrin glycosyltransferase {(Bacillus sterothermophilus)}
kntrayqviqklsslrrnnpalaygdteqrwingdvyvyerqfgkdvvlvavnrssssny
sitglftalpagtytdqlgglldgntiqvgsngsvnafdlgpgevgvwaysat
>d1cyg_4 3.1.1.1.3 (1-378) Cyclodextrin glycosyltransferase {(Bacillus stearothermophilus)}
agnlnkvnftsdvvyqivvdrfvdgntsnnpsgalfssgctnlrkycggdwqgiinkind
gyltdmgvtaiwisqpvenvfsvmndasgsasyhgywardfkkpnpffgtlsdfqrlvda
ahakgikviidfapnhtspasetnpsymengrlydngtllggytndanmyfhhnggttfs
sledgiyrnlfdladlnhqnpvidrylkdavkmwidmgidgirmdavkhmpfgwqkslmd
eidnyrpvftfgewflsenevdannhyfanesgmslldfrfgqklrqvlrnnsdnwygfn
qmiqdtasaydevldqvtfidnhdmdrfmidggdprkvdmalavlltsrgvpniyygteq
ymtgngdpnnrkmmssfn
>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__ 1.26.1.2.2 Interleukin-4 (IL-4) {human (Homo sapiens)}
hkcditlqeiiktlnslteqktlcteltvtdifaaskntteketfcraatvlrqfyshhe
kdtrclgataqqfhrhkqlirflkrldrnlwglaglnscpvkeanqstlenflerlktim
rekyskcss
>d1cyna_ 2.47.1.1.3 Cyclophilin B {Human (Homo sapiens)}
gpkvtvkvyfdlrigdedvgrvifglfgktvpktvdnfvalatgekgfgyknskfhrvik
dfmiqggdftrgdgtggksiygerfpdenfklkhygpgwvsmanagkdtngsqffittvk
tawldgkhvvfgkvlegmevvrkvestktdsrdkplkdviiadcgkievekpfaiake
>d1cyo__ 4.70.1.1.1 Cytochrome b5 {bovine (Bos taurus)}
skavkyytleeiqkhnnskstwlilhykvydltkfleehpggeevlreqaggdatenfed
vghstdarelsktfiigelhpddrskit
>d1cyu__ 4.13.1.2.2 Cystatin A (stefin A) {human (Homo sapiens)}
mipgglseakpatpeiqeivdkvkpqleektnetygkleavqyktqvvagtnyyikvrag
dnkylhlkvfkslpgqnedlvltgyqvdknkddeltgf
>d1cyv__ 4.13.1.2.2 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
>d1czie_ 2.38.1.2.13 Chymosin (synonim: renin) {bovine (Bos taurus)}
gevasvpltnyldsqyfgkiylgtppqeftvlfdtgssdfwvpsiycksnacknhqrfdp
rksstfqnlgkplsihygtgsmqgilgydtvtvsnivdiqqtvglstqepgdvftyaefd
gilgmaypslaseysipvfdnmmnrhlvaqdlfsvymdrngqesmltlgaidpsyytgsl
hwvpvtvqqywqftvdsvtisgvvvaceggcqaildtgtsklvgpssdilniqqaigatq
nqygefdidcdnlsymptvvfeingkmypltpsaytsqdqgfctsgfqsenhsqkwilgd
vfireyysvfdrannlvglakai
>d1czj__ 1.107.1.1.1 Cytochrome c3 {(Desulfovibrio desulfuricans), different strains}
tfeipesvtmspkqfegytpkkgdvtfnhashmdiacqqchhtvpdtytiescmtegchd
nikerteissvyrtfhttkdsekscvgchrelkrqgpsdaplacnschvq
>d1czm__ 2.56.1.1.1 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme I}
aspdwgyddkngpeqwsklypiangnnqspvdiktsetkhdtslkpisvsynpatakeii
nvghsfhvnfedndnrsvlkggpfsdsyrlfqfhfhwgstnehgsehtvdgvkysaelhv
ahwnsakysslaeaaskadglavigvlmkvgeanpklqkvldalqaiktkgkrapftnfd
pstllpssldfwtypgslthpplyesvtwiickesisvsseqlaqfrsllsnvegdnavp
mqhnnrptqplkgrtvrasf
>d1d66a2 7.32.1.1.1 (8-48) Gal4 {yeast (Saccharomyces cerevisiae)}
eqacdicrlkklkcskekpkcakclknnwecryspktkrsp
>d1d66b2 7.32.1.1.1 (8-48) Gal4 {yeast (Saccharomyces cerevisiae)}
eqacdicrlkklkcskekpkcakclknnwecryspktkrsp
>d1daaa_ 5.14.1.1.1 D-amino acid aminotransferase {(Bacillus sp.) strain YM-1}
gytlwndqivkdeevkidkedrgyqfgdgvyevvkvyngemftvnehidrlyasaekiri
tipytkdkfhqllhelveknelntghiyfqvtrgtsprahqfpentvkpviigytkenpr
plenlekgvkatfvedirwlrcdikslnllgavlakqeahekgcyeailhrnntvtegss
snvfgikdgilythpannmilkgitrdvviacaneinmpvkeipftthealkmdelfvts
ttseitpvieidgklirdgkvgewtrklqkqfetkip
>d1daab_ 5.14.1.1.1 D-amino acid aminotransferase {(Bacillus sp.) strain YM-1}
gytlwndqivkdeevkidkedrgyqfgdgvyevvkvyngemftvnehidrlyasaekiri
tipytkdkfhqllhelveknelntghiyfqvtrgtsprahqfpentvkpviigytkenpr
plenlekgvkatfvedirwlrcdikslnllgavlakqeahekgcyeailhrnntvtegss
snvfgikdgilythpannmilkgitrdvviacaneinmpvkeipftthealkmdelfvts
ttseitpvieidgklirdgkvgewtrklqkqfetkip
>d1dad__ 3.29.1.6.1 Dethiobiotin synthetase {(Escherichia coli)}
skryfvtgtdtevgktvascallqaakaagyrtagykpvasgsektpeglrnsdalalqr
nsslqldyatvnpytfaeptsphiisaqegrpieslvmsaglraleqqadwvlvegaggw
ftplsdtftfadwvtqeqlpvilvvgvklgcinhamltaqviqhagltlagwvandvtpp
gkrhaeymttltrmipapllgeipwlaenpenaatgkyinlall
>d1dae__ 3.29.1.6.1 Dethiobiotin synthetase {(Escherichia coli)}
skryfvtgtdtevgktvascallqaakaagyrtagykpvasgsektpeglrnsdalalqr
nsslqldyatvnpytfaeptsphiisaqegrpieslvmsaglraleqqadwvlvegaggw
ftplsdtftfadwvtqeqlpvilvvgvklgcinhamltaqviqhagltlagwvandvtpp
gkrhaeymttltrmipapllgeipwlaenpenaatgkyinlall
>d1daf__ 3.29.1.6.1 Dethiobiotin synthetase {(Escherichia coli)}
skryfvtgtdtevgktvascallqaakaagyrtagykpvasgsektpeglrnsdalalqr
nsslqldyatvnpytfaeptsphiisaqegrpieslvmsaglraleqqadwvlvegaggw
ftplsdtftfadwvtqeqlpvilvvgvklgcinhamltaqviqhagltlagwvandvtpp
gkrhaeymttltrmipapllgeipwlaenpenaatgkyinlall
>d1dag__ 3.29.1.6.1 Dethiobiotin synthetase {(Escherichia coli)}
skryfvtgtdtevgktvascallqaakaagyrtagykpvasgsektpeglrnsdalalqr
nsslqldyatvnpytfaeptsphiisaqegrpieslvmsaglraleqqadwvlvegaggw
ftplsdtftfadwvtqeqlpvilvvgvklgcinhamltaqviqhagltlagwvandvtpp
gkrhaeymttltrmipapllgeipwlaenpenaatgkyinlall
>d1dah__ 3.29.1.6.1 Dethiobiotin synthetase {(Escherichia coli)}
skryfvtgtdtevgktvascallqaakaagyrtagykpvasgsektpeglrnsdalalqr
nsslqldyatvnpytfaeptsphiisaqegrpieslvmsaglraleqqadwvlvegaggw
ftplsdtftfadwvtqeqlpvilvvgvklgcinhamltaqviqhagltlagwvandvtpp
gkrhaeymttltrmipapllgeipwlaenpenaatgkyinlall
>d1dai__ 3.29.1.6.1 Dethiobiotin synthetase {(Escherichia coli)}
skryfvtgtdtevgktvascallqaakaagyrtagykpvasgsektpeglrnsdalalqr
nsslqldyatvnpytfaeptsphiisaqegrpieslvmsaglraleqqadwvlvegaggw
ftplsdtftfadwvtqeqlpvilvvgvklgcinhamltaqviqhagltlagwvandvtpp
gkrhaeymttltrmipapllgeipwlaenpenaatgkyinlall
>d1daj__ 3.60.1.1.6 Dihydrofolate reductases, eukaryotic type {fungus (Pneumocystis carinii)}
mnqqksltlivalttsygigrsnslpwklkkeisyfkrvtsfvptfdsfesmnvvlmgrk
twesiplqfrplkgrinvvitrnesldlgngihsaksldhalellyrtygsessvqinri
fviggaqlykaamdhpkldrimatiiykdihcdvffplkfrdkewssvwkkekhsdlesw
vgtkvphgkinedgfdyefemwtrdl
>d1danh_ 2.35.1.2.18 Coagulation factor VIIa {human (Homo sapiens)}
ivggkvcpkgecpwqvlllvngaqlcggtlintiwvvsaahcfdkiknwrnliavlgehd
lsehdgdeqsrrvaqviipstyvpgttnhdiallrlhqpvvltdhvvplclpertfsert
lafvrfslvsgwgqlldrgatalelmvlnvprlmtqdclqqsrkvgdspniteymfcagy
sdgskdsckgdsggphathyrgtwyltgivswgqgcatvghfgvytrvsqyiewlqklmr
seprpgvllrapfp
>d1danl1 7.3.9.1.3 (47-86) Coagulation factor VIIa {human (Homo sapiens)}
gdqcasspcqnggsckdqlqsyicfclpafegrncethkd
>d1danl2 7.3.9.1.3 (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 3.21.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1daoa2 4.12.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1daob1 3.21.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1daob2 4.12.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1daoc1 3.21.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1daoc2 4.12.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1daod1 3.21.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1daod2 4.12.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1daoe1 3.21.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1daoe2 4.12.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1daof1 3.21.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1daof2 4.12.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1daog1 3.21.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1daog2 4.12.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1daoh1 3.21.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1daoh2 4.12.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1dapa1 3.22.1.3.9 (1-118,269-320) Diaminopimelic acid dehydrogenase (DAPDH) {(Corynebacterium glutamicum)}
mtnirvaivgygnlgrsvekliakqpdmdlvgifsrratldtktpvfdvadvdkhaddvd
vlflcmgsatdipeqapkfaqfactvdtydnhrdiprhrqvmneaataagnvalvstgXr
npdftassqiafgraahrmkqqgqsgaftvlevapyllspenlddliardv
>d1dapa2 4.42.1.2.1 (119-268) Diaminopimelic acid dehydrogenase (DAPDH) {(Corynebacterium glutamicum)}
wdpgmfsinrvyaaavlaehqqhtfwgpglsqghsdalrripgvqkavqytlpsedalek
arrgeagdltgkqthkrqcfvvadaadheriendirtmpdyfvgyevevnfideatfdse
htgmphgghvittgdtggfnhtveyilkld
>d1dapb1 3.22.1.3.9 (1-118,269-320) Diaminopimelic acid dehydrogenase (DAPDH) {(Corynebacterium glutamicum)}
mtnirvaivgygnlgrsvekliakqpdmdlvgifsrratldtktpvfdvadvdkhaddvd
vlflcmgsatdipeqapkfaqfactvdtydnhrdiprhrqvmneaataagnvalvstgXr
npdftassqiafgraahrmkqqgqsgaftvlevapyllspenlddliardv
>d1dapb2 4.42.1.2.1 (119-268) Diaminopimelic acid dehydrogenase (DAPDH) {(Corynebacterium glutamicum)}
wdpgmfsinrvyaaavlaehqqhtfwgpglsqghsdalrripgvqkavqytlpsedalek
arrgeagdltgkqthkrqcfvvadaadheriendirtmpdyfvgyevevnfideatfdse
htgmphgghvittgdtggfnhtveyilkld
>d1dar_1 2.32.3.1.4 (283-400) Elongation factor G (EF-G), domain II {(Thermus thermophilus)}
pldippikgttpegevveihpdpngplaalafkimadpyvgrltfirvysgtltsgsyvy
nttkgrkervarllrmhanhreeveelkagdlgavvglketitgdtlvgedaprvile
>d1dar_2 3.29.1.4.16 (1-282) Elongation factor G (EF-G), the N-terminal (G) domain {(Thermus thermophilus)}
mavkveydlkrlrnigiaahidagktttterilyytgrihkigevhegaatmdfmeqere
rgititaavttcfwkdhriniidtpghvdftieversmrvldgaivvfdssqgvepqset
vwrqaekykvpriafankmdktgadlwlvirtmqerlgarpvvmqlpigredtfsgiidv
lrmkaytygndlgtdireipipeeyldqareyheklvevaadfdenimlkylegeeptee
elvaairkgtidlkitpvflgsalknkgvqllldavvdylps
>d1dar_3 4.10.1.1.1 (477-599) Elongation factor G (EF-G), domain IV {(Thermus thermophilus)}
gkpqvayretitkpvdvegkfirqtggrgqyghvkikveplprgsgfefvnaivggvipk
eyipavqkgieeamqsgpligfpvvdikvtlydgsyhevdssemafkiagsmaikeavqk
gdp
>d1dar_4 4.34.13.1.1 (600-689) Elongation factor G (EF-G), domain V {(Thermus thermophilus)}
vilepimrvevttpeeymgdvigdlnarrgqilgmeprgnaqvirafvplaemfgyatdl
rsktqgrgsfvmffdhyqevpkqvqeklik
>d1dat__ 1.25.1.1.4 (Apo)ferritin {horse (Equus caballus), L chain}
ssqirqnysteveaavnrlvnlylrasytylslgfyfdrddvalegvchffrelaeekre
gaerllkmqnqrggralfqdlqkpsqdewgttpdamkaaivlekslnqalldlhalgsaq
adphlcdfleshfldeevklikkmgdhltniqrlvgsqaglgeylferltlkhd
>d1dbah1 2.1.1.1.15 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
qiqlvqsgpelkkpgetvkisckasgyaftnygvnwvkeapgkelkwmgwiniytgepty
vddfkgrfafsletsastayleinnlknedtatyfctrgdyvnwyfdvwgagttvtvs
>d1dbah2 2.1.1.2.24 (113-228) Immunoglobulin (constant domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
sakttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqs
dlytlsssvtvpssprpsetvtcnvahpasstkvdkkivpr
>d1dbal1 2.1.1.1.15 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
dvvmtqiplslpvnlgdqasiscrssqslihsngntylhwylqkpgqspkllmykvsnrf
ygvpdrfsgsgsgtdftlkisrveaedlgiyfcsqsshvpptfgggtkleik
>d1dbal2 2.1.1.2.24 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1dbbh1 2.1.1.1.15 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
qiqlvqsgpelkkpgetvkisckasgyaftnygvnwvkeapgkelkwmgwiniytgepty
vddfkgrfafsletsastayleinnlknedtatyfctrgdyvnwyfdvwgagttvtvs
>d1dbbh2 2.1.1.2.24 (113-228) Immunoglobulin (constant domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
sakttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqs
dlytlsssvtvpssprpsetvtcnvahpasstkvdkkivpr
>d1dbbl1 2.1.1.1.15 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
dvvmtqiplslpvnlgdqasiscrssqslihsngntylhwylqkpgqspkllmykvsnrf
ygvpdrfsgsgsgtdftlkisrveaedlgiyfcsqsshvpptfgggtkleik
>d1dbbl2 2.1.1.2.24 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1dbjh1 2.1.1.1.15 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
qiqlvqsgpelkkpgetvkisckasgyaftnygvnwvkeapgkelkwmgwiniytgepty
vddfkgrfafsletsastayleinnlknedtatyfctrgdyvnwyfdvwgagttvtvs
>d1dbjh2 2.1.1.2.24 (113-228) Immunoglobulin (constant domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
sakttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqs
dlytlsssvtvpssprpsetvtcnvahpasstkvdkkivpr
>d1dbjl1 2.1.1.1.15 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
dvvmtqiplslpvnlgdqasiscrssqslihsngntylhwylqkpgqspkllmykvsnrf
ygvpdrfsgsgsgtdftlkisrveaedlgiyfcsqsshvpptfgggtkleik
>d1dbjl2 2.1.1.2.24 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1dbkh1 2.1.1.1.15 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
qiqlvqsgpelkkpgetvkisckasgyaftnygvnwvkeapgkelkwmgwiniytgepty
vddfkgrfafsletsastayleinnlknedtatyfctrgdyvnwyfdvwgagttvtvs
>d1dbkh2 2.1.1.2.24 (113-228) Immunoglobulin (constant domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
sakttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqs
dlytlsssvtvpssprpsetvtcnvahpasstkvdkkivpr
>d1dbkl1 2.1.1.1.15 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
dvvmtqiplslpvnlgdqasiscrssqslihsngntylhwylqkpgqspkllmykvsnrf
ygvpdrfsgsgsgtdftlkisrveaedlgiyfcsqsshvpptfgggtkleik
>d1dbkl2 2.1.1.2.24 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1dbmh1 2.1.1.1.15 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
qiqlvqsgpelkkpgetvkisckasgyaftnygvnwvkeapgkelkwmgwiniytgepty
vddfkgrfafsletsastayleinnlknedtatyfctrgdyvnwyfdvwgagttvtvs
>d1dbmh2 2.1.1.2.24 (113-228) Immunoglobulin (constant domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
sakttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqs
dlytlsssvtvpssprpsetvtcnvahpasstkvdkkivpr
>d1dbml1 2.1.1.1.15 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
dvvmtqiplslpvnlgdqasiscrssqslihsngntylhwylqkpgqspkllmykvsnrf
ygvpdrfsgsgsgtdftlkisrveaedlgiyfcsqsshvpptfgggtkleik
>d1dbml2 2.1.1.2.24 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab DB3 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1dbp__ 3.81.1.1.1 D-ribose-binding protein {(Escherichia coli), strain k-12}
kdtialvvstlnnpffvslkdgaqkeadklgynlvvldsqnnpakelanvqdltvrgtki
llinptdsdavdnavkmanqanipvitldrqatkgevvshiasdnvlggkiagdyiakka
gegakvielqgiagtsaarergegfqqavaahkfnvlasqpadfdrikglnvmqnlltah
pdvqavfaqndemalgalralqtagksdvmvvgfdgtpdgekavndgklaatiaqlpdqi
gakgvetadkvlkgekvqakypvdlklvvkq
>d1dbqa_ 3.81.1.1.6 Purine repressor (PurR), C-terminal domain {(Escherichia coli)}
ksigllatsseaayfaeiieavekncfqkgytlilgnawnnlekqraylsmmaqkrvdgl
lvmcseypepllamleeyrhipmvvmdwgeakadftdavidnafeggymagrylierghr
eigvipgplerntgagrlagfmkameeamikvpeswivqgdfepesgyramqqilsqphr
ptavfcggdimamgalcaademglrvpqdvsligydnvrnaryftpalttihqpkdslge
tafnmlldrivnkreepqsievhprlierrsvadgpfrdyrr
>d1dbqb_ 3.81.1.1.6 Purine repressor (PurR), C-terminal domain {(Escherichia coli)}
ksigllatsseaayfaeiieavekncfqkgytlilgnawnnlekqraylsmmaqkrvdgl
lvmcseypepllamleeyrhipmvvmdwgeakadftdavidnafeggymagrylierghr
eigvipgplerntgagrlagfmkameeamikvpeswivqgdfepesgyramqqilsqphr
ptavfcggdimamgalcaademglrvpqdvsligydnvrnaryftpalttihqpkdslge
tafnmlldrivnkreepqsievhprlierrsvadgpfrdyrr
>d1dbra_ 3.49.1.1.3 Hypoxantine-guanine-xanthine PRTase {(Toxoplasma gondii)}
askpiedygkgkgriepmyipdntfynaddflvpphckpyidkillpgglvkdrveklay
dihrtyfgeelhiicilkgsrgffnllidylatiqkysgressvppffehyvrlksyqnd
nstgqltvlsddlsifrdkhvlivedivdtgftltefgerlkavgpksmriatlvekrtd
rsnslkgdfvgfsiedvwivgccydfnemfrdfdhvavlsdaarkkfekv
>d1dbrb_ 3.49.1.1.3 Hypoxantine-guanine-xanthine PRTase {(Toxoplasma gondii)}
askpiedygkgkgriepmyipdntfynaddflvpphckpyidkillpgglvkdrveklay
dihrtyfgeelhiicilkgsrgffnllidylatiqkysgressvppffehyvrlksyqnd
nstgqltvlsddlsifrdkhvlivedivdtgftltefgerlkavgpksmriatlvekrtd
rsnslkgdfvgfsiedvwivgccydfnemfrdfdhvavlsdaarkkfekv
>d1dbrc_ 3.49.1.1.3 Hypoxantine-guanine-xanthine PRTase {(Toxoplasma gondii)}
iedygkgkgriepmyipdntfynaddflvpphckpyidkillpgglvkdrveklaydihr
tyfgeelhiicilkgsrgffnllidylatiqkysgressvppffehyvrlksyqndnstg
qltvlsddlsifrdkhvlivedivdtgftltefgerlkavgpksmriatlvekrtdrsns
lkgdfvgfsiedvwivgccydfnemfrdfdhvavlsdaarkkfekv
>d1dbrd_ 3.49.1.1.3 Hypoxantine-guanine-xanthine PRTase {(Toxoplasma gondii)}
iedygkgkgriepmyipdntfynaddflvpphckpyidkillpgglvkdrveklaydihr
tyfgeelhiicilkgsrgffnllidylatiqkysgressvppffehyvrlksyqndnstg
qltvlsddlsifrdkhvlivedivdtgftltefgerlkavgpksmriatlvekrtdrsns
lkgdfvgfsiedvwivgccydfnemfrdfdhvavlsdaarkkfekv
>d1dbs__ 3.29.1.6.1 Dethiobiotin synthetase {(Escherichia coli)}
skryfvtgtdtevgktvascallqaakaagyrtagykpvasgsektpeglrnsdalalqr
nsslqldyatvnpytfaeptsphiisaqegrpieslvmsaglraleqqadwvlvegaggw
ftplsdtftfadwvtqeqlpvilvvgvklgcinhamltaqviqhagltlagwvandvtpp
gkrhaeymttltrmipapllgeipwlaenpenaatgkyinlall
>d1dbvo1 3.22.1.3.2 (1-148,313-333) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Bacillus stearothermophilus /nca 1503)}
vkvgingfgrigrnvfraalknpdievvavngltdantlahllkydsvhgrldaevsvng
nnlvvngkeiivkaerdpenlawgeigvdivvestgrftkredaakhleagakkviisap
akneditivmgvnqdkydpkahhvisnasXnetgyshrvvdlaayiaskgl
>d1dbvo2 4.42.1.1.2 (149-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Bacillus stearothermophilus /nca 1503)}
cttnclapfakvlheqfgivrgmmttvhsytndqrildashkdlrraraaaesiiptttg
aakavalvlpelkgklngmamrvptpnvsvvdlvaelekevtveevnaalkaaaegelkg
ilayseeplvsrdyngstvsstidalstmvidgkmvkvvswyd
>d1dbvp1 3.22.1.3.2 (1-148,313-333) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Bacillus stearothermophilus /nca 1503)}
vkvgingfgrigrnvfraalknpdievvavngltdantlahllkydsvhgrldaevsvng
nnlvvngkeiivkaerdpenlawgeigvdivvestgrftkredaakhleagakkviisap
akneditivmgvnqdkydpkahhvisnasXnetgyshrvvdlaayiaskgl
>d1dbvp2 4.42.1.1.2 (149-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Bacillus stearothermophilus /nca 1503)}
cttnclapfakvlheqfgivrgmmttvhsytndqrildashkdlrraraaaesiiptttg
aakavalvlpelkgklngmamrvptpnvsvvdlvaelekevtveevnaalkaaaegelkg
ilayseeplvsrdyngstvsstidalstmvidgkmvkvvswyd
>d1dbvq1 3.22.1.3.2 (1-148,313-333) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Bacillus stearothermophilus /nca 1503)}
vkvgingfgrigrnvfraalknpdievvavngltdantlahllkydsvhgrldaevsvng
nnlvvngkeiivkaerdpenlawgeigvdivvestgrftkredaakhleagakkviisap
akneditivmgvnqdkydpkahhvisnasXnetgyshrvvdlaayiaskgl
>d1dbvq2 4.42.1.1.2 (149-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Bacillus stearothermophilus /nca 1503)}
cttnclapfakvlheqfgivrgmmttvhsytndqrildashkdlrraraaaesiiptttg
aakavalvlpelkgklngmamrvptpnvsvvdlvaelekevtveevnaalkaaaegelkg
ilayseeplvsrdyngstvsstidalstmvidgkmvkvvswyd
>d1dbvr1 3.22.1.3.2 (1-148,313-333) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Bacillus stearothermophilus /nca 1503)}
vkvgingfgrigrnvfraalknpdievvavngltdantlahllkydsvhgrldaevsvng
nnlvvngkeiivkaerdpenlawgeigvdivvestgrftkredaakhleagakkviisap
akneditivmgvnqdkydpkahhvisnasXnetgyshrvvdlaayiaskgl
>d1dbvr2 4.42.1.1.2 (149-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Bacillus stearothermophilus /nca 1503)}
cttnclapfakvlheqfgivrgmmttvhsytndqrildashkdlrraraaaesiiptttg
aakavalvlpelkgklngmamrvptpnvsvvdlvaelekevtveevnaalkaaaegelkg
ilayseeplvsrdyngstvsstidalstmvidgkmvkvvswyd
>d1dca__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslctppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1dcb__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslctppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1dcc__ 1.72.1.1.3 Cytochrome c peroxidase {baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpfgaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1dcha_ 4.39.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dchb_ 4.39.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dchc_ 4.39.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dchd_ 4.39.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dche_ 4.39.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dchf_ 4.39.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dchg_ 4.39.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dchh_ 4.39.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcla1 2.1.1.1.117 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psaltqppsasgslgqsvtisctgtssnvggynyvswyqqhagkapkviiyevnkrpsgv
pdrfsgsksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1dcla2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1dclb1 2.1.1.1.117 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psaltqppsasgslgqsvtisctgtssnvggynyvswyqqhagkapkviiyevnkrpsgv
pdrfsgsksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1dclb2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1dcoa_ 4.39.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcob_ 4.39.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcoc_ 4.39.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcod_ 4.39.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcoe_ 4.39.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcof_ 4.39.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcog_ 4.39.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcoh_ 4.39.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcpa_ 4.39.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcpb_ 4.39.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcpc_ 4.39.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcpd_ 4.39.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcpe_ 4.39.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcpf_ 4.39.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcpg_ 4.39.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcph_ 4.39.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1dcta_ 3.53.1.5.3 DNA methylase HaeIII, coenzyme-binding domain {(Haemophilus aegyptius )}
mnlislfsgaggldlgfqkagfriicaneydksiwktyesnhsaklikgdiskissdefp
kcdgiiggppcqswseggslrgiddprgklfyeyirilkqkkpifflaenvkgmmaqrhn
kavqefiqefdnagydvhiillnandygvaqdrkrvfyigfrkelninylppiphlikpt
fkdviwdlkdnpipaldknktngnkciypnheyfigsystifmsrnrvrqwnepaftvqa
sgrqcqlhpqapvmlkvsknlnkfvegkehlyrrltvrecarvqgfpddfifhyeslndg
ykmignavpvnlayeiaktiksal
>d1dctb_ 3.53.1.5.3 DNA methylase HaeIII, coenzyme-binding domain {(Haemophilus aegyptius )}
mnlislfsgaggldlgfqkagfriicaneydksiwktyesnhsaklikgdiskissdefp
kcdgiiggppcqswseggslrgiddprgklfyeyirilkqkkpifflaenvkgmmaqrhn
kavqefiqefdnagydvhiillnandygvaqdrkrvfyigfrkelninylppiphlikpt
fkdviwdlkdnpipaldknktngnkciypnheyfigsystifmsrnrvrqwnepaftvqa
sgrqcqlhpqapvmlkvsknlnkfvegkehlyrrltvrecarvqgfpddfifhyeslndg
ykmignavpvnlayeiaktiksal
>d1ddf__ 1.67.1.1.2 Fas {Human (Homo sapiens)}
metvainlsdvdlskyittiagvmtlsqvkgfvrkngvneakideikndnvqdtaeqkvq
llrnwhqlhgkkeaydtlikdlkkanlctlaekiqtiilkditsdsensnfrneiqslvl
ehhhhhh
>d1ddoa1 3.21.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1ddoa2 4.12.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1ddob1 3.21.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1ddob2 4.12.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1ddoc1 3.21.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1ddoc2 4.12.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1ddod1 3.21.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1ddod2 4.12.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1ddoe1 3.21.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1ddoe2 4.12.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1ddof1 3.21.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1ddof2 4.12.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1ddog1 3.21.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1ddog2 4.12.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1ddoh1 3.21.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1ddoh2 4.12.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1ddra_ 3.60.1.1.1 Dihydrofolate reductase, prokaryotic type {(Escherichia coli)}
misliaalavdrvigmenampwnlpadlawfkrntlnkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1ddrb_ 3.60.1.1.1 Dihydrofolate reductase, prokaryotic type {(Escherichia coli)}
misliaalavdrvigmenampwnlpadlawfkrntlnkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1ddsa_ 3.60.1.1.1 Dihydrofolate reductase, prokaryotic type {(Escherichia coli)}
misliaalavdrvigmenampwnlpadlawfkrntlnkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1ddsb_ 3.60.1.1.1 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 4.103.1.1.3 (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_ 4.67.1.1.1 Thymidylate synthase {(Escherichia coli)}
mkqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihell
wflqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlk
ndpdsrriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfnias
yallvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesif
dyrfedfeiegydphpgikapvai
>d1ddub_ 4.67.1.1.1 Thymidylate synthase {(Escherichia coli)}
mkqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihell
wflqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlk
ndpdsrriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfnias
yallvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesif
dyrfedfeiegydphpgikapvai
>d1deaa_ 3.27.1.1.1 Glucosamine 6-phosphate deaminase {(Escherichia coli)}
mrliplttaeqvgkwaarhivnrinafkptadrpfvlglptggtpmttykalvemhkagq
vsfkhvvtfnmdeyvglpkehpesyysfmhrnffdhvdipaeninllngnapdidaecrq
yeekirsygkihlfmggvgndghiafnepasslasrtriktlthdtrvansrffdndvnq
vpkyaltvgvgtlldaeevmilvlgsqkalalqaavegcvnhmwtisclqlhpkaimvcd
epstmelkvktlryfneleaenikgl
>d1deab_ 3.27.1.1.1 Glucosamine 6-phosphate deaminase {(Escherichia coli)}
mrliplttaeqvgkwaarhivnrinafkptadrpfvlglptggtpmttykalvemhkagq
vsfkhvvtfnmdeyvglpkehpesyysfmhrnffdhvdipaeninllngnapdidaecrq
yeekirsygkihlfmggvgndghiafnepasslasrtriktlthdtrvansrffdndvnq
vpkyaltvgvgtlldaeevmilvlgsqkalalqaavegcvnhmwtisclqlhpkaimvcd
epstmelkvktlryfneleaenikgl
>d1dec__ 7.3.13.2.2 Decorsin {North american leech (Macrobdella decora)}
aprlpqcqgddqekclcnkdecppgqcrfprgdadpyce
>d1def__ 4.104.1.1.1 Peptide deformylase catalytic core {(Escherichia coli)}
svlqvlhipderlrkvakpveevnaeiqrivddmfetmyaeegiglaatqvdihqriivi
dvsenrderlvlinpelleksgetgieegclsipeqralvpraekvkiraldrdgkpfel
eadgllaiciqhemdhlvgklfmdyls
>d1deg__ 1.37.1.5.8 Calmodulin {bovine (Bos taurus)}
teeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngtid
fpefltmmarkmkdtdseeireafrvfdkdgngyisaaelrhvmtnlgekltdeevdemi
reanidgdgqvnyeefvqmmta
>d1deha1 2.25.1.2.2 (1-174,325-374) Alcohol dehydrogenase {human (Homo sapiens)}
stagkvikckaavlwevkkpfsiedvevappkayevrikmvavgicrtddhvvsgnlvtp
lpvilgheaagivesvgegvttvkpgdkviplftpqcgkcrvcknpesnyclkndlgnpr
gtlqdgtrrftcrgkpihhflgtstfsqytvvdenavakidaasplekvcligcXkegip
klvadfmakkfsldalithvlpfekinegfdllhsgksirtvltf
>d1deha2 3.22.1.1.2 (175-324) Alcohol dehydrogenase {human (Homo sapiens), different isozymes}
gfstgygsavnvakvtpgstcavfglggvglsavmgckaagaariiavdinkdkfakake
lgatecinpqdykkpiqevlkemtdggvdfsfevigrldtmmasllccheacgtsvivgv
ppasqnlsinpmllltgrtwkgavyggfks
>d1dehb1 2.25.1.2.2 (1-174,325-374) Alcohol dehydrogenase {human (Homo sapiens)}
stagkvikckaavlwevkkpfsiedvevappkayevrikmvavgicrtddhvvsgnlvtp
lpvilgheaagivesvgegvttvkpgdkviplftpqcgkcrvcknpesnyclkndlgnpr
gtlqdgtrrftcrgkpihhflgtstfsqytvvdenavakidaasplekvcligcXkegip
klvadfmakkfsldalithvlpfekinegfdllhsgksirtvltf
>d1dehb2 3.22.1.1.2 (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_ 3.29.1.1.3 Deoxynucleoside monophosphate kinase {(Bacteriophage t4)}
mkliflsgvkrsgkdttadfimsnysavkyqlagpikdalayawgvfaantdypxltrke
fegidydretnlnltklevitimeqafcylngkspikgvfvfddegkesvnfvafnkitd
vinniedqwsvrrlmqalgtdlivnnfdrmywvklfaldyldkfnsgydyyivpdtrqdh
emdaaramgatvihvvrpgqksndthiteaglpirdgdlvitndgsleelfskikntlkv
l
>d1dekb_ 3.29.1.1.3 Deoxynucleoside monophosphate kinase {(Bacteriophage t4)}
mkliflsgvkrsgkdttadfimsnysavkyqlagpikdalayawgvfaantdypxltrke
fegidydretnlnltklevitimeqafcylngkspikgvfvfddegkesvnfvafnkitd
vinniedqwsvrrlmqalgtdlivnnfdrmywvklfaldyldkfnsgydyyivpdtrqdh
emdaaramgatvihvvrpgqksndthiteaglpirdgdlvitndgsleelfskikntlkv
l
>d1dela_ 3.29.1.1.3 Deoxynucleoside monophosphate kinase {(Bacteriophage t4)}
mkliflsgvkrsgkdttadfimsnysavkyqlagpikdalayawgvfaantdypcltrke
fegidydretnlnltklevitimeqafcylngkspikgvfvfddegkesvnfvafnkitd
vinniedqwsvrrlmqalgtdlivnnfdrmywvklfaldyldkfnsgydyyivpdtrqdh
emdaaramgatvihvvrpgqksndthiteaglpirdgdlvitndgsleelfskikntlkv
l
>d1delb_ 3.29.1.1.3 Deoxynucleoside monophosphate kinase {(Bacteriophage t4)}
mkliflsgvkrsgkdttadfimsnysavkyqlagpikdalayawgvfaantdypcltrke
fegidydretnlnltklevitimeqafcylngkspikgvfvfddegkesvnfvafnkitd
vinniedqwsvrrlmqalgtdlivnnfdrmywvklfaldyldkfnsgydyyivpdtrqdh
emdaaramgatvihvvrpgqksndthiteaglpirdgdlvitndgsleelfskikntlkv
l
>d1dem__ 7.7.1.1.9 Dendrotoxin I {african elapid snake (Dendroaspis polylepis polylepis)}
qplrklcilhrnpgrcyqkipafyynqkkkqcegftwsgcggnsnrfktieecrrtcirk
>d1den__ 7.7.1.1.9 Dendrotoxin I {african elapid snake (Dendroaspis polylepis polylepis)}
qplrklcilhrnpgrcyqkipafyynqkkkqcegftwsgcggnsnrfktieecrrtcirk
>d1dera1 1.100.1.1.1 (2-136,410-526) GroEL, the ATPase domain {(Escherichia coli)}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlpk
>d1dera2 3.5.4.1.1 (191-366) GroEL {(Escherichia coli)}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1dera3 4.33.1.1.1 (137-190,367-409) The intermediate domain of GroEL {(Escherichia coli)}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1derb1 1.100.1.1.1 (2-136,410-526) GroEL, the ATPase domain {(Escherichia coli)}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlpk
>d1derb2 3.5.4.1.1 (191-366) GroEL {(Escherichia coli)}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1derb3 4.33.1.1.1 (137-190,367-409) The intermediate domain of GroEL {(Escherichia coli)}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1derc1 1.100.1.1.1 (2-136,410-526) GroEL, the ATPase domain {(Escherichia coli)}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlpk
>d1derc2 3.5.4.1.1 (191-366) GroEL {(Escherichia coli)}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1derc3 4.33.1.1.1 (137-190,367-409) The intermediate domain of GroEL {(Escherichia coli)}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1derd1 1.100.1.1.1 (2-136,410-526) GroEL, the ATPase domain {(Escherichia coli)}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlpk
>d1derd2 3.5.4.1.1 (191-366) GroEL {(Escherichia coli)}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1derd3 4.33.1.1.1 (137-190,367-409) The intermediate domain of GroEL {(Escherichia coli)}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1dere1 1.100.1.1.1 (2-136,410-526) GroEL, the ATPase domain {(Escherichia coli)}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlpk
>d1dere2 3.5.4.1.1 (191-366) GroEL {(Escherichia coli)}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1dere3 4.33.1.1.1 (137-190,367-409) The intermediate domain of GroEL {(Escherichia coli)}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1derf1 1.100.1.1.1 (2-136,410-526) GroEL, the ATPase domain {(Escherichia coli)}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlpk
>d1derf2 3.5.4.1.1 (191-366) GroEL {(Escherichia coli)}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1derf3 4.33.1.1.1 (137-190,367-409) The intermediate domain of GroEL {(Escherichia coli)}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1derg1 1.100.1.1.1 (2-136,410-526) GroEL, the ATPase domain {(Escherichia coli)}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlpk
>d1derg2 3.5.4.1.1 (191-366) GroEL {(Escherichia coli)}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1derg3 4.33.1.1.1 (137-190,367-409) The intermediate domain of GroEL {(Escherichia coli)}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1derh1 1.100.1.1.1 (2-136,410-526) GroEL, the ATPase domain {(Escherichia coli)}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlpk
>d1derh2 3.5.4.1.1 (191-366) GroEL {(Escherichia coli)}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1derh3 4.33.1.1.1 (137-190,367-409) The intermediate domain of GroEL {(Escherichia coli)}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1deri1 1.100.1.1.1 (2-136,410-526) GroEL, the ATPase domain {(Escherichia coli)}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlpk
>d1deri2 3.5.4.1.1 (191-366) GroEL {(Escherichia coli)}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1deri3 4.33.1.1.1 (137-190,367-409) The intermediate domain of GroEL {(Escherichia coli)}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1derj1 1.100.1.1.1 (2-136,410-526) GroEL, the ATPase domain {(Escherichia coli)}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlpk
>d1derj2 3.5.4.1.1 (191-366) GroEL {(Escherichia coli)}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1derj3 4.33.1.1.1 (137-190,367-409) The intermediate domain of GroEL {(Escherichia coli)}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1derk1 1.100.1.1.1 (2-136,410-526) GroEL, the ATPase domain {(Escherichia coli)}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlpk
>d1derk2 3.5.4.1.1 (191-366) GroEL {(Escherichia coli)}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1derk3 4.33.1.1.1 (137-190,367-409) The intermediate domain of GroEL {(Escherichia coli)}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1derl1 1.100.1.1.1 (2-136,410-526) GroEL, the ATPase domain {(Escherichia coli)}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlpk
>d1derl2 3.5.4.1.1 (191-366) GroEL {(Escherichia coli)}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1derl3 4.33.1.1.1 (137-190,367-409) The intermediate domain of GroEL {(Escherichia coli)}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1derm1 1.100.1.1.1 (2-136,410-526) GroEL, the ATPase domain {(Escherichia coli)}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlpk
>d1derm2 3.5.4.1.1 (191-366) GroEL {(Escherichia coli)}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1derm3 4.33.1.1.1 (137-190,367-409) The intermediate domain of GroEL {(Escherichia coli)}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1dern1 1.100.1.1.1 (2-136,410-526) GroEL, the ATPase domain {(Escherichia coli)}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlpk
>d1dern2 3.5.4.1.1 (191-366) GroEL {(Escherichia coli)}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1dern3 4.33.1.1.1 (137-190,367-409) The intermediate domain of GroEL {(Escherichia coli)}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1det__ 4.1.1.1.3 RNase T1 {(Aspergillus oryzae)}
acdytcgsncysssdvstaqaagyqlhedgetvgsnsyphkynnyegfdfsvsspyyewp
ilssgdvysggspgadrvvfnennqlagvithtgasgnnfvect
>d1dfbh1 2.1.1.1.16 (1-126) Immunoglobulin (variable domains of L and H chains) {Fab 3D6 (human), kappa L chain}
evqlvesggglvqpgrslrlscaasgftfndyamhwvrqapgkglewvsgiswdsssigy
adsvkgrftisrdnaknslylqmnslraedmalyycvkgrdyydsggyftvafdiwgqgt
mvtvss
>d1dfbh2 2.1.1.2.25 (127-229) Immunoglobulin (constant domains of L and H chains) {Fab 3D6 (human), kappa L chain}
astkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkvepksc
>d1dfbl1 2.1.1.1.16 (1-106) Immunoglobulin (variable domains of L and H chains) {Fab 3D6 (human), kappa L chain}
diqmtqspstlsasvgdrvtitcrasqsisrwlawyqqkpgkvpklliykasslesgvps
rfsgsgsgteftltisslqpddfatyycqqynsysfgpgtkvdikr
>d1dfbl2 2.1.1.2.25 (107-212) Immunoglobulin (constant domains of L and H chains) {Fab 3D6 (human), kappa L chain}
tvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqds
kdstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1dfga_ 3.22.1.2.11 Enoyl-ACP reductase {(Escherichia coli)}
gflsgkrilvtgvasklsiaygiaqamhregaelaftyqndklkgrveefaaqlgsdivl
qcdvaedasidtmfaelgkvwpkfdgfvhsigfapgdqldgdyvnavtregfkiahdiss
ysfvamakacrsmlnpgsalltlsylgaeraipnynvmglakasleanvrymanamgpeg
vrvnaisagpirtlaasgikdfrkmlahceavtpirrtvtiedvgnsaaflcsdlsagis
gevvhvdggfsiaamne
>d1dfgb_ 3.22.1.2.11 Enoyl-ACP reductase {(Escherichia coli)}
gflsgkrilvtgvasklsiaygiaqamhregaelaftyqndklkgrveefaaqlgsdivl
qcdvaedasidtmfaelgkvwpkfdgfvhsigfapgdqldgdyvnavtregfkiahdiss
ysfvamakacrsmlnpgsalltlsylgaeraipnynvmglakasleanvrymanamgpeg
vrvnaisagpirtlaasgikdfrkmlahceavtpirrtvtiedvgnsaaflcsdlsagis
gevvhvdggfsiaamne
>d1dfha_ 3.22.1.2.11 Enoyl-ACP reductase {(Escherichia coli)}
gflsgkrilvtgvasklsiaygiaqamhregaelaftyqndklkgrveefaaqlgsdivl
qcdvaedasidtmfaelgkvwpkfdgfvhsigfapgdqldgdyvnavtregfkiahdiss
ysfvamakacrsmlnpgsalltlsylgaeraipnynvmglakasleanvrymanamgpeg
vrvnaisagpirtlaasgikdfrkmlahceavtpirrtvtiedvgnsaaflcsdlsagis
gevvhvdggfsiaamne
>d1dfhb_ 3.22.1.2.11 Enoyl-ACP reductase {(Escherichia coli)}
gflsgkrilvtgvasklsiaygiaqamhregaelaftyqndklkgrveefaaqlgsdivl
qcdvaedasidtmfaelgkvwpkfdgfvhsigfapgdqldgdyvnavtregfkiahdiss
ysfvamakacrsmlnpgsalltlsylgaeraipnynvmglakasleanvrymanamgpeg
vrvnaisagpirtlaasgikdfrkmlahceavtpirrtvtiedvgnsaaflcsdlsagis
gevvhvdggfsiaamne
>d1dfia_ 3.22.1.2.11 Enoyl-ACP reductase {(Escherichia coli)}
gflsgkrilvtgvasklsiaygiaqamhregaelaftyqndklkgrveefaaqlgsdivl
qcdvaedasidtmfaelgkvwpkfdgfvhsigfapgdqldgdyvnavtregfkiahdiss
ysfvamakacrsmlnpgsalltlsylgaeraipnynvmglakasleanvrymanamgpeg
vrvnaisagpirtlaasgikdfrkmlahceavtpirrtvtiedvgnsaaflcsdlsagis
gevvhvdggfsiaamne
>d1dfib_ 3.22.1.2.11 Enoyl-ACP reductase {(Escherichia coli)}
gflsgkrilvtgvasklsiaygiaqamhregaelaftyqndklkgrveefaaqlgsdivl
qcdvaedasidtmfaelgkvwpkfdgfvhsigfapgdqldgdyvnavtregfkiahdiss
ysfvamakacrsmlnpgsalltlsylgaeraipnynvmglakasleanvrymanamgpeg
vrvnaisagpirtlaasgikdfrkmlahceavtpirrtvtiedvgnsaaflcsdlsagis
gevvhvdggfsiaamne
>d1dfic_ 3.22.1.2.11 Enoyl-ACP reductase {(Escherichia coli)}
gflsgkrilvtgvasklsiaygiaqamhregaelaftyqndklkgrveefaaqlgsdivl
qcdvaedasidtmfaelgkvwpkfdgfvhsigfapgdqldgdyvnavtregfkiahdiss
ysfvamakacrsmlnpgsalltlsylgaeraipnynvmglakasleanvrymanamgpeg
vrvnaisagpirtlaasgikdfrkmlahceavtpirrtvtiedvgnsaaflcsdlsagis
gevvhvdggfsiaamne
>d1dfid_ 3.22.1.2.11 Enoyl-ACP reductase {(Escherichia coli)}
gflsgkrilvtgvasklsiaygiaqamhregaelaftyqndklkgrveefaaqlgsdivl
qcdvaedasidtmfaelgkvwpkfdgfvhsigfapgdqldgdyvnavtregfkiahdiss
ysfvamakacrsmlnpgsalltlsylgaeraipnynvmglakasleanvrymanamgpeg
vrvnaisagpirtlaasgikdfrkmlahceavtpirrtvtiedvgnsaaflcsdlsagis
gevvhvdggfsiaamne
>d1dfje_ 4.4.1.1.1 Ribonuclease A (also ribonuclease B, S) {bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1dfji_ 3.7.1.1.1 Ribonuclease inhibitor {pig (Sus scrofa)}
mnldihceqlsdarwtellpllqqyevvrlddcglteehckdigsalranpsltelclrt
nelgdagvhlvlqglqsptckiqklslqncslteagcgvlpstlrslptlrelhlsdnpl
gdaglrllceglldpqchleklqleycrltaasceplasvlratralkeltvsnndigea
garvlgqgladsacqletlrlencgltpanckdlcgivasqaslreldlgsnglgdagia
elcpgllspasrlktlwlwecditasgcrdlcrvlqaketlkelslagnklgdegarllc
esllqpgcqleslwvkscsltaaccqhvslmltqnkhllelqlssnklgdsgiqelcqal
sqpgttlrvlclgdcevtnsgcsslaslllanrslreldlsnncvgdpgvlqllgsleqp
gcaleqlvlydtywteevedrlqalegskpglrvis
>d1dfna_ 7.8.1.1.1 Defensin HNP-3 {human (Homo sapiens)}
dcycripaciagerrygtciyqgrlwafcc
>d1dfnb_ 7.8.1.1.1 Defensin HNP-3 {human (Homo sapiens)}
dcycripaciagerrygtciyqgrlwafcc
>d1dfpa_ 2.35.1.2.23 Factor D {Human (Homo sapiens)}
ilggreaeaharpymasvqlngahlcggvlvaeqwvlsaahcledaadgkvqvllgahsl
sqpepskrlydvlravphpdsqpdtidhdllllqlsekatlgpavrplpwqrvdrdvapg
tlcdvagwgivnhagrrpdslqhvllpvldratcnrrthhdgaiterlmcaesnrrdsck
gdsggplvcggvlegvvtsgsrvcgnrkkpgiytrvasyaawidsvla
>d1dfpb_ 2.35.1.2.23 Factor D {Human (Homo sapiens)}
ilggreaeaharpymasvqlngahlcggvlvaeqwvlsaahcledaadgkvqvllgahsl
sqpepskrlydvlravphpdsqpdtidhdllllqlsekatlgpavrplpwqrvdrdvapg
tlcdvagwgivnhagrrpdslqhvllpvldratcnrrthhdgaiterlmcaesnrrdsck
gdsggplvcggvlegvvtsgsrvcgnrkkpgiytrvasyaawidsvla
>d1dgca_ 1.105.2.1.1 GCN4 {Yeast (Saccharomyces cerevisiae)}
paalkrarnteaarrsrarklqrmkqledkveellsknyhlenevarlkklvger
>d1dgd__ 3.54.1.3.1 Dialkylglycine decarboxylase {(Pseudomonas cepacia)}
lnddatfwrnarhhlvryggtfepmiierakgsfvydadgraildftsgqmsavlghchp
eivsvigeyagkldhlfsgmlsrpvvdlatrlanitppgldralllstgaesneaairma
klvtgkyeivgfaqswhgmtgaaasatysagrkgvgpaavgsfaipapftyrprfernga
ydylaeldyafdlidrqssgnlaafiaepilssggiielpdgymaalkrkceargmllil
deaqtgvgrtgtmfacqrdgvtpdiltlsktlgaglplaaivtsaaieerahelgylfyt
thvsdplpaavglrvldvvqrdglvaranvmgdrlrrglldlmerfdcigdvrgrglllg
veivkdrrtkepadglgakitrecmnlglsmnivqlpgmggvfriappltvsedeidlgl
sllgqaieral
>d1dge__ 3.54.1.3.1 Dialkylglycine decarboxylase {(Pseudomonas cepacia)}
lnddatfwrnarhhlvryggtfepmiierakgsfvydadgraildftsgqmsavlghchp
eivsvigeyagkldhlfsgmlsrpvvdlatrlanitppgldralllstgaesneaairma
klvtgkyeivgfaqswhgmtgaaasatysagrkgvgpaavgsfaipapftyrprfernga
ydylaeldyafdlidrqssgnlaafiaepilssggiielpdgymaalkrkceargmllil
deaqtgvgrtgtmfacqrdgvtpdiltlsktlgaglplaaivtsaaieerahelgylfyt
thvsdplpaavglrvldvvqrdglvaranvmgdrlrrglldlmerfdcigdvrgrglllg
veivkdrrtkepadglgakitrecmnlglsmnivqlpgmggvfriappltvsedeidlgl
sllgqaieral
>d1dhfa_ 3.60.1.1.5 Dihydrofolate reductases, eukaryotic type {human (Homo sapiens)}
lncivavsqnmgigkngdlpwpplrnefryfqrmtttssvegkqnlvimgkktwfsipek
nrplkgrinlvlsrelkeppqgahflsrslddalklteqpelankvdmvwivggssvyke
amnhpghlklfvtrimqdfesdtffpeidlekykllpeypgvlsdvqeekgikykfevye
kn
>d1dhfb_ 3.60.1.1.5 Dihydrofolate reductases, eukaryotic type {human (Homo sapiens)}
lncivavsqnmgigkngdlpwpplrnefryfqrmtttssvegkqnlvimgkktwfsipek
nrplkgrinlvlsrelkeppqgahflsrslddalklteqpelankvdmvwivggssvyke
amnhpghlklfvtrimqdfesdtffpeidlekykllpeypgvlsdvqeekgikykfevye
kn
>d1dhia_ 3.60.1.1.1 Dihydrofolate reductase, prokaryotic type {(Escherichia coli)}
misliaalavdrvigmenampwnlpaslawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1dhib_ 3.60.1.1.1 Dihydrofolate reductase, prokaryotic type {(Escherichia coli)}
misliaalavdrvigmenampwnlpaslawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1dhja_ 3.60.1.1.1 Dihydrofolate reductase, prokaryotic type {(Escherichia coli)}
misliaalavdrvigmenampwnlpaslawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvssefhdadaqnshsycfeilerr
>d1dhjb_ 3.60.1.1.1 Dihydrofolate reductase, prokaryotic type {(Escherichia coli)}
misliaalavdrvigmenampwnlpaslawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvssefhdadaqnshsycfeilerr
>d1dhka1 2.53.1.1.6 (404-496) Mammalian alpha-amylase {porcine (Sus scrofa)}
qpfanwwdngsnqvafgrgnrgfivfnnddwqlsstlqtglpggtycdvisgdkvgnsct
gikvyvssdgtaqfsisnsaedpfiaihaeskl
>d1dhka2 3.1.1.1.6 (2-403) Mammalian alpha-amylase {porcine (Sus scrofa)}
yapqtqsgrtsivhlfewrwvdialecerylgpkgfggvqvsppnenvvvtnpsrpwwer
yqpvsyklctrsgnenefrdmvtrcnnvgvriyvdavinhmcgsgaaagtgttcgsycnp
gsrefpavpysawdfndgkcktasggiesyndpyqvrdcqlvglldlalekdyvrsmiad
ylnklidigvagfridaskhmwpgdikavldklhnlntnwfpagsrpfifqevidlggea
iqsseyfgngrvtefkygaklgtvvrkwsgekmsylknwgegwgfmpsdralvfvdnhdn
qrghgaggasiltfwdarlykvavgfmlahpygftrvmssyrwarnfvngedvndwigpp
nnngvikevtinadttcgndwvcehrwreirnmvwfrnvvdg
>d1dhkb_ 2.21.1.1.12 Phytohemagglutinin-L, PHA-L, also arcelin {Kidney bean (Phaseolus vulgaris)}
atetsfiidafnktnlilqgdatvssngnlqlsynsydsmsrafysapiqirdsttgnva
sfdtnftmnirthrqansavgldfvlvpvqpeskgdtvtvefdtflsrisidvnnndiks
vpwdvhdydgqnaevritynsstkvfsvslsnpstgksnnvsttvelekevydwvsvgfs
atsgayqwsyethdvlswsfsskf
>d1dhma_ 4.34.9.1.2 Papillomavirus-1 E2 protein {(HUMAN PAPILLOMAVIRUS-31)}
mattpiihlkgdanilkclryrlskykqlyeqvsstwhwtctdgkhknaivtltyistsq
rddflntvkipntvsvstgymti
>d1dhmb_ 4.34.9.1.2 Papillomavirus-1 E2 protein {(HUMAN PAPILLOMAVIRUS-31)}
mattpiihlkgdanilkclryrlskykqlyeqvsstwhwtctdgkhknaivtltyistsq
rddflntvkipntvsvstgymti
>d1dhpa_ 3.1.3.1.2 Dihydrodipicolinate synthase {(Escherichia coli)}
mftgsivaivtpmdekgnvcraslkklidyhvasgtsaivsvgttgesatlnhdehadvv
mmtldladgripviagtganataeaisltqrfndsgivgcltvtpyynrpsqeglyqhfk
aiaehtdlpqilynvpsrtgcdllpetvgrlakvkniigikeatgnltrvnqikelvsdd
fvllsgddasaldfmqlgghgvisvtanvaardmaqmcklaaeghfaearvinqrlmplh
nklfvepnpipvkwackelglvatdtlrlpmtpitdsgretvraalkhagll
>d1dhpb_ 3.1.3.1.2 Dihydrodipicolinate synthase {(Escherichia coli)}
mftgsivaivtpmdekgnvcraslkklidyhvasgtsaivsvgttgesatlnhdehadvv
mmtldladgripviagtganataeaisltqrfndsgivgcltvtpyynrpsqeglyqhfk
aiaehtdlpqilynvpsrtgcdllpetvgrlakvkniigikeatgnltrvnqikelvsdd
fvllsgddasaldfmqlgghgvisvtanvaardmaqmcklaaeghfaearvinqrlmplh
nklfvepnpipvkwackelglvatdtlrlpmtpitdsgretvraalkhagll
>d1dhr__ 3.22.1.2.7 Dihydropteridin reductase {rat (Rattus norvegicus)}
earrvlvyggrgalgsrcvqafrarnwwvasidvveneeasasvivkmtdsfteqadqvt
aevgkllgdqkvdailcvaggwaggnakskslfkncdlmwkqsiwtstisshlatkhlke
gglltlagakaaldgtpgmigygmakgavhqlcqslagknsgmpsgaaaiavlpvtldtp
mnrksmpeadfsswtpleflvetfhdwitgnkrpnsgsliqvvttdgkteltpayf
>d1dhs__ 3.24.1.1.1 Deoxyhypusine synthase, DHS {Human (Homo sapiens)}
apagalaavlkhsstlppestqvrgydfnrgvnyralleafgttgfqatnfgravqqvna
miekklepltsctiflgytsnlissgiretirylvqhnmvdvlvttaggveedlikclap
tylgefslrgkelrenginrignllvpnenyckfedwlmpildqmvmeqntegvkwtpsk
miarlgkeinnpesvyywaqknhipvfspaltdgslgdmiffhsyknpglvldivedlrl
intqaifakctgmiilgggvvkhhiananlmrngadyavyintaqefdgsdsgarpdeav
swgkirvdaqpvkvyadaslvfpllvaetfaqkmdafmhekned
>d1dhx__ 2.8.1.4.16 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 4.20.1.3.1 (1-132) 2,3-Dihydroxybiphenyl dioxygenase (DHDB, BPHC enzyme) {(Pseudomonas sp.)}
sierlgylgfavkdvpawdhfltksvglmaagsagdaalyradqrawriavqpgelddla
yaglevddaaalermadklrqagvaftrgdealmqqrkvmgllclqdpfglpleiyygpa
eifhepflpsap
>d1dhy_2 4.20.1.3.1 (133-288) 2,3-Dihydroxybiphenyl dioxygenase (DHDB, BPHC enzyme) {(Pseudomonas sp.)}
vsgfvtgdqgighfvrcvpdtakamafytevlgfvlsdiidiqmgpetsvpahflhcngr
hhtialaafpipkrihhfmlqantiddvgyafdrldaagritsllgrhtndqtlsfyadt
pspmievefgwgprtvdsswtvarhsrtamwghksv
>d1dida_ 3.1.12.1.5 D-xylose isomerase {(Arthrobacter strain b3728)}
vqptpadhftfglwtvgwtgadpfgvatrknldpveavhklaelgaygitfhdndlipfd
ateaerekilgdfnqalkdtglkvpmvttnlfshpvfkdggftsndrsirrfalakvlhn
idlaaemgaetfvmwggregseydgskdlaaaldrmregvdtaagyikdkgynlrialep
kpneprgdiflptvghglafieqlehgdivglnpetgheqmaglnfthgiaqalwaeklf
hidlngqrgikydqdlvfghgdltsafftvdllengfpnggpkytgprhfdykpsrtdgy
dgvwdsakanmsmylllkeralafradpevqeamktsgvfelgettlnagesaadlmnds
asfagfdaeaaaernfafirlnqlaiehllgsr
>d1didb_ 3.1.12.1.5 D-xylose isomerase {(Arthrobacter strain b3728)}
vqptpadhftfglwtvgwtgadpfgvatrknldpveavhklaelgaygitfhdndlipfd
ateaerekilgdfnqalkdtglkvpmvttnlfshpvfkdggftsndrsirrfalakvlhn
idlaaemgaetfvmwggregseydgskdlaaaldrmregvdtaagyikdkgynlrialep
kpneprgdiflptvghglafieqlehgdivglnpetgheqmaglnfthgiaqalwaeklf
hidlngqrgikydqdlvfghgdltsafftvdllengfpnggpkytgprhfdykpsrtdgy
dgvwdsakanmsmylllkeralafradpevqeamktsgvfelgettlnagesaadlmnds
asfagfdaeaaaernfafirlnqlaiehllgsr
>d1diea_ 3.1.12.1.5 D-xylose isomerase {(Arthrobacter strain b3728)}
vqptpadhftfglwtvgwtgadpfgvatrknldpveavhklaelgaygitfhdndlipfd
ateaerekilgdfnqalkdtglkvpmvttnlfshpvfkdggftsndrsirrfalakvlhn
idlaaemgaetfvmwggregseydgskdlaaaldrmregvdtaagyikdkgynlrialep
kpneprgdiflptvghglafieqlehgdivglnpetgheqmaglnfthgiaqalwaeklf
hidlngqrgikydqdlvfghgdltsafftvdllengfpnggpkytgprhfdykpsrtdgy
dgvwdsakanmsmylllkeralafradpevqeamktsgvfelgettlnagesaadlmnds
asfagfdaeaaaernfafirlnqlaiehllgsr
>d1dieb_ 3.1.12.1.5 D-xylose isomerase {(Arthrobacter strain b3728)}
vqptpadhftfglwtvgwtgadpfgvatrknldpveavhklaelgaygitfhdndlipfd
ateaerekilgdfnqalkdtglkvpmvttnlfshpvfkdggftsndrsirrfalakvlhn
idlaaemgaetfvmwggregseydgskdlaaaldrmregvdtaagyikdkgynlrialep
kpneprgdiflptvghglafieqlehgdivglnpetgheqmaglnfthgiaqalwaeklf
hidlngqrgikydqdlvfghgdltsafftvdllengfpnggpkytgprhfdykpsrtdgy
dgvwdsakanmsmylllkeralafradpevqeamktsgvfelgettlnagesaadlmnds
asfagfdaeaaaernfafirlnqlaiehllgsr
>d1difa_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1difb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1dih_1 3.22.1.3.10 (2-130,241-273) Dihydrodipicolinate reductase {(Escherichia coli)}
hdanirvaiagaggrmgrqliqaalalegvqlgaaleregssllgsdagelagagktgvt
vqssldavkddfdvfidftrpegtlnhlafcrqhgkgmvigttgfdeagkqairdaaadi
aivfaanfsXmtfangavrsalwlsgkesglfdmrdvldlnnl
>d1dih_2 4.42.1.2.2 (131-240) Dihydrodipicolinate reductase {(Escherichia coli)}
vgvnvmlkllekaakvmgdytdieiieahhrhkvdapsgtalamgeaiahaldkdlkdca
vysreghtgervpgtigfatvragdivgehtamfadigerleithkassr
>d1dij_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {(Bacillus circulans)}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d1dij_2 2.3.1.1.1 (582-686) Cyclodextrin glycosyltransferase, C-terminal domain {(Bacillus circulans)}
lsgdqvsvrfvvnnattalgqnvyltgsvselgnwdpakaigpmynqvvyqypnwyydvs
vpagktiefkflkkqgstvtweggsnhtftapssgtatinvnwqp
>d1dij_3 2.53.1.1.2 (383-495) Cyclodextrin glycosyltransferase {(Bacillus circulans)}
tsttayqviqklaplrkcnpaiaygstqerwinndvliyerkfgsnvavvavnrnlnapa
sisglvtslpqgsyndvlggllngntlsvgsggaasnftlaaggtavwqytaa
>d1dij_4 3.1.1.1.2 (1-382) Cyclodextrin glycosyltransferase {(Bacillus circulans)}
apdtsvsnkqnfstdviyqiftdrfsdgnpannptgaafdgtctnlrlycggdwqgiink
indgyltgmgvtaiwisqpveniysiinysgvnntayhgywardfkktnpaygtiadfqn
liaaahaknikviidfapnhtspassdqpsfaengrlydngtllggytndtqnlfhhngg
tdfsttengiyknlfdladlnhnnstvdvylkdaikmwldlgidgirmdavkhmpfgwqk
sfmaavnnykpvftfgewflgvnevspenhkfanesgmslldfrfaqkvrqvfrdntdnm
yglkamlegsaadyaqvddqvtfidnhdmerfhasnanrrkleqalaftltsrgvpaiyy
gteqymsggtdpdnraripsfs
>d1dik_1 3.1.9.2.1 (510-874) Pyruvate phosphate dikinase, C-terminal domain {(Escherichia coli)}
ietqeasvsgsferimvwadkfrtlkvrtnadtpedtlnavklgaegiglcrtehmffea
drimkirkmilsdsveareealnelipfqkgdfkamykalegrpmtvryldpplhefvph
teeeqaelaknmgltlaevkakvdelhefnpmmghrgcrlavtypeiakmqtravmeaai
evkeetgidivpeimiplvgekkelkfvkdvvvevaeqvkkekgsdmqyhigtmieipra
altadaiaeeaeffsfgtndltqmtfgfsrddagkfldsyykakiyesdpfarldqtgvg
qlvemavkkgrqtrpglkcgicgehggdpssvefchkvglnyvscspfrvpiarlaaaqa
alnnk
>d1dik_2 3.5.1.1.1 (377-505) Pyruvate phosphate dikinase, central domain {(Escherichia coli)}
lhptfnpaalkagevigsalpaspgaaagkvyftadeakaahekgervilvrletspedi
egmhaaegiltvrggmtshaavvargmgtccvsgcgeikineeaktfelgghtfaegdyi
sldgstgki
>d1dik_3 4.89.1.5.1 (2-376) Pyruvate phosphate dikinase, N-terminal domain {(Escherichia coli)}
akwvykfeegnasmrnllggkgcnlaemtilgmpipqgftvtteacteyynsgkqitqei
qdqifeaitwleelngkkfgdtedpllvsvrsaarasmpgmmdtilnlglndvavegfak
ktgnprfaydsyrrfiqmysdvvmevpkshfekiidamkeekgvhfdtdltaddlkelae
kfkavykeamngeefpqepkdqlmgavkavfrswdnpraivyrrmndipgdwgtavnvqt
mvfgnkgetsgtgvaftrnpstgekgiygeylinaqgedvvagvrtpqpitqlendmpdc
ykqfmdlamklekhfrdmqdmeftieegklyflqtrngkrtapaalqiacdlvdegmite
eeavvrieaksldql
>d1dil__ 2.50.1.1.1 Salmonella sialidase {(Salmonella typhimurium), strain lt2}
tveksvvfkaegehftdqkgntivgsgsggttkyfripamcttskgtivvfadarhntas
dqsfidtaaarstdggktwnkkiaiyndrvnsklsrvmdptcivaniqgretilvmvgkw
nnndktwgayrdkapdtdwdlvlykstddgvtfskvetnihdivtkngtisamlggvgsg
lqlndgklvfpvqmvrtknittvlntsfiystdgitwslpsgycegfgsenniiefnasl
vnnirnsglrrsfetkdfgktwtefppmdkkvdnrnhgvqgstitipsgnklvaahssaq
nknndytrsdislyahnlysgevkliddfypkvgnasgagysclsyrknvdketlyvvye
angsiefqdlsrhlpviksyn
>d1dim__ 2.50.1.1.1 Salmonella sialidase {(Salmonella typhimurium), strain lt2}
tveksvvfkaegehftdqkgntivgsgsggttkyfripamcttskgtivvfadarhntas
dqsfidtaaarstdggktwnkkiaiyndrvnsklsrvmdptcivaniqgretilvmvgkw
nnndktwgayrdkapdtdwdlvlykstddgvtfskvetnihdivtkngtisamlggvgsg
lqlndgklvfpvqmvrtknittvlntsfiystdgitwslpsgycegfgsenniiefnasl
vnnirnsglrrsfetkdfgktwtefppmdkkvdnrnhgvqgstitipsgnklvaahssaq
nknndytrsdislyahnlysgevkliddfypkvgnasgagysclsyrknvdketlyvvye
angsiefqdlsrhlpviksyn
>d1din__ 3.56.1.4.1 Dienelactone hydrolase {(Pseudomonas sp.) B13}
mltegisiqsydghtfgalvgspakapapviviaqeifgvnafmretvswlvdqgyaavc
pdlyarqapgtaldpqderqreqayklwqafdmeagvgdleaairyarhqpysngkvglv
gyxlggalaflvaakgyvdravgyygvglekqlnkvpevkhpalfhmggqdhfvpapsrq
litegfganpllqvhwyeeaghsfartsssgyvasaaalanertldflaplqs
>d1dipa_ 1.105.10.1.1 Delta-sleep-iducing peptide immunoreactive peptide {Pig (Sus scrofa)}
mdlvknhlmyavreeveilkeqirelveknsqlerentllktlaspeqlekfqsrlspee
papetpeapeapggsav
>d1dipb_ 1.105.10.1.1 Delta-sleep-iducing peptide immunoreactive peptide {Pig (Sus scrofa)}
mdlvknhlmyavreeveilkeqirelveknsqlerentllktlaspeqlekfqsrlspee
papetpeapeapggsav
>d1dira_ 3.22.1.2.7 Dihydropteridin reductase {rat (Rattus norvegicus)}
earrvlvyggrgalgsrcvqafrarnwwvasidvveneeasasvivkmtdsfteqadqvt
aevgkllgdqkvdailcvaggwaggnakskslfkncdlmwkqsiwtstisshlatkhlke
gglltlagakaaldgtpgmigygmakgavhqlcqslagknsgmpsgaaaiavlpvtldtp
mnrksmpeadfsswtpleflvetfhdwitgnkrpnsgsliqvvttdgkteltpayf
>d1dirb_ 3.22.1.2.7 Dihydropteridin reductase {rat (Rattus norvegicus)}
earrvlvyggrgalgsrcvqafrarnwwvasidvveneeasasvivkmtdsfteqadqvt
aevgkllgdqkvdailcvaggwaggnakskslfkncdlmwkqsiwtstisshlatkhlke
gglltlagakaaldgtpgmigygmakgavhqlcqslagknsgmpsgaaaiavlpvtldtp
mnrksmpeadfsswtpleflvetfhdwitgnkrpnsgsliqvvttdgkteltpayf
>d1dirc_ 3.22.1.2.7 Dihydropteridin reductase {rat (Rattus norvegicus)}
earrvlvyggrgalgsrcvqafrarnwwvasidvveneeasasvivkmtdsfteqadqvt
aevgkllgdqkvdailcvaggwaggnakskslfkncdlmwkqsiwtstisshlatkhlke
gglltlagakaaldgtpgmigygmakgavhqlcqslagknsgmpsgaaaiavlpvtldtp
mnrksmpeadfsswtpleflvetfhdwitgnkrpnsgsliqvvttdgkteltpayf
>d1dird_ 3.22.1.2.7 Dihydropteridin reductase {rat (Rattus norvegicus)}
earrvlvyggrgalgsrcvqafrarnwwvasidvveneeasasvivkmtdsfteqadqvt
aevgkllgdqkvdailcvaggwaggnakskslfkncdlmwkqsiwtstisshlatkhlke
gglltlagakaaldgtpgmigygmakgavhqlcqslagknsgmpsgaaaiavlpvtldtp
mnrksmpeadfsswtpleflvetfhdwitgnkrpnsgsliqvvttdgkteltpayf
>d1dis__ 3.60.1.1.2 Dihydrofolate reductase, prokaryotic type {(Lactobacillus casei)}
taflwaqdrdgligkdghlpwhlpddlhyfraqtvgkimvvgrrtyesfpkrplpertnv
vlthqedyqaqgavvvhdvaavfayakqhpdqelviaggaqiftafkddvdtllvtrlag
sfegdtkmiplnwddftkvssrtvedtnpalthtyevwqkka
>e1dit.1h 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>e1dit.1l 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
geadcglrplfekksledkterellesyi
>d1diu__ 3.60.1.1.2 Dihydrofolate reductase, prokaryotic type {(Lactobacillus casei)}
taflwaqdrdgligkdghlpwhlpddlhyfraqtvgkimvvgrrtyesfpkrplpertnv
vlthqedyqaqgavvvhdvaavfayakqhpdqelviaggaqiftafkddvdtllvtrlag
sfegdtkmiplnwddftkvssrtvedtnpalthtyevwqkka
>d1div__ 4.88.1.1.1 Ribosomal protein L9 {(Bacillus stearothermophilus)}
mkviflkdvkgkgkkgeiknvadgyannflfkqglaieatpanlkaleaqkqkeqrqaae
elanakklkeqlekltvtipakageggrlfgsitskqiaeslqaqhglkldkrkielada
iralgytnvpvklhpevtatlkvhvteqk
>d1dja__ 5.4.1.1.3 beta-Lactamase, class A {(Staphylococcus aureus)}
mkelndlekkynahigvyaldtksgkevkfnsdkrfayastshainsailleqvpynkln
kkvhinkddivayspilekyvgkditlkalieasmtysdntannkiikeiggikkvkqrl
kelgdkvtnpvryeielnyyspkskkdtstpaafgktlnkliangklskenkkflldlml
nnksgdtlikdgvpkdykvadksgqaityasrndvafvypkgqsepivlviftnkdnksd
kpndklisetaksvmkef
>d1djb__ 5.4.1.1.3 beta-Lactamase, class A {(Staphylococcus aureus)}
kelndlekkynahigvyaldtksgkevkfnsdkrfayaatskainsailleqvpynklnk
kvhinkddivayspilekyvgkditlkalieasmtysdntannkiikeiggikkvkqrlk
elgdkvtnpvryeielnyyspkskkdtstpaafgktlnkliangklskenkkflldlmln
nksgdtlikdgvpkdykvadksgqaityasrndvafvypkgqsepivlviftnkdnksdk
pndklisetaksvmkef
>d1djc__ 5.4.1.1.3 beta-Lactamase, class A {(Staphylococcus aureus)}
kelndlekkynahigvyaldtksgkevkfnsdkrfayaatskainsailleqvpynklnk
kvhinkddivayspilekyvgkditlkalieasmtysdntannkiikeiggikkvkqrlk
elgdkvtnpvryeielnyyspkskkdtstpaafgktlnkliangklskenkkflldlmln
nksgdtlikdgvpkdykvadksgqaityasrndvafvypkgqsepivlviftnkdnksdk
pndklisetaksvmkef
>d1djga1 1.37.1.6.1 (200-281) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
eietfykmltqraeidrafeeaagsaetlsverlvtflqhqqreeeagpalalslierye
psetakaqrqmtkdgflmylls
>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 3.1.15.1.1 (299-606) Phospholipase C isozyme D1 (PLC-D1) {Rat (Rattus norvegicus)}
dqplshylvssshntylledqltgpssteayiralckgcrcleldcwdgpnqepiiyhgy
tftskilfcdvlrairdyafkaspypvilslenhcsleqqrvmarhlrailgpilldqpl
dgvttslpspeqlkgkillkgkklggllpaggengseatdvsdeveaaemedeavrsqvq
hkpkedklklvpelsdmiiycksvhfggfsspgtsgqafyemasfsesralrllqesgng
fvrhnvsclsriypagwrtdssnyspvemwnggcqivalnfqtpgpemdvylgcfqdngg
cgyvlkpa
>d1djgb1 1.37.1.6.1 (158-281) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
nkmnfkelkdflkelniqvddgyarkifrecdhsqtdsledeeietfykmltqraeidra
feeaagsaetlsverlvtflqhqqreeeagpalalslieryepsetakaqrqmtkdgflm
ylls
>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 3.1.15.1.1 (299-606) Phospholipase C isozyme D1 (PLC-D1) {Rat (Rattus norvegicus)}
dqplshylvssshntylledqltgpssteayiralckgcrcleldcwdgpnqepiiyhgy
tftskilfcdvlrairdyafkaspypvilslenhcsleqqrvmarhlrailgpilldqpl
dgvttslpspeqlkgkillkgkklggllpaggengseatdvsdeveaaemedeavrsqvq
hkpkedklklvpelsdmiiycksvhfggfsspgtsgqafyemasfsesralrllqesgng
fvrhnvsclsriypagwrtdssnyspvemwnggcqivalnfqtpgpemdvylgcfqdngg
cgyvlkpa
>d1djha1 1.37.1.6.1 (200-281) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
eietfykmltqraeidrafeeaagsaetlsverlvtflqhqqreeeagpalalslierye
psetakaqrqmtkdgflmylls
>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 3.1.15.1.1 (299-606) Phospholipase C isozyme D1 (PLC-D1) {Rat (Rattus norvegicus)}
dqplshylvssshntylledqltgpssteayiralckgcrcleldcwdgpnqepiiyhgy
tftskilfcdvlrairdyafkaspypvilslenhcsleqqrvmarhlrailgpilldqpl
dgvttslpspeqlkgkillkgkklggllpaggengseatdvsdeveaaemedeavrsqvq
hkpkedklklvpelsdmiiycksvhfggfsspgtsgqafyemasfsesralrllqesgng
fvrhnvsclsriypagwrtdssnyspvemwnggcqivalnfqtpgpemdvylgcfqdngg
cgyvlkpa
>d1djhb1 1.37.1.6.1 (158-281) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
nkmnfkelkdflkelniqvddgyarkifrecdhsqtdsledeeietfykmltqraeidra
feeaagsaetlsverlvtflqhqqreeeagpalalslieryepsetakaqrqmtkdgflm
ylls
>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 3.1.15.1.1 (299-606) Phospholipase C isozyme D1 (PLC-D1) {Rat (Rattus norvegicus)}
dqplshylvssshntylledqltgpssteayiralckgcrcleldcwdgpnqepiiyhgy
tftskilfcdvlrairdyafkaspypvilslenhcsleqqrvmarhlrailgpilldqpl
dgvttslpspeqlkgkillkgkklggllpaggengseatdvsdeveaaemedeavrsqvq
hkpkedklklvpelsdmiiycksvhfggfsspgtsgqafyemasfsesralrllqesgng
fvrhnvsclsriypagwrtdssnyspvemwnggcqivalnfqtpgpemdvylgcfqdngg
cgyvlkpa
>d1djia1 1.37.1.6.1 (200-281) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
eietfykmltqraeidrafeeaagsaetlsverlvtflqhqqreeeagpalalslierye
psetakaqrqmtkdgflmylls
>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 3.1.15.1.1 (299-606) Phospholipase C isozyme D1 (PLC-D1) {Rat (Rattus norvegicus)}
dqplshylvssshntylledqltgpssteayiralckgcrcleldcwdgpnqepiiyhgy
tftskilfcdvlrairdyafkaspypvilslenhcsleqqrvmarhlrailgpilldqpl
dgvttslpspeqlkgkillkgkklggllpaggengseatdvsdeveaaemedeavrsqvq
hkpkedklklvpelsdmiiycksvhfggfsspgtsgqafyemasfsesralrllqesgng
fvrhnvsclsriypagwrtdssnyspvemwnggcqivalnfqtpgpemdvylgcfqdngg
cgyvlkpa
>d1djib1 1.37.1.6.1 (158-281) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
nkmnfkelkdflkelniqvddgyarkifrecdhsqtdsledeeietfykmltqraeidra
feeaagsaetlsverlvtflqhqqreeeagpalalslieryepsetakaqrqmtkdgflm
ylls
>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 3.1.15.1.1 (299-606) Phospholipase C isozyme D1 (PLC-D1) {Rat (Rattus norvegicus)}
dqplshylvssshntylledqltgpssteayiralckgcrcleldcwdgpnqepiiyhgy
tftskilfcdvlrairdyafkaspypvilslenhcsleqqrvmarhlrailgpilldqpl
dgvttslpspeqlkgkillkgkklggllpaggengseatdvsdeveaaemedeavrsqvq
hkpkedklklvpelsdmiiycksvhfggfsspgtsgqafyemasfsesralrllqesgng
fvrhnvsclsriypagwrtdssnyspvemwnggcqivalnfqtpgpemdvylgcfqdngg
cgyvlkpa
>d1djwa1 1.37.1.6.1 (200-281) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
eietfykmltqraeidrafeeaagsaetlsverlvtflqhqqreeeagpalalslierye
psetakaqrqmtkdgflmylls
>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 3.1.15.1.1 (299-606) Phospholipase C isozyme D1 (PLC-D1) {Rat (Rattus norvegicus)}
dqplshylvssshntylledqltgpssteayiralckgcrcleldcwdgpnqepiiyhgy
tftskilfcdvlrairdyafkaspypvilslenhcsleqqrvmarhlrailgpilldqpl
dgvttslpspeqlkgkillkgkklggllpaggengseatdvsdeveaaemedeavrsqvq
hkpkedklklvpelsdmiiycksvhfggfsspgtsgqafyemasfsesralrllqesgng
fvrhnvsclsriypagwrtdssnyspvemwnggcqivalnfqtpgpemdvylgcfqdngg
cgyvlkpa
>d1djwb1 1.37.1.6.1 (158-281) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
nkmnfkelkdflkelniqvddgyarkifrecdhsqtdsledeeietfykmltqraeidra
feeaagsaetlsverlvtflqhqqreeeagpalalslieryepsetakaqrqmtkdgflm
ylls
>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 3.1.15.1.1 (299-606) Phospholipase C isozyme D1 (PLC-D1) {Rat (Rattus norvegicus)}
dqplshylvssshntylledqltgpssteayiralckgcrcleldcwdgpnqepiiyhgy
tftskilfcdvlrairdyafkaspypvilslenhcsleqqrvmarhlrailgpilldqpl
dgvttslpspeqlkgkillkgkklggllpaggengseatdvsdeveaaemedeavrsqvq
hkpkedklklvpelsdmiiycksvhfggfsspgtsgqafyemasfsesralrllqesgng
fvrhnvsclsriypagwrtdssnyspvemwnggcqivalnfqtpgpemdvylgcfqdngg
cgyvlkpa
>d1djxa1 1.37.1.6.1 (200-281) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
eietfykmltqraeidrafeeaagsaetlsverlvtflqhqqreeeagpalalslierye
psetakaqrqmtkdgflmylls
>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 3.1.15.1.1 (299-606) Phospholipase C isozyme D1 (PLC-D1) {Rat (Rattus norvegicus)}
dqplshylvssshntylledqltgpssteayiralckgcrcleldcwdgpnqepiiyhgy
tftskilfcdvlrairdyafkaspypvilslenhcsleqqrvmarhlrailgpilldqpl
dgvttslpspeqlkgkillkgkklggllpaggengseatdvsdeveaaemedeavrsqvq
hkpkedklklvpelsdmiiycksvhfggfsspgtsgqafyemasfsesralrllqesgng
fvrhnvsclsriypagwrtdssnyspvemwnggcqivalnfqtpgpemdvylgcfqdngg
cgyvlkpa
>d1djxb1 1.37.1.6.1 (158-281) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
nkmnfkelkdflkelniqvddgyarkifrecdhsqtdsledeeietfykmltqraeidra
feeaagsaetlsverlvtflqhqqreeeagpalalslieryepsetakaqrqmtkdgflm
ylls
>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 3.1.15.1.1 (299-606) Phospholipase C isozyme D1 (PLC-D1) {Rat (Rattus norvegicus)}
dqplshylvssshntylledqltgpssteayiralckgcrcleldcwdgpnqepiiyhgy
tftskilfcdvlrairdyafkaspypvilslenhcsleqqrvmarhlrailgpilldqpl
dgvttslpspeqlkgkillkgkklggllpaggengseatdvsdeveaaemedeavrsqvq
hkpkedklklvpelsdmiiycksvhfggfsspgtsgqafyemasfsesralrllqesgng
fvrhnvsclsriypagwrtdssnyspvemwnggcqivalnfqtpgpemdvylgcfqdngg
cgyvlkpa
>d1djya1 1.37.1.6.1 (200-281) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
eietfykmltqraeidrafeeaagsaetlsverlvtflqhqqreeeagpalalslierye
psetakaqrqmtkdgflmylls
>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 3.1.15.1.1 (299-606) Phospholipase C isozyme D1 (PLC-D1) {Rat (Rattus norvegicus)}
dqplshylvssshntylledqltgpssteayiralckgcrcleldcwdgpnqepiiyhgy
tftskilfcdvlrairdyafkaspypvilslenhcsleqqrvmarhlrailgpilldqpl
dgvttslpspeqlkgkillkgkklggllpaggengseatdvsdeveaaemedeavrsqvq
hkpkedklklvpelsdmiiycksvhfggfsspgtsgqafyemasfsesralrllqesgng
fvrhnvsclsriypagwrtdssnyspvemwnggcqivalnfqtpgpemdvylgcfqdngg
cgyvlkpa
>d1djyb1 1.37.1.6.1 (158-281) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
nkmnfkelkdflkelniqvddgyarkifrecdhsqtdsledeeietfykmltqraeidra
feeaagsaetlsverlvtflqhqqreeeagpalalslieryepsetakaqrqmtkdgflm
ylls
>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 3.1.15.1.1 (299-606) Phospholipase C isozyme D1 (PLC-D1) {Rat (Rattus norvegicus)}
dqplshylvssshntylledqltgpssteayiralckgcrcleldcwdgpnqepiiyhgy
tftskilfcdvlrairdyafkaspypvilslenhcsleqqrvmarhlrailgpilldqpl
dgvttslpspeqlkgkillkgkklggllpaggengseatdvsdeveaaemedeavrsqvq
hkpkedklklvpelsdmiiycksvhfggfsspgtsgqafyemasfsesralrllqesgng
fvrhnvsclsriypagwrtdssnyspvemwnggcqivalnfqtpgpemdvylgcfqdngg
cgyvlkpa
>d1djza1 1.37.1.6.1 (200-281) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
eietfykmltqraeidrafeeaagsaetlsverlvtflqhqqreeeagpalalslierye
psetakaqrqmtkdgflmylls
>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 3.1.15.1.1 (299-606) Phospholipase C isozyme D1 (PLC-D1) {Rat (Rattus norvegicus)}
dqplshylvssshntylledqltgpssteayiralckgcrcleldcwdgpnqepiiyhgy
tftskilfcdvlrairdyafkaspypvilslenhcsleqqrvmarhlrailgpilldqpl
dgvttslpspeqlkgkillkgkklggllpaggengseatdvsdeveaaemedeavrsqvq
hkpkedklklvpelsdmiiycksvhfggfsspgtsgqafyemasfsesralrllqesgng
fvrhnvsclsriypagwrtdssnyspvemwnggcqivalnfqtpgpemdvylgcfqdngg
cgyvlkpa
>d1djzb1 1.37.1.6.1 (158-281) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
nkmnfkelkdflkelniqvddgyarkifrecdhsqtdsledeeietfykmltqraeidra
feeaagsaetlsverlvtflqhqqreeeagpalalslieryepsetakaqrqmtkdgflm
ylls
>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 3.1.15.1.1 (299-606) Phospholipase C isozyme D1 (PLC-D1) {Rat (Rattus norvegicus)}
dqplshylvssshntylledqltgpssteayiralckgcrcleldcwdgpnqepiiyhgy
tftskilfcdvlrairdyafkaspypvilslenhcsleqqrvmarhlrailgpilldqpl
dgvttslpspeqlkgkillkgkklggllpaggengseatdvsdeveaaemedeavrsqvq
hkpkedklklvpelsdmiiycksvhfggfsspgtsgqafyemasfsesralrllqesgng
fvrhnvsclsriypagwrtdssnyspvemwnggcqivalnfqtpgpemdvylgcfqdngg
cgyvlkpa
>d1dka__ 3.54.1.3.1 Dialkylglycine decarboxylase {(Pseudomonas cepacia)}
lnddatfwrnarhhlvryggtfepmiierakgsfvydadgraildftsgqmsavlghchp
eivsvigeyagkldhlfsemlsrpvvdlatrlanitppgldralllstgaesneaairma
klvtgkyeivgfaqswhgmtgaaasatysagrkgvgpaavgsfaipapftyrprfernga
ydylaeldyafdlidrqssgnlaafiaepilssggiielpdgymaalkrkceargmllil
deaqtgvgrtgtmfacqrdgvtpdiltlsktlgaglplaaivtsaaieerahelgylfyt
thvsdplpaavglrvldvvqrdglvaranvmgdrlrrglldlmerfdcigdvrgrglllg
veivkdrrtkepadglgakitrecmnlglsmnivqlpgmggvfriappltvsedeidlgl
sllgqaieral
>d1dkga1 1.105.8.1.1 (34-138) The coiled-coil domain of nucleotide exchange factor GrpE {(Escherichia coli)}
aeqvdprdekvanleaqlaeaqtrerdgilrvkaemenlrrrteldiekahkfalekfin
ellpvidsldralevadkanpdmsamvedieltlksmldvvrkfg
>d1dkga2 2.55.1.1.1 (139-197) The head domain of nucleotide exchange factor GrpE {(Escherichia coli)}
veviaetnvpldpnvhqaiamvesddvapgnvlgimqkgytlngrtiraamvtvakaka
>d1dkgb1 1.105.8.1.1 (38-138) The coiled-coil domain of nucleotide exchange factor GrpE {(Escherichia coli)}
dprdekvanleaqlaeaqtrerdgilrvkaemenlrrrteldiekahkfalekfinellp
vidsldralevadkanpdmsamvedieltlksmldvvrkfg
>d1dkgb2 2.55.1.1.1 (139-195) The head domain of nucleotide exchange factor GrpE {(Escherichia coli)}
veviaetnvpldpnvhqaiamvesddvapgnvlgimqkgytlngrtiraamvtvaka
>d1dkgd_ 3.47.1.1.2 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_ 4.57.1.1.3 CksHs1 {Human (Homo sapiens)}
shkqiyysdkyddeefeyrhvmlpkdiaklvpkthlmsesewrnlgvqqsqgwvhymihe
pephillfrrplpkkp
>d1dksb_ 4.57.1.1.3 CksHs1 {Human (Homo sapiens)}
kqiyysdkyddeefeyrhvmlpkdiaklvpkthlmsesewrnlgvqqsqgwvhymihepe
phillfrrplpkk
>d1dkta_ 4.57.1.1.3 CksHs1 {Human (Homo sapiens)}
qiyysdkyddeefeyrhvmlpkdiaklvpkthlmsesewrnlgvqqsqgwvhymihepep
hillfrrplpkk
>d1dktb_ 4.57.1.1.3 CksHs1 {Human (Homo sapiens)}
qiyysdkyddeefeyrhvmlpkdiaklvpkthlmsesewrnlgvqqsqgwvhymihepep
hillfrrplpk
>d1dkxa_ 5.17.1.1.1 DnaK {(Escherichia coli)}
vllldvtplslgietmggvmttliaknttiptkhsqvfstaednqsavtihvlqgerkra
adnkslgqfnldginpaprgmpqievtfdidadgilhvsakdknsgkeqkitikassgln
edeiqkmvrdaeanaeadrkfdelvqtrnqgdhllhstrkqveeagdklpaddktaiesa
ltaletalkgedkaaieakmqelaqvsqklmeiaqqqha
>d1dkya_ 5.17.1.1.1 DnaK {(Escherichia coli)}
vllldvtplslgietmggvmttliaknttiptkhsqvfstaednqsavsihvlqgerkra
adnkslgqfnldginpaprgmpqievtfdidadgilhvsakdknsgkeqkitikassgln
edeiqkmvrdaeanaeadrkfeelvqtrnqgdhllhstrkqveeagdklpaddktaiesa
ltaletalkgedkaaieakmqelaqvsqklm
>d1dkyb_ 5.17.1.1.1 DnaK {(Escherichia coli)}
vllldvtplslgietmggvmttliaknttiptkhsqvfstaednqsavsihvlqgerkra
adnkslgqfnldginpaprgmpqievtfdidadgilhvsakdknsgkeqkitikassgln
edeiqkmvrdaeanaeadrkfeelvqtrnqgdhllhstrkqveeagdklpaddktaiesa
ltaletalkgedkaaieakmqel
>d1dkza_ 5.17.1.1.1 DnaK {(Escherichia coli)}
vllldvtplslgietmggvmttliaknttiptkhsqvfstaednqsavsihvlqgerkra
adnkslgqfnldginpaprgmpqievtfdidadgilhvsakdknsgkeqkitikassgln
edeiqkmvrdaeanaeadrkfeelvqtrnqgdhllhstrkqveeagdklpaddktaiesa
ltaletalkgedkaaieakmqelaqvsqklmeiaq
>d1dlaa_ 3.1.5.1.2 Aldose reductase (aldehyde reductase) {human (Homo sapiens)}
shlvlytgakmpilglgtwksppgkvteavkvaidlgyrhidcahvyqnenevglglqek
lqgqvvkredlfivsklwctdheknlvkgacqttlrdlkldyldlylihwptgfkpgkdp
fpldgdgnvvpdesdfvetweameelvdeglvkaigvsnfnhlqvekilnkpglkykpav
nqievhpyltqeklieyckskgivvtaysplgspdrpwakpedpslledprikaiaakyn
kttaqvlirfpmqrnlivipksvtperiaenfqvfdfelspedmntllsynrnwrvcalm
scashkdypfheey
>d1dlab_ 3.1.5.1.2 Aldose reductase (aldehyde reductase) {human (Homo sapiens)}
shlvlytgakmpilglgtwksppgkvteavkvaidlgyrhidcahvyqnenevglglqek
lqgqvvkredlfivsklwctdheknlvkgacqttlrdlkldyldlylihwptgfkpgkdp
fpldgdgnvvpdesdfvetweameelvdeglvkaigvsnfnhlqvekilnkpglkykpav
nqievhpyltqeklieyckskgivvtaysplgspdrpwakpedpslledprikaiaakyn
kttaqvlirfpmqrnlivipksvtperiaenfqvfdfelspedmntllsynrnwrvcalm
scashkdypfheey
>d1dlac_ 3.1.5.1.2 Aldose reductase (aldehyde reductase) {human (Homo sapiens)}
shlvlytgakmpilglgtwksppgkvteavkvaidlgyrhidcahvyqnenevglglqek
lqgqvvkredlfivsklwctdheknlvkgacqttlrdlkldyldlylihwptgfkpgkdp
fpldgdgnvvpdesdfvetweameelvdeglvkaigvsnfnhlqvekilnkpglkykpav
nqievhpyltqeklieyckskgivvtaysplgspdrpwakpedpslledprikaiaakyn
kttaqvlirfpmqrnlivipksvtperiaenfqvfdfelspedmntllsynrnwrvcalm
scashkdypfheey
>d1dlad_ 3.1.5.1.2 Aldose reductase (aldehyde reductase) {human (Homo sapiens)}
shlvlytgakmpilglgtwksppgkvteavkvaidlgyrhidcahvyqnenevglglqek
lqgqvvkredlfivsklwctdheknlvkgacqttlrdlkldyldlylihwptgfkpgkdp
fpldgdgnvvpdesdfvetweameelvdeglvkaigvsnfnhlqvekilnkpglkykpav
nqievhpyltqeklieyckskgivvtaysplgspdrpwakpedpslledprikaiaakyn
kttaqvlirfpmqrnlivipksvtperiaenfqvfdfelspedmntllsynrnwrvcalm
scashkdypfheey
>d1dlc_1 2.13.1.2.1 (500-644) delta-Endotoxin, C-terminal domain {(Bacillus thuringiensis tenebrionis), CRYIIIA (BT13)}
ffnmidskkitqlplvkayklqsgasvvagprftggdiiqctengsaatiyvtpdvsysq
kyrarihyastsqitftlsldgapfnqyyfdktinkgdtltynsfnlasfstpfelsgnn
lqigvtglsagdkvyidkiefipvn
>d1dlc_2 2.59.2.1.1 (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
>d1dlha1 2.1.1.2.114 (82-182) Class II MHC, C-terminal domains of alpha and beta chains {(human hla-dr1)}
itnvppevtvltnspvelrepnvlicfidkftppvvnvtwlrngkpvttgvsetvflpre
dhlfrkfhylpflpstedvydcrvehwgldepllkhwefda
>d1dlha2 4.15.1.1.3 (3-81) MHC class II, N-terminal domains of alpha and beta chains {(human hla-dr1)}
eehviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgalan
iavdkanleimtkrsnytp
>d1dlhb1 2.1.1.2.114 (93-190) Class II MHC, C-terminal domains of alpha and beta chains {(human hla-dr1)}
rrvepkvtvypsktqplqhhnllvcsvsgfypgsievrwfrngqeekagvvstgliqngd
wtfqtlvmletvprsgevytcqvehpsvtspltvewra
>d1dlhb2 4.15.1.1.3 (3-92) MHC class II, N-terminal domains of alpha and beta chains {(human hla-dr1)}
trprflwqlkfechffngtervrllerciynqeesvrfdsdvgeyravtelgrpdaeywn
sqkdlleqrraavdtycrhnygvgesftvq
>d1dlhd1 2.1.1.2.114 (82-182) Class II MHC, C-terminal domains of alpha and beta chains {(human hla-dr1)}
itnvppevtvltnspvelrepnvlicfidkftppvvnvtwlrngkpvttgvsetvflpre
dhlfrkfhylpflpstedvydcrvehwgldepllkhwefda
>d1dlhd2 4.15.1.1.3 (3-81) MHC class II, N-terminal domains of alpha and beta chains {(human hla-dr1)}
eehviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgalan
iavdkanleimtkrsnytp
>d1dlhe1 2.1.1.2.114 (93-190) Class II MHC, C-terminal domains of alpha and beta chains {(human hla-dr1)}
rrvepkvtvypsktqplqhhnllvcsvsgfypgsievrwfrngqeekagvvstgliqngd
wtfqtlvmletvprsgevytcqvehpsvtspltvewra
>d1dlhe2 4.15.1.1.3 (3-92) MHC class II, N-terminal domains of alpha and beta chains {(human hla-dr1)}
trprflwqlkfechffngtervrllerciynqeesvrfdsdvgeyravtelgrpdaeywn
sqkdlleqrraavdtycrhnygvgesftvq
>d1dloa1 3.47.3.1.4 (430-556) HIV RNase H (Domain of reverse transcriptase) {(human immunodeficiency virus type I)}
ekepivgaetfyvdgaanretklgkagyvtnkgrqkvvpltnttnqktelqaiylalqds
glevnivtdsqyalgiiqaqpdkseselvnqiieqlikkekvylawvpahkgiggneqvd
klvsagi
>d1dloa2 5.9.1.2.2 (1-429) HIV-1 reverse transcriptase {human immunodeficiency virus type 1 (Bh10 isolate)}
pispietvpvklkpgmdgpkvkqwplteekikalveictemekegkiskigpenpyntpv
faikkkdstkwrklvdfrelnkrtqdfwevqlgiphpaglkkkksvtvldvgdayfsvpl
dedfrkytaftipsinnetpgiryqynvlpqgwkgspaifqssmtkilepfkkqnpdivi
yqymddlyvgsdleigqhrtkieelrqhllrwglttpdkkhqkeppflwmgyelhpdkwt
vqpivlpekdswtvndiqklvgklnwasqiypgikvrqlskllrgtkalteviplteeae
lelaenreilkepvhgvyydpskdliaeiqkqgqgqwtyqiyqepfknlktgkyarmrga
htndvkqlteavqkittesiviwgktpkfklpiqketwetwwteywqatwipewefvntp
plvklwyql
>d1dlr__ 3.60.1.1.5 Dihydrofolate reductases, eukaryotic type {human (Homo sapiens)}
vgslncivavsqnmgigkngdfpwpplrnefryfqrmtttssvegkqnlvimgkktwfsi
peknrplkgrinlvlsrelkeppqgahflsrslddalklteqpelankvdmvwivggssv
ykeamnhpghlklfvtrimqdfesdtffpeidlekykllpeypgvlsdvqeekgikykfe
vyeknd
>d1dls__ 3.60.1.1.5 Dihydrofolate reductases, eukaryotic type {human (Homo sapiens)}
vgslncivavsqnmgigkngdypwpplrnefryfqrmtttssvegkqnlvimgkktwfsi
peknrplkgrinlvlsrelkeppqgahflsrslddalklteqpelankvdmvwivggssv
ykeamnhpghlklfvtrimqdfesdtffpeidlekykllpeypgvlsdvqeekgikykfe
vyeknd
>d1dmaa_ 4.103.1.1.4 Exotoxin A, C-terminal domain {(Pseudomonas aeruginosa)}
flgdggdvsfstrgtqnwtverllqahrqleergyvfvgyhgtfleaaqsivfggvrars
qdldaiwrgfyiagdpalaygyaqdqepdargrirngallrvyvprsslpgfyrtsltla
apeaageverlighplplrldaitgpeeeggrletilgwplaertvvipsaiptdprnvg
gdldpssipdkeqaisalpdyasqpgkppr
>d1dmab_ 4.103.1.1.4 Exotoxin A, C-terminal domain {(Pseudomonas aeruginosa)}
flgdggdvsfstrgtqnwtverllqahrqleergyvfvgyhgtfleaaqsivfggvrars
qdldaiwrgfyiagdpalaygyaqdqepdargrirngallrvyvprsslpgfyrtsltla
apeaageverlighplplrldaitgpeeeggrletilgwplaertvvipsaiptdprnvg
gdldpssipdkeqaisalpd
>d1dmb__ 3.82.1.1.6 D-maltodextrin-binding protein {(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__ 1.37.1.5.11 Calmodulin {African frog (Xenopus laevis)}
adqlteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgn
gtidfpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdee
vdemireanidgdgqvnyeefvqmmtak
>d1dmpa_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieixghkaigtvlvgptpvniigrnlltqigatlnf
>d1dmpb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieixghkaigtvlvgptpvniigrnlltqigatlnf
>d1dmr_1 2.39.2.2.2 (626-781) Dimethylsulfoxide reductase (DMSO reductase) {(Rhodobacter capsulatus)}
erldgpgakyplhiaashpfnrlhsqlngtvlregyavqghepclmhpddaaargiadgd
vvrvhndrgqiltgvkvtdavmkgviqiyeggwydpsdvtepgtldkygdvnvlsadigt
sklaqgncgqtvlaevekytgpavtltgfvapkaae
>d1dmr_2 3.69.1.1.2 (3-625) Dimethylsulfoxide reductase (DMSO reductase) {(Rhodobacter capsulatus)}
langtvmsgshwgvftatvengrataftpwekdphpspmlagvldsiysptrikypmvrr
eflekgvnadrstrgngdfvrvswdqaldlvaaevkrveetygpegvfggsygwkspgrl
hncttllrrmltlaggyvngagdystgaaqvimphvvgtlevyeqqtawpvlaentevmv
fwaadpiktsqigwvipehgaypglealkakgtkvividpvrtktveffgaehitpkpqt
dvaimlgmahtlvaedlydkdfianytsgfdkflpyldgetdstpktaewaegisgvpae
tikelarlfeskrtmlaagwsmqrmhhgeqahwmlvtlasmlgqiglpgggfglsyhysg
ggtpstsgpalagitdggaatkgpewlaasgasvipvarvvdmlenpgaefdfngtrskf
pdvkmaywvggnpfvhhqdrnrmvkawekletfvvhdfqwtptarhadivlpattsyern
dietigdysntgilamkkiveplyearsdydifaavaerlgkgaeftegkdemgwiksfy
ddaakqgkaagvqmpafdafwaegivefpvtdgadfvryasfredpllnplgtptgliei
yskniekmgyddcpahptwmepl
>d1dms_1 2.39.2.2.2 (626-781) Dimethylsulfoxide reductase (DMSO reductase) {(Rhodobacter capsulatus)}
erldgpgakyplhiaashpfnrlhsqlngtvlregyavqghepclmhpddaaargiadgd
vvrvhndrgqiltgvkvtdavmkgviqiyeggwydpsdvteagtldkygdvnvlsadigt
sklaqgncgqtvlaevekytgpavtltgfvapkaae
>d1dms_2 3.69.1.1.2 (3-625) Dimethylsulfoxide reductase (DMSO reductase) {(Rhodobacter capsulatus)}
langtvmsgshwgvftatvengrataftpwekdphptpmlegvldsiysptrikypmvrr
eflekgvnadrstrgngdfvrvswdqaldlvaaevkrveetygpqgvfggsygwkspgrl
hncttllrrmltlaggyvngagdystgaaqvimphvvgtlevyeqqtawpvlaentevmv
fwaadpiktsqigwvipehgaypglealkakgtkvividpvrtktveffgadhvtpkpqt
dvaimlgmahtlvaedlydkdfianytsgfdkflpylmgetdstpktaewasdisgvpae
tikelarlfkskrtmlaagwsmqrmhhgeqahwmlvtlasmlgqiglpgggfglsyhysg
ggtpsssgpalsgitdggaatkgpewlaasgasvipvarvvdmlenpgaefdfngtrskf
pdvkmaywvggnpfvhhqdrnrmvkawekletfivhdfqwtptarhadivlpattsyern
dietigdysntgilamkkiveplyearsdydifaavaerlgkgkeftegkdemgwiksfy
ddaakqgkaggvempafdafwaegivefpvtdgadfvryasfredpllnplgtptgliei
yskniekmgyddcpahptwmepl
>d1dmxa_ 2.56.1.1.4 Carbonic anhydrase {Murine (Mus musculus) liver, isozyme V}
gtrqspiniqwkdsvydpqlaplrvsydaascrylwntgyffqvefddscedsgisggpl
gnhyrlkqfhfhwgatdewgsehavdghtypaelhlvhwnstkyenykkasvgenglavi
gvflklgahhqalqklvdvlpevrhkdtqvamgpfdpsclmpacrdywtypgslttppla
esvtwivqktpvevspsqlsmfrtllfsgrgeeedvmvnnyrplqplrdrklrssfr
>d1dmxb_ 2.56.1.1.4 Carbonic anhydrase {Murine (Mus musculus) liver, isozyme V}
gtrqspiniqwkdsvydpqlaplrvsydaascrylwntgyffqvefddscedsgisggpl
gnhyrlkqfhfhwgatdewgsehavdghtypaelhlvhwnstkyenykkasvgenglavi
gvflklgahhqalqklvdvlpevrhkdtqvamgpfdpsclmpacrdywtypgslttppla
esvtwivqktpvevspsqlsmfrtllfsgrgeeedvmvnnyrplqplrdrklrssfr
>d1dmya_ 2.56.1.1.4 Carbonic anhydrase {Murine (Mus musculus) liver, isozyme V}
gtrqspiniqwkdsvydpqlaplrvsydaascrylwntgyffqvefddscedsgisggpl
gnhyrlkqfhfhwgatdewgsehavdghtypaelhlvhwnstkyenykkasvgenglavi
gvflklgahhqalqklvdvlpevrhkdtqvamgpfdpsclmpacrdywtypgslttppla
esvtwivqktpvevspsqlsmfrtllfsgrgeeedvmvnnyrplqplrdrklrssfr
>d1dmyb_ 2.56.1.1.4 Carbonic anhydrase {Murine (Mus musculus) liver, isozyme V}
gtrqspiniqwkdsvydpqlaplrvsydaascrylwntgyffqvefddscedsgisggpl
gnhyrlkqfhfhwgatdewgsehavdghtypaelhlvhwnstkyenykkasvgenglavi
gvflklgahhqalqklvdvlpevrhkdtqvamgpfdpsclmpacrdywtypgslttppla
esvtwivqktpvevspsqlsmfrtllfsgrgeeedvmvnnyrplqplrdrklrssfr
>d1dnc_1 3.4.1.4.1 (18-165,291-363) Glutathione reductase {human (Homo sapiens)}
vasydylvigggsgglasarraaelgaraavveshklggtcvnvgxvpkkvmwntavhse
fmhdhadygfpscegkfnwrvikekrdayvsrlnaiyqnnltkshieiirghaaftsdpk
ptievsgkkytaphiliatggmpstpheXrvpntkdlslnklgiqtddkghiivdefqnt
nvkgiyavgdvcgkalltpvaiaagrklahrlfeykedskld
>d1dnc_2 3.4.1.4.1 (166-290) Glutathione reductase {human (Homo sapiens)}
sqipgaslgitsdgffqleelpgrsvivgagyiavemagilsalgsktslmirhdkvlrs
fdsmistncteelenagvevlkfsqvkevkktlsglevsmvtavpgrlpvmtmipdvdcl
lwaig
>d1dnc_3 4.48.1.1.1 (364-478) Glutathione reductase {human (Homo sapiens)}
ynniptvvfshppigtvgltedeaihkygienvktystsftpmyhavtkrktkcvmkmvc
ankeekvvgihmqglgcdemlqgfavavkmgatkadfdntvaihptsseelvtlr
>d1dnka_ 4.93.1.1.2 Deoxyribonuclease I {bovine (Bos taurus)}
lkiaafnirtfgetkmsnatlasyivrivrrydivliqevrdshlvavgklldylnqddp
ntyhyvvseplgrnsykerylflfrpnkvsvldtyqyddgcescgndsfsrepavvkfss
hstkvkefaivalhsapsdavaeinslydvyldvqqkwhlndvmlmgdfnadcsyvtssq
wssirlrtsstfqwlipdsadttatstncaydrivvagsllqssvvpgsaapfdfqaayg
lsnemalaisdhypvevtlt
>d1dnpa1 1.77.1.1.1 (201-469) FAD-binding (C-terminal) domain of DNA photolyase {(Escherichia coli)}
pveekaaiaqlrqfcqngageyeqqrdfpavegtsrlsaslatgglsprqclhrllaeqp
qaldggagsvwlneliwrefyrhlityhpslckhrpfiawtdrvqwqsnpahlqawqegk
tgypivdaamrqlnstgwmhnrlrmitasflvkdllidwregeryfmsqlidgdlaanng
gwqwaastgtdaapyfrifnpttqgekfdhegefirqwlpelrdvpgkvvhepwkwaqka
gvtldypqpivehkearvqtlaayeaark
>d1dnpa2 3.19.1.1.1 (1-200) N-terminal domain of DNA photolyase {(Escherichia coli)}
tthlvwfrqdlrlhdnlalaaacrnssarvlalyiatprqwathnmsprqaelinaqlng
lqialaekgipllfrevddfvasveivkqvcaensvthlfynyqyevnerardveveral
rnvvcegfddsvilppgavmtgnhemykvftpfknawlkrlregmpecvaapkvrssgsi
epspsitlnyprqsfdtahf
>d1dnpb1 1.77.1.1.1 (201-469) FAD-binding (C-terminal) domain of DNA photolyase {(Escherichia coli)}
pveekaaiaqlrqfcqngageyeqqrdfpavegtsrlsaslatgglsprqclhrllaeqp
qaldggagsvwlneliwrefyrhlityhpslckhrpfiawtdrvqwqsnpahlqawqegk
tgypivdaamrqlnstgwmhnrlrmitasflvkdllidwregeryfmsqlidgdlaanng
gwqwaastgtdaapyfrifnpttqgekfdhegefirqwlpelrdvpgkvvhepwkwaqka
gvtldypqpivehkearvqtlaayeaark
>d1dnpb2 3.19.1.1.1 (1-200) N-terminal domain of DNA photolyase {(Escherichia coli)}
tthlvwfrqdlrlhdnlalaaacrnssarvlalyiatprqwathnmsprqaelinaqlng
lqialaekgipllfrevddfvasveivkqvcaensvthlfynyqyevnerardveveral
rnvvcegfddsvilppgavmtgnhemykvftpfknawlkrlregmpecvaapkvrssgsi
epspsitlnyprqsfdtahf
>d1dob_1 3.4.1.2.3 (1-173,276-394) p-Hydroxybenzoate hydroxylase (PHBH) {(Pseudomonas aeruginosa)}
mktqvaiigagpsglllgqllhkagidnvilerqtpdyvlgriragvleqgmvdllreag
vdrrmardglvhegveiafagqrrridlkrlsggktvtvygqtevtrdlmeareacgatt
vyqaaevrlhdlqgerpyvtferdgerlrldcdyiagcdgfhgisrqsipaerXmqhgrl
flagdaahivpptgakglnlaasdvstlyrlllkayregrgellerysaiclrriwkaer
fswwmtsvlhrfpdtdafsqriqqteleyylgseaglatiaenyvglpyeeie
>d1dob_2 4.12.1.2.2 (174-275) p-Hydroxybenzoate hydroxylase {(Pseudomonas aeruginosa)}
lkvfervypfgwlglladtppvsheliyanhprgfalcsqrsatrsryfvqvplsekved
wsderfwtelkarlpsevaeklvtgpsleksiaplrsfvvep
>d1doc_1 3.4.1.2.3 (1-173,276-394) p-Hydroxybenzoate hydroxylase (PHBH) {(Pseudomonas aeruginosa)}
mktqvaiigagpsglllgqllhkagidnvilerqtpdyvlgriragvleqgmvdllreag
vdrrmardglvhegveiafagqrrridlkrlsggktvtvygqtevtrdlmeareacgatt
vyqaaevrlhdlqgerpyvtferdgerlrldcdyiagcdgfhgisrqsipaerXmqhgrl
flagdaahivpptgakglnlaasdvstlyrlllkayregrgellerysaiclrriwkaer
fswwmtsvlhrfpdtdafsqriqqteleyylgseaglatiaenyvglpyeeie
>d1doc_2 4.12.1.2.2 (174-275) p-Hydroxybenzoate hydroxylase {(Pseudomonas aeruginosa)}
lkvfervypfgwlglladtppvsheliyanhprgfalcsqrsatrsryyvqvplsekved
wsderfwtelkarlpsevaeklvtgpsleksiaplrsfvvep
>d1dod_1 3.4.1.2.3 (1-173,276-394) p-Hydroxybenzoate hydroxylase (PHBH) {(Pseudomonas aeruginosa)}
mktqvaiigagpsglllgqllhkagidnvilerqtpdyvlgriragvleqgmvdllreag
vdrrmardglvhegveiafagqrrridlkrlsggktvtvygqtevtrdlmeareacgatt
vyqaaevrlhdlqgerpyvtferdgerlrldcdyiagcdgfhgisrqsipaerXmqhgrl
flagdaahivpptgakglnlaasdvstlyrlllkayregrgellerysaiclrriwkaer
fswwmtsvlhrfpdtdafsqriqqteleyylgseaglatiaenyvglpyeeie
>d1dod_2 4.12.1.2.2 (174-275) p-Hydroxybenzoate hydroxylase {(Pseudomonas aeruginosa)}
lkvfervypfgwlglladtppvsheliyanhprgfalcsqrsatrsryyvqvplsekved
wsderfwtelkarlpsevaeklvtgpsleksiaplrsfvvep
>d1doe_1 3.4.1.2.3 (1-173,276-394) p-Hydroxybenzoate hydroxylase (PHBH) {(Pseudomonas aeruginosa)}
mktqvaiigagpsglllgqllhkagidnvilerqtpdyvlgriragvleqgmvdllreag
vdrrmardglvhegveiafagqrrridlkrlsggktvtvygqtevtrdlmeareacgatt
vyqaaevrlhdlqgerpyvtferdgerlrldcdyiagcdgfhgisrqsipaerXmqhgrl
flagdaahivpptgakglnlaasdvstlyrlllkayregrgellerysaiclrriwkaer
fswwmtsvlhrfpdtdafsqriqqteleyylgseaglatiaenyvglpyeeie
>d1doe_2 4.12.1.2.2 (174-275) p-Hydroxybenzoate hydroxylase {(Pseudomonas aeruginosa)}
lkvfervypfgwlglladtppvsheliyanhprgfalcsqrsatrsryyvqvplsekved
wsderfwtelkarlpsevaeklvtgpsleksiaplrsfvvep
>d1dog__ 1.81.1.1.1 Glucoamylase {(Aspergillus awamori), variant x100}
atldswlsneatvartailnnigadgawvsgadsgivvaspstdnpdyfytwtrdsglvi
ktlvdlfrngdtdllstiehyissqaiiqgvsnpsgdlssgglgepkfnvdetaytgswg
rpqrdgpalratamigfgqwlldngytsaateivwplvrndlsyvaqywnqtgydlweev
ngssfftiavqhralvegsafatavgsscswcdsqapqilcylqsfwtgsyilanfdssr
sgkdtntllgsihtfdpeagcddstfqpcspralanhkevvdsfrsiytlndglsdseav
avgrypedsyyngnpwflctlaaaeqlydalyqwdkqgsleitdvsldffkalysgaatg
tyssssstyssivsavktfadgfvsivethaasngslseqfdksdgdelsardltwsyaa
lltannrrnsvvppswgetsassvpgtcaatsasgtyssvtvtswpsiva
>d1doi__ 4.11.5.1.8 2Fe-2S ferredoxin {(Haloarcula marismortui)}
ptveylnyevvddngwdmydddvfgeasdmdlddedygslevnegeyileaaeaqgydwp
fscragacancaaivlegdidmdmqqilsdeevedknvrltcigspdadevkivynakhl
dylqnrvi
>d1doka_ 4.7.1.1.8 Monocyte chemoattractant protein-1 (MCP-1, MCAF) {human (Homo sapiens)}
mqpdainapvtccynftnrkisvqrlasyrritsskcpkeavifktivakeicadpkqkw
vqdsmdhldkqt
>d1dokb_ 4.7.1.1.8 Monocyte chemoattractant protein-1 (MCP-1, MCAF) {human (Homo sapiens)}
mqpdainapvtccynftnrkisvqrlasyrritsskcpkeavifktivakeicadpkqkw
vqdsmdhldkqt
>d1dol__ 4.7.1.1.8 Monocyte chemoattractant protein-1 (MCP-1, MCAF) {human (Homo sapiens)}
mqpdainapvtccynftnrkisvqrlasyrritsskcpkeavifktivakeicadpkqkw
vqdsmdhldkq
>d1doma_ 4.7.1.1.8 Monocyte chemoattractant protein-1 (MCP-1, MCAF) {human (Homo sapiens)}
qpdainapvtccynftnrkisvqrlasyrritsskcpkeavifktivakeicadpkqkwv
qdsmdhldkqtqtpkt
>d1domb_ 4.7.1.1.8 Monocyte chemoattractant protein-1 (MCP-1, MCAF) {human (Homo sapiens)}
qpdainapvtccynftnrkisvqrlasyrritsskcpkeavifktivakeicadpkqkwv
qdsmdhldkqtqtpkt
>d1dona_ 4.7.1.1.8 Monocyte chemoattractant protein-1 (MCP-1, MCAF) {human (Homo sapiens)}
qpdainapvtccynftnrkisvqrlasyrritsskcpkeavifktivakeicadpkqkwv
qdsmdhldkqtqtpkt
>d1donb_ 4.7.1.1.8 Monocyte chemoattractant protein-1 (MCP-1, MCAF) {human (Homo sapiens)}
qpdainapvtccynftnrkisvqrlasyrritsskcpkeavifktivakeicadpkqkwv
qdsmdhldkqtqtpkt
>d1dora_ 3.1.7.1.1 Dihydroorotate dehydrogenase A {(Lactococcus lactis)}
mlnttfanakfanpfmnasgvhcmtiedleelkasqagayitksstlekregnplpryvd
lelgsinsmglpnlgfdyyldyvlknqkenaqegpiffsiagmsaaeniamlkkiqesdf
sgitelnlscpnvpgkpqlaydfeatekllkevftfftkplgvklppyfdlvhfdimaei
lnqfpltyvnsvnsignglfidpeaesvvikpkdgfggiggayikptalanvrafytrlk
peiqiigtggietgqdafehllcgatmlqigtalhkegpaifdriikeleeimnqkgyqs
iadfhgklksl
>d1dorb_ 3.1.7.1.1 Dihydroorotate dehydrogenase A {(Lactococcus lactis)}
mlnttfanakfanpfmnasgvhcmtiedleelkasqagayitksstlekregnplpryvd
lelgsinsmglpnlgfdyyldyvlknqkenaqegpiffsiagmsaaeniamlkkiqesdf
sgitelnlscpnvpgkpqlaydfeatekllkevftfftkplgvklppyfdlvhfdimaei
lnqfpltyvnsvnsignglfidpeaesvvikpkdgfggiggayikptalanvrafytrlk
peiqiigtggietgqdafehllcgatmlqigtalhkegpaifdriikeleeimnqkgyqs
iadfhgklksl
>d1dosa_ 3.1.4.1.1 Fructose-bisphosphate aldolase {(Escherichia coli)}
skifdfvkpgvitgddvqkvfqvakennfalpavncvgtdsinavletaakvkapvivqf
snggasfiagkgvksdvpqgaailgaisgahhvhqmaehygvpvilhtdhcakkllpwid
glldagekhfaatgkplfsshmidlseeslqenieicskylermskigmtleielgctgg
eedgvdnshmdasalytqpedvdyaytelskisprftiaasfgnvhgvykagnvvltpti
lrdsqeyvskkhnlphnslnfvfhggsgstaqeikdsvsygvvkmnidtdtqwatwegvl
nyykaneaylqgqlgnpkgedqpnkkyydprvwlragqtsmiarlekafqelnaidvl
>d1dosb_ 3.1.4.1.1 Fructose-bisphosphate aldolase {(Escherichia coli)}
skifdfvkpgvitgddvqkvfqvakennfalpavncvgtdsinavletaakvkapvivqf
snggasfiagkgvksdvpqgaailgaisgahhvhqmaehygvpvilhtdhcakkllpwid
glldagekhfaatgkplfsshmidlseeslqenieicskylermskigmtleielgctgg
eedgvdnshmdasalytqpedvdyaytelskisprftiaasfgnvhgvykagnvvltpti
lrdsqeyvskkhnlphnslnfvfhggsgstaqeikdsvsygvvkmnidtdtqwatwegvl
nyykaneaylqgqlgnpkgedqpnkkyydprvwlragqtsmiarlekafqelnaidvl
>d1dot_1 3.82.1.2.3 (1-334) Ovotransferrin {Duck (Anas platyrhynchos)}
appkttvrwctissaeekkcnslkdhmqqervtlscvqkatyldcikaisnneadaisld
ggqvfeaglapyklkpiaaevyersggsttsyyavavvkkgtdfmikdlrgktschtglg
rsagwnipigtlihrediewegiesgiseqavakffsascvpgatieqklcrqckgdakt
kclrngpysgysgafqclkdgkgdvafvkhttvqenapeekdeyellcldgsrqpvdsyk
tcnwarvaahavvarddskiddiwsflgmqayslgvdttsdfhlfgppgkkdpvlkdllf
kdsaimlkrvpelmdsqlylgfeyysaiqslrkd
>d1dot_2 3.82.1.2.3 (335-686) Ovotransferrin {Duck (Anas platyrhynchos)}
qltvgprenkiqwcavgkdekskcdrwsvvsngevectilddnkdcivkitkgeadaisl
dggfvytagvcglvpvvgesyedetqcskdeeqpayyfavavvkkssaitwnnlqgkksc
htavgrtagwnipmglihnktgscdfddyfsegcapgsppnsrlcklcqgsgenllekcv
asshekyygytgalrclveqgdvafikhstvgenvsgsnkddwakgltrddfellctngk
raktmdyktchlakvpthavvarpekankirellegqeklfglhgtekerfmmfqsqtkd
llfkaltkclvklrqgitykeflgdeyyasvaslntcnpsdllqvctfledk
>d1dox__ 4.11.5.1.4 2Fe-2S ferredoxin {(Synechocystis sp.)  PCC 6803}
asytvklitpdgessiecsddtyildaaeeagldlpyscragacstcagkitagsvdqsd
qsfldddqieagyvltcvayptsdctiethkeedly
>d1doy__ 4.11.5.1.4 2Fe-2S ferredoxin {(Synechocystis sp.)  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__ 3.82.1.1.8 Dipeptide-binding protein {(Escherichia coli)}
ktlvycsegspegfnpqlfisgttydassvplynrlvefkigttevipglaekwevsedg
ktytfhlrkgvkwhdnkefkptrelnaddvvfsfdrqknaqnpyhkvsggsyeyfegmgl
pelisevkkvddntvqfvltrpeapfladlamdfasilskeyadammkagtpekldlnpi
gtgpfqlqqyqkdsrirykafdgywgtkpqidtlvfsitpdasvryaklqknecqvmpyp
npadiarmkqdksinlmempglnvgylsynvqkkplddvkvrqaltyavnkdaiikavyq
gagvsaknlipptmwgynddvqdytydpekakallkeaglekgfsidlwampvqrpynpn
arrmaemiqadwakvgvqakivtyewgeylkrakdgehqtvmmgwtgdngdpdnffatef
scaaseqgsnyskwcykpfedliqparatddhnkrvelykqaqvvmhdqapaliiahstv
fepvrkevkgyvvdplgkhhfenvsie
>d1dpga1 3.22.1.3.12 (1-181,413-426) glucose 6-phosphate dehydrogenase, N-terminal domain {(Leuconostoc mesenteroides)}
vseiktlvtffggtgdlakrklypsvfnlykkgylqkhfaivgtarqalnddefkqlvrd
cikdftddqaqaeafiehfsyrahdvtdaasyavlkeaieeaadkfdidgnrifymsvap
rffgtiakylkseglladtgynrlmiekpfgtsydtaaelqndlenafddnqlfridhyl
gXepyermihdtmngd
>d1dpga2 4.42.1.3.2 (182-412,427-485) glucose 6-phosphate dehydrogenase {(Leuconostoc mesenteroides)}
kemvqniaalrfgnpifdaawnkdyiknvqvtlsevlgveeragyydtagalldmiqnht
mqivgwlamekpesftdkdiraaknaafnalkiydeaevnkyfvraqygagdsadfkpyl
eeldvpadsknntfiagelqfdlprwegvpfyvrsgkrlaakqtrvdivfkagtfnfgse
qeaqeavlsiiidpkgaielklnaksvedafntrtidlgwtvsdedkkntpXgsnfadwn
gvsiawkfvdaisavytadkapletyksgsmgpeasdkllaangdawvfkg
>d1dpgb1 3.22.1.3.12 (1-181,413-426) glucose 6-phosphate dehydrogenase, N-terminal domain {(Leuconostoc mesenteroides)}
vseiktlvtffggtgdlakrklypsvfnlykkgylqkhfaivgtarqalnddefkqlvrd
cikdftddqaqaeafiehfsyrahdvtdaasyavlkeaieeaadkfdidgnrifymsvap
rffgtiakylkseglladtgynrlmiekpfgtsydtaaelqndlenafddnqlfridhyl
gXepyermihdtmngd
>d1dpgb2 4.42.1.3.2 (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 3.47.3.4.1 (326-518) Exonuclease domain of DNA polymerase {(Escherichia coli)}
sydnyvtildeetlkawiaklekapvfafdtetdsldnisanlvglsfaiepgvaayipv
ahdyldapdqisreralellkplledekalkvgqnlkydrgilanygielrgiafdtmle
syilnsvagrhdmdslaerwlkhktitfeeiagkgknqltfnqialeeagryaaedadvt
lqlhlkmwpdlqk
>d1dpi_2 5.9.1.1.1 (519-928) DNA polymerase I (Klenow fragment) {(Escherichia coli)}
hkgplnvfeniemplvpvlsrierngvkidpkvlhnhseeltlrlaelekkaheiageef
nlsstkqlqtilfekqgikplkktpggapstseevleelaldyplpkvileyrglaklks
tytdklplminpktgrvhtsyhqavtatgrlsstdpnlqnipvrneegrrirqafiaped
yvivsadysqielrimahlsrdkglltafaegkdihrataaevfglpletvtseqrrsak
ainfgliygmsafglarqlniprkeaqkymdlyferypgvleymertraqakeqgyvetl
dgrrlylpdikssngarraaaeraainapmqgtaadiikramiavdawlqaeqprvrmim
qvhdelvfevhkddvdavakqihqlmenctrldvpllvevgsgenwdqah
>d1dpma_ 3.1.2.3.1 Phosphotriesterase {(Pseudomonas diminuta)}
arintvrgpitiseagftlthehicgssagflrawpeffgsrkalaekavrglrraraag
vrtivdvstfdigrdvsllaevsraadvhivaatglwfdpplsmrlrsveeltqfflrei
qygiedtgiragiikvattgkatpfqelvlkaaaraslatgvpvtthtaasqrdgeqqaa
ifeseglspsrvcighsddtddlsyltalaargyligldhiphsaiglednasasallgi
rswqtrallikalidqgymkqilvsndwlfgfssyvtnimdvmdrvnpdgmafiplrvip
flrekgvpqetlagitvtnparflsptlr
>d1dpmb_ 3.1.2.3.1 Phosphotriesterase {(Pseudomonas diminuta)}
arintvrgpitiseagftlthehicgssagflrawpeffgsrkalaekavrglrraraag
vrtivdvstfdigrdvsllaevsraadvhivaatglwfdpplsmrlrsveeltqfflrei
qygiedtgiragiikvattgkatpfqelvlkaaaraslatgvpvtthtaasqrdgeqqaa
ifeseglspsrvcighsddtddlsyltalaargyligldhiphsaiglednasasallgi
rswqtrallikalidqgymkqilvsndwlfgfssyvtnimdvmdrvnpdgmafiplrvip
flrekgvpqetlagitvtnparflsptlr
>d1dpo__ 2.35.1.2.3 Trypsin(ogen) {rat (Rattus rattus)}
ivggytcqensvpyqvslnsgyhfcggslindqwvvsaahcyksriqvrlgehninvleg
neqfvnaakiikhpnfdrktlnndimliklsspvklnarvatvalpsscapagtqclisg
wgntlssgvnepdllqcldapllpqadceasypgkitdnmvcvgfleggkdscqgdcggp
vvcngelqgivswgygcalpdnpgvytkvcnyvdwiqdtiaan
>d1dppa_ 3.82.1.1.8 Dipeptide-binding protein {(Escherichia coli)}
ktlvycsegspegfnpqlftsgttydassvplynrlvefkigttevipglaekwevsedg
ktytfhlrkgvkwhdnkefkptrelnaddvvfsfdrqknaqnpyhkvsggsyeyfegmgl
pelisevkkvddntvqfvltrpeapfladlamdfasilskeyadammkagtpekldlnpi
gtgpfqlqqyqkdsrirykafdgywgtkpqidtlvfsitpdasvryaklqknecqvmpyp
npadiarmkqdksinlmempglnvgylsynvqkkplddvkvrqaltyavnkdaiikavyq
gagvsaknlipptmwgynddvqdytydpekakallkeaglekgfsidlwampvqrpynpn
arrmaemiqadwakvgvqakivtyewgeylkrakdgehqtvmmgwtgdngdpdnffatlf
scaaseqgsnyskwcykpfedliqparatddhnkrvelykqaqvvmhdqapaliiahstv
fepvrkevkgyvvdplgkhhfenvsie
>d1dppc_ 3.82.1.1.8 Dipeptide-binding protein {(Escherichia coli)}
ktlvycsegspegfnpqlftsgttydassvplynrlvefkigttevipglaekwevsedg
ktytfhlrkgvkwhdnkefkptrelnaddvvfsfdrqknaqnpyhkvsggsyeyfegmgl
pelisevkkvddntvqfvltrpeapfladlamdfasilskeyadammkagtpekldlnpi
gtgpfqlqqyqkdsrirykafdgywgtkpqidtlvfsitpdasvryaklqknecqvmpyp
npadiarmkqdksinlmempglnvgylsynvqkkplddvkvrqaltyavnkdaiikavyq
gagvsaknlipptmwgynddvqdytydpekakallkeaglekgfsidlwampvqrpynpn
arrmaemiqadwakvgvqakivtyewgeylkrakdgehqtvmmgwtgdngdpdnffatlf
scaaseqgsnyskwcykpfedliqparatddhnkrvelykqaqvvmhdqapaliiahstv
fepvrkevkgyvvdplgkhhfenvsie
>d1dppe_ 3.82.1.1.8 Dipeptide-binding protein {(Escherichia coli)}
ktlvycsegspegfnpqlftsgttydassvplynrlvefkigttevipglaekwevsedg
ktytfhlrkgvkwhdnkefkptrelnaddvvfsfdrqknaqnpyhkvsggsyeyfegmgl
pelisevkkvddntvqfvltrpeapfladlamdfasilskeyadammkagtpekldlnpi
gtgpfqlqqyqkdsrirykafdgywgtkpqidtlvfsitpdasvryaklqknecqvmpyp
npadiarmkqdksinlmempglnvgylsynvqkkplddvkvrqaltyavnkdaiikavyq
gagvsaknlipptmwgynddvqdytydpekakallkeaglekgfsidlwampvqrpynpn
arrmaemiqadwakvgvqakivtyewgeylkrakdgehqtvmmgwtgdngdpdnffatlf
scaaseqgsnyskwcykpfedliqparatddhnkrvelykqaqvvmhdqapaliiahstv
fepvrkevkgyvvdplgkhhfenvsie
>d1dppg_ 3.82.1.1.8 Dipeptide-binding protein {(Escherichia coli)}
ktlvycsegspegfnpqlftsgttydassvplynrlvefkigttevipglaekwevsedg
ktytfhlrkgvkwhdnkefkptrelnaddvvfsfdrqknaqnpyhkvsggsyeyfegmgl
pelisevkkvddntvqfvltrpeapfladlamdfasilskeyadammkagtpekldlnpi
gtgpfqlqqyqkdsrirykafdgywgtkpqidtlvfsitpdasvryaklqknecqvmpyp
npadiarmkqdksinlmempglnvgylsynvqkkplddvkvrqaltyavnkdaiikavyq
gagvsaknlipptmwgynddvqdytydpekakallkeaglekgfsidlwampvqrpynpn
arrmaemiqadwakvgvqakivtyewgeylkrakdgehqtvmmgwtgdngdpdnffatlf
scaaseqgsnyskwcykpfedliqparatddhnkrvelykqaqvvmhdqapaliiahstv
fepvrkevkgyvvdplgkhhfenvsie
>d1dpra1 1.4.3.15.1 (3-64) Diphtheria toxin repressor (DtxR) {(Corynebacterium diphtheriae)}
dlvdttemylrtiyeleeegvtplrariaerleqsgptvsqtvarmerdglvvvasdrsl
qm
>d1dpra2 1.66.1.1.1 (65-136) Diphtheria toxin repressor (DtxR) dimerization domain {(Corynebacterium diphtheriae)}
tptgrtlatavmrkhrlaerlltdiigldinkvhdeacrwehvmsdeverrlvkvlkdvs
rspfgnpipgld
>d1dprb1 1.4.3.15.1 (3-64) Diphtheria toxin repressor (DtxR) {(Corynebacterium diphtheriae)}
dlvdttemylrtiyeleeegvtplrariaerleqsgptvsqtvarmerdglvvvasdrsl
qm
>d1dprb2 1.66.1.1.1 (65-136) Diphtheria toxin repressor (DtxR) dimerization domain {(Corynebacterium diphtheriae)}
tptgrtlatavmrkhrlaerlltdiigldinkvhdeacrwehvmsdeverrlvkvlkdvs
rspfgnpipgld
>d1dr1__ 3.60.1.1.4 Dihydrofolate reductases, eukaryotic type {chicken (Gallus gallus)}
vrslnsivavcqnmgigkdgnlpwpplrneykyfqrmtstshvegkqnavimgkktwfsi
peknrplkdrinivlsrelkeapkgahylskslddalalldspelkskvdmvwivggtav
ykaamekpinhrlfvtrilhefesdtffpeidykdfkllteypgvpadiqeedgiqykfe
vyqksv
>d1dr2__ 3.60.1.1.4 Dihydrofolate reductases, eukaryotic type {chicken (Gallus gallus)}
vrslnsivavcqnmgigkdgnlpwpplrneykyfqrmtstshvegkqnavimgkktwfsi
peknrplkdrinivlsrelkeapkgahylskslddalalldspelkskvdmvwivggtav
ykaamekpinhrlfvtrilhefesdtffpeidykdfkllteypgvpadiqeedgiqykfe
vyqksv
>d1dr3__ 3.60.1.1.4 Dihydrofolate reductases, eukaryotic type {chicken (Gallus gallus)}
vrslnsivavcqnmgigkdgnlpwpplrneykyfqrmtstshvegkqnavimgkktwfsi
peknrplkdrinivlsrelkeapkgahylskslddalalldspelkskvdmvwivggtav
ykaamekpinhrlfvtrilhefesdtffpeidykdfkllteypgvpadiqeedgiqykfe
vyqksv
>d1dr4__ 3.60.1.1.4 Dihydrofolate reductases, eukaryotic type {chicken (Gallus gallus)}
vrslnsivavcqnmgigkdgnlpwpplrneykyfqrmtstshvegkqnavimgkktwfsi
peknrplkdrinivlsrelkeapkgahylskslddalalldspelkskvdmvwivggtav
ykaamekpinhrlfvtrilhefesdtffpeidykdfkllteypgvpadiqeedgiqykfe
vyqksv
>d1dr5__ 3.60.1.1.4 Dihydrofolate reductases, eukaryotic type {chicken (Gallus gallus)}
vrslnsivavcqnmgigkdgnlpwpplrneykyfqrmtstshvegkqnavimgkktwfsi
peknrplkdrinivlsrelkeapkgahylskslddalalldspelkskvdmvwivggtav
ykaamekpinhrlfvtrilhefesdtffpeidykdfkllteypgvpadiqeedgiqykfe
vyqksv
>d1dr6__ 3.60.1.1.4 Dihydrofolate reductases, eukaryotic type {chicken (Gallus gallus)}
vrslnsivavcqnmgigkdgnlpwpplrneykyfqrmtstshvegkqnavimgkktwfsi
peknrplkdrinivlsrelkeapkgahylskslddalalldspelkskvdmvwivggtav
ykaamekpinhrlfvtrilhefesdtffpeidykdfkllteypgvpadiqeedgiqykfe
vyqksv
>d1dr7__ 3.60.1.1.4 Dihydrofolate reductases, eukaryotic type {chicken (Gallus gallus)}
vrslnsivavcqnmgigkdgnlpwpplrneykyfqrmtstshvegkqnavimgkktwfsi
peknrplkdrinivlsrelkeapkgahylskslddalalldspelkskvdmvwivggtav
ykaamekpinhrlfvtrilhefesdtffpeidykdfkllteypgvpadiqeedgiqykfe
vyqksv
>d1draa_ 3.60.1.1.1 Dihydrofolate reductase, prokaryotic type {(Escherichia coli)}
misliaalavdrvigmenampwnlpaelawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1drab_ 3.60.1.1.1 Dihydrofolate reductase, prokaryotic type {(Escherichia coli)}
misliaalavdrvigmenampwnlpaelawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1drba_ 3.60.1.1.1 Dihydrofolate reductase, prokaryotic type {(Escherichia coli)}
misliaalavdrvigmenampwnlpaclawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1drbb_ 3.60.1.1.1 Dihydrofolate reductase, prokaryotic type {(Escherichia coli)}
misliaalavdrvigmenampwnlpaclawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1dre__ 3.60.1.1.1 Dihydrofolate reductase, prokaryotic type {(Escherichia coli)}
misliaalavdrvigmenampwnlpadlawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1drf__ 3.60.1.1.5 Dihydrofolate reductases, eukaryotic type {human (Homo sapiens)}
vgslncivavsqnmgigkngdlpwpplrnefryfqrmtttssvegkqnlvimgkktwfsi
peknrplkgrinlvlsrelkeppqgahflsrslddalklteqpelankvdmvwivggssv
ykeamnhpghlklfvtrimqdfesdtffpeidlekykllpeypgvlsdvqeekgikykfe
vyeknd
>d1drh__ 3.60.1.1.1 Dihydrofolate reductase, prokaryotic type {(Escherichia coli)}
misliaalavdrvigmenampwnlpadlawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1drj__ 3.81.1.1.1 D-ribose-binding protein {(Escherichia coli), strain k-12}
kdtialvvstlnnpffvslkdgaqkeadklgynlvvldsqnnpakelanvqdltvrgtki
llinptdsdavgnavkmanqanipvitldrqatkgevvshiasdnvlggkiagdyiakka
gegakvielqgiartsaarergegfqqavaahkfnvlasqpadfdrikglnvmqnlltah
pdvqavfaqndemalgalralqtagksdvmvvgfdgtpdgekavndgklaatiaqlpdqi
gakgvetadkvlkgekvqakypvdlklvvkq
>d1drk__ 3.81.1.1.1 D-ribose-binding protein {(Escherichia coli), strain k-12}
kdtialvvstlnnpffvslkdgaqkeadklgynlvvldsqnnpakelanvqdltvrgtki
llinptdsdavgnavkmanqanipvitldrqatkgevvshiasdnvlggkiagdyiakka
gegakvielqgtaatsaarergegfqqavaahkfnvlasqpadfdrikglnvmqnlltah
pdvqavfaqndemalgalralqtagksdvmvvgfdgtpdgekavndgklaatiaqlpdqi
gakgvetadkvlkgekvqakypvdlklvvkq
>d1dro__ 2.41.1.1.3 beta-spectrin {fruit fly (Drosophila melanogaster)}
gsgtgageghegyvtrkhewdsttkkasnrswdkvymaakagrisfykdqkgyksnpelt
frgepsydlqnaaieiasdytkkkhvlrvklangalfllqahddtemsqwvtslkaqsds
ta
>d1drs__ 7.6.1.2.1 Dendroaspin {(Dendroaspis jamesoni kaimose)}
ricynhlgtkppttetcqedscykniwtfdniirrgcgcftprgdmpgpyccesdkcnl
>d1dru_1 3.22.1.3.10 (4-130,241-273) Dihydrodipicolinate reductase {(Escherichia coli)}
anirvaiagaggrmgrqliqaalalegvqlgaaleregssllgsdagelagagktgvtvq
ssldavkddfdvfidftrpegtlnhlafcrqhgkgmvigttgfdeagkqairdaaadiai
vfaanfsXmtfangavrsalwlsgkesglfdmrdvldlnnl
>d1dru_2 4.42.1.2.2 (131-240) Dihydrodipicolinate reductase {(Escherichia coli)}
vgvnvmlkllekaakvmgdytdieiieahhrhkvdapsgtalamgeaiahaldkdlkdca
vysreghtgervpgtigfatvragdivgehtamfadigerleithkassr
>d1drv_1 3.22.1.3.10 (4-130,241-273) Dihydrodipicolinate reductase {(Escherichia coli)}
anirvaiagaggrmgrqliqaalalegvqlgaaleregssllgsdagelagagktgvtvq
ssldavkddfdvfidftrpegtlnhlafcrqhgkgmvigttgfdeagkqairdaaadiai
vfaanfsXmtfangavrsalwlsgkesglfdmrdvldlnnl
>d1drv_2 4.42.1.2.2 (131-240) Dihydrodipicolinate reductase {(Escherichia coli)}
vgvnvmlkllekaakvmgdytdieiieahhrhkvdapsgtalamgeaiahaldkdlkdca
vysreghtgervpgtigfatvragdivgehtamfadigerleithkassr
>d1drw_1 3.22.1.3.10 (2-130,241-273) Dihydrodipicolinate reductase {(Escherichia coli)}
hdanirvaiagaggrmgrqliqaalalegvqlgaaleregssllgsdagelagagktgvt
vqssldavkddfdvfidftrpegtlnhlafcrqhgkgmvigttgfdeagkqairdaaadi
aivfaanfsXmtfangavrsalwlsgkesglfdmrdvldlnnl
>d1drw_2 4.42.1.2.2 (131-240) Dihydrodipicolinate reductase {(Escherichia coli)}
vgvnvmlkllekaakvmgdytdieiieahhrhkvdapsgtalamgeaiahaldkdlkdca
vysreghtgervpgtigfatvragdivgehtamfadigerleithkassr
>d1dsba1 1.42.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {(Escherichia coli)}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1dsba2 3.38.1.3.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) {(Escherichia coli)}
aqyedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsek
>d1dsbb1 1.42.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {(Escherichia coli)}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1dsbb2 3.38.1.3.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) {(Escherichia coli)}
aqyedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsek
>d1dsfh_ 2.1.1.1.101 Immunoglobulin (variable domains of L and H chains) {Anticancer Fv B1}
qlvesggglvkpggslklscaasgfifsdnymywvrqtpekclewvatisdggtyidysd
svkgrftisrdnaknnlylqmsslrsedtgmyycgrspiyydyapftywgqgtlvtvsa
>d1dsfl_ 2.1.1.1.101 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_ 1.1.1.1.25 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_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1dsl__ 2.9.1.1.1 gamma-Crystallin {bovine (Bos taurus) isoform II (B)}
tfrmriyerddfrgqmseitddcpslqdrfhltevhslnvlegswvlyempsyrgrqyll
rpgeyrryldwgamnakvgslrrvmdfy
>d1dsn__ 3.82.1.2.1 Lactoferrin {human (Homo sapiens)}
rrrsvqwcavsqpeatkcfqwqrnmrrvrgppvscikrdspiqciqaiaenradavtlsg
gfiyeaglapyklrpvaaevygterqprthyyavavvkkggsfqlnelqglkschtglrr
tagwnvpigtlrpflnwtgppepieaavarffsascvpgadkgqfpnlcrlcagtgenkc
afssqepyfsysgafkclrdgagdvafirestvfedlsdeaerdeyellcpdntrkpvdk
fkdchlarvpshavvarsvngkedaiwnllrqaqekfgkdkspkfqlfgspsgqkdllfk
dsaigfsrvpprids
>d1dst__ 2.35.1.2.23 Factor D {Human (Homo sapiens)}
ilggreaeaharpymasvqlngahlcggvlvaeqwvlsaahcledaadgkvqvllgahsl
sqpepskrlydvlravphpdyqpdtidhdllllqlsekatlgpavrplpwqrvdrdvapg
tlcdvagwgivnhagrrpdslqhvllpvldratcnrrthhdgaiterlmcaesnrrdsck
gdsggplvcggvlegvvswgsrvcgnrkkpgiytrvasyaawidsvla
>d1dsua_ 2.35.1.2.23 Factor D {Human (Homo sapiens)}
ilggreaeaharpymasvqlngahlcggvlvaeqwvlsaahcledaadgkvqvllgahsl
sqpepskrlydvlravphpdsqpdtidhdllllqlsekatlgpavrplpwqrvdrdvapg
tlcdvagwgivnhagrrpdslqhvllpvldratcnrrthhdgaiterlmcaesnrrdsck
gdsggplvcggvlegvvtsgsrvcgnrkkpgiytrvasyaawidsvla
>d1dsub_ 2.35.1.2.23 Factor D {Human (Homo sapiens)}
ilggreaeaharpymasvqlngahlcggvlvaeqwvlsaahcledaadgkvqvllgahsl
sqpepskrlydvlravphpdsqpdtidhdllllqlsekatlgpavrplpwqrvdrdvapg
tlcdvagwgivnhagrrpdslqhvllpvldratcnrrthhdgaiterlmcaesnrrdsck
gdsggplvcggvlegvvtsgsrvcgnrkkpgiytrvasyaawidsvla
>d1dtha_ 4.52.1.5.2 Snake venom metalloprotease {Atrolysin C: Western diamonback rattlesnake (Crotalus atrox)}
qnlpqryielvvvadhrvfmkynsdlntirtrvheivnfingfyrslnihvsltdleiws
nedqiniqsassdtlnafaewretdllnrkshdnaqlltaieldeetlglaplgtmcdpk
lsigivqdhspinllmgvtmahelghnlgmehdgkdclrgaslcimrpgltkgrsyefsd
dsmhyyerflkqykpqcilnkp
>d1dthb_ 4.52.1.5.2 Snake venom metalloprotease {Atrolysin C: Western diamonback rattlesnake (Crotalus atrox)}
qnlpqryielvvvadhrvfmkynsdlntirtrvheivnfingfyrslnihvsltdleiws
nedqiniqsassdtlnafaewretdllnrkshdnaqlltaieldeetlglaplgtmcdpk
lsigivqdhspinllmgvtmahelghnlgmehdgkdclrgaslcimrpgltkgrsyefsd
dsmhyyerflkqykpqcilnkp
>d1dtk__ 7.7.1.1.8 Dendrotoxin K {black mamba (Dendroaspis polylepis polylepis)}
aakycklplrigpckrkipsfyykwkakqclpfdysgcggnanrfktieecrrtcvg
>d1dtn_1 3.1.6.2.2 (133-359) Mandelate racemase {(Pseudomonas putida)}
pvqaydshsldgvklateravtaaelgfravktkigypaldqdlavvrsirqavgddfgi
mvdynqsldvpaaikrsqalqqegvtwieeptlqhdyeghqriqsklnvpvqmgenwlgp
eemfkalsigacrlampdamkiggvtgwirasalaqqfgipmsshlfqeisahllaatpt
ahwlqrldlagsvieptltfeggnavipdlpgvgiiwrekeigkylv
>d1dtn_2 4.32.1.1.4 (3-132) Mandelate racemase {(Pseudomonas putida)}
evlitglrtravnvplaypvhtavgtvgtaplvlidlatsagvvghsylfaytpvalksl
kqllddmaamivneplapvsleamlakrfclagytglirmaaagidmaawdalgkvhetp
lvkllganar
>d1dtp__ 4.103.1.1.3 Diphtheria toxin, N-terminal domain {(Corynebacterium diphtheriae)}
gaddvvdssksfvmenfssyhgtkpgyvdsiqkgiqkpksgtqgnydddwkgfystdnky
daagysvdnenplsgkaggvvkvtypgltkvlalkvdnaetikkelglslteplmeqvgt
eefikrfgdgasrvvlslpfaegsssveyinnweqakalsveleinfetrgkrgqdamye
ymaqacagnr
>d1dts__ 3.29.1.6.1 Dethiobiotin synthetase {(Escherichia coli)}
skryfvtgtdtevgktvascallqaakaagyrtagykpvasgsektpeglrnsdalalqr
nsslqldyatvnpytfaeptsphiisaqegrpieslvmsaglraleqqadwvlvegaggw
ftplsdtftfadwvtqeqlpvilvvgvklgcinhamltaqviqhagltlagwvandvtpp
gkrhaeymttltrmipapllgeipwlaeaatgkyinlall
>d1dtx__ 7.7.1.1.5 alpha-Dendrotoxin {green mamba (Dendroaspis angusticeps)}
xprrklcilhrnpgrcydkipafyynqkkkqcerfdwsgcggnsnrfktieecrrtcig
>d1duba_ 3.9.1.2.2 Enoyl-CoA hydratase {Rat (Rattus norvegicus)}
anfqyiitekkgknssvgliqlnrpkalnalcnglieelnqaletfeedpavgaivltgg
ekafaagadikemqnrtfqdcysgkflshwdhitrikkpviaavngyalgggcelammcd
iiyagekaqfgqpeillgtipgaggtqrltravgkslamemvltgdrisaqdakqaglvs
kifpvetlveeaiqcaekiannskiivamakesvnaafemtltegnklekklfystfatd
drregmsafvekrkanfkdh
>d1dubb_ 3.9.1.2.2 Enoyl-CoA hydratase {Rat (Rattus norvegicus)}
nfqyiitekkgknssvgliqlnrpkalnalcnglieelnqaletfeedpavgaivltgge
kafaagadikemqnrtfqdcysgkflshwdhitrikkpviaavngyalgggcelammcdi
iyagekaqfgqpeillgtipgaggtqrltravgkslamemvltgdrisaqdakqaglvsk
ifpvetlveeaiqcaekiannskiivamakesvnaafemtltegnklekklfystfatdd
rregmsafvekrkanfkdh
>d1dubc_ 3.9.1.2.2 Enoyl-CoA hydratase {Rat (Rattus norvegicus)}
nfqyiitekkgknssvgliqlnrpkalnalcnglieelnqaletfeedpavgaivltgge
kafaagadikemqnrtfqdcysgkflshwdhitrikkpviaavngyalgggcelammcdi
iyagekaqfgqpeillgtipgaggtqrltravgkslamemvltgdrisaqdakqaglvsk
ifpvetlveeaiqcaekiannskiivamakesvnaafemtltegnklekklfystfatdd
rregmsafvekrkanfkdh
>d1dubd_ 3.9.1.2.2 Enoyl-CoA hydratase {Rat (Rattus norvegicus)}
anfqyiitekkgknssvgliqlnrpkalnalcnglieelnqaletfeedpavgaivltgg
ekafaagadikemqnrtfqdcysgkflshwdhitrikkpviaavngyalgggcelammcd
iiyagekaqfgqpeillgtipgaggtqrltravgkslamemvltgdrisaqdakqaglvs
kifpvetlveeaiqcaekiannskiivamakesvnaafemtltegnklekklfystfatd
drregmsafvekrkanfkdh
>d1dube_ 3.9.1.2.2 Enoyl-CoA hydratase {Rat (Rattus norvegicus)}
anfqyiitekkgknssvgliqlnrpkalnalcnglieelnqaletfeedpavgaivltgg
ekafaagadikemqnrtfqdcysgkflshwdhitrikkpviaavngyalgggcelammcd
iiyagekaqfgqpeillgtipgaggtqrltravgkslamemvltgdrisaqdakqaglvs
kifpvetlveeaiqcaekiannskiivamakesvnaafemtltegnklekklfystfatd
drregmsafvekrkanfkdh
>d1dubf_ 3.9.1.2.2 Enoyl-CoA hydratase {Rat (Rattus norvegicus)}
nfqyiitekkgknssvgliqlnrpkalnalcnglieelnqaletfeedpavgaivltgge
kafaagadikemqnrtfqdcysgkflshwdhitrikkpviaavngyalgggcelammcdi
iyagekaqfgqpeillgtipgaggtqrltravgkslamemvltgdrisaqdakqaglvsk
ifpvetlveeaiqcaekiannskiivamakesvnaafemtltegnklekklfystfatdd
rregmsafvekrkanfkdh
>d1duc__ 2.66.3.1.3 Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) {(Equine infectious anemia virus)}
mlayqgtqikekrdedagfdlcvpydimipvsdtkiiptdvkiqvppnsfgwvtgkssma
kqgllinggiidegytgeiqvictnigksnikliegqkfaqliilqhhsnsrqpwden
>d1dud__ 2.66.3.1.1 Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) {(Escherichia coli)}
mmkkidvkildprvgkefplptyatsgsagldlraclndavelapgdttlvptglaihia
dpslaammlprsglghkhgivlgnlvglidsdyqgqlmisvwnrgqdsftiqpgeriaqm
ifvpvvqaefnlvedf
>d1dun__ 2.66.3.1.3 Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) {(Equine infectious anemia virus)}
mlayqgtqikekrdedagfdlcvpydimipvsdtkiiptdvkiqvppnsfgwvtgkssma
kqgllinggiidegytgeiqvictnigksnikliegqkfaqliilqhhsnsrqpwdenki
>d1dupa_ 2.66.3.1.1 Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) {(Escherichia coli)}
mmkkidvkildprvgkefplptyatsgsagldlraclndavelapgdttlvptglaihia
dpslaammlprsglghkhgivlgnlvglidsdyqgqlmisvwnrgqdsftiqpgeriaqm
ifvpvvqaefnlvedf
>d1duta_ 2.66.3.1.2 Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) {FIV (Feline immunodeficiency virus)}
miiegdgildkrsedagydllaakeihllpgevkviptgvklmlpkgywgliigkssigs
kgldvlggvidegyrgeigviminvsrksitlmerqkiaqliilpckhevleqgkvv
>d1dutb_ 2.66.3.1.2 Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) {FIV (Feline immunodeficiency virus)}
miiegdgildkrsedagydllaakeihllpgevkviptgvklmlpkgywgliigkssigs
kgldvlggvidegyrgeigviminvsrksitlmerqkiaqliilpckhevleqgkvv
>d1dvc__ 4.13.1.2.2 Cystatin A (stefin A) {human (Homo sapiens)}
mipgglseakpatpeiqeivdkvkpqleektnetygkleavqyktqvvagtnyyikvrag
dnkymhlkvfkslpgqnedlvltgyqvdknkddeltgf
>d1dvd__ 4.13.1.2.2 Cystatin A (stefin A) {human (Homo sapiens)}
mipgglseakpatpeiqeivdkvkpqleektnetygkleavqyktqvvagtnyyikvrag
dnkymhlkvfkslpgqnedlvltgyqvdknkddeltgf
>d1dvfa_ 2.1.1.1.39 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
divltqspaslsasvgetvtitcrasgnihnylawyqqkqgkspqllvyytttladgvps
rfsgsgsgtqyslkinslqpedfgsyycqhfwstprtfgggtkleik
>d1dvfb_ 2.1.1.1.39 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
qvqlqesgpglvapsqslsitctvsgfsltgygvnwvrqppgkglewlgmiwgdgntdyn
salksrlsiskdnsksqvflkmnslhtddtaryycarerdyrldywgqgttltvss
>d1dvfc_ 2.1.1.1.70 Immunoglobulin (variable domains of L and H chains) {Fv E5.2 (mouse), kappa L chain}
diqltqspsslsaslgdrvtiscrasqdisnylnwyqqkpdgtvklliyytsrlhsgvps
rfsgsgsgtdysltisnleqediatyfcqqgntlpwtfgggtkleik
>d1dvfd_ 2.1.1.1.70 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_ 1.37.1.6.2 Calpain domain VI {Rat (Rattus norvegicus)}
eeerqfrklfvqlagddmevsatelmnilnkvvtrhpdlktdgfgidtsrsmvavmdsdt
tgklgfeefkylwnnikkwqgiykrfdtdrsgtigsnelpgafeaagfhlnqhiysmiir
rysdetgnmdfdnfisclvrldamfrafrsldkngtgqiqvniqewlqltmys
>d1dvib_ 1.37.1.6.2 Calpain domain VI {Rat (Rattus norvegicus)}
eeerqfrklfvqlagddmevsatelmnilnkvvtrhpdlktdgfgidtsrsmvavmdsdt
tgklgfeefkylwnnikkwqgiykrfdtdrsgtigsnelpgafeaagfhlnqhiysmiir
rysdetgnmdfdnfisclvrldamfrafrsldkngtgqiqvniqewlqltmys
>d1dvra_ 3.29.1.1.8 Adenylate kinase {baker's yeast (Saccharomyces cerevisiae)}
ssesirmvligppgagkgtqapnlqerfhaahlatgdmlrsqiakgtqlgleakkimdqg
glvsddimvnmikdeltnnpackngfilvgfprtipqaekldqmlkeqgtplekaielkv
ddellvaritgrlihpasgrsyhkifnppkedmkddvtgealvqisddnadalkkrlaay
haqtepivdfykktgiwagvdasqppatvwadilnklgkn
>d1dvrb_ 3.29.1.1.8 Adenylate kinase {baker's yeast (Saccharomyces cerevisiae)}
ssesirmvligppgagkgtqapnlqerfhaahlatgdmlrsqiakgtqlgleakkimdqg
glvsddimvnmikdeltnnpackngfilvgfprtipqaekldqmlkeqgtplekaielkv
ddellvaritgrlihpasgrsyhkifnppkedmkddvtgealvqisddnadalkkrlaay
haqtepivdfykktgiwagvdasqppatvwadilnklgkn
>e1dwb.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1dwb.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
eadcglrplfekksledkterellesyid
>e1dwc.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1dwc.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
eadcglrplfekksledkterellesyid
>e1dwd.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1dwd.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
eadcglrplfekksledkterellesyid
>e1dwe.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1dwe.1l 2.35.1.2.10 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_ 3.1.12.1.2 D-xylose isomerase {(Streptomyces murinus)}
msfqptpedrftfglwtvgwqgrdpfgdatrpaldpvetvqrlaelgaygvtfhdddlip
fgssdtereshikrfrqaldatgmtvpmattnlfthpvfkdggftandrdvrryalrkti
gnidlaaelgaktyvawggregaesggakdvrdaldrmkeafdllgeyvtaqgydlrfai
epkpneprgdillptvghalafierlerpelygvnpevgheqmaglnfphgiaqalwagk
lfhidlngqsgikydqdlrfgagdlraafwlvdlletagyegprhfdfkpprtedfdgvw
asaagcmrnylilkdraaafradpevqealraarldqlaqptaadgldalladraafedf
dvdaaaargmafehldqlamdhllgarg
>d1dxib_ 3.1.12.1.2 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_ 1.1.1.1.25 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_ 1.1.1.1.25 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_ 1.1.1.1.25 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_ 1.1.1.1.25 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_ 1.1.1.1.25 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_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
ahltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1dxy_1 3.14.9.1.2 (1-100) D-2-hydroxyisocaproate dehydrogenase {(Lactobacillus casei)}
mkiiaygarvdeiqyfkqwakdtgntleyhtefldentvewakgfdginslqttpyaagv
fekmhaygikfltirnvgtdnidmtamkqygirlsnvpay
>d1dxy_2 3.22.1.4.2 (101-330) D-2-hydroxyisocaproate dehydrogenase {(Lactobacillus casei)}
spaaiaefaltdtlyllrnmgkvqaqlqagdyekagtfigkelgqqtvgvmgtghigqva
iklfkgfgakviaydpypmkgdhpdfdyvsledlfkqsdvidlhvpgieqnthiineaaf
nlmkpgaivintarpnlidtqamlsnlksgklagvgidtyeyetedllnlakhgsfkdpl
wdellgmpnvvlsphiayytetavhnmvyfslqhlvdfltkgetstevtg
>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_ 3.60.1.1.1 Dihydrofolate reductase, prokaryotic type {(Escherichia coli)}
misliaalavdrvigmenampwnlpadlawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1dyhb_ 3.60.1.1.1 Dihydrofolate reductase, prokaryotic type {(Escherichia coli)}
misliaalavdrvigmenampwnlpadlawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1dyia_ 3.60.1.1.1 Dihydrofolate reductase, prokaryotic type {(Escherichia coli)}
misliaalavdrvigmenampwnlpadlawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1dyib_ 3.60.1.1.1 Dihydrofolate reductase, prokaryotic type {(Escherichia coli)}
misliaalavdrvigmenampwnlpadlawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1dyja_ 3.60.1.1.1 Dihydrofolate reductase, prokaryotic type {(Escherichia coli)}
misliaalavdrvigmenampwnlpadlawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1dyjb_ 3.60.1.1.1 Dihydrofolate reductase, prokaryotic type {(Escherichia coli)}
misliaalavdrvigmenampwnlpadlawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1dyna_ 2.41.1.1.4 Dynamin {Human (Homo sapiens)}
ilvirkgwltinnigimkggskeywfvltaenlswykddeekekkymlsvdnlklrdvek
gfmsskhifalfnteqrnvykdyrqlelacetqeevdswkasflragvyperv
>d1dynb_ 2.41.1.1.4 Dynamin {Human (Homo sapiens)}
ilvirkgwltinnigimkggskeywfvltaenlswykddeekekkymlsvdnlklrdvek
gfmsskhifalfnteqrnvykdyrqlelacetqeevdswkasflragvyperv
>d1dyr__ 3.60.1.1.6 Dihydrofolate reductases, eukaryotic type {fungus (Pneumocystis carinii)}
nqqksltlivalttsygigrsnslpwklkkeisyfkrvtsfvptfdsfesmnvvlmgrkt
wesiplqfrplkgrinvvitrnesldlgngihsaksldhalellyrtygsessvqinrif
viggaqlykaamdhpkldrimatiiykdihcdvffplkfrdkewssvwkkekhsdleswv
gtkvphgkinedgfdyefemwtrdl
>d1e2aa_ 1.7.2.1.1 Enzyme IIa from the lactose specific PTS, IIa-lac {(Lactococcus lactis)}
mnreemtllgfeivayagdarskllealkaaengdfakadslvveagsciaeahssqtgm
lareasgeelpysvtmmhgqdhlmttillkdvihhlielykr
>d1e2ab_ 1.7.2.1.1 Enzyme IIa from the lactose specific PTS, IIa-lac {(Lactococcus lactis)}
mnreemtllgfeivayagdarskllealkaaengdfakadslvveagsciaeahssqtgm
lareasgeelpysvtmmhgqdhlmttillkdvihhlielykr
>d1e2ac_ 1.7.2.1.1 Enzyme IIa from the lactose specific PTS, IIa-lac {(Lactococcus lactis)}
mnreemtllgfeivayagdarskllealkaaengdfakadslvveagsciaeahssqtgm
lareasgeelpysvtmmhgqdhlmttillkdvihhlielykr
>d1e2b__ 3.36.2.1.1 Enzyme IIB-cellobiose {(Escherichia coli)}
mekkhiylfssagmstsllvskmraqaekyevpviieafpetlagekgqnadvvllgpqi
aymlpeiqrllpnkpvevidsllygkvdglgvlkaavaaikkaaan
>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_ 2.38.1.2.5 Acid protease {yeast (Candida albicans)}
qavpvtlhneqvtyaaditvgsnnqklnvivdtgssdlwvpdvnvdcqvtysdqtadfck
qkgtydpsgssasqdlntpfkigygdgsssqgtlykdtvgfggvsiknqvladvdstsid
qgilgvgyktneaggsydnvpvtlkkqgviaknayslylnspdaatgqiifggvdnakys
gslialpvtsdrelrislgsvevsgktintdnvdvlldsgttitylqqdladqiikafng
kltqdsngnsfyevdcnlsgdvvfnfsknakisvpasefaaslqgddgqpydkcqllfdv
ndanilgdnflrsayivydlddneislaqvkytsassisalt
>d1eal__ 2.45.1.2.11 Ileal lipid binding protein {pig (Sus scrofa)}
aftgkyeieseknydefmkrlalpsdaidkarnlkiisevkqdgqnftwsqqypgghsit
ntftigkecdietiggkkfkatvqmeggkvvvnspnyhhtaeivdgklvevstvggvsye
rvskkla
>d1eapa1 2.1.1.1.47 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab 17E8 (mouse), kappa L chain}
dieltqspsslsaslggkvtitckasqdikkyigwyqhkpgkgprllihytstllpgips
rfrgsgsgrdysfsisnleggdiatyyclqyynlrtfgggtkleik
>d1eapa2 2.1.1.2.54 (108-214) Immunoglobulin (constant domains of L and H chains) {Fab 17E8 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgseraqgvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1eapb1 2.1.1.1.47 (1-124) Immunoglobulin (variable domains of L and H chains) {Fab 17E8 (mouse), kappa L chain}
evqlqesgtelvkpgasvkisckasgyistdhaihwvkqrpeqglewigyispgngdiky
nekfkvkatltadqssstaymqlnsltsedsavyfckrsyygssyvdywgqgttltvss
>d1eapb2 2.1.1.2.54 (125-221) Immunoglobulin (constant domains of L and H chains) {Fab 17E8 (mouse), kappa L chain}
akttppsvyplapgcgdttgssvtlgclvkgyfpesvtvtwnsgglsssvhtfpallqsg
lytmsssvtvpgggwpsatvtcsvahpassttvdkkl
>d1eas__ 2.35.1.2.14 Elastase {porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1eat__ 2.35.1.2.14 Elastase {porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1eau__ 2.35.1.2.14 Elastase {porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1eaya_ 3.14.2.1.1 CheY protein {(Escherichia coli)}
adkelkflvvddfstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmp
nmdglellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleekln
kifeklgm
>d1eayb_ 3.14.2.1.1 CheY protein {(Escherichia coli)}
adkelkflvvddfstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmp
nmdglellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleekln
kifeklgm
>d1eayc_ 4.34.20.1.1 CheY-binding domain of CheA {(Escherichia coli)}
prriilsrlkagevdlleeelghlttltdvvkgadslsailpgdiaedditavlcfviea
dqitfet
>d1eayd_ 4.34.20.1.1 CheY-binding domain of CheA {(Escherichia coli)}
sprriilsrlkagevdlleeelghlttltdvvkgadslsailpgdiaedditavlcfvie
adqitfetv
>d1ebda1 3.4.1.4.9 (7-154,272-346) Dihydrolipoamide dehydrogenase {(Bacillus stearothermophilus)}
aietetlvvgagpggyvaairaaqlgqkvtivekgnlggvclnvgcipskalisashrye
qakhseemgikaenvtidfakvqewkasvvkkltggvegllkgnkveivkgeayfvdant
vrvvngdsaqtytfknaiiatgsrpielXvgrrpntdelgleqigikmtnrglievdqqc
rtsvpnifaigdivpgpalahkasyegkvaaeaiaghpsavdyv
>d1ebda2 3.4.1.4.9 (155-271) Dihydrolipoamide dehydrogenase {(Bacillus stearothermophilus)}
pnfkfsnrildstgalnlgevpkslvvigggyigielgtayanfgtkvtilegageilsg
fekqmaaiikkrlkkkgvevvtnalakgaeeredgvtvtyeangetktidadyvlvt
>d1ebda3 4.48.1.1.7 (347-461) Dihydrolipoamide dehydrogenase {(Bacillus stearothermophilus)}
aipavvfsdpecasvgyfeqqakdegidviaakfpfaangralalndtdgflklvvrked
gviigaqiigpnasdmiaelglaieagmtaedialtihahptlgeiameaaeval
>d1ebdb1 3.4.1.4.9 (7-154,272-346) Dihydrolipoamide dehydrogenase {(Bacillus stearothermophilus)}
aietetlvvgagpggyvaairaaqlgqkvtivekgnlggvclnvgcipskalisashrye
qakhseemgikaenvtidfakvqewkasvvkkltggvegllkgnkveivkgeayfvdant
vrvvngdsaqtytfknaiiatgsrpielXvgrrpntdelgleqigikmtnrglievdqqc
rtsvpnifaigdivpgpalahkasyegkvaaeaiaghpsavdyv
>d1ebdb2 3.4.1.4.9 (155-271) Dihydrolipoamide dehydrogenase {(Bacillus stearothermophilus)}
pnfkfsnrildstgalnlgevpkslvvigggyigielgtayanfgtkvtilegageilsg
fekqmaaiikkrlkkkgvevvtnalakgaeeredgvtvtyeangetktidadyvlvt
>d1ebdb3 4.48.1.1.7 (347-461) Dihydrolipoamide dehydrogenase {(Bacillus stearothermophilus)}
aipavvfsdpecasvgyfeqqakdegidviaakfpfaangralalndtdgflklvvrked
gviigaqiigpnasdmiaelglaieagmtaedialtihahptlgeiameaaeval
>d1ebdc_ 1.9.1.1.1 E3-binding domain of dihydrolipoamide acetyltransferase {(Bacillus stearothermophilus)}
iampsvrkyarekgvdirlvqgtgkngrvlkedidaflagg
>d1ebga1 3.1.6.1.1 (142-436) Enolase {baker's yeast (Saccharomyces cerevisiae)}
spyvlpvpflnvlnggshaggalalqefmiaptgaktfaealrigsevyhnlksltkkry
gasagnvgdeggvapniqtaeealdlivdaikaaghdgkvkigldcasseffkdgkydld
fknpnsdkskwltgpqladlyhslmkrypivsiedpfaeddweawshffktagiqivadd
ltvtnpkriataiekkaadalllkvnqigtlsesikaaqdsfaagwgvmvshrsgetedt
fiadlvvglrtgqiktgaparserlaklnqllrieeelgdnavfagenfhhgdkl
>d1ebga2 4.32.1.1.1 (1-141) Enolase {baker's yeast (Saccharomyces cerevisiae)}
avskvyarsvydsrgnptvevelttekgvfrsivpsgastgvhealemrdgdkskwmgkg
vlhavknvndviapafvkanidvkdqkavddflisldgtanksklganailgvslaasra
aaaeknvplykhladlskskt
>d1ebgb1 3.1.6.1.1 (142-436) Enolase {baker's yeast (Saccharomyces cerevisiae)}
spyvlpvpflnvlnggshaggalalqefmiaptgaktfaealrigsevyhnlksltkkry
gasagnvgdeggvapniqtaeealdlivdaikaaghdgkvkigldcasseffkdgkydld
fknpnsdkskwltgpqladlyhslmkrypivsiedpfaeddweawshffktagiqivadd
ltvtnpkriataiekkaadalllkvnqigtlsesikaaqdsfaagwgvmvshrsgetedt
fiadlvvglrtgqiktgaparserlaklnqllrieeelgdnavfagenfhhgdkl
>d1ebgb2 4.32.1.1.1 (1-141) Enolase {baker's yeast (Saccharomyces cerevisiae)}
avskvyarsvydsrgnptvevelttekgvfrsivpsgastgvhealemrdgdkskwmgkg
vlhavknvndviapafvkanidvkdqkavddflisldgtanksklganailgvslaasra
aaaeknvplykhladlskskt
>d1ebha1 3.1.6.1.1 (142-436) Enolase {baker's yeast (Saccharomyces cerevisiae)}
spyvlpvpflnvlnggshaggalalqefmiaptgaktfaealrigsevyhnlksltkkry
gasagnvgdeggvapniqtaeealdlivdaikaaghdgkvkigldcasseffkdgkydld
fknpnsdkskwltgpqladlyhslmkrypivsiedpfaeddweawshffktagiqivadd
ltvtnpkriataiekkaadalllkvnqigtlsesikaaqdsfaagwgvmvshrsgetedt
fiadlvvglrtgqiktgaparserlaklnqllrieeelgdnavfagenfhhgdkl
>d1ebha2 4.32.1.1.1 (1-141) Enolase {baker's yeast (Saccharomyces cerevisiae)}
avskvyarsvydsrgnptvevelttekgvfrsivpsgastgvhealemrdgdkskwmgkg
vlhavknvndviapafvkanidvkdqkavddflisldgtanksklganailgvslaasra
aaaeknvplykhladlskskt
>d1ebhb1 3.1.6.1.1 (142-436) Enolase {baker's yeast (Saccharomyces cerevisiae)}
spyvlpvpflnvlnggshaggalalqefmiaptgaktfaealrigsevyhnlksltkkry
gasagnvgdeggvapniqtaeealdlivdaikaaghdgkvkigldcasseffkdgkydld
fknpnsdkskwltgpqladlyhslmkrypivsiedpfaeddweawshffktagiqivadd
ltvtnpkriataiekkaadalllkvnqigtlsesikaaqdsfaagwgvmvshrsgetedt
fiadlvvglrtgqiktgaparserlaklnqllrieeelgdnavfagenfhhgdkl
>d1ebhb2 4.32.1.1.1 (1-141) Enolase {baker's yeast (Saccharomyces cerevisiae)}
avskvyarsvydsrgnptvevelttekgvfrsivpsgastgvhealemrdgdkskwmgkg
vlhavknvndviapafvkanidvkdqkavddflisldgtanksklganailgvslaasra
aaaeknvplykhladlskskt
>d1ebpa_ 2.1.2.1.8 Erythropoietin (EPO) receptor {human (homo sapiens)}
kfeskaallaargpeellcfterledlvcfweeaasagvgpgnysfsyqledepwklcrl
hqaptargavrfwcslptadtssfvplelrvtaasgapryhrvihinevvlldapvglva
rladesghvvlrwlpppetpmtshiryevdvsagngagsvqrveilegrtecvlsnlrgr
trytfavrarmaepsfggfwsawsepvsllt
>d1ebpb_ 2.1.2.1.8 Erythropoietin (EPO) receptor {human (homo sapiens)}
kfeskaallaargpeellcfterledlvcfweeaasagvgpgnysfsyqledepwklcrl
hqaptargavrfwcslptadtssfvplelrvtaasgapryhrvihinevvlldapvglva
rladesghvvlrwlpppetpmtshiryevdvsagngagsvqrveilegrtecvlsnlrgr
trytfavrarmaepsfggfwsawsepvsllt
>d1eca__ 1.1.1.1.13 Erythrocruorin {Midge (Chironomous thummi thummi), Fraction III}
lsadqistvqasfdkvkgdpvgilyavfkadpsimakftqfagkdlesikgtapfethan
rivgffskiigelpnieadvntfvashkprgvthdqlnnfragfvsymkahtdfagaeaa
wgatldtffgmifskm
>d1ecba1 3.49.1.1.5 (250-469) Glutamine PRPP amidotransferase, C-terminal domain {(Escherichia coli)}
npclfeyvyfarpdsfidkisvysarvnmgtklgekiarewedldidvvipipetscdia
leiarilgkpyrqgfvknryvgrtfimpgqqlrrksvrrklnanraefrdknvllvddsi
vrgttseqiiemareagakkvylasaapeirfpnvygidmpsateliahgrevdeirqii
gadglifqdlndlidavraenpdiqqfecsvfngvyvtkd
>d1ecba2 4.95.1.1.3 (1-249) Glutamine PRPP amidotransferase, N-terminal domain {(Escherichia coli)}
cgivgiagvmpvnqsiydaltvlqhrgqdaagiitidanncfrlrkanglvsdvfearhm
qrlqgnmgighvryptagsssaseaqpfyvnspygitlahngnltnahelrkklfeekrr
hinttsdseillnifaseldnfrhypleadnifaaiaatnrlirgayacvamiighgmva
frdpngirplvlgkrdidenrteymvasesvaldtlgfdflrdvapgeaiyiteegqlft
rqcadnpvs
>d1ecbb1 3.49.1.1.5 (250-469) Glutamine PRPP amidotransferase, C-terminal domain {(Escherichia coli)}
npclfeyvyfarpdsfidkisvysarvnmgtklgekiarewedldidvvipipetscdia
leiarilgkpyrqgfvknryvgrtfimpgqqlrrksvrrklnanraefrdknvllvddsi
vrgttseqiiemareagakkvylasaapeirfpnvygidmpsateliahgrevdeirqii
gadglifqdlndlidavraenpdiqqfecsvfngvyvtkd
>d1ecbb2 4.95.1.1.3 (1-249) Glutamine PRPP amidotransferase, N-terminal domain {(Escherichia coli)}
cgivgiagvmpvnqsiydaltvlqhrgqdaagiitidanncfrlrkanglvsdvfearhm
qrlqgnmgighvryptagsssaseaqpfyvnspygitlahngnltnahelrkklfeekrr
hinttsdseillnifaseldnfrhypleadnifaaiaatnrlirgayacvamiighgmva
frdpngirplvlgkrdidenrteymvasesvaldtlgfdflrdvapgeaiyiteegqlft
rqcadnpvs
>d1ecbc1 3.49.1.1.5 (250-469) Glutamine PRPP amidotransferase, C-terminal domain {(Escherichia coli)}
npclfeyvyfarpdsfidkisvysarvnmgtklgekiarewedldidvvipipetscdia
leiarilgkpyrqgfvknryvgrtfimpgqqlrrksvrrklnanraefrdknvllvddsi
vrgttseqiiemareagakkvylasaapeirfpnvygidmpsateliahgrevdeirqii
gadglifqdlndlidavraenpdiqqfecsvfngvyvtkd
>d1ecbc2 4.95.1.1.3 (1-249) Glutamine PRPP amidotransferase, N-terminal domain {(Escherichia coli)}
cgivgiagvmpvnqsiydaltvlqhrgqdaagiitidanncfrlrkanglvsdvfearhm
qrlqgnmgighvryptagsssaseaqpfyvnspygitlahngnltnahelrkklfeekrr
hinttsdseillnifaseldnfrhypleadnifaaiaatnrlirgayacvamiighgmva
frdpngirplvlgkrdidenrteymvasesvaldtlgfdflrdvapgeaiyiteegqlft
rqcadnpvs
>d1ecbd1 3.49.1.1.5 (250-469) Glutamine PRPP amidotransferase, C-terminal domain {(Escherichia coli)}
npclfeyvyfarpdsfidkisvysarvnmgtklgekiarewedldidvvipipetscdia
leiarilgkpyrqgfvknryvgrtfimpgqqlrrksvrrklnanraefrdknvllvddsi
vrgttseqiiemareagakkvylasaapeirfpnvygidmpsateliahgrevdeirqii
gadglifqdlndlidavraenpdiqqfecsvfngvyvtkd
>d1ecbd2 4.95.1.1.3 (1-249) Glutamine PRPP amidotransferase, N-terminal domain {(Escherichia coli)}
cgivgiagvmpvnqsiydaltvlqhrgqdaagiitidanncfrlrkanglvsdvfearhm
qrlqgnmgighvryptagsssaseaqpfyvnspygitlahngnltnahelrkklfeekrr
hinttsdseillnifaseldnfrhypleadnifaaiaatnrlirgayacvamiighgmva
frdpngirplvlgkrdidenrteymvasesvaldtlgfdflrdvapgeaiyiteegqlft
rqcadnpvs
>d1ecca1 3.49.1.1.5 (250-469) Glutamine PRPP amidotransferase, C-terminal domain {(Escherichia coli)}
npclfeyvyfarpdsfidkisvysarvnmgtklgekiarewedldidvvipipetscdia
leiarilgkpyrqgfvknryvgrtfimpgqqlrrksvrrklnanraefrdknvllvddsi
vrgttseqiiemareagakkvylasaapeirfpnvygidmpsateliahgrevdeirqii
gadglifqdlndlidavraenpdiqqfecsvfngvyvtkd
>d1ecca2 4.95.1.1.3 (1-249) Glutamine PRPP amidotransferase, N-terminal domain {(Escherichia coli)}
cgivgiagvmpvnqsiydaltvlqhrgqdaagiitidanncfrlrkanglvsdvfearhm
qrlqgnmgighvryptagsssaseaqpfyvnspygitlahngnltnahelrkklfeekrr
hinttsdseillnifaseldnfrhypleadnifaaiaatnrlirgayacvamiighgmva
frdpngirplvlgkrdidenrteymvasesvaldtlgfdflrdvapgeaiyiteegqlft
rqcadnpvs
>d1eccb1 3.49.1.1.5 (250-469) Glutamine PRPP amidotransferase, C-terminal domain {(Escherichia coli)}
npclfeyvyfarpdsfidkisvysarvnmgtklgekiarewedldidvvipipetscdia
leiarilgkpyrqgfvknryvgrtfimpgqqlrrksvrrklnanraefrdknvllvddsi
vrgttseqiiemareagakkvylasaapeirfpnvygidmpsateliahgrevdeirqii
gadglifqdlndlidavraenpdiqqfecsvfngvyvtkd
>d1eccb2 4.95.1.1.3 (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_ 3.1.1.3.5 Endocellulase E1 {(Acidothermus cellulolyticus)}
agggywhtsgreildannvpvriaginwfgfetcnyvvhglwsrdyrsmldqikslgynt
irlpysddilkpgtmpnsinfyqmnqdlqgltslqvmdkivayagqiglriildrhrpdc
sgqsalwytssvseatwisdlqalaqrykgnptvvgfdlhnephdpacwgcgdpsidwrl
aaeragnavlsvnpnllifvegvqsyngdsywwggnlqgagqypvvlnvpnrlvysahdy
atsvypqtwfsdptfpnnmpgiwnknwgylfnqniapvwlgefgttlqsttdqtwlktlv
qylrptaqygadsfqwtfwswnpdsgdtggilkddwqtvdtvkdgylapikssifdpv
>d1eceb_ 3.1.1.3.5 Endocellulase E1 {(Acidothermus cellulolyticus)}
agggywhtsgreildannvpvriaginwfgfetcnyvvhglwsrdyrsmldqikslgynt
irlpysddilkpgtmpnsinfyqmnqdlqgltslqvmdkivayagqiglriildrhrpdc
sgqsalwytssvseatwisdlqalaqrykgnptvvgfdlhnephdpacwgcgdpsidwrl
aaeragnavlsvnpnllifvegvqsyngdsywwggnlqgagqypvvlnvpnrlvysahdy
atsvypqtwfsdptfpnnmpgiwnknwgylfnqniapvwlgefgttlqsttdqtwlktlv
qylrptaqygadsfqwtfwswnpdsgdtggilkddwqtvdtvkdgylapikssifdpv
>d1ecfa1 3.49.1.1.5 (250-469) Glutamine PRPP amidotransferase, C-terminal domain {(Escherichia coli)}
npclfeyvyfarpdsfidkisvysarvnmgtklgekiarewedldidvvipipetscdia
leiarilgkpyrqgfvknryvgrtfimpgqqlrrksvrrklnanraefrdknvllvddsi
vrgttseqiiemareagakkvylasaapeirfpnvygidmpsateliahgrevdeirqii
gadglifqdlndlidavraenpdiqqfecsvfngvyvtkd
>d1ecfa2 4.95.1.1.3 (1-249) Glutamine PRPP amidotransferase, N-terminal domain {(Escherichia coli)}
cgivgiagvmpvnqsiydaltvlqhrgqdaagiitidanncfrlrkanglvsdvfearhm
qrlqgnmgighvryptagsssaseaqpfyvnspygitlahngnltnahelrkklfeekrr
hinttsdseillnifaseldnfrhypleadnifaaiaatnrlirgayacvamiighgmva
frdpngirplvlgkrdidenrteymvasesvaldtlgfdflrdvapgeaiyiteegqlft
rqcadnpvs
>d1ecfb1 3.49.1.1.5 (250-469) Glutamine PRPP amidotransferase, C-terminal domain {(Escherichia coli)}
npclfeyvyfarpdsfidkisvysarvnmgtklgekiarewedldidvvipipetscdia
leiarilgkpyrqgfvknryvgrtfimpgqqlrrksvrrklnanraefrdknvllvddsi
vrgttseqiiemareagakkvylasaapeirfpnvygidmpsateliahgrevdeirqii
gadglifqdlndlidavraenpdiqqfecsvfngvyvtkd
>d1ecfb2 4.95.1.1.3 (1-249) Glutamine PRPP amidotransferase, N-terminal domain {(Escherichia coli)}
cgivgiagvmpvnqsiydaltvlqhrgqdaagiitidanncfrlrkanglvsdvfearhm
qrlqgnmgighvryptagsssaseaqpfyvnspygitlahngnltnahelrkklfeekrr
hinttsdseillnifaseldnfrhypleadnifaaiaatnrlirgayacvamiighgmva
frdpngirplvlgkrdidenrteymvasesvaldtlgfdflrdvapgeaiyiteegqlft
rqcadnpvs
>d1ecga1 3.49.1.1.5 (250-469) Glutamine PRPP amidotransferase, C-terminal domain {(Escherichia coli)}
npclfeyvyfarpdsfidkisvysarvnmgtklgekiarewedldidvvipipetscdia
leiarilgkpyrqgfvknryvgrtfimpgqqlrrksvrrklnanraefrdknvllvddsi
vrgttseqiiemareagakkvylasaapeirfpnvygidmpsateliahgrevdeirqii
gadglifqdlndlidavraenpdiqqfecsvfngvyvtkd
>d1ecga2 4.95.1.1.3 (1-249) Glutamine PRPP amidotransferase, N-terminal domain {(Escherichia coli)}
cgivgiagvmpvnqsiydaltvlqhrgqdaagiitidanncfrlrkanglvsdvfearhm
qrlqgnmgighvryptagsssaseaqpfyvnspygitlahngnltnahelrkklfeekrr
hinttsdseillnifaseldnfrhypleadnifaaiaatnrlirgayacvamiighgmva
frdpngirplvlgkrdidenrteymvasesvaldtlgfdflrdvapgeaiyiteegqlft
rqcadnpvs
>d1ecgb1 3.49.1.1.5 (250-469) Glutamine PRPP amidotransferase, C-terminal domain {(Escherichia coli)}
npclfeyvyfarpdsfidkisvysarvnmgtklgekiarewedldidvvipipetscdia
leiarilgkpyrqgfvknryvgrtfimpgqqlrrksvrrklnanraefrdknvllvddsi
vrgttseqiiemareagakkvylasaapeirfpnvygidmpsateliahgrevdeirqii
gadglifqdlndlidavraenpdiqqfecsvfngvyvtkd
>d1ecgb2 4.95.1.1.3 (1-249) Glutamine PRPP amidotransferase, N-terminal domain {(Escherichia coli)}
cgivgiagvmpvnqsiydaltvlqhrgqdaagiitidanncfrlrkanglvsdvfearhm
qrlqgnmgighvryptagsssaseaqpfyvnspygitlahngnltnahelrkklfeekrr
hinttsdseillnifaseldnfrhypleadnifaaiaatnrlirgayacvamiighgmva
frdpngirplvlgkrdidenrteymvasesvaldtlgfdflrdvapgeaiyiteegqlft
rqcadnpvs
>d1ecia_ 1.31.1.1.1 Ectatomin, A & B chains {ant (Ectatomma tuberculatum) venom}
gvipkkiwetvcptvepwakkcsgdiatyikrecgkl
>d1ecib_ 1.31.1.1.1 Ectatomin, A & B chains {ant (Ectatomma tuberculatum) venom}
wstivklticptlksmakkcegsiatmikkkcdk
>d1ecja1 3.49.1.1.5 (250-469) Glutamine PRPP amidotransferase, C-terminal domain {(Escherichia coli)}
npclfeyvyfarpdsfidkisvysarvnmgtklgekiarewedldidvvipipetscdia
leiarilgkpyrqgfvknryvgrtfimpgqqlrrksvrrklnanraefrdknvllvddsi
vrgttseqiiemareagakkvylasaapeirfpnvygidmpsateliahgrevdeirqii
gadglifqdlndlidavraenpdiqqfecsvfngvyvtkd
>d1ecja2 4.95.1.1.3 (1-249) Glutamine PRPP amidotransferase, N-terminal domain {(Escherichia coli)}
cgivgiagvmpvnqsiydaltvlqhrgqdaagiitidanncfrlrkanglvsdvfearhm
qrlqgnmgighvryptagsssaseaqpfyvnspygitlahngnltnahelrkklfeekrr
hinttsdseillnifaseldnfrhypleadnifaaiaatnrlirgayacvamiighgmva
frdpngirplvlgkrdidenrteymvasesvaldtlgfdflrdvapgeaiyiteegqlft
rqcadnpvs
>d1ecjb1 3.49.1.1.5 (250-469) Glutamine PRPP amidotransferase, C-terminal domain {(Escherichia coli)}
npclfeyvyfarpdsfidkisvysarvnmgtklgekiarewedldidvvipipetscdia
leiarilgkpyrqgfvknryvgrtfimpgqqlrrksvrrklnanraefrdknvllvddsi
vrgttseqiiemareagakkvylasaapeirfpnvygidmpsateliahgrevdeirqii
gadglifqdlndlidavraenpdiqqfecsvfngvyvtkd
>d1ecjb2 4.95.1.1.3 (1-249) Glutamine PRPP amidotransferase, N-terminal domain {(Escherichia coli)}
cgivgiagvmpvnqsiydaltvlqhrgqdaagiitidanncfrlrkanglvsdvfearhm
qrlqgnmgighvryptagsssaseaqpfyvnspygitlahngnltnahelrkklfeekrr
hinttsdseillnifaseldnfrhypleadnifaaiaatnrlirgayacvamiighgmva
frdpngirplvlgkrdidenrteymvasesvaldtlgfdflrdvapgeaiyiteegqlft
rqcadnpvs
>d1ecjc1 3.49.1.1.5 (250-469) Glutamine PRPP amidotransferase, C-terminal domain {(Escherichia coli)}
npclfeyvyfarpdsfidkisvysarvnmgtklgekiarewedldidvvipipetscdia
leiarilgkpyrqgfvknryvgrtfimpgqqlrrksvrrklnanraefrdknvllvddsi
vrgttseqiiemareagakkvylasaapeirfpnvygidmpsateliahgrevdeirqii
gadglifqdlndlidavraenpdiqqfecsvfngvyvtkd
>d1ecjc2 4.95.1.1.3 (1-249) Glutamine PRPP amidotransferase, N-terminal domain {(Escherichia coli)}
cgivgiagvmpvnqsiydaltvlqhrgqdaagiitidanncfrlrkanglvsdvfearhm
qrlqgnmgighvryptagsssaseaqpfyvnspygitlahngnltnahelrkklfeekrr
hinttsdseillnifaseldnfrhypleadnifaaiaatnrlirgayacvamiighgmva
frdpngirplvlgkrdidenrteymvasesvaldtlgfdflrdvapgeaiyiteegqlft
rqcadnpvs
>d1ecjd1 3.49.1.1.5 (250-469) Glutamine PRPP amidotransferase, C-terminal domain {(Escherichia coli)}
npclfeyvyfarpdsfidkisvysarvnmgtklgekiarewedldidvvipipetscdia
leiarilgkpyrqgfvknryvgrtfimpgqqlrrksvrrklnanraefrdknvllvddsi
vrgttseqiiemareagakkvylasaapeirfpnvygidmpsateliahgrevdeirqii
gadglifqdlndlidavraenpdiqqfecsvfngvyvtkd
>d1ecjd2 4.95.1.1.3 (1-249) Glutamine PRPP amidotransferase, N-terminal domain {(Escherichia coli)}
cgivgiagvmpvnqsiydaltvlqhrgqdaagiitidanncfrlrkanglvsdvfearhm
qrlqgnmgighvryptagsssaseaqpfyvnspygitlahngnltnahelrkklfeekrr
hinttsdseillnifaseldnfrhypleadnifaaiaatnrlirgayacvamiighgmva
frdpngirplvlgkrdidenrteymvasesvaldtlgfdflrdvapgeaiyiteegqlft
rqcadnpvs
>d1ecl__ 5.11.1.1.1 DNA topoisomerase I, the 67K N-terminal domain {(Escherichia coli)}
gkalvivespakaktinkylgsdyvvkssvghirdltsgsaakksadststktakkpkkp
dergalvnrmgvdpwhnweahyevlpgkekvvselkqlaekadhiylatdldregeaiaw
hlreviggddarysrvvfneitknairqafnkpgelnidrvnaqqarrfmdrvvgymvsp
llwkkiarglsagrvqsvavrlvverereikafvpeefwevdastttpsgealalqvthq
ndkpfrpvnkeqtqaavsllekarysvleredkpttskpgapfitstlqqaastrlgfgv
kktmmmaqrlyeagyitymrtdstnlsqdavnmvrgyisdnfgkkylpespnqyaskgns
qeaheairpsdvnvmaeslkdmeadaqklyqliwrqfvacqmtpakydsttltvgagdfr
lkargrilrfdgwtkvmpalrkgdedrilpavnkgdaltlveltpaqhftkpparfseas
lvkelekrgigrpstyasiistiqdrgyvrvenrrfyaekmgeivtdrleenfrelmnyd
ftaqmensldqvanheaewkavldhffsdftqqldkaekdpeeggmrpn
>d1ecma_ 1.101.1.1.1 Chorismate mutase domain of P-protein {(Escherichia coli)}
npllalrekisaldekllallaerrelavevgkakllshrpvrdidrerdllerlitlgk
ahhldahyitrlfqliiedsvltqqallqqh
>d1ecmb_ 1.101.1.1.1 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_ 3.58.1.1.3 Purine nucleoside phosphorylase, PNP {(Escherichia coli)}
atphinaemgdfadvvlmpgdplrakyiaetfledarevnnvrgmlgftgtykgrkisvm
ghgmgipscsiytkelitdfgvkkiirvgscgavlphvklrdvvigmgactdskvnrirf
kdhdfaaiadfdmvrnavdaakalgidarvgnlfsadlfyspdgemfdvmekygilgvem
eaagiygvaaefgakaltictvsdhirtheqttaaerqttfndmikialesvllgdk
>d1ecpb_ 3.58.1.1.3 Purine nucleoside phosphorylase, PNP {(Escherichia coli)}
atphinaemgdfadvvlmpgdplrakyiaetfledarevnnvrgmlgftgtykgrkisvm
ghgmgipscsiytkelitdfgvkkiirvgscgavlphvklrdvvigmgactdskvnrirf
kdhdfaaiadfdmvrnavdaakalgidarvgnlfsadlfyspdgemfdvmekygilgvem
eaagiygvaaefgakaltictvsdhirtheqttaaerqttfndmikialesvllgdk
>d1ecpc_ 3.58.1.1.3 Purine nucleoside phosphorylase, PNP {(Escherichia coli)}
atphinaemgdfadvvlmpgdplrakyiaetfledarevnnvrgmlgftgtykgrkisvm
ghgmgipscsiytkelitdfgvkkiirvgscgavlphvklrdvvigmgactdskvnrirf
kdhdfaaiadfdmvrnavdaakalgidarvgnlfsadlfyspdgemfdvmekygilgvem
eaagiygvaaefgakaltictvsdhirtheqttaaerqttfndmikialesvllgdk
>d1ecpd_ 3.58.1.1.3 Purine nucleoside phosphorylase, PNP {(Escherichia coli)}
atphinaemgdfadvvlmpgdplrakyiaetfledarevnnvrgmlgftgtykgrkisvm
ghgmgipscsiytkelitdfgvkkiirvgscgavlphvklrdvvigmgactdskvnrirf
kdhdfaaiadfdmvrnavdaakalgidarvgnlfsadlfyspdgemfdvmekygilgvem
eaagiygvaaefgakaltictvsdhirtheqttaaerqttfndmikialesvllgdk
>d1ecpe_ 3.58.1.1.3 Purine nucleoside phosphorylase, PNP {(Escherichia coli)}
atphinaemgdfadvvlmpgdplrakyiaetfledarevnnvrgmlgftgtykgrkisvm
ghgmgipscsiytkelitdfgvkkiirvgscgavlphvklrdvvigmgactdskvnrirf
kdhdfaaiadfdmvrnavdaakalgidarvgnlfsadlfyspdgemfdvmekygilgvem
eaagiygvaaefgakaltictvsdhirtheqttaaerqttfndmikialesvllgdk
>d1ecpf_ 3.58.1.1.3 Purine nucleoside phosphorylase, PNP {(Escherichia coli)}
atphinaemgdfadvvlmpgdplrakyiaetfledarevnnvrgmlgftgtykgrkisvm
ghgmgipscsiytkelitdfgvkkiirvgscgavlphvklrdvvigmgactdskvnrirf
kdhdfaaiadfdmvrnavdaakalgidarvgnlfsadlfyspdgemfdvmekygilgvem
eaagiygvaaefgakaltictvsdhirtheqttaaerqttfndmikialesvllgdk
>d1ecra_ 5.3.1.1.1 Replication terminator protein (Tus) {(Escherichia coli)}
dlvdrlnttfrqmeqelaifaahleqhkllvarvfslpevkkedehnplnrievkqhlgn
daqslalrhfrhlfiqqqsenrsskaavrlpgvlcyqvdnlsqaalvshiqhinklkttf
ehivtveselptaarfewvhrhlpglitlnayrtltvlhdpatlrfgwankhiiknlhrd
evlaqlekslksprsvapwtreewqrklereyqdiaalpqnaklkikrpvkvqpiarvwy
kgdqkqvqhacptplialinrdngagvpdvgellnydadnvqhrykpqaqplrliiprlh
lyvad
>d1ecy__ 2.12.1.1.1 Ecotin, trypsin inhibitor {(Escherichia coli)}
aesvqplekiapypqaekgmkrqviqltpqedestlkvelligqtlevdcnlhrlggkle
nktlegwgydyyvfdkvsspvstmmacpdgkkekkfvtaylgdagmlrynsklpivvytp
dnvdvkyrvwkaeekidnavvr
>d1ecza_ 2.12.1.1.1 Ecotin, trypsin inhibitor {(Escherichia coli)}
aesvqplekiapypqaekgmkrqviqltpqedestlkvelligqtlevdcnlhrlggkle
nktlegwgydyyvfdkvsspvstmmacpdgkkekkfvtaylgdagmlrynsklpivvytp
dnvdvkyrvwkaeekidnavvr
>d1eczb_ 2.12.1.1.1 Ecotin, trypsin inhibitor {(Escherichia coli)}
aesvqplekiapypqaekgmkrqviqltpqedestlkvelligqtlevdcnlhrlggkle
nktlegwgydyyvfdkvsspvstmmacpdgkkekkfvtaylgdagmlrynsklpivvytp
dnvdvkyrvwkaeekidnavvr
>d1edb__ 3.56.1.3.1 Haloalkane dehalogenase {(Xanthobacter autotrophicus)}
minairtpdqrfsnldqypfspnylddlpgypglrahyldegnsdaedvflclhgeptws
ylyrkmipvfaesgarviapdffgfgksdkpvdeedytfefhrnfllalierldlrnitl
vvqdwggflgltlpmadpsrfkrliimnaclmtdpvtqpafsafvtqpadgftawkydlv
tpsdlrldqfmkrwaptlteaeasayaapfpdtsyqagvrkfpkmvaqrdqacidistea
isfwqndwngqtfmaigmkdkllgpdvmypmkalingcpepleiadaghfvqefgeqvar
ealkhfaete
>d1edd__ 3.56.1.3.1 Haloalkane dehalogenase {(Xanthobacter autotrophicus)}
minairtpdqrfsnldqypfspnylddlpgypglrahyldegnsdaedvflclhgeptws
ylyrkmipvfaesgarviapdffgfgksdkpvdeedytfefhrnfllalierldlrnitl
vvqdwggflgltlpmadpsrfkrliimnaclmtdpvtqpafsafvtqpadgftawkydlv
tpsdlrldqfmkrwaptlteaeasayaapfpdtsyqagvrkfpkmvaqrdqacidistea
isfwqndwngqtfmaigmkdkllgpdvmypmkalingcpepleiadaghfvqefgeqvar
ealkhfaete
>d1ede__ 3.56.1.3.1 Haloalkane dehalogenase {(Xanthobacter autotrophicus)}
minairtpdqrfsnldqypfspnylddlpgypglrahyldegnsdaedvflclhgeptws
ylyrkmipvfaesgarviapdffgfgksdkpvdeedytfefhrnfllalierldlrnitl
vvqdwggflgltlpmadpsrfkrliimnaclmtdpvtqpafsafvtqpadgftawkydlv
tpsdlrldqfmkrwaptlteaeasayaapfpdtsyqagvrkfpkmvaqrdqacidistea
isfwqndwngqtfmaigmkdkllgpdvmypmkalingcpepleiadaghfvqefgeqvar
ealkhfaete
>d1edg__ 3.1.1.3.2 Endoglucanase CelA {(Clostridium cellulolyticum)}
mydaslipnlqipqknipnndgmnfvkglrlgwnlgntfdafngtnitneldyetswsgi
kttkqmidaikqkgfntvripvswhphvsgsdykisdvwmnrvqevvnycidnkmyviln
thhdvdkvkgyfpssqymasskkyitsvwaqiaarfanydehlifegmneprlvghanew
wpeltnsdvvdsincinqlnqdfvntvratggknasrylmcpgyvaspdgatndyfrmpn
disgnnnkiivsvhaycpwnfaglamadggtnawnindskdqsevtwfmdniynkytsrg
ipviigecgavdknnlktrveymsyyvaqakargilcilwdnnnfsgtgelfgffdrrsc
qfkfpeiidgmvkyafglin
>d1edha_ 2.1.5.1.2 E-CADHERIN DOMAINS 1 AND 2 {mouse (Mus musculus)}
vippiscpenekgefpknlvqiksnrdketkvfysitgqgadkppvgvfiieretgwlkv
tqpldreaiakyilyshavssngeavedpmeivitvtdqndnrpeftqevfegsvaegav
pgtsvmkvsatdadddvntynaaiaytivsqdpelphknmftvnrdtgvisvltsgldre
syptytlvvqaadlqgeglsttakavitvkd
>d1edhb_ 2.1.5.1.2 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_ 7.3.9.1.1 Factor IX (IXa) {human (Homo sapiens)}
vdgdqcesnpclnggsckddinsyecwcpfgfegkncel
>d1edmc_ 7.3.9.1.1 Factor IX (IXa) {human (Homo sapiens)}
vdgdqcesnpclnggsckddinsyecwcpfgfegkncel
>d1edt__ 3.1.1.5.5 Endo-beta-N-acetylglucosaminidase {(Streptomyces plicatus), endoglycosidase H}
kqgptsvayvevnnnsmlnvgkytladgggnafdvavifaaninydtgtktaylhfnenv
qrvldnavtqirplqqqgikvllsvlgnhqgagfanfpsqqaasafakqlsdavakygld
gvdfddeyaeygnngtaqpndssfvhlvtalranmpdkiislynigpaasrlsyggvdvs
dkfdyawnpyygtwqvpgialpkaqlspaaveigrtsrstvadlarrtvdegygvyltyn
ldggdrtadvsaftrelygseavrt
>d1eedp_ 2.38.1.2.1 Endothiapepsin {chestnut blight fungus (Endothia parasitica)}
stgsatttpidslddayitpvqigtpaqtlnldfdtgssdlwvfssettasevdgqtiyt
psksttakllsgatwsisygdgssssgdvytdtvsvggltvtgqavesakkvsssfteds
tidgllglafstlntvsptqqktffdnakasldspvftadlgyhapgtynfgfidttayt
gsitytavstkqgfwewtstgyavgsgtfkstsidgiadtgttllylpatvvsaywaqvs
gakssssvggyvfpcsatlpsftfgvgsarivipgdyidfgpistgssscfggiqssagi
ginifgdvalkaafvvfngattptlgfask
>d1efga1 2.32.3.1.4 (283-403) Elongation factor G (EF-G), domain II {(Thermus thermophilus)}
pldippikgttpegevveihpdpngplaalafkimadpyvgrltfirvysgtltsgsyvy
nttkgrkervarllrmhanhreeveelkagdlgavvglketitgdtlvgedaprvilesi
e
>d1efga2 3.29.1.4.16 (1-282) Elongation factor G (EF-G), the N-terminal (G) domain {(Thermus thermophilus)}
mavkveydlkrlrnigiaahidagktttterilyytgrihkigevhegaatmdfmeqere
rgititaavttcfwkdhriniidtpghvdftieversmrvldgaivvfdssqgvepqset
vwrqaekykvpriafankmdktgadlwlvirtmqerlgarpvvmqlpigredtfsgiidv
lrmkaytygndlgtdireipipeeyldnareyheklvevaadfdenimlkylegeeptee
elvaairkgtidlkitpvflgsalknkgvqllldavvdylps
>d1efga3 4.10.1.1.1 (477-599) Elongation factor G (EF-G), domain IV {(Thermus thermophilus)}
gkpqvayretitkpvdvegkfirqtggrgqyghvkikveplprgsgfefvnaivggvipk
eyipavqkgieeamqsgpligfpvvdikvtlydgsyhevdssemafkiagsmaikeavqk
gdp
>d1efga4 4.34.13.1.1 (600-689) Elongation factor G (EF-G), domain V {(Thermus thermophilus)}
vilepimrvevttpeeymgdvigdlnarrgqilgmeprgnaqvirafvplaemfgyatdl
rsktqgrgsfvmffdhyqevpkqvqeklik
>d1efm__ 3.29.1.4.13 Elongation factor Tu (EF-Tu), the N-terminal (G) domain {(Escherichia coli)}
vnvgtighvdhgkttltaaittvlaktyggaarxxxxxxxxxxxxxxgitintshveydt
ptrhyahvdcpghadyvknmitgaaqmdgailvvaatdgpmpqtrehillgrqvgvpyii
vflnkcdmvddeellelvemevrellsqydfpgddtpivrgsalkalegdaeweakile
>d1efna_ 2.24.2.1.2 Fyn proto-oncogene tyrosine kinase, SH3 domain {human (Homo sapiens)}
alfvalydyeaiteddlsfhkgekfqilnssegdwwearslttgetgyipsnyvapv
>d1efnb_ 4.59.1.1.1 Regulatory factor Nef {(Human immunodeficiency virus type 1), HIV-1}
rpqvplrpmtykaavdlshflkekggleglihsqrrqdildlwiyhtqgyfpdwqnytpg
pgvrypltfgwcyklvpvepdkveeankgentsllhpvslhgmddperevlewrfdsrla
fhhvarelhpeyf
>d1efnc_ 2.24.2.1.2 Fyn proto-oncogene tyrosine kinase, SH3 domain {human (Homo sapiens)}
alfvalydyeaiteddlsfhkgekfqilnssegdwwearslttgetgyipsnyvapv
>d1efnd_ 4.59.1.1.1 Regulatory factor Nef {(Human immunodeficiency virus type 1), HIV-1}
rpqvplrpmtykaavdlshflkekggleglihsqrrqdildlwiyhtqgyfpdwqnytpg
pgvrypltfgwcyklvpvepdkveeankgentsllhpvslhgmddperevlewrfdsrla
fhhvarelhpeyf
>d1efra1 1.59.1.1.1 (380-510) The C-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
tramkqvagtmklelaqyrevaafaqfgsdldaatqqllsrgvrltellkqgqyspmaie
eqvaviyagvrgyldklepskitkfenaflshvisqhqallgkirtdgkiseesdaklke
ivtnflagfea
>d1efra2 2.37.1.1.1 (24-94) The N-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
dleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgndklik
egdivkrtgai
>d1efra3 3.29.1.7.2 (95-379) central domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
vdvpvgeellgrvvdalgnaidgkgpigskarrrvglkapgiiprisvrepmqtgikavd
slvpigrgqreliigdrqtgktsiaidtiinqkrfndgtdekkklyciyvaigqkrstva
qlvkrltdadamkytivvsatasdaaplqylapysgcsmgeyfrdngkhaliiyddlskq
avayrqmslllrrppgreaypgdvfylhsrlleraakmndafgggsltalpvietqagdv
sayiptnvisitdgqifletelfykgirpainvglsvsrvgsaaq
>d1efrb1 1.59.1.1.1 (380-510) The C-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
tramkqvagtmklelaqyrevaafaqfgsdldaatqqllsrgvrltellkqgqyspmaie
eqvaviyagvrgyldklepskitkfenaflshvisqhqallgkirtdgkiseesdaklke
ivtnflagfea
>d1efrb2 2.37.1.1.1 (24-94) The N-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
dleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgndklik
egdivkrtgai
>d1efrb3 3.29.1.7.2 (95-379) central domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
vdvpvgeellgrvvdalgnaidgkgpigskarrrvglkapgiiprisvrepmqtgikavd
slvpigrgqreliigdrqtgktsiaidtiinqkrfndgtdekkklyciyvaigqkrstva
qlvkrltdadamkytivvsatasdaaplqylapysgcsmgeyfrdngkhaliiyddlskq
avayrqmslllrrppgreaypgdvfylhsrlleraakmndafgggsltalpvietqagdv
sayiptnvisitdgqifletelfykgirpainvglsvsrvgsaaq
>d1efrc1 1.59.1.1.1 (380-510) The C-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
tramkqvagtmklelaqyrevaafaqfgsdldaatqqllsrgvrltellkqgqyspmaie
eqvaviyagvrgyldklepskitkfenaflshvisqhqallgkirtdgkiseesdaklke
ivtnflagfea
>d1efrc2 2.37.1.1.1 (19-94) The N-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
adtsvdleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgn
dklikegdivkrtgai
>d1efrc3 3.29.1.7.2 (95-379) central domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
vdvpvgeellgrvvdalgnaidgkgpigskarrrvglkapgiiprisvrepmqtgikavd
slvpigrgqreliigdrqtgktsiaidtiinqkrfndgtdekkklyciyvaigqkrstva
qlvkrltdadamkytivvsatasdaaplqylapysgcsmgeyfrdngkhaliiyddlskq
avayrqmslllrrppgreaypgdvfylhsrlleraakmndafgggsltalpvietqagdv
sayiptnvisitdgqifletelfykgirpainvglsvsrvgsaaq
>d1efrd1 1.59.1.1.1 (358-475) The C-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
mdpnivgsehydvargvqkilqdykslqdiiailgmdelseedkltvsrarkiqrflsqp
fqvaevftghlgklvplketikgfqqilageydhlpeqafymvgpieeavakadklae
>d1efrd2 2.37.1.1.1 (9-81) The N-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1efrd3 3.29.1.7.2 (82-357) central domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
iripvgpetlgrimnvigepidergpiktkqfaaihaeapefvemsveqeilvtgikvvd
llapyakggkiglfggagvgktvlimelinnvakahggysvfagvgertregndlyhemi
esgvinlkdatskvalvygqmneppgararvaltgltvaeyfrdqegqdvllfidnifrf
tqagsevsallgripsavgyqptlatdmgtmqeritttkkgsitsvqaiyvpaddltdpa
pattfahldattvlsraiaelgiypavdpldstsri
>d1efre1 1.59.1.1.1 (358-474) The C-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
mdpnivgsehydvargvqkilqdykslqdiiailgmdelseedkltvsrarkiqrflsqp
fqvaevftghlgklvplketikgfqqilageydhlpeqafymvgpieeavakadkla
>d1efre2 2.37.1.1.1 (9-81) The N-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1efre3 3.29.1.7.2 (82-357) central domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
iripvgpetlgrimnvigepidergpiktkqfaaihaeapefvemsveqeilvtgikvvd
llapyakggkiglfggagvgktvlimelinnvakahggysvfagvgertregndlyhemi
esgvinlkdatskvalvygqmneppgararvaltgltvaeyfrdqegqdvllfidnifrf
tqagsevsallgripsavgyqptlatdmgtmqeritttkkgsitsvqaiyvpaddltdpa
pattfahldattvlsraiaelgiypavdpldstsri
>d1efrf1 1.59.1.1.1 (358-474) The C-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
mdpnivgsehydvargvqkilqdykslqdiiailgmdelseedkltvsrarkiqrflsqp
fqvaevftghlgklvplketikgfqqilageydhlpeqafymvgpieeavakadkla
>d1efrf2 2.37.1.1.1 (9-81) The N-terminal domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1efrf3 3.29.1.7.2 (82-357) central domain of alpha and beta subunits of F1 ATP synthase {bovine (Bos taurus)}
iripvgpetlgrimnvigepidergpiktkqfaaihaeapefvemsveqeilvtgikvvd
llapyakggkiglfggagvgktvlimelinnvakahggysvfagvgertregndlyhemi
esgvinlkdatskvalvygqmneppgararvaltgltvaeyfrdqegqdvllfidnifrf
tqagsevsallgripsavgyqptlatdmgtmqeritttkkgsitsvqaiyvpaddltdpa
pattfahldattvlsraiaelgiypavdpldstsri
>d1efrg_ 1.19.1.1.1 ATP syntase (F1-ATPase), gamma subunit {Bovine (Bos taurus)}
atlkditrrlksikniqkitksmkmvaaakyaraerelkparvygvgslalyekadiktp
edkkkhliigvssdrglcgaihssvakqmkseaanlaaagkevkiigvgdkirsilhrth
sdqflvtfkevgrrpptfgdasvialellnsgyefdegsiifnrfrsvisykteekpifs
ldtissaesmsiyddidadvlrnyqeyslaniiyyslkesttseqsarmtamdnasknas
emidkltltfnrtrqavitkelieiisgaaal
>d1eft_1 2.32.3.1.2 (213-312) Elongation factor Tu (EF-Tu), domain 2 {(Thermus aquaticus)}
pvrdvdkpflmpvedvftitgrgtvatgriergkvkvgdeveivglapetrktvvtgvem
hrktlqegiagdnvglllrgvsreevergqvlakpgsitp
>d1eft_2 2.33.1.1.2 (313-405) Elongation factor Tu (EF-Tu), the C-terminal domain {(Thermus aquaticus)}
htkfeasvyvlkkeeggrhtgffsgyrpqfyfrttdvtgvvrlpqgvemvmpgdnvtftv
elikpvaleeglrfaireggrtvgagvvtkile
>d1eft_3 3.29.1.4.14 (1-212) Elongation factor Tu (EF-Tu), the N-terminal (G) domain {(Thermus aquaticus)}
akgefirtkphvnvgtighvdhgkttltaaltfvtaaenpnvevkdygdidkapeerarg
itintahveyetakrhyshvdcpghadyiknmitgaaqmdgailvvsaadgpmpqtrehi
llarqvgvpyivvfmnkvdmvddpelldlvemevrdllnqyefpgdevpvirgsallale
emhknpktkrgenewvdkiwelldaideyipt
>d1efua1 2.32.3.1.1 (205-296) Elongation factor Tu (EF-Tu), domain 2 {(Escherichia coli)}
aidkpfllpiedvfsisgrgtvvtgrvergiikvgeeveivgiketqkstctgvemfrkl
ldegragenvgvllrgikreeiergqvlakpg
>d1efua2 2.33.1.1.1 (297-393) Elongation factor Tu (EF-Tu), the C-terminal domain {(Escherichia coli)}
tikphtkfesevyilskdeggrhtpffkgyrpqfyfrttdvtgtielpegvemvmpgdni
kmvvtlihpiamddglrfaireggrtvgagvvakvls
>d1efua3 3.29.1.4.13 (9-204) Elongation factor Tu (EF-Tu), the N-terminal (G) domain {(Escherichia coli)}
kphvnvgtighvdhgkttltaaittvlaktyggaarafdqidnapeekargitintshve
ydtptrhyahvdcpghadyvknmitgaaqmdgailvvaatdgpmpqtrehillgrqvgvp
yiivflnkcdmvddeellelvemevrellsqydfpgddtpivrgsalkalegdaeweaki
lelagfldsyipeper
>d1efub1 4.25.1.1.1 (1-139) Elongation factor Ts (EF-Ts), dimerisation domain {(Escherichia coli)}
aeitaslvkelrertgagmmdckkalteangdielaienmrksgaikaakkagnvaadgv
iktkidgnygiilevncqtdfvakdagfqafadkvldaavagkitdvevlkaqfeeerva
lvakigeninirrvaaleg
>d1efub2 4.25.1.1.1 (140-282) Elongation factor Ts (EF-Ts), dimerisation domain {(Escherichia coli)}
dvlgsyqhgarigvlvaakgadeelvkhiamhvaaskpefikpedvsaevvekeyqvqld
iamqsgkpkeiaekmvegrmkkftgevsltgqpfvmepsktvgqllkehnaevtgfirfe
vgegiekvetdfaaevaamskqs
>d1efuc1 2.32.3.1.1 (205-296) Elongation factor Tu (EF-Tu), domain 2 {(Escherichia coli)}
aidkpfllpiedvfsisgrgtvvtgrvergiikvgeeveivgiketqkstctgvemfrkl
ldegragenvgvllrgikreeiergqvlakpg
>d1efuc2 2.33.1.1.1 (297-393) Elongation factor Tu (EF-Tu), the C-terminal domain {(Escherichia coli)}
tikphtkfesevyilskdeggrhtpffkgyrpqfyfrttdvtgtielpegvemvmpgdni
kmvvtlihpiamddglrfaireggrtvgagvvakvls
>d1efuc3 3.29.1.4.13 (9-204) Elongation factor Tu (EF-Tu), the N-terminal (G) domain {(Escherichia coli)}
kphvnvgtighvdhgkttltaaittvlaktyggaarafdqidnapeekargitintshve
ydtptrhyahvdcpghadyvknmitgaaqmdgailvvaatdgpmpqtrehillgrqvgvp
yiivflnkcdmvddeellelvemevrellsqydfpgddtpivrgsalkalegdaeweaki
lelagfldsyipeper
>d1efud1 4.25.1.1.1 (1-139) Elongation factor Ts (EF-Ts), dimerisation domain {(Escherichia coli)}
aeitaslvkelrertgagmmdckkalteangdielaienmrksgaikaakkagnvaadgv
iktkidgnygiilevncqtdfvakdagfqafadkvldaavagkitdvevlkaqfeeerva
lvakigeninirrvaaleg
>d1efud2 4.25.1.1.1 (140-282) Elongation factor Ts (EF-Ts), dimerisation domain {(Escherichia coli)}
dvlgsyqhgarigvlvaakgadeelvkhiamhvaaskpefikpedvsaevvekeyqvqld
iamqsgkpkeiaekmvegrmkkftgevsltgqpfvmepsktvgqllkehnaevtgfirfe
vgegiekvetdfaaevaamskqs
>d1efva1 3.24.1.2.1 (208-331) C-terminal domain of the electron transfer flavoprotein alpha subunit {Human (Homo sapiens)}
drpeltgakvvvsggrglksgenfkllydladqlhaavgasraavdagfvpndmqvgqtg
kivapelyiavgisgaiqhlagmkdsktivainkdpeapifqvadygivadlfkvvpemt
eilk
>d1efva2 3.32.1.1.1 (20-207) Electron transfer flavoprotein {Human (Homo sapiens)}
qstlviaehandslapitlntitaatrlggevsclvagtkcdkvaqdlckvagiakvlva
qhdvykgllpeeltplilatqkqfnythicagasafgknllprvaaklevapisdiiaik
spdtfvrtiyagnalctvkcdekvkvfsvrgtsfdaaatsggsassekasstspveisew
ldqkltks
>d1eg1a_ 2.21.1.8.2 Endoglucanase I {(Trichoderma reesei)}
qpgtstpevhpklttykctksggcvaqdtsvvldwnyrwmhdanynsctvnggvnttlcp
deatcgkncfiegvdyaasgvttsgssltmnqympsssggyssvsprlylldsdgeyvml
klngqelsfdvdlsalpcgengslylsqmdengganqyntaganygsgycdaqcpvqtwr
ngtlntshqgfccnemdilegnsranaltphsctatacdsagcgfnpygsgyksyygpgd
tvdtsktftiitqfntdngspsgnlvsitrkyqqngvdipsaqpggdtisscpsasaygg
latmgkalssgmvlvfsiwndnsqymnwldsgnagpcsstegnpsnilannpnthvvfsn
irwgdigstt
>d1eg1c_ 2.21.1.8.2 Endoglucanase I {(Trichoderma reesei)}
qpgtstpevhpklttykctksggcvaqdtsvvldwnyrwmhdanynsctvnggvnttlcp
deatcgkncfiegvdyaasgvttsgssltmnqympsssggyssvsprlylldsdgeyvml
klngqelsfdvdlsalpcgengslylsqmdengganqyntaganygsgycdaqcpvqtwr
ngtlntshqgfccnemdilegnsranaltphsctatacdsagcgfnpygsgyksyygpgd
tvdtsktftiitqfntdngspsgnlvsitrkyqqngvdipsaqpggdtisscpsasaygg
latmgkalssgmvlvfsiwndnsqymnwldsgnagpcsstegnpsnilannpnthvvfsn
irwgdigstt
>d1egca1 1.24.6.1.3 (242-396) Medium chain acyl-CoA dehydrogenase {human (homo sapiens)}
gagfkvamgafdkerpvvaagavglaqraldeatkyalerktfgkllvehqaisfmlaem
amkvelarmsyqraawevdsgrrntyyasiakafagdianqlatdavqilggngfnteyp
veklmrdakiyqiyggtsqiqrlivarehidkykn
>d1egca2 5.7.1.1.3 (10-241) Medium chain acyl-CoA dehydrogenase {human (homo sapiens)}
lgfsfefteqqkefqatarkfareeiipvaaeydktgeypvplirrawelglmnthipen
cgglglgtfdacliseelaygctgvqtaiegnslgqmpiiiagndqqkkkylgrmteepl
mcaycvtepgagsdvagiktkaekkgdeyiingqkmwitnggkanwyfllarsdpdpkap
ankaftgfiveadtpgiqigrkelnmgqrcsdtrgivfedvkvpkenvligd
>d1egcb1 1.24.6.1.3 (242-396) Medium chain acyl-CoA dehydrogenase {human (homo sapiens)}
gagfkvamgafdkerpvvaagavglaqraldeatkyalerktfgkllvehqaisfmlaem
amkvelarmsyqraawevdsgrrntyyasiakafagdianqlatdavqilggngfnteyp
veklmrdakiyqiyggtsqiqrlivarehidkykn
>d1egcb2 5.7.1.1.3 (10-241) Medium chain acyl-CoA dehydrogenase {human (homo sapiens)}
lgfsfefteqqkefqatarkfareeiipvaaeydktgeypvplirrawelglmnthipen
cgglglgtfdacliseelaygctgvqtaiegnslgqmpiiiagndqqkkkylgrmteepl
mcaycvtepgagsdvagiktkaekkgdeyiingqkmwitnggkanwyfllarsdpdpkap
ankaftgfiveadtpgiqigrkelnmgqrcsdtrgivfedvkvpkenvligd
>d1egcc1 1.24.6.1.3 (242-396) Medium chain acyl-CoA dehydrogenase {human (homo sapiens)}
gagfkvamgafdkerpvvaagavglaqraldeatkyalerktfgkllvehqaisfmlaem
amkvelarmsyqraawevdsgrrntyyasiakafagdianqlatdavqilggngfnteyp
veklmrdakiyqiyggtsqiqrlivarehidkykn
>d1egcc2 5.7.1.1.3 (10-241) Medium chain acyl-CoA dehydrogenase {human (homo sapiens)}
lgfsfefteqqkefqatarkfareeiipvaaeydktgeypvplirrawelglmnthipen
cgglglgtfdacliseelaygctgvqtaiegnslgqmpiiiagndqqkkkylgrmteepl
mcaycvtepgagsdvagiktkaekkgdeyiingqkmwitnggkanwyfllarsdpdpkap
ankaftgfiveadtpgiqigrkelnmgqrcsdtrgivfedvkvpkenvligd
>d1egcd1 1.24.6.1.3 (242-396) Medium chain acyl-CoA dehydrogenase {human (homo sapiens)}
gagfkvamgafdkerpvvaagavglaqraldeatkyalerktfgkllvehqaisfmlaem
amkvelarmsyqraawevdsgrrntyyasiakafagdianqlatdavqilggngfnteyp
veklmrdakiyqiyggtsqiqrlivarehidkykn
>d1egcd2 5.7.1.1.3 (10-241) Medium chain acyl-CoA dehydrogenase {human (homo sapiens)}
lgfsfefteqqkefqatarkfareeiipvaaeydktgeypvplirrawelglmnthipen
cgglglgtfdacliseelaygctgvqtaiegnslgqmpiiiagndqqkkkylgrmteepl
mcaycvtepgagsdvagiktkaekkgdeyiingqkmwitnggkanwyfllarsdpdpkap
ankaftgfiveadtpgiqigrkelnmgqrcsdtrgivfedvkvpkenvligd
>d1egda1 1.24.6.1.3 (242-396) Medium chain acyl-CoA dehydrogenase {human (homo sapiens)}
gagfkvamgafdkerpvvaagavglaqraldeatkyalerktfgkllvehqaisfmlaem
amkvelarmsyqraawevdsgrrntyyasiakafagdianqlatdavqilggngfnteyp
veklmrdakiyqiyggtsqiqrlivarehidkykn
>d1egda2 5.7.1.1.3 (10-241) Medium chain acyl-CoA dehydrogenase {human (homo sapiens)}
lgfsfefteqqkefqatarkfareeiipvaaeydktgeypvplirrawelglmnthipen
cgglglgtfdacliseelaygctgvqtaiegnslgqmpiiiagndqqkkkylgrmteepl
mcaycvtepgagsdvagiktkaekkgdeyiingqkmwitnggkanwyfllarsdpdpkap
ankaftgfiveadtpgiqigrkelnmgqrcsdtrgivfedvkvpkenvligd
>d1egdb1 1.24.6.1.3 (242-396) Medium chain acyl-CoA dehydrogenase {human (homo sapiens)}
gagfkvamgafdkerpvvaagavglaqraldeatkyalerktfgkllvehqaisfmlaem
amkvelarmsyqraawevdsgrrntyyasiakafagdianqlatdavqilggngfnteyp
veklmrdakiyqiyggtsqiqrlivarehidkykn
>d1egdb2 5.7.1.1.3 (10-241) Medium chain acyl-CoA dehydrogenase {human (homo sapiens)}
lgfsfefteqqkefqatarkfareeiipvaaeydktgeypvplirrawelglmnthipen
cgglglgtfdacliseelaygctgvqtaiegnslgqmpiiiagndqqkkkylgrmteepl
mcaycvtepgagsdvagiktkaekkgdeyiingqkmwitnggkanwyfllarsdpdpkap
ankaftgfiveadtpgiqigrkelnmgqrcsdtrgivfedvkvpkenvligd
>d1egdc1 1.24.6.1.3 (242-396) Medium chain acyl-CoA dehydrogenase {human (homo sapiens)}
gagfkvamgafdkerpvvaagavglaqraldeatkyalerktfgkllvehqaisfmlaem
amkvelarmsyqraawevdsgrrntyyasiakafagdianqlatdavqilggngfnteyp
veklmrdakiyqiyggtsqiqrlivarehidkykn
>d1egdc2 5.7.1.1.3 (10-241) Medium chain acyl-CoA dehydrogenase {human (homo sapiens)}
lgfsfefteqqkefqatarkfareeiipvaaeydktgeypvplirrawelglmnthipen
cgglglgtfdacliseelaygctgvqtaiegnslgqmpiiiagndqqkkkylgrmteepl
mcaycvtepgagsdvagiktkaekkgdeyiingqkmwitnggkanwyfllarsdpdpkap
ankaftgfiveadtpgiqigrkelnmgqrcsdtrgivfedvkvpkenvligd
>d1egdd1 1.24.6.1.3 (242-396) Medium chain acyl-CoA dehydrogenase {human (homo sapiens)}
gagfkvamgafdkerpvvaagavglaqraldeatkyalerktfgkllvehqaisfmlaem
amkvelarmsyqraawevdsgrrntyyasiakafagdianqlatdavqilggngfnteyp
veklmrdakiyqiyggtsqiqrlivarehidkykn
>d1egdd2 5.7.1.1.3 (10-241) Medium chain acyl-CoA dehydrogenase {human (homo sapiens)}
lgfsfefteqqkefqatarkfareeiipvaaeydktgeypvplirrawelglmnthipen
cgglglgtfdacliseelaygctgvqtaiegnslgqmpiiiagndqqkkkylgrmteepl
mcaycvtepgagsdvagiktkaekkgdeyiingqkmwitnggkanwyfllarsdpdpkap
ankaftgfiveadtpgiqigrkelnmgqrcsdtrgivfedvkvpkenvligd
>d1egea1 1.24.6.1.3 (242-396) Medium chain acyl-CoA dehydrogenase {human (homo sapiens)}
gagfkvamgafdktrpvvaagavglaqraldeatkyalerktfgkllvehqaisfmlaem
amkvelarmsyqraawevdsgrrntyyasiakafagdianqlatdavqilggngfnteyp
veklmrdakiyqiyegtsqiqrlivarehidkykn
>d1egea2 5.7.1.1.3 (10-241) Medium chain acyl-CoA dehydrogenase {human (homo sapiens)}
lgfsfefteqqkefqatarkfareeiipvaaeydktgeypvplirrawelglmnthipen
cgglglgtfdacliseelaygctgvqtaiegnslgqmpiiiagndqqkkkylgrmteepl
mcaycvtepgagsdvagiktkaekkgdeyiingqkmwitnggkanwyfllarsdpdpkap
ankaftgfiveadtpgiqigrkelnmgqrcsdtrgivfedvkvpkenvligd
>d1egeb1 1.24.6.1.3 (242-396) Medium chain acyl-CoA dehydrogenase {human (homo sapiens)}
gagfkvamgafdktrpvvaagavglaqraldeatkyalerktfgkllvehqaisfmlaem
amkvelarmsyqraawevdsgrrntyyasiakafagdianqlatdavqilggngfnteyp
veklmrdakiyqiyegtsqiqrlivarehidkykn
>d1egeb2 5.7.1.1.3 (10-241) Medium chain acyl-CoA dehydrogenase {human (homo sapiens)}
lgfsfefteqqkefqatarkfareeiipvaaeydktgeypvplirrawelglmnthipen
cgglglgtfdacliseelaygctgvqtaiegnslgqmpiiiagndqqkkkylgrmteepl
mcaycvtepgagsdvagiktkaekkgdeyiingqkmwitnggkanwyfllarsdpdpkap
ankaftgfiveadtpgiqigrkelnmgqrcsdtrgivfedvkvpkenvligd
>d1egec1 1.24.6.1.3 (242-396) Medium chain acyl-CoA dehydrogenase {human (homo sapiens)}
gagfkvamgafdktrpvvaagavglaqraldeatkyalerktfgkllvehqaisfmlaem
amkvelarmsyqraawevdsgrrntyyasiakafagdianqlatdavqilggngfnteyp
veklmrdakiyqiyegtsqiqrlivarehidkykn
>d1egec2 5.7.1.1.3 (10-241) Medium chain acyl-CoA dehydrogenase {human (homo sapiens)}
lgfsfefteqqkefqatarkfareeiipvaaeydktgeypvplirrawelglmnthipen
cgglglgtfdacliseelaygctgvqtaiegnslgqmpiiiagndqqkkkylgrmteepl
mcaycvtepgagsdvagiktkaekkgdeyiingqkmwitnggkanwyfllarsdpdpkap
ankaftgfiveadtpgiqigrkelnmgqrcsdtrgivfedvkvpkenvligd
>d1eged1 1.24.6.1.3 (242-396) Medium chain acyl-CoA dehydrogenase {human (homo sapiens)}
gagfkvamgafdktrpvvaagavglaqraldeatkyalerktfgkllvehqaisfmlaem
amkvelarmsyqraawevdsgrrntyyasiakafagdianqlatdavqilggngfnteyp
veklmrdakiyqiyegtsqiqrlivarehidkykn
>d1eged2 5.7.1.1.3 (10-241) Medium chain acyl-CoA dehydrogenase {human (homo sapiens)}
lgfsfefteqqkefqatarkfareeiipvaaeydktgeypvplirrawelglmnthipen
cgglglgtfdacliseelaygctgvqtaiegnslgqmpiiiagndqqkkkylgrmteepl
mcaycvtepgagsdvagiktkaekkgdeyiingqkmwitnggkanwyfllarsdpdpkap
ankaftgfiveadtpgiqigrkelnmgqrcsdtrgivfedvkvpkenvligd
>d1egf__ 7.3.9.1.11 Epidermal growth factor, EGF {mouse (Mus musculus)}
nsypgcpssydgyclnggvcmhiesldsytcncvigysgdrcqtrdlrwwelr
>d1egl__ 4.22.1.1.1 Eglin C {leech (Hirudo medicinalis)}
tefgselksfpevvgktvdqareyftlhypqydvyflpegspvtldlrynrvrvfynpgt
nvvnhvphvg
>d1ego__ 3.38.1.1.5 Glutaredoxin {(bacteriophage t4)}
mqtvifgrsgcpycvrakdlaeklsnerddfqyqyvdiraegitkedlqqkagkpvetvp
qifvdqqhiggytdfaawvkenlda
>e1egp.1a 4.22.1.1.1 Eglin C {leech (Hirudo medicinalis)}
lksfpevvgktvdqareyftlhypqynvyflpegspvtl
>e1egp.1b 4.22.1.1.1 Eglin C {leech (Hirudo medicinalis)}
ynrvrvfynpgtnvvnhvphvg
>d1egr__ 3.38.1.1.5 Glutaredoxin {(bacteriophage t4)}
mqtvifgrsgcpycvrakdlaeklsnerddfqyqyvdiraegitkedlqqkagkpvetvp
qifvdqqhiggytdfaawvkenlda
>d1ehc__ 3.14.2.1.1 CheY protein {(Escherichia coli)}
adkelkflvvdkfstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmp
nmdglellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleekln
kifeklgm
>d1ehs__ 7.2.1.1.1 Heat-stable enterotoxin B {(Escherichia coli)}
stqsnkkdlcehyrqiakesckkgflgvrdgtagacfgaqimvaakgc
>d1eit__ 7.3.5.2.2 mu-Agatoxin-I {funnel web spider (Agelenopsis aperta)}
ecvpenghcrdwydeccegfycscrqppkcicrnnn
>d1elaa_ 2.35.1.2.14 Elastase {porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1elba_ 2.35.1.2.14 Elastase {porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1elca_ 2.35.1.2.14 Elastase {porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1elde_ 2.35.1.2.14 Elastase {porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1elee_ 2.35.1.2.14 Elastase {porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1elf__ 2.35.1.2.14 Elastase {porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1elg__ 2.35.1.2.14 Elastase {porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1elo_1 2.32.3.1.4 (283-399) Elongation factor G (EF-G), domain II {(Thermus thermophilus)}
pldippikgttpegevveihpdpngplaalafkimadpyvgrltfirvysgtltsgsyvy
nttkgrkervarllrmhanhreeveelkagdlgavvglketitgdtlvgedaprvil
>d1elo_2 3.29.1.4.16 (5-282) Elongation factor G (EF-G), the N-terminal (G) domain {(Thermus thermophilus)}
veydlkrlrnigiaahidagktttterilyytgrihkigevhegaatmdfmeqerergit
itaavttcfwkdhriniidtpghvdftieversmrvldgaivvfdssqgvepqsetvwrq
aekykvpriafankmdktgadlwlvirtmqerlgarpvvmqlpigredtfsgiidvlrmk
aytygndlgtdireipipeeyldqareyheklvevaadfdenimlkylegeepteeelva
airkgtidlkitpvflgsalknkgvqllldavvdylps
>d1elo_3 4.10.1.1.1 (477-599) Elongation factor G (EF-G), domain IV {(Thermus thermophilus)}
gkpqvayretitkpvdvegkfirqtggrgqyghvkikveplprgsgfefvnaivggvipk
eyipavqkgieeamqsgpligfpvvdikvtlydgsyhevdssemafkiagsmaikeavqk
gdp
>d1elo_4 4.34.13.1.1 (600-689) Elongation factor G (EF-G), domain V {(Thermus thermophilus)}
vilepimrvevttpeeymgdvigdlnarrgqilgmeprgnaqvirafvplaemfgyatdl
rsktqgrgsfvmffdhyqevpkqvqeklik
>d1elpa1 2.9.1.1.2 (1-85) gamma-Crystallin {bovine (Bos taurus) isoform IIIb (D)}
gkitfyedrgfqgrhyecssdhsnlqpylgrcnsvrvdsgcwmiyeqpnylgpqyflrrg
dypdyqqwmglndsirscrliphag
>d1elpa2 2.9.1.1.2 (87-174) gamma-Crystallin {bovine (Bos taurus) isoform IIIb (D)}
shrlrlyeredyrgqmieitedcsslqdrfhfneihslnvlegswvlyelpnyrgrqyll
rpgeyrryhdwgamnakvgslrrvidiy
>d1elpb1 2.9.1.1.2 (1-85) gamma-Crystallin {bovine (Bos taurus) isoform IIIb (D)}
gkitfyedrgfqgrhyecssdhsnlqpylgrcnsvrvdsgcwmiyeqpnylgpqyflrrg
dypdyqqwmglndsirscrliphag
>d1elpb2 2.9.1.1.2 (87-174) gamma-Crystallin {bovine (Bos taurus) isoform IIIb (D)}
shrlrlyeredyrgqmieitedcsslqdrfhfneihslnvlegswvlyelpnyrgrqyll
rpgeyrryhdwgamnakvgslrrvidiy
>d1els_1 3.1.6.1.1 (142-436) Enolase {baker's yeast (Saccharomyces cerevisiae)}
spyvlpvpflnvlnggshaggalalqefmiaptgaktfaealrigsevyhnlksltkkry
gasagnvgdeggvapniqtaeealdlivdaikaaghdgkvkigldcasseffkdgkydld
fknpnsdkskwltgpqladlyhslmkrypivsiedpfaeddweawshffktagiqivadd
ltvtnpkriataiekkaadalllkvnqigtlsesikaaqdsfaagwgvmvshrsgetedt
fiadlvvglrtgqiktgaparserlaklnqllrieeelgdnavfagenfhhgdkl
>d1els_2 4.32.1.1.1 (1-141) Enolase {baker's yeast (Saccharomyces cerevisiae)}
avskvyarsvydsrgnptvevelttekgvfrsivpsgastgvhealemrdgdkskwmgkg
vlhavknvndviapafvkanidvsdqkavddflisldgtanksklganailgvslaasra
aaaeknvplykhladlskskt
>d1elt__ 2.35.1.2.15 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__ 4.17.1.1.1 Green fluorescent protein {Jellyfish (Aequorea victoria)}
skgeelftgvvpilveldgdvnghkfsvsgegegdatygkltlkficttgklpvpwptlv
ttfxvqcfsrypdhxkrhdffksaxpegyvqertiffkddgnyktraevkfegdtlvnri
elkgidfkedgnilghkleynynshnvyixadkqkngikvnfkirhniedgsvqladhyq
qntpigdgpvllpdnhylstqsalskdpnekrdhxvllefvtaagi
>d1emb__ 4.17.1.1.1 Green fluorescent protein {Jellyfish (Aequorea victoria)}
skgeelftgvvpilveldgdvnghkfsvsgegegdatygkltlkficttgklpvpwptlv
ttfxvqcfsrypdhmkrhdffksampegyvqertiffkddgnyktraevkfegdtlvnri
elkgidfkedgnilghkleynynshnvyimadkqkngikvnfkirhniedgsvqladhyq
qntpigdgpvllpdnhylstqsalskdpnekrdhmvllefvtaagi
>d1emca_ 4.17.1.1.1 Green fluorescent protein {Jellyfish (Aequorea victoria)}
geelftgvvpilveldgdvnghkfsvsgegegdatygkltlkficttgklpvpwptlvtt
lxvqcfsrypdhmkrhdffksampegyvqertiffkddgnyktraevkfegdtlvnriel
kgidfkedgnilghkleynynshnvyimadkqkngikvnfktrhniedgsvqladhyqqn
tpigdgpvllpdnhylstqsalskdpnekrdhmvllefvtaagit
>d1emcb_ 4.17.1.1.1 Green fluorescent protein {Jellyfish (Aequorea victoria)}
geelftgvvpilveldgdvnghkfsvsgegegdatygkltlkficttgklpvpwptlvtt
lxvqcfsrypdhmkrhdffksampegyvqertiffkddgnyktraevkfegdtlvnriel
kgidfkedgnilghkleynynshnvyimadkqkngikvnfktrhniedgsvqladhyqqn
tpigdgpvllpdnhylstqsalskdpnekrdhmvllefvtaagit
>d1emcc_ 4.17.1.1.1 Green fluorescent protein {Jellyfish (Aequorea victoria)}
geelftgvvpilveldgdvnghkfsvsgegegdatygkltlkficttgklpvpwptlvtt
lxvqcfsrypdhmkrhdffksampegyvqertiffkddgnyktraevkfegdtlvnriel
kgidfkedgnilghkleynynshnvyimadkqkngikvnfktrhniedgsvqladhyqqn
tpigdgpvllpdnhylstqsalskdpnekrdhmvllefvtaagith
>d1emcd_ 4.17.1.1.1 Green fluorescent protein {Jellyfish (Aequorea victoria)}
geelftgvvpilveldgdvnghkfsvsgegegdatygkltlkficttgklpvpwptlvtt
lxvqcfsrypdhmkrhdffksampegyvqertiffkddgnyktraevkfegdtlvnriel
kgidfkedgnilghkleynynshnvyimadkqkngikvnfktrhniedgsvqladhyqqn
tpigdgpvllpdnhylstqsalskdpnekrdhmvllefvtaagit
>d1emd_1 3.22.1.5.2 (1-145) Malate dehydrogenase {(Escherichia coli)}
mkvavlgaaggigqalalllktqlpsgselslydiapvtpgvavdlshiptavkikgfsg
edatpalegadvvlisagvrrkpgmdrsdlfnvnagivknlvqqvaktcpkacigiitnp
vnttvaiaaevlkkagvydknklfg
>d1emd_2 4.100.1.1.2 (146-312) Malate dehydrogenase {(Escherichia coli)}
vttldiirsntfvaelkgkqpgevevpvigghsgvtilpllsqvpgvsfteqevadltkr
iqnagtevveakagggsatlsmgqaaarfglslvralqgeqgvvecayvegdgqyarffs
qplllgkngveerksigtlsafeqnalegmldtlkkdialgqefvnk
>d1eme__ 4.17.1.1.1 Green fluorescent protein {Jellyfish (Aequorea victoria)}
elftgvvpilveldgdvnghkfsvsgegegdatygkltlkficttgklpvpwptlvttlx
vqcfsrypdhmkrhdffksampegyvqertiffkddgnyktraevkfegdtlvnrielkg
idfkedgnilghkleynynshnvyimadkqkngikvnfktrhniedgsvqladhyqqntp
igdgpvllpdnhylstqsalskdpnekrdhmvllefvtaagit
>d1emf__ 4.17.1.1.1 Green fluorescent protein {Jellyfish (Aequorea victoria)}
elftgvvpilveldgdvnghkfsvsgegegdatygkltlkficttgklpvpwptlvttlx
vqcfsrypdhmkrhdffksampegyvqertiffkddgnyktraevkfegdtlvnrielkg
idfkedgnilghkleynynshnvyimadkqkngikanfkirhniedgsvqladhyqqntp
igdgpvllpdnhylstqsalskdpnekrdhmvllefvtaagit
>d1emk__ 4.17.1.1.1 Green fluorescent protein {Jellyfish (Aequorea victoria)}
elftgvvpilveldgdvnghkfsvsgegegdatygkltlkficttgklpvpwptlvttlx
vqcfsrypdhmkrhdffksampegyvqertiffkddgnyktraevkfegdtlvnrielkg
idfkedgnilghkleynynshnvyimadkqkngikvnfktrhniedgsvqladhyqqntp
igdgpvllpdnhylstqsalskdpnekrdhmvllefvtaagi
>d1eml__ 4.17.1.1.1 Green fluorescent protein {Jellyfish (Aequorea victoria)}
lftgvvpilveldgdvnghkfsvsgegegdatygkltlkficttgklpvpwptlvttlxv
qcfsrypdhmkrhdffksampegyvqertiffkddgnyktraevkfegdtlvnrielkgi
dfkedgnilghkleynynshnvyimadkqkngikvnfktrhniedgsvqladhyqqntpi
gdgpvllpdnhylstqsalskdpnekrdhmvllefvtaagi
>d1emm__ 4.17.1.1.1 Green fluorescent protein {Jellyfish (Aequorea victoria)}
lftgvvpilveldgdvnghkfsvsgegegdatygkltlkficttgklpvpwptlvttlxv
qcfsrypdhmkrhdffksampegyvqertiffkddgnyktraevkfegdtlvnrielkgi
dfkedgnilghkleynynshnvyimadkqkngikvnfkirhniedgsvqladhyqqntpi
gdgpvllpdnhylstqsalskdpnekrdhmvllefvtaagi
>d1emn_1 7.3.9.1.17 (2124-2166) Fibrillin-1 fragment (residues 2124-2205) {Human (Homo sapiens)}
savdmdeckepdvckhgqcintdgsyrcecpfgyilagnecvd
>d1emn_2 7.3.9.1.17 (2167-2205) Fibrillin-1 fragment (residues 2124-2205) {Human (Homo sapiens)}
tdecsvgnpcgngtcknviggfectceegfepgpmmtce
>d1emo_1 7.3.9.1.17 (2124-2166) Fibrillin-1 fragment (residues 2124-2205) {Human (Homo sapiens)}
savdmdeckepdvckhgqcintdgsyrcecpfgyilagnecvd
>d1emo_2 7.3.9.1.17 (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__ 2.29.1.1.1 Staphylococcal nuclease {(Staphylococcal aureus)}
lhkepatlikaidgetvklmykgqpmtfrlllvdtpetkhpkkgvekygpeasaftkkmv
enakkievefdkgqrtdkygrglayiyadgkmvnealvrqglakvayvykpnntheqhlr
kseaqakkeklniws
>d1enc__ 2.29.1.1.1 Staphylococcal nuclease {(Staphylococcal aureus)}
lhkepatlikaidgetvklmykgqpmtfrlllvdtpetkhpkkgvekygpeasaftkkmv
enakkievefdkgqrtdkygrglayiyadgkmvnealvrqglakvayvykpnntheqhlr
kseaqakkeklniws
>d1enh__ 1.4.1.1.1 engrailed Homeodomain {(Drosophila melanogaster)}
rprtafsseqlarlkrefnenrylterrrqqlsselglneaqikiwfqnkraki
>d1eni__ 1.17.1.1.1 T4 endonuclease V {(Escherichia coli) bacteriophage T4}
tqinltlvseladqhlmaeyrelprvfgavrkhvangkrvrdfkisptfilgaghvtffy
dkleflrkrqieliaeclkrgfnikdttvqdisdipqefrgdyipheasiaisqarldek
iaqrptwykyygkaiya
>d1enj__ 1.17.1.1.1 T4 endonuclease V {(Escherichia coli) bacteriophage T4}
trinltlvseladqhlmaeyrqlprvfgavrkhvangkrvrdfkisptfilgaghvtffy
dkleflrkrqieliaeclkrgfnikdttvqdisdipqefrgdyipheasiaisqarldek
iaqrptwykyygkaiya
>d1enk__ 1.17.1.1.1 T4 endonuclease V {(Escherichia coli) bacteriophage T4}
trinltlvseladqhlmaeyrdlprvfgavrkhvangkrvrdfkisptfilgaghvtffy
dkleflrkrqieliaeclkrgfnikdttvqdisdipqefrgdyipheasiaisqarldek
iaqrptwykyygkaiya
>d1eno__ 3.22.1.2.9 Enoyl-ACP reductase {Oil seed rape (Brassica napus)}
lpidlrgkrafiagiaddngygwavakslaaagaeilvgtwvpalnifetslrrgkfdqs
rvlpdgslmeikkvypldavfdnpedvpedvkankryagssnwtvqeaaecvrqdfgsid
ilvhslangpevskplletsrkgylaaisassysfvsllshflpimnpggasisltyias
eriipgygggmssakaalesdtrvlafeagrkqnirvntisagplgsraakaigfidtmi
eysynnapiqktltadevgnaaaflvsplasaitgatiyvdnglnsmgvaldspvfk
>d1enp__ 3.22.1.2.9 Enoyl-ACP reductase {Oil seed rape (Brassica napus)}
lpidlrgkrafiagiaddngygwavakslaaagaeilvgtwvpalnifetslrrgkfdqs
rvlpdgslmeikkvypldavfdnpedvpedvkankryagssnwtvqeaaecvrqdfgsid
ilvhslangpevskplletsrkgylaaisassysfvsllshflpimnpggasisltyias
eriipgygggmssakaalesdtrvlafeagrkqnirvntisagplgsraakaigfidtmi
eysynnapiqktltadevgnaaaflvsplasaitgatiyvdnglnsmgvaldspvfk
>d1enqa_ 2.21.1.1.1 Concanavalin A {jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1enqb_ 2.21.1.1.1 Concanavalin A {jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1enqc_ 2.21.1.1.1 Concanavalin A {jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1enqd_ 2.21.1.1.1 Concanavalin A {jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1enr__ 2.21.1.1.1 Concanavalin A {jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1ensa_ 2.21.1.1.1 Concanavalin A {jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1ensb_ 2.21.1.1.1 Concanavalin A {jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1ente_ 2.38.1.2.1 Endothiapepsin {chestnut blight fungus (Endothia parasitica)}
stgsatttpidslddayitpvqigtpaqtlnldfdtgssdlwvfssettasevdgqtiyt
psksttakllsgatwsisygdgssssgdvytdtvsvggltvtgqavesakkvsssfteds
tidgllglafstlntvsptqqktffdnakasldspvftadlgyhapgtynfgfidttayt
gsitytavstkqgfwewtstgyavgsgtfkstsidgiadtgttllylpatvvsaywaqvs
gakssssvggyvfpcsatlpsftfgvgsarivipgdyidfgpistgssscfggiqssagi
ginifgdvalkaafvvfngattptlgfask
>d1enva_ 6.2.2.1.1 HIV-1 gp41 protease-resistant core {(human immunodeficiency virus type 1)}
qiedkieeilskiyhieneiarikkligearqllsgivqqqnnllraieaqqhllqltvw
gikqlqarilaverylkdqnnmtwmewdreinnytslihslieesqnqqekneqelleld
k
>d1enxa_ 2.21.1.9.4 Xylanase II {(Trichoderma reesei) xynII}
xtiqpgtgynngyfysywndghggvtytngpggqfsvnwsnsgnfvggkgwqpgtknkvi
nfsgsynpngnsylsvygwsrnplieyyivenfgtynpstgatklgevtsdgsvydiyrt
qrvnqpsiigtatfyqywsvrrnhrssgsvntanhfnawaqqgltlgtmdyqivavegyf
ssgsasitvs
>d1enxb_ 2.21.1.9.4 Xylanase II {(Trichoderma reesei) xynII}
xtiqpgtgynngyfysywndghggvtytngpggqfsvnwsnsgnfvggkgwqpgtknkvi
nfsgsynpngnsylsvygwsrnplieyyivenfgtynpstgatklgevtsdgsvydiyrt
qrvnqpsiigtatfyqywsvrrnhrssgsvntanhfnawaqqgltlgtmdyqivavegyf
ssgsasitvs
>d1eny__ 3.22.1.2.10 Enoyl-ACP reductase {TB (Mycobacterium tuberculosis), gene InhA}
aglldgkrilvsgiitdssiafhiarvaqeqgaqlvltgfdrlrliqritdrlpakapll
eldvqneehlaslagrvteaigagnkldgvvhsigfmpqtgmginpffdapyadvskgih
isaysyasmakallpimnpggsivgmdfdpsrampaynwmtvaksalesvnrfvareagk
ygvrsnlvaagpirtlamsaivggalgeeagaqiqlleegwdqrapigwnmkdatpvakt
vcallsdwlpattgdiiyadggahtqll
>d1enz__ 3.22.1.2.10 Enoyl-ACP reductase {TB (Mycobacterium tuberculosis), gene InhA}
aglldgkrilvsgiitdssiafhiarvaqeqgaqlvltgfdrlrliqritdrlpakapll
eldvqneehlaslagrvteaigagnkldgvvhaigfmpqtgmginpffdapyadvskgih
isaysyasmakallpimnpggsivgmdfdpsrampaynwmtvaksalesvnrfvareagk
ygvrsnlvaagpirtlamsaivggalgeeagaqiqlleegwdqrapigwnmkdatpvakt
vcallsdwlpattgdiiyadggahtqll
>d1epaa_ 2.45.1.1.8 Retinoic acid-binding protein {rat (Rattus norvegicus, albino)}
vkdfdiskflgfwyeiafaskmgtpglahkeekmgamvvelkenllaltttyysedhcvl
ekvtategdgpakfqvtrlsgkkevvveatdyltyaiiditslvagavhrtmklysrsld
dngealynfrkitsdhgfsetdlyilkhdltcvkvlqsaa
>d1epab_ 2.45.1.1.8 Retinoic acid-binding protein {rat (Rattus norvegicus, albino)}
avvkdfdiskflgfwyeiafaskmgtpglahkeekmgamvvelkenllaltttyysedhc
vlekvtategdgpakfqvtrlsgkkevvveatdyltyaiiditslvagavhrtmklysrs
lddngealynfrkitsdhgfsetdlyilkhdltcvkvlqsaaes
>d1epba_ 2.45.1.1.8 Retinoic acid-binding protein {rat (Rattus norvegicus, albino)}
vkdfdiskflgfwyeiafaskmgtpglahkeekmgamvvelkenllaltttyysedhcvl
ekvtategdgpakfqvtrlsgkkevvveatdyltyaiiditslvagavhrtmklysrsld
dngealynfrkitsdhgfsetdlyilkhdltcvkvlqsaa
>d1epbb_ 2.45.1.1.8 Retinoic acid-binding protein {rat (Rattus norvegicus, albino)}
avvkdfdiskflgfwyeiafaskmgtpglahkeekmgamvvelkenllaltttyysedhc
vlekvtategdgpakfqvtrlsgkkevvveatdyltyaiiditslvagavhrtmklysrs
lddngealynfrkitsdhgfsetdlyilkhdltcvkvlqsaaes
>d1epg__ 7.3.9.1.11 Epidermal growth factor, EGF {mouse (Mus musculus)}
nsypgcpssydgyclnggvcmhiesldsytcncvigysgdrcqtrdlrwwelr
>d1eph__ 7.3.9.1.11 Epidermal growth factor, EGF {mouse (Mus musculus)}
nsypgcpssydgyclnggvcmhiesldsytcncvigysgdrcqtrdlrwwelr
>d1epi__ 7.3.9.1.11 Epidermal growth factor, EGF {mouse (Mus musculus)}
nsypgcpssydgyclnggvcmhiesldsytcncvigysgdrcqtrdlrwwelr
>d1epj__ 7.3.9.1.11 Epidermal growth factor, EGF {mouse (Mus musculus)}
nsypgcpssydgyclnggvcmhiesldsytcncvigysgdrcqtrdlrwwelr
>d1eple_ 2.38.1.2.1 Endothiapepsin {chestnut blight fungus (Endothia parasitica)}
stgsatttpidslddayitpvqigtpaqtlnldfdtgssdlwvfssettasevdgqtiyt
psksttakllsgatwsisygdgssssgdvytdtvsvggltvtgqavesakkvsssfteds
tidgllglafstlntvsptqqktffdnakasldspvftadlgyhapgtynfgfidttayt
gsitytavstkqgfwewtstgyavgsgtfkstsidgiadtgttllylpatvvsaywaqvs
gakssssvggyvfpcsatlpsftfgvgsarivipgdyidfgpistgssscfggiqssagi
ginifgdvalkaafvvfngattptlgfask
>d1epme_ 2.38.1.2.1 Endothiapepsin {chestnut blight fungus (Endothia parasitica)}
stgsatttpidslddayitpvqigtpaqtlnldfdtgssdlwvfssettasevdgqtiyt
psksttakllsgatwsisygdgssssgdvytdtvsvggltvtgqavesakkvsssfteds
tidgllglafstlntvsptqqktffdnakasldspvftadlgyhapgtynfgfidttayt
gsitytavstkqgfwewtstgyavgsgtfkstsidgiadtgttllylpatvvsaywaqvs
gakssssvggyvfpcsatlpsftfgvgsarivipgdyidfgpistgssscfggiqssagi
ginifgdvalkaafvvfngattptlgfask
>d1epne_ 2.38.1.2.1 Endothiapepsin {chestnut blight fungus (Endothia parasitica)}
stgsatttpidslddayitpvqigtpaqtlnldfdtgssdlwvfssettasevdgqtiyt
psksttakllsgatwsisygdgssssgdvytdtvsvggltvtgqavesakkvsssfteds
tidgllglafstlntvsptqqktffdnakasldspvftadlgyhapgtynfgfidttayt
gsitytavstkqgfwewtstgyavgsgtfkstsidgiadtgttllylpatvvsaywaqvs
gakssssvggyvfpcsatlpsftfgvgsarivipgdyidfgpistgssscfggiqssagi
ginifgdvalkaafvvfngattptlgfask
>d1epoe_ 2.38.1.2.1 Endothiapepsin {chestnut blight fungus (Endothia parasitica)}
stgsatttpidslddayitpvqigtpaqtlnldfdtgssdlwvfssettasevdgqtiyt
psksttakllsgatwsisygdgssssgdvytdtvsvggltvtgqavesakkvsssfteds
tidgllglafstlntvsptqqktffdnakasldspvftadlgyhapgtynfgfidttayt
gsitytavstkqgfwewtstgyavgsgtfkstsidgiadtgttllylpatvvsaywaqvs
gakssssvggyvfpcsatlpsftfgvgsarivipgdyidfgpistgssscfggiqssagi
ginifgdvalkaafvvfngattptlgfask
>d1eppe_ 2.38.1.2.1 Endothiapepsin {chestnut blight fungus (Endothia parasitica)}
stgsatttpidslddayitpvqigtpaqtlnldfdtgssdlwvfssettasevdgqtiyt
psksttakllsgatwsisygdgssssgdvytdtvsvggltvtgqavesakkvsssfteds
tidgllglafstlntvsptqqktffdnakasldspvftadlgyhapgtynfgfidttayt
gsitytavstkqgfwewtstgyavgsgtfkstsidgiadtgttllylpatvvsaywaqvs
gakssssvggyvfpcsatlpsftfgvgsarivipgdyidfgpistgssscfggiqssagi
ginifgdvalkaafvvfngattptlgfask
>d1epqe_ 2.38.1.2.1 Endothiapepsin {chestnut blight fungus (Endothia parasitica)}
stgsatttpidslddayitpvqigtpaqtlnldfdtgssdlwvfssettasevdgqtiyt
psksttakllsgatwsisygdgssssgdvytdtvsvggltvtgqavesakkvsssfteds
tidgllglafstlntvsptqqktffdnakasldspvftadlgyhapgtynfgfidttayt
gsitytavstkqgfwewtstgyavgsgtfkstsidgiadtgttllylpatvvsaywaqvs
gakssssvggyvfpcsatlpsftfgvgsarivipgdyidfgpistgssscfggiqssagi
ginifgdvalkaafvvfngattptlgfask
>d1epre_ 2.38.1.2.1 Endothiapepsin {chestnut blight fungus (Endothia parasitica)}
stgsatttpidslddayitpvqigtpaqtlnldfdtgssdlwvfssettasevdgqtiyt
psksttakllsgatwsisygdgssssgdvytdtvsvggltvtgqavesakkvsssfteds
tidgllglafstlntvsptqqktffdnakasldspvftadlgyhapgtynfgfidttayt
gsitytavstkqgfwewtstgyavgsgtfkstsidgiadtgttllylpatvvsaywaqvs
gakssssvggyvfpcsatlpsftfgvgsarivipgdyidfgpistgssscfggiqssagi
ginifgdvalkaafvvfngattptlgfask
>d1eps__ 4.36.2.1.3 5-enol-pyruvyl shikimate-3-phosphate(EPSP) synthase {(Escherichia coli)}
mesltlqpiarvdgtinlpgsktvsnralllaalahgktvltnlldsddvrhmlnaltal
gvsytlsadrtrceiignggplhaegalelflgnagtamrplaaalclgsndivltgepr
mkerpighlvdalrlggakityleqenypplrlqggftggnvdvdgsvssqfltallmta
plapedtvirikgdlvskpyiditlnlmktfgveienqhyqqfvvkggqsyqspgtylve
gdassasyflaaaaikggtvkvtgigrnsmqgdirfadvlekmgaticwgddyisctrge
lnaidmdmnhipdaamtiataalfakgttrlrniynwrvketdrlfamatelrkvgaeve
eghdyiritppeklnfaeiatyndhrmamcfslvalsdtpvtildpkctaktfpdyfeql
arisqaa
>e1ept.1a 2.35.1.2.2 Trypsin(ogen) {porcine (Sus scrofa)}
ivggytcaansipyqvslnsgshfcggslinsqwvvsaahcyk
>e1ept.1b 2.35.1.2.2 Trypsin(ogen) {porcine (Sus scrofa)}
sriqvrlgehnidvlegneqfinaakiithpnfngntldndimliklsspatlnsrvatv
slprscaaagteclisgwgntk
>e1ept.1c 2.35.1.2.2 Trypsin(ogen) {porcine (Sus scrofa)}
ssgssypsllqclkapvlsnssckssypgqitgnmicvgflqggkdscqgdsggpvvcng
qlqgivswgygcaqknkpgvytkvcnyvnwiqqtiaan
>d1er8e_ 2.38.1.2.1 Endothiapepsin {chestnut blight fungus (Endothia parasitica)}
stgsatttpidslddayitpvqigtpaqtlnldfdtgssdlwvfssettasevdgqtiyt
psksttakllsgatwsisygdgssssgdvytdtvsvggltvtgqavesakkvsssfteds
tidgllglafstlntvsptqqktffdnakasldspvftadlgyhapgtynfgfidttayt
gsitytavstkqgfwewtstgyavgsgtfkstsidgiadtgttllylpatvvsaywaqvs
gakssssvggyvfpcsatlpsftfgvgsarivipgdyidfgpistgssscfggiqssagi
ginifgdvalkaafvvfngattptlgfask
>d1era__ 7.6.1.1.1 Erabutoxin B (also neurotoxin B) {sea snake (Laticauda semifasciata)}
ricfnhqssqpqttktcspgesscyhkqwsdfrgtiiergcgcptvkpgiklsccesevc
nn
>d1erb__ 2.45.1.1.1 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
>d1erg__ 7.6.1.3.1 CD59, extracellular domain {human (Homo sapiens)}
lqcyncpnptadcktavncssdfdaclitkaglqvynkcwkfehcnfndvttrlrenelt
yycckkdlcn
>d1erh__ 7.6.1.3.1 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__ 5.1.1.1.11 MAP kinase Erk2 {rat (Rattus norvegicus)}
aaaaaagpemvrgqvfdvgprytnlsyigegaygmvcsaydnlnkvrvaikkispfehqt
ycqrtlreikillrfrheniigindiiraptieqmkdvyivqdlmetdlykllktqhlsn
dhicyflyqilrglkyihsanvlhrdlkpsnlllnttcdlkicdfglarvadpdhdhtgf
lteyvatrwyrapeimlnskgytksidiwsvgcilaemlsnrpifpgkhyldqlnhilgi
lgspsqedlnciinlkarnyllslphknkvpwnrlfpnadskaldlldkmltfnphkrie
veqalahpyleqyydpsdepiaeapfkfdmelddlpkeklkelifeetarfqpgyrs
>d1erp__ 1.10.1.1.3 ER-10 {(Euplotes raikovi)}
dlceqsalqcneqgchnfcspedkpgclgmvwnpelcp
>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__ 2.35.1.2.14 Elastase {porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1esb__ 2.35.1.2.14 Elastase {porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
a
>d1esc__ 3.14.8.1.1 Esterase {(Streptomyces scabies)}
dpvptvffgdsytanfgiapvtnqdsergwcfqakenypavatrsladkgitldvqadvs
cggalihhfwekqelpfgagelppqqdalkqdtqltvgslggntlgfnrilkqcsdelrk
psllpgdpvdgdepaakcgeffgtgdgkqwlddqfervgaeleelldrigyfapdakrvl
vgyprlvpedttkcltaapgqtqlpfadipqdalpvldqiqkrlndamkkaaadggadfv
dlyagtgantacdgadrgigglledsqlellgtkipwyahpndkgrdiqakqvadkieei
ln
>d1esd__ 3.14.8.1.1 Esterase {(Streptomyces scabies)}
dpvptvffgdsytanfgiapvtnqdsergwcfqakenypavatrsladkgitldvqadvs
cggalihhfwekqelpfgagelppqqdalkqdtqltvgslggntlgfnrilkqcsdelrk
psllpgdpvdgdepaakcgeffgtgdgkqwlddqfervgaeleelldrigyfapdakrvl
vgyprlvpedttkcltaapgqtqlpfadipqdalpvldqiqkrlndamkkaaadggadfv
dlyagtgantacdgadrgigglledsqlellgtkipwyahpndkgrdiqakqvadkieei
ln
>d1ese__ 3.14.8.1.1 Esterase {(Streptomyces scabies)}
dpvptvffgdsytanfgiapvtnqdsergwcfqakenypavatrsladkgitldvqadvs
cggalihhfwekqelpfgagelppqqdalkqdtqltvgslggntlgfnrilkqcsdelrk
psllpgdpvdgdepaakcgeffgtgdgkqwlddqfervgaeleelldrigyfapdakrvl
vgyprlvpedttkcltaapgqtqlpfadipqdalpvldqiqkrlndamkkaaadggadfv
dlyagtgantacdgadrgigglledsqlellgtkipwyahpndkgrdiqakqvadkieei
ln
>d1esfa1 2.29.2.2.1 (1-120) Staphylococcal enterotoxin A, SEA {(Staphylococcus aureus)}
sekseeinekdlrkkselqgtalgnlkqiyyynekaktenkeshdqflqhtilfkgfftd
hswyndllvdfdskdivdkykgkkvdlygayygyqcaggtpnktacmyggvtlhdnnrlt
>d1esfa2 4.11.6.1.1 (121-233) Staphylococcal enterotoxin A, SEA {(Staphylococcus aureus)}
eekkvpinlwldgkqntvpletvktnkknvtvqeldlqarrylqekynlynsdvfdgkvq
rglivfhtstepsvnydlfgaqgqysntllriyrdnktinsenmhidiylyts
>d1esfb1 2.29.2.2.1 (1-120) Staphylococcal enterotoxin A, SEA {(Staphylococcus aureus)}
sekseeinekdlrkkselqgtalgnlkqiyyynekaktenkeshdqflqhtilfkgfftd
hswyndllvdfdskdivdkykgkkvdlygayygyqcaggtpnktacmyggvtlhdnnrlt
>d1esfb2 4.11.6.1.1 (121-233) Staphylococcal enterotoxin A, SEA {(Staphylococcus aureus)}
eekkvpinlwldgkqntvpletvktnkknvtvqeldlqarrylqekynlynsdvfdgkvq
rglivfhtstepsvnydlfgaqgqysntllriyrdnktinsenmhidiylyts
>d1esl_1 4.105.1.1.3 (1-118) E-selectin {human (Homo sapiens)}
wsyntsteamtydeasaycqqrythlvaiqnkeeieylnsilsyspsyywigirkvnnvw
vwvgtqkplteeaknwapgepnnrqkdedcveiyikrekdvgmwndercskkklalcy
>d1esl_2 7.3.9.1.4 (119-157) E-selectin, EGF-domain {human (Homo sapiens)}
taactntscsghgecvetinnytckcdpgfsglkceqiv
>d1eso__ 2.1.7.1.7 Cu,Zn superoxide dismutase, SOD {(Escherichia coli)}
asekvemnlvtsqgvgqsigsvtitetdkglefspdlkalppgehgfhihakgscqpatk
dgkasaaesagghldpqntgkhegpegaghlgdlpalvvnndgkatdaviaprlksldei
kdkalmvhvggdnmsdqpkplggggeryacgvik
>d1esp_1 1.57.1.1.3 (157-317) Neutral protease {(Bacillus cereus), strain dsm 3101}
iyqnesgalneaisdifgtlvefydnrnpdweigediytpgkagdalrsmsdptkygdpd
hyskrytgssdnggvhtnsgiinkqayllanggthygvtvtgigkdklgaiyyrantqyf
tqsttfsqaragavqaaadlygansaevaavkqsfsavgvn
>d1esp_2 4.52.1.2.3 (1-156) Neutral protease {(Bacillus cereus), strain dsm 3101}
vtgtnkvgtgkgvlgdtkslnttlsgssyylqdntrgatiftydaknrstlpgtlwadad
nvfnaaydaaavdahyyagktydyykatfnrnsindagaplkstvhygsnynnafwngsq
mvygdgdgvtftslsggidvighslthavtenssnl
>d1est__ 2.35.1.2.14 Elastase {porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1eta1_ 2.3.2.1.1 Transthyretin (synonym: prealbumin) {human (Homo sapiens)}
gptgtgeskcplmvkvldavrgspainvavhvfrkaaddtwepfasgktsesgelhgltt
eeefvegiykveidtksywkalgispfhehaevvftandsgprrytiaallspysystta
vvtnpke
>d1eta2_ 2.3.2.1.1 Transthyretin (synonym: prealbumin) {human (Homo sapiens)}
gptgtgeskcplmvkvldavrgspainvavhvfrkaaddtwepfasgktsesgelhgltt
eeefvegiykveidtksywkalgispfhehaevvftandsgprrytiaallspysystta
vvtnpke
>d1etb1_ 2.3.2.1.1 Transthyretin (synonym: prealbumin) {human (Homo sapiens)}
kcplmvkvldavrgspainvavhvfrkaaddtwepfasgktsesgelhgltteeefvegi
ykveidtksywkalgispfhehaevvftandsgprrytiatllspysysttavvtnpk
>d1etb2_ 2.3.2.1.1 Transthyretin (synonym: prealbumin) {human (Homo sapiens)}
kcplmvkvldavrgspainvavhvfrkaaddtwepfasgktsesgelhgltteeefvegi
ykveidtksywkalgispfhehaevvftandsgprrytiatllspysysttavvtnp
>d1etc__ 1.4.3.12.2 ETS-1 transcription factor, residues 331-440 {Murine (Mus musculus)}
iqlwqfllelltdkscqsfiswtgdgwefklsdpdevarrwgkrknkpkmnyeklsrglr
yyydkniihktagkryvyrfvcdlqsllgytpeelhamldvkpdad
>d1etd__ 1.4.3.12.2 ETS-1 transcription factor, residues 331-440 {Murine (Mus musculus)}
iqlwqfllelltdkscqsfiswtgdgwefklsdpdevarrwgkrknkpkmnyeklsrglr
yyydkniihktagkryvyrfvcdlqsllgytpeelhamldvkpdad
>d1etha1 2.10.2.1.2 (337-448) Pancreatic lipase, C-terminal domain {pig (Sus scrofa)}
arwrykvsvtlsgkkvtghilvslfgnegnsrqyeiykgtlqpdnthsdefdsdvevgdl
qkvkfiwynvinptlprvgaskitverndgkvydfcsqetvreevlltlnpc
>d1etha2 3.56.1.11.2 (1-336) Pancreatic lipase, N-terminal domain {pig (Sus scrofa)}
sevcfprlgcfsddapwagivqrplkilpwspkdvdtrfllytnqnqnnyqelvadpsti
tnsnfrmdrktrfiihgfidkgeedwlsnicknlfkvesvncicvdwkggsrtgytqasq
nirivgaevayfvevlksslgyspsnvhvighslgshaageagrrtngtieritgldpae
pcfqgtpelvrldpsdakfvdvihtdaapiipnlgfgmsqtvghldffpnggkqmpgcqk
nilsqivdidgiwegtrdfvacnhlrsykyyadsilnpdgfagfpcdsynvftankcfpc
psegcpqmghyadrfpgktngvsqvfylntgdasnf
>d1ethb1 7.3.8.1.1 (4-44) (Pro)colipase {pig (Sus scrofa)}
prgiiinldegelclnsaqcksnccqhdtilslsrcalkar
>d1ethb2 7.3.8.1.1 (45-90) (Pro)colipase {pig (Sus scrofa)}
ensecsaftlygvyykcpcergltcegdkslvgsitntnfgichnv
>d1ethc1 2.10.2.1.2 (337-448) Pancreatic lipase, C-terminal domain {pig (Sus scrofa)}
arwrykvsvtlsgkkvtghilvslfgnegnsrqyeiykgtlqpdnthsdefdsdvevgdl
qkvkfiwynvinptlprvgaskitverndgkvydfcsqetvreevlltlnpc
>d1ethc2 3.56.1.11.2 (1-336) Pancreatic lipase, N-terminal domain {pig (Sus scrofa)}
sevcfprlgcfsddapwagivqrplkilpwspkdvdtrfllytnqnqnnyqelvadpsti
tnsnfrmdrktrfiihgfidkgeedwlsnicknlfkvesvncicvdwkggsrtgytqasq
nirivgaevayfvevlksslgyspsnvhvighslgshaageagrrtngtieritgldpae
pcfqgtpelvrldpsdakfvdvihtdaapiipnlgfgmsqtvghldffpnggkqmpgcqk
nilsqivdidgiwegtrdfvacnhlrsykyyadsilnpdgfagfpcdsynvftankcfpc
psegcpqmghyadrfpgktngvsqvfylntgdasnf
>d1ethd1 7.3.8.1.1 (4-44) (Pro)colipase {pig (Sus scrofa)}
prgiiinldegelclnsaqcksnccqhdtilslsrcalkar
>d1ethd2 7.3.8.1.1 (45-90) (Pro)colipase {pig (Sus scrofa)}
ensecsaftlygvyykcpcergltcegdkslvgsitntnfgichnv
>d1etja_ 2.5.1.1.17 Azurin {(Pseudomonas aeruginosa)}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctfpghsal
ekgtltlk
>d1etjb_ 2.5.1.1.17 Azurin {(Pseudomonas aeruginosa)}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctfpghsal
ekgtltlk
>d1etjc_ 2.5.1.1.17 Azurin {(Pseudomonas aeruginosa)}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctfpghsal
ekgtltlk
>d1etjd_ 2.5.1.1.17 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 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
ivegqdaevglspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftvddll
vrigkhsrtryerkvekismldkiyihprynwkenldrdiallklkrpielsdyihpvcl
pdkqtaakllhagfkgrvtgwgnrretwttsvaevqpsvlqvvnlplverpvckastrir
itdnmfcagykpgegkrgdacegdsggpfvmkspynnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidrlgs
>e1etr.1l 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1ets.1h 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
ivegqdaevglspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftvddll
vrigkhsrtryerkvekismldkiyihprynwkenldrdiallklkrpielsdyihpvcl
pdkqtaakllhagfkgrvtgwgnrretwttsvaevqpsvlqvvnlplverpvckastrir
itdnmfcagykpgegkrgdacegdsggpfvmkspynnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidrlgs
>e1ets.1l 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1ett.1h 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
ivegqdaevglspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftvddll
vrigkhsrtryerkvekismldkiyihprynwkenldrdiallklkrpielsdyihpvcl
pdkqtaakllhagfkgrvtgwgnrretwttsvaevqpsvlqvvnlplverpvckastrir
itdnmfcagykpgegkrgdacegdsggpfvmkspynnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidrlgs
>e1ett.1l 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>d1etu__ 3.29.1.4.13 Elongation factor Tu (EF-Tu), the N-terminal (G) domain {(Escherichia coli)}
fertkphvnvgtighvdhgkttltaaittvlaktyggaaxxxxxxxxxxxxxxxgitint
shveydtptrhyahvdcpghadyvknmitgaaqmdgailvvaatdgpmpqtrehillgrq
vgvpyiivflnkcdmvddeellelvemevrellsqydfpgddtpivrgsalkalegdaew
eakilelagfldsyip
>d1eur__ 2.50.1.1.4 Micromonospora sialidase, N-terminal domain {(Micromonospora viridifaciens)}
geplyteqdlavngregfpnyripaltvtpdgdllasydgrptgidapgpnsilqrrstd
ggrtwgeqqvvsagqttapikgfsdpsylvdretgtifnfhvysqrqgfagsrpgtdpad
pnvlhanvatstdggltwshrtitaditpdpgwrsrfaasgegiqlrygphagrliqqyt
iinaagafqavsvysddhgrtwrageavgvgmdenktvelsdgrvllnsrdsarsgyrkv
avstdgghsygpvtidrdlpdptnnasiirafpdapagsarakvllfsnaasqtsrsqgt
irmscddgqtwpvskvfqpgsmsystltalpdgtygllyepgtgiryanfnlawlggica
p
>d1eus__ 2.50.1.1.4 Micromonospora sialidase, N-terminal domain {(Micromonospora viridifaciens)}
geplyteqdlavngregfpnyripaltvtpdgdllasydgrptgidapgpnsilqrrstd
ggrtwgeqqvvsagqttapikgfsdpsylvdretgtifnfhvysqrqgfagsrpgtdpad
pnvlhanvatstdggltwshrtitaditpdpgwrsrfaasgegiqlrygphagrliqqyt
iinaagafqavsvysddhgrtwrageavgvgmdenktvelsdgrvllnsrdsarsgyrkv
avstdgghsygpvtidrdlpdptnnasiirafpdapagsarakvllfsnaasqtsrsqgt
irmscddgqtwpvskvfqpgsmsystltalpdgtygllyepgtgiryanfnlawlggi
>d1eut_1 2.1.1.5.13 (403-505) Sialidase, the linker domain {(Micromonospora viridifaciens)}
gicapftipdvalepgqqvtvpvavtnqsgiavpkpslqldaspdwqvqgsveplmpgrq
akgqvtitvpagttpgryrvgatlrtsagnasttftvtvglld
>d1eut_2 2.13.1.1.2 (506-647) Sialidase, C-terminal domain {(Micromonospora viridifaciens)}
qarmsiadvdseetaredgrasnvidgnpstfwhtewsradapgyphrisldlggthtis
glqytrrqnsaneqvadyeiytslngttwdgpvasgrfttslapqravfpardaryirlv
alseqtghkyaavaelevegqr
>d1eut_3 2.50.1.1.4 (47-402) Micromonospora sialidase, N-terminal domain {(Micromonospora viridifaciens)}
geplyteqdlavngregfpnyripaltvtpdgdllasydgrptgidapgpnsilqrrstd
ggrtwgeqqvvsagqttapikgfsdpsylvdretgtifnfhvysqrqgfagsrpgtdpad
pnvlhanvatstdggltwshrtitaditpdpgwrsrfaasgegiqlrygphagrliqqyt
iinaagafqavsvysddhgrtwrageavgvgmdenktvelsdgrvllnsrdsarsgyrkv
avstdgghsygpvtidrdlpdptnnasiirafpdapagsarakvllfsnaasqtsrsqgt
irmscddgqtwpvskvfqpgsmsystltalpdgtygllyepgtgiryanfnlawlg
>d1euu_1 2.1.1.5.13 (403-505) Sialidase, the linker domain {(Micromonospora viridifaciens)}
gicapftipdvalepgqqvtvpvavtnqsgiavpkpslqldaspdwqvqgsveplmpgrq
akgqvtitvpagttpgryrvgatlrtsagnasttftvtvglld
>d1euu_2 2.13.1.1.2 (506-647) Sialidase, C-terminal domain {(Micromonospora viridifaciens)}
qarmsiadvdseetaredgrasnvidgnpstfwhtewsradapgyphrisldlggthtis
glqytrrqnsaneqvadyeiytslngttwdgpvasgrfttslapqravfpardaryirlv
alseqtghkyaavaelevegqr
>d1euu_3 2.50.1.1.4 (47-402) Micromonospora sialidase, N-terminal domain {(Micromonospora viridifaciens)}
geplyteqdlavngregfpnyripaltvtpdgdllasydgrptgidapgpnsilqrrstd
ggrtwgeqqvvsagqttapikgfsdpsylvdretgtifnfhvysqrqgfagsrpgtdpad
pnvlhanvatstdggltwshrtitaditpdpgwrsrfaasgegiqlrygphagrliqqyt
iinaagafqavsvysddhgrtwrageavgvgmdenktvelsdgrvllnsrdsarsgyrkv
avstdgghsygpvtidrdlpdptnnasiirafpdapagsarakvllfsnaasqtsrsqgt
irmscddgqtwpvskvfqpgsmsystltalpdgtygllyepgtgiryanfnlawlg
>d1exfa_ 2.35.1.1.8 Epidermolytic toxin A {(Staphylococcus aureus)}
vsaeeikkheekwnkyygvnafnlpkelfskvdekdrqkypyntignvfvkgqtsatgvl
igkntvltnrhiakfangdpskvsfrpsintddngntetpygeyevkeilqepfgagvdl
alirlkpdqngvslgdkispakigtsndlkdgdkleligypfdhkvnqmhrseielttls
rglryygftvpgnsgsgifnsngelvgihsskvshldrehqinygvgignyvkriinekn
e
>d1exg__ 2.2.2.1.1 Exo-1,4-beta-D-glycanase (cellulase, xylanase) {(Cellumonas fimi)}
assgpagcqvlwgvnqwntgftanvtvkntssapvdgwtltfsfpsgqqvtqawsstvtq
sgsavtvrnapwngsipaggtaqfgfngshtgtnaaptafslngtpctvg
>d1exh__ 2.2.2.1.1 Exo-1,4-beta-D-glycanase (cellulase, xylanase) {(Cellumonas fimi)}
assgpagcqvlwgvnqwntgftanvtvkntssapvdgwtltfsfpsgqqvtqawsstvtq
sgsavtvrnapwngsipaggtaqfgfngshtgtnaaptafslngtpctvg
>d1exna_ 3.45.1.3.1 T5 5'-exonuclease {(bacteriophage T5)}
rnlxivdgtnlgfrfkhnnskkpfassyvstiqslaksysarttivlgdkgksvfrlehl
peykgnrdekyaqrteeekaldeqffeylkdafelckttfptftirgveaddxaayivkl
ighlydhvwlistdgdwdtlltdkvsrfsfttrreyhlrdxyehhnvddveqfislkaix
gdlgdnirgvegigakrgyniirefgnvldiidqlplpgkqkyiqnlnaseellfrnlil
vdlptycvdaiaavgqdvldkftkdileiae
>d1exnb_ 3.45.1.3.1 T5 5'-exonuclease {(bacteriophage T5)}
rnlxivdgtnlgfrfkhnnskkpfassyvstiqslaksysarttivlgdkgksvfrlehl
peykgnrdekyaqrteeekaldeqffeylkdafelckttfptftirgveaddxaayivkl
ighlydhvwlistdgdwdtlltdkvsrfsfttrreyhlrdxyehhnvddveqfislkaix
gdlgdnirgvegigakrgyniirefgnvldiidqlplpgkqkyiqnlnaseellfrnlil
vdlptycvdaiaavgqdvldkftkdileiaeq
>d1exp__ 3.1.1.3.3 beta-1,4-glycanase Cex, catalytic domain {(Cellulomonas fimi) ATCC 484}
attlkeaadgagrdfgfaldpnrlseaqykaiadsefnlvvaenamkwdatepsqnsfsf
gagdrvasyaadtgkelyghtlvwhsqlpdwaknlngsafesamvnhvtkvadhfegkva
swdvvneafadgggrrqdsafqqklgngyietafraaraadptaklcindynveginaks
nslydlvkdfkargvpldcvgfqshlivgqvpgdfrqnlqrfadlgvdvriteldirmrt
psdatklatqaadykkvvqacmqvtrcqgvtvwgitdkyswvpdvfpgegaalvwdasya
kkpayaavmeaf
>d1exta1 7.24.1.1.1 (13-70) Tumor necrosis factor (TNF) receptor {human (Homo sapiens)}
svcpqgkyihpqnnsicctkchkgtylyndcpgpgqdtdcrecesgsftasenhlrhc
>d1exta2 7.24.1.1.1 (71-114) Tumor necrosis factor (TNF) receptor {human (Homo sapiens)}
lscskcrkemgqveissctvdrdtvcgcrknqyrhywsenlfqc
>d1exta3 7.24.1.1.1 (115-172) Tumor necrosis factor (TNF) receptor {human (Homo sapiens)}
fncslclngtvhlscqekqntvctchagfflrenecvscsnckkslectklclpqien
>d1extb1 7.24.1.1.1 (11-70) Tumor necrosis factor (TNF) receptor {human (Homo sapiens)}
mdsvcpqgkyihpqnnsicctkchkgtylyndcpgpgqdtdcrecesgsftasenhlrhc
>d1extb2 7.24.1.1.1 (71-114) Tumor necrosis factor (TNF) receptor {human (Homo sapiens)}
lscskcrkemgqveissctvdrdtvcgcrknqyrhywsenlfqc
>d1extb3 7.24.1.1.1 (115-168) Tumor necrosis factor (TNF) receptor {human (Homo sapiens)}
fncslclngtvhlscqekqntvctchagfflrenecvscsnckkslectklclp
>d1eza__ 3.5.1.2.1 N-terminal domain of enzyme I of the PEP:sugar phosphotransferase system {(Escherichia coli)}
misgilaspgiafgkalllkedeividrkkisadqvdqeverflsgrakasaqletiktk
agetfgeekeaifeghimlledeeleqeiialikdkhmtadaaaheviegqasaleeldd
eylkeraadvrdigkrllrnilglkiidlsaiqdevilvaadltpsetaqlnlkkvlgfi
tdaggrtshtsimarslelpaivgtgsvtsqvknddylildavnnqvyvnptnevidkmr
avqeqvasekaelaklkdr
>d1ezb__ 3.5.1.2.1 N-terminal domain of enzyme I of the PEP:sugar phosphotransferase system {(Escherichia coli)}
misgilaspgiafgkalllkedeividrkkisadqvdqeverflsgrakasaqletiktk
agetfgeekeaifeghimlledeeleqeiialikdkhmtadaaaheviegqasaleeldd
eylkeraadvrdigkrllrnilglkiidlsaiqdevilvaadltpsetaqlnlkkvlgfi
tdaggrtshtsimarslelpaivgtgsvtsqvknddylildavnnqvyvnptnevidkmr
avqeqvasekaelaklkdr
>d1ezc__ 3.5.1.2.1 N-terminal domain of enzyme I of the PEP:sugar phosphotransferase system {(Escherichia coli)}
misgilaspgiafgkalllkedeividrkkisadqvdqeverflsgrakasaqletiktk
agetfgeekeaifeghimlledeeleqeiialikdkhmtadaaaheviegqasaleeldd
eylkeraadvrdigkrllrnilglkiidlsaiqdevilvaadltpsetaqlnlkkvlgfi
tdaggrtshtsimarslelpaivgtgsvtsqvknddylildavnnqvyvnptnevidkmr
avqeqvasekaelaklkdr
>d1ezd__ 3.5.1.2.1 N-terminal domain of enzyme I of the PEP:sugar phosphotransferase system {(Escherichia coli)}
misgilaspgiafgkalllkedeividrkkisadqvdqeverflsgrakasaqletiktk
agetfgeekeaifeghimlledeeleqeiialikdkhmtadaaaheviegqasaleeldd
eylkeraadvrdigkrllrnilglkiidlsaiqdevilvaadltpsetaqlnlkkvlgfi
tdaggrtshtsimarslelpaivgtgsvtsqvknddylildavnnqvyvnptnevidkmr
avqeqvasekaelaklkdr
>d1ezm_1 1.57.1.1.1 (154-298) Elastase {(Pseudomonas aeruginosa)}
iyrgqsggmneafsdmageaaefymrgkndfligydikkgsgalrymdqpsrdgrsidna
sqyyngidvhhssgvynrafyllanspgwdtrkafevfvdanryywtatsnynsgacgvi
rsaqnrnysaadvtrafstvgvtcp
>d1ezm_2 4.52.1.2.1 (1-153) Elastase {(Pseudomonas aeruginosa)}
aeaggpggnqkigkytygsdygplivndrcemddgnvitvdmnsstddskttpfrfacpt
ntykqvngaysplndahffggvvfklyrdwfgtsplthklymkvhygrsvenaywdgtam
lfgdgatmfyplvsldvaahevshgfteqnsgl
>d1f36a_ 1.84.1.1.1 FIS protein {(Escherichia coli)}
vltvstvnsqdqvtqkplrdsvkqalenyfaqlngqdvndlyelvlaeveqplldmvmqy
trgnqtraalmmginrgtlrkklkkygmn
>d1f36b_ 1.84.1.1.1 FIS protein {(Escherichia coli)}
vltvstvnsqdqvtqkplrdsvkqalenyfaqlngqdvndlyelvlaeveqplldmvmqy
trgnqtraalmmginrgtlrkklkkygmn
>d1f3g__ 2.65.3.1.2 Glucose-specific factor III (glsIII) {(Escherichia coli)}
tieiiaplsgeivniedvpdvvfaekivgdgiaikptgnkmvapvdgtigkifetnhafs
iesdsgvelfvhfgidtvelkgegfkriaeegqrvkvgdtviefdlplleekakstltpv
visnmdeikeliklsgsvtvgetpvirikk
>d1f3z__ 2.65.3.1.2 Glucose-specific factor III (glsIII) {(Escherichia coli)}
tieiiaplsgeivniedvpdvvfaekivgdgiaikptgnkmvapvdgtigkifetnhafs
iesdsgvelfvhfgidtvelkgegfkriaeegqrvkvgdtviefdlplleekakstltpv
visnmdeikeliklsgsvtvgetpvirikk
>d1faga_ 1.83.1.1.2 Cytochrome P450 {(Bacillus megaterium)}
tikempqpktfgelknlpllntdkpvqalmkiadelgeifkfeapgrvtrylssqrlike
acdesrfdknlsqalkfvrdfagdglftswtheknwkkahnillpsfsqqamkgyhammv
diavqlvqkwerlnadehievpedmtrltldtiglcgfnyrfnsfyrdqphpfitsmvra
ldeamnklqranpddpaydenkrqfqedikvmndlvdkiiadrkasgeqsddllthmlng
kdpetgeplddeniryqiitfliaghettsgllsfalyflvknphvlqkaaeeaarvlvd
pvpsykqvkqlkyvgmvlnealrlwptapafslyakedtvlggeyplekgdelmvlipql
hrdktiwgddveefrperfenpsaipqhafkpfgngqracigqqfalheatlvlgmmlkh
fdfedhtnyeldiketltlkpegfvvkakskkipl
>d1fagb_ 1.83.1.1.2 Cytochrome P450 {(Bacillus megaterium)}
tikempqpktfgelknlpllntdkpvqalmkiadelgeifkfeapgrvtrylssqrlike
acdesrfdknlsqalkfvrdfagdglftswtheknwkkahnillpsfsqqamkgyhammv
diavqlvqkwerlnadehievpedmtrltldtiglcgfnyrfnsfyrdqphpfitsmvra
ldeamnklqranpddpaydenkrqfqedikvmndlvdkiiadrkasgeqsddllthmlng
kdpetgeplddeniryqiitfliaghettsgllsfalyflvknphvlqkaaeeaarvlvd
pvpsykqvkqlkyvgmvlnealrlwptapafslyakedtvlggeyplekgdelmvlipql
hrdktiwgddveefrperfenpsaipqhafkpfgngqracigqqfalheatlvlgmmlkh
fdfedhtnyeldiketltlkpegfvvkakskkipl
>d1fagc_ 1.83.1.1.2 Cytochrome P450 {(Bacillus megaterium)}
tikempqpktfgelknlpllntdkpvqalmkiadelgeifkfeapgrvtrylssqrlike
acdesrfdknlsqalkfvrdfagdglftswtheknwkkahnillpsfsqqamkgyhammv
diavqlvqkwerlnadehievpedmtrltldtiglcgfnyrfnsfyrdqphpfitsmvra
ldeamnklqranpddpaydenkrqfqedikvmndlvdkiiadrkasgeqsddllthmlng
kdpetgeplddeniryqiitfliaghettsgllsfalyflvknphvlqkaaeeaarvlvd
pvpsykqvkqlkyvgmvlnealrlwptapafslyakedtvlggeyplekgdelmvlipql
hrdktiwgddveefrperfenpsaipqhafkpfgngqracigqqfalheatlvlgmmlkh
fdfedhtnyeldiketltlkpegfvvkakskkipl
>d1fagd_ 1.83.1.1.2 Cytochrome P450 {(Bacillus megaterium)}
tikempqpktfgelknlpllntdkpvqalmkiadelgeifkfeapgrvtrylssqrlike
acdesrfdknlsqalkfvrdfagdglftswtheknwkkahnillpsfsqqamkgyhammv
diavqlvqkwerlnadehievpedmtrltldtiglcgfnyrfnsfyrdqphpfitsmvra
ldeamnklqranpddpaydenkrqfqedikvmndlvdkiiadrkasgeqsddllthmlng
kdpetgeplddeniryqiitfliaghettsgllsfalyflvknphvlqkaaeeaarvlvd
pvpsykqvkqlkyvgmvlnealrlwptapafslyakedtvlggeyplekgdelmvlipql
hrdktiwgddveefrperfenpsaipqhafkpfgngqracigqqfalheatlvlgmmlkh
fdfedhtnyeldiketltlkpegfvvkakskkipl
>d1faha_ 1.83.1.1.2 Cytochrome P450 {(Bacillus megaterium)}
tikempqpktfgelknlpllntdkpvqalmkiadelgeifkfeapgrvtrylssqrlike
acdesrfdknlsqalkfvrdfagdglftswtheknwkkahnillpsfsqqamkgyhammv
diavqlvqkwerlnadehievpedmtrltldtiglcgfnyrfnsfyrdqphpfitsmvra
ldeamnklqranpddpaydenkrqfqedikvmndlvdkiiadrkasgeqsddllthmlng
kdpetgeplddeniryqiitfliagheatsgllsfalyflvknphvlqkaaeeaarvlvd
pvpsykqvkqlkyvgmvlnealrlwptapafslyakedtvlggeyplekgdelmvlipql
hrdktiwgddveefrperfenpsaipqhafkpfgngqracigqqfalheatlvlgmmlkh
fdfedhtnyeldiketltlkpegfvvkakskkipl
>d1fahb_ 1.83.1.1.2 Cytochrome P450 {(Bacillus megaterium)}
tikempqpktfgelknlpllntdkpvqalmkiadelgeifkfeapgrvtrylssqrlike
acdesrfdknlsqalkfvrdfagdglftswtheknwkkahnillpsfsqqamkgyhammv
diavqlvqkwerlnadehievpedmtrltldtiglcgfnyrfnsfyrdqphpfitsmvra
ldeamnklqranpddpaydenkrqfqedikvmndlvdkiiadrkasgeqsddllthmlng
kdpetgeplddeniryqiitfliagheatsgllsfalyflvknphvlqkaaeeaarvlvd
pvpsykqvkqlkyvgmvlnealrlwptapafslyakedtvlggeyplekgdelmvlipql
hrdktiwgddveefrperfenpsaipqhafkpfgngqracigqqfalheatlvlgmmlkh
fdfedhtnyeldiketltlkpegfvvkakskkipl
>d1faih1 2.1.1.1.21 (1-123) Immunoglobulin (variable domains of L and H chains) {Fab R19.9 (mouse), kappa L chain}
qvqlqqsgaelvragssvkmsckasgytftsygvnwvkqrpgqglewigyinpgkgylsy
nekfkgkttltvdrssstaymqlrsltsedaavyfcarsfyggsdlavyyfdswgqgttl
tvs
>d1faih2 2.1.1.2.29 (124-221) Immunoglobulin (constant domains of L and H chains) {Fab R19.9 (mouse), kappa L chain}
sakttppsvyplapgcgdttgssvtlgclvkgyfpesvtvtwnsgslsssvhtfpallqs
alytmsssvtvpsstwpsqtvtcsvahpassttvdkkl
>d1fail1 2.1.1.1.21 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab R19.9 (mouse), kappa L chain}
diqmtqttsslsaslgdrvtiscrasqdisnylnwyqqkpdgtvklliyytsrlhsgvps
rfsgsgsgtdysltisnlehediatyfcqqgstlprtfgggtkleikr
>d1fail2 2.1.1.2.29 (109-214) Immunoglobulin (constant domains of L and H chains) {Fab R19.9 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1faj__ 2.29.5.1.2 Inorganic pyrophosphatase {(Escherichia coli)}
sllnvpagkdlpediyvvieipanadpikyeidkesgalfvdrfmstamfypcnygyinh
tlsldgdpvdvlvptpyplqpgsvircrpvgvlkmtdeagedaklvavphsklskeydhi
kdvndlpellkaqiahffehykdlekgkwvkvegwenaeaakaeivasferak
>d1fan__ 7.7.1.1.1 Pancreatic trypsin inhibitor {bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnaksaedcmrtcgga
>d1fapa_ 4.19.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1fapb_ 1.24.7.1.1 FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP) {human (Homo sapiens)}
rvailwhemwhegleeasrlyfgernvkgmfevleplhammergpqtlketsfnqaygrd
lmeaqewcrkymksgnvkdltqawdlyyhvfrris
>d1faq__ 7.40.1.1.2 RAF-1 {human (Homo sapiens)}
ltthnfarktflklafcdicqkfllngfrcqtcgykfhehcstkvptmcvdw
>d1far__ 7.40.1.1.2 RAF-1 {human (Homo sapiens)}
ltthnfarktflklafcdicqkfllngfrcqtcgykfhehcstkvptmcvdw
>d1fas__ 7.6.1.1.3 Fasciculin {green mamba (Dendroaspis angusticeps)}
tmcyshtttsrailtncgenscyrksrrhppkmvlgrgcgcppgddylevkcctspdkcn
y
>d1fata_ 2.21.1.1.12 Phytohemagglutinin-L, PHA-L, also arcelin {Kidney bean (Phaseolus vulgaris)}
sndiyfnfqrfnetnlilqrdasvsssgqlrltnlngngeprvgslgrafysapiqiwdn
ttgtvasfatsftfniqvpnnagpadglafalvpvgsqpkdkggflglfdgsnsnfhtva
vefdtlynkdwdpterhigidvnsirsikttrwdfvngenaevlitydsstnllvaslvy
psqktsfivsdtvdlksvlpewvsvgfsattginkgnvetndvlswsfaskls
>d1fatb_ 2.21.1.1.12 Phytohemagglutinin-L, PHA-L, also arcelin {Kidney bean (Phaseolus vulgaris)}
sndiyfnfqrfnetnlilqrdasvsssgqlrltnlngngeprvgslgrafysapiqiwdn
ttgtvasfatsftfniqvpnnagpadglafalvpvgsqpkdkggflglfdgsnsnfhtva
vefdtlynkdwdpterhigidvnsirsikttrwdfvngenaevlitydsstnllvaslvy
psqktsfivsdtvdlksvlpewvsvgfsattginkgnvetndvlswsfaskls
>d1fatc_ 2.21.1.1.12 Phytohemagglutinin-L, PHA-L, also arcelin {Kidney bean (Phaseolus vulgaris)}
sndiyfnfqrfnetnlilqrdasvsssgqlrltnlngngeprvgslgrafysapiqiwdn
ttgtvasfatsftfniqvpnnagpadglafalvpvgsqpkdkggflglfdgsnsnfhtva
vefdtlynkdwdpterhigidvnsirsikttrwdfvngenaevlitydsstnllvaslvy
psqktsfivsdtvdlksvlpewvsvgfsattginkgnvetndvlswsfaskls
>d1fatd_ 2.21.1.1.12 Phytohemagglutinin-L, PHA-L, also arcelin {Kidney bean (Phaseolus vulgaris)}
sndiyfnfqrfnetnlilqrdasvsssgqlrltnlngngeprvgslgrafysapiqiwdn
ttgtvasfatsftfniqvpnnagpadglafalvpvgsqpkdkggflglfdgsnsnfhtva
vefdtlynkdwdpterhigidvnsirsikttrwdfvngenaevlitydsstnllvaslvy
psqktsfivsdtvdlksvlpewvsvgfsattginkgnvetndvlswsfaskls
>d1faxa_ 2.35.1.2.26 Coagulation factor Xa (Chrismas factor), protease domain {Human (Homo sapiens)}
ivggqeckdgecpwqallineenegfcggtilsefyiltaahclyqakrfkvrvgdrnta
aeeggeavhevevvikhnrftketydfdiavlrlktpitfrmnvapaclperdwaestlm
tqktgivsgfgrthekgrqstrlkmlevpyvdrnscklsssfiitqnmfcagydtkqeda
cqgdsggphvtrfkdtyfvtgivswgegcarkgkygiytkvtaflkwidrsmktr
>d1faxl_ 7.3.9.1.5 Factor X, N-terminal module {human (Homo sapiens)}
trklcsldngdcdqfcheeqasvvcscargytladngkaciptgpypcgkqtler
>d1fbaa_ 3.1.3.1.4 Fructose-1,6-bisphosphate aldolase {(Drosophila melanogaster), strain sevelen (Wild type, pupea)}
xttyfnypskelqdelreiaqkivapgkgilaadesgptmgkrlqdigventednrrayr
qllfstdpklaenisgvilfhetlyqkaddgtpfaeilkkkgiilgikvdkgvvplfgse
devttqglddlaarcaqykkdgcdfakwrcvlkigkntpsyqsilenanvlaryasicqs
qrivpivepevlpdgdhdldraqkvtetvlaavykalsdhhvylegtllkpnmvtagqsa
kkntpeeialatvqalrrtvpaavtgvtflsggqseeeatvnlsainnvplirpwaltfs
ygralqasvlrawagkkeniaagqnellkrakangdaaqgkyvagsagagsgslfvanha
y
>d1fbab_ 3.1.3.1.4 Fructose-1,6-bisphosphate aldolase {(Drosophila melanogaster), strain sevelen (Wild type, pupea)}
xttyfnypskelqdelreiaqkivapgkgilaadesgptmgkrlqdigventednrrayr
qllfstdpklaenisgvilfhetlyqkaddgtpfaeilkkkgiilgikvdkgvvplfgse
devttqglddlaarcaqykkdgcdfakwrcvlkigkntpsyqsilenanvlaryasicqs
qrivpivepevlpdgdhdldraqkvtetvlaavykalsdhhvylegtllkpnmvtagqsa
kkntpeeialatvqalrrtvpaavtgvtflsggqseeeatvnlsainnvplirpwaltfs
ygralqasvlrawagkkeniaagqnellkrakangdaaqgkyvagsagagsgslfvanha
y
>d1fbac_ 3.1.3.1.4 Fructose-1,6-bisphosphate aldolase {(Drosophila melanogaster), strain sevelen (Wild type, pupea)}
xttyfnypskelqdelreiaqkivapgkgilaadesgptmgkrlqdigventednrrayr
qllfstdpklaenisgvilfhetlyqkaddgtpfaeilkkkgiilgikvdkgvvplfgse
devttqglddlaarcaqykkdgcdfakwrcvlkigkntpsyqsilenanvlaryasicqs
qrivpivepevlpdgdhdldraqkvtetvlaavykalsdhhvylegtllkpnmvtagqsa
kkntpeeialatvqalrrtvpaavtgvtflsggqseeeatvnlsainnvplirpwaltfs
ygralqasvlrawagkkeniaagqnellkrakangdaaqgkyvagsagagsgslfvanha
y
>d1fbad_ 3.1.3.1.4 Fructose-1,6-bisphosphate aldolase {(Drosophila melanogaster), strain sevelen (Wild type, pupea)}
xttyfnypskelqdelreiaqkivapgkgilaadesgptmgkrlqdigventednrrayr
qllfstdpklaenisgvilfhetlyqkaddgtpfaeilkkkgiilgikvdkgvvplfgse
devttqglddlaarcaqykkdgcdfakwrcvlkigkntpsyqsilenanvlaryasicqs
qrivpivepevlpdgdhdldraqkvtetvlaavykalsdhhvylegtllkpnmvtagqsa
kkntpeeialatvqalrrtvpaavtgvtflsggqseeeatvnlsainnvplirpwaltfs
ygralqasvlrawagkkeniaagqnellkrakangdaaqgkyvagsagagsgslfvanha
y
>d1fbca_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
dtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnvt
gdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssni
dclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfml
dpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvg
smvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldiv
ptdihqrapiilgspedvtelleiyqkha
>d1fbcb_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
afdtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstn
vtgdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgss
nidclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncf
mldpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygary
vgsmvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavld
ivptdihqrapiilgspedvtelleiyqkha
>d1fbda_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
dtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnvt
gdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssni
dclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfml
dpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvg
smvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldiv
ptdihqrapiilgspedvtelleiyqkha
>d1fbdb_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
afdtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstn
vtgdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgss
nidclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncf
mldpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygary
vgsmvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavld
ivptdihqrapiilgspedvtelleiyqkha
>d1fbea_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
dtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnvt
gdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssni
dclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfml
dpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvg
smvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldiv
ptdihqrapiilgspedvtelleiyqkha
>d1fbeb_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
afdtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstn
vtgdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgss
nidclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncf
mldpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygary
vgsmvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavld
ivptdihqrapiilgspedvtelleiyqkha
>d1fbfa_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
dtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnvt
gdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssni
dclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfml
dpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvg
smvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldiv
ptdihqrapiilgspedvtelleiyqkha
>d1fbfb_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
afdtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstn
vtgdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgss
nidclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncf
mldpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygary
vgsmvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavld
ivptdihqrapiilgspedvtelleiyqkha
>d1fbga_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
dtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnvt
gdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssni
dclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfml
dpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvg
smvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldiv
ptdihqrapiilgspedvtelleiyqkha
>d1fbgb_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
afdtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstn
vtgdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgss
nidclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncf
mldpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygary
vgsmvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavld
ivptdihqrapiilgspedvtelleiyqkha
>d1fbha_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
dtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnvt
gdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssni
dclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfml
dpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvg
smvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldiv
ptdihqrapiilgspedvtelleiyqkha
>d1fbhb_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
fdtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnv
tgdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssn
idclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfm
ldpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryv
gsmvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldi
vptdihqrapiilgspedvtelleiyqkha
>d1fbih1 2.1.1.1.49 (1-121) Immunoglobulin (variable domains of L and H chains) {Fab F9.13.7 (mouse), kappa L chain}
qvqlqqpgaelvkpgasvklsckasgytftsywmhwvkqgpgqglewigeidpsdsypny
nekfkgkatltvdkssstaymqlssltsedsavyycaslyyygtsygvldywgqgtsvtv
s
>d1fbih2 2.1.1.2.56 (122-221) Immunoglobulin (constant domains of L and H chains) {Fab F9.13.7 (mouse), kappa L chain}
sakttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqs
dlytlsssvtvpssprpsetvtcnvahpasstkvdkkivp
>d1fbil1 2.1.1.1.49 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab F9.13.7 (mouse), kappa L chain}
diqmtqttsslsaslgdrvtiscrasqdisnylnwyqkkpdgtvklliyytsrlhsgvps
rfsgsgsgtdysltirnleqediatyfcqqgytlpytfgggtkleik
>d1fbil2 2.1.1.2.56 (108-214) Immunoglobulin (constant domains of L and H chains) {Fab F9.13.7 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1fbip1 2.1.1.1.49 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab F9.13.7 (mouse), kappa L chain}
diqmtqttsslsaslgdrvtiscrasqdisnylnwyqkkpdgtvklliyytsrlhsgvps
rfsgsgsgtdysltirnleqediatyfcqqgytlpytfgggtkleik
>d1fbip2 2.1.1.2.56 (108-214) Immunoglobulin (constant domains of L and H chains) {Fab F9.13.7 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1fbiq1 2.1.1.1.49 (1-121) Immunoglobulin (variable domains of L and H chains) {Fab F9.13.7 (mouse), kappa L chain}
qvqlqqpgaelvkpgasvklsckasgytftsywmhwvkqgpgqglewigeidpsdsypny
nekfkgkatltvdkssstaymqlssltsedsavyycaslyyygtsygvldywgqgtsvtv
s
>d1fbiq2 2.1.1.2.56 (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 2.49.1.1.3 (272-466) Collagenase, C-terminal domain {Porcine (Sus scroffa)}
pqtpqvcdskltfdaittlrgelmffkdrfymrtnsfypevelnfisvfwpqvpnglqaa
yeiadrdevrffkgnkywavrgqdvlygypkdihrsfgfpstvknidaavfeedtgktyf
fvahecwrydeykqsmdtgypkmiaeefpgignkvdavfqkdgflyffhgtrqyqfdfkt
kriltlqkanswfnc
>d1fbl_2 4.52.1.7.4 (100-271) Stromelysin-1 (MMP-3) {Porcine (Sus scroffa) fibroblast}
fvltpgnprwenthltyrienytpdlsredvdraiekafqlwsnvspltftkvsegqadi
misfvrgdhrdnspfdgpggnlahafqpgpgiggdahfdederwtknfrdynlyrvaahe
lghslglshstdigalmypnyiytgdvqlsqddidgiqaiygpsenpvqpsg
>d1fbpa_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
fdtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnv
tgdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssn
idclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfm
ldpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryv
gsmvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldi
vptdihqrapiilgspedvtelleiyqkha
>d1fbpb_ 5.8.1.1.1 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_ 3.48.1.4.1 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, phosphatase domain {Rat (Rattus norvegicus)}
rsiylcrhgeselnlrgriggdsglsargkqyayalanfirsqgisslkvwtshxkrtiq
taealgvpyeqwkalneidagvceextyeeiqehypeefalrdqdkyryrypkgesyedl
vqrlepvixelerqenvlvichqavxrcllayfldkssdelpylkcplhtvlkltpvayg
crvesiylnv
>d1fbtb_ 3.48.1.4.1 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, phosphatase domain {Rat (Rattus norvegicus)}
rsiylcrhgeselnlrgriggdsglsargkqyayalanfirsqgisslkvwtshxkrtiq
taealgvpyeqwkalneidagvceextyeeiqehypeefalrdqdkyryrypkgesyedl
vqrlepvixelerqenvlvichqavxrcllayfldkssdelpylkcplhtvlkltpvayg
crvesiylnv
>d1fc1a1 2.1.1.2.107 (238-341) Immunoglobulin (constant domains of L and H chains) {Fc (human) IgG1 class}
psvflfppkpkdtlmisrtpevtcvvvdvshedpqvkfnwyvdgvqvhnaktkpreqqyn
styrvvsvltvlhqnwldgkeykckvsnkalpapiektiskakg
>d1fc1a2 2.1.1.2.107 (342-443) Immunoglobulin (constant domains of L and H chains) {Fc (human) IgG1 class}
qprepqvytlppsreemtknqvsltclvkgfypsdiavewesngqpennykttppvldsd
gsfflyskltvdksrwqqgnvfscsvmhealhnhytqkslsl
>d1fc1b1 2.1.1.2.107 (238-341) Immunoglobulin (constant domains of L and H chains) {Fc (human) IgG1 class}
psvflfppkpkdtlmisrtpevtcvvvdvshedpqvkfnwyvdgvqvhnaktkpreqqyn
styrvvsvltvlhqnwldgkeykckvsnkalpapiektiskakg
>d1fc1b2 2.1.1.2.107 (342-443) Immunoglobulin (constant domains of L and H chains) {Fc (human) IgG1 class}
qprepqvytlppsreemtknqvsltclvkgfypsdiavewesngqpennykttppvldsd
gsfflyskltvdksrwqqgnvfscsvmhealhnhytqkslsl
>d1fc2c_ 1.8.1.1.1 Immunoglobulin-binding protein A modules {(Staphylococcus aureus)}
fnkeqqnafyeilhlpnlneeqrngfiqslkddpsqsanllaea
>d1fc2d1 2.1.1.2.107 (238-341) Immunoglobulin (constant domains of L and H chains) {Fc (human) IgG1 class}
psvflfppkpkdtlmisrtpevtcvvvdvshedpqvkfnwyvdgvqvhnaktkpreqqyn
styrvvsvltvlhqnwldgkeykckvsnkalpapiektiskakg
>d1fc2d2 2.1.1.2.107 (342-443) Immunoglobulin (constant domains of L and H chains) {Fc (human) IgG1 class}
qprepqvytlppsreemtknqvsltclvkgfypsdiavewesngqpennykttppvldsd
gsfflyskltvdksrwqqgnvfscsvmhealhnhytqkslsl
>d1fca__ 4.34.1.1.3 Ferredoxin II {(Closridium acidi-urici)}
ayvineaciscgacepecpvdaisqggsryvidadtcidcgacagvcpvdapvqa
>d1fcba1 3.1.7.1.5 (98-511) Flavocytochrome b2, C-terminal domain {yeast (Saccharomyces cerevisiae)}
apgetkediarkeqlksllppldniinlydfeylasqtltkqawayyssgandevthren
hnayhriffkpkilvdvrkvdistdmlgshvdvpfyvsatalcklgnplegekdvargcg
qgvtkvpqmistlascspeeiieaapsdkqiqwyqlyvnsdrkitddlvknveklgvkal
fvtvdapslgqrekdmklkfsntkagpkamkktnveesqgasralskfidpsltwkdiee
lkkktklpivikgvqrtedvikaaeigvsgvvlsnhggrqldfsrapievlaetmpileq
rnlkdklevfvdggvrrgtdvlkalclgakgvglgrpflyanscygrngvekaieilrde
iemsmrllgvtsiaelkpdlldlstlkartvgvpndvlynevyegptltefeda
>d1fcba2 4.70.1.1.3 (1-97) Flavocytochrome b2, N-terminal domain {yeast (Saccharomyces cerevisiae)}
epkldmnkqkispaevakhnkpddcwvvingyvydltrflpnhpggqdvikfnagkdvta
ifeplhapnvidkyiapekklgplqgsmppelvcppy
>d1fcca1 2.1.1.2.107 (238-341) Immunoglobulin (constant domains of L and H chains) {Fc (human) IgG1 class}
psvflfppkpkdtlmisrtpevtcvvvdvshedpqvkfnwyvdgvqvhnaktkpreqqyn
styrvvsvltvlhqnwldgkeykckvsnkalpapiektiskakg
>d1fcca2 2.1.1.2.107 (342-443) Immunoglobulin (constant domains of L and H chains) {Fc (human) IgG1 class}
qprepqvytlppsreemtknqvsltclvkgfypsdiavewesngqpennykttppvldsd
gsfflyskltvdksrwqqgnvfscsvmhealhnhytqkslsl
>d1fccc_ 4.11.1.1.1 Immunoglobulin-binding protein G, separate domains {group G streptococcus (Streptomyces griseus)}
ttyklvingktlkgettteavdaataekvfkqyandngvdgewtyddatktftvte
>d1fcda1 3.4.1.4.11 (1-114,256-327) Flavocytochrome c sulfide dehydrogenase, FCSD, flavin-binding subunit {Purple phototrophic bacterium (Chromatium vinosum)}
agrkvvvvgggtggataakyikladpsievtliepntdyytcylsneviggdrklesikh
gydglrahgiqvvhdsatgidpdkklvktaggaefgydrcvvapgieliydkieXqragk
iaqiagltndagwcpvdiktfessihkgihvigdasianpmpksgysansqgkvaaaavv
vllkgee
>d1fcda2 3.4.1.4.11 (115-255) Flavocytochrome c sulfide dehydrogenase, FCSD, flavin-binding subunit {Purple phototrophic bacterium (Chromatium vinosum)}
gyseeaaaklphawkageqtailrkqledmadggtvviappaapfrcppgpyerasqvay
ylkahkpmskviildssqtfskqsqfskgwerlygfgtenamiewhpgpdsavvkvdgge
mmvetafgdefkadvinlipp
>d1fcda3 4.48.1.1.9 (328-401) Flavocytochrome c sulfide dehydrogenase, FCSD, flavin-binding subunit {Purple phototrophic bacterium (Chromatium vinosum)}
pgtpsylntcysilapaygisvaaiyrpnadgsaiesvpdsggvtpvdapdwvlerevqy
ayswynnivhdtfg
>d1fcdb1 3.4.1.4.11 (1-114,256-327) Flavocytochrome c sulfide dehydrogenase, FCSD, flavin-binding subunit {Purple phototrophic bacterium (Chromatium vinosum)}
agrkvvvvgggtggataakyikladpsievtliepntdyytcylsneviggdrklesikh
gydglrahgiqvvhdsatgidpdkklvktaggaefgydrcvvapgieliydkieXqragk
iaqiagltndagwcpvdiktfessihkgihvigdasianpmpksgysansqgkvaaaavv
vllkgee
>d1fcdb2 3.4.1.4.11 (115-255) Flavocytochrome c sulfide dehydrogenase, FCSD, flavin-binding subunit {Purple phototrophic bacterium (Chromatium vinosum)}
gyseeaaaklphawkageqtailrkqledmadggtvviappaapfrcppgpyerasqvay
ylkahkpmskviildssqtfskqsqfskgwerlygfgtenamiewhpgpdsavvkvdgge
mmvetafgdefkadvinlipp
>d1fcdb3 4.48.1.1.9 (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
>d1fcs__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
mkasedlkkvgvrvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihv
lhsrhpgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1fd2__ 4.34.1.2.1 Ferredoxin {(Azotobacter vinelandii )}
afvvtdncikckytdcvevapvdcfyegpnflvihpdecidcalcepecpaqaifsedev
pedmqefiqlnaelaevwpnitekkdplpdaedwdgvkgklqhler
>d1fda__ 4.34.1.2.1 Ferredoxin {(Azotobacter vinelandii )}
afvvtdncikckytdcvevcpvdcfyegpnflvihpdecidcalcepecpaqaifsedev
pedmqefiqlnaelaevwpnitekkdplpdaedwdgvkgklqhler
>d1fdb__ 4.34.1.2.1 Ferredoxin {(Azotobacter vinelandii )}
afvvtdncikckytdcvevcpvdcfyegpnflvihpdecidcalcepecpaqaifsedev
pedmqefiqlnaelaevwpnitekkdplpdaedwdgvkgklqhler
>d1fdc__ 4.34.1.2.1 Ferredoxin {(Azotobacter vinelandii )}
afvvtdncikckytdcvevcpvdcfyegpnflvihpdecidcalcepecpaqaifsedev
pedmqefiqlnaelaevwpnitekkdplpdaedwdgvkgklqhler
>d1fdd__ 4.34.1.2.1 Ferredoxin {(Azotobacter vinelandii )}
afvvtdncikckytncvevcpvdcfyegpnflvihpdecidcalcepecpaqaifsedev
pedmqefiqlnaelaevwpnitekkdplpdaedwdgvkgklqhler
>d1fdha_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1fdhg_ 1.1.1.1.26 Hemoglobin, beta-chain {human fetus (Homo sapiens), gamma-chain}
xghfteedkatitslwgkvnvedaggetlgrllvvypwtqrffdsfgnlssasaimgnpk
vkahgkkvltslgdaikhlddlkgtfaqlselhcdklhvdpenfkllgnvlvtvlaihfg
keftpevqaswqkmvtgvasalssryh
>d1fdi_1 2.39.2.2.3 (565-715) Formate dehydrogenase H {(Escherichia coli)}
pidkltdeypmvlstvrevghyscrsmtgncaalaaladepgyaqintedakrlgiedea
lvwvhsrkgkiitraqvsdrpnkgaiymtyqwwigacnelvtenlspitktpeykycavr
vepiadqraaeqyvideynklktrlreaala
>d1fdi_2 3.69.1.1.3 (1-564) Formate dehydrogenase H {(Escherichia coli)}
mkkvvtvcpycasgckinlvvdngkivraeaaqgktnqgtlclkgyygwdfindtqiltp
rlktpmirrqrggklepvswdealnyvaerlsaikekygpdaiqttgssrgtgnetnyvm
qkfaravigtnnvdccarvxhgpsvaglhqsvgngamsnaineidntdlvfvfgynpads
hpivanhvinakrngakiivcdprkietariadmhialkngsniallnamghviieenly
dkafvasrtegfeeyrkivegytpesveditgvsaseirqaarmyaqaksaailwgmgvt
qfyqgvetvrsltslamltgnlgkphagvnpvrgqnnvqgacdmgalpdtypgyqyvkdp
anrekfakawgveslpahtgyriselphraahgevraayimgedplqtdaelsavrkafe
dlelvivqdifmtktasaadvilpstswgehegvftaadrgfqrffkavepkwdlktdwq
iiseiatrmgypmhynntqeiwdelrhlcpdfygatyekmgelgfiqwpcrdtsdadqgt
sylfkekfdtpnglaqfftcdwva
>d1fdlh1 2.1.1.1.39 (1-116) Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
qvqlkesgpglvapsqslsitctvsgfsltgygvnwvrqppgkglewlgmiwgdgntdyn
salksrlsiskdnsksqvflkmnslhtddtaryycarerdyrldywgqgttltvss
>d1fdlh2 2.1.1.2.47 (117-218) Immunoglobulin (constant domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
asttppsvfplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpssprpsetvtcnvahpasstkvdkkivprdc
>d1fdll1 2.1.1.1.39 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
diqmtqspaslsasvgetvtitcrasgnihnylawyqqkqgkspqllvyytttladgvps
rfsgsgsgtqyslkinslqpedfgsyycqhfwstprtfgggtkleik
>d1fdll2 2.1.1.2.47 (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
>d1fdm__ 1.105.3.1.1 Inovirus (filamentous phage) major coat protein {strain fd}
aegddpakaafdslqasateyigyawamvvvivgatigiklfkkftskas
>d1fdn__ 4.34.1.1.3 Ferredoxin II {(Closridium acidi-urici)}
ayvineaciscgacepecpvnaissgddryvidadtcidcgacagvcpvdapvqa
>d1fdo_1 2.39.2.2.3 (565-715) Formate dehydrogenase H {(Escherichia coli)}
pidkltdeypmvlstvrevghyscrsmtgncaalaaladepgyaqintedakrlgiedea
lvwvhsrkgkiitraqvsdrpnkgaiymtyqwwigacnelvtenlspitktpeykycavr
vepiadqraaeqyvideynklktrlreaala
>d1fdo_2 3.69.1.1.3 (1-564) Formate dehydrogenase H {(Escherichia coli)}
mkkvvtvcpycasgckinlvvdngkivraeaaqgktnqgtlclkgyygwdfindtqiltp
rlktpmirrqrggklepvswdealnyvaerlsaikekygpdaiqttgssrgtgnetnyvm
qkfaravigtnnvdccarvxhgpsvaglhqsvgngamsnaineidntdlvfvfgynpads
hpivanhvinakrngakiivcdprkietariadmhialkngsniallnamghviieenly
dkafvasrtegfeeyrkivegytpesveditgvsaseirqaarmyaqaksaailwgmgvt
qfyqgvetvrsltslamltgnlgkphagvnpvrgqnnvqgacdmgalpdtypgyqyvkdp
anrekfakawgveslpahtgyriselphraahgevraayimgedplqtdaelsavrkafe
dlelvivqdifmtktasaadvilpstswgehegvftaadrgfqrffkavepkwdlktdwq
iiseiatrmgypmhynntqeiwdelrhlcpdfygatyekmgelgfiqwpcrdtsdadqgt
sylfkekfdtpnglaqfftcdwva
>d1fdr_1 2.32.1.1.3 (2-100) Ferredoxin reductase (flavodoxin reductase) {(Escherichia coli)}
adwvtgkvtkvqnwtdalfsltvhapvlpftagqftklgleidgervqraysyvnspdnp
dlefylvtvpdgklsprlaalkpgdevqvvseaagffvl
>d1fdr_2 3.16.1.1.3 (101-248) Ferredoxin reductase (flavodoxin reductase) {(Escherichia coli)}
devphcetlwmlatgtaigpylsilrlgkdldrfknlvlvhaaryaadlsylplmqelek
ryegklriqtvvsretaagsltgripaliesgelestiglpmnketshvmlcgnpqmvrd
tqqllketrqmtkhlrrrpghmtaehyw
>d1fds__ 3.22.1.2.3 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylahskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevfgdv
>d1fdt__ 3.22.1.2.3 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylahskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevfg
>d1fdua_ 3.22.1.2.3 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylalskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevfg
>d1fdub_ 3.22.1.2.3 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylalskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevfg
>d1fduc_ 3.22.1.2.3 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylalskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevfg
>d1fdud_ 3.22.1.2.3 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylalskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevfg
>d1fdva_ 3.22.1.2.3 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylalskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevfg
>d1fdvb_ 3.22.1.2.3 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylalskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevfgd
>d1fdvc_ 3.22.1.2.3 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylalskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevfg
>d1fdvd_ 3.22.1.2.3 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylalskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevfgd
>d1fdw__ 3.22.1.2.3 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylaqskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevfg
>d1fdx__ 4.34.1.1.2 Ferredoxin II {(Peptococcus aerogenes)}
ayvindsciacgackpecpvniiqgsiyaidadscidcgscasvcpvgapnped
>d1fdya_ 3.1.3.1.1 N-acetylneuraminate lyase {(Escherichia coli)}
nlrgvmaalltpfdqqqaldkaslrrlvqfniqqgidglyvggstgeafvqslsereqvl
eivaeegkgkikliahvgcvttaesqqlaasakrygfdavsavtpfyypfsfeehcdhyr
aiidsadglpmvvynipalsgvkltldqintlvtlpgvgalkqtsgdlyqmeqirrehpd
lvlyngydeifasgllagadggigstynimgwryqgivkalkegdiqtaqklqtecnkvi
dlliktgvfrglktvlhymdvvsvplcrkpfgpvdekylpelkalaqqlmqe
>d1fdyb_ 3.1.3.1.1 N-acetylneuraminate lyase {(Escherichia coli)}
nlrgvmaalltpfdqqqaldkaslrrlvqfniqqgidglyvggstgeafvqslsereqvl
eivaeegkgkikliahvgcvttaesqqlaasakrygfdavsavtpfyypfsfeehcdhyr
aiidsadglpmvvynipalsgvkltldqintlvtlpgvgalkqtsgdlyqmeqirrehpd
lvlyngydeifasgllagadggigstynimgwryqgivkalkegdiqtaqklqtecnkvi
dlliktgvfrglktvlhymdvvsvplcrkpfgpvdekylpelkalaqqlmq
>d1fdyc_ 3.1.3.1.1 N-acetylneuraminate lyase {(Escherichia coli)}
nlrgvmaalltpfdqqqaldkaslrrlvqfniqqgidglyvggstgeafvqslsereqvl
eivaeegkgkikliahvgcvttaesqqlaasakrygfdavsavtpfyypfsfeehcdhyr
aiidsadglpmvvynipalsgvkltldqintlvtlpgvgalkqtsgdlyqmeqirrehpd
lvlyngydeifasgllagadggigstynimgwryqgivkalkegdiqtaqklqtecnkvi
dlliktgvfrglktvlhymdvvsvplcrkpfgpvdekylpelkalaqqlmq
>d1fdyd_ 3.1.3.1.1 N-acetylneuraminate lyase {(Escherichia coli)}
nlrgvmaalltpfdqqqaldkaslrrlvqfniqqgidglyvggstgeafvqslsereqvl
eivaeegkgkikliahvgcvttaesqqlaasakrygfdavsavtpfyypfsfeehcdhyr
aiidsadglpmvvynipalsgvkltldqintlvtlpgvgalkqtsgdlyqmeqirrehpd
lvlyngydeifasgllagadggigstynimgwryqgivkalkegdiqtaqklqtecnkvi
dlliktgvfrglktvlhymdvvsvplcrkpfgpvdekylpelkalaqqlmq
>d1fdza_ 3.1.3.1.1 N-acetylneuraminate lyase {(Escherichia coli)}
nlrgvmaalltpfdqqqaldkaslrrlvqfniqqgidglyvggstgeafvqslsereqvl
eivaeegkgkikliahvgcvttaesqqlaasakrygfdavsavtpfyypfsfeehcdhyr
aiidsadglpmvvynipalsgvkltldqintlvtlpgvgalkqtsgdlyqmeqirrehpd
lvlyngydeifasgllagadggigstynimgwryqgivkalkegdiqtaqklqtecnkvi
dlliktgvfrglktvlhymdvvsvplcrkpfgpvdekylpelkalaqqlmqe
>d1fdzb_ 3.1.3.1.1 N-acetylneuraminate lyase {(Escherichia coli)}
nlrgvmaalltpfdqqqaldkaslrrlvqfniqqgidglyvggstgeafvqslsereqvl
eivaeegkgkikliahvgcvttaesqqlaasakrygfdavsavtpfyypfsfeehcdhyr
aiidsadglpmvvynipalsgvkltldqintlvtlpgvgalkqtsgdlyqmeqirrehpd
lvlyngydeifasgllagadggigstynimgwryqgivkalkegdiqtaqklqtecnkvi
dlliktgvfrglktvlhymdvvsvplcrkpfgpvdekylpelkalaqqlmq
>d1fdzc_ 3.1.3.1.1 N-acetylneuraminate lyase {(Escherichia coli)}
nlrgvmaalltpfdqqqaldkaslrrlvqfniqqgidglyvggstgeafvqslsereqvl
eivaeegkgkikliahvgcvttaesqqlaasakrygfdavsavtpfyypfsfeehcdhyr
aiidsadglpmvvynipalsgvkltldqintlvtlpgvgalkqtsgdlyqmeqirrehpd
lvlyngydeifasgllagadggigstynimgwryqgivkalkegdiqtaqklqtecnkvi
dlliktgvfrglktvlhymdvvsvplcrkpfgpvdekylpelkalaqqlmq
>d1fdzd_ 3.1.3.1.1 N-acetylneuraminate lyase {(Escherichia coli)}
nlrgvmaalltpfdqqqaldkaslrrlvqfniqqgidglyvggstgeafvqslsereqvl
eivaeegkgkikliahvgcvttaesqqlaasakrygfdavsavtpfyypfsfeehcdhyr
aiidsadglpmvvynipalsgvkltldqintlvtlpgvgalkqtsgdlyqmeqirrehpd
lvlyngydeifasgllagadggigstynimgwryqgivkalkegdiqtaqklqtecnkvi
dlliktgvfrglktvlhymdvvsvplcrkpfgpvdekylpelkalaqqlmqe
>d1feaa1 3.4.1.4.3 (1-169,287-357) Trypanothione reductase {(Crithidia fasciculata)}
sraydlvvigagsggleagwnaaslhkkrvavidlqkhhgpphyaalggtcvnvgcvpkk
lmvtganymdtiresagfgweldresvrpnwkaliaaknkavsgindsyegmfadteglt
fhqgfgalqdnhtvlvresadpnsavletldteyillatgswpqhlgieXvprsqtlqle
kagvevakngaikvdaysktnvdniyaigdvtdrvmltpvainegaafvdtvfankprat
d
>d1feaa2 3.4.1.4.3 (170-286) Trypanothione reductase {(Crithidia fasciculata)}
gddlcitsneafyldeapkralcvgggyisiefagifnaykarggqvdlayrgdmilrgf
dselrkqlteqlranginvrthenpakvtknadgtrhvvfesgaeadydvvmlaigr
>d1feaa3 4.48.1.1.3 (358-487) Trypanothione reductase {(Crithidia fasciculata)}
htkvacavfsippmgvcgyveedaakkydqvavyessftplmhnisgstykkfmvrivtn
hadgevlgvhmlgdsspeiiqsvaiclkmgakisdfyntigvhptsaeelcsmrtpayfy
ekgkrvekid
>d1feab1 3.4.1.4.3 (1-169,287-357) Trypanothione reductase {(Crithidia fasciculata)}
sraydlvvigagsggleagwnaaslhkkrvavidlqkhhgpphyaalggtcvnvgcvpkk
lmvtganymdtiresagfgweldresvrpnwkaliaaknkavsgindsyegmfadteglt
fhqgfgalqdnhtvlvresadpnsavletldteyillatgswpqhlgieXvprsqtlqle
kagvevakngaikvdaysktnvdniyaigdvtdrvmltpvainegaafvdtvfankprat
d
>d1feab2 3.4.1.4.3 (170-286) Trypanothione reductase {(Crithidia fasciculata)}
gddlcitsneafyldeapkralcvgggyisiefagifnaykarggqvdlayrgdmilrgf
dselrkqlteqlranginvrthenpakvtknadgtrhvvfesgaeadydvvmlaigr
>d1feab3 4.48.1.1.3 (358-484) Trypanothione reductase {(Crithidia fasciculata)}
htkvacavfsippmgvcgyveedaakkydqvavyessftplmhnisgstykkfmvrivtn
hadgevlgvhmlgdsspeiiqsvaiclkmgakisdfyntigvhptsaeelcsmrtpayfy
ekgkrve
>d1feac1 3.4.1.4.3 (1-169,287-357) Trypanothione reductase {(Crithidia fasciculata)}
sraydlvvigagsggleagwnaaslhkkrvavidlqkhhgpphyaalggtcvnvgcvpkk
lmvtganymdtiresagfgweldresvrpnwkaliaaknkavsgindsyegmfadteglt
fhqgfgalqdnhtvlvresadpnsavletldteyillatgswpqhlgieXvprsqtlqle
kagvevakngaikvdaysktnvdniyaigdvtdrvmltpvainegaafvdtvfankprat
d
>d1feac2 3.4.1.4.3 (170-286) Trypanothione reductase {(Crithidia fasciculata)}
gddlcitsneafyldeapkralcvgggyisiefagifnaykarggqvdlayrgdmilrgf
dselrkqlteqlranginvrthenpakvtknadgtrhvvfesgaeadydvvmlaigr
>d1feac3 4.48.1.1.3 (358-487) Trypanothione reductase {(Crithidia fasciculata)}
htkvacavfsippmgvcgyveedaakkydqvavyessftplmhnisgstykkfmvrivtn
hadgevlgvhmlgdsspeiiqsvaiclkmgakisdfyntigvhptsaeelcsmrtpayfy
ekgkrvekid
>d1fead1 3.4.1.4.3 (1-169,287-357) Trypanothione reductase {(Crithidia fasciculata)}
sraydlvvigagsggleagwnaaslhkkrvavidlqkhhgpphyaalggtcvnvgcvpkk
lmvtganymdtiresagfgweldresvrpnwkaliaaknkavsgindsyegmfadteglt
fhqgfgalqdnhtvlvresadpnsavletldteyillatgswpqhlgieXvprsqtlqle
kagvevakngaikvdaysktnvdniyaigdvtdrvmltpvainegaafvdtvfankprat
d
>d1fead2 3.4.1.4.3 (170-286) Trypanothione reductase {(Crithidia fasciculata)}
gddlcitsneafyldeapkralcvgggyisiefagifnaykarggqvdlayrgdmilrgf
dselrkqlteqlranginvrthenpakvtknadgtrhvvfesgaeadydvvmlaigr
>d1fead3 4.48.1.1.3 (358-484) Trypanothione reductase {(Crithidia fasciculata)}
htkvacavfsippmgvcgyveedaakkydqvavyessftplmhnisgstykkfmvrivtn
hadgevlgvhmlgdsspeiiqsvaiclkmgakisdfyntigvhptsaeelcsmrtpayfy
ekgkrve
>d1feba1 3.4.1.4.3 (1-169,287-357) Trypanothione reductase {(Crithidia fasciculata)}
sraydlvvigagsggleagwnaaslhkkrvavidlqkhhgpphyaalggtcvnvgcvpkk
lmvtganymdtiresagfgweldresvrpnwkaliaaknkavsgindsyegmfadteglt
fhqgfgalqdnhtvlvresadpnsavletldteyillatgswpqhlgieXvprsqtlqle
kagvevakngaikvdaysktnvdniyaigdvtdrvmltpvainegaafvdtvfankprat
d
>d1feba2 3.4.1.4.3 (170-286) Trypanothione reductase {(Crithidia fasciculata)}
gddlcitsneafyldeapkralcvgggyisiefagifnaykarggqvdlayrgdmilrgf
dselrkqlteqlranginvrthenpakvtknadgtrhvvfesgaeadydvvmlaigr
>d1feba3 4.48.1.1.3 (358-487) Trypanothione reductase {(Crithidia fasciculata)}
htkvacavfsippmgvcgyveedaakkydqvavyessftplmhnisgstykkfmvrivtn
hadgevlgvhmlgdsspeiiqsvaiclkmgakisdfyntigvhptsaeelcsmrtpayfy
ekgkrvekid
>d1febb1 3.4.1.4.3 (1-169,287-357) Trypanothione reductase {(Crithidia fasciculata)}
sraydlvvigagsggleagwnaaslhkkrvavidlqkhhgpphyaalggtcvnvgcvpkk
lmvtganymdtiresagfgweldresvrpnwkaliaaknkavsgindsyegmfadteglt
fhqgfgalqdnhtvlvresadpnsavletldteyillatgswpqhlgieXvprsqtlqle
kagvevakngaikvdaysktnvdniyaigdvtdrvmltpvainegaafvdtvfankprat
d
>d1febb2 3.4.1.4.3 (170-286) Trypanothione reductase {(Crithidia fasciculata)}
gddlcitsneafyldeapkralcvgggyisiefagifnaykarggqvdlayrgdmilrgf
dselrkqlteqlranginvrthenpakvtknadgtrhvvfesgaeadydvvmlaigr
>d1febb3 4.48.1.1.3 (358-484) Trypanothione reductase {(Crithidia fasciculata)}
htkvacavfsippmgvcgyveedaakkydqvavyessftplmhnisgstykkfmvrivtn
hadgevlgvhmlgdsspeiiqsvaiclkmgakisdfyntigvhptsaeelcsmrtpayfy
ekgkrve
>d1feca1 3.4.1.4.3 (1-169,287-357) Trypanothione reductase {(Crithidia fasciculata)}
sraydlvvigagsggleagwnaaslhkkrvavidlqkhhgpphyaalggtcvnvgcvpkk
lmvtganymdtiresagfgweldresvrpnwkaliaaknkavsgindsyegmfadteglt
fhqgfgalqdnhtvlvresadpnsavletldteyillatgswpqhlgieXvprsqtlqle
kagvevakngaikvdaysktnvdniyaigdvtdrvmltpvainegaafvdtvfankprat
d
>d1feca2 3.4.1.4.3 (170-286) Trypanothione reductase {(Crithidia fasciculata)}
gddlcitsneafyldeapkralcvgggyisiefagifnaykarggqvdlayrgdmilrgf
dselrkqlteqlranginvrthenpakvtknadgtrhvvfesgaeadydvvmlaigr
>d1feca3 4.48.1.1.3 (358-485) Trypanothione reductase {(Crithidia fasciculata)}
htkvacavfsippmgvcgyveedaakkydqvavyessftplmhnisgstykkfmvrivtn
hadgevlgvhmlgdsspeiiqsvaiclkmgakisdfyntigvhptsaeelcsmrtpayfy
ekgkrvek
>d1fecb1 3.4.1.4.3 (2-169,287-357) Trypanothione reductase {(Crithidia fasciculata)}
raydlvvigagsggleagwnaaslhkkrvavidlqkhhgpphyaalggtcvnvgcvpkkl
mvtganymdtiresagfgweldresvrpnwkaliaaknkavsgindsyegmfadtegltf
hqgfgalqdnhtvlvresadpnsavletldteyillatgswpqhlgieXvprsqtlqlek
agvevakngaikvdaysktnvdniyaigdvtdrvmltpvainegaafvdtvfankpratd
>d1fecb2 3.4.1.4.3 (170-286) Trypanothione reductase {(Crithidia fasciculata)}
gddlcitsneafyldeapkralcvgggyisiefagifnaykarggqvdlayrgdmilrgf
dselrkqlteqlranginvrthenpakvtknadgtrhvvfesgaeadydvvmlaigr
>d1fecb3 4.48.1.1.3 (358-486) Trypanothione reductase {(Crithidia fasciculata)}
htkvacavfsippmgvcgyveedaakkydqvavyessftplmhnisgstykkfmvrivtn
hadgevlgvhmlgdsspeiiqsvaiclkmgakisdfyntigvhptsaeelcsmrtpayfy
ekgkrveki
>d1fel__ 2.45.1.1.1 Retinol binding protein {bovine (Bos taurus)}
erdcrvssfrvkenfdkarfagtwyamakkdpeglflqdnivaefsvdenghmsatakgr
vrllnnwdvcadmvgtftdtedpakfkmkywgvasflqkgnddhwiidtdyetfavqysc
rllnldgtcadsysfvfardpsgfspevqkivrqrqeelclarqyrliphngycd
>d1fem__ 2.45.1.1.1 Retinol binding protein {bovine (Bos taurus)}
erdcrvssfrvkenfdkarfagtwyamakkdpeglflqdnivaefsvdenghmsatakgr
vrllnnwdvcadmvgtftdtedpakfkmkywgvasflqkgnddhwiidtdyetfavqysc
rllnldgtcadsysfvfardpsgfspevqkivrqrqeelclarqyrliphngycdgk
>d1fen__ 2.45.1.1.1 Retinol binding protein {bovine (Bos taurus)}
erdcrvssfrvkenfdkarfagtwyamakkdpeglflqdnivaefsvdenghmsatakgr
vrllnnwdvcadmvgtftdtedpakfkmkywgvasflqkgnddhwiidtdyetfavqysc
rllnldgtcadsysfvfardpsgfspevqkivrqrqeelclarqyrliphngycdgk
>d1fer__ 4.34.1.2.1 Ferredoxin {(Azotobacter vinelandii )}
afvvtdncikckytdcvevcpvdcfyegpnflvihpdecidcalcepecpaqaifsedev
pedmqefiqlnaelaevwpnitekkdplpdaedwdgvkgklqhler
>d1ffa__ 3.14.7.1.1 Cutinase {fungus (Fusarium solani, subsp. pisi)}
rttrddlingnsascrdvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdaalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1ffb__ 3.14.7.1.1 Cutinase {fungus (Fusarium solani, subsp. pisi)}
rttrddlingnsascrdvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgddalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1ffc__ 3.14.7.1.1 Cutinase {fungus (Fusarium solani, subsp. pisi)}
rttrddlingnsascrdvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdlalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1ffd__ 3.14.7.1.1 Cutinase {fungus (Fusarium solani, subsp. pisi)}
rttrddlingnsascrdvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdwalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1ffe__ 3.14.7.1.1 Cutinase {fungus (Fusarium solani, subsp. pisi)}
rttrddlingnsascrdvifiyargatetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1ffh_1 1.28.1.1.1 (2-88) Signal sequence recognition protein Ffh {(Thermus aquaticus)}
fqqlsarlqeaigrlrgrgriteedlkatlreirralmdadvnlevtrdfvervreealg
kqvlesltpaevilatvyealkealgg
>d1ffh_2 3.29.1.6.4 (89-295) GTPase domain of the signal sequence recognition protein Ffh {(Thermus aquaticus)}
earlpvlkdrnlwflvglqgsgktttaaklalyykgkgrrpllvaadtqrpaareqlrll
gekvgvpvlevmdgespesirrrveekarleardlilvdtagrlqideplmgelarlkev
lgpdevllvldamtgqealsvarafdekvgvtglvltkldgdarggaalsarhvtgkpiy
fagvsekpeglepfyperlagrilgmg
>d1fga__ 2.31.1.1.1 Basic FGF {human (Homo sapiens)}
pkrlycknggfflrihpdgrvdgvreksdphiklqlqaeergvvsikgvcanrylamked
grllaskcvtdecffferlesnnyntyrsrkytswyvalkrtgqyklgsktgpgqkailf
lpms
>d1fgbd_ 2.29.2.1.3 Cholera toxin {(Vibrio cholerae)}
tpqnitdlcaeyhntqihtlndkifsyteslagkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1fgbe_ 2.29.2.1.3 Cholera toxin {(Vibrio cholerae)}
tpqnitdlcaeyhntqihtlndkifsyteslagkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1fgbf_ 2.29.2.1.3 Cholera toxin {(Vibrio cholerae)}
tpqnitdlcaeyhntqihtlndkifsyteslagkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1fgbg_ 2.29.2.1.3 Cholera toxin {(Vibrio cholerae)}
tpqnitdlcaeyhntqihtlndkifsyteslagkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1fgbh_ 2.29.2.1.3 Cholera toxin {(Vibrio cholerae)}
tpqnitdlcaeyhntqihtlndkifsyteslagkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktphaiaaisman
>d1fgh_1 3.5.2.1.2 (529-754) Aconitase, C-terminal domain {bovine (Bos taurus)}
vdvsptsqrlqllepfdkwdgkdledlqilikvkgkcttdhisaagpwlkfrghldnisn
nlligainsenrkansvrnavtqefgpvpdtaryykqhgirwvvigdenygegssrehsa
leprflggraiitksfarihetnlkkqgllpltfadpadynkihpvdkltiqglkdfapg
kpltciikhpngtqetillnhtfnetqiewfragsalnrmkelqqk
>d1fgh_2 3.71.1.1.2 (2-528) Aconitase, first 3 domains {bovine (Bos taurus)}
rakvamshfepheyirydlleknidivrkrlnrpltlsekivyghlddpanqeiergkty
lrlrpdrvamqdataqmamlqfissglpkvavpstihcdhlieaqlggekdlrrakdinq
evynflatagakygvgfwrpgsgiihqiilenyaypgvlligtdshtpnggglggicigv
ggadavdvmagipwelkcpkvigvkltgslsgwtspkdvilkvagiltvkggtgaiveyh
gpgvdsisctgmaticnmgaeigattsvfpynhrmkkylsktgradianladefkdhlvp
dsgchydqlieinlselkphingpftpdlahpvaevgsvaekegwpldirvgligsctns
syedmgrsaavakqalahglkcksqftitpgseqiratierdgyaqvlrdvggivlanac
gpcigqwdrkdikkgekntivtsynrnftgrndanpethafvtspeivtalaiagtlkfn
petdfltgkdgkkfkleapdadelpraefdpgqdtyqhppkdssgqr
>d1fgia_ 5.1.1.2.5 Fibroblast growth factor receptor 1 {human (Homo sapiens)}
elpedprwelprdrlvlgkplgegafgqvvlaeaigldkdkpnrvtkvavkmlksdatek
dlsdlisememmkmigkhkniinllgactqdgplyviveyaskgnlreylqarrppgley
synpshnpeeqlsskdlvscayqvargmeylaskkcihrdlaarnvlvtednvmkiadfg
lardihhidyykkttngrlpvkwmapealfdriythqsdvwsfgvllweiftlggspypg
vpveelfkllkeghrmdkpsnctnelymmmrdcwhavpsqrptfkqlvedldrivalts
>d1fgib_ 5.1.1.2.5 Fibroblast growth factor receptor 1 {human (Homo sapiens)}
seyelpedprwelprdrlvlgkplgegafgqvvlaeaigldkdkpnrvtkvavkmlksda
tekdlsdlisememmkmigkhkniinllgactqdgplyviveyaskgnlreylqarrppg
leysynpshnpeeqlsskdlvscayqvargmeylaskkcihrdlaarnvlvtednvmkia
dfglardihhidyykkttngrlpvkwmapealfdriythqsdvwsfgvllweiftlggsp
ypgvpveelfkllkeghrmdkpsnctnelymmmrdcwhavpsqrptfkqlvedldrival
t
>d1fgja_ 1.107.1.4.1 Hydroxylamine oxidoreductase {(Nitrosomonas europaea)}
distvpdetydalkldrgkatpketyealvkrykdpahgagkgtmgdywepiaisiymdp
ntfykppvspkevaerkdcvechsdetpvwvrawkrsthanldkirnlksddplyykkgk
leevennlrsmgklgeketlkevgcidchvdvnkkdkadhtkdirmptadtcgtchlref
aereserdtmvwpngqwpagrpshaldytaniettvwatmpqrevaegctmchtnqnkcd
nchtrhefsaaesrkpeacatchsgvdhnnweaytmskhgklaemnrdkwnwevrlkdaf
skggqnaptcaachmeyegeythnitrktrwanypfvpgiaenitsdwsearldswvltc
tqchserfarsyldlmdkgtleglakyqeanaivhkmyedgtltgqktnrpnppepekpg
fgiftqlfwskgnnpaslelkvlemgennlakmhvglahvnpggwtytegwgpmnrayve
iqdeytkmqelsalqarvn
>d1fgjb_ 1.107.1.4.1 Hydroxylamine oxidoreductase {(Nitrosomonas europaea)}
distvpdetydalkldrgkatpketyealvkrykdpahgagkgtmgdywepiaisiymdp
ntfykppvspkevaerkdcvechsdetpvwvrawkrsthanldkirnlksddplyykkgk
leevennlrsmgklgeketlkevgcidchvdvnkkdkadhtkdirmptadtcgtchlref
aereserdtmvwpngqwpagrpshaldytaniettvwatmpqrevaegctmchtnqnkcd
nchtrhefsaaesrkpeacatchsgvdhnnweaytmskhgklaemnrdkwnwevrlkdaf
skggqnaptcaachmeyegeythnitrktrwanypfvpgiaenitsdwsearldswvltc
tqchserfarsyldlmdkgtleglakyqeanaivhkmyedgtltgqktnrpnppepekpg
fgiftqlfwskgnnpaslelkvlemgennlakmhvglahvnpggwtytegwgpmnrayve
iqdeytkmqelsalqarvn
>d1fgka_ 5.1.1.2.5 Fibroblast growth factor receptor 1 {human (Homo sapiens)}
elpedprwelprdrlvlgkplgegafgqvvlaeaigldkdkpnrvtkvavkmlksdatek
dlsdlisememmkmigkhkniinllgactqdgplyviveyaskgnlreylqarrppgley
synpshnpeeqlsskdlvscayqvargmeylaskkcihrdlaarnvlvtednvmkiadfg
lardihhidyykkttngrlpvkwmapealfdriythqsdvwsfgvllweiftlggspypg
vpveelfkllkeghrmdkpsnctnelymmmrdcwhavpsqrptfkqlvedldrivalts
>d1fgkb_ 5.1.1.2.5 Fibroblast growth factor receptor 1 {human (Homo sapiens)}
seyelpedprwelprdrlvlgkplgegafgqvvlaeaigldkdkpnrvtkvavkmlksda
tekdlsdlisememmkmigkhkniinllgactqdgplyviveyaskgnlreylqarrppg
leysynpshnpeeqlsskdlvscayqvargmeylaskkcihrdlaarnvlvtednvmkia
dfglardihhidyykkttngrlpvkwmapealfdriythqsdvwsfgvllweiftlggsp
ypgvpveelfkllkeghrmdkpsnctnelymmmrdcwhavpsqrptfkqlvedldrival
t
>d1fgla_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
mvnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgf
mcqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictakte
wldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1fgnh1 2.1.1.1.95 (1-117) Immunoglobulin (variable domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
eiqlqqsgaelvrpgalvklsckasgfnikdyymhwvkqrpeqglewiglidpengntiy
dpkfqgkasitadtssntaylqlssltsedtavyycardnsyyfdywgqgttltvss
>d1fgnh2 2.1.1.2.95 (118-212) Immunoglobulin (constant domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpsstwpsetvtcnvahpasstkvdk
>d1fgnl1 2.1.1.1.95 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
dikmtqspssmyaslgervtitckasqdirkylnwyqqkpwkspktliyyatsladgvps
rfsgsgsgqdysltisslesddtatyyclqhgespytfgggtkleinr
>d1fgnl2 2.1.1.2.95 (109-213) Immunoglobulin (constant domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrne
>d1fgp__ 2.27.1.1.1 The n-terminal domains of the minor coat protein g3p {fd phage (bacteriophage fd)}
etvesclakphtensftnvwkddktldryanyegclwnatgvvvctgdetqcygtwvpig
laipenaaah
>d1fgvh_ 2.1.1.1.24 Immunoglobulin (variable domains of L and H chains) {Fab H52 (synthetic, humanised version), kappa L chain}
evqlvesggglvqpggslrlscatsgytfteytmhwmrqapgkglewvaginpknggtsy
adsvkgrftisvdkskntlylqmnslraedtavyycarwrglnygfdvryfdvwgqgtlv
tvss
>d1fgvl_ 2.1.1.1.24 Immunoglobulin (variable domains of L and H chains) {Fab H52 (synthetic, humanised version), kappa L chain}
diqmtqspsslsasvgdrvtitcrasqdinnylnwyqqkpgkapklliyytstlesgvps
rfsgsgsgtdytltisslqpedfatyycqqgntlpptfgagtkveik
>d1fha__ 1.25.1.1.3 (Apo)ferritin {human (Homo sapiens), H chain}
tsqvrqnyhqdseaainrqinlelyasyvylsmsyyfdrddvalknfakyflhqsheere
haeklmklqnqrggriflqdiqkpdcddwesglnamecalhleknvnqsllelhklatdk
ndphlcdfiethylneqvkaikelgdhvtnlrkmgapesglaeylfdkhtlg
>d1fhb__ 1.3.1.1.6 Mitochondrial cytochrome c {baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrqsgqaegysytdanikk
nvlwdennmseyltnpkkyipgtkaafgglkkekdrndlitylkkase
>d1fhi__ 4.9.1.1.2 FHIT (fragile histidine triad protein) {Human (Homo sapiens)}
sfrfgqhlikpsvvflktelsfalvnrkpvvpghvlvcplrpverfhdlrpdevadlfqt
tqrvgtvvekhfhgtsltfsmqdgpeagqtvkhvhvhvlprkagdfhrndsiyeelqkhd
kedfpaswrseeemaaeaaalrvyfq
>d1fhs__ 4.53.1.1.7 Growth factor receptor-bound protein 2 (GRB2) {human (Homo sapiens)}
giemkphpwffgkiprakaeemlskqrhdgafliresesapgdfslsvkfgndvqhfkvl
rdgagkyflwvvkfnslnelvdyhrstsvsrnqqiflrdieqvpqqptyvqa
>d1fht__ 4.34.7.1.2 U1A protein {human (Homo sapiens)}
avpetrpnhtiyinnlnekikkdelkkslyaifsqfgqildilvsrslkmrgqafvifke
vssatnalrsmqgfpfydkpmriqyaktdsdiiakmkgtfverdrkrekrkpksqe
>d1fiaa_ 1.84.1.1.1 FIS protein {(Escherichia coli)}
vltvstvnsqdqvtqkplrdsvkqalknyfaqlngqdvndlyelvlaeveqplldmvmqy
trgnqtraalmmginrgtlrkklkkygmn
>d1fiab_ 1.84.1.1.1 FIS protein {(Escherichia coli)}
vltvstvnsqdqvtqkplrdsvkqalknyfaqlngqdvndlyelvlaeveqplldmvmqy
trgnqtraalmmginrgtlrkklkkygmn
>d1fib__ 4.106.1.1.1 beta- and gamma-Fibrinogen C-terminal domains {human (Homo sapiens)}
qihditgkdcqdiankgakqsglyfikplkanqqflvyceidgsgngwtvfqkrldgsvd
fkknwiqykegfghlsptgttefwlgnekihlistqsaipyalrveledwngrtstadya
mfkvgpeadkyrltyayfaggdagdafdgfdfgddpsdkfftshngmqfstwdndndkfe
gncaeqdgsgwwmnkchaghlngvyyqggtyskastpngydngiiwatwktrwysmkktt
mkiipfnrl
>d1fica_ 4.106.1.1.1 beta- and gamma-Fibrinogen C-terminal domains {human (Homo sapiens)}
qihditgkdcqdiankgakqsglyfikplkanqqflvyceidgsgngwtvfqkrldgsvd
fkknwiqykegfghlsptgttefwlgnekihlistqsaipyalrveledwngrtstadya
mfkvgpeadkyrltyayfaggdagdafdgfdfgddpsdkfftshngmqfstwdndndkfe
gncaeqdgsgwwmnkchaghlngvyyqggtyskastpngydngiiwatwktrwysmkktt
mkiipfnrltigegqqhhlg
>d1ficb_ 4.106.1.1.1 beta- and gamma-Fibrinogen C-terminal domains {human (Homo sapiens)}
vqihditgkdcqdiankgakqsglyfikplkanqqflvyceidgsgngwtvfqkrldgsv
dfkknwiqykegfghlsptgttefwlgnekihlistqsaipyalrveledwngrtstady
amfkvgpeadkyrltyayfaggdagdafdgfdfgddpsdkfftshngmqfstwdndndkf
egncaeqdgsgwwmnkchaghlngvyyqggtyskastpngydngiiwatwktrwysmkkt
tmkiipfnrltigegqqhhlg
>d1fid__ 4.106.1.1.1 beta- and gamma-Fibrinogen C-terminal domains {human (Homo sapiens)}
qihditgkdcqdiankgakqsglyfikplkanqqflvyceidgsgngwtvfqkrldgsvd
fkknwiqykegfghlsptgttefwlgnekihlistqsaipyalrveledwngrtstadya
mfkvgpeadkyrltyayfaggdagdafdgfdfgddpsdkfftshngmqfstwdndndkfe
gncaeqdgsgwwmnkchaghlngvyyqggtyskastpngydngiiwatwktrwysmkktt
mkiipfnrltigegqqhhl
>d1fiea1 2.1.1.5.12 (9-190) Transglutaminase factor XIII, N-terminal domain {Human (Homo sapiens) blood}
ggrravppnnsnaaeddlptvelqgvvprgvnlqeflnvtsvhlfkerwdtnkvdhhtdk
yennklivrrgqsfyvqidfsrpydprrdlfrveyvigrypqenkgtyipvpivselqsg
kwgakivmredrsvrlsiqsspkcivgkfrmyvavwtpygvlrtsrnpetdtyilfnpwc
ed
>d1fiea2 2.1.4.1.1 (516-627) Coagulation factor XIII, two C-terminal domains {Human (Homo sapiens) blood}
snvdmdfevenavlgkdfklsitfrnnshnrytitaylsanitfytgvpkaefkketfdv
tleplsfkkeavliqageymgqlleqaslhffvtarinetrdvlakqkstvl
>d1fiea3 2.1.4.1.1 (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 2.1.1.5.12 (10-190) Transglutaminase factor XIII, N-terminal domain {Human (Homo sapiens) blood}
grravppnnsnaaeddlptvelqgvvprgvnlqeflnvtsvhlfkerwdtnkvdhhtdky
ennklivrrgqsfyvqidfsrpydprrdlfrveyvigrypqenkgtyipvpivselqsgk
wgakivmredrsvrlsiqsspkcivgkfrmyvavwtpygvlrtsrnpetdtyilfnpwce
d
>d1fieb2 2.1.4.1.1 (516-627) Coagulation factor XIII, two C-terminal domains {Human (Homo sapiens) blood}
snvdmdfevenavlgkdfklsitfrnnshnrytitaylsanitfytgvpkaefkketfdv
tleplsfkkeavliqageymgqlleqaslhffvtarinetrdvlakqkstvl
>d1fieb3 2.1.4.1.1 (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 2.1.1.1.37 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab 1F7 (mouse), kappa L chain}
dvqlqqsgpelekpgasvkisckasgfslpghninwivqrngkslewignidpyyggtnf
npkfkgkatltvdkssstlymhltslqsedsavyycarrrdgnygftywgqgtlvtvsa
>d1figh2 2.1.1.2.45 (114-223) Immunoglobulin (constant domains of L and H chains) {Fab 1F7 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpsstwpsetvtcnvahpasstkvdkki
>d1figl1 2.1.1.1.37 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab 1F7 (mouse), kappa L chain}
envltqspaimsaspgekvtmacrasssvsstylhwyqqksgaspklliystsnlasgvp
arfsgsgsgtsysltissveaedaatyycqqysgypltfgagtklelkr
>d1figl2 2.1.1.2.45 (109-214) Immunoglobulin (constant domains of L and H chains) {Fab 1F7 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1fik__ 4.63.1.1.2 Profilin (actin-binding protein) {human (Homo sapiens)}
agwnayidnlmadgtcqdaaivgykdspsvwaavpgktfvnitpaevgvlvgkdrssfyv
ngltlggqkcsvirdsllqdgefsmdlrtkstggaptfnvtvtktdktlvllmgkegvhg
glinkkcyemashlrrsqy
>d1fil__ 4.63.1.1.2 Profilin (actin-binding protein) {human (Homo sapiens)}
agwnayidnlmadgtcqdaaivgykdspsvwaavpgktfvnitpaevgvlvgkdrssfyv
ngltlggqkcsvirdsllqdgefsmdlrtkstggaptfnvtvtktdktlvllmgkegvhg
glinkkcyemashlrrsqy
>d1fim__ 4.41.1.3.2 Microphage migration inhibition factor (MIF) {Rat (Rattus norvegicus)}
pafivntnvprasvpegflseltqqlaqatgkpaqyiavhvvpdqlxtfsgtsdpcalcs
lhsigkiggaqnrnyskllcgllsdrlhispdrvyinyydana
>d1fina_ 5.1.1.1.1 Cyclin-dependent PK {Human (Homo sapiens)}
menfqkvekigegtygvvykarnkltgevvalkkirldtetegvpstaireisllkelnh
pnivklldvihtenklylvfeflhqdlkkfmdasaltgiplpliksylfqllqglafchs
hrvlhrdlkpqnllintegaikladfglarafgvpvrtythevvtlwyrapeillgckyy
stavdiwslgcifaemvtrralfpgdseidqlfrifrtlgtpdevvwpgvtsmpdykpsf
pkwarqdfskvvppldedgrsllsqmlhydpnkrisakaalahpffqdvtkpvphlrl
>d1finb1 1.63.1.1.1 (173-309) Cyclin A {Human (Homo sapiens)}
nevpdyhedihtylremevkckpkvgymkkqpditnsmrailvdwlvevgeeyklqnetl
hlavnyidrflssmsvlrgklqlvgtaamllaskfeeiyppevaefvyitddtytkkqvl
rmehlvlkvltfdlaap
>d1finb2 1.63.1.1.1 (310-432) Cyclin A {Human (Homo sapiens)}
tvnqfltqyflhqqpanckveslamflgelslidadpylkylpsviagaafhlalytvtg
qswpeslirktgytleslkpclmdlhqtylkapqhaqqsirekyknskyhgvsllnppet
lnl
>d1finc_ 5.1.1.1.1 Cyclin-dependent PK {Human (Homo sapiens)}
menfqkvekigegtygvvykarnkltgevvalkkirldtetegvpstaireisllkelnh
pnivklldvihtenklylvfeflhqdlkkfmdasaltgiplpliksylfqllqglafchs
hrvlhrdlkpqnllintegaikladfglarafgvpvrtythevvtlwyrapeillgckyy
stavdiwslgcifaemvtrralfpgdseidqlfrifrtlgtpdevvwpgvtsmpdykpsf
pkwarqdfskvvppldedgrsllsqmlhydpnkrisakaalahpffqdvtkpvphlrl
>d1find1 1.63.1.1.1 (173-309) Cyclin A {Human (Homo sapiens)}
nevpdyhedihtylremevkckpkvgymkkqpditnsmrailvdwlvevgeeyklqnetl
hlavnyidrflssmsvlrgklqlvgtaamllaskfeeiyppevaefvyitddtytkkqvl
rmehlvlkvltfdlaap
>d1find2 1.63.1.1.1 (310-432) Cyclin A {Human (Homo sapiens)}
tvnqfltqyflhqqpanckveslamflgelslidadpylkylpsviagaafhlalytvtg
qswpeslirktgytleslkpclmdlhqtylkapqhaqqsirekyknskyhgvsllnppet
lnl
>d1fipa_ 1.84.1.1.1 FIS protein {(Escherichia coli)}
plrdsvkqalknyfaqlngqdvndlyelvlaeveqalldmvmqytrgnqtraalmmginr
gtlrkklkkygmn
>d1fipb_ 1.84.1.1.1 FIS protein {(Escherichia coli)}
plrdsvkqalknyfaqlngqdvndlyelvlaeveqalldmvmqytrgnqtraalmmginr
gtlrkklkkygmn
>d1fit__ 4.9.1.1.2 FHIT (fragile histidine triad protein) {Human (Homo sapiens)}
sfrfgqhlikpsvvflktelsfalvnrkpvvpghvlvcplrpverfhdlrpdevadlfqt
tqrvgtvvekhfhgtsltfsxqdgpeagqtvkhvhvhvlprkagdfhrndsiyeelqkhd
kedfpaswrseeexaaeaaalrvyfq
>d1fiva_ 2.38.1.1.2 Feline immunodeficiency virus (FIV) protease {Feline (Felis catus) immunodeficiency virus}
vgttttlekrpeilifvngypikflldtgaditilnrrdfqvknsiengrqnmigvgggk
rgtnyinvhleirdenyktqcifgnvcvlednsliqpllgrdnmikfnirlvm
>d1fjla_ 1.4.1.1.13 Paired protein {fruit fly (Drosophila melanogaster)}
kqrrsrttfsasqldelerafertqypdiytreelaqrtnlteariqvwfqnrrarlrkq
htsvs
>d1fjlb_ 1.4.1.1.13 Paired protein {fruit fly (Drosophila melanogaster)}
qrrsrttfsasqldelerafertqypdiytreelaqrtnlteariqvwfqnrrarlrk
>d1fjlc_ 1.4.1.1.13 Paired protein {fruit fly (Drosophila melanogaster)}
kqrrsrttfsasqldelerafertqypdiytreelaqrtnlteariqvwfqnrrarlrk
>d1fjma_ 4.99.1.2.1 Protein phosphatase-1 (PP-1) {Rabbit (Oryctolagus cuniculus)}
lnldsiigrllevqgsrpgknvqlteneirglclksreiflsqpilleleaplkicgdih
gqyydllrlfeyggfppesnylflgdyvdrgkqsleticlllaykikypenffllrgnhe
casinriygfydeckrryniklwktftdcfnclpiaaivdekifcchgglspdlqsmeqi
rrimrptdvpdqgllcdllwsdpdkdvqgwgendrgvsftfgaevvakflhkhdldlicr
ahqvvedgyeffakrqlvtlfsapnycgefdnagammsvdetlmcsfqilkpad
>d1fjmb_ 4.99.1.2.1 Protein phosphatase-1 (PP-1) {Rabbit (Oryctolagus cuniculus)}
lnldsiigrllevqgsrpgknvqlteneirglclksreiflsqpilleleaplkicgdih
gqyydllrlfeyggfppesnylflgdyvdrgkqsleticlllaykikypenffllrgnhe
casinriygfydeckrryniklwktftdcfnclpiaaivdekifcchgglspdlqsmeqi
rrimrptdvpdqgllcdllwsdpdkdvqgwgendrgvsftfgaevvakflhkhdldlicr
ahqvvedgyeffakrqlvtlfsapnycgefdnagammsvdetlmcsfqilkpa
>d1fkb__ 4.19.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1fkd__ 4.19.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1fkf__ 4.19.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1fkg__ 4.19.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1fkh__ 4.19.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1fkia_ 4.19.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1fkib_ 4.19.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1fkj__ 4.19.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1fkk__ 4.19.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfvlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiippnatlifdvellkle
>d1fkl__ 4.19.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfvlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiippnatlifdvellkle
>d1fkr__ 4.19.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1fks__ 4.19.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1fkt__ 4.19.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1fkw__ 3.1.2.1.1 Adenosine deaminase {mouse (Mus musculus)}
tpafnkpkvelhvhldgaikpetilyfgkkrgialpadtveelrniigmdkplslpgfla
kfdyympviagcreaikriayefvemkakegvvyvevrysphllanskvdpmpwnqtegd
vtpddvvdlvnqglqegeqafgikvrsilccmrhqpswslevlelckkynqktvvamdla
gdetiegsslfpghveayegavkngihrtvhagevgspevvreavdilktervghgyhti
edealynrllkenmhfevcpwssyltgawdpktthavvrfkndkanyslntedplifkst
ldtdyqmtkkdmgfteeefkrlninaakssflpeeekkellerlyreyq
>d1fkx__ 3.1.2.1.1 Adenosine deaminase {mouse (Mus musculus)}
tpafnkpkvelhvhldgaikpetilyfgkkrgialpadtveelrniigmdkplslpgfla
kfdyympviagcreaikriayefvemkakegvvyvevrysphllanskvdpmpwnqtegd
vtpddvvdlvnqglqegeqafgikvrsilccmrhqpswslevlelckkynqktvvamdla
gdetiegsslfpghveayegavkngihrtvhagevgspevvreavdilktervghgyhti
edealynrllkenmhfevcpwssyltgawdpktthavvrfkndkanyslntdaplifkst
ldtdyqmtkkdmgfteeefkrlninaakssflpeeekkellerlyreyq
>d1fla__ 3.14.4.1.7 Flavodoxin {(Clostridium beijerinckii)}
mkivywsgtgntekmaeliakgiiesgkdvntinvsdvnidellnedililgcsamddev
leesefepfieeistkisgkkvalfgsygwgdgkwmrdfeermngygcvvvetplivqne
pdeaeqdciefgkkiani
>d1fld__ 3.14.4.1.7 Flavodoxin {(Clostridium beijerinckii)}
mkivywsgtgntekmaeliakgiiesgkdvntinvsdvnidellnedililgcsamtdev
leesefepfieeistkisgkkvalfgsygwgdgkwmrdfeermngygcvvvetplivqne
pdeaeqdciefgkkiani
>d1flee_ 2.35.1.2.14 Elastase {porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1flei_ 7.3.12.1.1 Elafin, elastase-specific inhibitor {human (Homo sapiens)}
tkpgscpiilircamlnppnrclkdtdcpgikkccegscgmacfvpq
>d1flia_ 1.4.3.12.1 Fli-1 {Human (Homo sapiens)}
pgsgqiqlwqfllellsdsanascitwegtngefkmtdpdevarrwgerkskpnmnydkl
sralryyydknimtkvhgkryaykfdfhgiaqalqphp
>d1fln__ 3.14.4.1.7 Flavodoxin {(Clostridium beijerinckii)}
mkivywsgtgntekmaeliakgiiesgkdvntinvsdvnidellnedililgcsamgpev
leesefepfieeistkisgkkvalfgsygwgdgkwmrdfeermngygcvvvetplivqne
pdeaeqdciefgkkiani
>d1flp__ 1.1.1.1.2 Hemoglobin I {clam (Lucina pectinata)}
sleaaqksnvtsswakasaawgtagpeffmalfdahddvfakfsglfsgaakgtvkntpe
maaqaqsfkglvsnwvdnldnagalegqcktfaanhkargisagqleaafkvlsgfmksy
ggdegawtavagalmgeiepdm
>d1flrh1 2.1.1.1.33 (1-118) Immunoglobulin (variable domains of L and H chains) {Fab 4-4-20 (mouse), kappa L chain}
evkldetggglvqpgrpmklscvasgftfsdywmnwvrqspekglewvaqirnkpynyet
yysdsvkgrftisrddskssvylqmnnlrvedmgiyyctgsyygmdywgqgtsvtvss
>d1flrh2 2.1.1.2.41 (119-218) Immunoglobulin (constant domains of L and H chains) {Fab 4-4-20 (mouse), kappa L chain}
akttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsd
lytlsssvtvtsstwpsqsitcnvahpasstkvdkkiepr
>d1flrl1 2.1.1.1.33 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab 4-4-20 (mouse), kappa L chain}
dvvmtqtplslpvslgdqasiscrssqslvhsngntylrwylqkpgqspkvliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyfcsqsthvpwtfgggtkleik
>d1flrl2 2.1.1.2.41 (113-219) Immunoglobulin (constant domains of L and H chains) {Fab 4-4-20 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1flv__ 3.14.4.1.3 Flavodoxin {(Anabaena 7120)}
kkiglfygtqtgktesvaeiirdefgndvvtlhdvsqaevtdlndyqyliigcptwnige
lqsdweglyselddvdfngklvayfgtgdqigyadnfqdaigileekisqrggktvgyws
tdgydfndskalrngkfvglaldednqsdltddrikswvaqlksefgl
>d1fmb__ 2.38.1.1.7 EIAV protease {(Equine infection anemia virus), EIAV}
vtynlekrpttivlindtplnvlldtgadtsvlttahynrlkyrgrkyqgtgiggvggnv
etfstpvtikkkgrhiktrmlvadipvtilgrdilqdlgaklvl
>d1fmca_ 3.22.1.2.4 7-alpha-hydroxysteroid dehydrogenase {(Escherichia coli)}
mfnsdnlrldgkcaiitgagagigkeiaitfatagasvvvsdinadaanhvvdeiqqlgg
qafacrcditseqelsaladfaisklgkvdilvnnaggggpkpfdmpmadfrrayelnvf
sffhlsqlvapemekngggviltitsmaaenkninmtsyasskaaashlvrnmafdlgek
nirvngiapgailtdalksvitpeieqkmlqhtpirrlgqpqdianaalflcspaaswvs
gqiltvsgggvqeln
>d1fmcb_ 3.22.1.2.4 7-alpha-hydroxysteroid dehydrogenase {(Escherichia coli)}
mfnsdnlrldgkcaiitgagagigkeiaitfatagasvvvsdinadaanhvvdeiqqlgg
qafacrcditseqelsaladfaisklgkvdilvnnaggggpkpfdmpmadfrrayelnvf
sffhlsqlvapemekngggviltitsmaaenkninmtsyasskaaashlvrnmafdlgek
nirvngiapgailtdalksvitpeieqkmlqhtpirrlgqpqdianaalflcspaaswvs
gqiltvsgggvqeln
>d1fmd1_ 2.8.1.4.2 Foot-and-mouth desease virus {foot-and-mouth disease virus (Strain bfs, 1860)}
ttttgesadpvtttvenyggetqvqrrhhtdvafvldrfvkvtvsdnqhtldvmqahkdn
ivgallraatyyfsdleiavthtgkltwvpngapvsalnnttnptayhkgpvtrlalpyt
aphrvlataytgtttytasargdlahlttthaahlptsfnfgavkaetitellvrmkrae
lycprpilpiqptgdrhkqplvapakq
>d1fmd2_ 2.8.1.4.2 Foot-and-mouth desease virus {foot-and-mouth disease virus (Strain bfs, 1860)}
dkkteettlledrilttrnghttsttqssvgvtfgyataedstsgpntsaletrvhqaer
ffkmalfdwvpsqnfghmhkvvlphepkgvygglvksyaymrngwdvevtavgnqfnggc
llvalvpemgdisdrekyqltlyphqfinprtnmtahitvpyvgvnrydqykqhrpwtlv
vmvvaplttntagaqqikvyaniaptnvhvagelpske
>d1fmd3_ 2.8.1.4.2 Foot-and-mouth desease virus {foot-and-mouth disease virus (Strain bfs, 1860)}
gifpvacsdgygnmvttdpktadpaygkvynpprtalpgrftnyldvaeacptflmfenv
pyvstrtdgqrllakfdvslaakhmsntylaglaqyytqytgtinlhfmftgptdakary
mvayvppgmdapdnpeeaahcihaewdtglnskftfsipyisaadytytasheaettcvq
gwvcvyqithgkadadalvvsasagkdfelrlpvdarqq
>d1fmk_1 2.24.2.1.11 (82-145) c-src tyrosine kinase {human (Homo sapiens)}
mvttfvalydyesrtetdlsfkkgerlqivnntegdwwlahslstgqtgyipsnyvapsd
siqa
>d1fmk_2 4.53.1.1.3 (146-248) c-src tyrosine kinase {human (Homo sapiens)}
eewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkhykir
kldsggfyitsrtqfnslqqlvayyskhadglchrlttvcpts
>d1fmk_3 5.1.1.2.3 (249-533) c-src tyrosine kinase {human (Homo sapiens)}
kpqtqglakdaweipreslrlevklgqgcfgevwmgtwngttrvaiktlkpgtmspeafl
qeaqvmkklrheklvqlyavvseepiyivteymskgslldflkgetgkylrlpqlvdmaa
qiasgmayvermnyvhrdlraanilvgenlvckvadfglarliedneytarqgakfpikw
tapeaalygrftiksdvwsfgilltelttkgrvpypgmvnrevldqvergyrmpcppecp
eslhdlmcqcwrkepeerptfeylqafledyftstepqxqpgenl
>d1fmoe_ 5.1.1.1.4 cAMP-dependent PK, catalytic subunit {mouse (Mus musculus)}
esvkeflakakedflkkwetpsqntaqldqfdriktlgtgsfgrvmlvkhkesgnhyamk
ildkqkvvklkqiehtlnekrilqavnfpflvklefsfkdnsnlymvmeyvaggemfshl
rrigrfsepharfyaaqivltfeylhsldliyrdlkpenllidqqgyiqvtdfgfakrvk
grtwxlcgtpeylapeiilskgynkavdwwalgvliyemaagyppffadqpiqiyekivs
gkvrfpshfssdlkdllrnllqvdltkrfgnlkngvndiknhkwfattdwiaiyqrkvea
pfipkfkgpgdtsnfddyeeeeirvxinekcgkeftef
>d1fmp__ 4.102.1.1.6 Ricin A-chain {castor bean (Ricinus communis)}
ifpkqypiinfttagatvqsytnfiravrgrlttgadvrheipvlpnrvglpinqrfilv
elsnhaelsvtlaldvtnayvvgyragnsayffhpdnqedaeaithlftdvqnrytfafg
gnydrleqlagnlrenielgngpleeaisalyyystggtqlptlarsfiiciqmiseaar
fqyiegemrtrirynrrsapdpsvitlenswgrlstaiqesnqgafaspiqlqrrngskf
svydvsilipiialmvyrcapppssqf
>d1fmta1 2.34.1.1.1 (207-314) Methionyl-tRNAfmet formyltransferase, the C-terminal domain {(Escherichia coli)}
lskeearidwslsaaqlercirafnpwpmswleiegqpvkvwkasvidtatnaapgtile
ankqgiqvatgdgilnllslqpagkkamsaqdllnsrrewfvpgnrlv
>d1fmta2 3.52.1.1.2 (1-206) Methionyl-tRNAfmet formyltransferase {(Escherichia coli)}
seslriifagtpdfaarhldallssghnvvgvftqpdrpagrgkklmpspvkvlaeekgl
pvfqpvslrpqenqqlvaelqadvmvvvayglilpkavlemprlgcinvhgsllprwrga
apiqrslwagdaetgvtimqmdvgldtgdmlyklscpitaedtsgtlydklaelgpqgli
ttlkqladgtakpevqdetlvtyaek
>d1fmtb1 2.34.1.1.1 (207-314) Methionyl-tRNAfmet formyltransferase, the C-terminal domain {(Escherichia coli)}
lskeearidwslsaaqlercirafnpwpmswleiegqpvkvwkasvidtatnaapgtile
ankqgiqvatgdgilnllslqpagkkamsaqdllnsrrewfvpgnrlv
>d1fmtb2 3.52.1.1.2 (2-206) Methionyl-tRNAfmet formyltransferase {(Escherichia coli)}
eslriifagtpdfaarhldallssghnvvgvftqpdrpagrgkklmpspvkvlaeekglp
vfqpvslrpqenqqlvaelqadvmvvvayglilpkavlemprlgcinvhgsllprwrgaa
piqrslwagdaetgvtimqmdvgldtgdmlyklscpitaedtsgtlydklaelgpqglit
tlkqladgtakpevqdetlvtyaek
>d1fna__ 2.1.2.1.3 Fibronectin, different Fn3 modules {human (Homo sapiens)}
gskstatisglkpgvdytitvyavtgrgdspasskpisinyrtei
>d1fnb_1 2.32.1.1.1 (19-154) Ferredoxin reductase (flavodoxin reductase) {spinach (Spinacia oleracea)}
hskkmeegitvnkfkpktpyvgrcllntkitgddapgetwhmvfshegeipyregqsvgv
ipdgedkngkphklrlysiassalgdfgdaksvslcvkrliytndagetikgvcsnflcd
lkpgaevkltgpvgke
>d1fnb_2 3.16.1.1.1 (155-314) Ferredoxin reductase (flavodoxin reductase) {spinach (Spinacia oleracea)}
mlmpkdpnatiimlgtgtgiapfrsflwkmffekhddykfnglawlflgvptsssllyke
efekmkekapdnfrldfavsreqtnekgekmyiqtrmaqyavelwemlkkdntyvymcgl
kgmekgiddimvslaaaegidwieykrqlkkaeqwnvevy
>d1fnc_1 2.32.1.1.1 (19-154) Ferredoxin reductase (flavodoxin reductase) {spinach (Spinacia oleracea)}
hskkmeegitvnkfkpktpyvgrcllntkitgddapgetwhmvfshegeipyregqsvgv
ipdgedkngkphklrlysiassalgdfgdaksvslcvkrliytndagetikgvcsnflcd
lkpgaevkltgpvgke
>d1fnc_2 3.16.1.1.1 (155-314) Ferredoxin reductase (flavodoxin reductase) {spinach (Spinacia oleracea)}
mlmpkdpnatiimlgtgtgiapfrsflwkmffekhddykfnglawlflgvptsssllyke
efekmkekapdnfrldfavsreqtnekgekmyiqtrmaqyavelwemlkkdntyvymcgl
kgmekgiddimvslaaaegidwieykrqlkkaeqwnvevy
>d1fnd_1 2.32.1.1.1 (19-154) Ferredoxin reductase (flavodoxin reductase) {spinach (Spinacia oleracea)}
hskkmeegitvnkfkpktpyvgrcllntkitgddapgetwhmvfshegeipyregqsvgv
ipdgedkngkphklrlysiassalgdfgdaksvslcvkrliytndagetikgvcsnflcd
lkpgaevkltgpvgke
>d1fnd_2 3.16.1.1.1 (155-314) Ferredoxin reductase (flavodoxin reductase) {spinach (Spinacia oleracea)}
mlmpkdpnatiimlgtgtgiapfrsflwkmffekhddykfnglawlflgvptsssllyke
efekmkekapdnfrldfavsreqtnekgekmyiqtrmaqyavelwemlkkdntyvymcgl
kgmekgiddimvslaaaegidwieykrqlkkaeqwnvevy
>d1fnf_1 2.1.2.1.3 (1142-1235) Fibronectin, different Fn3 modules {human (Homo sapiens)}
plspptnlhleanpdtgvltvswersttpditgyritttptngqqgnsleevvhadqssc
tfdnlspgleynvsvytvkddkesvpisdtiipa
>d1fnf_2 2.1.2.1.3 (1236-1326) Fibronectin, different Fn3 modules {human (Homo sapiens)}
vppptdlrftnigpdtmrvtwapppsidltnflvryspvkneedvaelsispsdnavvlt
nllpgteyvvsvssvyeqhestplrgrqktg
>d1fnf_3 2.1.2.1.3 (1327-1415) Fibronectin, different Fn3 modules {human (Homo sapiens)}
ldsptgidfsditansftvhwiapratitgyrirhhpehfsgrpredrvphsrnsitltn
ltpgteyvvsivalngreesplligqqst
>d1fnf_4 2.1.2.1.3 (1416-1509) Fibronectin, different Fn3 modules {human (Homo sapiens)}
vsdvprdlevvaatptslliswdapavtvryyritygetggnspvqeftvpgskstatis
glkpgvdytitvyavtgrgdspasskpisinyrt
>d1fod1_ 2.8.1.4.2 Foot-and-mouth desease virus {foot-and-mouth disease virus (Strain bfs, 1860)}
ttsagesadpvtttvenyggetqiqrrqhtdvsfimdrfvkvtpqnqinildlmqvpsht
lvggllrastyyfsdleiavkhegdltwvpngapekaldnttnptayhkapltrlalpyt
aphrvlatvyngecrysrnavpnlrgdlqvlaqkvartlptsfnygaikatrvtellyrm
kraetycprpllaihptearhkqkivapvk
>d1fod2_ 2.8.1.4.2 Foot-and-mouth desease virus {foot-and-mouth disease virus (Strain bfs, 1860)}
eettlledrilttrnghttsttqssvgvtygyataedfvsgpntsgletrvvqaerffkt
hlfdwvtsdsfgrchllelptdhkgvygsltdsyaymrngwdvevtavgnqfnggcllva
mvpelcsiqkrelyqltlfphqfinprtnmtahitvpfvgvnrydqykvhkpwtlvvmvv
apltvntegapqikvyaniaptnvhvagefpske
>d1fod3_ 2.8.1.4.2 Foot-and-mouth desease virus {foot-and-mouth disease virus (Strain bfs, 1860)}
gifpvacsdgygglvttdpktadpvygkvfnpprnqlpgrftnlldvaeacptflrfegg
vpyvttktdsdrvlaqfdmslaakhmsntflaglaqyytqysgtinlhfmftgptdakar
ymvayappgmeppktpeaaahcihaewdtglnskftfsipylsaadytytasdvaettnv
qgwvclfqithgkadgdalvvlasagkdfelrlpvdarae
>d1foha1 3.4.1.2.4 (1-240) Phenol hydroxylase {Soil-living yeast (Trichosporon cutaneum)}
tkysesycdvlivgagpaglmaarvlseyvrqkpdlkvriidkrstkvyngqadglqcrt
leslknlgladkilseandmstialynpdenghirrtdripdtlpgisryhqvvlhqgri
erhildsiaeisdtrikverplipekmeidsskaedpeaypvtmtlrymsdhestplqfg
hktenslfhsnlqtqeeedanyrlpegkeageietvhckyvigcdgghswvrrtlgfemi
>d1foha2 3.4.1.2.4 (342-461) Phenol hydroxylase {Soil-living yeast (Trichosporon cutaneum)}
vtekfskdervfiagdachthspkagqgmntsmmdtynlgwklglvltgrakrdilktye
eerhafaqalidfdhqfsrlfsgrpakdvademgvsmdvfkeafvkgnefasgtainyde
>d1foha3 3.38.1.8.1 (463-662) Phenol hydroxylase, C-terminal domain {Soil-living yeast (Trichosporon cutaneum)}
lvtdkksskqelakncvvgtrfksqpvvrhseglwmhfgdrlvtdgrfriivfagkatda
tqmsrikkfsayldsensvislytpkvsdrnsridvitihschrddiemhdfpapalhpk
wqydfiyadcdswhhphpksyqawgvdetkgavvvvrpdgytslvtdlegtaeidryfsg
ilvepkeksgaqteadwtks
>d1foha4 4.12.1.2.3 (241-341) Phenol hydroxylase {Soil-living yeast (Trichosporon cutaneum)}
geqtdyiwgvldavpasnfpdirsrcaihsaesgsimiiprennlvrfyvqlqaraekgg
rvdrtkftpevvianakkifhpytfdvqqldwftayhigqr
>d1fohb1 3.4.1.2.4 (1-240) Phenol hydroxylase {Soil-living yeast (Trichosporon cutaneum)}
tkysesycdvlivgagpaglmaarvlseyvrqkpdlkvriidkrstkvyngqadglqcrt
leslknlgladkilseandmstialynpdenghirrtdripdtlpgisryhqvvlhqgri
erhildsiaeisdtrikverplipekmeidsskaedpeaypvtmtlrymsdhestplqfg
hktenslfhsnlqtqeeedanyrlpegkeageietvhckyvigcdgghswvrrtlgfemi
>d1fohb2 3.4.1.2.4 (342-461) Phenol hydroxylase {Soil-living yeast (Trichosporon cutaneum)}
vtekfskdervfiagdachthspkagqgmntsmmdtynlgwklglvltgrakrdilktye
eerhafaqalidfdhqfsrlfsgrpakdvademgvsmdvfkeafvkgnefasgtainyde
>d1fohb3 3.38.1.8.1 (463-662) Phenol hydroxylase, C-terminal domain {Soil-living yeast (Trichosporon cutaneum)}
lvtdkksskqelakncvvgtrfksqpvvrhseglwmhfgdrlvtdgrfriivfagkatda
tqmsrikkfsayldsensvislytpkvsdrnsridvitihschrddiemhdfpapalhpk
wqydfiyadcdswhhphpksyqawgvdetkgavvvvrpdgytslvtdlegtaeidryfsg
ilvepkeksgaqteadwtks
>d1fohb4 4.12.1.2.3 (241-341) Phenol hydroxylase {Soil-living yeast (Trichosporon cutaneum)}
geqtdyiwgvldavpasnfpdirsrcaihsaesgsimiiprennlvrfyvqlqaraekgg
rvdrtkftpevvianakkifhpytfdvqqldwftayhigqr
>d1fohc1 3.4.1.2.4 (1-240) Phenol hydroxylase {Soil-living yeast (Trichosporon cutaneum)}
tkysesycdvlivgagpaglmaarvlseyvrqkpdlkvriidkrstkvyngqadglqcrt
leslknlgladkilseandmstialynpdenghirrtdripdtlpgisryhqvvlhqgri
erhildsiaeisdtrikverplipekmeidsskaedpeaypvtmtlrymsdhestplqfg
hktenslfhsnlqtqeeedanyrlpegkeageietvhckyvigcdgghswvrrtlgfemi
>d1fohc2 3.4.1.2.4 (342-461) Phenol hydroxylase {Soil-living yeast (Trichosporon cutaneum)}
vtekfskdervfiagdachthspkagqgmntsmmdtynlgwklglvltgrakrdilktye
eerhafaqalidfdhqfsrlfsgrpakdvademgvsmdvfkeafvkgnefasgtainyde
>d1fohc3 3.38.1.8.1 (463-662) Phenol hydroxylase, C-terminal domain {Soil-living yeast (Trichosporon cutaneum)}
lvtdkksskqelakncvvgtrfksqpvvrhseglwmhfgdrlvtdgrfriivfagkatda
tqmsrikkfsayldsensvislytpkvsdrnsridvitihschrddiemhdfpapalhpk
wqydfiyadcdswhhphpksyqawgvdetkgavvvvrpdgytslvtdlegtaeidryfsg
ilvepkeksgaqteadwtks
>d1fohc4 4.12.1.2.3 (241-341) Phenol hydroxylase {Soil-living yeast (Trichosporon cutaneum)}
geqtdyiwgvldavpasnfpdirsrcaihsaesgsimiiprennlvrfyvqlqaraekgg
rvdrtkftpevvianakkifhpytfdvqqldwftayhigqr
>d1fohd1 3.4.1.2.4 (1-240) Phenol hydroxylase {Soil-living yeast (Trichosporon cutaneum)}
tkysesycdvlivgagpaglmaarvlseyvrqkpdlkvriidkrstkvyngqadglqcrt
leslknlgladkilseandmstialynpdenghirrtdripdtlpgisryhqvvlhqgri
erhildsiaeisdtrikverplipekmeidsskaedpeaypvtmtlrymsdhestplqfg
hktenslfhsnlqtqeeedanyrlpegkeageietvhckyvigcdgghswvrrtlgfemi
>d1fohd2 3.4.1.2.4 (342-461) Phenol hydroxylase {Soil-living yeast (Trichosporon cutaneum)}
vtekfskdervfiagdachthspkagqgmntsmmdtynlgwklglvltgrakrdilktye
eerhafaqalidfdhqfsrlfsgrpakdvademgvsmdvfkeafvkgnefasgtainyde
>d1fohd3 3.38.1.8.1 (463-662) Phenol hydroxylase, C-terminal domain {Soil-living yeast (Trichosporon cutaneum)}
lvtdkksskqelakncvvgtrfksqpvvrhseglwmhfgdrlvtdgrfriivfagkatda
tqmsrikkfsayldsensvislytpkvsdrnsridvitihschrddiemhdfpapalhpk
wqydfiyadcdswhhphpksyqawgvdetkgavvvvrpdgytslvtdlegtaeidryfsg
ilvepkeksgaqteadwtks
>d1fohd4 4.12.1.2.3 (241-341) Phenol hydroxylase {Soil-living yeast (Trichosporon cutaneum)}
geqtdyiwgvldavpasnfpdirsrcaihsaesgsimiiprennlvrfyvqlqaraekgg
rvdrtkftpevvianakkifhpytfdvqqldwftayhigqr
>d1foka1 1.4.3.8.1 (4-143) Restriction endonuclease FokI, the N-terminal (recognition) domain {(Flavobacterium okeanokoites)}
kirtfgwvqnpgkfenlkrvvqvfdrnskvhnevknikiptlvkeskiqkelvaimnqhd
liytykelvgtgtsirseapcdaiiqatiadqgnkkgyidnwssdgflrwahalgfieyi
nksdsfvitdvglaysksad
>d1foka2 1.4.3.8.1 (144-281) Restriction endonuclease FokI, the N-terminal (recognition) domain {(Flavobacterium okeanokoites)}
gsaiekeilieaissyppairiltlledgqhltkfdlgknlgfsgesgftslpegilldt
lanampkdkgeirnnwegssdkyarmiggwldklglvkqgkkefiiptpdnkefishafk
itgeglkvlrrakgs
>d1foka3 1.4.3.8.1 (287-386) Restriction endonuclease FokI, the N-terminal (recognition) domain {(Flavobacterium okeanokoites)}
vpkrvywemlatnltdkeyvrtrralileilikagslkieqiqdnlkklgfdevietien
dikglintgifieikgrfyqlkdhilqfvipnrgvtkqlv
>d1foka4 3.43.1.6.1 (387-579) Restriction endonuclease FokI, the C-terminal (catalytic) domain {(Flavobacterium okeanokoites)}
kseleekkselrhklkyvpheyielieiarnstqdrilemkvmeffmkvygyrgkhlggs
rkpdgaiytvgspidygvivdtkaysggynlpigqademqryveenqtrnkhinpnewwk
vypssvtefkflfvsghfkgnykaqltrlnhitncngavlsveelliggemikagtltle
evrrkfnngeinf
>d1fona_ 2.35.1.2.12 Procarboxypeptidase A-S6 subunit III (zymogen E) {bovine (Bos taurus)}
swswqvslqyekdgafhhtcggsliapdwvvtaghcistsrtyqvvlgeydrsvlegseq
vipinagdlfvhplwnsncvacgndialvklsrsaqlgdkvqlanlppagdilpneapcy
isgwgrlytggplpdklqqallptvdyehcsqwdwwgitvkktmvcaggdtrsgcngdsg
gplncpaadgswqvhgvtsfvsafgcntikkptvftrvsafidwidetiasn
>d1fonb_ 2.35.1.2.12 Procarboxypeptidase A-S6 subunit III (zymogen E) {bovine (Bos taurus)}
swswqvslqyekdgafhhtcggsliapdwvvtaghcistsrtyqvvlgeydrsvlegseq
vipinagdlfvhplwnsncvacgndialvklsrsaqlgdkvqlanlppagdilpneapcy
isgwgrlytggplpdklqqallptvdyehcsqwdwwgitvkktmvcaggdtrsgcngdsg
gplncpaadgswqvhgvtsfvsafgcntikkptvftrvsafidwidetiasn
>d1forh1 2.1.1.1.45 (1-120) Immunoglobulin (variable domains of L and H chains) {Fab 17-Ia (mouse), kappa L chain}
qgqlqqsgaelvrpgssvkisckasgyafssfwvnwvkqrpgqglewigqiypgdgdnky
ngkfkgkatltadkssttaymqlysltsedsavyfcarsgnypyamdywgqgtsvtvssa
>d1forh2 2.1.1.2.52 (121-219) Immunoglobulin (constant domains of L and H chains) {Fab 17-Ia (mouse), kappa L chain}
kttapsvyplapvcggttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsgl
ytlsssvtvtsstwpsqtitcnvahpasstkvdkkiepr
>d1forl1 2.1.1.1.45 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab 17-Ia (mouse), kappa L chain}
qivltqspaimsafpgekvtitcsatssvnymhwfqqkpgtspklwiysssnlasgvpar
fsgsgsgtsysltisrmeaedaatyycqqrssypitfgsgtkleikr
>d1forl2 2.1.1.2.52 (108-210) Immunoglobulin (constant domains of L and H chains) {Fab 17-Ia (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1fose_ 1.105.2.1.5 C-fos {Human (Homo sapiens)}
krrirrernkmaaaksrnrrreltdtlqaetdqledeksalqteianllkekeklefila
>d1fosf_ 1.105.2.1.6 C-jun {Human (Homo sapiens)}
rkrmrnriaasksrkrkleriarleekvktlkaqnselastanmlreqvaqlkqkvm
>d1fosg_ 1.105.2.1.5 C-fos {Human (Homo sapiens)}
rrirrernkmaaaksrnrrreltdtlqaetdqledeksalqteianllkekeklefila
>d1fosh_ 1.105.2.1.6 C-jun {Human (Homo sapiens)}
erkrmrnriaasksrkrkleriarleekvktlkaqnselastanmlreqvaqlkqkvm
>d1fow__ 1.4.4.1.1 Ribosomal protein L11, the C-terminal domain {(Bacillus stearothermophilus)}
mtfitktppaavllkkaagiesgsgepnrnkvatikrdkvreiaelkmpdlnaasieaam
rmiegtarsmgivved
>d1fox__ 1.4.4.1.1 Ribosomal protein L11, the C-terminal domain {(Bacillus stearothermophilus)}
mtfitktppaavllkkaagiesgsgepnrnkvatikrdkvreiaelkmpdlnaasieaam
rmiegtarsmgivved
>d1foy__ 1.4.4.1.1 Ribosomal protein L11, the C-terminal domain {(Bacillus stearothermophilus)}
mtfitktppaavllkkaagiesgsgepnrnkvatikrdkvreiaelkmpdlnaasieaam
rmiegtarsmgivved
>d1fpba_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
fdtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnv
tgdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssn
idclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfm
ldpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryv
gsmvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldi
vptdihqrapiilgspedvtelleiyqkha
>d1fpbb_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
fdtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnv
tgdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssn
idclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfm
ldpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryv
gsmvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldi
vptdihqrapiilgspedvtelleiyqkha
>e1fpc.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidq
>e1fpc.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
dcglrplfekksledkterellesyi
>d1fpda_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
nivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnvtgd
qvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssnidc
lvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfmldp
aigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvgsm
vadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldivpt
dihqrapiilgspedvtelleiyqkha
>d1fpdb_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
nivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnvtgd
qvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssnidc
lvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfmldp
aigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvgsm
vadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldivpt
dihqrapiilgspedvtelleiyqkha
>d1fpea_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
nivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnvtgd
qvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssnidc
lvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfmldp
aigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvgsm
vadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldivpt
dihqrapiilgspedvtelleiyqkha
>d1fpeb_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
nivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnvtgd
qvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssnidc
lvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfmldp
aigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvgsm
vadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldivpt
dihqrapiilgspedvtelleiyqkha
>d1fpfa_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
nivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnvtgd
qvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssnidc
lvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfmldp
aigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvgsm
vadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldivpt
dihqrapiilgspedvtelleiyqkha
>d1fpfb_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
nivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnvtgd
qvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssnidc
lvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfmldp
aigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvgsm
vadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldivpt
dihqrapiilgspedvtelleiyqkha
>d1fpga_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
nivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnvtgd
qvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssnidc
lvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfmldp
aigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvgsm
vadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldivpt
dihqrapiilgspedvtelleiyqkha
>d1fpgb_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
nivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnvtgd
qvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssnidc
lvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfmldp
aigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvgsm
vadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldivpt
dihqrapiilgspedvtelleiyqkha
>e1fph.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>e1fph.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>d1fpia_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
nivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnvtgd
qvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssnidc
lvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfmldp
aigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvgsm
vadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldivpt
dihqrapiilgspedvtelleiyqkha
>d1fpib_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
nivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnvtgd
qvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssnidc
lvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfmldp
aigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvgsm
vadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldivpt
dihqrapiilgspedvtelleiyqkha
>d1fpja_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
nivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnvtgd
qvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssnidc
lvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfmldp
aigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvgsm
vadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldivpt
dihqrapiilgspedvtelleiyqkha
>d1fpjb_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
nivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnvtgd
qvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssnidc
lvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfmldp
aigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvgsm
vadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldivpt
dihqrapiilgspedvtelleiyqkha
>d1fpka_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
dtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnvt
gdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssni
dclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfml
dpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvg
smvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldiv
ptdihqrapiilgspedvtelleiyqkha
>d1fpkb_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
dtnivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnvt
gdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssni
dclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfml
dpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvg
smvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldiv
ptdihqrapiilgspedvtelleiyqkha
>d1fpla_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
nivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnvtgd
qvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssnidc
lvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfmldp
aigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvgsm
vadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldivpt
dihqrapiilgspedvtelleiyqkha
>d1fplb_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
nivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagstnvtgd
qvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssnidc
lvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfmldp
aigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvgsm
vadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldivpt
dihqrapiilgspedvtelleiyqkha
>d1fps__ 1.99.1.1.1 Farnesyl diphosphate synthase {Chicken (Gallus gallus)}
spvvverereefvgffpqivrdltedgighpevgdavarlkevlqynapggkcnrgltvv
aayrelsgpgqkdaeslrcalavgwcielfqafflvaddimdqsltrrgqlcwykkegvg
ldaindsfllessvyrvlkkycrqrpyyvhllelflqtayqtelgqmldlitapvskvdl
shfseerykaivkyktafysfylpvaaamymvgidskeehenakaillemgeyfqiqddy
ldcfgdpaltgkvgtdiqdnkcswlvvqclqrvtpeqrqllednygrkepekvakvkely
eavgmraafqqyeessyrrlqeliekhsnrlpkeiflglaqkiykrqk
>d1fpth1 2.1.1.1.51 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab C3(?), neutralizing type 1 poliovirus, (mouse), kapppa L chain}
qvqlqqsgaelvrpgtsvkvsckasgyaftnyliqwikqrpgqglewigvinpgsggtdy
nanfkgkatltadksssivymqlssltsddsavyfcardfydydvgfdywgqgttltvss
>d1fpth2 2.1.1.2.58 (114-228) Immunoglobulin (constant domains of L and H chains) {Fab C3(?), neutralizing type 1 poliovirus, (mouse), kapppa L chain}
akttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsd
lytlsssvtvtsstwpsqsitcnvahpasstkvdkkiepr
>d1fptl1 2.1.1.1.51 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab C3(?), neutralizing type 1 poliovirus, (mouse), kapppa L chain}
dvvmtqtplslpvslgdqasiscsssqslvhsngktylhwylqkpgqspklliykvsnrf
sgvpdrfsgsgsgtyftlkisrveaedlgvyfcsqsthvpytfgggtkleikr
>d1fptl2 2.1.1.2.58 (109-213) Immunoglobulin (constant domains of L and H chains) {Fab C3(?), neutralizing type 1 poliovirus, (mouse), kapppa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgsevqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrne
>d1fpv__ 2.8.1.4.14 Feline panleukopenia virus coat protein vp2 {feline panleukopenia virus (Strain b)}
gvgistgtfnnqtefkflengwveitanssrlvhlnmpesenykrvvvnnmdktavkgnm
alddihveivtpwslvdanawgvwfnpgdwqlivntmselhlvsfeqeifnvvlktvses
atqpptkvynndltaslmvaldsnntmpftpaamrsetlgfypwkptiptpwryyfqwdr
tlipshtgtsgtptnvyhgtdpddvqfytiensvpvhllrtgdefatgtfffdckpcrlt
htwqtnralglppflnslpqsegatnfgdigvqqdkrrgvtqmgntdyiteatimrpaev
gysapyysfeastqgpfktpiaagrggaqtdenqaadgdpryafgrqhgqkttttgetpe
rftyiahqdtgrypegdwiqninfnlpvtndnvllptdpiggktginytnifntygplta
lnnvppvypngqiwdkefdtdlkprlhinapfvcqnncpgqlfvkvapnltnqydpdasa
nmsrivtysdfwwkgklvfkaklrashtwnpiqqmsinvdnqfnyvpnnigamkivyeks
qlaprkly
>d1fra__ 7.6.1.1.1 Erabutoxin B (also neurotoxin B) {sea snake (Laticauda semifasciata)}
ricfnhqssqpqttktcspgesscyhkqwsdfrgtiiergcgcptvkpgiklsccesevc
nn
>d1frb__ 3.1.5.1.1 FR-1 (fibroblast growth factor-induced) protein {mouse (Mus musculus)}
atfvelstkakmpivglgtwksppnqvkeavkaaidagyrhidcayaycnenevgeaiqe
kikekavqredlfivsklwptcfekkllkeafqktltdlkldyldlylihwpqglqpgke
lfpkddqgriltskttfleawegmeelvdqglvkalgvsnfnhfqierllnkpglkhkpv
tnqvechpyltqekliqychskgisvtaysplgspdrpsakpedpslledpkikeiaakh
ektsaqvlirfhiqrnvvvipksvtpsriqeniqvfdfqlsdeematilsfnrnwracll
petvnmeeypydaey
>d1frd__ 4.11.5.1.1 2Fe-2S ferredoxin {Cyanobacterium (Anabaena sp.)}
asyqvrlinkkqdidttieideettildgaeengielpfschsgscsscvgkvvegevdq
sdqiflddeqmgkgfallcvtyprsnctikthqepyla
>d1fre__ 7.36.1.1.1 Nuclear factor XNF7 {African clawed frog (Xenopus laevis)}
ekcsehderlklyckddgtlscvicrdslkhashnflpi
>d1frgh1 2.1.1.1.38 (218-336) Immunoglobulin (variable domains of L and H chains) {Fab 26/9 (mouse), kappa L chain}
evllvesggdlvkpggflklscaasgftfssfgmswvrhtpdkrlewvatisngggytyy
qdsvkgrftisrdnakntlflemtslksedaglyycarrerydekgfaywgrgtlvtvs
>d1frgh2 2.1.1.2.46 (337-437) Immunoglobulin (constant domains of L and H chains) {Fab 26/9 (mouse), kappa L chain}
aakttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqs
dlytlsssvtvtsstwpsqsitcnvahpasstkvdkkiepr
>d1frgl1 2.1.1.1.38 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab 26/9 (mouse), kappa L chain}
divmtqspssltvtagekvtmsckssqslfnsgkrknfltwyhqkpgqppklliywastr
esgvpdrfsgsgsgtdftltitsvqaedlaiyycqndyshpltfgagt
>d1frgl2 2.1.1.2.46 (112-217) Immunoglobulin (constant domains of L and H chains) {Fab 26/9 (mouse), kappa L chain}
lkradaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtd
qdskdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1frh__ 4.34.1.2.1 Ferredoxin {(Azotobacter vinelandii )}
ayvvtdncikckytdcvevcpvdcfyegpnflvihpdecidcalcepecpaqaifsedev
pedmqefiqlnaelaevwpnitekkdplpdaedwdgvkgklqhler
>d1fri__ 4.34.1.2.1 Ferredoxin {(Azotobacter vinelandii )}
afvvtdncikckytdcvevcpvncfyegpnflvihpdecidcalcepecpaqaifsedev
pedmqefiqlnaelaevwpnitekkdplpdaedwdgvkgklqhler
>d1frj__ 4.34.1.2.1 Ferredoxin {(Azotobacter vinelandii )}
afvvtdncikckytdcvevcpvdciyegpnflvihpdecidcalcepecpaqaifsedev
pedmqefiqlnaelaevwpnitekkdplpdaedwdgvkgklqhler
>d1frk__ 4.34.1.2.1 Ferredoxin {(Azotobacter vinelandii )}
afvvtdncikckytdcvevcpvdcfyegpnflvidpdecidcalcepecpaqaifsedev
pedmqefiqlnaelaevwpnitekkdplpdaedwdgvkgklqhler
>d1frl__ 4.34.1.2.1 Ferredoxin {(Azotobacter vinelandii )}
afvvtdncikckytdcvevcpvdcfyegpnflvihpdscidcalcepecpaqaifsedev
pedmqefiqlnaelaevwpnitekkdplpdaedwdgvkgklqhler
>d1frm__ 4.34.1.2.1 Ferredoxin {(Azotobacter vinelandii )}
afvvtdncikckytdcvevcpvdcfyegpnflvihpdecidcalcapecpaqaifsedev
pedmqefiqlnaelaevwpnitekkdplpdaedwdgvkgklqhler
>d1frn_1 2.32.1.1.1 (19-154) Ferredoxin reductase (flavodoxin reductase) {spinach (Spinacia oleracea)}
hskkmeegitvnkfkpktpyvgrcllntkitgddapgetwhmvfshegeipyregqsvgv
ipdgedkngkphklrlyviassalgdfgdaksvslcvkrliytndagetikgvcsnflcd
lkpgaevkltgpvgke
>d1frn_2 3.16.1.1.1 (155-314) Ferredoxin reductase (flavodoxin reductase) {spinach (Spinacia oleracea)}
mlmpkdpnatiimlgtgtgiapfrsflwkmffekhddykfnglawlflgvptsssllyke
efekmkekapdnfrldfavsreqtnekgekmyiqtrmaqyavelwemlkkdntyfymcgl
kgmekgiddimvslaaaegidwieykrqlkkaeqwnvevy
>d1froa_ 4.20.1.1.1 Glyoxalase I {human (Homo sapiens)}
ggltdeaalsccsdadpstkdfllqqtmlrvkdpkksldfytrvlgmtliqkcdfpimkf
slyflayedkndipkekdekiawalsrkatlelthnwgteddetqsyhngnsdprgfghi
giavpdvysackrfeelgvkfvkkpddgkmkglafiqdpdgywieilnpnkmatlm
>d1frob_ 4.20.1.1.1 Glyoxalase I {human (Homo sapiens)}
ggltdeaalsccsdadpstkdfllqqtmlrvkdpkksldfytrvlgmtliqkcdfpimkf
slyflayedkndipkekdekiawalsrkatlelthnwgteddetqsyhngnsdprgfghi
giavpdvysackrfeelgvkfvkkpddgkmkglafiqdpdgywieilnpnkmatlm
>d1froc_ 4.20.1.1.1 Glyoxalase I {human (Homo sapiens)}
ggltdeaalsccsdadpstkdfllqqtmlrvkdpkksldfytrvlgmtliqkcdfpimkf
slyflayedkndipkekdekiawalsrkatlelthnwgteddetqsyhngnsdprgfghi
giavpdvysackrfeelgvkfvkkpddgkmkglafiqdpdgywieilnpnkmatlm
>d1frod_ 4.20.1.1.1 Glyoxalase I {human (Homo sapiens)}
ggltdeaalsccsdadpstkdfllqqtmlrvkdpkksldfytrvlgmtliqkcdfpimkf
slyflayedkndipkekdekiawalsrkatlelthnwgteddetqsyhngnsdprgfghi
giavpdvysackrfeelgvkfvkkpddgkmkglafiqdpdgywieilnpnkmatlm
>d1frpa_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
nivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagatnvtgd
qvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssnidc
lvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfmldp
aigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvgsm
vadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldivpt
dihqrapiilgspedvtelleiyqkha
>d1frpb_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
nivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagatnvtgd
qvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssnidc
lvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfmldp
aigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvgsm
vadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldivpt
dihqrapiilgspedvtelleiyqkha
>d1frra_ 4.11.5.1.7 2Fe-2S ferredoxin {(Equisetum arvense)}
ayktvlktpsgeftldvpegttildaaeeagydlpfscragacssclgkvvsgsvdeseg
sflddgqmeegfvltciaipesdlviethkeeelf
>d1frrb_ 4.11.5.1.7 2Fe-2S ferredoxin {(Equisetum arvense)}
ayktvlktpsgeftldvpegttildaaeeagydlpfscragacssclgkvvsgsvdeseg
sflddgqmeegfvltciaipesdlviethkeeelf
>d1frsa_ 4.46.1.1.3 fr coat protein {(bacteriophage fr)}
asnfeefvlvdnggtgdvkvapsnfangvaewissnsrsqaykvtcsvrqssannrkytv
kvevpkvatqvqggvelpvaawrsymnmeltipvfatnddcalivkalqgtfktgnpiat
aiaansgiy
>d1frsb_ 4.46.1.1.3 fr coat protein {(bacteriophage fr)}
asnfeefvlvdnggtgdvkvapsnfangvaewissnsrsqaykvtcsvrqssannrkytv
kvevpkvatqvqggvelpvaawrsymnmeltipvfatnddcalivkalqgtfktgnpiat
aiaansgiy
>d1frsc_ 4.46.1.1.3 fr coat protein {(bacteriophage fr)}
asnfeefvlvdnggtgdvkvapsnfangvaewissnsrsqaykvtcsvrqssannrkytv
kvevpkvatqvqggvelpvaawrsymnmeltipvfatnddcalivkalqgtfktgnpiat
aiaansgiy
>d1frta1 2.1.1.2.1 (179-269) Fc (IgG) receptor, alpha-3 domain and beta subunit {rat (Rattus norvegicus)}
keppsmrlkarpgnsgssvltcaafsfyppelkfrflrnglasgsgncstgpngdgsfha
wsllevkrgdehhyqcqveheglaqpltvdl
>d1frta2 4.15.1.1.1 (1-178) Fc (IgG) receptor, alpha-1 and alpha-2 domains {rat (Rattus norvegicus)}
aeprlplmyhlaavsdlstglpsfwatgwlgaqqyltynnlrqeadpcgawiwenqvswy
wekettdlkskeqlfleairtlenqingtftlqgllgcelapdnsslptavfalngeefm
rfnprtgnwsgewpetdivgnlwmkqpeaarkeseflltscperllghlergrqnlew
>d1frtc1 2.1.1.2.108 (239-341) Immunoglobulin (constant domains of L and H chains) {Fc (rat) IgG}
svflfppkpkdtlmisrtpevtcvvvdvshedpqvkfnwyvdgvqvhnaktkpreqqyns
tyrvvsvltvlhqnwldgkeykckvsnkalpapiektiskakg
>d1frtc2 2.1.1.2.108 (342-443) Immunoglobulin (constant domains of L and H chains) {Fc (rat) IgG}
qprepqvytlppsreemtknqvsltclvkgfypsdiavewesngqpennykttppvldsd
gsfflyskltvdksrwqqgnvfscsvmhealhnhytqkslsl
>d1frva_ 5.16.1.1.1 Nickel-iron hydrogenase, small subunit {(Desulfovibrio gigas)}
akkrpsvvylhnaectgcsesllrtvdpyvdelildvismdyhetlmagaghaveealhe
aikgdfvcvieggipmgdggywgkvgrrnmydicaevapkakaviaigtcatyggvqaak
pnptgtvgvnealgklgvkainiagcppnpmnfvgtvvhlltkgmpeldkqgrpvmffge
tvhdncprlkhfeagefatsfgspeakkgyclyelgckgpdtynncpkqlfnqvnwpvqa
ghpciacsepnfwdlyspfysa
>d1frvb_ 5.15.1.1.1 Nickel-iron hydrogenase, large subunit {(Desulfovibrio gigas)}
nkivvdpitrieghlrieveveggkiknawsmstlfrglemilkgrdprdaqhftqracg
vctyvhalasvravdncvgvkipenatlmrnltmgaqymhdhlvhfyhlhaldwvnvana
lnadpakaarlandlsprkttteslkavqakvkalvesgqlgiftnayflgghpayvlpa
evdliatahylealrvqvkaaramaifgaknphtqftvvggctnydslrperiaefrkly
kevrefieqvyitdllavagfyknwagigktsnfltcgefptdeydlnsrytpqgviwgn
dlskvddfnpdlieehvkyswyegadahhpykgvtkpkwtefhgedryswmkaprykgea
fevgplasvlvayakkheptvkavdlvlktlgvgpealfstlgrtaargiqcltaaqeve
vwldkleanvkagkddlytdwqyptesqgvgfvnaprgmlshwivqrggkienfqhvvps
twnlgprcaerklsaveqaligtpiadpkrpveilrtvhsydpciacgvh
>d1frvc_ 5.16.1.1.1 Nickel-iron hydrogenase, small subunit {(Desulfovibrio gigas)}
akkrpsvvylhnaectgcsesllrtvdpyvdelildvismdyhetlmagaghaveealhe
aikgdfvcvieggipmgdggywgkvgrrnmydicaevapkakaviaigtcatyggvqaak
pnptgtvgvnealgklgvkainiagcppnpmnfvgtvvhlltkgmpeldkqgrpvmffge
tvhdncprlkhfeagefatsfgspeakkgyclyelgckgpdtynncpkqlfnqvnwpvqa
ghpciacsepnfwdlyspfysa
>d1frvd_ 5.15.1.1.1 Nickel-iron hydrogenase, large subunit {(Desulfovibrio gigas)}
nkivvdpitrieghlrieveveggkiknawsmstlfrglemilkgrdprdaqhftqracg
vctyvhalasvravdncvgvkipenatlmrnltmgaqymhdhlvhfyhlhaldwvnvana
lnadpakaarlandlsprkttteslkavqakvkalvesgqlgiftnayflgghpayvlpa
evdliatahylealrvqvkaaramaifgaknphtqftvvggctnydslrperiaefrkly
kevrefieqvyitdllavagfyknwagigktsnfltcgefptdeydlnsrytpqgviwgn
dlskvddfnpdlieehvkyswyegadahhpykgvtkpkwtefhgedryswmkaprykgea
fevgplasvlvayakkheptvkavdlvlktlgvgpealfstlgrtaargiqcltaaqeve
vwldkleanvkagkddlytdwqyptesqgvgfvnaprgmlshwivqrggkienfqhvvps
twnlgprcaerklsaveqaligtpiadpkrpveilrtvhsydpciacgvh
>d1frx__ 4.34.1.2.1 Ferredoxin {(Azotobacter vinelandii )}
afvvtdncikckytdcvevspvdcfyegpnflvihpdecidcalcepecpaqaifsedev
pedmqefiqlnaelaevwpnitekkdplpdaedwdgvkgklqhler
>d1fsaa_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
tdqaafdtnivtltrfvmeqgrkargtgemtqllnslctavaaistavrkagiahlygia
gstnvtgdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpl
dgssnidclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvng
vncfmldpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapy
garyvgsmvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgke
avldivptdihqrapiilgspedvtelleiyqkhaak
>d1fsab_ 5.8.1.1.1 Fructose-1,6-bisphosphatase {pig (Sus scrofa)}
tdqaafdtnivtltrfvmeqgrkargtgemtqllnslctavaaistavrkagiahlygia
gstnvtgdqvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpl
dgssnidclvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvng
vncfmldpaigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapy
garyvgsmvadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgke
avldivptdihqrapiilgspedvtelleiyqkhaak
>d1fsb__ 7.3.9.1.10 P-selectin, EGF-domain {human (Homo sapiens)}
tascqdmscskqgecletignytcscypgfygpeceyvre
>d1fsc__ 7.6.1.1.3 Fasciculin {green mamba (Dendroaspis angusticeps)}
tmcyshtttsrailtncgenscyrksrrhppkmvlgrgcgcppgddnlevkcctspdkcn
y
>d1fsla_ 1.1.1.1.15 Leghemoglobin {Soybean (Glycine max), isoform A}
vaftekqdalvsssfeafkanipqysvvfytsilekapaakdlfsflangvdptnpkltg
haeklfalvrdsagqlkasgtvvadaalgsvhaqkavtdpqfvvvkeallktikaavgdk
wsdelsrawevaydelaaaikka
>d1fslb_ 1.1.1.1.15 Leghemoglobin {Soybean (Glycine max), isoform A}
vaftekqdalvsssfeafkanipqysvvfytsilekapaakdlfsflangvdptnpkltg
haeklfalvrdsagqlkasgtvvadaalgsvhaqkavtdpqfvvvkeallktikaavgdk
wsdelsrawevaydelaaaikka
>d1fsp__ 3.14.2.1.6 Sporulation response regulator Spo0F {(Bacillus subtilis)}
mmnekilivddqygirillnevfnkegyqtfqaanglqaldivtkerpdlvlldmkipgm
dgieilkrmkvidenirviimtaygeldmiqeskelgalthfakpfdideirdavkkylp
lksn
>d1fssa_ 3.56.1.1.2 Acetylcholinesterase {Electric eel (Electrophorus electricus)}
sellvntksgkvmgtrvpvlsshisaflgipfaeppvgnmrfrrpepkkpwsgvwnasty
pnncqqyvdeqfpgfsgsemwnpnremsedclylniwvpsprpksttvmvwiygggfysg
sstldvyngkylayteevvlvslsyrvgafgflalhgsqeapgnvglldqrmalqwvhdn
iqffggdpktvtifgesaggasvgmhilspgsrdlfrrailqsgspncpwasvsvaegrr
ravelgrnlncnlnsdeelihclrekkpqelidvewnvlpfdsifrfsfvpvidgeffpt
slesmlnsgnfkktqillgvnkdegsffllygapgfskdseskisredfmsgvklsvpha
ndlgldavtlqytdwmddnngiknrdglddivgdhnvicplmhfvnkytkfgngtylyff
nhrasnlvwpewmgvihgyeiefvfglplvkelnytaeeealsrrimhywatfaktgnpn
ephsqeskwplfttkeqkfidlntepmkvhqrlrvqmcvfwnqflpkllnat
>d1fssb_ 7.6.1.1.3 Fasciculin {green mamba (Dendroaspis angusticeps)}
tmcyshtttsrailtncgenscyrksrrhppkmvlgrgcgcppgddnlevkcctspdkcn
y
>d1fsu__ 3.64.1.2.2 Arylsulfatase B (4-sulfatase) {Human (Homo sapiens)}
srpphlvflladdlgwndvgfhgsrirtphldalaaggvlldnyytqplxtpsrsqlltg
ryqirtglqhqiiwpcqpscvpldekllpqllkeagytthmvgkwhlgmyrkeclptrrg
fdtyfgyllgsedyysherctlidalnvtrcaldfrdgeevatgyknmystniftkraia
litnhppekplflylalqsvheplqvpeeylkpydfiqdknrhhyagmvslmdeavgnvt
aalkssglwnntvfifstdnggqtlaggnnwplrgrkwslweggvrgvgfvaspllkqkg
vknrelihisdwlptlvklarghtngtkpldgfdvwktisegspspriellhnidpnfvd
sspcprnsmapakddsslpeysafntsvhaairhgnwklltgypgcgywfpppsqynvse
ipssdpptktlwlfdidrdpeerhdlsreyphivtkllsrlqfyhkhsvpvyfpaqdprc
dpkatgvwgpwm
>d1fsz_1 3.25.1.1.1 (23-231) Cell-division protein FtsZ {(Methanococcus jannaschii)}
spedkelleylqqtkakitvvgcggagnntitrlkmegiegaktvaintdaqqlirtkad
kkiligkkltrglgaggnpkigeeaakesaeeikaaiqdsdmvfitcglgggtgtgsapv
vaeiskkigaltvavvtlpfvmegkvrmknameglerlkqhtdtlvvipneklfeivpnm
plklafkvadevlinavkglvelitkdgl
>d1fsz_2 4.40.2.1.1 (232-356) Cell-division protein FtsZ {(Methanococcus jannaschii)}
invdfadvkavmnngglamigigesdsekrakeavsmalnsplldvdidgatgalihvmg
pedltleearevvatvssrldpnatiiwgatidenlentvrvllvitgvqsrieftdtgl
krkkl
>d1ft1a_ 1.91.6.1.1 Protein farnesyltransferase, alpha-subunit {Rat (Rattus norvegicus)}
flsldsptyvlyrdraewadidpvpqndgpspvvqiiysekfrdvydyfravlqrderse
rafkltrdaielnaanytvwhfrrvllrslqkdlqeemnyiiaiieeqpknyqvwhhrrv
lvewlkdpsqelefiadilnqdaknyhawqhrqwviqefrlwdnelqyvdqllkedvrnn
svwnqrhfvisnttgysdravlerevqytlemiklvphnesawnylkgilqdrglsrypn
llnqlldlqpshsspyliaflvdiyedmlenqcdnkedilnkalelceilakekdtirke
ywryigrslqskhsr
>d1ft1b_ 1.81.2.3.1 Protein farnesyltransferase, beta-subunit {Rat (Rattus norvegicus)}
plyslrpeharerlqddsvetvtsieqakveekiqevfssykfnhlvprlvlqrekhfhy
lkrglrqltdayecldasrpwlcywilhslelldepipqivatdvcqflelcqspdggfg
ggpgqyphlaptyaavnalciigteeaynvinrekllqylyslkqpdgsflmhvggevdv
rsaycaasvasltniitpdlfegtaewiarcqnweggiggvpgmeahggytfcglaalvi
lkkerslnlksllqwvtsrqmrfeggfqgrcnklvdgcysfwqagllpllhralhaqgdp
alsmshwmfhqqalqeyilmccqcpagglldkpgksrdfyhtcyclsglsiaqhfgsgam
lhdvvmgvpenvlqpthpvynigpdkviqatthflqkpvpgfeecedavtsdpatd
>d1ftaa_ 5.8.1.1.2 Fructose-1,6-bisphosphatase {human (Homo sapiens)}
dvvtltrfvmeegrkargtgeltqllnslctavkaissavrkagiahlygiagstnvtgd
qvkkldvlsndlvmnmlkssfatcvlvseedkhaiivepekrgkyvvcfdpldgssnidc
lvsvgtifgiyrkkstdepsekdalqpgrnlvaagyalygsatmlvlamdcgvncfmldp
aigefilvdkdvkikkkgkiyslneayakdfdpavteyiqrkkfppdnsapygaryvgsm
vadvhrtlvyggiflypankkspngklrllyecnpmayvmekaggmattgkeavldvipt
dihqrapiilgspddvleflkvyekhs
>d1ftab_ 5.8.1.1.2 Fructose-1,6-bisphosphatase {human (Homo sapiens)}
dvvtltrfvmeegrkargtgeltqllnslctavkaissavrkagiahlygiagstnvtgd
qvkkldvlsndlvmnmlkssfatcvlvseedkhaiivepekrgkyvvcfdpldgssnidc
lvsvgtifgiyrkkstdepsekdalqpgrnlvaagyalygsatmlvlamdcgvncfmldp
aigefilvdkdvkikkkgkiyslneayakdfdpavteyiqrkkfppdnsapygaryvgsm
vadvhrtlvyggiflypankkspngklrllyecnpmayvmekaggmattgkeavldvipt
dihqrapiilgspddvleflkvyekhs
>d1ftac_ 5.8.1.1.2 Fructose-1,6-bisphosphatase {human (Homo sapiens)}
dvvtltrfvmeegrkargtgeltqllnslctavkaissavrkagiahlygiagstnvtgd
qvkkldvlsndlvmnmlkssfatcvlvseedkhaiivepekrgkyvvcfdpldgssnidc
lvsvgtifgiyrkkstdepsekdalqpgrnlvaagyalygsatmlvlamdcgvncfmldp
aigefilvdkdvkikkkgkiyslneayakdfdpavteyiqrkkfppdnsapygaryvgsm
vadvhrtlvyggiflypankkspngklrllyecnpmayvmekaggmattgkeavldvipt
dihqrapiilgspddvleflkvyekhs
>d1ftad_ 5.8.1.1.2 Fructose-1,6-bisphosphatase {human (Homo sapiens)}
dvvtltrfvmeegrkargtgeltqllnslctavkaissavrkagiahlygiagstnvtgd
qvkkldvlsndlvmnmlkssfatcvlvseedkhaiivepekrgkyvvcfdpldgssnidc
lvsvgtifgiyrkkstdepsekdalqpgrnlvaagyalygsatmlvlamdcgvncfmldp
aigefilvdkdvkikkkgkiyslneayakdfdpavteyiqrkkfppdnsapygaryvgsm
vadvhrtlvyggiflypankkspngklrllyecnpmayvmekaggmattgkeavldvipt
dihqrapiilgspddvleflkvyekhs
>d1ftca_ 4.34.1.2.1 Ferredoxin {(Azotobacter vinelandii )}
afvvtdncikckxtdcvevcpvdcfyegpnflvihpdecidcalcepecpaqaifsedev
pedmqefiqlnaelaevwpnitekkdplpdaedwdgvkgklqhler
>d1ftcb_ 4.34.1.2.1 Ferredoxin {(Azotobacter vinelandii )}
afvvtdncikckxtdcvevcpvdcfyegpnflvihpdecidcalcepecpaqaifsedev
pedmqefiqlnaelaevwpnitekkdplpdaedwdgvkgklqhler
>d1ftg__ 3.14.4.1.4 Flavodoxin {(Anabaena sp.) PCC 7119}
kkiglfygtqtgktesvaeiirdefgndvvtlhdvsqaevtdlndyqyliigcptwnige
lqsdweglyselddvdfngklvayfgtgdqigyadnfqdaigileekisqrggktvgyws
tdgydfndskalrngkfvglaldednqsdltddrikswvaqlksefgl
>d1ftn__ 3.29.1.4.7 RhoA {Human (Homo sapiens)}
irkklvivgdgacgktcllivnskdqfpevyvptvfenyvadievdgkqvelalwdtagq
edydrlrplsypdtdvilmcfsidspdslenipekwtpevkhfcpnvpiilvgnkkdlrn
dehtrrelakmkqepvkpeegrdmanrigafgymecsaktkdgvrevfematraalq
>d1ftpa_ 2.45.1.2.5 Fatty acid-binding protein {desert locust (Schistocerca gregaria)}
vkefagikykldsqtnfeeymkaigvgaierkaglalspvieleildgdkfkltsktaik
nteftfklgeefdeetldgrkvkstitqdgpnklvheqkgdhptiiirefskeqcvitik
lgdlvatriykaq
>d1ftpb_ 2.45.1.2.5 Fatty acid-binding protein {desert locust (Schistocerca gregaria)}
vkefagikykldsqtnfeeymkaigvgaierkaglalspvieleildgdkfkltsktaik
nteftfklgeefdeetldgrkvkstitqdgpnklvheqkgdhptiiirefskeqcvitik
lgdlvatriykaq
>d1fts_1 1.28.1.1.2 (201-284) Signal recognition particle receptor, FtsY {(Escherichia coli)}
rsllktkenlgsgfislfrgkkidddlfeeleeqlliadvgvettrkiitnltegasrkq
lrdaealygllkeemgeilakvde
>d1fts_2 3.29.1.6.5 (285-495) GTPase domain of the signal recognition particle receptor FtsY {(Escherichia coli)}
plnvegkapfvilmvgvngvgktttigklarqfeqqgksvmlaagdtfraaaveqlqvwg
qrnnipviaqhtgadsasvifdaiqaakarnidvliadtagrlqnkshlmeelkkivrvm
kkldveaphevmltidastgqnavsqaklfheavgltgitltkldgtakggvifsvadqf
gipiryigvgeriedlrpfkaddfiealfar
>d1ftt__ 1.4.1.1.7 Thyroid transcription factor 1 homeodomain {rat (Rattus rattus)}
mrrkrrvlfsqaqvyelerrfkqqkylsaperehlasmihltptqvkiwfqnhrykmkrq
akdkaaqq
>d1ftz__ 1.4.1.1.11 Fushi Tarazu protein {fruit fly (Drosophila melanogaster)}
mdskrtrqtytryqtlelekefhfnryitrrrridianalslserqikiwfqnrrmkskk
drtldsspeh
>d1fua__ 3.63.1.1.1 L-fuculose-1-phospate aldolase {(Escherichia coli)}
mernklarqiidtclemtrlglnqgtagnvsvryqdgmlitptgipyeklteshivfidg
ngkheegklpssewrfhmaayqsrpdanavvhnhavhctavsilnrsipaihymiaaagg
nsipcapyatfgtrelsehvalalknrkatllqhhgliacevnlekalwlahevevlaql
ylttlaitdpvpvlsdeeiavvlekf
>d1fuga1 4.80.1.1.1 (1-101) S-adenosylmethionine synthetase. MAT {(Escherichia coli)}
akhlftsesvseghpdkiadqisdavldaileqdpkarvacetyvktgmvlvggeittsa
wvdieeitrntvreigyvhsdmgfdanscavlsaigkqspd
>d1fuga2 4.80.1.1.1 (108-231) S-adenosylmethionine synthetase. MAT {(Escherichia coli)}
radpleqgagdqglmfgyatnetdvlmpapityahrlvqrqaevrkngtlpwlrpdaksq
vtfqyddgkivgidavvlstqhseeidqkslqeavmeeiikpilpaewltsatkffinpt
grfv
>d1fuga3 4.80.1.1.1 (232-383) S-adenosylmethionine synthetase. MAT {(Escherichia coli)}
iggpmgdcgltgrkiivdtyggmarhgggafsgkdpskvdrsaayaaryvaknivaagla
drceiqvsyaigvaeptsimvetfgtekvpseqltllvreffdlrpygliqmldllhpiy
ketaayghfgrehfpwektdkaqllrdaaglk
>d1fugb1 4.80.1.1.1 (1-101) S-adenosylmethionine synthetase. MAT {(Escherichia coli)}
akhlftsesvseghpdkiadqisdavldaileqdpkarvacetyvktgmvlvggeittsa
wvdieeitrntvreigyvhsdmgfdanscavlsaigkqspd
>d1fugb2 4.80.1.1.1 (108-231) S-adenosylmethionine synthetase. MAT {(Escherichia coli)}
radpleqgagdqglmfgyatnetdvlmpapityahrlvqrqaevrkngtlpwlrpdaksq
vtfqyddgkivgidavvlstqhseeidqkslqeavmeeiikpilpaewltsatkffinpt
grfv
>d1fugb3 4.80.1.1.1 (232-383) S-adenosylmethionine synthetase. MAT {(Escherichia coli)}
iggpmgdcgltgrkiivdtyggmarhgggafsgkdpskvdrsaayaaryvaknivaagla
drceiqvsyaigvaeptsimvetfgtekvpseqltllvreffdlrpygliqmldllhpiy
ketaayghfgrehfpwektdkaqllrdaaglk
>d1fuia1 2.32.2.1.1 (356-591) L-fucose isomerase, C-terminal domain {(Escherichia coli)}
aqvfadvrtywspeaiervtghkldglaehgiihlinsgsaaldgsckqrdsegnptmkp
hweisqqeadaclaatewcpaiheyfrgggyssrflteggvpftmtrvniikglgpvlqi
aegwsvelpkdvhdilnkrtnstwpttwfaprltgkgpftdvysvmanwganhgvltigh
vgadfitlasmlripvcmhnveetkvyrpsawaahgmdiegqdyracqnygplykr
>d1fuia2 3.73.1.1.1 (1-355) L-fucose isomerase, N-terminal and second domains {(Escherichia coli)}
mkkislpkigirpvidgrrmgvresleeqtmnmakataallteklrhacgaavecvisdt
ciagmaeaaaceekfssqnvgltitvtpcwcygsetidmdptrpkaiwgfngterpgavy
laaalaahsqkgipafsiyghdvqdaddtsipadveekllrfaraglavasmkgksylsl
ggvsmgiagsivdhnffeswlgmkvqavdmtelrrridqkiydeaelemalawadknfry
gedennkqyqrnaeqsravlresllmamcirdmmqgnskladigrveeslgynaiaagfq
gqrhwtdqypngdtaeailnssfdwngvrepfvvatendslngvamlmghqltgt
>d1fuib1 2.32.2.1.1 (356-591) L-fucose isomerase, C-terminal domain {(Escherichia coli)}
aqvfadvrtywspeaiervtghkldglaehgiihlinsgsaaldgsckqrdsegnptmkp
hweisqqeadaclaatewcpaiheyfrgggyssrflteggvpftmtrvniikglgpvlqi
aegwsvelpkdvhdilnkrtnstwpttwfaprltgkgpftdvysvmanwganhgvltigh
vgadfitlasmlripvcmhnveetkvyrpsawaahgmdiegqdyracqnygplykr
>d1fuib2 3.73.1.1.1 (1-355) L-fucose isomerase, N-terminal and second domains {(Escherichia coli)}
mkkislpkigirpvidgrrmgvresleeqtmnmakataallteklrhacgaavecvisdt
ciagmaeaaaceekfssqnvgltitvtpcwcygsetidmdptrpkaiwgfngterpgavy
laaalaahsqkgipafsiyghdvqdaddtsipadveekllrfaraglavasmkgksylsl
ggvsmgiagsivdhnffeswlgmkvqavdmtelrrridqkiydeaelemalawadknfry
gedennkqyqrnaeqsravlresllmamcirdmmqgnskladigrveeslgynaiaagfq
gqrhwtdqypngdtaeailnssfdwngvrepfvvatendslngvamlmghqltgt
>d1fuic1 2.32.2.1.1 (356-591) L-fucose isomerase, C-terminal domain {(Escherichia coli)}
aqvfadvrtywspeaiervtghkldglaehgiihlinsgsaaldgsckqrdsegnptmkp
hweisqqeadaclaatewcpaiheyfrgggyssrflteggvpftmtrvniikglgpvlqi
aegwsvelpkdvhdilnkrtnstwpttwfaprltgkgpftdvysvmanwganhgvltigh
vgadfitlasmlripvcmhnveetkvyrpsawaahgmdiegqdyracqnygplykr
>d1fuic2 3.73.1.1.1 (1-355) L-fucose isomerase, N-terminal and second domains {(Escherichia coli)}
mkkislpkigirpvidgrrmgvresleeqtmnmakataallteklrhacgaavecvisdt
ciagmaeaaaceekfssqnvgltitvtpcwcygsetidmdptrpkaiwgfngterpgavy
laaalaahsqkgipafsiyghdvqdaddtsipadveekllrfaraglavasmkgksylsl
ggvsmgiagsivdhnffeswlgmkvqavdmtelrrridqkiydeaelemalawadknfry
gedennkqyqrnaeqsravlresllmamcirdmmqgnskladigrveeslgynaiaagfq
gqrhwtdqypngdtaeailnssfdwngvrepfvvatendslngvamlmghqltgt
>d1fuid1 2.32.2.1.1 (356-591) L-fucose isomerase, C-terminal domain {(Escherichia coli)}
aqvfadvrtywspeaiervtghkldglaehgiihlinsgsaaldgsckqrdsegnptmkp
hweisqqeadaclaatewcpaiheyfrgggyssrflteggvpftmtrvniikglgpvlqi
aegwsvelpkdvhdilnkrtnstwpttwfaprltgkgpftdvysvmanwganhgvltigh
vgadfitlasmlripvcmhnveetkvyrpsawaahgmdiegqdyracqnygplykr
>d1fuid2 3.73.1.1.1 (1-355) L-fucose isomerase, N-terminal and second domains {(Escherichia coli)}
mkkislpkigirpvidgrrmgvresleeqtmnmakataallteklrhacgaavecvisdt
ciagmaeaaaceekfssqnvgltitvtpcwcygsetidmdptrpkaiwgfngterpgavy
laaalaahsqkgipafsiyghdvqdaddtsipadveekllrfaraglavasmkgksylsl
ggvsmgiagsivdhnffeswlgmkvqavdmtelrrridqkiydeaelemalawadknfry
gedennkqyqrnaeqsravlresllmamcirdmmqgnskladigrveeslgynaiaagfq
gqrhwtdqypngdtaeailnssfdwngvrepfvvatendslngvamlmghqltgt
>d1fuie1 2.32.2.1.1 (356-591) L-fucose isomerase, C-terminal domain {(Escherichia coli)}
aqvfadvrtywspeaiervtghkldglaehgiihlinsgsaaldgsckqrdsegnptmkp
hweisqqeadaclaatewcpaiheyfrgggyssrflteggvpftmtrvniikglgpvlqi
aegwsvelpkdvhdilnkrtnstwpttwfaprltgkgpftdvysvmanwganhgvltigh
vgadfitlasmlripvcmhnveetkvyrpsawaahgmdiegqdyracqnygplykr
>d1fuie2 3.73.1.1.1 (1-355) L-fucose isomerase, N-terminal and second domains {(Escherichia coli)}
mkkislpkigirpvidgrrmgvresleeqtmnmakataallteklrhacgaavecvisdt
ciagmaeaaaceekfssqnvgltitvtpcwcygsetidmdptrpkaiwgfngterpgavy
laaalaahsqkgipafsiyghdvqdaddtsipadveekllrfaraglavasmkgksylsl
ggvsmgiagsivdhnffeswlgmkvqavdmtelrrridqkiydeaelemalawadknfry
gedennkqyqrnaeqsravlresllmamcirdmmqgnskladigrveeslgynaiaagfq
gqrhwtdqypngdtaeailnssfdwngvrepfvvatendslngvamlmghqltgt
>d1fuif1 2.32.2.1.1 (356-591) L-fucose isomerase, C-terminal domain {(Escherichia coli)}
aqvfadvrtywspeaiervtghkldglaehgiihlinsgsaaldgsckqrdsegnptmkp
hweisqqeadaclaatewcpaiheyfrgggyssrflteggvpftmtrvniikglgpvlqi
aegwsvelpkdvhdilnkrtnstwpttwfaprltgkgpftdvysvmanwganhgvltigh
vgadfitlasmlripvcmhnveetkvyrpsawaahgmdiegqdyracqnygplykr
>d1fuif2 3.73.1.1.1 (1-355) L-fucose isomerase, N-terminal and second domains {(Escherichia coli)}
mkkislpkigirpvidgrrmgvresleeqtmnmakataallteklrhacgaavecvisdt
ciagmaeaaaceekfssqnvgltitvtpcwcygsetidmdptrpkaiwgfngterpgavy
laaalaahsqkgipafsiyghdvqdaddtsipadveekllrfaraglavasmkgksylsl
ggvsmgiagsivdhnffeswlgmkvqavdmtelrrridqkiydeaelemalawadknfry
gedennkqyqrnaeqsravlresllmamcirdmmqgnskladigrveeslgynaiaagfq
gqrhwtdqypngdtaeailnssfdwngvrepfvvatendslngvamlmghqltgt
>d1fuja_ 2.35.1.2.29 Myeloblastin, PR3 {human (Homo sapiens)}
ivggheaqphsrpymaslqmrgnpgshfcggtlihpsfvltaahclrdipqrlvnvvlga
hnvrtqeptqqhfsvaqvflnnydaenklndilliqlsspanlsasvatvqlpqqdqpvp
hgtqclamgwgrvgahdppaqvlqelnvtvvtffcrphnictfvprrkagicfgdsggpl
icdgiiqgidsfviwgcatrlfpdfftrvalyvdwirstlr
>d1fujb_ 2.35.1.2.29 Myeloblastin, PR3 {human (Homo sapiens)}
ivggheaqphsrpymaslqmrgnpgshfcggtlihpsfvltaahclrdipqrlvnvvlga
hnvrtqeptqqhfsvaqvflnnydaenklndilliqlsspanlsasvatvqlpqqdqpvp
hgtqclamgwgrvgahdppaqvlqelnvtvvtffcrphnictfvprrkagicfgdsggpl
icdgiiqgidsfviwgcatrlfpdfftrvalyvdwirstlr
>d1fujc_ 2.35.1.2.29 Myeloblastin, PR3 {human (Homo sapiens)}
ivggheaqphsrpymaslqmrgnpgshfcggtlihpsfvltaahclrdipqrlvnvvlga
hnvrtqeptqqhfsvaqvflnnydaenklndilliqlsspanlsasvatvqlpqqdqpvp
hgtqclamgwgrvgahdppaqvlqelnvtvvtffcrphnictfvprrkagicfgdsggpl
icdgiiqgidsfviwgcatrlfpdfftrvalyvdwirstlr
>d1fujd_ 2.35.1.2.29 Myeloblastin, PR3 {human (Homo sapiens)}
ivggheaqphsrpymaslqmrgnpgshfcggtlihpsfvltaahclrdipqrlvnvvlga
hnvrtqeptqqhfsvaqvflnnydaenklndilliqlsspanlsasvatvqlpqqdqpvp
hgtqclamgwgrvgahdppaqvlqelnvtvvtffcrphnictfvprrkagicfgdsggpl
icdgiiqgidsfviwgcatrlfpdfftrvalyvdwirstlr
>d1fuoa_ 1.98.1.2.1 Fumarase {(Escherichia coli)}
vrsekdsmgaidvpadklwgaqtqrslehfristekmptslihalaltkraaakvnedlg
llseekasairqaadevlagqhddefplaiwqtgsgtqsnmnmnevlanrasellggvrg
merkvhpnddvnksqssndvfptamhvaallalrkqlipqlktltqtlneksrafadivk
igrthlqdatpltlgqeisgwvamlehnlkhieyslphvaelalggtavgtglnthpeya
rrvadelavitcapfvtapnkfealatcdalvqahgalkglaaslmkiandvrwlasgpr
cgigeisipenepgssimpgkvnptqcealtmlccqvmgndvainmggasgnfelnvfrp
mvihnflqsvrlladgmesfnkhcavgiepnrerinqllneslmlvtalnthigydkaae
iakkahkegltlkaaalalgylseaefdswvrpeqm
>d1fuob_ 1.98.1.2.1 Fumarase {(Escherichia coli)}
mntvrsekdsmgaidvpadklwgaqtqrslehfristekmptslihalaltkraaakvne
dlgllseekasairqaadevlagqhddefplaiwqtgsgtqsnmnmnevlanrasellgg
vrgmerkvhpnddvnksqssndvfptamhvaallalrkqlipqlktltqtlneksrafad
ivkigrthlqdatpltlgqeisgwvamlehnlkhieyslphvaelalggtavgtglnthp
eyarrvadelavitcapfvtapnkfealatcdalvqahgalkglaaslmkiandvrwlas
gprcgigeisipenepgssimpgkvnptqcealtmlccqvmgndvainmggasgnfelnv
frpmvihnflqsvrlladgmesfnkhcavgiepnrerinqllneslmlvtalnthigydk
aaeiakkahkegltlkaaalalgylseaefdswvrpeqm
>d1fupa_ 1.98.1.2.1 Fumarase {(Escherichia coli)}
rsekdsmgaidvpadklwgaqtqrslehfristekmptslihalaltkraaakvnedlgl
lseekasairqaadevlagqhddefplaiwqtgsgtqsnmnmnevlanrasellggvrgm
erkvhpnddvnksqssndvfptamhvaallalrkqlipqlktltqtlneksrafadivki
grthlqdatpltlgqeisgwvamlehnlkhieyslphvaelalggtavgtglnthpeyar
rvadelavitcapfvtapnkfealatcdalvqahgalkglaaslmkiandvrwlasgprc
gigeisipenepgssimpgkvnptqcealtmlccqvmgndvainmggasgnfelnvfrpm
vihnflqsvrlladgmesfnkhcavgiepnrerinqllneslmlvtalnthigydkaaei
akkahkegltlkaaalalgylseaefdswvrpeqm
>d1fupb_ 1.98.1.2.1 Fumarase {(Escherichia coli)}
mntvrsekdsmgaidvpadklwgaqtqrslehfristekmptslihalaltkraaakvne
dlgllseekasairqaadevlagqhddefplaiwqtgsgtqsnmnmnevlanrasellgg
vrgmerkvhpnddvnksqssndvfptamhvaallalrkqlipqlktltqtlneksrafad
ivkigrthlqdatpltlgqeisgwvamlehnlkhieyslphvaelalggtavgtglnthp
eyarrvadelavitcapfvtapnkfealatcdalvqahgalkglaaslmkiandvrwlas
gprcgigeisipenepgssimpgkvnptqcealtmlccqvmgndvainmggasgnfelnv
frpmvihnflqsvrlladgmesfnkhcavgiepnrerinqllneslmlvtalnthigydk
aaeiakkahkegltlkaaalalgylseaefdswvrpeqm
>d1fuqa_ 1.98.1.2.1 Fumarase {(Escherichia coli)}
vrsekdsmgaidvpadklwgaqtqrslehfristekmptslihalaltkraaakvnedlg
llseekasairqaadevlagqhddefplaiwqtgsgtqsnmnmnevlanrasellggvrg
merkvhpnddvnksqssndvfptamhvaallalrkqlipqlktltqtlneksrafadivk
igrthlqdatpltlgqeisgwvamlehnlkhieyslphvaelalggtavgtglnthpeya
rrvadelavitcapfvtapnkfealatcdalvqahgalkglaaslmkiandvrwlasgpr
cgigeisipenepgssimpgkvnptqcealtmlccqvmgndvainmggasgnfelnvfrp
mvihnflqsvrlladgmesfnkhcavgiepnrerinqllneslmlvtalnthigydkaae
iakkahkegltlkaaalalgylseaefdswvrpeqm
>d1fuqb_ 1.98.1.2.1 Fumarase {(Escherichia coli)}
mntvrsekdsmgaidvpadklwgaqtqrslehfristekmptslihalaltkraaakvne
dlgllseekasairqaadevlagqhddefplaiwqtgsgtqsnmnmnevlanrasellgg
vrgmerkvhpnddvnksqssndvfptamhvaallalrkqlipqlktltqtlneksrafad
ivkigrthlqdatpltlgqeisgwvamlehnlkhieyslphvaelalggtavgtglnthp
eyarrvadelavitcapfvtapnkfealatcdalvqahgalkglaaslmkiandvrwlas
gprcgigeisipenepgssimpgkvnptqcealtmlccqvmgndvainmggasgnfelnv
frpmvihnflqsvrlladgmesfnkhcavgiepnrerinqllneslmlvtalnthigydk
aaeiakkahkegltlkaaalalgylseaefdswvrpeqm
>d1fura_ 1.98.1.2.1 Fumarase {(Escherichia coli)}
vrsekdsmgaidvpadklwgaqtqrslehfristekmptslihalaltkraaakvnedlg
llseekasairqaadevlagqhddefplaiwqtgsgtqsnmnmnevlanrasellggvrg
merkvhpnddvnksqssndvfptamhvaallalrkqlipqlktltqtlneksrafadivk
igrtnlqdatpltlgqeisgwvamlehnlkhieyslphvaelalggtavgtglnthpeya
rrvadelavitcapfvtapnkfealatcdalvqahgalkglaaslmkiandvrwlasgpr
cgigeisipenepgssimpgkvnptqcealtmlccqvmgndvainmggasgnfelnvfrp
mvihnflqsvrlladgmesfnkhcavgiepnrerinqllneslmlvtalnthigydkaae
iakkahkegltlkaaalalgylseaefdswvrpeqm
>d1furb_ 1.98.1.2.1 Fumarase {(Escherichia coli)}
mntvrsekdsmgaidvpadklwgaqtqrslehfristekmptslihalaltkraaakvne
dlgllseekasairqaadevlagqhddefplaiwqtgsgtqsnmnmnevlanrasellgg
vrgmerkvhpnddvnksqssndvfptamhvaallalrkqlipqlktltqtlneksrafad
ivkigrtnlqdatpltlgqeisgwvamlehnlkhieyslphvaelalggtavgtglnthp
eyarrvadelavitcapfvtapnkfealatcdalvqahgalkglaaslmkiandvrwlas
gprcgigeisipenepgssimpgkvnptqcealtmlccqvmgndvainmggasgnfelnv
frpmvihnflqsvrlladgmesfnkhcavgiepnrerinqllneslmlvtalnthigydk
aaeiakkahkegltlkaaalalgylseaefdswvrpeqm
>d1fus__ 4.1.1.1.2 RNase F1 {(Fusarium moniliforme)}
xsattcgstnysasqvraaanaacqyyqnddtagsstyphtynnyegfdfpvdgpyqefp
iksggvytggspgadrvvintnceyagaithtgasgnnfvgcsgtn
>d1fut__ 4.1.1.1.2 RNase F1 {(Fusarium moniliforme)}
xsattcgstnysasqvraaanaacqyyqnddtagsstyphtynnyegfdfpvdgpyqefp
iksggvytggspgadrvvintnceyagaithtgasgnnfvgcsgtn
>d1fvca_ 2.1.1.1.26 Immunoglobulin (variable domains of L and H chains) {Fab 4D5 (synthetic, humanised version), kappa L chain}
diqmtqspsslsasvgdrvtitcrasqdvntavawyqqkpgkapklliysasflysgvps
rfsgsrsgtdftltisslqpedfatyycqqhyttpptfgqgtkveikrt
>d1fvcb_ 2.1.1.1.26 Immunoglobulin (variable domains of L and H chains) {Fab 4D5 (synthetic, humanised version), kappa L chain}
evqlvesggglvqpggslrlscaasgfnikdtyihwvrqapgkglewvariyptngytry
adsvkgrftisadtskntaylqmnslraedtavyycsrwggdgfyamdywgqgtlvtvss
>d1fvcc_ 2.1.1.1.26 Immunoglobulin (variable domains of L and H chains) {Fab 4D5 (synthetic, humanised version), kappa L chain}
diqmtqspsslsasvgdrvtitcrasqdvntavawyqqkpgkapklliysasflysgvps
rfsgsrsgtdftltisslqpedfatyycqqhyttpptfgqgtkveikr
>d1fvcd_ 2.1.1.1.26 Immunoglobulin (variable domains of L and H chains) {Fab 4D5 (synthetic, humanised version), kappa L chain}
evqlvesggglvqpggslrlscaasgfnikdtyihwvrqapgkglewvariyptngytry
adsvkgrftisadtskntaylqmnslraedtavyycsrwggdgfyamdywgqgtlvtvss
>d1fvda1 2.1.1.1.26 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab 4D5 (synthetic, humanised version), kappa L chain}
diqmtqspsslsasvgdrvtitcrasqdvntavawyqqkpgkapklliysasflesgvps
rfsgsrsgtdftltisslqpedfatyycqqhyttpptfgqgtkveikr
>d1fvda2 2.1.1.2.34 (109-214) Immunoglobulin (constant domains of L and H chains) {Fab 4D5 (synthetic, humanised version), kappa L chain}
tvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqds
kdstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1fvdb1 2.1.1.1.26 (1-120) Immunoglobulin (variable domains of L and H chains) {Fab 4D5 (synthetic, humanised version), kappa L chain}
evqlvesggglvqpggslrlscaasgfnikdtyihwvrqapgkglewvariyptngytry
adsvkgrftisadtskntlylqmnslraedtavyycsrwggdgfyamdvwgqgtlvtvss
>d1fvdb2 2.1.1.2.34 (121-223) Immunoglobulin (constant domains of L and H chains) {Fab 4D5 (synthetic, humanised version), kappa L chain}
astkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkvepksc
>d1fvdc1 2.1.1.1.26 (1-114) Immunoglobulin (variable domains of L and H chains) {Fab 4D5 (synthetic, humanised version), kappa L chain}
diqmtqspsslsasvgdrvtitcrasqdvntavawyqqkpgkapklliysasflesgvps
rfsgsrsgtdftltisslqpedfatyycqqhyttpptfgqgtkveikrtvaaps
>d1fvdc2 2.1.1.2.34 (115-214) Immunoglobulin (constant domains of L and H chains) {Fab 4D5 (synthetic, humanised version), kappa L chain}
vfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqdskdstys
lsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1fvdd1 2.1.1.1.26 (1-121) Immunoglobulin (variable domains of L and H chains) {Fab 4D5 (synthetic, humanised version), kappa L chain}
evqlvesggglvqpggslrlscaasgfnikdtyihwvrqapgkglewvariyptngytry
adsvkgrftisadtskntlylqmnslraedtavyycsrwggdgfyamdvwgqgtlvtvss
a
>d1fvdd2 2.1.1.2.34 (122-223) Immunoglobulin (constant domains of L and H chains) {Fab 4D5 (synthetic, humanised version), kappa L chain}
stkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqssg
lyslssvvtvpssslgtqtyicnvnhkpsntkvdkkvepksc
>d1fvea1 2.1.1.1.26 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab 4D5 (synthetic, humanised version), kappa L chain}
diqmtqspsslsasvgdrvtitcrasqdvntavawyqqkpgkapklliysasflesgvps
rfsgsrsgtdftltisslqpedfatyycqqhyttpptfgqgtkveikr
>d1fvea2 2.1.1.2.34 (109-214) Immunoglobulin (constant domains of L and H chains) {Fab 4D5 (synthetic, humanised version), kappa L chain}
tvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqds
kdstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1fveb1 2.1.1.1.26 (1-120) Immunoglobulin (variable domains of L and H chains) {Fab 4D5 (synthetic, humanised version), kappa L chain}
evqlvesggglvqpggslrlscaasgfnikdtyihwvrqapgkglewvariyptngytry
adsvkgrftisadtskntaylqmnslraedtavyycsrwggdgfyamdywgqgtlvtvss
>d1fveb2 2.1.1.2.34 (121-223) Immunoglobulin (constant domains of L and H chains) {Fab 4D5 (synthetic, humanised version), kappa L chain}
astkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkvepksc
>d1fvec1 2.1.1.1.26 (1-114) Immunoglobulin (variable domains of L and H chains) {Fab 4D5 (synthetic, humanised version), kappa L chain}
diqmtqspsslsasvgdrvtitcrasqdvntavawyqqkpgkapklliysasflesgvps
rfsgsrsgtdftltisslqpedfatyycqqhyttpptfgqgtkveikrtvaaps
>d1fvec2 2.1.1.2.34 (115-214) Immunoglobulin (constant domains of L and H chains) {Fab 4D5 (synthetic, humanised version), kappa L chain}
vfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqdskdstys
lsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1fved1 2.1.1.1.26 (1-121) Immunoglobulin (variable domains of L and H chains) {Fab 4D5 (synthetic, humanised version), kappa L chain}
evqlvesggglvqpggslrlscaasgfnikdtyihwvrqapgkglewvariyptngytry
adsvkgrftisadtskntaylqmnslraedtavyycsrwggdgfyamdywgqgtlvtvss
a
>d1fved2 2.1.1.2.34 (122-223) Immunoglobulin (constant domains of L and H chains) {Fab 4D5 (synthetic, humanised version), kappa L chain}
stkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqssg
lyslssvvtvpssslgtqtyicnvnhkpsntkvdkkvepksc
>d1fvja1 1.42.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {(Escherichia coli)}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1fvja2 3.38.1.3.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) {(Escherichia coli)}
aqyedgkqyttlekpvagapqvleffsffcpycyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsek
>d1fvjb1 1.42.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {(Escherichia coli)}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1fvjb2 3.38.1.3.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) {(Escherichia coli)}
aqyedgkqyttlekpvagapqvleffsffcpycyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsek
>d1fvka1 1.42.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {(Escherichia coli)}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1fvka2 3.38.1.3.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) {(Escherichia coli)}
aqyedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsek
>d1fvkb1 1.42.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {(Escherichia coli)}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1fvkb2 3.38.1.3.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) {(Escherichia coli)}
aqyedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsek
>d1fvl__ 7.19.1.1.2 Flavoridin {Snake (Trimeresurus flavoviridis)}
geecdcgspsnpccdaatcklrpgaqcadglccdqcrfkkkrticriargdfpddrctgl
sndcprwndl
>d1fvpa_ 3.1.13.2.2 non-fluorescent flavoprotein (luxF, FP390) {(Photobacterium phosphoreum)}
mnkwnygvffvnfynkgqqepsktmnnaletlriidedtsiydviniddhylvkkdsedk
klapfitlgeklyvlatsentvdiaakyalplvfkwddineerlkllsfynasaskynkn
idlvrhqlmlhvnvneaetvakeelklyienyvactqpsnfngsidsiiqsnvtgsykdc
lsyvanlagkfdntvdfllcfesmqdqnkkksvmidlnnqvikfrqdnnli
>d1fvpb_ 3.1.13.2.2 non-fluorescent flavoprotein (luxF, FP390) {(Photobacterium phosphoreum)}
mnkwnygvffvnfynkgqqepsktmnnaletlriidedtsiydviniddhylvkkdsedk
klapfitlgeklyvlatsentvdiaakyalplvfkwddineerlkllsfynasaskynkn
idlvrhqlmlhvnvneaetvakeelklyienyvactqpsnfngsidsiiqsnvtgsykdc
lsyvanlagkfdntvdfllcfesmqdqnkkksvmidlnnqvikfrqdnnli
>d1fvx__ 3.14.4.1.7 Flavodoxin {(Clostridium beijerinckii)}
mkivywsgtgntekmaeliakgiiesgkdvntinvsdvnidellnedililgcsamndev
leesefepfieeistkisgkkvalfgsygwgdgkwmrdfeermngygcvvvetplivqne
pdeaeqdciefgkkiani
>d1fwaa_ 4.6.1.1.1 Urease, gamma-subunit {(Klebsiella aerogenes)}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1fwab_ 2.66.2.1.1 Urease, beta-subunit {(Klebsiella aerogenes)}
mipgeyhvkpgqialntgratcrvvvenhgdrpiqvgshyhfaevnpalkfdrqqaagyr
lnipagtavrfepgqkrevelvafaghravfgfrgevmgpl
>d1fwac1 2.69.1.1.1 (2-129,423-475) alpha-Subunit of urease, composite domain {(Klebsiella aerogenes)}
snisrqayadmfgptvgdkvrladtelwieveddlttygeevkfgggkvirdgmgqgqml
aadcvdlvltnalivdhwgivkadigvkdgrifaigkagnpdiqpnvtipigaateviaa
egkivtagXsievgkladlvvwspaffgvkpatvikggmiaiapmgdinasiptpqpvhy
rp
>d1fwac2 3.1.2.2.1 (130-422,476-567) alpha-subunit of urease, catalytic domain {(Klebsiella aerogenes)}
gidthihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagviglxihedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvahhldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf
>d1fwba_ 4.6.1.1.1 Urease, gamma-subunit {(Klebsiella aerogenes)}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1fwbb_ 2.66.2.1.1 Urease, beta-subunit {(Klebsiella aerogenes)}
mipgeyhvkpgqialntgratcrvvvenhgdrpiqvgshyhfaevnpalkfdrqqaagyr
lnipagtavrfepgqkrevelvafaghravfgfrgevmgpl
>d1fwbc1 2.69.1.1.1 (2-129,423-475) alpha-Subunit of urease, composite domain {(Klebsiella aerogenes)}
snisrqayadmfgptvgdkvrladtelwieveddlttygeevkfgggkvirdgmgqgqml
aadcvdlvltnalivdhwgivkadigvkdgrifaigkagnpdiqpnvtipigaateviaa
egkivtagXsievgkladlvvwspaffgvkpatvikggmiaiapmgdinasiptpqpvhy
rp
>d1fwbc2 3.1.2.2.1 (130-422,476-567) alpha-subunit of urease, catalytic domain {(Klebsiella aerogenes)}
gidthihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagviglxihedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvahhldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf
>d1fwca_ 4.6.1.1.1 Urease, gamma-subunit {(Klebsiella aerogenes)}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1fwcb_ 2.66.2.1.1 Urease, beta-subunit {(Klebsiella aerogenes)}
mipgeyhvkpgqialntgratcrvvvenhgdrpiqvgshyhfaevnpalkfdrqqaagyr
lnipagtavrfepgqkrevelvafaghravfgfrgevmgpl
>d1fwcc1 2.69.1.1.1 (2-129,423-475) alpha-Subunit of urease, composite domain {(Klebsiella aerogenes)}
snisrqayadmfgptvgdkvrladtelwieveddlttygeevkfgggkvirdgmgqgqml
aadcvdlvltnalivdhwgivkadigvkdgrifaigkagnpdiqpnvtipigaateviaa
egkivtagXsievgkladlvvwspaffgvkpatvikggmiaiapmgdinasiptpqpvhy
rp
>d1fwcc2 3.1.2.2.1 (130-422,476-567) alpha-subunit of urease, catalytic domain {(Klebsiella aerogenes)}
gidthihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagviglxihedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvahhldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf
>d1fwda_ 4.6.1.1.1 Urease, gamma-subunit {(Klebsiella aerogenes)}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1fwdb_ 2.66.2.1.1 Urease, beta-subunit {(Klebsiella aerogenes)}
mipgeyhvkpgqialntgratcrvvvenhgdrpiqvgshyhfaevnpalkfdrqqaagyr
lnipagtavrfepgqkrevelvafaghravfgfrgevmgpl
>d1fwdc1 2.69.1.1.1 (2-129,423-475) alpha-Subunit of urease, composite domain {(Klebsiella aerogenes)}
snisrqayadmfgptvgdkvrladtelwieveddlttygeevkfgggkvirdgmgqgqml
aadcvdlvltnalivdhwgivkadigvkdgrifaigkagnpdiqpnvtipigaateviaa
egkivtagXsievgkladlvvwspaffgvkpatvikggmiaiapmgdinasiptpqpvhy
rp
>d1fwdc2 3.1.2.2.1 (130-422,476-567) alpha-subunit of urease, catalytic domain {(Klebsiella aerogenes)}
gidthihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagviglxihedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvahhldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf
>d1fwea_ 4.6.1.1.1 Urease, gamma-subunit {(Klebsiella aerogenes)}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1fweb_ 2.66.2.1.1 Urease, beta-subunit {(Klebsiella aerogenes)}
mipgeyhvkpgqialntgratcrvvvenhgdrpiqvgshyhfaevnpalkfdrqqaagyr
lnipagtavrfepgqkrevelvafaghravfgfrgevmgpl
>d1fwec1 2.69.1.1.1 (2-129,423-475) alpha-Subunit of urease, composite domain {(Klebsiella aerogenes)}
snisrqayadmfgptvgdkvrladtelwieveddlttygeevkfgggkvirdgmgqgqml
aadcvdlvltnalivdhwgivkadigvkdgrifaigkagnpdiqpnvtipigaateviaa
egkivtagXsievgkladlvvwspaffgvkpatvikggmiaiapmgdinasiptpqpvhy
rp
>d1fwec2 3.1.2.2.1 (130-422,476-567) alpha-subunit of urease, catalytic domain {(Klebsiella aerogenes)}
gidthihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagviglxihedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvahhldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf
>d1fwfa_ 4.6.1.1.1 Urease, gamma-subunit {(Klebsiella aerogenes)}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1fwfb_ 2.66.2.1.1 Urease, beta-subunit {(Klebsiella aerogenes)}
mipgeyhvkpgqialntgratcrvvvenhgdrpiqvgshyhfaevnpalkfdrqqaagyr
lnipagtavrfepgqkrevelvafaghravfgfrgevmgpl
>d1fwfc1 2.69.1.1.1 (2-129,423-475) alpha-Subunit of urease, composite domain {(Klebsiella aerogenes)}
snisrqayadmfgptvgdkvrladtelwieveddlttygeevkfgggkvirdgmgqgqml
aadcvdlvltnalivdhwgivkadigvkdgrifaigkagnpdiqpnvtipigaateviaa
egkivtagXsievgkladlvvwspaffgvkpatvikggmiaiapmgdinasiptpqpvhy
rp
>d1fwfc2 3.1.2.2.1 (130-422,476-567) alpha-subunit of urease, catalytic domain {(Klebsiella aerogenes)}
gidthihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagviglxihedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvdhhldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf
>d1fwga_ 4.6.1.1.1 Urease, gamma-subunit {(Klebsiella aerogenes)}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1fwgb_ 2.66.2.1.1 Urease, beta-subunit {(Klebsiella aerogenes)}
mipgeyhvkpgqialntgratcrvvvenhgdrpiqvgshyhfaevnpalkfdrqqaagyr
lnipagtavrfepgqkrevelvafaghravfgfrgevmgpl
>d1fwgc1 2.69.1.1.1 (2-129,423-475) alpha-Subunit of urease, composite domain {(Klebsiella aerogenes)}
snisrqayadmfgptvgdkvrladtelwieveddlttygeevkfgggkvirdgmgqgqml
aadcvdlvltnalivdhwgivkadigvkdgrifaigkagnpdiqpnvtipigaateviaa
egkivtagXsievgkladlvvwspaffgvkpatvikggmiaiapmgdinasiptpqpvhy
rp
>d1fwgc2 3.1.2.2.1 (130-422,476-567) alpha-subunit of urease, catalytic domain {(Klebsiella aerogenes)}
gidthihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagviglxihedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvshhldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf
>d1fwha_ 4.6.1.1.1 Urease, gamma-subunit {(Klebsiella aerogenes)}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1fwhb_ 2.66.2.1.1 Urease, beta-subunit {(Klebsiella aerogenes)}
mipgeyhvkpgqialntgratcrvvvenhgdrpiqvgshyhfaevnpalkfdrqqaagyr
lnipagtavrfepgqkrevelvafaghravfgfrgevmgpl
>d1fwhc1 2.69.1.1.1 (2-129,423-475) alpha-Subunit of urease, composite domain {(Klebsiella aerogenes)}
snisrqayadmfgptvgdkvrladtelwieveddlttygeevkfgggkvirdgmgqgqml
aadcvdlvltnalivdhwgivkadigvkdgrifaigkagnpdiqpnvtipigaateviaa
egkivtagXsievgkladlvvwspaffgvkpatvikggmiaiapmgdinasiptpqpvhy
rp
>d1fwhc2 3.1.2.2.1 (130-422,476-567) alpha-subunit of urease, catalytic domain {(Klebsiella aerogenes)}
gidthihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagviglxihedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvyhhldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf
>d1fwia_ 4.6.1.1.1 Urease, gamma-subunit {(Klebsiella aerogenes)}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1fwib_ 2.66.2.1.1 Urease, beta-subunit {(Klebsiella aerogenes)}
mipgeyhvkpgqialntgratcrvvvenhgdrpiqvgshyhfaevnpalkfdrqqaagyr
lnipagtavrfepgqkrevelvafaghravfgfrgevmgpl
>d1fwic1 2.69.1.1.1 (2-129,423-475) alpha-Subunit of urease, composite domain {(Klebsiella aerogenes)}
snisrqayadmfgptvgdkvrladtelwieveddlttygeevkfgggkvirdgmgqgqml
aadcvdlvltnalivdhwgivkadigvkdgrifaigkagnpdiqpnvtipigaateviaa
egkivtagXsievgkladlvvwspaffgvkpatvikggmiaiapmgdinasiptpqpvhy
rp
>d1fwic2 3.1.2.2.1 (130-422,476-567) alpha-subunit of urease, catalytic domain {(Klebsiella aerogenes)}
gidtaihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagviglxihedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvchhldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf
>d1fwja_ 4.6.1.1.1 Urease, gamma-subunit {(Klebsiella aerogenes)}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1fwjb_ 2.66.2.1.1 Urease, beta-subunit {(Klebsiella aerogenes)}
mipgeyhvkpgqialntgratcrvvvenhgdrpiqvgshyhfaevnpalkfdrqqaagyr
lnipagtavrfepgqkrevelvafaghravfgfrgevmgpl
>d1fwjc1 2.69.1.1.1 (2-129,423-475) alpha-Subunit of urease, composite domain {(Klebsiella aerogenes)}
snisrqayadmfgptvgdkvrladtelwieveddlttygeevkfgggkvirdgmgqgqml
aadcvdlvltnalivdhwgivkadigvkdgrifaigkagnpdiqpnvtipigaateviaa
egkivtagXsievgkladlvvwspaffgvkpatvikggmiaiapmgdinasiptpqpvhy
rp
>d1fwjc2 3.1.2.2.1 (130-422,476-567) alpha-subunit of urease, catalytic domain {(Klebsiella aerogenes)}
gidthihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagviglxihedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvchhldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf
>d1fwp__ 4.34.20.1.1 CheY-binding domain of CheA {(Escherichia coli)}
prriilsrlkagevdlleeelghlttltdvvkgadslsailpgdiaedditavlcfviea
dqitfetve
>d1fx1__ 3.14.4.1.2 Flavodoxin {(Desulfovibrio vulgaris)}
pkalivygsttgnteytaetiarqlanagyevdsrdaasveagglfegfdlvllgcstwg
ddsielqddfiplfdsleetgaqgrkvacfgcgdssyeyfcgavdaieeklknlgaeivq
dglridgdpraarddivgwahdvrgai
>d1fxaa_ 4.11.5.1.1 2Fe-2S ferredoxin {Cyanobacterium (Anabaena sp.)}
atfkvtlineaegtkheievpddeyildaaeeqgydlpfscragacstcagklvsgtvdq
sdqsfldddqieagyvltcvayptsdvviqthkeedly
>d1fxab_ 4.11.5.1.1 2Fe-2S ferredoxin {Cyanobacterium (Anabaena sp.)}
atfkvtlineaegtkheievpddeyildaaeeqgydlpfscragacstcagklvsgtvdq
sdqsfldddqieagyvltcvayptsdvviqthkeedly
>d1fxd__ 4.34.1.1.1 Ferredoxin II {(Desulfovibrio gigas)}
pievnddcmaceacveicpdvfemneegdkavvinpdsdldcveeaidscpaeaivrs
>d1fxia_ 4.11.5.1.3 2Fe-2S ferredoxin {cyanobacterium (Aphanothece sacrum)}
asykvtlktpdgdnvitvpddeyildvaeeegldlpyscragacstcagklvsgpapded
qsfldddqiqagyiltcvayptgdcviethkeealy
>d1fxib_ 4.11.5.1.3 2Fe-2S ferredoxin {cyanobacterium (Aphanothece sacrum)}
asykvtlktpdgdnvitvpddeyildvaeeegldlpyscragacstcagklvsgpapded
qsfldddqiqagyiltcvayptgdcviethkeealy
>d1fxic_ 4.11.5.1.3 2Fe-2S ferredoxin {cyanobacterium (Aphanothece sacrum)}
asykvtlktpdgdnvitvpddeyildvaeeegldlpyscragacstcagklvsgpapded
qsfldddqiqagyiltcvayptgdcviethkeealy
>d1fxid_ 4.11.5.1.3 2Fe-2S ferredoxin {cyanobacterium (Aphanothece sacrum)}
asykvtlktpdgdnvitvpddeyildvaeeegldlpyscragacstcagklvsgpapded
qsfldddqiqagyiltcvayptgdcviethkeealy
>d1fxra_ 4.34.1.4.2 Ferredoxin I {Sulfate-reducing bacteria (Desulfovibrio africanus)}
arkfyvdqdeciacescveiapgafamdpeiekayvkdvegasqeeveeamdtcpvqcih
wede
>d1fxrb_ 4.34.1.4.2 Ferredoxin I {Sulfate-reducing bacteria (Desulfovibrio africanus)}
arkfyvdqdeciacescveiapgafamdpeiekayvkdvegasqeeveeamdtcpvqcih
wede
>d1fxya_ 2.35.1.2.27 Coagulation factor Xa-trypsin chimera {Synthetic based on (Homo sapiens)}
ivggynckdgevpwqallineenegfcggtilsefyiltaahclyqakrfkvrvgdrnte
qeeggeavhevevvikhnrftketydfdiavlrlktpitfrmnvapaslptappatgtkc
lisgwgntassgadypdelqcldapvlsqakceasypgkitsnmfcvgfleggkdscqgd
sggpvvcngqlqgvvswgdgcaqknkpgvytkvynyvkwikntiaans
>d1fyc__ 2.65.1.1.5 The ipoyl domain of dihydrolipoamide acetyltransferase {human (Homo sapiens)}
gsnmsypphmqvllpalsptmtmgtvqrwekkvgeklsegdllaeietdkatigfevqee
gylakilvpegtrdvplgtplciivekeadisafadyrptevtdlk
>d1fyna_ 2.24.2.1.2 Fyn proto-oncogene tyrosine kinase, SH3 domain {human (Homo sapiens)}
gtgvtlfvalydyearteddlsfhkgekfqilnssegdwwearslttgetgyipsnyvap
vd
>d1fzab1 1.105.7.1.1 (148-199) Fibrinogen coiled-coil region {Human (Homo sapiens)}
khqlyidetvnsniptnlrvlrsilenlrskiqklesdvsaqmeycrtpctv
>d1fzab2 4.106.1.1.1 (200-459) beta- and gamma-Fibrinogen C-terminal domains {human (Homo sapiens)}
scnipvvsgkeceeiirkggetsemyliqpdssvkpyrvycdmntenggwtviqnrqdgs
vdfgrkwdpykqgfgnvatntdgknycglpgeywlgndkisqltrmgptelliemedwkg
dkvkahyggftvqneankyqisvnkyrgtagnalmdgasqlmgenrtmtihngmffstyd
rdndgwltsdprkqcskedgggwwynrchaanpngryywggqytwdmakhgtddgvvwmn
wkgswysmrkmsmkirpffp
>d1fzac1 1.105.7.1.1 (88-141) Fibrinogen coiled-coil region {Human (Homo sapiens)}
kmleeimkyeasilthdssirylqeiynsnnqkivnlkekvaqleaqcqepckd
>d1fzac2 4.106.1.1.1 (142-396) beta- and gamma-Fibrinogen C-terminal domains {human (Homo sapiens)}
tvqihditgkdcqdiankgakqsglyfikplkanqqflvyceidgsgngwtvfqkrldgs
vdfkknwiqykegfghlsptgttefwlgnekihlistqsaipyalrveledwngrtstad
yamfkvgpeadkyrltyayfaggdagdafdgfdfgddpsdkfftshngmqfstwdndndk
fegncaeqdgsgwwmnkchaghlngvyyqggtyskastpngydngiiwatwktrwysmkk
ttmkiipfnrltige
>d1fzae1 1.105.7.1.1 (148-199) Fibrinogen coiled-coil region {Human (Homo sapiens)}
khqlyidetvnsniptnlrvlrsilenlrskiqklesdvsaqmeycrtpctv
>d1fzae2 4.106.1.1.1 (200-459) beta- and gamma-Fibrinogen C-terminal domains {human (Homo sapiens)}
scnipvvsgkeceeiirkggetsemyliqpdssvkpyrvycdmntenggwtviqnrqdgs
vdfgrkwdpykqgfgnvatntdgknycglpgeywlgndkisqltrmgptelliemedwkg
dkvkahyggftvqneankyqisvnkyrgtagnalmdgasqlmgenrtmtihngmffstyd
rdndgwltsdprkqcskedgggwwynrchaanpngryywggqytwdmakhgtddgvvwmn
wkgswysmrkmsmkirpffp
>d1fzaf1 1.105.7.1.1 (88-141) Fibrinogen coiled-coil region {Human (Homo sapiens)}
kmleeimkyeasilthdssirylqeiynsnnqkivnlkekvaqleaqcqepckd
>d1fzaf2 4.106.1.1.1 (142-396) beta- and gamma-Fibrinogen C-terminal domains {human (Homo sapiens)}
tvqihditgkdcqdiankgakqsglyfikplkanqqflvyceidgsgngwtvfqkrldgs
vdfkknwiqykegfghlsptgttefwlgnekihlistqsaipyalrveledwngrtstad
yamfkvgpeadkyrltyayfaggdagdafdgfdfgddpsdkfftshngmqfstwdndndk
fegncaeqdgsgwwmnkchaghlngvyyqggtyskastpngydngiiwatwktrwysmkk
ttmkiipfnrltige
>d1fzbb1 1.105.7.1.1 (148-199) Fibrinogen coiled-coil region {Human (Homo sapiens)}
khqlyidetvnsniptnlrvlrsilenlrskiqklesdvsaqmeycrtpctv
>d1fzbb2 4.106.1.1.1 (200-459) beta- and gamma-Fibrinogen C-terminal domains {human (Homo sapiens)}
scnipvvsgkeceeiirkggetsemyliqpdssvkpyrvycdmntenggwtviqnrqdgs
vdfgrkwdpykqgfgnvatntdgknycglpgeywlgndkisqltrmgptelliemedwkg
dkvkahyggftvqneankyqisvnkyrgtagnalmdgasqlmgenrtmtihngmffstyd
rdndgwltsdprkqcskedgggwwynrchaanpngryywggqytwdmakhgtddgvvwmn
wkgswysmrkmsmkirpffp
>d1fzbc1 1.105.7.1.1 (88-141) Fibrinogen coiled-coil region {Human (Homo sapiens)}
kmleeimkyeasilthdssirylqeiynsnnqkivnlkekvaqleaqcqepckd
>d1fzbc2 4.106.1.1.1 (142-396) beta- and gamma-Fibrinogen C-terminal domains {human (Homo sapiens)}
tvqihditgkdcqdiankgakqsglyfikplkanqqflvyceidgsgngwtvfqkrldgs
vdfkknwiqykegfghlsptgttefwlgnekihlistqsaipyalrveledwngrtstad
yamfkvgpeadkyrltyayfaggdagdafdgfdfgddpsdkfftshngmqfstwdndndk
fegncaeqdgsgwwmnkchaghlngvyyqggtyskastpngydngiiwatwktrwysmkk
ttmkiipfnrltige
>d1fzbe1 1.105.7.1.1 (148-199) Fibrinogen coiled-coil region {Human (Homo sapiens)}
khqlyidetvnsniptnlrvlrsilenlrskiqklesdvsaqmeycrtpctv
>d1fzbe2 4.106.1.1.1 (200-459) beta- and gamma-Fibrinogen C-terminal domains {human (Homo sapiens)}
scnipvvsgkeceeiirkggetsemyliqpdssvkpyrvycdmntenggwtviqnrqdgs
vdfgrkwdpykqgfgnvatntdgknycglpgeywlgndkisqltrmgptelliemedwkg
dkvkahyggftvqneankyqisvnkyrgtagnalmdgasqlmgenrtmtihngmffstyd
rdndgwltsdprkqcskedgggwwynrchaanpngryywggqytwdmakhgtddgvvwmn
wkgswysmrkmsmkirpffp
>d1fzbf1 1.105.7.1.1 (88-141) Fibrinogen coiled-coil region {Human (Homo sapiens)}
kmleeimkyeasilthdssirylqeiynsnnqkivnlkekvaqleaqcqepckd
>d1fzbf2 4.106.1.1.1 (142-396) beta- and gamma-Fibrinogen C-terminal domains {human (Homo sapiens)}
tvqihditgkdcqdiankgakqsglyfikplkanqqflvyceidgsgngwtvfqkrldgs
vdfkknwiqykegfghlsptgttefwlgnekihlistqsaipyalrveledwngrtstad
yamfkvgpeadkyrltyayfaggdagdafdgfdfgddpsdkfftshngmqfstwdndndk
fegncaeqdgsgwwmnkchaghlngvyyqggtyskastpngydngiiwatwktrwysmkk
ttmkiipfnrltige
>d1g3p_1 2.27.1.1.1 (1-65,91-117) The n-terminal domains of the minor coat protein g3p {fd phage (bacteriophage fd)}
aetvesclakshtensftnvxkddktldryanyegclwnatgvvvctgdetqcygtwvpi
glaipXenegggsegggsegggsegggtkppeygdtpipgytyinpldgtyppgteqn
>d1gab__ 1.8.1.2.1 An albumin-binding domain {(Peptostreptococcus magnus)}
tidqwllknakedaiaelkkagitsdfyfnainkaktveevnalkneilkaha
>d1gado1 3.22.1.3.1 (1-148,313-330) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Escherichia coli)}
ikvgingfgrigrivfraaqkrsdieivaindlldadymaymlkydsthgrfdgtvevkd
ghlivngkkirvtaerdpanlkwdevgvdvvaeatglfltdetarkhitagakkvvmtgp
skdntpmfvkganfdkyagqdivsnasXnetgysnkvldliahisk
>d1gado2 4.42.1.1.1 (149-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Escherichia coli)}
cttnclaplakvindnfgiieglmttvhattatqktvdgpshkdwrggrgasqniipsst
gaakavgkvlpelngkltgmafrvptpnvsvvdltvrlekaatyeqikaavkaaaegemk
gvlgyteddvvstdfngevctsvfdakagialndnfvklvswyd
>d1gadp1 3.22.1.3.1 (1-148,313-330) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Escherichia coli)}
ikvgingfgrigrivfraaqkrsdieivaindlldadymaymlkydsthgrfdgtvevkd
ghlivngkkirvtaerdpanlkwdevgvdvvaeatglfltdetarkhitagakkvvmtgp
skdntpmfvkganfdkyagqdivsnasXnetgysnkvldliahisk
>d1gadp2 4.42.1.1.1 (149-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Escherichia coli)}
cttnclaplakvindnfgiieglmttvhattatqktvdgpshkdwrggrgasqniipsst
gaakavgkvlpelngkltgmafrvptpnvsvvdltvrlekaatyeqikaavkaaaegemk
gvlgyteddvvstdfngevctsvfdakagialndnfvklvswyd
>d1gaeo1 3.22.1.3.1 (1-148,313-330) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Escherichia coli)}
ikvgingfgrigrivfraaqkrsdieivaindlldadymaymlkydsthgrfdgtvevkd
ghlivngkkirvtaerdpanlkwdevgvdvvaeatglfltdetarkhitagakkvvmtgp
skdntpmfvkganfdkyagqdivsnasXtetgysnkvldliahisk
>d1gaeo2 4.42.1.1.1 (149-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Escherichia coli)}
cttnclaplakvindnfgiieglmttvhattatqktvdgpshkdwrggrgasqniipsst
gaakavgkvlpelngkltgmafrvptpnvsvvdltvrlekaatyeqikaavkaaaegemk
gvlgyteddvvstdfngevctsvfdakagialndnfvklvswyd
>d1gaep1 3.22.1.3.1 (1-148,313-330) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Escherichia coli)}
ikvgingfgrigrivfraaqkrsdieivaindlldadymaymlkydsthgrfdgtvevkd
ghlivngkkirvtaerdpanlkwdevgvdvvaeatglfltdetarkhitagakkvvmtgp
skdntpmfvkganfdkyagqdivsnasXtetgysnkvldliahisk
>d1gaep2 4.42.1.1.1 (149-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Escherichia coli)}
cttnclaplakvindnfgiieglmttvhattatqktvdgpshkdwrggrgasqniipsst
gaakavgkvlpelngkltgmafrvptpnvsvvdltvrlekaatyeqikaavkaaaegemk
gvlgyteddvvstdfngevctsvfdakagialndnfvklvswyd
>d1gafh1 2.1.1.1.64 (1-114) Immunoglobulin (variable domains of L and H chains) {Fab 48G7 (mouse/human), kappa L chain}
qvqlqqsgaelvkpgasvklsctasgfnikdtymhwvkqrpkqglewigridpanvdtky
dpkfqdkatitadtsskttylqlssltsedtavyycasyygiywgqgttltvss
>d1gafh2 2.1.1.2.68 (115-217) Immunoglobulin (constant domains of L and H chains) {Fab 48G7 (mouse/human), kappa L chain}
astkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkvepksc
>d1gafl1 2.1.1.1.64 (1-109) Immunoglobulin (variable domains of L and H chains) {Fab 48G7 (mouse/human), kappa L chain}
diqmtqspsslsaslgervsltcrasqeingylgwlqqkpdgtikrliyaastlhsgvpk
rfsgsrsgsdysltisslesedfadyyclqyasyprtfgggtkveikrt
>d1gafl2 2.1.1.2.68 (110-214) Immunoglobulin (constant domains of L and H chains) {Fab 48G7 (mouse/human), kappa L chain}
vaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqdsk
dstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1gah__ 1.81.1.1.1 Glucoamylase {(Aspergillus awamori), variant x100}
atldswlsneatvartailnnigadgawvsgadsgivvaspstdnpdyfytwtrdsglvi
ktlvdlfrngdtdllstiehyissqaiiqgvsnpsgdlssgglgepkfnvdetaytgswg
rpqrdgpalratamigfgqwlldngytsaateivwplvrndlsyvaqywnqtgydlweev
ngssfftiavqhralvegsafatavgsscswcdsqapqilcylqsfwtgsyilanfdssr
sgkdtntllgsihtfdpeagcddstfqpcspralanhkevvdsfrsiytlndglsdseav
avgrypedsyyngnpwflctlaaaeqlydalyqwdkqgsleitdvsldffkalysgaatg
tyssssstyssivsavktfadgfvsivethaasngslseqfdksdgdelsardltwsyaa
lltannrrnsvvppswgetsassvpgtcaatsasgtyssvtvtswpsivat
>d1gai__ 1.81.1.1.1 Glucoamylase {(Aspergillus awamori), variant x100}
atldswlsneatvartailnnigadgawvsgadsgivvaspstdnpdyfytwtrdsglvi
ktlvdlfrngdtdllstiehyissqaiiqgvsnpsgdlssgglgepkfnvdetaytgswg
rpqrdgpalratamigfgqwlldngytsaateivwplvrndlsyvaqywnqtgydlweev
ngssfftiavqhralvegsafatavgsscswcdsqapqilcylqsfwtgsyilanfdssr
sgkdtntllgsihtfdpeagcddstfqpcspralanhkevvdsfrsiytlndglsdseav
avgrypedsyyngnpwflctlaaaeqlydalyqwdkqgsleitdvsldffkalysgaatg
tyssssstyssivsavktfadgfvsivethaasngslseqfdksdgdelsardltwsyaa
lltannrrnsvvppswgetsassvpgtcaatsasgtyssvtvtswpsivatg
>d1gal_1 3.4.1.2.5 (3-324) Glucose oxidase {(Aspergillus niger)}
gieaslltdpkdvsgrtvdyiiagggltglttaarltenpnisvlviesgsyesdrgpii
edlnaygdifgssvdhayetvelatnnqtalirsgnglggstlvnggtwtrphkaqvdsw
etvfgnegwnwdnvaayslqaerarapnakqiaaghyfnaschgvngtvhagprdtgddy
spivkalmsavedrgvptkkdfgcgdphgvsmfpntlhedqvrsdaarewllpnyqrpnl
qvltgqyvgkvllsqngttpravgvefgthkgnthnvyakhevllaagsavsptileysg
igmksileplgidtvvdlpvgl
>d1gal_2 4.12.1.4.1 (518-583) Glucose oxidase {(Aspergillus niger)}
vgtcsmmpkemggvvdnaarvygvqglrvidgsipptqmsshvmtvfyamalkisdaile
dyasmq
>d1gama_ 2.9.1.1.1 gamma-Crystallin {bovine (Bos taurus) isoform II (B)}
tfrmriyerddfrgqmseitadcpslqdrfhltevhslnvlegswvlyempsyrgrqyll
rpgeyrryldwgamnakvgslrrvmd
>d1gamb_ 2.9.1.1.1 gamma-Crystallin {bovine (Bos taurus) isoform II (B)}
tfrmriyerddfrgqmseitadcpslqdrfhltevhslnvlegswvlyempsyrgrqyll
rpgeyrryldwgamnakvgslrrvmd
>d1gana_ 2.21.1.3.3 S-lectin (galectin-1) {toad (Bufo arenarum)}
asagvavtnlnlkpghcveikgsippdckgfavnlgedasnfllhfnarfdlhgdvnkiv
cnskeadawgseqregvfpfqqgaevmvcfeyqtdkiiikfssgdqfsfpvrkvlpsipf
lsleglqfksitte
>d1ganb_ 2.21.1.3.3 S-lectin (galectin-1) {toad (Bufo arenarum)}
asagvavtnlnlkpghcveikgsippdckgfavnlgedasnfllhfnarfdlhgdvnkiv
cnskeadawgseqregvfpfqqgaevmvcfeyqtdkiiikfssgdqfsfpvrkvlpsipf
lsleglqfksitte
>d1gara_ 3.52.1.1.1 Glycinamide ribonucleotide transformylase {(Escherichia coli), k12 strain tx635, with plasmid pjs167}
mnivvlisgngsnlqaiidacktnkikgtvravfsnkadafglerarqagiathtliasa
fdsreaydreliheidmyapdvvvlagfmrilspafvshyagrllnihpsllpkypglht
hrqalengdeehgtsvhfvtdeldggpvilqakvpvfagdsedditarvqtqehaiyplv
iswfadgrlkmhenaawldgqrlppqgya
>d1garb_ 3.52.1.1.1 Glycinamide ribonucleotide transformylase {(Escherichia coli), k12 strain tx635, with plasmid pjs167}
mnivvlisgngsnlqaiidacktnkikgtvravfsnkadafglerarqagiathtliasa
fdsreaydreliheidmyapdvvvlagfmrilspafvshyagrllnihpsllpkypglht
hrqalengdeehgtsvhfvtdeldggpvilqakvpvfagdsedditarvqtqehaiyplv
iswfadgrlkmhenaawldgqrlppqgya
>d1gata_ 7.33.1.1.1 Erythroid transcription factor GATA-1 {chicken (Gallus gallus)}
kragtvcsncqtstttlwrrspmgdpvcnacglyyklhqvnrpltmrkdgiqtrnrkvss
>d1gaua_ 7.33.1.1.1 Erythroid transcription factor GATA-1 {chicken (Gallus gallus)}
kragtvcsncqtstttlwrrspmgdpvcnacglyyklhqvnrpltmrkdgiqtrnrkvss
>d1gav0_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gav1_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gav2_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gav3_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gav4_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gav5_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gav6_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gav7_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gav8_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gav9_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gava_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gavb_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gavc_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gavd_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gave_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gavf_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gavg_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gavh_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gavi_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gavj_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gavk_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gavl_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gavm_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gavn_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gavo_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gavp_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gavq_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gavr_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gavs_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gavt_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gavu_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gavv_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gavw_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gavx_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gavy_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gavz_ 4.46.1.1.2 GA coat protein {(bacteriophage GA)}
atlrsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtviskslaglfkvgnpiaea
issqsgfya
>d1gb1__ 4.11.1.1.1 Immunoglobulin-binding protein G, separate domains {group G streptococcus (Streptomyces griseus)}
mtyklilngktlkgettteavdaataekvfkqyandngvdgewtyddatktftvte
>d1gb4__ 4.11.1.1.1 Immunoglobulin-binding protein G, separate domains {group G streptococcus (Streptomyces griseus)}
mttfkliingktlkgeitieavdaaeaekifkqyandngidgewtyddatktftvte
>d1gbaa_ 2.35.1.1.2 alpha-Lytic protease {(Lysobacter enzymogenes 495)}
anivggieysinnaslcsvgfsvtrgatkgfvtaghcgtvnatariggavvgtfaarvfp
gndrawvsltsaqtllprvangssfvtvrgsteaavgaavcrsgrttgyqcgtitaknvt
anyaegavrgltqgnacagrgdsggswitsagqaqgvmsganvqsngnncgipasqrssl
ferlqpilsqyglslvtg
>d1gbba_ 2.35.1.1.2 alpha-Lytic protease {(Lysobacter enzymogenes 495)}
anivggieysinnaslcsvgfsvtrgatkgfvtaghcgtvnatariggavvgtfaarvfp
gndrawvsltsaqtllprvangssfvtvrgsteaavgaavcrsgrttgyqcgtitaknvt
anyaegavrgltqgnacagrgdsggswitsagqaqgvmsganvqsngnncgipasqrssl
ferlqpilsqyglslvtg
>d1gbca_ 2.35.1.1.2 alpha-Lytic protease {(Lysobacter enzymogenes 495)}
anivggieysinnaslcsvgfsvtrgatkgfvtaghcgtvnatariggavvgtfaarvfp
gndrawvsltsaqtllprvangssfvtvrgsteaavgaavcrsgrttgyqcgtitaknvt
anyaegavrgltqgnacagrgdsggswitsagqaqgvmsganvqsngnncgipasqrssl
ferlqpilsqyglslvtg
>d1gbda_ 2.35.1.1.2 alpha-Lytic protease {(Lysobacter enzymogenes 495)}
anivggieysinnaslcsvgfsvtrgatkgfvtaghcgtvnatariggavvgtfaarvfp
gndrawvsltsaqtllprvangssfvtvrgsteaavgaavcrsgrttgyqcgtitaknvt
anyaegavrgltqgnacagrgdsggswitsagqaqgvmsganvqsngnncgipasqrssl
ferlqpilsqyglslvtg
>d1gbea_ 2.35.1.1.2 alpha-Lytic protease {(Lysobacter enzymogenes 495)}
anivggieysinnaslcsvgfsvtrgatkgfvtaghcgtvnatariggavvgtfaarvfp
gndrawvsltsaqtllprvangssfvtvrgsteaavgaavcrsgrttgyqcgtitaknvt
anyaegavrgltqgnacagrgdsggswitsagqaqgvmsglnvqsngnncgipasqrssl
ferlqpilsqyglslvtg
>d1gbfa_ 2.35.1.1.2 alpha-Lytic protease {(Lysobacter enzymogenes 495)}
anivggieysinnaslcsvgfsvtrgatkgfvtaghcgtvnatariggavvgtfaarvfp
gndrawvsltsaqtllprvangssfvtvrgsteaavgaavcrsgrttgyqcgtitaknvt
anyaegavrgltqgnacagrgdsggswitsagqaqgvmsglnvqsngnncgipasqrssl
ferlqpilsqyglslvtg
>d1gbg__ 2.21.1.2.1 Bacillus 1-3,1-4-beta-glucanase {(Bacillus licheniformis)}
qtggsfyepfnnyntglwqkadgysngnmfnctwrannvsmtslgemrlsltspsynkfd
cgenrsvqtygyglyevnmkpaknvgivssfftytgptdgtpwdeidieflgkdttkvqf
nyytngvgnhekivnlgfdaansyhtyafdwqpnsikwyvdgqlkhtattqipqtpgkim
mnlwngagvdewlgsyngvtplyahynwvrytkr
>d1gbha_ 2.35.1.1.2 alpha-Lytic protease {(Lysobacter enzymogenes 495)}
anivggieysinnaslcsvgfsvtrgatkgfvtaghcgtvnatariggavvgtfaarvfp
gndrawvsltsaqtllprvangssfvtvrgsteaavgaavcrsgrttgyqcgtitaknvt
anyaegavrgltqgnacagrgdsggswitsagqaqgvmsglnvqsngnncgipasqrssl
ferlqpilsqyglslvtg
>d1gbia_ 2.35.1.1.2 alpha-Lytic protease {(Lysobacter enzymogenes 495)}
anivggieysinnaslcsvgfsvtrgatkgfvtaghcgtvnatariggavvgtfaarvfp
gndrawvsltsaqtllprvangssfvtvrgsteaavgaavcrsgrttgyqcgtitaknvt
anyaegavrgltqgnacagrgdsggswitsagqaqgvmsglnvqsngnncgipasqrssl
ferlqpilsqyglslvtg
>d1gbja_ 2.35.1.1.2 alpha-Lytic protease {(Lysobacter enzymogenes 495)}
anivggieysinnaslcsvgfsvtrgatkgfvtaghcgtvnatariggavvgtfaarvfp
gndrawvsltsaqtllprvangssfvtvrgsteaavgaavcrsgrttgyqcgtitaknvt
anyaegavrgltqgnacagrgdsggswitsagqaqgvmsggnvqsngnncgipasqrssl
ferlqpilsqyglslvtg
>d1gbka_ 2.35.1.1.2 alpha-Lytic protease {(Lysobacter enzymogenes 495)}
anivggieysinnaslcsvgfsvtrgatkgfvtaghcgtvnatariggavvgtfaarvfp
gndrawvsltsaqtllprvangssfvtvrgsteaavgaavcrsgrttgyqcgtitaknvt
anyaegavrgltqgnacagrgdsggswitsagqaqgvmsggnvqsngnncgipasqrssl
ferlqpilsqyglslvtg
>d1gbla_ 2.35.1.1.2 alpha-Lytic protease {(Lysobacter enzymogenes 495)}
anivggieysinnaslcsvgfsvtrgatkgfvtaghcgtvnatariggavvgtfaarvfp
gndrawvsltsaqtllprvangssfvtvrgsteaavgaavcrsgrttgyqcgtitaknvt
anyaegavrgltqgnacagrgdsggswitsagqaqgvmsggnvqsngnncgipasqrssl
ferlqpilsqyglslvtg
>d1gbma_ 2.35.1.1.2 alpha-Lytic protease {(Lysobacter enzymogenes 495)}
anivggieysinnaslcsvgfsvtrgatkgfvtaghcgtvnatariggavvgtfaarvfp
gndrawvsltsaqtllprvangssfvtvrgsteaavgaavcrsgrttgyqcgtitaknvt
anyaegavrgltqgnacagrgdsggswitsagqaqgvmsggnvqsngnncgipasqrssl
ferlqpilsqyglslvtg
>d1gbna_ 3.54.1.3.3 Ornithine aminotransferase {Human (Homo sapiens)}
ptsddifereykygahnyhplpvalergkgiylwdvegrkyfdflssysavnqghchpki
vnalksqvdkltltsrafynnvlgeyeeyitklfnyhkvlpmntgveagetacklarkwg
ytvkgiqkykakivfaagnfwgrtlsaissstdptsydgfgpfmpgfdiipyndlpaler
alqdpnvaafmvepiqgeagvvvpdpgylmgvrelctrhqvlfiadeiqtglartgrwla
vdyenvrpdivllgkalsgglypvsavlcdddimltikpgehgstyggnplgcrvaiaal
evleeenlaenadklgiilrnelmklpsdvvtavrgkgllnaiviketkdwdawkvclrl
rdngllakpthgdiirfapplvikedelresieiinktilsf
>d1gbnb_ 3.54.1.3.3 Ornithine aminotransferase {Human (Homo sapiens)}
ptsddifereykygahnyhplpvalergkgiylwdvegrkyfdflssysavnqghchpki
vnalksqvdkltltsrafynnvlgeyeeyitklfnyhkvlpmntgveagetacklarkwg
ytvkgiqkykakivfaagnfwgrtlsaissstdptsydgfgpfmpgfdiipyndlpaler
alqdpnvaafmvepiqgeagvvvpdpgylmgvrelctrhqvlfiadeiqtglartgrwla
vdyenvrpdivllgkalsgglypvsavlcdddimltikpgehgstyggnplgcrvaiaal
evleeenlaenadklgiilrnelmklpsdvvtavrgkgllnaiviketkdwdawkvclrl
rdngllakpthgdiirfapplvikedelresieiinktilsf
>d1gbnc_ 3.54.1.3.3 Ornithine aminotransferase {Human (Homo sapiens)}
ptsddifereykygahnyhplpvalergkgiylwdvegrkyfdflssysavnqghchpki
vnalksqvdkltltsrafynnvlgeyeeyitklfnyhkvlpmntgveagetacklarkwg
ytvkgiqkykakivfaagnfwgrtlsaissstdptsydgfgpfmpgfdiipyndlpaler
alqdpnvaafmvepiqgeagvvvpdpgylmgvrelctrhqvlfiadeiqtglartgrwla
vdyenvrpdivllgkalsgglypvsavlcdddimltikpgehgstyggnplgcrvaiaal
evleeenlaenadklgiilrnelmklpsdvvtavrgkgllnaiviketkdwdawkvclrl
rdngllakpthgdiirfapplvikedelresieiinktilsf
>d1gbqa_ 2.24.2.1.15 Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {mouse (Mus musculus)}
meaiakydfkataddelsfkrgdilkvlneecdqnwykaelngkdgfipknyiemkp
>d1gbra_ 2.24.2.1.15 Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {mouse (Mus musculus)}
gsrrasvgsmeaiakydfkataddelsfkrgdilkvlneecdqnwykaelngkdgfipkn
yiemkphpefivtd
>d1gbs__ 4.2.1.5.2 Lysozyme {Australian black swan (Cygnus atratus)}
rtdcygnvnridttgascktakpeglsycgvpasktiaerdlkamdryktiikkvgeklc
vepaviagiisreshagkvlkngwgdrgngfglmqvdkrshkpqgtwngevhitqgttil
tdfikriqkkfpswtkdqqlkggisaynagagnvrsyarmdigtthddyandvvaraqyy
kqhgy
>d1gbt__ 2.35.1.2.1 Trypsin(ogen) {bovine (Bos taurus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1gbua_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1gbub_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhadklhvdpenfrllgnvlvgvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1gbuc_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1gbud_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhadklhvdpenfrllgnvlvgvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1gbva_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1gbvb_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvgvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1gbvc_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1gbvd_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvgvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1gc1c1 2.1.1.1.3 (1-97) CD4 {human (Homo sapiens)}
kkvvlgkkgdtveltctasqkksiqfhwknsnqikilgnqgsfltkgpsklndradsrrs
lwdqgnfpliiknlkiedsdtyicevedqkeevqllv
>d1gc1c2 2.1.1.3.4 (98-181) CD4 {human (Homo sapiens)}
fgltansdthllqgqsltltlesppgsspsvqcrsprgkniqggktlsvsqlelqdsgtw
tctvlqnqkkvefkidivvlafqk
>d1gc1g_ 4.108.1.1.1 gp120 core {HIV-1 (Human immunodeficiency virus type 1)}
tenfnmwkndmveqmhediislwdqslkpcvkltplcvgagscntsvitqacpkvsfepi
pihycapagfailkcnnktfngtgpctnvstvqcthgirpvvstqlllngslaeeevvir
svnftdnaktiivqlntsveinctgaghcnisrakwnntlkqiasklreqfgnnktiifk
qssggdpeivthsfncggeffycnstqlfnstwfnstwstkgsnntegsdtitlpcrikq
iinmwqkvgkamyappisgqircssnitgllltrdggnsnneseifrpgggdmrdnwrse
lykykvvkie
>d1gc1h1 2.1.1.1.104 (1-129) Immunoglobulin (variable domains of L and H chains) {HIV-1 neutralizing Fab 17B (human), kappa L chain}
qvqllesgaevkkpgssvkvsckasgdtfirysftwvrqapgqglewmgriitildvahy
aphlqgrvtitadkststvylelrnlrsddtavyfcagvyegeadegeydnngflkhwgq
gtlvtvtsa
>d1gc1h2 2.1.1.2.102 (130-229) Immunoglobulin (constant domains of L and H chains) {HIV-1 neutralizing Fab 17B (human), kappa L chain}
stkgpsvfplapsskstsggtaalgclvkdyfpqpvtvswnsgaltsgvhtfpavlqssg
lyslssvvtvpssslgtqtyicnvnhkpsntkvdkkvepk
>d1gc1l1 2.1.1.1.104 (1-109) Immunoglobulin (variable domains of L and H chains) {HIV-1 neutralizing Fab 17B (human), kappa L chain}
eleltqspatlsvspgeratlscrasesvssdlawyqqkpgqaprlliygastratgvpa
rfsgsgsgaeftltisslqsedfavyycqqynnwpprytfgqgtrleik
>d1gc1l2 2.1.1.2.102 (110-213) Immunoglobulin (constant domains of L and H chains) {HIV-1 neutralizing Fab 17B (human), kappa L chain}
rtvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqd
skdstyslsstltlskadyekhkvyacevthqglsspvtksfnr
>d1gca__ 3.81.1.1.4 Galactose/glucose-binding protein {(Salmonella typhimurium), strain lt2}
adtrigvtiykyddnfmsvvrkaiekdgksapdvqllmndsqndqskqndqidvllakgv
kalainlvdpaaagtviekargqnvpvvffnkepsrkaldsydkayyvgtdskesgviqg
dliakhwqanqgwdlnkdgkiqyvllkgepghpdaearttyvvkelndkgiqteqlaldt
amwdtaqakdkmdawlsgpnankievvianndamamgavealkahnkssipvfgvdalpe
alalvksgamagtvlndannqakatfdlaknlaegkgaadgtswkienkivrvpyvgvdk
dnlseftqk
>d1gcb__ 4.3.1.1.9 Bleomycin hydrolase, Gal6 {Baker's yeast (Saccharomyces cerevisiae)}
sssidiskinswnkefqsdlthqlattvlknynaddallnktrlqkqdnrvfntvvstds
tpvtnqkssgrcwlfaatnqlrlnvlselnlkefelsqaylffydklekanyfldqivss
adqdidsrlvqyllaaptedggqysmflnlvkkyglipkdlygdlpysttasrkwnsllt
tklrefaetlrtalkersaddsiivtlreqmqreifrlmslfmdippvqpneqftweyvd
kdkkihtikstplefaskyakldpstpvslindprhpygklikidrlgnvlggdaviyln
vdnetlsklvvkrlqnnkavffgshtpkfmdkktgvmdielwnypaigynlpqqkasrir
yheslmthamlitgchvdetsklplryrvenswgkdsgkdglyvmtqkyfeeycfqivvd
inelpkelaskftsgkeepivlpiwdpmgala
>d1gcd__ 2.35.1.2.7 (alpha, gamma-)chymotrypsin(ogen) {bovine (Bos taurus)}
cgvpaiqpvlsglsrivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgv
ttsdvvvagefdqgsssekiqklkiakvfknskynsltinnditllklstaasfsqtvsa
vclpsasddfaagttcvttgwgltrytnantpdrlqqaslpllsntnckkywgtkikdam
icagasgvsscmgdsggplvckkngawtlvgivswgsstcststpgvyarvtalvnwvqq
tlaan
>d1gcf__ 2.1.2.1.10 Granulocyte colony-stimulating factor (GC-SF) receptor {mouse (Mus musculus)}
gssleppmlqaldigpdvvshqpgclwlswkpwkpseymeqecelryqpqlkganwtlvf
hlpsskdqfelcglhqapvytlqmrcirsslpgfwspwspglqlrptmk
>d1gcg__ 3.81.1.1.4 Galactose/glucose-binding protein {(Salmonella typhimurium), strain lt2}
adtrigvtiykyddnfmsvvrkaiekdgksapdvqllmndsqndqskqndqidvllakgv
kalainlvdpaaagtviekargqnvpvvffnkepsrkaldsydkayyvgtdskesgviqg
dliakhwqanqgwdlnkdgkiqyvllkgepghpdaearttyvvkelndkgiqteqlaldt
amwdtaqakdkmdawlsgpnankievvianndamamgavealkahnkssipvfgvdalpe
alalvksgamagtvlndannqakatfdlaknlaegkgaadgtswkienkivrvpyvgvdk
dnlseftqk
>d1gcla_ 1.105.2.1.1 GCN4 {Yeast (Saccharomyces cerevisiae)}
xrmkqiedkleeilsklyhienelarikkllg
>d1gclb_ 1.105.2.1.1 GCN4 {Yeast (Saccharomyces cerevisiae)}
xrmkqiedkleeilsklyhienelarikkllg
>d1gclc_ 1.105.2.1.1 GCN4 {Yeast (Saccharomyces cerevisiae)}
xrmkqiedkleeilsklyhienelarikkllg
>d1gcld_ 1.105.2.1.1 GCN4 {Yeast (Saccharomyces cerevisiae)}
xrmkqiedkleeilsklyhienelarikkllg
>d1gcma_ 1.105.2.1.1 GCN4 {Yeast (Saccharomyces cerevisiae)}
xrmkqiedkieeilskiyhieneiarikklig
>d1gcmb_ 1.105.2.1.1 GCN4 {Yeast (Saccharomyces cerevisiae)}
xrmkqiedkieeilskiyhieneiarikklige
>d1gcmc_ 1.105.2.1.1 GCN4 {Yeast (Saccharomyces cerevisiae)}
xrmkqiedkieeilskiyhieneiarikkliger
>d1gcs_1 2.9.1.1.1 (1-85) gamma-Crystallin {bovine (Bos taurus) isoform II (B)}
gkitfyedrgfqghcyecssdcpnlqpyfsrcnsirvdsgcwmlyerpnyqghqyflrrg
dypdyqqwmgfndsirscrlipqht
>d1gcs_2 2.9.1.1.1 (86-174) gamma-Crystallin {bovine (Bos taurus) isoform II (B)}
gtfrmriyerddfrgqmseitddcpslqdrfhltevhslnvlegswvlyempsyrgrqyl
lrpgeyrryldwgamnakvgslrrvmdfy
>d1gcta_ 2.35.1.2.7 (alpha, gamma-)chymotrypsin(ogen) {bovine (Bos taurus)}
cgvpaiqpvlsglxxivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgv
ttsdvvvagefdqgsssekiqklkiakvfknskynsltinnditllklstaasfsqtvsa
vclpsasddfaagttcvttgwgltryxxantpdrlqqaslpllsntnckkywgtkikdam
icagasgvsscmgdsggplvckkngawtlvgivswgsstcststpgvyarvtalvnwvqq
tlaan
>d1gd1o1 3.22.1.3.2 (1-148,313-333) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Bacillus stearothermophilus /nca 1503)}
vkvgingfgrigrnvfraalknpdievvavndltdantlahllkydsvhgrldaevsvng
nnlvvngkeiivkaerdpenlawgeigvdivvestgrftkredaakhleagakkviisap
akneditivmgvnqdkydpkahhvisnasXnetgyshrvvdlaayiaskgl
>d1gd1o2 4.42.1.1.2 (149-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Bacillus stearothermophilus /nca 1503)}
cttnclapfakvlheqfgivrgmmttvhsytndqrildlphkdlrraraaaesiiptttg
aakavalvlpelkgklngmamrvptpnvsvvdlvaelekevtveevnaalkaaaegelkg
ilayseeplvsrdyngstvsstidalstmvidgkmvkvvswyd
>d1gd1p1 3.22.1.3.2 (1-148,313-333) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Bacillus stearothermophilus /nca 1503)}
vkvgingfgrigrnvfraalknpdievvavndltdantlahllkydsvhgrldaevsvng
nnlvvngkeiivkaerdpenlawgeigvdivvestgrftkredaakhleagakkviisap
akneditivmgvnqdkydpkahhvisnasXnetgyshrvvdlaayiaskgl
>d1gd1p2 4.42.1.1.2 (149-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Bacillus stearothermophilus /nca 1503)}
cttnclapfakvlheqfgivrgmmttvhsytndqrildlphkdlrraraaaesiiptttg
aakavalvlpelkgklngmamrvptpnvsvvdlvaelekevtveevnaalkaaaegelkg
ilayseeplvsrdyngstvsstidalstmvidgkmvkvvswyd
>d1gd1q1 3.22.1.3.2 (1-148,313-333) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Bacillus stearothermophilus /nca 1503)}
vkvgingfgrigrnvfraalknpdievvavndltdantlahllkydsvhgrldaevsvng
nnlvvngkeiivkaerdpenlawgeigvdivvestgrftkredaakhleagakkviisap
akneditivmgvnqdkydpkahhvisnasXnetgyshrvvdlaayiaskgl
>d1gd1q2 4.42.1.1.2 (149-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Bacillus stearothermophilus /nca 1503)}
cttnclapfakvlheqfgivrgmmttvhsytndqrildlphkdlrraraaaesiiptttg
aakavalvlpelkgklngmamrvptpnvsvvdlvaelekevtveevnaalkaaaegelkg
ilayseeplvsrdyngstvsstidalstmvidgkmvkvvswyd
>d1gd1r1 3.22.1.3.2 (1-148,313-333) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Bacillus stearothermophilus /nca 1503)}
vkvgingfgrigrnvfraalknpdievvavndltdantlahllkydsvhgrldaevsvng
nnlvvngkeiivkaerdpenlawgeigvdivvestgrftkredaakhleagakkviisap
akneditivmgvnqdkydpkahhvisnasXnetgyshrvvdlaayiaskgl
>d1gd1r2 4.42.1.1.2 (149-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Bacillus stearothermophilus /nca 1503)}
cttnclapfakvlheqfgivrgmmttvhsytndqrildlphkdlrraraaaesiiptttg
aakavalvlpelkgklngmamrvptpnvsvvdlvaelekevtveevnaalkaaaegelkg
ilayseeplvsrdyngstvsstidalstmvidgkmvkvvswyd
>d1gdc__ 7.33.1.2.4 Glucocorticoid receptor DNA-binding domain {rat (Rattus norvegicus)}
lclvcsdeasgchygvltcgsckvffkravegqhnylcagrndciidkirrkncpacryr
kclqagmnlear
>d1gdd_1 1.56.1.1.2 (61-181) Transducin (alpha subunit), insertion domain {rat (Rattus rattus)}
yseeeckqykavvysntiqsiiaiiramgrlkidfgdaaraddarqlfvlagaaeegfmt
aelagvikrlwkdsgvqacfnrsreyqlndsaayylndldriaqpnyiptqqdvlrtrvk
t
>d1gdd_2 3.29.1.4.12 (9-60,182-354) Transducin (alpha subunit) {rat (Rattus rattus)}
dkaaverskmidrnlredgekaarevkllllgagesgkstivkqmkiiheagXtgiveth
ftfkdlhfkmfdvggqrserkkwihcfegvtaiifcvalsdydlvlaedeemnrmhesmk
lfdsicnnkwftdtsiilflnkkdlfeekikksplticypeyagsntyeeaaayiqcqfe
dlnkrkdtkeiythftcatdtknvqfvfdavtdviiknnlkdcglf
>d1gdf__ 2.1.1.5.16 Rho GDP-dissociation inhibitor 1, RhoGDI {Bovine (Bos taurus)}
avsadpnvpnvvvtrltlvcstapgpleldltgdlesfkkqsfvlkegveyrikisfrvn
reivsgmkyiqhtyrkgvkidktdymvgsygpraeeyefltpmeeapkgmlargsyniks
rftdddrtdhlswewnltikkewkd
>d1gdha1 3.14.9.1.3 (2-100,292-321) D-glycerate dehydrogenase {(Hyphomicrobium methylovorum)}
kkkilitwplpeaamararesydviahgddpkitidemietaksvdallitlnekcrkev
idripenikcistysigfdhidldackargikvgnaphgXatqaredmahqandlidalf
ggadmsyala
>d1gdha2 3.22.1.4.3 (101-291) D-glycerate dehydrogenase {(Hyphomicrobium methylovorum)}
vtvataeiamllllgsarragegekmirtrswpgweplelvgekldnktlgiygfgsigq
alakraqgfdmdidyfdthrasssdeasyqatfhdsldsllsvsqffslnapstpetryf
fnkatikslpqgaivvntargdlvdnelvvaaleagrlayagfdvfagepninegyydlp
ntflfphigsa
>d1gdhb1 3.14.9.1.3 (2-100,292-321) D-glycerate dehydrogenase {(Hyphomicrobium methylovorum)}
kkkilitwplpeaamararesydviahgddpkitidemietaksvdallitlnekcrkev
idripenikcistysigfdhidldackargikvgnaphgXatqaredmahqandlidalf
ggadmsyala
>d1gdhb2 3.22.1.4.3 (101-291) D-glycerate dehydrogenase {(Hyphomicrobium methylovorum)}
vtvataeiamllllgsarragegekmirtrswpgweplelvgekldnktlgiygfgsigq
alakraqgfdmdidyfdthrasssdeasyqatfhdsldsllsvsqffslnapstpetryf
fnkatikslpqgaivvntargdlvdnelvvaaleagrlayagfdvfagepninegyydlp
ntflfphigsa
>d1gdi__ 1.1.1.1.14 Leghemoglobin {yellow lupin (Lupinus luteus l)}
galtesqaalvkssweefnanipkhthrffilvleiapaakdlfsflkgtsevpqnnpel
qahagkvfklvyeaaiqlevtgvvvtdatlknlgsvhvskgvadahfpvvkeailktike
vvgakwseelnsawtiaydelaivikkemddaa
>d1gdj__ 1.1.1.1.14 Leghemoglobin {yellow lupin (Lupinus luteus l)}
galtesqaalvkssweefnanipkhthrffilvleiapaakdlfsflkgtsevpqnnpel
qahagkvfklvyeaaiqlevtgvvvtdatlknlgsvhvskgvadahfpvvkeailktike
vvgakwseelnsawtiaydelaivikkemddaa
>d1gdk__ 1.1.1.1.14 Leghemoglobin {yellow lupin (Lupinus luteus l)}
galtesqaalvkssweefnanipkhthrffilvleiapaakdlfsflkgtsevpqnnpel
qahagkvfklvyeaaiqlevtgvvvtdatlknlgsvhvskgvadahfpvvkeailktike
vvgakwseelnsawtiaydelaivikkemddaa
>d1gdl__ 1.1.1.1.14 Leghemoglobin {yellow lupin (Lupinus luteus l)}
galtesqaalvkssweefnanipkhthrffilvleiapaakdlfsflkgtsevpqnnpel
qahagkvfklvyeaaiqlevtgvvvtdatlknlgsvhvskgvadahfpvvkeailktike
vvgakwseelnsawtiaydelaivikkemddaa
>d1gdoa_ 4.95.1.1.1 Glucosamine 6-phosphate synthase, N-terminal domain {(Escherichia coli)}
cgivgaiaqrdvaeilleglrrleyrgydsaglavvdaeghmtrlrrlgkvqmlaqaaee
hplhggtgiahtrwathgepsevnahphvsehivvvhngiienheplreelkargytfvs
etdteviahlvnwelkqggtlreavlraipqlrgaygtvimdsrhpdtllaarsgsplvi
glgmgenfiasdqlallpvtrrfifleegdiaeitrrsvnifdktgaevkrqdiesnl
>d1gdob_ 4.95.1.1.1 Glucosamine 6-phosphate synthase, N-terminal domain {(Escherichia coli)}
cgivgaiaqrdvaeilleglrrleyrgydsaglavvdaeghmtrlrrlgkvqmlaqaaee
hplhggtgiahtrwathgepsevnahphvsehivvvhngiienheplreelkargytfvs
etdteviahlvnwelkqggtlreavlraipqlrgaygtvimdsrhpdtllaarsgsplvi
glgmgenfiasdqlallpvtrrfifleegdiaeitrrsvnifdktgaevkrqdiesnlq
>d1gdoc_ 4.95.1.1.1 Glucosamine 6-phosphate synthase, N-terminal domain {(Escherichia coli)}
cgivgaiaqrdvaeilleglrrleyrgydsaglavvdaeghmtrlrrlgkvqmlaqaaee
hplhggtgiahtrwathgepsevnahphvsehivvvhngiienheplreelkargytfvs
etdteviahlvnwelkqggtlreavlraipqlrgaygtvimdsrhpdtllaarsgsplvi
glgmgenfiasdqlallpvtrrfifleegdiaeitrrsvnifdktgaevkrqdiesnl
>d1gdod_ 4.95.1.1.1 Glucosamine 6-phosphate synthase, N-terminal domain {(Escherichia coli)}
cgivgaiaqrdvaeilleglrrleyrgydsaglavvdaeghmtrlrrlgkvqmlaqaaee
hplhggtgiahtrwathgepsevnahphvsehivvvhngiienheplreelkargytfvs
etdteviahlvnwelkqggtlreavlraipqlrgaygtvimdsrhpdtllaarsgsplvi
glgmgenfiasdqlallpvtrrfifleegdiaeitrrsvnifdktgaevkrqdiesnlq
>d1gdr__ 3.44.1.1.1 gamma,delta resolvase, large fragment {(Escherichia coli)}
mrlfgyarvstsqqsldiqvralkdagvkanriftdkasgsssdrkgldllrmkveegdv
ilvkkldrlgrdtadmiqlikefdaqgvsirfiddgistdgemgkmvvtilsava
>d1gds__ 1.61.1.1.1 HIV-1 capsid protein, N-terminal core domain {Human immunodeficiency virus type 1 (HIV-1)}
pivqnlqgqmvhqaisprtlnawvkvveekafspevipmfsalsegatpqdlntmlntvg
ghqaamqmlketineeaaewdrlhpvhagpiapgqmreprgsdiagttstlqeqigwmth
nppipvgeiykrwiilglnkivrmysptsil
>d1gdta1 1.4.1.2.2 (141-183) gamma,delta resolvase (C-terminal domain) {(Escherichia coli)}
grkrkidrdavlnmwqqglgashisktmniarstvykvinesn
>d1gdta2 3.44.1.1.1 (1-140) gamma,delta resolvase, large fragment {(Escherichia coli)}
mrlfgyarvstsqqsldiqvralkdagvkanriftdkasgsssdrkgldllrmkveegdv
ilvkkldrlgrdtadmiqlikefdaqgvsirfiddgistdgemgkmvvtilsavaqaerq
rilertnegrqeamakgvvf
>d1gdtb1 1.4.1.2.2 (141-183) gamma,delta resolvase (C-terminal domain) {(Escherichia coli)}
grkrkidrdavlnmwqqglgashisktmniarstvykvinesn
>d1gdtb2 3.44.1.1.1 (1-140) gamma,delta resolvase, large fragment {(Escherichia coli)}
mrlfgyarvstsqqsldiqvralkdagvkanriftdkasgsssdrkgldllrmkveegdv
ilvkkldrlgrdtadmiqlikefdaqgvsirfiddgistdgemgkmvvtilsavaqaerq
rilertnegrqeamakgvvf
>d1gdy__ 1.61.1.1.1 HIV-1 capsid protein, N-terminal core domain {Human immunodeficiency virus type 1 (HIV-1)}
pivqnlqgqmvhqaisprtlnawvkvveekafspevipmfsalsegatpqdlntmlntvg
ghqaamqmlketineeaaewdrlhpvhagpiapgqmreprgsdiagttstlqeqigwmth
nppipvgeiykrwiilglnkivrmysptsil
>d1gdz__ 1.61.1.1.1 HIV-1 capsid protein, N-terminal core domain {Human immunodeficiency virus type 1 (HIV-1)}
pivqnlqgqmvhqaisprtlnawvkvveekafspevipmfsalsegatpqdlntmlntvg
ghqaamqmlketineeaaewdrlhpvhagpiapgqmreprgsdiagttstlqeqigwmth
nppipvgeiykrwiilglnkivrmysptsil
>d1gece_ 4.3.1.1.7 Glycyl endopeptidase {papaya (Carica papaya)}
lpesvdwrakgavtpvkhqgycescwafstvatveginkiktgnlvelseqelvdcdlqs
ygcnrgyqstslqyvaqngihlrakypyiakqqtcranqvggpkvktngvgrvqsnnegs
llnaiahqpvsvvvesagrdfqnykggifegscgtkvdhavtavgygksggkgyilikns
wgpgwgengyirirrasgnspgvcgvyrssyypikn
>d1gen__ 2.49.1.1.2 Gelatinase A (MMP-2), C-terminal domain {human (Homo sapiens)}
lgpvtpeickqdivfdgiaqirgeifffkdrfiwrtvtprdkpmgpllvatfwpelpeki
davyeapqeekavffagneywiysastlergypkpltslglppdvqrvdaafnwsknkkt
yifagdkfwrynevkkkmdpgfpkliadawnaipdnldavvdlqggghsyffkgayylkl
enqslksvkfgsiksdwlgc
>d1gera1 3.4.1.4.2 (3-146,263-335) Glutathione reductase {(Escherichia coli)}
khydyiaigggsggiasinraamygqkcalieakelggtcvnvgcvpkkvmwhaaqirea
ihmygpdygfdttinkfnwetliasrtayidrihtsyenvlgknnvdvikgfarfvdakt
levngetitadhiliatggrpshpXrepandninleaagvktnekgyivvdkyqntnieg
iyavgdntgaveltpvavaagrrlserlfnnkpdehld
>d1gera2 3.4.1.4.2 (147-262) Glutathione reductase {(Escherichia coli)}
dipgveygidsdgffalpalpervavvgagyiavelagvinglgakthlfvrkhaplrsf
dpmisetlvevmnaegpqlhtnaipkavvkntdgsltleledgrsetvdcliwaig
>d1gera3 4.48.1.1.2 (336-450) Glutathione reductase {(Escherichia coli)}
ysniptvvfshppigtvgltepqareqygddqvkvykssftamytavtthrqpcrmklvc
vgseekivgihgigfgmdemlqgfavalkmgatkkdfdntvaihptaaeefvtmr
>d1gerb1 3.4.1.4.2 (2-146,263-335) Glutathione reductase {(Escherichia coli)}
tkhydyiaigggsggiasinraamygqkcalieakelggtcvnvgcvpkkvmwhaaqire
aihmygpdygfdttinkfnwetliasrtayidrihtsyenvlgknnvdvikgfarfvdak
tlevngetitadhiliatggrpshpXrepandninleaagvktnekgyivvdkyqntnie
giyavgdntgaveltpvavaagrrlserlfnnkpdehld
>d1gerb2 3.4.1.4.2 (147-262) Glutathione reductase {(Escherichia coli)}
dipgveygidsdgffalpalpervavvgagyiavelagvinglgakthlfvrkhaplrsf
dpmisetlvevmnaegpqlhtnaipkavvkntdgsltleledgrsetvdcliwaig
>d1gerb3 4.48.1.1.2 (336-450) Glutathione reductase {(Escherichia coli)}
ysniptvvfshppigtvgltepqareqygddqvkvykssftamytavtthrqpcrmklvc
vgseekivgihgigfgmdemlqgfavalkmgatkkdfdntvaihptaaeefvtmr
>d1gesa1 3.4.1.4.2 (3-146,263-335) Glutathione reductase {(Escherichia coli)}
khydyiaigggsggiasinraamygqkcalieakelggtcvnvgcvpkkvmwhaaqirea
ihmygpdygfdttinkfnwetliasrtayidrihtsyenvlgknnvdvikgfarfvdakt
levngetitadhiliatggrpshpXrepandninleaagvktnekgyivvdkyqntnieg
iyavgdntgaveltpvavaagrrlserlfnnkpdehld
>d1gesa2 3.4.1.4.2 (147-262) Glutathione reductase {(Escherichia coli)}
dipgveygidsdgffalpalpervavvgagyigvelggvinglgakthlfemfdaplpsf
dpmisetlvevmnaegpqlhtnaipkavvkntdgsltleledgrsetvdcliwaig
>d1gesa3 4.48.1.1.2 (336-450) Glutathione reductase {(Escherichia coli)}
ysniptvvfshppigtvgltepqareqygddqvkvykssftamytavtthrqpcrmklvc
vgseekivgihgigfgmdemlqgfavalkmgatkkdfdntvaihptaaeefvtmr
>d1gesb1 3.4.1.4.2 (2-146,263-335) Glutathione reductase {(Escherichia coli)}
tkhydyiaigggsggiasinraamygqkcalieakelggtcvnvgcvpkkvmwhaaqire
aihmygpdygfdttinkfnwetliasrtayidrihtsyenvlgknnvdvikgfarfvdak
tlevngetitadhiliatggrpshpXrepandninleaagvktnekgyivvdkyqntnie
giyavgdntgaveltpvavaagrrlserlfnnkpdehld
>d1gesb2 3.4.1.4.2 (147-262) Glutathione reductase {(Escherichia coli)}
dipgveygidsdgffalpalpervavvgagyigvelggvinglgakthlfemfdaplpsf
dpmisetlvevmnaegpqlhtnaipkavvkntdgsltleledgrsetvdcliwaig
>d1gesb3 4.48.1.1.2 (336-450) Glutathione reductase {(Escherichia coli)}
ysniptvvfshppigtvgltepqareqygddqvkvykssftamytavtthrqpcrmklvc
vgseekivgihgigfgmdemlqgfavalkmgatkkdfdntvaihptaaeefvtmr
>d1geta1 3.4.1.4.2 (3-146,263-335) Glutathione reductase {(Escherichia coli)}
khydyiaigggsggiasinraamygqkcalieakelggtcvnvgcvpkkvmwhaaqirea
ihmygpdygfdttinkfnwetliasrtayidrihtsyenvlgknnvdvikgfarfvdakt
levngetitadhiliatggrpshpXrepandninleaagvktnekgyivvdkyqntnieg
iyavgdntgaveltpvavaagrrlserlfnnkpdehld
>d1geta2 3.4.1.4.2 (147-262) Glutathione reductase {(Escherichia coli)}
dipgveygidsdgffalpalpervavvgagyiavelagvinglgakthlfvrkhaplrsf
dpmisetlvevmnaegpqlhtnaipkavvkntdgsltleledgrsetvdcliwaig
>d1geta3 4.48.1.1.2 (336-450) Glutathione reductase {(Escherichia coli)}
ysniptvvfshppigtvgltepqareqygddqvkvykssftamytavtthrqpcrmklvc
vgseekivgihgigfgmdemlqgfavalkmgatkkdfdntvaihptaaeefvtmr
>d1getb1 3.4.1.4.2 (2-146,263-335) Glutathione reductase {(Escherichia coli)}
tkhydyiaigggsggiasinraamygqkcalieakelggtcvnvgcvpkkvmwhaaqire
aihmygpdygfdttinkfnwetliasrtayidrihtsyenvlgknnvdvikgfarfvdak
tlevngetitadhiliatggrpshpXrepandninleaagvktnekgyivvdkyqntnie
giyavgdntgaveltpvavaagrrlserlfnnkpdehld
>d1getb2 3.4.1.4.2 (147-262) Glutathione reductase {(Escherichia coli)}
dipgveygidsdgffalpalpervavvgagyiavelagvinglgakthlfvrkhaplrsf
dpmisetlvevmnaegpqlhtnaipkavvkntdgsltleledgrsetvdcliwaig
>d1getb3 4.48.1.1.2 (336-450) Glutathione reductase {(Escherichia coli)}
ysniptvvfshppigtvgltepqareqygddqvkvykssftamytavtthrqpcrmklvc
vgseekivgihgigfgmdemlqgfavalkmgatkkdfdntvaihptaaeefvtmr
>d1geua1 3.4.1.4.2 (3-146,263-335) Glutathione reductase {(Escherichia coli)}
khydyiaigggsggiasinraamygqkcalieakelggtcvnvgcvpkkvmwhaaqirea
ihmygpdygfdttinkfnwetliasrtayidrihtsyenvlgknnvdvikgfarfvdakt
levngetitadhiliatggrpshpXrepandninleaagvktnekgyivvdkyqntnieg
iyavgdntgaveltpvavaagrrlserlfnnkpdehld
>d1geua2 3.4.1.4.2 (147-262) Glutathione reductase {(Escherichia coli)}
dipgveygidsdgffalpalpervavvgagyigvelggvinglgakthlfemfdaplpsf
dpmisetlvevmnaegpqlhtnaipkavvkntdgsltleledgrsetvdcliwaig
>d1geua3 4.48.1.1.2 (336-450) Glutathione reductase {(Escherichia coli)}
ysniptvvfshppigtvgltepqareqygddqvkvykssftamytavtthrqpcrmklvc
vgseekivgihgigfgmdemlqgfavalkmgatkkdfdntvaihptaaeefvtmr
>d1geub1 3.4.1.4.2 (2-146,263-335) Glutathione reductase {(Escherichia coli)}
tkhydyiaigggsggiasinraamygqkcalieakelggtcvnvgcvpkkvmwhaaqire
aihmygpdygfdttinkfnwetliasrtayidrihtsyenvlgknnvdvikgfarfvdak
tlevngetitadhiliatggrpshpXrepandninleaagvktnekgyivvdkyqntnie
giyavgdntgaveltpvavaagrrlserlfnnkpdehld
>d1geub2 3.4.1.4.2 (147-262) Glutathione reductase {(Escherichia coli)}
dipgveygidsdgffalpalpervavvgagyigvelggvinglgakthlfemfdaplpsf
dpmisetlvevmnaegpqlhtnaipkavvkntdgsltleledgrsetvdcliwaig
>d1geub3 4.48.1.1.2 (336-450) Glutathione reductase {(Escherichia coli)}
ysniptvvfshppigtvgltepqareqygddqvkvykssftamytavtthrqpcrmklvc
vgseekivgihgigfgmdemlqgfavalkmgatkkdfdntvaihptaaeefvtmr
>d1gfc__ 2.24.2.1.14 Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {human (Homo sapiens)}
gstyvqalfdfdpqedgelgfrrgdfihvmdnsdpnwwkgachgqtgmfprnyvtpvnr
>d1gfd__ 2.24.2.1.14 Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {human (Homo sapiens)}
gstyvqalfdfdpqedgelgfrrgdfihvmdnsdpnwwkgachgqtgmfprnyvtpvnr
>d1gff1_ 2.8.1.1.2 Bacteriophage capsid proteins {(bacteriophage G4)}
vphdlshlvfeagkigrlktiswtpvvagdsfecdmvgairlsplrrglavdsrvdifsf
yiphrhiygqqwinfmkdgvnasplppvtcssgwdsaaylgtipsstlkvpkflhqgyln
iynnyfkppwsddltyanpsnmpsedykwgvrvanlksiwtaplppdtrtsenmttgtst
idimglqaayaklhteqerdyfmtryrdimkefgghtsydgdnrplllmrsefwasgydv
dgtdqsslgqfsgrvqqtfnhkvprfyvpehgvimtlavtrfppthememhylvgkenlt
ytdiacdpalmanlpprevslkeffhsspdsakfkiaegqwyrtqpdrvafpynaldgfp
fysalpstdlkdrvlvntnnydeifqsmqlahwnmqtkfninvyrhmpttrdsimts
>d1gff2_ 2.8.1.1.2 Bacteriophage capsid proteins {(bacteriophage G4)}
mfqkfiskhnapinstqlaatktpavaapvlsvpnlsrstilinatttavtthsglchvv
ridetnptnhhalsiagslsnvpadmiafairfevadgvvptavpalydvypietfnngk
aisfkdavtidshprtvgndvyagimlwsnawtastisgvlsvnqvnreatvlqplk
>d1gfi_1 1.56.1.1.2 (61-181) Transducin (alpha subunit), insertion domain {rat (Rattus rattus)}
yseeeckqykavvysntiqsiiaiiramgrlkidfgdaaraddarqlfvlagaaeegfmt
aelagvikrlwkdsgvqacfnrsreyqlndsaayylndldriaqpnyiptqqdvlrtrvk
t
>d1gfi_2 3.29.1.4.12 (33-60,182-345) Transducin (alpha subunit) {rat (Rattus rattus)}
evkllllgagesgkstivkqmkiiheagXtgivethftfkdlhfkmfdvggqrserkkwi
hcfegvtaiifcvalsdydlvlaedeemnrmhesmklfdsicnnkwftdtsiilflnkkd
lfeekikksplticypeyagsntyeeaaayiqcqfedlnkrkdtkeiythftcatdtknv
qfvfdavtdviik
>d1gfla_ 4.17.1.1.1 Green fluorescent protein {Jellyfish (Aequorea victoria)}
askgeelftgvvpilveldgdvnghkfsvsgegegdatygkltlkficttgklpvpwptl
vttfsygvqcfsrypdhmkrhdffksampegyvqertiffkddgnyktraevkfegdtlv
nrielkgidfkedgnilghkleynynshnvyimadkqkngikvnfkirhniedgsvqlad
hyqqntpigdgpvllpdnhylstqsalskdpnekrdhmvllefvtaagit
>d1gflb_ 4.17.1.1.1 Green fluorescent protein {Jellyfish (Aequorea victoria)}
askgeelftgvvpilveldgdvnghkfsvsgegegdatygkltlkficttgklpvpwptl
vttfsygvqcfsrypdhmkrhdffksampegyvqertiffkddgnyktraevkfegdtlv
nrielkgidfkedgnilghkleynynshnvyimadkqkngikvnfkirhniedgsvqlad
hyqqntpigdgpvllpdnhylstqsalskdpnekrdhmvllefvtaagit
>d1gfm__ 6.7.1.1.1 Porin {(Escherichia coli)}
aeiynkdgnkvdlygkavglhyfskgngensyggngdmtyarlgfkgetqinsdltgygq
weynfqgnnsegadaqtgnktrlafaglkyadvgsfdygrnygvvydalgytgmlpefgg
dtaysddffvgrvggvatyrnsnffglvdglnfavqylgknerdtarrsngdgvggsisy
eyegfgivgaygaadrtnlqeaqplgngkkaeqwatglkydanniylaanygetrnatpi
tnkftntsgfanktqdvllvaqyqfdfglrpsiaytkskakdvegigdvdlvnyfevgat
yyfnknmstyvdyiinqidsdnklgvgsddtvavgivyqf
>d1gfn__ 6.7.1.1.1 Porin {(Escherichia coli)}
aeiynkdgnkvdlygkavglhyfskgngensyggngdmtyarlgfkgetqinsdltgygq
weynfqgnnsegadaqtgnktrlafaglkyadvgsfdygrnygvvydalpefggdtaysd
dffvgrvggvatyrnsnffglvdglnfavqylgknerdtarrsngdgvggsisyeyegfg
ivgaygaadrtnlqeaqplgngkkaeqwatglkydanniylaanygetrnatpitnkftn
tsgfanktqdvllvaqyqfdfglrpsiaytkskakdvegigdvdlvnyfevgatyyfnkn
mstyvdyiinqidsdnklgvgsddtvavgivyqf
>d1gfo__ 6.7.1.1.1 Porin {(Escherichia coli)}
aeiynkdgnkvdlygkavglhyfskgngensyggngdmtyarlgfkgetqinsdltgygq
weynfqgnnsegadaqtgnktrlafaglkyadvgsfdygrnygvvydalgytdmlpefgg
dtaysddffvgpvggvatyrnsnffglvdglnfavqylgknerdtarrsngdgvggsisy
eyegfgivgaygaadrtnlqeaqplgngkkaeqwatglkydanniylaanygetrnatpi
tnkftntsgfanktqdvllvaqyqfdfglrpsiaytkskakdvegigdvdlvnyfevgat
yyfnknmstyvdyiinqidsdnklgvgsddtvavgivyqf
>d1gfp__ 6.7.1.1.1 Porin {(Escherichia coli)}
aeiynkdgnkvdlygkavglhyfskgngensyggngdmtyaclgfkgetqinsdltgygq
weynfqgnnsegadaqtgnktrlafaglkyadvgsfdygrnygvvydalgytdmlpefgg
dtaysddffvgrvggvatyrnsnffglvdglnfavqylgknerdtarrsngdgvggsisy
eyegfgivgaygaadrtnlqeaqplgngkkaeqwatglkydanniylaanygetrnatpi
tnkftntsgfanktqdvllvaqyqfdfglrpsiaytkskakdvegigdvdlvnyfevgat
yyfnknmstyvdyiinqidsdnklgvgsddtvavgivyqf
>d1gfq__ 6.7.1.1.1 Porin {(Escherichia coli)}
aeiynkdgnkvdlygkavglhyfskgngensyggngdmtyarlgfkgetqinsdltgygq
weynfqgnnsegadaqtgnktclafaglkyadvgsfdygrnygvvydalgytdmlpefgg
dtaysddffvgrvggvatyrnsnffglvdglnfavqylgknerdtarrsngdgvggsisy
eyegfgivgaygaadrtnlqeaqplgngkkaeqwatglkydanniylaanygetrnatpi
tnkftntsgfanktqdvllvaqyqfdfglrpsiaytkskakdvegigdvdlvnyfevgat
yyfnknmstyvdyiinqidsdnklgvgsddtvavgivyqf
>d1gg2a1 1.56.1.1.2 (61-181) Transducin (alpha subunit), insertion domain {rat (Rattus rattus)}
yseeeckqykavvysntiqsiiaiiramgrlkidfgdaaraddarqlfvlagaaeegfmt
aelagvikrlwkdsgvqacfnrsreyqlndsaayylndldriaqpnyiptqqdvlrtrvk
t
>d1gg2a2 3.29.1.4.12 (5-60,182-348) Transducin (alpha subunit) {rat (Rattus rattus)}
lsaedkaaverskmidrnlredgekaarevkllllgagesgkstivkqmkiiheagXtgi
vethftfkdlhfkmfdvgaqrserkkwihcfegvtaiifcvalsdydlvlaedeemnrmh
esmklfdsicnnkwftdtsiilflnkkdlfeekikksplticypeyagsntyeeaaayiq
cqfedlnkrkdtkeiythftcatdtknvqfvfdavtdviiknnl
>d1gg2b_ 2.51.3.1.1 beta1-subunit of the signal-transducing G protein heterotrimer {Bovine (Bos taurus)}
seldqlrqeaeqlknqirdarkacadatlsqitnnidpvgriqmrtrrtlrghlakiyam
hwgtdsrllvsasqdgkliiwdsyttnkvhaiplrsswvmtcayapsgnyvacggldnic
siynlktregnvrvsrelaghtgylsccrflddnqivtssgdttcalwdietgqqtttft
ghtgdvmslslapdtrlfvsgacdasaklwdvregmcrqtftghesdinaicffpngnaf
atgsddatcrlfdlradqelmtyshdniicgitsvsfsksgrlllagyddfncnvwdalk
adragvlaghdnrvsclgvtddgmavatgswdsflkiwn
>d1gg2g_ 1.106.2.1.1 Transducin (heterotrimeric G protein), gamma chain {Bovine (Bos taurus)}
siaqarklveqlkmeanidrikvskaaadlmayceahakedplltpvpasenpf
>d1ggaa1 3.22.1.3.5 (1-164,334-358) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Trypanosoma brucei brucei), glycosome}
tikvgingfgrigrmvfqalcddgllgneidvvavvdmntdaryfayqmkydsvhgkfkh
svsttkskpsvakddtlvvnghrilcvkaqrnpadlpwgklgveyviestglftvksaae
ghlrggarkvvisapasggaktfvmgvnhnnynpreqhvvsnasXnewgyshrvvdlvrh
maardraakl
>d1ggaa2 4.42.1.1.5 (165-333) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Trypanosoma brucei brucei), glycosome}
cttnclaplvhvlvkegfgistglmttvhsytatqktvdgvsvkdwrggraaalniipst
tgaakavgmvipstqgkltgmafrvptadvsvvdltfiatrdtsikeidaalkrasktym
knilgytdeelvsadfisdsrssiydskatlqnnlpnerrffkivswyd
>d1ggab1 3.22.1.3.5 (1-164,334-358) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Trypanosoma brucei brucei), glycosome}
tikvgingfgrigrmvfqalcddgllgneidvvavvdmntdaryfayqmkydsvhgkfkh
svsttkskpsvakddtlvvnghrilcvkaqrnpadlpwgklgveyviestglftvksaae
ghlrggarkvvisapasggaktfvmgvnhnnynpreqhvvsnasXnewgyshrvvdlvrh
maardraakl
>d1ggab2 4.42.1.1.5 (165-333) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Trypanosoma brucei brucei), glycosome}
cttnclaplvhvlvkegfgistglmttvhsytatqktvdgvsvkdwrggraaalniipst
tgaakavgmvipstqgkltgmafrvptadvsvvdltfiatrdtsikeidaalkrasktym
knilgytdeelvsadfisdsrssiydskatlqnnlpnerrffkivswyd
>d1ggao1 3.22.1.3.5 (1-164,334-358) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Trypanosoma brucei brucei), glycosome}
tikvgingfgrigrmvfqalcddgllgneidvvavvdmntdaryfayqmkydsvhgkfkh
svsttkskpsvakddtlvvnghrilcvkaqrnpadlpwgklgveyviestglftvksaae
ghlrggarkvvisapasggaktfvmgvnhnnynpreqhvvsnasXnewgyshrvvdlvrh
maardraakl
>d1ggao2 4.42.1.1.5 (165-333) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Trypanosoma brucei brucei), glycosome}
cttnclaplvhvlvkegfgistglmttvhsytatqktvdgvsvkdwrggraaalniipst
tgaakavgmvipstqgkltgmafrvptadvsvvdltfiatrdtsikeidaalkrasktym
knilgytdeelvsadfisdsrssiydskatlqnnlpnerrffkivswyd
>d1ggap1 3.22.1.3.5 (1-164,334-358) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Trypanosoma brucei brucei), glycosome}
tikvgingfgrigrmvfqalcddgllgneidvvavvdmntdaryfayqmkydsvhgkfkh
svsttkskpsvakddtlvvnghrilcvkaqrnpadlpwgklgveyviestglftvksaae
ghlrggarkvvisapasggaktfvmgvnhnnynpreqhvvsnasXnewgyshrvvdlvrh
maardraakl
>d1ggap2 4.42.1.1.5 (165-333) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Trypanosoma brucei brucei), glycosome}
cttnclaplvhvlvkegfgistglmttvhsytatqktvdgvsvkdwrggraaalniipst
tgaakavgmvipstqgkltgmafrvptadvsvvdltfiatrdtsikeidaalkrasktym
knilgytdeelvsadfisdsrssiydskatlqnnlpnerrffkivswyd
>d1ggaq1 3.22.1.3.5 (1-164,334-358) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Trypanosoma brucei brucei), glycosome}
tikvgingfgrigrmvfqalcddgllgneidvvavvdmntdaryfayqmkydsvhgkfkh
svsttkskpsvakddtlvvnghrilcvkaqrnpadlpwgklgveyviestglftvksaae
ghlrggarkvvisapasggaktfvmgvnhnnynpreqhvvsnasXnewgyshrvvdlvrh
maardraakl
>d1ggaq2 4.42.1.1.5 (165-333) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Trypanosoma brucei brucei), glycosome}
cttnclaplvhvlvkegfgistglmttvhsytatqktvdgvsvkdwrggraaalniipst
tgaakavgmvipstqgkltgmafrvptadvsvvdltfiatrdtsikeidaalkrasktym
knilgytdeelvsadfisdsrssiydskatlqnnlpnerrffkivswyd
>d1ggar1 3.22.1.3.5 (1-164,334-358) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Trypanosoma brucei brucei), glycosome}
tikvgingfgrigrmvfqalcddgllgneidvvavvdmntdaryfayqmkydsvhgkfkh
svsttkskpsvakddtlvvnghrilcvkaqrnpadlpwgklgveyviestglftvksaae
ghlrggarkvvisapasggaktfvmgvnhnnynpreqhvvsnasXnewgyshrvvdlvrh
maardraakl
>d1ggar2 4.42.1.1.5 (165-333) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Trypanosoma brucei brucei), glycosome}
cttnclaplvhvlvkegfgistglmttvhsytatqktvdgvsvkdwrggraaalniipst
tgaakavgmvipstqgkltgmafrvptadvsvvdltfiatrdtsikeidaalkrasktym
knilgytdeelvsadfisdsrssiydskatlqnnlpnerrffkivswyd
>d1ggbh1 2.1.1.1.27 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab 50.1 (mouse), kappa L chain}
qvqlqesgpgilqpsqtlsltcsfsgfslstygmgvswirqpsgkglewlahifwdgdkr
ynpslksrlkiskdtsnnqvflkitsvdtadtatyycvqegyiywgqgtsvtvs
>d1ggbh2 2.1.1.2.35 (113-228) Immunoglobulin (constant domains of L and H chains) {Fab 50.1 (mouse), kappa L chain}
sakttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqs
dlytlsssvtvtsstwpsqsitcnvahpasstkvdkkiepr
>d1ggbl1 2.1.1.1.27 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab 50.1 (mouse), kappa L chain}
divltqspgslavslgqratiscrasesvdddgnsflhwyqqkpgqppklliyrssnlis
gipdrfsgsgsrtdftltinpveaddvatyycqqsnedpltfgagtkleik
>d1ggbl2 2.1.1.2.35 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab 50.1 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1ggch1 2.1.1.1.27 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab 50.1 (mouse), kappa L chain}
qvqlqesgpgilqpsqtlsltcsfsgfslstygmgvswirqpsgkglewlahifwdgdkr
ynpslksrlkiskdtsnnqvflkitsvdtadtatyycvqegyiywgqgtsvtvs
>d1ggch2 2.1.1.2.35 (113-228) Immunoglobulin (constant domains of L and H chains) {Fab 50.1 (mouse), kappa L chain}
sakttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqs
dlytlsssvtvtsstwpsqsitcnvahpasstkvdkkiepr
>d1ggcl1 2.1.1.1.27 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab 50.1 (mouse), kappa L chain}
divltqspgslavslgqratiscrasesvdddgnsflhwyqqkpgqppklliyrssnlis
gipdrfsgsgsrtdftltinpveaddvatyycqqsnedpltfgagtkleik
>d1ggcl2 2.1.1.2.35 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab 50.1 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1ggga_ 3.82.1.1.12 Glutamine-binding protein {(Escherichia coli)}
lvvatdtafvpfefkqgdlyvgfdvdlwaaiakelkldyelkpmdfsgiipalqtknvdl
alagititderkkaidfsdgyyksgllvmvkannndvksvkdldgkvvavksgtgsvdya
kaniktkdlrqfpnidnaymelgtnradavlhdtpnilyfiktagngqfkavgdsleaqq
ygiafpkgsdelrdkvngalktlrengtyneiykkwfgte
>d1gggb_ 3.82.1.1.12 Glutamine-binding protein {(Escherichia coli)}
lvvatdtafvpfefkqgdlyvgfdvdlwaaiakelkldyelkpmdfsgiipalqtknvdl
alagititderkkaidfsdgyyksgllvmvkannndvksvkdldgkvvavksgtgsvdya
kaniktkdlrqfpnidnaymelgtnradavlhdtpnilyfiktagngqfkavgdsleaqq
ygiafpkgsdelrdkvngalktlrengtyneiykkwfgte
>d1ggih1 2.1.1.1.27 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab 50.1 (mouse), kappa L chain}
qvqlkesgpgilqpsqtlsltcsfsgfslstygmgvswirqpsgkglewlahifwdgdkr
ynpslksrlkiskdtsnnqvflkitsvdtadtatyycvqegyiywgqgtsvtvs
>d1ggih2 2.1.1.2.35 (113-228) Immunoglobulin (constant domains of L and H chains) {Fab 50.1 (mouse), kappa L chain}
sakttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqs
dlytlsssvtvtsstwpsqsitcnvahpasstkvdkkiepr
>d1ggij1 2.1.1.1.27 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab 50.1 (mouse), kappa L chain}
qvqlkesgpgilqpsqtlsltcsfsgfslstygmgvswirqpsgkglewlahifwdgdkr
ynpslksrlkiskdtsnnqvflkitsvdtadtatyycvqegyiywgqgtsvtvs
>d1ggij2 2.1.1.2.35 (113-228) Immunoglobulin (constant domains of L and H chains) {Fab 50.1 (mouse), kappa L chain}
sakttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqs
dlytlsssvtvtsstwpsqsitcnvahpasstkvdkkiepr
>d1ggil1 2.1.1.1.27 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab 50.1 (mouse), kappa L chain}
divltqspgslavslgqratiscrasesvdddgnsflhwyqqkpgqppklliyrssnlis
gipdrfsgsgsrtdftltinpveaddvatyycqqsnedpltfgagtkleik
>d1ggil2 2.1.1.2.35 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab 50.1 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1ggim1 2.1.1.1.27 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab 50.1 (mouse), kappa L chain}
divltqspgslavslgqratiscrasesvdddgnsflhwyqqkpgqppklliyrssnlis
gipdrfsgsgsrtdftltinpveaddvatyycqqsnedpltfgagtkleik
>d1ggim2 2.1.1.2.35 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab 50.1 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1ggta1 2.1.1.5.12 (8-190) Transglutaminase factor XIII, N-terminal domain {Human (Homo sapiens) blood}
fggrravppnnsnaaeddlptvelqgvvprgvnlqeflnvtsvhlfkerwdtnkvdhhtd
kyennklivrrgqsfyvqidfsrpydprrdlfrveyvigrypqenkgtyipvpivselqs
gkwgakivmredrsvrlsiqsspkcivgkfrmyvavwtpygvlrtsrnpetdtyilfnpw
ced
>d1ggta2 2.1.4.1.1 (516-627) Coagulation factor XIII, two C-terminal domains {Human (Homo sapiens) blood}
snvdmdfevenavlgkdfklsitfrnnshnrytitaylsanitfytgvpkaefkketfdv
tleplsfkkeavliqageymgqlleqaslhffvtarinetrdvlakqkstvl
>d1ggta3 2.1.4.1.1 (628-729) Coagulation factor XIII, two C-terminal domains {Human (Homo sapiens) blood}
tipeiiikvrgtqvvgsdmtvtveftnplketlrnvwvhldgpgvtrpmkkmfreirpns
tvqweevcrpwvsghrkliasmssdslrhvygeldvqiqrrp
>d1ggta4 4.3.1.2.1 (191-515) Coagulation factor XIII, catalytic domain {Human (Homo sapiens) blood}
davyldnekereeyvlndigvifygevndiktrswsygqfedgildtclyvmdraqmdls
grgnpikvsrvgsamvnakddegvlvgswdniyaygvppsawtgsvdilleyrssenpvr
ygqcwvfagvfntflrclgiparivtnyfsahdndanlqmdifleedgnvnskltkdsvw
nyhcwneawmtrpdlpvgfggwqavdstpqensdgmyrcgpasvqaikhghvcfqfdapf
vfaevnsdliyitakkdgthvvenvdathigklivtkqiggdgmmditdtykfqegqeee
rlaletalmygakkplntegvmksr
>d1ggtb1 2.1.1.5.12 (8-190) Transglutaminase factor XIII, N-terminal domain {Human (Homo sapiens) blood}
fggrravppnnsnaaeddlptvelqgvvprgvnlqeflnvtsvhlfkerwdtnkvdhhtd
kyennklivrrgqsfyvqidfsrpydprrdlfrveyvigrypqenkgtyipvpivselqs
gkwgakivmredrsvrlsiqsspkcivgkfrmyvavwtpygvlrtsrnpetdtyilfnpw
ced
>d1ggtb2 2.1.4.1.1 (516-627) Coagulation factor XIII, two C-terminal domains {Human (Homo sapiens) blood}
snvdmdfevenavlgkdfklsitfrnnshnrytitaylsanitfytgvpkaefkketfdv
tleplsfkkeavliqageymgqlleqaslhffvtarinetrdvlakqkstvl
>d1ggtb3 2.1.4.1.1 (628-727) Coagulation factor XIII, two C-terminal domains {Human (Homo sapiens) blood}
tipeiiikvrgtqvvgsdmtvtveftnplketlrnvwvhldgpgvtrpmkkmfreirpns
tvqweevcrpwvsghrkliasmssdslrhvygeldvqiqr
>d1ggtb4 4.3.1.2.1 (191-515) Coagulation factor XIII, catalytic domain {Human (Homo sapiens) blood}
davyldnekereeyvlndigvifygevndiktrswsygqfedgildtclyvmdraqmdls
grgnpikvsrvgsamvnakddegvlvgswdniyaygvppsawtgsvdilleyrssenpvr
ygqcwvfagvfntflrclgiparivtnyfsahdndanlqmdifleedgnvnskltkdsvw
nyhcwneawmtrpdlpvgfggwqavdstpqensdgmyrcgpasvqaikhghvcfqfdapf
vfaevnsdliyitakkdgthvvenvdathigklivtkqiggdgmmditdtykfqegqeee
rlaletalmygakkplntegvmksr
>d1ghae_ 2.35.1.2.7 (alpha, gamma-)chymotrypsin(ogen) {bovine (Bos taurus)}
cgvpaiqpvlsglxxivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgv
ttsdvvvagefdqgsssekiqklkiakvfknskynsltinnditllklstaasfsqtvsa
vclpsasddfaagttcvttgwgltryxxantpdrlqqaslpllsntnckkywgtkikdam
icagasgvsscmgdsggplvckkngawtlvgivswgsstcststpgvyarvtalvnwvqq
tlaan
>d1ghbe_ 2.35.1.2.7 (alpha, gamma-)chymotrypsin(ogen) {bovine (Bos taurus)}
cgvpaiqpvlsglxxivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgv
ttsdvvvagefdqgsssekiqklkiakvfknskynsltinnditllklstaasfsqtvsa
vclpsasddfaagttcvttgwgltryxxantpdrlqqaslpllsntnckkywgtkikdam
icagasgvsscmgdsggplvckkngawtlvgivswgsstcststpgvyarvtalvnwvqq
tlaan
>d1ghc__ 1.4.3.9.2 Histone H1, globular domain {chicken (Gallus gallus)}
magpsvtelitkavsaskerkglslaalkkalaaggydveknnsriklglkslvskgtlv
qtkgtgasgsfrlsk
>d1ghfh1 2.1.1.1.71 (1-115) Immunoglobulin (variable domains of L and H chains) {Fab GH1002 (mouse), kappa L chain}
vqlqqsgpelkkpgetvkiscklwytftdygmnwvkqapgkglkwmgwiqtnteeptyga
efkgrfafsletsaftaykqinnlknedmatyfcarveagfdywaqgttltvss
>d1ghfh2 2.1.1.2.74 (116-213) Immunoglobulin (constant domains of L and H chains) {Fab GH1002 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpssprpsetvtcnvahpasstkvdkkii
>d1ghfl1 2.1.1.1.71 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab GH1002 (mouse), kappa L chain}
diqmtqttsslsaslgdrvtiscresqdisnslnwyqqkpdgtvklliyytsrlhsgvps
rfsgsgtgtdysltisnleqedfatyfcqqgntlpytfgggtkleik
>d1ghfl2 2.1.1.2.74 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab GH1002 (mouse), kappa L chain}
radaaqtvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1ghj__ 2.65.1.1.6 The lipoyl domain of the 2-oxoglutarate dehydrogenase complex {(Azotobacter vinelandii)}
aidikaptfpesiadgtvatwhkkpgeavkrdelivdietdkvvmevlaeadgviaeivk
negdtvlsgellgkltegg
>d1ghk__ 2.65.1.1.6 The lipoyl domain of the 2-oxoglutarate dehydrogenase complex {(Azotobacter vinelandii)}
aidikaptfpesiadgtvatwhkkpgeavkrdelivdietdkvvmevlaeadgviaeivk
negdtvlsgellgkltegg
>d1ghla_ 4.2.1.2.4 Lysozyme {pheasant (Phasianus colchicus)}
gkvygrcelaaamkrmgldnyrgyslgnwvcaakfesnfntgatnrntdgstdygilqin
srwwcndgrtpgsknlchipcsallssditasvncakkivsdgngmnawvawrkhckgtd
vnvwirgcrl
>d1ghlb_ 4.2.1.2.4 Lysozyme {pheasant (Phasianus colchicus)}
gkvygrcelaaamkrmgldnyrgyslgnwvcaakfesnfntgatnrntdgstdygilqin
srwwcndgrtpgsknlchipcsallssditasvncakkivsdgngmnawvawrkhckgtd
vnvwirgcrl
>d1ghr__ 3.1.1.3.7 plant beta-glucanases {barley (Hordeum vulgare) 1,3-1,4-beta-glucanase}
igvcygmsannlpaastvvsmfksngiksmrlyapnqaalqavggtginvvvgapndvls
nlaaspaaaaswvksniqaypkvsfryvcvgnevaggatrnlvpamknvhgalvaaglgh
ikvttsvsqailgvfsppsagsftgeaaafmgpvvqflartnaplmaniypylawaynps
amdmgyalfnasgtvvrdgaygyqnlfdttvdafytamgkhggssvklvvsesgwpsggg
taatpanarfynqhlinhvgrgtprhpgaietyifamfnenqkdsgveqnwglfypnmqh
vypinf
>d1ghsa_ 3.1.1.3.6 plant beta-glucanases {barley (Hordeum vulgare) 1,3-beta-glucanase}
igvcygvignnlpsrsdvvqlyrskgingmriyfadgqalsalrnsgiglildigndqla
niaastsnaaswvqnnvrpyypavnikyiaagnevqggatqsilpamrnlnaalsaaglg
aikvstsirfdevansfppsagvfknaymtdvarllastgapllanvypyfayrdnpgsi
slnyatfqpgttvrdqnngltytslfdamvdavyaalekagapavkvvvsesgwpsaggf
aasagnartynqglinhvgggtpkkrealetyifamfnenqktgdatersfglfnpdksp
ayniqf
>d1ghsb_ 3.1.1.3.6 plant beta-glucanases {barley (Hordeum vulgare) 1,3-beta-glucanase}
igvcygvignnlpsrsdvvqlyrskgingmriyfadgqalsalrnsgiglildigndqla
niaastsnaaswvqnnvrpyypavnikyiaagnevqggatqsilpamrnlnaalsaaglg
aikvstsirfdevansfppsagvfknaymtdvarllastgapllanvypyfayrdnpgsi
slnyatfqpgttvrdqnngltytslfdamvdavyaalekagapavkvvvsesgwpsaggf
aasagnartynqglinhvgggtpkkrealetyifamfnenqktgdatersfglfnpdksp
ayniqf
>d1ghu__ 4.53.1.1.7 Growth factor receptor-bound protein 2 (GRB2) {human (Homo sapiens)}
gswffgkiprakaeemlskqrhdgafliresesapgdfslsvkfgndvqhfkvlrdgagk
yflwvvkfnslnelvdyhrstsvsrnqqiflrdie
>d1gia_1 1.56.1.1.2 (61-181) Transducin (alpha subunit), insertion domain {rat (Rattus rattus)}
yseeeckqykavvysntiqsiiaiiramgrlkidfgdaaraddarqlfvlagaaeegfmt
aelagvikrlwkdsgvqacfnrsreyqlndsaayylndldriaqpnyiptqqdvlrtrvk
t
>d1gia_2 3.29.1.4.12 (34-60,182-343) Transducin (alpha subunit) {rat (Rattus rattus)}
vkllllgagesgkstivkqmkiiheagXtgivethftfkdlhfkmfdvggqrserkkwih
cfegvtaiifcvalsdydlvlaedeemnrmhesmklfdsicnnkwftdtsiilflnkkdl
feekikksplticypeyagsntyeeaaayiqcqfedlnkrkdtkeiythftcatdtknvq
fvfdavtdvi
>d1gica_ 2.21.1.1.1 Concanavalin A {jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1gicb_ 2.21.1.1.1 Concanavalin A {jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1gifa_ 4.41.1.3.1 Microphage migration inhibition factor (MIF) {Human (Homo sapiens)}
mpmfivntnvprasvpdgflseltqqlaqatgkppqyiavhvvpdqlmafggssepcalc
slhsigkiggaqnrsyskllcgllaerlrispdrvyinyydmnaanvgwnnstfa
>d1gifb_ 4.41.1.3.1 Microphage migration inhibition factor (MIF) {Human (Homo sapiens)}
mpmfivntnvprasvpdgflseltqqlaqatgkppqyiavhvvpdqlmafggssepcalc
slhsigkiggaqnrsyskllcgllaerlrispdrvyinyydmnaanvgwnnstfa
>d1gifc_ 4.41.1.3.1 Microphage migration inhibition factor (MIF) {Human (Homo sapiens)}
mpmfivntnvprasvpdgflseltqqlaqatgkppqyiavhvvpdqlmafggssepcalc
slhsigkiggaqnrsyskllcgllaerlrispdrvyinyydmnaanvgwnnstfa
>d1gigh1 2.1.1.1.35 (1-120) Immunoglobulin (variable domains of L and H chains) {Fab HC19 (mouse), lambda L chain}
qvqlkesgpglvapsqslsitctvsgfllisngvhwvrqppgkglewlgviwaggntnyn
salmsrvsiskdnsksqvflkmkslqtddtamyycardfydydvfyyamdywgqgtsvtv
>d1gigh2 2.1.1.2.43 (121-221) Immunoglobulin (constant domains of L and H chains) {Fab HC19 (mouse), lambda L chain}
ssakttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlq
sdlytlsssvtvpsstwpsetvtcnvahpasstkvdkkivp
>d1gigl1 2.1.1.1.35 (1-110) Immunoglobulin (variable domains of L and H chains) {Fab HC19 (mouse), lambda L chain}
qavvtqesalttspgetvtltcrsstgavttsnyanwvqekpdhlftgliggtnnrapgv
parfsgsligdkaaltitgaqtedeaiyfcalwysnhwvfgggtkltvlg
>d1gigl2 2.1.1.2.43 (111-210) Immunoglobulin (constant domains of L and H chains) {Fab HC19 (mouse), lambda L chain}
qpksspsvtlfppsseeletnkatlvctitdfypgvvtvdwkvdgtpvtqgmettqpskq
snnkymassyltltarawerhssyscqvtheghtveksls
>d1gil_1 1.56.1.1.2 (61-181) Transducin (alpha subunit), insertion domain {rat (Rattus rattus)}
yseeeckqykavvysntiqsiiaiiramgrlkidfgdaaraddarqlfvlagaaeegfmt
aelagvikrlwkdsgvqacfnrsreyqlndsaayylndldriaqpnyiptqqdvlrtrvk
t
>d1gil_2 3.29.1.4.12 (34-60,182-343) Transducin (alpha subunit) {rat (Rattus rattus)}
vkllllgagesgkstivkqmkiiheagXtgivethftfkdlhfkmfdvgglrserkkwih
cfegvtaiifcvalsdydlvlaedeemnrmhesmklfdsicnnkwftdtsiilflnkkdl
feekikksplticypeyagsntyeeaaayiqcqfedlnkrkdtkeiythftcatdtknvq
fvfdavtdvi
>d1gim__ 3.29.1.6.2 Adenylosuccinate synthetase (gene purA product) {(Escherichia coli)}
gnnvvvlgtqwgdegkgkivdllterakyvvryqgghnaghtlvingektvlhlipsgil
renvtsiigngvvlspaalmkemkeledrgipvrerlllseacplildyhvaldnareka
rgakaigttgrgigpayedkvarrglrvgdlfdketfaeklkevmeyhnfqlvnyykaea
vdyqkvlddtmavadiltsmvvdvsdlldqarqrgdfvmfegaqgtlldidhgtypyvts
snttaggvatgsglgpryvdyvlgilkaystrvgagpfptelfdetgeflckqgnefgat
tgrrrrtgwldtvavrravqlnslsgfcltkldvldglkevklcvayrmpdgrevtttpl
aaddwkgvepiyetmpgwsestfgvkdrsglpqaalnyikrieeltgvpidiistgpdrt
etmilrdpfda
>d1gin__ 3.29.1.6.2 Adenylosuccinate synthetase (gene purA product) {(Escherichia coli)}
gnnvvvlgtqwgdegkgkivdllterakyvvryqgghnaghtlvingektvlhlipsgil
renvtsiigngvvlspaalmkemkeledrgipvrerlllseacplildyhvaldnareka
rgakaigttgrgigpayedkvarrglrvgdlfdketfaeklkevmeyhnfqlvnyykaea
vdyqkvlddtmavadiltsmvvdvsdlldqarqrgdfvmfegaqgtlldidhgtypyvts
snttaggvatgsglgpryvdyvlgilkaystrvgagpfptelfdetgeflckqgnefgat
tgrrrrtgwldtvavrravqlnslsgfcltkldvldglkevklcvayrmpdgrevtttpl
aaddwkgvepiyetmpgwsestfgvkdrsglpqaalnyikrieeltgvpidiistgpdrt
etmilrdpfda
>d1gio__ 4.4.1.1.5 Angiogenin {Bovine (Bos taurus)}
aqddyryihfltqhydakpkgrndeycfnmmknrrltrpckdrntfihgnkndikaiced
rngqpyrgdlrisksefqitickhkggssrppcrygatedsrvivvgcenglpvhfdesf
itprh
>d1git_1 1.56.1.1.2 (61-181) Transducin (alpha subunit), insertion domain {rat (Rattus rattus)}
yseeeckqykavvysntiqsiiaiiramgrlkidfgdaaraddarqlfvlagaaeegfmt
aelagvikrlwkdsgvqacfnrsreyqlndsaayylndldriaqpnyiptqqdvlrtrvk
t
>d1git_2 3.29.1.4.12 (32-60,182-348) Transducin (alpha subunit) {rat (Rattus rattus)}
revkllllgagesgkstivkqmkiiheagXtgivethftfkdlhfkmfdvgaqrserkkw
ihcfegvtaiifcvalsdydlvlaedeemnrmhesmklfdsicnnkwftdtsiilflnkk
dlfeekikksplticypeyagsntyeeaaayiqcqfedlnkrkdtkeiythftcatdtkn
vqfvfdavtdviiknnl
>d1gkea_ 2.3.2.1.2 Transthyretin (synonym: prealbumin) {Rat (Rattus norvegicus)}
skcplmvkvldavrgspavdvavkvfkktadgswepfasgktaesgelhglttdekfteg
vyrveldtksywkalgispfheyaevvftandsghrhytiaallspysysttavvsnpqn
>d1gkeb_ 2.3.2.1.2 Transthyretin (synonym: prealbumin) {Rat (Rattus norvegicus)}
skcplmvkvldavrgspavdvavkvfkktadgswepfasgktaesgelhglttdekfteg
vyrveldtksywkalgispfheyaevvftandsghrhytiaallspysysttavvsnpqn
>d1gkec_ 2.3.2.1.2 Transthyretin (synonym: prealbumin) {Rat (Rattus norvegicus)}
skcplmvkvldavrgspavdvavkvfkktadgswepfasgktaesgelhglttdekfteg
vyrveldtksywkalgispfheyaevvftandsghrhytiaallspysysttavvsnpqn
>d1gked_ 2.3.2.1.2 Transthyretin (synonym: prealbumin) {Rat (Rattus norvegicus)}
skcplmvkvldavrgspavdvavkvfkktadgswepfasgktaesgelhglttdekfteg
vyrveldtksywkalgispfheyaevvftandsghrhytiaallspysysttavvsnpqn
>d1gkh__ 2.29.4.8.1 Gene V protein {(Bacteriophage f1)}
mikveikpsqaqfttrsgvsrqgkpyslneqlcyvdlgneypvlvkitldegqpayapgl
ytvhlssfhvgqfgslmidrlrlvpa
>d1gks__ 1.3.1.1.21 Cytochrome c551 {(Ectothiorhodospira halophila)}
dgesiyingtaptcsschdrgvagapelnapedwadrpssvdelvestlagkgampaydg
radredlvkaieymlstl
>d1gky__ 3.29.1.1.1 Guanylate kinase {baker's yeast (Saccharomyces cerevisiae)}
xsrpivisgpsgtgkstllkklfaeypdsfgfsvssttrtpragevngkdynfvsvdefk
smiknnefiewaqfsgnyygstvasvkqvsksgktcildidmqgvksvkaipelnarflf
iappsvedlkkrlegrgteteesinkrlsaaqaelayaetgahdkvivnddldkaykelk
dfifaek
>d1glaf_ 2.65.3.1.2 Glucose-specific factor III (glsIII) {(Escherichia coli)}
glfdklkslvsddkkdtgtieiiaplsgeivniedvpdvvfaekivgdgiaikptgnkmv
apvdgtigkifetnhafsiesdsgvelfvhfgidtvelkgegfkriaeegqrvkvgdtvi
efdlplleekakstltpvvisnmdeikeliklsgsvtvgetpvirikk
>d1glag1 3.47.1.3.1 (4-253) Glycerate kinase {(Escherichia coli)}
kyivaldqgttssravvmdhdaniisvsqrefeqiypkpgwvehdpmeiwatqsstlvev
lakadissdqiaaigitnqrettivweketgkpiynaivwqcrrtaeicehlkrdgledy
irsntglvidpyfsgtkvkwildhvegsrerarrgellfgtvdtwliwkmtqgrvhvtdy
tnasrtmlfnihtldwddkmlevldipremlpevrrssevygqtniggkggtripisgia
gdqqaalfgq
>d1glag2 3.47.1.3.1 (254-499) Glycerate kinase {(Escherichia coli)}
lcvkegmakntygtgcfmlmntgekavksengllttiacgptgevnyalegavfmagasi
qwlrdemklindaydseyfatkvqntngvyvvpaftglgapywdpyargaifgltrgvna
nhiiratlesiayqtrdvleamqadsgirlhalrvdggavannflmqfqsdilgtrverp
evrevtalgaaylaglavgfwqnldelqekavierefrpgietternyryagwkkavkra
maweeh
>d1glbf_ 2.65.3.1.2 Glucose-specific factor III (glsIII) {(Escherichia coli)}
glfdklkslvsddkkdtgtieiiaplsgeivniedvpdvvfaekivgdgiaikptgnkmv
apvdgtigkifetnhafsiesdsgvelfvhfgidtvelkgegfkriaeegqrvkvgdtvi
efdlplleekakstltpvvisnmdeikeliklsgsvtvgetpvirikk
>d1glbg1 3.47.1.3.1 (4-253) Glycerate kinase {(Escherichia coli)}
kyivaldqgttssravvmdhdaniisvsqrefeqiypkpgwvehdpmeiwatqsstlvev
lakadissdqiaaigitnqrettivweketgkpiynaivwqcrrtaeicehlkrdgledy
irsntglvidpyfsgtkvkwildhvegsrerarrgellfgtvdtwliwkmtqgrvhvtdy
tnasrtmlfnihtldwddkmlevldipremlpevrrssevygqtniggkggtripisgia
gdqqaalfgq
>d1glbg2 3.47.1.3.1 (254-499) Glycerate kinase {(Escherichia coli)}
lcvkegmakntygtgcfmlmntgekavksengllttiacgptgevnyalegavfmagasi
qwlrdemklindaydseyfatkvqntngvyvvpaftglgapywdpyargaifgltrgvna
nhiiratlesiayqtrdvleamqadsgirlhalrvdggavannflmqfqsdilgtrverp
evrevtalgaaylaglavgfwqnldelqekavierefrpgietternyryagwkkavkra
maweeh
>d1glcf_ 2.65.3.1.2 Glucose-specific factor III (glsIII) {(Escherichia coli)}
glfdklkslvsddkkdtgtieiiaplsgeivniedvpdvvfaekivgdgiaikptgnkmv
apvdgtigkifetnhafsiesdsgvelfvhfgidtvelkgegfkriaeegqrvkvgdtvi
efdlplleekakstltpvvisnmdeikeliklsgsvtvgetpvirikk
>d1glcg1 3.47.1.3.1 (4-253) Glycerate kinase {(Escherichia coli)}
kyivaldqgttssravvmdhdaniisvsqrefeqiypkpgwvehdpmeiwatqsstlvev
lakadissdqiaaigitnqrettivweketgkpiynaivwqcrrtaeicehlkrdgledy
irsntglvidpyfsgtkvkwildhvegsrerarrgellfgtvdtwliwkmtqgrvhvtdy
tnasrtmlfnihtldwddkmlevldipremlpevrrssevygqtniggkggtripisgia
gdqqaalfgq
>d1glcg2 3.47.1.3.1 (254-499) Glycerate kinase {(Escherichia coli)}
lcvkegmakntygtgcfmlmntgekavksengllttiacgptgevnyalegavfmagasi
qwlrdemklindaydseyfatkvqntngvyvvpaftglgapywdpyargaifgltrgvna
nhiiratlesiayqtrdvleamqadsgirlhalrvdggavannflmqfqsdilgtrverp
evrevtalgaaylaglavgfwqnldelqekavierefrpgietternyryagwkkavkra
maweeh
>d1gldf_ 2.65.3.1.2 Glucose-specific factor III (glsIII) {(Escherichia coli)}
glfdklkslvsddkkdtgtieiiaplsgeivniedvpdvvfaekivgdgiaikptgnkmv
apvdgtigkifetnhafsiesdsgvelfvhfgidtvelkgegfkriaeegqrvkvgdtvi
efdlplleekakstltpvvisnmdeikeliklsgsvtvgetpvirikk
>d1gldg1 3.47.1.3.1 (4-253) Glycerate kinase {(Escherichia coli)}
kyivaldqgttssravvmdhdaniisvsqrefeqiypkpgwvehdpmeiwatqsstlvev
lakadissdqiaaigitnqrettivweketgkpiynaivwqcrrtaeicehlkrdgledy
irsntglvidpyfsgtkvkwildhvegsrerarrgellfgtvdtwliwkmtqgrvhvtdy
tnasrtmlfnihtldwddkmlevldipremlpevrrssevygqtniggkggtripisgia
gdqqaalfgq
>d1gldg2 3.47.1.3.1 (254-499) Glycerate kinase {(Escherichia coli)}
lcvkegmakntygtgcfmlmntgekavksengllttiacgptgevnyalegavfmagasi
qwlrdemklindaydseyfatkvqntngvyvvpaftglgapywdpyargaifgltrgvna
nhiiratlesiayqtrdvleamqadsgirlhalrvdggavannflmqfqsdilgtrverp
evrevtalgaaylaglavgfwqnldelqekavierefrpgietternyryagwkkavkra
maweeh
>d1glef_ 2.65.3.1.2 Glucose-specific factor III (glsIII) {(Escherichia coli)}
glfdklkslvsddkkdtgtieiiaplsgeivniedvpdvvfaekivgdgiaikptgnkmv
apvdgtigkifetnhafsiesdsgvelfvhfgidtvelkgegfkriaeegqrvkvgdtvi
efdlplleekakstltpvvisnmdeikeliklsgsvtvgetpvirikk
>d1gleg1 3.47.1.3.1 (4-253) Glycerate kinase {(Escherichia coli)}
kyivaldqgttssravvmdhdaniisvsqrefeqiypkpgwvehdpmeiwatqsstlvev
lakadissdqiaaigitnqrettivweketgkpiynaivwqcrrtaeicehlkrdgledy
irsntglvidpyfsgtkvkwildhvegsrerarrgellfgtvdtwliwkmtqgrvhvtdy
tnasrtmlfnihtldwddkmlevldipremlpevrrssevygqtniggkggtripisgia
gdqqaalfgq
>d1gleg2 3.47.1.3.1 (254-499) Glycerate kinase {(Escherichia coli)}
lcvkegmakntygtgcfmlmntgekavksengllttiacgptgevnyalegavfmagasi
qwlrdemklindaydseyfatkvqntngvyvvpaftglgapywdpyargaifgltrgvna
nhiiratlesiayqtrdvleamqadsgirlhalrvdggavannflmqfqsdilgtrverp
evrevtalgaaylaglavgfwqnldelqekavierefrpgietternyryagwkkavkra
maweeh
>d1glg__ 3.81.1.1.4 Galactose/glucose-binding protein {(Salmonella typhimurium), strain lt2}
adtrigvtiykyddnfmsvvrkaieqdakaapdvqllmndsqndqskqndqidvllakgv
kalainlvdpaaagtviekargqnvpvvffnkepsrkaldsydkayyvgtdskesgiiqg
dliakhwaanqgwdlnkdgqiqfvllkgepghpdaearttyvikelndkgikteqlqldt
amwdtaqakdkmdawlsgpnankievvianndamamgavealkahnkssipvfgvdalpe
alalvksgalagtvlndannqakatfdlaknladgkgaadgtnwkidnkvvrvpyvgvdk
dnlaefskk
>d1glh__ 2.21.1.2.2 Bacillus 1-3,1-4-beta-glucanase {hybrid protein: residues 1-16 from (Bacillus amyloliquefaciens) and (Bacillus macerans)}
qtggsffepfnsynsgtwekadgysnggvfnctwrannvnftndgklklgltssaynkfd
caeyrstniygyglyevsmkpakntgivssfftytgpahgtqwdeidieflgkdttkvqf
nyytngvgghekvislgfdaskgfhtyafdwqpgyikwyvdgvlkhtatanipstpgkim
mnlwngtgvddwlgsynganplyaeydwvkytsn
>d1glia_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
mlspadktnvkaawgkvgahageygaealermflsfpwtktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1glib_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1glic_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
mlspadktnvkaawgkvgahageygaealermflsfpwtktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1glid_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1glm__ 1.81.1.1.1 Glucoamylase {(Aspergillus awamori), variant x100}
atldswlsneatvartailnnigadgawvsgadsgivvaspstdnpdyfytwtrdsglvi
ktlvdlfrngdtdllstiehyissqaiiqgvsnpsgdlssgglgepkfnvdetaytgswg
rpqrdgpalratamigfgqwlldngytsaateivwplvrndlsyvaqywnqtgydlweev
ngssfftiavqhralvegsafatavgsscswcdsqapqilcylqsfwtgsyilanfdssr
sgkdtntllgsihtfdpeagcddstfqpcspralanhkevvdsfrsiytlndglsdseav
avgrypedsyyngnpwflctlaaaeqlydalyqwdkqgsleitdvsldffkalysgaatg
tyssssstyssivsavktfadgfvsivethaasngslseqfdksdgdelsardltwsyaa
lltannrrnsvvppswgetsassvpgtcaatsasgtyssvtvtswpsiva
>d1gln_1 1.75.1.1.1 (306-468) Anticodon-binding (C-terminal) domain of glutamyl-tRNA synthetase (GluRS) {(Thermus thermophilus)}
dleklrwmngkyirevlsleevaervkpflreaglsweseaylrravelmrprfdtlkef
pekarylftedypvsekaqrkleeglpllkelyprlraqeewteaaleallrgfaaekgv
klgqvaqplraaltgsletpglfeilallgkeralrrlerala
>d1gln_2 3.17.1.1.3 (1-305) Glutamyl-tRNA synthetase (GluRS) {(Thermus thermophilus)}
mvvtriapsptgdphvgtayialfnyawarrnggrfivriedtdraryvpgaeerilaal
kwlglsydegpdvaaptgpyrqserlplyqkyaeellkrgwayrafetpeeleqirkekg
gydgrarnippeeaeerarrgephvirlkvprpgttevkdelrgvvvydnqeipdvvllk
sdgyptyhlanvvddhlmgvtdviraeewlvstpihvllyrafgweaprfyhmpllrnpd
ktkiskrkshtsldwykaegflpealrnylclmgfsmpdgreiftleefiqaftwervsl
ggpvf
>d1glpa1 1.43.1.1.2 (79-209) Glutathione S-transferase {mouse (Mus musculus)}
ygknqreaaqmdmvndgvedlrgkyvtliytnyengkndyvkalpghlkpfetllsqnqg
gkafivgdqisfadynlldlllihqvlapgcldnfpllsayvarlsarpkikaflsspeh
vnrpingngkq
>d1glpa2 3.38.1.4.2 (1-78) Glutathione S-transferase {mouse (Mus musculus) class pi}
ppytivyfpvrgrceamrmlladqgqswkeevvtidtwmqgllkptclygqlpkfedgdl
tlyqsnailrhlgrslgl
>d1glpb1 1.43.1.1.2 (79-209) Glutathione S-transferase {mouse (Mus musculus)}
ygknqreaaqmdmvndgvedlrgkyvtliytnyengkndyvkalpghlkpfetllsqnqg
gkafivgdqisfadynlldlllihqvlapgcldnfpllsayvarlsarpkikaflsspeh
vnrpingngkq
>d1glpb2 3.38.1.4.2 (1-78) Glutathione S-transferase {mouse (Mus musculus) class pi}
ppytivyfpvrgrceamrmlladqgqswkeevvtidtwmqgllkptclygqlpkfedgdl
tlyqsnailrhlgrslgl
>d1glqa1 1.43.1.1.2 (79-209) Glutathione S-transferase {mouse (Mus musculus)}
ygknqreaaqmdmvndgvedlrgkyvtliytnyengkndyvkalpghlkpfetllsqnqg
gkafivgdqisfadynlldlllihqvlapgcldnfpllsayvarlsarpkikaflsspeh
vnrpingngkq
>d1glqa2 3.38.1.4.2 (1-78) Glutathione S-transferase {mouse (Mus musculus) class pi}
ppytivyfpvrgrceamrmlladqgqswkeevvtidtwmqgllkptclygqlpkfedgdl
tlyqsnailrhlgrslgl
>d1glqb1 1.43.1.1.2 (79-209) Glutathione S-transferase {mouse (Mus musculus)}
ygknqreaaqmdmvndgvedlrgkyvtliytnyengkndyvkalpghlkpfetllsqnqg
gkafivgdqisfadynlldlllihqvlapgcldnfpllsayvarlsarpkikaflsspeh
vnrpingngkq
>d1glqb2 3.38.1.4.2 (1-78) Glutathione S-transferase {mouse (Mus musculus) class pi}
ppytivyfpvrgrceamrmlladqgqswkeevvtidtwmqgllkptclygqlpkfedgdl
tlyqsnailrhlgrslgl
>d1glua_ 7.33.1.2.4 Glucocorticoid receptor DNA-binding domain {rat (Rattus norvegicus)}
mkparpclvcsdeasgchygvltcgsckvffkravegqhnylcagrndciidkirrkncp
acryrkclqagmnlearktkk
>d1glub_ 7.33.1.2.4 Glucocorticoid receptor DNA-binding domain {rat (Rattus norvegicus)}
mkparpclvcsdeasgchygvltcgsckvffkravegqhnylcagrndciidkirrkncp
acryrkclqagmnlearktkk
>d1glv_1 3.23.1.3.1 (2-122) Glutathione synthetase, N-terminal domain {(Escherichia coli)}
iklgivmdpianinikkdssfamlleaqrrgyelhymemgdlylingearahtrtlnvkq
nyeewfsfvgeqdlpladldvilmrkdppfdtefiyatyileraeekgtlivnkpqslrd
c
>d1glv_2 4.89.1.1.1 (123-316) Glutathione synthetase {(Escherichia coli)}
neklftawfsdltpetlvtrnkaqlkafwekhsdiilkpldgmggasifrvkegdpnlgv
iaetltehgtrycmaqnylpaikdgdkrvlvvdgepvpyclarggggeprpltesdwkia
rqigptlkekglifvgldiigdrlteinvtsptcireieaefpvsitgmlmdaiearlqq
q
>d1gmca_ 2.35.1.2.7 (alpha, gamma-)chymotrypsin(ogen) {bovine (Bos taurus)}
cgvpaiqpvlsglxxivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgv
ttsdvvvagefdqgsssekiqklkiakvfknskynsltinnditllklstaasfsqtvsa
vclpsasddfaagttcvttgwgltryxxantpdrlqqaslpllsntnckkywgtkikdam
icagasgvsscmgdsggplvckkngawtlvgivswgsstcststpgvyarvtalvnwvqq
tlaan
>d1gmda_ 2.35.1.2.7 (alpha, gamma-)chymotrypsin(ogen) {bovine (Bos taurus)}
cgvpaiqpvlsglxxivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgv
ttsdvvvagefdqgsssekiqklkiakvfknskynsltinnditllklstaasfsqtvsa
vclpsasddfaagttcvttgwgltryxxantpdrlqqaslpllsntnckkywgtkikdam
icagasgvsscmgdsggplvckkngawtlvgivswgsstcststpgvyarvtalvnwvqq
tlaan
>d1gmh__ 2.35.1.2.7 (alpha, gamma-)chymotrypsin(ogen) {bovine (Bos taurus)}
cgvpaiqpvlsglxxivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgv
ttsdvvvagefdqgsssekiqklkiakvfknskynsltinnditllklstaasfsqtvsa
vclpsasddfaagttcvttgwgltryxxantpdrlqqaslpllsntnckkywgtkikdam
icagasgvsscmgdsggplvckkngawtlvgivswgsstcststpgvyarvtalvnwvqq
tlaan
>d1gmpa_ 4.1.1.1.1 RNase Sa {(Streptomyces aureofaciens)}
dvsgtvclsalppeatdtlnliasdgpfpysqdgvvfqnresvlptqsygyyheytvitp
gartrgtrriicgeatqedyytgdhyatfslidqtc
>d1gmpb_ 4.1.1.1.1 RNase Sa {(Streptomyces aureofaciens)}
dvsgtvclsalppeatdtlnliasdgpfpysqdgvvfqnresvlptqsygyyheytvitp
gartrgtrriicgeatqedyytgdhyatfslidqtc
>d1gmqa_ 4.1.1.1.1 RNase Sa {(Streptomyces aureofaciens)}
dvsgtvclsalppeatdtlnliasdgpfpysqdgvvfqnresvlptqsygyyheytvitp
gartrgtrriicgeatqedyytgdhyatfslidqtc
>d1gmqb_ 4.1.1.1.1 RNase Sa {(Streptomyces aureofaciens)}
dvsgtvclsalppeatdtlnliasdgpfpysqdgvvfqnresvlptqsygyyheytvitp
gartrgtrriicgeatqedyytgdhyatfslidqtc
>d1gmra_ 4.1.1.1.1 RNase Sa {(Streptomyces aureofaciens)}
dvsgtvclsalppeatdtlnliasdgpfpysqdgvvfqnresvlptqsygyyheytvitp
gartrgtrriicgeatqedyytgdhyatfslidqtc
>d1gmrb_ 4.1.1.1.1 RNase Sa {(Streptomyces aureofaciens)}
dvsgtvclsalppeatdtlnliasdgpfpysqdgvvfqnresvlptqsygyyheytvitp
gartrgtrriicgeatqedyytgdhyatfslidqtc
>d1gmsa_ 4.95.1.1.1 Glucosamine 6-phosphate synthase, N-terminal domain {(Escherichia coli)}
cgivgaiaqrdvaeilleglrrleyrgydsaglavvdaeghmtrlrrlgkvqmlaqaaee
hplhggtgiahtrwathgepsevnahphvsehivvvhngiienheplreelkargytfvs
etdteviahlvnwelkqggtlreavlraipqlrgaygtvimdsrhpdtllaarsgsplvi
glgmgenfiasdqlallpvtrrfifleegdiaeitrrsvnifdktgaevkrqdiesnl
>d1gmsc_ 4.95.1.1.1 Glucosamine 6-phosphate synthase, N-terminal domain {(Escherichia coli)}
cgivgaiaqrdvaeilleglrrleyrgydsaglavvdaeghmtrlrrlgkvqmlaqaaee
hplhggtgiahtrwathgepsevnahphvsehivvvhngiienheplreelkargytfvs
etdteviahlvnwelkqggtlreavlraipqlrgaygtvimdsrhpdtllaarsgsplvi
glgmgenfiasdqlallpvtrrfifleegdiaeitrrsvnifdktgaevkrqdiesnlq
>d1gmse_ 4.95.1.1.1 Glucosamine 6-phosphate synthase, N-terminal domain {(Escherichia coli)}
cgivgaiaqrdvaeilleglrrleyrgydsaglavvdaeghmtrlrrlgkvqmlaqaaee
hplhggtgiahtrwathgepsevnahphvsehivvvhngiienheplreelkargytfvs
etdteviahlvnwelkqggtlreavlraipqlrgaygtvimdsrhpdtllaarsgsplvi
glgmgenfiasdqlallpvtrrfifleegdiaeitrrsvnifdktgaevkrqdiesnl
>d1gmsg_ 4.95.1.1.1 Glucosamine 6-phosphate synthase, N-terminal domain {(Escherichia coli)}
cgivgaiaqrdvaeilleglrrleyrgydsaglavvdaeghmtrlrrlgkvqmlaqaaee
hplhggtgiahtrwathgepsevnahphvsehivvvhngiienheplreelkargytfvs
etdteviahlvnwelkqggtlreavlraipqlrgaygtvimdsrhpdtllaarsgsplvi
glgmgenfiasdqlallpvtrrfifleegdiaeitrrsvnifdktgaevkrqdiesnlq
>d1gnc__ 1.26.1.1.1 Granulocyte-colony stimulating factor (G-CSF) {human (Homo sapiens)}
mtplgpasslpqsfllkcleqvrkiqgdgaalqeklvsecatyklchpeelvllghslgi
pwaplsscpsqalqlagclsqlhsglflyqgllqalegispelgptldtlqldvadfatt
iwqqmeelgmapalqptqgampafasafqrraggvlvashlqsflevsyrvlrhlaqp
>d1gnd_1 3.4.1.3.1 (1-291,389-430) Guanine nucleotide dissosiation inhibitor, GDI {Bovine (Bos taurus)}
mdeeydvivlgtgltecilsgimsvngkkvlhmdrnpyyggesssitpleelykrfqlle
gppetmgrgrdwnvdlipkflmangqlvkmllytevtryldfkvvegsfvykggkiykvp
stetealasnlmgmfekrrfrkflvfvanfdendpktfegvdpqntsmrdvyrkfdlgqd
vidftghalalyrtddyldqpcletinriklyseslarygkspylyplyglgelpqgfar
lsaiyggtymlnkpvddiimengkvvgvksegevarckqlicdpsyvpdrvXpiddgses
qvfcscsydatthfettcndikdiykrmagsafd
>d1gnd_2 4.12.1.5.1 (292-388) Guanine nucleotide dissosiation inhibitor, GDI {Bovine (Bos taurus)}
rkagqviriicilshpikntndanscqiiipqnqvnrksdiyvcmisyahnvaaqgkyia
iasttvettdpekevepalellepidqkfvaisdlye
>d1gne_1 1.43.1.1.11 (80-232) Glutathione S-transferase {(Schistosoma japonicum)}
mlggcpkeraeismlegavldirygvsriayskdfetlkvdflsklpemlkmfedrlchk
tylngdhvthpdfmlydaldvvlymdpmcldafpklvcfkkrieaipqidkylksskyia
wplqgwqatfgggdhppksdlvprgsmeldkwa
>d1gne_2 3.38.1.4.11 (1-79) Glutathione S-transferase {(Schistosoma japonicum)}
spilgywkikglvqptrllleyleekyeehlyerdegdkwrnkkfelglefpnlpyyidg
dvkltqsmaiiryiadkhn
>d1gnha_ 2.21.1.4.2 C-reactive protein (CRP) {Human (Homo sapiens)}
qtdmsrkafvfpkesdtsyvslkapltkplkaftvclhfytelsstrgysifsyatkrqd
neilifwskdigysftvggseilfevpevtvapvhictswesasgivefwvdgkprvrks
lkkgytvgaeasiilgqeqdsfggnfegsqslvgdignvnmwdfvlspdeintiylggpf
spnvlnwralkyevqgevftkpqlwp
>d1gnhb_ 2.21.1.4.2 C-reactive protein (CRP) {Human (Homo sapiens)}
qtdmsrkafvfpkesdtsyvslkapltkplkaftvclhfytelsstrgysifsyatkrqd
neilifwskdigysftvggseilfevpevtvapvhictswesasgivefwvdgkprvrks
lkkgytvgaeasiilgqeqdsfggnfegsqslvgdignvnmwdfvlspdeintiylggpf
spnvlnwralkyevqgevftkpqlwp
>d1gnhc_ 2.21.1.4.2 C-reactive protein (CRP) {Human (Homo sapiens)}
qtdmsrkafvfpkesdtsyvslkapltkplkaftvclhfytelsstrgysifsyatkrqd
neilifwskdigysftvggseilfevpevtvapvhictswesasgivefwvdgkprvrks
lkkgytvgaeasiilgqeqdsfggnfegsqslvgdignvnmwdfvlspdeintiylggpf
spnvlnwralkyevqgevftkpqlwp
>d1gnhd_ 2.21.1.4.2 C-reactive protein (CRP) {Human (Homo sapiens)}
qtdmsrkafvfpkesdtsyvslkapltkplkaftvclhfytelsstrgysifsyatkrqd
neilifwskdigysftvggseilfevpevtvapvhictswesasgivefwvdgkprvrks
lkkgytvgaeasiilgqeqdsfggnfegsqslvgdignvnmwdfvlspdeintiylggpf
spnvlnwralkyevqgevftkpqlwp
>d1gnhe_ 2.21.1.4.2 C-reactive protein (CRP) {Human (Homo sapiens)}
qtdmsrkafvfpkesdtsyvslkapltkplkaftvclhfytelsstrgysifsyatkrqd
neilifwskdigysftvggseilfevpevtvapvhictswesasgivefwvdgkprvrks
lkkgytvgaeasiilgqeqdsfggnfegsqslvgdignvnmwdfvlspdeintiylggpf
spnvlnwralkyevqgevftkpqlwp
>d1gnhf_ 2.21.1.4.2 C-reactive protein (CRP) {Human (Homo sapiens)}
qtdmsrkafvfpkesdtsyvslkapltkplkaftvclhfytelsstrgysifsyatkrqd
neilifwskdigysftvggseilfevpevtvapvhictswesasgivefwvdgkprvrks
lkkgytvgaeasiilgqeqdsfggnfegsqslvgdignvnmwdfvlspdeintiylggpf
spnvlnwralkyevqgevftkpqlwp
>d1gnhg_ 2.21.1.4.2 C-reactive protein (CRP) {Human (Homo sapiens)}
qtdmsrkafvfpkesdtsyvslkapltkplkaftvclhfytelsstrgysifsyatkrqd
neilifwskdigysftvggseilfevpevtvapvhictswesasgivefwvdgkprvrks
lkkgytvgaeasiilgqeqdsfggnfegsqslvgdignvnmwdfvlspdeintiylggpf
spnvlnwralkyevqgevftkpqlwp
>d1gnhh_ 2.21.1.4.2 C-reactive protein (CRP) {Human (Homo sapiens)}
qtdmsrkafvfpkesdtsyvslkapltkplkaftvclhfytelsstrgysifsyatkrqd
neilifwskdigysftvggseilfevpevtvapvhictswesasgivefwvdgkprvrks
lkkgytvgaeasiilgqeqdsfggnfegsqslvgdignvnmwdfvlspdeintiylggpf
spnvlnwralkyevqgevftkpqlwp
>d1gnhi_ 2.21.1.4.2 C-reactive protein (CRP) {Human (Homo sapiens)}
qtdmsrkafvfpkesdtsyvslkapltkplkaftvclhfytelsstrgysifsyatkrqd
neilifwskdigysftvggseilfevpevtvapvhictswesasgivefwvdgkprvrks
lkkgytvgaeasiilgqeqdsfggnfegsqslvgdignvnmwdfvlspdeintiylggpf
spnvlnwralkyevqgevftkpqlwp
>d1gnhj_ 2.21.1.4.2 C-reactive protein (CRP) {Human (Homo sapiens)}
qtdmsrkafvfpkesdtsyvslkapltkplkaftvclhfytelsstrgysifsyatkrqd
neilifwskdigysftvggseilfevpevtvapvhictswesasgivefwvdgkprvrks
lkkgytvgaeasiilgqeqdsfggnfegsqslvgdignvnmwdfvlspdeintiylggpf
spnvlnwralkyevqgevftkpqlwp
>d1gnma_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpdniigrnlltqigctlnf
>d1gnmb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpdniigrnlltqigctlnf
>d1gnna_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpnniigrnlltqigctlnf
>d1gnnb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpnniigrnlltqigctlnf
>d1gnoa_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1gnob_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1gnp__ 3.29.1.4.1 cH-p21 Ras protein {human (Homo sapiens)}
mteyklvvvgaggvgksaltiqliqnhfvdeydptiedsyrkqvvidgetclldildtag
qeeysamrdqymrtgegflcvfainntksfedihqyreqikrvkdsddvpmvlvgnkcdl
aartvesrqaqdlarsygipyietsaktrqgvedafytlvreirqh
>d1gnq__ 3.29.1.4.1 cH-p21 Ras protein {human (Homo sapiens)}
mteyklvvvgaggvgksaltiqliqnhfvdeydptiedsyrkqvvidgetclldildtag
qeeysamrdqymrtgegflcvfainntksfedihqyreqikrvkdsddvpmvlvgnkcdl
aartvesrqaqdlarsygipyietsaktrqgvedafytlvreirqh
>d1gnr__ 3.29.1.4.1 cH-p21 Ras protein {human (Homo sapiens)}
mteyklvvvgaggvgksaltiqliqnhfvdeydptiedsyrkqvvidgetclldildtag
qeeysamrdqymrtgegflcvfainntksfedihqyreqikrvkdsddvpmvlvgnkcdl
aartvesrqaqdlarsygipyietsaktrqgvedafytlvreirqh
>d1gnwa1 1.43.1.1.12 (86-211) Glutathione S-transferase {mouse-ear cress (Arabidopsis thaliana)}
lqtdsknisqyaimaigmqvedhqfdpvasklafeqifksiyglttdeavvaeeeaklak
vldvyearlkefkylagetftltdlhhipaiqyllgtptkklfterprvnewvaeitkrp
asekvq
>d1gnwa2 3.38.1.4.12 (2-85) Glutathione S-transferase {mouse-ear cress (Arabidopsis thaliana)}
gikvfghpasiatrrvlialheknldfelvhvelkdgehkkepflsrnpfgqvpafedgd
lklfesraitqyiahryenqgtnl
>d1gnwb1 1.43.1.1.12 (86-211) Glutathione S-transferase {mouse-ear cress (Arabidopsis thaliana)}
lqtdsknisqyaimaigmqvedhqfdpvasklafeqifksiyglttdeavvaeeeaklak
vldvyearlkefkylagetftltdlhhipaiqyllgtptkklfterprvnewvaeitkrp
asekvq
>d1gnwb2 3.38.1.4.12 (2-85) Glutathione S-transferase {mouse-ear cress (Arabidopsis thaliana)}
gikvfghpasiatrrvlialheknldfelvhvelkdgehkkepflsrnpfgqvpafedgd
lklfesraitqyiahryenqgtnl
>d1goa__ 3.47.3.1.1 RNase H {(Escherichia coli)}
mlkqveiftdgsclgnpgpggygailryrgrektfsagytrttnnrmelmaaivalealk
ehcevilstdsqyvrqgitqgwihnwkkrgwktadkkpvknvdlwqrldaalgqhqikwe
wvkghaghpenercdelaraaamnptledtgyqvev
>d1gob__ 3.47.3.1.1 RNase H {(Escherichia coli)}
mlkqveiftdgsclgnpgpggygailryrgrektfsagytrttnnrmelmaaivalealk
ehcevilstdsqyvrqaitqwihnwkkrgwktadkkpvknvdlwqrldaalgqhqikwew
vkghaghpenercdelaraaamnptledtgyqvev
>d1goc__ 3.47.3.1.1 RNase H {(Escherichia coli)}
mlkqveiftdgsclgnpgpggygailryrgrektfsagytrttnnrmelmaaivalealk
ehcevilstdsqyvrqaitqgwihnwkkrgwktadkkpvknvdlwqrldaalgqhqikwe
wvkghaghpenercdelaraaamnptledtgyqvev
>d1gof_1 2.1.1.5.1 (538-639) Galactose oxidase, C-terminal domain {(Dactylium dendroides)}
gnlatrpkitrtstqsvkvggritistdssiskaslirygtathtvntdqrripltltnn
ggnsysfqvpsdsgvalpgywmlfvmnsagvpsvastirvtq
>d1gof_2 2.13.1.1.1 (1-150) Galactose oxidase, N-terminal domain {(Dactylium dendroides)}
asapigsaisrnnwavtcdsaqsgnecnkaidgnkdtfwhtfygangdpkpphtytidmk
ttqnvnglsmlprqdgnqngwigrhevylssdgtnwgspvasgswfadsttkysnfetrp
aryvrlvaiteangqpwtsiaeinvfqass
>d1gof_3 2.51.1.1.1 (151-537) Galactose oxidase, central domain {(Dactylium dendroides)}
ytapqpglgrwgptidlpivpaaaaieptsgrvlmwssyrndafggspggitltsswdps
tgivsdrtvtvtkhdmfcpgismdgngqivvtggndakktslydsssdswipgpdmqvar
gyqssatmsdgrvftiggswsggvfekngevyspssktwtslpnakvnpmltadkqglyr
sdnhawlfgwkkgsvfqagpstamnwyytsgsgdvksagkrqsnrgvapdamcgnavmyd
avkgkiltfggspdyqdsdattnahiitlgepgtspntvfasnglyfartfhtsvvlpdg
stfitggqrrgipfedstpvftpeiyvpeqdtfykqnpnsivrvyhsislllpdgrvfng
ggglcgdcttnhfdaqiftpnylynsn
>d1gog_1 2.1.1.5.1 (538-639) Galactose oxidase, C-terminal domain {(Dactylium dendroides)}
gnlatrpkitrtstqsvkvggritistdssiskaslirygtathtvntdqrripltltnn
ggnsysfqvpsdsgvalpgywmlfvmnsagvpsvastirvtq
>d1gog_2 2.13.1.1.1 (1-150) Galactose oxidase, N-terminal domain {(Dactylium dendroides)}
asapigsaisrnnwavtcdsaqsgnecnkaidgnkdtfwhtfygangdpkpphtytidmk
ttqnvnglsmlprqdgnqngwigrhevylssdgtnwgspvasgswfadsttkysnfetrp
aryvrlvaiteangqpwtsiaeinvfqass
>d1gog_3 2.51.1.1.1 (151-537) Galactose oxidase, central domain {(Dactylium dendroides)}
ytapqpglgrwgptidlpivpaaaaieptsgrvlmwssyrndafggspggitltsswdps
tgivsdrtvtvtkhdmfcpgismdgngqivvtggndakktslydsssdswipgpdmqvar
gyqssatmsdgrvftiggswsggvfekngevyspssktwtslpnakvnpmltadkqglyr
sdnhawlfgwkkgsvfqagpstamnwyytsgsgdvksagkrqsnrgvapdamcgnavmyd
avkgkiltfggspdyqdsdattnahiitlgepgtspntvfasnglyfartfhtsvvlpdg
stfitggqrrgipfedstpvftpeiyvpeqdtfykqnpnsivrvyhsislllpdgrvfng
ggglcgdcttnhfdaqiftpnylynsn
>d1goh_1 2.1.1.5.1 (538-639) Galactose oxidase, C-terminal domain {(Dactylium dendroides)}
gnlatrpkitrtstqsvkvggritistdssiskaslirygtathtvntdqrripltltnn
ggnsysfqvpsdsgvalpgywmlfvmnsagvpsvastirvtq
>d1goh_2 2.13.1.1.1 (1-150) Galactose oxidase, N-terminal domain {(Dactylium dendroides)}
asapigsaisrnnwavtcdsaqsgnecnkaidgnkdtfwhtfygangdpkpphtytidmk
ttqnvnglsmlprqdgnqngwigrhevylssdgtnwgspvasgswfadsttkysnfetrp
aryvrlvaiteangqpwtsiaeinvfqass
>d1goh_3 2.51.1.1.1 (151-537) Galactose oxidase, central domain {(Dactylium dendroides)}
ytapqpglgrwgptidlpivpaaaaieptsgrvlmwssyrndafggspggitltsswdps
tgivsdrtvtvtkhdmfcpgismdgngqivvtggndakktslydsssdswipgpdmqvar
gyqssatmsdgrvftiggswsggvfekngevyspssktwtslpnakvnpmltadkqglyr
sdnhawlfgwkkgsvfqagpstamnwyytsgsgdvksagkrqsnrgvapdamcgnavmyd
avkgkiltfggspdyqdsdattnahiitlgepgtspntvfasnglyfartfhtsvvlpdg
stfitggqrrgipfedstpvftpeiyvpeqdtfykqnpnsivrvyhsislllpdgrvfng
ggglcgdcttnhfdaqiftpnylynsn
>d1gol__ 5.1.1.1.11 MAP kinase Erk2 {rat (Rattus norvegicus)}
aaaaaagpemvrgqvfdvgprytnlsyigegaygmvcsaydnlnkvrvairkispfehqt
ycqrtlreikillrfrheniigindiiraptieqmkdvyivqdlmetdlykllktqhlsn
dhicyflyqilrglkyihsanvlhrdlkpsnlllnttcdlkicdfglarvadpdhdhtgf
lteyvatrwyrapeimlnskgytksidiwsvgcilaemlsnrpifpgkhyldqlnhilgi
lgspsqedlnciinlkarnyllslphknkvpwnrlfpnadskaldlldkmltfnphkrie
veqalahpyleqyydpsdepiaeapfkfdmelddlpkeklkelifeetarfqpgyrs
>d1gota1 1.56.1.1.2 (61-181) Transducin (alpha subunit), insertion domain {rat (Rattus rattus)}
eclefiaiiygntlqsilaivraxttlniqygdsarqddarklxhxadtieegtxpkexs
diiqrlwkdsgiqacfdraseyqlndsagyylsdlerlvtpgyvpteqdvlrsrvkttgi
i
>d1gota2 3.29.1.4.12 (6-60,182-343) Transducin (alpha subunit) {rat (Rattus rattus)}
saeekhsrelekklkedaekdartvkllllgagesgkstivkqxkiihqdgysleXetqf
sfkdlnfrxfdvggqrserkkwihcfegvtaiifcvalsdydlvlaedeexnrxhesxkl
fdsicnnkwftdtsiilflnkkdlfeekikksplticypeyagsntyeeagnyikvqfle
lnxrrdvkeiyshxtcatdtqnvkfvfdavtdiiiken
>d1gotb_ 2.51.3.1.1 beta1-subunit of the signal-transducing G protein heterotrimer {Bovine (Bos taurus)}
seldqlrqeaeqlknqirdarkacadatlsqitnnidpvgriqmrtrrtlrghlakiyam
hwgtdsrlllsasqdgkliiwdsyttnkvhaiplrsswvmtcayapsgnyvacggldnic
siynlktregnvrvsrelaghtgylsccrflddnqivtssgdttcalwdietgqqtttft
ghtgdvmslslapdtrlfvsgacdasaklwdvregmcrqtftghesdinaicffpngnaf
atgsddatcrlfdlradqelmtyshdniicgitsvsfsksgrlllagyddfncnvwdalk
adragvlaghdnrvsclgvtddgmavatgswdsflkiwn
>d1gotg_ 1.106.2.1.1 Transducin (heterotrimeric G protein), gamma chain {Bovine (Bos taurus)}
ltekdklkmevdqlkkevtlermlvskcceefrdyveersgedplvkgipedknpfke
>d1gowa_ 3.1.1.4.5 beta-Glycosidase {(Sulfolobus solfataricus)}
mysfpnsfrfgwsqagfqsemgtpgsedpntdwykwvhdpenmaaglvsgdlpengpgyw
gnyktfhdnaqkmglkiarlnsewsrqfpnplprpqnfdeskqdvteveinenelkrlde
yankdalnhyreifkdlksrglyfiqnmyhwplplwlhdpirvrrgdftgpsgwlstrtv
yefarfsaytawkfddlvdeystmnepnvvgglgyvgvksgfppgylsfelsrramynii
qaharaydgiksvskkpvgiiyanssfqpltdkdmeavemaendnrwwffdaiirgeitr
gnekivrddlkgrldwigvnyytrtvvkrtekgyvslggyghgcernsvslaglptsdfg
weffpeglydvltkywnryhlymyvtengiaddadyqrpyylvshvyqvhrainsgadvr
gylhwsladnyewasgfsmrfgllkvdyntkrlywrpsalvyreiatngaitdeiehlns
vppvkplrh
>d1gowb_ 3.1.1.4.5 beta-Glycosidase {(Sulfolobus solfataricus)}
mysfpnsfrfgwsqagfqsemgtpgsedpntdwykwvhdpenmaaglvsgdlpengpgyw
gnyktfhdnaqkmglkiarlnsewsrqfpnplprpqnfdeskqdvteveinenelkrlde
yankdalnhyreifkdlksrglyfiqnmyhwplplwlhdpirvrrgdftgpsgwlstrtv
yefarfsaytawkfddlvdeystmnepnvvgglgyvgvksgfppgylsfelsrramynii
qaharaydgiksvskkpvgiiyanssfqpltdkdmeavemaendnrwwffdaiirgeitr
gnekivrddlkgrldwigvnyytrtvvkrtekgyvslggyghgcernsvslaglptsdfg
weffpeglydvltkywnryhlymyvtengiaddadyqrpyylvshvyqvhrainsgadvr
gylhwsladnyewasgfsmrfgllkvdyntkrlywrpsalvyreiatngaitdeiehlns
vppvkplrh
>d1gox__ 3.1.7.1.3 Glycolate oxidase {spinach (Spinacia oleracea)}
meitnvneyeaiakqklpkmvydyyasgaedqwtlaenrnafsrilfrprilidvtnidm
tttilgfkismpimiaptamqkmahpegeyataraasaagtimtlsswatssveevastg
pgirffqlyvykdrnvvaqlvrraeragfkaialtvdtprlgrreadiknrfvlppfltl
knfegidlgkmdkandsglssyvagqidrslswkdvawlqtitslpilvkgvitaedarl
avqhgaagiivsnhgarqldyvpatimaleevvkaaqgripvfldggvrrgtdvfkalal
gaagvfigrpvvfslaaegeagvkkvlqmmrdefeltmalsgcrslkeisrshiaadwd
>d1gp1a_ 3.38.1.6.1 Glutathione peroxidase {bovine (Bos taurus)}
rtvyafsarplaggepfnlsslrgkvllienvaslxgttvrdytqmndlqrrlgprglvv
lgfpcnqfghqenakneeilnclkyvrpgggfepnfmlfekcevngekahplfaflrevl
ptpsddatalmtdpkfitwspvcrndvswnfekflvgpdgvpvrrysrrfltidiepdie
tllsq
>d1gp1b_ 3.38.1.6.1 Glutathione peroxidase {bovine (Bos taurus)}
rtvyafsarplaggepfnlsslrgkvllienvaslxgttvrdytqmndlqrrlgprglvv
lgfpcnqfghqenakneeilnclkyvrpgggfepnfmlfekcevngekahplfaflrevl
ptpsddatalmtdpkfitwspvcrndvswnfekflvgpdgvpvrrysrrfltidiepdie
tllsq
>d1gp2a1 1.56.1.1.2 (61-181) Transducin (alpha subunit), insertion domain {rat (Rattus rattus)}
yseeeckqykavvysntiqsiiaiiramgrlkidfgdaaraddarqlfvlagaaeegfmt
aelagvikrlwkdsgvqacfnrsreyqlndsaayylndldriaqpnyiptqqdvlrtrvk
t
>d1gp2a2 3.29.1.4.12 (5-60,182-348) Transducin (alpha subunit) {rat (Rattus rattus)}
lsaedkaaverskmidrnlredgekaarevkllllgagesgkstivkqmkiiheagXtgi
vethftfkdlhfkmfdvggqrserkkwihcfegvtaiifcvalsdydlvlaedeemnrmh
esmklfdsicnnkwftdtsiilflnkkdlfeekikksplticypeyagsntyeeaaayiq
cqfedlnkrkdtkeiythftcatdtknvqfvfdavtdviiknnl
>d1gp2b_ 2.51.3.1.1 beta1-subunit of the signal-transducing G protein heterotrimer {Bovine (Bos taurus)}
seldqlrqeaeqlknqirdarkacadatlsqitnnidpvgriqmrtrrtlrghlakiyam
hwgtdsrllvsasqdgkliiwdsyttnkvhaiplrsswvmtcayapsgnyvacggldnic
siynlktregnvrvsrelaghtgylsccrflddnqivtssgdttcalwdietgqqtttft
ghtgdvmslslapdtrlfvsgacdasaklwdvregmcrqtftghesdinaicffpngnaf
atgsddatcrlfdlradqelmtyshdniicgitsvsfsksgrlllagyddfncnvwdalk
adragvlaghdnrvsclgvtddgmavatgswdsflkiwn
>d1gp2g_ 1.106.2.1.1 Transducin (heterotrimeric G protein), gamma chain {Bovine (Bos taurus)}
siaqarklveqlkmeanidrikvskaaadlmayceahakedplltpvpasenpf
>d1gpaa_ 3.76.1.2.1 Glycogen phosphorylase {rabbit (Oryctolagus cuniculus)}
rkqisvrglagvenvtelkknfnrhlhftlvkdrnvatprdyyfalahtvrdhlvgrwir
tqqhyyekdpkriyylslefymgrtlqntmvnlalenacdeatyqlgldmeeleeieeda
glgngglgrlaacfldsmatlglaaygygiryefgifnqkicggwqmeeaddwlrygnpw
ekarpeftlpvhfygrvehtsqgakwvdtqvvlampydtpvpgyrnnvvntmrlwsakap
ndfnlkdfnvggyiqavldrnlaenisrvlypndnffegkelrlkqeyfvvaatlqdiir
rfksskfgcrdpvrtnfdafpdkvaiqlndthpslaipelmrvlvdlerldwdkawevtv
ktcaytnhtvipealerwpvhlletllprhlqiiyeinqrflnrvaaafpgdvdrlrrms
lveegavkrinmahlciagshavngvarihseilkktifkdfyelephkfqnktngitpr
rwlvlcnpglaeiiaerigeeyisdldqlrkllsyvddeafirdvakvkqenklkfaayl
ereykvhinpnslfdvqvkriheykrqllnclhvitlynrikkepnkfvvprtvmiggka
apgyhmakmiiklitaigdvvnhdpvvgdrlrviflenyrvslaekvipaadlseqista
gteasgtgnmkfmlngaltigtmdganvemaeeageenffifgmrvedvdrldqrgynaq
eyydripelrqiieqlssgffspkqpdlfkdivnmlmhhdrfkvfadyeeyvkcqervsa
lyknprewtrmvirniatsgkfssdrtiaqyareiwgvepsrqrlpap
>d1gpab_ 3.76.1.2.1 Glycogen phosphorylase {rabbit (Oryctolagus cuniculus)}
rkqisvrglagvenvtelkknfnrhlhftlvkdrnvatprdyyfalahtvrdhlvgrwir
tqqhyyekdpkriyylslefymgrtlqntmvnlalenacdeatyqlgldmeeleeieeda
glgngglgrlaacfldsmatlglaaygygiryefgifnqkicggwqmeeaddwlrygnpw
ekarpeftlpvhfygrvehtsqgakwvdtqvvlampydtpvpgyrnnvvntmrlwsakap
ndfnlkdfnvggyiqavldrnlaenisrvlypndnffegkelrlkqeyfvvaatlqdiir
rfksskfgcrdpvrtnfdafpdkvaiqlndthpslaipelmrvlvdlerldwdkawevtv
ktcaytnhtvipealerwpvhlletllprhlqiiyeinqrflnrvaaafpgdvdrlrrms
lveegavkrinmahlciagshavngvarihseilkktifkdfyelephkfqnktngitpr
rwlvlcnpglaeiiaerigeeyisdldqlrkllsyvddeafirdvakvkqenklkfaayl
ereykvhinpnslfdvqvkriheykrqllnclhvitlynrikkepnkfvvprtvmiggka
apgyhmakmiiklitaigdvvnhdpvvgdrlrviflenyrvslaekvipaadlseqista
gteasgtgnmkfmlngaltigtmdganvemaeeageenffifgmrvedvdrldqrgynaq
eyydripelrqiieqlssgffspkqpdlfkdivnmlmhhdrfkvfadyeeyvkcqervsa
lyknprewtrmvirniatsgkfssdrtiaqyareiwgvepsrqrlpapde
>d1gpac_ 3.76.1.2.1 Glycogen phosphorylase {rabbit (Oryctolagus cuniculus)}
rkqisvrglagvenvtelkknfnrhlhftlvkdrnvatprdyyfalahtvrdhlvgrwir
tqqhyyekdpkriyylslefymgrtlqntmvnlalenacdeatyqlgldmeeleeieeda
glgngglgrlaacfldsmatlglaaygygiryefgifnqkicggwqmeeaddwlrygnpw
ekarpeftlpvhfygrvehtsqgakwvdtqvvlampydtpvpgyrnnvvntmrlwsakap
ndfnlkdfnvggyiqavldrnlaenisrvlypndnffegkelrlkqeyfvvaatlqdiir
rfksskfgcrdpvrtnfdafpdkvaiqlndthpslaipelmrvlvdlerldwdkawevtv
ktcaytnhtvipealerwpvhlletllprhlqiiyeinqrflnrvaaafpgdvdrlrrms
lveegavkrinmahlciagshavngvarihseilkktifkdfyelephkfqnktngitpr
rwlvlcnpglaeiiaerigeeyisdldqlrkllsyvddeafirdvakvkqenklkfaayl
ereykvhinpnslfdvqvkriheykrqllnclhvitlynrikkepnkfvvprtvmiggka
apgyhmakmiiklitaigdvvnhdpvvgdrlrviflenyrvslaekvipaadlseqista
gteasgtgnmkfmlngaltigtmdganvemaeeageenffifgmrvedvdrldqrgynaq
eyydripelrqiieqlssgffspkqpdlfkdivnmlmhhdrfkvfadyeeyvkcqervsa
lyknprewtrmvirniatsgkfssdrtiaqyareiwgvepsrqrlpap
>d1gpad_ 3.76.1.2.1 Glycogen phosphorylase {rabbit (Oryctolagus cuniculus)}
rkqisvrglagvenvtelkknfnrhlhftlvkdrnvatprdyyfalahtvrdhlvgrwir
tqqhyyekdpkriyylslefymgrtlqntmvnlalenacdeatyqlgldmeeleeieeda
glgngglgrlaacfldsmatlglaaygygiryefgifnqkicggwqmeeaddwlrygnpw
ekarpeftlpvhfygrvehtsqgakwvdtqvvlampydtpvpgyrnnvvntmrlwsakap
ndfnlkdfnvggyiqavldrnlaenisrvlypndnffegkelrlkqeyfvvaatlqdiir
rfksskfgcrdpvrtnfdafpdkvaiqlndthpslaipelmrvlvdlerldwdkawevtv
ktcaytnhtvipealerwpvhlletllprhlqiiyeinqrflnrvaaafpgdvdrlrrms
lveegavkrinmahlciagshavngvarihseilkktifkdfyelephkfqnktngitpr
rwlvlcnpglaeiiaerigeeyisdldqlrkllsyvddeafirdvakvkqenklkfaayl
ereykvhinpnslfdvqvkriheykrqllnclhvitlynrikkepnkfvvprtvmiggka
apgyhmakmiiklitaigdvvnhdpvvgdrlrviflenyrvslaekvipaadlseqista
gteasgtgnmkfmlngaltigtmdganvemaeeageenffifgmrvedvdrldqrgynaq
eyydripelrqiieqlssgffspkqpdlfkdivnmlmhhdrfkvfadyeeyvkcqervsa
lyknprewtrmvirniatsgkfssdrtiaqyareiwgvepsrqrlpap
>d1gpb__ 3.76.1.2.1 Glycogen phosphorylase {rabbit (Oryctolagus cuniculus)}
agvenvtelkknfnrhlhftlvkdrnvatprdyyfalahtvrdhlvgrwirtqqhyyekd
pkriyylslefymgrtlqntmvnlalenacdeatyqlgldmeeleeieedaglgngglgr
laacfldsmatlglaaygygiryefgifnqkicggwqmeeaddwlrygnpwekarpeftl
pvhfygrvehtsqgakwvdtqvvlampydtpvpgyrnnvvntmrlwsakapndfnlkdfn
vggyiqavldrnlaenisrvlypndnffegkelrlkqeyfvvaatlqdiirrfksskfgc
rdpvrtnfdafpdkvaiqlndthpslaipelmrvlvdlerldwdkawevtvktcaytnht
vipealerwpvhlletllprhlqiiyeinqrflnrvaaafpgdvdrlrrmslveegavkr
inmahlciagshavngvarihseilkktifkdfyelephkfqnktngitprrwlvlcnpg
laeiiaerigeeyisdldqlrkllsyvddeafirdvakvkqenklkfaaylereykvhin
pnslfdvqvkriheykrqllnclhvitlynrikkepnkfvvprtvmiggkaapgyhmakm
iiklitaigdvvnhdpvvgdrlrviflenyrvslaekvipaadlseqistagteasgtgn
mkfmlngaltigtmdganvemaeeageenffifgmrvedvdrldqrgynaqeyydripel
rqiieqlssgffspkqpdlfkdivnmlmhhdrfkvfadyeeyvkcqervsalyknprewt
rmvirniatsgkfssdrtiaqyareiwgvepsrqrlpapdeki
>d1gpc__ 2.29.4.8.3 Gene 32 protein (GP32) core {bacteriophage T4}
gfssedkgewklkldnagngqavirflpskndeqapfailvnhgfkkngkwyietcssth
gdydscpvcqyiskndlyntdnkeyslvkrktsywanilvvkdpaapenegkvfkyrfgk
kiwdkinamiavdvemgetpvdvtcpweganfvlkvkqvsgfsnydeskflnqsaipnid
desfqkelfeqmvdlsemtskdkfksfeelntkfgqvm
>d1gpdg1 3.22.1.3.7 (1-148,313-334) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {lobster (Homarus americanus)}
skigingfgrigrlvlraalscgaqvvavndpfialeymvymfkydsthgvfkgevkmed
galvvdgkkitvfnemkpenipwskagaeyivestgvfttiekasahfkggakkvvisap
sadapmfvcgvnlekyskdmtvvsnasXnefgysqrvidllkhmqkvdsa
>d1gpdg2 4.42.1.1.7 (149-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {lobster (Homarus americanus)}
cttnclapvakvlhenfeiveglmttvhavtatqktvdgpsakdwrggrgaaqniipsst
gaakavgkvipeldgkltgmafrvptpdvsvvdltvrlgkecsyddikaamktasegplq
gflgyteddvvssdfigdnrssifdakagiqlsktfvkvvswyd
>d1gpdr1 3.22.1.3.7 (1-148,313-334) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {lobster (Homarus americanus)}
skigingfgrigrlvlraalscgaqvvavndpfialeymvymfkydsthgvfkgevkmed
galvvdgkkitvfnemkpenipwskagaeyivestgvfttiekasahfkggakkvvisap
sadapmfvcgvnlekyskdmtvvsnasXnefgysqrvidllkhmqkvdsa
>d1gpdr2 4.42.1.1.7 (149-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {lobster (Homarus americanus)}
cttnclapvakvlhenfeiveglmttvhavtatqktvdgpsakdwrggrgaaqniipsst
gaakavgkvipeldgkltgmafrvptpdvsvvdltvrlgkecsyddikaamktasegplq
gflgyteddvvssdfigdnrssifdakagiqlsktfvkvvswyd
>d1gph11 3.49.1.1.4 (235-465) Glutamine PRPP amidotransferase, C-terminal domain {(Bacillus subtilis)}
icsmeyiyfsrpdsnidginvhsarknlgkmlaqesaveadvvtgvpdssisaaigyaea
tgipyelgliknryvgrtfiqpsqalreqgvrmklsavrgvvegkrvvmvddsivrgtts
rrivtmlreagatevhvkissppiahpcfygidtstheeliasshsvdeirqeigadtls
flsvegllkgigrkyddsncgqclacftgkypteiyqdtvlphvkeavltk
>d1gph12 4.95.1.1.2 (1-234) Glutamine PRPP amidotransferase, N-terminal domain {(Bacillus subtilis)}
cgvfgiwgheeapqityyglhslqhrgqegagivatdgekltahkgqglitevfqngels
kvkgkgaighvryataggggyenvqpllfrsqnngslalahngnlvnatqlkqqlenqgs
ifqtssdtevlahlikrsghftlkdqiknslsmlkgayaflimtetemivaldpnglrpl
sigmmgdayvvasetcafdvvgatylrevepgemliindegmkserfsmninrs
>d1gph21 3.49.1.1.4 (235-465) Glutamine PRPP amidotransferase, C-terminal domain {(Bacillus subtilis)}
icsmeyiyfsrpdsnidginvhsarknlgkmlaqesaveadvvtgvpdssisaaigyaea
tgipyelgliknryvgrtfiqpsqalreqgvrmklsavrgvvegkrvvmvddsivrgtts
rrivtmlreagatevhvkissppiahpcfygidtstheeliasshsvdeirqeigadtls
flsvegllkgigrkyddsncgqclacftgkypteiyqdtvlphvkeavltk
>d1gph22 4.95.1.1.2 (1-234) Glutamine PRPP amidotransferase, N-terminal domain {(Bacillus subtilis)}
cgvfgiwgheeapqityyglhslqhrgqegagivatdgekltahkgqglitevfqngels
kvkgkgaighvryataggggyenvqpllfrsqnngslalahngnlvnatqlkqqlenqgs
ifqtssdtevlahlikrsghftlkdqiknslsmlkgayaflimtetemivaldpnglrpl
sigmmgdayvvasetcafdvvgatylrevepgemliindegmkserfsmninrs
>d1gph31 3.49.1.1.4 (235-465) Glutamine PRPP amidotransferase, C-terminal domain {(Bacillus subtilis)}
icsmeyiyfsrpdsnidginvhsarknlgkmlaqesaveadvvtgvpdssisaaigyaea
tgipyelgliknryvgrtfiqpsqalreqgvrmklsavrgvvegkrvvmvddsivrgtts
rrivtmlreagatevhvkissppiahpcfygidtstheeliasshsvdeirqeigadtls
flsvegllkgigrkyddsncgqclacftgkypteiyqdtvlphvkeavltk
>d1gph32 4.95.1.1.2 (1-234) Glutamine PRPP amidotransferase, N-terminal domain {(Bacillus subtilis)}
cgvfgiwgheeapqityyglhslqhrgqegagivatdgekltahkgqglitevfqngels
kvkgkgaighvryataggggyenvqpllfrsqnngslalahngnlvnatqlkqqlenqgs
ifqtssdtevlahlikrsghftlkdqiknslsmlkgayaflimtetemivaldpnglrpl
sigmmgdayvvasetcafdvvgatylrevepgemliindegmkserfsmninrs
>d1gph41 3.49.1.1.4 (235-465) Glutamine PRPP amidotransferase, C-terminal domain {(Bacillus subtilis)}
icsmeyiyfsrpdsnidginvhsarknlgkmlaqesaveadvvtgvpdssisaaigyaea
tgipyelgliknryvgrtfiqpsqalreqgvrmklsavrgvvegkrvvmvddsivrgtts
rrivtmlreagatevhvkissppiahpcfygidtstheeliasshsvdeirqeigadtls
flsvegllkgigrkyddsncgqclacftgkypteiyqdtvlphvkeavltk
>d1gph42 4.95.1.1.2 (1-234) Glutamine PRPP amidotransferase, N-terminal domain {(Bacillus subtilis)}
cgvfgiwgheeapqityyglhslqhrgqegagivatdgekltahkgqglitevfqngels
kvkgkgaighvryataggggyenvqpllfrsqnngslalahngnlvnatqlkqqlenqgs
ifqtssdtevlahlikrsghftlkdqiknslsmlkgayaflimtetemivaldpnglrpl
sigmmgdayvvasetcafdvvgatylrevepgemliindegmkserfsmninrs
>d1gpl_1 2.10.2.1.4 (337-449) Pancreatic lipase, C-terminal domain {Guinea pig (Cavia porcellus)}
rwrykvsvtlsgkkvtghilvslfgnkgnskqyeifkgtlkpdsthsnefdsdvdvgdlq
mvkfiwynnvinptlprvgaskiivetnvgkqfnfcspetvreevlltltpc
>d1gpl_2 3.56.1.11.4 (1-336) Pancreatic lipase, N-terminal domain {Guinea pig (Cavia porcellus)}
aevcyshlgcfsdekpwagtsqrpikslpsdpkkintrfllytnenqnsyqlitatdiat
ikasnfnlnrktrfiihgftdsgenswlsdmcknmfqvekvncicvdwkggskaqysqas
qnirvvgaevaylvqvlstslnyapenvhiighslgahtageagkrlnglvgritgldpa
epyfqdtpeevrldpsdakfvdvihtdispilpslgfgmsqkvghmdffpnggkdmpgck
tgiscnhhrsieyyhssilnpegflgypcasydefqesgcfpcpakgcpkmghfadqypg
ktnaveqtfflntgasdnft
>d1gpma1 3.17.2.1.1 (208-404) GMP synthetase, central domain {(Escherichia coli)}
wtpakiiddavarireqvgddkvilglsggvdssvtamllhraigknltcvfvdngllrl
neaeqvldmfgdhfglnivhvpaedrflsalagendpeakrkiigrvfvevfdeealkle
dvkwlaqgtiypdviesaasatgkahvikshhnvgglpkemkmglveplkelfkdevrki
glelglpydmlyrhpfp
>d1gpma2 3.55.1.1.1 (3-207) GMP synthetase {(Escherichia coli)}
enihkhrilildfgsqytqlvarrvrelgvycelwawdvteaqirdfnpsgiilsggpes
tteensprapqyvfeagvpvfgvcygmqtmamqlgghveasnerefgyaqvevvndsalv
rgiedaltadgkplldvwmshgdkvtaipsdfitvastescpfaimaneekrfygvqfhp
evthtrqgmrmlerfvrdicqceal
>d1gpma3 4.31.1.1.1 (405-525) GMP synthetase, the C-terminal, dimerisation domain {(Escherichia coli)}
gpglgvrvlgevkkeycdllrradaifieelrkadlydkvsqaftvflpvrsvgvmgdgr
kydwvvslravetidfmtahwahlpydflgrvsnriinevngisrvvydisgkppatiew
e
>d1gpmb1 3.17.2.1.1 (208-404) GMP synthetase, central domain {(Escherichia coli)}
wtpakiiddavarireqvgddkvilglsggvdssvtamllhraigknltcvfvdngllrl
neaeqvldmfgdhfglnivhvpaedrflsalagendpeakrkiigrvfvevfdeealkle
dvkwlaqgtiypdviesaasatgkahvikshhnvgglpkemkmglveplkelfkdevrki
glelglpydmlyrhpfp
>d1gpmb2 3.55.1.1.1 (3-207) GMP synthetase {(Escherichia coli)}
enihkhrilildfgsqytqlvarrvrelgvycelwawdvteaqirdfnpsgiilsggpes
tteensprapqyvfeagvpvfgvcygmqtmamqlgghveasnerefgyaqvevvndsalv
rgiedaltadgkplldvwmshgdkvtaipsdfitvastescpfaimaneekrfygvqfhp
evthtrqgmrmlerfvrdicqceal
>d1gpmb3 4.31.1.1.1 (405-525) GMP synthetase, the C-terminal, dimerisation domain {(Escherichia coli)}
gpglgvrvlgevkkeycdllrradaifieelrkadlydkvsqaftvflpvrsvgvmgdgr
kydwvvslravetidfmtahwahlpydflgrvsnriinevngisrvvydisgkppatiew
e
>d1gpmc1 3.17.2.1.1 (208-404) GMP synthetase, central domain {(Escherichia coli)}
wtpakiiddavarireqvgddkvilglsggvdssvtamllhraigknltcvfvdngllrl
neaeqvldmfgdhfglnivhvpaedrflsalagendpeakrkiigrvfvevfdeealkle
dvkwlaqgtiypdviesaasatgkahvikshhnvgglpkemkmglveplkelfkdevrki
glelglpydmlyrhpfp
>d1gpmc2 3.55.1.1.1 (3-207) GMP synthetase {(Escherichia coli)}
enihkhrilildfgsqytqlvarrvrelgvycelwawdvteaqirdfnpsgiilsggpes
tteensprapqyvfeagvpvfgvcygmqtmamqlgghveasnerefgyaqvevvndsalv
rgiedaltadgkplldvwmshgdkvtaipsdfitvastescpfaimaneekrfygvqfhp
evthtrqgmrmlerfvrdicqceal
>d1gpmc3 4.31.1.1.1 (405-525) GMP synthetase, the C-terminal, dimerisation domain {(Escherichia coli)}
gpglgvrvlgevkkeycdllrradaifieelrkadlydkvsqaftvflpvrsvgvmgdgr
kydwvvslravetidfmtahwahlpydflgrvsnriinevngisrvvydisgkppatiew
e
>d1gpmd1 3.17.2.1.1 (208-404) GMP synthetase, central domain {(Escherichia coli)}
wtpakiiddavarireqvgddkvilglsggvdssvtamllhraigknltcvfvdngllrl
neaeqvldmfgdhfglnivhvpaedrflsalagendpeakrkiigrvfvevfdeealkle
dvkwlaqgtiypdviesaasatgkahvikshhnvgglpkemkmglveplkelfkdevrki
glelglpydmlyrhpfp
>d1gpmd2 3.55.1.1.1 (3-207) GMP synthetase {(Escherichia coli)}
enihkhrilildfgsqytqlvarrvrelgvycelwawdvteaqirdfnpsgiilsggpes
tteensprapqyvfeagvpvfgvcygmqtmamqlgghveasnerefgyaqvevvndsalv
rgiedaltadgkplldvwmshgdkvtaipsdfitvastescpfaimaneekrfygvqfhp
evthtrqgmrmlerfvrdicqceal
>d1gpmd3 4.31.1.1.1 (405-525) GMP synthetase, the C-terminal, dimerisation domain {(Escherichia coli)}
gpglgvrvlgevkkeycdllrradaifieelrkadlydkvsqaftvflpvrsvgvmgdgr
kydwvvslravetidfmtahwahlpydflgrvsnriinevngisrvvydisgkppatiew
e
>d1gpoh1 2.1.1.1.97 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab M41 (artifitial design)}
evklqesgpslvkpsqtlsltcsvtgdsitsdfwswirqfpgnrleymgfvqysgetayn
pslksrisitrdtsknqyyldlnsvttedtavyycanwhgdywgqgttvtvss
>d1gpoh2 2.1.1.2.97 (114-214) Immunoglobulin (constant domains of L and H chains) {Fab M41 (artifitial design)}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpsstwpsetvtcnvahpasstkvdkkivprd
>d1gpoi1 2.1.1.1.97 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab M41 (artifitial design)}
evklqesgpslvkpsqtlsltcsvtgdsitsdfwswirqfpgnrleymgfvqysgetayn
pslksrisitrdtsknqyyldlnsvttedtavyycanwhgdywgqgttvtvss
>d1gpoi2 2.1.1.2.97 (114-212) Immunoglobulin (constant domains of L and H chains) {Fab M41 (artifitial design)}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpsstwpsetvtcnvahpasstkvdkkivp
>d1gpol1 2.1.1.1.97 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab M41 (artifitial design)}
dieltqspatlsvtpgnsvsiscrasqslvnedgntylfwyqqkshesprllikyasqsi
sgipsrfsgsgsgtdftlsinsvetedlavyfcqqitdwpftfgggtkleik
>d1gpol2 2.1.1.2.97 (113-216) Immunoglobulin (constant domains of L and H chains) {Fab M41 (artifitial design)}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1gpom1 2.1.1.1.97 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab M41 (artifitial design)}
dieltqspatlsvtpgnsvsiscrasqslvnedgntylfwyqqkshesprllikyasqsi
sgipsrfsgsgsgtdftlsinsvetedlavyfcqqitdwpftfgggtkleik
>d1gpom2 2.1.1.2.97 (113-215) Immunoglobulin (constant domains of L and H chains) {Fab M41 (artifitial design)}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfn
>d1gpr__ 2.65.3.1.1 Glucose permease IIa domain, IIa-glc {(Bacillus subtilis)}
eplqneigeevfvspitgeihpitdvpdqvfsgkmmgdgfailpsegivvspvrgkilnv
fptkhaiglqsdggreilihfgidtvslkgegftsfvsegdrvepgqkllevdldavkpn
vpslmtpivftnlaegetvsikasgsvnreqedivkie
>d1gps__ 7.3.6.4.2 gamma-Thionin {wheat (Triticum turgidum)}
kicrrrsagfkgpcmsnkncaqvcqqegwgggncdgpfrrckcirqc
>d1gpt__ 7.3.6.4.1 gamma-Thionin {barley (Hordeum vulgare)}
ricrrrsagfkgpcvsnkncaqvcmqegwgggncdgplrrckcmrrc
>d1gpy__ 3.76.1.2.1 Glycogen phosphorylase {rabbit (Oryctolagus cuniculus)}
svrglagvenvtelkknfnrhlhftlvkdrnvatprdyyfalahtvrdhlvgrwirtqqh
yyekdpkriyylslefymgrtlqntmvnlalenacdeatyqlgldmeeleeieedaglgn
gglgrlaacfldsmatlglaaygygiryefgifnqkicggwqmeeaddwlrygnpwekar
peftlpvhfygrvehtsqgakwvdtqvvlampydtpvpgyrnnvvntmrlwsakapndfn
lkdfnvggyiqavldrnlaenisrvlypndnffegkelrlkqeyfvvaatlqdiirrfks
skfgcrdpvrtnfdafpdkvaiqlndthpslaipelmrvlvdlerldwdkawevtvktca
ytnhtvlpealerwpvhlletllprhlqiiyeinqrflnrvaaafpgdvdrlrrmslvee
gavkrinmahlciagshavngvarihseilkktifkdfyelephkfqnktngitprrwlv
lcnpglaeiiaerigeeyisdldqlrkllsyvddeafirdvakvkqenklkfaaylerey
kvhinpnslfdvqvkriheykrqllnclhvitlynrikkepnkfvvprtvmiggkaapgy
hmakmiiklitaigdvvnhdpvvgdrlrviflenyrvslaekvipaadlseqistagtea
sgtgnmkfmlngaltigtmdganvemaeeageenffifgmrvedvdrldqrgynaqeyyd
ripelrqiieqlssgffspkqpdlfkdivnmlmhhdrfkvfadyeeyvkcqervsalykn
prewtrmvirniatsgkfssdrtiaqyareiwgvepsrqrlpapdeki
>d1gra_1 3.4.1.4.1 (18-165,291-363) Glutathione reductase {human (Homo sapiens)}
vasydylvigggsgglasarraaelgaraavveshklggtcvnvgcvpkkvmwntavhse
fmhdhadygfpscegkfnwrvikekrdayvsrlnaiyqnnltkshieiirghaaftsdpk
ptievsgkkytaphiliatggmpstpheXrvpntkdlslnklgiqtddkghiivdefqnt
nvkgiyavgdvcgkalltpvaiaagrklahrlfeykedskld
>d1gra_2 3.4.1.4.1 (166-290) Glutathione reductase {human (Homo sapiens)}
sqipgaslgitsdgffqleelpgrsvivgagyiavemagilsalgsktslmirhdkvlrs
fdsmistncteelenagvevlkfsqvkevkktlsglevsmvtavpgrlpvmtmipdvdcl
lwaig
>d1gra_3 4.48.1.1.1 (364-478) Glutathione reductase {human (Homo sapiens)}
ynniptvvfshppigtvgltedeaihkygienvktystsftpmyhavtkrktkcvmkmvc
ankeekvvgihmqglgcdemlqgfavavkmgatkadfdntvaihptsseelvtlr
>d1grb_1 3.4.1.4.1 (18-165,291-363) Glutathione reductase {human (Homo sapiens)}
vasydylvigggsgglasarraaelgaraavveshklggtcvnvgcvpkkvmwntavhse
fmhdhadygfpscegkfnwrvikekrdayvsrlnaiyqnnltkshieiirghaaftsdpk
ptievsgkkytaphiliatggmpstpheXrvpntkdlslnklgiqtddkghiivdefqnt
nvkgiyavgdvcgkalltpvaiaagrklahrlfeykedskld
>d1grb_2 3.4.1.4.1 (166-290) Glutathione reductase {human (Homo sapiens)}
sqipgaslgitsdgffqleelpgrsvivgagyiavemagilsalgsktslmirhdkvlrs
fdsmistncteelenagvevlkfsqvkevkktlsglevsmvtavpgrlpvmtmipdvdcl
lwaig
>d1grb_3 4.48.1.1.1 (364-478) Glutathione reductase {human (Homo sapiens)}
ynniptvvfshppigtvgltedeaihkygienvktystsftpmyhavtkrktkcvmkmvc
ankeekvvgihmqglgcdemlqgfavavkmgatkadfdntvaihptsseelvtlr
>d1grca_ 3.52.1.1.1 Glycinamide ribonucleotide transformylase {(Escherichia coli), k12 strain tx635, with plasmid pjs167}
mnivvlisgngsnlqaiidacktnkikgtvravfsnkadafglerarqagiathtliasa
fdsreaydreliheidmyapdvvvlagfmrilspafvshyagrllnihpsllpkypglht
hrqalengdeehgtsvhfvtdeldggpvilqakvpvfagdsedditarvqtqehaiyplv
iswfadgrlkmhenaawldgqrlppqgya
>d1grcb_ 3.52.1.1.1 Glycinamide ribonucleotide transformylase {(Escherichia coli), k12 strain tx635, with plasmid pjs167}
mnivvlisgngsnlqaiidacktnkikgtvravfsnkadafglerarqagiathtliasa
fdsreaydreliheidmyapdvvvlagfmrilspafvshyagrllnihpsllpkypglht
hrqalengdeehgtsvhfvtdeldggpvilqakvpvfagdsedditarvqtqehaiyplv
iswfadgrlkmhenaawldgqrlppqgya
>d1gre_1 3.4.1.4.1 (18-165,291-363) Glutathione reductase {human (Homo sapiens)}
vasydylvigggsgglasarraaelgaraavveshklggtcvnvgcvpkkvmwntavhse
fmhdhadygfpscegkfnwrvikekrdayvsrlnaiyqnnltkshieiirghaaftsdpk
ptievsgkkytaphiliatggmpstpheXrvpntkdlslnklgiqtddkghiivdefqnt
nvkgiyavgdvcgkalltpvaiaagrklahrlfeykedskld
>d1gre_2 3.4.1.4.1 (166-290) Glutathione reductase {human (Homo sapiens)}
sqipgaslgitsdgffqleelpgrsvivgagyiavemagilsalgsktslmirhdkvlrs
fdsmistncteelenagvevlkfsqvkevkktlsglevsmvtavpgrlpvmtmipdvdcl
lwaig
>d1gre_3 4.48.1.1.1 (364-478) Glutathione reductase {human (Homo sapiens)}
ynniptvvfshppigtvgltedeaihkygienvktystsftpmyhavtkrktkcvmkmvc
ankeekvvgihmqglgcdemlqgfavavkmgatkadfdntvaihptsseelvtlr
>d1grf_1 3.4.1.4.1 (18-165,291-363) Glutathione reductase {human (Homo sapiens)}
vasydylvigggsgglasarraaelgaraavveshklggtcvnvgcvpkkvmwntavhse
fmhdhadygfpscegkfnwrvikekrdayvsrlnaiyqnnltkshieiirghaaftsdpk
ptievsgkkytaphiliatggmpstpheXrvpntkdlslnklgiqtddkghiivdefqnt
nvkgiyavgdvcgkalltpvaiaagrklahrlfeykedskld
>d1grf_2 3.4.1.4.1 (166-290) Glutathione reductase {human (Homo sapiens)}
sqipgaslgitsdgffqleelpgrsvivgagyiavemagilsalgsktslmirhdkvlrs
fdsmistncteelenagvevlkfsqvkevkktlsglevsmvtavpgrlpvmtmipdvdcl
lwaig
>d1grf_3 4.48.1.1.1 (364-478) Glutathione reductase {human (Homo sapiens)}
ynniptvvfshppigtvgltedeaihkygienvktystsftpmyhavtkrktkcvmkmvc
ankeekvvgihmqglgcdemlqgfavavkmgatkadfdntvaihptsseelvtlr
>d1grg_1 3.4.1.4.1 (18-165,291-363) Glutathione reductase {human (Homo sapiens)}
vasydylvigggsgglasarraaelgaraavveshklggtcvnvgcvpkkvmwntavhse
fmhdhadygfpscegkfnwrvikekrdayvsrlnaiyqnnltkshieiirghaaftsdpk
ptievsgkkytaphiliatggmpstpheXrvpntkdlslnklgiqtddkghiivdefqnt
nvkgiyavgdvcgkalltpvaiaagrklahrlfeykedskld
>d1grg_2 3.4.1.4.1 (166-290) Glutathione reductase {human (Homo sapiens)}
sqipgaslgitsdgffqleelpgrsvivgagyiavemagilsalgsktslmirhdkvlrs
fdsmistncteelenagvevlkfsqvkevkktlsglevsmvtavpgrlpvmtmipdvdcl
lwaig
>d1grg_3 4.48.1.1.1 (364-478) Glutathione reductase {human (Homo sapiens)}
ynniptvvfshppigtvgltedeaihkygienvktystsftpmyhavtkrktkcvmkmvc
ankeekvvgihmqglgcdemlqgfavavkmgatkadfdntvaihptsseelvtlr
>d1gria1 2.24.2.1.14 (1-56) Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {human (Homo sapiens)}
meaiakydfkataddelsfkrgdilkvlneecdqnwykaelngkdgfipknyiemk
>d1gria2 2.24.2.1.14 (157-217) Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {human (Homo sapiens)}
qptyvqalfdfdpqedgelgfrrgdfihvmdnsdpnwwkgachgqtgmfprnyvtpvnrn
v
>d1gria3 4.53.1.1.7 (57-156) Growth factor receptor-bound protein 2 (GRB2) {human (Homo sapiens)}
phpwffgkiprakaeemlskqrhdgafliresesapgdfslsvkfgndvqhfkvlrdgag
kyflwvvkfnslnelvdyhrstsvsrnqqiflrdieqvpq
>d1grib1 2.24.2.1.14 (1-56) Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {human (Homo sapiens)}
meaiakydfkataddelsfkrgdilkvlneecdqnwykaelngkdgfipknyiemk
>d1grib2 2.24.2.1.14 (157-217) Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {human (Homo sapiens)}
qptyvqalfdfdpqedgelgfrrgdfihvmdnsdpnwwkgachgqtgmfprnyvtpvnrn
v
>d1grib3 4.53.1.1.7 (57-156) Growth factor receptor-bound protein 2 (GRB2) {human (Homo sapiens)}
phpwffgkiprakaeemlskqrhdgafliresesapgdfslsvkfgndvqhfkvlrdgag
kyflwvvkfnslnelvdyhrstsvsrnqqiflrdieqvpq
>d1grj_1 1.2.1.1.1 (2-79) GreA transcript cleavage protein, N-terminal domain {(Escherichia coli)}
qaipmtlrgaeklreeldflksvrrpeiiaaiaearehgdlkenaeyhaareqqgfcegr
ikdieaklsnaqvidvtk
>d1grj_2 4.19.4.1.1 (80-158) GreA transcript cleavage factor, C-terminal domain {(Escherichia coli)}
mpnngrvifgatvtvlnldsdeeqtyrivgddeadfkqnlisvnspiargligkeeddvv
viktpggevefevikveyl
>d1grl_1 1.100.1.1.1 (6-136,410-523) GroEL, the ATPase domain {(Escherichia coli)}
vkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareieledk
fenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgidkavt
vaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrqivln
cgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvaglmitt
ecmvtd
>d1grl_2 3.5.4.1.1 (191-366) GroEL {(Escherichia coli)}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatavvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1grl_3 4.33.1.1.1 (137-190,376-409) The intermediate domain of GroEL {(Escherichia coli)}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXvavik
vgaatevemkekkarvedalhatraavee
>d1gro__ 3.65.1.1.5 Isocitrate dehydrogenase {(Escherichia coli)}
skvvvpaqgkkitlqngklnvpenpiipyiegdgigvdvtpamlkvvdaavekaykgerk
iswmeiytgekstqvygqdvwlpaetldlireyrvaikgplttpvgggirellvalrqel
dlyiclrpvryyqgtpspvkhpeltdmvifrensediyagiewkadsadaekvikflree
mgvkkirfpdhcgigikpcseegtkrlvraaieyaiandrdsvtlvhkgnimkftegafk
dwgyqlareefggelidggpwlkvknpntgkeivikdviadaflqqillrpaeydviacm
nlngdyisdalaaqvggigiapganigdecalfeathgtapkyagqdkvnpgsiilsaem
mlrhmgwteaadlivkgmegainaktvtydferlmdgakllkcsefgdaiienm
>d1grp__ 3.65.1.1.5 Isocitrate dehydrogenase {(Escherichia coli)}
skvvvpaqgkkitlqngklnvpenpiipyiegdgigvdvtpamlkvvdaavekaykgerk
iswmeiytgekstqvygqdvwlpaetldlireyrvaikgplttpvgggirsllvalrqel
dlyiclrpvryyqgtpspvkhpeltdmvifrensediyagiewkadsadaekvikflree
mgvkkirfpdhcgigikpcseegtkrlvraaieyaiandrdsvtlvhkgnimkftegafk
dwgyqlareefggelidggpwlkvknpntgkeivikdviadaflqqillrpaeydviacm
nlngdyisdalaaqvggigiapganigdecalfeathgtapkyagqdkvnpgsiilsaem
mlrhmgwteaadlivkgmegainaktvtydferlmdgakllkcsefgdaiienm
>d1grt_1 3.4.1.4.1 (17-165,291-363) Glutathione reductase {human (Homo sapiens)}
avasydylvigggsgglesawraaelgaraavveshklggtcvnvgcvpkkvmwntavhs
efmhdhadygfpscegkfnwrvikekrdayvsrlnaiyqnnltkshieiirghaaftsdp
kptievsgkkytaphiliatggmpstpheXrvpntkdlslnklgiqtddkghiivdefqn
tnvkgiyavgdvcgkalltpvaiaagrklahrlfeykedskld
>d1grt_2 3.4.1.4.1 (166-290) Glutathione reductase {human (Homo sapiens)}
sqipgaslgitsdgffqleelpgrsvivgagyiavemagilsalgsktslmirhdkvlrs
fdsmistncteelenagvevlkfsqvkevkktlsglevsmvtavpgrlpvmtmipdvdcl
lwaig
>d1grt_3 4.48.1.1.1 (364-478) Glutathione reductase {human (Homo sapiens)}
ynniptvvfshppigtvgltedeaihkygienvktystsftpmyhavtkrktkcvmkmvc
ankeekvvgihmqglgcdemlqgfavavkmgatkadfdntvaihptsseelvtlr
>d1grx__ 3.38.1.1.5 Glutaredoxin {(bacteriophage t4)}
mqtvifgrsgcpysvrakdlaeklsnerddfqyqyvdiraegitkedlqqkagkpvetvp
qifvdqqhiggytdfaawvkenlda
>d1gsa_1 3.23.1.3.1 (1-122) Glutathione synthetase, N-terminal domain {(Escherichia coli)}
miklgivmdpianinikkdssfamlleaqrrgyelhymemgdlylingearahtrtlnvk
qnyeewfsfvgeqdlpladldvilmrkdppfdtefiyatyileraeekgtlivnkpqslr
dc
>d1gsa_2 4.89.1.1.1 (123-314) Glutathione synthetase {(Escherichia coli)}
neklftawfsdltpetlvtrnkaqlkafwekhsdiilkpldgmggasifrvkegdpnlgv
iaetltehgtrycmaqnylpaikdgdkrvlvvdgepvpyclaripqggetrgnlaaggrg
eprpltesdwkiarqigptlkekglifvgldiigdrlteinvtsptcireieaefpvsit
gmlmdaiearlq
>d1gsba1 1.43.1.1.1 (85-217) Glutathione S-transferase {rat (Rattus rattus), class mu}
lcgeteeeriradivenqvmdnrmqlimlcynpdfekqkpeflktipekmklyseflgkr
pwfagdkvtyvdflaydildqyhifepkcldafpnlkdflarfeglkkisaymkssryls
tpifsklaqwsnk
>d1gsba2 3.38.1.4.1 (1-84) Glutathione S-transferase {rat (Rattus rattus)}
pmilgywnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d1gsbb1 1.43.1.1.1 (85-217) Glutathione S-transferase {rat (Rattus rattus), class mu}
lcgeteeeriradivenqvmdnrmqlimlcynpdfekqkpeflktipekmklyseflgkr
pwfagdkvtyvdflaydildqyhifepkcldafpnlkdflarfeglkkisaymkssryls
tpifsklaqwsnk
>d1gsbb2 3.38.1.4.1 (1-84) Glutathione S-transferase {rat (Rattus rattus)}
pmilgywnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d1gsbc1 1.43.1.1.1 (85-217) Glutathione S-transferase {rat (Rattus rattus), class mu}
lcgeteeeriradivenqvmdnrmqlimlcynpdfekqkpeflktipekmklyseflgkr
pwfagdkvtyvdflaydildqyhifepkcldafpnlkdflarfeglkkisaymkssryls
tpifsklaqwsnk
>d1gsbc2 3.38.1.4.1 (1-84) Glutathione S-transferase {rat (Rattus rattus)}
pmilgywnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d1gsbd1 1.43.1.1.1 (85-217) Glutathione S-transferase {rat (Rattus rattus), class mu}
lcgeteeeriradivenqvmdnrmqlimlcynpdfekqkpeflktipekmklyseflgkr
pwfagdkvtyvdflaydildqyhifepkcldafpnlkdflarfeglkkisaymkssryls
tpifsklaqwsnk
>d1gsbd2 3.38.1.4.1 (1-84) Glutathione S-transferase {rat (Rattus rattus)}
pmilgywnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d1gsca1 1.43.1.1.1 (85-217) Glutathione S-transferase {rat (Rattus rattus), class mu}
lcgeteeeriradivenqvmdnrmqlimlcynpdfekqkpeflktipekmklyseflgkr
pwfagdkvtyvdflaydildqyhifepkcldafpnlkdflarfeglkkisaymkssryls
tpifsklaqwsnk
>d1gsca2 3.38.1.4.1 (1-84) Glutathione S-transferase {rat (Rattus rattus)}
pmilgywnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d1gscb1 1.43.1.1.1 (85-217) Glutathione S-transferase {rat (Rattus rattus), class mu}
lcgeteeeriradivenqvmdnrmqlimlcynpdfekqkpeflktipekmklyseflgkr
pwfagdkvtyvdflaydildqyhifepkcldafpnlkdflarfeglkkisaymkssryls
tpifsklaqwsnk
>d1gscb2 3.38.1.4.1 (1-84) Glutathione S-transferase {rat (Rattus rattus)}
pmilgywnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d1gscc1 1.43.1.1.1 (85-217) Glutathione S-transferase {rat (Rattus rattus), class mu}
lcgeteeeriradivenqvmdnrmqlimlcynpdfekqkpeflktipekmklyseflgkr
pwfagdkvtyvdflaydildqyhifepkcldafpnlkdflarfeglkkisaymkssryls
tpifsklaqwsnk
>d1gscc2 3.38.1.4.1 (1-84) Glutathione S-transferase {rat (Rattus rattus)}
pmilgywnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d1gscd1 1.43.1.1.1 (85-217) Glutathione S-transferase {rat (Rattus rattus), class mu}
lcgeteeeriradivenqvmdnrmqlimlcynpdfekqkpeflktipekmklyseflgkr
pwfagdkvtyvdflaydildqyhifepkcldafpnlkdflarfeglkkisaymkssryls
tpifsklaqwsnk
>d1gscd2 3.38.1.4.1 (1-84) Glutathione S-transferase {rat (Rattus rattus)}
pmilgywnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d1gsda1 1.43.1.1.8 (81-209) Glutathione S-transferase {human (Homo sapiens), class alpha}
lygkdikeralidmyiegiadlgemilllpvcppeekdaklalikekiknryfpafekvl
kshgqdylvgnklsradihlvellyyveeldsslissfpllkalktrisnlptvkkflqp
gsprkppmd
>d1gsda2 3.38.1.4.8 (2-80) Glutathione S-transferase {human (Homo sapiens) class alpha}
aekpklhyfnargrmestrwllaaagvefeekfiksaedldklrndgylmfqqvpmveid
gmklvqtrailnyiaskyn
>d1gsdb1 1.43.1.1.8 (81-209) Glutathione S-transferase {human (Homo sapiens), class alpha}
lygkdikeralidmyiegiadlgemilllpvcppeekdaklalikekiknryfpafekvl
kshgqdylvgnklsradihlvellyyveeldsslissfpllkalktrisnlptvkkflqp
gsprkppmd
>d1gsdb2 3.38.1.4.8 (2-80) Glutathione S-transferase {human (Homo sapiens) class alpha}
aekpklhyfnargrmestrwllaaagvefeekfiksaedldklrndgylmfqqvpmveid
gmklvqtrailnyiaskyn
>d1gsea1 1.43.1.1.8 (81-222) Glutathione S-transferase {human (Homo sapiens), class alpha}
lygkdikeralidmyiegiadlgemilllpvcppeekdaklalikekiknryfpafekvl
kshgqdylvgnklsradihlvellyyveeldsslissfpllkalktrisnlptvkkflqp
gsprkppmdeksleearkifrf
>d1gsea2 3.38.1.4.8 (2-80) Glutathione S-transferase {human (Homo sapiens) class alpha}
aekpklhyfnargkmestrwllaaagvefeekfiksaedldklrndgylmfqqvpmveid
gmklvqtrailnyiaskyn
>d1gseb1 1.43.1.1.8 (81-222) Glutathione S-transferase {human (Homo sapiens), class alpha}
lygkdikeralidmyiegiadlgemilllpvcppeekdaklalikekiknryfpafekvl
kshgqdylvgnklsradihlvellyyveeldsslissfpllkalktrisnlptvkkflqp
gsprkppmdeksleearkifrf
>d1gseb2 3.38.1.4.8 (2-80) Glutathione S-transferase {human (Homo sapiens) class alpha}
aekpklhyfnargkmestrwllaaagvefeekfiksaedldklrndgylmfqqvpmveid
gmklvqtrailnyiaskyn
>d1gsfa1 1.43.1.1.8 (81-222) Glutathione S-transferase {human (Homo sapiens), class alpha}
lygkdikeralidmyiegiadlgemilllpvcppeekdaklalikekiknryfpafekvl
kshgqdylvgnklsradihlvellyyveeldsslissfpllkalktrisnlptvkkflqp
gsprkppmdeksleearkifrf
>d1gsfa2 3.38.1.4.8 (2-80) Glutathione S-transferase {human (Homo sapiens) class alpha}
aekpklhyfnargrmestrwllaaagvefeekfiksaedldklrndgylmfqqvpmveid
gmklvqtrailnyiaskyn
>d1gsfb1 1.43.1.1.8 (81-222) Glutathione S-transferase {human (Homo sapiens), class alpha}
lygkdikeralidmyiegiadlgemilllpvcppeekdaklalikekiknryfpafekvl
kshgqdylvgnklsradihlvellyyveeldsslissfpllkalktrisnlptvkkflqp
gsprkppmdeksleearkifrf
>d1gsfb2 3.38.1.4.8 (2-80) Glutathione S-transferase {human (Homo sapiens) class alpha}
aekpklhyfnargrmestrwllaaagvefeekfiksaedldklrndgylmfqqvpmveid
gmklvqtrailnyiaskyn
>d1gsgp1 2.40.1.1.1 (339-547) Gln-tRNA synthetase (GlnRS), C-terminal (anticodon-binding) domain {(Escherichia coli)}
apramavidpvklvienyqgegemvtmpnhpnkpemgsrqvpfsgeiwidradfreeank
qykrlvlgkevrlrnayvikaervekdaegnittifctydadtlskdpadgrkvkgvihw
vsaahalpveirlydrlfsvpnpgaaddflsvinpeslvikqgfaepslkdavagkafqf
eregyfcldsrhstaekpvfnrtvglrdt
>d1gsgp2 3.17.1.1.2 (8-338) Glutaminyl-tRNA synthetase (GlnRS) {(Escherichia coli)}
tnfirqiidedlasgkhttvhtrfppepngylhighaksiclnfgiaqdykgqcnlrfdd
tnpvkedieyvesikndvewlgfhwsgnvryssdyfdqlhayaielinkglayvdeltpe
qireyrgtltqpgknspyrdrsveenlalfekmraggfeegkaclrakidmaspfivmrd
pvlyrikfaehhqtgnkwciypmydfthcisdalegithslctlefqdnrrlydwvldni
tipvhprqyefsrlnleytvmskrklnllvtdkhvegwddprmptisglrrrgytaasir
efckrigvtkqdntiemaslesciredlnen
>d1gsh_1 3.23.1.3.1 (1-122) Glutathione synthetase, N-terminal domain {(Escherichia coli)}
miklgivmdpianinikkdssfamlleaqrrgyelhymemgdlylingearahtrtlnvk
qnyeewfsfvgeqdlpladldvilmrkdppfdtefiyatyileraeekgtlivnkpqslr
dc
>d1gsh_2 4.89.1.1.1 (123-316) Glutathione synthetase {(Escherichia coli)}
neklftawfsdltpetlvtrnkaqlkafwekhsdiilkpldgmggasifrvkegdpnlgv
iaetltehgtrycmaqnylpaikdgdkrvlvvdgepvpyclaripqggetrgnlaaggrg
eprpltesdwkiarqigptlkekglifvgldiigdrlteinvtsptcireieaefpvsit
gmlmdaiearlqqq
>d1gsl__ 2.21.1.1.5 Lectin {the west-central african legume (Griffonia simplicifolia)}
ntvnftypdfwsyslkngteitflgdatripgalqltktdangnpvrssagqasysepvf
lwdstgkaasfytsftfllknygaptadglafflapvdssvkdyggflglfrhetaadps
knqvvavefdtwinkdwndppyphigidvnsivsvattrwenddaygssiatahitydar
skiltvllsyehgrdyilshvvdlakvlpqkvrigfsagvgydevtyilswhffstldgt
nk
>d1gsn_1 3.4.1.4.1 (18-165,291-363) Glutathione reductase {human (Homo sapiens)}
vasydylvigggsgglasarraaelgaraavveshklggtcvnvgxvpkkvmwntavhse
fmhdhadygfpscegkfnwrvikekrdayvsrlnaiyqnnltkshieiirghaaftsdpk
ptievsgkkytaphiliatggmpstpheXrvpntkdlslnklgiqtddkghiivdefqnt
nvkgiyavgdvcgkalltpvaiaagrklahrlfeykedskld
>d1gsn_2 3.4.1.4.1 (166-290) Glutathione reductase {human (Homo sapiens)}
sqipgaslgitsdgffqleelpgrsvivgagyiavemagilsalgsktslmirhdkvlrs
fdsmistnxteelenagvevlkfsqvkevkktlsglevsmvtavpgrlpvmtmipdvdxl
lwaig
>d1gsn_3 4.48.1.1.1 (364-478) Glutathione reductase {human (Homo sapiens)}
ynniptvvfshppigtvgltedeaihkygienvktystsftpmyhavtkrktkcvmkmvx
ankeekvvgihmqglgcdemlqgfavavkmgatkadfdntvaihptsseelvtlr
>d1gsp__ 4.1.1.1.3 RNase T1 {(Aspergillus oryzae)}
acdytcgsncysssdvstaqaagyklhedgetvgsnsyphkynnyegfdfsvsspyyewp
ilssgdvysggspgadrvvfnennqlagvithtgasgnnfvect
>d1gsq_1 1.43.1.1.10 (76-202) Glutathione S-transferase {Squid (Ommastrephes sloani pacificus)}
ldgktslekyrvdeitetlqdifndvvkikfapeaakeavqqnyeksckrlapflegllv
sngggdgffvgnsmtladlhcyvalevplkhtpellkdcpkivalrkrvaecpkiaaylk
krpvrdf
>d1gsq_2 3.38.1.4.10 (1-75) Glutathione S-transferase {Squid (Ommastrephes sloani pacificus)}
pkytlhyfplmgraelcrfvlaahgeeftdrvvemadwpnlkatmysnampvldidgtkm
sqsmciarhlarefg
>d1gssa1 1.43.1.1.4 (77-207) Glutathione S-transferase {human (Homo sapiens), class pi}
ygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqnqg
gktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflaspey
vnlpingngkq
>d1gssa2 3.38.1.4.4 (1-76) Glutathione S-transferase {human (Homo sapiens) class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtlgl
>d1gssb1 1.43.1.1.4 (77-207) Glutathione S-transferase {human (Homo sapiens), class pi}
ygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqnqg
gktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflaspey
vnlpingngkq
>d1gssb2 3.38.1.4.4 (1-76) Glutathione S-transferase {human (Homo sapiens) class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtlgl
>d1gsua1 1.43.1.1.7 (85-217) Glutathione S-transferase {SP Chicken (Gallus gallus), class mu}
mcgetevekqrvdvlenhlmdlrmafarlcyspdfeklkpayleqlpgklrqlsrflgsr
swfvgdkltfvdflaydvldqqrmfvpdcpelqgnlsqflqrfealekisaymrsgrfmk
apifwytalwnnk
>d1gsua2 3.38.1.4.7 (1-84) Glutathione S-transferase {Chicken (Gallus gallus) class mu}
vvtlgywdirglahairllleytetpyqerrykagpapdfdpsdwtnekeklgldfpnlp
ylidgdvkltqsnailryiarkhn
>d1gsub1 1.43.1.1.7 (85-217) Glutathione S-transferase {SP Chicken (Gallus gallus), class mu}
mcgetevekqrvdvlenhlmdlrmafarlcyspdfeklkpayleqlpgklrqlsrflgsr
swfvgdkltfvdflaydvldqqrmfvpdcpelqgnlsqflqrfealekisaymrsgrfmk
apifwytalwnnk
>d1gsub2 3.38.1.4.7 (1-84) Glutathione S-transferase {Chicken (Gallus gallus) class mu}
vvtlgywdirglahairllleytetpyqerrykagpapdfdpsdwtnekeklgldfpnlp
ylidgdvkltqsnailryiarkhn
>d1gsya1 1.43.1.1.5 (79-209) Glutathione S-transferase {Mouse (Mus musculus), class pi}
ygknqreaaqmdmvndgvedlrgkyvtliytnyengkndyvkalpghlkpfetllsqnqg
gkafivgdqisfadynlldlllihqvlapgcldnfpllsayvarlsarpkikaflsspeh
vnrpingngkq
>d1gsya2 3.38.1.4.5 (1-78) Glutathione S-transferase {Mouse (Mus musculus) class pi}
ppytivyfpvrgrceamrmlladqgqswkeevvtidtwmqgllkptclygqlpkfedgdl
tlyqsnailrhlgrslgl
>d1gsyb1 1.43.1.1.5 (79-209) Glutathione S-transferase {Mouse (Mus musculus), class pi}
ygknqreaaqmdmvndgvedlrgkyvtliytnyengkndyvkalpghlkpfetllsqnqg
gkafivgdqisfadynlldlllihqvlapgcldnfpllsayvarlsarpkikaflsspeh
vnrpingngkq
>d1gsyb2 3.38.1.4.5 (1-78) Glutathione S-transferase {Mouse (Mus musculus) class pi}
ppytivyfpvrgrceamrmlladqgqswkeevvtidtwmqgllkptclygqlpkfedgdl
tlyqsnailrhlgrslgl
>d1gta_1 1.43.1.1.11 (81-218) Glutathione S-transferase {(Schistosoma japonicum)}
mlggcpkeraeismlegavldirygvsriayskdfetlkvdflsklpemlkmfedrlchk
tylngdhvthpdfmlydaldvvlymdpmcldafpklvcfkkrieaipqidkylksskyia
wplqgwqatfgggdhppk
>d1gta_2 3.38.1.4.11 (1-80) Glutathione S-transferase {(Schistosoma japonicum)}
mspilgywkikglvqptrllleyleekyeehlyerdegdkwrnkkfelglefpnlpyyid
gdvkltqsmaiiryiadkhn
>d1gtb_1 1.43.1.1.11 (81-218) Glutathione S-transferase {(Schistosoma japonicum)}
mlggcpkeraeismlegavldirygvsriayskdfetlkvdflsklpemlkmfedrlchk
tylngdhvthpdfmlydaldvvlymdpmcldafpklvcfkkrieaipqidkylksskyia
wplqgwqatfgggdhppk
>d1gtb_2 3.38.1.4.11 (1-80) Glutathione S-transferase {(Schistosoma japonicum)}
mspilgywkikglvqptrllleyleekyeehlyerdegdkwrnkkfelglefpnlpyyid
gdvkltqsmaiiryiadkhn
>d1gtma1 3.22.1.7.2 (181-419) Glutamate dehydrogenase, C-terminal domain {(Pyrococcus furiosis)}
ggslgrieatargasytireaakvlgwdtlkgktiaiqgygnagyylakimsedfgmkvv
avsdskggiynpdglnadevlkwknehgsvkdfpgatnitneellelevdvlapaaieev
itkknadnikakivaevangpvtpeadeilfekgilqipdflcnaggvtvsyfewvqnit
gyywtieevrerldkkmtkafydvyniakeknihmrdaayvvavqrvyqamldrgwvkh
>d1gtma2 3.61.1.1.2 (3-180) Glutamate dehydrogenase, N-terminal domain {(Pyrococcus furiosis)}
adpyeivikqleraaqymeiseealeflkrpqrivevtipvemddgsvkvftgfrvqhnw
argptkggirwhpeetlstvkalaawmtwktavmdlpygggkggiivdpkklsdrekerl
argyiraiydvispyedipapdvytnpqimawmmdeyetisrrktpafgiitgkplsi
>d1gtmb1 3.22.1.7.2 (181-419) Glutamate dehydrogenase, C-terminal domain {(Pyrococcus furiosis)}
ggslgrieatargasytireaakvlgwdtlkgktiaiqgygnagyylakimsedfgmkvv
avsdskggiynpdglnadevlkwknehgsvkdfpgatnitneellelevdvlapaaieev
itkknadnikakivaevangpvtpeadeilfekgilqipdflcnaggvtvsyfewvqnit
gyywtieevrerldkkmtkafydvyniakeknihmrdaayvvavqrvyqamldrgwvkh
>d1gtmb2 3.61.1.1.2 (3-180) Glutamate dehydrogenase, N-terminal domain {(Pyrococcus furiosis)}
adpyeivikqleraaqymeiseealeflkrpqrivevtipvemddgsvkvftgfrvqhnw
argptkggirwhpeetlstvkalaawmtwktavmdlpygggkggiivdpkklsdrekerl
argyiraiydvispyedipapdvytnpqimawmmdeyetisrrktpafgiitgkplsi
>d1gtmc1 3.22.1.7.2 (181-419) Glutamate dehydrogenase, C-terminal domain {(Pyrococcus furiosis)}
ggslgrieatargasytireaakvlgwdtlkgktiaiqgygnagyylakimsedfgmkvv
avsdskggiynpdglnadevlkwknehgsvkdfpgatnitneellelevdvlapaaieev
itkknadnikakivaevangpvtpeadeilfekgilqipdflcnaggvtvsyfewvqnit
gyywtieevrerldkkmtkafydvyniakeknihmrdaayvvavqrvyqamldrgwvkh
>d1gtmc2 3.61.1.1.2 (3-180) Glutamate dehydrogenase, N-terminal domain {(Pyrococcus furiosis)}
adpyeivikqleraaqymeiseealeflkrpqrivevtipvemddgsvkvftgfrvqhnw
argptkggirwhpeetlstvkalaawmtwktavmdlpygggkggiivdpkklsdrekerl
argyiraiydvispyedipapdvytnpqimawmmdeyetisrrktpafgiitgkplsi
>d1gtoa_ 1.29.1.1.1 ROP protein {(Escherichia coli)}
gtkqektalnmarfirsqtltlleklnelgadeqadiceslhdhadelyrsclarfgddg
en
>d1gtob_ 1.29.1.1.1 ROP protein {(Escherichia coli)}
gtkqektalnmarfirsqtltlleklnelgadeqadiceslhdhadelyrsclarfg
>d1gtoc_ 1.29.1.1.1 ROP protein {(Escherichia coli)}
gtkqektalnmarfirsqtltlleklnelgadeqadiceslhdhadelyrsclarfg
>d1gtpa_ 4.56.1.1.1 GTP cyclohydrolase I {(Escherichia coli)}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstcehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1gtpb_ 4.56.1.1.1 GTP cyclohydrolase I {(Escherichia coli)}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstcehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1gtpc_ 4.56.1.1.1 GTP cyclohydrolase I {(Escherichia coli)}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstcehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1gtpd_ 4.56.1.1.1 GTP cyclohydrolase I {(Escherichia coli)}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstcehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1gtpe_ 4.56.1.1.1 GTP cyclohydrolase I {(Escherichia coli)}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstcehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1gtpf_ 4.56.1.1.1 GTP cyclohydrolase I {(Escherichia coli)}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstcehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1gtpg_ 4.56.1.1.1 GTP cyclohydrolase I {(Escherichia coli)}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstcehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1gtph_ 4.56.1.1.1 GTP cyclohydrolase I {(Escherichia coli)}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstcehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1gtpi_ 4.56.1.1.1 GTP cyclohydrolase I {(Escherichia coli)}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstcehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1gtpj_ 4.56.1.1.1 GTP cyclohydrolase I {(Escherichia coli)}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstcehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1gtpk_ 4.56.1.1.1 GTP cyclohydrolase I {(Escherichia coli)}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstcehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1gtpl_ 4.56.1.1.1 GTP cyclohydrolase I {(Escherichia coli)}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstcehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1gtpm_ 4.56.1.1.1 GTP cyclohydrolase I {(Escherichia coli)}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstcehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1gtpn_ 4.56.1.1.1 GTP cyclohydrolase I {(Escherichia coli)}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstcehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1gtpo_ 4.56.1.1.1 GTP cyclohydrolase I {(Escherichia coli)}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstcehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1gtpp_ 4.56.1.1.1 GTP cyclohydrolase I {(Escherichia coli)}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstcehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1gtpq_ 4.56.1.1.1 GTP cyclohydrolase I {(Escherichia coli)}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstcehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1gtpr_ 4.56.1.1.1 GTP cyclohydrolase I {(Escherichia coli)}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstcehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1gtps_ 4.56.1.1.1 GTP cyclohydrolase I {(Escherichia coli)}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstcehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1gtpt_ 4.56.1.1.1 GTP cyclohydrolase I {(Escherichia coli)}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstcehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1gtqa_ 4.56.1.1.2 6-pyruvoyl tetrahydropterin synthase {rat (Rattus rattus)}
lrrrarlsrlvsfsashrlhspslsaeenlkvfgkcnnpnghghnykvvvtihgeidpvt
gmvmnltdlkeymeeaimkpldhknldldvpyfadvvsttenvavyiwenlqrllpvgal
ykvkvyetdnnivvykge
>d1gtqb_ 4.56.1.1.2 6-pyruvoyl tetrahydropterin synthase {rat (Rattus rattus)}
lrrrarlsrlvsfsashrlhspslsaeenlkvfgkcnnpnghghnykvvvtihgeidpvt
gmvmnltdlkeymeeaimkpldhknldldvpyfadvvsttenvavyiwenlqrllpvgal
ykvkvyetdnnivvykge
>d1gtra1 2.40.1.1.1 (339-547) Gln-tRNA synthetase (GlnRS), C-terminal (anticodon-binding) domain {(Escherichia coli)}
apramavidpvklvienyqgegemvtmpnhpnkpemgsrqvpfsgeiwidradfreeank
qykrlvlgkevrlrnayvikaervekdaegnittifctydadtlskdpadgrkvkgvihw
vsaahalpveirlydrlfsvpnpgaaddflsvinpeslvikqgfaepslkdavagkafqf
eregyfcldsrhstaekpvfnrtvglrdt
>d1gtra2 3.17.1.1.2 (8-338) Glutaminyl-tRNA synthetase (GlnRS) {(Escherichia coli)}
tnfirqiidedlasgkhttvhtrfppepngylhighaksiclnfgiaqdykgqcnlrfdd
tnpvkedieyvesikndvewlgfhwsgnvryssdyfdqlhayaielinkglayvdeltpe
qireyrgtltqpgknspyrdrsveenlalfekmraggfeegkaclrakidmaspfivmrd
pvlyrikfaehhqtgnkwciypmydfthcisdalegithslctlefqdnrrlydwvldni
tipvhprqyefsrlnleytvmskrklnllvtdkhvegwddprmptisglrrrgytaasir
efckrigvtkqdntiemaslesciredlnen
>d1gtsa1 2.40.1.1.1 (339-547) Gln-tRNA synthetase (GlnRS), C-terminal (anticodon-binding) domain {(Escherichia coli)}
apramavidpvklvienyqgegemvtmpnhpnkpemgsrqvpfsgeiwidradfreeank
qykrlvlgkevrlrnayvikaervekdaegnittifctydadtlskdpadgrkvkgvihw
vsaahalpveirlydrlfsvpnpgaaddflsvinpeslvikqgfaepslkdavagkafqf
eregyfcldsrhstaekpvfnrtvglrdt
>d1gtsa2 3.17.1.1.2 (8-338) Glutaminyl-tRNA synthetase (GlnRS) {(Escherichia coli)}
tnfirqiidedlasgkhttvhtrfppepngylhighaksiclnfgiaqdykgqcnlrfdd
tnpvkedieyvesikndvewlgfhwsgnvryssdyfdqlhayaielinkglayvdeltpe
qireyrgtltqpgknspyrdrsveenlalfekmraggfeegkaclrakidmaspfivmrd
pvlyrikfaehhqtgnkwciypmydfthcisdalegithslctlefqdnrrlydwvldni
tipvhprqyefsrlnleytvmskrklnllvtdkhvegwddprmptisglrrrgytaasir
efckrigvtkqdntiemaslesciredlnen
>d1guaa_ 3.29.1.4.3 Rap1A {Human (Homo sapiens)}
mreyklvvlgsggvgksaltvqfvqgifvdeydptiedsyrkqvevdcqqcmleildtag
teqftamrdlymkngqgfalvysitaqstfndlqdlreqilrvkdtedvpmilvgnkcdl
edervvgkeqgqnlarqwcncaflessakskinvneifydlvrqinr
>d1guab_ 4.11.3.1.1 c-Raf1 RBD {Human (Homo sapiens)}
ntirvflpnkqrtvvnvrngmslhdclmkalkvrglqpeccavfrllhehkgkkarldwn
tdaasligeelqvdfl
>d1guha1 1.43.1.1.8 (81-222) Glutathione S-transferase {human (Homo sapiens), class alpha}
lygkdikeralidmyiegiadlgemilllpvcppeekdaklalikekiknryfpafekvl
kshgqdylvgnklsradihlvellyyveeldsslissfpllkalktrisnlptvkkflqp
gsprkppmdeksleearkifrf
>d1guha2 3.38.1.4.8 (2-80) Glutathione S-transferase {human (Homo sapiens) class alpha}
aekpklhyfnargrmestrwllaaagvefeekfiksaedldklrndgylmfqqvpmveid
gmklvqtrailnyiaskyn
>d1guhb1 1.43.1.1.8 (81-222) Glutathione S-transferase {human (Homo sapiens), class alpha}
lygkdikeralidmyiegiadlgemilllpvcppeekdaklalikekiknryfpafekvl
kshgqdylvgnklsradihlvellyyveeldsslissfpllkalktrisnlptvkkflqp
gsprkppmdeksleearkifrf
>d1guhb2 3.38.1.4.8 (2-80) Glutathione S-transferase {human (Homo sapiens) class alpha}
aekpklhyfnargrmestrwllaaagvefeekfiksaedldklrndgylmfqqvpmveid
gmklvqtrailnyiaskyn
>d1guka1 1.43.1.1.9 (80-219) Glutathione S-transferase {Mouse (Mus musculus)}
nlygkdlkervridmyadgtqdlmmmiavapfktpkekeesydlilsraktryfpvfeki
lkdhgeaflvgnqlswadiqlleailmveelsapvlsdfpllqafktrisniptikkflq
pgsqrkpppdgpyvevvriv
>d1guka2 3.38.1.4.9 (5-79) Glutathione S-transferase {Mouse (Mus musculus)}
pklyyfngrgrmesirwllaaagvefeeefletreqyekmqkdghllfgqvplveidgmm
ltqtrailsylaaky
>d1gukb1 1.43.1.1.9 (80-219) Glutathione S-transferase {Mouse (Mus musculus)}
nlygkdlkervridmyadgtqdlmmmiavapfktpkekeesydlilsraktryfpvfeki
lkdhgeaflvgnqlswadiqlleailmveelsapvlsdfpllqafktrisniptikkflq
pgsqrkpppdgpyvevvriv
>d1gukb2 3.38.1.4.9 (5-79) Glutathione S-transferase {Mouse (Mus musculus)}
pklyyfngrgrmesirwllaaagvefeeefletreqyekmqkdghllfgqvplveidgmm
ltqtrailsylaaky
>d1gupa1 4.9.1.2.1 (2-177) Galactose-1-phosphate uridylyltransferase {(Escherichia coli)}
tqfnpvdhphrrynpltgqwilvsphrakrpwqgaqetpakqvlpahdpdcflcagnvrv
tgdknpdytgtyvftndfaalmsdtpdapeshdplmrcqsargtsrvicfspdhsktlpe
lsvaalteivktwqeqtaelgktypwvqvfenkgaamgcsnphpggqiwansflpn
>d1gupa2 4.9.1.2.1 (178-348) Galactose-1-phosphate uridylyltransferase {(Escherichia coli)}
eaeredrlqkeyfaeqkspmlvdyvqreladgsrtvvetehwlavvpywaawpfetlllp
kahvlritdltdaqrsdlalalkkltsrydnlfqcsfpysmgwhgapfngeenqhwqlha
hfyppllrsatvrkfmvgyemlaetqrdltaeqaaerlravsdihfresgv
>d1gupb1 4.9.1.2.1 (2-177) Galactose-1-phosphate uridylyltransferase {(Escherichia coli)}
tqfnpvdhphrrynpltgqwilvsphrakrpwqgaqetpakqvlpahdpdcflcagnvrv
tgdknpdytgtyvftndfaalmsdtpdapeshdplmrcqsargtsrvicfspdhsktlpe
lsvaalteivktwqeqtaelgktypwvqvfenkgaamgcsnphpggqiwansflpn
>d1gupb2 4.9.1.2.1 (178-345) Galactose-1-phosphate uridylyltransferase {(Escherichia coli)}
eaeredrlqkeyfaeqkspmlvdyvqreladgsrtvvetehwlavvpywaawpfetlllp
kahvlritdltdaqrsdlalalkkltsrydnlfqcsfpysmgwhgapfngeenqhwqlha
hfyppllrsatvrkfmvgyemlaetqrdltaeqaaerlravsdihfre
>d1gupc1 4.9.1.2.1 (2-177) Galactose-1-phosphate uridylyltransferase {(Escherichia coli)}
tqfnpvdhphrrynpltgqwilvsphrakrpwqgaqetpakqvlpahdpdcflcagnvrv
tgdknpdytgtyvftndfaalmsdtpdapeshdplmrcqsargtsrvicfspdhsktlpe
lsvaalteivktwqeqtaelgktypwvqvfenkgaamgcsnphpggqiwansflpn
>d1gupc2 4.9.1.2.1 (178-345) Galactose-1-phosphate uridylyltransferase {(Escherichia coli)}
eaeredrlqkeyfaeqkspmlvdyvqreladgsrtvvetehwlavvpywaawpfetlllp
kahvlritdltdaqrsdlalalkkltsrydnlfqcsfpysmgwhgapfngeenqhwqlha
hfyppllrsatvrkfmvgyemlaetqrdltaeqaaerlravsdihfre
>d1gupd1 4.9.1.2.1 (2-177) Galactose-1-phosphate uridylyltransferase {(Escherichia coli)}
tqfnpvdhphrrynpltgqwilvsphrakrpwqgaqetpakqvlpahdpdcflcagnvrv
tgdknpdytgtyvftndfaalmsdtpdapeshdplmrcqsargtsrvicfspdhsktlpe
lsvaalteivktwqeqtaelgktypwvqvfenkgaamgcsnphpggqiwansflpn
>d1gupd2 4.9.1.2.1 (178-345) Galactose-1-phosphate uridylyltransferase {(Escherichia coli)}
eaeredrlqkeyfaeqkspmlvdyvqreladgsrtvvetehwlavvpywaawpfetlllp
kahvlritdltdaqrsdlalalkkltsrydnlfqcsfpysmgwhgapfngeenqhwqlha
hfyppllrsatvrkfmvgyemlaetqrdltaeqaaerlravsdihfre
>d1guqa1 4.9.1.2.1 (2-177) Galactose-1-phosphate uridylyltransferase {(Escherichia coli)}
tqfnpvdhphrrynpltgqwilvsphrakrpwqgaqetpakqvlpahdpdcflcagnvrv
tgdknpdytgtyvftndfaalmsdtpdapeshdplmrcqsargtsrvicfspdhsktlpe
lsvaalteivktwqeqtaelgktypwvqvfenkgaamgcsnphpggqiwansflpn
>d1guqa2 4.9.1.2.1 (178-348) Galactose-1-phosphate uridylyltransferase {(Escherichia coli)}
eaeredrlqkeyfaeqkspmlvdyvqreladgsrtvvetehwlavvpywaawpfetlllp
kahvlritdltdaqrsdlalalkkltsrydnlfqcsfpysmgwhgapfngeenqhwqlha
hfyppllrsatvrkfmvgyemlaetqrdltaeqaaerlravsdihfresgv
>d1guqb1 4.9.1.2.1 (2-177) Galactose-1-phosphate uridylyltransferase {(Escherichia coli)}
tqfnpvdhphrrynpltgqwilvsphrakrpwqgaqetpakqvlpahdpdcflcagnvrv
tgdknpdytgtyvftndfaalmsdtpdapeshdplmrcqsargtsrvicfspdhsktlpe
lsvaalteivktwqeqtaelgktypwvqvfenkgaamgcsnphpggqiwansflpn
>d1guqb2 4.9.1.2.1 (178-345) Galactose-1-phosphate uridylyltransferase {(Escherichia coli)}
eaeredrlqkeyfaeqkspmlvdyvqreladgsrtvvetehwlavvpywaawpfetlllp
kahvlritdltdaqrsdlalalkkltsrydnlfqcsfpysmgwhgapfngeenqhwqlha
hfyppllrsatvrkfmvgyemlaetqrdltaeqaaerlravsdihfre
>d1guqc1 4.9.1.2.1 (2-177) Galactose-1-phosphate uridylyltransferase {(Escherichia coli)}
tqfnpvdhphrrynpltgqwilvsphrakrpwqgaqetpakqvlpahdpdcflcagnvrv
tgdknpdytgtyvftndfaalmsdtpdapeshdplmrcqsargtsrvicfspdhsktlpe
lsvaalteivktwqeqtaelgktypwvqvfenkgaamgcsnphpggqiwansflpn
>d1guqc2 4.9.1.2.1 (178-345) Galactose-1-phosphate uridylyltransferase {(Escherichia coli)}
eaeredrlqkeyfaeqkspmlvdyvqreladgsrtvvetehwlavvpywaawpfetlllp
kahvlritdltdaqrsdlalalkkltsrydnlfqcsfpysmgwhgapfngeenqhwqlha
hfyppllrsatvrkfmvgyemlaetqrdltaeqaaerlravsdihfre
>d1guqd1 4.9.1.2.1 (2-177) Galactose-1-phosphate uridylyltransferase {(Escherichia coli)}
tqfnpvdhphrrynpltgqwilvsphrakrpwqgaqetpakqvlpahdpdcflcagnvrv
tgdknpdytgtyvftndfaalmsdtpdapeshdplmrcqsargtsrvicfspdhsktlpe
lsvaalteivktwqeqtaelgktypwvqvfenkgaamgcsnphpggqiwansflpn
>d1guqd2 4.9.1.2.1 (178-345) Galactose-1-phosphate uridylyltransferase {(Escherichia coli)}
eaeredrlqkeyfaeqkspmlvdyvqreladgsrtvvetehwlavvpywaawpfetlllp
kahvlritdltdaqrsdlalalkkltsrydnlfqcsfpysmgwhgapfngeenqhwqlha
hfyppllrsatvrkfmvgyemlaetqrdltaeqaaerlravsdihfre
>d1gur__ 7.3.4.1.1 Gurmarin, a sweet taste-suppressing polypeptide {(Gymnema sylveste)}
qcvkkdelcipyyldccepleckkvnwwdhkcig
>d1gvp__ 2.29.4.8.1 Gene V protein {(Bacteriophage f1)}
mikveikpsqaqfttrsgvsrqgkpyslneqlcyvdlgneypvlvkitldegqpayapgl
ytvhlssfkvgqfgslmidrlrlvpak
>d1gya__ 2.1.1.1.5 CD2 {human (Homo sapiens)}
keitnaletwgalgqdinldipsfqmsddiddikwektsdkkkiaqfrkeketfkekdty
klfkngtlkikhlktddqdiykvsiydtkgknvlekifdlkiqer
>d1gyla_ 3.1.7.1.3 Glycolate oxidase {spinach (Spinacia oleracea)}
meitnvneyeaiakqklpkmvydfyasgaedqwtlaenrnafsrilfrprilidvtnidm
tttilgfkismpimiaptamqkmahpegeyataraasaagtimtlsswatssveevastg
pgirffqlyvykdrnvvaqlvrraeragfkaialtvdtprlgrreadiknrfvlppfltl
knfegidlgkmdkandsglssyvagqidrslswkdvawlqtitslpilvkgvitaedarl
avqhgaagiivsnhgarqldyvpatimaleevvkaaqgripvfldggvrrgtdvfkalal
gaagvfigrpvvfslaaegeagvkkvlqmmrdefeltmalsgcrslkeisrshiaadwd
>d1gylb_ 3.1.7.1.3 Glycolate oxidase {spinach (Spinacia oleracea)}
meitnvneyeaiakqklpkmvydfyasgaedqwtlaenrnafsrilfrprilidvtnidm
tttilgfkismpimiaptamqkmahpegeyataraasaagtimtlsswatssveevastg
pgirffqlyvykdrnvvaqlvrraeragfkaialtvdtprlgrreadiknrfvlppfltl
knfegidlgkmdkandsglssyvagqidrslswkdvawlqtitslpilvkgvitaedarl
avqhgaagiivsnhgarqldyvpatimaleevvkaaqgripvfldggvrrgtdvfkalal
gaagvfigrpvvfslaaegeagvkkvlqmmrdefeltmalsgcrslkeisrshiaadwd
>d1gym__ 3.1.15.2.1 Phosphatidylinositol-specific phospholipase C {(Bacillus cereus)}
assvnelenwskwmqpipdsiplarisipgthdsgtfklqnpikqvwgmtqeydfryqmd
hgarifdirgrltddntivlhhgplylyvtlhefineakqflkdnpsetiimslkkeyed
mkgaedsfsstfekkyfvdpiflktegniklgdargkivllkrysgsnepggynnfywpd
netftttvnqnanvtvqdkykvsydekvksikdtmdetmnnsedlnhlyinftslssggt
awnspyyyasyinpeianyikqknparvgwviqdyinekwspllyqeviranksli
>d1gypa1 3.22.1.3.6 (1-165,335-358) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Leishmania mexicana)}
apikvgingfgrigrmvfqaicdqgligteidvvavvdmstnaeyfayqmkhdtvhgrpk
ytveavksspsvetadvlvvnghrikcvkaqrnpadlpwgklgvdyviestglftdklka
eghikggakkvvisapasggaktivmgvnqheyspashhvvsnasXnewayshrvvdlvr
ymaakdaass
>d1gypa2 4.42.1.1.6 (166-334) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Leishmania mexicana)}
cttnclapivhvltkenfgietglmttihsytatqktvdgvslkdwrggraaavniipst
tgaakavgmvipstkgkltgmsfrvptpdvsvvdltfratrdtsiqeidkaikkaaqtym
kgilgftdeelvsadfindnrssvydskatlqnnlpgekrffkvvswyd
>d1gypb1 3.22.1.3.6 (1-165,335-358) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Leishmania mexicana)}
apikvgingfgrigrmvfqaicdqgligteidvvavvdmstnaeyfayqmkhdtvhgrpk
ytveavksspsvetadvlvvnghrikcvkaqrnpadlpwgklgvdyviestglftdklka
eghikggakkvvisapasggaktivmgvnqheyspashhvvsnasXnewayshrvvdlvr
ymaakdaass
>d1gypb2 4.42.1.1.6 (166-334) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Leishmania mexicana)}
cttnclapivhvltkenfgietglmttihsytatqktvdgvslkdwrggraaavniipst
tgaakavgmvipstkgkltgmsfrvptpdvsvvdltfratrdtsiqeidkaikkaaqtym
kgilgftdeelvsadfindnrssvydskatlqnnlpgekrffkvvswyd
>d1gypc1 3.22.1.3.6 (1-165,335-358) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Leishmania mexicana)}
apikvgingfgrigrmvfqaicdqgligteidvvavvdmstnaeyfayqmkhdtvhgrpk
ytveavksspsvetadvlvvnghrikcvkaqrnpadlpwgklgvdyviestglftdklka
eghikggakkvvisapasggaktivmgvnqheyspashhvvsnasXnewayshrvvdlvr
ymaakdaass
>d1gypc2 4.42.1.1.6 (166-334) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Leishmania mexicana)}
cttnclapivhvltkenfgietglmttihsytatqktvdgvslkdwrggraaavniipst
tgaakavgmvipstkgkltgmsfrvptpdvsvvdltfratrdtsiqeidkaikkaaqtym
kgilgftdeelvsadfindnrssvydskatlqnnlpgekrffkvvswyd
>d1gypd1 3.22.1.3.6 (1-165,335-358) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Leishmania mexicana)}
apikvgingfgrigrmvfqaicdqgligteidvvavvdmstnaeyfayqmkhdtvhgrpk
ytveavksspsvetadvlvvnghrikcvkaqrnpadlpwgklgvdyviestglftdklka
eghikggakkvvisapasggaktivmgvnqheyspashhvvsnasXnewayshrvvdlvr
ymaakdaass
>d1gypd2 4.42.1.1.6 (166-334) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Leishmania mexicana)}
cttnclapivhvltkenfgietglmttihsytatqktvdgvslkdwrggraaavniipst
tgaakavgmvipstkgkltgmsfrvptpdvsvvdltfratrdtsiqeidkaikkaaqtym
kgilgftdeelvsadfindnrssvydskatlqnnlpgekrffkvvswyd
>d1gza__ 1.72.1.1.2 Peroxidase {(Arthromyces ramous)}
svtcpggqstsnsqccvwfdvlddlqtnfyqgskcespvrkilrivfhdaigfspaltaa
gqfggggadgsiiahsnielafpanggltdtiealravginhgvsfgdliqfatavgmsn
cpgsprlefltgrsnssqpsppslipgpgntvtaildrmgdagfspdevvdllaahslas
qeglnsaifrspldstpqvfdtqfyietllkgttqpgpslgfaeelspfpgefrmrsdal
lardsrtacrwqsmtssnevmgqryraamakmsvlgfdrnaltdcsdvipsavsnnaapv
ipggltvddievscpsepfpeiatasgplpslapap
>d1gzb__ 1.72.1.1.2 Peroxidase {(Arthromyces ramous)}
svtcpggqstsnsqccvwfdvlddlqtnfyqgskcespvrkilrivfhdaigfspaltaa
gqfggggadgsiiahsnielafpanggltdtiealravginhgvsfgdliqfatavgmsn
cpgsprlefltgrsnssqpsppslipgpgntvtaildrmgdagfspdevvdllaahslas
qeglnsaifrspldstpqvfdtqfyietllkgttqpgpslgfaeelspfpgefrmrsdal
lardsrtacrwqsmtssnevmgqryraamakmsvlgfdrnaltdcsdvipsavsnnaapv
ipggltvddievscpsepfpeiatasgplpslapap
>d1gzi__ 2.66.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus)}
nqasvvanqlipintaltlvmmrsevvtpvgipaediprlvsmqvnravplgttlmpdmv
kgyaa
>d1h4n__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfnfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasfk
>d1h9n__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelnlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasfk
>d1h9q__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelqlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1ha1_1 4.34.7.1.1 (8-92) Nuclear ribonucleoprotein A1, RNP A1, UP1 {human (homo sapiens)}
epeqlrklfigglsfettdeslrshfeqwgtltdcvvmrdpntkrsrgfgfvtyatveev
daamnarphkvdgrvvepkravsre
>d1ha1_2 4.34.7.1.1 (99-180) Nuclear ribonucleoprotein A1, RNP A1, UP1 {human (homo sapiens)}
ahltvkkifvggikedteehhlrdyfeqygkievieimtdrgsgkkrgfafvtfddhdsv
dkiviqkyhtvnghncevrkal
>d1haba_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1habb_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1habc_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1habd_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1haca_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1hacb_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1hacc_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1hacd_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1hae__ 7.3.9.1.15 Heregulin-alpha, EGF-like domain {human (Homo sapiens)}
shlvkcaekektfcvnggecfmvkdlsnpsrylckcqpgftgarctenvpmkvqnqekae
ely
>d1haf__ 7.3.9.1.15 Heregulin-alpha, EGF-like domain {human (Homo sapiens)}
shlvkcaekektfcvnggecfmvkdlsnpsrylckcqpgftgarctenvpmkvqnqekae
ely
>d1hage_ 2.35.1.2.10 Thrombin {human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgrivegsdaeigmspwqvmlfrkspq
ellcgaslisdrwvltaahcllyppwdknftendllvrigkhsrtryerniekismleki
yihprynwrenldrdialmklkkpvafsdyihpvclpdretaasllqagykgrvtgwgnl
ketwtanvgkgqpsvlqvvnlpiverpvckdstriritdnmfcagykpdegkrgdacegd
sggpfvmkspfnnrwyqmgivswgegcdrdgkygfythvfrlkkwiqkvidqfge
>e1hah.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>e1hah.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1hai.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>e1hai.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>d1han_1 4.20.1.3.2 (2-132) 2,3-Dihydroxybiphenyl dioxygenase (DHDB, BPHC enzyme) {(Pseudomonas cepacia)}
sirslgymgfavsdvaawrsfltqklglmeagttdngdlfridsrawriavqqgevddla
fagyevadaaglaqmadklkqagiavttgdaslarrrgvtglitfadpfglpleiyygas
evfekpflpga
>d1han_2 4.20.1.3.2 (133-288) 2,3-Dihydroxybiphenyl dioxygenase (DHDB, BPHC enzyme) {(Pseudomonas cepacia)}
avsgfltgeqglghfvrcvpdsdkalafytdvlgfqlsdvidmkmgpdvtvpayflhcne
rhhtlaiaafplpkrihhfmlevaslddvgfafdrvdadglitstlgrhtndhmvsfyas
tpsgveveygwsartvdrswvvvrhdspsmwghksv
>e1hao.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>e1hao.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1hap.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>e1hap.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
adcglrplfekksledkterellesyi
>d1har__ 5.9.1.2.2 HIV-1 reverse transcriptase {human immunodeficiency virus type 1 (Bh10 isolate)}
pispietvpvklkpgmdgpkvaqwpltaakiaalvaictemekegkiskigpenpyntpv
faikkkdstkwaklvdfrelnkrtqdfwevqlgiphpaglkkkksvtvldvgdayfsvpl
dedfrkytaftipsinnetpgiryqynvlpqgwkgspaifqssmtkilapfkaanpdivi
yqymddlyvgsdlaigahrtkieelrqhllrwgltt
>d1hava_ 2.35.1.4.2 3C cysteine protease (picornain 3C) {Human hepatitis A virus}
stleiaglvrknlvqfgvgekngsvrwvmnalgvkddwllvpshaykfekdyemmefyfn
rggtyysisagnvviqsldvgfqdvvlmkvptipkfrditqhfikkgdvpralnrlatlv
ttvngtpmlisegplkmeekatyvhkkndgttvdltvdqawrgkgeglpgmcggalvssn
qsiqnailgihvaggnsilvaklvtqemfqnidkki
>d1havb_ 2.35.1.4.2 3C cysteine protease (picornain 3C) {Human hepatitis A virus}
stleiaglvrknlvqfgvgekngsvrwvmnalgvkddwllvpshaykfekdyemmefyfn
rggtyysisagnvviqsldvgfqdvvlmkvptipkfrditqhfikkgdvpralnrlatlv
ttvngtpmlisegplkmeekatyvhkkndgttvdltvdqawrgkgeglpgmxggalvssn
qsiqnailgihvaggnsilvaklvtqemfqnidk
>d1hbaa_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1hbab_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvyprtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1hbac_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1hbad_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvyprtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1hbba_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1hbbb_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1hbbc_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1hbbd_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1hbg__ 1.1.1.1.3 Glycera globin {marine bloodworm (Glycera dibranchiata)}
glsaaqrqviaatwkdiagadngagvgkkclikflsahpqmaavfgfsgasdpgvaalga
kvlaqigvavshlgdegkmvaqmkavgvrhkgygnkhikaqyfeplgasllsamehrigg
kmnaaakdawaaayadisgalisglqs
>d1hbha_ 1.1.1.1.23 Hemoglobin, alpha-chain {antarctic fish (Pagothenia bernacchii)}
xslsdkdkaavralwskigksadaigndalsrmivvypqtktyfshwpdvtpgsphikah
gkkvmggialavskiddlktglmelseqhayklrvdpanfkilnhcilvvistmfpkeft
peahvsldkflsgvalalaeryr
>d1hbhb_ 1.1.1.1.34 Hemoglobin, beta-chain {antartic fish (Pagothenia bernacchii)}
vewtdkersiisdifshmdyddigpkalsrclivypwtqrhfsgfgnlynaeaiignanv
aahgikvlhgldrgvknmdniaatyadlstlhseklhvdpdnfkllsdcitivlaakmgh
aftaetqgafqkflavvvsalgkqyh
>d1hbhc_ 1.1.1.1.23 Hemoglobin, alpha-chain {antarctic fish (Pagothenia bernacchii)}
xslsdkdkaavralwskigksadaigndalsrmivvypqtktyfshwpdvtpgsphikah
gkkvmggialavskiddlktglmelseqhayklrvdpanfkilnhcilvvistmfpkeft
peahvsldkflsgvalalaeryr
>d1hbhd_ 1.1.1.1.34 Hemoglobin, beta-chain {antartic fish (Pagothenia bernacchii)}
vewtdkersiisdifshmdyddigpkalsrclivypwtqrhfsgfgnlynaeaiignanv
aahgikvlhgldrgvknmdniaatyadlstlhseklhvdpdnfkllsdcitivlaakmgh
aftaetqgafqkflavvvsalgkqyh
>d1hbia_ 1.1.1.1.1 Hemoglobin I {ark clam (Scapharca inaequivalvis)}
svydaaaqltadvkkdlrdswkvigsdkkgngvalmttlfadnqetigyfkrlgnvsqgm
andklrghsitlmyalqnfidqldnpddlvcvvekfavnhitrkisaaefgkingpikkv
lasknfgdkyanawaklvavvqaal
>d1hbib_ 1.1.1.1.1 Hemoglobin I {ark clam (Scapharca inaequivalvis)}
svydaaaqltadvkkdlrdswkvigsdkkgngvalmttlfadnqetigyfkrlgnvsqgm
andklrghsitlmyalqnfidqldnpddlvcvvekfavnhitrkisaaefgkingpikkv
lasknfgdkyanawaklvavvqaal
>d1hbp__ 2.45.1.1.1 Retinol binding protein {bovine (Bos taurus)}
erdcrvssfrvkenfdkarfagtwyamakkdpeglflqdnivaefsvdenghmsatakgr
vrllnnwdvcadmvgtftdtedpakfkmkywgvasflqkgnddhwiidtdyetfavqysc
rllnldgtcadsysfvfardpsgfspevqkivrqrqeelclarqyrliphngycd
>d1hbq__ 2.45.1.1.1 Retinol binding protein {bovine (Bos taurus)}
erdcrvssfrvkenfdkarfagtwyamakkdpeglflqdnivaefsvdengqmsatakgr
vrllnnwdvcadmvgtftdtedpakfkmkywgvasflqkgnddhwiidtdyetfavqysc
rllnldgtcadsysfvfardpsgfspevqkivrqrqeelclarqyrliphngycngk
>d1hbsa_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1hbsb_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpveksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1hbsc_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1hbsd_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpveksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1hbse_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1hbsf_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpveksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1hbsg_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1hbsh_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpveksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>e1hbt.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqf
>e1hbt.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
adcglrplfekksledkterellesyi
>d1hbva_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hbvb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hc1_1 1.78.1.1.2 (5-398) Hemocyanin, N-terminal and middle domains {spiny lobster (Panulirus interruptus)}
tgnaqkqqdinhlldkiyeptkypdlkdiaenfnplgdtsiyndhgaavetlmkelndhr
lleqrhwyslfntrqrkealmlfavlnqckewycfrsnaayfrermnegefvyalyvsvi
hsklgdgivlpplyqitphmftnsevidkaysakmtqkpgtfnvsftgtkknreqrvayf
gedigmnihhvtwhmdfpfwwedsygyhldrkgelffwvhhqltarfdferlsnwldpvd
elhwdriiregfapltsykyggefpvrpdnihfedvdgvahvhdleitesriheaidhgy
itdsdghtidirqpkgiellgdiiesskyssnvqyygslhntahvmlgrqgdphgkfnlp
pgvmehfetatrdpsffrlhkymdnifkkhtdsf
>d1hc1_2 2.1.1.5.9 (399-653) Hemocyanin, C-terminal domain {spiny lobster (Panulirus interruptus)}
ppythdnlefsgmvvngvaidgelitffdefqyslinavdsgeniedveinarvhrlnhn
eftykitmsnnndgerlatfriflcpiednngitltldearwfcieldkffqkvpsgpet
iersskdssvtvpdmpsfqslkeqadnavngghdldlsayerscgipdrmllpkskpegm
efnlyvavtdgdkdteghngghdyggthaqcgvhgeaypdnrplgyplerripdervidg
vsnikhvvvkivhhl
>d1hc2_1 1.78.1.1.2 (5-398) Hemocyanin, N-terminal and middle domains {spiny lobster (Panulirus interruptus)}
tgnaqkqqdinhlldkiyeptkypdlkdiaenfnplgdtsiyndhgaavetlmkelndhr
lleqrhwyslfntrqrkealmlfavlnqckewycfrsnaayfrermnegefvyalyvsvi
hsklgdgivlpplyqitphmftnsevidkaysakmtqkpgtfnvsftgtkknreqrvayf
gedigmnihhvtwhmdfpfwwedsygyhldrkgelffwvhhqltarfdferlsnwldpvd
elhwdriiregfapltsykyggefpvrpdnihfedvdgvahvhdleitesriheaidhgy
itdsdghtidirqpkgiellgdiiesskyssnvqyygslhntahvmlgrqgdphgkfnlp
pgvmehfetatrdpsffrlhkymdnifkkhtdsf
>d1hc2_2 2.1.1.5.9 (399-653) Hemocyanin, C-terminal domain {spiny lobster (Panulirus interruptus)}
ppythdnlefsgmvvngvaidgelitffdefqyslinavdsgeniedveinarvhrlnhn
eftykitmsnnndgerlatfriflcpiednngitltldearwfcieldkffqkvpsgpet
iersskdssvtvpdmpsfqslkeqadnavngghdldlsayerscgipdrmllpkskpegm
efnlyvavtdgdkdteghngghdyggthaqcgvhgeaypdnrplgyplerripdervidg
vsnikhvvvkivhhl
>d1hc3_1 1.78.1.1.2 (5-398) Hemocyanin, N-terminal and middle domains {spiny lobster (Panulirus interruptus)}
tgnaqkqqdinhlldkiyeptkypdlkdiaenfnplgdtsiyndhgaavetlmkelndhr
lleqrhwyslfntrqrkealmlfavlnqckewycfrsnaayfrermnegefvyalyvsvi
hsklgdgivlpplyqitphmftnsevidkaysakmtqkpgtfnvsftgtkknreqrvayf
gedigmnihhvtwhmdfpfwwedsygyhldrkgelffwvhhqltarfdferlsnwldpvd
elhwdriiregfapltsykyggefpvrpdnihfedvdgvahvhdleitesriheaidhgy
itdsdghtidirqpkgiellgdiiesskyssnvqyygslhntahvmlgrqgdphgkfnlp
pgvmehfetatrdpsffrlhkymdnifkkhtdsf
>d1hc3_2 2.1.1.5.9 (399-653) Hemocyanin, C-terminal domain {spiny lobster (Panulirus interruptus)}
ppythdnlefsgmvvngvaidgelitffdefqyslinavdsgeniedveinarvhrlnhn
eftykitmsnnndgerlatfriflcpiednngitltldearwfcieldkffqkvpsgpet
iersskdssvtvpdmpsfqslkeqadnavngghdldlsayerscgipdrmllpkskpegm
efnlyvavtdgdkdteghngghdyggthaqcgvhgeaypdnrplgyplerripdervidg
vsnikhvvvkivhhl
>d1hc4_1 1.78.1.1.2 (5-398) Hemocyanin, N-terminal and middle domains {spiny lobster (Panulirus interruptus)}
tgnaqkqqdinhlldkiyeptkypdlkdiaenfnplgdtsiyndhgaavetlmkelndhr
lleqrhwyslfntrqrkealmlfavlnqckewycfrsnaayfrermnegefvyalyvsvi
hsklgdgivlpplyqitphmftnsevidkaysakmtqkpgtfnvsftgtkknreqrvayf
gedigmnihhvtwhmdfpfwwedsygyhldrkgelffwvhhqltarfdferlsnwldpvd
elhwdriiregfapltsykyggefpvrpdnihfedvdgvahvhdleitesriheaidhgy
itdsdghtidirqpkgiellgdiiesskyssnvqyygslhntahvmlgrqgdphgkfnlp
pgvmehfetatrdpsffrlhkymdnifkkhtdsf
>d1hc4_2 2.1.1.5.9 (399-653) Hemocyanin, C-terminal domain {spiny lobster (Panulirus interruptus)}
ppythdnlefsgmvvngvaidgelitffdefqyslinavdsgeniedveinarvhrlnhn
eftykitmsnnndgerlatfriflcpiednngitltldearwfcieldkffqkvpsgpet
iersskdssvtvpdmpsfqslkeqadnavngghdldlsayerscgipdrmllpkskpegm
efnlyvavtdgdkdteghngghdyggthaqcgvhgeaypdnrplgyplerripdervidg
vsnikhvvvkivhhl
>d1hc5_1 1.78.1.1.2 (5-398) Hemocyanin, N-terminal and middle domains {spiny lobster (Panulirus interruptus)}
tgnaqkqqdinhlldkiyeptkypdlkdiaenfnplgdtsiyndhgaavetlmkelndhr
lleqrhwyslfntrqrkealmlfavlnqckewycfrsnaayfrermnegefvyalyvsvi
hsklgdgivlpplyqitphmftnsevidkaysakmtqkpgtfnvsftgtkknreqrvayf
gedigmnihhvtwhmdfpfwwedsygyhldrkgelffwvhhqltarfdferlsnwldpvd
elhwdriiregfapltsykyggefpvrpdnihfedvdgvahvhdleitesriheaidhgy
itdsdghtidirqpkgiellgdiiesskyssnvqyygslhntahvmlgrqgdphgkfnlp
pgvmehfetatrdpsffrlhkymdnifkkhtdsf
>d1hc5_2 2.1.1.5.9 (399-653) Hemocyanin, C-terminal domain {spiny lobster (Panulirus interruptus)}
ppythdnlefsgmvvngvaidgelitffdefqyslinavdsgeniedveinarvhrlnhn
eftykitmsnnndgerlatfriflcpiednngitltldearwfcieldkffqkvpsgpet
iersskdssvtvpdmpsfqslkeqadnavngghdldlsayerscgipdrmllpkskpegm
efnlyvavtdgdkdteghngghdyggthaqcgvhgeaypdnrplgyplerripdervidg
vsnikhvvvkivhhl
>d1hc6_1 1.78.1.1.2 (5-398) Hemocyanin, N-terminal and middle domains {spiny lobster (Panulirus interruptus)}
tgnaqkqqdinhlldkiyeptkypdlkdiaenfnplgdtsiyndhgaavetlmkelndhr
lleqrhwyslfntrqrkealmlfavlnqckewycfrsnaayfrermnegefvyalyvsvi
hsklgdgivlpplyqitphmftnsevidkaysakmtqkpgtfnvsftgtkknreqrvayf
gedigmnihhvtwhmdfpfwwedsygyhldrkgelffwvhhqltarfdferlsnwldpvd
elhwdriiregfapltsykyggefpvrpdnihfedvdgvahvhdleitesriheaidhgy
itdsdghtidirqpkgiellgdiiesskyssnvqyygslhntahvmlgrqgdphgkfnlp
pgvmehfetatrdpsffrlhkymdnifkkhtdsf
>d1hc6_2 2.1.1.5.9 (399-653) Hemocyanin, C-terminal domain {spiny lobster (Panulirus interruptus)}
ppythdnlefsgmvvngvaidgelitffdefqyslinavdsgeniedveinarvhrlnhn
eftykitmsnnndgerlatfriflcpiednngitltldearwfcieldkffqkvpsgpet
iersskdssvtvpdmpsfqslkeqadnavngghdldlsayerscgipdrmllpkskpegm
efnlyvavtdgdkdteghngghdyggthaqcgvhgeaypdnrplgyplerripdervidg
vsnikhvvvkivhhl
>d1hca__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1hcb__ 2.56.1.1.1 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme I}
pdwgyddkngpeqwsklypiangnnqspvdiktsetkhdtslkpisvsynpatakeiinv
ghsfhvnfedndnrsvlkggpfsdsyrlfqfhfhwgstnehgsehtvdgvkysaelhvah
wnsakysslaeaaskadglavigvlmkvgeanpklqkvldalqaiktkgkrapftnfdps
tllpssldfwtypgslthpplyesvtwiickesisvsseqlaqfrsllsnvegdnavpmq
hnnrptqplkgrtvrasf
>d1hcc__ 7.17.1.1.1 Factor H, 15th and 16th modules {human (Homo sapiens)}
eglpcksppeishgvvahmsdsyqygeevtykcfegfgidgpaiakclgekwshppsci
>d1hcd__ 2.31.5.1.1 Histidine-rich actin-binding protein (hisactophilin) {(Dictyostelium discoideum)}
mgnrafkshhghflsaegeavkthhghhdhhthfhvenhggkvalkthcgkylsigdhkq
vylshhlhgdhslfhlehhggkvsikghhhhyisadhhghvstkehhdhdttfeeiii
>d1hce__ 2.31.5.1.1 Histidine-rich actin-binding protein (hisactophilin) {(Dictyostelium discoideum)}
mgnrafkshhghflsaegeavkthhghhdhhthfhvenhggkvalkthcgkylsigdhkq
vylshhlhgdhslfhlehhggkvsikghhhhyisadhhghvstkehhdhdttfeeiii
>d1hcga_ 2.35.1.2.26 Coagulation factor Xa (Chrismas factor), protease domain {Human (Homo sapiens)}
ivggqeckdgecpwqallineenegfcggtilsefyiltaahclyqakrfkvrvgdrnte
qeeggeavhevevvikhnrftketydfdiavlrlktpitfrmnvapaclperdwaestlm
tqktgivsgfgrthekgrqstrlkmlevpyvdrnscklsssfiitqnmfcagydtkqeda
cqgdsggphvtrfkdtyfvtgivswgegcarkgkygiytkvtaflkwidrsmktrglpka
k
>d1hcgb_ 7.3.9.1.5 Factor X, N-terminal module {human (Homo sapiens)}
csldngdcdqfcheeqnsvvcscargytladngkaciptgpypcgkqtler
>d1hck__ 5.1.1.1.1 Cyclin-dependent PK {Human (Homo sapiens)}
menfqkvekigegtygvvykarnkltgevvalkkirldtetegvpstaireisllkelnh
pnivklldvihtenklylvfeflhqdlkkfmdasaltgiplpliksylfqllqglafchs
hrvlhrdlkpqnllintegaikladfglarafgvpvrtythevvtlwyrapeillgckyy
stavdiwslgcifaemvtrralfpgdseidqlfrifrtlgtpdevvwpgvtsmpdykpsf
pkwarqdfskvvppldedgrsllsqmlhydpnkrisakaalahpffqdvtkpvphlrl
>d1hcl__ 5.1.1.1.1 Cyclin-dependent PK {Human (Homo sapiens)}
menfqkvekigegtygvvykarnkltgevvalkkirldtetegvpstaireisllkelnh
pnivklldvihtenklylvfeflhqdlkkfmdasaltgiplpliksylfqllqglafchs
hrvlhrdlkpqnllintegaikladfglarafgvpvrtythevvtlwyrapeillgckyy
stavdiwslgcifaemvtrralfpgdseidqlfrifrtlgtpdevvwpgvtsmpdykpsf
pkwarqdfskvvppldedgrsllsqmlhydpnkrisakaalahpffqdvtkpvphlrl
>d1hcna_ 7.16.1.4.1 Gonadotropin, A and B chains {Human (Homo sapiens)}
qdcpectlqenpffsqpgapilqcmgccfsrayptplrskktmlvqknvtsestccvaks
ynrvtvmggfkvenhtachcstcyy
>d1hcnb_ 7.16.1.4.1 Gonadotropin, A and B chains {Human (Homo sapiens)}
keplrprcrpinatlavekegcpvcitvntticagycptmtrvlqgvlpalpqvvcnyrd
vrfesirlpgcprgvnpvvsyavalscqcalcrrsttdcggpkdhpltcd
>d1hcoa_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1hcob_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1hcp__ 7.33.1.2.3 Estrogen receptor DNA-binding domain {human (Homo sapiens)/chicken (Gallus gallus)}
mketrycavcndyasgyhygvwscegckaffkrsiqghndymcpatnqctidknrrkscq
acrlrkcyevgmmkg
>d1hcqa_ 7.33.1.2.3 Estrogen receptor DNA-binding domain {human (Homo sapiens)/chicken (Gallus gallus)}
mketrycavcndyasgyhygvwscegckaffkrsiqghndymcpatnqctidknrrkscq
acrlrkcyevgmmk
>d1hcqb_ 7.33.1.2.3 Estrogen receptor DNA-binding domain {human (Homo sapiens)/chicken (Gallus gallus)}
trycavcndyasgyhygvwscegckaffkrsiqghndymcpatnqctidknrrkscqacr
lrkcyevgmmk
>d1hcqe_ 7.33.1.2.3 Estrogen receptor DNA-binding domain {human (Homo sapiens)/chicken (Gallus gallus)}
mketrycavcndyasgyhygvwscegckaffkrsiqghndymcpatnqctidknrrkscq
acrlrkcyevgmmk
>d1hcqf_ 7.33.1.2.3 Estrogen receptor DNA-binding domain {human (Homo sapiens)/chicken (Gallus gallus)}
ketrycavcndyasgyhygvwscegckaffkrsiqghndymcpatnqctidknrrkscqa
crlrkcyevgmmk
>d1hcra_ 1.4.1.2.1 HIN recombinase (DNA-binding domain) {Synthetic}
grprainkheqeqisrllekghprqqlaiifgigvstlyryfpassikkrmn
>d1hcsb_ 4.53.1.1.3 c-src tyrosine kinase {human (Homo sapiens)}
mdsiqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnv
khykirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1hctb_ 4.53.1.1.3 c-src tyrosine kinase {human (Homo sapiens)}
mdsiqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnv
khykirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1hcv__ 2.1.1.1.107 Immunoglobulin (variable domains of L and H chains) {llama (lama glama) VH domain}
vqlqesggglvqaggslrlscaasgrtgstydmgwfrqapgkeresvaainwdsartyya
ssvrgrftisrdnakktvylqmnslkpedtavytcgageggtwdswgqgtqvtvss
>d1hcy_1 1.78.1.1.2 (1-398) Hemocyanin, N-terminal and middle domains {spiny lobster (Panulirus interruptus)}
dalgtgnaqkqqdinhlldkiyeptkypdlkdiaenfnplgdtsiyndhgaavetlmkel
ndhrlleqrhwyslfntrqrkealmlfavlnqckewycfrsnaayfrermnegefvyaly
vsvihsklgdgivlpplyqitphmftnsevidkaysakmtqkpgtfnvsftgtkknreqr
vayfgedigmnihhvtwhmdfpfwwedsygyhldrkgelffwvhhqltarfdferlsnwl
dpvdelhwdriiregfapltsykyggefpvrpdnihfedvdgvahvhdleitesriheai
dhgyitdsdghtidirqpkgiellgdiiesskyssnvqyygslhntahvmlgrqgdphgk
fnlppgvmehfetatrdpsffrlhkymdnifkkhtdsf
>d1hcy_2 2.1.1.5.9 (399-653) Hemocyanin, C-terminal domain {spiny lobster (Panulirus interruptus)}
ppythdnlefsgmvvngvaidgelitffdefqyslinavdsgeniedveinarvhrlnhn
eftykitmsnnndgerlatfriflcpiednngitltldearwfcieldkffqkvpsgpet
iersskdssvtvpdmpsfqslkeqadnavngghdldlsayerscgipdrmllpkskpegm
efnlyvavtdgdkdteghngghdyggthaqcgvhgeaypdnrplgyplerripdervidg
vsnikhvvvkivhhl
>d1hcz_1 2.2.5.1.1 (1-167,231-250) Cytochrome f, large domain {turnip (Brassica rapa)}
ypifaqqnyenpreatgrivcanchlaskpvdievpqavlpdtvfeavvkipydmqlkqv
langkkgalnvgavlilpegfelappdrispemkekignlsfqnyrpnkknilvigpvpg
qkyseitfpilapdpatnkdvhflkypiyvggnrgrgqiypdgsksnXpnvggfgqgdae
ivlqdplr
>d1hcz_2 2.65.2.2.1 (168-230) Cytochrome f, small domain {turnip (Brassica rapa)}
ntvynataggiiskilrkekggyeitivdasnerqvidiiprglellvsegesikldqpl
tsn
>d1hdaa_ 1.1.1.1.19 Hemoglobin, alpha-chain {bovine (Bos taurus)}
vlsaadkgnvkaawgkvgghaaeygaealermflsfpttktyfphfdlshgsaqvkghga
kvaaaltkavehlddlpgalselsdlhahklrvdpvnfkllshsllvtlashlpsdftpa
vhasldkflanvstvltskyr
>d1hdab_ 1.1.1.1.30 Hemoglobin, beta-chain {bovine (Bos taurus)}
mltaeekaavtafwgkvkvdevggealgrllvvypwtqrffesfgdlstadavmnnpkvk
ahgkkvldsfsngmkhlddlkgtfaalselhcdklhvdpenfkllgnvlvvvlarnfgke
ftpvlqadfqkvvagvanalahryh
>d1hdac_ 1.1.1.1.19 Hemoglobin, alpha-chain {bovine (Bos taurus)}
vlsaadkgnvkaawgkvgghaaeygaealermflsfpttktyfphfdlshgsaqvkghga
kvaaaltkavehlddlpgalselsdlhahklrvdpvnfkllshsllvtlashlpsdftpa
vhasldkflanvstvltskyr
>d1hdad_ 1.1.1.1.30 Hemoglobin, beta-chain {bovine (Bos taurus)}
mltaeekaavtafwgkvkvdevggealgrllvvypwtqrffesfgdlstadavmnnpkvk
ahgkkvldsfsngmkhlddlkgtfaalselhcdklhvdpenfkllgnvlvvvlarnfgke
ftpvlqadfqkvvagvanalahryh
>d1hdba_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1hdbb_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkktlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1hdbc_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1hdbd_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkktlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1hdca_ 3.22.1.2.5 3-alpha,20-beta-hydroxysteroid dehydrogenase {(Streptomyces hydrogenans)}
ndlsgktviitggarglgaeaarqavaagarvvladvldeegaatarelgdaaryqhldv
tieedwqrvvayareefgsvdglvnnagistgmfletesverfrkvveinltgvfigmkt
vipamkdagggsivnissaaglmglaltssygaskwgvrglsklaavelgtdrirvnsvh
pgmtytpmtaetgirqgegnypntpmgrvgepgeiagavvkllsdtssyvtgaelavdgg
wttgptvkyvmgq
>d1hdcb_ 3.22.1.2.5 3-alpha,20-beta-hydroxysteroid dehydrogenase {(Streptomyces hydrogenans)}
ndlsgktviitggarglgaeaarqavaagarvvladvldeegaatarelgdaaryqhldv
tieedwqrvvayareefgsvdglvnnagistgmfletesverfrkvveinltgvfigmkt
vipamkdagggsivnissaaglmglaltssygaskwgvrglsklaavelgtdrirvnsvh
pgmtytpmtaetgirqgegnypntpmgrvgepgeiagavvkllsdtssyvtgaelavdgg
wttgptvkyvmgq
>d1hdcc_ 3.22.1.2.5 3-alpha,20-beta-hydroxysteroid dehydrogenase {(Streptomyces hydrogenans)}
ndlsgktviitggarglgaeaarqavaagarvvladvldeegaatarelgdaaryqhldv
tieedwqrvvayareefgsvdglvnnagistgmfletesverfrkvveinltgvfigmkt
vipamkdagggsivnissaaglmglaltssygaskwgvrglsklaavelgtdrirvnsvh
pgmtytpmtaetgirqgegnypntpmgrvgepgeiagavvkllsdtssyvtgaelavdgg
wttgptvkyvmgq
>d1hdcd_ 3.22.1.2.5 3-alpha,20-beta-hydroxysteroid dehydrogenase {(Streptomyces hydrogenans)}
ndlsgktviitggarglgaeaarqavaagarvvladvldeegaatarelgdaaryqhldv
tieedwqrvvayareefgsvdglvnnagistgmfletesverfrkvveinltgvfigmkt
vipamkdagggsivnissaaglmglaltssygaskwgvrglsklaavelgtdrirvnsvh
pgmtytpmtaetgirqgegnypntpmgrvgepgeiagavvkllsdtssyvtgaelavdgg
wttgptvkyvmgq
>d1hddc_ 1.4.1.1.1 engrailed Homeodomain {(Drosophila melanogaster)}
rprtafsseqlarlkrefnenrylterrrqqlsselglneaqikiwfqnkrakikks
>d1hddd_ 1.4.1.1.1 engrailed Homeodomain {(Drosophila melanogaster)}
rprtafsseqlarlkrefnenrylterrrqqlsselglneaqikiwfqnkrakikks
>d1hdea_ 3.56.1.3.1 Haloalkane dehalogenase {(Xanthobacter autotrophicus)}
minairtpdqrfsnldqypfspnylddlpgypglrahyldegnsdaedvflclhgeptws
ylyrkmipvfaesgarviapdffgfgksdkpvdeedytfefhrnfllalierldlrnitl
vvqdwggflgltlpmadpsrfkrliimnaclmtdpvtqpafsafvtqpadgwtawkydlv
tpsdlrldqfmkrwaptlteaeasayaapfpdtsyqagvrkfpkmvaqrdqacidistea
isfwqndwngqtfmaigmkdkllgpdvmypmkalingcpepleiadaghfvqefgeqvar
ealkhfaete
>d1hdeb_ 3.56.1.3.1 Haloalkane dehalogenase {(Xanthobacter autotrophicus)}
minairtpdqrfsnldqypfspnylddlpgypglrahyldegnsdaedvflclhgeptws
ylyrkmipvfaesgarviapdffgfgksdkpvdeedytfefhrnfllalierldlrnitl
vvqdwggflgltlpmadpsrfkrliimnaclmtdpvtqpafsafvtqpadgwtawkydlv
tpsdlrldqfmkrwaptlteaeasayaapfpdtsyqagvrkfpkmvaqrdqacidistea
isfwqndwngqtfmaigmkdkllgpdvmypmkalingcpepleiadaghfvqefgeqvar
ealkhfaete
>d1hdgo1 3.22.1.3.4 (1-148,313-331) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Thermotoga maritima)}
arvaingfgrigrlvyriiyerknpdievvaindltdtktlahllkydsvhkkfpgkvey
tenslivdgkeikvfaepdpsklpwkdlgvdfviestgvfrnrekaelhlqagakkviit
apakgeditvvigcnedqlkpehtiiscasXneygysnrvvdtlelllkm
>d1hdgo2 4.42.1.1.4 (149-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Thermotoga maritima)}
cttnsiapivkvlhekfgivsgmlttvhsytndqrvldlphkdlrraraaavniiptttg
aakavalvvpevkgkldgmairvptpdgsitdltvlvekettveevnavmkeategrlkg
iigyndepivssdiigttfsgifdatitnviggklvkvaswyd
>d1hdgq1 3.22.1.3.4 (1-148,313-331) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Thermotoga maritima)}
arvaingfgrigrlvyriiyerknpdievvaindltdtktlahllkydsvhkkfpgkvey
tenslivdgkeikvfaepdpsklpwkdlgvdfviestgvfrnrekaelhlqagakkviit
apakgeditvvigcnedqlkpehtiiscasXneygysnrvvdtlelllkm
>d1hdgq2 4.42.1.1.4 (149-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Thermotoga maritima)}
cttnsiapivkvlhekfgivsgmlttvhsytndqrvldlphkdlrraraaavniiptttg
aakavalvvpevkgkldgmairvptpdgsitdltvlvekettveevnavmkeategrlkg
iigyndepivssdiigttfsgifdatitnviggklvkvaswyd
>d1hdj__ 1.2.2.1.1 HSP40 {Human (Homo sapiens)}
mgkdyyqtlglargasdeeikrayrrqalryhpdknkepgaeekfkeiaeaydvlsdprk
reifdrygeeglkgsgc
>d1hdn__ 4.54.1.1.3 Histidine-containing phosphocarrier proteins (HPr) {(Escherichia coli)}
mfqqevtitapnglhtrpaaqfvkeakgftseitvtsngksasakslfklqtlgltqgtv
vtisaegedeqkavehlvklmaele
>d1hdp__ 1.4.1.1.8 Oct-2 POU Homeodomain {human (Homo sapiens)}
rrkkrtsietnvrfaleksflanqkptseeilliaeqlhmekevirvwfcnrrqkekrin
pcs
>d1hdr__ 3.22.1.2.8 Dihydropteridin reductase {human (Homo sapiens)}
earrvlvyggrgalgsrcvqafrarnwwvasvdvveneeasasiivkmtdsfteqadqvt
aevgkllgeekvdailcvaggwaggnakskslfkncdlmwkqsiwtstisshlatkhlke
gglltlagakaaldgtpgmigygmakgavhqlcqslagknsgmppgaaaiavlpvtldtp
mnrksmpeadfsswtpleflvetfhdwitgknrpssgsliqvvttegrteltpayf
>d1hdsa_ 1.1.1.1.18 Hemoglobin, alpha-chain {deer (Odocoileus virginianus)}
vlsaanksnvkaawgkvggnapaygaqalqrmflsfpttktyfphfdlshgsaqqkahgq
kvanaltkaqghlndlpgtlsnlsnlhahklrvnpvnfkllshsllvtlashlptnftpa
vhanlnkflandstvltskyr
>d1hdsb_ 1.1.1.1.29 Hemoglobin, beta-chain {deer (Odocoileus virginianus)}
mltaeekaavtgfwgkvdvdvvgaqalgrllvvypwtqrffqhfgnlssagavmnnpkvk
ahgkrvldaftqglkhlddlkgafaqlsglhcnklhvnpqnfrllgnvlalvvarnfggq
ftpnvqalfqkvvagvanalahkyh
>d1hdsc_ 1.1.1.1.18 Hemoglobin, alpha-chain {deer (Odocoileus virginianus)}
vlsaanksnvkaawgkvggnapaygaqalqrmflsfpttktyfphfdlshgsaqqkahgq
kvanaltkaqghlndlpgtlsnlsnlhahklrvnpvnfkllshsllvtlashlptnftpa
vhanlnkflandstvltskyr
>d1hdsd_ 1.1.1.1.29 Hemoglobin, beta-chain {deer (Odocoileus virginianus)}
mltaeekaavtgfwgkvdvdvvgaqalgrllvvypwtqrffqhfgnlssagavmnnpkvk
ahgkrvldaftqglkhlddlkgafaqlsglhcnklhvnpqnfrllgnvlalvvarnfggq
ftpnvqalfqkvvagvanalahkyh
>e1hdt.1h 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>e1hdt.1l 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
sgeadcglrplfekksledkterellesyidgr
>d1hdxa1 2.25.1.2.2 (1-174,325-374) Alcohol dehydrogenase {human (Homo sapiens)}
stagkvikckaavlwevkkpfsiedvevappkayevrikmvavgicrtddhvvsgnlvtp
lpvilgheaagivesvgegvttvkpgdkviplftpqcgkcrvcknpesnyclkndlgnpr
gtlqdgtrrftcrgkpihhflgtstfsqytvvdenavakidaasplekvcligcXkegip
klvadfmakkfsldalithvlpfekinegfdllhsgksirtvltf
>d1hdxa2 3.22.1.1.2 (175-324) Alcohol dehydrogenase {human (Homo sapiens), different isozymes}
gfstgygsavnvakvtpgstcavfglggvglsavmgckaagaariiavdinkdkfakake
lgatecinpqdykkpiqevlkemtdggvdfsfevigrldtmmasllccheacgtsvivgv
ppasqnlsinpmllltgrtwkgavyggfks
>d1hdxb1 2.25.1.2.2 (1-174,325-374) Alcohol dehydrogenase {human (Homo sapiens)}
stagkvikckaavlwevkkpfsiedvevappkayevrikmvavgicrtddhvvsgnlvtp
lpvilgheaagivesvgegvttvkpgdkviplftpqcgkcrvcknpesnyclkndlgnpr
gtlqdgtrrftcrgkpihhflgtstfsqytvvdenavakidaasplekvcligcXkegip
klvadfmakkfsldalithvlpfekinegfdllhsgksirtvltf
>d1hdxb2 3.22.1.1.2 (175-324) Alcohol dehydrogenase {human (Homo sapiens), different isozymes}
gfstgygsavnvakvtpgstcavfglggvglsavmgckaagaariiavdinkdkfakake
lgatecinpqdykkpiqevlkemtdggvdfsfevigrldtmmasllccheacgtsvivgv
ppasqnlsinpmllltgrtwkgavyggfks
>d1hdya1 2.25.1.2.2 (1-174,325-374) Alcohol dehydrogenase {human (Homo sapiens)}
stagkvikckaavlwevkkpfsiedvevappkayevrikmvavgichtddhvvsgnlvtp
lpvilgheaagivesvgegvttvkpgdkviplftpqcgkcrvcknpesnyclkndlgnpr
gtlqdgtrrftcrgkpihhflgtstfsqytvvdenavakidaasplekvcligcXkegip
klvadfmakkfsldalithvlpfekinegfdllhsgksirtvltf
>d1hdya2 3.22.1.1.2 (175-324) Alcohol dehydrogenase {human (Homo sapiens), different isozymes}
gfstgygsavnvakvtpgstcavfglggvglsavmgckaagaariiavdinkdkfakake
lgatecinpqdykkpiqevlkemtdggvdfsfevigrldtmmasllccheacgtsvivgv
ppasqnlsinpmllltgrtwkgavyggfks
>d1hdyb1 2.25.1.2.2 (1-174,325-374) Alcohol dehydrogenase {human (Homo sapiens)}
stagkvikckaavlwevkkpfsiedvevappkayevrikmvavgichtddhvvsgnlvtp
lpvilgheaagivesvgegvttvkpgdkviplftpqcgkcrvcknpesnyclkndlgnpr
gtlqdgtrrftcrgkpihhflgtstfsqytvvdenavakidaasplekvcligcXkegip
klvadfmakkfsldalithvlpfekinegfdllhsgksirtvltf
>d1hdyb2 3.22.1.1.2 (175-324) Alcohol dehydrogenase {human (Homo sapiens), different isozymes}
gfstgygsavnvakvtpgstcavfglggvglsavmgckaagaariiavdinkdkfakake
lgatecinpqdykkpiqevlkemtdggvdfsfevigrldtmmasllccheacgtsvivgv
ppasqnlsinpmllltgrtwkgavyggfks
>d1hdza1 2.25.1.2.2 (1-174,325-374) Alcohol dehydrogenase {human (Homo sapiens)}
stagkvikckaavlwevkkpfsiedvevappkayevrikmvavgicgtddhvvsgnlvtp
lpvilgheaagivesvgegvttvkpgdkviplftpqcgkcrvcknpesnyclkndlgnpr
gtlqdgtrrftcrgkpihhflgtstfsqytvvdenavakidaasplekvcligcXkegip
klvadfmakkfsldalithvlpfekinegfdllhsgksirtvltf
>d1hdza2 3.22.1.1.2 (175-324) Alcohol dehydrogenase {human (Homo sapiens), different isozymes}
gfstgygsavnvakvtpgstcavfglggvglsavmgckaagaariiavdinkdkfakake
lgatecinpqdykkpiqevlkemtdggvdfsfevigrldtmmasllccheacgtsvivgv
ppasqnlsinpmllltgrtwkgavyggfks
>d1hdzb1 2.25.1.2.2 (1-174,325-374) Alcohol dehydrogenase {human (Homo sapiens)}
stagkvikckaavlwevkkpfsiedvevappkayevrikmvavgicgtddhvvsgnlvtp
lpvilgheaagivesvgegvttvkpgdkviplftpqcgkcrvcknpesnyclkndlgnpr
gtlqdgtrrftcrgkpihhflgtstfsqytvvdenavakidaasplekvcligcXkegip
klvadfmakkfsldalithvlpfekinegfdllhsgksirtvltf
>d1hdzb2 3.22.1.1.2 (175-324) Alcohol dehydrogenase {human (Homo sapiens), different isozymes}
gfstgygsavnvakvtpgstcavfglggvglsavmgckaagaariiavdinkdkfakake
lgatecinpqdykkpiqevlkemtdggvdfsfevigrldtmmasllccheacgtsvivgv
ppasqnlsinpmllltgrtwkgavyggfks
>d1hea__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgsrttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasf
>d1heb__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgsettppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1hec__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgshttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasf
>d1hed__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgsattppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1hefe_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleenslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hege_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleenslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hel__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1hem__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditatvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1hen__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygvlqins
rwwcndgrtpgsrnlcnipcsallssditatvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1heo__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygvlqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1hep__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfnsqatnrntdgstdygvlqins
rwwcndgrtpgsrnlcnipcsallssditatvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1heq__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfnsqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditatvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1her__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfnsqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1hev__ 7.3.1.1.2 Hevein {(Hevea brasiliensis)}
eqcgrqaggklcpnnlccsqwgwcgstdeycspdhncqsnckd
>d1hew__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1hex__ 3.65.1.1.1 3-isopropylmalate dehydrogenase {(Thermus thermophilus), strain HB8}
mkvavlpgdgigpevteaalkvlraldeaeglglayevfpfggaaidafgepfpeptrkg
veeaeavllgsvggpkwdglprkirpetgllslrksqdlfanlrpakvfpglerlsplke
eiargvdvlivreltggiyfgeprgmseaeawnteryskpevervarvafeaarkrrkhv
vsvdkanvlevgefwrktveevgrgypdvalehqyvdamamhlvrsparfdvvvtgnifg
dilsdlasvlpgslgllpsaslgrgtpvfepvhgsapdiagkgianptaailsaammleh
afglvelarkvedavakalletpppdlggsagteaftatvlrhla
>d1hey__ 3.14.2.1.1 CheY protein {(Escherichia coli)}
dkelkflvvgnggtgkstvrnllkelgfnnvedaedgvdalnklqaggygfvisdwnmpn
mdglellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleeklnk
ifeklgm
>d1hfc__ 4.52.1.7.1 Fibroblast collagenase {human (Homo sapiens)}
prweqthltyrienytpdlpradvdhaiekafqlwsnvtpltftkvsegqadimisfvrg
dhrdnspfdgpggnlahafqpgpgiggdahfdederwtnnfreynlhrvaahelghslgl
shstdigalmypsytfsgdvqlaqddidgiqaiygrs
>d1hfh_1 7.17.1.1.1 (1-63) Factor H, 15th and 16th modules {human (Homo sapiens)}
ekipcsqppqiehgtinssrssqesyahgtklsytceggfriseenettcymgkwssppq
ceg
>d1hfh_2 7.17.1.1.1 (64-120) Factor H, 15th and 16th modules {human (Homo sapiens)}
lpcksppeishgvvahmsdsyqygeevtykcfegfgidgpaiakclgekwshppsci
>d1hfi__ 7.17.1.1.1 Factor H, 15th and 16th modules {human (Homo sapiens)}
ekipcsqppqiehgtinssrssqesyahgtklsytceggfriseenettcymgkwssppq
ce
>d1hfp__ 3.60.1.1.5 Dihydrofolate reductases, eukaryotic type {human (Homo sapiens)}
vgslncivavsqnmgigkngdlpwpplrnegryfqrmtttssvegkqnlvimgkktwfsi
peknrplkgrinlvlsrelkeppqgahflsrslddalklteqpelankvdmvwivggssv
ykeamnhpghlklfvtrimqdfesdtffpeidlekykllpeypgvlsdvqeekgikykfe
vyeknd
>d1hfq__ 3.60.1.1.5 Dihydrofolate reductases, eukaryotic type {human (Homo sapiens)}
vgslncivavsqnmgigkngdlpwpplrnesryfqrmtttssvegkqnlvimgkktwfsi
peknrplkgrinlvlsrelkeppqgahflsrslddalklteqpelankvdmvwivggssv
ykeamnhpghlklfvtrimqdfesdtffpeidlekykllpeypgvlsdvqeekgikykfe
vyeknd
>d1hfr__ 3.60.1.1.5 Dihydrofolate reductases, eukaryotic type {human (Homo sapiens)}
vgslncivavsqnmgigkngdlpwpplrnefryfqrmtttssvegkqnlvimgkktwfsi
peknrplkgrinlvlsrelkeppqgahflsrslddalklteqpelankvdmvwivggssv
ykeamnhpghlklfvtrimqdfesdtffpeidlekykllpeypgvlsdvqeekgikykfe
vyeknd
>d1hfs__ 4.52.1.7.3 Stromelysin-1 (MMP-3) {human (Homo sapiens) fibroblast}
gipkwrkthltyrivnytpdlpkdavdsavekalkvweevtpltfsrlyegeadimisfa
vrehgdfypfdgpgnvlahayapgpgingdahfdddeqwtkdttgtnlflvaaheighsl
glfhsantealmyplyhsltdltrfrlsqddingiqslyg
>d1hfx__ 4.2.1.2.15 alpha-Lactalbumin {guinea pig (Gavia porcellus)}
kqltkcalshelndlagyrditlpewlciifhisgydtqaivknsdhkeyglfqindkdf
cessttvqsrnicdiscdklldddltddimcvkkildikgidywlahkplcsdkleqwyc
eaq
>d1hfya_ 4.2.1.2.16 alpha-Lactalbumin {goat (Capra hircus)}
eqltkcevfqklkdlkdyggvslpewvctafhtsgydtqaivqnndsteyglfqinnkiw
ckddqnphsrnicniscdkfldddltddivcakkildkvginywlahkalcsekldqwlc
>d1hfyb_ 4.2.1.2.16 alpha-Lactalbumin {goat (Capra hircus)}
eqltkcevfqklkdlkdyggvslpewvctafhtsgydtqaivqnndsteyglfqinnkiw
ckddqnphsrnicniscdkfldddltddivcakkildkvginywlahkalcsekldqwlc
>d1hfza_ 4.2.1.2.17 alpha-Lactalbumin {bovine (Bos taurus)}
meqltkcevfrelkdlkgyggvslpewvcttfhtsgydtqaivqnndsteyglfqinnki
wckddqnphssnicniscdkfldddltddivcvkkildkvginywlahkalcsekldqwl
cek
>d1hfzb_ 4.2.1.2.17 alpha-Lactalbumin {bovine (Bos taurus)}
meqltkcevfrelkdlkgyggvslpewvcttfhtsgydtqaivqnndsteyglfqinnki
wckddqnphssnicniscdkfldddltddivcvkkildkvginywlahkalcsekldqwl
ce
>d1hfzc_ 4.2.1.2.17 alpha-Lactalbumin {bovine (Bos taurus)}
meqltkcevfrelkdlkgyggvslpewvcttfhtsgydtqaivqnndsteyglfqinnki
wckddqnphssnicniscdkfldddltddivcvkkildkvginywlahkalcsekldqwl
ce
>d1hfzd_ 4.2.1.2.17 alpha-Lactalbumin {bovine (Bos taurus)}
meqltkcevfrelkdlkgyggvslpewvcttfhtsgydtqaivqnndsteyglfqinnki
wckddqnphssnicniscdkfldddltddivcvkkildkvginywlahkalcsekldqwl
cekl
>d1hgaa_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1hgab_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1hgac_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1hgad_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1hgba_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1hgbb_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1hgbc_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1hgbd_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1hgca_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1hgcb_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1hgcc_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1hgcd_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1hgda_ 2.14.1.2.1 Hemagglutinin, headpiece {influenza virus (Strain x-31)}
qdlpgndnstatlclghhavpngtlvktitddqievtnatelvqssstgkicnnphrild
gidctlidallgdphcdvfqnetwdlfverskafsncypydvpdyaslrslvassgtlef
itegftwtgvtqngrsnackrgpgsgffsrlnwltksgstypvlnvtmpnndnfdklyiw
gihhpstnqeqtslyvqasgrvtvstrrsqqtiipnigsrpwvrglssrisiywtivkpg
dvlvinsngnliaprgyfkmrtgkssimrsdapidtcisecitpngsipndkpfqnvnki
tygacpkyvkqntlklatgmrnvpekqt
>d1hgdb_ 6.2.1.1.1 Influenza hemagglutinin (stalk) {(Influenza virus A)}
glfgaiagfiengwegmidgwygfrhqnsegtgqaadlkstqaaidqingklnrviektn
ekfhqiekefsevegriqdlekyvedtkidlwsynaellvalenqhtidltdsemnklfe
ktrrqlrenaeemgngcfkiyhkcdnaciesirngtydhdvyrdealnnrfqikg
>d1hgdc_ 2.14.1.2.1 Hemagglutinin, headpiece {influenza virus (Strain x-31)}
qdlpgndnstatlclghhavpngtlvktitddqievtnatelvqssstgkicnnphrild
gidctlidallgdphcdvfqnetwdlfverskafsncypydvpdyaslrslvassgtlef
itegftwtgvtqngrsnackrgpgsgffsrlnwltksgstypvlnvtmpnndnfdklyiw
gihhpstnqeqtslyvqasgrvtvstrrsqqtiipnigsrpwvrglssrisiywtivkpg
dvlvinsngnliaprgyfkmrtgkssimrsdapidtcisecitpngsipndkpfqnvnki
tygacpkyvkqntlklatgmrnvpekqt
>d1hgdd_ 6.2.1.1.1 Influenza hemagglutinin (stalk) {(Influenza virus A)}
glfgaiagfiengwegmidgwygfrhqnsegtgqaadlkstqaaidqingklnrviektn
ekfhqiekefsevegriqdlekyvedtkidlwsynaellvalenqhtidltdsemnklfe
ktrrqlrenaeemgngcfkiyhkcdnaciesirngtydhdvyrdealnnrfqikg
>d1hgde_ 2.14.1.2.1 Hemagglutinin, headpiece {influenza virus (Strain x-31)}
qdlpgndnstatlclghhavpngtlvktitddqievtnatelvqssstgkicnnphrild
gidctlidallgdphcdvfqnetwdlfverskafsncypydvpdyaslrslvassgtlef
itegftwtgvtqngrsnackrgpgsgffsrlnwltksgstypvlnvtmpnndnfdklyiw
gihhpstnqeqtslyvqasgrvtvstrrsqqtiipnigsrpwvrglssrisiywtivkpg
dvlvinsngnliaprgyfkmrtgkssimrsdapidtcisecitpngsipndkpfqnvnki
tygacpkyvkqntlklatgmrnvpekqt
>d1hgdf_ 6.2.1.1.1 Influenza hemagglutinin (stalk) {(Influenza virus A)}
glfgaiagfiengwegmidgwygfrhqnsegtgqaadlkstqaaidqingklnrviektn
ekfhqiekefsevegriqdlekyvedtkidlwsynaellvalenqhtidltdsemnklfe
ktrrqlrenaeemgngcfkiyhkcdnaciesirngtydhdvyrdealnnrfqikg
>d1hgea_ 2.14.1.2.1 Hemagglutinin, headpiece {influenza virus (Strain x-31)}
qdlpgndnstatlclghhavpngtlvktitddqievtnatelvqssstgkicnnphrild
gidctlidallgdphcdvfqnetwdlfverskafsncypydvpdyaslrslvassgtlef
itegftwtgvtqngrsnackrgpgsgffsrlnwltksgstypvlnvtmpnndnfdklyiw
gihhpstnqeqtslyvqasgrvtvstrrsqqtiipnigsrpwvrglssrisiywtivkpg
dvlvinsngnliaprgyfkmrtgkssimrsdapidtcisecitpngsipndkpfqnvnki
tygacpkyvkqntlklatgmrnvpekqt
>d1hgeb_ 6.2.1.1.1 Influenza hemagglutinin (stalk) {(Influenza virus A)}
glfgaiagfiengwegmidgwygfrhqnsegtgqaadlkstqaaidqingklnrviektn
ekfhqiekefsevegriqdlekyvedtkidlwsynaellvalenqhtidltdsemnklfe
ktrrqlrenaeemgngcfkiyhkcdnaciesirngtydhdvyrdealnnrfqikg
>d1hgec_ 2.14.1.2.1 Hemagglutinin, headpiece {influenza virus (Strain x-31)}
qdlpgndnstatlclghhavpngtlvktitddqievtnatelvqssstgkicnnphrild
gidctlidallgdphcdvfqnetwdlfverskafsncypydvpdyaslrslvassgtlef
itegftwtgvtqngrsnackrgpgsgffsrlnwltksgstypvlnvtmpnndnfdklyiw
gihhpstnqeqtslyvqasgrvtvstrrsqqtiipnigsrpwvrglssrisiywtivkpg
dvlvinsngnliaprgyfkmrtgkssimrsdapidtcisecitpngsipndkpfqnvnki
tygacpkyvkqntlklatgmrnvpekqt
>d1hged_ 6.2.1.1.1 Influenza hemagglutinin (stalk) {(Influenza virus A)}
glfgaiagfiengwegmidgwygfrhqnsegtgqaadlkstqaaidqingklnrviektn
ekfhqiekefsevegriqdlekyvedtkidlwsynaellvalenqhtidltdsemnklfe
ktrrqlrenaeemgngcfkiyhkcdnaciesirngtydhdvyrdealnnrfqikg
>d1hgee_ 2.14.1.2.1 Hemagglutinin, headpiece {influenza virus (Strain x-31)}
qdlpgndnstatlclghhavpngtlvktitddqievtnatelvqssstgkicnnphrild
gidctlidallgdphcdvfqnetwdlfverskafsncypydvpdyaslrslvassgtlef
itegftwtgvtqngrsnackrgpgsgffsrlnwltksgstypvlnvtmpnndnfdklyiw
gihhpstnqeqtslyvqasgrvtvstrrsqqtiipnigsrpwvrglssrisiywtivkpg
dvlvinsngnliaprgyfkmrtgkssimrsdapidtcisecitpngsipndkpfqnvnki
tygacpkyvkqntlklatgmrnvpekqt
>d1hgef_ 6.2.1.1.1 Influenza hemagglutinin (stalk) {(Influenza virus A)}
glfgaiagfiengwegmidgwygfrhqnsegtgqaadlkstqaaidqingklnrviektn
ekfhqiekefsevegriqdlekyvedtkidlwsynaellvalenqhtidltdsemnklfe
ktrrqlrenaeemgngcfkiyhkcdnaciesirngtydhdvyrdealnnrfqikg
>d1hgfa_ 2.14.1.2.1 Hemagglutinin, headpiece {influenza virus (Strain x-31)}
qdlpgndnstatlclghhavpngtlvktitddqievtnatelvqssstgkicnnphrild
gidctlidallgdphcdvfqnetwdlfverskafsncypydvpdyaslrslvassgtlef
itegftwtgvtqnggsnackrgpgsgffsrlnwltksgstypvlnvtmpnndnfdklyiw
gihhpstnqeqtslyvqasgrvtvstrrsqqtiipnigsrpwvrglssrisiywtivkpg
dvlvinsngnliaprgyfkmrtgkssimrsdapidtcisecitpngsipndkpfqnvnki
tygacpkyvkqntlklatgmrnvpekqt
>d1hgfb_ 6.2.1.1.1 Influenza hemagglutinin (stalk) {(Influenza virus A)}
glfgaiagfiengwegmidgwygfrhqnsegtgqaadlkstqaaidqingklnrviektn
ekfhqiekefsevegriqdlekyvedtkidlwsynaellvalenqhtidltdsemnklfe
ktrrqlrenaeemgngcfkiyhkcdnaciesirngtydhdvyrdealnnrfqikg
>d1hgfc_ 2.14.1.2.1 Hemagglutinin, headpiece {influenza virus (Strain x-31)}
qdlpgndnstatlclghhavpngtlvktitddqievtnatelvqssstgkicnnphrild
gidctlidallgdphcdvfqnetwdlfverskafsncypydvpdyaslrslvassgtlef
itegftwtgvtqnggsnackrgpgsgffsrlnwltksgstypvlnvtmpnndnfdklyiw
gihhpstnqeqtslyvqasgrvtvstrrsqqtiipnigsrpwvrglssrisiywtivkpg
dvlvinsngnliaprgyfkmrtgkssimrsdapidtcisecitpngsipndkpfqnvnki
tygacpkyvkqntlklatgmrnvpekqt
>d1hgfd_ 6.2.1.1.1 Influenza hemagglutinin (stalk) {(Influenza virus A)}
glfgaiagfiengwegmidgwygfrhqnsegtgqaadlkstqaaidqingklnrviektn
ekfhqiekefsevegriqdlekyvedtkidlwsynaellvalenqhtidltdsemnklfe
ktrrqlrenaeemgngcfkiyhkcdnaciesirngtydhdvyrdealnnrfqikg
>d1hgfe_ 2.14.1.2.1 Hemagglutinin, headpiece {influenza virus (Strain x-31)}
qdlpgndnstatlclghhavpngtlvktitddqievtnatelvqssstgkicnnphrild
gidctlidallgdphcdvfqnetwdlfverskafsncypydvpdyaslrslvassgtlef
itegftwtgvtqnggsnackrgpgsgffsrlnwltksgstypvlnvtmpnndnfdklyiw
gihhpstnqeqtslyvqasgrvtvstrrsqqtiipnigsrpwvrglssrisiywtivkpg
dvlvinsngnliaprgyfkmrtgkssimrsdapidtcisecitpngsipndkpfqnvnki
tygacpkyvkqntlklatgmrnvpekqt
>d1hgff_ 6.2.1.1.1 Influenza hemagglutinin (stalk) {(Influenza virus A)}
glfgaiagfiengwegmidgwygfrhqnsegtgqaadlkstqaaidqingklnrviektn
ekfhqiekefsevegriqdlekyvedtkidlwsynaellvalenqhtidltdsemnklfe
ktrrqlrenaeemgngcfkiyhkcdnaciesirngtydhdvyrdealnnrfqikg
>d1hgga_ 2.14.1.2.1 Hemagglutinin, headpiece {influenza virus (Strain x-31)}
qdlpgndnstatlclghhavpngtlvktitddqievtnatelvqssstgkicnnphrild
gidctlidallgdphcdvfqnetwdlfverskafsncypydvpdyaslrslvassgtlef
itegftwtgvtqnggsnackrgpgsgffsrlnwltksgstypvlnvtmpnndnfdklyiw
gihhpstnqeqtslyvqasgrvtvstrrsqqtiipnigsrpwvrglssrisiywtivkpg
dvlvinsngnliaprgyfkmrtgkssimrsdapidtcisecitpngsipndkpfqnvnki
tygacpkyvkqntlklatgmrnvpekqt
>d1hggb_ 6.2.1.1.1 Influenza hemagglutinin (stalk) {(Influenza virus A)}
glfgaiagfiengwegmidgwygfrhqnsegtgqaadlkstqaaidqingklnrviektn
ekfhqiekefsevegriqdlekyvedtkidlwsynaellvalenqhtidltdsemnklfe
ktrrqlrenaeemgngcfkiyhkcdnaciesirngtydhdvyrdealnnrfqikg
>d1hggc_ 2.14.1.2.1 Hemagglutinin, headpiece {influenza virus (Strain x-31)}
qdlpgndnstatlclghhavpngtlvktitddqievtnatelvqssstgkicnnphrild
gidctlidallgdphcdvfqnetwdlfverskafsncypydvpdyaslrslvassgtlef
itegftwtgvtqnggsnackrgpgsgffsrlnwltksgstypvlnvtmpnndnfdklyiw
gihhpstnqeqtslyvqasgrvtvstrrsqqtiipnigsrpwvrglssrisiywtivkpg
dvlvinsngnliaprgyfkmrtgkssimrsdapidtcisecitpngsipndkpfqnvnki
tygacpkyvkqntlklatgmrnvpekqt
>d1hggd_ 6.2.1.1.1 Influenza hemagglutinin (stalk) {(Influenza virus A)}
glfgaiagfiengwegmidgwygfrhqnsegtgqaadlkstqaaidqingklnrviektn
ekfhqiekefsevegriqdlekyvedtkidlwsynaellvalenqhtidltdsemnklfe
ktrrqlrenaeemgngcfkiyhkcdnaciesirngtydhdvyrdealnnrfqikg
>d1hgge_ 2.14.1.2.1 Hemagglutinin, headpiece {influenza virus (Strain x-31)}
qdlpgndnstatlclghhavpngtlvktitddqievtnatelvqssstgkicnnphrild
gidctlidallgdphcdvfqnetwdlfverskafsncypydvpdyaslrslvassgtlef
itegftwtgvtqnggsnackrgpgsgffsrlnwltksgstypvlnvtmpnndnfdklyiw
gihhpstnqeqtslyvqasgrvtvstrrsqqtiipnigsrpwvrglssrisiywtivkpg
dvlvinsngnliaprgyfkmrtgkssimrsdapidtcisecitpngsipndkpfqnvnki
tygacpkyvkqntlklatgmrnvpekqt
>d1hggf_ 6.2.1.1.1 Influenza hemagglutinin (stalk) {(Influenza virus A)}
glfgaiagfiengwegmidgwygfrhqnsegtgqaadlkstqaaidqingklnrviektn
ekfhqiekefsevegriqdlekyvedtkidlwsynaellvalenqhtidltdsemnklfe
ktrrqlrenaeemgngcfkiyhkcdnaciesirngtydhdvyrdealnnrfqikg
>d1hgha_ 2.14.1.2.1 Hemagglutinin, headpiece {influenza virus (Strain x-31)}
qdlpgndnstatlclghhavpngtlvktitddqievtnatelvqssstgkicnnphrild
gidctlidallgdphcdvfqnetwdlfverskafsncypydvpdyaslrslvassgtlef
itegftwtgvtqnggsnackrgpgsgffsrlnwltksgstypvlnvtmpnndnfdklyiw
gihhpstnqeqtslyvqasgrvtvstrrsqqtiipnigsrpwvrglssrisiywtivkpg
dvlvinsngnliaprgyfkmrtgkssimrsdapidtcisecitpngsipndkpfqnvnki
tygacpkyvkqntlklatgmrnvpekqt
>d1hghb_ 6.2.1.1.1 Influenza hemagglutinin (stalk) {(Influenza virus A)}
glfgaiagfiengwegmidgwygfrhqnsegtgqaadlkstqaaidqingklnrviektn
ekfhqiekefsevegriqdlekyvedtkidlwsynaellvalenqhtidltdsemnklfe
ktrrqlrenaeemgngcfkiyhkcdnaciesirngtydhdvyrdealnnrfqikg
>d1hghc_ 2.14.1.2.1 Hemagglutinin, headpiece {influenza virus (Strain x-31)}
qdlpgndnstatlclghhavpngtlvktitddqievtnatelvqssstgkicnnphrild
gidctlidallgdphcdvfqnetwdlfverskafsncypydvpdyaslrslvassgtlef
itegftwtgvtqnggsnackrgpgsgffsrlnwltksgstypvlnvtmpnndnfdklyiw
gihhpstnqeqtslyvqasgrvtvstrrsqqtiipnigsrpwvrglssrisiywtivkpg
dvlvinsngnliaprgyfkmrtgkssimrsdapidtcisecitpngsipndkpfqnvnki
tygacpkyvkqntlklatgmrnvpekqt
>d1hghd_ 6.2.1.1.1 Influenza hemagglutinin (stalk) {(Influenza virus A)}
glfgaiagfiengwegmidgwygfrhqnsegtgqaadlkstqaaidqingklnrviektn
ekfhqiekefsevegriqdlekyvedtkidlwsynaellvalenqhtidltdsemnklfe
ktrrqlrenaeemgngcfkiyhkcdnaciesirngtydhdvyrdealnnrfqikg
>d1hghe_ 2.14.1.2.1 Hemagglutinin, headpiece {influenza virus (Strain x-31)}
qdlpgndnstatlclghhavpngtlvktitddqievtnatelvqssstgkicnnphrild
gidctlidallgdphcdvfqnetwdlfverskafsncypydvpdyaslrslvassgtlef
itegftwtgvtqnggsnackrgpgsgffsrlnwltksgstypvlnvtmpnndnfdklyiw
gihhpstnqeqtslyvqasgrvtvstrrsqqtiipnigsrpwvrglssrisiywtivkpg
dvlvinsngnliaprgyfkmrtgkssimrsdapidtcisecitpngsipndkpfqnvnki
tygacpkyvkqntlklatgmrnvpekqt
>d1hghf_ 6.2.1.1.1 Influenza hemagglutinin (stalk) {(Influenza virus A)}
glfgaiagfiengwegmidgwygfrhqnsegtgqaadlkstqaaidqingklnrviektn
ekfhqiekefsevegriqdlekyvedtkidlwsynaellvalenqhtidltdsemnklfe
ktrrqlrenaeemgngcfkiyhkcdnaciesirngtydhdvyrdealnnrfqikg
>d1hgia_ 2.14.1.2.1 Hemagglutinin, headpiece {influenza virus (Strain x-31)}
qdlpgndnstatlclghhavpngtlvktitddqievtnatelvqssstgkicnnphrild
gidctlidallgdphcdvfqnetwdlfverskafsncypydvpdyaslrslvassgtlef
itegftwtgvtqnggsnackrgpgsgffsrlnwltksgstypvlnvtmpnndnfdklyiw
gihhpstnqeqtslyvqasgrvtvstrrsqqtiipnigsrpwvrglssrisiywtivkpg
dvlvinsngnliaprgyfkmrtgkssimrsdapidtcisecitpngsipndkpfqnvnki
tygacpkyvkqntlklatgmrnvpekqt
>d1hgib_ 6.2.1.1.1 Influenza hemagglutinin (stalk) {(Influenza virus A)}
glfgaiagfiengwegmidgwygfrhqnsegtgqaadlkstqaaidqingklnrviektn
ekfhqiekefsevegriqdlekyvedtkidlwsynaellvalenqhtidltdsemnklfe
ktrrqlrenaeemgngcfkiyhkcdnaciesirngtydhdvyrdealnnrfqikg
>d1hgic_ 2.14.1.2.1 Hemagglutinin, headpiece {influenza virus (Strain x-31)}
qdlpgndnstatlclghhavpngtlvktitddqievtnatelvqssstgkicnnphrild
gidctlidallgdphcdvfqnetwdlfverskafsncypydvpdyaslrslvassgtlef
itegftwtgvtqnggsnackrgpgsgffsrlnwltksgstypvlnvtmpnndnfdklyiw
gihhpstnqeqtslyvqasgrvtvstrrsqqtiipnigsrpwvrglssrisiywtivkpg
dvlvinsngnliaprgyfkmrtgkssimrsdapidtcisecitpngsipndkpfqnvnki
tygacpkyvkqntlklatgmrnvpekqt
>d1hgid_ 6.2.1.1.1 Influenza hemagglutinin (stalk) {(Influenza virus A)}
glfgaiagfiengwegmidgwygfrhqnsegtgqaadlkstqaaidqingklnrviektn
ekfhqiekefsevegriqdlekyvedtkidlwsynaellvalenqhtidltdsemnklfe
ktrrqlrenaeemgngcfkiyhkcdnaciesirngtydhdvyrdealnnrfqikg
>d1hgie_ 2.14.1.2.1 Hemagglutinin, headpiece {influenza virus (Strain x-31)}
qdlpgndnstatlclghhavpngtlvktitddqievtnatelvqssstgkicnnphrild
gidctlidallgdphcdvfqnetwdlfverskafsncypydvpdyaslrslvassgtlef
itegftwtgvtqnggsnackrgpgsgffsrlnwltksgstypvlnvtmpnndnfdklyiw
gihhpstnqeqtslyvqasgrvtvstrrsqqtiipnigsrpwvrglssrisiywtivkpg
dvlvinsngnliaprgyfkmrtgkssimrsdapidtcisecitpngsipndkpfqnvnki
tygacpkyvkqntlklatgmrnvpekqt
>d1hgif_ 6.2.1.1.1 Influenza hemagglutinin (stalk) {(Influenza virus A)}
glfgaiagfiengwegmidgwygfrhqnsegtgqaadlkstqaaidqingklnrviektn
ekfhqiekefsevegriqdlekyvedtkidlwsynaellvalenqhtidltdsemnklfe
ktrrqlrenaeemgngcfkiyhkcdnaciesirngtydhdvyrdealnnrfqikg
>d1hgja_ 2.14.1.2.1 Hemagglutinin, headpiece {influenza virus (Strain x-31)}
qdlpgndnstatlclghhavpngtlvktitddqievtnatelvqssstgkicnnphrild
gidctlidallgdphcdvfqnetwdlfverskafsncypydvpdyaslrslvassgtlef
itegftwtgvtqnggsnackrgpgsgffsrlnwltksgstypvlnvtmpnndnfdklyiw
gihhpstnqeqtslyvqasgrvtvstrrsqqtiipnigsrpwvrglssrisiywtivkpg
dvlvinsngnliaprgyfkmrtgkssimrsdapidtcisecitpngsipndkpfqnvnki
tygacpkyvkqntlklatgmrnvpekqt
>d1hgjb_ 6.2.1.1.1 Influenza hemagglutinin (stalk) {(Influenza virus A)}
glfgaiagfiengwegmidgwygfrhqnsegtgqaadlkstqaaidqingklnrviektn
ekfhqiekefsevegriqdlekyvedtkidlwsynaellvalenqhtidltdsemnklfe
ktrrqlrenaeemgngcfkiyhkcdnaciesirngtydhdvyrdealnnrfqikg
>d1hgjc_ 2.14.1.2.1 Hemagglutinin, headpiece {influenza virus (Strain x-31)}
qdlpgndnstatlclghhavpngtlvktitddqievtnatelvqssstgkicnnphrild
gidctlidallgdphcdvfqnetwdlfverskafsncypydvpdyaslrslvassgtlef
itegftwtgvtqnggsnackrgpgsgffsrlnwltksgstypvlnvtmpnndnfdklyiw
gihhpstnqeqtslyvqasgrvtvstrrsqqtiipnigsrpwvrglssrisiywtivkpg
dvlvinsngnliaprgyfkmrtgkssimrsdapidtcisecitpngsipndkpfqnvnki
tygacpkyvkqntlklatgmrnvpekqt
>d1hgjd_ 6.2.1.1.1 Influenza hemagglutinin (stalk) {(Influenza virus A)}
glfgaiagfiengwegmidgwygfrhqnsegtgqaadlkstqaaidqingklnrviektn
ekfhqiekefsevegriqdlekyvedtkidlwsynaellvalenqhtidltdsemnklfe
ktrrqlrenaeemgngcfkiyhkcdnaciesirngtydhdvyrdealnnrfqikg
>d1hgje_ 2.14.1.2.1 Hemagglutinin, headpiece {influenza virus (Strain x-31)}
qdlpgndnstatlclghhavpngtlvktitddqievtnatelvqssstgkicnnphrild
gidctlidallgdphcdvfqnetwdlfverskafsncypydvpdyaslrslvassgtlef
itegftwtgvtqnggsnackrgpgsgffsrlnwltksgstypvlnvtmpnndnfdklyiw
gihhpstnqeqtslyvqasgrvtvstrrsqqtiipnigsrpwvrglssrisiywtivkpg
dvlvinsngnliaprgyfkmrtgkssimrsdapidtcisecitpngsipndkpfqnvnki
tygacpkyvkqntlklatgmrnvpekqt
>d1hgjf_ 6.2.1.1.1 Influenza hemagglutinin (stalk) {(Influenza virus A)}
glfgaiagfiengwegmidgwygfrhqnsegtgqaadlkstqaaidqingklnrviektn
ekfhqiekefsevegriqdlekyvedtkidlwsynaellvalenqhtidltdsemnklfe
ktrrqlrenaeemgngcfkiyhkcdnaciesirngtydhdvyrdealnnrfqikg
>e1hgt.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>e1hgt.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>d1hgu__ 1.26.1.1.6 Growth hormone, somatotropin {human (Homo sapiens)}
ptiplsrlfqnamlrahrlhqlafdtyeefeeayipkeqkysflqapqaslcfsesiptp
snreqaqqksnlqllrisllliqswlepvgflrsvfanslvygasdsdvydllkdleegi
qtlmgrledgsprtgqafkqtyakfdanshnddallknygllycfrkdmdkvetflrivq
crsvegscg
>d1hgxa_ 3.49.1.1.2 Hypoxantine-guanine-xanthine PRTase {(Tritrichomonas foetus)}
mddlervlynqddiqkrirelaaeltefyedknpvmicvltgavffytdllkhldfqlep
dyiicssysgtkstgnltiskdlktniegrhvlvvediidtgltmyqllnnlqmrkpasl
kvctlcdkdigkkaydvpidycgfvvenryiigygfdfhnkyrnlpvigilke
>d1hgxb_ 3.49.1.1.2 Hypoxantine-guanine-xanthine PRTase {(Tritrichomonas foetus)}
mddlervlynqddiqkrirelaaeltefyedknpvmicvltgavffytdllkhldfqlep
dyiicssysgtkstgnltiskdlktniegrhvlvvediidtgltmyqllnnlqmrkpasl
kvctlcdkdigkkaydvpidycgfvvenryiigygfdfhnkyrnlpvigilkesvyt
>d1hhga1 2.1.1.2.4 (182-275) Class I MHC, beta2-microglobulin and alpha-3 domain {human (Homo sapiens) hla-a0201}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrdgedqtqdtelvetrpagdgtf
qkwaavvvpsgqeqrytchvqheglpkpltlrwe
>d1hhga2 4.15.1.1.8 (1-181) MHC class I, alpha-1 and alpha-2 domains {(human hla-a0201)}
gshsmryfftsvsrpgrgeprfiavgyvddtqfvrfdsdaasqrmeprapwieqegpeyw
dgetrkvkahsqthrvdlgtlrgyynqseagshtvqrmygcdvgsdwrflrgyhqyaydg
kdyialkedlrswtaadmaaqttkhkweaahvaeqlraylegtcvewlrrylengketlq
r
>d1hhgd1 2.1.1.2.4 (182-275) Class I MHC, beta2-microglobulin and alpha-3 domain {human (Homo sapiens) hla-a0201}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrdgedqtqdtelvetrpagdgtf
qkwaavvvpsgqeqrytchvqheglpkpltlrwe
>d1hhgd2 4.15.1.1.8 (1-181) MHC class I, alpha-1 and alpha-2 domains {(human hla-a0201)}
gshsmryfftsvsrpgrgeprfiavgyvddtqfvrfdsdaasqrmeprapwieqegpeyw
dgetrkvkahsqthrvdlgtlrgyynqseagshtvqrmygcdvgsdwrflrgyhqyaydg
kdyialkedlrswtaadmaaqttkhkweaahvaeqlraylegtcvewlrrylengketlq
r
>d1hhha1 2.1.1.2.4 (182-275) Class I MHC, beta2-microglobulin and alpha-3 domain {human (Homo sapiens) hla-a0201}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrdgedqtqdtelvetrpagdgtf
qkwaavvvpsgqeqrytchvqheglpkpltlrwe
>d1hhha2 4.15.1.1.8 (1-181) MHC class I, alpha-1 and alpha-2 domains {(human hla-a0201)}
gshsmryfftsvsrpgrgeprfiavgyvddtqfvrfdsdaasqrmeprapwieqegpeyw
dgetrkvkahsqthrvdlgtlrgyynqseagshtvqrmygcdvgsdwrflrgyhqyaydg
kdyialkedlrswtaadmaaqttkhkweaahvaeqlraylegtcvewlrrylengketlq
r
>d1hhia1 2.1.1.2.4 (182-275) Class I MHC, beta2-microglobulin and alpha-3 domain {human (Homo sapiens) hla-a0201}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrdgedqtqdtelvetrpagdgtf
qkwaavvvpsgqeqrytchvqheglpkpltlrwe
>d1hhia2 4.15.1.1.8 (1-181) MHC class I, alpha-1 and alpha-2 domains {(human hla-a0201)}
gshsmryfftsvsrpgrgeprfiavgyvddtqfvrfdsdaasqrmeprapwieqegpeyw
dgetrkvkahsqthrvdlgtlrgyynqseagshtvqrmygcdvgsdwrflrgyhqyaydg
kdyialkedlrswtaadmaaqttkhkweaahvaeqlraylegtcvewlrrylengketlq
r
>d1hhid1 2.1.1.2.4 (182-275) Class I MHC, beta2-microglobulin and alpha-3 domain {human (Homo sapiens) hla-a0201}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrdgedqtqdtelvetrpagdgtf
qkwaavvvpsgqeqrytchvqheglpkpltlrwe
>d1hhid2 4.15.1.1.8 (1-181) MHC class I, alpha-1 and alpha-2 domains {(human hla-a0201)}
gshsmryfftsvsrpgrgeprfiavgyvddtqfvrfdsdaasqrmeprapwieqegpeyw
dgetrkvkahsqthrvdlgtlrgyynqseagshtvqrmygcdvgsdwrflrgyhqyaydg
kdyialkedlrswtaadmaaqttkhkweaahvaeqlraylegtcvewlrrylengketlq
r
>d1hhja1 2.1.1.2.4 (182-275) Class I MHC, beta2-microglobulin and alpha-3 domain {human (Homo sapiens) hla-a0201}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrdgedqtqdtelvetrpagdgtf
qkwaavvvpsgqeqrytchvqheglpkpltlrwe
>d1hhja2 4.15.1.1.8 (1-181) MHC class I, alpha-1 and alpha-2 domains {(human hla-a0201)}
gshsmryfftsvsrpgrgeprfiavgyvddtqfvrfdsdaasqrmeprapwieqegpeyw
dgetrkvkahsqthrvdlgtlrgyynqseagshtvqrmygcdvgsdwrflrgyhqyaydg
kdyialkedlrswtaadmaaqttkhkweaahvaeqlraylegtcvewlrrylengketlq
r
>d1hhjd1 2.1.1.2.4 (182-275) Class I MHC, beta2-microglobulin and alpha-3 domain {human (Homo sapiens) hla-a0201}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrdgedqtqdtelvetrpagdgtf
qkwaavvvpsgqeqrytchvqheglpkpltlrwe
>d1hhjd2 4.15.1.1.8 (1-181) MHC class I, alpha-1 and alpha-2 domains {(human hla-a0201)}
gshsmryfftsvsrpgrgeprfiavgyvddtqfvrfdsdaasqrmeprapwieqegpeyw
dgetrkvkahsqthrvdlgtlrgyynqseagshtvqrmygcdvgsdwrflrgyhqyaydg
kdyialkedlrswtaadmaaqttkhkweaahvaeqlraylegtcvewlrrylengketlq
r
>d1hhka1 2.1.1.2.4 (182-275) Class I MHC, beta2-microglobulin and alpha-3 domain {human (Homo sapiens) hla-a0201}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrdgedqtqdtelvetrpagdgtf
qkwaavvvpsgqeqrytchvqhegl
>d1hhka2 4.15.1.1.8 (1-181) MHC class I, alpha-1 and alpha-2 domains {(human hla-a0201)}
gshsmryfftsvsrpgrgeprfiavgyvddtqfvrfdsdaasqrmeprapwieqegpeyw
dgetrkvkahsqthrvdlgtlrgyynqseagshtvqrmygcdvgsdwrflrgyhqyaydg
kdyialkedlrswtaadmaaqttkhkweaahvaeqlraylegtcvewlrrylengketlq
r
>d1hhkd1 2.1.1.2.4 (182-275) Class I MHC, beta2-microglobulin and alpha-3 domain {human (Homo sapiens) hla-a0201}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrdgedqtqdtelvetrpagdgtf
qkwaavvvpsgqeqrytchvqheglpkpltlrwe
>d1hhkd2 4.15.1.1.8 (1-181) MHC class I, alpha-1 and alpha-2 domains {(human hla-a0201)}
gshsmryfftsvsrpgrgeprfiavgyvddtqfvrfdsdaasqrmeprapwieqegpeyw
dgetrkvkahsqthrvdlgtlrgyynqseagshtvqrmygcdvgsdwrflrgyhqyaydg
kdyialkedlrswtaadmaaqttkhkweaahvaeqlraylegtcvewlrrylengketlq
r
>d1hhl__ 4.2.1.2.3 Lysozyme {guinea fowl (Numida meleagris)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfnsqatnrntdgstdygvlqins
rwwcndgrtpgsrnlcnipcsalqssditatancakkivsdgdgmnawvawrkhckgtdv
rvwikgcrl
>d1hhoa_ 1.1.1.1.16 Hemoglobin, alpha-chain {human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1hhob_ 1.1.1.1.25 Hemoglobin, beta-chain {human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1hhp__ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>e1hia.1a 2.35.1.2.20 Kallikrein A {porcine (Sus scrofa)}
iiggreceknshpwqvaiyhyssfqcggvlvnpkwvltaahckndnyevwlgrhnlfene
ntaqffgvtadfphpgfnls
>e1hia.1b 2.35.1.2.20 Kallikrein A {porcine (Sus scrofa)}
gkdyshdlmllrlqspakitdavkvlelptqepelgstceasgwgsiepgpddfefpdei
qcvqltllqntfcadahpdkvtesmlcagylpggkdtcmgdsggplicngmwqgitswgh
tpcgsankpsiytklifyldwiddtitenp
>e1hia.2x 2.35.1.2.20 Kallikrein A {porcine (Sus scrofa)}
iiggreceknshpwqvaiyhyssfqcggvlvnpkwvltaahckndnyevwlgrhnlfene
ntaqffgvtadfphpgfnls
>e1hia.2y 2.35.1.2.20 Kallikrein A {porcine (Sus scrofa)}
gkdyshdlmllrlqspakitdavkvlelptqepelgstceasgwgsiepgpddfefpdei
qcvqltllqntfcadahpdkvtesmlcagylpggkdtcmgdsggplicngmwqgitswgh
tpcgsankpsiytklifyldwiddtitenp
>e1hia.3i 7.3.13.1.1 Hirustasin {Medicinal leech (Hirudo medicinalis)}
tcggetcsaaqvclkgkcvcnevhcrirckyglkkdengceypcscak
>e1hia.3j 7.3.13.1.1 Hirustasin {Medicinal leech (Hirudo medicinalis)}
tcggetcsaaqvclkgkcvcnevhcrirckyglkkdengceypcscak
>d1hib__ 2.31.1.2.1 Interleukin-1beta {human (Homo sapiens)}
vrslncglrdsqqkslvmsgpyelkalhlqgqdmeqqvvfsmsfvqgeesndkipvalgl
keknlylscvlkddkptlqlesvdpknypkkkmekrfvfnkieinnklefesaqfpnwyi
stsqaenmpvflggtkggqditdftmqfvss
>d1hic__ 7.3.13.2.1 Hirudin {leech (Hirudo medicinalis)}
vvytdctesgqnlclcegsnvcgqgnkcilgsdgeknqcvtgegtpkpqsh
>d1higa_ 1.26.1.3.8 Interferon-gamma {human (Homo sapiens)}
qdpyvkeaenlkkyfnaghsdvadngtlflgilknwkeesdrkimqsqivsfyfklfknf
kddqsiqksvetikedmnvkffnsnkkkrddfekltnysvtdlnvqrkaiheliqvmael
spa
>d1higb_ 1.26.1.3.8 Interferon-gamma {human (Homo sapiens)}
qdpyvkeaenlkkyfnaghsdvadngtlflgilknwkeesdrkimqsqivsfyfklfknf
kddqsiqksvetikedmnvkffnsnkkkrddfekltnysvtdlnvqrkaiheliqvmael
spa
>d1higc_ 1.26.1.3.8 Interferon-gamma {human (Homo sapiens)}
qdpyvkeaenlkkyfnaghsdvadngtlflgilknwkeesdrkimqsqivsfyfklfknf
kddqsiqksvetikedmnvkffnsnkkkrddfekltnysvtdlnvqrkaiheliqvmael
spa
>d1higd_ 1.26.1.3.8 Interferon-gamma {human (Homo sapiens)}
qdpyvkeaenlkkyfnaghsdvadngtlflgilknwkeesdrkimqsqivsfyfklfknf
kddqsiqksvetikedmnvkffnsnkkkrddfekltnysvtdlnvqrkaiheliqvmael
spa
>d1hiha_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hihb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hiia_ 2.38.1.1.3 Human immunodeficiency virus type 2 protease {HIV-2 (rod isolate)}
pqfslwkrpvvtayiegqpvevlldtgaddsivagielgnnyspkivggiggfintkeyk
nveievlnkkvratimtgdtpinifgrniltalgmslnl
>d1hiib_ 2.38.1.1.3 Human immunodeficiency virus type 2 protease {HIV-2 (rod isolate)}
pqfslwkrpvvtayiegqpvevlldtgaddsivagielgnnyspkivggiggfintkeyk
nveievlnkkvratimtgdtpinifgrniltalgmslnl
>d1hij__ 1.26.1.2.2 Interleukin-4 (IL-4) {human (Homo sapiens)}
hkcditlqeiiktlnslteqktlcteltvtdifaaskntteketfcraatvlrqfyshhe
kdtrclgataqqfhrhkqlirflkrldqnlwglaglnscpvkeanqstlenflerlktim
rekyskcss
>d1hik__ 1.26.1.2.2 Interleukin-4 (IL-4) {human (Homo sapiens)}
hkcditlqeiiktlnslteqktlcteltvtdifaaskntteketfcraatvlrqfyshhe
kdtrclgataqqfhrhkqlirflkrldrnlwglaglnscpvkeanqstlenflerlktim
rekyskcss
>d1hila1 2.1.1.1.14 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab 17/9 (mouse), kappa L chain}
divmtqspssltvtagekvtmsctssqslfnsgkqknyltwyqqkpgqppkvliywastr
esgvpdrftgsgsgtdftltissvqaedlavyycqndysnpltfgggtklelkr
>d1hila2 2.1.1.2.23 (109-211) Immunoglobulin (constant domains of L and H chains) {Fab 17/9 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1hilb1 2.1.1.1.14 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab 17/9 (mouse), kappa L chain}
evqlvesggdlvkpggslklscaasgfsfssygmswvrqtpdkrlewvatisngggytyy
pdsvkgrftisrdnakntlylqmsslksedsamyycarrerydengfaywgqgtlvtvs
>d1hilb2 2.1.1.2.23 (113-228) Immunoglobulin (constant domains of L and H chains) {Fab 17/9 (mouse), kappa L chain}
aakttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqs
dlytlsssvtvtsstwpsqsitcnvahpasstkvdkkiepr
>d1hilc1 2.1.1.1.14 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab 17/9 (mouse), kappa L chain}
divmtqspssltvtagekvtmsctssqslfnsgkqknyltwyqqkpgqppkvliywastr
esgvpdrftgsgsgtdftltissvqaedlavyycqndysnpltfgggtklelkr
>d1hilc2 2.1.1.2.23 (109-211) Immunoglobulin (constant domains of L and H chains) {Fab 17/9 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1hild1 2.1.1.1.14 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab 17/9 (mouse), kappa L chain}
evqlvesggdlvkpggslklscaasgfsfssygmswvrqtpdkrlewvatisngggytyy
pdsvkgrftisrdnakntlylqmsslksedsamyycarrerydengfaywgqgtlvtvs
>d1hild2 2.1.1.2.23 (113-227) Immunoglobulin (constant domains of L and H chains) {Fab 17/9 (mouse), kappa L chain}
aakttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqs
dlytlsssvtvtsstwpsqsitcnvahpasstkvdkkiep
>d1himh1 2.1.1.1.14 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab 17/9 (mouse), kappa L chain}
divmtqspssltvtagekvtmsctssqslfnsgkqknyltwyqqkpgqppkvliywastr
esgvpdrftgsgsgtdftltissvqaedlavyycqndysnpltfgggtklelkradaa
>d1himh2 2.1.1.2.23 (113-211) Immunoglobulin (constant domains of L and H chains) {Fab 17/9 (mouse), kappa L chain}
ptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqdskdst
ysmsstltltkdeyerhnsytceathktstspivksfnr
>d1himj1 2.1.1.1.14 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab 17/9 (mouse), kappa L chain}
divmtqspssltvtagekvtmsctssqslfnsgkqknyltwyqqkpgqppkvliywastr
esgvpdrftgsgsgtdftltissvqaedlavyycqndysnpltfgggtklelkradaa
>d1himj2 2.1.1.2.23 (113-211) Immunoglobulin (constant domains of L and H chains) {Fab 17/9 (mouse), kappa L chain}
ptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqdskdst
ysmsstltltkdeyerhnsytceathktstspivksfnr
>d1himl1 2.1.1.1.14 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab 17/9 (mouse), kappa L chain}
evqlvesggdlvkpggslklscaasgfsfssygmswvrqtpdkrlewvatisngggytyy
pdsvkgrftisrdnakntlylqmsslksedsamyycarrerydengfaywgqgtl
>d1himl2 2.1.1.2.23 (109-227) Immunoglobulin (constant domains of L and H chains) {Fab 17/9 (mouse), kappa L chain}
vtvsaakttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpa
vlqsdlytlsssvtvtsstwpsqsitcnvahpasstkvdkkiep
>d1himm1 2.1.1.1.14 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab 17/9 (mouse), kappa L chain}
evqlvesggdlvkpggslklscaasgfsfssygmswvrqtpdkrlewvatisngggytyy
pdsvkgrftisrdnakntlylqmsslksedsamyycarrerydengfaywgqgtl
>d1himm2 2.1.1.2.23 (109-227) Immunoglobulin (constant domains of L and H chains) {Fab 17/9 (mouse), kappa L chain}
vtvsaakttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpa
vlqsdlytlsssvtvtsstwpsqsitcnvahpasstkvdkkiep
>d1hinh1 2.1.1.1.14 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab 17/9 (mouse), kappa L chain}
evqlvesggdlvkpggslklscaasgfsfssygmswvrqtpdkrlewvatisngggytyy
pdsvkgrftisrdnakntlylqmsslksedsamyycarrerydengfaywgqgtlvtvs
>d1hinh2 2.1.1.2.23 (113-228) Immunoglobulin (constant domains of L and H chains) {Fab 17/9 (mouse), kappa L chain}
aakttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqs
dlytlsssvtvtsstwpsqsitcnvahpasstkvdkkiepr
>d1hinl1 2.1.1.1.14 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab 17/9 (mouse), kappa L chain}
divmtqspssltvtagekvtmsctssqslfnsgkqknyltwyqqkpgqppkvliywastr
esgvpdrftgsgsgtdftltissvqaedlavyycqndysnpltfgggtklelkr
>d1hinl2 2.1.1.2.23 (109-211) Immunoglobulin (constant domains of L and H chains) {Fab 17/9 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1hip__ 7.30.1.1.2 HIPIP (high potential iron protein) {(Cromatium vinosum )}
sapanavaadnataialkynqdatkservaaarpglppeeqhcadcqfmqadaagatdew
kgcqlfpgklinvngwcaswtlkag
>e1hiq.1a 7.1.1.1.2 Insulin {human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1hiq.1b 7.1.1.1.2 Insulin {human (Homo sapiens)}
fvnqhlcgshlvealylvcgergsfytpkt
>e1his.1a 7.1.1.1.2 Insulin {human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1his.1b 7.1.1.1.2 Insulin {human (Homo sapiens)}
fvnqhlcgshlvealylvcgergff
>e1hit.1a 7.1.1.1.2 Insulin {human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1hit.1b 7.1.1.1.2 Insulin {human (Homo sapiens)}
fvnqhlcgshlvealylvcgerggfytpkt
>d1hiva_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hivb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hiwa_ 1.62.1.1.1 HIV-1 matrix protein (HIV-1 MA, HIVp17, p17, MA) {Human immunodeficiency virus type 1 (HIV-1)}
vlsggeldkwekirlrpggkkqyklkhivwasrelerfavnpglletsegcrqilgqlqp
slqtgseelrslyntiavlycvhqridvkdtkealdkieeeqnkskkkaqqaaad
>d1hiwb_ 1.62.1.1.1 HIV-1 matrix protein (HIV-1 MA, HIVp17, p17, MA) {Human immunodeficiency virus type 1 (HIV-1)}
vlsggeldkwekirlrpggkkqyklkhivwasrelerfavnpglletsegcrqilgqlqp
slqtgseelrslyntiavlycvhqridvkdtkealdkieeeqnkskkkaq
>d1hiwc_ 1.62.1.1.1 HIV-1 matrix protein (HIV-1 MA, HIVp17, p17, MA) {Human immunodeficiency virus type 1 (HIV-1)}
vlsggeldkwekirlrpggkkqyklkhivwasrelerfavnpglletsegcrqilgqlqp
slqtgseelrslyntiavlycvhqridvkdtkealdkieeeqnkskkkaqqaa
>d1hiwq_ 1.62.1.1.1 HIV-1 matrix protein (HIV-1 MA, HIVp17, p17, MA) {Human immunodeficiency virus type 1 (HIV-1)}
vlsggeldkwekirlrpggkkqyklkhivwasrelerfavnpglletsegcrqilgqlqp
slqtgseelrslyntiavlycvhqridvkdtkealdkieeeqnks
>d1hiwr_ 1.62.1.1.1 HIV-1 matrix protein (HIV-1 MA, HIVp17, p17, MA) {Human immunodeficiency virus type 1 (HIV-1)}
vlsggeldkwekirlrpggkkqyklkhivwasrelerfavnpglletsegcrqilgqlqp
slqtgseelrslyntiavlycvhqridvkdtkealdkieeeqnkskkkaqqa
>d1hiws_ 1.62.1.1.1 HIV-1 matrix protein (HIV-1 MA, HIVp17, p17, MA) {Human immunodeficiency virus type 1 (HIV-1)}
vlsggeldkwekirlrpggkkqyklkhivwasrelerfavnpglletsegcrqilgqlqp
slqtgseelrslyntiavlycvhqridvkdtkealdkieeeqn
>e1hja.1b 2.35.1.2.7 (alpha, gamma-)chymotrypsin(ogen) {bovine (Bos taurus)}
ivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgvttsdvvvagefdqgs
ssekiqklkiakvfknskynsltinnditllklstaasfsqtvsavclpsasddfaagtt
cvttgwgltry
>e1hja.1c 2.35.1.2.7 (alpha, gamma-)chymotrypsin(ogen) {bovine (Bos taurus)}
antpdrlqqaslpllsntnckkywgtkikdamicagasgvsscmgdsggplvckkngawt
lvgivswgsstcststpgvyarvtalvnwvqqtlaan
>d1hjai_ 7.14.1.1.1 Ovomucoid III domain {turkey (Meleagris gallopavo)}
vdcseypkpactkeyrplcgsdnktygnkcnfcnavvesngtltlshfgkc
>d1hjka_ 3.64.1.1.1 Alkaline phosphatase {(Escherichia coli)}
tpempvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdxaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdqaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1hjkb_ 3.64.1.1.1 Alkaline phosphatase {(Escherichia coli)}
tpempvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdxaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdqaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1hjp_1 1.5.1.1.1 (158-203) DNA helicase RuvA subunit, C-terminal domain {(Escherichia coli)}
daeqeavaalvalgykpqeasrmvskiarpdassetlirealraal
>d1hjp_2 1.64.1.1.1 (65-140) DNA helicase RuvA subunit, the middle domain {(Escherichia coli)}
nkqertlfkeliktngvgpklalailsgmsaqqfvnavereevgalvklpgigkktaerl
ivemkdrfkglhgdlf
>d1hjp_3 2.29.4.2.1 (1-64) DNA helicase RuvA subunit, N-terminal domain {(Escherichia coli)}
migrlrgiiiekqpplvlievggvgyevhmpmtcfyelpeagqeaivfthfvvredaqll
ygfn
>d1hjra_ 3.47.3.6.1 RuvC resolvase {(Escherichia coli)}
aiilgidpgsrvtgygvirqvgrqlsylgsgcirtkvddlpsrlkliyagvteiitqfqp
dyfaieqvfmaknadsalklgqargvaivaavnqelpvfeyaarqvkqtvvgigsaeksq
vqhmvrtllklpanpqadaadalaiaithchvsqnamq
>d1hjrb_ 3.47.3.6.1 RuvC resolvase {(Escherichia coli)}
aiilgidpgsrvtgygvirqvgrqlsylgsgcirtkvddlpsrlkliyagvteiitqfqp
dyfaieqvfmaknadsalklgqargvaivaavnqelpvfeyaarqvkqtvvgigsaeksq
vqhmvrtllklpanpqadaadalaiaithchvsqnamq
>d1hjrc_ 3.47.3.6.1 RuvC resolvase {(Escherichia coli)}
aiilgidpgsrvtgygvirqvgrqlsylgsgcirtkvddlpsrlkliyagvteiitqfqp
dyfaieqvfmaknadsalklgqargvaivaavnqelpvfeyaarqvkqtvvgigsaeksq
vqhmvrtllklpanpqadaadalaiaithchvsqnamq
>d1hjrd_ 3.47.3.6.1 RuvC resolvase {(Escherichia coli)}
aiilgidpgsrvtgygvirqvgrqlsylgsgcirtkvddlpsrlkliyagvteiitqfqp
dyfaieqvfmaknadsalklgqargvaivaavnqelpvfeyaarqvkqtvvgigsaeksq
vqhmvrtllklpanpqadaadalaiaithchvsqnamq
>d1hjt__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgyqg
>d1hkba1 3.47.1.2.3 (16-222) Mammalian type I hexokinase {Human (Homo sapiens)}
ddqvkkidkylyamrlsdetlidimtrfrkemknglsrdfnptatvkmlptfvrsipdgs
ekgdfialdlggssfrilrvqvnheknqnvhmesevydtpenivhgsgsqlfdhvaeclg
dfmekrkikdkklpvgftfsfpcqqskideailitwtkrfkasgvegadvvkllnkaikk
rgdydanivavvndtvgtmmtcgyddq
>d1hkba2 3.47.1.2.3 (223-465) Mammalian type I hexokinase {Human (Homo sapiens)}
hcevgliigtgtnacymeelrhidlvegdegrmcintewgafgddgsledirtefdreid
rgslnpgkqlfekmvsgmylgelvrlilvkmakegllfegritpelltrgkfntsdvsai
eknkeglhnakeiltrlgvepsdddcvsvqhvctivsfrsanlvaatlgailnrlrdnkg
tprlrttvgvdgslykthpqysrrfhktlrrlvpdsdvrfllsesgsgkgaamvtavayr
lae
>d1hkba3 3.47.1.2.3 (466-670) Mammalian type I hexokinase {Human (Homo sapiens)}
qhrqieetlahfhltkdmllevkkrmraemelglrkqthnnavvkmlpsfvrrtpdgten
gdflaldlggtnfrvllvkirsgkkrtvemhnkiyaipieimqgtgeelfdhivscisdf
ldymgikgprmplgftfsfpcqqtsldagilitwtkgfkatdcvghdvvtllrdaikrre
efdldvvavvndtvgtmmtcayeep
>d1hkba4 3.47.1.2.3 (671-914) Mammalian type I hexokinase {Human (Homo sapiens)}
tcevglivgtgsnacymeemknvemvegdqgqmcinmewgafgdngclddirthydrlvd
eyslnagkqryekmisgmylgeivrnilidftkkgflfrgqisetlktrgifetkflsqi
esdrlallqvrailqqlglnstcddsilvktvcgvvsrraaqlcgagmaavvdkirenrg
ldrlnvtvgvdgtlyklhphfsrimhqtvkelspkcnvsfllsedgsgkgaalitavgvr
lrte
>d1hkbb1 3.47.1.2.3 (16-222) Mammalian type I hexokinase {Human (Homo sapiens)}
ddqvkkidkylyamrlsdetlidimtrfrkemknglsrdfnptatvkmlptfvrsipdgs
ekgdfialdlggssfrilrvqvnheknqnvhmesevydtpenivhgsgsqlfdhvaeclg
dfmekrkikdkklpvgftfsfpcqqskideailitwtkrfkasgvegadvvkllnkaikk
rgdydanivavvndtvgtmmtcgyddq
>d1hkbb2 3.47.1.2.3 (223-465) Mammalian type I hexokinase {Human (Homo sapiens)}
hcevgliigtgtnacymeelrhidlvegdegrmcintewgafgddgsledirtefdreid
rgslnpgkqlfekmvsgmylgelvrlilvkmakegllfegritpelltrgkfntsdvsai
eknkeglhnakeiltrlgvepsdddcvsvqhvctivsfrsanlvaatlgailnrlrdnkg
tprlrttvgvdgslykthpqysrrfhktlrrlvpdsdvrfllsesgsgkgaamvtavayr
lae
>d1hkbb3 3.47.1.2.3 (466-670) Mammalian type I hexokinase {Human (Homo sapiens)}
qhrqieetlahfhltkdmllevkkrmraemelglrkqthnnavvkmlpsfvrrtpdgten
gdflaldlggtnfrvllvkirsgkkrtvemhnkiyaipieimqgtgeelfdhivscisdf
ldymgikgprmplgftfsfpcqqtsldagilitwtkgfkatdcvghdvvtllrdaikrre
efdldvvavvndtvgtmmtcayeep
>d1hkbb4 3.47.1.2.3 (671-914) Mammalian type I hexokinase {Human (Homo sapiens)}
tcevglivgtgsnacymeemknvemvegdqgqmcinmewgafgdngclddirthydrlvd
eyslnagkqryekmisgmylgeivrnilidftkkgflfrgqisetlktrgifetkflsqi
esdrlallqvrailqqlglnstcddsilvktvcgvvsrraaqlcgagmaavvdkirenrg
ldrlnvtvgvdgtlyklhphfsrimhqtvkelspkcnvsfllsedgsgkgaalitavgvr
lrte
>d1hkg_1 3.47.1.2.2 (2-202) Hexokinase A {yeast (Saccharomyces cerevisiae)}
aasxdxslvevhxxvfivppxilqavvsiattrxddxdsaaasipmvpgwvlkqvxgsqa
gsflaivmgggdlevilixlagyqessixasrslaasmxttaipsdlwgnxaxsnaafss
xefssxagsvplgftfxeagakexvikgqitxqaxafslaxlxklisamxnaxfpagdxx
xxvadixdshgilxxvnytda
>d1hklh1 2.1.1.1.64 (1-114) Immunoglobulin (variable domains of L and H chains) {Fab 48G7 (mouse/human), kappa L chain}
qvqlqqsgaelvkpgasvklsctasgfnikdtymhwvkqrpkqglewigridpanvdtky
dpkfqdkatitadtsskttylqlssltsedtavyycasyygiywgqgttltvssa
>d1hklh2 2.1.1.2.68 (115-216) Immunoglobulin (constant domains of L and H chains) {Fab 48G7 (mouse/human), kappa L chain}
stkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqssg
lyslssvvtvpssslgtqtyicnvnhkpsntkvdkkvepksc
>d1hkll1 2.1.1.1.64 (1-109) Immunoglobulin (variable domains of L and H chains) {Fab 48G7 (mouse/human), kappa L chain}
diqmtqspsslsaslgervsltcrasqeingylgwlqqkpdgtikrliyaastlhsgvpk
rfsgsrsgsdysltisslesedfadyyclqyasyprtfgggtkveikrt
>d1hkll2 2.1.1.2.68 (110-214) Immunoglobulin (constant domains of L and H chains) {Fab 48G7 (mouse/human), kappa L chain}
vaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqdsk
dstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1hks__ 1.4.3.13.1 Heat-shock transcription factor {(Drosophila melanogaster)}
gsgvpaflaklwrlvddadtnrlicwtkdgqsfviqnqaqfakellplnykhnnmasfir
qlnmygfhkitsidngglrfdrdeiefshpffkrnspflldqikrk
>d1hkt__ 1.4.3.13.1 Heat-shock transcription factor {(Drosophila melanogaster)}
gsgvpaflaklwrlvddadtnrlicwtkdgqsfviqnqaqfakellplnykhnnmasfir
qlnmygfhkitsidngglrfdrdeiefshpffkrnspflldqikrk
>d1hlaa1 2.1.1.2.3 (182-270) Class I MHC, beta2-microglobulin and alpha-3 domain {human (Homo sapiens) HLA-A2}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrdgedqtqdtelvetrpagdgtf
qkwaavvvpsgqeqrytchvqheglpkpl
>d1hlaa2 4.15.1.1.7 (1-181) MHC class I, alpha-1 and alpha-2 domains {(human hla-a2)}
gshsmryfftsvsrpgrgeprfiavgyvddtqfvrfdsdaasqrmeprapwieqegpeyw
dgetrkvkahsqthrvdlgtlrgyynqseagshtvqrmygcdvgsdwrflrgyhqyaydg
kdyialkedlrswtaadmaaqttkhkweaahvaeqlraylegtcvewlrrylengketlq
r
>d1hlb__ 1.1.1.1.39 Hemoglobin {sea cucumber (Caudina (Molpadia) arenicola)}
xggtlaiqaqgdltlaqkkivrktwhqlmrnktsfvtdvfirifaydpsaqnkfpqmagm
sasqlrssrqmqahairvssimseyveeldsdilpellatlarthdlnkvgadhynlfak
vlmealqaelgsdfnektrdawakafsvvqavllvkhg
>d1hlca_ 2.21.1.3.2 S-lectin (galectin-1) {human (Homo sapiens)}
elevknmdmkpgstlkitgsiadgtdgfvinlgqgtdklnlhfnprfsestivcnsldgs
nwgqeqredhlcfspgsevkftvtfesdkfkvklpdgheltfpnrlghshlsylsvrggf
nmssfklke
>d1hlcb_ 2.21.1.3.2 S-lectin (galectin-1) {human (Homo sapiens)}
elevknmdmkpgstlkitgsiadgtdgfvinlgqgtdklnlhfnprfsestivcnsldgs
nwgqeqredhlcfspgsevkftvtfesdkfkvklpdgheltfpnrlghshlsylsvrggf
nmssfklke
>d1hlda1 2.25.1.2.1 (1-174,325-374) Alcohol dehydrogenase {horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1hlda2 3.22.1.1.1 (175-324) Alcohol dehydrogenase {horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1hldb1 2.25.1.2.1 (1-174,325-374) Alcohol dehydrogenase {horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1hldb2 3.22.1.1.1 (175-324) Alcohol dehydrogenase {horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>e1hle.1a 5.2.1.1.1 Elastase inhibitor {horse (Equus caballus)}
xmeqlstanthfavdlfralnesdptgnifisplsissalamiflgtrgntaaqvskaly
fdtvedihsrfqslnadinkpgapyilklanrlygektynfladflastqkmygaelasv
dfqqapedarkeinewvkgqtegkipellvkgmvdnmtklvlvnaiyfkgnwqqkfmkea
trdapfrlnkkdtktvkmmyqkkkfpynyiedlkcrvlelpyqgkelsmiillpddiede
stglekiekqltldklrewtkpenlylaevnvhlprfkleesydltshlarlgvqdlfnr
gkadlsgmsgardlfvskiihksfvdlneegteaaaatagtilla
>e1hle.1b 5.2.1.1.1 Elastase inhibitor {horse (Equus caballus)}
eenfnadhpfiffirhnpsanilflgrfssp
>d1hlm__ 1.1.1.1.39 Hemoglobin {sea cucumber (Caudina (Molpadia) arenicola)}
xgatqsfqsvgdltpaekdlirstwdqlmthrtgfvadvfirifhndptaqrkfpqmagl
spaelrtsrqmhahairvsalmttyidemdtevlpellatltrthdknhvgkknydlfgk
vlmeaikaelgvgftkqvhdawaktfaivqgvlitkhas
>d1hloa_ 1.36.1.1.1 Max protein {Human (Homo sapiens)}
nddievesdadkrahhnalerkrrdhikdsfhslrdsvpslqgekasraqildkateyiq
ymrrknhthqqdiddlkrqn
>d1hlob_ 1.36.1.1.1 Max protein {Human (Homo sapiens)}
sdadkrahhnalerkrrdhikdsfhslrdsvpslqgekasraqildkateyiqymrrknh
thqqdiddlkrqn
>d1hlpa1 3.22.1.5.4 (21-146) Malate dehydrogenase {(Haloarcula marismortui)}
tkvsvvgaagtvgaaagynialrdiadevvfvdipdkeddtvgqaadtnhgiaydsntrv
rqggyedtagsdvvvitagiprqpgqtridlagdnapimediqssldehnddyislttsn
pvdllnrh
>d1hlpa2 4.100.1.1.4 (147-328) Malate dehydrogenase {(Haloarcula marismortui)}
lyeagdrsreqvigfggrldsarfryvlseefdapvqnvegtilgehgdaqvpvfskvrv
dgtdpefsgdekeqllgdlqesamdvierkgatewgpargvahmveailhdtgevlpasv
klegefghedtafgvpvrlgsngveeivewdlddyeqdlmadaaeklsdqydkis
>d1hlpb1 3.22.1.5.4 (21-146) Malate dehydrogenase {(Haloarcula marismortui)}
tkvsvvgaagtvgaaagynialrdiadevvfvdipdkeddtvgqaadtnhgiaydsntrv
rqggyedtagsdvvvitagiprqpgqtridlagdnapimediqssldehnddyislttsn
pvdllnrh
>d1hlpb2 4.100.1.1.4 (147-328) Malate dehydrogenase {(Haloarcula marismortui)}
lyeagdrsreqvigfggrldsarfryvlseefdapvqnvegtilgehgdaqvpvfskvrv
dgtdpefsgdekeqllgdlqesamdvierkgatewgpargvahmveailhdtgevlpasv
klegefghedtafgvpvrlgsngveeivewdlddyeqdlmadaaeklsdqydkis
>e1hls.1a 7.1.1.1.2 Insulin {human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1hls.1b 7.1.1.1.2 Insulin {human (Homo sapiens)}
fvnqhlcgshlvealhlvcgergffytpkt
>e1hlt.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidq
>e1hlt.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1hlt.2j 2.35.1.2.10 Thrombin {human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1hlt.2k 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidq
>d1hlua1 3.47.1.1.3 (2-146) Actin {bovine (Bos taurus) pancreas}
dddiaalvvdngsgmckagfagddapravfpsivgrprhqgvmvgmgqkdsyvgdeaqsk
rgiltlkypiexgivtnwddmekiwhhtfynelrvapeehpvllteaplnpkanrekmtq
imfetfntpamyvaiqavlslyasg
>d1hlua2 3.47.1.1.3 (147-375) Actin {bovine (Bos taurus) pancreas}
rttgivmdsgdgvthtvpiyegyalphailrldlagrdltdylmkiltergysftttaer
eivrdikeklcyvaldfeqemataassssleksyelpdgqvitignerfrcpealfqpsf
lgmescgihettfnsimkcdvdirkdlyantvlsggttmypgiadrmqkeitalapstmk
ikiiapperkysvwiggsilaslstfqqmwiskqeydesgpsivhrkcf
>d1hlup_ 4.63.1.1.1 Profilin (actin-binding protein) {bovine (Bos taurus)}
agwnayidnlmadgtcqdaaivgykdspsvwaavpgktfvnitpaevgilvgkdrssffv
ngltlggqkcsvirdsllqdgeftmdlrtkstggaptfnitvtmtaktlvllmgkegvhg
gminkkcyemashlrrsqy
>d1hma__ 1.21.1.1.3 HMG-D {(Drosophila melanogaster)}
sdkpkrplsaymlwlnsaresikrenpgikvtevakrggelwramkdkseweakaakakd
dydravkefeang
>d1hmca_ 1.26.1.2.4 Macrophage colony-stimulating factor (M-CSF) {human (Homo sapiens)}
seycshmigsghlqslqrlidsqmetscqitfefvdqeqlkdpvcylkkafllvqdimed
tmrfrdntpnaiaivqlqelslrlkscftkdyeehdkacvrtfyetplqllekvknvfne
tknlldkdwnifskncnnsfaecssqgh
>d1hmcb_ 1.26.1.2.4 Macrophage colony-stimulating factor (M-CSF) {human (Homo sapiens)}
seycshmigsghlqslqrlidsqmetscqitfefvdqeqlkdpvcylkkafllvqdimed
tmrfrdntpnaiaivqlqelslrlkscftkdyeehdkacvrtfyetplqllekvknvfne
tknlldkdwnifskncnnsfaec
>d1hmda_ 1.24.4.1.1 Hemerythrin {sipunculid worm (Themiste dyscrita)}
gfpipdpycwdisfrtfytiiddehktlfngilllsqadnadhlnelrrctgkhflneqq
lmqssqyagyaehkkahddfihkldtwdgdvtyaknwlvnhiktidfkyrgki
>d1hmdb_ 1.24.4.1.1 Hemerythrin {sipunculid worm (Themiste dyscrita)}
gfpipdpycwdisfrtfytiiddehktlfngilllsqadnadhlnelrrctgkhflneqq
lmqssqyagyaehkkahddfihkldtwdgdvtyaknwlvnhiktidfkyrgki
>d1hmdc_ 1.24.4.1.1 Hemerythrin {sipunculid worm (Themiste dyscrita)}
gfpipdpycwdisfrtfytiiddehktlfngilllsqadnadhlnelrrctgkhflneqq
lmqssqyagyaehkkahddfihkldtwdgdvtyaknwlvnhiktidfkyrgki
>d1hmdd_ 1.24.4.1.1 Hemerythrin {sipunculid worm (Themiste dyscrita)}
gfpipdpycwdisfrtfytiiddehktlfngilllsqadnadhlnelrrctgkhflneqq
lmqssqyagyaehkkahddfihkldtwdgdvtyaknwlvnhiktidfkyrgki
>d1hme__ 1.21.1.1.1 HMG1, fragments A and B {rat/hamster (Rattus norvegicus/Cricetulus griseus)}
fkdpnapkrppsafflfcseyrpkikgehpglsigdvakklgemwnntaaddkqpyekka
aklkekyekdiaayrak
>d1hmf__ 1.21.1.1.1 HMG1, fragments A and B {rat/hamster (Rattus norvegicus/Cricetulus griseus)}
fkdpnapkrppsafflfcseyrpkikgehpglsigdvakklgemwnntaaddkqpyekka
aklkekyekdiaayrak
>d1hmia1 3.47.3.1.4 (430-556) HIV RNase H (Domain of reverse transcriptase) {(human immunodeficiency virus type I)}
ekepivgaetfyvdgaanretklgkagyvtnkgrqkvvpltnttnqktelqaiylalqds
glevnivtdsqyalgiiqaqpdkseselvnqiieqlikkekvylawvpahkgiggneqvd
klvsagi
>d1hmia2 5.9.1.2.2 (1-429) HIV-1 reverse transcriptase {human immunodeficiency virus type 1 (Bh10 isolate)}
pispietvpvklkpgmdgpkvkqwplteekikalveictemekegkiskigpenpyntpv
faikkkdstkwrklvdfrelnkrtqdfwevqlgiphpaglkkkksvtvldvgdayfsvpl
dedfrkytaftipsinnetpgiryqynvlpqgwkgspaifqssmtkilepfkkqnpdivi
yqymddlyvgsdleigqhrtkieelrqhllrwglttpdkkhqkeppflwmgyelhpdkwt
vqpivlpekdswtvndiqklvgklnwasqiypgikvrqlskllrgtkalteviplteeae
lelaenreilkepvhgvyydpskdliaeiqkqgqgqwtyqiyqepfknlktgkyarmrga
htndvkqlteavqkittesiviwgktpkfklpiqketwetwwteywqatwipewefvntp
plvklwyql
>d1hml__ 4.2.1.2.14 alpha-Lactalbumin {human (Homo sapiens)}
kqftkcelsqllkdidgyggialpelictmfhtsgydtqaivennesteyglfqisnklw
ckssqvpqsrnicdiscdkflddditddimcakkildikgidywlahkalctekleqwlc
ekl
>d1hmoa_ 1.24.4.1.1 Hemerythrin {sipunculid worm (Themiste dyscrita)}
gfpipdpycwdisfrtfytiiddehktlfngilllsqadnadhlnelrrctgkhflneqq
lmqssqyagyaehkkahddfihkldtwdgdvtyaknwlvnhiktidfkyrgki
>d1hmob_ 1.24.4.1.1 Hemerythrin {sipunculid worm (Themiste dyscrita)}
gfpipdpycwdisfrtfytiiddehktlfngilllsqadnadhlnelrrctgkhflneqq
lmqssqyagyaehkkahddfihkldtwdgdvtyaknwlvnhiktidfkyrgki
>d1hmoc_ 1.24.4.1.1 Hemerythrin {sipunculid worm (Themiste dyscrita)}
gfpipdpycwdisfrtfytiiddehktlfngilllsqadnadhlnelrrctgkhflneqq
lmqssqyagyaehkkahddfihkldtwdgdvtyaknwlvnhiktidfkyrgki
>d1hmod_ 1.24.4.1.1 Hemerythrin {sipunculid worm (Themiste dyscrita)}
gfpipdpycwdisfrtfytiiddehktlfngilllsqadnadhlnelrrctgkhflneqq
lmqssqyagyaehkkahddfihkldtwdgdvtyaknwlvnhiktidfkyrgki
>d1hmpa_ 3.49.1.1.6 Hypoxantine-guanine PRTase {Human (Homo sapiens)}
spgvvisddepgydldlfcipnhyaedlervfiphglimdrterlardvmkemgghhiva
lcvlkggykffadlldyikalnrnsdrsipmtvdfirlksycndqstgdikviggddlst
ltgknvlivediidtgktmqtllslvrqynpkmvkvasllvkrtprsvgykpdfvgfeip
dkfvvgyaldyneyfrdlnhvcvisetgkakyka
>d1hmpb_ 3.49.1.1.6 Hypoxantine-guanine PRTase {Human (Homo sapiens)}
spgvvisddepgydldlfcipnhyaedlervfiphglimdrterlardvmkemgghhiva
lcvlkggykffadlldyikalnrnsdrsipmtvdfirlksycndqstgdikviggddlst
ltgknvlivediidtgktmqtllslvrqynpkmvkvasllvkrtprsvgykpdfvgfeip
dkfvvgyaldyneyfrdlnhvcvisetgkakyka
>d1hmr__ 2.45.1.2.1 Muscle fatty acid binding protein (m-fabp) {human (Homo sapiens)}
vdaflgtwklvdsknfddymkslgvgfatrqvasmtkpttiiekngdiltlkthstfknt
eisfklgvefdettaddrkvksivtldggklvhlqkwdgqettlvrelidgkliltlthg
tavctrtyeke
>d1hms__ 2.45.1.2.1 Muscle fatty acid binding protein (m-fabp) {human (Homo sapiens)}
vdaflgtwklvdsknfddymkslgvgfatrqvasmtkpttiiekngdiltlkthstfknt
eisfklgvefdettaddrkvksivtldggklvhlqkwdgqettlvrelidgkliltlthg
tavctrtyeke
>d1hmt__ 2.45.1.2.1 Muscle fatty acid binding protein (m-fabp) {human (Homo sapiens)}
vdaflgtwklvdsknfddymkslgvgfatrqvasmtkpttiiekngdiltlkthstfknt
eisfklgvefdettaddrkvksivtldggklvhlqkwdgqettlvrelidgkliltlthg
tavctrtyeke
>d1hmva1 3.47.3.1.4 (430-554) HIV RNase H (Domain of reverse transcriptase) {(human immunodeficiency virus type I)}
ekepivgaetfyvdgaanretklgkagyvtnkgrqkvvpltnttnqktelqaiylalqds
glevnivtdsqyalgiiqaqpdkseselvnqiieqlikkekvylawvpahkgiggneqvd
klvsa
>d1hmva2 5.9.1.2.2 (1-429) HIV-1 reverse transcriptase {human immunodeficiency virus type 1 (Bh10 isolate)}
pispietvpvklkpgmdgpkvkqwplteekikalveictemekegkiskigpenpyntpv
faikkkdstkwrklvdfrelnkrtqdfwevqlgiphpaglkkkksvtvldvgdayfsvpl
dedfrkytaftipsinnetpgiryqynvlpqgwkgspaifqssmtkilepfkkqnpdivi
yqymddlyvgsdleigqhrtkieelrqhllrwglttpdkkhqkeppflwmgyelhpdkwt
vqpivlpekdswtvndiqklvgklnwasqiypgikvrqlckllrgtkalteviplteeae
lelaenreilkepvhgvyydpskdliaeiqkqgqgqwtyqiyqepfknlktgkyarmrga
htndvkqlteavqkittesiviwgktpkfklpiqketwetwwteywqatwipewefvntp
plvklwyql
>d1hmy__ 3.53.1.5.1 DNA methylase HhaI, coenzyme-binding domain {(Haemophilus haemolyticus)}
mieikdkqltglrfidlfaglggfrlalescgaecvysnewdkyaqevyemnfgekpegd
itqvnektipdhdilcagfpcqafsisgkqkgfedsrgtlffdiarivrekkpkvvfmen
vknfashdngntlevvkntmneldysfhakvlnaldygipqkreriymicfrndlniqnf
qfpkpfelntfvkdlllpdsevehlvidrkdlvmtnqeieqttpktvrlgivgkggqger
iystrgiaitlsaygggifaktggylvngktrklhprecarvmgypdsykvhpstsqayk
qfgnsvvinvlqyiaynigsslnfkpy
>d1hna_1 1.43.1.1.6 (85-217) Glutathione S-transferase {human (Homo sapiens), class mu}
lcgesekeqiredilenqfmdsrmqlaklcydpdfeklkpeylqalpemlklysqflgkq
pwflgdkitfvdfiaydvlernqvfepscldafpnlkdfisrfeglekisaymkssrflp
rpvftkmavfgnk
>d1hna_2 3.38.1.4.6 (1-84) Glutathione S-transferase {human (Homo sapiens) class mu}
pmtlgywnirglahsirllleytdssyeekkytmgdapdydrsqwlnekfklgldfpnlp
ylidgthkitqsnailryiarkhn
>d1hnba1 1.43.1.1.6 (85-217) Glutathione S-transferase {human (Homo sapiens), class mu}
lcgesekeqiredilenqfmdsrmqlaklcydpdfeklkpeylqalpemlklysqflgkq
pwflgdkitfvdfiaydvlernqvfepscldafpnlkdfisrfeglekisaymkssrflp
rpvftkmavfgnk
>d1hnba2 3.38.1.4.6 (1-84) Glutathione S-transferase {human (Homo sapiens) class mu}
pmtlgywnirglahsirllleytdssyeekkytmgdapdydrsqwlnekfklgldfpnlp
ylidgthkitqsnailryiarkhn
>d1hnbb1 1.43.1.1.6 (85-217) Glutathione S-transferase {human (Homo sapiens), class mu}
lcgesekeqiredilenqfmdsrmqlaklcydpdfeklkpeylqalpemlklysqflgkq
pwflgdkitfvdfiaydvlernqvfepscldafpnlkdfisrfeglekisaymkssrflp
rpvftkmavfgnk
>d1hnbb2 3.38.1.4.6 (1-84) Glutathione S-transferase {human (Homo sapiens) class mu}
pmtlgywnirglahsirllleytdssyeekkytmgdapdydrsqwlnekfklgldfpnlp
ylidgthkitqsnailryiarkhn
>d1hnca1 1.43.1.1.6 (85-217) Glutathione S-transferase {human (Homo sapiens), class mu}
lcgesekeqiredilenqfmdsrmqlaklcydpdfeklkpeylqalpemlklysqflgkq
pwflgdkitfvdfiaydvlernqvfepscldafpnlkdfisrfeglekisaymkssrflp
rpvftkmavfgnk
>d1hnca2 3.38.1.4.6 (1-84) Glutathione S-transferase {human (Homo sapiens) class mu}
pmtlgywnirglahsirllleytdssyeekkytmgdapdydrsqwlnekfklgldfpnlp
ylidgthkitqsnailryiarkhn
>d1hncb1 1.43.1.1.6 (85-217) Glutathione S-transferase {human (Homo sapiens), class mu}
lcgesekeqiredilenqfmdsrmqlaklcydpdfeklkpeylqalpemlklysqflgkq
pwflgdkitfvdfiaydvlernqvfepscldafpnlkdfisrfeglekisaymkssrflp
rpvftkmavfgnk
>d1hncb2 3.38.1.4.6 (1-84) Glutathione S-transferase {human (Homo sapiens) class mu}
pmtlgywnirglahsirllleytdssyeekkytmgdapdydrsqwlnekfklgldfpnlp
ylidgthkitqsnailryiarkhn
>d1hncc1 1.43.1.1.6 (85-217) Glutathione S-transferase {human (Homo sapiens), class mu}
lcgesekeqiredilenqfmdsrmqlaklcydpdfeklkpeylqalpemlklysqflgkq
pwflgdkitfvdfiaydvlernqvfepscldafpnlkdfisrfeglekisaymkssrflp
rpvftkmavfgnk
>d1hncc2 3.38.1.4.6 (1-84) Glutathione S-transferase {human (Homo sapiens) class mu}
pmtlgywnirglahsirllleytdssyeekkytmgdapdydrsqwlnekfklgldfpnlp
ylidgthkitqsnailryiarkhn
>d1hncd1 1.43.1.1.6 (85-217) Glutathione S-transferase {human (Homo sapiens), class mu}
lcgesekeqiredilenqfmdsrmqlaklcydpdfeklkpeylqalpemlklysqflgkq
pwflgdkitfvdfiaydvlernqvfepscldafpnlkdfisrfeglekisaymkssrflp
rpvftkmavfgnk
>d1hncd2 3.38.1.4.6 (1-84) Glutathione S-transferase {human (Homo sapiens) class mu}
pmtlgywnirglahsirllleytdssyeekkytmgdapdydrsqwlnekfklgldfpnlp
ylidgthkitqsnailryiarkhn
>d1hnee_ 2.35.1.2.13 Elastase {human (Homo sapiens)}
ivggrrarphawpfmvslqlrgghfcgatliapnfvmsaahcvanvnvravrvvlgahnl
srreptrqvfavqrifedgydpvnllndivilqlngsatinanvqvaqlpaqgrrlgngv
qclamgwgllgrnrgiasvlqelnvtvvtslcrrsnvctlvrgrqagvcfgdsgsplvcn
glihgiasfvrggcasglypdafapvaqfvnwidsiiq
>d1hnf_1 2.1.1.1.5 (4-104) CD2 {human (Homo sapiens)}
tnaletwgalgqdinldipsfqmsddiddikwektsdkkkiaqfrkeketfkekdtyklf
kngtlkikhlktddqdiykvsiydtkgknvlekifdlkiqe
>d1hnf_2 2.1.1.3.6 (105-182) CD2 {human (Homo sapiens)}
rvskpkiswtcinttltcevmngtdpelnlyqdgkhlklsqrvithkwttslsakfkcta
gnkvskessvepvscpek
>d1hnga1 2.1.1.1.6 (2-99) CD2 {rat (Rattus rattus)}
dsgtvwgalghginlnipnfqmtddidevrwergstlvaefkrkmkpflksgafeilang
dlkiknltrddsgtynvtvystngtrilnkaldlrile
>d1hnga2 2.1.1.3.7 (101-176) CD2 {rat (Rattus rattus)}
vskpmiywecsnatltcevlegtdvelklyqgkehlrslrqktmsyqwtnlrapfkckav
nrvsqesemevvncpe
>d1hngb1 2.1.1.1.6 (2-99) CD2 {rat (Rattus rattus)}
dsgtvwgalghginlnipnfqmtddidevrwergstlvaefkrkmkpflksgafeilang
dlkiknltrddsgtynvtvystngtrilnkaldlrile
>d1hngb2 2.1.1.3.7 (101-176) CD2 {rat (Rattus rattus)}
vskpmiywecsnatltcevlegtdvelklyqgkehlrslrqktmsyqwtnlrapfkckav
nrvsqesemevvncpe
>d1hnia1 3.47.3.1.4 (430-558) HIV RNase H (Domain of reverse transcriptase) {(human immunodeficiency virus type I)}
ekepivgaetfyvdgaanretklgkagyvtnkgrqkvvpltnttnqktelqaiylalqds
glevnivtdsqyalgiiqaqpdkseselvnqiieqlikkekvylawvpahkgiggneqvd
klvsagirk
>d1hnia2 5.9.1.2.2 (1-429) HIV-1 reverse transcriptase {human immunodeficiency virus type 1 (Bh10 isolate)}
pispietvpvklkpgmdgpkvkqwplteekikalveictemekegkiskigpenpyntpv
faikkkdstkwrklvdfrelnkrtqdfwevqlgiphpaglkkkksvtvldvgdayfsvpl
dedfrkytaftipsinnetpgiryqynvlpqgwkgspaifqssmtkilepfkkqnpdivi
yqymddlyvgsdleigqhrtkieelrqhllrwglttpdkkhqkeppflwmgyelhpdkwt
vqpivlpekdswtvndiqklvgklnwasqiypgikvrqlskllrgtkalteviplteeae
lelaenreilkepvhgvyydpskdliaeiqkqgqgqwtyqiyqepfknlktgkyarmrga
htndvkqlteavqkittesiviwgktpkfklpiqketwetwwteywqatwipewefvntp
plvklwyql
>d1hnl__ 4.2.1.2.8 Lysozyme {human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnaahlscsallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1hnr__ 1.51.1.1.2 DNA-binding domain of H1 protein, (H-NS) {(Escherichia coli)}
aqrpakysyvdengetktwtgqgrtpavikkamdeqgkslddflikq
>d1hns__ 1.51.1.1.2 DNA-binding domain of H1 protein, (H-NS) {(Escherichia coli)}
aqrpakysyvdengetktwtgqgrtpavikkamdeqgkslddflikq
>d1hnva1 3.47.3.1.4 (430-558) HIV RNase H (Domain of reverse transcriptase) {(human immunodeficiency virus type I)}
ekepivgaetfyvdgaanretklgkagyvtnkgrqkvvpltnttnqktelqaiylalqds
glevnivtdsqyalgiiqaqpdkseselvnqiieqlikkekvylawvpahkgiggneqvd
klvsagirk
>d1hnva2 5.9.1.2.2 (1-429) HIV-1 reverse transcriptase {human immunodeficiency virus type 1 (Bh10 isolate)}
pispietvpvklkpgmdgpkvkqwplteekikalveictemekegkiskigpenpyntpv
faikkkdstkwrklvdfrelnkrtqdfwevqlgiphpaglkkkksvtvldvgdayfsvpl
dedfrkytaftipsinnetpgiryqynvlpqgwkgspaifqssmtkilepfkkqnpdivi
yqymddlyvgsdleigqhrtkieelrqhllrwglttpdkkhqkeppflwmgyelhpdkwt
vqpivlpekdswtvndiqklvgklnwasqiypgikvrqlskllrgtkalteviplteeae
lelaenreilkepvhgvyydpskdliaeiqkqgqgqwtyqiyqepfknlktgkyarmrga
htndvkqlteavqkittesiviwgktpkfklpiqketwetwwteywqatwipewefvntp
plvklwyql
>d1hny_1 2.53.1.1.7 (404-496) Mammalian alpha-amylase {human (Homo sapiens)}
qpftnwydngsnqvafgrgnrgfivfnnddwsfsltlqtglpagtycdvisgdkingnct
gikiyvsddgkahfsisnsaedpfiaihaeskl
>d1hny_2 3.1.1.1.7 (1-403) Mammalian alpha-amylase {human (Homo sapiens)}
xyspntqqgrtsivhlfewrwvdialecerylapkgfggvqvsppnenvaiynpfrpwwe
ryqpvsyklctrsgnedefrnmvtrcnnvgvriyvdavinhmcgnavsagtsstcgsyfn
pgsrdfpavpysgwdfndgkcktgsgdienyndatqvrdcrltglldlalekdyvrskia
eymnhlidigvagfrldaskhmwpgdikaildklhnlnsnwfpagskpfiyqevidlgge
pikssdyfgngrvtefkygaklgtvirkwngekmsylknwgegwgfvpsdralvfvdnhd
nqrghgaggasiltfwdarlykmavgfmlahpygftrvmssyrwprqfqngndvndwvgp
pnnngvikevtinpdttcgndwvcehrwrqirnmvifrnvvdg
>d1hoca1 2.1.1.2.12 (182-272) Class I MHC, beta2-microglobulin and alpha-3 domain {mouse (Mus musculus) h-2d (B)}
tdspkahvthhprskgevtlrcwalgfypaditltwqlngeeltqdmelvetrpagdgtf
qkwasvvvplgkeqnytcrvyheglpepltl
>d1hoca2 4.15.1.1.16 (1-181) MHC class I, alpha-1 and alpha-2 domains {mouse h-2d (B)}
gphsmryfetavsrpgleepryisvgyvdnkefvrfdsdaenpryeprapwmeqegpeyw
eretqkakgqeqwfrvslrnllgyynqsaggshtlqqmsgcdlgsdwrllrgylqfayeg
rdyialnedlktwtaadmaaqitrrkweqsgaaehykaylegecvewlhrylkngnatll
r
>d1hoe__ 2.4.1.1.1 HOE-467A {(Streptomyces tendae 4158)}
dttvsepapscvtlyqswrysqadngcaetvtvkvvyeddteglcyavapgqittvgdgy
igshgharylarcl
>d1hom__ 1.4.1.1.10 antennapedia Homeodomain {(Drosophila melanogaster)}
mrkrgrqtytryqtlelekefhfnryltrrrrieiahalclterqikiwfqnrrmkwkke
nktkgepg
>d1hona_ 3.29.1.6.2 Adenylosuccinate synthetase (gene purA product) {(Escherichia coli)}
gnnvvvlgtqwgdegkgkivdllterakyvvryqgghnaghtlvingektvlhlipsgil
renvtsiigngvvlspaalmkemkeledrgipvrerlllseacplildyhvaldnareka
rgakaigttgrgigpayedkvarrglrvgdlfdketfaeklkevmeyhnfqlvnyykaea
vdyqkvlddtmavadiltsmvvdvsdlldqarqrgdfvmfegaqgtlldidhgtypyvts
snttaggvatgsglgpryvdyvlgilkaystrvgagpfptelfdetgeflckqgnefgat
tgrrrrtgwldtvavrravqlnslsgfcltkldvldglkevklcvayrmpdgrevtttpl
aaddwkgvepiyetmpgwsestfgvkdrsglpqaalnyikrieeltgvpidiistgpdrt
etmilrdpfda
>d1honb_ 3.29.1.6.2 Adenylosuccinate synthetase (gene purA product) {(Escherichia coli)}
gnnvvvlgtqwgdegkgkivdllterakyvvryqgghnaghtlvingektvlhlipsgil
renvtsiigngvvlspaalmkemkeledrgipvrerlllseacplildyhvaldnareka
rgakaigttgrgigpayedkvarrglrvgdlfdketfaeklkevmeyhnfqlvnyykaea
vdyqkvlddtmavadiltsmvvdvsdlldqarqrgdfvmfegaqgtlldidhgtypyvts
snttaggvatgsglgpryvdyvlgilkaystrvgagpfptelfdetgeflckqgnefgat
tgrrrrtgwldtvavrravqlnslsgfcltkldvldglkevklcvayrmpdgrevtttpl
aaddwkgvepiyetmpgwsestfgvkdrsglpqaalnyikrieeltgvpidiistgpdrt
etmilrdpfda
>d1hooa_ 3.29.1.6.2 Adenylosuccinate synthetase (gene purA product) {(Escherichia coli)}
gnnvvvlgtqwgdegkgkivdllterakyvvryqgghnaghtlvingektvlhlipsgil
renvtsiigngvvlspaalmkemkeledrgipvrerlllseacplildyhvaldnareka
rgakaigttgrgigpayedkvarrglrvgdlfdketfaeklkevmeyhnfqlvnyykaea
vdyqkvlddtmavadiltsmvvdvsdlldqarqrgdfvmfegaqgtlldidhgtypyvts
snttaggvatgsglgpryvdyvlgilkaystrvgagpfptelfdetgeflckqgnefgat
tgrrrrtgwldtvavrravqlnslsgfcltkldvldglkevklcvayrmpdgrevtttpl
aaddwkgvepiyetmpgwsestfgvkdrsglpqaalnyikrieeltgvpidiistgpdrt
etmilrdpfda
>d1hoob_ 3.29.1.6.2 Adenylosuccinate synthetase (gene purA product) {(Escherichia coli)}
gnnvvvlgtqwgdegkgkivdllterakyvvryqgghnaghtlvingektvlhlipsgil
renvtsiigngvvlspaalmkemkeledrgipvrerlllseacplildyhvaldnareka
rgakaigttgrgigpayedkvarrglrvgdlfdketfaeklkevmeyhnfqlvnyykaea
vdyqkvlddtmavadiltsmvvdvsdlldqarqrgdfvmfegaqgtlldidhgtypyvts
snttaggvatgsglgpryvdyvlgilkaystrvgagpfptelfdetgeflckqgnefgat
tgrrrrtgwldtvavrravqlnslsgfcltkldvldglkevklcvayrmpdgrevtttpl
aaddwkgvepiyetmpgwsestfgvkdrsglpqaalnyikrieeltgvpidiistgpdrt
etmilrdpfda
>d1hopa_ 3.29.1.6.2 Adenylosuccinate synthetase (gene purA product) {(Escherichia coli)}
gnnvvvlgtqwgdegkgkivdllterakyvvryqgghnaghtlvingektvlhlipsgil
renvtsiigngvvlspaalmkemkeledrgipvrerlllseacplildyhvaldnareka
rgakaigttgrgigpayedkvarrglrvgdlfdketfaeklkevmeyhnfqlvnyykaea
vdyqkvlddtmavadiltsmvvdvsdlldqarqrgdfvmfegaqgtlldidhgtypyvts
snttaggvatgsglgpryvdyvlgilkaystrvgagpfptelfdetgeflckqgnefgat
tgrrrrtgwldtvavrravqlnslsgfcltkldvldglkevklcvayrmpdgrevtttpl
aaddwkgvepiyetmpgwsestfgvkdrsglpqaalnyikrieeltgvpidiistgpdrt
etmilrdpfda
>d1hopb_ 3.29.1.6.2 Adenylosuccinate synthetase (gene purA product) {(Escherichia coli)}
gnnvvvlgtqwgdegkgkivdllterakyvvryqgghnaghtlvingektvlhlipsgil
renvtsiigngvvlspaalmkemkeledrgipvrerlllseacplildyhvaldnareka
rgakaigttgrgigpayedkvarrglrvgdlfdketfaeklkevmeyhnfqlvnyykaea
vdyqkvlddtmavadiltsmvvdvsdlldqarqrgdfvmfegaqgtlldidhgtypyvts
snttaggvatgsglgpryvdyvlgilkaystrvgagpfptelfdetgeflckqgnefgat
tgrrrrtgwldtvavrravqlnslsgfcltkldvldglkevklcvayrmpdgrevtttpl
aaddwkgvepiyetmpgwsestfgvkdrsglpqaalnyikrieeltgvpidiistgpdrt
etmilrdpfda
>d1hora_ 3.27.1.1.1 Glucosamine 6-phosphate deaminase {(Escherichia coli)}
mrliplttaeqvgkwaarhivnrinafkptadrpfvlglptggtpmttykalvemhkagq
vsfkhvvtfnmdeyvglpkehpesyysfmhrnffdhvdipaeninllngnapdidaecrq
yeekirsygkihlfmggvgndghiafnepasslasrtriktlthdtrvansrffdndvnq
vpkyaltvgvgtlldaeevmilvlgsqkalalqaavegcvnhmwtisclqlhpkaimvcd
epstmelkvktlryfneleaenikgl
>d1horb_ 3.27.1.1.1 Glucosamine 6-phosphate deaminase {(Escherichia coli)}
mrliplttaeqvgkwaarhivnrinafkptadrpfvlglptggtpmttykalvemhkagq
vsfkhvvtfnmdeyvglpkehpesyysfmhrnffdhvdipaeninllngnapdidaecrq
yeekirsygkihlfmggvgndghiafnepasslasrtriktlthdtrvansrffdndvnq
vpkyaltvgvgtlldaeevmilvlgsqkalalqaavegcvnhmwtisclqlhpkaimvcd
epstmelkvktlryfneleaenikgl
>d1hosa_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hosb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hota_ 3.27.1.1.1 Glucosamine 6-phosphate deaminase {(Escherichia coli)}
mrliplttaeqvgkwaarhivnrinafkptadrpfvlglptggtpmttykalvemhkagq
vsfkhvvtfnmdeyvglpkehpesyysfmhrnffdhvdipaeninllngnapdidaecrq
yeekirsygkihlfmggvgndghiafnepasslasrtriktlthdtrvansrffdndvnq
vpkyaltvgvgtlldaeevmilvlgsqkalalqaavegcvnhmwtisclqlhpkaimvcd
epstmelkvktlryfneleaenikgl
>d1hotb_ 3.27.1.1.1 Glucosamine 6-phosphate deaminase {(Escherichia coli)}
mrliplttaeqvgkwaarhivnrinafkptadrpfvlglptggtpmttykalvemhkagq
vsfkhvvtfnmdeyvglpkehpesyysfmhrnffdhvdipaeninllngnapdidaecrq
yeekirsygkihlfmggvgndghiafnepasslasrtriktlthdtrvansrffdndvnq
vpkyaltvgvgtlldaeevmilvlgsqkalalqaavegcvnhmwtisclqlhpkaimvcd
epstmelkvktlryfneleaenikgl
>d1hp8__ 1.16.1.1.1 p8-MTCP1 {Human (Homo sapiens)}
mpqkdpcqkqaceiqkclqansymeskcqaviqelrkccaqypkgrsvvcsgfekeeeen
ltrksask
>d1hpbp_ 3.82.1.1.10 Histidine-binding protein {(Salmonella typhimurium)}
aipqkirigtdptyapfesknaqgelvgfdidlakelckrintqctfvenpldalipslk
akkidaimsslsitekrqqeiaftdklyaadsrlvvaknsdiqptvaslkgkrvgvlqgt
tqetfgnehwapkgieivsyqgqdniysdltagridaafqdevaasegflkqpvgkdykf
ggpavkdeklfgvgtgmglrkednelrealnkafaemradgtyeklakkyfdfdvygg
>d1hpca_ 2.65.1.1.2 Protein H of glycine cleavage system {Pea (Pisum sativum)}
snvldglkyapshewvkhegsvatigitdhaqdhlgevvfvelpepgvsvtkgkgfgave
svkatsdvnspisgevievntgltgkpglinsspyedgwmikikptspdelesllgakey
tkfceeedaah
>d1hpcb_ 2.65.1.1.2 Protein H of glycine cleavage system {Pea (Pisum sativum)}
snvldglkyapshewvkhegsvatigitdhaqdhlgevvfvelpepgvsvtkgkgfgave
svkatsdvnspisgevievntgltgkpglinsspyedgwmikikptspdelesllgakey
tkfceeedaah
>d1hpga_ 2.35.1.1.4 Glutamic acid-specific protease {(Streptomyces griseus)}
vlgggaiygggsrcsaafnvtkggaryfvtaghctnisanwsassggsvvgvregtsfpt
ndygivrytdgsspagtvdlyngstqdissaanavvgqaikksgsttkvtsgtvtavnvt
vnygdgpvynmvrttacsaggdsggahfagsvalgihsgssgcsgtagsaihqpvteals
aygvtvy
>d1hpi__ 7.30.1.1.4 HIPIP (high potential iron protein) {(Ectothiorhodospira vacuolata )}
merlseddpaaqaleyrhdassvqhpayeegqtclncllytdasaqdwgpcsvfpgklvs
angwctawvar
>d1hpj__ 7.13.1.1.3 Plasminogen kringles {human (Homo sapiens)}
cktgngknyrgtmsktkngitcqkwsstsphrprfspathpsegleenycrnpdndpqgp
wcyttdpekrydycdilec
>d1hpk__ 7.13.1.1.3 Plasminogen kringles {human (Homo sapiens)}
cktgngknyrgtmsktkngitcqkwsstsphrprfspathpsegleenycrnpdndpqgp
wcyttdpekrydycdilec
>d1hpla1 2.10.2.1.1 (337-449) Pancreatic lipase, C-terminal domain {horse (Equus caballus)}
rwryrvdvtlsgkkvtghvlvslfgnkgnsrqyeifqgtlkpdntysnefdsdvevgdle
kvkfiwynnvinltlpkvgaskitverndgsvfnfcseetvredvlltltac
>d1hpla2 3.56.1.11.1 (1-336) Pancreatic lipase, N-terminal domain {horse (Equus caballus)}
nevcyerlgcfsddspwagiverplkilpwspekvntrfllytnenpdnfqeivadpsti
qssnfntgrktrfiihgfidkgeeswlstmcqnmfkvesvncicvdwksgsrtaysqasq
nvrivgaevaylvgvlqssfdyspsnvhiighslgshaageagrrtngavgritgldpae
pcfqgtpelvrldpsdaqfvdvihtdiapfipnlgfgmsqtaghldffpnggkempgcqk
nvlsqivdidgiwqgtrdfaacnhlrsykyytdsilnpdgfagfscasysdftankcfpc
ssegcpqmghyadrfpgrtkgvgqlfylntgdasnfa
>d1hplb1 2.10.2.1.1 (337-449) Pancreatic lipase, C-terminal domain {horse (Equus caballus)}
rwryrvdvtlsgkkvtghvlvslfgnkgnsrqyeifqgtlkpdntysnefdsdvevgdle
kvkfiwynnvinltlpkvgaskitverndgsvfnfcseetvredvlltltac
>d1hplb2 3.56.1.11.1 (1-336) Pancreatic lipase, N-terminal domain {horse (Equus caballus)}
nevcyerlgcfsddspwagiverplkilpwspekvntrfllytnenpdnfqeivadpsti
qssnfntgrktrfiihgfidkgeeswlstmcqnmfkvesvncicvdwksgsrtaysqasq
nvrivgaevaylvgvlqssfdyspsnvhiighslgshaageagrrtngavgritgldpae
pcfqgtpelvrldpsdaqfvdvihtdiapfipnlgfgmsqtaghldffpnggkempgcqk
nvlsqivdidgiwqgtrdfaacnhlrsykyytdsilnpdgfagfscasysdftankcfpc
ssegcpqmghyadrfpgrtkgvgqlfylntgdasnfa
>d1hpm_1 3.47.1.1.1 (4-188) Heat shock protein 70kDa, ATPase fragment {bovine (Bos taurus)}
gpavgidlgttyscvgvfqhgkveiiandqgnrttpsyvaftdterligdaaknqvamnp
tntvfdakrligrrfddavvqsdmkhwpfmvvndagrpkvqveykgetksfypeevssmv
ltkmkeiaeaylgktvtnavvtvpayfndsqrqatkdagtiaglnvlriineptaaaiay
gldkk
>d1hpm_2 3.47.1.1.1 (189-381) Heat shock protein 70kDa, ATPase fragment {bovine (Bos taurus)}
vgaernvlifdlgggtfdvsiltiedgifevkstagdthlggedfdnrmvnhfiaefkrk
hkkdisenkravrrlrtacerakrtlssstqasieidslyegidfytsitrarfeelnad
lfrgtldpvekalrdakldksqihdivlvggstripkiqkllqdffngkelnksinpdea
vaygaavqaails
>d1hpoa_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwkrplvtikiggqlkealldtgaddtvieemslpgrwkpkmiggiggfikvrqyd
qiiieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hpob_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwkrplvtikiggqlkealldtgaddtvieemslpgrwkpkmiggiggfikvrqyd
qiiieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hpsa_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hpsb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hpt__ 7.14.1.1.4 Secretory trypsin inhibitor {human (Homo sapiens)}
dslgreakcynelngctyeyrpvcgtdgdtypnecvlcfenrkrqtsiliqksgpc
>d1hpva_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hpvb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hpxa_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hpxb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hqaa_ 3.64.1.1.1 Alkaline phosphatase {(Escherichia coli)}
mpvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseitaarn
yaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngalgvd
ihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpgnal
ekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsdaasl
nsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptlaqmt
dkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkegntl
vivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqeqtgsqlriaayg
phaanvvgltdqtdlfytmkaalglk
>d1hqab_ 3.64.1.1.1 Alkaline phosphatase {(Escherichia coli)}
mpvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseitaarn
yaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngalgvd
ihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpgnal
ekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsdaasl
nsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptlaqmt
dkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkegntl
vivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqeqtgsqlriaayg
phaanvvgltdqtdlfytmkaalglk
>d1hqi__ 4.84.1.1.1 Phenol hydroxylase P2 protein {(Pseudomonas sp.) CF600}
msslvyiafqdndnaryvveaiiqdnphavvqhhpamirieaekrleirretveenlgra
wdvqemlvdvitiggnvdedddrfvlewkn
>d1hra__ 7.33.1.2.5 Retinoic acid receptor DNA-binding domain {human (Homo sapiens)}
miytchrdkncvinkvtrnrcqycrlqkcfevgmskesvrn
>d1hrb__ 1.24.4.1.2 Hemerythrin {(Phascolopsis gouldi)}
gfpipdpyvwdpsfrtfysiiddehktlfngifhlaiddnadnlgelrrctgkhflnqev
lmeasqyqfydehkkehdgfinaldnwkgdvkwakawlvnhiktidfkykgki
>d1hrc__ 1.3.1.1.7 Mitochondrial cytochrome c {horse (Equus caballus)}
xgdvekgkkifvqkcaqchtvekggkhktgpnlhglfgrktgqapgftytdanknkgitw
keetlmeylenpkkyipgtkmifagikkkteredliaylkkatne
>d1hrda1 3.22.1.7.1 (195-449) Glutamate dehydrogenase, C-terminal domain {(Clostridium symbiosum)}
karsfggslvrpeatgygsvyyveavmkhendtlvgktvalagfgnvawgaakklaelga
kavtlsgpdgyiydpegitteekinymlemrasgrnkvqdyadkfgvqffpgekpwgqkv
diimpcatqndvdleqakkivannvkyyievanmpttnealrflmqqpnmvvapskavna
ggvlvsgfemsqnserlswtaeevdsklhqvmtdihdgsaaaaeryglgynlvaganivg
fqkiadammaqgiaw
>d1hrda2 3.61.1.1.1 (1-194) Glutamate dehydrogenase, N-terminal domain {(Clostridium symbiosum)}
skyvdrviaevekkyadepefvqtveevlsslgpvvdahpeyeevallermvipervief
rvpweddngkvhvntgyrvqfngaigpykgglrfapsvnlsimkflgfeqafkdslttlp
mggakggsdfdpngksdrevmrfcqafmtelyrhigpdidvpagdlgvgareigymygqy
rkivggfyngvltg
>d1hrdb1 3.22.1.7.1 (195-449) Glutamate dehydrogenase, C-terminal domain {(Clostridium symbiosum)}
karsfggslvrpeatgygsvyyveavmkhendtlvgktvalagfgnvawgaakklaelga
kavtlsgpdgyiydpegitteekinymlemrasgrnkvqdyadkfgvqffpgekpwgqkv
diimpcatqndvdleqakkivannvkyyievanmpttnealrflmqqpnmvvapskavna
ggvlvsgfemsqnserlswtaeevdsklhqvmtdihdgsaaaaeryglgynlvaganivg
fqkiadammaqgiaw
>d1hrdb2 3.61.1.1.1 (1-194) Glutamate dehydrogenase, N-terminal domain {(Clostridium symbiosum)}
skyvdrviaevekkyadepefvqtveevlsslgpvvdahpeyeevallermvipervief
rvpweddngkvhvntgyrvqfngaigpykgglrfapsvnlsimkflgfeqafkdslttlp
mggakggsdfdpngksdrevmrfcqafmtelyrhigpdidvpagdlgvgareigymygqy
rkivggfyngvltg
>d1hrdc1 3.22.1.7.1 (195-449) Glutamate dehydrogenase, C-terminal domain {(Clostridium symbiosum)}
karsfggslvrpeatgygsvyyveavmkhendtlvgktvalagfgnvawgaakklaelga
kavtlsgpdgyiydpegitteekinymlemrasgrnkvqdyadkfgvqffpgekpwgqkv
diimpcatqndvdleqakkivannvkyyievanmpttnealrflmqqpnmvvapskavna
ggvlvsgfemsqnserlswtaeevdsklhqvmtdihdgsaaaaeryglgynlvaganivg
fqkiadammaqgiaw
>d1hrdc2 3.61.1.1.1 (1-194) Glutamate dehydrogenase, N-terminal domain {(Clostridium symbiosum)}
skyvdrviaevekkyadepefvqtveevlsslgpvvdahpeyeevallermvipervief
rvpweddngkvhvntgyrvqfngaigpykgglrfapsvnlsimkflgfeqafkdslttlp
mggakggsdfdpngksdrevmrfcqafmtelyrhigpdidvpagdlgvgareigymygqy
rkivggfyngvltg
>d1hre__ 7.3.9.1.15 Heregulin-alpha, EGF-like domain {human (Homo sapiens)}
gtshlvkcaekektfcvnggecfmvkdlsnpsrylckcqpgftgarctenvpmkvqnqek
aeelyqk
>d1hrf__ 7.3.9.1.15 Heregulin-alpha, EGF-like domain {human (Homo sapiens)}
gtshlvkcaekektfcvnggecfmvkdlsnpsrylckcqpgftgarctenvpmkvqnqek
aeelyqk
>d1hrha_ 3.47.3.1.4 HIV RNase H (Domain of reverse transcriptase) {(human immunodeficiency virus type I)}
yqlekepivgaetfyvdgaanretklgkagyvtnkgrqkvvpltnttnqktelqaiylal
qdsglevnivtdsqyalgiiqaqpdkseselvnqiieqlikkekvylawvpahkgiggne
qvdklvsagi
>d1hrhb_ 3.47.3.1.4 HIV RNase H (Domain of reverse transcriptase) {(human immunodeficiency virus type I)}
yqlekepivgaetfyvdgaanretklgkagyvtnkgrqkvvpltnttnqktelqaiylal
qdsglevnivtdsqyalgiiqaqpdkseselvnqiieqlikkekvylawvpahkgiggne
qvdklvsa
>d1hri1_ 2.8.1.4.7 Rhinovirus coat protein {Human (Homo sapiens) rhinovirus 14}
tvasissgpkhtqkvpiltanetgatmpvlpsdsietrttymhfngsetdvecflgraac
vhvteiqnkdatgidnhreaklfndwkinlsslvqlrkklelftyvrfdseytilatasq
pdsanyssnlvvqamyvppgapnpkewddytwqsasnpsvffkvgdtsrfsvpyvglasa
yncfydgyshddaetqygitvlnhmgsmafrivnehdehktlvkirvyhrakhveawipr
apralpytsigrtnypkntepvikkrkgdiksy
>d1hri2_ 2.8.1.4.7 Rhinovirus coat protein {Human (Homo sapiens) rhinovirus 14}
gysdrvqqitlgnstittqeaanavvcyaewpeylpdvdasdvnktskpdtsvcrfytld
sktwttgskgwcwklpdalkdmgvfgqnmffhslgrsgytvhvqcnatkfhsgcllvvvi
pehqlasheggnvsvkytfthpgergidlssanevggpvkdvlynmngtllgnllifphq
finlrtnntativipyinsvpidsmtrhnnvslmvipiapltvptgatpslpitvtiapm
ctefsgirsksivpq
>d1hri3_ 2.8.1.4.7 Rhinovirus coat protein {Human (Homo sapiens) rhinovirus 14}
glptttlpgsgqflttddrqspsalpnyeptprihipgkvhnlleiiqvdtlipmnntht
kdevnsyliplnanrqneqvfgtnlfigdgvfkttllgeivqyythwsgslrfslmytgp
alssaklilaytppgargpqdrreamlgthvvwdiglqstivmtipwtsgvqfrytdpdt
ytsagflscwyqtslilppettgqvyllsfisacpdfklrlmkdtqtisqtvalte
>d1hrja_ 4.7.1.1.7 RANTES (regulated upon activation, normal T-cell expressed and secreted) {human (Homo sapiens)}
spyssdttpccfayiarplprahikeyfytsgkcsnpavvfvtrknrqvcanpekkwvre
yinslems
>d1hrjb_ 4.7.1.1.7 RANTES (regulated upon activation, normal T-cell expressed and secreted) {human (Homo sapiens)}
spyssdttpccfayiarplprahikeyfytsgkcsnpavvfvtrknrqvcanpekkwvre
yinslems
>d1hrm__ 1.1.1.1.8 Myoglobin {horse (Equus caballus)}
glsdgewqqvlnvwgkveadiaghgqevlirlftghpetlekfdkfkhlkteaemkased
lkkhgtvvltalggilkkkghheaelkplaqsyatkhkipikylefisdaiihvlhskhp
gdfgadaqgamtkalelfrndiaakykelgfqg
>d1hrna_ 2.38.1.2.14 Chymosin (synonim: renin) {human (Homo sapiens)}
gnttssviltnymdtqyygeigigtppqtfkvvfdtgssnvwvpsskcsrlytacvyhkl
fdasdsssykhngteltlrystgtvsgflsqdiitvggitvtqmfgevtempalpfmlae
fdgvvgmgfieqaigrvtpifdniisqgvlkedvfsfyynrdsensqslggqivlggsdp
qhyegnfhyinliktgvwqiqmkgvsvgsstllcedgclalvdtgasyisgstssieklm
ealgakkrlfdyvvkcnegptlpdisfhlggkeytltsadyvfqesysskklctlaiham
dippptgptwalgatfirkfytefdrrnnrigfalar
>d1hrnb_ 2.38.1.2.14 Chymosin (synonim: renin) {human (Homo sapiens)}
gnttssviltnymdtqyygeigigtppqtfkvvfdtgssnvwvpsskcsrlytacvyhkl
fdasdsssykhngteltlrystgtvsgflsqdiitvggitvtqmfgevtempalpfmlae
fdgvvgmgfieqaigrvtpifdniisqgvlkedvfsfyynrdsensqslggqivlggsdp
qhyegnfhyinliktgvwqiqmkgvsvgsstllcedgclalvdtgasyisgstssieklm
ealgakkrlfdyvvkcnegptlpdisfhlggkeytltsadyvfqesysskklctlaiham
dippptgptwalgatfirkfytefdrrnnrigfalar
>d1hroa_ 1.3.1.1.15 Cytochrome c2 {(Rhodopila globiformis)}
sappgdpvegkhlfhticitchtdikgankvgpslygvvgrhsgiepgynyseaniksgi
vwtpdvlfkyiehpqkivpgtkmgypgqpdpqkradiiayletlk
>d1hrob_ 1.3.1.1.15 Cytochrome c2 {(Rhodopila globiformis)}
sappgdpvegkhlfhticitchtdikgankvgpslygvvgrhsgiepgynyseaniksgi
vwtpdvlfkyiehpqkivpgtkmgypgqpdpqkradiiayletlk
>d1hrpa_ 7.16.1.4.1 Gonadotropin, A and B chains {Human (Homo sapiens)}
tqdcpectlqenpffsqpgapilqcmgccfsrayptplrskktmlvqknvtsestccvak
synrvtvmggfkvenhtachcstcyy
>d1hrpb_ 7.16.1.4.1 Gonadotropin, A and B chains {Human (Homo sapiens)}
keplrprcrpinatlavekegcpvcitvntticagycptmtrvlqgvlpalpqvvcnyrd
vrfesirlpgcprgvnpvvsyavalscqcalcrrsttdcggpkdhpltcd
>d1hrq__ 7.30.1.1.2 HIPIP (high potential iron protein) {(Cromatium vinosum )}
sapanavaaddataialkynqdatkservaaarpglppeeqhcancqfmqadaagatdew
kgcqlfpgklinvngwcaswtlkag
>d1hrr__ 7.30.1.1.2 HIPIP (high potential iron protein) {(Cromatium vinosum )}
sapanavaaddataialkynqdatkservaaarpglppeeqhcancqfmqadaagatdew
kgcqlfpgklinvngwcaswtlkag
>d1hrs__ 1.25.1.1.4 (Apo)ferritin {horse (Equus caballus), L chain}
ssqirqnysteveaavnrlvnlylrasytylslgfyfdrddvalegvchffrelaeekre
gaerllkmqnqrggralfqdlqkpsqdewgttldamkaaivlekslnqalldlhalgsaq
adphlcdfleshfldeevklikkmgdhltniqrlvgsqaglgeylferltlkhd
>e1hrt.1h 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
ivegqdaevglspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftvddll
vrigkhsrtryerkvekismldkiyihprynwkenldrdiallklkrpielsdyihpvcl
pdkqtaakllhagfkgrvtgwgnrretwttsvaevqpsvlqvvnlplverpvckastrir
itdnmfcagykpgegkrgdacegdsggpfvmkspynnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidrlgs
>e1hrt.1l 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>d1hrti_ 7.3.13.2.1 Hirudin {leech (Hirudo medicinalis)}
vvytdctesgqnlclcegsnvcgqgnkcilgsdgeknqcvtgegtpkpqshndgdfeeip
eeylq
>d1hrv1_ 2.8.1.4.7 Rhinovirus coat protein {Human (Homo sapiens) rhinovirus 14}
tvasissgpkhtqkvpiltanetgatmpvlpsdsietrttymhfngsetdvecflgraac
vhvteiqnkdatgidnhreaklfndwkinlsslvqlrkklelftyvrfdseytilatasq
pdsanyssnlvvqamyvppgapnpkewddytwqsasnpsvffkvgdtsrfsvpyvglasa
yncfydgyshddaetqygitvlnhmgsmafrivnehdehktlvkirvyhrakhveawipr
apralpytsigrtnypkntepvikkrkgdiksy
>d1hrv2_ 2.8.1.4.7 Rhinovirus coat protein {Human (Homo sapiens) rhinovirus 14}
gysdrvqqitlgnstittqeaanavvcyaewpeylpdvdasdvnktskpdtsvcrfytld
sktwttgskgwcwklpdalkdmgvfgqnmffhslgrsgytvhvqcnatkfhsgcllvvvi
pehqlasheggnvsvkytfthpgergidlssanevggpvkdvlynmngtllgnllifphq
finlrtnntativipyinsvpidsmtrhnnvslmvipiapltvptgatpslpitvtiapm
ctefsgirsksivpq
>d1hrv3_ 2.8.1.4.7 Rhinovirus coat protein {Human (Homo sapiens) rhinovirus 14}
glptttlpgsgqflttddrqspsalpnyeptprihipgkvhnlleiiqvdtlipmnntht
kdevnsyliplnanrqneqvfgtnlfigdgvfkttllgeivqyythwsgslrfslmytgp
alssaklilaytppgargpqdrreamlgthvvwdiglqstivmtipwtsgvqfrytdpdt
ytsagflscwyqtslilppettgqvyllsfisacpdfklrlmkdtqtisqtvalte
>d1hrya_ 1.21.1.1.4 SRY {Human (Homo sapiens)}
drvkrpmnafivwsrdqrrkmalenprmrnseiskqlgyqwkmlteaekwpffqeaqklq
amhrekypnykyr
>d1hrza_ 1.21.1.1.4 SRY {Human (Homo sapiens)}
drvkrpmnafivwsrdqrrkmalenprmrnseiskqlgyqwkmlteaekwpffqeaqklq
amhrekypnykyr
>d1hsaa1 2.1.1.2.6 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain {human (Homo sapiens) hla-b2705}
adppkthvthhpisdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrwep
>d1hsaa2 4.15.1.1.10 (1-181) MHC class I, alpha-1 and alpha-2 domains {(human hla-b2705)}
gshsmryfhtsvsrpgrgeprfitvgyvddtlfvrfdsdaaspreeprapwieqegpeyw
dretqickakaqtdredlrtllryynqseagshtlqnmygcdvgpdgrllrgyhqdaydg
kdyialnedlsswtaadtaaqitqrkweaarvaeqlraylegecvewlrrylengketlq
r
>d1hsad1 2.1.1.2.6 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain {human (Homo sapiens) hla-b2705}
adppkthvthhpisdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrwep
>d1hsad2 4.15.1.1.10 (1-181) MHC class I, alpha-1 and alpha-2 domains {(human hla-b2705)}
gshsmryfhtsvsrpgrgeprfitvgyvddtlfvrfdsdaaspreeprapwieqegpeyw
dretqickakaqtdredlrtllryynqseagshtlqnmygcdvgpdgrllrgyhqdaydg
kdyialnedlsswtaadtaaqitqrkweaarvaeqlraylegecvewlrrylengketlq
r
>d1hsba1 2.1.1.2.7 (182-270) Class I MHC, beta2-microglobulin and alpha-3 domain {human (Homo sapiens) hla-aw68}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrdgedqtqdtelvetrpagdgtf
qkwvavvvpsgqeqrytchvqheglpkpl
>d1hsba2 4.15.1.1.11 (1-181) MHC class I, alpha-1 and alpha-2 domains {(human hla-aw68)}
gshsmryfytsvsrpgrgeprfiavgyvddtqfvrfdsdaasqrmeprapwieqegpeyw
drntrnvkaqsqtdrvdlgtlrgyynqseagshtiqmmygcdvgsdgrflrgyrqdaydg
kdyialkedlrswtaadmaaqttkhkweaahvaeqwraylegtcvewlrrylengketlq
r
>d1hse__ 3.82.1.2.1 Lactoferrin {human (Homo sapiens)}
rsvqwcavsqpeatkcfqwqrnmrrvrgppvscikrdspiqciqaiaenradavtldggf
iyeaglapyklrpvaaevygterqprthyyavavvkkggsfqlnelqglkschtglrrta
gwnvpigtlrpflnwtgppepieaavarffsascvpgadkgqfpnlcrlcagtgenkcaf
ssqepyfsysgafkclrdgagdvafirestvfedlsdeaerdeyellcpdntrkpvdkfk
dchlarvpsmavvarsvngkedaiwnllrqaqekfgkdkspkfqlfgspsgqkdllfkds
aigfsrvppridsglyl
>d1hsga_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hsgb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hsha_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqfslwkrpvvtayiegqpvevlldtgaddsivagielgnnyspkivggiggfintkeyk
nveievlnkkvratimtgdtpinifgrniltalgmslnl
>d1hshb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqfslwkrpvvtayiegqpvevlldtgaddsivagielgnnyspkivggiggfintkeyk
nveievlnkkvratimtgdtpinifgrniltalgmslnl
>d1hshc_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqfslwkrpvvtayiegqpvevlldtgaddsivagielgnnyspkivggiggfintkeyk
nveievlnkkvratimtgdtpinifgrniltalgmslnl
>d1hshd_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqfslwkrpvvtayiegqpvevlldtgaddsivagielgnnyspkivggiggfintkeyk
nveievlnkkvratimtgdtpinifgrniltalgmslnl
>d1hsia_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqfslwkrpvvtayiegqpvevlldtgaddsivagielgnnyspkivggiggfintkeyk
nveievlnkkvratimtgdtpinifgrniltalgmslnl
>d1hsib_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqfslwkrpvvtayiegqpvevlldtgaddsivagielgnnyspkivggiggfintkeyk
nveievlnkkvratimtgdtpinifgrniltalgmslnl
>d1hsla_ 3.82.1.1.9 Histidine-binding protein {(Escherichia coli), strain k-12}
aipqkirigtdptyapfesknaqgelvgfdidlakelckrintqctfvenpldalipslk
akkidaimsslsitekrqqeiaftdklyaadsrlvvaknsdiqptvaslkgkrvgvlqgt
tqetfgnehwapkgieivsyqgqdniysdltagridaafqdevaasegflkqpvgkdykf
ggpavkdeklfgvgtgmglrkednelrealnkafaemradgtyeklakkyfdfdvygg
>d1hslb_ 3.82.1.1.9 Histidine-binding protein {(Escherichia coli), strain k-12}
aipqkirigtdptyapfesknaqgelvgfdidlakelckrintqctfvenpldalipslk
akkidaimsslsitekrqqeiaftdklyaadsrlvvaknsdiqptvaslkgkrvgvlqgt
tqetfgnehwapkgieivsyqgqdniysdltagridaafqdevaasegflkqpvgkdykf
ggpavkdeklfgvgtgmglrkednelrealnkafaemradgtyeklakkyfdfdvygg
>d1hsm__ 1.21.1.1.1 HMG1, fragments A and B {rat/hamster (Rattus norvegicus/Cricetulus griseus)}
napkrppsafflfcseyrpkikgehpglsigdvakklgemwnntaaddkqpyekkaaklk
ekyekdiaayrakgkpdaa
>d1hsn__ 1.21.1.1.1 HMG1, fragments A and B {rat/hamster (Rattus norvegicus/Cricetulus griseus)}
napkrppsafflfcseyrpkikgehpglsigdvakklgemwnntaaddkqpyekkaaklk
ekyekdiaayrakgkpdaa
>d1hsq__ 2.24.2.1.17 Phospholipase C, SH3 domain {human (Homo sapiens)}
gsptfkcavkalfdykaqredeltfiksaiiqnvekqeggwwrgdyggkkqlwfpsnyve
emvnpegihrd
>d1hsr__ 1.72.1.1.2 Peroxidase {(Arthromyces ramous)}
svtcpggqstsnsqccvwfdvlddlqtnfyqgskcespvrkilrivfhdaigfspaltaa
gqfggggadgsiiahsnielafpanggltdtiealravginhgvsfgdliqfatavgmsn
cpgsprlefltgrsnssqpsppslipgpgntvtaildrmgdagfspdevvdllaahslas
qeglnsaifrspldstpqvfdtqfyietllkgttqpgpslgfaeelspfpgefrmrsdal
lardsrtacrwqsmtssnevmgqryraamakmsvlgfdrnaltdcsdvipsavsnnaapv
ipggltvddievscpsepfpeiatasgplpslapap
>d1hssa_ 1.47.1.2.1 0.19 alpha-amylase inhibitor {Wheat (Triticum aestivum)}
mcypgqafqvpalpacrpllrlqcngsqvpeavlrdccqqlahisewcrcgalysmldsm
ykehgaqegqagtgafprcrrevvkltaasitavcrlpivvdasgdgayvckdvaaypda
>d1hssb_ 1.47.1.2.1 0.19 alpha-amylase inhibitor {Wheat (Triticum aestivum)}
mcypgqafqvpalpacrpllrlqcngsqvpeavlrdccqqlahisewcrcgalysmldsm
ykehgaqegqagtgafprcrrevvkltaasitavcrlpivvdasgdgayvckdvaaypda
>d1hssc_ 1.47.1.2.1 0.19 alpha-amylase inhibitor {Wheat (Triticum aestivum)}
mcypgqafqvpalpacrpllrlqcngsqvpeavlrdccqqlahisewcrcgalysmldsm
ykehgaqegqagtgafprcrrevvkltaasitavcrlpivvdasgdgayvckdvaaypda
>d1hssd_ 1.47.1.2.1 0.19 alpha-amylase inhibitor {Wheat (Triticum aestivum)}
mcypgqafqvpalpacrpllrlqcngsqvpeavlrdccqqlahisewcrcgalysmldsm
ykehgaqegqagtgafprcrrevvkltaasitavcrlpivvdasgdgayvckdvaaypda
>d1hsta_ 1.4.3.9.1 Histone H5, globular domain {chicken (Gallus gallus)}
shptysemiaaairaeksrggssrqsiqkyikshykvghnadlqiklsirrllaagvlkq
tkgvgasgsfrlak
>d1hstb_ 1.4.3.9.1 Histone H5, globular domain {chicken (Gallus gallus)}
shptysemiaaairaeksrggssrqsiqkyikshykvghnadlqiklsirrllaagvlkq
tkgvgasgsfrlak
>d1hsy__ 1.1.1.1.8 Myoglobin {horse (Equus caballus)}
glsdgewqqvlnvwgkveadiaghgqevlirlftghpetlekfdkfkhlkteaemkased
lkktgtvvltalggilkkkghheaelkplaqshatkhkipikylefisdaiihvlhskhp
gdfgadaqgamtkalelfrndiaakykelgfqg
>d1htba1 2.25.1.2.2 (1-174,325-374) Alcohol dehydrogenase {human (Homo sapiens)}
stagkvikckaavlwevkkpfsiedvevappkayevrikmvavgicrtddhvvsgnlvtp
lpvilgheaagivesvgegvttvkpgdkviplftpqcgkcrvcknpesnyclkndlgnpr
gtlqdgtrrftcrgkpihhflgtstfsqytvvdenavakidaasplekvcligcXkegip
klvadfmakkfsldalithvlpfekinegfdllhsgksictvltf
>d1htba2 3.22.1.1.2 (175-324) Alcohol dehydrogenase {human (Homo sapiens), different isozymes}
gfstgygsavnvakvtpgstcavfglggvglsavmgckaagaariiavdinkdkfakake
lgatecinpqdykkpiqevlkemtdggvdfsfevigrldtmmasllccheacgtsvivgv
ppasqnlsinpmllltgrtwkgavyggfks
>d1htbb1 2.25.1.2.2 (1-174,325-374) Alcohol dehydrogenase {human (Homo sapiens)}
stagkvikckaavlwevkkpfsiedvevappkayevrikmvavgicrtddhvvsgnlvtp
lpvilgheaagivesvgegvttvkpgdkviplftpqcgkcrvcknpesnyclkndlgnpr
gtlqdgtrrftcrgkpihhflgtstfsqytvvdenavakidaasplekvcligcXkegip
klvadfmakkfsldalithvlpfekinegfdllhsgksictvltf
>d1htbb2 3.22.1.1.2 (175-324) Alcohol dehydrogenase {human (Homo sapiens), different isozymes}
gfstgygsavnvakvtpgstcavfglggvglsavmgckaagaariiavdinkdkfakake
lgatecinpqdykkpiqevlkemtdggvdfsfevigrldtmmasllccheacgtsvivgv
ppasqnlsinpmllltgrtwkgavyggfks
>d1htda_ 4.52.1.5.2 Snake venom metalloprotease {Atrolysin C: Western diamonback rattlesnake (Crotalus atrox)}
lpqryielvvvadhrvfmkynsdlntirtrvheivnfingfyrslnihvsltdleiwsne
dqiniqsassdtlnafaewretdllnrkshdnaqlltaieldeetlglaplgtmcdpkls
igivqdhspinllmgvtmahelghnlgmehdgkdclrgaslcimrpgltkgrsyefsdds
mhyyerflkqykpqcilnkp
>d1htdb_ 4.52.1.5.2 Snake venom metalloprotease {Atrolysin C: Western diamonback rattlesnake (Crotalus atrox)}
lpqryielvvvadhrvfmkynsdlntirtrvheivnfingfyrslnihvsltdleiwsne
dqiniqsassdtlnafaewretdllnrkshdnaqlltaieldeetlglaplgtmcdpkls
igivqdhspinllmgvtmahelghnlgmehdgkdclrgaslcimrpgltkgrsyefsdds
mhyyerflkqykpqcilnkp
>d1htea_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hteb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1htfa_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1htfb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1htga_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1htgb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1htia_ 3.1.11.1.2 Triosephosphate isomerase {Human (Homo sapiens)}
apsrkffvggnwkmngrkqslgeligtlnaakvpadtevvcapptayidfarqkldpkia
vaaqncykvtngaftgeispgmikdcgatwvvlghserrhvfgesdeligqkvahalaeg
lgviacigekldereagitekvvfeqtkviadnvkdwskvvlayepvwaigtgktatpqq
aqevheklrgwlksnvsdavaqstriiyggsvtgatckelasqpdvdgflvggaslkpef
vdiinakq
>d1htib_ 3.1.11.1.2 Triosephosphate isomerase {Human (Homo sapiens)}
apsrkffvggnwkmngrkqslgeligtlnaakvpadtevvcapptayidfarqkldpkia
vaaqncykvtngaftgeispgmikdcgatwvvlghserrhvfgesdeligqkvahalaeg
lgviacigekldereagitekvvfeqtkviadnvkdwskvvlayepvwaigtgktatpqq
aqevheklrgwlksnvsdavaqstriiyggsvtgatckelasqpdvdgflvggaslkpef
vdiinakq
>e1htl.1a 4.103.1.1.1 Heat-labile toxin, A-chain {(Escherichia coli) type IB}
rlyradsrppdeikrsgglmprghneyfdrgtqmninlydhargtqtgfvryddgyvsts
lslrsahlagqsilsgystyyiyviatapnmfnkndvlgvysphpyeqevsalggipysq
iygwyrvnfgviderlhrnreyrdryyrnlniapaedgyrlagfppdhqawreepwihha
pqgcg
>e1htl.1c 4.103.1.1.1 Heat-labile toxin, A-chain {(Escherichia coli) type IB}
gdtcneetqnlstiylreyqskvkrqifsdyqsevdiynri
>d1htld_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1htle_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1htlf_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1htlg_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1htlh_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1htmb_ 6.2.1.1.1 Influenza hemagglutinin (stalk) {(Influenza virus A)}
stqaaidqingklnrviektnekfhqiekefsevegriqdlekyvedtkidlwsynaell
valenqhtidltdsemnklfektrrqlrenaeemgngcfkiyhkcdnaciesir
>d1htmd_ 6.2.1.1.1 Influenza hemagglutinin (stalk) {(Influenza virus A)}
stqaaidqingklnrviektnekfhqiekefsevegriqdlekyvedtkidlwsynaell
valenqhtidltdsemnklfektrrqlrenaeemgngcfkiyhkcdnaciesirngtydh
dvy
>d1htmf_ 6.2.1.1.1 Influenza hemagglutinin (stalk) {(Influenza virus A)}
stqaaidqingklnrviektnekfhqiekefsevegriqdlekyvedtkidlwsynaell
valenqhtidltdsemnklfektrrqlrenaeemgngcfkiyhkcdnaciesirngtydh
dvy
>d1htn_1 1.105.1.1.3 (26-53) Tetranectin {Human (Homo sapiens)}
lksrldtlsqevallkeqqalqtvclkg
>d1htn_2 4.105.1.1.6 (54-181) Tetranectin {Human (Homo sapiens)}
tkvhmkcflaftqtktfheasedcisrggtlstpqtgsendalyeylrqsvgneaeiwlg
lndmaaegtwvdmtgariayknweteitaqpdggktencavlsgaangkwfdkrcrdqlp
yicqfgiv
>d1htp__ 2.65.1.1.2 Protein H of glycine cleavage system {Pea (Pisum sativum)}
snvldglkyapshewvkhegsvatigitdhaqdhlgevvfvelpepgvsvtkgkgfgave
svkatsdvnspisgevievntgltgkpglinsspyedgwmikikptspdelesllgakey
tkfceeedaah
>e1htr.1b 2.38.1.2.9 Pepsin(ogen) {human (Homo sapiens) progastricsin (pepsinogen C)}
svtyepmaymdaayfgeisigtppqnflvlfdtgssnlwvpsvycqsqactshsrfnpse
sstystngqtfslqygsgsltgffgydtltvqsiqvpnqefglsenepgtnfvyaqfdgi
mglaypalsvdeattamqgmvqegaltspvfsvylsnqqgssggavvfggvdsslytgqi
ywapvtqelywqigieefliggqasgwcsegcqaivdtgtslltvpqqymsallqatgaq
edeygqflvncnsiqnlpsltfiingvefplppssyilsnngyctvgveptylssqngqp
lwilgdvflrsyysvydlgnnrvgfataa
>e1htr.1p 2.38.1.2.9 Pepsin(ogen) {human (Homo sapiens) progastricsin (pepsinogen C)}
avvkvplkkfksiretmkekgllgeflrthkydpawkyrfgdl
>d1htta1 3.42.1.1.1 (326-424) Histidyl-tRNA synthetase (HisRS), C-terminal domain {(Escherichia coli)}
dpvvdiylvasgadtqsaamalaerlrdelpgvklmtnhgggnfkkqfaradkwgarvav
vlgesevangtavvkdlrsgeqtavaqdsvaahlrtllg
>d1htta2 4.61.1.1.3 (4-325) Histidyl-tRNA synthetase (HisRS) {(Escherichia coli)}
niqairgmndylpgetaiwqriegtlknvlgsygyseirlpiveqtplfkraigevtdvv
ekemytfedrngdsltlrpegtagcvragiehgllynqeqrlwyigpmfrherpqkgryr
qfhqlgcevfglqgpdidaelimltarwwralgisehvtlelnsigslearanyrdalva
fleqhkekldedckrrmytnplrvldsknpevqallndapalgdyldeesrehfaglckl
lesagiaytvnqrlvrgldyynrtvfewvtnslgsqgtvcaggrydglveqlggratpav
gfamglerlvllvqavnpefka
>d1httb1 3.42.1.1.1 (326-424) Histidyl-tRNA synthetase (HisRS), C-terminal domain {(Escherichia coli)}
dpvvdiylvasgadtqsaamalaerlrdelpgvklmtnhgggnfkkqfaradkwgarvav
vlgesevangtavvkdlrsgeqtavaqdsvaahlrtllg
>d1httb2 4.61.1.1.3 (4-325) Histidyl-tRNA synthetase (HisRS) {(Escherichia coli)}
niqairgmndylpgetaiwqriegtlknvlgsygyseirlpiveqtplfkraigevtdvv
ekemytfedrngdsltlrpegtagcvragiehgllynqeqrlwyigpmfrherpqkgryr
qfhqlgcevfglqgpdidaelimltarwwralgisehvtlelnsigslearanyrdalva
fleqhkekldedckrrmytnplrvldsknpevqallndapalgdyldeesrehfaglckl
lesagiaytvnqrlvrgldyynrtvfewvtnslgsqgtvcaggrydglveqlggratpav
gfamglerlvllvqavnpefka
>d1httc1 3.42.1.1.1 (326-424) Histidyl-tRNA synthetase (HisRS), C-terminal domain {(Escherichia coli)}
dpvvdiylvasgadtqsaamalaerlrdelpgvklmtnhgggnfkkqfaradkwgarvav
vlgesevangtavvkdlrsgeqtavaqdsvaahlrtllg
>d1httc2 4.61.1.1.3 (4-325) Histidyl-tRNA synthetase (HisRS) {(Escherichia coli)}
niqairgmndylpgetaiwqriegtlknvlgsygyseirlpiveqtplfkraigevtdvv
ekemytfedrngdsltlrpegtagcvragiehgllynqeqrlwyigpmfrherpqkgryr
qfhqlgcevfglqgpdidaelimltarwwralgisehvtlelnsigslearanyrdalva
fleqhkekldedckrrmytnplrvldsknpevqallndapalgdyldeesrehfaglckl
lesagiaytvnqrlvrgldyynrtvfewvtnslgsqgtvcaggrydglveqlggratpav
gfamglerlvllvqavnpefka
>d1httd1 3.42.1.1.1 (326-424) Histidyl-tRNA synthetase (HisRS), C-terminal domain {(Escherichia coli)}
dpvvdiylvasgadtqsaamalaerlrdelpgvklmtnhgggnfkkqfaradkwgarvav
vlgesevangtavvkdlrsgeqtavaqdsvaahlrtllg
>d1httd2 4.61.1.1.3 (4-325) Histidyl-tRNA synthetase (HisRS) {(Escherichia coli)}
niqairgmndylpgetaiwqriegtlknvlgsygyseirlpiveqtplfkraigevtdvv
ekemytfedrngdsltlrpegtagcvragiehgllynqeqrlwyigpmfrherpqkgryr
qfhqlgcevfglqgpdidaelimltarwwralgisehvtlelnsigslearanyrdalva
fleqhkekldedckrrmytnplrvldsknpevqallndapalgdyldeesrehfaglckl
lesagiaytvnqrlvrgldyynrtvfewvtnslgsqgtvcaggrydglveqlggratpav
gfamglerlvllvqavnpefka
>e1huc.1a 4.3.1.1.5 (Pro)cathepsin B {Human (Homo sapiens)}
lpasfdareqwpqcptikeirdqgscgscwafgaveaisdricihtn
>e1huc.1b 4.3.1.1.5 (Pro)cathepsin B {Human (Homo sapiens)}
vsvevsaedlltccgsmcgdgcnggypaeawnfwtrkglvsgglyeshvgcrpysippce
hhvngsrppctgegdtpkcskicepgysptykqdkhygynsysvsnsekdimaeiykngp
vegafsvysdfllyksgvyqhvtgemmgghairilgwgvengtpywlvanswntdwgdng
ffkilrgqdhcgiesevvagiprtd
>e1huc.2c 4.3.1.1.5 (Pro)cathepsin B {Human (Homo sapiens)}
lpasfdareqwpqcptikeirdqgscgscwafgaveaisdricihtn
>e1huc.2d 4.3.1.1.5 (Pro)cathepsin B {Human (Homo sapiens)}
vsvevsaedlltccgsmcgdgcnggypaeawnfwtrkglvsgglyeshvgcrpysippce
hhvngsrppctgegdtpkcskicepgysptykqdkhygynsysvsnsekdimaeiykngp
vegafsvysdfllyksgvyqhvtgemmgghairilgwgvengtpywlvanswntdwgdng
ffkilrgqdhcgiesevvagiprtd
>d1huea_ 1.51.1.1.3 HU protein {(Bacillus stearothermophilus)}
mnktelinavaetsglskkdatkavdavfdsitealrkgdkvqligfgnfevreraarkg
rnpqtgeemeipaskvpafkpgkalkdavk
>d1hueb_ 1.51.1.1.3 HU protein {(Bacillus stearothermophilus)}
mnktelinavaetsglskkdatkavdavfdsitealrkgdkvqligfgnfevreraarkg
rnpqtgeemeipaskvpafkpgkalkdavk
>d1hug__ 2.56.1.1.1 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme I}
wgyddkngpeqwsklypiangnnqspvdiktsetkhdtslkpisvsynpatakeiinvgh
sfhvnfedndnrsvlkggpfsdsyrlfqfhfhwgstnehgsehtvdgvkysaelhvahwn
sakysslaeaaskadglavigvlmkvgeanpklqkvldalqaiktkgkrapftnfdpstl
lpssldfwtypgslthpplyesvtwiickesisvsseqlaqfrsllsnvegdnavpmqhn
nrptqplkgrtvrasf
>d1huh__ 2.56.1.1.1 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme I}
dwgyddkngpeqwsklypiangnnqspvdiktsetkhdtslkpisvsynpatakeiinvg
hsfhvnfedndnrsvlkggpfsdsyrlfqfhfhwgstnehgsehtvdgvkysaelhvahw
nsakysslaeaaskadglavigvlmkvgeanpklqkvldalqaiktkgkrapftnfdpst
llpssldfwtypgslthpplyesvtwiickesisvsseqlaqfrsllsnvegdnavpmqh
nnrptqplkgrtvrasf
>e1hui.1a 7.1.1.1.2 Insulin {human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1hui.1b 7.1.1.1.2 Insulin {human (Homo sapiens)}
evnqhlcgselvealelvcgergffyepk
>d1huja_ 2.29.5.1.1 Inorganic pyrophosphatase {baker's yeast (Saccharomyces cerevisiae)}
tyttrqigakntleykvyiekdgkpvsafhdiplyadkennifnmvveiprwtnakleit
reetlnpiiqdtkkgklrfvrncfphhgyihnygafpqtwedpnvshpetkavgdndpid
vleigetiaytgqvkqvkalgimalldegetdwkviaidindplapklndiedvekyfpg
llratnewfriykipdgkpenqfafsgeaknkkyaldiikethdswkqliagkssdskgi
dltnvtlpdtptyskaasdaippaslkadapidksidkwff
>d1hujb_ 2.29.5.1.1 Inorganic pyrophosphatase {baker's yeast (Saccharomyces cerevisiae)}
tyttrqigakntleykvyiekdgkpvsafhdiplyadkennifnmvveiprwtnakleit
reetlnpiiqdtkkgklrfvrncfphhgyihnygafpqtwedpnvshpetkavgdndpid
vleigetiaytgqvkqvkalgimalldegetdwkviaidindplapklndiedvekyfpg
llratnewfriykipdgkpenqfafsgeaknkkyaldiikethdswkqliagkssdskgi
dltnvtlpdtptyskaasdaippaslkadapidksidkwff
>d1huka_ 2.29.5.1.1 Inorganic pyrophosphatase {baker's yeast (Saccharomyces cerevisiae)}
tyttrqigakntleykvyiekdgkpvsafhdiplyadkennifnmvveiprwtnakleit
keetlnpiiqdtkkgklrfvrncfphhgyihnygafpqtwedpnvshpetkavgdndpid
vleigetiaytgqvkqvkalgimalldegetdwkviaidindplapklndiedvekyfpg
llratnewfriykipdgkpenqfafsgeaknkkyaldiikethdswkqliagkssdskgi
dltnvtlpdtptyskaasdaippaslkadapidksidkwff
>d1hukb_ 2.29.5.1.1 Inorganic pyrophosphatase {baker's yeast (Saccharomyces cerevisiae)}
tyttrqigakntleykvyiekdgkpvsafhdiplyadkennifnmvveiprwtnakleit
keetlnpiiqdtkkgklrfvrncfphhgyihnygafpqtwedpnvshpetkavgdndpid
vleigetiaytgqvkqvkalgimalldegetdwkviaidindplapklndiedvekyfpg
llratnewfriykipdgkpenqfafsgeaknkkyaldiikethdswkqliagkssdskgi
dltnvtlpdtptyskaasdaippaslkadapidksidkwff
>d1hula_ 1.26.1.2.3 Interleukin-5 {human (Homo sapiens)}
iptsalvketlallsthrtllianetlripvpvhknhqlcteeifqgigtlesqtvqggt
verlfknlslikkyidgqkkkcgeerrrvnqfldylqeflgvmntewi
>d1hulb_ 1.26.1.2.3 Interleukin-5 {human (Homo sapiens)}
iptsalvketlallsthrtllianetlripvpvhknhqlcteeifqgigtlesqtvqggt
verlfknlslikkyidgqkkkcgeerrrvnqfldylqeflgvmntewi
>d1huma_ 4.7.1.1.6 Macrophage inflammatory protein 1-beta {human (Homo sapiens)}
apmgsdpptaccfsytarklprnfvvdyyetsslcsqpavvfqtkrskqvcadpseswvq
eyvydleln
>d1humb_ 4.7.1.1.6 Macrophage inflammatory protein 1-beta {human (Homo sapiens)}
apmgsdpptaccfsytarklprnfvvdyyetsslcsqpavvfqtkrskqvcadpseswvq
eyvydleln
>d1huna_ 4.7.1.1.6 Macrophage inflammatory protein 1-beta {human (Homo sapiens)}
apmgsdpptaccfsytarklprnfvvdyyetsslcsqpavvfqtkrskqvcadpseswvq
eyvydleln
>d1hunb_ 4.7.1.1.6 Macrophage inflammatory protein 1-beta {human (Homo sapiens)}
apmgsdpptaccfsytarklprnfvvdyyetsslcsqpavvfqtkrskqvcadpseswvq
eyvydleln
>d1hup_1 1.105.1.1.2 (88-111) Mannose-binding protein A {human (Homo sapiens)}
aaserkalqtemarikkwltfslg
>d1hup_2 4.105.1.1.4 (112-228) Mannose-binding protein A, lectin domain {human (Homo sapiens)}
kqvgnkffltngeimtfekvkalcvkfqasvatprnaaengaiqnlikeeaflgitdekt
egqfvdltgnrltytnwnegepnnagsdedcvlllkngqwndvpcstshlavcefpi
>d1hura_ 3.29.1.4.8 ADP-ribosylation factor 1 (ARF1) {human (Homo sapiens)}
gnifanlfkglfgkkemrilmvgldaagkttilyklklgeivttiptigfnvetveykni
sftvwdvggqdkirplwrhyfqntqglifvvdsndrervneareelmrmlaedelrdavl
lvfankqdlpnamnaaeitdklglhslrhrnwyiqatcatsgdglyegldwlsnqlrnqk
>d1hurb_ 3.29.1.4.8 ADP-ribosylation factor 1 (ARF1) {human (Homo sapiens)}
gnifanlfkglfgkkemrilmvgldaagkttilyklklgeivttiptigfnvetveykni
sftvwdvggqdkirplwrhyfqntqglifvvdsndrervneareelmrmlaedelrdavl
lvfankqdlpnamnaaeitdklglhslrhrnwyiqatcatsgdglyegldwlsnqlrnqk
>d1hus__ 1.65.1.1.1 Ribosomal protein S7 {(Bacillus stearothermophilus)}
rdvlpdpiynsklvtrlinkixidgkkskaqkilytafdiirertgkdpxevfeqalknv
xpvlevrarrvgganyqvpvevrpdrrvslglrwlvqyarlrnektxeerlaneixdaan
ntgaavkkredthkxaean
>e1hut.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>e1hut.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>d1huw__ 1.26.1.1.6 Growth hormone, somatotropin {human (Homo sapiens)}
fptiplsrladnawlradrlnqlafdtyqefeeayipkeqihsfwwnpqtslcpsesipt
psnkeetqqksnlellrisllliqswlepvqflrsvfanslvygasdsnvydllkdleeg
iqtlmgrleallknygllycfnkdmskvstylrtvqcrsvegscgf
>d1hva__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfcfhwgsldgqgsehtvdkkkyaaelhlvhwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d1hvc__ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtiriggqlkealldtgaddtvleemnlpgkwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnfggssgpqitlwqrplvtikig
gqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqydqilieicghkaigtvl
vgptpvniigrnlltqigctlnf
>d1hvd__ 1.55.1.1.5 Annexin V {human (Homo sapiens)}
vlrgtvtdfpgfdgradaetlrkamkglgtdeesiltlltsrsnaqrqeisaafktlfgr
dllddlkseltgkfeklivalmkpsrlydayelkhalkgagtnekvlteiiasrtpeelr
aikqvyeeeygssleddvvgdtsgyyqrmlvvllqanrdpdagideaqveqdaqalfqag
elkwgtdeekfitifgtrsvshlrkvfdkymtisgfqieetidretsgnleqlllavvks
irsipaylaetlyyamkgagtddhtlirvmvsrseidlfnirkefrknfatslysmikgd
tsgdykkallllc
>d1hve__ 1.55.1.1.5 Annexin V {human (Homo sapiens)}
lrgtvtdfpgfderadaetlrkamkglgtdeesiltlltsrsnaqrqeisaafktlfgrd
llddlkseltgkfqklivalmkpsrlydayelkhalkgagtnekvlteiiasrtpeelra
ikqvyeeeygssleddvvgdtsgyyqrmlvvllqanrdpdagideaqveqdaqalfqage
lkwgtdeekfitifgtrsvshlrkvfdkymtisgfqieetidretsgnleqlllavvksi
rsipaylaetlyyamkgagtddhtlirvmvsrseidlfnirkefrknfatslysmikgdt
sgdykkallllc
>d1hvf__ 1.55.1.1.5 Annexin V {human (Homo sapiens)}
vlrgtvtdfpgfdgradaetlrkamkglgtdeesiltlltsrsnaqrqeisaafktlfgr
dllddlkseltgkfqklivalmkpsrlydayelkhalkgagtnekvlteiiasrtpeelr
aikqvyeeeygssleddvvgdtsgyyqrmlvvllqanrdpdagideaqveqdaqalfqag
elkwgtdeekfitifgtrsvshlrkvfdkymtisgfqieetidretsgnleqlllavvks
irsipaylaetlyyamkgagtddhtlirvmvsrseidlfnirkefrknfatslysmikgd
tsgdykkallllc
>d1hvg__ 1.55.1.1.5 Annexin V {human (Homo sapiens)}
vlrgtvtdfpgfderadaetlrkamkglgtdeesiltlltsrsnaqrqeisaafktlfgr
dllddlkseltgkfqklivalmkpsrlydayelkhalkgagtnekvlteiiasrtpeelr
aikqvyeeeygssleddvvgdtsgyyqrmlvvllqanrdpdagideaqveqdaqalfqag
elkwgtdeekfitifgtrsvshlrkvfdkymtisgfqieetidretsgnleqlllavvks
irsipaylaetlyyamkgagtddhtlirvmvsrseidlfnirkefrknfatslysmikgd
tsgdykkallllc
>d1hvia_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hvib_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hvja_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hvjb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hvka_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hvkb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hvla_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hvlb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hvq__ 3.1.1.5.1 Hevamine A (chitinase/lysozyme) {Para rubber tree (Hevea brasiliensis)}
ggiaiywgqngnegtltqtcstrkysyvniaflnkfgngqtpqinlaghcnpaaggctiv
sngirscqiqgikvmlslgggigsytlasqadaknvadylwnnflggksssrplgdavld
gidfdiehgstlywddlarylsayskqgkkvyltaapqcpfpdrylgtalntglfdyvwv
qfynnppcqyssgninniinswnrwttsinagkiflglpaapeaagsgyvppdvlisril
peikkspkyggvmlwskfyddkngysssildsv
>d1hvra_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigatlnf
>d1hvrb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigatlnf
>d1hvsa_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpaniigrnlltqigctlnf
>d1hvsb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpaniigrnlltqigctlnf
>d1hwa__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1hwga_ 1.26.1.1.6 Growth hormone, somatotropin {human (Homo sapiens)}
fptiplsrlfdnamlrahrlhqlafdtyqefeeayipkeqkysflqnpqtslcfsesipt
psnreetqqksnlellrisllliqswlepvqflrsvfanslvygasdsnvydllkdleeg
iqtlmgrledgsprtgqifkqtyskfdtnshnddallknygllycfrkdmdkvetflriv
qcrsvegscg
>d1hwgb1 2.1.2.1.7 (32-130) Growth hormone receptor {human (Homo sapiens)}
epkftkcrsperetfschwtdevhhgtknlgpiqlfytrrntqewtqewkecpdyvsage
nscyfnssftsiwipycikltsnggtvdekcfsvdeivq
>d1hwgb2 2.1.2.1.7 (131-234) Growth hormone receptor {human (Homo sapiens)}
pdppialnwtllnvsltgihadiqvrweaprnadiqkgwmvleyelqykevnetkwkmmd
pilttsvpvyslkvdkeyevrvrskqrnsgnygefsevlyvtlp
>d1hwgc1 2.1.2.1.7 (32-130) Growth hormone receptor {human (Homo sapiens)}
epkftkcrsperetfschwtdevhhgtknlgpiqlfytrrntqewtqewkecpdyvsage
nscyfnssftsiwipycikltsnggtvdekcfsvdeivq
>d1hwgc2 2.1.2.1.7 (131-237) Growth hormone receptor {human (Homo sapiens)}
pdppialnwtllnvsltgihadiqvrweaprnadiqkgwmvleyelqykevnetkwkmmd
pilttsvpvyslkvdkeyevrvrskqrnsgnygefsevlyvtlpqms
>d1hwha_ 1.26.1.1.6 Growth hormone, somatotropin {human (Homo sapiens)}
fptiplsrlfdnamlrahrlhqlafdtyqefeeayipkeqkysflqnpqtslcfsesipt
psnreetqqksnlellrisllliqswlepvqflrsvfanslvygasdsnvydllkdleer
iqtlmgrledgsprtgqifkqtyskfdtnshnddallknygllycfrkdmdkvetflriv
qcrsvegscgf
>d1hwhb1 2.1.2.1.7 (32-130) Growth hormone receptor {human (Homo sapiens)}
epkftkcrsperetfschwtdevhhgtknlgpiqlfytrrntqewtqewkecpdyvsage
nscyfnssftsiwipycikltsnggtvdekcfsvdeivq
>d1hwhb2 2.1.2.1.7 (131-237) Growth hormone receptor {human (Homo sapiens)}
pdppialnwtllnvsltgihadiqvrweaprnadiqkgwmvleyelqykevnetkwkmmd
pilttsvpvyslkvdkeyevrvrskqrnsgnygefsevlyvtlpqms
>d1hxba_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hxbb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>e1hxe.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlkegqpsvlqvvnlpiverpvckdstriritdnmfca
gykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfythvfrlkk
wiqkvidq
>e1hxe.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
dcglrplfekksledkterellesyi
>e1hxf.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidq
>e1hxf.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
dcglrplfekksledkterellesyi
>d1hxn__ 2.49.1.1.1 Hemopexin, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
estrcdpdlvlsamvsdnhgatyvfsgshywrldtnrdgwhswpiahqwpqgpstvdaaf
swedklyliqdtkvyvfltkggytlvngypkrlekelgsppvisleavdaafvcpgssrl
himagrrlwwldlksgaqatwtelpwphekvdgalcmekplgpnscstsgpnlylihgpn
lycyrhvdklnaaknlpqpqrvsrllgcth
>d1hxpa1 4.9.1.2.1 (2-177) Galactose-1-phosphate uridylyltransferase {(Escherichia coli)}
tqfnpvdhphrrynpltgqwilvsphrakrpwegaqetpakqvlpahdpdcflcagnvrv
tgdknpdytgtyvftndfaalmsdtpdapeshdplmrcqsargtsrvicfspdhsktlpe
lsvaalteivktwqeqtaelgktypwvqvfenkgaamgcsnphphgqiwansflpn
>d1hxpa2 4.9.1.2.1 (178-348) Galactose-1-phosphate uridylyltransferase {(Escherichia coli)}
eaeredrlqkeyfaeqkspmlvdyvqreladgsrtvvetehwlavvpywaawpfetlllp
kahvlritdltdaqrsdlalalkkltsrydnlfqcsfpysmgwhgapfngeenqhwqlha
hfyppllrsatvrkfmvgyemlaetqrdltaeqaaerlravsdihfresgv
>d1hxpb1 4.9.1.2.1 (2-177) Galactose-1-phosphate uridylyltransferase {(Escherichia coli)}
tqfnpvdhphrrynpltgqwilvsphrakrpwegaqetpakqvlpahdpdcflcagnvrv
tgdknpdytgtyvftndfaalmsdtpdapeshdplmrcqsargtsrvicfspdhsktlpe
lsvaalteivktwqeqtaelgktypwvqvfenkgaamgcsnphphgqiwansflpn
>d1hxpb2 4.9.1.2.1 (178-346) Galactose-1-phosphate uridylyltransferase {(Escherichia coli)}
eaeredrlqkeyfaeqkspmlvdyvqreladgsrtvvetehwlavvpywaawpfetlllp
kahvlritdltdaqrsdlalalkkltsrydnlfqcsfpysmgwhgapfngeenqhwqlha
hfyppllrsatvrkfmvgyemlaetqrdltaeqaaerlravsdihfres
>d1hxqa1 4.9.1.2.1 (2-177) Galactose-1-phosphate uridylyltransferase {(Escherichia coli)}
tqfnpvdhphrrynpltgqwilvsphrakrpwqgaqetpakqvlpahdpdcflcagnvrv
tgdknpdytgtyvftndfaalmsdtpdapeshdplmrcqsargtsrvicfspdhsktlpe
lsvaalteivktwqeqtaelgktypwvqvfenkgaamgcsnphphgqiwansflpn
>d1hxqa2 4.9.1.2.1 (178-348) Galactose-1-phosphate uridylyltransferase {(Escherichia coli)}
eaeredrlqkeyfaeqkspmlvdyvqreladgsrtvvetehwlavvpywaawpfetlllp
kahvlritdltdaqrsdlalalkkltsrydnlfqcsfpysmgwhgapfngeanqhwqlha
hfyppllrsatvrkfmvgyemlaetqrdltaeqaaerlravsdihfresgv
>d1hxqb1 4.9.1.2.1 (2-177) Galactose-1-phosphate uridylyltransferase {(Escherichia coli)}
tqfnpvdhphrrynpltgqwilvsphrakrpwqgaqetpakqvlpahdpdcflcagnvrv
tgdknpdytgtyvftndfaalmsdtpdapeshdplmrcqsargtsrvicfspdhsktlpe
lsvaalteivktwqeqtaelgktypwvqvfenkgaamgcsnphphgqiwansflpn
>d1hxqb2 4.9.1.2.1 (178-346) Galactose-1-phosphate uridylyltransferase {(Escherichia coli)}
eaeredrlqkeyfaeqkspmlvdyvqreladgsrtvvetehwlavvpywaawpfetlllp
kahvlritdltdaqrsdlalalkkltsrydnlfqcsfpysmgwhgapfngeenqhwqlha
hfyppllrsatvrkfmvgyemlaetqrdltaeqaaerlravsdihfres
>d1hxwa_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemnlpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hxwb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwqrplvtikiggqlkealldtgaddtvleemnlpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1hyha1 3.22.1.5.5 (21-166) L-2-hydroxyisocapronate dehydrogenase, L-HICDH {(Lactobacillus confusus)}
arkigiiglgnvgaavahgliaqgvaddyvfidaneakvkadqidfqdamanleahgniv
indwaaladadvvistlgniklqqdnptgdrfaelkftssmvqsvgtnlkesgfhgvlvv
isnpvdvitalfqhvtgfpahkvigt
>d1hyha2 4.100.1.1.5 (167-329) L-2-hydroxyisocapronate dehydrogenase, L-HICDH {(Lactobacillus confusus)}
gtlldtarmqravgeafdldprsvsgynlgehgnsqfvawstvrvmgqpivtladagdid
laaieeearkggftvlngkgytsygvatsairiakavmadahaelvvsnrrddmgmylsy
paiigrdgvlaettldlttdeqekllqsrdyiqqrfdeivdtl
>d1hyhb1 3.22.1.5.5 (21-166) L-2-hydroxyisocapronate dehydrogenase, L-HICDH {(Lactobacillus confusus)}
arkigiiglgnvgaavahgliaqgvaddyvfidaneakvkadqidfqdamanleahgniv
indwaaladadvvistlgniklqqdnptgdrfaelkftssmvqsvgtnlkesgfhgvlvv
isnpvdvitalfqhvtgfpahkvigt
>d1hyhb2 4.100.1.1.5 (167-326) L-2-hydroxyisocapronate dehydrogenase, L-HICDH {(Lactobacillus confusus)}
gtlldtarmqravgeafdldprsvsgynlgehgnsqfvawstvrvmgqpivtladagdid
laaieeearkggftvlngkgytsygvatsairiakavmadahaelvvsnrrddmgmylsy
paiigrdgvlaettldlttdeqekllqsrdyiqqrfdeiv
>d1hyhc1 3.22.1.5.5 (21-166) L-2-hydroxyisocapronate dehydrogenase, L-HICDH {(Lactobacillus confusus)}
arkigiiglgnvgaavahgliaqgvaddyvfidaneakvkadqidfqdamanleahgniv
indwaaladadvvistlgniklqqdnptgdrfaelkftssmvqsvgtnlkesgfhgvlvv
isnpvdvitalfqhvtgfpahkvigt
>d1hyhc2 4.100.1.1.5 (167-329) L-2-hydroxyisocapronate dehydrogenase, L-HICDH {(Lactobacillus confusus)}
gtlldtarmqravgeafdldprsvsgynlgehgnsqfvawstvrvmgqpivtladagdid
laaieeearkggftvlngkgytsygvatsairiakavmadahaelvvsnrrddmgmylsy
paiigrdgvlaettldlttdeqekllqsrdyiqqrfdeivdtl
>d1hyhd1 3.22.1.5.5 (21-166) L-2-hydroxyisocapronate dehydrogenase, L-HICDH {(Lactobacillus confusus)}
arkigiiglgnvgaavahgliaqgvaddyvfidaneakvkadqidfqdamanleahgniv
indwaaladadvvistlgniklqqdnptgdrfaelkftssmvqsvgtnlkesgfhgvlvv
isnpvdvitalfqhvtgfpahkvigt
>d1hyhd2 4.100.1.1.5 (167-329) L-2-hydroxyisocapronate dehydrogenase, L-HICDH {(Lactobacillus confusus)}
gtlldtarmqravgeafdldprsvsgynlgehgnsqfvawstvrvmgqpivtladagdid
laaieeearkggftvlngkgytsygvatsairiakavmadahaelvvsnrrddmgmylsy
paiigrdgvlaettldlttdeqekllqsrdyiqqrfdeivdtl
>d1hyla_ 2.35.1.2.9 HL collagenase {Common cattle grub (Hypoderma lineatum)}
iingyeaytglfpyqaglditlqdqrrvwcggslidnkwiltaahcvhdavsvvvylgsa
vqyegeavvnseriishsmfnpdtylndvalikiphveytdniqpirlpsgeelnnkfen
iwatvsgwgqsntdtvilqytynlvidndrcaqeyppgiivesticgdtsdgkspcfgds
ggpfvlsdknlligvvsfvsgagcesgkpvgfsrvtsymdwiqqntgikf
>d1hylb_ 2.35.1.2.9 HL collagenase {Common cattle grub (Hypoderma lineatum)}
iingyeaytglfpyqaglditlqdqrrvwcggslidnkwiltaahcvhdavsvvvylgsa
vqyegeavvnseriishsmfnpdtylndvalikiphveytdniqpirlpsgeelnnkfen
iwatvsgwgqsntdtvilqytynlvidndrcaqeyppgiivesticgdtsdgkspcfgds
ggpfvlsdknlligvvsfvsgagcesgkpvgfsrvtsymdwiqqntgikf
>e1hym.1a 4.22.1.1.3 Trypsin inhibitor V {pumpkin (Cucurbita maxima)}
xsscpgksswphlvgvggsvakaiierqnpnvkavileegtpvtk
>e1hym.1b 4.22.1.1.3 Trypsin inhibitor V {pumpkin (Cucurbita maxima)}
dfrcnrvriwvnkrglvvspprig
>d1hyp__ 1.47.1.1.1 Soybean hydrophobic protein {soybean (Glycine max)}
pscpdlsiclnilggslgtvddccaligglgdieaivclciqlralgilnlnrnlqliln
scgrsypsnatcprt
>d1hyt_1 1.57.1.1.2 (156-316) Thermolysin {(Bacillus thermoproteolyticus)}
iyqnesgaineaisdifgtlvefyanknpdweigedvytpgisgdslrsmsdpakygdpd
hyskrytgtqdnggvhinsgiinkaaylisqggthygvsvvgigrdklgkifyraltqyl
tptsnfsqlraaavqsatdlygstsqevasvkqafdavgvk
>d1hyt_2 4.52.1.2.2 (1-155) Thermolysin {(Bacillus thermoproteolyticus)}
itgtstvgvgrgvlgdqkninttystyyylqdntrgdgiftydakyrttlpgslwadadn
qffasydapavdahyyagvtydyyknvhnrlsydgnnaairssvhysqgynnafwngsem
vygdgdgqtfiplsggidvvahelthavtdytagl
>d1hyxh1 2.1.1.1.85 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab 6D9 (mouse), kappa L chain}
evkllesggglvkpggslklscaasgftfsnyamswvrqtpekrlewvvsissggsiyyl
dsvkgrftvsrdnarnilylqmtslrsedtamyfcarvshydgsrdwyfdvwgagtsvtv
ss
>d1hyxh2 2.1.1.2.87 (114-215) Immunoglobulin (constant domains of L and H chains) {Fab 6D9 (mouse). kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpsstwpsetvtcnvahpasstkvdkkivprdc
>d1hyxl1 2.1.1.1.85 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab 6D9 (mouse), kappa L chain}
elvmtqtplslpvslgdqasiscrssqtivhsngdtyldwflqkpgqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyycfqgshvpptfgggtkleik
>d1hyxl2 2.1.1.2.87 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab 6D9 (mouse). kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1hyyh1 2.1.1.1.85 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab 6D9 (mouse), kappa L chain}
evkllesggglvkpggslklscaasgftfsnyamswvrqtpekrlewvvsissggsiyyl
dsvkgrftvsrdnarnilylqmtslrsedtamyfcarvshydgsrdwyfdvwgagtsvtv
ss
>d1hyyh2 2.1.1.2.87 (114-215) Immunoglobulin (constant domains of L and H chains) {Fab 6D9 (mouse). kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpsstwpsetvtcnvahpasstkvdkkivprdc
>d1hyyl1 2.1.1.1.85 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab 6D9 (mouse), kappa L chain}
elvmtqtplslpvslgdqasiscrssqtivhsngdtyldwflqkpgqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyycfqgshvpptfgggtkleik
>d1hyyl2 2.1.1.2.87 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab 6D9 (mouse). kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1i1b__ 2.31.1.2.1 Interleukin-1beta {human (Homo sapiens)}
vrslnctlrdsqqkslvmsgpyelkalhlqgqdmeqqvvfsmsfvqgeesndkipvalgl
keknlylscvlkddkptlqlesvdpknypkkkmekrfvfnkieinnklefesaqfpnwyi
stsqaenmpvflggtkggqditdftmqfvss
>d1iaa__ 4.52.1.4.1 Astacin {The european fresh water crayfish (Astacus astacus L.)}
aailgdeylwsggvipytfagvsgadqsailsgmqeleektcirfvprttesdyveifts
gsgcwsyvgrisgaqqvslqangcvyhgtiihelmhaigfyhehtrmdrdnyvtinyqnv
dpsmtsnfdidtysryvgedyqyysimhygkysfsiqwgvletivplqngidltdpydka
hmlqtdanqinnlytnecsl
>d1iab__ 4.52.1.4.1 Astacin {The european fresh water crayfish (Astacus astacus L.)}
aailgdeylwsggvipytfagvsgadqsailsgmqeleektcirfvprttesdyveifts
gsgcwsyvgrisgaqqvslqangcvyhgtiihelmhaigfyhehtrmdrdnyvtinyqnv
dpsmtsnfdidtysryvgedyqyysimhygkysfsiqwgvletivplqngidltdpydka
hmlqtdanqinnlytnecsl
>d1iac__ 4.52.1.4.1 Astacin {The european fresh water crayfish (Astacus astacus L.)}
aailgdeylwsggvipytfagvsgadqsailsgmqeleektcirfvprttesdyveifts
gsgcwsyvgrisgaqqvslqangcvyhgtiihelmhaigfyhehtrmdrdnyvtinyqnv
dpsmtsnfdidtysryvgedyqyysimhygkysfsiqwgvletivplqngidltdpydka
hmlqtdanqinnlytnecsl
>d1iad__ 4.52.1.4.1 Astacin {The european fresh water crayfish (Astacus astacus L.)}
aailgdeylwsggvipytfagvsgadqsailsgmqeleektcirfvprttesdyveifts
gsgcwsyvgrisgaqqvslqangcvyhgtiihelmhaigfyhehtrmdrdnyvtinyqnv
dpsmtsnfdidtysryvgedyqyysimhygkysfsiqwgvletivplqngidltdpydka
hmlqtdanqinnlytnecsl
>d1iae__ 4.52.1.4.1 Astacin {The european fresh water crayfish (Astacus astacus L.)}
aailgdeylwsggvipytfagvsgadqsailsgmqeleektcirfvprttesdyveifts
gsgcwsyvgrisgaqqvslqangcvyhgtiihelmhaigfyhehtrmdrdnyvtinyqnv
dpsmtsnfdidtysryvgedyqyysimhygkysfsiqwgvletivplqngidltdpydka
hmlqtdanqinnlytnecsl
>d1iag__ 4.52.1.5.1 Snake venom metalloprotease {Adamalysin II: Eastern diamondback rattlesnake (Crotalus adamanteus)}
nlpqryielvvvadrrvfmkynsdlniirtrvheivniinkfyrslnirvsltdleiwsg
qdfitiqssssntlnsfgewrervlliwkrhdnaqlltainfegkiigkaytssmcnprs
svgivkdhspinllvavtmahelghnlgmehdgkdclrgaslcimrpgltpgrsyefsdd
smgyyqkflnqykpqcilnkp
>d1iaih1 2.1.1.1.61 (1-121) Immunoglobulin (variable domains of L and H chains) {Fab 730.1.4 (mouse), kappa L chain}
qiqlvqsgpelkkpgetvkisckasgytftnygmnwvkqapgkglkwmawintytgepty
addfkgrfafsletsastaylqinnlknedtatyfcardgyyenyyamdywgqgtsvtvs
s
>d1iaih2 2.1.1.2.65 (122-219) Immunoglobulin (constant domains of L and H chains) {Fab 730.1.4 (mouse), kappa L chain}
akttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsd
lytlsssvtvtssttpsqsitcnvahpasstkvdkkid
>d1iaii1 2.1.1.1.62 (1-121) Immunoglobulin (variable domains of L and H chains) {Fab 409.5.3 (mouse), kappa L chain}
evklqesggglvqpggsmklscvasgftfnnywmswvrqspekglewvaeirlnsdnfat
hyaesvkgkfiisrddsksrlylqmnslraedtgiyycvlrplfyyavdywgqgtsvtvs
s
>d1iaii2 2.1.1.2.66 (122-218) Immunoglobulin (constant domains of L and H chains) {Fab 409.5.3 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpstwrpsetvtcnvahpasstkvdkki
>d1iail1 2.1.1.1.61 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab 730.1.4 (mouse), kappa L chain}
divmtqshkfmstsvgdrvsitckasqdvstavawyqqkpgqspklliysasyqytgvpd
rftgsgsrtdftftinsvqaedlavyychqhystpftfgsgtkleikr
>d1iail2 2.1.1.2.65 (109-214) Immunoglobulin (constant domains of L and H chains) {Fab 730.1.4 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1iaim1 2.1.1.1.62 (1-109) Immunoglobulin (variable domains of L and H chains) {Fab 409.5.3 (mouse), kappa L chain}
diqltqspafmaaspgekvtitcsvsssisssnlhwyqqksetspkpwiygtsnlasgvp
vrfsgsgsgtsysltissmeaedaatyycqqwnsypytfgggtkleikr
>d1iaim2 2.1.1.2.66 (110-215) Immunoglobulin (constant domains of L and H chains) {Fab 409.5.3 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1iaka1 2.1.1.2.116 (82-181) Class II MHC, C-terminal domains of alpha and beta chains {(human hla i-ak)}
atneapqatvfpkspvllgqpntlicfvdnifppvinitwlrnsksvtdgvyetsffvnr
dysfhklsyltfipsdddiydckvehwgleepvlkhwepe
>d1iaka2 4.15.1.1.5 (3-81) MHC class II, N-terminal domains of alpha and beta chains {(human hla i-ak)}
adhvgsygitvyqspgdigqytfefdgdelfyvdldkketvwmlpefaqlrrfepqgglq
niatgkhnleiltkrsnstp
>d1iakb1 2.1.1.2.116 (93-190) Class II MHC, C-terminal domains of alpha and beta chains {(human hla i-ak)}
rleqpsvvislsrtealnhhntlvcsvtdfypakikvrwfrngqeetvgvsstqlirngd
wtfqvlvmlemtprrgevytchvehpsltspitvewra
>d1iakb2 4.15.1.1.5 (5-92) MHC class II, N-terminal domains of alpha and beta chains {(human hla i-ak)}
gsfvhqfqpfcyftngtqrirlviryiynreeyvrfdsdvgeyravtelgrpdaeywnkq
ylertraeldtvcrhnyektetptslr
>d1iam_1 2.1.1.3.2 (83-185) The second domain of intercellular cell adhesion molecule-1 (ICAM-1) {human (Homo sapiens)}
ywtpervelaplpswqpvgkqltlrcqveggapraqltvvllrgekelkrepavgepaev
tttvlvrrdhhgaqfscrteldlrpqglelfentsapyqlqtf
>d1iam_2 2.1.1.4.2 (1-82) N-terminal domain of intracellular adhesion molecule-1, ICAM-1 {human (Homo sapiens)}
qtsvspskvilprggsvlvtcstscdqpkllgietplpkkelllpgnnrkvyelsnvqed
sqpmcysncpdgqstaktfltv
>d1ian__ 5.1.1.1.9 MAP kinase p38 {human (Homo sapiens)}
rptfyrqelnktiwevperyqnlspvgsgaygsvcaafdtktglrvavkklsrpfqsiih
akrtyrelrllkhmkhenviglldvftparsleefndvylvthlmgadlnnivkcqkltd
dhvqfliyqilrglkyihsadiihrdlkpsnlavnedcelkildfglarhtddemtgyva
trwyrapeimlnwmhynqtvdiwsvgcimaelltgrtlfpgtdhidqlklilrlvgtpga
ellkkissesarnyiqsltqmpkmnfanvfiganplavdllekmlvldsdkritaaqala
hayfaqyhdpddepvadpydqsfesrdllidewksltydevisfvppp
>d1iba__ 4.55.1.1.1 Glucose permease domain IIB {(Escherichia coli)}
mapalvaafggkenitnldacitrlrvsvadvskvdqaglkklgaagvvvagsgvqaifg
tksdnlktemdeyirnfg
>e1ibc.1a 3.11.1.1.2 Interleukin-1beta converting enzyme (a cysteine protease) {Human (Homo sapiens)}
gnvklcsleeaqriwkqksaeiypimdkssrtrlaliicneefdsiprrtgaevditgmt
mllqnlgysvdvkknltasdmtteleafahrpehktsdstflvfmshgiregicgkkhse
qvpdilqlnaifnmlntkncpslkdkpkviiiqacrgdspgvvwfkd
>e1ibc.1b 3.11.1.1.2 Interleukin-1beta converting enzyme (a cysteine protease) {Human (Homo sapiens)}
aikkahiekdfiafcsstpdnvswrhptmgsvfigrliehmqeyacscdveeifrkvrfs
feqpagraqmpttervtltrcfylfpgh
>d1ibea_ 1.1.1.1.17 Hemoglobin, alpha-chain {horse (Equus caballus)}
vlsaadktnvkaawskvgghagefgaealermflgfpttktyfphfdlshgsaqvkahgk
kvgdaltlavghlddlpgalsdlsnlhahklrvdpvnfkllshcllstlavhlpndftpa
vhasldkflssvstvltskyr
>d1ibeb_ 1.1.1.1.28 Hemoglobin, beta-chain {horse (Equus caballus)}
vqlsgeekaavlalwdkvneeevggealgrllvvypwtqrffdsfgdlsnpgavmgnpkv
kahgkkvlhsfgegvhhldnlkgtfaalselhcdklhvdpenfrllgnvlvvvlarhfgk
dftpelqasyqkvvagvanalahkyh
>d1ibgh1 2.1.1.1.56 (2-113) Immunoglobulin (variable domains of L and H chains) {Fab 40-50 (mouse), kappa L chain}
vhlvqsgpglvapsqslsitctvsgfslttygvhwfrqppgkglewlgliwaggntdyns
almsrlsinkdnsksqvflkmnslqaddtamyycarfrfasyydyavdywgqgtsvtvss
>d1ibgh2 2.1.1.2.61 (114-223) Immunoglobulin (constant domains of L and H chains) {Fab 40-50 (mouse), kappa L chain}
akttppsvyplapgcgdttgssvtsgclvkgyfpepvtvtwnsgslsssvhtfpallqsg
lytmsssvtvpsstwpsqtvtcsvahpassttvdkkl
>d1ibgl1 2.1.1.1.56 (2-107) Immunoglobulin (variable domains of L and H chains) {Fab 40-50 (mouse), kappa L chain}
ivltqspaslavslgqratiscrasksvstsgyshihwyqqkpgqppklliylasilesg
vparfsgsgsgtdftlnihpveeedaatyycqhsreypltfgagtelelk
>d1ibgl2 2.1.1.2.61 (108-214) Immunoglobulin (constant domains of L and H chains) {Fab 40-50 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1ic1a1 2.1.1.3.2 (83-190) The second domain of intercellular cell adhesion molecule-1 (ICAM-1) {human (Homo sapiens)}
ywtpervelaplpswqpvgknltlrcqveggapranltvvllrgekelkrepavgepaev
tttvlvrrdhhganfscrteldlrpqglelfentsapyqlqtfvlpat
>d1ic1a2 2.1.1.4.2 (1-82) N-terminal domain of intracellular adhesion molecule-1, ICAM-1 {human (Homo sapiens)}
qtsvspskvilprggsvlvtcstscdqpkllgietplpkkelllpgnnrkvyelsnvqed
sqpmcysncpdgqstaktfltv
>d1ic1b1 2.1.1.3.2 (83-190) The second domain of intercellular cell adhesion molecule-1 (ICAM-1) {human (Homo sapiens)}
ywtpervelaplpswqpvgknltlrcqveggapranltvvllrgekelkrepavgepaev
tttvlvrrdhhganfscrteldlrpqglelfentsapyqlqtfvlpat
>d1ic1b2 2.1.1.4.2 (1-82) N-terminal domain of intracellular adhesion molecule-1, ICAM-1 {human (Homo sapiens)}
qtsvspskvilprggsvlvtcstscdqpkllgietplpkkelllpgnnrkvyelsnvqed
sqpmcysncpdgqstaktfltv
>d1ica__ 7.3.6.3.2 Defensin A {Flesh fly (Phormia terranovae) larva}
atcdllsgtginhsacaahcllrgnrggycngkgvcvcrn
>e1ice.1a 3.11.1.1.2 Interleukin-1beta converting enzyme (a cysteine protease) {Human (Homo sapiens)}
gnvklcsleeaqriwkqksaeiypimdkssrtrlaliicneefdsiprrtgaevditgmt
mllqnlgysvdvkknltasdmtteleafahrpehktsdstflvfmshgiregicgkkhse
qvpdilqlnaifnmlntkncpslkdkpkviiiqacrgdspgvvwfkd
>e1ice.1b 3.11.1.1.2 Interleukin-1beta converting enzyme (a cysteine protease) {Human (Homo sapiens)}
aikkahiekdfiafcsstpdnvswrhptmgsvfigrliehmqeyacscdveeifrkvrfs
feqpdgraqmpttervtltrcfylfpgh
>d1icm__ 2.45.1.2.2 Intestinal fatty acid binding protein {rat (Rattus rattus)}
afdgtwkvdrnenyekfmekmginvvkrklgahdnlkltitqegnkftvkessnfrnidv
vfelgvdfaysladgteltgtwtmegnklvgkfkrvdngkeliavreisgneliqtytye
gveakrifkke
>d1icn__ 2.45.1.2.2 Intestinal fatty acid binding protein {rat (Rattus rattus)}
afdgtwkvdrnenyekfmekmginvvkrklgahdnlkltitqegnkftvkessnfrnidv
vfelgvdfaysladgteltgtwtmegnklvgkfkrvdngkeliavqeisgneliqtytye
gveakrifkke
>d1icwa_ 4.7.1.1.1 Interleukin-8, IL-8 {human (Homo sapiens)}
elrcqciktyskpfhpkfikelrviesgphcantciivklsdgrelaldpkenwvqrvve
kflkraens
>d1icwb_ 4.7.1.1.1 Interleukin-8, IL-8 {human (Homo sapiens)}
cqciktyskpfhpkfikelrviesgphcantciivklsdgrelaldpkenwvqrvvekfl
kraens
>d1idaa_ 2.38.1.1.3 Human immunodeficiency virus type 2 protease {HIV-2 (rod isolate)}
pqfslwkrpvvtayiegqpvevlldtgaddsivagielgnnyspkivggiggfintkeyk
nveievlnkkvratimtgdtpinifgrniltalgmslnl
>d1idab_ 2.38.1.1.3 Human immunodeficiency virus type 2 protease {HIV-2 (rod isolate)}
pqfslwkrpvvtayiegqpvevlldtgaddsivagielgnnyspkivggiggfintkeyk
nveievlnkkvratimtgdtpinifgrniltalgmslnl
>d1idba_ 2.38.1.1.3 Human immunodeficiency virus type 2 protease {HIV-2 (rod isolate)}
pqfslwkrpvvtayiegqpvevlldtgaddsivagielgnnyspkivggiggfintkeyk
nveievlnkkvratimtgdtpinifgrniltalgmslnl
>d1idbb_ 2.38.1.1.3 Human immunodeficiency virus type 2 protease {HIV-2 (rod isolate)}
pqfslwkrpvvtayiegqpvevlldtgaddsivagielgnnyspkivggiggfintkeyk
nveievlnkkvratimtgdtpinifgrniltalgmslnl
>d1idc__ 3.65.1.1.5 Isocitrate dehydrogenase {(Escherichia coli)}
skvvvpaqgkkitlqngklnvpenpiipyiegdgigvdvtpamlkvvdaavekaykgerk
iswmeiytgekstqvygqdvwlpaetldlireyrvaikgplttpvgggirslnvalrqel
dlyiclrpvryyqgtpspvkhpeltdmvifrensediyagiewkadsadaekvikflree
mgvkkirfpehcgigikpcseegtkrlvraaieyaiandrdsvtlvhmgnimkftegafk
dwgyqlareefggelidggpwlkvknpntgkeivikdviadaflqqillrpaeydviacm
nlngdyisdalaaqvggigiapganigdecalfeathgtapkyagqdkvnpgsiilsaem
mlrhmgwteaadlivkgmegainaktvtydferlmdgakllkcsefgdaiienm
>d1idd__ 3.65.1.1.5 Isocitrate dehydrogenase {(Escherichia coli)}
skvvvpaqgkkitlqngklnvpenpiipyiegdgigvdvtpamlkvvdaavekaykgerk
iswmeiytgekstqvygqdvwlpaetldlireyrvaikgplttpvgggirslnvalrqel
dlyiclrpvryyqgtpspvkhpeltdmvifrensedifagiewkadsadaekvikflree
mgvkkirfpehcgigikpcseegtkrlvraaieyaiandrdsvtlvhkgnimkftegafk
dwgyqlareefggelidggpwlkvknpntgkeivikdviadaflqqillrpaeydviacm
nlngdyisdalaaqvggigiapganigdecalfeathgtapkyagqdkvnpgsiilsaem
mlrhmgwteaadlivkgmegainaktvtydferlmdgakllkcsefgdaiienm
>d1ide__ 3.65.1.1.5 Isocitrate dehydrogenase {(Escherichia coli)}
skvvvpaqgkkitlqngklnvpenpiipyiegdgigvdvtpamlkvvdaavekaykgerk
iswmeiytgekstqvygqdvwlpaetldlireyrvaikgplttpvgggirslnvalrqel
dlyiclrpvryyqgtpspvkhpeltdmvifrensedifagiewkadsadaekvikflree
mgvkkirfpehcgigikpcseegtkrlvraaieyaiandrdsvtlvhkgnimkftegafk
dwgyqlareefggelidggpwlkvknpntgkeivikdviadaflqqillrpaeydviacm
nlngdyisdalaaqvggigiapganigdecalfeathgtapkyagqdkvnpgsiilsaem
mlrhmgwteaadlivkgmegainaktvtydferlmdgakllkcsefgdaiienm
>d1idf__ 3.65.1.1.5 Isocitrate dehydrogenase {(Escherichia coli)}
skvvvpaqgkkitlqngklnvpenpiipyiegdgigvdvtpamlkvvdaavekaykgerk
iswmeiytgekstqvygqdvwlpaetldlireyrvaikgplttpvgggirslnvalrqel
dlyiclrpvryyqgtpspvkhpeltdmvifrensediyagiewkadsadaekvikflree
mgvkkirfpehcgigikpcseegtkrlvraaieyaiandrdsvtlvhmgnimkftegafk
dwgyqlareefggelidggpwlkvknpntgkeivikdviadaflqqillrpaeydviacm
nlngdyisdalaaqvggigiapganigdecalfeathgtapkyagqdkvnpgsiilsaem
mlrhmgwteaadlivkgmegainaktvtydferlmdgakllkcsefgdaiienm
>d1idja_ 2.62.1.2.1 Pectin lyase A {(Aspergillus niger)}
vgvsgsaegfaegvtgggdatpvypdtidelvsylgddearvivltktfdftdsegtttg
tgcapwgtasacqvaidqddwcenyepdapsvsveyynagvlgitvtsnksligegssga
ikgkglrivsgaeniiiqniavtdinpkyvwggdaitlddcdlvwidhvttarigrqhyv
lgtsadnrvsltnnyidgvsdysatcdgyhywgiyldgdadlvtmkgnyiyhtsgrspkv
qdntllhcvnnyfydisghafeigeggyvlaegnvfqnvdtvletyegaaftvpsttage
vcstylgrdcvingfgcsgtfsedstsflsdfegkniasasaytsvasrvvanagqgnl
>d1idjb_ 2.62.1.2.1 Pectin lyase A {(Aspergillus niger)}
vgvsgsaegfaegvtgggdatpvypdtidelvsylgddearvivltktfdftdsegtttg
tgcapwgtasacqvaidqddwcenyepdapsvsveyynagvlgitvtsnksligegssga
ikgkglrivsgaeniiiqniavtdinpkyvwggdaitlddcdlvwidhvttarigrqhyv
lgtsadnrvsltnnyidgvsdysatcdgyhywgiyldgdadlvtmkgnyiyhtsgrspkv
qdntllhcvnnyfydisghafeigeggyvlaegnvfqnvdtvletyegaaftvpsttage
vcstylgrdcvingfgcsgtfsedstsflsdfegkniasasaytsvasrvvanagqgnl
>d1idk__ 2.62.1.2.1 Pectin lyase A {(Aspergillus niger)}
vgvsgsaegfakgvtgggsatpvypdtidelvsylgddearvivltktfdftdsegtttg
tgcapwgtasacqvaidqddwcenyepdapsvsveyynagtlgitvtsnksligegssga
ikgkglrivsgaeniiiqniavtdinpkyvwggdaitlddcdlvwidhvttarigrqhyv
lgtsadnrvsltnnyidgvsdysatcdgyhywaiyldgdadlvtmkgnyiyhtsgrspkv
qdntllhavnnywydisghafeigeggyvlaegnvfqnvdtvletyegeaftvpsstage
vcstylgrdcvingfgssgtfsedstsflsdfegkniasasaytsvasrvvanagqgnl
>d1idm__ 3.65.1.1.1 3-isopropylmalate dehydrogenase {(Thermus thermophilus), strain HB8}
mkvavlpgdgigpevteaalkvlraldeaeglglayevfpfggaaidafgepfpeptrkg
veeaeavllgsvggpkwgtgsvrpeqgllslrksqdlfanlrpakvfpglerlsplkeei
argvdvlivreltggiyfgeprgmseaeawnteryskpevervarvafeaarkrrkhvvs
vdkanvlevgefwrktveevgrgypdvalehqyvdamamhlvrsparfdvvvtgnifgdi
lsdlasvlpgslgllpsaslgrgtpvfepvhgsapdiagkgianptaailsaammlehaf
glvelarkvedavakalletpppdlggsagteaftatvlrhla
>d1ido__ 3.50.1.1.3 Integrin CR3 (CD11b/CD18), alpha subunit {Human (Homo sapiens)}
dsdiaflidgsgsiiphdfrrmkefvstvmeqlkksktlfslmqyseefrihftfkefqn
npnprslvkpitqllgrthtatgirkvvrelfnitngarknafkilvvitdgekfgdplg
yedvipeadregviryvigvgdafrseksrqelntiaskpprdhvfqvnnfealktiqnq
lrek
>d1idsa1 1.2.4.1.1 (2-85) Fe superoxide dismutase (SOD) {(Mycobacterium tuberculosis)}
aeytlpdldwdygalephisgqinelhhskhhatyvkgandavakleearakedhsaill
neknlafnlaghvnhtiwwknlsp
>d1idsa2 4.26.1.1.6 (86-199) Fe superoxide dismutase (SOD) {(Mycobacterium tuberculosis)}
nggdkptgelaaaiadafgsfdkfraqfhaaattvqgsgwaalgwdtlgnkllifqvydh
qtnfplgivplllldmwehafylqyknvkvdfakafwnvvnwadvqsryaaats
>d1idsb1 1.2.4.1.1 (2-85) Fe superoxide dismutase (SOD) {(Mycobacterium tuberculosis)}
aeytlpdldwdygalephisgqinelhhskhhatyvkgandavakleearakedhsaill
neknlafnlaghvnhtiwwknlsp
>d1idsb2 4.26.1.1.6 (86-199) Fe superoxide dismutase (SOD) {(Mycobacterium tuberculosis)}
nggdkptgelaaaiadafgsfdkfraqfhaaattvqgsgwaalgwdtlgnkllifqvydh
qtnfplgivplllldmwehafylqyknvkvdfakafwnvvnwadvqsryaaats
>d1idsc1 1.2.4.1.1 (2-85) Fe superoxide dismutase (SOD) {(Mycobacterium tuberculosis)}
aeytlpdldwdygalephisgqinelhhskhhatyvkgandavakleearakedhsaill
neknlafnlaghvnhtiwwknlsp
>d1idsc2 4.26.1.1.6 (86-199) Fe superoxide dismutase (SOD) {(Mycobacterium tuberculosis)}
nggdkptgelaaaiadafgsfdkfraqfhaaattvqgsgwaalgwdtlgnkllifqvydh
qtnfplgivplllldmwehafylqyknvkvdfakafwnvvnwadvqsryaaats
>d1idsd1 1.2.4.1.1 (2-85) Fe superoxide dismutase (SOD) {(Mycobacterium tuberculosis)}
aeytlpdldwdygalephisgqinelhhskhhatyvkgandavakleearakedhsaill
neknlafnlaghvnhtiwwknlsp
>d1idsd2 4.26.1.1.6 (86-199) Fe superoxide dismutase (SOD) {(Mycobacterium tuberculosis)}
nggdkptgelaaaiadafgsfdkfraqfhaaattvqgsgwaalgwdtlgnkllifqvydh
qtnfplgivplllldmwehafylqyknvkvdfakafwnvvnwadvqsryaaats
>d1idy__ 1.4.1.3.2 c-Myb, DNA-binding domain {mouse (Mus musculus)}
mevkktswteeedrilyqahkrlgnrwaeiakllpgrtdnaiknhwnstmrrkv
>d1idz__ 1.4.1.3.2 c-Myb, DNA-binding domain {mouse (Mus musculus)}
mevkktswteeedrilyqahkrlgnrwaeiakllpgrtdnaiknhwnstmrrkv
>d1ieaa1 4.15.1.1.6 (1-81) MHC class II, N-terminal domains of alpha and beta chains {(mouse I-EK)}
ikeehtiiqaefyllpdkrgefmfdfdgdeifhvdieksetiwrleefakfasfeaqgal
aniavdkanldvmkersnntp
>d1ieab1 4.15.1.1.6 (4-92) MHC class II, N-terminal domains of alpha and beta chains {(mouse I-EK)}
rpwfleycksechfyngtqrvrllvryfynleenlrfdsdvgefravtelgrpdaenwns
qpefleqkraevdtvcrhnyeifdnflvp
>d1ieac1 4.15.1.1.6 (1-81) MHC class II, N-terminal domains of alpha and beta chains {(mouse I-EK)}
ikeehtiiqaefyllpdkrgefmfdfdgdeifhvdieksetiwrleefakfasfeaqgal
aniavdkanldvmkersnntp
>d1iead1 4.15.1.1.6 (4-92) MHC class II, N-terminal domains of alpha and beta chains {(mouse I-EK)}
rpwfleycksechfyngtqrvrllvryfynleenlrfdsdvgefravtelgrpdaenwns
qpefleqkraevdtvcrhnyeifdnflvp
>d1ieba1 4.15.1.1.6 (1-81) MHC class II, N-terminal domains of alpha and beta chains {(mouse I-EK)}
ikeehtiiqaefyllpdkrgefmfdfdgdeifhvdieksetiwrleefakfasfeaqgal
aniavdkanldvmkersnntp
>d1iebb1 4.15.1.1.6 (4-92) MHC class II, N-terminal domains of alpha and beta chains {(mouse I-EK)}
rpwfleycksechfyngtqrvrllvryfynleenlrfdsdvgefravtelgrpdaenwns
qpefleqkraevdtvcrhnyeifdnflvp
>d1iebc1 4.15.1.1.6 (1-81) MHC class II, N-terminal domains of alpha and beta chains {(mouse I-EK)}
ikeehtiiqaefyllpdkrgefmfdfdgdeifhvdieksetiwrleefakfasfeaqgal
aniavdkanldvmkersnntp
>d1iebd1 4.15.1.1.6 (4-92) MHC class II, N-terminal domains of alpha and beta chains {(mouse I-EK)}
rpwfleycksechfyngtqrvrllvryfynleenlrfdsdvgefravtelgrpdaenwns
qpefleqkraevdtvcrhnyeifdnflvp
>d1ier__ 1.25.1.1.4 (Apo)ferritin {horse (Equus caballus), L chain}
ssqirqnysteveaavnrlvnlylrasytylslgfyfdrddvalegvchffrelaeekre
gaerllkmqnqrggralfqdlqkpsqdewgttldamkaaivlekslnqalldlhalgsaq
adphlcdfleshfldeevklikkmgdhltniqrlvgsqaglgeylferltlkhd
>d1iesa_ 1.25.1.1.4 (Apo)ferritin {horse (Equus caballus), L chain}
ssqirqnysteveaavnrlvnlylrasytylslgfyfdrddvalegvchffrelaeekre
gaerllkmqnqrggralfqdlqkpsqdewgttldamkaaivlekslnqalldlhalgsaq
adphlcdfleshfldeevklikkmgdhltniqrlvgsqaglgeylferltlkhd
>d1iesb_ 1.25.1.1.4 (Apo)ferritin {horse (Equus caballus), L chain}
ssqirqnysteveaavnrlvnlylrasytylslgfyfdrddvalegvchffrelaeekre
gaerllkmqnqrggralfqdlqkpsqdewgttldamkaaivlekslnqalldlhalgsaq
adphlcdfleshfldeevklikkmgdhltniqrlvgsqaglgeylferltlkhd
>d1iesc_ 1.25.1.1.4 (Apo)ferritin {horse (Equus caballus), L chain}
ssqirqnysteveaavnrlvnlylrasytylslgfyfdrddvalegvchffrelaeekre
gaerllkmqnqrggralfqdlqkpsqdewgttldamkaaivlekslnqalldlhalgsaq
adphlcdfleshfldeevklikkmgdhltniqrlvgsqaglgeylferltlkhd
>d1iesd_ 1.25.1.1.4 (Apo)ferritin {horse (Equus caballus), L chain}
ssqirqnysteveaavnrlvnlylrasytylslgfyfdrddvalegvchffrelaeekre
gaerllkmqnqrggralfqdlqkpsqdewgttldamkaaivlekslnqalldlhalgsaq
adphlcdfleshfldeevklikkmgdhltniqrlvgsqaglgeylferltlkhd
>d1iese_ 1.25.1.1.4 (Apo)ferritin {horse (Equus caballus), L chain}
ssqirqnysteveaavnrlvnlylrasytylslgfyfdrddvalegvchffrelaeekre
gaerllkmqnqrggralfqdlqkpsqdewgttldamkaaivlekslnqalldlhalgsaq
adphlcdfleshfldeevklikkmgdhltniqrlvgsqaglgeylferltlkhd
>d1iesf_ 1.25.1.1.4 (Apo)ferritin {horse (Equus caballus), L chain}
ssqirqnysteveaavnrlvnlylrasytylslgfyfdrddvalegvchffrelaeekre
gaerllkmqnqrggralfqdlqkpsqdewgttldamkaaivlekslnqalldlhalgsaq
adphlcdfleshfldeevklikkmgdhltniqrlvgsqaglgeylferltlkhd
>d1iet__ 4.70.1.1.2 Cytochrome b5 {rat (Rattus norvegicus)}
dkdvkyytleeiqkhkdskstwvilhhkvydltkfleehpggeevlreqaggdatenfed
vghstdarelsktyiigelhpddrskiakpsetl
>d1ieu__ 4.70.1.1.2 Cytochrome b5 {rat (Rattus norvegicus)}
dkdvkyytleeiqkhkdskstwvilhhkvydltkfleehpggeevlreqaggdatenfed
vghstdarelsktyiigelhpddrskiakpsetl
>d1if1a_ 1.4.3.14.1 Interferon regulatory factor 1 (IRF-1) {Synthetic yes}
rmrpwlemqinsnqipgliwinkeemifqipwkhaakhgwdinkdaclfrswaihtgryk
agekepdpktwkanfrcamnslpdieevkdqsrnkgssavrvyrm
>d1if1b_ 1.4.3.14.1 Interferon regulatory factor 1 (IRF-1) {Synthetic yes}
mrpwlemqinsnqipgliwinkeemifqipwkhaakhgwdinkdaclfrswaihtgryka
gekepdpktwkanfrcamnslpdieevkdqsrnkgssavrvyrm
>d1ifa__ 1.26.1.3.4 Interferon-beta {mouse (Mus musculus)}
ykqlqlqertnirkcqelleqlngkinltyradfkipmemtekmqksytafaiqemlqnv
flvfrnnfsstgwnetivvrlldelhqqtvflktvleekqeerltwemsstalhlksyyw
rvqrylklmkynsyawmvvraeifrnfliirrltrnfq
>d1ifb__ 2.45.1.2.2 Intestinal fatty acid binding protein {rat (Rattus rattus)}
afdgtwkvdrnenyekfmekmginvvkrklgahdnlkltitqegnkftvkessnfrnidv
vfelgvdfaysladgteltgtwtmegnklvgkfkrvdngkeliavreisgneliqtytye
gveakrifkke
>d1ifc__ 2.45.1.2.2 Intestinal fatty acid binding protein {rat (Rattus rattus)}
afdgtwkvdrnenyekfmekmginvvkrklgahdnlkltitqegnkftvkessnfrnidv
vfelgvdfaysladgteltgtwtmegnklvgkfkrvdngkeliavreisgneliqtytye
gveakrifkke
>d1ifd__ 1.105.3.1.1 Inovirus (filamentous phage) major coat protein {strain fd}
aegddpakaafdslqasateyigyawamvvvivgatigiklfkkftskas
>d1ife__ 4.36.1.1.2 Translation initiation factor IF3 {(Escherichia coli), strain: JM83}
viqvkeikfrpgtdegdyqvklrslirfleegdkakitlrfrgremahqqigmevlnrvk
ddlqelavvesfptkiegrqmimvlapkkkq
>d1ifhh1 2.1.1.1.14 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab 17/9 (mouse), kappa L chain}
evqlvesggdlvkpggslklscaasgfsfssygmswvrqtpdkrlewvatisngggytyy
pdsvkgrftisrdnakntlylqmsslksedsamyycarrerydengfaywgqgtlvtvs
>d1ifhh2 2.1.1.2.23 (113-227) Immunoglobulin (constant domains of L and H chains) {Fab 17/9 (mouse), kappa L chain}
aakttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqs
dlytlsssvtvtsstwpsqsitcnvahpasstkvdkkiep
>d1ifhl1 2.1.1.1.14 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab 17/9 (mouse), kappa L chain}
divmtqspssltvtagekvtmsctssqslfnsgkqknyltwyqqkpgqppkvliywastr
esgvpdrftgsgsgtdftltissvqaedlavyycqndysnpltfgggtklelkr
>d1ifhl2 2.1.1.2.23 (109-211) Immunoglobulin (constant domains of L and H chains) {Fab 17/9 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1ifi__ 1.105.3.1.1 Inovirus (filamentous phage) major coat protein {strain fd}
aegddpakaafdslqasateyigyawamvvvivgatigiklfkkftskas
>d1ifj__ 1.105.3.1.1 Inovirus (filamentous phage) major coat protein {strain fd}
aegddpakaafdslqasateyigyawamvvvivgatigiklfkkftskas
>d1ifk__ 1.105.3.1.3 Inovirus (filamentous phage) major coat protein {strain if1}
addatsqakaafdsltaqatemsgyawalvvlvvgatvgiklfkkfvsras
>d1ifl__ 1.105.3.1.4 Inovirus (filamentous phage) major coat protein {strain ike}
aepnaatnyateamdslktqaidlisqtwpvvttvvvaglvirlfkkfsskav
>d1ifm__ 1.105.3.1.2 Inovirus (filamentous phage) major coat protein {strain pf1}
gvidtsavesaitdgqgdmkaiggyivgalvilavagliysmlrka
>d1ifn__ 1.105.3.1.2 Inovirus (filamentous phage) major coat protein {strain pf1}
gvidtsavesaitdgqgdmkaiggyivgalvilavagliysmlrka
>d1ifs__ 4.102.1.1.6 Ricin A-chain {castor bean (Ricinus communis)}
ypiinfttagatvqsytnfiravrgrlttgadvrheipvlpnrvglpinqrfilvelsnh
aelsvtlaldvtnayvvgyragnsayffhpdnqedaeaithlftdvqnrytfafggnydr
leqlagnlrenielgngpleeaisalyyystggtqlptlarsfiiciqmiseaarfqyie
gemrtrirynrrsapdpsvitlenswgrlstaiqesnqgafaspiqlqrrngskfsvydv
silipiialmvyrcappp
>d1ift__ 4.102.1.1.6 Ricin A-chain {castor bean (Ricinus communis)}
ypiinfttagatvqsytnfiravrgrlttgadvrheipvlpnrvglpinqrfilvelsnh
aelsvtlaldvtnayvvgyragnsayffhpdnqedaeaithlftdvqnrytfafggnydr
leqlagnlrenielgngpleeaisalyyystggtqlptlarsfiiciqmiseaarfqyie
gemrtrirynrrsapdpsvitlenswgrlstaiqesnqgafaspiqlqrrngskfsvydv
silipiialmvyrcappp
>d1ifu__ 4.102.1.1.6 Ricin A-chain {castor bean (Ricinus communis)}
ypiinfttagatvqsytnfiravrgrlttgadvrheipvlpnrvglpinqrfilvelsnh
aelsvtlaldvtnayvvgyragnsayffhpdnqedaeaithlftdvqnrytfafggnydr
leqlagnlrenielgngpleeaisalyyystggtqlptlarsfiiciqmiseaarfqyie
gemrtrirynrrsapdpsvitlenswgrlstaiqesnqgafaspiqlqrrngskfsvydv
silipiialmvyrcappp
>d1igb__ 3.58.4.4.1 Aminopeptidase {(Aeromonas proteolytica)}
mppitqqatvtawlpqvdasqitgtisslesftnrfytttsgaqasdwiasewqalsasl
pnasvkqvshsgynqksvvmtitgseapdewivigghldstigshtneqsvapgadddas
giaavtevirvlsennfqpkrsiafmayaaeevglrgsqdlanqyksegknvvsalqldm
tnykgsaqdvvfitdytdsnftqyltqlmdeylpsltygfdtcgyacsdhaswhnagypa
ampfeskfndynprihttqdtlansdptgshakkftqlglayaiemgsatg
>d1igca_ 4.11.1.1.1 Immunoglobulin-binding protein G, separate domains {group G streptococcus (Streptomyces griseus)}
avttyklvingktlkgetttkavdaetaekafkqyandngvdgvwtyddatktftvte
>d1igch1 2.1.1.1.55 (1-119) Immunoglobulin (variable domains of L and H chains) {Fab MoPC21 (mouse), kappa L chain}
dvqlvesggglvqpggsrklscaasgftfssfgmhwvrqapekglewvayissgsstlhy
adtvkgrftisrdnpkntlflqmtslrsedtgmyycarwgnypyyamdywgqgtsvtvs
>d1igch2 2.1.1.2.60 (120-222) Immunoglobulin (constant domains of L and H chains) {Fab MoPC21 (mouse), kappa L chain}
sakttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqs
dlytlsssvtvpssprpsetvtcnvahpasstkvdkkivprdc
>d1igcl1 2.1.1.1.55 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab MoPC21 (mouse), kappa L chain}
nivmtqspksmsmsvgervtltckasenvvtyvswyqqkpeqspklliygasnrytgvpd
rftgsgsatdftltissvqaedladyhcgqgnsypytfgggtkleikr
>d1igcl2 2.1.1.2.60 (109-213) Immunoglobulin (constant domains of L and H chains) {Fab MoPC21 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidserqngvlnswtdqdsk
dstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1igd__ 4.11.1.1.1 Immunoglobulin-binding protein G, separate domains {group G streptococcus (Streptomyces griseus)}
mtpavttyklvingktlkgetttkavdaetaekafkqyandngvdgvwtyddatktftvt
e
>d1igfh1 2.1.1.1.17 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab B13I2 (mouse), kappa L chain}
evqlvesggdlvkpggslklscaasgftfsrcamswvrqtpekrlewvagissggsytfy
pdtvkgrfiisrnnarntlslqmsslrsedtaiyyctryssdpfyfdywgqgttltvss
>d1igfh2 2.1.1.2.26 (114-227) Immunoglobulin (constant domains of L and H chains) {Fab B13I2 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpssprpsetvtcnvahpasstkvdkkivp
>d1igfj1 2.1.1.1.17 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab B13I2 (mouse), kappa L chain}
evqlvesggdlvkpggslklscaasgftfsrcamswvrqtpekrlewvagissggsytfy
pdtvkgrfiisrnnarntlslqmsslrsedtaiyyctryssdpfyfdywgqgttltvss
>d1igfj2 2.1.1.2.26 (114-227) Immunoglobulin (constant domains of L and H chains) {Fab B13I2 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpssprpsetvtcnvahpasstkvdkkivp
>d1igfl1 2.1.1.1.17 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab B13I2 (mouse), kappa L chain}
dvlmtqtplslpvslgdqasiscrsnqtillsdgdtylewylqkpgqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyycfqgshvpptfgggtkleik
>d1igfl2 2.1.1.2.26 (108-214) Immunoglobulin (constant domains of L and H chains) {Fab B13I2 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1igfm1 2.1.1.1.17 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab B13I2 (mouse), kappa L chain}
dvlmtqtplslpvslgdqasiscrsnqtillsdgdtylewylqkpgqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyycfqgshvpptfgggtkleik
>d1igfm2 2.1.1.2.26 (108-214) Immunoglobulin (constant domains of L and H chains) {Fab B13I2 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1igih1 2.1.1.1.18 (2-114) Immunoglobulin (variable domains of L and H chains) {Fab 26-10 (mouse), kappa L chain}
vqlqqsgpelvkpgasvrmsckssgyiftdfymnwvrqshgksldyigyispysgvtgyn
qkfkgkatltvdkssstaymelrsltsedsavyycagssgnkwamdywghgasvtvssa
>d1igih2 2.1.1.2.27 (115-227) Immunoglobulin (constant domains of L and H chains) {Fab 26-10 (mouse), kappa L chain}
kttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsdl
ytlsssvtvtsstwpsqsitcnvahpasstkvdkkiep
>d1igil1 2.1.1.1.18 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab 26-10 (mouse), kappa L chain}
dvvmtqtplslpvslgdqasiscrssqslvhsngntylnwylqkagqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgiyfcsqtthvpptfgggtkleik
>d1igil2 2.1.1.2.27 (108-213) Immunoglobulin (constant domains of L and H chains) {Fab 26-10 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrne
>d1igja1 2.1.1.1.18 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab 26-10 (mouse), kappa L chain}
dvvmtqtplslpvslgdqasiscrssqslvhsngntylnwylqkagqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgiyfcsqtthvpptfgggtkleik
>d1igja2 2.1.1.2.27 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab 26-10 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1igjb1 2.1.1.1.18 (2-114) Immunoglobulin (variable domains of L and H chains) {Fab 26-10 (mouse), kappa L chain}
vqlqqsgpelvkpgasvrmsckssgyiftdfymnwvrqshgksldyigyispysgvtgyn
qkfkgkatltvdkssstaymelrsltsedsavyycagssgnkwamdywghgasvtvssa
>d1igjb2 2.1.1.2.27 (115-227) Immunoglobulin (constant domains of L and H chains) {Fab 26-10 (mouse), kappa L chain}
kttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsdl
ytlsssvtvtsstwpsqsitcnvahpasstkvdkkiep
>d1igjc1 2.1.1.1.18 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab 26-10 (mouse), kappa L chain}
dvvmtqtplslpvslgdqasiscrssqslvhsngntylnwylqkagqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgiyfcsqtthvpptfgggtkleik
>d1igjc2 2.1.1.2.27 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab 26-10 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1igjd1 2.1.1.1.18 (2-114) Immunoglobulin (variable domains of L and H chains) {Fab 26-10 (mouse), kappa L chain}
vqlqqsgpelvkpgasvrmsckssgyiftdfymnwvrqshgksldyigyispysgvtgyn
qkfkgkatltvdkssstaymelrsltsedsavyycagssgnkwamdywghgasvtvssa
>d1igjd2 2.1.1.2.27 (115-227) Immunoglobulin (constant domains of L and H chains) {Fab 26-10 (mouse), kappa L chain}
kttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsdl
ytlsssvtvtsstwpsqsitcnvahpasstkvdkkiep
>d1igl__ 7.1.1.1.5 Insulin-like growth factor {human (Homo sapiens)}
ayrpsetlcggelvdtlqfvcgdrgfyfsrpasrvsrrsrgiveeccfrscdlalletyc
atpakse
>d1igmh_ 2.1.1.1.19 Immunoglobulin (variable domains of L and H chains) {Fv POT (human) Ig-M, kappa L chain}
evhllesggnlvqpggslrlscaasgftfnifvmswvrqapgkglewvsgvfgsggntdy
adavkgrftitrdnskntlylqmnslraedtaiyycakhrvsyvltgfdswgqgtlvtvs
sgsasaptl
>d1igml_ 2.1.1.1.19 Immunoglobulin (variable domains of L and H chains) {Fv POT (human) Ig-M, kappa L chain}
diqmtqspsslsasvgdrvtitcqasqdisnylawyqqkpgkapelriydasnletgvps
rfsgsgsgtdftftisslqpediatyycqqyqnlpltfgpgtkvdikrtvaapsv
>d1igna1 1.4.1.5.1 (360-445) DNA-binding domain of rap1 {baker's yeast (Saccharomyces cerevisiae)}
kasftdeedefildvvrknptrrtthtlydeishyvpnhtgnsirhrfrvylskrleyvy
evdkfgklvrdddgnliktkvlppsi
>d1igna2 1.4.1.5.1 (446-594) DNA-binding domain of rap1 {baker's yeast (Saccharomyces cerevisiae)}
krkfsadedytlaiavkkqfyrdlfqidpdtgrslitdedtptaiarrnmtmdpnhvpgs
epnfaayrtqsrrgpiareffkhfaeehaahtenawrdrfrkfllaygiddyisyyeaek
aqnrepepmknltnrpkrpgvptpgnyns
>d1ignb1 1.4.1.5.1 (360-445) DNA-binding domain of rap1 {baker's yeast (Saccharomyces cerevisiae)}
kasftdeedefildvvrknptrrtthtlydeishyvpnhtgnsirhrfrvylskrleyvy
evdkfgklvrdddgnliktkvlppsi
>d1ignb2 1.4.1.5.1 (446-594) DNA-binding domain of rap1 {baker's yeast (Saccharomyces cerevisiae)}
krkfsadedytlaiavkkqfyrdlfqidpdtgrslitdedtptaiarrnmtmdpnhvpgs
epnfaayrtqsrrgpiareffkhfaeehaahtenawrdrfrkfllaygiddyisyyeaek
aqnrepepmknltnrpkrpgvptpgnyns
>d1igp__ 2.29.5.1.2 Inorganic pyrophosphatase {(Escherichia coli)}
sllnvpagkdlpediyvvieipanadpikyeidkesgalfvdrfmstamfypcnygyinh
tlsldgdpvdvlvptpyplqpgsvtrcrpvgvlkmtdeagedaklvavphsklskeydhi
kdvndlpellkaqiahffehykdlekgkwvkvegwenaeaakaeivasferaknk
>d1igs__ 3.1.8.1.4 Indole-3-glycerophosphate (IGP) synthase {(Sulfolobus solfataricus)}
prylkgwlkdvvqlslrrpsfrasrqrpiislnerilefnkrnitaiiaeykrkspsgld
verdpieyskfmeryavglsilteekyfngsyetlrkiassvsipilmkdfivkesqidd
aynlgadtvllivkiltereleslleyarsygmeplieindendldialrigarfigins
rdletleinkenqrklismipsnvvkvaesgiserneieelrklgvnafligsslmrnpe
kikefil
>d1igta1 2.1.1.1.7 (1-108) Immunoglobulin (variable domains of L and H chains) {Intact IgG2a antidody Mab231 (mouse), kappa L chain}
divltqspsslsaslgdtititchasqninvwlswyqqkpgnipklliykasnlhtgvps
rfsgsgsgtgftltisslqpediatyycqqgqsypltfgggtkleikr
>d1igta2 2.1.1.2.16 (109-214) Immunoglobulin (constant domains of L and H chains) {Intact IgG2a antidody Mab231 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1igtb1 2.1.1.1.7 (1-114) Immunoglobulin (variable domains of L and H chains) {Intact IgG2a antidody Mab231 (mouse), kappa L chain}
evklqesggglvqpggslklscatsgftfsdyymywvrqtpekrlewvayisngggstyy
pdtvkgrftisrdnakntlylqmsrlksedtamyycarhggyyamdywgqgttvtvssa
>d1igtb2 2.1.1.2.16 (115-235) Immunoglobulin (constant domains of L and H chains) {Intact IgG2a antidody Mab231 (mouse), kappa L chain}
kttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsdl
ytlsssvtvtsstwpsqsitcnvahpasstkvdkkieprgptik
>d1igtb3 2.1.1.2.16 (236-361) Immunoglobulin (constant domains of L and H chains) {Intact IgG2a antidody Mab231 (mouse), kappa L chain}
pcppckcpapnllggpsvfifppkikdvlmislspivtcvvvdvseddpdvqiswfvnnv
evhtaqtqthredynstlrvvsalpiqhqdwmsgkefkckvnnkdlpapiertiskpkg
>d1igtb4 2.1.1.2.16 (363-474) Immunoglobulin (constant domains of L and H chains) {Intact IgG2a antidody Mab231 (mouse), kappa L chain}
svrapqvyvlpppeeemtkkqvtltcmvtdfmpediyvewtnngktelnykntepvldsd
gsyfmysklrvekknwvernsyscsvvheglhnhhttksfsr
>d1igtc1 2.1.1.1.7 (1-108) Immunoglobulin (variable domains of L and H chains) {Intact IgG2a antidody Mab231 (mouse), kappa L chain}
divltqspsslsaslgdtititchasqninvwlswyqqkpgnipklliykasnlhtgvps
rfsgsgsgtgftltisslqpediatyycqqgqsypltfgggtkleikr
>d1igtc2 2.1.1.2.16 (109-214) Immunoglobulin (constant domains of L and H chains) {Intact IgG2a antidody Mab231 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1igtd1 2.1.1.1.7 (1-114) Immunoglobulin (variable domains of L and H chains) {Intact IgG2a antidody Mab231 (mouse), kappa L chain}
evklqesggglvqpggslklscatsgftfsdyymywvrqtpekrlewvayisngggstyy
pdtvkgrftisrdnakntlylqmsrlksedtamyycarhggyyamdywgqgttvtvssa
>d1igtd2 2.1.1.2.16 (115-235) Immunoglobulin (constant domains of L and H chains) {Intact IgG2a antidody Mab231 (mouse), kappa L chain}
kttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsdl
ytlsssvtvtsstwpsqsitcnvahpasstkvdkkieprgptik
>d1igtd3 2.1.1.2.16 (236-361) Immunoglobulin (constant domains of L and H chains) {Intact IgG2a antidody Mab231 (mouse), kappa L chain}
pcppckcpapnllggpsvfifppkikdvlmislspivtcvvvdvseddpdvqiswfvnnv
evhtaqtqthredynstlrvvsalpiqhqdwmsgkefkckvnnkdlpapiertiskpkg
>d1igtd4 2.1.1.2.16 (363-474) Immunoglobulin (constant domains of L and H chains) {Intact IgG2a antidody Mab231 (mouse), kappa L chain}
svrapqvyvlpppeeemtkkqvtltcmvtdfmpediyvewtnngktelnykntepvldsd
gsyfmysklrvekknwvernsyscsvvheglhnhhttksfsr
>d1igya1 2.1.1.1.8 (2-107) Immunoglobulin (variable domains of L and H chains) {Intact IgG1 antidody Mab61.1.3 (mouse), kappa L chain}
kcahtvsksmsmsvgervtltckasenvvtyvswyqqkpeqspklliygasnrytgvpdr
ftgsgsatdftltissvqaedladyhcgqgysypytfgggtkleik
>d1igya2 2.1.1.2.17 (108-214) Immunoglobulin (constant domains of L and H chains) {Intact IgG1 antidody Mab61.1.3 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1igyb1 2.1.1.1.8 (2-113) Immunoglobulin (variable domains of L and H chains) {Intact IgG1 antidody Mab61.1.3 (mouse), kappa L chain}
vklqesgaelarpgasvkmsckasgytfttytihwikqrpgqglewigyinpssvytnyn
qrfkdkatltrdrssntanihlssltsddsavyycvregevpywgqgttvtvss
>d1igyb2 2.1.1.2.17 (114-235) Immunoglobulin (constant domains of L and H chains) {Intact IgG1 antidody Mab61.1.3 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpssprpsetvtcnvahpasstkvdkkivprdc
>d1igyb3 2.1.1.2.17 (236-361) Immunoglobulin (constant domains of L and H chains) {Intact IgG1 antidody Mab61.1.3 (mouse), kappa L chain}
gckpcictvpevssvfifppkpkdtllitvtpkvtcvvvdiskddpevqfswfvdnvevh
taqtqpreeqfnstfrvvsalpimhqdwlngkefkcrvnsaafpapiektisktkg
>d1igyb4 2.1.1.2.17 (363-474) Immunoglobulin (constant domains of L and H chains) {Intact IgG1 antidody Mab61.1.3 (mouse), kappa L chain}
kprapqvytipppkeqmakdkvsltcmitdffpeditvewqsdgqapenykntqpimdtd
gsyfvysklnvqksnweagntftcsvlheglhnhhtekslsh
>d1igyc1 2.1.1.1.8 (2-107) Immunoglobulin (variable domains of L and H chains) {Intact IgG1 antidody Mab61.1.3 (mouse), kappa L chain}
kcahtvsksmsmsvgervtltckasenvvtyvswyqqkpeqspklliygasnrytgvpdr
ftgsgsatdftltissvqaedladyhcgqgysypytfgggtkleik
>d1igyc2 2.1.1.2.17 (108-214) Immunoglobulin (constant domains of L and H chains) {Intact IgG1 antidody Mab61.1.3 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1igyd1 2.1.1.1.8 (2-113) Immunoglobulin (variable domains of L and H chains) {Intact IgG1 antidody Mab61.1.3 (mouse), kappa L chain}
vklqesgaelarpgasvkmsckasgytfttytihwikqrpgqglewigyinpssvytnyn
qrfkdkatltrdrssntanihlssltsddsavyycvregevpywgqgttvtvss
>d1igyd2 2.1.1.2.17 (114-235) Immunoglobulin (constant domains of L and H chains) {Intact IgG1 antidody Mab61.1.3 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpssprpsetvtcnvahpasstkvdkkivprdc
>d1igyd3 2.1.1.2.17 (236-361) Immunoglobulin (constant domains of L and H chains) {Intact IgG1 antidody Mab61.1.3 (mouse), kappa L chain}
gckpcictvpevssvfifppkpkdtllitvtpkvtcvvvdiskddpevqfswfvdnvevh
taqtqpreeqfnstfrvvsalpimhqdwlngkefkcrvnsaafpapiektisktkg
>d1igyd4 2.1.1.2.17 (363-474) Immunoglobulin (constant domains of L and H chains) {Intact IgG1 antidody Mab61.1.3 (mouse), kappa L chain}
kprapqvytipppkeqmakdkvsltcmitdffpeditvewqsdgqapenykntqpimdtd
gsyfvysklnvqksnweagntftcsvlheglhnhhtekslsh
>d1ihfa_ 1.51.1.1.1 Integration host factor (IHF) {(Escherichia coli)}
altkaemseylfdklglskrdakelvelffeeirralengeqvklsgfgnfdlrdknqrp
grnpktgedipitarrvvtfrpgqklksrvenaspk
>d1ihfb_ 1.51.1.1.1 Integration host factor (IHF) {(Escherichia coli)}
mtkselierlatqqshipaktvedavkemlehmastlaqgerieirgfgsfslhyraprt
grnpktgdkvelegkyvphfkpgkelrdraniyg
>d1ihp__ 3.48.1.3.1 Phytase (myo-inositol-hexakisphosphate-3-phosphohydrolase) {(Aspergillus ficuum)}
scdtvdqgyqcfsetshlwgqyapffslanesvispevpagcrvtfaqvlsrhgaryptd
skgkkysalieeiqqnattfdgkyaflktynyslgaddltpfgeqelvnsgikfyqryes
ltrnivpfirssgssrviasgkkfiegfqstklkdpraqpgqsspkidvviseasssnnt
ldpgtctvfedseladtveanftatfvpsirqrlendlsgvtltdtevtylmdmcsfdti
ststvdtklspfcdlfthdewinydylqslkkyyghgagnplgptqgvgyaneliarlth
spvhddtssnhtldsspatfplnstlyadfshdngiisilfalglyngtkplstttveni
tqtdgfssawtvpfasrlyvemmqcqaeqeplvrvlvndrvvplhgcpvdalgrctrdsf
vrglsfarsggdwaecfa
>e1ihs.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>e1ihs.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
geadcglrplfekksledkterellesyid
>e1iht.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>e1iht.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
geadcglrplfekksledkterellesyid
>d1ihva_ 2.24.8.1.1 DNA-binding domain of HIV-1 integrase {human immunodeficiency virus, HIV-1}
miqnfrvyyrdsrdpvwkgpakllwkgegavviqdnsdikvvprrkakiird
>d1ihvb_ 2.24.8.1.1 DNA-binding domain of HIV-1 integrase {human immunodeficiency virus, HIV-1}
miqnfrvyyrdsrdpvwkgpakllwkgegavviqdnsdikvvprrkakiird
>d1ihwa_ 2.24.8.1.1 DNA-binding domain of HIV-1 integrase {human immunodeficiency virus, HIV-1}
miqnfrvyyrdsrdpvwkgpakllwkgegavviqdnsdikvvprrkakiird
>d1ihwb_ 2.24.8.1.1 DNA-binding domain of HIV-1 integrase {human immunodeficiency virus, HIV-1}
miqnfrvyyrdsrdpvwkgpakllwkgegavviqdnsdikvvprrkakiird
>d1iiba_ 3.36.2.1.1 Enzyme IIB-cellobiose {(Escherichia coli)}
kkhiylfssagmstsllvskmraqaekyevpviieafpetlagekgqnadvvllgpqiay
mlpeiqrllpnkpvevidsllygkvdglgvlkaavaaikkaaa
>d1iibb_ 3.36.2.1.1 Enzyme IIB-cellobiose {(Escherichia coli)}
kkhiylfssagmstsllvskmraqaekyevpviieafpetlagekgqnadvvllgpqiay
mlpeiqrllpnkpvevidsllygkvdglgvlkaavaaikkaaa
>d1ijsp_ 2.8.1.4.5 Parvovirus capsid {Host: canine (Canis familiaris)}
gvgistgtfnnqtefkflengwvyitanssrlvhlnmpesenyrrvvvnnmdktavngnm
alddihaeivtpwslvdanawgvwfnpgdwqlivntmselhlvsfeqeifnvvlktvses
atqpptkvynndltaslmvaldsnntmpftpaamrsetlgfypwkptiptpwryyfqwdr
tlipshtgtsgtptniyhgtdpddvqfytiensvpvhllrtgdefatgtfffdckpcrlt
htwqtnralglppflnslpqsegdtnfgdigvqqdkrrgvtqmgntnyiteatimrpaev
gysapyysfeastqgpfktpiaagrggaqtdenqaadgnpryafgrqhgqkttttgetpe
rftyiahqdtgrypegdwiqninfnlpvtndnvllptdpiggktginytnifntygplta
lnnvppvypngqiwdkefdtdlkprlhvnapfvcqnncpgqlfvkvapnltnqydpdasa
nmsrivtysdfwwkgklvfkaklrashtwnpiqqmsinvdnqfnyvpsniggmkivyeks
qlaprkly
>d1ika__ 3.65.1.1.5 Isocitrate dehydrogenase {(Escherichia coli)}
skvvvpaqgkkitlqngklnvpenpiipyiegdgigvdvtpamlkvvdaavekaykgerk
iswmeiytgekstqvygqdvwlpaetldlireyrvaikgplttpvgggirslnvalrqel
dlyiclrpvryyqgtpspvkhpeltdmvifrensediyagiewkadsadaekvikflree
mgvkkirfpehcgigikpcseegtkrlvraaieyaiandrdsvtlvhkgnimkftegafk
dwgyqlareefggelidggpwlkvknpntgkeivikdviadaflqqillrpaeydviacm
nlngdyisdalaaqvggigiapganigdecalfeathgtapkyagqdkvnpgsiilsaem
mlrhmgwteaadlivkgmegainaktvtydferlmdgakllkcsefgdaiienm
>d1ikfh1 2.1.1.1.52 (1-126) Immunoglobulin (variable domains of L and H chains) {Fab, anti-cyclosporin A, (mouse), kappa L chain}
evklvesggglvqpggslklscatsgftfsdyymywvrqnsekrlewvafisngggsafy
adivkgrftisrdnakntlylqmsrlksedtamyyctrhtlydtlygnypvwfadwgqgt
lvtvsa
>d1ikfh2 2.1.1.2.59 (127-228) Immunoglobulin (constant domains of L and H chains) {Fab, anti-cyclosporin A, (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpsssrpsetvtcnvahpasstkvdkkivprdc
>d1ikfl1 2.1.1.1.52 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab, anti-cyclosporin A, (mouse), kappa L chain}
diqmtqttsslsaslgdrvtiscrasqdistylnwyqqkpdgtvkllifytsrlrsgvps
rfsgsgsgtdysltisnleqediatyfcqqgsripptfgggtkleil
>d1ikfl2 2.1.1.2.59 (108-214) Immunoglobulin (constant domains of L and H chains) {Fab, anti-cyclosporin A, (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnraac
>d1ikl__ 4.7.1.1.1 Interleukin-8, IL-8 {human (Homo sapiens)}
elrcqciktyskpfhpkfikelrviesgphcanteiivklsdgrelcldpkenwvqrvve
kflkraens
>d1ikm__ 4.7.1.1.1 Interleukin-8, IL-8 {human (Homo sapiens)}
elrcqciktyskpfhpkfikelrviesgphcanteiivklsdgrelcldpkenwvqrvve
kflkraens
>d1iku__ 1.37.1.5.21 Recoverin {bovine (Bos taurus)}
gnsksgalskeileelqlntkfteeelsswyqsflkecpsgritrqefqtiyskffpead
pkayaqhvfrsfdansdgtldfkeyvialhmtsagktnqklewafslydvdgngtiskne
vleivtaifkmispedtkhlpedentpekraekiwgffgkkdddkltekefiegtlanke
ilrliqfe
>d1il6__ 1.26.1.1.4 Interleukin-6 {Human (Homo sapiens)}
ltsseridkqiryildgisalrketcnksnmcesskealaennlnlpkmaekdgcfqsgf
neetclvkiitgllefevyleylqnrfesseeqaravqmstkvliqflqkkaknldaitt
pdpttnaslltklqaqnqwlqdmtthlilrsfkeflqsslralrqm
>d1il8a_ 4.7.1.1.1 Interleukin-8, IL-8 {human (Homo sapiens)}
akelrcqciktyskpfhpkfikelrviesgphcanteiivklsdgrelcldpkenwvqrv
vekflkraens
>d1il8b_ 4.7.1.1.1 Interleukin-8, IL-8 {human (Homo sapiens)}
akelrcqciktyskpfhpkfikelrviesgphcanteiivklsdgrelcldpkenwvqrv
vekflkraens
>d1ilk__ 1.26.1.3.1 Interleukin-10 (cytokine synthesis inhibitory factor, CSIF) {human (Homo sapiens)}
nscthfpgnlpnmlrdlrdafsrvktffqmkdqldnlllkeslledfkgylgcqalsemi
qfyleevmpqaenqdpdikahvnslgenlktlrlrlrrchrflpcenkskaveqvknafn
klqekgiykamsefdifinyieaymtmkirn
>d1ilr1_ 2.31.1.2.3 Interleukin-1 receptor antagonist protein {Human (Homo sapiens)}
skmqafriwdvnqktfylrnnqlvagylqgpnvnleekidvvpiephalflgihggkmcl
scvksgdetrlqleavnitdlsenrkqdkrfafirsdsgpttsfesaacpgwflctamea
dqpvsltnmpdegvmvtkfyfqede
>d1ilr2_ 2.31.1.2.3 Interleukin-1 receptor antagonist protein {Human (Homo sapiens)}
kmqafriwdvnqktfylrnnqlvagylqgpnvnleekidvvpiephalflgihggkmcls
cvksgdetrlqleavnitdlsenrkqdkrfafirsdsgpttsfesaacpgwflctamead
qpvsltnmpdegvmvtkfyfqede
>d1ilsa_ 2.5.1.1.17 Azurin {(Pseudomonas aeruginosa)}
aecsvdsqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctfpghsal
mkgtltlk
>d1ilsb_ 2.5.1.1.17 Azurin {(Pseudomonas aeruginosa)}
aecsvdsqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctfpghsal
mkgtltlk
>d1ilsc_ 2.5.1.1.17 Azurin {(Pseudomonas aeruginosa)}
aecsvdsqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctfpghsal
mkgtltlk
>d1ilsd_ 2.5.1.1.17 Azurin {(Pseudomonas aeruginosa)}
aecsvdsqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctfpghsal
mkgtltlk
>d1ilta_ 2.31.1.2.3 Interleukin-1 receptor antagonist protein {Human (Homo sapiens)}
mqafriwdvnqktfylrnnqlvagylqgpnvnleekidvvpiephalflgihggkmclsc
vksgdetrlqleavnitdlsenrkqdkrfafirsdsgpttsfesaacpgwflctameadq
pvsltnmpdegvmvtkfyfqede
>d1iltb_ 2.31.1.2.3 Interleukin-1 receptor antagonist protein {Human (Homo sapiens)}
mqafriwdvnqktfylrnnqlvagylqgpnvnleekidvvpiephalflgihggkmclsc
vksgdetrlqleavnitdlsenrkqdkrfafirsdsgpttsfesaacpgwflctameadq
pvsltnmpdegvmvtkfyfqede
>d1ilua_ 2.5.1.1.17 Azurin {(Pseudomonas aeruginosa)}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymsfctfpghsal
mkgtltlk
>d1ilub_ 2.5.1.1.17 Azurin {(Pseudomonas aeruginosa)}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymsfctfpghsal
mkgtltlk
>d1iluc_ 2.5.1.1.17 Azurin {(Pseudomonas aeruginosa)}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymsfctfpghsal
mkgtltlk
>d1ilud_ 2.5.1.1.17 Azurin {(Pseudomonas aeruginosa)}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymsfctfpghsal
mkgtltlk
>d1ilue_ 2.5.1.1.17 Azurin {(Pseudomonas aeruginosa)}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymsfctfpghsal
mkgtltlk
>d1iluf_ 2.5.1.1.17 Azurin {(Pseudomonas aeruginosa)}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymsfctfpghsal
mkgtltlk
>d1ilug_ 2.5.1.1.17 Azurin {(Pseudomonas aeruginosa)}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymsfctfpghsal
mkgtltlk
>d1iluh_ 2.5.1.1.17 Azurin {(Pseudomonas aeruginosa)}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymsfctfpghsal
mkgtltlk
>d1ilui_ 2.5.1.1.17 Azurin {(Pseudomonas aeruginosa)}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymsfctfpghsal
mkgtltlk
>d1iluk_ 2.5.1.1.17 Azurin {(Pseudomonas aeruginosa)}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymsfctfpghsal
mkgtltlk
>d1ilul_ 2.5.1.1.17 Azurin {(Pseudomonas aeruginosa)}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymsfctfpghsal
mkgtltlk
>d1ilum_ 2.5.1.1.17 Azurin {(Pseudomonas aeruginosa)}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymsfctfpghsal
mkgtltlk
>d1imaa_ 5.8.1.2.1 Inositol monophosphatase {human (Homo sapiens)}
wqecmdyavtlarqagevvceaiknemnvmlksspvdlvtatdqkvekmlissikekyps
hsfigeesvaageksiltdnptwiidpidgttnfvhrfpfvavsigfavnkkiefgvvys
cvegkmytarkgkgafcngqklqvsqqeditksllvtelgssrtpetvrmvlsnmeklfc
ipvhgirsvgtaavnmclvatggadayyemgihcwdvagagiivteaggvlmdvtggpfd
lmsrrviaannrilaeriakeiqviplqrdded
>d1imab_ 5.8.1.2.1 Inositol monophosphatase {human (Homo sapiens)}
wqecmdyavtlarqagevvceaiknemnvmlksspvdlvtatdqkvekmlissikekyps
hsfigeesvaageksiltdnptwiidpidgttnfvhrfpfvavsigfavnkkiefgvvys
cvegkmytarkgkgafcngqklqvsqqeditksllvtelgssrtpetvrmvlsnmeklfc
ipvhgirsvgtaavnmclvatggadayyemgihcwdvagagiivteaggvlmdvtggpfd
lmsrrviaannrilaeriakeiqviplqrdded
>d1imba_ 5.8.1.2.1 Inositol monophosphatase {human (Homo sapiens)}
wqecmdyavtlarqagevvceaiknemnvmlksspvdlvtatdqkvekmlissikekyps
hsfigeesvaageksiltdnptwiidpidgttnfvhrfpfvavsigfavnkkiefgvvys
cvegkmytarkgkgafcngqklqvsqqeditksllvtelgssrtpetvrmvlsnmeklfc
ipvhgirsvgtaavnmclvatggadayyemgihcwdvagagiivteaggvlmdvtggpfd
lmsrrviaannrilaeriakeiqviplqrdded
>d1imbb_ 5.8.1.2.1 Inositol monophosphatase {human (Homo sapiens)}
wqecmdyavtlarqagevvceaiknemnvmlksspvdlvtatdqkvekmlissikekyps
hsfigeesvaageksiltdnptwiidpidgttnfvhrfpfvavsigfavnkkiefgvvys
cvegkmytarkgkgafcngqklqvsqqeditksllvtelgssrtpetvrmvlsnmeklfc
ipvhgirsvgtaavnmclvatggadayyemgihcwdvagagiivteaggvlmdvtggpfd
lmsrrviaannrilaeriakeiqviplqrdded
>d1imca_ 5.8.1.2.1 Inositol monophosphatase {human (Homo sapiens)}
wqecmdyavtlarqagevvceaiknemnvmlksspvdlvtatdqkvekmlissikekyps
hsfigeesvaageksiltdnptwiidpidgttnfvhrfpfvavsigfavnkkiefgvvys
cvegkmytarkgkgafcngqklqvsqqeditksllvtelgssrtpetvrmvlsnmeklfc
ipvhgirsvgtaavnmclvatggadayyemgihcwdvagagiivteaggvlmdvtggpfd
lmsrrviaannrilaeriakeiqvipl
>d1imcb_ 5.8.1.2.1 Inositol monophosphatase {human (Homo sapiens)}
wqecmdyavtlarqagevvceaiknemnvmlksspvdlvtatdqkvekmlissikekyps
hsfigeesvaageksiltdnptwiidpidgttnfvhrfpfvavsigfavnkkiefgvvys
cvegkmytarkgkgafcngqklqvsqqeditksllvtelgssrtpetvrmvlsnmeklfc
ipvhgirsvgtaavnmclvatggadayyemgihcwdvagagiivteaggvlmdvtggpfd
lmsrrviaannrilaeriakeiqviplqrdded
>d1imda_ 5.8.1.2.1 Inositol monophosphatase {human (Homo sapiens)}
wqecmdyavtlarqagevvceaiknemnvmlksspvdlvtatdqkvekmlissikekyps
hsfigeesvaageksiltdnptwiidpidgttnfvhrfpfvavsigfavnkkiefgvvys
cvegkmytarkgkgafcngqklqvsqqeditksllvtelgssrtpetvrmvlsnmeklfc
ipvhgirsvgtaavnmclvatggadayyemgihcwdvagagiivteaggvlmdvtggpfd
lmsrrviaannrilaeriakeiqvipl
>d1imdb_ 5.8.1.2.1 Inositol monophosphatase {human (Homo sapiens)}
wqecmdyavtlarqagevvceaiknemnvmlksspvdlvtatdqkvekmlissikekyps
hsfigeesvaageksiltdnptwiidpidgttnfvhrfpfvavsigfavnkkiefgvvys
cvegkmytarkgkgafcngqklqvsqqeditksllvtelgssrtpetvrmvlsnmeklfc
ipvhgirsvgtaavnmclvatggadayyemgihcwdvagagiivteaggvlmdvtggpfd
lmsrrviaannrilaeriakeiqviplqrdded
>d1imea_ 5.8.1.2.1 Inositol monophosphatase {human (Homo sapiens)}
wqecmdyavtlarqagevvceaiknemnvmlksspvdlvtatdqkvekmlissikekyps
hsfigeesvaageksiltdnptwiidpidgttnfvhrfpfvavsigfavnkkiefgvvys
cvegkmytarkgkgafcngqklqvsqqeditksllvtelgssrtpetvrmvlsnmeklfc
ipvhgirsvgtaavnmclvatggadayyemgihcwdvagagiivteaggvlmdvtggpfd
lmsrrviaannrilaeriakeiqviplqrdded
>d1imeb_ 5.8.1.2.1 Inositol monophosphatase {human (Homo sapiens)}
wqecmdyavtlarqagevvceaiknemnvmlksspvdlvtatdqkvekmlissikekyps
hsfigeesvaageksiltdnptwiidpidgttnfvhrfpfvavsigfavnkkiefgvvys
cvegkmytarkgkgafcngqklqvsqqeditksllvtelgssrtpetvrmvlsnmeklfc
ipvhgirsvgtaavnmclvatggadayyemgihcwdvagagiivteaggvlmdvtggpfd
lmsrrviaannrilaeriakeiqviplqrdded
>d1imf__ 5.8.1.2.1 Inositol monophosphatase {human (Homo sapiens)}
wqecmdyavtlarqagevvceaiknemnvmlksspvdlvtatdqkvekmlissikekyps
hsfigeesvaageksiltdnptwiidpidgttnfvhrfpfvavsigfavnkkiefgvvys
cvegkmytarkgkgafcngqklqvsqqeditksllvtelgssrtpetvrmvlsnmeklfc
ipvhgirsvgtaavnmclvatggadayyemgihcwdvagagiivteaggvlmdvtggpfd
lmsrrviaannrilaeriakeiqviplqrdded
>d1iml_1 7.33.1.3.3 (1-28) Cysteine-rich (intestinal) protein, CRP, CRIP {Rat (Rattus rattus)}
pkcpkcdkevyfaervtslgkdwhrpcl
>d1iml_2 7.33.1.3.3 (29-76) Cysteine-rich (intestinal) protein, CRP, CRIP {Rat (Rattus rattus)}
kcekcgktltsgghaehegkpycnhpcysamfgpkgfgrggaeshtfk
>d1imp__ 1.27.2.1.2 ImE9 protein {(Escherichia coli)}
melkhsisdyteaeflqlvtticnadtsseeelvklvthfeemtehpsgsdliyypkegd
ddspsgivntvkqwraangksgfkqg
>d1imq__ 1.27.2.1.2 ImE9 protein {(Escherichia coli)}
melkhsisdyteaeflqlvtticnadtsseeelvklvthfeemtehpsgsdliyypkegd
ddspsgivntvkqwraangksgfkqg
>d1inc__ 2.35.1.2.14 Elastase {porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1indh1 2.1.1.1.20 (1-114) Immunoglobulin (variable domains of L and H chains) {Fab Cha255 (mouse), lambda L chain}
evtlvesggdsvkpggslklscaasgftlsgetmswvrqtpekrlewvattlsgggftfy
sasvkgrftisrdnaqnnlylqlnslrsedtalyfcashrfvhwghgtlvtvsa
>d1indh2 2.1.1.2.28 (115-213) Immunoglobulin (constant domains of L and H chains) {Fab Cha255 (mouse), lambda L chain}
kttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlesdl
ytlsssvtvpssprpsetvtcnvahpasstkvdkkivpr
>d1indl1 2.1.1.1.20 (2-109) Immunoglobulin (variable domains of L and H chains) {Fab Cha255 (mouse), lambda L chain}
avvtqesalttspgetvtltcrsstgavttsnyanwvqekpdhlftgliggtnnrapgvp
arfsgsligdkaaltitgaqtedearyfcalwysnlwvfgggtkltvl
>d1indl2 2.1.1.2.28 (110-212) Immunoglobulin (constant domains of L and H chains) {Fab Cha255 (mouse), lambda L chain}
gqpksspsvtlfppsseeletnkatlvctiidfypgvvtvdwkvdgtpvtqgmettqpsk
qsnnkymassyltltarewerhssyscqvtheghtvekslsra
>d1ineh1 2.1.1.1.20 (1-114) Immunoglobulin (variable domains of L and H chains) {Fab Cha255 (mouse), lambda L chain}
evtlvesggdsvkpggslklscaasgftlsgetmswvrqtpekrlewvattlsgggftfy
sasvkgrftisrdnaqnnlylqlnslrsedtalyfcashrfvhwghgtlvtvsa
>d1ineh2 2.1.1.2.28 (115-213) Immunoglobulin (constant domains of L and H chains) {Fab Cha255 (mouse), lambda L chain}
kttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlesdl
ytlsssvtvpssprpsetvtcnvahpasstkvdkkivpr
>d1inel1 2.1.1.1.20 (2-109) Immunoglobulin (variable domains of L and H chains) {Fab Cha255 (mouse), lambda L chain}
avvtqesalttspgetvtltcrsstgavttsnyanwvqekpdhlftgliggtnnrapgvp
arfsgsligdkaaltitgaqtedearyfcalwysnlwvfgggtkltvl
>d1inel2 2.1.1.2.28 (110-212) Immunoglobulin (constant domains of L and H chains) {Fab Cha255 (mouse), lambda L chain}
gqpksspsvtlfppsseeletnkatlvctiidfypgvvtvdwkvdgtpvtqgmettqpsk
qsnnkymassyltltarewerhssyscqvtheghtvekslsra
>d1inf__ 2.50.1.1.3 Influenza neuraminidase {(influenza virus B), different strains}
epewtyprlscqgstfqkallisphrfgeikgnsapliirepfvacgpkecrhfalthya
aqpggyyngtrkdrnklrhlvsvklgkiptvensifhmaawsgsachdgrewtyigvdgp
dndalvkikygeaytdtyhsyahnilrtqesacnciggdcylmitdgsasgiskcrflki
regriikeilptgrvehteectcgfasnktiecacrdnsytakrpfvklnvetdtaeirl
mctktyldtprpddgsiagpcesngdkwlggikggfvhqrmaskigrwysrtmsktnrmg
melyvkydgdpwtdsdaltlsgvmvsieepgwysfgfeikdkkcdvpcigiemvhdggkd
twhsaataiyclmgsgqllwdtvtgvdmal
>d1inga_ 2.50.1.1.2 Influenza neuraminidase {(influenza virus A), different strains}
veyrnwskpqcqitgfapfskdnsirlsaggdiwvtrepyvscdpvkcyqfalgqgttld
nkhsndtvhdriphrtllmnelgvpfhlgtrqvciawsssschdgkawlhvcitgddkna
tasfiydgrlvdsigswsqnilrtqesecvcingtctvvmtdgsasgradtrilfieegk
ivhisplagsaqhveecscyprypgvrcicrdnwkgsnrpvvdinmedysidssyvcsgl
vgdtprnddrssnsncrdpnnergtqgvkgwafdngndlwmgrtiskdlrsgyetfkvig
gwstpnsksqinrqvivdsdnrsgysgifsvegkscinrcfyvelirgrkqetrvwwtsn
sivvfcgtsgtygtgswpdganinfmpi
>d1ingb_ 2.50.1.1.2 Influenza neuraminidase {(influenza virus A), different strains}
veyrnwskpqcqitgfapfskdnsirlsaggdiwvtrepyvscdpvkcyqfalgqgttld
nkhsndtvhdriphrtllmnelgvpfhlgtrqvciawsssschdgkawlhvcitgddkna
tasfiydgrlvdsigswsqnilrtqesecvcingtctvvmtdgsasgradtrilfieegk
ivhisplagsaqhveecscyprypgvrcicrdnwkgsnrpvvdinmedysidssyvcsgl
vgdtprnddrssnsncrdpnnergtqgvkgwafdngndlwmgrtiskdlrsgyetfkvig
gwstpnsksqinrqvivdsdnrsgysgifsvegkscinrcfyvelirgrkqetrvwwtsn
sivvfcgtsgtygtgswpdganinfmpi
>d1inha_ 2.50.1.1.2 Influenza neuraminidase {(influenza virus A), different strains}
veyrnwskpqcqitgfapfskdnsirlsaggdiwvtrepyvscdpvkcyqfalgqgttld
nkhsndtvhdriphrtllmnelgvpfhlgtrqvciawsssschdgkawlhvcitgddkna
tasfiydgrlvdsigswsqnilrtqesecvcingtctvvmtdgsasgradtrilfieegk
ivhisplagsaqhveecscyprypgvrcicrdnwkgsnrpvvdinmedysidssyvcsgl
vgdtprnddrssnsncrdpnnergtqgvkgwafdngndlwmgrtiskdlrsgyetfkvig
gwstpnsksqinrqvivdsdnrsgysgifsvegkscinrcfyvelirgrkqetrvwwtsn
sivvfcgtsgtygtgswpdganinfmpi
>d1inhb_ 2.50.1.1.2 Influenza neuraminidase {(influenza virus A), different strains}
veyrnwskpqcqitgfapfskdnsirlsaggdiwvtrepyvscdpvkcyqfalgqgttld
nkhsndtvhdriphrtllmnelgvpfhlgtrqvciawsssschdgkawlhvcitgddkna
tasfiydgrlvdsigswsqnilrtqesecvcingtctvvmtdgsasgradtrilfieegk
ivhisplagsaqhveecscyprypgvrcicrdnwkgsnrpvvdinmedysidssyvcsgl
vgdtprnddrssnsncrdpnnergtqgvkgwafdngndlwmgrtiskdlrsgyetfkvig
gwstpnsksqinrqvivdsdnrsgysgifsvegkscinrcfyvelirgrkqetrvwwtsn
sivvfcgtsgtygtgswpdganinfmpi
>d1ino__ 2.29.5.1.2 Inorganic pyrophosphatase {(Escherichia coli)}
sllnvpagkdlpediyvvieipanadpikyeidkesgalfvdrfmstamfypcnygyinh
tlsldgdpvdvlvptpyplqpgsvircrpvgvlkmtdeagedaklvavphsklskeydhi
kdvndlpellkaqiahffehykdlekgkwvkvegwenaeaakaeivasferaknk
>d1inp__ 5.8.1.3.1 Inositol polyphosphate 1-phospatase {Bovine (Bos taurus) brain}
msdilqellrvsekaaniaracrqqetlfqllieekkegeknkkfavdfktladvlvqev
ikenmenkfpglgkkifgeesneltndlgekiimrlgpteeetvallskvlngnklasea
lakvvhqdvffsdpaldsveinipqdilgiwvdpidstyqyikgsaditpnqgifpsglq
cvtvligvydiqtgvplmgvinqpfvsqdlhtrrwkgqcywglsylgtnihsllppvstr
snseaqsqgtqnpssegscrfsvvistseketikgalshvcgerifraagagykslcvil
gladiyifsedttfkwdscaahailramgggmvdlkeclernpdtgldlpqlvyhvgneg
aagvdqwankggliayrsekqletflsrllqhlapvatht
>d1inr__ 1.26.1.3.1 Interleukin-10 (cytokine synthesis inhibitory factor, CSIF) {human (Homo sapiens)}
nlpnmlrdlrdafsrvktffqmkdqldnlllkeslledfkgylgcqalsemiqfyleevm
pqaenqdpdikahvnslgenlktlrlrlrrchrflpcenkskaveqvknafnklqekgiy
kamsefdifinyieaymtmkir
>d1inv__ 2.50.1.1.3 Influenza neuraminidase {(influenza virus B), different strains}
epewtyprlscqgstfqkallisphrfgeikgnsapliirepfvacgpkecrhfalthya
aqpggyyngtrkdrnklrhlvsvklgkiptvensifhmaawsgsachdgrewtyigvdgp
dndalvkikygeaytdtyhsyahnilrtqesacnciggdcylmitdgsasgiskcrflki
regriikeilptgrvehteectcgfasnktiecacrdnsytakrpfvklnvetdtaeirl
mctktyldtprpddgsiagpcesngdkwlggikggfvhqrmaskigrwysrtmsktnrmg
melyvrydgdpwtdsdaltlsgvmvsieepgwysfgfeikdkkcdvpcigiemvhdggkd
twhsaataiyclmgsgqllwdtvtgvdmal
>d1inw__ 2.50.1.1.2 Influenza neuraminidase {(influenza virus A), different strains}
veyrnwskpqcqitgfapfskdnsirlsaggdiwvtrepyvscdpvkcyqfalgqgttld
nkhsndtvhdriphrtllmnelgvpfhlgtrqvciawsssschdgkawlhvcitgddkna
tasfiydgrlvdsigswsqnilrtqesecvcingtctvvmtdgsasgradtrilfieegk
ivhisplagsaqhveecscyprypgvrcicrdnwkgsnrpvvdinmedysidssyvcsgl
vgdtprnddrssnsncrdpnnergtqgvkgwafdngndlwmgrtiskdlrsgyetfkvig
gwstpnsksqinrqvivdsdnrsgysgifsvegkscinrcfyvelirgrkqetrvwwtsn
sivvfcgtsgtygtgswpdganinfmpi
>d1inx__ 2.50.1.1.2 Influenza neuraminidase {(influenza virus A), different strains}
veyrnwskpqcqitgfapfskdnsirlsaggdiwvtrepyvscdpvkcyqfalgqgttld
nkhsndtvhdriphrtllmnelgvpfhlgtrqvciawsssschdgkawlhvcitgddkna
tasfiydgrlvdsigswsqnilrtqesecvcingtctvvmtdgsasgradtrilfieegk
ivhisplagsaqhveecscyprypgvrcicrdnwkgsnrpvvdinmedysidssyvcsgl
vgdtprnddrssnsncrdpnnergtqgvkgwafdngndlwmgrtiskdlrsgyetfkvig
gwstpnsksqinrqvivdsdnrsgysgifsvegkscinrcfyvelirgrkqetrvwwtsn
sivvfcgtsgtygtgswpdganinfmpi
>d1iny__ 2.50.1.1.2 Influenza neuraminidase {(influenza virus A), different strains}
rdfnnltkglctinswhiygkdnavrigedsdvlvtrepyvscdpdecrfyalsqgttir
gkhsngtihdrsqyraliswplsspptvynsrvecigwsstschdgktrmsicisgpnnn
asaviwynrrpvteintwarnilrtqesecvchngvcpvvftdgsatgpaetriyyfkeg
kilkweplagtakhieecscygeraeitctcrdnwqgsnrpviridpvamthtsqyicsp
vltdnprpndptvgkcndpypgnnnngvkgfsyldgvntwlgrtisialrsgyemlkvpn
altddkskptqgqtivlntdwsgysgsfmdywaegecyracfyvelirgrpkedkvwwts
nsivsmcssteflgqwdwpdgakieyfl
>d1ioaa_ 2.21.1.1.13 Phytohemagglutinin-L, PHA-L, also arcelin {Kidney bean (Phaseolus vulgaris) G02771, arcelin-5a}
atetsfnfpnfhtddklilqgnatisskgqlqltgvgsnelprvdslgrafysdpiqikd
snnvasfntnftfiiraknqsisayglafalvpvnsppqkkqeflgifntnnpepnartv
avvfntfknridfdknfikpyvnencdfhkyngektdvqitydssnndlrvflhftvsqv
kcsvsatvhlekevdewvsvgfsptsgltedttethdvlswsfsskfr
>d1ioab_ 2.21.1.1.13 Phytohemagglutinin-L, PHA-L, also arcelin {Kidney bean (Phaseolus vulgaris) G02771, arcelin-5a}
atetsfnfpnfhtddklilqgnatisskgqlqltgvgsnelprvdslgrafysdpiqikd
snnvasfntnftfiiraknqsisayglafalvpvnsppqkkqeflgifntnnpepnartv
avvfntfknridfdknfikpyvnencdfhkyngektdvqitydssnndlrvflhftvsqv
kcsvsatvhlekevdewvsvgfsptsgltedttethdvlswsfsskfr
>d1iob__ 2.31.1.2.1 Interleukin-1beta {human (Homo sapiens)}
apvrslnctlrdsqqkslvmsgpyelkalhlqgqdmeqqvvfsmsfvqgeesndkipval
glkeknlylscvlkddkptlqlesvdpknypkkkmekrfvfnkieinnklefesaqfpnw
yistsqaenmpvflggtkggqditdftmqfvss
>d1iol__ 3.22.1.2.3 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvlevnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylahskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevf
>d1iop__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgyqg
>d1iov_1 3.23.1.2.1 (1-96) D-Ala-D-Ala ligase, N-terminal domain {(Escherichia coli), gene ddlB}
mtdkiavllggtsaerevslnsgaavlaglreggidaypvdpkevdvtqlksmgfqkvfi
alhgrggedgtlqgmlelmglpytgsgvmasalsmd
>d1iov_2 4.89.1.1.2 (97-306) D-ala-D-ala ligase {(Escherichia coli ddlB) gene}
klrskllwqgaglpvapwvaltraefekglsdkqlaeisalglpvivkpsregssvgmsk
vvaenalqdalrlafqhdeevliekwlsgpeftvailgeeilpsiriqpsgtfydyeaky
lsdetqyfcpagleasqeanlqalvlkawttlgckgwgridvmldsdgqfylleantspg
mtshslvpmaarqagmsfsqlvvrilelad
>d1iow_1 3.23.1.2.1 (1-96) D-Ala-D-Ala ligase, N-terminal domain {(Escherichia coli), gene ddlB}
mtdkiavllggtsaerevslnsgaavlaglreggidaypvdpkevdvtqlksmgfqkvfi
alhgrggedgtlqgmlelmglpytgsgvmasalsmd
>d1iow_2 4.89.1.1.2 (97-306) D-ala-D-ala ligase {(Escherichia coli ddlB) gene}
klrskllwqgaglpvapwvaltraefekglsdkqlaeisalglpvivkpsregssvgmsk
vvaenalqdalrlafqhdeevliekwlsgpeftvailgeeilpsiriqpsgtfydyeakf
lsdetqyfcpagleasqeanlqalvlkawttlgckgwgridvmldsdgqfylleantspg
mtshslvpmaarqagmsfsqlvvrilelad
>d1ipd__ 3.65.1.1.1 3-isopropylmalate dehydrogenase {(Thermus thermophilus), strain HB8}
mkvavlpgdgigpevteaalkvlraldeaeglglayevfpfggaaidafgepfpeptrkg
veeaeavllgsvggpkwdglprkispetgllslrksqdlfanlrpakvfpglerlsplke
eiargvdvlivreltggiyfgeprgmseaeawnteryskpevervarvafeaarkrrkhv
vsvdkanvlevgefwrktveevgrgypdvalehqyvdamamhlvrsparfdvvvtgnifg
dilsdlasvlpgslgllpsaslgrgtpvfepvhgsapdiagkgianptaailsaammleh
afglvelarkvedavakalletpppdlggsagteaftatvlrhla
>d1ipha1 3.14.1.1.2 (598-753) Catalase, C-terminal domain {(Escherichia coli) HPII}
vkgrvvaillndevrsadllailkalkakgvhakllysrmgevtaddgtvlpiaatfaga
psltvdavivpcgniadiadngdanyylmeaykhlkpialagdarkfkatikiadqgeeg
iveadsadgsfmdelltlmaahrvwsripkidkipa
>d1ipha2 5.6.1.1.5 (27-597) Catalase {(Escherichia coli) PHII}
dslapedgshrpaaeptppgaqptapgslkapdtrneklnsledvrkgsenyalttnqgv
riaddqnslragsrgptlledfilrekithfdheriperivhargsaahgyfqpykslsd
itkadflsdpnkitpvfvrfstvqggagsadtvrdirgfatkfyteegifdlvgnntpif
fiqdahkfpdfvhavkpephwaipqgqsahdtfwdyvslqpetlhnvmwamsdrgiprsy
rtmegfgihtfrlinaegkatfvrfhwkplagkaslvwdeaqkltgrdpdfhrrelweai
eagdfpeyelgfqlipeedefkfdfdlldptklipeelvpvqrvgkmvlnrnpdnffaen
eqaafhpghivpgldftndpllqgrlfsytdtqisrlggpnfheipinrptcpyhnfqrd
gmhrmgidtnpanyepnsindnwpretppgpkrggfesyqervegnkvrerspsfgeyys
hprlfwlsqtpfeqrhivdgfsfelskvvrpyirervvdqlahidltlaqavaknlgiel
tddqlnitpppdvnglkkdpslslyaipdgd
>d1iphb1 3.14.1.1.2 (598-753) Catalase, C-terminal domain {(Escherichia coli) HPII}
vkgrvvaillndevrsadllailkalkakgvhakllysrmgevtaddgtvlpiaatfaga
psltvdavivpcgniadiadngdanyylmeaykhlkpialagdarkfkatikiadqgeeg
iveadsadgsfmdelltlmaahrvwsripkidkipa
>d1iphb2 5.6.1.1.5 (27-597) Catalase {(Escherichia coli) PHII}
dslapedgshrpaaeptppgaqptapgslkapdtrneklnsledvrkgsenyalttnqgv
riaddqnslragsrgptlledfilrekithfdheriperivhargsaahgyfqpykslsd
itkadflsdpnkitpvfvrfstvqggagsadtvrdirgfatkfyteegifdlvgnntpif
fiqdahkfpdfvhavkpephwaipqgqsahdtfwdyvslqpetlhnvmwamsdrgiprsy
rtmegfgihtfrlinaegkatfvrfhwkplagkaslvwdeaqkltgrdpdfhrrelweai
eagdfpeyelgfqlipeedefkfdfdlldptklipeelvpvqrvgkmvlnrnpdnffaen
eqaafhpghivpgldftndpllqgrlfsytdtqisrlggpnfheipinrptcpyhnfqrd
gmhrmgidtnpanyepnsindnwpretppgpkrggfesyqervegnkvrerspsfgeyys
hprlfwlsqtpfeqrhivdgfsfelskvvrpyirervvdqlahidltlaqavaknlgiel
tddqlnitpppdvnglkkdpslslyaipdgd
>d1iphc1 3.14.1.1.2 (598-753) Catalase, C-terminal domain {(Escherichia coli) HPII}
vkgrvvaillndevrsadllailkalkakgvhakllysrmgevtaddgtvlpiaatfaga
psltvdavivpcgniadiadngdanyylmeaykhlkpialagdarkfkatikiadqgeeg
iveadsadgsfmdelltlmaahrvwsripkidkipa
>d1iphc2 5.6.1.1.5 (27-597) Catalase {(Escherichia coli) PHII}
dslapedgshrpaaeptppgaqptapgslkapdtrneklnsledvrkgsenyalttnqgv
riaddqnslragsrgptlledfilrekithfdheriperivhargsaahgyfqpykslsd
itkadflsdpnkitpvfvrfstvqggagsadtvrdirgfatkfyteegifdlvgnntpif
fiqdahkfpdfvhavkpephwaipqgqsahdtfwdyvslqpetlhnvmwamsdrgiprsy
rtmegfgihtfrlinaegkatfvrfhwkplagkaslvwdeaqkltgrdpdfhrrelweai
eagdfpeyelgfqlipeedefkfdfdlldptklipeelvpvqrvgkmvlnrnpdnffaen
eqaafhpghivpgldftndpllqgrlfsytdtqisrlggpnfheipinrptcpyhnfqrd
gmhrmgidtnpanyepnsindnwpretppgpkrggfesyqervegnkvrerspsfgeyys
hprlfwlsqtpfeqrhivdgfsfelskvvrpyirervvdqlahidltlaqavaknlgiel
tddqlnitpppdvnglkkdpslslyaipdgd
>d1iphd1 3.14.1.1.2 (598-753) Catalase, C-terminal domain {(Escherichia coli) HPII}
vkgrvvaillndevrsadllailkalkakgvhakllysrmgevtaddgtvlpiaatfaga
psltvdavivpcgniadiadngdanyylmeaykhlkpialagdarkfkatikiadqgeeg
iveadsadgsfmdelltlmaahrvwsripkidkipa
>d1iphd2 5.6.1.1.5 (27-597) Catalase {(Escherichia coli) PHII}
dslapedgshrpaaeptppgaqptapgslkapdtrneklnsledvrkgsenyalttnqgv
riaddqnslragsrgptlledfilrekithfdheriperivhargsaahgyfqpykslsd
itkadflsdpnkitpvfvrfstvqggagsadtvrdirgfatkfyteegifdlvgnntpif
fiqdahkfpdfvhavkpephwaipqgqsahdtfwdyvslqpetlhnvmwamsdrgiprsy
rtmegfgihtfrlinaegkatfvrfhwkplagkaslvwdeaqkltgrdpdfhrrelweai
eagdfpeyelgfqlipeedefkfdfdlldptklipeelvpvqrvgkmvlnrnpdnffaen
eqaafhpghivpgldftndpllqgrlfsytdtqisrlggpnfheipinrptcpyhnfqrd
gmhrmgidtnpanyepnsindnwpretppgpkrggfesyqervegnkvrerspsfgeyys
hprlfwlsqtpfeqrhivdgfsfelskvvrpyirervvdqlahidltlaqavaknlgiel
tddqlnitpppdvnglkkdpslslyaipdgd
>d1ipsa_ 2.64.3.1.1 Isopenicillin N synthase {(Emericella nidulans)}
vskanvpkidvsplfgddqaakmrvaqqidaasrdtgffyavnhginvqrlsqktkefhm
sitpeekwdlairaynkehqdqvragyylsipgkkavesfcylnpnftpdhpriqaktpt
hevnvwpdetkhpgfqdfaeqyywdvfglssallkgyalalgkeenffarhfkpddtlas
vvlirypyldpypeaaiktaadgtklsfewhedvslitvlyqsnvqnlqvetaagyqdie
addtgylincgsymahltnnyykapihrvkwvnaerqslpffvnlgydsvidpfdprepn
gksdreplsygdylqnglvslinkngqt
>d1ipsb_ 2.64.3.1.1 Isopenicillin N synthase {(Emericella nidulans)}
vskanvpkidvsplfgddqaakmrvaqqidaasrdtgffyavnhginvqrlsqktkefhm
sitpeekwdlairaynkehqdqvragyylsipgkkavesfcylnpnftpdhpriqaktpt
hevnvwpdetkhpgfqdfaeqyywdvfglssallkgyalalgkeenffarhfkpddtlas
vvlirypyldpypeaaiktaadgtklsfewhedvslitvlyqsnvqnlqvetaagyqdie
addtgylincgsymahltnnyykapihrvkwvnaerqslpffvnlgydsvidpfdprepn
gksdreplsygdylqnglvslinkngqt
>d1ipwa_ 2.29.5.1.2 Inorganic pyrophosphatase {(Escherichia coli)}
sllnvpagkdlpediyvvieipanadpikyeidkesgalfvdrfmstamfypcnygyinh
tlsldgdpvdvlvptpyplqpgsvircrpvgvlkmtdeagedaklvavphsklskeydhi
kdvndlpellkaqiahffehykdlekgkwvkvegwenaeaakaeivasferak
>d1ipwb_ 2.29.5.1.2 Inorganic pyrophosphatase {(Escherichia coli)}
sllnvpagkdlpediyvvieipanadpikyeidkesgalfvdrfmstamfypcnygyinh
tlsldgdpvdvlvptpyplqpgsvircrpvgvlkmtdeagedaklvavphsklskeydhi
kdvndlpellkaqiahffehykdlekgkwvkvegwenaeaakaeivasferak
>d1ir3a_ 5.1.1.2.6 insulin receptor {Human (Homo sapiens)}
ssvfvpdewevsrekitllrelgqgsfgmvyegnardiikgeaetrvavktvnesaslre
rieflneasvmkgftchhvvrllgvvskgqptlvvmelmahgdlksylrslrpeaennpg
rppptlqemiqmaaeiadgmaylnakkfvhrdlaarncmvahdftvkigdfgmtrdixet
dxxrkggkgllpvrwmapeslkdgvfttssdmwsfgvvlweitslaeqpyqglsneqvlk
fvmdggyldqpdncpervtdlmrmcwqfnpkmrptfleivnllkddlhpsfpevsffhse
enk
>d1irax_ 2.31.1.2.3 Interleukin-1 receptor antagonist protein {Human (Homo sapiens)}
sskmqafriwdvnqktfylrnnqlvagylqgpnvnleekidvvpiephalflgihggkmc
lscvksgdetrlqleavnitdlsenrkqdkrfafirsdsgpttsfesaacpgwflctame
adqpvsltnmpdegvmvtkfyfqed
>d1iray1 2.1.1.4.9 (6-101) Type-1 interleukin-1 receptor {Human (Homo sapiens)}
reekiilvssaneidvrpcplnpnehkgtitwykddsktpvsteqasrihqhkeklwfvp
akvedsghyycvvrnssyclrikisakfvenepnlc
>d1iray2 2.1.1.4.9 (102-204) Type-1 interleukin-1 receptor {Human (Homo sapiens)}
ynaqaifkqklpvagdgglvcpymeffknennelpklqwykdckpllldnihfsgvkdrl
ivmnvaekhrgnytchasytylgkqypitrviefitleenkpt
>d1iray3 2.1.1.4.9 (205-311) Type-1 interleukin-1 receptor {Human (Homo sapiens)}
rpvivspanetmevdlgsqiqlicnvtgqlsdiaywkwngsvideddpvlgedyysvenp
ankrrstlitvlniseiesrfykhpftcfaknthgidaayiqliypv
>d1irb__ 1.103.1.2.11 Phospholipase A2 {bovine (Bos taurus l.) pancreas}
alwqfngmikckipsseplldfnnygcycglggsgtpvddldrccqthdncykqakklds
ckvlvdnpytnnysyscsnneitcssennaceaficncdrnaaicfskvpynkehknlda
anc
>d1irc__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqsgatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgyq
>d1irf__ 1.4.3.14.2 Interferon regulatory factor-2, IRF-2 {Mouse (Mus musculus)}
pvermrmrpwleeqinsntipglkwlnkekkifqipwmhaarhgwdvekdaplfrnwaih
tgkhqpgidkpdpktwkanfrcamnslpdieevkdrsikkgnnafrvyrmlp
>d1irg__ 1.4.3.14.2 Interferon regulatory factor-2, IRF-2 {Mouse (Mus musculus)}
pvermrmrpwleeqinsntipglkwlnkekkifqipwmhaarhgwdvekdaplfrnwaih
tgkhqpgidkpdpktwkanfrcamnslpdieevkdrsikkgnnafrvyrmlp
>d1irk__ 5.1.1.2.6 insulin receptor {Human (Homo sapiens)}
ssvfvpdewevsrekitllrelgqgsfgmvyegnardiikgeaetrvavktvnesaslre
rieflneasvmkgftchhvvrllgvvskgqptlvvmelmahgdlksylrslrpeaennpg
rppptlqemiqmaaeiadgmaylnakkfvhrdlaarncmvahdftvkigdfgmtrdiyet
dyyrkggkgllpvrwmapeslkdgvfttssdmwsfgvvlweitslaeqpyqglsneqvlk
fvmdggyldqpdncpervtdlmrmcwqfnpkmrptfleivnllkddlhpsfpevsffhse
enk
>d1irl__ 1.26.1.2.5 Interleukin-2 (IL-2) {human (Homo sapiens)}
aptssstkktqlqlehllldlqmilnginnyknpkltrmltakfympkkatelkhlqcle
eelkpleevlnlaqsknfhlrprdlisninvivlelkgsettfmceyadetativeflnr
witfcqsiistlt
>d1irn__ 7.35.4.1.4 Rubredoxin {(Clostridium pasteurianum)}
mkkytctvcgyiynpedgdpdngvnpgtdfkdipddwvcplcgvgkdqfeeve
>d1iro__ 7.35.4.1.4 Rubredoxin {(Clostridium pasteurianum)}
mkkytctvcgyiynpedgdpdngvnpgtdfkdipddwvcplcgvgkdqfeeve
>d1irp__ 2.31.1.2.3 Interleukin-1 receptor antagonist protein {Human (Homo sapiens)}
mrpsgrksskmqafriwdvnqktfylrnnqlvagylqgpnvnleekidvvpiephalflg
ihggkmclscvksgdetrlqleavnitdlsenrkqdkrfafirsdsgpttsfesaacpgw
flctameadqpvsltnmpdegvmvtkfyfqede
>d1irsa_ 2.41.1.2.2 Insulin receptor substrate 1, IRS-1 {human (Homo sapiens)}
mgpafkevwqvilkpkglgqtknligiyrlcltsktisfvklnseaaavvlqlmnirrcg
hsenfffievgrsavtgpgefwmqvddsvvaqnmhetileamramsdefrpr
>d1irv__ 1.3.1.1.6 Mitochondrial cytochrome c {baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdanikk
nvlwdennmseyltnpxkympgtkmafgglkkekdrndlitylkkate
>d1irw__ 1.3.1.1.6 Mitochondrial cytochrome c {baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdaaikk
nvlwdennmseyltnpxkyipgtkmafgglkkekdrndlitylkkate
>d1isaa1 1.2.4.1.3 (1-82) Fe superoxide dismutase (SOD) {(Escherichia coli)}
sfelpalpyakdalaphisaetieyhygkhhqtyvtnlnnlikgtafegksleeiirsse
ggvfnnaaqvwnhtfywnclap
>d1isaa2 4.26.1.1.5 (83-192) Fe superoxide dismutase (SOD) {(Escherichia coli)}
naggeptgkvaeaiaasfgsfadfkaqftdaaiknfgsgwtwlvknsdgklaivstsnag
tplttdatplltvdvwehayyidyrnarpgylehfwalvnwefvaknlaa
>d1isab1 1.2.4.1.3 (1-82) Fe superoxide dismutase (SOD) {(Escherichia coli)}
sfelpalpyakdalaphisaetieyhygkhhqtyvtnlnnlikgtafegksleeiirsse
ggvfnnaaqvwnhtfywnclap
>d1isab2 4.26.1.1.5 (83-192) Fe superoxide dismutase (SOD) {(Escherichia coli)}
naggeptgkvaeaiaasfgsfadfkaqftdaaiknfgsgwtwlvknsdgklaivstsnag
tplttdatplltvdvwehayyidyrnarpgylehfwalvnwefvaknlaa
>d1isba1 1.2.4.1.3 (1-82) Fe superoxide dismutase (SOD) {(Escherichia coli)}
sfelpalpyakdalaphisaetieyhygkhhqtyvtnlnnlikgtafegksleeiirsse
ggvfnnaaqvwnhtfywnclap
>d1isba2 4.26.1.1.5 (83-192) Fe superoxide dismutase (SOD) {(Escherichia coli)}
naggeptgkvaeaiaasfgsfadfkaqftdaaiknfgsgwtwlvknsdgklaivstsnag
tplttdatplltvdvwehayyidyrnarpgylehfwalvnwefvaknlaa
>d1isbb1 1.2.4.1.3 (1-82) Fe superoxide dismutase (SOD) {(Escherichia coli)}
sfelpalpyakdalaphisaetieyhygkhhqtyvtnlnnlikgtafegksleeiirsse
ggvfnnaaqvwnhtfywnclap
>d1isbb2 4.26.1.1.5 (83-192) Fe superoxide dismutase (SOD) {(Escherichia coli)}
naggeptgkvaeaiaasfgsfadfkaqftdaaiknfgsgwtwlvknsdgklaivstsnag
tplttdatplltvdvwehayyidyrnarpgylehfwalvnwefvaknlaa
>d1isca1 1.2.4.1.3 (1-82) Fe superoxide dismutase (SOD) {(Escherichia coli)}
sfelpalpyakdalaphisaetieyhygkhhqtyvtnlnnlikgtafegksleeiirsse
ggvfnnaaqvwnhtfywnclap
>d1isca2 4.26.1.1.5 (83-192) Fe superoxide dismutase (SOD) {(Escherichia coli)}
naggeptgkvaeaiaasfgsfadfkaqftdaaiknfgsgwtwlvknsdgklaivstsnag
tplttdatplltvdvwehayyidyrnarpgylehfwalvnwefvaknlaa
>d1iscb1 1.2.4.1.3 (1-82) Fe superoxide dismutase (SOD) {(Escherichia coli)}
sfelpalpyakdalaphisaetieyhygkhhqtyvtnlnnlikgtafegksleeiirsse
ggvfnnaaqvwnhtfywnclap
>d1iscb2 4.26.1.1.5 (83-192) Fe superoxide dismutase (SOD) {(Escherichia coli)}
naggeptgkvaeaiaasfgsfadfkaqftdaaiknfgsgwtwlvknsdgklaivstsnag
tplttdatplltvdvwehayyidyrnarpgylehfwalvnwefvaknlaa
>d1iska_ 4.13.3.3.1 Delta-5-3-ketosteroid isomerase, steroid delta-isomerase, KSI {(Comamonas testosteroni) (Pseudomonas testosteroni))}
mntpehmtavvqryvaalnagdldgivalfaddatvedpvgseprsgtaairefyanslk
lplaveltqevravaneaafaftvsfeyqgrktvvapidhfrfngagkvvsmralfgekn
ihaga
>d1iskb_ 4.13.3.3.1 Delta-5-3-ketosteroid isomerase, steroid delta-isomerase, KSI {(Comamonas testosteroni) (Pseudomonas testosteroni))}
mntpehmtavvqryvaalnagdldgivalfaddatvedpvgseprsgtaairefyanslk
lplaveltqevravaneaafaftvsfeyqgrktvvapidhfrfngagkvvsmralfgekn
ihaga
>d1iso__ 3.65.1.1.5 Isocitrate dehydrogenase {(Escherichia coli)}
skvvvpaqgkkitlqngklnvpenpiipyiegdgigvdvtpamlkvvdaavekaykgerk
iswmeiytgekstqvygqdvwlpaetldlireyrvaikgplttpvgggirslnvalrqel
dlyiclrpvryyqgtpspvkhpeltdmvifrensediyagiewkadsadaekvikflree
mgvkkirfpehcgigikpmseegtkrlvraaieyaiandrdsvtlvhkgnimkftegafk
dwgyqlareefggelidggpwlkvknpntgkeivikdviadaflqqillrpaeydviacm
nlngdyisdalaaqvggigiapganigdeyalfeathgtapdiagqdkanpgsiilsaem
mlrhmgwteaadlivkgmegainaktvtkdfeslmdgakllkcsefgdaiienm
>d1isua_ 7.30.1.1.1 HIPIP (high potential iron protein) {(Rodocyclus tenuis )}
gtnaamrkafnyqdtakngkkcsgcaqfvpgasptaaggckvipgdnqiapggycdafiv
kk
>d1isub_ 7.30.1.1.1 HIPIP (high potential iron protein) {(Rodocyclus tenuis )}
gtnaamrkafnyqdtakngkkcsgcaqfvpgasptaaggckvipgdnqiapggycdafiv
kk
>d1itba_ 2.31.1.2.1 Interleukin-1beta {human (Homo sapiens)}
apvrslnctlrdsqqkslvmsgpyelkalhlqgqdmeqqvvfsmsfvqgeesndkipval
glkeknlylscvlkddkptlqlesvdpknypkkkmekrfvfnkieinnklefesaqfpnw
yistsqaenmpvflggtkggqditdftmqfvss
>d1itbb1 2.1.1.4.9 (6-101) Type-1 interleukin-1 receptor {Human (Homo sapiens)}
ckereekiilvssaneidvrpcplnpnehkgtitwykddsktpvsteqasrihqhkeklw
fvpakvedsghyycvvrnssyclrikisakfvenep
>d1itbb2 2.1.1.4.9 (102-204) Type-1 interleukin-1 receptor {Human (Homo sapiens)}
nlcynaqaifkqklpvagdgglvcpymeffknennelpklqwykdckpllldnihfsgvk
drlivmnvaekhrgnytchasytylgkqypitrviefitleen
>d1itbb3 2.1.1.4.9 (205-315) Type-1 interleukin-1 receptor {Human (Homo sapiens)}
kptrpvivspanetmevdlgsqiqlicnvtgqlsdiaywkwngsvideddpvlgedyysv
enpankrrstlitvlniseiesrfykhpftcfaknthgidaayiqliypvt
>d1itf__ 1.26.1.3.6 Interferon-alpha 2a {Human (Homo sapiens)}
cdlpqthslgsrrtlmllaqmrkislfsclkdrhdfgfpqeefgnqfqkaetipvlhemi
qqifnlfstkdssaawdetlldkfytelyqqlndleacviqgvgvtetplmkedsilavr
kyfqritlylkekkyspcawevvraeimrsfslstnlqeslrske
>d1itg__ 3.47.3.2.2 HIV integrase, catalytic domain {(human immunodeficiency virus)}
dcspgiwqldcthlegkvilvavhvasgyieaevipaetgqetayfllklagrwpvktvh
tdngsnftsttvkaacwwagikqefgipynpqsqgviesmnkelkkiigqvrdqaehlkt
avqmavfihnkkrkggiggysagerivdiiatdiq
>d1itha_ 1.1.1.1.38 Hemoglobin {innkeeper worm (Urechis caupo)}
gltaaqikaiqdhwflnikgclqaaadsiffkyltaypgdlaffhkfssvplyglrsnpa
ykaqtltvinyldkvvdalggnagalmkakvpshdamgitpkhfgqllklvggvfqeefs
adpttvaawgdaagvlvaamk
>d1ithb_ 1.1.1.1.38 Hemoglobin {innkeeper worm (Urechis caupo)}
gltaaqikaiqdhwflnikgclqaaadsiffkyltaypgdlaffhkfssvplyglrsnpa
ykaqtltvinyldkvvdalggnagalmkakvpshdamgitpkhfgqllklvggvfqeefs
adpttvaawgdaagvlvaamk
>d1iti__ 1.26.1.2.2 Interleukin-4 (IL-4) {human (Homo sapiens)}
eaeahkcditlqeiiktlnslteqktlcteltvtdifaaskdtteketfcraatvlrqfy
shhekdtrclgataqqfhrhkqlirflkrldrnlwglaglnscpvkeadqstlenflerl
ktimrekyskcss
>d1itl__ 1.26.1.2.2 Interleukin-4 (IL-4) {human (Homo sapiens)}
mhkcditlqeiiktlnslteqktlcteltvtdifaaskntteketfcraatvlrqfyshh
ekdtrclgataqqfhrhkqlirflkrldrnlwglaglnscpvkeanqstlenflerlkti
mrekyskcss
>d1itm__ 1.26.1.2.2 Interleukin-4 (IL-4) {human (Homo sapiens)}
mhkcditlqeiiktlnslteqktlcteltvtdifaaskntteketfcraatvlrqfyshh
ekdtrclgataqqfhrhkqlirflkrldrnlwglaglnscpvkeanqstlenflerlkti
mrekyskcss
>d1iud__ 3.82.1.1.6 D-maltodextrin-binding protein {(Escherichia coli)}
egklviwingdkgynglaevgkkfekdtgikvtvehpdkleekfpqvaatgdgpdiifwa
hdrfggyaqsgllaeitpdkafqdklypftwdavryngkliaypiavealsliynkdllp
nppktweeipdpqdprvrglyfpaggldpgksalmfnlqepyftwpliaadggyafkyen
gkydikdvgvdnagakagltflvdliknkhmnadtdysiaeaafnkgetamtingpwaws
nidtskvnygvtvlptfkgqpskpfvgvlsaginaaspnkelakeflenylltdegleav
nkdkplgavalksyeeelakdpriaatmenaqkgeimpnipqmsafwyavrtavinaasg
rqtvdealkdaqtritk
>d1ius_1 3.4.1.2.3 (1-173,276-394) p-Hydroxybenzoate hydroxylase (PHBH) {(Pseudomonas aeruginosa)}
mktqvaiigagpsglllgqllhkagidnvilerqtpdyvlgriragvleqgmvdllreag
vdrrmardglvhegveiafagqrrridlkrlsggktvtvygqtevtrdlmeareacgatt
vyqaaevrlhdlqgerpyvtferdgerlrldcdyiagcdgfhgisrqsipaerXmqhgrl
flagdaahivpptgakglnlaasdvstlyrlllkayregrgellerysaiclrriwkaer
fswwmtsvlhrfpdtdafsqriqqteleyylgseaglatiaenyvglpyeeie
>d1ius_2 4.12.1.2.2 (174-275) p-Hydroxybenzoate hydroxylase {(Pseudomonas aeruginosa)}
lkvfervypfgwlglladtppvsheliyanhprgfalcsqrsatrsryyvqvplsekved
wsderfwtelkarlpsevaeklvtgpsleksiaplrsfvvep
>d1iut_1 3.4.1.2.3 (1-173,276-394) p-Hydroxybenzoate hydroxylase (PHBH) {(Pseudomonas aeruginosa)}
mktqvaiigagpsglllgqllhkagidnvilerqtpdyvlgriragvleqgmvdllreag
vdrrmardglvhegveiafagqrrridlkrlsggktvtvygqtevtrdlmeareacgatt
vyqaaevrlhdlqgerpyvtferdgerlrldcdyiagcdgfhgisrqsipaerXmqhgrl
flagdaahivpptgakglnlaasdvstlyrlllkayregrgellerysaiclrriwkaer
fswwmtsvlhrfpdtdafsqriqqteleyylgseaglatiaenyvglpyeeie
>d1iut_2 4.12.1.2.2 (174-275) p-Hydroxybenzoate hydroxylase {(Pseudomonas aeruginosa)}
lkvfervypfgwlglladtppvsheliyanhprgfalcsqrsatrsryyvqvplsekved
wsderfwtelkarlpsevaeklvtgpsleksiaplrsfvvep
>d1iuu_1 3.4.1.2.3 (1-173,276-394) p-Hydroxybenzoate hydroxylase (PHBH) {(Pseudomonas aeruginosa)}
mktqvaiigagpsglllgqllhkagidnvilerqtpdyvlgriragvleqgmvdllreag
vdrrmardglvhegveiafagqrrridlkrlsggktvtvygqtevtrdlmeareacgatt
vyqaaevrlhdlqgerpyvtferdgerlrldcdyiagcdgfhgisrqsipaerXmqhgrl
flagdaahivpptgakglnlaasdvstlyrlllkayregrgellerysaiclrriwkaer
fswwmtsvlhrfpdtdafsqriqqteleyylgseaglatiaenyvglpyeeie
>d1iuu_2 4.12.1.2.2 (174-275) p-Hydroxybenzoate hydroxylase {(Pseudomonas aeruginosa)}
lkvfervypfgwlglladtppvsheliyanhprgfalcsqrsatrsryyvqvplsekved
wsderfwtelkarlpsevaeklvtgpsleksiaplrsfvvep
>d1iuv_1 3.4.1.2.3 (1-173,276-394) p-Hydroxybenzoate hydroxylase (PHBH) {(Pseudomonas aeruginosa)}
mktqvaiigagpsglllgqllhkagidnvilerqtpdyvlgriragvleqgmvdllreag
vdrrmardglvhegveiafagqrrridlkrlsggktvtvygqtevtrdlmeareacgatt
vyqaaevrlhdlqgerpyvtferdgerlrldcdyiagcdgfhgisrqsipaerXmqhgrl
flagdaahivpptgakglnlaasdvstlyrlllkayregrgellerysaiclrriwkaer
fswwmtsvlhrfpdtdafsqriqqteleyylgseaglatiaenyvglpyeeie
>d1iuv_2 4.12.1.2.2 (174-275) p-Hydroxybenzoate hydroxylase {(Pseudomonas aeruginosa)}
lkvfervypfgwlglladtppvsheliyanhprgfalcsqrsatrsryyvqvplsekved
wsderfwtelkarlpsevaeklvtgpsleksiaplrsfvvep
>d1iuw_1 3.4.1.2.3 (1-173,276-394) p-Hydroxybenzoate hydroxylase (PHBH) {(Pseudomonas aeruginosa)}
mktqvaiigagpsglllgqllhkagidnvilerqtpdyvlgriragvleqgmvdllreag
vdrrmardglvhegveiafagqrrridlkrlsggktvtvygqtevtrdlmeareacgatt
vyqaaevrlhdlqgerpyvtferdgerlrldcdyiagcdgfhgisrqsipaerXmqhgrl
flagdaahivpptgakglnlaasdvstlyrlllkayregrgellerysaiclrriwkaer
fswwmtsvlhrfpdtdafsqriqqteleyylgseaglatiaenyvglpyeeie
>d1iuw_2 4.12.1.2.2 (174-275) p-Hydroxybenzoate hydroxylase {(Pseudomonas aeruginosa)}
lkvfervypfgwlglladtppvsheliyanhprgfalcsqrsatrsryyvqvplsekved
wsderfwtelkarlpsevaeklvtgpsleksiaplrsfvvep
>d1iux_1 3.4.1.2.3 (1-173,276-394) p-Hydroxybenzoate hydroxylase (PHBH) {(Pseudomonas aeruginosa)}
mktqvaiigagpsglllgqllhkagidnvilerqtpdyvlgriragvleqgmvdllreag
vdrrmardglvhegveiafagqrrridlkrlsggktvtvygqtevtrdlmeareacgatt
vyqaaevrlhdlqgerpyvtferdgerlrldcdyiagcdgfhgisrqsipaerXmqhgrl
flagdaahivpptgakglnlaasdvstlyrlllkayregrgellerysaiclrriwkaer
fswwmtsvlhrfpdtdafsqriqqteleyylgseaglatiaenyvglpyeeie
>d1iux_2 4.12.1.2.2 (174-275) p-Hydroxybenzoate hydroxylase {(Pseudomonas aeruginosa)}
lkvfervypfgwlglladtppvsheliyanhprgfalcsqrsatrsryyvqvplsekved
wsderfwtelkarlpsevaeklvtgpsleksiaplrsfvvep
>d1iuz__ 2.5.1.1.5 Plastocyanin {sea lettuce (Ulva pertusa)}
aqivklggddgslafvpskisvaageaiefvnnagfphnivfdedavpagvdadaisydd
ylnskgetvvrklstpgvygvycephagagmkmtitvq
>d1iva__ 7.3.5.2.1 omega-Agatoxin IV, IVa, IVb {funnel web spider (Agelenopsis aperta)}
kkkciakdygrckwggtpccrgrgcicsimgtnceckprlimeglgla
>d1ivb__ 2.50.1.1.3 Influenza neuraminidase {(influenza virus B), different strains}
epewtyprlscqgstfqkallisphrfgeikgnsapliirepfvacgpkecrhfalthya
aqpggyyngtrkdrnklrhlvsvklgkiptvensifhmaawsgsachdgrewtyigvdgp
dndalvkikygeaytdtyhsyahnilrtqesacnciggdcylmitdgsasgiskcrflki
regriikeilptgrvehteectcgfasnktiecacrdnsytakrpfvklnvetdtaeirl
mctktyldtprpddgsiagpcesngdkwlggikggfvhqrmaskigrwysrtmsktnrmg
melyvrydgdpwtdsdaltlsgvmvsieepgwysfgfeikdkkcdvpcigiemvhdggkd
twhsaataiyclmgsgqllwdtvtgvdmal
>d1ivc__ 2.50.1.1.2 Influenza neuraminidase {(influenza virus A), different strains}
veyrnwskpqcqitgfapfskdnsirlsaggdiwvtrepyvscdpvkcyqfalgqgttld
nkhsndtvhdriphrtllmnelgvpfhlgtrqvciawsssschdgkawlhvcitgddkna
tasfiydgrlvdsigswsqnilrtqesecvcingtctvvmtdgsasgradtrilfieegk
ivhisplagsaqhveecscyprypgvrcicrdnwkgsnrpvvdinmedysidssyvcsgl
vgdtprnddrssnsncrdpnnergtqgvkgwafdngndlwmgrtiskdlrsgyetfkvig
gwstpnsksqinrqvivdsdnrsgysgifsvegkscinrcfyvelirgrkqetrvwwtsn
sivvfcgtsgtygtgswpdganinfmpi
>d1ivd__ 2.50.1.1.2 Influenza neuraminidase {(influenza virus A), different strains}
veyrnwskpqcqitgfapfskdnsirlsaggdiwvtrepyvscdpvkcyqfalgqgttld
nkhsndtvhdriphrtllmnelgvpfhlgtrqvciawsssschdgkawlhvcitgddkna
tasfiydgrlvdsigswsqnilrtqesecvcingtctvvmtdgsasgradtrilfieegk
ivhisplagsaqhveecscyprypgvrcicrdnwkgsnrpvvdinmedysidssyvcsgl
vgdtprnddrssnsncrdpnnergtqgvkgwafdngndlwmgrtiskdlrsgyetfkvig
gwstpnsksqinrqvivdsdnrsgysgifsvegkscinrcfyvelirgrkqetrvwwtsn
sivvfcgtsgtygtgswpdganinfmpi
>d1ive__ 2.50.1.1.2 Influenza neuraminidase {(influenza virus A), different strains}
veyrnwskpqcqitgfapfskdnsirlsaggdiwvtrepyvscdpvkcyqfalgqgttld
nkhsndtvhdriphrtllmnelgvpfhlgtrqvciawsssschdgkawlhvcitgddkna
tasfiydgrlvdsigswsqnilrtqesecvcingtctvvmtdgsasgradtrilfieegk
ivhisplagsaqhveecscyprypgvrcicrdnwkgsnrpvvdinmedysidssyvcsgl
vgdtprnddrssnsncrdpnnergtqgvkgwafdngndlwmgrtiskdlrsgyetfkvig
gwstpnsksqinrqvivdsdnrsgysgifsvegkscinrcfyvelirgrkqetrvwwtsn
sivvfcgtsgtygtgswpdganinfmpi
>d1ivf__ 2.50.1.1.2 Influenza neuraminidase {(influenza virus A), different strains}
veyrnwskpqcqitgfapfskdnsirlsaggdiwvtrepyvscdpvkcyqfalgqgttld
nkhsndtvhdriphrtllmnelgvpfhlgtrqvciawsssschdgkawlhvcitgddkna
tasfiydgrlvdsigswsqnilrtqesecvcingtctvvmtdgsasgradtrilfieegk
ivhisplagsaqhveecscyprypgvrcicrdnwkgsnrpvvdinmedysidssyvcsgl
vgdtprnddrssnsncrdpnnergtqgvkgwafdngndlwmgrtiskdlrsgyetfkvig
gwstpnsksqinrqvivdsdnrsgysgifsvegkscinrcfyvelirgrkqetrvwwtsn
sivvfcgtsgtygtgswpdganinfmpi
>d1ivg__ 2.50.1.1.2 Influenza neuraminidase {(influenza virus A), different strains}
veyrnwskpqcqitgfapfskdnsirlsaggdiwvtrepyvscdpvkcyqfalgqgttld
nkhsndtvhdriphrtllmnelgvpfhlgtrqvciawsssschdgkawlhvcitgddkna
tasfiydgrlvdsigswsqnilrtqesecvcingtctvvmtdgsasgradtrilfieegk
ivhisplagsaqhveecscyprypgvrcicrdnwkgsnrpvvdinmedysidssyvcsgl
vgdtprnddrssnsncrdpnnergtqgvkgwafdngndlwmgrtiskdlrsgyetfkvig
gwstpnsksqinrqvivdsdnrsgysgifsvegkscinrcfyvelirgrkqetrvwwtsn
sivvfcgtsgtygtgswpdganinfmpi
>d1ivha1 1.24.6.1.4 (242-392) Isovaleryl-CoA dehydrogenase {Human (Homo sapiens)}
kgvyvlmsgldlerlvlaggplglmqavldhtipylhvreafgqkighfqlmqgkmadmy
trlmacrqyvynvakacdeghctakdcagvilysaecatqvaldgiqcfggngyindfpm
grflrdaklyeigagtsevrrlvigrafnad
>d1ivha2 5.7.1.1.4 (6-241) Isovaleryl-coa dehydrogenase {Human (Homo sapiens)}
vddainglseeqrqlrqtmakflqehlapkaqeidrsnefknlrefwkqlgnlgvlgita
pvqyggsglgylehvlvmeeisrasgavglsygahsnlcinqlvrngneaqkekylpkli
sgeyigalamsepnagsdvvsmklkaekkgnhyilngnkfwitngpdadvlivyaktdla
avpasrgitafivekgmpgfstskkldklgmrgsntcelifedckipaanilghen
>d1ivhb1 1.24.6.1.4 (242-392) Isovaleryl-CoA dehydrogenase {Human (Homo sapiens)}
kgvyvlmsgldlerlvlaggplglmqavldhtipylhvreafgqkighfqlmqgkmadmy
trlmacrqyvynvakacdeghctakdcagvilysaecatqvaldgiqcfggngyindfpm
grflrdaklyeigagtsevrrlvigrafnad
>d1ivhb2 5.7.1.1.4 (6-241) Isovaleryl-coa dehydrogenase {Human (Homo sapiens)}
vddainglseeqrqlrqtmakflqehlapkaqeidrsnefknlrefwkqlgnlgvlgita
pvqyggsglgylehvlvmeeisrasgavglsygahsnlcinqlvrngneaqkekylpkli
sgeyigalamsepnagsdvvsmklkaekkgnhyilngnkfwitngpdadvlivyaktdla
avpasrgitafivekgmpgfstskkldklgmrgsntcelifedckipaanilghen
>d1ivhc1 1.24.6.1.4 (242-392) Isovaleryl-CoA dehydrogenase {Human (Homo sapiens)}
kgvyvlmsgldlerlvlaggplglmqavldhtipylhvreafgqkighfqlmqgkmadmy
trlmacrqyvynvakacdeghctakdcagvilysaecatqvaldgiqcfggngyindfpm
grflrdaklyeigagtsevrrlvigrafnad
>d1ivhc2 5.7.1.1.4 (6-241) Isovaleryl-coa dehydrogenase {Human (Homo sapiens)}
vddainglseeqrqlrqtmakflqehlapkaqeidrsnefknlrefwkqlgnlgvlgita
pvqyggsglgylehvlvmeeisrasgavglsygahsnlcinqlvrngneaqkekylpkli
sgeyigalamsepnagsdvvsmklkaekkgnhyilngnkfwitngpdadvlivyaktdla
avpasrgitafivekgmpgfstskkldklgmrgsntcelifedckipaanilghen
>d1ivhd1 1.24.6.1.4 (242-392) Isovaleryl-CoA dehydrogenase {Human (Homo sapiens)}
kgvyvlmsgldlerlvlaggplglmqavldhtipylhvreafgqkighfqlmqgkmadmy
trlmacrqyvynvakacdeghctakdcagvilysaecatqvaldgiqcfggngyindfpm
grflrdaklyeigagtsevrrlvigrafnad
>d1ivhd2 5.7.1.1.4 (6-241) Isovaleryl-coa dehydrogenase {Human (Homo sapiens)}
vddainglseeqrqlrqtmakflqehlapkaqeidrsnefknlrefwkqlgnlgvlgita
pvqyggsglgylehvlvmeeisrasgavglsygahsnlcinqlvrngneaqkekylpkli
sgeyigalamsepnagsdvvsmklkaekkgnhyilngnkfwitngpdadvlivyaktdla
avpasrgitafivekgmpgfstskkldklgmrgsntcelifedckipaanilghen
>d1ivla_ 2.1.1.1.108 Immunoglobulin (variable domains of L and H chains) {VL domain (kappa) of antibody M29B, dimer synthetic}
dieltqspatlsvtpgnsvsiscrasqsignrlfwyqqkshesprllikyasqsisgips
rfsgsgsgtdftlsinsvetedlavyfcqqvsewpftfgggtkleik
>d1ivlb_ 2.1.1.1.108 Immunoglobulin (variable domains of L and H chains) {VL domain (kappa) of antibody M29B, dimer synthetic}
dieltqspatlsvtpgnsvsiscrasqsignrlfwyqqkshesprllikyasqsisgips
rfsgsgsgtdftlsinsvetedlavyfcqqvsewpftfgggtkleik
>d1ivpa_ 2.38.1.1.3 Human immunodeficiency virus type 2 protease {HIV-2 (rod isolate)}
pqfslwkrpvvtayiegqpvevlldtgaddsivagielgnnyspkivggiggfintleyk
nveievlnkkvratimtgdtpinifgrniltalgmslnl
>d1ivpb_ 2.38.1.1.3 Human immunodeficiency virus type 2 protease {HIV-2 (rod isolate)}
pqfslwkrpvvtayiegqpvevlldtgaddsivagielgnnyspkivggiggfintleyk
nveievlnkkvratimtgdtpinifgrniltalgmslnl
>d1ivqa_ 2.38.1.1.3 Human immunodeficiency virus type 2 protease {HIV-2 (rod isolate)}
pqfslwkrpvvtayiegqpvevlldtgaddsivagielgnnyspkivggiggfintleyk
nveievlnkkvratimtgdtpinifgrniltalgmslnl
>d1ivqb_ 2.38.1.1.3 Human immunodeficiency virus type 2 protease {HIV-2 (rod isolate)}
pqfslwkrpvvtayiegqpvevlldtgaddsivagielgnnyspkivggiggfintleyk
nveievlnkkvratimtgdtpinifgrniltalgmslnl
>d1ivya_ 3.56.1.2.4 human 'protective protein', HPP {(Homo sapiens)}
apdqdeiqrlpglakqpsfrqysgylkssgskhlhywfvesqkdpenspvvlwlnggpgc
ssldglltehgpflvqpdgvtleynpyswnlianvlylespagvgfsysddkfyatndte
vaqsnfealqdffrlfpeyknnklfltgesyagiyiptlavlvmqdpsmnlqglavgngl
ssyeqndnslvyfayyhgllgnrlwsslqthccsqnkcnfydnkdlecvtnlqevarivg
nsglniynlyapcaggvpshfryekdtvvvqdlgniftrlplkrmwhqallrsgdkvrmd
ppctnttaastylnnpyvrkalnipeqlpqwdmcnflvnlqyrrlyrsmnsqylkllssq
kyqillyngdvdmacnfmgdewfvdslnqkmevqrrpwlvkygdsgeqiagfvkefshia
fltikgaghmvptdkplaaftmfsrflnkqpy
>d1ivyb_ 3.56.1.2.4 human 'protective protein', HPP {(Homo sapiens)}
apdqdeiqrlpglakqpsfrqysgylkssgskhlhywfvesqkdpenspvvlwlnggpgc
ssldglltehgpflvqpdgvtleynpyswnlianvlylespagvgfsysddkfyatndte
vaqsnfealqdffrlfpeyknnklfltgesyagiyiptlavlvmqdpsmnlqglavgngl
ssyeqndnslvyfayyhgllgnrlwsslqthccsqnkcnfydnkdlecvtnlqevarivg
nsglniynlyapcaggvpshfryekdtvvvqdlgniftrlplkrmwhqallrsgdkvrmd
ppctnttaastylnnpyvrkalnipeqlpqwdmcnflvnlqyrrlyrsmnsqylkllssq
kyqillyngdvdmacnfmgdewfvdslnqkmevqrrpwlvkygdsgeqiagfvkefshia
fltikgaghmvptdkplaaftmfsrflnkqpy
>d1ixa__ 7.3.9.1.1 Factor IX (IXa) {human (Homo sapiens)}
vdgdqcesnpclnggsckddinsyecwcpfgfegkncel
>d1ixg__ 3.82.1.1.5 Phosphate-binding protein {(Escherichia coli)}
easltgagatfpapvyakwadtyqketgnkvnyqgigssggvkqiiantvdfgasdapls
deklaqeglfqfptviggvvlavnipglksgelvldgktlgdiylgkikkwddeaiakln
pglklpsqniavvrradgsgdsfvftsylakvneewknnvgtgstvkwpiglggkgndgi
aafvqrlpgaigyveyayakqnnlaytklisadgkpvspteenfanaakgadwsktfaqd
ltnqkgedawpitsttfilihkdqkkpeqgtevlkffdwayktgakqandldyaslpdsv
veqvraawktnikdssgkply
>d1ixh__ 3.82.1.1.5 Phosphate-binding protein {(Escherichia coli)}
easltgagatfpapvyakwadtyqketgnkvnyqgigssggvkqiiantvdfgasdapls
deklaqeglfqfptviggvvlavnipglksgelvldgktlgdiylgkikkwddeaiakln
pglklpsqniavvrradgsgtsfvftsylakvneewknnvgtgstvkwpiglggkgndgi
aafvqrlpgaigyveyayakqnnlaytklisadgkpvspteenfanaakgadwsktfaqd
ltnqkgedawpitsttfilihkdqkkpeqgtevlkffdwayktgakqandldyaslpdsv
veqvraawktnikdssgkply
>d1ixi__ 3.82.1.1.5 Phosphate-binding protein {(Escherichia coli)}
easltgagatfpapvyakwadtyqketgnkvnyqgigssggvkqiiantvdfgasnapls
deklaqeglfqfptviggvvlavnipglksgelvldgktlgdiylgkikkwddeaiakln
pglklpsqniavvrradgsgtsfvftsylakvneewknnvgtgstvkwpiglggkgndgi
aafvqrlpgaigyveyayakqnnlaytklisadgkpvspteenfanaakgadwsktfaqd
ltnqkgedawpitsttfilihkdqkkpeqgtevlkffdwayktgakqandldyaslpdsv
veqvraawktnikdssgkply
>d1ixxa_ 4.105.1.1.2 Coagulation factors IX/X-binding protein (IX/X-BP) {Habu snake (Trimeresurus flavoviridis)}
dclsgwssyeghcykafekyktwedaervcteqakgahlvsiessgeadfvaqlvtqnmk
rldfyiwiglrvqgkvkqcnsewsdgssvsyenwieaesktclgleketdfrkwvniycg
qqnpfvcea
>d1ixxb_ 4.105.1.1.2 Coagulation factors IX/X-binding protein (IX/X-BP) {Habu snake (Trimeresurus flavoviridis)}
dcpsdwssyeghcykpfsepknwadaenfctqqhagghlvsfqsseeadfvvklafqtfg
hsifwmglsnvwnqcnwqwsnaamlrykawaeesycvyfkstnnkwrsracrmmaqfvce
fqa
>d1ixxc_ 4.105.1.1.2 Coagulation factors IX/X-binding protein (IX/X-BP) {Habu snake (Trimeresurus flavoviridis)}
dclsgwssyeghcykafekyktwedaervcteqakgahlvsiessgeadfvaqlvtqnmk
rldfyiwiglrvqgkvkqcnsewsdgssvsyenwieaesktclgleketdfrkwvniycg
qqnpfvcea
>d1ixxd_ 4.105.1.1.2 Coagulation factors IX/X-binding protein (IX/X-BP) {Habu snake (Trimeresurus flavoviridis)}
dcpsdwssyeghcykpfsepknwadaenfctqqhagghlvsfqsseeadfvvklafqtfg
hsifwmglsnvwnqcnwqwsnaamlrykawaeesycvyfkstnnkwrsracrmmaqfvce
fqa
>d1ixxe_ 4.105.1.1.2 Coagulation factors IX/X-binding protein (IX/X-BP) {Habu snake (Trimeresurus flavoviridis)}
dclsgwssyeghcykafekyktwedaervcteqakgahlvsiessgeadfvaqlvtqnmk
rldfyiwiglrvqgkvkqcnsewsdgssvsyenwieaesktclgleketdfrkwvniycg
qqnpfvcea
>d1ixxf_ 4.105.1.1.2 Coagulation factors IX/X-binding protein (IX/X-BP) {Habu snake (Trimeresurus flavoviridis)}
dcpsdwssyeghcykpfsepknwadaenfctqqhagghlvsfqsseeadfvvklafqtfg
hsifwmglsnvwnqcnwqwsnaamlrykawaeesycvyfkstnnkwrsracrmmaqfvce
fqa
>d1iyu__ 2.65.1.1.4 The ipoyl domain of dihydrolipoamide acetyltransferase {(azotobacter vinelandii)}
seiirvpdiggdgeviellvktgdlieveqglvvlesakasmevpspkagvvksvsvklg
dklkegdaiielepaagar
>d1iyv__ 2.65.1.1.4 The ipoyl domain of dihydrolipoamide acetyltransferase {(azotobacter vinelandii)}
seiirvpdiggdgeviellvktgdlieveqglvvlesakasmevpspkagvvksvsvklg
dklkegdaiielepaagar
>e1iza.1a 7.1.1.1.3 Insulin {pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e1iza.1b 7.1.1.1.3 Insulin {pig (Sus scrofa)}
fvnqhlcgshlvqalylvcgergffytpkt
>e1iza.2c 7.1.1.1.3 Insulin {pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e1iza.2d 7.1.1.1.3 Insulin {pig (Sus scrofa)}
fvnqhlcgshlvqalylvcgergffytpkt
>e1izb.1a 7.1.1.1.3 Insulin {pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e1izb.1b 7.1.1.1.3 Insulin {pig (Sus scrofa)}
fvnqhlcgshlvqalylvcgergffytpkt
>e1izb.2c 7.1.1.1.3 Insulin {pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e1izb.2d 7.1.1.1.3 Insulin {pig (Sus scrofa)}
fvnqhlcgshlvqalylvcgergffytpkt
>e1jac.1a 2.59.3.1.1 Jacalin, a moraceae plant lectin {jackfruit (artocarpus integrifolia)}
gkafddgaftgireinlsynketaigdfqvvydlngspyvgqnhksfitgftpvkisldf
pseyimevsgytgnvsgyvvvrsltfktnkktygpygvtsgtpfnlpienglivgfkgsi
gywldyfsmylsl
>e1jac.2c 2.59.3.1.1 Jacalin, a moraceae plant lectin {jackfruit (artocarpus integrifolia)}
gkafddgaftgireinlsynketaigdfqvvydlngspyvgqnhksfitgftpvkisldf
pseyimevsgytgnvsgyvvvrsltfktnkktygpygvtsgtpfnlpienglivgfkgsi
gywldyfsmylsl
>e1jac.3e 2.59.3.1.1 Jacalin, a moraceae plant lectin {jackfruit (artocarpus integrifolia)}
gkafddgaftgireinlsynketaigdfqvvydlngspyvgqnhksfitgftpvkisldf
pseyimevsgytgnvsgyvvvrsltfktnkktygpygvtsgtpfnlpienglivgfkgsi
gywldyfsmylsl
>e1jac.4g 2.59.3.1.1 Jacalin, a moraceae plant lectin {jackfruit (artocarpus integrifolia)}
gkafddgaftgireinlsynketaigdfqvvydlngspyvgqnhksfitgftpvkisldf
pseyimevsgytgnvsgyvvvrsltfktnkktygpygvtsgtpfnlpienglivgfkgsi
gywldyfsmylsl
>d1jafa_ 1.24.3.2.5 Cytochrome c' {(Rhodocyclus gelatinosus)}
qfqkpgdaieyrqsaftlianhfgrvaamaqgkapfdakvaaenialvstlsklpltafg
pgtdkghgteakpavwsdaagfkaaadkfaaavdkldaagktgdfaqikaavgetggack
gchdkfke
>d1jafb_ 1.24.3.2.5 Cytochrome c' {(Rhodocyclus gelatinosus)}
qfqkpgdaieyrqsaftlianhfgrvaamaqgkapfdakvaaenialvstlsklpltafg
pgtdkghgteakpavwsdaagfkaaadkfaaavdkldaagktgdfaqikaavgetggack
gchdkfke
>d1jah__ 3.29.1.4.1 cH-p21 Ras protein {human (Homo sapiens)}
mteyklvvvgapgvgksaltiqliqnhfvdeydptiedsyrkqvvidgetclldildtag
qeeysamrdqymrtgegflcvfainntksfedihqyreqikrvkdsddvpmvlvgnkcdl
agrtvesrqaqdlarsygipyietsaktrqgvedafytlvreirqh
>d1jai__ 3.29.1.4.1 cH-p21 Ras protein {human (Homo sapiens)}
mteyklvvvgapgvgksaltiqliqnhfvdeydptiedsyrkqvvidgetclldildtag
qeeysamrdqymrtgegflcvfainntksfedihqyreqikrvkdsddvpmvlvgnkcdl
aartvesrqaqdlarsygipyietsaktrqgvedafytlvreirqh
>d1jana_ 4.52.1.7.2 Neutrophil collagenase (MMP-8) {Human (Homo sapiens)}
fmltpgnpkwertnltyrirnytpqlseaeveraikdafelwsvaspliftrisqgeadi
niafyqrdhgdnspfdgpngilahafqpgqgiggdahfdaeetwtntsanynlflvaahe
fghslglahssdpgalmypnyafretsnyslpqddidgiqaiyg
>d1jaoa_ 4.52.1.7.2 Neutrophil collagenase (MMP-8) {Human (Homo sapiens)}
npkwertnltyrirnytpqlseaeveraikdafelwsvaspliftrisqgeadiniafyq
rdhgdnspfdgpngilahafqpgqgiggdahfdaeetwtntsanynlflvaahefghslg
lahssdpgalmypnyafretsnyslpqddidgiqaiyg
>d1japa_ 4.52.1.7.2 Neutrophil collagenase (MMP-8) {Human (Homo sapiens)}
pkwertnltyrirnytpqlseaeveraikdafelwsvaspliftrisqgeadiniafyqr
dhgdnspfdgpngilahafqpgqgiggdahfdaeetwtntsanynlflvaahefghslgl
ahssdpgalmypnyafretsnyslpqddidgiqaiyg
>d1jaqa_ 4.52.1.7.2 Neutrophil collagenase (MMP-8) {Human (Homo sapiens)}
npkwertnltyrirnytpqlseaeveraikdafelwsvaspliftrisqgeadiniafyq
rdhgdnspfdgpngilahafqpgqgiggdahfdaeetwtntsanynlflvaahefghslg
lahssdpgalmypnyafretsnyslpqddidgiqaiyg
>d1jbc__ 2.21.1.1.1 Concanavalin A {jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1jcka1 2.1.1.1.121 (3-117) T-cell antigen receptor {Mouse (Mus musculus), beta-chain}
avtqsprnkvavtggkvtlscqqtnnhnnmywyrqdtghglrlihysygagstekgdipd
gykasrpsqeqfslilelatpsqtsvyfcasgggrgsyaeqffgpgtrltvle
>d1jcka2 2.1.1.2.111 (118-246) T-cell antigen receptor {Mouse (Mus musculus), beta-chain}
dlrqvtppkvslfepskaeiankqkatlvclargffpdhvelswwvngkevhsgvstdpq
aykesnysyclssrlrvsatfwhnprnhfrcqvqfhglseedkwpegspkpvtqnisaea
wgrad
>d1jckb1 2.29.2.2.5 (1-121) Staphylococcal enterotoxin C3, SEC3 {(Staphylococcus aureus)}
esqpdpmpddlhksseftgtmgnmkylyddhyvsatkvksvdkflahdliynindkklnn
ydkvktellnedlankykdevvdvygsnyyvncyfsskdnvgkvtsgktcmyggitkheg
n
>d1jckb2 4.11.6.1.5 (122-239) Staphylococcal enterotoxin C3, SEC3 {(Staphylococcus aureus)}
hfdngnlqnvlirvyenkrntisfevqtdkksvtaqeldikarnflinkknlyefnsspy
etgyikfiesngntfwydmmpapgdkfdqskylmiykdnkmvdsksvkievhlttkng
>d1jckc1 2.1.1.1.121 (3-117) T-cell antigen receptor {Mouse (Mus musculus), beta-chain}
avtqsprnkvavtggkvtlscqqtnnhnnmywyrqdtghglrlihysygagstekgdipd
gykasrpsqeqfslilelatpsqtsvyfcasgggrgsyaeqffgpgtrltvle
>d1jckc2 2.1.1.2.111 (118-246) T-cell antigen receptor {Mouse (Mus musculus), beta-chain}
dlrqvtppkvslfepskaeiankqkatlvclargffpdhvelswwvngkevhsgvstdpq
aykesnysyclssrlrvsatfwhnprnhfrcqvqfhglseedkwpegspkpvtqnisaea
wgrad
>d1jckd1 2.29.2.2.5 (1-121) Staphylococcal enterotoxin C3, SEC3 {(Staphylococcus aureus)}
esqpdpmpddlhksseftgtmgnmkylyddhyvsatkvksvdkflahdliynindkklnn
ydkvktellnedlankykdevvdvygsnyyvncyfsskdnvgkvtsgktcmyggitkheg
n
>d1jckd2 4.11.6.1.5 (122-239) Staphylococcal enterotoxin C3, SEC3 {(Staphylococcus aureus)}
hfdngnlqnvlirvyenkrntisfevqtdkksvtaqeldikarnflinkknlyefnsspy
etgyikfiesngntfwydmmpapgdkfdqskylmiykdnkmvdsksvkievhlttkng
>d1jcv__ 2.1.7.1.5 Cu,Zn superoxide dismutase, SOD {yeast (Saccharomyces cerevisiae)}
vqavavlkgdagvsgvvkfeqasesepttvsyeiagnspnaergfhihefgdatngcvsa
gphfnpfkkthgaptdevrhvgdmgnvktdengvakgsfkdslikligptsvvgrsvvih
agqddlgkgdteeslktgnagprpacgvigltn
>d1jcw__ 2.1.7.1.5 Cu,Zn superoxide dismutase, SOD {yeast (Saccharomyces cerevisiae)}
vqavavlkgdagvsgvvkfeqasesepttvsyeiagnspnaergfhihefgdatngcvsa
gphfnpfkkthgaptdevrhvgdmgnvktdengvakgsfkdslikligptsvvgrsvvih
agqddlgkgdteeslktgnagprpacgvigltn
>d1jda_1 2.53.1.1.10 (358-418) G4-amylase (1,4-alpha-D-glucan maltotetrahydrolase {(Pseudomonas stutzeri)}
radsaisfhsgysglvatvsgsqqtlvvalnsdlgnpgqvasgsfseavnasngqvrvwr
s
>d1jda_2 3.1.1.1.10 (1-357) G4-amylase (1,4-alpha-D-glucan maltotetrahydrolase) {(Pseudomonas stutzeri)}
dqagkspnavryhggdeiilqgfhwnvvreapndwynilrqqaatiaadgfsaiwmpvpw
rdfsswsdgsksgggegyfwhdfnkngrygsdaqlrqaasalggagvkvlydvvpnhmnr
gypdkeinlpagqgfwrndcadpgnypndcddgdrfiggdadlntghpqvygmfrdeftn
lrsqygaggfrfdfvrgyapervnswmtdsadnsfcvgqlwkgpseypnwdwrntaswqq
iikdwsdrakcpvfdfalkermqngsiadwkhglngnpdprwrevavtfvdnhdtgyspg
qnggqhhwalqdglirqayayiltspgtpvvywdhmydwgygdfirqliqvrraagv
>d1jdbb1 1.71.1.1.1 (403-555) Carbamoyl phosphate synthetase, large subunit connection domain {(Escherichia coli)}
vgatgfdpkvslddpealtkirrelkdagadriwyiadafraglsvdgvfnltnidrwfl
vqieelvrleekvaevgitglnadflrqlkrkgfadarlaklagvreaeirklrdqydlh
pvykrvdtcaaefatdtaymystyeeeceanps
>d1jdbb2 3.15.1.1.1 (936-1072) Carbamoyl phosphate synthetase, large subunit allosteric, C-terminal domain {(Escherichia coli)}
stmkkhgrallsvregdkervvdlaakllkqgfeldathgtaivlgeaginprlvnkvhe
grphiqdrikngeytyiinttsgrraiedsrvirrsalqykvhydttlnggfatamalna
datekvisvqemhaqik
>d1jdbb3 3.23.1.1.2 (1-127) Carbamoyl phosphate synthetase (CPS), large subunit {(Escherichia coli)}
pkrtdiksililgagpivigqacefdysgaqackalreegyrvilvnsnpatimtdpema
datyiepihwevvrkiiekerpdavlptmggqtalncalelerqgvleefgvtmigatad
aidkaed
>d1jdbb4 3.23.1.1.2 (556-676) Carbamoyl phosphate synthetase (CPS), large subunit {(Escherichia coli)}
tdrekimvlgggpnrigqgiefdyccvhaslalredgyetimvncnpetvstdydtsdrl
yfepvtledvleivriekpkgvivqyggqtplklaraleaagvpvigtspdaidraedre
r
>d1jdbb5 4.89.1.2.2 (128-402) Carbamoyl phosphate synthetase (CPS), large subunit {(Escherichia coli)}
rrrfdvamkkigletarsgiahtmeealavaadvgfpciirpsftmggsgggiaynreef
eeicargldlsptkellidesligwkeyemevvrdkndnciivcsienfdamgihtgdsi
tvapaqtltdkeyqimrnasmavlreigvetggsnvqfavnpkngrliviemnprvsrss
alaskatgfpiakvaaklavgytldelmnditggrtpasfepsidyvvtkiprfnfekfa
gandrlttqmksvgevmaigrtqqeslqkalrgle
>d1jdbb6 4.89.1.2.2 (677-935) Carbamoyl phosphate synthetase (CPS), large subunit {(Escherichia coli)}
fqhaverlklkqpanatvtaiemavekakeigyplvvrpsyvlggrameivydeadlrry
fqtavsvsndapvlldhflddavevdvdaicdgemvliggimehieqagvhsgdsacslp
aytlsqeiqdvmrqqvqklafelqvrglmnvqfavknnevylievnpraartvpfvskat
gvplakvaarvmagkslaeqgvtkevippyysvkevvlpfnkfpgvdpllgpemrstgev
mgvgrtfaeafakaqlgsn
>d1jdbc1 3.5.3.1.1 (2-152) Carbamoyl phosphate synthetase, small subunit N-terminal domain {(Escherichia coli)}
iksallvledgtqfhgraigatgsavgevvfntsmtgyqeiltdpsysrqivtltyphig
nvgtndadeessqvhaqglvirdlpliasnfrntedlssylkrhnivaiadidtrkltrl
lrekgaqngciiagdnpdaalalekarafpg
>d1jdbc2 3.55.1.1.2 (153-380) Carbamoyl phosphate synthetase, small subunit C-terminal domain {(Escherichia coli)}
lngmdlakevttaeayswtqgswtltgglpqakkedelpfhvvaydfgakrnilrmlvdr
gcrltivpaqtsaedvlkmnpdgiflsngpgdpapcdyaitaiqkfletdipvfgiclgh
qllalasgaktvkmkfghhggnhpvkdveknvvmitaqnhgfavdeatlpanlrvthksl
fdgtlqgihrtdkpafsfqghpeaspgphdaaplfdhfielieqyrkt
>d1jdbe1 1.71.1.1.1 (403-555) Carbamoyl phosphate synthetase, large subunit connection domain {(Escherichia coli)}
vgatgfdpkvslddpealtkirrelkdagadriwyiadafraglsvdgvfnltnidrwfl
vqieelvrleekvaevgitglnadflrqlkrkgfadarlaklagvreaeirklrdqydlh
pvykrvdtcaaefatdtaymystyeeeceanps
>d1jdbe2 3.15.1.1.1 (936-1072) Carbamoyl phosphate synthetase, large subunit allosteric, C-terminal domain {(Escherichia coli)}
stmkkhgrallsvregdkervvdlaakllkqgfeldathgtaivlgeaginprlvnkvhe
grphiqdrikngeytyiinttsgrraiedsrvirrsalqykvhydttlnggfatamalna
datekvisvqemhaqik
>d1jdbe3 3.23.1.1.2 (1-127) Carbamoyl phosphate synthetase (CPS), large subunit {(Escherichia coli)}
pkrtdiksililgagpivigqacefdysgaqackalreegyrvilvnsnpatimtdpema
datyiepihwevvrkiiekerpdavlptmggqtalncalelerqgvleefgvtmigatad
aidkaed
>d1jdbe4 3.23.1.1.2 (556-676) Carbamoyl phosphate synthetase (CPS), large subunit {(Escherichia coli)}
tdrekimvlgggpnrigqgiefdyccvhaslalredgyetimvncnpetvstdydtsdrl
yfepvtledvleivriekpkgvivqyggqtplklaraleaagvpvigtspdaidraedre
r
>d1jdbe5 4.89.1.2.2 (128-402) Carbamoyl phosphate synthetase (CPS), large subunit {(Escherichia coli)}
rrrfdvamkkigletarsgiahtmeealavaadvgfpciirpsftmggsgggiaynreef
eeicargldlsptkellidesligwkeyemevvrdkndnciivcsienfdamgihtgdsi
tvapaqtltdkeyqimrnasmavlreigvetggsnvqfavnpkngrliviemnprvsrss
alaskatgfpiakvaaklavgytldelmnditggrtpasfepsidyvvtkiprfnfekfa
gandrlttqmksvgevmaigrtqqeslqkalrgle
>d1jdbe6 4.89.1.2.2 (677-935) Carbamoyl phosphate synthetase (CPS), large subunit {(Escherichia coli)}
fqhaverlklkqpanatvtaiemavekakeigyplvvrpsyvlggrameivydeadlrry
fqtavsvsndapvlldhflddavevdvdaicdgemvliggimehieqagvhsgdsacslp
aytlsqeiqdvmrqqvqklafelqvrglmnvqfavknnevylievnpraartvpfvskat
gvplakvaarvmagkslaeqgvtkevippyysvkevvlpfnkfpgvdpllgpemrstgev
mgvgrtfaeafakaqlgsn
>d1jdbf1 3.5.3.1.1 (2-152) Carbamoyl phosphate synthetase, small subunit N-terminal domain {(Escherichia coli)}
iksallvledgtqfhgraigatgsavgevvfntsmtgyqeiltdpsysrqivtltyphig
nvgtndadeessqvhaqglvirdlpliasnfrntedlssylkrhnivaiadidtrkltrl
lrekgaqngciiagdnpdaalalekarafpg
>d1jdbf2 3.55.1.1.2 (153-380) Carbamoyl phosphate synthetase, small subunit C-terminal domain {(Escherichia coli)}
lngmdlakevttaeayswtqgswtltgglpqakkedelpfhvvaydfgakrnilrmlvdr
gcrltivpaqtsaedvlkmnpdgiflsngpgdpapcdyaitaiqkfletdipvfgiclgh
qllalasgaktvkmkfghhggnhpvkdveknvvmitaqnhgfavdeatlpanlrvthksl
fdgtlqgihrtdkpafsfqghpeaspgphdaaplfdhfielieqyrkt
>d1jdbh1 1.71.1.1.1 (403-555) Carbamoyl phosphate synthetase, large subunit connection domain {(Escherichia coli)}
vgatgfdpkvslddpealtkirrelkdagadriwyiadafraglsvdgvfnltnidrwfl
vqieelvrleekvaevgitglnadflrqlkrkgfadarlaklagvreaeirklrdqydlh
pvykrvdtcaaefatdtaymystyeeeceanps
>d1jdbh2 3.15.1.1.1 (936-1072) Carbamoyl phosphate synthetase, large subunit allosteric, C-terminal domain {(Escherichia coli)}
stmkkhgrallsvregdkervvdlaakllkqgfeldathgtaivlgeaginprlvnkvhe
grphiqdrikngeytyiinttsgrraiedsrvirrsalqykvhydttlnggfatamalna
datekvisvqemhaqik
>d1jdbh3 3.23.1.1.2 (1-127) Carbamoyl phosphate synthetase (CPS), large subunit {(Escherichia coli)}
pkrtdiksililgagpivigqacefdysgaqackalreegyrvilvnsnpatimtdpema
datyiepihwevvrkiiekerpdavlptmggqtalncalelerqgvleefgvtmigatad
aidkaed
>d1jdbh4 3.23.1.1.2 (556-676) Carbamoyl phosphate synthetase (CPS), large subunit {(Escherichia coli)}
tdrekimvlgggpnrigqgiefdyccvhaslalredgyetimvncnpetvstdydtsdrl
yfepvtledvleivriekpkgvivqyggqtplklaraleaagvpvigtspdaidraedre
r
>d1jdbh5 4.89.1.2.2 (128-402) Carbamoyl phosphate synthetase (CPS), large subunit {(Escherichia coli)}
rrrfdvamkkigletarsgiahtmeealavaadvgfpciirpsftmggsgggiaynreef
eeicargldlsptkellidesligwkeyemevvrdkndnciivcsienfdamgihtgdsi
tvapaqtltdkeyqimrnasmavlreigvetggsnvqfavnpkngrliviemnprvsrss
alaskatgfpiakvaaklavgytldelmnditggrtpasfepsidyvvtkiprfnfekfa
gandrlttqmksvgevmaigrtqqeslqkalrgle
>d1jdbh6 4.89.1.2.2 (677-935) Carbamoyl phosphate synthetase (CPS), large subunit {(Escherichia coli)}
fqhaverlklkqpanatvtaiemavekakeigyplvvrpsyvlggrameivydeadlrry
fqtavsvsndapvlldhflddavevdvdaicdgemvliggimehieqagvhsgdsacslp
aytlsqeiqdvmrqqvqklafelqvrglmnvqfavknnevylievnpraartvpfvskat
gvplakvaarvmagkslaeqgvtkevippyysvkevvlpfnkfpgvdpllgpemrstgev
mgvgrtfaeafakaqlgsn
>d1jdbi1 3.5.3.1.1 (2-152) Carbamoyl phosphate synthetase, small subunit N-terminal domain {(Escherichia coli)}
iksallvledgtqfhgraigatgsavgevvfntsmtgyqeiltdpsysrqivtltyphig
nvgtndadeessqvhaqglvirdlpliasnfrntedlssylkrhnivaiadidtrkltrl
lrekgaqngciiagdnpdaalalekarafpg
>d1jdbi2 3.55.1.1.2 (153-380) Carbamoyl phosphate synthetase, small subunit C-terminal domain {(Escherichia coli)}
lngmdlakevttaeayswtqgswtltgglpqakkedelpfhvvaydfgakrnilrmlvdr
gcrltivpaqtsaedvlkmnpdgiflsngpgdpapcdyaitaiqkfletdipvfgiclgh
qllalasgaktvkmkfghhggnhpvkdveknvvmitaqnhgfavdeatlpanlrvthksl
fdgtlqgihrtdkpafsfqghpeaspgphdaaplfdhfielieqyrkt
>d1jdbk1 1.71.1.1.1 (403-555) Carbamoyl phosphate synthetase, large subunit connection domain {(Escherichia coli)}
vgatgfdpkvslddpealtkirrelkdagadriwyiadafraglsvdgvfnltnidrwfl
vqieelvrleekvaevgitglnadflrqlkrkgfadarlaklagvreaeirklrdqydlh
pvykrvdtcaaefatdtaymystyeeeceanps
>d1jdbk2 3.15.1.1.1 (936-1072) Carbamoyl phosphate synthetase, large subunit allosteric, C-terminal domain {(Escherichia coli)}
stmkkhgrallsvregdkervvdlaakllkqgfeldathgtaivlgeaginprlvnkvhe
grphiqdrikngeytyiinttsgrraiedsrvirrsalqykvhydttlnggfatamalna
datekvisvqemhaqik
>d1jdbk3 3.23.1.1.2 (1-127) Carbamoyl phosphate synthetase (CPS), large subunit {(Escherichia coli)}
pkrtdiksililgagpivigqacefdysgaqackalreegyrvilvnsnpatimtdpema
datyiepihwevvrkiiekerpdavlptmggqtalncalelerqgvleefgvtmigatad
aidkaed
>d1jdbk4 3.23.1.1.2 (556-676) Carbamoyl phosphate synthetase (CPS), large subunit {(Escherichia coli)}
tdrekimvlgggpnrigqgiefdyccvhaslalredgyetimvncnpetvstdydtsdrl
yfepvtledvleivriekpkgvivqyggqtplklaraleaagvpvigtspdaidraedre
r
>d1jdbk5 4.89.1.2.2 (128-402) Carbamoyl phosphate synthetase (CPS), large subunit {(Escherichia coli)}
rrrfdvamkkigletarsgiahtmeealavaadvgfpciirpsftmggsgggiaynreef
eeicargldlsptkellidesligwkeyemevvrdkndnciivcsienfdamgihtgdsi
tvapaqtltdkeyqimrnasmavlreigvetggsnvqfavnpkngrliviemnprvsrss
alaskatgfpiakvaaklavgytldelmnditggrtpasfepsidyvvtkiprfnfekfa
gandrlttqmksvgevmaigrtqqeslqkalrgle
>d1jdbk6 4.89.1.2.2 (677-935) Carbamoyl phosphate synthetase (CPS), large subunit {(Escherichia coli)}
fqhaverlklkqpanatvtaiemavekakeigyplvvrpsyvlggrameivydeadlrry
fqtavsvsndapvlldhflddavevdvdaicdgemvliggimehieqagvhsgdsacslp
aytlsqeiqdvmrqqvqklafelqvrglmnvqfavknnevylievnpraartvpfvskat
gvplakvaarvmagkslaeqgvtkevippyysvkevvlpfnkfpgvdpllgpemrstgev
mgvgrtfaeafakaqlgsn
>d1jdbl1 3.5.3.1.1 (2-152) Carbamoyl phosphate synthetase, small subunit N-terminal domain {(Escherichia coli)}
iksallvledgtqfhgraigatgsavgevvfntsmtgyqeiltdpsysrqivtltyphig
nvgtndadeessqvhaqglvirdlpliasnfrntedlssylkrhnivaiadidtrkltrl
lrekgaqngciiagdnpdaalalekarafpg
>d1jdbl2 3.55.1.1.2 (153-380) Carbamoyl phosphate synthetase, small subunit C-terminal domain {(Escherichia coli)}
lngmdlakevttaeayswtqgswtltgglpqakkedelpfhvvaydfgakrnilrmlvdr
gcrltivpaqtsaedvlkmnpdgiflsngpgdpapcdyaitaiqkfletdipvfgiclgh
qllalasgaktvkmkfghhggnhpvkdveknvvmitaqnhgfavdeatlpanlrvthksl
fdgtlqgihrtdkpafsfqghpeaspgphdaaplfdhfielieqyrkt
>d1jdc_1 2.53.1.1.10 (358-418) G4-amylase (1,4-alpha-D-glucan maltotetrahydrolase {(Pseudomonas stutzeri)}
radsaisfhsgysglvatvsgsqqtlvvalnsdlgnpgqvasgsfseavnasngqvrvwr
s
>d1jdc_2 3.1.1.1.10 (1-357) G4-amylase (1,4-alpha-D-glucan maltotetrahydrolase) {(Pseudomonas stutzeri)}
dqagkspnavryhggdeiilqgfhwnvvreapndwynilrqqaatiaadgfsaiwmpvpw
rdfsswsdgsksgggegyfwhdfnkngrygsdaqlrqaasalggagvkvlydvvpnhmnr
gypdkeinlpagqgfwrndcadpgnypndcddgdrfiggdadlntghpqvygmfrdeftn
lrsqygaggfrfdfvrgyapervnswmtdsadnsfcvgqlwkgpseypnwdwrntaswqq
iikdwsdrakcpvfdfalkermqngsiadwkhglngnpdprwrevavtfvdnhdtgyspg
qnggqhhwalqdglirqayayiltspgtpvvywdhmydwgygdfirqliqvrraagv
>d1jdd_1 2.53.1.1.10 (358-418) G4-amylase (1,4-alpha-D-glucan maltotetrahydrolase {(Pseudomonas stutzeri)}
radsaisfhsgysglvatvsgsqqtlvvalnsdlgnpgqvasgsfseavnasngqvrvwr
s
>d1jdd_2 3.1.1.1.10 (1-357) G4-amylase (1,4-alpha-D-glucan maltotetrahydrolase) {(Pseudomonas stutzeri)}
dqagkspnavryhggdeiilqgfhwnvvreapndwynilrqqaatiaadgfsaiwmpvpw
rdfsswsdgsksgggegyfwhdfnkngrygsdaqlrqaasalggagvkvlydvvpnhmnr
gypdkeinlpagqgfwrndcadpgnypndcddgdrfiggdadlntghpqvygmfrdeftn
lrsqygaggfrfdfvrgyapervnswmtdsadnsfcvgqlwkgpseypnwdwrntaswqq
iikdwsdrakcpvfdfalkermqngsiadwkhglngnpdprwrevavtfvdnhdtgyspg
qnggqhhwalqdglirqayayiltspgtpvvywdhmydwgygdfirqliqvrraagv
>d1jdo__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdifirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1jdw__ 4.76.1.1.1 L-arginine: glycine amidinotransferase {Human (Homo sapiens)}
cpvssynewdpleevivgraenacvppftievkantyekywpfyqkqgghyfpkdhlkka
vaeieemcnilktegvtvrrpdpidwslkyktpdfestglysamprdilivvgneiieap
mawrsrffeyrayrsiikdyfhrgakwttapkptmadelynqdypihsvedrhklaaqgk
fvttefepcfdaadfiragrdifaqrsqvtnylgiewmrrhlapdyrvhiisfkdpnpmh
idatfniigpgivlsnpdrpchqidlfkkagwtiitpptpiipddhplwmsskwlsmnvl
mldekrvmvdanevpiqkmfeklgittikvnirnanslgggfhcwtcdvrrrgtlqsyld
>d1jdya1 3.72.1.1.1 (1-190) Phosphoglucomutase, first 3 domains {rabbit (Oryctolagus cuniculus)}
vkivtvktkaypdqkpgtsglrkrvkvfqsstnyaenfiqsiistvepaqrqeatlvvgg
dgrfymkeaiqlivriaaangigrlvigqngilstpavsciirkikaiggiiltaxhnpg
gpngdfgikfnisnggpapeaitdkifqisktieeyaicpdlkvdlgvlgkqqfdlenkf
kpftveivds
>d1jdya2 3.72.1.1.1 (191-303) Phosphoglucomutase, first 3 domains {rabbit (Oryctolagus cuniculus)}
veayatmlrnifdfnalkellsgpnrlkiridamhgvvgpyvkkilceelgapansavnc
vpledfgghhpdpnltyaadlvetmksgehdfgaafdgdgdrnmilgkhgffv
>d1jdya3 3.72.1.1.1 (304-420) Phosphoglucomutase, first 3 domains {rabbit (Oryctolagus cuniculus)}
npsdsvaviaanifsipyfqqtgvrgfarsmptsgaldrvanatkialyetptgwkffgn
lmdasklslcgeesfgtgsdhirekdglwavlawlsilatrkqsvedilkdhwhkfg
>d1jdya4 4.79.2.1.1 (421-561) Phosphoglucomutase, the C-terminal domain {rabbit (Oryctolagus cuniculus)}
rnfftrydyeeveaegatkmmkdlealmfdrsfvgkqfsandkvytvekadnfeyhdpvd
gsvsknqglrlifadgsriifrlsgtgsagatirlyidsyekdnakinqdpqvmlaplis
ialkvsqlqertgrtaptvit
>d1jdyb1 3.72.1.1.1 (1-190) Phosphoglucomutase, first 3 domains {rabbit (Oryctolagus cuniculus)}
vkivtvktkaypdqkpgtsglrkrvkvfqsstnyaenfiqsiistvepaqrqeatlvvgg
dgrfymkeaiqlivriaaangigrlvigqngilstpavsciirkikaiggiiltaxhnpg
gpngdfgikfnisnggpapeaitdkifqisktieeyaicpdlkvdlgvlgkqqfdlenkf
kpftveivds
>d1jdyb2 3.72.1.1.1 (191-303) Phosphoglucomutase, first 3 domains {rabbit (Oryctolagus cuniculus)}
veayatmlrnifdfnalkellsgpnrlkiridamhgvvgpyvkkilceelgapansavnc
vpledfgghhpdpnltyaadlvetmksgehdfgaafdgdgdrnmilgkhgffv
>d1jdyb3 3.72.1.1.1 (304-420) Phosphoglucomutase, first 3 domains {rabbit (Oryctolagus cuniculus)}
npsdsvaviaanifsipyfqqtgvrgfarsmptsgaldrvanatkialyetptgwkffgn
lmdasklslcgeesfgtgsdhirekdglwavlawlsilatrkqsvedilkdhwhkfg
>d1jdyb4 4.79.2.1.1 (421-561) Phosphoglucomutase, the C-terminal domain {rabbit (Oryctolagus cuniculus)}
rnfftrydyeeveaegatkmmkdlealmfdrsfvgkqfsandkvytvekadnfeyhdpvd
gsvsknqglrlifadgsriifrlsgtgsagatirlyidsyekdnakinqdpqvmlaplis
ialkvsqlqertgrtaptvit
>d1jea__ 3.33.1.1.5 Subtilisin BL {(Bacillus lentus)}
aqsvpwgisrvqapaahnrgltgsgvkvavldtgisthpdlnirggasfvpgepstqdgn
ghgthvagtiaalnnsigvlgvapsaelyavkvlgasgsgsvssiaqglewagnngmhva
nlslgspspsatleqavnsatsrgvlvvaasgnsgagsisyparyanamavgatdqnnnr
asfsqygagldivapgvnvqstypgstyaslngtsmatphvagaaalvkqknpswsnvqi
rnhlkntatslgstnlygsglvnaeaatr
>d1jef__ 4.2.1.2.2 Lysozyme {turkey (Meleagris gallopavo)}
kvygrcelaaamkrlgldnyrgyslgnwvcaakfesnfnthatnrntdgstdygilqins
rwwcndgrtpgsknlcnipcsallssditasvncakkiasggngmnawvawrnrckgtdv
hawirgcrl
>d1jem__ 4.54.1.1.1 Histidine-containing phosphocarrier proteins (HPr) {(Bacillus subtilis)}
aqktfkvtadsgixarpatvlvqtaskydadvnleyngktvnlksimgvvslgiakgaei
tisasgadendalnaleetmkseglge
>d1jer__ 2.5.1.1.21 Stellacyanin {cucumber (Cucumis sativus)}
mqstvhivgdntgwsvpsspnfysqwaagktfrvgdslqfnfpanahnvhemetkqsfda
cnfvnsdndvertspvierldelgmhyfvctvgthcsngqklsinvvaan
>d1jeta_ 3.82.1.1.1 Oligo-peptide binding protein (OPPA) {(Salmonella typhimurium)}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1jeua_ 3.82.1.1.1 Oligo-peptide binding protein (OPPA) {(Salmonella typhimurium)}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1jeva_ 3.82.1.1.1 Oligo-peptide binding protein (OPPA) {(Salmonella typhimurium)}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1jfda_ 2.29.5.1.2 Inorganic pyrophosphatase {(Escherichia coli)}
sllnvpagkdlpediyvvieipanadpikyeidkesgalfvdrfmstamfypcnygyinh
tlsldgdpvdvlvptpyplqpgsvircrpvgvlkmtdeagedaklvavphsklskeydhi
kdvndlpellkaqiahffehykdlekgkwvkvegwenaeaakaeivasferaknk
>d1jfdb_ 2.29.5.1.2 Inorganic pyrophosphatase {(Escherichia coli)}
sllnvpagkdlpediyvvieipanadpikyeidkesgalfvdrfmstamfypcnygyinh
tlsldgdpvdvlvptpyplqpgsvircrpvgvlkmtdeagedaklvavphsklskeydhi
kdvndlpellkaqiahffehykdlekgkwvkvegwenaeaakaeivasferaknk
>d1jfo__ 1.47.1.2.2 Trypsin/alpha-amylase inhibitor RBI {Ragi (Elucine coracana gaertneri) seeds}
svgtscipgmaiphnpldscrwyvstrtcgvgprlatqemkarccrqleaipaycrceav
rilmdgvvtpsgqhegrllqdlpgcprqvqrafapklvtevecnlatihggpfclsllga
ge
>d1jfra_ 3.56.1.8.1 Lipase {(Streptomyces exfoliatus)}
npyergpaptnasieasrgpyatsqtsvsslvasgfgggtiyyptstadgtfgavvispg
ftayqssiawlgprlasqgfvvftidtnttldqpdsrgrqllsaldyltqrssvrtrvda
trlgvmghsmggggsleaaksrtslkaaipltgwntdktwpelrtptlvvgadgdtvapv
athskpfyeslpgsldkaylelrgashftpntsdttiakysiswlkrfidsdtryeqflc
piprpsltiaeyrgtcphts
>d1jfrb_ 3.56.1.8.1 Lipase {(Streptomyces exfoliatus)}
npyergpaptnasieasrgpyatsqtsvsslvasgfgggtiyyptstadgtfgavvispg
ftayqssiawlgprlasqgfvvftidtnttldqpdsrgrqllsaldyltqrssvrtrvda
trlgvmghsmggggsleaaksrtslkaaipltgwntdktwpelrtptlvvgadgdtvapv
athskpfyeslpgsldkaylelrgashftpntsdttiakysiswlkrfidsdtryeqflc
piprpsltiaeyrgtcphts
>d1jhga_ 1.85.1.1.1 Trp repressor {(Escherichia coli)}
saamaeqrhqewlrfvdllknayqndlhlpllnlmltpderealgtrvriieellrgems
qrelknelgagiatitrgsnslkaapvelrqwleevllksd
>d1jhla_ 4.2.1.2.4 Lysozyme {pheasant (Phasianus colchicus)}
kvygrcelaaamkrmgldnyrgyslgnwvcaakfesnfntgatnrntdgstdygilqins
rwwcndgrtpgsknlchipcsallssditasvncakkivsdgdgmnawvawrkhckgtdv
nvwirgcrl
>d1jhlh_ 2.1.1.1.40 Immunoglobulin (variable domains of L and H chains) {Fv D11.15 (mouse), kappa L chain}
qvqlqqsgaelvrpgasvklsckasgytfisywinwvkqrpgqglewigniypsdsytny
nqkfkdkatltvdkssstaymqlssptsedsavyyctrddnygamdywgqgttvtv
>d1jhll_ 2.1.1.1.40 Immunoglobulin (variable domains of L and H chains) {Fv D11.15 (mouse), kappa L chain}
dieltqspsylvaspgetitincrasksiskslawyqekpgktnnlliysgstlqsgips
rfsgsgsgtdftltisslepedfamyicqqhneypwtfgggtkleikr
>d1jiaa_ 1.103.1.2.4 Snake phospholipase A2 {chinese water moccasin (Agkistrodon halys pallas), different isoforms}
hllqfrkmikkmtgkepvvsyafygcycgsggrgkpkdatdrccfvhdccyekvtgcdpk
wddytyswkngtivcggddpckkevcecdkaaaicfrdnlktykkrymaypdilcsskse
kc
>d1jiab_ 1.103.1.2.4 Snake phospholipase A2 {chinese water moccasin (Agkistrodon halys pallas), different isoforms}
hllqfrkmikkmtgkepvvsyafygcycgsggrgkpkdatdrccfvhdccyekvtgcdpk
wddytyswkngtivcggddpckkevcecdkaaaicfrdnlktykkrymaypdilcsskse
kc
>d1jim__ 2.35.1.2.14 Elastase {porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1jka__ 4.2.1.2.8 Lysozyme {human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwdsgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1jkb__ 4.2.1.2.8 Lysozyme {human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwasgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1jkc__ 4.2.1.2.8 Lysozyme {human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirafvawrnrcqnrd
vrqyvqgcgv
>d1jkd__ 4.2.1.2.8 Lysozyme {human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgiraavawrnrcqnrd
vrqyvqgcgv
>d1jkw_1 1.63.1.1.3 (11-161) Cyclin h (mcs2) {human (Homo sapiens)}
wtfsseeqlarlradanrkfrckavangkvlpndpvflepheemtlckyyekrllefcsv
fkpamprsvvgtacmyfkrfylnnsvmeyhpriimltcaflackvdefnvsspqfvgnlr
esplgqekaleqileyellliqqlnfhlivh
>d1jkw_2 1.63.1.1.3 (162-287) Cyclin h (mcs2) {human (Homo sapiens)}
npyrpfegflidlktrypilenpeilrktaddflnrialtdayllytpsqialtailssa
sragitmesylseslmlkenrtclsqlldimksmrnlvkkyepprseevavlkqkldrch
saelal
>d1jlda_ 2.38.1.1.3 Human immunodeficiency virus type 2 protease {HIV-2 (rod isolate)}
pqfslwkrpvvtayiegqpvevlldtgaddsivagielgnnyspkivggiggfintkeyk
nveievlnkkvratimtgdtpinifgrniltalgmslnl
>d1jldb_ 2.38.1.1.3 Human immunodeficiency virus type 2 protease {HIV-2 (rod isolate)}
pqfslwkrpvvtayiegqpvevlldtgaddsivagielgnnyspkivggiggfintkeyk
nveievlnkkvratimtgdtpinifgrniltalgmslnl
>d1jli__ 1.26.1.2.6 Interleukin-3 (IL-3) {human (Homo sapiens)}
ancsimideiihhlkrppnplldpnnlnsedmdilmernlrtpnllafvravkhlenasa
iesilknllpclplataaptrhpihikdgdwnefrrkltfylktlenaqaqq
>d1jlm__ 3.50.1.1.3 Integrin CR3 (CD11b/CD18), alpha subunit {Human (Homo sapiens)}
dsdiaflidgsgsiiphdfrrmkefvstvmeqlkksktlfslmqyseefrihftfkefqn
npnprslvkpitqllgrthtatgirkvvrelfnitngarknafkilvvitdgekfgdplg
yedvipeadregviryvigvgdafrseksrqelntiaskpprdhvfqvnnfealktiqnq
lrekifa
>d1jlxa1 2.31.3.1.1 (1-153) Agglutinin {Love-lies-bleeding (Amaranthus caudatus)}
aglpvimclksnnhqkylryqsdniqqygllqfsadkildplaqfevepsktydglvhik
srytnkylvrwspnhywitasanepdenksnwactlfkplyveegnmkkvrllhvqlghy
tqnytvggsfvsylfaessqidtgskdvfhvid
>d1jlxa2 2.31.3.1.1 (154-299) Agglutinin {Love-lies-bleeding (Amaranthus caudatus)}
wksifqfpkgyvtfkgnngkylgvitinqlpclqfgydnlndpkvahqmfvtsngticik
snymnkfwrlstddwilvdgndpretneaaalfrsdvhdfnvisllnmqktwfikrftsg
kpgfincmnaatqnvdetaileiiel
>d1jlxb1 2.31.3.1.1 (1-153) Agglutinin {Love-lies-bleeding (Amaranthus caudatus)}
aglpvimclksnnhqkylryqsdniqqygllqfsadkildplaqfevepsktydglvhik
srytnkylvrwspnhywitasanepdenksnwactlfkplyveegnmkkvrllhvqlghy
tqnytvggsfvsylfaessqidtgskdvfhvid
>d1jlxb2 2.31.3.1.1 (154-299) Agglutinin {Love-lies-bleeding (Amaranthus caudatus)}
wksifqfpkgyvtfkgnngkylgvitinqlpclqfgydnlndpkvahqmfvtsngticik
snymnkfwrlstddwilvdgndpretneaaalfrsdvhdfnvisllnmqktwfikrftsg
kpgfincmnaatqnvdetaileiiel
>d1jlya1 2.31.3.1.1 (1-153) Agglutinin {Love-lies-bleeding (Amaranthus caudatus)}
aglpvimclksnnhqkylryqsdniqqygllqfsadkildplaqfevepsktydglvhik
srytnkylvrwspnhywitasanepdenksnwactlfkplyveegnmkkvrllhvqlghy
tqnytvggsfvsylfaessqidtgskdvfhvid
>d1jlya2 2.31.3.1.1 (154-299) Agglutinin {Love-lies-bleeding (Amaranthus caudatus)}
wksifqfpkgyvtfkgnngkylgvitinqlpclqfgydnlndpkvahqmfvtsngticik
snymnkfwrlstddwilvdgndpretneaaalfrsdvhdfnvisllnmqktwfikrftsg
kpgfincmnaatqnvdetaileiiel
>d1jlyb1 2.31.3.1.1 (1-153) Agglutinin {Love-lies-bleeding (Amaranthus caudatus)}
aglpvimclksnnhqkylryqsdniqqygllqfsadkildplaqfevepsktydglvhik
srytnkylvrwspnhywitasanepdenksnwactlfkplyveegnmkkvrllhvqlghy
tqnytvggsfvsylfaessqidtgskdvfhvid
>d1jlyb2 2.31.3.1.1 (154-299) Agglutinin {Love-lies-bleeding (Amaranthus caudatus)}
wksifqfpkgyvtfkgnngkylgvitinqlpclqfgydnlndpkvahqmfvtsngticik
snymnkfwrlstddwilvdgndpretneaaalfrsdvhdfnvisllnmqktwfikrftsg
kpgfincmnaatqnvdetaileiiel
>d1jmca1 2.29.4.3.3 (183-298) Replication protein A fragment {human (Homo sapiens)}
kvvpiasltpyqskwticarvtnksqirtwsnsrgegklfslelvdesgeiratafneqv
dkffplievnkvyyfskgtlkiankqftavkndyemtfnnetsvmpceddhhlptv
>d1jmca2 2.29.4.3.3 (299-420) Replication protein A fragment {human (Homo sapiens)}
qfdftgiddlenkskdslvdiigicksyedatkitvrsnnrevakrniylmdtsgkvvta
tlwgedadkfdgsrqpvlaikgarvsdfggrslsvlssstiianpdipeayklrgwfdae
gq
>d1jmf__ 4.67.1.1.2 Thymidylate synthase {(Lactobacillus casei )}
mleqpyldlakkvldeghfkpdrthtgtysifghqmrfdlskgfpllttkkvpfglikse
llwflhgdtnirfllqhrnhiwdewafekwvksdeyhgpdmtdfghrsqkdpefaavyhe
emakfddrvlhddafaakygdlglvygsqwrawhtskgdtidqlgdvieqikthpysrrl
ivsawnpedvptmalppchtlyqfyvndgklslqlyqrsadiflgvpfaiasyallthlv
ahecglevgefihtfgdahlyvnhldqikeqlsrtprpaptlqlnpdkhdifdfdmkdik
llnydpypaikapvav
>d1jmg__ 4.67.1.1.2 Thymidylate synthase {(Lactobacillus casei )}
mleqpyldlakkvldeghfkpdrthtgtysifghqmrfdlskgfpllttkkvpfglikse
llwflhgdtnirfllqhrnhiwdewafekwvksdeyhgpdmtdfghrsqkdpefaavyhe
emakfddrvlhddafaakygdlglvygsqwrawhtskgdtidqlgdvieqikthpysrrl
ivsawnpedvptmalppchtlyqfyvndgklslqlyqrsadiflgvpfgiasyallthlv
ahecglevgefihtfgdahlyvnhldqikeqlsrtprpaptlqlnpdkhdifdfdmkdik
llnydpypaikapvav
>d1jmh__ 4.67.1.1.2 Thymidylate synthase {(Lactobacillus casei )}
mleqpyldlakkvldeghfkpdrthtgtysifghqmrfdlskgfpllttkkvpfglikse
llwflhgdtnirfllqhrnhiwdewafekwvksdeyhgpdmtdfghrsqkdpefaavyhe
emakfddrvlhddafaakygdlglvygsqwrawhtskgdtidqlgdvieqikthpysrrl
ivsawnpedvptmalppchtlyqfyvndgklslqlyqrsadiflgvpfiiasyallthlv
ahecglevgefihtfgdahlyvnhldqikeqlsrtprpaptlqlnpdkhdifdfdmkdik
llnydpypaikapvav
>d1jmi__ 4.67.1.1.2 Thymidylate synthase {(Lactobacillus casei )}
mleqpyldlakkvldeghfkpdrthtgtysifghqmrfdlskgfpllttkkvpfglikse
llwflhgdtnirfllqhrnhiwdewafekwvksdeyhgpdmtdfghrsqkdpefaavyhe
emakfddrvlhddafaakygdlglvygsqwrawhtskgdtidqlgdvieqikthpysrrl
ivsawnpedvptmalppchtlyqfyvndgklslqlyqrsadiflgvpfsiasyallthlv
ahecglevgefihtfgdahlyvnhldqikeqlsrtprpaptlqlnpdkhdifdfdmkdik
llnydpypaikapvav
>d1joa_1 3.4.1.4.7 (1-119,243-321) NADH peroxidase {(Streptococcus, Enterococcus faecalis)}
mkvivlgsshggyeaveellnlhpdaeiqwyekgdfisflsxgmqlylegkvkdvnsvry
mtgekmesrgvnvfsnteitaiqpkehqvtvkdlvsgeervenydkliispgavpfeldX
gvrpntawlkgtlelhpngliktdeymrtsepdvfavgdatlikynpadtevnialatna
rkqgrfavknleepvkpfp
>d1joa_2 3.4.1.4.7 (120-242) NADH peroxidase {(Streptococcus, Enterococcus faecalis)}
ipgkdldniylmrgrqwaiklkqktvdpevnnvvvigsgyigieaaeafakagkkvtvid
ildrplgvyldkeftdvlteemeannitiatgetveryegdgrvqkvvtdknaydadlvv
vav
>d1joa_3 4.48.1.1.5 (322-447) NADH peroxidase {(Enterococcus faecalis)}
gvqgssglavfdykfastginevmaqklgketkavtvvedylmdfnpdkqkawfklvydp
ettqilgaqlmskadltaninaislaiqakmtiedlayadfffqpafdkpwniintaale
avkqer
>d1joi__ 2.5.1.1.18 Azurin {(Pseudomanas fluorescens)}
aeckvtvdstdqmsfntkaieidkscktftvelthsgslpknvmghnwvlssaadmpgia
sdgmaagidknylkegdtrviahtkiigagekdsvtfdvsklaagtdyaffcsfpghism
mkgtvtvk
>d1jola_ 3.60.1.1.1 Dihydrofolate reductase, prokaryotic type {(Escherichia coli)}
misliaalavdrvigmenampwnlpadlawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1jolb_ 3.60.1.1.1 Dihydrofolate reductase, prokaryotic type {(Escherichia coli)}
misliaalavdrvigmenampwnlpadlawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1jom__ 3.60.1.1.1 Dihydrofolate reductase, prokaryotic type {(Escherichia coli)}
misliaalavdrvigmenampwnlpadlawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d1jon__ 3.5.4.1.1 GroEL {(Escherichia coli)}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgv
>d1jpc__ 2.60.1.1.1 Lectin (agglutinin) {Snowdrop (Galanthus nivalis)}
dnilysgetlstgeflnygsfvfimqedcnlvlydvdkpiwatntgglsrscflsmqtdg
nlvvynpsnkpiwasntggqngnyvcilqkdrnvviygtdrwatgtht
>d1jpo__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1jrhh1 2.1.1.1.96 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab A6 (mouse), kappa L chain}
avklqesgpgilkpsqtlsltcsfsgfslttygmgvgwirqssgkglewlahiwwdddky
ynpslksrltiskdtsrnqvflkitsvatadtatyycarrapfygnhamdywgqgttvtv
ss
>d1jrhh2 2.1.1.2.96 (114-219) Immunoglobulin (constant domains of L and H chains) {Fab A6 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpssprpsetvtcnvahpasstkv
>d1jrhi_ 2.1.2.1.11 Interferon-gamma receptor alpha chain {human (Homo sapiens)}
svptptnvtiesynmnpivyweyqimpqvpvftvevknygvknsewidacinishhycni
sdhvgdpsnslwvrvkarvgqkesayakseefavs
>d1jrhl1 2.1.1.1.96 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab A6 (mouse), kappa L chain}
svemtqspssfsvslgdrvtitckasediynrlawyqqkpgnaprllisgatsletevps
rfsgsgsgkdytlsitslqtedvatyycqqywstwtfgggtkleik
>d1jrhl2 2.1.1.2.96 (108-207) Immunoglobulin (constant domains of L and H chains) {Fab A6 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivk
>d1jrsa_ 2.35.1.2.1 Trypsin(ogen) {bovine (Bos taurus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1jrta_ 2.35.1.2.1 Trypsin(ogen) {bovine (Bos taurus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1js4a1 1.81.1.2.2 (1-460) Endo/exocellulase:cellobiose E-4, N-terminal domain {(Thermomonospora fusca)}
epafnyaealqksmffyeaqrsgklpennrvswrgdsglndgadvgldltggwydagdhv
kfgfpmaftatmlawgaiespegyirsgqmpylkdnlrwvndyfikahpspnvlyvqvgd
gdadhkwwgpaevmpmerpsfkvdpscpgsdvaaetaaamaassivfadddpayaatlvq
hakqlytfadtyrgvysdcvpagafynswsgyqdelvwgaywlykatgddsylakaeyey
dflsteqqtdlrsyrwtiawddksygtyvllaketgkqkyiddanrwldywtvgvngqrv
pyspggmavldtwgalryaantafvalvyakviddpvrkqryhdfavrqinyalgdnprn
ssyvvgfgnnpprnphhrtahgswtdsiaspaenrhvlygalvggpgspndaytddrqdy
vanevatdynagfssalamlveeyggtpladfppteepdg
>d1js4a2 2.2.2.2.2 (461-605) Endo/exocellulase:cellobiose E-4, C-terminal domain {(Thermomonospora fusca)}
peifveaqintpgttfteikamirnqsgwparmldkgtfrywftldegvdpaditvssay
nqcatpedvhhvsgdlyyveidctgekifpggqsehrrevqfriaggpgwdpsndwsfqg
ignelapapyivlyddgvpvwgtap
>d1js4b1 1.81.1.2.2 (1-460) Endo/exocellulase:cellobiose E-4, N-terminal domain {(Thermomonospora fusca)}
epafnyaealqksmffyeaqrsgklpennrvswrgdsglndgadvgldltggwydagdhv
kfgfpmaftatmlawgaiespegyirsgqmpylkdnlrwvndyfikahpspnvlyvqvgd
gdadhkwwgpaevmpmerpsfkvdpscpgsdvaaetaaamaassivfadddpayaatlvq
hakqlytfadtyrgvysdcvpagafynswsgyqdelvwgaywlykatgddsylakaeyey
dflsteqqtdlrsyrwtiawddksygtyvllaketgkqkyiddanrwldywtvgvngqrv
pyspggmavldtwgalryaantafvalvyakviddpvrkqryhdfavrqinyalgdnprn
ssyvvgfgnnpprnphhrtahgswtdsiaspaenrhvlygalvggpgspndaytddrqdy
vanevatdynagfssalamlveeyggtpladfppteepdg
>d1js4b2 2.2.2.2.2 (461-605) Endo/exocellulase:cellobiose E-4, C-terminal domain {(Thermomonospora fusca)}
peifveaqintpgttfteikamirnqsgwparmldkgtfrywftldegvdpaditvssay
nqcatpedvhhvsgdlyyveidctgekifpggqsehrrevqfriaggpgwdpsndwsfqg
ignelapapyivlyddgvpvwgtap
>d1jsa__ 1.37.1.5.20 Recoverin {human (Homo sapiens)}
xgnsksgalskeileelqlntkfteeelsswyqsflkecpsgritrqefqtiyskffpea
dpkayaqhvfrsfdansdgtldfkeyvialhmtsagktnqklewafslydvdgngtiskn
evleivtaifkmispedtkhlpedentpekraekiwgffgkkdddkltekefiegtlank
eilrliqfe
>d1jse__ 4.2.1.2.2 Lysozyme {turkey (Meleagris gallopavo)}
kvygrcelaaamkrlgldnyrgyslgnwvcaakfesnfnthatnrntdgstdygilqins
rwwcndgrtpgsknlcnipcsallssditasvncakkiasggngmnawvawrnrckgtdv
hawirgcrl
>d1jsf__ 4.2.1.2.8 Lysozyme {human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1jsg__ 2.48.1.1.1 p14-TCL1 {Human (Homo sapiens)}
cptlgeavtdhpdrlwawekfvyldekqhawlpltieikdrlqlrvllrredvvlgrpmt
ptqigpsllpimwqlypdgryrssdssfwrlvyhikidgvedmllellpdd
>d1jsta_ 5.1.1.1.1 Cyclin-dependent PK {Human (Homo sapiens)}
menfqkvekigegtygvvykarnkltgevvalkkirldtetegvpstaireisllkelnh
pnivklldvihtenklylvfeflhqdlkkfmdasaltgiplpliksylfqllqglafchs
hrvlhrdlkpqnllintegaikladfglarafgvpvrtyxhevvtlwyrapeillgckyy
stavdiwslgcifaemvtrralfpgdseidqlfrifrtlgtpdevvwpgvtsmpdykpsf
pkwarqdfskvvppldedgrsllsqmlhydpnkrisakaalahpffqdvtkpvphlrl
>d1jstb1 1.63.1.1.1 (175-309) Cyclin A {Human (Homo sapiens)}
vpdyhedihtylremevkckpkvgymkkqpditnsmrailvdwlvevgeeyklqnetlhl
avnyidrflssmsvlrgklqlvgtaamllaskfeeiyppevaefvyitddtytkkqvlrm
ehlvlkvltfdlaap
>d1jstb2 1.63.1.1.1 (310-432) Cyclin A {Human (Homo sapiens)}
tvnqfltqyflhqqpanckveslamflgelslidadpylkylpsviagaafhlalytvtg
qswpeslirktgytleslkpclmdlhqtylkapqhaqqsirekyknskyhgvsllnppet
lnl
>d1jstc_ 5.1.1.1.1 Cyclin-dependent PK {Human (Homo sapiens)}
menfqkvekigegtygvvykarnkltgevvalkkirldtetegvpstaireisllkelnh
pnivklldvihtenklylvfeflhqdlkkfmdasaltgiplpliksylfqllqglafchs
hrvlhrdlkpqnllintegaikladfglarafgvpvrtyxhevvtlwyrapeillgckyy
stavdiwslgcifaemvtrralfpgdseidqlfrifrtlgtpdevvwpgvtsmpdykpsf
pkwarqdfskvvppldedgrsllsqmlhydpnkrisakaalahpffqdvtkpvphlrl
>d1jstd1 1.63.1.1.1 (175-309) Cyclin A {Human (Homo sapiens)}
vpdyhedihtylremevkckpkvgymkkqpditnsmrailvdwlvevgeeyklqnetlhl
avnyidrflssmsvlrgklqlvgtaamllaskfeeiyppevaefvyitddtytkkqvlrm
ehlvlkvltfdlaap
>d1jstd2 1.63.1.1.1 (310-432) Cyclin A {Human (Homo sapiens)}
tvnqfltqyflhqqpanckveslamflgelslidadpylkylpsviagaafhlalytvtg
qswpeslirktgytleslkpclmdlhqtylkapqhaqqsirekyknskyhgvsllnppet
lnl
>d1jsua_ 5.1.1.1.1 Cyclin-dependent PK {Human (Homo sapiens)}
gtygvvykarnkltgevvalkkirldtetegvpstaireisllkelnhpnivklldviht
enklylvfeflhqdlkkfmdasaltgiplpliksylfqllqglafchshrvlhrdlkpqn
llintegaikladfglarafgvpvrtyxhevvtlwyrapeillgckyystavdiwslgci
faemvtrralfpgdseidqlfrifrtlgtpdevvwpgvtsmpdykpsfpkwarqdfskvv
ppldedgrsllsqmlhydpnkrisakaalahpffqdvtkpvphlrl
>d1jsub1 1.63.1.1.1 (175-309) Cyclin A {Human (Homo sapiens)}
vpdyhedihtylremevkckpkvgymkkqpditnsmrailvdwlvevgeeyklqnetlhl
avnyidrflssmsvlrgklqlvgtaamllaskfeeiyppevaefvyitddtytkkqvlrm
ehlvlkvltfdlaap
>d1jsub2 1.63.1.1.1 (310-432) Cyclin A {Human (Homo sapiens)}
tvnqfltqyflhqqpanckveslamflgelslidadpylkylpsviagaafhlalytvtg
qswpeslirktgytleslkpclmdlhqtylkapqhaqqsirekyknskyhgvsllnppet
lnl
>d1jswa_ 1.98.1.1.1 L-aspartate ammonia lyase {(Escherichia coli)}
msnnirieedllgtrevpadayygvhtlraienfyisnnkisdipefvrgmvmvkkaaam
ankelqtipksvanaiiaacdevlnngkcmdqfpvdvyqggagtsvnmntnevlanigle
lmghqkgeyqylnpndhvnkcqstndayptgfriavyssliklvdainqlregferkave
fqdilkmgrtqlqdavpmtlgqefrafsillkeevkniqrtaelllevnlgataigtgln
tpkeysplavkklaevtgfpcvpaedlieatsdcgayvmvhgalkrlavkmskicndlrl
lssgpraglneinlpelqagssimpakvnpvvpevvnqvcfkvigndttvtmaaeagqlq
lnvmepvigqamfesvhiltnacynllekcingitankevcegyvynsigivtylnpfig
hhngdivgkicaetgksvrevvlergllteaelddifsv
>d1jswb_ 1.98.1.1.1 L-aspartate ammonia lyase {(Escherichia coli)}
msnnirieedllgtrevpadayygvhtlraienfyisnnkisdipefvrgmvmvkkaaam
ankelqtipksvanaiiaacdevlnngkcmdqfpvdvyqggagtsvnmntnevlanigle
lmghqkgeyqylnpndhvnkcqstndayptgfriavyssliklvdainqlregferkave
fqdilkmgrtqlqdavpmtlgqefrafsillkeevkniqrtaelllevnlgataigtgln
tpkeysplavkklaevtgfpcvpaedlieatsdcgayvmvhgalkrlavkmskicndlrl
lssgpraglneinlpelqagssimpakvnpvvpevvnqvcfkvigndttvtmaaeagqlq
lnvmepvigqamfesvhiltnacynllekcingitankevcegyvynsigivtylnpfig
hhngdivgkicaetgksvrevvlergllteaelddifsvq
>d1jswc_ 1.98.1.1.1 L-aspartate ammonia lyase {(Escherichia coli)}
irieedllgtrevpadayygvhtlraienfyisnnkisdipefvrgmvmvkkaaamanke
lqtipksvanaiiaacdevlnngkcmdqfpvdvyqggagtsvnmntnevlaniglelmgh
qkgeyqylnpndhvnkcqstndayptgfriavyssliklvdainqlregferkavefqdi
lkmgrtqlqdavpmtlgqefrafsillkeevkniqrtaelllevnlgataigtglntpke
ysplavkklaevtgfpcvpaedlieatsdcgayvmvhgalkrlavkmskicndlrllssg
praglneinlpelqagssimpakvnpvvpevvnqvcfkvigndttvtmaaeagqlqlnvm
epvigqamfesvhiltnacynllekcingitankevcegyvynsigivtylnp
>d1jswd_ 1.98.1.1.1 L-aspartate ammonia lyase {(Escherichia coli)}
msnnirieedllgtrevpadayygvhtlraienfyisnnkisdipefvrgmvmvkkaaam
ankelqtipksvanaiiaacdevlnngkcmdqfpvdvyqggagtsvnmntnevlanigle
lmghqkgeyqylnpndhvnkcqstndayptgfriavyssliklvdainqlregferkave
fqdilkmgrtqlqdavpmtlgqefrafsillkeevkniqrtaelllevnlgataigtgln
tpkeysplavkklaevtgfpcvpaedlieatsdcgayvmvhgalkrlavkmskicndlrl
lssgpraglneinlpelqagssimpakvnpvvpevvnqvcfkvigndttvtmaaeagqlq
lnvmepvigqamfesvhiltnacynllekcingitankevcegyvynsigivtylnpfig
hhngdivgkicaetgksvrevvlergllteaelddifsv
>d1jtb__ 1.47.1.1.3 plant non-specific lipid-transfer protein (ns-LTP) {Barley (Hordeum vulgare)}
lncgqvdskmkpcltyvqggpgpsgeccngvrdlhnqaqssgdrqtvcnclkgiargihn
lnlnnaasipskcnvnvpytispdidcsriy
>d1jud__ 5.18.1.1.1 L-2-Haloacid dehalogenase {(Pseudomonas sp)}
yikgiafdlygtlfdvhsvvgrcdeafpgrgreisalwrqkqleytwlrslmnryvnfqq
atedalrftcrhlgldldartrstlcdaylrlapfsevpdslrelkrrglklailsngsp
qsidavvshaglrdgfdhllsvdpvqvykpdnrvyelaeqalgldrsailfvssnawdat
garyfgfptcwinrtgnvfeemgqtpdwevtslravvelf
>d1jug__ 4.2.1.2.10 Lysozyme {Australian echidna (Tachyglossus aculeatus)}
kilkkqelcknlvaqgmngyqhitlpnwvctafhessyntratnhntdgstdygilqins
rywchdgktpgsknacniscskllddditddlkcakkiageakgltpwvawkskcrghdl
skfkc
>d1juk__ 3.1.8.1.4 Indole-3-glycerophosphate (IGP) synthase {(Sulfolobus solfataricus)}
prylkgwlkdvvqlslrrpsfrasrqrpiislnerilefnkrnitaiiaeykrkspsgld
verdpieyskfmeryavglsilteekyfngsyetlrkiassvsipilmkdfivkesqidd
aynlgadtvllivkiltereleslleyarsygmeplieindendldialrigarfigins
rdletleinkenqrklismipsnvvkvaesgiserneieelrklgvnafligsslmrnpe
kikefil
>d1jul__ 3.1.8.1.4 Indole-3-glycerophosphate (IGP) synthase {(Sulfolobus solfataricus)}
prylkgwlkdvvqlslrrpsfrasrqrpiislnerilefnkrnitaiiaeykrkspsgld
verdpieyskfmeryavglsilteekyfngsyetlrkiassvsipilmkdfivkesqidd
aynlgadtvllivkiltereleslleyarsygmeplieindendldialrigarfigins
rdletleinkenqrklismipsnvvkvaesgiserneieelrklgvnafligsslmrnpe
kikefil
>d1juna_ 1.105.2.1.6 C-jun {Human (Homo sapiens)}
cggriarleekvktlkaqnselastanmlreqvaqlkqkvmny
>d1junb_ 1.105.2.1.6 C-jun {Human (Homo sapiens)}
cggriarleekvktlkaqnselastanmlreqvaqlkqkvmny
>d1juy__ 3.29.1.6.2 Adenylosuccinate synthetase (gene purA product) {(Escherichia coli)}
gnnvvvlgtqwgdegkgkivdllterakyvvryqgghnaghtlvingektvlhlipsgil
renvtsiigngvvlspaalmkemkeledrgipvrerlllseacplildyhvaldnareka
rgakaigttgrgigpayedkvarrglrvgdlfdketfaeklkevmeyhnfqlvnyykaea
vdyqkvlddtmavadiltsmvvdvsdlldqarqrgdfvmfegaqgtlldidhgtypyvts
snttaggvatgsglgpryvdyvlgilkaystrvgagpfptelfdetgeflckqgnefgat
tgrrrrtgwldtvavrravqlnslsgfcltkldvldglkevklcvayrmpdgrevtttpl
aaddwkgvepiyetmpgwsestfgvkdrsglpqaalnyikrieeltgvpidiistgpdrt
etmilrdpfda
>d1jvr__ 1.62.1.2.1 HTLV-II matrix protein {TTLV-II (Human t-cell leukemia virus type II)}
hmgqihglsptpipkaprglsthhwlnflqaayrlqpgpsdfdfqqlrrflklalktpiw
lnpidysllaslipkgypgrvveiinilvknqvspsapaapvptpicptttpppppppsp
eahvpppyveptttqcf
>d1jxe_1 3.47.3.4.2 (293-450) Exonuclease domain of DNA polymerase {(Thermus aquaticus)}
aleeapwpppegafvgfvlsrkepmwadllalaaarggrvhrapepykalrdlkeargll
akdlsvlalreglglppgddpmllaylldpsnttpegvarryggewteeageraalserl
fanlwgrlegeerllwlyreverplsavlahmeatgvr
>d1jxe_2 5.9.1.1.2 (451-832) DNA polymerase I (Klenow fragment) {(Thermus aquaticus)}
ldvaylralslevaeeiarleaevfrlaghpfnlnsrdqlervlfdelglpaigktektg
krstsaavlealreahpivekilqyreltklkstyidplpdlihprtgrlhtrfnqtata
tgrlsssdpnlqnipvrtplgqrirrafiaeegwllvaldysqielrvlahlsgdenlir
vfqegrdihtetaswmfgvpreavdplmrraaktinfgvlygmsahrlsqelaipyeeaq
afieryfqsfpkvrawiektleegrrrgyvetlfgrrryvpdlearvksvreaaermafn
mpvqgtaadlmklamvklfprleemgarmllqvhdelvleapkeraeavarlakevmegv
yplavplevevgigedwlsake
>e1jxp.1a 2.35.1.3.3 NS3 protease {(Human hepatitis C virus) Bk strain}
itaysqqtrgllgciitsltgrdknqvegevqvvstatqsflatcvngvcwtvyhgagsk
tlagpkgpitqmytnvdqdlvgwqappgarsltpctcgssdlylvtrhadvipvrrrgds
rgsllsprpvsylkgssggpllcpsghavgifraavctrgvakavdfvpvesmettm
>e1jxp.2b 2.35.1.3.3 NS3 protease {(Human hepatitis C virus) Bk strain}
itaysqqtrgllgciitsltgrdknqvegevqvvstatqsflatcvngvcwtvyhgagsk
tlagpkgpitqmytnvdqdlvgwqappgarsltpctcgssdlylvtrhadvipvrrrgds
rgsllsprpvsylkgssggpllcpsghavgifraavctrgvakavdfvpvesmettm
>d1kaa__ 2.29.1.1.1 Staphylococcal nuclease {(Staphylococcal aureus)}
klhkepatlikaidgdtvklmykgqpmtfrlllvdtpetkhpkkgvekygpeasaftkkm
venakkievefdkgqrtdkygrglayiyadgkmvnealvrqglakvayvyapnntheqhl
rkseaqakkeklniws
>d1kab__ 2.29.1.1.1 Staphylococcal nuclease {(Staphylococcal aureus)}
klhkepatlikaidgdtvklmykgqpmtfrlllvdtpetkhpkkgvekygpeasaftkkm
venakkievefdkgqrtdkygrglayiyadgkmvnealvrqglakvayvygpnntheqhl
rkseaqakkeklniws
>d1kal__ 7.3.3.1.1 Kalata B1 {african plant (Oldenlandia affinis Dc)}
swpvctrnglpvcgetcvggtcntpgctc
>d1kana_ 5.10.1.2.1 Kanamycin nucleotidyltransferase (KNTase) {(Staphylococcus aureus)}
mngpiimtreermkivheikerildkygddvkaigvygslgrqtdgpysdiemmcvmste
eaefshewttgewkvevnfyseeilldyasqvesdwplthgqffsilpiydsggylekvy
qtaksveaqkfhdaicaliveelfeyagkwrnirvqgpttflpsltvqvamagamliglh
hricyttsasvlteavkqsdlpsgydhlcqfvmsgqlsdseklleslenfwngiqewter
hgyivdvskripf
>d1kanb_ 5.10.1.2.1 Kanamycin nucleotidyltransferase (KNTase) {(Staphylococcus aureus)}
mngpiimtreermkivheikerildkygddvkaigvygslgrqtdgpysdiemmcvmste
eaefshewttgewkvevnfyseeilldyasqvesdwplthgqffsilpiydsggylekvy
qtaksveaqkfhdaicaliveelfeyagkwrnirvqgpttflpsltvqvamagamliglh
hricyttsasvlteavkqsdlpsgydhlcqfvmsgqlsdseklleslenfwngiqewter
hgyivdvskripf
>d1kao__ 3.29.1.4.4 Rap2a {Human (Homo sapiens)}
mreykvvvlgsggvgksaltvqfvtgtfiekydptiedfyrkeievdsspsvleildtag
teqfasmrdlyikngqgfilvyslvnqqsfqdikpmrdqiirvkryekvpvilvgnkvdl
eserevsssegralaeewgcpfmetsaksktmvdelfaeivrqmnya
>d1kapp1 2.61.1.1.1 (247-470) Metalloprotease, C-terminal domain {(Pseudomonas aeruginosa) (alkaline protease)}
ganlttrtgdtvygfnsnterdfysatssssklvfsvwdaggndtldfsgfsqnqkinln
ekalsdvgglkgnvsiaagvtvenaiggsgsdlligndvanvlkggagndilygglgadq
lwggagadtfvygdiaessaaapdtlrdfvsgqdkidlsgldafvngglvlqyvdafagk
agqailsydaaskagslaidfsgdahadfainligqatqadivv
>d1kapp2 4.52.1.6.1 (1-239) Metallo protease, catalytic (N-terminal) domain {(Pseudomonas aeruginosa) alkaline protease}
grsdaytqvdnflhayarggdelvnghpsytvdqaaeqilreqaswqkapgdsvltlsys
fltkpndffntpwkyvsdiyslgkfsafsaqqqaqaklslqswsdvtnihfvdagqgdqg
dltfgnfsssvggaafaflpdvpdalkgqswylinssysanvnpangnygrqtltheigh
tlglshpgdynagegdptyadatyaedtraysvmsyweeqntgqdfkgayssapllddi
>d1kawa_ 2.29.4.3.2 ssDNA-binding protein {(Escherichia coli)}
rgvnkvilvgnlgqdpevrympnggavanitlatseswrdkatgemkeqtewhrvvlfgk
laevaseylrkgsqvyiegqlrtrkwtdqsgqdryttevvvnvggtmqml
>d1kawb_ 2.29.4.3.2 ssDNA-binding protein {(Escherichia coli)}
rgvnkvilvgnlgqdpevrympnggavanitlatseswrdkatgemkeqtewhrvvlfgk
laevaseylrkgsqvyiegqlrtrkwtdqsgqdryttevvvnvggtmqml
>d1kawc_ 2.29.4.3.2 ssDNA-binding protein {(Escherichia coli)}
rgvnkvilvgnlgqdpevrympnggavanitlatseswrdkatgemkeqtewhrvvlfgk
laevaseylrkgsqvyiegqlrtrkwtdqsgqdryttevvvnvggtmqml
>d1kawd_ 2.29.4.3.2 ssDNA-binding protein {(Escherichia coli)}
rgvnkvilvgnlgqdpevrympnggavanitlatseswrdkatgemkeqtewhrvvlfgk
laevaseylrkgsqvyiegqlrtrkwtdqsgqdryttevvvnvggtmqml
>d1kax_1 3.47.1.1.1 (4-188) Heat shock protein 70kDa, ATPase fragment {bovine (Bos taurus)}
gpavgidlgttyscvgvfqhgkveiiandqgnrttpsyvaftdterligdaaknqvamnp
tntvfdamrligrrfddavvqsdmkhwpfmvvndagrpkvqveykgetksfypeevssmv
ltkmkeiaeaylgktvtnavvtvpayfndsqrqatkdagtiaglnvlriineptaaaiay
gldkk
>d1kax_2 3.47.1.1.1 (189-381) Heat shock protein 70kDa, ATPase fragment {bovine (Bos taurus)}
vgaernvlifdlgggtfdvsiltiedgifevkstagdthlggedfdnrmvnhfiaefkrk
hkkdisenkravrrlrtacerakrtlssstqasieidslyegidfytsitrarfeelnad
lfrgtldpvekalrdakldksqihdivlvggstripkiqkllqdffngkelnksinpdea
vaygaavqaails
>d1kay_1 3.47.1.1.1 (4-188) Heat shock protein 70kDa, ATPase fragment {bovine (Bos taurus)}
gpavgidlgttyscvgvfqhgkveiiandqgnrttpsyvaftdterligdaaknqvamnp
tntvfdaarligrrfddavvqsdmkhwpfmvvndagrpkvqveykgetksfypeevssmv
ltkmkeiaeaylgktvtnavvtvpayfndsqrqatkdagtiaglnvlriineptaaaiay
gldkk
>d1kay_2 3.47.1.1.1 (189-381) Heat shock protein 70kDa, ATPase fragment {bovine (Bos taurus)}
vgaernvlifdlgggtfdvsiltiedgifevkstagdthlggedfdnrmvnhfiaefkrk
hkkdisenkravrrlrtacerakrtlssstqasieidslyegidfytsitrarfeelnad
lfrgtldpvekalrdakldksqihdivlvggstripkiqkllqdffngkelnksinpdea
vaygaavqaails
>d1kaz_1 3.47.1.1.1 (4-188) Heat shock protein 70kDa, ATPase fragment {bovine (Bos taurus)}
gpavgidlgttyscvgvfqhgkveiiandqgnrttpsyvaftdterligdaaknqvamnp
tntvfdaerligrrfddavvqsdmkhwpfmvvndagrpkvqveykgetksfypeevssmv
ltkmkeiaeaylgktvtnavvtvpayfndsqrqatkdagtiaglnvlriineptaaaiay
gldkk
>d1kaz_2 3.47.1.1.1 (189-381) Heat shock protein 70kDa, ATPase fragment {bovine (Bos taurus)}
vgaernvlifdlgggtfdvsiltiedgifevkstagdthlggedfdnrmvnhfiaefkrk
hkkdisenkravrrlrtacerakrtlssstqasieidslyegidfytsitrarfeelnad
lfrgtldpvekalrdakldksqihdivlvggstripkiqkllqdffngkelnksinpdea
vaygaavqaails
>d1kb5a_ 2.1.1.1.119 T-cell antigen receptor {Mouse (Mus musculus), alpha-chain}
qqvrqspqsltvwegetailncsyedstfnyfpwyqqfpgegpallisirsvsdkkedgr
ftiffnkrekklslhitdsqpgdsatyfcaaryqggralifgtgttvsvspgsad
>d1kb5b_ 2.1.1.1.121 T-cell antigen receptor {Mouse (Mus musculus), beta-chain}
vtlleqnprwrlvprgqavnlrcilknsqypwmswyqqdlqkqlqwlftlrspgdkevks
lpgadylatrvtdtelrlqvanmsqgrtlyctcsaapdwgasaetlyfgsgtrltvl
>d1kb5h1 2.1.1.1.98 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab Desire-1 (mouse), kappa L chain}
evqlqqsgpelekpgasvkisckasgysftgynmnwvkqsngkslewignidpyyggisy
nqkfkgratltvdkssstaymqlksltsedsavyycarsrtdlyyfdywgqgttltvss
>d1kb5h2 2.1.1.2.98 (114-213) Immunoglobulin (constant domains of L and H chains) {Fab Desire-1 (mouse), kappa L chain}
akttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsd
lytlsssvtvtsstwpsqsitcnvahpasstkvdkkiepr
>d1kb5l1 2.1.1.1.98 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab Desire-1 (mouse), kappa L chain}
diqmtqspaslsasvgetvtitcraskniysylawyqqkqgkspqllvynaktlgegvps
rfsgsgsgtqfslkinslqpedfgsyycqhhygtpytfgggtkleikr
>d1kb5l2 2.1.1.2.98 (109-214) Immunoglobulin (constant domains of L and H chains) {Fab Desire-1 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1kbaa_ 7.6.1.1.11 Bungarotoxin {kappa-bungarotoxin: (Bungarus multicinctus)}
rtclispsstpqtcpngqdicflkaqcdkfcsirgpvieqgcvatcpqfrsnyrsllcct
tdncnh
>d1kbab_ 7.6.1.1.11 Bungarotoxin {kappa-bungarotoxin: (Bungarus multicinctus)}
rtclispsstpqtcpngqdicflkaqcdkfcsirgpvieqgcvatcpqfrsnyrsllcct
tdncnh
>d1kbca_ 4.52.1.7.2 Neutrophil collagenase (MMP-8) {Human (Homo sapiens)}
fmltpgnpkwertnltyrirnytpqlseaeveraikdafelwsvaspliftrisqgeadi
niafyqrdhgdnspfdgpngilahafqpgqgiggdahfdaeetwtntsanynlflvaahe
fghslglahssdpgalmypnyafretsnyslpqddidgiqaiyg
>d1kbcb_ 4.52.1.7.2 Neutrophil collagenase (MMP-8) {Human (Homo sapiens)}
fmltpgnpkwertnltyrirnytpqlseaeveraikdafelwsvaspliftrisqgeadi
niafyqrdhgdnspfdgpngilahafqpgqgiggdahfdaeetwtntsanynlflvaahe
fghslglahssdpgalmypnyafretsnyslpqddidgiqaiyg
>d1kbpa1 2.1.9.1.1 (9-120) Purple acid phosphatase, N-terminal domain {Kidney bean (Phaseolus vulgaris)}
rdmpldsdvfrvppgynapqqvhitqgdlvgramiiswvtmdepgssavrywsekngrkr
iakgkmstyrffnyssgfihhttirklkyntkyyyevglrnttrrfsfitpp
>d1kbpa2 4.99.1.1.1 (121-432) Purple acid phosphatase, catalytic domain {Kidney bean (Phaseolus vulgaris)}
qtgldvpytfgligdlgqsfdsnttlshyelspkkgqtvlfvgdlsyadrypnhdnvrwd
twgrftersvayqpwiwtagnheiefapeinetepfkpfsyryhvpyeasqstspfwysi
krasahiivlssysaygrgtpqytwlkkelrkvkrsetpwlivlmhsplynsynhhfmeg
eamrtkfeawfvkykvdvvfaghvhayerservsniaykitdglctpvkdqsapvyitig
dagnygvidsnmiqpqpeysafreasfghgmfdiknrthahfswnrnqdgvaveadsvwf
fnrhwypvddst
>d1kbpb1 2.1.9.1.1 (9-120) Purple acid phosphatase, N-terminal domain {Kidney bean (Phaseolus vulgaris)}
rdmpldsdvfrvppgynapqqvhitqgdlvgramiiswvtmdepgssavrywsekngrkr
iakgkmstyrffnyssgfihhttirklkyntkyyyevglrnttrrfsfitpp
>d1kbpb2 4.99.1.1.1 (121-432) Purple acid phosphatase, catalytic domain {Kidney bean (Phaseolus vulgaris)}
qtgldvpytfgligdlgqsfdsnttlshyelspkkgqtvlfvgdlsyadrypnhdnvrwd
twgrftersvayqpwiwtagnheiefapeinetepfkpfsyryhvpyeasqstspfwysi
krasahiivlssysaygrgtpqytwlkkelrkvkrsetpwlivlmhsplynsynhhfmeg
eamrtkfeawfvkykvdvvfaghvhayerservsniaykitdglctpvkdqsapvyitig
dagnygvidsnmiqpqpeysafreasfghgmfdiknrthahfswnrnqdgvaveadsvwf
fnrhwypvddst
>d1kbpc1 2.1.9.1.1 (9-120) Purple acid phosphatase, N-terminal domain {Kidney bean (Phaseolus vulgaris)}
rdmpldsdvfrvppgynapqqvhitqgdlvgramiiswvtmdepgssavrywsekngrkr
iakgkmstyrffnyssgfihhttirklkyntkyyyevglrnttrrfsfitpp
>d1kbpc2 4.99.1.1.1 (121-432) Purple acid phosphatase, catalytic domain {Kidney bean (Phaseolus vulgaris)}
qtgldvpytfgligdlgqsfdsnttlshyelspkkgqtvlfvgdlsyadrypnhdnvrwd
twgrftersvayqpwiwtagnheiefapeinetepfkpfsyryhvpyeasqstspfwysi
krasahiivlssysaygrgtpqytwlkkelrkvkrsetpwlivlmhsplynsynhhfmeg
eamrtkfeawfvkykvdvvfaghvhayerservsniaykitdglctpvkdqsapvyitig
dagnygvidsnmiqpqpeysafreasfghgmfdiknrthahfswnrnqdgvaveadsvwf
fnrhwypvddst
>d1kbpd1 2.1.9.1.1 (9-120) Purple acid phosphatase, N-terminal domain {Kidney bean (Phaseolus vulgaris)}
rdmpldsdvfrvppgynapqqvhitqgdlvgramiiswvtmdepgssavrywsekngrkr
iakgkmstyrffnyssgfihhttirklkyntkyyyevglrnttrrfsfitpp
>d1kbpd2 4.99.1.1.1 (121-432) Purple acid phosphatase, catalytic domain {Kidney bean (Phaseolus vulgaris)}
qtgldvpytfgligdlgqsfdsnttlshyelspkkgqtvlfvgdlsyadrypnhdnvrwd
twgrftersvayqpwiwtagnheiefapeinetepfkpfsyryhvpyeasqstspfwysi
krasahiivlssysaygrgtpqytwlkkelrkvkrsetpwlivlmhsplynsynhhfmeg
eamrtkfeawfvkykvdvvfaghvhayerservsniaykitdglctpvkdqsapvyitig
dagnygvidsnmiqpqpeysafreasfghgmfdiknrthahfswnrnqdgvaveadsvwf
fnrhwypvddst
>d1kbs__ 7.6.1.1.17 Cardiotoxin IV {taiwan cobra (Naja naja atra)}
rkcnklvplfyktcpagknlcykmfmvsnltvpvkrgcidvcpknsalvkyvccntdrcn
>d1kbt__ 7.6.1.1.17 Cardiotoxin IV {taiwan cobra (Naja naja atra)}
rkcnklvplfyktcpagknlcykmfmvsnltvpvkrgcidvcpknsalvkyvccntdrcn
>d1kcea_ 4.67.1.1.1 Thymidylate synthase {(Escherichia coli)}
kqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihellw
flqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlkn
dpdsrriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfniasy
allvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesifd
yrfedfeiegydphpgikapvai
>d1kceb_ 4.67.1.1.1 Thymidylate synthase {(Escherichia coli)}
kqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihellw
flqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlkn
dpdsrriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfniasy
allvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesifd
yrfedfeiegydphpgikapvai
>d1kct__ 5.2.1.1.4 Antitrypsin, alpha-1 {human (Homo sapiens)}
hptfnkitpnlaefafslyrqlahqsnstniffspvsiaaafamlslgakgdthdeileg
lnfnlteipeaqihegfqellrtlnqpdsqlqlttgnglflseglklvdkfledvkklyh
seaftvnfgdteeakkqindyvekgtqgkivdlvkeldrdtvfalvnyiffkgkwerpfe
vkdteeedfhvdqvttvkvpmmkrlgmfniqhckklsswvllmkylgnataifflpdegk
lqhlenelthdiitkflenedrrsaslhlpklsitgtydlksvlgqlgitkvfsngadls
gvteeaplklskavhkavltidekgteaagamfleaipmsippevkfnkpfvflmieqnt
ksplfmgkvvnptqk
>d1kcw_1 2.5.1.3.5 (1-192) Ceruloplasmin {Human (Homo sapiens)}
kekhyyigiiettwdyasdhgekklisvdtehsniylqngpdrigrlykkalylqytdet
frttiekpvwlgflgpiikaetgdkvyvhlknlasrpytfhshgityykehegaiypdnt
tdfqraddkvypgeqytymllateeqspgegdgncvtriyhshidapkdiasgligplii
ckkdsldkekek
>d1kcw_2 2.5.1.3.5 (193-338) Ceruloplasmin {Human (Homo sapiens)}
hidrefvvmfsvvdenfswyledniktycsepekvdkdnedfqesnrmysvngytfgslp
glsmcaedrvkwylfgmgnevdvhaaffhgqaltnknyridtinlfpatlfdaymvaqnp
gewmlscqnlnhlkaglqaffqvqec
>d1kcw_3 2.5.1.3.5 (347-553) Ceruloplasmin {Human (Homo sapiens)}
irgkhvrhyyiaaeeiiwnyapsgidiftkenltapgsdsavffeqgttriggsykklvy
reytdasftnrkergpeeehlgilgpviwaevgdtirvtfhnkgayplsiepigvrfnkn
negtyyspnynpqsrsvppsashvaptetftyewtvpkevgptnadpvclakmyysavdp
tkdiftgligpmkickkgslhangrqk
>d1kcw_4 2.5.1.3.5 (554-705) Ceruloplasmin {Human (Homo sapiens)}
dvdkefylfptvfdeneslllednirmfttapdqvdkededfqesnkmhsmngfmygnqp
gltmckgdsvvwylfsagneadvhgiyfsgntylwrgerrdtanlfpqtsltlhmwpdte
gtfnveclttdhytggmkqkytvnqcrrqsed
>d1kcw_5 2.5.1.3.5 (706-884) Ceruloplasmin {Human (Homo sapiens)}
stfylgertyyiaavevewdyspqrewekelhhlqeqnvsnafldkgefyigskykkvvy
rqytdstfrvpverkaeeehlgilgpqlhadvgdkvkiifknmatrpysihahgvqtess
tvtptlpgetltyvwkipersgagtedsacipwayystvdqvkdlysgligplivcrrp
>d1kcw_6 2.5.1.3.5 (892-1040) Ceruloplasmin {Human (Homo sapiens)}
rrklefallflvfdeneswylddniktysdhpekvnkddeefiesnkmhaingrmfgnlq
gltmhvgdevnwylmgmgneidlhtvhfhghsfqykhrgvyssdvfdifpgtyqtlemfp
rtpgiwllhchvtdhihagmettytvlqn
>d1kda__ 2.29.1.1.1 Staphylococcal nuclease {(Staphylococcal aureus)}
klhkepatlikaidgdtvklmykgqpmtfrlllvdtpetkhpkkgvekygpeasaftkkm
venakkievefdkgqrtdkygrglayiyadgkmvnealvrqglakvayvydpnntheqhl
rkseaqakkeklniwse
>d1kdb__ 2.29.1.1.1 Staphylococcal nuclease {(Staphylococcal aureus)}
klhkepatlikaidgdtvklmykgqpmtfrlllvdtpetkhpkkgvekygpeasaftkkm
venakkievefdkgqrtdkygrglayiyadgkmvnealvrqglakvayvyepnntheqhl
rkseaqakkeklniwse
>d1kdc__ 2.29.1.1.1 Staphylococcal nuclease {(Staphylococcal aureus)}
klhkepatlikaidgdtvklmykgqpmtfrlllvdtpetkhpkkgvekygpeasaftkkm
venakkievefdkgqrtdkygrglayiyadgkmvnealvrqglakvayvynpnntheqhl
rkseaqakkeklniwse
>d1kde__ 2.66.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus)}
nqasvvanqlipintaltlvmmrsevvtpvgipaediprlvsmqvnravplgttlmpdmv
kgyaa
>d1kdf__ 2.66.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus)}
nqasvvanqlipintaltlvmmrsevvtpvgipaediprlvsmqvnravplgttlmpdmv
kgyaa
>d1kdna_ 4.34.6.1.2 Nucleoside diphosphate kinases {(Dictyostelium discodeum)}
vnkertflavkpdgvarglvgeiiaryekkgfvlvglkqlvptkdlaeshyaehkerpff
gglvsfitsgpvvamvfegkgvvasarlmigvtnplasapgsirgdfgvdvgrniihgsd
svesanreialwfkpeelltevkpnpnlye
>d1kdnb_ 4.34.6.1.2 Nucleoside diphosphate kinases {(Dictyostelium discodeum)}
vnkertflavkpdgvarglvgeiiaryekkgfvlvglkqlvptkdlaeshyaehkerpff
gglvsfitsgpvvamvfegkgvvasarlmigvtnplasapgsirgdfgvdvgrniihgsd
svesanreialwfkpeelltevkpnpnlye
>d1kdnc_ 4.34.6.1.2 Nucleoside diphosphate kinases {(Dictyostelium discodeum)}
vnkertflavkpdgvarglvgeiiaryekkgfvlvglkqlvptkdlaeshyaehkerpff
gglvsfitsgpvvamvfegkgvvasarlmigvtnplasapgsirgdfgvdvgrniihgsd
svesanreialwfkpeelltevkpnpnlye
>d1kdu__ 7.13.1.1.7 Urokinase-type plasminogen activator {human (Homo sapiens)}
tcyegnghfyrgkastdtmgrpclpwnsatvlqqtyhahrsdalqlglgkhnycrnpdnr
rrpwcyvqvglkplvqecmvhdcad
>d1kelh1 2.1.1.1.73 (1-115) Immunoglobulin (variable domains of L and H chains) {Fab 28B4 (mouse), kappa L chain}
evklvesggglgqpggslrlscatsgftftdyyfnwarqppgkalewlgfirnkakgytt
eysasvkgrftisrdnsqgilylqmntlraedsatyycarwgsyamdywgqgtsv
>d1kelh2 2.1.1.2.76 (116-218) Immunoglobulin (constant domains of L and H chains) {Fab 28B4 (mouse), kappa L chain}
tvssakttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpav
lqsdlytlsssvtvpssprpsetvtcnvahpasstkvdkkivp
>d1kell1 2.1.1.1.73 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab 28B4 (mouse), kappa L chain}
dvlmtqtplslpvslgdqasiscrfsqsivhsngntylewylqksgqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyycfqgshvprtfgggtkleik
>d1kell2 2.1.1.2.76 (113-217) Immunoglobulin (constant domains of L and H chains) {Fab 28B4 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrn
>d1kemh1 2.1.1.1.73 (1-115) Immunoglobulin (variable domains of L and H chains) {Fab 28B4 (mouse), kappa L chain}
evklvesggglgqpggslrlscatsgftftdyyfnwarqppgkalewlgfirnkakgytt
eysasvkgrftisrdnsqgilylqmntlraedsatyycarwgsyamdywgqgtsv
>d1kemh2 2.1.1.2.76 (116-218) Immunoglobulin (constant domains of L and H chains) {Fab 28B4 (mouse), kappa L chain}
tvssakttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpav
lqsdlytlsssvtvpssprpsetvtcnvahpasstkvdkkivp
>d1keml1 2.1.1.1.73 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab 28B4 (mouse), kappa L chain}
dvlmtqtplslpvslgdqasiscrfsqsivhsngntylewylqksgqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyycfqgshvprtfgggtkleik
>d1keml2 2.1.1.2.76 (113-217) Immunoglobulin (constant domains of L and H chains) {Fab 28B4 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrn
>d1keva1 2.25.1.2.3 (1-150,315-351) Bacterial secondary alcohol dehydrogenase {(Clostridium beijerinckii)}
mkgfamlginklgwiekerpvagsydaivrplavspctsdihtvfegalgdrknmilghe
avgevvevgsevkdfkpgdrvivpcttpdwrslevqagfqqhsngmlagwkfsnfkdgvf
geyfhvndadmnlailpkdmplenavmitdXdlsklvthvyhgfdhieealllmkdkpkd
likavvil
>d1keva2 3.22.1.1.3 (151-314) Bacterial secondary alcohol dehydrogenase {(Clostridium beijerinckii)}
mmttgfhgaeladiqmgssvvvigigavglmgiagaklrgagriigvgsrpicveaakfy
gatdilnyknghivdqvmkltngkgvdrvimagggsetlsqavsmvkpggiisninyhgs
gdalliprvewgcgmahktikgglcpggrlraemlrdmvvynrv
>d1kevb1 2.25.1.2.3 (1-150,315-351) Bacterial secondary alcohol dehydrogenase {(Clostridium beijerinckii)}
mkgfamlginklgwiekerpvagsydaivrplavspctsdihtvfegalgdrknmilghe
avgevvevgsevkdfkpgdrvivpcttpdwrslevqagfqqhsngmlagwkfsnfkdgvf
geyfhvndadmnlailpkdmplenavmitdXdlsklvthvyhgfdhieealllmkdkpkd
likavvil
>d1kevb2 3.22.1.1.3 (151-314) Bacterial secondary alcohol dehydrogenase {(Clostridium beijerinckii)}
mmttgfhgaeladiqmgssvvvigigavglmgiagaklrgagriigvgsrpicveaakfy
gatdilnyknghivdqvmkltngkgvdrvimagggsetlsqavsmvkpggiisninyhgs
gdalliprvewgcgmahktikgglcpggrlraemlrdmvvynrv
>d1kevc1 2.25.1.2.3 (1-150,315-351) Bacterial secondary alcohol dehydrogenase {(Clostridium beijerinckii)}
mkgfamlginklgwiekerpvagsydaivrplavspctsdihtvfegalgdrknmilghe
avgevvevgsevkdfkpgdrvivpcttpdwrslevqagfqqhsngmlagwkfsnfkdgvf
geyfhvndadmnlailpkdmplenavmitdXdlsklvthvyhgfdhieealllmkdkpkd
likavvil
>d1kevc2 3.22.1.1.3 (151-314) Bacterial secondary alcohol dehydrogenase {(Clostridium beijerinckii)}
mmttgfhgaeladiqmgssvvvigigavglmgiagaklrgagriigvgsrpicveaakfy
gatdilnyknghivdqvmkltngkgvdrvimagggsetlsqavsmvkpggiisninyhgs
gdalliprvewgcgmahktikgglcpggrlraemlrdmvvynrv
>d1kevd1 2.25.1.2.3 (1-150,315-351) Bacterial secondary alcohol dehydrogenase {(Clostridium beijerinckii)}
mkgfamlginklgwiekerpvagsydaivrplavspctsdihtvfegalgdrknmilghe
avgevvevgsevkdfkpgdrvivpcttpdwrslevqagfqqhsngmlagwkfsnfkdgvf
geyfhvndadmnlailpkdmplenavmitdXdlsklvthvyhgfdhieealllmkdkpkd
likavvil
>d1kevd2 3.22.1.1.3 (151-314) Bacterial secondary alcohol dehydrogenase {(Clostridium beijerinckii)}
mmttgfhgaeladiqmgssvvvigigavglmgiagaklrgagriigvgsrpicveaakfy
gatdilnyknghivdqvmkltngkgvdrvimagggsetlsqavsmvkpggiisninyhgs
gdalliprvewgcgmahktikgglcpggrlraemlrdmvvynrv
>d1kfd_1 3.47.3.4.1 (324-518) Exonuclease domain of DNA polymerase {(Escherichia coli)}
visydnyvtildeetlkawiaklekapvfafdtetdsldnisanlvglsfaiepgvaayi
pvahdyldapdqisreralellkplledekalkvgqnlkydrgilanygielrgiafdtm
lesyilnsvagrhdmdslaerwlkhktitfeeiagkgknqltfnqialeeagryaaedad
vtlqlhlkmwpdlqk
>d1kfd_2 5.9.1.1.1 (519-928) DNA polymerase I (Klenow fragment) {(Escherichia coli)}
hkgplnvfeniemplvpvlsrierngvkidpkvlhnhseeltlrlaelekkaheiageef
nlsstkqlqtilfekqgikplkktpggapstseevleelaldyplpkvileyrglaklks
tytdklplminpktgrvhtsyhqavtatgrlsstdpnlqnipvrneegrrirqafiaped
yvivsadysqielrimahlsrdkglltafaegkdihrataaevfglpletvtseqrrsak
ainfgliygmsafglarqlniprkeaqkymdlyferypgvleymertraqakeqgyvetl
dgrrlylpdikssngarraaaeraainapmqgtaadiikramiavdawlqaeqprvrmim
qvhdelvfevhkddvdavakqihqlmenctrldvpllvevgsgenwdqah
>d1kfsa1 3.47.3.4.1 (324-518) Exonuclease domain of DNA polymerase {(Escherichia coli)}
misydnyvtildeetlkawiaklekapvfafdtetdsldnisanlvglsfaiepgvaayi
pvahdyldapdqisreralellkplledekalkvgqnlkydrgilanygielrgiafdtm
lesyilnsvagrhdmdslaerwlkhktitfeeiagkgknqltfnqialeeagryaaedad
vtlqlhlkmwpdlqk
>d1kfsa2 5.9.1.1.1 (519-928) DNA polymerase I (Klenow fragment) {(Escherichia coli)}
hkgplnvfeniemplvpvlsrierngvkidpkvlhnhseeltlrlaelekkaheiageef
nlsstkqlqtilfekqgikplkktpggapstseevleelaldyplpkvileyrglaklks
tytdklplminpktgrvhtsyhqavtatgrlsstdpnlqnipvrneegrrirqafiaped
yvivsadysqielrimahlsrdkglltafaegkdihrataaevfglpletvtseqrrsak
ainfgliygmsafglarqlniprkeaqkymdlyferypgvleymertraqakeqgyvetl
dgrrlylpdikssngarraaaeraainapmqgtaadiikramiavdawlqaeqprvrmim
qvhdelvfevhkddvdavakqihqlmenctrldvpllvevgsgenwdqah
>d1kge__ 5.4.1.1.3 beta-Lactamase, class A {(Staphylococcus aureus)}
kelndlekkynahigvyaldtksgkevkfnsdkrfayastskainsailleqvpynklnk
kvhinkddivayspilekyvgkditlkalieasmtysdntannkiikeiggikkvkqrlk
elgdkvtnpvryeielmyyspkskkdtstpaafgktlnkliangklskenkkflldlmln
nksgdtlikdgvpkdykvadksgqaityasrndvafvypkgqsepivlviftnkdnksdk
pndklisetaksvmkef
>d1kgf__ 5.4.1.1.3 beta-Lactamase, class A {(Staphylococcus aureus)}
kelndlekkynahigvyaldtksgkevkfnsdkrfayastskainsailleqvpynklnk
kvhinkddivayspilekyvgkditlkalieasmtysdntannkiikeiggikkvkqrlk
elgdkvtnpvryeielqyyspkskkdtstpaafgktlnkliangklskenkkflldlmln
nksgdtlikdgvpkdykvadksgqaityasrndvafvypkgqsepivlviftnkdnksdk
pndklisetaksvmkef
>d1kid__ 3.5.4.1.1 GroEL {(Escherichia coli)}
glvprgsegmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavaka
gkplliiaedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtvise
eigmelekatledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydre
klqervaklaggv
>d1kifa1 3.21.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1kifa2 4.12.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1kifb1 3.21.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1kifb2 4.12.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1kifc1 3.21.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1kifc2 4.12.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1kifd1 3.21.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1kifd2 4.12.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1kife1 3.21.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1kife2 4.12.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1kiff1 3.21.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1kiff2 4.12.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1kifg1 3.21.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1kifg2 4.12.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1kifh1 3.21.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernl
>d1kifh2 4.12.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1kima_ 3.29.1.1.5 Thymidine kinase {(Herpes simplex virus) type 1, HSV1}
mptllrvyidgphgmgkttttqllvalgsrddivyvpepmtywrvlgasetianiyttqh
rldqgeisagdaavvmtsaqitmgmpyavtdavlaphiggeagsshapppaltlifdrhp
iaallcypaarylmgsmtpqavlafvalipptlpgtnivlgalpedrhidrlakrqrpge
rldlamlaairrvygllantvrylqcggswredwgqlsgtavppqgaepqsnagprphig
dtlftlfrapellapngdlynvfawaldvlakrlrsmhvfildydqspagcrdallqlts
gmvqthvttpgsipticdlartfaremgea
>d1kimb_ 3.29.1.1.5 Thymidine kinase {(Herpes simplex virus) type 1, HSV1}
mptllrvyidgphgmgkttttqllvalgsrddivyvpepmtywrvlgasetianiyttqh
rldqgeisagdaavvmtsaqitmgmpyavtdavlaphiggeagsshapppaltlifdrhp
iaallcypaarylmgsmtpqavlafvalipptlpgtnivlgalpedrhidrlakrqrpge
rldlamlaairrvygllantvrylqcggswredwgqlsgtavppqgaepqsnagprphig
dtlftlfrapellapngdlynvfawaldvlakrlrsmhvfildydqspagcrdallqlts
gmvqthvttpgsipticdlartfaremgea
>d1kipa_ 2.1.1.1.39 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
divltqspaslsasvgetvtitcrasgnihnylawyqqkqgkspqllvyytttladgvps
rfsgsgsgtqyslkinslqpedfgsyycqhfwstprtfgggtkleik
>d1kipb_ 2.1.1.1.39 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
qvqlqesgpglvapsqslsitctvsgfsltgagvnwvrqppgkglewlgmiwgdgntdyn
salksrlsiskdnsksqvflkmnslhtddtaryycarerdyrldywgqgttltvss
>d1kipc_ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1kiqa_ 2.1.1.1.39 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
divltqspaslsasvgetvtitcrasgnihnylawyqqkqgkspqllvyytttladgvps
rfsgsgsgtqyslkinslqpedfgsyycqhfwstprtfgggtkleik
>d1kiqb_ 2.1.1.1.39 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
qvqlqesgpglvapsqslsitctvsgfsltgygvnwvrqppgkglewlgmiwgdgntdyn
salksrlsiskdnsksqvflkmnslhtddtaryycarerdfrldywgqgttltvss
>d1kiqc_ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1kira_ 2.1.1.1.39 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
divltqspaslsasvgetvtitcrasgnihnylawyqqkqgkspqllvystttladgvps
rfsgsgsgtqyslkinslqpedfgsyycqhfwstprtfgggtkleik
>d1kirb_ 2.1.1.1.39 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
qvqlqesgpglvapsqslsitctvsgfsltgygvnwvrqppgkglewlgmiwgdgntdyn
salksrlsiskdnsksqvflkmnslhtddtaryycarerdyrldywgqgttltvss
>d1kirc_ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1kit_1 2.21.1.7.1 (25-216) Vibrio cholerae sialidase, N-terminal and insertion domains {(Vibrio cholerae)}
alfdynatgdtefdspakqgwmqdntnngsgvltnadgmpawlvqgiggraqwtyslstn
qhaqassfgwrmttemkvlsggmitnyyangtqrvlpiisldssgnlvvefegqtgrtvl
atgtaateyhkfelvflpgsnpsasfyfdgklirdniqptaskqnmivwgngssntdgva
ayrdikfeiqgd
>d1kit_2 2.21.1.7.1 (347-543) Vibrio cholerae sialidase, N-terminal and insertion domains {(Vibrio cholerae)}
dvtdqvkersfqiagwggselyrrntslnsqqdwqsnakirivdgaanqiqvadgsrkyv
vtlsidesgglvanlngvsapiilqsehakvhsfhdyelqysalnhtttlfvdgqqittw
agevsqenniqfgnadaqidgrlhvqkivltqqghnlvefdafylaqqtpevekdleklg
wtkiktgntmslygnas
>d1kit_3 2.50.1.1.5 (217-346,544-781) Vibrio cholerae sialidase {(Vibrio cholerae)}
vifrgpdripsivassvtpgvvtafaekrvgggdpgalsntndiitrtsrdggitwdtel
nlteqinvsdefdfsdprpiydpssntvlvsyarwptdaaqngdrikpwmpngifysvyd
vasgnwqapiXvnpgpghgitltrqqnisgsqngrliypaivldrfflnvmsiysddggs
nwqtgstlpipfrwksssiletlepseadmvelqngdllltarldfnqivngvnysprqq
flskdggitwslleannanvfsnistgtvdasitrfeqsdgshfllftnpqgnpagtngr
qnlglwfsfdegvtwkgpiqlvngasaysdiyqldsenaivivetdnsnmrilrmpitll
kqkltlsqn
>d1kjs__ 1.45.1.1.1 C5a anaphylotoxin {human (Homo sapiens)}
mlqkkieeiaakykhsvvkkccydgacvnndetceqraarislgprcikafteccvvasq
lranishkdmqlgr
>d1klaa_ 7.16.1.2.3 TGF-beta1 {human (Homo sapiens)}
aldtnycfssteknccvrqlyidfrkdlgwkwihepkgyhanfclgpcpyiwsldtqysk
vlalynqhnpgasaapccvpqaleplpivyyvgrkpkveqlsnmivrsckcs
>d1klab_ 7.16.1.2.3 TGF-beta1 {human (Homo sapiens)}
aldtnycfssteknccvrqlyidfrkdlgwkwihepkgyhanfclgpcpyiwsldtqysk
vlalynqhnpgasaapccvpqaleplpivyyvgrkpkveqlsnmivrsckcs
>d1klca_ 7.16.1.2.3 TGF-beta1 {human (Homo sapiens)}
aldtnycfssteknccvrqlyidfrkdlgwkwihepkgyhanfclgpcpyiwsldtqysk
vlalynqhnpgasaapccvpqaleplpivyyvgrkpkveqlsnmivrsckcs
>d1klcb_ 7.16.1.2.3 TGF-beta1 {human (Homo sapiens)}
aldtnycfssteknccvrqlyidfrkdlgwkwihepkgyhanfclgpcpyiwsldtqysk
vlalynqhnpgasaapccvpqaleplpivyyvgrkpkveqlsnmivrsckcs
>d1klda_ 7.16.1.2.3 TGF-beta1 {human (Homo sapiens)}
aldtnycfssteknccvrqlyidfrkdlgwkwihepkgyhanfclgpcpyiwsldtqysk
vlalynqhnpgasaapccvpqaleplpivyyvgrkpkveqlsnmivrsckcs
>d1kldb_ 7.16.1.2.3 TGF-beta1 {human (Homo sapiens)}
aldtnycfssteknccvrqlyidfrkdlgwkwihepkgyhanfclgpcpyiwsldtqysk
vlalynqhnpgasaapccvpqaleplpivyyvgrkpkveqlsnmivrsckcs
>d1klma1 3.47.3.1.4 (430-539) HIV RNase H (Domain of reverse transcriptase) {(human immunodeficiency virus type I)}
ekepivgaetfyvdgaanretklgkagyvtnrgrqkvvtltdttnqktelqaiylalqds
glevnivtdsqyalgiiqaqpdqseselvnqiieqlikkekvylawvpah
>d1klma2 5.9.1.2.2 (2-429) HIV-1 reverse transcriptase {human immunodeficiency virus type 1 (Bh10 isolate)}
ispietvpvklkpgmdgpkvkqwplteekikalveictemekegkiskigpenpyntpvf
aikkkdstkwrklvdfrelnkrtqdfwevqlgiphpaglkkkksvtvldvgdayfsvpld
edfrkytaftipsinnetpgiryqynvlpqgwkgspaifqssmtkilepfrkqnpdiviy
qymddlyvgsdleigqhrtkieelrqhllrwglttpdkkhqkeppflwmgyelhpdkwtv
qpivlpekdswtvndiqklvgklnwasqiypgikvrqlxkllrgtkalteviplteeael
elaenreilkepvhgvyydpskdliaeiqkqgqgqwtyqiyqepfknlktgkyarmrgah
tndvkqlteavqkittesiviwgktpkfklpiqketwetwwteywqatwipewefvntpp
lvklwyql
>d1klna1 3.47.3.4.1 (324-518) Exonuclease domain of DNA polymerase {(Escherichia coli)}
visydnyvtildeetlkawiaklekapvfafatetdsldnisanlvglsfaiepgvaayi
pvahdyldapdqisreralellkplledekalkvgqnlkydrgilanygielrgiafdtm
lesyilnsvagrhdmdslaerwlkhktitfeeiagkgknqltfnqialeeagryaaedad
vtlqlhlkmwpdlqk
>d1klna2 5.9.1.1.1 (519-928) DNA polymerase I (Klenow fragment) {(Escherichia coli)}
hkgplnvfeniemplvpvlsrierngvkidpkvlhnhseeltlrlaelekkaheiageef
nlsstkqlqtilfekqgikplkktpggapstseevleelaldyplpkvileyrglaklks
tytdklplminpktgrvhtsyhqavtatgrlsstdpnlqnipvrneegrrirqafiaped
yvivsadysqielrimahlsrdkglltafaegkdihrataaevfglpletvtseqrrsak
ainfgliygmsafglarqlniprkeaqkymdlyferypgvleymertraqakeqgyvetl
dgrrlylpdikssngarraaaeraainapmqgtaadiikramiavdawlqaeqprvrmim
qvhdelvfevhkddvdavakqihqlmenctrldvpllvevgsgenwdqah
>d1klo_1 7.3.9.2.1 (11-65) Laminin gamma1 chain {Mouse (Mus musculus)}
cpcpggsscaivpktkevvcthcptgtagkrcelcddgyfgdplgsngpvrlcrp
>d1klo_2 7.3.9.2.1 (66-121) Laminin gamma1 chain {Mouse (Mus musculus)}
cqcndnidpnavgncnrltgeclkciyntagfycdrckegffgnplapnpadkcka
>d1klo_3 7.3.9.2.1 (122-172) Laminin gamma1 chain {Mouse (Mus musculus)}
cacnpygtvqqqsscnpvtgqcqclphvsgrdcgtcdpgyynlqsgqgcer
>d1kmb11 1.105.1.1.1 (73-104) Mannose-binding protein A {rat (Rattus rattus)}
aievklanmeaeintlkskleltnklhafsmg
>d1kmb12 4.105.1.1.5 (105-221) Mannose-binding protein A, lectin domain {rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdepndhgsgedcvtivdnglwndiscqkkktavcefpa
>d1kmb21 1.105.1.1.1 (73-104) Mannose-binding protein A {rat (Rattus rattus)}
aievklanmeaeintlkskleltnklhafsmg
>d1kmb22 4.105.1.1.5 (105-221) Mannose-binding protein A, lectin domain {rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdepndhgsgedcvtivdnglwndiscqkkktavcefpa
>d1kmb31 1.105.1.1.1 (73-104) Mannose-binding protein A {rat (Rattus rattus)}
aievklanmeaeintlkskleltnklhafsmg
>d1kmb32 4.105.1.1.5 (105-221) Mannose-binding protein A, lectin domain {rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdepndhgsgedcvtivdnglwndiscqkkktavcefpa
>d1kmma1 3.42.1.1.1 (326-424) Histidyl-tRNA synthetase (HisRS), C-terminal domain {(Escherichia coli)}
dpvvdiylvasgadtqsaamalaerlrdelpgvklmtnhgggnfkkqfaradkwgarvav
vlgesevangtavvkdlrsgeqtavaqdsvaahlrtllg
>d1kmma2 4.61.1.1.3 (4-325) Histidyl-tRNA synthetase (HisRS) {(Escherichia coli)}
niqairgmndylpgetaiwqriegtlknvlgsygyseirlpiveqtplfkraigevtdvv
ekemytfedrngdsltlrpegtagcvragiehgllynqeqrlwyigpmfrherpqkgryr
qfhqlgcevfglqgpdidaelimltarwwralgisehvtlelnsigslearanyrdalva
fleqhkekldedckrrmytnplrvldsknpevqallndapalgdyldeesrehfaglckl
lesagiaytvnqrlvrgldyynrtvfewvtnslgsqgtvcaggrydglveqlggratpav
gfamglerlvllvqavnpefka
>d1kmmb1 3.42.1.1.1 (326-424) Histidyl-tRNA synthetase (HisRS), C-terminal domain {(Escherichia coli)}
dpvvdiylvasgadtqsaamalaerlrdelpgvklmtnhgggnfkkqfaradkwgarvav
vlgesevangtavvkdlrsgeqtavaqdsvaahlrtllg
>d1kmmb2 4.61.1.1.3 (4-325) Histidyl-tRNA synthetase (HisRS) {(Escherichia coli)}
niqairgmndylpgetaiwqriegtlknvlgsygyseirlpiveqtplfkraigevtdvv
ekemytfedrngdsltlrpegtagcvragiehgllynqeqrlwyigpmfrherpqkgryr
qfhqlgcevfglqgpdidaelimltarwwralgisehvtlelnsigslearanyrdalva
fleqhkekldedckrrmytnplrvldsknpevqallndapalgdyldeesrehfaglckl
lesagiaytvnqrlvrgldyynrtvfewvtnslgsqgtvcaggrydglveqlggratpav
gfamglerlvllvqavnpefka
>d1kmmc1 3.42.1.1.1 (326-424) Histidyl-tRNA synthetase (HisRS), C-terminal domain {(Escherichia coli)}
dpvvdiylvasgadtqsaamalaerlrdelpgvklmtnhgggnfkkqfaradkwgarvav
vlgesevangtavvkdlrsgeqtavaqdsvaahlrtllg
>d1kmmc2 4.61.1.1.3 (4-325) Histidyl-tRNA synthetase (HisRS) {(Escherichia coli)}
niqairgmndylpgetaiwqriegtlknvlgsygyseirlpiveqtplfkraigevtdvv
ekemytfedrngdsltlrpegtagcvragiehgllynqeqrlwyigpmfrherpqkgryr
qfhqlgcevfglqgpdidaelimltarwwralgisehvtlelnsigslearanyrdalva
fleqhkekldedckrrmytnplrvldsknpevqallndapalgdyldeesrehfaglckl
lesagiaytvnqrlvrgldyynrtvfewvtnslgsqgtvcaggrydglveqlggratpav
gfamglerlvllvqavnpefka
>d1kmmd1 3.42.1.1.1 (326-424) Histidyl-tRNA synthetase (HisRS), C-terminal domain {(Escherichia coli)}
dpvvdiylvasgadtqsaamalaerlrdelpgvklmtnhgggnfkkqfaradkwgarvav
vlgesevangtavvkdlrsgeqtavaqdsvaahlrtllg
>d1kmmd2 4.61.1.1.3 (4-325) Histidyl-tRNA synthetase (HisRS) {(Escherichia coli)}
niqairgmndylpgetaiwqriegtlknvlgsygyseirlpiveqtplfkraigevtdvv
ekemytfedrngdsltlrpegtagcvragiehgllynqeqrlwyigpmfrherpqkgryr
qfhqlgcevfglqgpdidaelimltarwwralgisehvtlelnsigslearanyrdalva
fleqhkekldedckrrmytnplrvldsknpevqallndapalgdyldeesrehfaglckl
lesagiaytvnqrlvrgldyynrtvfewvtnslgsqgtvcaggrydglveqlggratpav
gfamglerlvllvqavnpefka
>d1kmna1 3.42.1.1.1 (326-424) Histidyl-tRNA synthetase (HisRS), C-terminal domain {(Escherichia coli)}
dpvvdiylvasgadtqsaamalaerlrdelpgvklmtnhgggnfkkqfaradkwgarvav
vlgesevangtavvkdlrsgeqtavaqdsvaahlrtllg
>d1kmna2 4.61.1.1.3 (4-325) Histidyl-tRNA synthetase (HisRS) {(Escherichia coli)}
niqairgmndylpgetaiwqriegtlknvlgsygyseirlpiveqtplfkraigevtdvv
ekemytfedrngdsltlrpegtagcvragiehgllynqeqrlwyigpmfrherpqkgryr
qfhqlgcevfglqgpdidaelimltarwwralgisehvtlelnsigslearanyrdalva
fleqhkekldedckrrmytnplrvldsknpevqallndapalgdyldeesrehfaglckl
lesagiaytvnqrlvrgldyynrtvfewvtnslgsqgtvcaggrydglveqlggratpav
gfamglerlvllvqavnpefka
>d1kmnb1 3.42.1.1.1 (326-424) Histidyl-tRNA synthetase (HisRS), C-terminal domain {(Escherichia coli)}
dpvvdiylvasgadtqsaamalaerlrdelpgvklmtnhgggnfkkqfaradkwgarvav
vlgesevangtavvkdlrsgeqtavaqdsvaahlrtllg
>d1kmnb2 4.61.1.1.3 (4-325) Histidyl-tRNA synthetase (HisRS) {(Escherichia coli)}
niqairgmndylpgetaiwqriegtlknvlgsygyseirlpiveqtplfkraigevtdvv
ekemytfedrngdsltlrpegtagcvragiehgllynqeqrlwyigpmfrherpqkgryr
qfhqlgcevfglqgpdidaelimltarwwralgisehvtlelnsigslearanyrdalva
fleqhkekldedckrrmytnplrvldsknpevqallndapalgdyldeesrehfaglckl
lesagiaytvnqrlvrgldyynrtvfewvtnslgsqgtvcaggrydglveqlggratpav
gfamglerlvllvqavnpefka
>d1kmnc1 3.42.1.1.1 (326-424) Histidyl-tRNA synthetase (HisRS), C-terminal domain {(Escherichia coli)}
dpvvdiylvasgadtqsaamalaerlrdelpgvklmtnhgggnfkkqfaradkwgarvav
vlgesevangtavvkdlrsgeqtavaqdsvaahlrtllg
>d1kmnc2 4.61.1.1.3 (4-325) Histidyl-tRNA synthetase (HisRS) {(Escherichia coli)}
niqairgmndylpgetaiwqriegtlknvlgsygyseirlpiveqtplfkraigevtdvv
ekemytfedrngdsltlrpegtagcvragiehgllynqeqrlwyigpmfrherpqkgryr
qfhqlgcevfglqgpdidaelimltarwwralgisehvtlelnsigslearanyrdalva
fleqhkekldedckrrmytnplrvldsknpevqallndapalgdyldeesrehfaglckl
lesagiaytvnqrlvrgldyynrtvfewvtnslgsqgtvcaggrydglveqlggratpav
gfamglerlvllvqavnpefka
>d1kmnd1 3.42.1.1.1 (326-424) Histidyl-tRNA synthetase (HisRS), C-terminal domain {(Escherichia coli)}
dpvvdiylvasgadtqsaamalaerlrdelpgvklmtnhgggnfkkqfaradkwgarvav
vlgesevangtavvkdlrsgeqtavaqdsvaahlrtllg
>d1kmnd2 4.61.1.1.3 (4-325) Histidyl-tRNA synthetase (HisRS) {(Escherichia coli)}
niqairgmndylpgetaiwqriegtlknvlgsygyseirlpiveqtplfkraigevtdvv
ekemytfedrngdsltlrpegtagcvragiehgllynqeqrlwyigpmfrherpqkgryr
qfhqlgcevfglqgpdidaelimltarwwralgisehvtlelnsigslearanyrdalva
fleqhkekldedckrrmytnplrvldsknpevqallndapalgdyldeesrehfaglckl
lesagiaytvnqrlvrgldyynrtvfewvtnslgsqgtvcaggrydglveqlggratpav
gfamglerlvllvqavnpefka
>d1knb__ 2.16.1.1.1 Adenovirus type 5 fiber protein, knob domain {Adenovirus type 5}
ndkltlwttpapspncrlnaekdakltlvltkcgsqilatvsvlavkgslapisgtvqsa
hliirfdengvllnnsfldpeywnfrngdltegtaytnavgfmpnlsaypkshgktaksn
ivsqvylngdktkpvtltitlngtqetgdttpsaysmsfswdwsghnyineifatssytf
syiaqe
>d1knoa1 2.1.1.1.46 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab CNJ206 (mouse), kappa L chain}
qiqmtqspsslsaslgervsltcrasqeisgylswlqqkpdgtikrliyaastldsgvpk
rfsgsrsgsdysltisslesedfadyyclqyasspytfgggtkleilr
>d1knoa2 2.1.1.2.53 (109-214) Immunoglobulin (constant domains of L and H chains) {Fab CNJ206 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1knob1 2.1.1.1.46 (1-119) Immunoglobulin (variable domains of L and H chains) {Fab CNJ206 (mouse), kappa L chain}
dvklvesggglvqpggsrklscaasgftfssfgmhwvrqapekglewvayissgsstiyy
adtvkgrftisrdnpkntlflqmtslrsedtamyycargdyygsrgaywgqgtlvtvsa
>d1knob2 2.1.1.2.53 (120-235) Immunoglobulin (constant domains of L and H chains) {Fab CNJ206 (mouse), kappa L chain}
akttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsd
lytlsssvtvtsstwpsqsitcnvahpasstkvdkkieprg
>d1knoc1 2.1.1.1.46 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab CNJ206 (mouse), kappa L chain}
qiqmtqspsslsaslgervsltcrasqeisgylswlqqkpdgtikrliyaastldsgvpk
rfsgsrsgsdysltisslesedfadyyclqyasspytfgggtkleilr
>d1knoc2 2.1.1.2.53 (109-214) Immunoglobulin (constant domains of L and H chains) {Fab CNJ206 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1knod1 2.1.1.1.46 (1-119) Immunoglobulin (variable domains of L and H chains) {Fab CNJ206 (mouse), kappa L chain}
dvklvesggglvqpggsrklscaasgftfssfgmhwvrqapekglewvayissgsstiyy
adtvkgrftisrdnpkntlflqmtslrsedtamyycargdyygsrgaywgqgtlvtvsa
>d1knod2 2.1.1.2.53 (120-235) Immunoglobulin (constant domains of L and H chains) {Fab CNJ206 (mouse), kappa L chain}
akttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsd
lytlsssvtvtsstwpsqsitcnvahpasstkvdkkieprg
>d1knoe1 2.1.1.1.46 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab CNJ206 (mouse), kappa L chain}
qiqmtqspsslsaslgervsltcrasqeisgylswlqqkpdgtikrliyaastldsgvpk
rfsgsrsgsdysltisslesedfadyyclqyasspytfgggtkleilr
>d1knoe2 2.1.1.2.53 (109-214) Immunoglobulin (constant domains of L and H chains) {Fab CNJ206 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1knof1 2.1.1.1.46 (1-119) Immunoglobulin (variable domains of L and H chains) {Fab CNJ206 (mouse), kappa L chain}
dvklvesggglvqpggsrklscaasgftfssfgmhwvrqapekglewvayissgsstiyy
adtvkgrftisrdnpkntlflqmtslrsedtamyycargdyygsrgaywgqgtlvtvsa
>d1knof2 2.1.1.2.53 (120-235) Immunoglobulin (constant domains of L and H chains) {Fab CNJ206 (mouse), kappa L chain}
akttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsd
lytlsssvtvtsstwpsqsitcnvahpasstkvdkkieprg
>d1knt__ 7.7.1.1.2 Collagen type VI (domain C5 from the alpha 3 chain) {human (Homo sapiens)}
tdicklpkdegtcrdfilkwyydpntkscarfwyggcggnenkfgsqkecekvca
>d1knya_ 5.10.1.2.1 Kanamycin nucleotidyltransferase (KNTase) {(Staphylococcus aureus)}
mngpiimtreermkivheikerildkygddvkaigvygslgrqtdgpysdiemmcvmste
eaefshewttgewkvevnfyseeilldyasqvesdwplthgqffsilpiydsggylekvy
qtaksveaqtfhdaicaliveelfeyagkwrnirvqgpttflpsltvqvamagamliglh
hricyttsasvlteavkqsdlpsgydhlcqfvmsgqlsdseklleslenfwngiqewter
hgyivdvskripf
>d1knyb_ 5.10.1.2.1 Kanamycin nucleotidyltransferase (KNTase) {(Staphylococcus aureus)}
mngpiimtreermkivheikerildkygddvkaigvygslgrqtdgpysdiemmcvmste
eaefshewttgewkvevnfyseeilldyasqvesdwplthgqffsilpiydsggylekvy
qtaksveaqtfhdaicaliveelfeyagkwrnirvqgpttflpsltvqvamagamliglh
hricyttsasvlteavkqsdlpsgydhlcqfvmsgqlsdseklleslenfwngiqewter
hgyivdvskripf
>d1koa_1 2.1.1.4.7 (6265-6361) Twitchin {Nematode (Caenorhabditis elegans)}
qprfivkpygtevgegqsanfycrviassppvvtwhkddrelkqsvkymkryngndyglt
inrvkgddkgeytvraknsygtkeeivflnvtrhsep
>d1koa_2 5.1.1.1.8 (5915-6264) Twitchin, kinase domain {(Caenorhabditis elegans), pjk4}
ydnyvfdiwkqyypqpveikhdhvldhydiheelgtgafgvvhrvteratgnnfaakfvm
tphesdketvrkeiqtmsvlrhptlvnlhdafeddnemvmiyefmsggelfekvadehnk
msedeaveymrqvckglchmhennyvhldlkpenimfttkrsnelklidfgltahldpkq
svkvttgtaefaapevaegkpvgyytdmwsvgvlsyillsglspfggenddetlrnvksc
dwnmddsafsgisedgkdfirkllladpntrmtihqalehpwltpgnapgrdsqipssry
tkirdsiktkydawpeplpplgrisnysslrkhrpqeysirdafwdrsea
>d1koba_ 5.1.1.1.7 Twitchin, kinase domain {california sea hare (aplysia californica), twk43}
indydkfyediwkkyvpqpvevkqgsvydyydileelgsgafgvvhrcvekatgrvfvak
fintpypldkytvkneisimnqlhhpklinlhdafedkyemvlileflsggelfdriaae
dykmseaevinymrqaceglkhmhehsivhldikpenimcetkkassvkiidfglatkln
pdeivkvttataefaapeivdrepvgfytdmwaigvlgyvllsglspfageddletlqnv
krcdwefdedafssvspeakdfiknllqkeprkrltvhdalehpwlkgdhsnltsripss
rynkirqkikekyadwpapqpaigrianfsslrkhrpqeyqiydsyfdrkeav
>d1kobb_ 5.1.1.1.7 Twitchin, kinase domain {california sea hare (aplysia californica), twk43}
indydkfyediwkkyvpqpvevkqgsvydyydileelgsgafgvvhrcvekatgrvfvak
fintpypldkytvkneisimnqlhhpklinlhdafedkyemvlileflsggelfdriaae
dykmseaevinymrqaceglkhmhehsivhldikpenimcetkkassvkiidfglatkln
pdeivkvttataefaapeivdrepvgfytdmwaigvlgyvllsglspfageddletlqnv
krcdwefdedafssvspeakdfiknllqkeprkrltvhdalehpwlkgdhsnltsripss
rynkirqkikekyadwpapqpaigrianfsslrkhrpqeyqiydsyfdrkea
>d1kpaa_ 4.9.1.1.3 Protein kinase C inhibitor-1, PKCI-1 {human (Homo sapiens)}
ggdtifgkiirkeipakiifeddrclafhdispqapthflvipkkhisqisvaedddesl
lghlmivgkkcaadlglnkgyrmvvnegsdggqsvyhvhlhvlggrqmhwppg
>d1kpab_ 4.9.1.1.3 Protein kinase C inhibitor-1, PKCI-1 {human (Homo sapiens)}
ggdtifgkiirkeipakiifeddrclafhdispqapthflvipkkhisqisvaedddesl
lghlmivgkkcaadlglnkgyrmvvnegsdggqsvyhvhlhvlggrqmhwppg
>d1kpba_ 4.9.1.1.3 Protein kinase C inhibitor-1, PKCI-1 {human (Homo sapiens)}
ggdtifgkiirkeipakiifeddrclafhdispqapthflvipkkhisqisvaedddesl
lghlmivgkkcaadlglnkgyrmvvnegsdggqsvyhvhlhvlggrqmhwppg
>d1kpbb_ 4.9.1.1.3 Protein kinase C inhibitor-1, PKCI-1 {human (Homo sapiens)}
ggdtifgkiirkeipakiifeddrclafhdispqapthflvipkkhisqisvaedddesl
lghlmivgkkcaadlglnkgyrmvvnegsdggqsvyhvhlhvlggrqmhwppg
>d1kpca_ 4.9.1.1.3 Protein kinase C inhibitor-1, PKCI-1 {human (Homo sapiens)}
dtifgkiirkeipakiifeddrclafhdispqapthflvipkkhisqisvaedddesllg
hlmivgkkcaadlglnkgyrmvvnegsdggqsvyhvhlhvlggrqmhwppg
>d1kpcb_ 4.9.1.1.3 Protein kinase C inhibitor-1, PKCI-1 {human (Homo sapiens)}
dtifgkiirkeipakiifeddrclafhdispqapthflvipkkhisqisvaedddesllg
hlmivgkkcaadlglnkgyrmvvnegsdggqsvyhvhlhvlggrqmhwppg
>d1kpcc_ 4.9.1.1.3 Protein kinase C inhibitor-1, PKCI-1 {human (Homo sapiens)}
dtifgkiirkeipakiifeddrclafhdispqapthflvipkkhisqisvaedddesllg
hlmivgkkcaadlglnkgyrmvvnegsdggqsvyhvhlhvlggrqmhwppg
>d1kpcd_ 4.9.1.1.3 Protein kinase C inhibitor-1, PKCI-1 {human (Homo sapiens)}
ifgkiirkeipakiifeddrclafhdispqapthflvipkkhisqisvaedddesllghl
mivgkkcaadlglnkgyrmvvnegsdggqsvyhvhlhvlggrqmhwppg
>d1kpea_ 4.9.1.1.3 Protein kinase C inhibitor-1, PKCI-1 {human (Homo sapiens)}
ggdtifgkiirkeipakiifeddrclafhdispqapthflvipkkhisqisvaedddesl
lghlmivgkkcaadlglnkgyrmvvnegsdggqsvyhvhlhvlggrqmhwppg
>d1kpeb_ 4.9.1.1.3 Protein kinase C inhibitor-1, PKCI-1 {human (Homo sapiens)}
ggdtifgkiirkeipakiifeddrclafhdispqapthflvipkkhisqisvaedddesl
lghlmivgkkcaadlglnkgyrmvvnegsdggqsvyhvhlhvlggrqmhwppg
>d1kpf__ 4.9.1.1.3 Protein kinase C inhibitor-1, PKCI-1 {human (Homo sapiens)}
dtifgkiirkeipakiifeddrclafhdispqapthflvipkkhisqisvaedddesllg
hlmivgkkcaadlglnkgyrmvvnegsdggqsvyhvhlhvlggrqmhwppg
>d1kpta_ 4.37.1.1.1 Virally encoded KP4 toxin {(Ustilago maydis) P4 strain}
lgincrgssqcglsggnlmvrirdqacgnqgqtwcpgerrakvcgtgnsisayvqstnnc
isgteacrhltnlvnhgcrvcgsdplyagndvsrgqltvnyvnsc
>d1kptb_ 4.37.1.1.1 Virally encoded KP4 toxin {(Ustilago maydis) P4 strain}
lgincrgssqcglsggnlmvrirdqacgnqgqtwcpgerrakvcgtgnsisayvqstnnc
isgteacrhltnlvnhgcrvcgsdplyagndvsrgqltvnyvnsc
>d1kraa_ 4.6.1.1.1 Urease, gamma-subunit {(Klebsiella aerogenes)}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1krab_ 2.66.2.1.1 Urease, beta-subunit {(Klebsiella aerogenes)}
mipgeyhvkpgqialntgratcrvvvenhgdrpiqvgshyhfaevnpalkfdrqqaagyr
lnipagtavrfepgqkrevelvafaghravfgfrgevmgpl
>d1krac1 2.69.1.1.1 (2-129,423-475) alpha-Subunit of urease, composite domain {(Klebsiella aerogenes)}
snisrqayadmfgptvgdkvrladtelwieveddlttygeevkfgggkvirdgmgqgqml
aadcvdlvltnalivdhwgivkadigvkdgrifaigkagnpdiqpnvtipigaateviaa
egkivtagXsievgkladlvvwspaffgvkpatvikggmiaiapmgdinasiptpqpvhy
rp
>d1krac2 3.1.2.2.1 (130-422,476-567) alpha-subunit of urease, catalytic domain {(Klebsiella aerogenes)}
gidthihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagviglkihedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvchhldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf
>d1krba_ 4.6.1.1.1 Urease, gamma-subunit {(Klebsiella aerogenes)}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1krbb_ 2.66.2.1.1 Urease, beta-subunit {(Klebsiella aerogenes)}
mipgeyhvkpgqialntgratcrvvvenhgdrpiqvgshyhfaevnpalkfdrqqaagyr
lnipagtavrfepgqkrevelvafaghravfgfrgevmgpl
>d1krbc1 2.69.1.1.1 (2-129,423-475) alpha-Subunit of urease, composite domain {(Klebsiella aerogenes)}
snisrqayadmfgptvgdkvrladtelwieveddlttygeevkfgggkvirdgmgqgqml
aadcvdlvltnalivdhwgivkadigvkdgrifaigkagnpdiqpnvtipigaateviaa
egkivtagXsievgkladlvvwspaffgvkpatvikggmiaiapmgdinasiptpqpvhy
rp
>d1krbc2 3.1.2.2.1 (130-422,476-567) alpha-subunit of urease, catalytic domain {(Klebsiella aerogenes)}
gidthihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagviglkiaedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvchhldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf
>d1krca_ 4.6.1.1.1 Urease, gamma-subunit {(Klebsiella aerogenes)}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1krcb_ 2.66.2.1.1 Urease, beta-subunit {(Klebsiella aerogenes)}
mipgeyhvkpgqialntgratcrvvvenhgdrpiqvgshyhfaevnpalkfdrqqaagyr
lnipagtavrfepgqkrevelvafaghravfgfrgevmgpl
>d1krcc1 2.69.1.1.1 (2-129,423-475) alpha-Subunit of urease, composite domain {(Klebsiella aerogenes)}
snisrqayadmfgptvgdkvrladtelwieveddlttygeevkfgggkvirdgmgqgqml
aadcvdlvltnalivdhwgivkadigvkdgrifaigkagnpdiqpnvtipigaateviaa
egkivtagXsievgkladlvvwspaffgvkpatvikggmiaiapmgdinasiptpqpvhy
rp
>d1krcc2 3.1.2.2.1 (130-422,476-567) alpha-subunit of urease, catalytic domain {(Klebsiella aerogenes)}
gidthihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagviglkihedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvcahldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf
>d1krn__ 7.13.1.1.1 Plasminogen kringle 4 {human (Homo sapiens)}
dcyhgdgqsyrgtssttttgkkcqswssmtphrhqktpenypnagltmnycrnpdadkgp
wcfttdpsvrweycnlkkc
>d1krpa1 3.47.3.4.1 (324-518) Exonuclease domain of DNA polymerase {(Escherichia coli)}
misydnyvtildeetlkawiaklekapvfafdtetdsldnisanlvglsfaiepgvaayi
pvahdyldapdqisreralellkplledekalkvgqnlkydrgilanygielrgiafdtm
lesyilnsvagrhdmdslaerwlkhktitfeeiagkgknqltfnqialeeagryaaedad
vtlqlhlkmwpdlqk
>d1krpa2 5.9.1.1.1 (519-928) DNA polymerase I (Klenow fragment) {(Escherichia coli)}
hkgplnvfeniemplvpvlsrierngvkidpkvlhnhseeltlrlaelekkaheiageef
nlsstkqlqtilfekqgikplkktpggapstseevleelaldyplpkvileyrglaklks
tytdklplminpktgrvhtsyhqavtatgrlsstdpnlqnipvrneegrrirqafiaped
yvivsadysqielrimahlsrdkglltafaegkdihrataaevfglpletvtseqrrsak
ainfgliygmsafglarqlniprkeaqkymdlyferypgvleymertraqakeqgyvetl
dgrrlylpdikssngarraaaeraainapmqgtaadiikramiavdawlqaeqprvrmim
qvhdelvfevhkddvdavakqihqlmenctrldvpllvevgsgenwdqah
>d1krs__ 2.29.4.1.3 Lysyl-tRNA synthetase (LysRS) {(Escherichia coli, lysS) gene}
frrdhtsdqlhaefdgkeneelealnievavagrmmtrrimgkasfvtlqdvggriqlyv
arddlpegvyneqfkkwdlgdilgakgklfktktgelsihctelrlltka
>d1krt__ 2.29.4.1.3 Lysyl-tRNA synthetase (LysRS) {(Escherichia coli, lysS) gene}
frrdhtsdqlhaefdgkeneelealnievavagrmmtrrimgkasfvtlqdvggriqlyv
arddlpegvyneqfkkwdlgdilgakgklfktktgelsihctelrlltka
>d1ksaa_ 2.57.1.1.2 Bacteriochlorophyl A protein {Green sulfur bacterium (Chlorobium tepidum)}
ttahsdyeivleggssswgkvkarakvnappaspllpadcdvklnvkpldpakgfvrisa
vfesivdstknkltieadianetkerrisvgegmvsvgdfshtfsfegsvvnlfyyrsda
vrrnvpnpiymqgrqfhdilmkvpldnndlidtwegtvkaigstgafndwirdfwfigpa
ftalneggqrisrievnglntesgpkgpvgvsrwrfshggsgmvdsisrwaelfpsdkln
rpaqveagfrsdsqgievkvdgefpgvsvdaggglrrilnhpliplvhhgmvgkfnnfnv
daqlkvvlpkgykiryaapqyrsqnleeyrwsggayarwvehvckggvgqfeilyaq
>d1ksab_ 2.57.1.1.2 Bacteriochlorophyl A protein {Green sulfur bacterium (Chlorobium tepidum)}
ttahsdyeivleggssswgkvkarakvnappaspllpadcdvklnvkpldpakgfvrisa
vfesivdstknkltieadianetkerrisvgegmvsvgdfshtfsfegsvvnlfyyrsda
vrrnvpnpiymqgrqfhdilmkvpldnndlidtwegtvkaigstgafndwirdfwfigpa
ftalneggqrisrievnglntesgpkgpvgvsrwrfshggsgmvdsisrwaelfpsdkln
rpaqveagfrsdsqgievkvdgefpgvsvdaggglrrilnhpliplvhhgmvgkfnnfnv
daqlkvvlpkgykiryaapqyrsqnleeyrwsggayarwvehvckggvgqfeilyaq
>d1ksia1 2.22.2.1.2 (207-647) Copper amine oxidase, domain 3 (catalytic) {Pea seedling (Pivum sativum)}
vskqsppfgpkqhsltshqpqgpgfqinghsvswanwkfhigfdvragivislasiydle
khksrrvlykgyiselfvpyqdpteefyfktffdsgefgfglstvslipnrdcpphaqfi
dtyvhsangtpillknaicvfeqygnimwrhtengipnesieesrtevnlivrtivtvgn
xdnvidwefkasgsikpsialsgileikgtnikhkdeikedlhgklvsansigiyhdhfy
iyyldfdidgthnsfektslktvrikdgsskrksywttetqtaktesdakitiglapael
vvvnpniktavgnevgyrlipaipahpllteddypqirgaftnynvwvtaynrtekwagg
lyvdhsrgddtlavwtkqnreivnkdivmwhvvgihhvpaqedfpimpllstsfelrptn
ffernpvlktlsprdvawpgc
>d1ksia2 4.13.2.1.2 (6-98) Copper amine oxidase, domains 1 and 2 {Pea seedling (Pivum sativum)}
vqhpldpltkeeflavqtivqnkypisnnrlafhyiglddpekdhvlryethptlvsipr
kifvvaiinsqtheilinlrirsivsdnihngy
>d1ksia3 4.13.2.1.2 (99-206) Copper amine oxidase, domains 1 and 2 {Pea seedling (Pivum sativum)}
gfpilsvdeqslaiklplkyppfidsvkkrglnlseivcssftmgwfgeeknvrtvrldc
fmkestvniyvrpitgitivadldlmkiveyhdrdieavptaenteyq
>d1ksib1 2.22.2.1.2 (207-647) Copper amine oxidase, domain 3 (catalytic) {Pea seedling (Pivum sativum)}
vskqsppfgpkqhsltshqpqgpgfqinghsvswanwkfhigfdvragivislasiydle
khksrrvlykgyiselfvpyqdpteefyfktffdsgefgfglstvslipnrdcpphaqfi
dtyvhsangtpillknaicvfeqygnimwrhtengipnesieesrtevnlivrtivtvgn
xdnvidwefkasgsikpsialsgileikgtnikhkdeikedlhgklvsansigiyhdhfy
iyyldfdidgthnsfektslktvrikdgsskrksywttetqtaktesdakitiglapael
vvvnpniktavgnevgyrlipaipahpllteddypqirgaftnynvwvtaynrtekwagg
lyvdhsrgddtlavwtkqnreivnkdivmwhvvgihhvpaqedfpimpllstsfelrptn
ffernpvlktlsprdvawpgc
>d1ksib2 4.13.2.1.2 (6-98) Copper amine oxidase, domains 1 and 2 {Pea seedling (Pivum sativum)}
vqhpldpltkeeflavqtivqnkypisnnrlafhyiglddpekdhvlryethptlvsipr
kifvvaiinsqtheilinlrirsivsdnihngy
>d1ksib3 4.13.2.1.2 (99-206) Copper amine oxidase, domains 1 and 2 {Pea seedling (Pivum sativum)}
gfpilsvdeqslaiklplkyppfidsvkkrglnlseivcssftmgwfgeeknvrtvrldc
fmkestvniyvrpitgitivadldlmkiveyhdrdieavptaenteyq
>d1kspa1 3.47.3.4.1 (324-518) Exonuclease domain of DNA polymerase {(Escherichia coli)}
misydnyvtildeetlkawiaklekapvfafdtetdsldnisanlvglsfaiepgvaayi
pvahdyldapdqisreralellkplledekalkvgqnlkydrgilanygielrgiafdtm
lesyilnsvagrhdmdslaerwlkhktitfeeiagkgknqltfnqialeeagryaaedad
vtlqlhlkmwpdlqk
>d1kspa2 5.9.1.1.1 (519-928) DNA polymerase I (Klenow fragment) {(Escherichia coli)}
hkgplnvfeniemplvpvlsrierngvkidpkvlhnhseeltlrlaelekkaheiageef
nlsstkqlqtilfekqgikplkktpggapstseevleelaldyplpkvileyrglaklks
tytdklplminpktgrvhtsyhqavtatgrlsstdpnlqnipvrneegrrirqafiaped
yvivsadysqielrimahlsrdkglltafaegkdihrataaevfglpletvtseqrrsak
ainfgliygmsafglarqlniprkeaqkymdlyferypgvleymertraqakeqgyvetl
dgrrlylpdikssngarraaaeraainapmqgtaadiikramiavdawlqaeqprvrmim
qvhdelvfevhkddvdavakqihqlmenctrldvpllvevgsgenwdqah
>d1ksr__ 2.1.1.5.14 The F-actin cross-linking gelation factor (ABP-120), one repeat (ROD 4) {slime mold (Dictyostelium discoideum)}
adpeksyaegpgldggecfqpskfkihavdpdgvhrtdggdgfvvtiegpapvdpvmvdn
gdgtydvefepkeagdyvinltldgdnvngfpktvtvkpa
>d1kst__ 7.19.1.1.3 Kistrin {(Agkistrodon rhodostoma)}
gkecdcsspenpccdaatcklrpgaqcgeglcceqckfsragkicriprgdmpddrctgq
sadcpryh
>d1ksz__ 3.29.1.6.2 Adenylosuccinate synthetase (gene purA product) {(Escherichia coli)}
gnnvvvlgtqwgdegkgkivdllterakyvvryqgghnaghtlvingektvlhlipsgil
renvtsiigngvvlspaalmkemkeledrgipvrerlllseacplildyhvaldnareka
rgakaigttgrgigpayedkvarrglrvgdlfdketfaeklkevmeyhnfqlvnyykaea
vdyqkvlddtmavadiltsmvvdvsdlldqarqrgdfvmfegaqgtlldidhgtypyvts
snttaggvatgsglgpryvdyvlgilkaystrvgagpfptelfdetgeflckqgnefgat
tgrrrrtgwldtvavrravqlnslsgfcltkldvldglkevklcvayrmpdgrevtttpl
aaddwkgvepiyetmpgwsestfgvkdrsglpqaalnyikrieeltgvpidiistgpdrt
etmilrdpfda
>d1kte__ 3.38.1.1.6 thioltransferase {Pig (Sus scrofa)}
aqafvnskiqpgkvvvfikptcpfcrktqellsqlpfkegllefvditatsdtneiqdyl
qqltgartvprvfigkeciggctdlesmhkrgelltrlqqvgavk
>d1ktq_1 3.47.3.4.2 (290-450) Exonuclease domain of DNA polymerase {(Thermus aquaticus)}
spkaleeapwpppegafvgfvlsrkepmwadllalaaarggrvhrapepykalrdlkear
gllakdlsvlalreglglppgddpmllaylldpsnttpegvarryggewteeageraals
erlfanlwgrlegeerllwlyreverplsavlahmeatgvr
>d1ktq_2 5.9.1.1.2 (451-832) DNA polymerase I (Klenow fragment) {(Thermus aquaticus)}
ldvaylralslevaeeiarleaevfrlaghpfnlnsrdqlervlfdelglpaigktektg
krstsaavlealreahpivekilqyreltklkstyidplpdlihprtgrlhtrfnqtata
tgrlsssdpnlqnipvrtplgqrirrafiaeegwllvaldysqielrvlahlsgdenlir
vfqegrdihtetaswmfgvpreavdplmrraaktinfgvlygmsahrlsqelaipyeeaq
afieryfqsfpkvrawiektleegrrrgyvetlfgrrryvpdlearvksvreaaermafn
mpvqgtaadlmklamvklfprleemgarmllqvhdelvleapkeraeavarlakevmegv
yplavplevevgigedwlsake
>d1ktx__ 7.3.6.2.13 Kaliotoxin (KTX) {(Androctonus mauretanicus mauretanicus)}
gveinvkcsgspqclkpckdagmrfgkcmnrkchctp
>d1kuh__ 4.52.1.1.1 Zinc protease {(Streptomyces caespitosus)}
tvtvtydpsnapsfqqeianaaqiwnssvrnvqlraggnadfsyyegndsrgsyaqtdgh
grgyifldyqqnqqydstrvtahetghvlglpdhyqgpcselmsgggpgpsctnpypnaq
ersrvnalwang
>d1kul__ 2.3.1.1.5 Glucoamilase, granular starch-binding domain {(Aspergillus niger)}
cttptavavtfdltatttygeniylvgsisqlgdwetsdgialsadkytssdplwyvtvt
lpagesfeykfiriesddsvewesdpnreytvpqacgtstatvtdtwr
>d1kum__ 2.3.1.1.5 Glucoamilase, granular starch-binding domain {(Aspergillus niger)}
cttptavavtfdltatttygeniylvgsisqlgdwetsdgialsadkytssdplwyvtvt
lpagesfeykfiriesddsvewesdpnreytvpqacgtstatvtdtwr
>d1kun__ 7.7.1.1.2 Collagen type VI (domain C5 from the alpha 3 chain) {human (Homo sapiens)}
etdicklpkdegtcrdfilkwyydpntkscarfwyggcggnenkfgsqkecekvcapv
>d1kva__ 3.47.3.1.2 RNase H {(Escherichia coli), RNase HI}
mlkqveiftdgsclgnpgpggygailryrgrektfsagytrttnnrmelmaaivalealk
ehcevilstdsqyvrqgitqwihnwkkrgwktadkkpvknvdlwqrldaalgqhqikwew
vkghaghpenercaelaraaamnptledtgyqvev
>d1kvb__ 3.47.3.1.2 RNase H {(Escherichia coli), RNase HI}
mlkqveiftdgsclgnpgpggygailryrgrektfsagytrttnnrmelmaaivalealk
ehcevilstdsqyvrqgitqwihnwkkrgwktadkkpvknvdlwqrldaalgqhqikwew
vkghaghpenerchelaraaamnptledtgyqvev
>d1kvc__ 3.47.3.1.2 RNase H {(Escherichia coli), RNase HI}
mlkqveiftdgsclgnpgpggygailryrgrektfsagytrttnnrmelmaaivalealk
ehcevilstdsqyvrqgitqwihnwkkrgwktadkkpvknvdlwqrldaalgqhqikwew
vkghaghpenercnelaraaamnptledtgyqvev
>e1kvd.1a 4.37.1.2.1 SMK toxin {halotolerant yeast (Pichia farinosa)}
wslrwrmqksttiaaiagcsgaatfgglaggivgciaagilailqgfevnwhnggggdrs
npv
>e1kvd.1b 4.37.1.2.1 SMK toxin {halotolerant yeast (Pichia farinosa)}
geattiwgvgadeaidkgtpskndlqnmsadlakngfkghqgvacstvkdgnkdvymikf
slaggsndpggspcsdd
>e1kvd.2c 4.37.1.2.1 SMK toxin {halotolerant yeast (Pichia farinosa)}
wslrwrmqksttiaaiagcsgaatfgglaggivgciaagilailqgfevnwhnggggdrs
npv
>e1kvd.2d 4.37.1.2.1 SMK toxin {halotolerant yeast (Pichia farinosa)}
geattiwgvgadeaidkgtpskndlqnmsadlakngfkghqgvacstvkdgnkdvymikf
slaggsndpggspcsdd
>e1kve.1a 4.37.1.2.1 SMK toxin {halotolerant yeast (Pichia farinosa)}
wslrwrmqksttiaaiagcsgaatfgglaggivgciaagilailqgfevnwhnggggdrs
npv
>e1kve.1b 4.37.1.2.1 SMK toxin {halotolerant yeast (Pichia farinosa)}
geattiwgvgadeaidkgtpskndlqnmsadlakngfkghqgvacstvkdgnkdvymikf
slaggsndpggspcsdd
>e1kve.2c 4.37.1.2.1 SMK toxin {halotolerant yeast (Pichia farinosa)}
wslrwrmqksttiaaiagcsgaatfgglaggivgciaagilailqgfevnwhnggggdrs
npv
>e1kve.2d 4.37.1.2.1 SMK toxin {halotolerant yeast (Pichia farinosa)}
geattiwgvgadeaidkgtpskndlqnmsadlakngfkghqgvacstvkdgnkdvymikf
slaggsndpggspcsdd
>d1kvoa_ 1.103.1.2.10 Phospholipase A2 {human (Homo sapiens) synovial fluid}
nlvnfhrmiklttgkeaalsygfygchcgvggrgspkdatdrccvthdccykrlekrgcg
tkflsykfsnsgsritcakqdscrsqlcecdkaaatcfarnkttynkkyqyysnkhcrgs
tprc
>d1kvob_ 1.103.1.2.10 Phospholipase A2 {human (Homo sapiens) synovial fluid}
nlvnfhrmiklttgkeaalsygfygchcgvggrgspkdatdrccvthdccykrlekrgcg
tkflsykfsnsgsritcakqdscrsqlcecdkaaatcfarnkttynkkyqyysnkhcrgs
tprc
>d1kvoc_ 1.103.1.2.10 Phospholipase A2 {human (Homo sapiens) synovial fluid}
nlvnfhrmiklttgkeaalsygfygchcgvggrgspkdatdrccvthdccykrlekrgcg
tkflsykfsnsgsritcakqdscrsqlcecdkaaatcfarnkttynkkyqyysnkhcrgs
tprc
>d1kvod_ 1.103.1.2.10 Phospholipase A2 {human (Homo sapiens) synovial fluid}
nlvnfhrmiklttgkeaalsygfygchcgvggrgspkdatdrccvthdccykrlekrgcg
tkflsykfsnsgsritcakqdscrsqlcecdkaaatcfarnkttynkkyqyysnkhcrgs
tprc
>d1kvoe_ 1.103.1.2.10 Phospholipase A2 {human (Homo sapiens) synovial fluid}
nlvnfhrmiklttgkeaalsygfygchcgvggrgspkdatdrccvthdccykrlekrgcg
tkflsykfsnsgsritcakqdscrsqlcecdkaaatcfarnkttynkkyqyysnkhcrgs
tprc
>d1kvof_ 1.103.1.2.10 Phospholipase A2 {human (Homo sapiens) synovial fluid}
nlvnfhrmiklttgkeaalsygfygchcgvggrgspkdatdrccvthdccykrlekrgcg
tkflsykfsnsgsritcakqdscrsqlcecdkaaatcfarnkttynkkyqyysnkhcrgs
tprc
>d1kvq__ 3.22.1.2.1 Uridine diphosphogalactose-4-epimerase (UDP-galactose 4-epimerase) {(Escherichia coli)}
mrvlvtggsgyigshtcvqllqnghdviildnlcnskrsvlpvierlggkhptfvegdir
nealmteilhdhaidtvihfaglkavgesvqkpleyydnnvngtlrlisamraanvknfi
fssaatvygdnpkipyvesfptgtpqspygksklmveqiltdlqkaqpdwsiallryfnp
vgahpsgdmgedpqgipnnlmpyiaqvavgrrdslaifgndyptedgtgvrdyihvmdla
dghvvameklankpgvhiynlgagvgnsvldvvnafskacgkpvnyhfaprregdlpayw
adaskadrelnwrvtrtldemaqdtwhwqsrhpqgypd
>d1kvr__ 3.22.1.2.1 Uridine diphosphogalactose-4-epimerase (UDP-galactose 4-epimerase) {(Escherichia coli)}
mrvlvtggsgyigshtcvqllqnghdviildnlcnskrsvlpvierlggkhptfvegdir
nealmteilhdhaidtvihfaglkavgesvqkpleyydnnvngtlrlisamraanvknfi
fssaatvygdqpkipyvesfptgtpqspygksklmveqiltdlqkaqpdwsiallryfnp
vgahpsgdmgedpqgipnnlmpyiaqvavgrrdslaifgndyptedgtgvrdyihvmdla
dghvvameklankpgvhiynlgagvgnsvldvvnafskacgkpvnyhfaprregdlpayw
adaskadrelnwrvtrtldemaqdtwhwqsrhpqgypd
>d1kvs__ 3.22.1.2.1 Uridine diphosphogalactose-4-epimerase (UDP-galactose 4-epimerase) {(Escherichia coli)}
mrvlvtggsgyigshtcvqllqnghdviildnlcnskrsvlpvierlggkhptfvegdir
nealmteilhdhaidtvihfaglkavgesvqkpleyydnnvngtlrlisamraanvknfi
fsstatvygdnpkipyvesfptgtpqspygksklmveqiltdlqkaqpdwsiallryfnp
vgahpsgdmgedpqgipnnlmpyiaqvavgrrdslaifgndyptedgtgvrdyihvmdla
dghvvameklankpgvhiynlgagvgnsvldvvnafskacgkpvnyhfaprregdlpayw
adaskadrelnwrvtrtldemaqdtwhwqsrhpqgypd
>d1kvt__ 3.22.1.2.1 Uridine diphosphogalactose-4-epimerase (UDP-galactose 4-epimerase) {(Escherichia coli)}
mrvlvtggsgyigshtcvqllqnghdviildnlcnskrsvlpvierlggkhptfvegdir
nealmteilhdhaidtvihfaglkavgesvqkpleyydnnvngtlrlisamraanvknfi
fssvatvygdnpkipyvesfptgtpqspygksklmveqiltdlqkaqpdwsiallryfnp
vgahpsgdmgedpqgipnnlmpyiaqvavgrrdslaifgndyptedgtgvrdyihvmdla
dghvvameklankpgvhiynlgagvgnsvldvvnafskacgkpvnyhfaprregdlpayw
adaskadrelnwrvtrtldemaqdtwhwqsrhpqgypd
>d1kvu__ 3.22.1.2.1 Uridine diphosphogalactose-4-epimerase (UDP-galactose 4-epimerase) {(Escherichia coli)}
mrvlvtggsgyigshtcvqllqnghdviildnlcnskrsvlpvierlggkhptfvegdir
nealmteilhdhaidtvihfaglkavgesvqkpleyydnnvngtlrlisamraanvknfi
fsssatvygdqpkipyvesfptgtpqspfgksklmveqiltdlqkaqpdwsiallryfnp
vgahpsgdmgedpqgipnnlmpyiaqvavgrrdslaifgndyptedgtgvrdyihvmdla
dghvvameklankpgvhiynlgagvgnsvldvvnafskacgkpvnyhfaprregdlpayw
adaskadrelnwrvtrtldemaqdtwhwqsrhpqgypd
>d1kwaa_ 2.26.1.1.2 Cask/Lin-2 {Human (Homo sapiens)}
rsrlvqfqkntdepmgitlkmnelnhcivarimhggmihrqgtlhvgdeireingisvan
qtveqlqkmlremrgsitfkivpsyref
>d1kwab_ 2.26.1.1.2 Cask/Lin-2 {Human (Homo sapiens)}
rsrlvqfqkntdepmgitlkmlnhcivarimhggmihrqgtlhvgdeireingisvanqt
veqlqkmlremrgsitfkivpsyref
>d1kxa__ 2.35.1.3.1 viral capsid protein {(Sindbis virus)}
alkleadrlfdvknedgdvighalamegkvmkplhvkgtidhpvlsklkftkssaydmef
aqlpvnmrseaftytsehpegfynwhhgavqysggrftiprgvggrgdsgrpimdnsgrv
vaivlggadegtrtalsvvtwnskgktikttpegteew
>d1kxb__ 2.35.1.3.1 viral capsid protein {(Sindbis virus)}
alkleadrlfdvknedgdvighalamegkvmkplhvkgtidhpvlsklkftkssaydmef
aqlpvnmrseaftytsehpegfynwhhgavqysggrftiprgvggrgdagrpimdnsgrv
vaivlggadegtrtalsvvtwnskgktikttpegteew
>d1kxc__ 2.35.1.3.1 viral capsid protein {(Sindbis virus)}
alkleadrlfdvknedgdvighalamegkvmkplhvkgtidhpvlsklkftkssaydmef
aqlpvnmrseaftytsehpegfykwhhgavqysggrftiprgvggrgdsgrpimdnsgrv
vaivlggadegtrtalsvvtwnskgktikttpegteew
>d1kxd__ 2.35.1.3.1 viral capsid protein {(Sindbis virus)}
alkleadrlfdvknedgdvighalamegkvmkplhvkgtidhpvlsklkftkssaydmef
aqlpvnmrseaftytsehpegfynwhhgavqysggrftiprgvggrgdsgrpimdlsgrv
vaivlggadegtrtalsvvtwnskgktikttpegteew
>d1kxe__ 2.35.1.3.1 viral capsid protein {(Sindbis virus)}
lkleadrlfdvknedgdvighalamegkvmkplhvkgtidhpvlsklkftkssaydmefa
qlpvnmrseaftstsghpegfynwhhgavqysggrftiprgvggrgdsgrpimdnsgrvv
aivlggadegtrtalsvvtwnskgktikttpegteew
>d1kxf__ 2.35.1.3.1 viral capsid protein {(Sindbis virus)}
malkleadrlfdvknedgdvighalamegkvmkplhvkgtidhpvlsklkftkssaydme
faqlpvnmrseaftytsehpegfynwhhgavqysggrftiprgvggrgdsgrpimdnsgr
vvaivlggadegtrtalsvvtwnskgktikttpegteew
>d1kxia_ 7.6.1.1.6 Cardiotoxin V {taiwan cobra (Naja naja atra)}
lkchntqlpfiyktcpegknlcfkatlkkfplkfpvkrgcadncpknsallkyvccstdk
cn
>d1kxib_ 7.6.1.1.6 Cardiotoxin V {taiwan cobra (Naja naja atra)}
lkchntqlpfiyktcpegknlcfkatlkkfplkfpvkrgcadncpknsallkyvccstdk
cn
>d1kxu_1 1.63.1.1.3 (11-161) Cyclin h (mcs2) {human (Homo sapiens)}
wtfsseeqlarlradanrkfrckavangkvlpndpvflepheemtlckyyekrllefcsv
fkpamprsvvgtacmyfkrfylnnsvmeyhpriimltcaflackvdefnvsspqfvgnlr
esplgqekaleqileyellliqqlnfhlivh
>d1kxu_2 1.63.1.1.3 (162-286) Cyclin h (mcs2) {human (Homo sapiens)}
npyrpfegflidlktrypilenpeilrktaddflnrialtdayllytpsqialtailssa
sragitmesylseslmlkenrtclsqlldimksmrnlvkkyepprseevavlkqklerch
saela
>d1kxw__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgdwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1kxx__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhglnnyrgyslgdwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1kxy__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhglnnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1kzua_ 6.6.1.1.1 Light-harvesting complex LH2 {Purple bacterium (Rhodopseudomonas acidophila)}
nqgkiwtvvnpaigipallgsvtviailvhlailshttwfpaywqggv
>d1kzub_ 6.6.1.1.1 Light-harvesting complex LH2 {Purple bacterium (Rhodopseudomonas acidophila)}
atltaeqseelhkyvidgtrvflglalvahflafsatpwlh
>d1kzud_ 6.6.1.1.1 Light-harvesting complex LH2 {Purple bacterium (Rhodopseudomonas acidophila)}
nqgkiwtvvnpaigipallgsvtviailvhlailshttwfpaywqggv
>d1kzue_ 6.6.1.1.1 Light-harvesting complex LH2 {Purple bacterium (Rhodopseudomonas acidophila)}
atltaeqseelhkyvidgtrvflglalvahflafsatpwlh
>d1kzug_ 6.6.1.1.1 Light-harvesting complex LH2 {Purple bacterium (Rhodopseudomonas acidophila)}
nqgkiwtvvnpaigipallgsvtviailvhlailshttwfpaywqggv
>d1kzuh_ 6.6.1.1.1 Light-harvesting complex LH2 {Purple bacterium (Rhodopseudomonas acidophila)}
atltaeqseelhkyvidgtrvflglalvahflafsatpwlh
>d1l00__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfamgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l01__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfragiwdayknl
>d1l02__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgawdayknl
>d1l03__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgcwdayknl
>d1l04__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgdwdayknl
>d1l05__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgdwdayknl
>d1l06__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgewdayknl
>d1l07__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgfwdayknl
>d1l08__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtggwdayknl
>d1l09__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtghwdayknl
>d1l10__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgiwdayknl
>d1l11__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtglwdayknl
>d1l12__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgnwdayknl
>d1l13__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgrwdayknl
>d1l14__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgswdayknl
>d1l15__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgvwdayknl
>d1l16__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtdtwdayknl
>d1l17__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnvfemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l18__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnyfemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l19__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspdlnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l20__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpdrakrvittfrtgtwdayknl
>d1l21__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncggvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l22__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqgrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l23__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrailrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l24__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnpklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l25__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkavydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l26__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkcvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l27__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkdvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l28__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkgvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l29__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkhvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l30__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklklvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l31__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkrvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l32__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklksvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l33__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaaanlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l34__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrhcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l35__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrcdeglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknc
>d1l36__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdaaaaalaksrwynqtpnrakrvittfrtgtwdayk
>d1l37__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagfenslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l38__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqekrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l39__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtperakrvittfrtgtwdayknl
>d1l40__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtperakrvittfrtgtwdayknl
>d1l41__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnahlkpvydsldavrraalinmvfqmgetgvdgftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l42__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrleiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l43__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrleiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l44__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslem
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l45__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaesrwynqtpnrakrvittfrtgtwdayknl
>d1l46__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnraervittfrtgtwdayknl
>d1l47__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfetgtwdayknl
>d1l48__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcvlinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l49__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcvlinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvitsfrtgtwdayknl
>d1l50__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcvlinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrcitsfrtgtwdayknl
>d1l51__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcvlinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakriitsfrtgtwdayknl
>d1l52__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvitsfrtgtwdayknl
>d1l53__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrcittfrtgtwdayknl
>d1l54__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinkvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l55__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydslnavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1l56__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitp
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l57__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftdslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1l58__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtanrakrvittfrtgtwdayknl
>d1l59__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgengvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1l60__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvaaftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l61__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspnlnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1l62__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgedgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1l63__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1l64__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslaaaaaaaaaaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1l65__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakselakaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1l66__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaaaseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1l67__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseadkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1l68__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakaeldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1l69__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnaaksrwynqtpnrakrvittfrtgtwdayk
>d1l70__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaaaalaksrwynqtpnrakrvittfrtgtwdayk
>d1l71__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdaaaanlaksrwynqtpnrakrvittfrtgtwdayk
>d1l72__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwaaaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1l73__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwaaaaaalaksrwynqtpnrakrvittfrtgtwdayk
>d1l74__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdaaaaaaaksrwynqtpnrakrvittfrtgtwdayk
>d1l75__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwaaaaaaaaksrwynqtpnrakrvittfrtgtwdayk
>d1l76__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvpaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1l77__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinlvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1l79__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraafinmvfqmgetgiagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1l80__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraafinlvfqmgetgiagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1l81__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraafinlvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittlrtgtwdayk
>d1l82__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraafinlvfqmgetgiagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittlrtgtwdayk
>d1l83__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraaainmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1l84__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraaainmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittartgtwdayk
>d1l85__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittartgtwdayk
>d1l86__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittirtgtwdayk
>d1l87__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittlrtgtwdayk
>d1l88__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittmrtgtwdayk
>d1l89__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraaainmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittartgtwdayk
>d1l90__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraaainmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1l91__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraafinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1l92__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraaiinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1l93__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraaminmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1l94__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraavinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1l95__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittvrtgtwdayk
>d1l96__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnpfemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1l97a_ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnpfemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l97b_ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnpfemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l98__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfemgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1l99__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfgmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1laa__ 4.2.1.2.8 Lysozyme {human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrsteygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1lab__ 2.65.1.1.3 The ipoyl domain of dihydrolipoamide acetyltransferase {(Bacillus stearothermophilus)}
afefklpdigegihegeivkwfvkpgdevneddvlcevqndkavveipspvkgkvleilv
pegtvatvgqtlitldapgy
>d1lac__ 2.65.1.1.3 The ipoyl domain of dihydrolipoamide acetyltransferase {(Bacillus stearothermophilus)}
afefklpdigegihegeivkwfvkpgdevneddvlcevqndkavveipspvkgkvleilv
pegtvatvgqtlitldapgy
>d1lafe_ 3.82.1.1.3 Lysine-,arginine-,ornithine-binding (LAO) protein {(Salmonella typhimurium)}
alpqtvrigtdttyapfsskdakgefigfdidlgnemckrmqvkctwvasdfdalipslk
akkidaiisslsitdkrqqeiafsdklyaadsrliaakgspiqptleslkgkhvgvlqgs
tqeayandnwrtkgvdvvayanqdliysdltagrldaalqdevaasegflkqpagkeyaf
agpsvkdkkyfgdgtgvglrkddtelkaafdkaltelrqdgtydkmakkyfdfnvygd
>d1lage_ 3.82.1.1.3 Lysine-,arginine-,ornithine-binding (LAO) protein {(Salmonella typhimurium)}
alpqtvrigtdttyapfsskdakgefigfdidlgnemckrmqvkctwvasdfdalipslk
akkidaiisslsitdkrqqeiafsdklyaadsrliaakgspiqptleslkgkhvgvlqgs
tqeayandnwrtkgvdvvayanqdliysdltagrldaalqdevaasegflkqpagkeyaf
agpsvkdkkyfgdgtgvglrkddtelkaafdkaltelrqdgtydkmakkyfdfnvygd
>d1lahe_ 3.82.1.1.3 Lysine-,arginine-,ornithine-binding (LAO) protein {(Salmonella typhimurium)}
alpqtvrigtdttyapfsskdakgefigfdidlgnemckrmqvkctwvasdfdalipslk
akkidaiisslsitdkrqqeiafsdklyaadsrliaakgspiqptleslkgkhvgvlqgs
tqeayandnwrtkgvdvvayanqdliysdltagrldaalqdevaasegflkqpagkeyaf
agpsvkdkkyfgdgtgvglrkddtelkaafdkaltelrqdgtydkmakkyfdfnvygd
>d1lam_1 3.41.1.1.1 (1-159) Leucine aminopeptidase, N-terminal domain {bovine (Bos taurus)}
tkglvlgiyskekeedepqftsagenfnklvsgklreilnisgpplkagktrtfyglhed
fpsvvvvglgkktagideqenwhegkeniraavaagcrqiqdleipsvevdpcgdaqaaa
egavlglyeyddlkqkrkvvvsaklhgsedqeawqrgvl
>d1lam_2 3.58.4.3.1 (160-484) Leucine aminopeptidase, C-terminal domain {bovine (Bos taurus)}
fasgqnlarrlmetpanemtptkfaeiveenlksasiktdvfirpkswieeqemgsflsv
akgseeppvfleihykgspnasepplvfvgkgitfdsggisikaaanmdlmradmggaat
icsaivsaakldlpinivglaplcenmpsgkankpgdvvrarngktiqvdntdaegrlil
adalcyahtfnpkviinaatltgamdialgsgatgvftnsswlwnklfeasietgdrvwr
mplfehytrqvidcqladvnnigkyrsagactaaaflkefvthpkwahldiagvmtnkde
vpylrkgmagrptrtlieflfrfsq
>d1lana1 3.41.1.1.1 (1-159) Leucine aminopeptidase, N-terminal domain {bovine (Bos taurus)}
tkglvlgiyskekeedepqftsagenfnklvsgklreilnisgpplkagktrtfyglhed
fpsvvvvglgkktagideqenwhegkeniraavaagcrqiqdleipsvevdpcgdaqaaa
egavlglyeyddlkqkrkvvvsaklhgsedqeawqrgvl
>d1lana2 3.58.4.3.1 (160-484) Leucine aminopeptidase, C-terminal domain {bovine (Bos taurus)}
fasgqnlarrlmetpanemtptkfaeiveenlksasiktdvfirpkswieeqemgsflsv
akgseeppvfleihykgspnasepplvfvgkgitfdsggisikaaanmdlmradmggaat
icsaivsaakldlpinivglaplcenmpsgkankpgdvvrarngktiqvdntdaegrlil
adalcyahtfnpkviinaatltgamdialgsgatgvftnsswlwnklfeasietgdrvwr
mplfehytrqvidcqladvnnigkyrsagactaaaflkefvthpkwahldiagvmtnkde
vpylrkgmagrptrtlieflfrfsq
>d1lap_1 3.41.1.1.1 (1-159) Leucine aminopeptidase, N-terminal domain {bovine (Bos taurus)}
tkglvlgiyskekeedepqftsagenfnklvsgklreilnisgpplkagktrtfyglhed
fpsvvvvglgkktagideqenwhegkeniraavaagcrqiqdleipsvevdpcgdaqaaa
egavlglyeyddlkqkrkvvvsaklhgsedqeawqrgvl
>d1lap_2 3.58.4.3.1 (160-484) Leucine aminopeptidase, C-terminal domain {bovine (Bos taurus)}
fasgqnlarrlmetpanemtptkfaeiveenlksasiktdvfirpkswieeqemgsflsv
akgseeppvfleihykgspnasepplvfvgkgitfdsggisikaaanmdlmradmggaat
icsaivsaakldlpinivglaplcenmpsgkankpgdvvrarngktiqvdntdaegrlil
adalcyahtfnpkviinaatltgamdialgsgatgvftnsswlwnklfeasietgdrvwr
mplfehytrqvidcqladvnnigkyrsagactaaaflkefvthpkwahldiagvmtnkde
vpylrkgmagrptrtlieflfrfsq
>d1lata_ 7.33.1.2.4 Glucocorticoid receptor DNA-binding domain {rat (Rattus norvegicus)}
rpclvcsdeasgchygvltcegckaffkravegqhnylckyegkciidkirrkncpacry
rkclqagmnle
>d1latb_ 7.33.1.2.4 Glucocorticoid receptor DNA-binding domain {rat (Rattus norvegicus)}
arpclvcsdeasgchygvltcegckaffkravegqhnylckyegkciidkirrkncpacr
yrkclqagmnlear
>d1laue_ 3.12.1.1.2 Uracil-DNA glycosylase {(Herpes simplex virus type-1) HSV1}
ldwttfrrvfliddawrplmepelanpltahllaeynrrcqteevlppredvfswtryct
pdevrvviigqdpyhhpgqahglafsvranvppppslrnvlaavkncypearmsghgcle
kwardgvlllnttltvkrgaaashsrigwdrfvggvirrlaarrpglvfmlwgthaqnai
rpdprvhcvlkfshpsplskvpfgtcqhflvanryletrsispidwsv
>d1lav__ 3.47.3.1.1 RNase H {(Escherichia coli)}
mlkqveiftdgsclgnpgpggygailryrgrektfsagytrttnnrmelmaaivalealk
ehcevilstdsqylrqgitqwihnwkkrgwktadkkpvknvdlwqrldaalgqhqikwew
vkghaghpenercdelaraaamnptledtgyqvev
>d1law__ 3.47.3.1.1 RNase H {(Escherichia coli)}
mlkqveiftdgsclgnpgpggygailryrgrektfsagytrttnnrmelmaaivalealk
ehcevilstdsqyirqgitqwihnwkkrgwktadkkpvknvdlwqrldaalgqhqikwew
vkghaghpenercdelaraaamnptledtgyqvev
>d1lay__ 2.43.1.1.1 Human cytomegalovirus protease {(Human cytomegalovirus), hCMV}
qavapvyvggflarydqspdeaelllprdvvehwlhaqgqgqpslsvalplninhddtav
vghvaamqsvrdglfclgcvtsprfleivrrasekselvsrgpvsplqpdkvveflsgsy
aglslssrrcddvevatslsgsettpfkhvalcsvgrrrgtlavygrdpewvtqrfpdlt
aadrdglraqwqrcgstavdasgdpfrsdsygllgnsvdalyirerlpklrydkqlvgvt
eresyvka
>d1lba__ 4.68.1.1.1 Bacteriophage T7 lysozyme (Zn amidase) {(bacteriophage T7)}
akqrestdaifvhcsatkpsqnvgvreirqwhkeqgwldvgyhfiikrdgtveagrdema
vgshakgynhnsigvclvggiddkgkfdanftpaqmqslrsllvtllakyegavlrahhe
vapkacpsfdlkrwweknelvtsdrg
>d1lbd__ 1.95.1.1.1 retinoid-X receptor (RXR-alpha) {Human (Homo sapiens)}
sanedmpverileaelavepktetyveanmglnpsspndpvtnicqaadkqlftlvewak
riphfselplddqvillragwnelliasfshrsiavkdgillatglhvhrnsahsagvga
ifdrvltelvskmrdmqmdktelgclraivlfnpdskglsnpaevealrekvyasleayc
khkypeqpgrfaklllrlpalrsiglkclehlfffkligdtpidtflmemleaphqmt
>d1lbea_ 5.5.1.1.1 ADP ribosyl cyclase {sea hare (Aplysia californica)}
ivptrelenvflgrckdyeitryldilprvrsdcsalwkdffkafsfknpcdldlgsykd
fftsaqqqlpknkvmfwsgvydeahdyantgrkyitledtlpgymlnslvwcgqranpgf
nekvcpdfktcpvqaresfwgmasssyahsaegevtymvdgsnpkvpayrpdsffgkyel
pnltnkvtrvkvivlhrlgekiiekcgagslldleklvkakhfafdcvenpravlfllcs
dnpnarecrl
>d1lbeb_ 5.5.1.1.1 ADP ribosyl cyclase {sea hare (Aplysia californica)}
ivptrelenvflgrckdyeitryldilprvrsdcsalwkdffkafsfknpcdldlgsykd
fftsaqqqlpknkvmfwsgvydeahdyantgrkyitledtlpgymlnslvwcgqranpgf
nekvcpdfktcpvqaresfwgmasssyahsaegevtymvdgsnpkvpayrpdsffgkyel
pnltnkvtrvkvivlhrlgekiiekcgagslldleklvkakhfafdcvenpravlfllcs
dnpnarec
>d1lbga1 1.32.1.3.2 (1-60) Lac repressor (LacR), N-terminal domain {(Escherichia coli), strain bmh 74-12}
mkpvtlydvaeyagvsyqtvsrvvnqashvsaktrekveaamaelnyipnrvaqqlagkq
>d1lbga2 3.81.1.1.8 (61-357) Lac-repressor (lacR) core (C-terminal domain) {(Escherichia coli)}
slligvatsslalhapsqivaaiksradqlgasvvvsmversgveacktavhnllaqrvs
gliinyplddqdaiaveaactnvpalfldvsdqtpinsiifshedgtrlgvehlvalghq
qiallagplssvsarlrlagwhkyltrnqiqpiaeregdwsamsgfqqtmqmlnegivpt
amlvandqmalgamraitesglrvgadisvvgyddtedsscyipplttikqdfrllgqts
vdrllqlsqgqavkgnqllpvslvkrkttlapntqtaspraladslmqlarqvsrle
>d1lbgb1 1.32.1.3.2 (1-60) Lac repressor (LacR), N-terminal domain {(Escherichia coli), strain bmh 74-12}
mkpvtlydvaeyagvsyqtvsrvvnqashvsaktrekveaamaelnyipnrvaqqlagkq
>d1lbgb2 3.81.1.1.8 (61-357) Lac-repressor (lacR) core (C-terminal domain) {(Escherichia coli)}
slligvatsslalhapsqivaaiksradqlgasvvvsmversgveacktavhnllaqrvs
gliinyplddqdaiaveaactnvpalfldvsdqtpinsiifshedgtrlgvehlvalghq
qiallagplssvsarlrlagwhkyltrnqiqpiaeregdwsamsgfqqtmqmlnegivpt
amlvandqmalgamraitesglrvgadisvvgyddtedsscyipplttikqdfrllgqts
vdrllqlsqgqavkgnqllpvslvkrkttlapntqtaspraladslmqlarqvsrle
>d1lbgc1 1.32.1.3.2 (1-60) Lac repressor (LacR), N-terminal domain {(Escherichia coli), strain bmh 74-12}
mkpvtlydvaeyagvsyqtvsrvvnqashvsaktrekveaamaelnyipnrvaqqlagkq
>d1lbgc2 3.81.1.1.8 (61-357) Lac-repressor (lacR) core (C-terminal domain) {(Escherichia coli)}
slligvatsslalhapsqivaaiksradqlgasvvvsmversgveacktavhnllaqrvs
gliinyplddqdaiaveaactnvpalfldvsdqtpinsiifshedgtrlgvehlvalghq
qiallagplssvsarlrlagwhkyltrnqiqpiaeregdwsamsgfqqtmqmlnegivpt
amlvandqmalgamraitesglrvgadisvvgyddtedsscyipplttikqdfrllgqts
vdrllqlsqgqavkgnqllpvslvkrkttlapntqtaspraladslmqlarqvsrle
>d1lbgd1 1.32.1.3.2 (1-60) Lac repressor (LacR), N-terminal domain {(Escherichia coli), strain bmh 74-12}
mkpvtlydvaeyagvsyqtvsrvvnqashvsaktrekveaamaelnyipnrvaqqlagkq
>d1lbgd2 3.81.1.1.8 (61-357) Lac-repressor (lacR) core (C-terminal domain) {(Escherichia coli)}
slligvatsslalhapsqivaaiksradqlgasvvvsmversgveacktavhnllaqrvs
gliinyplddqdaiaveaactnvpalfldvsdqtpinsiifshedgtrlgvehlvalghq
qiallagplssvsarlrlagwhkyltrnqiqpiaeregdwsamsgfqqtmqmlnegivpt
amlvandqmalgamraitesglrvgadisvvgyddtedsscyipplttikqdfrllgqts
vdrllqlsqgqavkgnqllpvslvkrkttlapntqtaspraladslmqlarqvsrle
>d1lbha_ 3.81.1.1.8 Lac-repressor (lacR) core (C-terminal domain) {(Escherichia coli)}
lligvatsslalhapsqivaaiksradqlgasvvvsmversgveacktavhnllaqrvsg
liinyplddqdaiaveaactnvpalfldvsdqtpinsiifshedgtrlgvehlvalghqq
iallagplssvsarlrlagwhkyltrnqiqpiaeregdwsamsgfqqtmqmlnegivpta
mlvandqmalgamraitesglrvgadisvvgyddtedsscyipplttikqdfrllgqtsv
drllqlsqgqavkgnqllpvslvkrkttlapntqtaspraladslmqlarqvsrle
>d1lbhb_ 3.81.1.1.8 Lac-repressor (lacR) core (C-terminal domain) {(Escherichia coli)}
lligvatsslalhapsqivaaiksradqlgasvvvsmversgveacktavhnllaqrvsg
liinyplddqdaiaveaactnvpalfldvsdqtpinsiifshedgtrlgvehlvalghqq
iallagplssvsarlrlagwhkyltrnqiqpiaeregdwsamsgfqqtmqmlnegivpta
mlvandqmalgamraitesglrvgadisvvgyddtedsscyipplttikqdfrllgqtsv
drllqlsqgqavkgnqllpvslvkrkttlapntqtaspraladslmqlarqvsrle
>d1lbhc_ 3.81.1.1.8 Lac-repressor (lacR) core (C-terminal domain) {(Escherichia coli)}
lligvatsslalhapsqivaaiksradqlgasvvvsmversgveacktavhnllaqrvsg
liinyplddqdaiaveaactnvpalfldvsdqtpinsiifshedgtrlgvehlvalghqq
iallagplssvsarlrlagwhkyltrnqiqpiaeregdwsamsgfqqtmqmlnegivpta
mlvandqmalgamraitesglrvgadisvvgyddtedsscyipplttikqdfrllgqtsv
drllqlsqgqavkgnqllpvslvkrkttlapntqtaspraladslmqlarqvsrle
>d1lbhd_ 3.81.1.1.8 Lac-repressor (lacR) core (C-terminal domain) {(Escherichia coli)}
lligvatsslalhapsqivaaiksradqlgasvvvsmversgveacktavhnllaqrvsg
liinyplddqdaiaveaactnvpalfldvsdqtpinsiifshedgtrlgvehlvalghqq
iallagplssvsarlrlagwhkyltrnqiqpiaeregdwsamsgfqqtmqmlnegivpta
mlvandqmalgamraitesglrvgadisvvgyddtedsscyipplttikqdfrllgqtsv
drllqlsqgqavkgnqllpvslvkrkttlapntqtaspraladslmqlarqvsrle
>d1lbia_ 3.81.1.1.8 Lac-repressor (lacR) core (C-terminal domain) {(Escherichia coli)}
lligvatsslalhapsqivaaiksradqlgasvvvsmversgveacktavhnllaqrvsg
liinyplddqdaiaveaactnvpalfldvsdqtpinsiifshedgtrlgvehlvalghqq
iallagplssvsarlrlagwhkyltrnqiqpiaeregdwsamsgfqqtmqmlnegivpta
mlvandqmalgamraitesglrvgadisvvgyddtedsscyipplttikqdfrllgqtsv
drllqlsqgqavkgnqllpvslvkrkttlapntqtaspraladslmqlarqvsrle
>d1lbib_ 3.81.1.1.8 Lac-repressor (lacR) core (C-terminal domain) {(Escherichia coli)}
lligvatsslalhapsqivaaiksradqlgasvvvsmversgveacktavhnllaqrvsg
liinyplddqdaiaveaactnvpalfldvsdqtpinsiifshedgtrlgvehlvalghqq
iallagplssvsarlrlagwhkyltrnqiqpiaeregdwsamsgfqqtmqmlnegivpta
mlvandqmalgamraitesglrvgadisvvgyddtedsscyipplttikqdfrllgqtsv
drllqlsqgqavkgnqllpvslvkrkttlapntqtaspraladslmqlarqvsrle
>d1lbic_ 3.81.1.1.8 Lac-repressor (lacR) core (C-terminal domain) {(Escherichia coli)}
lligvatsslalhapsqivaaiksradqlgasvvvsmversgveacktavhnllaqrvsg
liinyplddqdaiaveaactnvpalfldvsdqtpinsiifshedgtrlgvehlvalghqq
iallagplssvsarlrlagwhkyltrnqiqpiaeregdwsamsgfqqtmqmlnegivpta
mlvandqmalgamraitesglrvgadisvvgyddtedsscyipplttikqdfrllgqtsv
drllqlsqgqavkgnqllpvslvkrkttlapntqtaspraladslmqlarqvsrle
>d1lbid_ 3.81.1.1.8 Lac-repressor (lacR) core (C-terminal domain) {(Escherichia coli)}
lligvatsslalhapsqivaaiksradqlgasvvvsmversgveacktavhnllaqrvsg
liinyplddqdaiaveaactnvpalfldvsdqtpinsiifshedgtrlgvehlvalghqq
iallagplssvsarlrlagwhkyltrnqiqpiaeregdwsamsgfqqtmqmlnegivpta
mlvandqmalgamraitesglrvgadisvvgyddtedsscyipplttikqdfrllgqtsv
drllqlsqgqavkgnqllpvslvkrkttlapntqtaspraladslmqlarqvsrle
>d1lbs__ 3.56.1.9.1 Triacylglycerol lipase {yeast (Candida antarctica) form b}
lpsgsdpafsqpksvldagltcqgaspssvskpillvpgtgttgpqsfdsnwiplstqlg
ytpcwispppfmlndtqvnteymvnaitalyagsgnnklpvltwsqgglvaqwgltffps
irskvdrlmafapdykgtvlagpldalavsapsvwqqttgsalttalrnaggltqivptt
nlysatdeivqpqvsnspldssylfngknvqaqavcgplfvidhagsltsqfsyvvgrsa
lrsttgqarsadygitdcnplpandltpeqkvaaaallapaaaaivagpkqncepdlmpy
arpfavgkrtcsgivtp
>d1lbt__ 3.56.1.9.1 Triacylglycerol lipase {yeast (Candida antarctica) form b}
lpsgsdpafsqpksvldagltcqgaspssvskpillvpgtgttgpqsfdsnwiplstqlg
ytpcwispppfmlndtqvnteymvnaitalyagsgnnklpvltwsqgglvaqwgltffps
irskvdrlmafapdykgtvlagpldalavsapsvwqqttgsalttalrnaggltqivptt
nlysatdeivqpqvsnspldssylfngknvqaqavcgplfvidhagsltsqfsyvvgrsa
lrsttgqarsadygitdcnplpandltpeqkvaaaallapaaaaivagpkqncepdlmpy
arpfavgkrtcsgivtp
>d1lbu_1 1.20.1.1.1 (1-83) Zn2+ DD-carboxypeptidase, the N-terminal domain {(Streptomyces albus) G}
dgcytwsgtlsegssgeavrqlqirvagypgtgaqlaidgqfgpatkaavqrfqsaygla
adgiagpatfnkiyqlqdddctp
>d1lbu_2 4.35.1.1.1 (84-213) Zn2+ DD-carboxypeptidase, the C-terminal, catalytic domain {(Streptomyces albus) G}
vnftyaelnrcnsdwsggkvsaataranalvtmwklqamrhamgdkpitvnggfrsvtcn
snvggasnsrhmyghaadlgagsqgfcalaqaarnhgfteilgpgypghndhthvaggdg
rfwsapscgi
>d1lca__ 4.67.1.1.2 Thymidylate synthase {(Lactobacillus casei )}
mleqpyldlakkvldeghfkpdrthtgtysifghqmrfdlskgfpllttkkvpfglikse
llwflhgdtnirfllqhrnhiwdewafekwvksdeyhgpdmtdfghrsqkdpefaavyhe
emakfddrvlhddafaakygdlglvygsqwrawhtskgdtidqlgdvieqikthpysrrl
ivsawnpedvptmalppchtlyqfyvndgklslqlyqrsadiflgvpfniasyallthlv
ahecglevgefihtfgdahlyvnhldqikeqlsrtprpaptlqlnpdkhdifdfdmkdik
llnydpypaikapvav
>d1lcb__ 4.67.1.1.2 Thymidylate synthase {(Lactobacillus casei )}
mleqpyldlakkvldeghfkpdrthtgtysifghqmrfdlskgfpllttkkvpfglikse
llwflhgdtnirfllqhrnhiwdewafekwvksdeyhgpdmtdfghrsqkdpefaavyhe
emakfddrvlhddafaakygdlglvygsqwrawhtskgdtidqlgdvieqikthpysrrl
ivsawnpedvptmalppchtlyqfyvndgklslqlyqrsadiflgvpfniasyallthlv
ahecglevgefihtfgdahlyvnhldqikeqlsrtprpaptlqlnpdkhdifdfdmkdik
llnydpypaikapvav
>d1lcca_ 1.32.1.3.2 Lac repressor (LacR), N-terminal domain {(Escherichia coli), strain bmh 74-12}
mkpvtlydvaeyagvsyqtvsrvvnqashvsaktrekveaamaelnyipnr
>d1lcda_ 1.32.1.3.2 Lac repressor (LacR), N-terminal domain {(Escherichia coli), strain bmh 74-12}
mkpvtlydvaeyagvsyqtvsrvvnqashvsaktrekveaamaelnyipnr
>d1lce__ 4.67.1.1.2 Thymidylate synthase {(Lactobacillus casei )}
mleqpyldlakkvldeghfkpdrthtgtysifghqmrfdlskgfpllttkkvpfglikse
llwflhgdtnirfllqhrnhiwdewafekwvksdeyhgpdmtdfghrsqkdpefaavyhe
emakfddrvlhddafaakygdlglvygsqwrawhtskgdtidqlgdvieqikthpysrrl
ivsawnpedvptmalppchtlyqfyvndgklslqlyqrsadiflgvpfniasyallthlv
ahecglevgefihtfgdahlyvnhldqikeqlsrtprpaptlqlnpdkhdifdfdmkdik
llnydpypaikapvav
>d1lcf_1 3.82.1.2.1 (1-334) Lactoferrin {human (Homo sapiens)}
grrrsvqwcavsnpeatkcfqwqrnmrkvrgppvsclkrdspiqciqaiaenradavtld
ggfiyeaglapyklrpvaaevygterqprthyyavavvkkggsfqlnelqglkschtglr
rtagwnvpigtlrpflnwtgppepieaavarffsascvpgadkgqfpnlcrlcagtgenk
cafssqepyfsysgafkclkdgagdvafirestvfedlsdeaerdeyellcpdntrkpvd
kfkdchlarvpshavvarsvngkedaiwnllrqaqekfgkdkspkfqlfgspsgqkdllf
kdsaigfsrvppridsglylgsgyftaiqnlrks
>d1lcf_2 3.82.1.2.1 (335-691) Lactoferrin {human (Homo sapiens)}
eeevaarrarvvwcavgeqelrkcnqwsglsegsvtcssasttedcialvlkgeadamsl
dggyvytagkcglvpvlaenyksqqssdpdpncvdrpvegylavavvrrsdtsltwnsvk
gkkschtavdrtagwnipmgllfnqtgsckfdeyfsqscapgsdprsnlcalcigdeqge
nkcvpnsneryygytgafrclaenagdvafvkdvtvlqntdgnnneawakdlkladfall
cldgkrkpvtearschlamapnhavvsrmdkverlkqvllhqqakfgrngsdcpdkfclf
qsetknllfndnteclarlhgkttyekylgpqyvagitnlkkcstsplleaceflrk
>d1lci__ 5.19.1.1.1 Luciferase {Firefly (Phontinus pyralis)}
aknikkgpapfypledgtageqlhkamkryalvpgtiaftdahievnityaeyfemsvrl
aeamkryglntnhrivvcsenslqffmpvlgalfigvavapandiynerellnsmnisqp
tvvfvskkglqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfvp
esfdrdktialimnssgstglpkgvalphrtacvrfshardpifgnqiipdtailsvvpf
hhgfgmfttlgylicgfrvvlmyrfeeelflrslqdykiqsallvptlfsffakstlidk
ydlsnlheiasggaplskevgeavakrfhlpgirqgygltettsailitpegddkpgavg
kvvpffeakvvdldtgktlgvnqrgelcvrgpmimsgyvnnpeatnalidkdgwlhsgdi
aywdedehffivdrlkslikykgyqvapaelesillqhpnifdagvaglpdddagelpaa
vvvlehgktmtekeivdyvasqvttakklrggvvfvdevpkgltgkldarkireilikak
k
>d1lcja_ 4.53.1.1.1 p56-lck tyrosine kinase {human (Homo sapiens)}
epepwffknlsrkdaerqllapgnthgsfliresestagsfslsvrdfdqnqgevvkhyk
irnldnggfyispritfpglhelvrhytnasdglctrlsrpcqt
>d1lcka1 2.24.2.1.21 (63-116) p56-lck tyrosine kinase, SH3 domain {human (Homo sapiens)}
dnlvialhsyepshdgdlgfekgeqlrileqsgewwkaqslttgqegfipfnfv
>d1lcka2 4.53.1.1.1 (117-226) p56-lck tyrosine kinase {human (Homo sapiens)}
akanslepepwffknlsrkdaerqllapgnthgsfliresestagsfslsvrdfdqnqge
vvkhykirnldnggfyispritfpglhelvrhytnasdglctrlsrpcqt
>d1lcl__ 2.21.1.3.4 Charcot-Leyden crystal (CLC) protein {human (Homo sapiens)}
sllpvpyteaaslstgstvtikgrplvcflnepylqvdfhtemkeesdivfhfqvcfgrr
vvmnsreygawkqqvesknmpfqdgqefelsisvlpdkyqvmvngqssytfdhrikpeav
kmvqvwrdisltkfnvsylkr
>d1lcoa1 3.1.7.1.5 (98-511) Flavocytochrome b2, C-terminal domain {yeast (Saccharomyces cerevisiae)}
apgetkediarkeqlksllppldniinlydfeylasqtltkqawafyssgandevthren
hnayhriffkpkilvdvrkvdistdmlgshvdvpfyvsatalcklgnplegekdvargcg
qgvtkvpqmistlascspeeiieaapsdkqiqwyqlyvnsdrkitddlvknveklgvkal
fvtvdapslgqrekdmklkfsntkagpkamkktnveesqgasralskfidpsltwkdiee
lkkktklpivikgvqrtedvikaaeigvsgvvlsnhggrqldfsrapievlaetmpileq
rnlkdklevfvdggvrrgtdvlkalclgakgvglgrpflyanscygrngvekaieilrde
iemsmrllgvtsiaelkpdlldlstlkartvgvpndvlynevyegptltefeda
>d1lcoa2 4.70.1.1.3 (10-97) Flavocytochrome b2, N-terminal domain {yeast (Saccharomyces cerevisiae)}
kispaevakhnkpddcwvvingyvydltrflpnhpggqdvikfnagkdvtaifeplhapn
vidkyiapekklgplqgsmppelvcppy
>d1lcpa1 3.41.1.1.1 (1-159) Leucine aminopeptidase, N-terminal domain {bovine (Bos taurus)}
tkglvlgiyskekeedepqftsagenfnklvsgklreilnisgpplkagktrtfyglhed
fpsvvvvglgkktagideqenwhegkeniraavaagcrqiqdleipsvevdpcgdaqaaa
egavlglyeyddlkqkrkvvvsaklhgsedqeawqrgvl
>d1lcpa2 3.58.4.3.1 (160-484) Leucine aminopeptidase, C-terminal domain {bovine (Bos taurus)}
fasgqnlarrlmetpanemtptkfaeiveenlksasiktdvfirpkswieeqemgsflsv
akgseeppvfleihykgspnasepplvfvgkgitfdsggisikaaanmdlmradmggaat
icsaivsaakldlpinivglaplcenmpsgkankpgdvvrarngktiqvdntdaegrlil
adalcyahtfnpkviinaatltgamdialgsgatgvftnsswlwnklfeasietgdrvwr
mplfehytrqvidcqladvnnigkyrsagactaaaflkefvthpkwahldiagvmtnkde
vpylrkgmagrptrtlieflfrfsq
>d1lcpb1 3.41.1.1.1 (1-159) Leucine aminopeptidase, N-terminal domain {bovine (Bos taurus)}
tkglvlgiyskekeedepqftsagenfnklvsgklreilnisgpplkagktrtfyglhed
fpsvvvvglgkktagideqenwhegkeniraavaagcrqiqdleipsvevdpcgdaqaaa
egavlglyeyddlkqkrkvvvsaklhgsedqeawqrgvl
>d1lcpb2 3.58.4.3.1 (160-484) Leucine aminopeptidase, C-terminal domain {bovine (Bos taurus)}
fasgqnlarrlmetpanemtptkfaeiveenlksasiktdvfirpkswieeqemgsflsv
akgseeppvfleihykgspnasepplvfvgkgitfdsggisikaaanmdlmradmggaat
icsaivsaakldlpinivglaplcenmpsgkankpgdvvrarngktiqvdntdaegrlil
adalcyahtfnpkviinaatltgamdialgsgatgvftnsswlwnklfeasietgdrvwr
mplfehytrqvidcqladvnnigkyrsagactaaaflkefvthpkwahldiagvmtnkde
vpylrkgmagrptrtlieflfrfsq
>d1lct__ 3.82.1.2.1 Lactoferrin {human (Homo sapiens)}
rsvqwcavsnpeatkcfqwqrnmrkvrgppvscikrdspiqciqaiaenradavtldggf
iyeaglapyklrpvaaevygterqprthyyavavvkkggsfqlnelqglkschtglrrta
gwnvpigtlrpflnwtgppepieaavarffsascvpgadkgqfpnlcrlcagtgenkcaf
ssqepyfsysgafkclrdgagdvafirestvfedlsdeaerdeyellcpdntrkpvdkfk
dchlarvpshavvarsvngkedaiwnllrqaqekfgkdkspkfqlfgspsgqkdllfkds
aigfsrvppridsglylgsgyfta
>d1ld9a1 2.1.1.2.14 (182-268) Class I MHC, beta2-microglobulin and alpha-3 domain {mouse (Mus musculus) H-2LD}
tdspkahvthhprskgevtlrcwalgfypaditltwqlngeeltqdmelvetrpagdgtf
qkwasvvvplgkeqnytcrvyheglpe
>d1ld9a2 4.15.1.1.18 (1-181) MHC class I, alpha-1 and alpha-2 domains {mouse (Mus musculus) H-2LD}
gphsmryfetavsrpglgepryisvgyvdnkefvrfdsdaenpryepqapwmeqegpeyw
eritqiakgqeqwfrvnlrtllgyynqsaggthtlqwmygcdvgsdgrllrgyeqfaydg
cdyialnedlktwtaadmaaqitrrkweqagaaeyyraylegecvewlhrylkngnatll
r
>d1ld9d1 2.1.1.2.14 (182-268) Class I MHC, beta2-microglobulin and alpha-3 domain {mouse (Mus musculus) H-2LD}
tdspkahvthhprskgevtlrcwalgfypaditltwqlngeeltqdmelvetrpagdgtf
qkwasvvvplgkeqnytcrvyheglpe
>d1ld9d2 4.15.1.1.18 (1-181) MHC class I, alpha-1 and alpha-2 domains {mouse (Mus musculus) H-2LD}
gphsmryfetavsrpglgepryisvgyvdnkefvrfdsdaenpryepqapwmeqegpeyw
eritqiakgqeqwfrvnlrtllgyynqsaggthtlqwmygcdvgsdgrllrgyeqfaydg
cdyialnedlktwtaadmaaqitrrkweqagaaeyyraylegecvewlhrylkngnatll
r
>d1ldb_1 3.22.1.5.10 (15-162) Lactate dehydrogenase {(Bacillus stearothermophilus)}
mknnggarvvvigagfvgasyvfalmnqgiadeivlidaneskaigdamdfnhgkvfapk
pvdiwhgdyddcrdadlvvicaganqkpgetrldlvdkniaifrsivesvmasgfqglfl
vatnpvdiltyatwkfsglphervigsg
>d1ldb_2 4.100.1.1.10 (163-331) Lactate dehydrogenase {(Bacillus stearothermophilus)}
tildtarfrfllgeyfsvapqnvhayiigehgdtelpvwsqayigvmpirklveskgeea
qkdlerifvnvrdaayqiiekkgatyygiamglarvtrailhnenailtvsayldglyge
rdvyigvpavinrngirevieielnddeknrfhhsaatlksvlaraftr
>d1ldca1 3.1.7.1.5 (98-511) Flavocytochrome b2, C-terminal domain {yeast (Saccharomyces cerevisiae)}
apgetkediarkeqlksllppldniinlydfeylasqtltkqawafyssgandevthren
hnayhriffkpkilvdvrkvdistdmlgshvdvpfyvsatalcklgnplegekdvargcg
qgvtkvpqmistlascspeeiieaapsdkqiqwyqlyvnsdrkitddlvknveklgvkal
fvtvdapslgqrekdmklkfsntkagpkamkktnveesqgasralskfidpsltwkdiee
lkkktklpivikgvqrtedvikaaeigvsgvvlsnhggrqldfsrapievlaetmpileq
rnlkdklevfvdggvrrgtdvlkalclgakgvglgrpflyanscygrngvekaieilrde
iemsmrllgvtsiaelkpdlldlstlkartvgvpndvlynevyegptltefeda
>d1ldca2 4.70.1.1.3 (10-97) Flavocytochrome b2, N-terminal domain {yeast (Saccharomyces cerevisiae)}
kispaevakhnkpddcwvvingyvydltrflpnhpggqdvikfnagkdvtaifeplhapn
vidkyiapekklgplqgsmppelvcppy
>d1ldea1 2.25.1.2.1 (1-174,325-374) Alcohol dehydrogenase {horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1ldea2 3.22.1.1.1 (175-324) Alcohol dehydrogenase {horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1ldeb1 2.25.1.2.1 (1-174,325-374) Alcohol dehydrogenase {horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1ldeb2 3.22.1.1.1 (175-324) Alcohol dehydrogenase {horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1ldec1 2.25.1.2.1 (1-174,325-374) Alcohol dehydrogenase {horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1ldec2 3.22.1.1.1 (175-324) Alcohol dehydrogenase {horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1lded1 2.25.1.2.1 (1-174,325-374) Alcohol dehydrogenase {horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1lded2 3.22.1.1.1 (175-324) Alcohol dehydrogenase {horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1ldg_1 3.22.1.5.9 (18-163) Lactate dehydrogenase {malarial parasite (Plasmodium falciparum)}
apkakivlvgsgmiggvmatlivqknlgdvvlfdivknmphgkaldtshtnvmaysnckv
sgsntyddlagsdvvivtagftkapgksdkewnrldllplnnkimieigghikkncpnaf
iivvtnpvdvmvqllhqhsgvpknkiigl
>d1ldg_2 4.100.1.1.9 (164-329) Lactate dehydrogenase {malarial parasite (Plasmodium falciparum)}
ggvldtsrlkyyisqklnvcprdvnahivgahgnkmvllkryitvggiplqefinnklis
daeleaifdrtvntaleivnlhaspyvapaaaiiemaesylkdlkkvlicstllegqygh
sdifggtpvvlgangveqvielqlnseekakfdeaiaetkrmkala
>d1ldl__ 7.11.1.1.1 Ligand-binding domain of low-density lipoprotein receptor {human (Homo sapiens)}
avgdrcernefqcqdgkcisykwvcdgsaecqdgsdesqetclsvt
>d1ldm_1 3.22.1.5.8 (1-160) Lactate dehydrogenase {dogfish (Squalus acanthias)}
atlkdklighlatsqeprsynkitvvgvgavgmacaisilmkdladevalvdvmedklkg
emmdlqhgslflhtakivsgkdysvsagsklvvitagarqqegesrlnlvqrnvnifkfi
ipnivkhspdciilvvsnpvdvltyvawklsglpmhriig
>d1ldm_2 4.100.1.1.8 (161-329) Lactate dehydrogenase {dogfish (Squalus acanthias)}
sgcnldsarfrylmgerlgvhscschgwvigehgdsvpsvwsgmnvasiklhpldgtnkd
kqdwkklhkdvvdsayeviklkgytswaiglsvadlaetimknlcrvhpvstmvkdfygi
kdnvflslpcvlndhgisnivkmklkpneeqqlqksattlwdiqkdlkf
>d1ldna1 3.22.1.5.10 (15-162) Lactate dehydrogenase {(Bacillus stearothermophilus)}
mknnggarvvvigagfvgasyvfalmnqgiadeivlidaneskaigdamdfnhgkvfapk
pvdiwhgdyddcrdadlvvicaganqkpgetrldlvdkniaifrsivesvmasgfqglfl
vatnpvdiltyatwkfsglphervigsg
>d1ldna2 4.100.1.1.10 (163-330) Lactate dehydrogenase {(Bacillus stearothermophilus)}
tildtarfrfllgeyfsvapqnvhayiigehgdtelpvwsqayigvmpirklveskgeea
qkdlerifvnvrdaayqiiekkgatyygiamglarvtrailhnenailtvsayldglyge
rdvyigvpavinrngirevieielnddeknrfhhsaatlksvlaraft
>d1ldnb1 3.22.1.5.10 (15-162) Lactate dehydrogenase {(Bacillus stearothermophilus)}
mknnggarvvvigagfvgasyvfalmnqgiadeivlidaneskaigdamdfnhgkvfapk
pvdiwhgdyddcrdadlvvicaganqkpgetrldlvdkniaifrsivesvmasgfqglfl
vatnpvdiltyatwkfsglphervigsg
>d1ldnb2 4.100.1.1.10 (163-330) Lactate dehydrogenase {(Bacillus stearothermophilus)}
tildtarfrfllgeyfsvapqnvhayiigehgdtelpvwsqayigvmpirklveskgeea
qkdlerifvnvrdaayqiiekkgatyygiamglarvtrailhnenailtvsayldglyge
rdvyigvpavinrngirevieielnddeknrfhhsaatlksvlaraft
>d1ldnc1 3.22.1.5.10 (15-162) Lactate dehydrogenase {(Bacillus stearothermophilus)}
mknnggarvvvigagfvgasyvfalmnqgiadeivlidaneskaigdamdfnhgkvfapk
pvdiwhgdyddcrdadlvvicaganqkpgetrldlvdkniaifrsivesvmasgfqglfl
vatnpvdiltyatwkfsglphervigsg
>d1ldnc2 4.100.1.1.10 (163-330) Lactate dehydrogenase {(Bacillus stearothermophilus)}
tildtarfrfllgeyfsvapqnvhayiigehgdtelpvwsqayigvmpirklveskgeea
qkdlerifvnvrdaayqiiekkgatyygiamglarvtrailhnenailtvsayldglyge
rdvyigvpavinrngirevieielnddeknrfhhsaatlksvlaraft
>d1ldnd1 3.22.1.5.10 (15-162) Lactate dehydrogenase {(Bacillus stearothermophilus)}
mknnggarvvvigagfvgasyvfalmnqgiadeivlidaneskaigdamdfnhgkvfapk
pvdiwhgdyddcrdadlvvicaganqkpgetrldlvdkniaifrsivesvmasgfqglfl
vatnpvdiltyatwkfsglphervigsg
>d1ldnd2 4.100.1.1.10 (163-330) Lactate dehydrogenase {(Bacillus stearothermophilus)}
tildtarfrfllgeyfsvapqnvhayiigehgdtelpvwsqayigvmpirklveskgeea
qkdlerifvnvrdaayqiiekkgatyygiamglarvtrailhnenailtvsayldglyge
rdvyigvpavinrngirevieielnddeknrfhhsaatlksvlaraft
>d1ldne1 3.22.1.5.10 (15-162) Lactate dehydrogenase {(Bacillus stearothermophilus)}
mknnggarvvvigagfvgasyvfalmnqgiadeivlidaneskaigdamdfnhgkvfapk
pvdiwhgdyddcrdadlvvicaganqkpgetrldlvdkniaifrsivesvmasgfqglfl
vatnpvdiltyatwkfsglphervigsg
>d1ldne2 4.100.1.1.10 (163-330) Lactate dehydrogenase {(Bacillus stearothermophilus)}
tildtarfrfllgeyfsvapqnvhayiigehgdtelpvwsqayigvmpirklveskgeea
qkdlerifvnvrdaayqiiekkgatyygiamglarvtrailhnenailtvsayldglyge
rdvyigvpavinrngirevieielnddeknrfhhsaatlksvlaraft
>d1ldnf1 3.22.1.5.10 (15-162) Lactate dehydrogenase {(Bacillus stearothermophilus)}
mknnggarvvvigagfvgasyvfalmnqgiadeivlidaneskaigdamdfnhgkvfapk
pvdiwhgdyddcrdadlvvicaganqkpgetrldlvdkniaifrsivesvmasgfqglfl
vatnpvdiltyatwkfsglphervigsg
>d1ldnf2 4.100.1.1.10 (163-330) Lactate dehydrogenase {(Bacillus stearothermophilus)}
tildtarfrfllgeyfsvapqnvhayiigehgdtelpvwsqayigvmpirklveskgeea
qkdlerifvnvrdaayqiiekkgatyygiamglarvtrailhnenailtvsayldglyge
rdvyigvpavinrngirevieielnddeknrfhhsaatlksvlaraft
>d1ldng1 3.22.1.5.10 (15-162) Lactate dehydrogenase {(Bacillus stearothermophilus)}
mknnggarvvvigagfvgasyvfalmnqgiadeivlidaneskaigdamdfnhgkvfapk
pvdiwhgdyddcrdadlvvicaganqkpgetrldlvdkniaifrsivesvmasgfqglfl
vatnpvdiltyatwkfsglphervigsg
>d1ldng2 4.100.1.1.10 (163-330) Lactate dehydrogenase {(Bacillus stearothermophilus)}
tildtarfrfllgeyfsvapqnvhayiigehgdtelpvwsqayigvmpirklveskgeea
qkdlerifvnvrdaayqiiekkgatyygiamglarvtrailhnenailtvsayldglyge
rdvyigvpavinrngirevieielnddeknrfhhsaatlksvlaraft
>d1ldnh1 3.22.1.5.10 (15-162) Lactate dehydrogenase {(Bacillus stearothermophilus)}
mknnggarvvvigagfvgasyvfalmnqgiadeivlidaneskaigdamdfnhgkvfapk
pvdiwhgdyddcrdadlvvicaganqkpgetrldlvdkniaifrsivesvmasgfqglfl
vatnpvdiltyatwkfsglphervigsg
>d1ldnh2 4.100.1.1.10 (163-330) Lactate dehydrogenase {(Bacillus stearothermophilus)}
tildtarfrfllgeyfsvapqnvhayiigehgdtelpvwsqayigvmpirklveskgeea
qkdlerifvnvrdaayqiiekkgatyygiamglarvtrailhnenailtvsayldglyge
rdvyigvpavinrngirevieielnddeknrfhhsaatlksvlaraft
>d1ldph1 2.1.1.2.14 (182-272) Class I MHC, beta2-microglobulin and alpha-3 domain {mouse (Mus musculus) H-2LD}
tdspkahvthhprskgevtlrcwalgfypaditltwqlngeeltqdmelvetrpagdgtf
qkwasvvvplgkeqnytcrvyheglpepltl
>d1ldph2 4.15.1.1.18 (1-181) MHC class I, alpha-1 and alpha-2 domains {mouse (Mus musculus) H-2LD}
gphsmryfetavsrpglgepryisvgyvdnkefvrfdsdaenpryepqapwmeqegpeyw
eritqiakgqeqwfrvnlrtllgyynqsaggthtlqwmygcdvgsdgrllrgyeqfaydg
cdyialnedlktwtaadmaaqitrrkweqagaaeyyraylegecvewlhrylkngnatll
r
>d1ldr__ 7.11.1.1.1 Ligand-binding domain of low-density lipoprotein receptor {human (Homo sapiens)}
lsvtcksgdfscggrvnrcipqfwrcdgqvdcdngsdeqgc
>d1ldtl_ 7.14.1.1.10 leech derived tryptase inhibitor (LDTI-C) {Medicinal leech (Hirudo medicinalis)}
kkvcacpkilkpvcgsdgrtyansciarcngvsiksegscptgiln
>d1ldtt_ 2.35.1.2.2 Trypsin(ogen) {porcine (Sus scrofa)}
ivggytcaansipyqvslnsgshfcggslinsqwvvsaahcyksriqvrlgehnidvleg
neqfinaakiithpnfngntldndimliklsspatlnsrvatvslprscaaagteclisg
wgntkssgssypsllqclkapvlsdssckssypgqitgnmicvgfleggkdscqgdsggp
vvcngqlqgivswgygcaqknkpgvytkvcnyvnwiqqtiaan
>d1ldya1 2.25.1.2.1 (1-174,325-374) Alcohol dehydrogenase {horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1ldya2 3.22.1.1.1 (175-324) Alcohol dehydrogenase {horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1ldyb1 2.25.1.2.1 (1-174,325-374) Alcohol dehydrogenase {horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1ldyb2 3.22.1.1.1 (175-324) Alcohol dehydrogenase {horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1ldyc1 2.25.1.2.1 (1-174,325-374) Alcohol dehydrogenase {horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1ldyc2 3.22.1.1.1 (175-324) Alcohol dehydrogenase {horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1ldyd1 2.25.1.2.1 (1-174,325-374) Alcohol dehydrogenase {horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1ldyd2 3.22.1.1.1 (175-324) Alcohol dehydrogenase {horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1le2__ 1.24.1.1.2 Apolipoprotein E2 {human (Homo sapiens)}
gqrwelalgrfwdylrwvqtlseqvqeellssqvtqelralmdetmkelkaykseleeql
tpvaeetrarlskelqaaqarlgadmedvcgrlvqyrgevqamlgqsteelrvrlashlr
klrkrllrdaddlqkclavyqaga
>d1le4__ 1.24.1.1.3 Apolipoprotein E4 {human (Homo sapiens)}
qrwelalgrfwdylrwvqtlseqvqeellssqvtqelralmdetmkelkaykseleeqlt
pvaeetrarlskelqaaqarlgadmedvrgrlvqyrgevqamlgqsteelrvrlashlrk
lrkrllrdaddlqkrlavy
>d1lea__ 1.4.3.2.1 LexA repressor, N-terminal DNA-binding domain {(Escherichia coli)}
mkaltarqqevfdlirdhisqtgmpptraeiaqrlgfrspnaaeehlkalarkgvieivs
gasrgirllqee
>d1leb__ 1.4.3.2.1 LexA repressor, N-terminal DNA-binding domain {(Escherichia coli)}
mkaltarqqevfdlirdhisqtgmpptraeiaqrlgfrspnaaeehlkalarkgvieivs
gasrgirllqee
>d1lec__ 2.21.1.1.5 Lectin {the west-central african legume (Griffonia simplicifolia)}
xntvnftypdfwsyslkngteitflgdatripgalqltktdangnpvrssagqasysepv
flwdstgkaasfytsftfllknygaptadglafflapvdssvkdyggflglfrhetaadp
sknqvvavefdtwinkdwndppyphigidvnsivsvattrwenddaygssiatahityda
rskiltvllsyehgrdyilshvvdlakvlpqkvrigfsagvgydevtyilswhffstldg
tnk
>d1led__ 2.21.1.1.5 Lectin {the west-central african legume (Griffonia simplicifolia)}
xntvnftypdfwsyslkngteitflgdatripgalqltktdangnpvrssagqasysepv
flwdstgkaasfytsftfllknygaptadglafflapvdssvkdyggflglfrhetaadp
sknqvvavefdtwinkdwndppyphigidvnsivsvattrwenddaygssiatahityda
rskiltvllsyehgrdyilshvvdlakvlpqkvrigfsagvgydevtyilswhffstldg
tnk
>d1lefa_ 1.21.1.1.6 Lymphoid enhancer-binding factor, LEF1 {mouse (Mus musculus)}
mhikkplnafmlymkemranvvaestlkesaainqilgrrwhalsreeqakyyelarker
qlhmqlypgwsardnygkkkkrkrek
>d1leha1 3.22.1.7.3 (135-364) Leucine dehydrogenase, C-terminal domain {(Bacillus sphaericus)}
gispafgssgnpspvtaygvyrgmkaaakeafgsdsleglavsvqglgnvakalckklnt
egaklvvtdvnkaavsaavaeegadavapnaiygvtcdifapcalgavlndftipqlkak
viagsadnqlkdprhgkylhelgivyapdyvinaggvinvadelygynrtramkrvdgiy
dsiekifaiskrdgvpsyvaadrmaeeriakvakarsqflqdqrnilngr
>d1leha2 3.61.1.1.3 (1-134) Leucine dehydrogenase, N-terminal domain {(Bacillus sphaericus)}
meifkymekydyeqlvfcqdeasglkaviaihdttlgpalggarmwtynaeeeaiedalr
largmtyknaaaglnlgggktviigdpfadknedmfralgrfiqglngryitaedvgttv
ddmdlihqetdyvt
>d1lehb1 3.22.1.7.3 (135-364) Leucine dehydrogenase, C-terminal domain {(Bacillus sphaericus)}
gispafgssgnpspvtaygvyrgmkaaakeafgsdsleglavsvqglgnvakalckklnt
egaklvvtdvnkaavsaavaeegadavapnaiygvtcdifapcalgavlndftipqlkak
viagsadnqlkdprhgkylhelgivyapdyvinaggvinvadelygynrtramkrvdgiy
dsiekifaiskrdgvpsyvaadrmaeeriakvakarsqflqdqrnilngr
>d1lehb2 3.61.1.1.3 (1-134) Leucine dehydrogenase, N-terminal domain {(Bacillus sphaericus)}
meifkymekydyeqlvfcqdeasglkaviaihdttlgpalggarmwtynaeeeaiedalr
largmtyknaaaglnlgggktviigdpfadknedmfralgrfiqglngryitaedvgttv
ddmdlihqetdyvt
>d1lema_ 2.21.1.1.4 Lectin {common lentil (Lens culinaris)}
tettsfsitkfspdqqnlifqgdgyttkgkltltkavkstvgralystpihiwdrdtgnv
anfvtsftfvidapssynvadgftffiapvdtkpqtgggylgvfnskeydktsqtvavef
dtfynaawdpsnkerhigidvnsiksvntkswnlqngeranvviafnaatnvltvtltyp
n
>d1lemb_ 2.21.1.1.4 Lectin {common lentil (Lens culinaris)}
vtsytlnevvplkdvvpewvrigfsattgaefaaqevhswsfnsqlg
>e1len.1a 2.21.1.1.4 Lectin {common lentil (Lens culinaris)}
tettsfsitkfspdqqnlifqgdgyttkgkltltkavkstvgralystpihiwdrdtgnv
anfvtsftfvidapssynvadgftffiapvdtkpqtgggylgvfnskeydktsqtvavef
dtfynaawdpsnkerhigidvnsiksvntkswnlqngeranvviafnaatnvltvtltyp
n
>e1len.1b 2.21.1.1.4 Lectin {common lentil (Lens culinaris)}
vtsytlnevvplkdvvpewvrigfsattgaefaaqevhswsfnsqlg
>e1len.2c 2.21.1.1.4 Lectin {common lentil (Lens culinaris)}
tettsfsitkfspdqqnlifqgdgyttkgkltltkavkstvgralystpihiwdrdtgnv
anfvtsftfvidapssynvadgftffiapvdtkpqtgggylgvfnskeydktsqtvavef
dtfynaawdpsnkerhigidvnsiksvntkswnlqngeranvviafnaatnvltvtltyp
n
>e1len.2d 2.21.1.1.4 Lectin {common lentil (Lens culinaris)}
vtsytlnevvplkdvvpewvrigfsattgaefaaqevhswsfnsqlg
>d1leo__ 4.34.6.1.2 Nucleoside diphosphate kinases {(Dictyostelium discodeum)}
vnkertflavkpdgvarglvgeiiaryekkgfvlvglkqlvptkdlaeshyaehkerpff
gglvsfitsgpvvamvfegkgvvasarlmigvtnslasapgsirgdfgvdvgrniihgsd
svesanreialwfkpeelltevkpnpnlye
>d1lepa_ 2.25.1.1.2 Chaperonin-10 (GroES) {(Mycobacterium leprae)}
akvkikpledkilvqageaetmtpsglvipenakekpqegtvvavgpgrwdedgakripv
dvsegdiviyskyggteikyngeeylilsardvlavvsk
>d1lepb_ 2.25.1.1.2 Chaperonin-10 (GroES) {(Mycobacterium leprae)}
akvkikpledkilvqageaetmtpsglvipenakekpqegtvvavgpgrwdedgakripv
dvsegdiviyskyggteikyngeeylilsardvlavvsk
>d1lepc_ 2.25.1.1.2 Chaperonin-10 (GroES) {(Mycobacterium leprae)}
akvkikpledkilvqageaetmtpsglvipenakekpqegtvvavgpgrwdedgakripv
dvsegdiviyskyggteikyngeeylilsardvlavvsk
>d1lepd_ 2.25.1.1.2 Chaperonin-10 (GroES) {(Mycobacterium leprae)}
akvkikpledkilvqageaetmtpsglvipenakekpqegtvvavgpgrwdedgakripv
dvsegdiviyskyggteikyngeeylilsardvlavvsk
>d1lepe_ 2.25.1.1.2 Chaperonin-10 (GroES) {(Mycobacterium leprae)}
akvkikpledkilvqageaetmtpsglvipenakekpqegtvvavgpgrwdedgakripv
dvsegdiviyskyggteikyngeeylilsardvlavvsk
>d1lepf_ 2.25.1.1.2 Chaperonin-10 (GroES) {(Mycobacterium leprae)}
akvkikpledkilvqageaetmtpsglvipenakekpqegtvvavgpgrwdedgakripv
dvsegdiviyskyggteikyngeeylilsardvlavvsk
>d1lepg_ 2.25.1.1.2 Chaperonin-10 (GroES) {(Mycobacterium leprae)}
akvkikpledkilvqageaetmtpsglvipenakekpqegtvvavgpgrwdedgakripv
dvsegdiviyskyggteikyngeeylilsardvlavvsk
>d1lesa_ 2.21.1.1.4 Lectin {common lentil (Lens culinaris)}
tettsfsitkfspdqqnlifqgdgyttkgkltltkavkstvgralystpihiwdrdtgnv
anfvtsftfvidapssynvadgftffiapvdtkpqtgggylgvfnskeydktsqtvavef
dtfynaawdpsnkerhigidvnsiksvntkswnlqngeranvviafnaatnvltvtltyp
n
>d1lesb_ 2.21.1.1.4 Lectin {common lentil (Lens culinaris)}
vtsytlnevvplkdvvpewvrigfsattgaefaahevhswsfhsqlg
>d1lesc_ 2.21.1.1.4 Lectin {common lentil (Lens culinaris)}
tettsfsitkfspdqqnlifqgdgyttkgkltltkavkstvgralystpihiwdrdtgnv
anfvtsftfvidapssynvadgftffiapvdtkpqtgggylgvfnskeydktsqtvavef
dtfynaawdpsnkerhigidvnsiksvntkswnlqngeranvviafnaatnvltvtltyp
n
>d1lesd_ 2.21.1.1.4 Lectin {common lentil (Lens culinaris)}
vtsytlnevvplkdvvpewvrigfsattgaefaahevhswsfhsqlg
>d1lfaa_ 3.50.1.1.1 Integrin CD11a/CD18 (LFA-1) {Human (Homo sapiens)}
gnvdlvflfdgsmslqpdefqkildfmkdvmkklsntsyqfaavqfstsyktefdfsdyv
krkdpdallkhvkhmllltntfgainyvatevfreelgarpdatkvliiitdgeatdsgn
idaakdiiryiigigkhfqtkesqetlhkfaskpasefvkildtfeklkdlftelqkkiy
vie
>d1lfab_ 3.50.1.1.1 Integrin CD11a/CD18 (LFA-1) {Human (Homo sapiens)}
gnvdlvflfdgsmslqpdefqkildfmkdvmkklsntsyqfaavqfstsyktefdfsdyv
krkdpdallkhvkhmllltntfgainyvatevfreelgarpdatkvliiitdgeatdsgn
idaakdiiryiigigkhfqtkesqetlhkfaskpasefvkildtfeklkdlftelqkkiy
vi
>d1lfb__ 1.4.1.1.4 Transcription factor LFB1 {rat (Rattus rattus)}
rfkwgpasqqilfqayerqknpskeeretlveecnraeciqrgvspsqaqglgsnlvtev
rvynwfanrrkeeafrhk
>d1lfg_1 3.82.1.2.6 (1-334) Transferrin {human (Homo sapiens)}
grrrsvqwcavsnpeatkcfqwqrnmrkvrgppvscikrdspiqciqaiaenradavtld
ggfiyeaglapyklrpvaaevygterqprthyyavavvkkggsfqlnelqglkschtglr
rtagwnvpigtlrpflnwtgppepieaavarffsascvpgadkgqfpnlcrlcagtgenk
cafssqepyfsysgafkclkdgagdvafirestvfedlsdeaerdeyellcpdntrkpvd
kfkdchlarvpshavvarsvngkedaiwnllrqaqekfgkdkspkfqlfgspsgqkdllf
kdsaigfsrvppridsglylgsgyftaiqnlrks
>d1lfg_2 3.82.1.2.6 (335-691) Transferrin {human (Homo sapiens)}
eeevaarrarvvwcavgeqelrkcnqwsglsegsvtcssasttedcialvlkgeadamsl
dggyvytagkcglvpvlaenyksaqssdpdpncvdrpvegylavavvrrsdtsltwnsvk
gkkschtavdrtagwnipmgllfnqtgsckfdeyfsqscapgsdpasnlcalcigdeege
nkcvpnsneryygytgafrclaenagdvafvkdvtvlqntdgnnneawakdlkladfall
cldgkrkpvtearschlamapnhavvsrmdkverlkqvllhqqakfgrngsdcpdkfclf
qsetknllfndnteclarlhgkttyekylgpqyvagitnlkkcstsplleaceflrk
>d1lfh_1 3.82.1.2.1 (1-334) Lactoferrin {human (Homo sapiens)}
grrrsvqwcavsnpeatkcfqwqrnmrkvrgppvscikrdspiqciqaiaenradavtld
ggfiyeaglapyklrpvaaevygterqprthyyavavvkkggsfqlnelqglkschtglr
rtagwnvpigtlrpflnwtgppepieaavarffsascvpgadkgqfpnlcrlcagtgenk
cafssqepyfsysgafkclkdgagdvafirestvfedlsdeaerdeyellcpdntrkpvd
kfkdchlarvpshavvarsvngkedaiwnllrqaqekfgkdkspkfqlfgspsgqkdllf
kdsaigfsrvppridsglylgsgyftaiqnlrks
>d1lfh_2 3.82.1.2.1 (335-691) Lactoferrin {human (Homo sapiens)}
eeevaarrarvvwcavgeqelrkcnqwsglsegsvtcssasttedcialvlkgeadamsl
dggyvytagkcglvpvlaenyksqqssdpdpncvdrpvegylavavvrrsdtsltwnsvk
gkkschtavdrtagwnipmgllfnqtgsckfdeyfsqscapgsdprsnlcalcigdeege
nkcvpnsneryygytgafrclaenagdvafvkdvtvlqntdgnnneawakdlkladfall
cldgkrkpvtearschlamapnhavvsrmdkverlkqvllhqqakfgrngsdcpdkfclf
qsetknllfndnteclarlhgkttyekylgpqyvagitnlkkcstsplleaceflrk
>d1lfi_1 3.82.1.2.1 (1-334) Lactoferrin {human (Homo sapiens)}
grrrsvqwcavsnpeatkcfqwqrnmrkvrgppvscikrdspiqciqaiaenradavtld
ggfiyeaglapyklrpvaaevygterqprthyyavavvkkggsfqlnelqglkschtglr
rtagwnvpigtlrpflnwtgppepieaavarffsascvpgadkgqfpnlcrlcagtgenk
cafssqepyfsysgafkclrdgagdvafirestvfedlsdeaerdeyellcpdntrkpvd
kfkdchlarvpshavvarsvngkedaiwnllrqaqekfgkdkspkfqlfgspsgqkdllf
kdsaigfsrvppridsglylgsgyftaiqnlrks
>d1lfi_2 3.82.1.2.1 (335-691) Lactoferrin {human (Homo sapiens)}
eeevaarrarvvwcavgeqelrkcnqwsglsegsvtcssasttedcialvlkgeadamsl
dggyvytagkcglvpvlaenyksqqssdpdpncvdrpvegylavavvrrsdtsltwnsvk
gkkschtavdrtagwnipmgllfnqtgsckfdeyfsqscapgsdprsnlcalcigdeege
nkcvpnsneryygytgafrclaenagdvafvkdvtvlqntdgnnneawakdlkladfall
cldgkrkpvtearschlamapnhavvsrmdkverlkqvllhqqakfgrngsdcpdkfclf
qsetknllfndnteclarlhgkttyekylgpqyvagitnlkkcstsplleaceflrk
>d1lfo__ 2.45.1.2.9 Liver fatty acid binding protein {rat (Rattus norvegicus)}
mnfsgkyqvqsqenfepfmkamglpedliqkgkdikgvseivhegkkvkltitygskvih
neftlgeexeletmtgekvkavvkmegdnkmvttfkgiksvtefngdtitntmtlgdivy
krvskri
>d1lgaa_ 1.72.1.1.1 Lignin peroxidase {white rot basidiomycete (Phanerochaete chrysosporium)}
atcangktvgdasccawfdvlddiqanmfhggqcgaeahesirlvfhdsiaispameakg
kfggggadgsimifdtietafhpnigldevvamqkpfvqkhgvtpgdfiafagavalsnc
pgapqmnfftgrkpatqpapdglvpepfhtvdqiiarvndagefdelelvwmlsahsvaa
vndvdptvqglpfdstpgifdsqffvetqfrgtlfpgsggnqgevesgmageiriqtdht
lardsrtacewqsfvgnqsklvddfqfiflaltqlgqdpnamtdcsdviplskpipgngp
fsffppgkshsdieqacaetpfpslvtlpgpatsvaripphka
>d1lgab_ 1.72.1.1.1 Lignin peroxidase {white rot basidiomycete (Phanerochaete chrysosporium)}
atcangktvgdasccawfdvlddiqanmfhggqcgaeahesirlvfhdsiaispameakg
kfggggadgsimifdtietafhpnigldevvamqkpfvqkhgvtpgdfiafagavalsnc
pgapqmnfftgrkpatqpapdglvpepfhtvdqiiarvndagefdelelvwmlsahsvaa
vndvdptvqglpfdstpgifdsqffvetqfrgtlfpgsggnqgevesgmageiriqtdht
lardsrtacewqsfvgnqsklvddfqfiflaltqlgqdpnamtdcsdviplskpipgngp
fsffppgkshsdieqacaetpfpslvtlpgpatsvaripph
>e1lgb.1a 2.21.1.1.9 Lectin {Isolectin II from (Lathyrus ochrus)}
tettsfsitkfgpdqpnlifqgdgyttkerltltkavrntvgralysspihiwdsktgnv
anfvtsftfvidapnsynvadgftffiapvdtkpqtgggylgvfnskdydktsqtvavef
dtfyntawdpsngdrhigidvnsiksintkswalqngkeanvviafngatnvltvsltyp
n
>e1lgb.1b 2.21.1.1.9 Lectin {Isolectin II from (Lathyrus ochrus)}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfnselav
>d1lgbc_ 3.82.1.2.1 Lactoferrin {human (Homo sapiens)}
hyyavavvkkggsfqlnelqglkschtglrrtagwnvpigtlrpflnwtgppepieaava
rffsascvpgadkgqfpnlcrlcagtgenkcafssqepyfsysgafkclkdgagdvafir
estvfedlsdeaerdeyellcpdntrkpvdkfkdchlar
>e1lgc.1a 2.21.1.1.9 Lectin {Isolectin II from (Lathyrus ochrus)}
tettsfsitkfgpdqpnlifqgdgyttkerltltkavrntvgralysspihiwdsktgnv
anfvtsftfvidapnsynvadgftffiapvdtkpqtgggylgvfnskdydktsqtvavef
dtfyntawdpsngdrhigidvnsiksintkswklqngkeanvviafngatnvltvsltyp
n
>e1lgc.1b 2.21.1.1.9 Lectin {Isolectin II from (Lathyrus ochrus)}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfnselsvtss
>e1lgc.2c 2.21.1.1.9 Lectin {Isolectin II from (Lathyrus ochrus)}
tettsfsitkfgpdqpnlifqgdgyttkerltltkavrntvgralysspihiwdsktgnv
anfvtsftfvidapnsynvadgftffiapvdtkpqtgggylgvfnskdydktsqtvavef
dtfyntawdpsngdrhigidvnsiksintkswklqngkeanvviafngatnvltvsltyp
n
>e1lgc.2d 2.21.1.1.9 Lectin {Isolectin II from (Lathyrus ochrus)}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfnselsv
>e1lgc.3e 2.21.1.1.9 Lectin {Isolectin II from (Lathyrus ochrus)}
tettsfsitkfgpdqpnlifqgdgyttkerltltkavrntvgralysspihiwdsktgnv
anfvtsftfvidapnsynvadgftffiapvdtkpqtgggylgvfnskdydktsqtvavef
dtfyntawdpsngdrhigidvnsiksintkswklqngkeanvviafngatnvltvsltyp
n
>e1lgc.3f 2.21.1.1.9 Lectin {Isolectin II from (Lathyrus ochrus)}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfnselsv
>d1lgha_ 6.6.1.1.2 Light-harvesting complex LH2 {(Rhodospirillum molischianum)}
snpkddykiwlvinpstwlpviwivatvvaiavhaavlaapgfnwialgaaksaak
>d1lghb_ 6.6.1.1.2 Light-harvesting complex LH2 {(Rhodospirillum molischianum)}
rslsglteeeaiavhdqfkttfsafiilaavahvlvwvwkpwf
>d1lghd_ 6.6.1.1.2 Light-harvesting complex LH2 {(Rhodospirillum molischianum)}
snpkddykiwlvinpstwlpviwivatvvaiavhaavlaapgfnwialgaaksaak
>d1lghe_ 6.6.1.1.2 Light-harvesting complex LH2 {(Rhodospirillum molischianum)}
rslsglteeeaiavhdqfkttfsafiilaavahvlvwvwkpwf
>d1lghg_ 6.6.1.1.2 Light-harvesting complex LH2 {(Rhodospirillum molischianum)}
snpkddykiwlvinpstwlpviwivatvvaiavhaavlaapgfnwialgaaksaak
>d1lghh_ 6.6.1.1.2 Light-harvesting complex LH2 {(Rhodospirillum molischianum)}
rslsglteeeaiavhdqfkttfsafiilaavahvlvwvwkpwf
>d1lghj_ 6.6.1.1.2 Light-harvesting complex LH2 {(Rhodospirillum molischianum)}
snpkddykiwlvinpstwlpviwivatvvaiavhaavlaapgfnwialgaaksaak
>d1lghk_ 6.6.1.1.2 Light-harvesting complex LH2 {(Rhodospirillum molischianum)}
rslsglteeeaiavhdqfkttfsafiilaavahvlvwvwkpwf
>d1lgna_ 2.21.1.4.1 Serum amyloid P component (SAP) {human (Homo sapiens)}
htdlsgkvfvfpresvtdhvnlitplekplqnftlcfraysdlsrayslfsyntqgrdne
llvykervgeyslyigrhkvtskviekfpapvhicvswesssgiaefwingtplvkkglr
qgyfveaqpkivlgqeqdsyggkfdrsqsfvgeigdlymwdsvlppenilsayqgtplpa
nildwqalnyeirgyviikplvwv
>d1lgnb_ 2.21.1.4.1 Serum amyloid P component (SAP) {human (Homo sapiens)}
htdlsgkvfvfpresvtdhvnlitplekplqnftlcfraysdlsrayslfsyntqgrdne
llvykervgeyslyigrhkvtskviekfpapvhicvswesssgiaefwingtplvkkglr
qgyfveaqpkivlgqeqdsyggkfdrsqsfvgeigdlymwdsvlppenilsayqgtplpa
nildwqalnyeirgyviikplvwv
>d1lgnc_ 2.21.1.4.1 Serum amyloid P component (SAP) {human (Homo sapiens)}
htdlsgkvfvfpresvtdhvnlitplekplqnftlcfraysdlsrayslfsyntqgrdne
llvykervgeyslyigrhkvtskviekfpapvhicvswesssgiaefwingtplvkkglr
qgyfveaqpkivlgqeqdsyggkfdrsqsfvgeigdlymwdsvlppenilsayqgtplpa
nildwqalnyeirgyviikplvwv
>d1lgnd_ 2.21.1.4.1 Serum amyloid P component (SAP) {human (Homo sapiens)}
htdlsgkvfvfpresvtdhvnlitplekplqnftlcfraysdlsrayslfsyntqgrdne
llvykervgeyslyigrhkvtskviekfpapvhicvswesssgiaefwingtplvkkglr
qgyfveaqpkivlgqeqdsyggkfdrsqsfvgeigdlymwdsvlppenilsayqgtplpa
nildwqalnyeirgyviikplvwv
>d1lgne_ 2.21.1.4.1 Serum amyloid P component (SAP) {human (Homo sapiens)}
htdlsgkvfvfpresvtdhvnlitplekplqnftlcfraysdlsrayslfsyntqgrdne
llvykervgeyslyigrhkvtskviekfpapvhicvswesssgiaefwingtplvkkglr
qgyfveaqpkivlgqeqdsyggkfdrsqsfvgeigdlymwdsvlppenilsayqgtplpa
nildwqalnyeirgyviikplvwv
>d1lgr_1 4.11.8.1.1 (1-100) Glutamine synthetase, N-terminal domain {(Salmonella typhimurium)}
saehvltmlnehevkfvdlrftdtkgkeqhvtipahqvnaeffeegkmfdgssiggwkgi
nesdmvlmpdastavidpffadstliircdilepgtlqgy
>d1lgr_2 4.78.1.1.1 (101-468) Glutamine synthetase, C-terminal domain {(Salmonella typhimurium)}
drdprsiakraedylratgiadtvlfgpepefflfddirfgasisgshvaiddiegawns
stkyeggnkghrpgvkggyfpvppvdsaqdirsemclvmeqmglvveahhhevatagqne
vatrfntmtkkadeiqiykyvvhnvahrfgktatfmpkpmfgdngsgmhchmslakngtn
lfsgdkyaglseqalyyiggvikhakainalanpttnsykrlvpgyeapvmlaysarnrs
asiripvvaspkarrievrfpdpaanpylcfaallmagldgiknkihpgepmdknlydlp
peeakeipqvagsleealnaldldreflkaggvftdeaidayialrreeddrvrmtphpv
efelyysv
>d1lgya_ 3.56.1.9.5 Triacylglycerol lipase {(Rhizopus niveus)}
kvvaattaqiqeftkyagiaataycrsvvpgnkwdcvqcqkwvpdgkiittftsllsdtn
gyvlrsdkqktiylvfrgtnsfrsaitdivfnfsdykpvkgakvhagflssyeqvvndyf
pvvqeqltahptykvivtghslggaqallagmdlyqreprlspknlsiftvggprvgnpt
fayyvestgipfqrtvhkrdivphvppqsfgflhpgveswiksgtsnvqictseietkdc
snsivpftsildhlsyfdinegscl
>d1lgyb_ 3.56.1.9.5 Triacylglycerol lipase {(Rhizopus niveus)}
kvvaattaqiqeftkyagiaataycrsvvpgnkwdcvqcqkwvpdgkiittftsllsdtn
gyvlrsdkqktiylvfrgtnsfrsaitdivfnfsdykpvkgakvhagflssyeqvvndyf
pvvqeqltahptykvivtghslggaqallagmdlyqreprlspknlsiftvggprvgnpt
fayyvestgipfqrtvhkrdivphvppqsfgflhpgveswiksgtsnvqictseietkdc
snsivpftsildhlsyfdinegscl
>d1lgyc_ 3.56.1.9.5 Triacylglycerol lipase {(Rhizopus niveus)}
kvvaattaqiqeftkyagiaataycrsvvpgnkwdcvqcqkwvpdgkiittftsllsdtn
gyvlrsdkqktiylvfrgtnsfrsaitdivfnfsdykpvkgakvhagflssyeqvvndyf
pvvqeqltahptykvivtghslggaqallagmdlyqreprlspknlsiftvggprvgnpt
fayyvestgipfqrtvhkrdivphvppqsfgflhpgveswiksgtsnvqictseietkdc
snsivpftsildhlsyfdinegscl
>d1lh1__ 1.1.1.1.14 Leghemoglobin {yellow lupin (Lupinus luteus l)}
galtesqaalvkssweefnanipkhthrffilvleiapaakdlfsflkgtsevpqnnpel
qahagkvfklvyeaaiqlevtgvvvtdatlknlgsvhvskgvadahfpvvkeailktike
vvgakwseelnsawtiaydelaivikkemddaa
>d1lh2__ 1.1.1.1.14 Leghemoglobin {yellow lupin (Lupinus luteus l)}
galtesqaalvkssweefnanipkhthrffilvleiapaakdlfsflkgtsevpqnnpel
qahagkvfklvyeaaiqlevtgvvvtdatlknlgsvhvskgvadahfpvvkeailktike
vvgakwseelnsawtiaydelaivikkemddaa
>d1lh3__ 1.1.1.1.14 Leghemoglobin {yellow lupin (Lupinus luteus l)}
galtesqaalvkssweefnanipkhthrffilvleiapaakdlfsflkgtsevpqnnpel
qahagkvfklvyeaaiqlevtgvvvtdatlknlgsvhvskgvadahfpvvkeailktike
vvgakwseelnsawtiaydelaivikkemddaa
>d1lh5__ 1.1.1.1.14 Leghemoglobin {yellow lupin (Lupinus luteus l)}
galtesqaalvkssweefnanipkhthrffilvleiapaakdlfsflkgtsevpqnnpel
qahagkvfklvyeaaiqlevtgvvvtdatlknlgsvhvskgvadahfpvvkeailktike
vvgakwseelnsawtiaydelaivikkemddaa
>d1lh6__ 1.1.1.1.14 Leghemoglobin {yellow lupin (Lupinus luteus l)}
galtesqaalvkssweefnanipkhthrffilvleiapaakdlfsflkgtsevpqnnpel
qahagkvfklvyeaaiqlevtgvvvtdatlknlgsvhvskgvadahfpvvkeailktike
vvgakwseelnsawtiaydelaivikkemddaa
>d1lh7__ 1.1.1.1.14 Leghemoglobin {yellow lupin (Lupinus luteus l)}
galtesqaalvkssweefnanipkhthrffilvleiapaakdlfsflkgtsevpqnnpel
qahagkvfklvyeaaiqlevtgvvvtdatlknlgsvhvskgvadahfpvvkeailktike
vvgakwseelnsawtiaydelaivikkemddaa
>e1lhc.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqf
>e1lhc.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1lhd.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqf
>e1lhd.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1lhe.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqf
>e1lhe.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1lhf.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqf
>e1lhf.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1lhg.1h 2.35.1.2.10 Thrombin {human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqf
>e1lhg.1l 2.35.1.2.10 Thrombin {human (Homo sapiens)}
adcglrplfekksledkterellesy
>d1lhh__ 4.2.1.2.8 Lysozyme {human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawpawrnrcqnrd
vrqyvqgcgv
>d1lhi__ 4.2.1.2.8 Lysozyme {human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktggavnachlscsallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1lhj__ 4.2.1.2.8 Lysozyme {human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdgqgirawvawrnrcqnrd
vrqyvqgcgv
>d1lhk__ 4.2.1.2.8 Lysozyme {human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniapavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1lhl__ 4.2.1.2.8 Lysozyme {human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynpgdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1lhm__ 4.2.1.2.8 Lysozyme {human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnaahlscsallqdniadavaaakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1lhs__ 1.1.1.1.11 Myoglobin {Loggerhead sea turtle (Caretta caretta)}
glsddewnhvlgiwakvepdlsahgqeviirlfqlhpetqerfakfknlttidalkssee
vkkhgttvltalgrilkqknnheqelkplaeshatkhkipvkyleficeiivkviaekhp
sdfgadsqaamkkalelfrndmaskykefgfqg
>d1lht__ 1.1.1.1.11 Myoglobin {Loggerhead sea turtle (Caretta caretta)}
glsddewnhvlgiwakvepdlsahgqeviirlfqlhpetqerfakfknlttidalkssee
vkkhgttvltalgrilkqknnheqelkplaeshatkhkipvkyleficeiivkviaekhp
sdfgadsqaamkkalelfrndmaskykefgfqg
>d1liaa_ 1.1.1.2.4 R-phycoerythrin {red algae (Polysiphonia urceolata)}
mksvitttisaadaagrypstsdlqsvqgniqraaarleaaeklgsnheavvkeagdacf
skygynknpgeagenqekinkcyrdidhymrlinytlvvggtgpldewgiagarevyrtl
nlpsaayiaafvftrdrlciprdmsaqagvefctaldylinsls
>d1liab_ 1.1.1.2.4 R-phycoerythrin {red algae (Polysiphonia urceolata)}
mldafsrvvvnsdskaayvsgsdlqalktfindgnkrldavnyivsnsscivsdaisgmi
cenpglitpggncytnrrmaaclrdgeiilryvsyallagdasvledrclnglketyial
gvptnstvravsimkaaavcfisntasqrkveviegdcsalasevasycdrvvaavs
>d1liak_ 1.1.1.2.4 R-phycoerythrin {red algae (Polysiphonia urceolata)}
mksvitttisaadaagrypstsdlqsvqgniqraaarleaaeklgsnheavvkeagdacf
skygynknpgeagenqekinkcyrdidhymrlinytlvvggtgpldewgiagarevyrtl
nlpsaayiaafvftrdrlciprdmsaqagvefctaldylinsls
>d1lial_ 1.1.1.2.4 R-phycoerythrin {red algae (Polysiphonia urceolata)}
mldafsrvvvnsdskaayvsgsdlqalktfindgnkrldavnyivsnsscivsdaisgmi
cenpglitpggncytnrrmaaclrdgeiilryvsyallagdasvledrclnglketyial
gvptnstvravsimkaaavcfisntasqrkveviegdcsalasevasycdrvvaavs
>d1lib__ 2.45.1.2.3 Adipocyte lipid-binding protein, ALBP {mouse (Mus musculus)}
cdafvgtwklvssenfddymkevgvgfatrkvagmakpnmiisvngdlvtirsestfknt
eisfklgvefdeitaddrkvksiitldggalvqvqkwdgksttikrkrdgdklvvecvmk
gvtstrvyera
>d1lic__ 2.45.1.2.3 Adipocyte lipid-binding protein, ALBP {mouse (Mus musculus)}
cdafvgtwklvssenfddymkevgvgfatrkvagmakpnmiisvngdlvtirsestfknt
eisfklgvefdeitaddrkvksiitldggalvqvqkwdgksttikrkrdgdklvvecvmk
gvtstrvyera
>d1lid__ 2.45.1.2.3 Adipocyte lipid-binding protein, ALBP {mouse (Mus musculus)}
cdafvgtwklvssenfddymkevgvgfatrkvagmakpnmiisvngdlvtirsestfknt
eisfklgvefdeitaddrkvksiitldggalvqvqkwdgksttikrkrdgdklvvecvmk
gvtstrvyera
>d1lie__ 2.45.1.2.3 Adipocyte lipid-binding protein, ALBP {mouse (Mus musculus)}
cdafvgtwklvssenfddymkevgvgfatrkvagmakpnmiisvngdlvtirsestfknt
eisfklgvefdeitaddrkvksiitldggalvqvqkwdgksttikrkrdgdklvvecvmk
gvtstrvyera
>d1lif__ 2.45.1.2.3 Adipocyte lipid-binding protein, ALBP {mouse (Mus musculus)}
cdafvgtwklvssenfddymkevgvgfatrkvagmakpnmiisvngdlvtirsestfknt
eisfklgvefdeitaddrkvksiitldggalvqvqkwdgksttikrkrdgdklvvecvmk
gvtstrvyera
>d1lih__ 1.24.2.1.2 Aspartate receptor, ligand-binding domain {(Salmonella typhimurium)}
mggllfsslqhcqqgfvisnelrqqqseltstwdlmlqtrinlsrsaarmmmdasnqqss
aktdllqnakttlaqaaahyanfknmtplpamaeasanvdekyqryqaalaeliqfldng
nmdayfaqptqgmqnalgealgnyarvsenlyrqtfdqsa
>d1lila1 2.1.1.1.115 (2-107) Immunoglobulin (variable domains of L and H chains) {Bence-Jones lambda L chain dimer CLE (human)}
yevtqppslsvspgqtaritcsgeklgdayvcwyqqrpgqspvvviyqdnrrpsgiperf
sgsssgntatltisgtqtldeadyycqvwdsnasvvfgggtkltvlg
>d1lila2 2.1.1.2.103 (108-215) Immunoglobulin (constant domains of L and H chains) {Bence-Jones lambda L chain dimer CLE (human)}
qpkaapsvtlfppsseelqankatlvclisdfypgavtvawkadsspvkagvetttpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1lilb1 2.1.1.1.115 (2-107) Immunoglobulin (variable domains of L and H chains) {Bence-Jones lambda L chain dimer CLE (human)}
yevtqppslsvspgqtaritcsgeklgdayvcwyqqrpgqspvvviyqdnrrpsgiperf
sgsssgntatltisgtqtldeadyycqvwdsnasvvfgggtkltvlg
>d1lilb2 2.1.1.2.103 (108-215) Immunoglobulin (constant domains of L and H chains) {Bence-Jones lambda L chain dimer CLE (human)}
qpkaapsvtlfppsseelqankatlvclisdfypgavtvawkadsspvkagvetttpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1lin__ 1.37.1.5.8 Calmodulin {bovine (Bos taurus)}
qlteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngt
idfpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevd
emireadidgdgqvnyeefvqmmtak
>d1lip__ 1.47.1.1.3 plant non-specific lipid-transfer protein (ns-LTP) {Barley (Hordeum vulgare)}
lncgqvdskmkpcltyvqggpgpsgeccngvrdlhnqaqssgdrqtvcnclkgiargihn
lnlnnaasipskcnvnvpytispdidcsriy
>d1lir__ 7.3.6.2.15 LQ2 toxin {Scorpion (Leiurus quinquestriatus hebraus)}
ftqesctasnqcwsickrlhntnrgkcmnkkcrcys
>d1lis__ 1.18.1.1.1 Lysin {red abalone (Haliotis rufescens)}
hyvepkflnkafevalkvqiiagfdrglvkwlrvhgrtlstvqkkalyfvnrrymqthwa
nymlwinkkidalgrtpvvgdytrlgaeigrridmayfydflkdknmipkylpymeeinr
mrpadvpvkym
>d1lit__ 4.105.1.1.1 Lithostathine, inhibitor of stone formation {human (Homo sapiens)}
cpegtnayrsycyyfnedretwvdadlycqnmnsgnlvsvltqaegafvaslikesgtdd
fnvwiglhdpkknrrwhwssgslvsykswgigapssvnpgycvsltsstgfqkwkdvpce
dkfsfvckfkn
>d1lki__ 1.26.1.1.5 Leukemia inhibitory factor (LIF) {mouse (Mus musculus)}
natcairhpchgnlmnqiknqlaqlngsanalfisyytaqgepfpnnveklcapnmtdfp
sfhgngtektklvelyrmvaylsasltnitrdqkvlnptavslqvklnatidvmrgllsn
vlcrlcnkyrvghvdvppvpdhsdkeafqrkklgcqllgtykqvisvvvqaf
>d1lkka_ 4.53.1.1.1 p56-lck tyrosine kinase {human (Homo sapiens)}
lepepwffknlsrkdaerqllapgnthgsfliresestagsfslsvrdfdqnqgevvkhy
kirnldnggfyispritfpglhelvrhytnasdglctrlsrpcqt
>d1lkla_ 4.53.1.1.1 p56-lck tyrosine kinase {human (Homo sapiens)}
epepwffknlsrkdaerqllapgnthgsfliresestagsfslsvrdfdqnqgevvkhyk
irnldnggfyispritfpglhelvrhytnasdglctrlsrpcqt
>d1lkra_ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1lkrb_ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1lks__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1lkta_ 2.68.1.1.1 Head-binding domain of phage p22 tailspike protein {(Bacteriophage p22)}
anvvvsnprpiftesrsfkavangkiyigqidtdpvnpanqipvyienedgshvqitqpl
iinaagkivyngqlvkivtvqghsmaiydangsqvdyianvlky
>d1lktb_ 2.68.1.1.1 Head-binding domain of phage p22 tailspike protein {(Bacteriophage p22)}
anvvvsnprpiftesrsfkavangkiyigqidtdpvnpanqipvyienedgshvqitqpl
iinaagkivyngqlvkivtvqghsmaiydangsqvdyianvlky
>d1lktc_ 2.68.1.1.1 Head-binding domain of phage p22 tailspike protein {(Bacteriophage p22)}
anvvvsnprpiftesrsfkavangkiyigqidtdpvnpanqipvyienedgshvqitqpl
iinaagkivyngqlvkivtvqghsmaiydangsqvdyianvlky
>d1lktd_ 2.68.1.1.1 Head-binding domain of phage p22 tailspike protein {(Bacteriophage p22)}
anvvvsnprpiftesrsfkavangkiyigqidtdpvnpanqipvyienedgshvqitqpl
iinaagkivyngqlvkivtvqghsmaiydangsqvdyianvlky
>d1lkte_ 2.68.1.1.1 Head-binding domain of phage p22 tailspike protein {(Bacteriophage p22)}
anvvvsnprpiftesrsfkavangkiyigqidtdpvnpanqipvyienedgshvqitqpl
iinaagkivyngqlvkivtvqghsmaiydangsqvdyianvlky
>d1lktf_ 2.68.1.1.1 Head-binding domain of phage p22 tailspike protein {(Bacteriophage p22)}
anvvvsnprpiftesrsfkavangkiyigqidtdpvnpanqipvyienedgshvqitqpl
iinaagkivyngqlvkivtvqghsmaiydangsqvdyianvlky
>d1ll1_1 1.78.1.1.1 (1-379) Hemocyanin, N-terminal and middle domains {(Limulus polyphemus)}
tlhdkqirvchlfeqlssatvirlknvgklqpgaifscfhpdhleearhlyevfweagdf
ndfieiakeartfvneglfafaaevavlhrddckglyvppvqeifpdkfipsaaineafk
kilvdvgnildpeyrlayyredvginahhwhwhlvypstwnpkyfgkkkdrkgelfyymh
qqmcarydcerlsngmhrmlpfnnfdeplagyaphlthvasgkyysprpdglklrdlgdi
eisemvrmrerildsihlgyvisedgshktldelhgtdilgalvessyesvnheyygnlh
nwghvtmarihdpdgrfheepgvmsdtstslrdpifynwhrfidnifheykntlk
>d1ll1_2 2.1.1.5.8 (380-628) Hemocyanin, C-terminal domain {Horseshoe crab(Limulus polyphemus) hemolymph}
pydhdvlnfpdiqvqdvtlharvdnvvhtfmreqelelkhginpgnarsikaryyhldhe
pfsyavnvqnnsasdkhatvriflapkydelgneikadelrrtaieldkfktdlhpgknt
vvrhsldssvtlshqptfedllseycscgwpshllvpkgnikgmeyhlfvmltdwdkdkv
vacvdavsycgardhkypdkkpmgfpfdrpihtehisdfltnnmfikdikikfhe
>d1lla_1 1.78.1.1.1 (2-379) Hemocyanin, N-terminal and middle domains {(Limulus polyphemus)}
lhdkqirichlfeqlssatvigdgdkhkhsdrlknvgklqpgaifscfhpdhleearhly
evfweagdfndfieiakeartfvneglfafaaevavlhrddckglyvppvqeifpdkfip
saaineafkkahvrpefdespilvdvqdtgnildpeyrlayyredvginahhwhwhlvyp
stwnpkyfgkkkdrkgelfyymhqqmcarydcerlsngmhrmlpfnnfdeplagyaphlt
hvasgkyysprpdglklrdlgdieisemvrmrerildsihlgyvisedgshktldelhgt
dilgalvessyesvnheyygnlhnwghvtmarihdpdgrfheepgvmsdtstslrdpify
nwhrfidnifheykntlk
>d1lla_2 2.1.1.5.8 (380-628) Hemocyanin, C-terminal domain {Horseshoe crab(Limulus polyphemus) hemolymph}
pydhdvlnfpdiqvqdvtlharvdnvvhtfmreqelelkhginpgnarsikaryyhldhe
pfsyavnvqnnsasdkhatvriflapkydelgneikadelrrtaieldkfktdlhpgknt
vvrhsldssvtlshqptfedllhgvglnehkseycscgwpshllvpkgnikgmeyhlfvm
ltdwdkdkvdgsesvacvdavsycgardhkypdkkpmgfpfdrpihtehisdfltnnmfi
kdikikfhe
>d1llc_1 3.22.1.5.11 (13-164) Lactate dehydrogenase {(Lactobacillus casei)}
asitdkdhqkvilvgdgavgssyafamvlqgiaqeigivdifkdktkgdaidlsnalpft
spkkiysaeysdakdadlvvitagapkqpgetrldlvnknlkilksivdpivdsgfnlif
lvaanpvdiltyatwklsgfpknrvvgsg
>d1llc_2 4.100.1.1.11 (165-333) Lactate dehydrogenase {(Lactobacillus casei)}
tsldtarfrqsiaemvnvdarsvhayimgehgdtefpvwshaniggvtiaewvkahpeik
edklvkmfedvrdaayeiiklkgatfygiatalariskailndenavlplsvymdgqygi
ndlyigtpavinrngiqnileipltdheeesmqksasqlkkvltdafaknd
>d1llda1 3.22.1.5.12 (7-149) Lactate dehydrogenase {(Bifidobacterium longum), strain am101-2}
ptklavigagavgstlafaaaqrgiareivlediakerveaevldmqhgssfyptvsidg
sddpeicrdadmvvitagprqkpgqsrlelvgatvnilkaimpnlvkvapnaiymlitnp
vdiathvaqkltglpenqifgsg
>d1llda2 4.100.1.1.12 (150-319) Lactate dehydrogenase {(Bifidobacterium longum), strain am101-2}
tnldsarlrfliaqqtgvnvknvhayiagehgdsevplwesatiggvpmsdwtplpghdp
ldadkreeihqevknaaykiingkgatnyaigmsgvdiieavlhdtnrilpvssmlkdfh
gisdicmsvptllnrqgvnntintpvsdkelaalkrsaetlketaaqfgf
>d1lldb1 3.22.1.5.12 (7-149) Lactate dehydrogenase {(Bifidobacterium longum), strain am101-2}
ptklavigagavgstlafaaaqrgiareivlediakerveaevldmqhgssfyptvsidg
sddpeicrdadmvvitagprqkpgqsrlelvgatvnilkaimpnlvkvapnaiymlitnp
vdiathvaqkltglpenqifgsg
>d1lldb2 4.100.1.1.12 (150-319) Lactate dehydrogenase {(Bifidobacterium longum), strain am101-2}
tnldsarlrfliaqqtgvnvknvhayiagehgdsevplwesatiggvpmsdwtplpghdp
ldadkreeihqevknaaykiingkgatnyaigmsgvdiieavlhdtnrilpvssmlkdfh
gisdicmsvptllnrqgvnntintpvsdkelaalkrsaetlketaaqfgf
>d1llia_ 1.32.1.2.1 lambda C1 repressor, DNA-binding domain {(Escherichia coli) bacteriophage Lambda}
kkpltqeqledarrlkaiyekkknelglsqesladklgmgqsgigalfnginalnaynaa
llakilkvsveefspsiareiyemyeavs
>d1llib_ 1.32.1.2.1 lambda C1 repressor, DNA-binding domain {(Escherichia coli) bacteriophage Lambda}
stkkkpltqeqledarrlkaiyekkknelglsqesladklgmgqsgigalfnginalnay
naallakilkvsveefspsiareiyemyeavs
>d1llo__ 3.1.1.5.1 Hevamine A (chitinase/lysozyme) {Para rubber tree (Hevea brasiliensis)}
ggiaiywgqngnegtltqtcstrkysyvniaflnkfgngqtpqinlaghcnpaaggctiv
sngirscqiqgikvmlslgggigsytlasqadaknvadylwnnflggksssrplgdavld
gidfdiehgstlywddlarylsayskqgkkvyltaapqcpfpdrylgtalntglfdyvwv
qfynnppcqyssgninniinswnrwttsinagkiflglpaapeaagsgyvppdvlisril
peikkspkyggvmlwskfyddkngysssildsv
>d1llp__ 1.72.1.1.1 Lignin peroxidase {white rot basidiomycete (Phanerochaete chrysosporium)}
atcangktvgdasccawfdvlddiqanmfhggqcgaeahesirlvfhdsiaispameakg
kfggggadgsimifdtietafhpnigldevvamqkpfvqkhgvtpgdfiafagavalsnc
pgapqmnfftgrkpatqpapdglvpepfhtvdqiiarvndagefdelelvwmlsahsvaa
vndvdptvqglpfdstpgifdsqffvetqfrgtlfpgsggnqgevesgmageiriqtdht
lardsrtacewqsfvgnqsklvddfqfiflaltqlgqdpnamtdcsdviplskpipgngp
fsffppgkshsdieqacaetpfpslvtlpgpatsvaripphka
>d1lma__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1lmb3_ 1.32.1.2.1 lambda C1 repressor, DNA-binding domain {(Escherichia coli) bacteriophage Lambda}
pltqeqledarrlkaiyekkknelglsqesvadkmgmgqsgvgalfnginalnaynaall
akilkvsveefspsiareiyemyeavs
>d1lmb4_ 1.32.1.2.1 lambda C1 repressor, DNA-binding domain {(Escherichia coli) bacteriophage Lambda}
stkkkpltqeqledarrlkaiyekkknelglsqesvadkmgmgqsgvgalfnginalnay
naallakilkvsveefspsiareiyemyeavs
>d1lmc__ 4.2.1.2.11 Lysozyme {rainbow trout (Oncorhynchus mykiss)}
kvydrcelaralkasgmdgyagnslpnwvclskwessyntqatnrntdgstdygifqins
rywcddgrtpgaknvcgircsqlltddltvaircakrvvldpngigawvawrlhcqnqdl
rsyvagcgv
>d1lmka1 2.1.1.1.53 (2-127) Immunoglobulin (variable domains of L and H chains) {scFv dimer (L5MK16 diabody), based on: (mouse), kappa L chain}
vqlqqsgtelmkpgrslkisckttgyifsnywiewvkqrpghglewigkilpgggsntyn
dkfkgkatftadtssniaymqlssltsedsavyycargedyyaywyvldywgqgttvtvs
sggggs
>d1lmka2 2.1.1.1.53 (201-312) Immunoglobulin (variable domains of L and H chains) {scFv dimer (L5MK16 diabody), based on: (mouse), kappa L chain}
dieltqsplslpvslgdqasiscrssqslvhsngntslhwylkkpgqspklliykvstrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyfcsqsthvpftfgsgtklelk
>d1lmkc1 2.1.1.1.53 (2-127) Immunoglobulin (variable domains of L and H chains) {scFv dimer (L5MK16 diabody), based on: (mouse), kappa L chain}
vqlqqsgtelmkpgrslkisckttgyifsnywiewvkqrpghglewigkilpgggsntyn
dkfkgkatftadtssniaymqlssltsedsavyycargedyyaywyvldywgqgttvtvs
sggggs
>d1lmkc2 2.1.1.1.53 (201-312) Immunoglobulin (variable domains of L and H chains) {scFv dimer (L5MK16 diabody), based on: (mouse), kappa L chain}
dieltqsplslpvslgdqasiscrssqslvhsngntslhwylkkpgqspklliykvstrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyfcsqsthvpftfgsgtklelk
>d1lmke1 2.1.1.1.53 (2-127) Immunoglobulin (variable domains of L and H chains) {scFv dimer (L5MK16 diabody), based on: (mouse), kappa L chain}
vqlqqsgtelmkpgrslkisckttgyifsnywiewvkqrpghglewigkilpgggsntyn
dkfkgkatftadtssniaymqlssltsedsavyycargedyyaywyvldywgqgttvtvs
sggggs
>d1lmke2 2.1.1.1.53 (201-312) Immunoglobulin (variable domains of L and H chains) {scFv dimer (L5MK16 diabody), based on: (mouse), kappa L chain}
dieltqsplslpvslgdqasiscrssqslvhsngntslhwylkkpgqspklliykvstrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyfcsqsthvpftfgsgtklelk
>d1lmkg1 2.1.1.1.53 (2-127) Immunoglobulin (variable domains of L and H chains) {scFv dimer (L5MK16 diabody), based on: (mouse), kappa L chain}
vqlqqsgtelmkpgrslkisckttgyifsnywiewvkqrpghglewigkilpgggsntyn
dkfkgkatftadtssniaymqlssltsedsavyycargedyyaywyvldywgqgttvtvs
sggggs
>d1lmkg2 2.1.1.1.53 (201-312) Immunoglobulin (variable domains of L and H chains) {scFv dimer (L5MK16 diabody), based on: (mouse), kappa L chain}
dieltqsplslpvslgdqasiscrssqslvhsngntslhwylkkpgqspklliykvstrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyfcsqsthvpftfgsgtklelk
>d1lml__ 4.52.1.3.1 Leishmanolysin {(Leishmania major)}
vvrdvnwgalriavstedltdpayhcarvgqhvkdhagaivtctaediltnekrdilvkh
lipqavqlhterlkvqqvqgkwkvtdmvgdicgdfkvpqahitegfsntdfvmyvasvps
eegvlawattcqtfsdghpavgvinipaaniasrydqlvtrvvthemahalgfsgpffed
arivanvpnvrgknfdvpvinsstavakareqygcdtleylevedqggagsagshikmrn
aqdelmapaaaagyytaltmaifqdlgfyqadfskaevmpwgqnagcafltnkcmeqsvt
qwpamfcnesedaircptsrlslgacgvtrhpglppywqyftdpslagvsafmdycpvvv
pysdgsctqraseahasllpfnvfsdaarcidgafrpkatdgivksyaglcanvqcdtat
rtysvqvhgsndytnctpglrvelstvsnafegggyitcppyvevcqgnvqaakd
>d1lmn__ 4.2.1.2.11 Lysozyme {rainbow trout (Oncorhynchus mykiss)}
kvydrcelaralkasgmdgyagnslpnwvclskwessyntqatnrntdgstdygifqins
rywcddgrtpgaknvcgircsqlltddltvaircakrvvldpngigawvawrlhcqnqdl
rsyvagcgv
>d1lmo__ 4.2.1.2.11 Lysozyme {rainbow trout (Oncorhynchus mykiss)}
kvydrcelaralkasgmdgyagnslpnwvclskwessyntqatnrntdgstdygifqins
rywcddgrtpgaknvcgircsqlltddltvaircakrvvldpngigawvawrlhcqnqdl
rsyvagcgv
>d1lmp__ 4.2.1.2.11 Lysozyme {rainbow trout (Oncorhynchus mykiss)}
kvydrcelaralkasgmdgyagnslpnwvclskwessyntqatnrntdgstdygifqins
rywcddgrtpgaknvcgircsqlltddltvaircakrvvldpngigawvawrlhcqnqdl
rsyvagcgv
>d1lmq__ 4.2.1.2.11 Lysozyme {rainbow trout (Oncorhynchus mykiss)}
kvydrcelaralkasgmdgyagnslpnwvclskwessyntqatnrntdgstdygifqins
rywcddgrtpgaknvcgircsqlltddltvaircakrvvldpngigawvawrlhcqnqdl
rsyvagcgv
>d1lmt__ 4.2.1.2.8 Lysozyme {human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavcrgdscnachlscsallqdniadavacakrvvrdpqgirawvawrn
rcqnrdvrqyvqgcgv
>e1lmw.1b 2.35.1.2.31 Urokinase-type plasminogen activator (LMW U-PA), catalytic domain {Human (Homo sapiens)}
iiggefttienqpwfaaiyrrhrggsvtyvcggslmspcwvisathcfidypkkedyivy
lgrsrlnsntqgemkfevenlilhkdysadtlahhndiallkirskegrcaqpsrtiqti
clpsmyndpqfgtsceitgfgkenstdylypeqlkmtvvklishrecqqphyygsevttk
mlcaadpqwktdscqgdsggplvcslqgrmtltgivswgrgcalkdkpgvytrvshflpw
irshtkee
>e1lmw.2d 2.35.1.2.31 Urokinase-type plasminogen activator (LMW U-PA), catalytic domain {Human (Homo sapiens)}
iiggefttienqpwfaaiyrrhrggsvtyvcggslmspcwvisathcfidypkkedyivy
lgrsrlnsntqgemkfevenlilhkdysadtlahhndiallkirskegrcaqpsrtiqti
clpsmyndpqfgtsceitgfgkenstdylypeqlkmtvvklishrecqqphyygsevttk
mlcaadpqwktdscqgdsggplvcslqgrmtltgivswgrgcalkdkpgvytrvshflpw
irshtkee
>d1lnae1 1.57.1.1.2 (156-316) Thermolysin {(Bacillus thermoproteolyticus)}
iyqnesgaineaisdifgtlvefyanknpdweigedvytpgisgdslrsmsdpakygdpd
hyskrytgtqdnggvhinsgiinkaaylisqggthygvsvvgigrdklgkifyraltqyl
tptsnfsqlraaavqsatdlygstsqevasvkqafdavgvk
>d1lnae2 4.52.1.2.2 (1-155) Thermolysin {(Bacillus thermoproteolyticus)}
itgtstvgvgrgvlgdqkninttystyyylqdntrgdgiftydakyrttlpgslwadadn
qffasydapavdahyyagvtydyyknvhnrlsydgnnaairssvhysqgynnafwngsem
vygdgdgqtfiplsggidvvahelthavtdytagl
>d1lnbe1 1.57.1.1.2 (156-316) Thermolysin {(Bacillus thermoproteolyticus)}
iyqnesgaineaisdifgtlvefyanknpdweigedvytpgisgdslrsmsdpakygdpd
hyskrytgtqdnggvhinsgiinkaaylisqggthygvsvvgigrdklgkifyraltqyl
tptsnfsqlraaavqsatdlygstsqevasvkqafdavgvk
>d1lnbe2 4.52.1.2.2 (1-155) Thermolysin {(Bacillus thermoproteolyticus)}
itgtstvgvgrgvlgdqkninttystyyylqdntrgdgiftydakyrttlpgslwadadn
qffasydapavdahyyagvtydyyknvhnrlsydgnnaairssvhysqgynnafwngsem
vygdgdgqtfiplsggidvvahelthavtdytagl
>d1lnce1 1.57.1.1.2 (156-316) Thermolysin {(Bacillus thermoproteolyticus)}
iyqnesgaineaisdifgtlvefyanknpdweigedvytpgisgdslrsmsdpakygdpd
hyskrytgtqdnggvhinsgiinkaaylisqggthygvsvvgigrdklgkifyraltqyl
tptsnfsqlraaavqsatdlygstsqevasvkqafdavgvk
>d1lnce2 4.52.1.2.2 (1-155) Thermolysin {(Bacillus thermoproteolyticus)}
itgtstvgvgrgvlgdqkninttystyyylqdntrgdgiftydakyrttlpgslwadadn
qffasydapavdahyyagvtydyyknvhnrlsydgnnaairssvhysqgynnafwngsem
vygdgdgqtfiplsggidvvahelthavtdytagl
>d1lnde1 1.57.1.1.2 (156-316) Thermolysin {(Bacillus thermoproteolyticus)}
iyqnesgaineaisdifgtlvefyanknpdweigedvytpgisgdslrsmsdpakygdpd
hyskrytgtqdnggvhinsgiinkaaylisqggthygvsvvgigrdklgkifyraltqyl
tptsnfsqlraaavqsatdlygstsqevasvkqafdavgvk
>d1lnde2 4.52.1.2.2 (1-155) Thermolysin {(Bacillus thermoproteolyticus)}
itgtstvgvgrgvlgdqkninttystyyylqdntrgdgiftydakyrttlpgslwadadn
qffasydapavdahyyagvtydyyknvhnrlsydgnnaairssvhysqgynnafwngsem
vygdgdgqtfiplsggidvvahelthavtdytagl
>d1lnee1 1.57.1.1.2 (156-316) Thermolysin {(Bacillus thermoproteolyticus)}
iyqnesgaineaisdifgtlvefyanknpdweigedvytpgisgdslrsmsdpakygdpd
hyskrytgtqdnggvhinsgiinkaaylisqggthygvsvvgigrdklgkifyraltqyl
tptsnfsqlraaavqsatdlygstsqevasvkqafdavgvk
>d1lnee2 4.52.1.2.2 (1-155) Thermolysin {(Bacillus thermoproteolyticus)}
itgtstvgvgrgvlgdqkninttystyyylqdntrgdgiftydakyrttlpgslwadadn
qffasydapavdahyyagvtydyyknvhnrlsydgnnaairssvhysqgynnafwngsem
vygdgdgqtfiplsggidvvahelthavtdytagl
>d1lnfe1 1.57.1.1.2 (156-316) Thermolysin {(Bacillus thermoproteolyticus)}
iyqnesgaineaisdifgtlvefyanknpdweigedvytpgisgdslrsmsdpakygdpd
hyskrytgtqdnggvhinsgiinkaaylisqggthygvsvvgigrdklgkifyraltqyl
tptsnfsqlraaavqsatdlygstsqevasvkqafdavgvk
>d1lnfe2 4.52.1.2.2 (1-155) Thermolysin {(Bacillus thermoproteolyticus)}
itgtstvgvgrgvlgdqkninttystyyylqdntrgdgiftydakyrttlpgslwadadn
qffasydapavdahyyagvtydyyknvhnrlsydgnnaairssvhysqgynnafwngsem
vygdgdgqtfiplsggidvvahelthavtdytagl
>d1lnh_1 1.92.1.1.2 (168-857) Lipoxigenase, C-terminal domain {Soybean (Glycine max), isozyme L3}
lpsetpaplvkyreeelhnlrgdgtgerkeweriydydvyndlgdpdkgenharpvlggn
dtfpyprrgrtgrkptrkdpnsesrsndvylprdeafghlkssdfltyglksvsqnvlpl
lqsafdlnftprefdsfdevhglysggiklptdiiskisplpvlkeifrtdgeqalkfpp
pkviqvsksawmtdeefaremlagvnpnlirclkdfpprskldsqvygdhtsqitkehle
pnlegltvdeaiqnkrlflldhhdpimpylrrinatstkayatrtilflkndgtlrplai
elslphpqgdqsgafsqvflpadegvessiwllakayvvvndscyhqlvshwlnthavve
pfiiatnrhlsvvhpiykllhphyrdtmninglarlslvndggvieqtflwgrysvemsa
vvykdwvftdqalpadlikrgmaiedpscphgirlviedypytvdgleiwdaiktwvhey
vflyyksddtlredpelqacwkelvevghgdkknepwwpkmqtreelveacaiiiwtasa
lhaavnfgqypygglilnrptlsrrfmpekgsaeyeelrknpqkaylktitpkfqtlidl
svieilsrhasdevylgerdnpnwtsdtraleafkrfgnklaqienklsernndeklrnr
cgpvqmpytlllpsskegltfrgipnsisi
>d1lnh_2 2.10.1.1.2 (9-167) Lipoxigenase, N-terminal domain {Soybean (Glycine max), isozyme L3}
ghkikgtvvlmrknvldvnsvtsvggiigqgldlvgstldtltaflgrsvslqlisatka
dangkgklgkatflegiitslptlgagqsafkinfewddgsgipgafyiknfmqtefflv
sltledipnhgsihfvcnswiynaklfksdriffanqty
>e1loa.1a 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tettsfsitkfgpdqqnlifqgdgyttkerltltkavrntvgralysspihiwdsktgnv
anfvtsftfvidapnsynvadgftffiapvdtkpqtgggylgvfnskdydktsqtvavef
dtfyntawdpsngdrhigidvnsiksintkswalqngkeanvviafnaatnvltvsltyp
>e1loa.1b 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1loa.2c 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tettsfsitkfgpdqqnlifqgdgyttkerltltkavrntvgralysspihiwdsktgnv
anfvtsftfvidapnsynvadgftffiapvdtkpqtgggylgvfnskdydktsqtvavef
dtfyntawdpsngdrhigidvnsiksintkswalqngkeanvviafnaatnvltvsltyp
>e1loa.2d 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfhselag
>e1loa.3e 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tettsfsitkfgpdqqnlifqgdgyttkerltltkavrntvgralysspihiwdsktgnv
anfvtsftfvidapnsynvadgftffiapvdtkpqtgggylgvfnskdydktsqtvavef
dtfyntawdpsngdrhigidvnsiksintkswalqngkeanvviafnaatnvltvsltyp
>e1loa.3f 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1loa.4g 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tettsfsitkfgpdqqnlifqgdgyttkerltltkavrntvgralysspihiwdsktgnv
anfvtsftfvidapnsynvadgftffiapvdtkpqtgggylgvfnskdydktsqtvavef
dtfyntawdpsngdrhigidvnsiksintkswalqngkeanvviafnaatnvltvsltyp
>e1loa.4h 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfhselag
>e1lob.1a 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tettsfsitkfgpdqqnlifqgdgyttkerltltkavrntvgralysspihiwdsktgnv
anfvtsftfvidapnsynvadgftffiapvdtkpqtgggylgvfnskdydktsqtvavef
dtfyntawdpsngdrhigidvnsiksintkswalqngkeanvviafnaatnvltvsltyp
>e1lob.1b 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1lob.2c 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tettsfsitkfgpdqqnlifqgdgyttkerltltkavrntvgralysspihiwdsktgnv
anfvtsftfvidapnsynvadgftffiapvdtkpqtgggylgvfnskdydktsqtvavef
dtfyntawdpsngdrhigidvnsiksintkswalqngkeanvviafnaatnvltvsltyp
>e1lob.2d 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfhselag
>e1lob.3e 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tettsfsitkfgpdqqnlifqgdgyttkerltltkavrntvgralysspihiwdsktgnv
anfvtsftfvidapnsynvadgftffiapvdtkpqtgggylgvfnskdydktsqtvavef
dtfyntawdpsngdrhigidvnsiksintkswalqngkeanvviafnaatnvltvsltyp
>e1lob.3f 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1lob.4g 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tettsfsitkfgpdqqnlifqgdgyttkerltltkavrntvgralysspihiwdsktgnv
anfvtsftfvidapnsynvadgftffiapvdtkpqtgggylgvfnskdydktsqtvavef
dtfyntawdpsngdrhigidvnsiksintkswalqngkeanvviafnaatnvltvsltyp
>e1lob.4h 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfhselag
>e1loc.1a 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tettsfsitkfgpdqqnlifqgdgyttkerltltkavrntvgralysspihiwdsktgnv
anfvtsftfvidapnsynvadgftffiapvdtkpqtgggylgvfnskdydktsqtvavef
dtfyntawdpsngdrhigidvnsiksintkswalqngkeanvviafnaatnvltvsltyp
>e1loc.1b 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1loc.2c 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tettsfsitkfgpdqqnlifqgdgyttkerltltkavrntvgralysspihiwdsktgnv
anfvtsftfvidapnsynvadgftffiapvdtkpqtgggylgvfnskdydktsqtvavef
dtfyntawdpsngdrhigidvnsiksintkswalqngkeanvviafnaatnvltvsltyp
>e1loc.2d 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfhselag
>e1loc.3e 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tettsfsitkfgpdqqnlifqgdgyttkerltltkavrntvgralysspihiwdsktgnv
anfvtsftfvidapnsynvadgftffiapvdtkpqtgggylgvfnskdydktsqtvavef
dtfyntawdpsngdrhigidvnsiksintkswalqngkeanvviafnaatnvltvsltyp
>e1loc.3f 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1loc.4g 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tettsfsitkfgpdqqnlifqgdgyttkerltltkavrntvgralysspihiwdsktgnv
anfvtsftfvidapnsynvadgftffiapvdtkpqtgggylgvfnskdydktsqtvavef
dtfyntawdpsngdrhigidvnsiksintkswalqngkeanvviafnaatnvltvsltyp
>e1loc.4h 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfhselag
>e1lod.1a 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tettsfsitkfgpdqqnlifqgdgyttkerltltkavrntvgralysspihiwdsktgnv
anfvtsftfvidapnsynvadgftffiapvdtkpqtgggylgvfnskdydktsqtvavef
dtfyntawdpsngdrhigidvnsiksintkswalqngkeanvviafnaatnvltvsltyp
>e1lod.1b 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1lod.2c 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tettsfsitkfgpdqqnlifqgdgyttkerltltkavrntvgralysspihiwdsktgnv
anfvtsftfvidapnsynvadgftffiapvdtkpqtgggylgvfnskdydktsqtvavef
dtfyntawdpsngdrhigidvnsiksintkswalqngkeanvviafnaatnvltvsltyp
>e1lod.2d 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfhselag
>e1lod.3e 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tettsfsitkfgpdqqnlifqgdgyttkerltltkavrntvgralysspihiwdsktgnv
anfvtsftfvidapnsynvadgftffiapvdtkpqtgggylgvfnskdydktsqtvavef
dtfyntawdpsngdrhigidvnsiksintkswalqngkeanvviafnaatnvltvsltyp
>e1lod.3f 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1lod.4g 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tettsfsitkfgpdqqnlifqgdgyttkerltltkavrntvgralysspihiwdsktgnv
anfvtsftfvidapnsynvadgftffiapvdtkpqtgggylgvfnskdydktsqtvavef
dtfyntawdpsngdrhigidvnsiksintkswalqngkeanvviafnaatnvltvsltyp
>e1lod.4h 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfhselag
>e1loe.1a 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tettsfsitkfgpdqqnlifqgdgyttkerltltkavrntvgralysspihiwdsktgnv
anfvtsftfvidapnsynvadgftffiapvdtkpqtgggylgvfnskdydktsqtvavef
dtfyntawdpsngdrhigidvnsiksintkswalqngkeanvviafnaatnvltvsltyp
>e1loe.1b 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1loe.2c 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tettsfsitkfgpdqqnlifqgdgyttkerltltkavrntvgralysspihiwdsktgnv
anfvtsftfvidapnsynvadgftffiapvdtkpqtgggylgvfnskdydktsqtvavef
dtfyntawdpsngdrhigidvnsiksintkswalqngkeanvviafnaatnvltvsltyp
n
>e1loe.2d 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1lof.1a 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tettsfsitkfgpdqqnlifqgdgyttkerltltkavrntvgralysspihiwdsktgnv
anfvtsftfvidapnsynvadgftffiapvdtkpqtgggylgvfnskdydktsqtvavef
dtfyntawdpsngdrhigidvnsiksintkswalqngkeanvviafnaatnvltvsltyp
n
>e1lof.1b 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1lof.2c 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tettsfsitkfgpdqqnlifqgdgyttkerltltkavrntvgralysspihiwdsktgnv
anfvtsftfvidapnsynvadgftffiapvdtkpqtgggylgvfnskdydktsqtvavef
dtfyntawdpsngdrhigidvnsiksintkswklqngkeanvviafnaatnvltvsltyp
>e1lof.2d 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhselagtssn
>e1log.1a 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tettsfsitkfgpdqqnlifqgdgyttkerltltkavrntvgralysspihiwdsktgnv
anfvtsftfvidapnsynvadgftffiapvdtkpqtgggylgvfnskdydktsqtvavef
dtfyntawdpsngdrhigidvnsiksintkswalqngkeanvviafnaatnvltvsltyp
>e1log.1b 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1log.2c 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
tettsfsitkfgpdqqnlifqgdgyttkerltltkavrntvgralysspihiwdsktgnv
anfvtsftfvidapnsynvadgftffiapvdtkpqtgggylgvfnskdydktsqtvavef
dtfyntawdpsngdrhigidvnsiksintkswalqngkeanvviafnaatnvltvsltyp
n
>e1log.2d 2.21.1.1.8 Lectin {Isolectin I from (Lathyrus ochrus)}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhselagtss
>d1lopa_ 2.47.1.1.5 Cyclophilin {(Escherichia coli)}
mvtfhtnhgdiviktfddkapetvknfldycregfynntifhrvingfmiqgggfepgmk
qkatkepikneannglkntrgtlamartqaphsataqffinvvdndflnfsgeslqgwgy
cvfaevvdgmdevdkikgvatgrsgmhqdvpkedviiesvtvse
>d1loz__ 4.2.1.2.8 Lysozyme {human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygtfqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1lpaa1 7.3.8.1.1 (6-44) (Pro)colipase {pig (Sus scrofa)}
giiinldegelclnsaqcksnccqhdtilsllrcalkar
>d1lpaa2 7.3.8.1.1 (45-90) (Pro)colipase {pig (Sus scrofa)}
ensecsaftlygvyykcpcergltcegdkslvgsitntnfgichnv
>d1lpab1 2.10.2.1.3 (337-449) Pancreatic lipase, C-terminal domain {human (Homo sapience)}
rwrykvsvtlsgkkvtghilvslfgnkgnskqyeifkgtlkpdsthsnefdsdvdvgdlq
mvkfiwynnvinptlprvgaskiivetnvgkqfnfcspetvreevlltltpc
>d1lpab2 3.56.1.11.3 (1-336) Pancreatic lipase, N-terminal domain {human (Homo sapience)}
kevcyerlgcfsddspwsgiterplhilpwspkdvntrfllytnenpnnfqevaadsssi
sgsnfktnrktrfiihgfidkgeenwlanvcknlfkvesvncicvdwkggsrtgytqasq
nirivgaevayfveflqsafgyspsnvhvighslgahaageagrrtngtigritgldpae
pcfqgtpelvrldpsdakfvdvihtdgapivpnlgfgmsqvvghldffpnggvempgckk
nilsqivdidgiwegtrdfaacnhlrsykyytdsivnpdgfagfpcasynvftankcfpc
psggcpqmghyadrypgktndvgqkfyldtgdasnfa
>d1lpba1 7.3.8.1.1 (6-44) (Pro)colipase {pig (Sus scrofa)}
giiinldegelclnsaqcksnccqhdtilslsrcalkar
>d1lpba2 7.3.8.1.1 (45-90) (Pro)colipase {pig (Sus scrofa)}
ensecsaftlygvyykcpcergltcegdkslvgsitntnfgichnv
>d1lpbb1 2.10.2.1.3 (337-449) Pancreatic lipase, C-terminal domain {human (Homo sapience)}
rwrykvsvtlsgkkvtghilvslfgnkgnskqyeifkgtlkpdsthsnefdsdvdvgdlq
mvkfiwynnvinptlprvgaskiivetnvgkqfnfcspetvreevlltltpc
>d1lpbb2 3.56.1.11.3 (1-336) Pancreatic lipase, N-terminal domain {human (Homo sapience)}
kevcyerlgcfsddspwsgiterplhilpwspkdvntrfllytnenpnnfqevaadsssi
sgsnfktnrktrfiihgfidkgeenwlanvcknlfkvesvncicvdwkggsrtgytqasq
nirivgaevayfveflqsafgyspsnvhvighslgahaageagrrtngtigritgldpae
pcfqgtpelvrldpsdakfvdvihtdgapivpnlgfgmsqvvghldffpnggvempgckk
nilsqivdidgiwegtrdfaacnhlrsykyytdsivnpdgfagfpcasynvftankcfpc
psggcpqmghyadrypgktndvgqkfyldtgdasnfa
>d1lpe__ 1.24.1.1.1 Apolipoprotein E3 {human (Homo sapiens)}
gqrwelalgrfwdylrwvqtlseqvqeellssqvtqelralmdetmkelkaykseleeql
tpvaeetrarlskelqaaqarlgadmedvcgrlvqyrgevqamlgqsteelrvrlashlr
klrkrllrdaddlqkrlavyqaga
>d1lpfa1 3.4.1.4.8 (1-158,278-348) Dihydrolipoamide dehydrogenase {(Pseudomonas putida)}
sqkfdvvvigagpggyvaairaaqlglktaciekyigkegkvalggtclnvgcipskall
dssykyheakeafkvhgieakgvtidvpamvarkanivknltggiatlfkangvtsfegh
gkllankqvevtgldgktqvleaenviiasgsrpveipXrrpvttdllaadsgvtlderg
fiyvddhcktsvpgvfaigdvvrgamlahkaseegvmvaeriaghkaqmn
>d1lpfa2 3.4.1.4.8 (159-277) Dihydrolipoamide dehydrogenase {(Pseudomonas putida)}
paplsddiivdstgalefqavpkklgvigagviglelgsvwarlgaevtvlealdkflpa
adeqiakealkvltkqglnirlgarvtasevkkkqvtvtftdangeqketfdklivavg
>d1lpfa3 4.48.1.1.6 (349-472) Dihydrolipoamide dehydrogenase {(Pseudomonas putida)}
ydlipsviythpeiawvgkteqtlkaegvevnvgtfpfaasgramaandttglvkviada
ktdrvlgvhvigpsaaelvqqgaigmefgtsaedlgmmvfshptlsealheaalavngha
ihia
>d1lpfb1 3.4.1.4.8 (1-158,278-348) Dihydrolipoamide dehydrogenase {(Pseudomonas putida)}
sqkfdvvvigagpggyvaairaaqlglktaciekyigkegkvalggtclnvgcipskall
dssykyheakeafkvhgieakgvtidvpamvarkanivknltggiatlfkangvtsfegh
gkllankqvevtgldgktqvleaenviiasgsrpveipXrrpvttdllaadsgvtlderg
fiyvddhcktsvpgvfaigdvvrgamlahkaseegvmvaeriaghkaqmn
>d1lpfb2 3.4.1.4.8 (159-277) Dihydrolipoamide dehydrogenase {(Pseudomonas putida)}
paplsddiivdstgalefqavpkklgvigagviglelgsvwarlgaevtvlealdkflpa
adeqiakealkvltkqglnirlgarvtasevkkkqvtvtftdangeqketfdklivavg
>d1lpfb3 4.48.1.1.6 (349-472) Dihydrolipoamide dehydrogenase {(Pseudomonas putida)}
ydlipsviythpeiawvgkteqtlkaegvevnvgtfpfaasgramaandttglvkviada
ktdrvlgvhvigpsaaelvqqgaigmefgtsaedlgmmvfshptlsealheaalavngha
ihia
>e1lph.1a 7.1.1.1.2 Insulin {human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1lph.1b 7.1.1.1.2 Insulin {human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytkpt
>e1lph.2c 7.1.1.1.2 Insulin {human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1lph.2d 7.1.1.1.2 Insulin {human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytkpt
>d1lpi__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1lpm__ 3.56.1.9.8 type-B carboxylesterase/lipase {fungus (Candida rugosa, formerly cylindracea)}
aptatlangdtitglnaiineaflgipfaeppvgnlrfkdpvpysgsldgqkftsygpsc
mqqnpegtyeenlpkaaldlvmqskvfeavspssedcltinvvrppgtkaganlpvmlwi
fgggfevggtstfppaqmitksiamgkpiihvsvnyrvsswgflagdeikaegsanaglk
dqrlgmqwvadniaafggdptkvtifgesagsmsvmchilwndgdntykgkplfragimq
sgamvpsdavdgiygneifdllasnagcgsasdklaclrgvssdtledatnntpgflays
slrlsylprpdgvnitddmyalvregkyanipviigdqndegtffgtsslnvttdaqare
yfkqsfvhasdaeidtlmtaypgditqgspfdtgilnaltpqfkrisavlgdlgftlarr
yflnhytggtkysflskqlsglpvlgtfhsndivfqdyllgsgsliynnafiafatdldp
ntagllvkwpeytsssqsgnnlmminalglytgkdnfrtagydalfsnppsffv
>d1lpn__ 3.56.1.9.8 type-B carboxylesterase/lipase {fungus (Candida rugosa, formerly cylindracea)}
aptatlangdtitglnaiineaflgipfaeppvgnlrfkdpvpysgsldgqkftsygpsc
mqqnpegtyeenlpkaaldlvmqskvfeavspssedcltinvvrppgtkaganlpvmlwi
fgggfevggtstfppaqmitksiamgkpiihvsvnyrvsswgflagdeikaegsanaglk
dqrlgmqwvadniaafggdptkvtifgesagsmsvmchilwndgdntykgkplfragimq
sgamvpsdavdgiygneifdllasnagcgsasdklaclrgvssdtledatnntpgflays
slrlsylprpdgvnitddmyalvregkyanipviigdqndegtffgtsslnvttdaqare
yfkqsfvhasdaeidtlmtaypgditqgspfdtgilnaltpqfkrisavlgdlgftlarr
yflnhytggtkysflskqlsglpvlgtfhsndivfqdyllgsgsliynnafiafatdldp
ntagllvkwpeytsssqsgnnlmminalglytgkdnfrtagydalfsnppsffv
>d1lpo__ 3.56.1.9.8 type-B carboxylesterase/lipase {fungus (Candida rugosa, formerly cylindracea)}
aptatlangdtitglnaiineaflgipfaeppvgnlrfkdpvpysgsldgqkftsygpsc
mqqnpegtyeenlpkaaldlvmqskvfeavspssedcltinvvrppgtkaganlpvmlwi
fgggfevggtstfppaqmitksiamgkpiihvsvnyrvsswgflagdeikaegsanaglk
dqrlgmqwvadniaafggdptkvtifgesagsmsvmchilwndgdntykgkplfragimq
sgamvpsdavdgiygneifdllasnagcgsasdklaclrgvssdtledatnntpgflays
slrlsylprpdgvnitddmyalvregkyanipviigdqndegtffgtsslnvttdaqare
yfkqsfvhasdaeidtlmtaypgditqgspfdtgilnaltpqfkrisavlgdlgftlarr
yflnhytggtkysflskqlsglpvlgtfhsndivfqdyllgsgsliynnafiafatdldp
ntagllvkwpeytsssqsgnnlmminalglytgkdnfrtagydalfsnppsffv
>d1lpp__ 3.56.1.9.8 type-B carboxylesterase/lipase {fungus (Candida rugosa, formerly cylindracea)}
aptatlangdtitglnaiineaflgipfaeppvgnlrfkdpvpysgsldgqkftsygpsc
mqqnpegtyeenlpkaaldlvmqskvfeavspssedcltinvvrppgtkaganlpvmlwi
fgggfevggtstfppaqmitksiamgkpiihvsvnyrvsswgflagdeikaegsanaglk
dqrlgmqwvadniaafggdptkvtifgesagsmsvmchilwndgdntykgkplfragimq
sgamvpsdavdgiygneifdllasnagcgsasdklaclrgvssdtledatnntpgflays
slrlsylprpdgvnitddmyalvregkyanipviigdqndegtffgtsslnvttdaqare
yfkqsfvhasdaeidtlmtaypgditqgspfdtgilnaltpqfkrisavlgdlgftlarr
yflnhytggtkysflskqlsglpvlgtfhsndivfqdyllgsgsliynnafiafatdldp
ntagllvkwpeytsssqsgnnlmminalglytgkdnfrtagydalfsnppsffv
>d1lps__ 3.56.1.9.8 type-B carboxylesterase/lipase {fungus (Candida rugosa, formerly cylindracea)}
aptatlangdtitglnaiineaflgipfaeppvgnlrfkdpvpysgsldgqkftsygpsc
mqqnpegtyeenlpkaaldlvmqskvfeavspssedcltinvvrppgtkaganlpvmlwi
fgggfevggtstfppaqmitksiamgkpiihvsvnyrvsswgflagdeikaegsanaglk
dqrlgmqwvadniaafggdptkvtifgesagsmsvmchilwndgdntykgkplfragimq
sgamvpsdavdgiygneifdllasnagcgsasdklaclrgvssdtledatnntpgflays
slrlsylprpdgvnitddmyalvregkyanipviigdqndegtffgtsslnvttdaqare
yfkqsfvhasdaeidtlmtaypgditqgspfdtgilnaltpqfkrisavlgdlgftlarr
yflnhytggtkysflskqlsglpvlgtfhsndivfqdyllgsgsliynnafiafatdldp
ntagllvkwpeytsssqsgnnlmminalglytgkdnfrtagydalfsnppsffv
>d1lpt__ 1.47.1.1.2 plant non-specific lipid-transfer protein (ns-LTP) {wheat (Triticum aestivum) L. seeds}
idcghvdslvrpclsyvqggpgpsgqccdgvknlhnqarsqsdrqsacnclkgiargihn
lnednarsippkcgvnlpytislnidcsrv
>d1lqc__ 1.32.1.3.2 Lac repressor (LacR), N-terminal domain {(Escherichia coli), strain bmh 74-12}
mkpvtlydvaeyagvsyqtvsrvvnqashvsaktrekveaamaelnyipnrvaqql
>d1lqh__ 7.3.6.2.14 Alpha toxin {scorpion (Leiurus quinquestriatus hebraeus)}
mvrdayiaknyncvyecfrdaycnelctkngassgycqwagkygnacwcyalpdnvpirv
pgkcr
>d1lqi__ 7.3.6.2.14 Alpha toxin {scorpion (Leiurus quinquestriatus hebraeus)}
mvrdayiaknyncvyecfrdaycnelctkngassgycqwagkygnacwcyalpdnvpirv
pgkcr
>d1lqq__ 7.3.6.2.16 LQQIII toxin {Egyptian scorpion (Leiurus quinquestriatus)}
vrdayiaknyncvyecfrdsycndlctkngassgycqwagkygnacwcyalpdnvpirvp
gkch
>d1lra__ 4.1.1.1.3 RNase T1 {(Aspergillus oryzae)}
acdytcgsncysssdvstaqaagyklhedgetvgsnsyphkynnyegfdfsvsspyyawp
ilssgdvysggspgadrvvfnennqlagvithtgasgnnfvect
>d1lre__ 1.13.1.1.1 alpha-2-Macroglobulin receptor associated protein (RAP) domain 1 {human (Homo sapiens)}
geefrmeklnqlwekaqrlhlppvrlaelhadlkiqerdelawkklkldgldedgekear
lirnlnvilakygldgkkdar
>d1lrp__ 1.32.1.2.1 lambda C1 repressor, DNA-binding domain {(Escherichia coli) bacteriophage Lambda}
kkpltqeqledarrlkaiyekkknelglsqesvadkmgmgqsgvgalfnginalnaynaa
llakilkvsveefspsiareiyemyeavs
>d1lrv__ 1.91.2.1.1 A leucine-rich repeat variant {(Azotobacter vinelandii)}
tpigdcrvcsfrmsllltgrctpgdacvavesgrqidrffrnnphlavqyladpfwerra
iavryspvealtplirdsdevvrravayrlpreqlsalmfdedrevritvadrlpleqle
qmaadrdylvrayvvqrippgrlfrfmrdedrqvrklvakrlpeeslglmtqdpepevrr
ivasrlrgddllellhdpdwtvrlaavehaslealreldepdpevrlaiagrl
>d1lsa__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1lsb__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1lsc__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1lsd__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1lse__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1lsf__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1lsg__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
mkvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqin
srwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtd
vqawirgcrlqqhhlggakqagdv
>d1lsi__ 7.6.1.1.8 Long neurotoxin 1 (component LSIII) {sea snake (Laticauda semifasciata)}
recylnphdtqtcpsgqeicyvkswcnawcssrgkvlefgcaatcpsvntgteikccsad
kcntyp
>d1lsm__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygllqins
rwwcndgrtpgsrnlcnipcsallssditatvncakkivssgngmnawvawrnrckgtdv
qawirgcrl
>d1lsn__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditaavncakkivsngngmnawvawrnrckgtdv
qawirgcrl
>d1lsp__ 4.2.1.5.2 Lysozyme {Australian black swan (Cygnus atratus)}
rtdcygnvnridttgascktakpeglsycgvpasktiaerdlkamdryktiikkvgeklc
vepaviagiisreshagkvlkngwgdrgngfglmqvdkrshkpqgtwngevhitqgttil
tdfikriqkkfpswtkdqqlkggisaynagagnvrsyarmdigtthddyandvvaraqyy
kqhgy
>d1lsqa_ 4.4.1.1.1 Ribonuclease A (also ribonuclease B, S) {bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackxgqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1lsqb_ 4.4.1.1.1 Ribonuclease A (also ribonuclease B, S) {bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackxgqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1lst__ 3.82.1.1.3 Lysine-,arginine-,ornithine-binding (LAO) protein {(Salmonella typhimurium)}
alpqtvrigtdttyapfsskdakgefigfdidlgnemckrmqvkctwvasdfdalipslk
akkidaiisslsitdkrqqeiafsdklyaadsrliaakgspiqptleslkgkhvgvlqgs
tqeayandnwrtkgvdvvayanqdliysdltagrldaalqdevaasegflkqpagkeyaf
agpsvkdkkyfgdgtgvglrkddtelkaafdkaltelrqdgtydkmakkyfdfnvygdk
>d1lsy__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstsygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1lsz__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstsygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1lt3a_ 4.103.1.1.1 Heat-labile toxin, A-chain {(Escherichia coli) type IB}
rlyradsrppdeikrsgglmprghneyfdrgtqmniclydhargtqtgfvryddgyvsts
lslrsahlagqsilsgystyyiyviatapnmfnvndvlgvysphpyeqevsalggipysq
iygwyrvnfgviderlhrnreyrdryyrnlniapaedgyrlacfppdhqawreepwihha
pqgcgnssrtitgdtcneetqnlstiylreyqskvkrqifsdyqsevdiynri
>d1lt3d_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1lt3e_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1lt3f_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1lt3g_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1lt3h_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1lt4a_ 4.103.1.1.1 Heat-labile toxin, A-chain {(Escherichia coli) type IB}
rlyradsrppdeikrsgglmprghneyfdrgtqmninlydhargtqtgfvryddgyvstk
lslrsahlagqsilsgystyyiyviatapnmfnvndvlgvysphpyeqevsalggipysq
iygwyrvnfgviderlhrnreyrdryyrnlniapaedgyrlagfppdhqawreepwihha
pqgcgnssnssrtitrtitgdtcneetqnlstiylreyqskvkrqifsdyqsevdiynri
>d1lt4d_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1lt4e_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1lt4f_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1lt4g_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1lt4h_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1lt5d_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1lt5e_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1lt5f_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1lt5g_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1lt5h_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1lt6d_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1lt6e_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1lt6f_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1lt6g_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1lt6h_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1lt6l_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1lt6m_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1lt6n_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1lt6o_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1lt6p_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>e1lta.1a 4.103.1.1.1 Heat-labile toxin, A-chain {(Escherichia coli) type IB}
ngdrlyradsrppdeikrsgglmprghneyfdrgtqmninlydhargtqtgfvryddgyv
stslslrsahlagqsilsgystyyiyviatapnmfnvndvlgvysphpyeqevsalggip
ysqiygwyrvnfgviderlhrnreyrdryyrnlniapaedgyrlagfppdhqawreepwi
hhapqgcg
>e1lta.1c 4.103.1.1.1 Heat-labile toxin, A-chain {(Escherichia coli) type IB}
gdtcneetqnlstiylreyqskvkrqifsdyqsevdiynr
>d1ltad_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1ltae_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1ltaf_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1ltag_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1ltah_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>e1ltb.1a 4.103.1.1.1 Heat-labile toxin, A-chain {(Escherichia coli) type IB}
rlyradsrppdeikrsgglmprghneyfdrgtqmninlydhargtqtgfvryddgyvsts
lslrsahlagqsilsgystyyiyviatapnmfnvndvlgvysphpyeqevsalggipysq
iygwyrvnfgviderlhrnreyrdryyrnlniapaedgyrlagfppdhqawreepwihha
pqgcg
>e1ltb.1c 4.103.1.1.1 Heat-labile toxin, A-chain {(Escherichia coli) type IB}
gdtcneetqnlstiylreyqskvkrqifsdyqsevdi
>d1ltbd_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1ltbe_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1ltbf_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1ltbg_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1ltbh_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1ltda1 3.1.7.1.5 (98-511) Flavocytochrome b2, C-terminal domain {yeast (Saccharomyces cerevisiae)}
apgetkediarkeqlksllppldniinlydfeylasqtltkqawayyssgandevthren
hnayhriffkpkilvdvrkvdistdmlgshvdvpfyvsatalcklgnplegekdvargcg
qgvtkvpqmistlascspeeiieaapsdkqiqwyqlyvnsdrkitddlvknveklgvkal
fvtvdapslgqrekdmklkfsntkagpkamkktnveesqgasralskfidpsltwkdiee
lkkktklpivikgvqrtedvikaaeigvsgvvlsnhggrqldfsrapievlaetmpileq
rnlkdklevfvdggvrrgtdvlkalclgakgvglgrpflyanscygrngvekaieilrde
iemsmrllgvtsiaelkpdlldlstlkartvgvpndvlynevyegptltefeda
>d1ltda2 4.70.1.1.3 (10-97) Flavocytochrome b2, N-terminal domain {yeast (Saccharomyces cerevisiae)}
kispaevakhnkpddcwvvingyvydltrflpnhpggqdvikfnagkdvtaifeplhapn
vidkyiapekklgplqgsmppelvcppy
>d1lte__ 2.21.1.1.6 Lectin {coral tree (Erythrina corallodendron)}
vetisfsfsefepgndnltlqgaslitqsgvlqltkinqngmpawdstgrtlyakpvhiw
dmttgtvasfetrfsfsieqpytrplpadglvffmgptkskpaqgygylgifnqskqdns
yqtlgvefdtfsnpwdppqvphigidvnsirsiktqpfqldngqvanvvikydasskllh
avlvypssgaiytiaeivdvkqvlpewvdvglsgatgaqrdaaethdvyswsfqaslpe
>e1ltg.1a 4.103.1.1.1 Heat-labile toxin, A-chain {(Escherichia coli) type IB}
rlykadsrppdeikrsgglmprghneyfdrgtqmninlydhargtqtgfvryddgyvsts
lslrsahlagqsilsgystyyiyviatapnmfnvndvlgvysphpyeqevsalggipysq
iygwyrvnfgviderlhrnreyrdryyrnlniapaedgyrlagfppdhqawreepwihha
pqgcg
>e1ltg.1c 4.103.1.1.1 Heat-labile toxin, A-chain {(Escherichia coli) type IB}
gdtcneetqnlstiylreyqskvkrqifsdyqsevdiynri
>d1ltgd_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1ltge_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1ltgf_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1ltgg_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1ltgh_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1lthr1 3.22.1.5.12 (7-149) Lactate dehydrogenase {(Bifidobacterium longum), strain am101-2}
ptklavigagavgstlafaaaqrgiareivlediakerveaevldmqhgssfyptvsidg
sddpeicrdadmvvitagprqkpgqsrlelvgatvnilkaimpnlvkvapnaiymlitnp
vdiathvaqkltglpenqifgsg
>d1lthr2 4.100.1.1.12 (150-319) Lactate dehydrogenase {(Bifidobacterium longum), strain am101-2}
tnldsarlrfliaqqtgvnvknvhayiagehgdsevplwesatiggvpmsdwtplpghdp
ldadkreeihqevknaaykiingkgatnyaigmsgvdiieavlhdtnrilpvssmlkdfh
gisdicmsvptllnrqgvnntintpvsdkelaalkrsaetlketaaqfgf
>d1ltht1 3.22.1.5.12 (7-149) Lactate dehydrogenase {(Bifidobacterium longum), strain am101-2}
ptklavigagavgstlafaaaqrgiareivlediakerveaevldmqhgssfyptvsidg
sddpeicrdadmvvitagprqkpgqsrlelvgatvnilkaimpnlvkvapnaiymlitnp
vdiathvaqkltglpenqifgsg
>d1ltht2 4.100.1.1.12 (150-319) Lactate dehydrogenase {(Bifidobacterium longum), strain am101-2}
tnldsarlrfliaqqtgvnvknvhayiagehgdsevplwesatiggvpmsdwtplpghdp
ldadkreeihqevknaaykiingkgatnyaigmsgvdiieavlhdtnrilpvssmlkdfh
gisdicmsvptllnrqgvnntintpvsdkelaalkrsaetlketaaqfgf
>e1lti.1a 4.103.1.1.1 Heat-labile toxin, A-chain {(Escherichia coli) type IB}
rlyradsrppdeikrsgglmprghneyfdrgtqmninlydhargtqtgfvryddgyvsts
lslrsahlagqsilsgystyyiyviatapnmfnvndvlgvysphpyeqevsalggipysq
iygwyrvnfgviderlhrnreyrdryyrnlniapaedgyrlagfppdhqawreepwihha
pqgcg
>e1lti.1c 4.103.1.1.1 Heat-labile toxin, A-chain {(Escherichia coli) type IB}
gdtcneetqnlstiylreyqskvkrqifsdyqsevdiynri
>d1ltid_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1ltie_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1ltif_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1ltig_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1ltih_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>e1lts.1a 4.103.1.1.1 Heat-labile toxin, A-chain {(Escherichia coli) type IB}
rlyradsrppdeikrsgglmprghneyfdrgtqmninlydhargtqtgfvryddgyvsts
lslrsahlagqsilsgystyyiyviatapnmfnvndvlgvysphpyeqevsalggipysq
iygwyrvnfgviderlhrnreyrdryyrnlniapaedgyrlagfppdhqawreepwihha
pqgcg
>e1lts.1c 4.103.1.1.1 Heat-labile toxin, A-chain {(Escherichia coli) type IB}
gdtcneetqnlstiylreyqskvkrqifsdyqsevdiynri
>d1ltsd_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1ltse_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1ltsf_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1ltsg_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1ltsh_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>e1ltt.1a 4.103.1.1.1 Heat-labile toxin, A-chain {(Escherichia coli) type IB}
rlyradsrppdeikrsgglmprghneyfdrgtqmninlydhargtqtgfvryddgyvsts
lslrsahlagqsilsgystyyiyviatapnmfnvndvlgvysphpyeqevsalggipysq
iygwyrvnfgviderlhrnreyrdryyrnlniapaedgyrlagfppdhqawreepwihha
pqgcg
>e1ltt.1c 4.103.1.1.1 Heat-labile toxin, A-chain {(Escherichia coli) type IB}
gdtcneetqnlstiylreyqskvkrqifsdyqsevdiynri
>d1lttd_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1ltte_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1lttf_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1lttg_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1ltth_ 2.29.2.1.1 Heat-labile toxin {(Escherichia coli) type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1ltw__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdiwirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1luca_ 3.1.13.1.1 Bacterial luciferase (alkanal monooxygenase) {(Vibrio harveyi)}
mkfgnflltyqppelsqtevmkrlvnlgkasegcgfdtvwllehhftefgllgnpyvaaa
hllgatetlnvgtaaivlptahpvrqaedvnlldqmskgrfrfgicrglydkdfrvfgtd
mdnsralmdcwydlmkegfnegyiaadnehikfpkiqlnpsaytqggapvyvvaesastt
ewaaerglpmilswiinthekkaqldlynevatehgydvtkidhclsyitsvdhdsnrak
dicrnflghwydsyvnatkifddsdqtkgydfnkgqwrdfvlkghkdtnrridysyeinp
vgtpeeciaiiqqdidatgidniccgfeangseeeiiasmklfqsdvmpylkekq
>d1lucb_ 3.1.13.1.1 Bacterial luciferase (alkanal monooxygenase) {(Vibrio harveyi)}
mkfglfflnfmnskrssdqvieemldtahyvdqlkfdtlavyenhfsnngvvgapltvag
fllgmtknakvaslnhvitthhpvrvaeeaclldqmsegrfafgfsdceksadmrffnrp
tdsqfqlfsechkiindafttgychpnndfysfpkisvnphafteggpaqfvnatskevv
ewaaklglplvfrwddsnaqrkeyaglyhevaqahgvdvsqvrhkltllvnqnvdgeaar
aearvyleefvresysntdfeqkmgellsenaigtyeestqaarvaieccgaadllmsfe
smedkaqqravidvvnaniv
>d1lve__ 2.1.1.1.114 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (kappa) domain LEN (human)}
divmtqspdslavslgeratinckssqsvlyssnsknylawyqqkpgqppklliywastr
esgvpdrfsgsgsgtdftltisslqaedvavyycqqyystpysfgqgtkleikr
>d1lvk_1 2.24.3.1.2 (34-79) Myosin S1 fragment, N-terminal domain {(Dictyostelium discoideum)}
yiwynpdpkerdsyecgeivsetsdsftfktsdgqdrqvkkddanq
>d1lvk_2 3.29.1.5.2 (2-33,80-759) Myosin S1, motor domain {Slime mold (Dictyostelium discoideum)}
npihdrtsdyhkylkvkqgdsdlfkltvsdkrXrnpikfdgvedmselsylnepavfhnl
rvrynqdliytysglflvavnpfkripiytqemvdifkgrrrnevaphifaisdvayrsm
lddrqnqsllitgesgagktentkkviqylasvagrnqangsgvleqqilqanpileafg
nakttrnnnssrfgkfieiqfnnagfisgasiqsylleksrvvfqstsernyhifyqlla
gataeekkalhlagpesfnylnqsgcvdikgvsdedefkitrqamdivgfsqeeqmsifk
iiagilhlgnikfekgagegavlkdktalnaastvfgvnpsvlekalmeprilagrdlva
qhlnvekssssrdalvkalygrlflwlvkkinnvlcserkayfigvldisgfeifkvnsf
eqlcinytneklqqffnhhmfkveqekylkekinwtfidfgldsqatidlidgrqppgil
alldeqsvfpnatdntlitklhshfskknakyeeprfsktefgvthyagqvmyeiqdwle
knkdplqqdlelcfkdssdnvvtklfndpniasrakkganfltvaaqykeqlaslmatle
ttnphfvrciipnnkqlpakledkvvldqlrcngvlegiritrkgfpnriiyadfvkryy
dlapnvprdaedsqkatdavlkhlnidpeqfrfgitkiffragqlarieeare
>d1lvl_1 3.4.1.4.8 (1-150,266-335) Dihydrolipoamide dehydrogenase {(Pseudomonas putida)}
qqtiqttlliigggpggyvaairagqlgiptvlvegqalggtclnigcipskalihvaeq
fhqasrftepsplgisvasprldigqsvawkdgivdrlttgvaallkkhgvkvvhgwakv
ldgkqvevdgqriqcehlllatgsssvelpXrrprtkgfnlecldlkmngaaiaidercq
tsmhnvwaigdvagepmlahramaqgemvaeiiagkarrfe
>d1lvl_2 3.4.1.4.8 (151-265) Dihydrolipoamide dehydrogenase {(Pseudomonas putida)}
mlplggpvisstealapkalpqhlvvvgggyiglelgiayrklgaqvsvvearerilpty
dseltapvaeslkklgialhlghsvegyengcllandgkggqlrleadrvlvavg
>d1lvl_3 4.48.1.1.6 (336-458) Dihydrolipoamide dehydrogenase {(Pseudomonas putida)}
paaiaavcftdpevvvvgktpeqasqqgldcivaqfpfaangramslesksgfvrvvarr
dnhlilgwqavgvavselstafaqslemgacledvagtihahptlgeavqeaalralgha
lhi
>d1lvy__ 2.35.1.2.14 Elastase {porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1lwia_ 3.1.5.1.5 3-alpha-hydroxysteroid dehydrogenase {rat (Rattus norvegicus) sprague-dawley strain}
mdsislrvalndgnfipvlgfgttvpekvakdevikatkiaidngfrhfdsaylyeveee
vgqairskiedgtvkredifytsklwstfhrpelvrtclektlkstqldyvdlyiihfpm
alqpgdiffprdehgkllfetvdicdtweamekckdaglaksigvsnfncrqlerilnkp
glkykpvcnqvechlylnqskmldyckskdiilvsyctlgssrdktwvdqkspvllddpv
lcaiakkykqtpalvalryqlqrgvvplirsfnakrikeltqvfefqlasedmkaldgln
rnfrynnakyf
>d1lwib_ 3.1.5.1.5 3-alpha-hydroxysteroid dehydrogenase {rat (Rattus norvegicus) sprague-dawley strain}
mdsislrvalndgnfipvlgfgttvpekvakdevikatkiaidngfrhfdsaylyeveee
vgqairskiedgtvkredifytsklwstfhrpelvrtclektlkstqldyvdlyiihfpm
alqpgdiffprdehgkllfetvdicdtweamekckdaglaksigvsnfncrqlerilnkp
glkykpvcnqvechlylnqskmldyckskdiilvsyctlgssrdktwvdqkspvllddpv
lcaiakkykqtpalvalryqlqrgvvplirsfnakrikeltqvfefqlasedmkaldgln
rnfrynnakyf
>d1lwxa_ 4.34.6.1.2 Nucleoside diphosphate kinases {(Dictyostelium discodeum)}
vnkertflavkpdgvarglvgeiiaryekkgfvlvglkqlvptkdlaeshyaehkerpff
gglvsfitsgpvvamvfegkgvvasarlmigvtnplasapgsirgdfgvdvgraiihgsd
svesanreialwfkpeelltevkpnpnlye
>d1lwxb_ 4.34.6.1.2 Nucleoside diphosphate kinases {(Dictyostelium discodeum)}
vnkertflavkpdgvarglvgeiiaryekkgfvlvglkqlvptkdlaeshyaehkerpff
gglvsfitsgpvvamvfegkgvvasarlmigvtnplasapgsirgdfgvdvgraiihgsd
svesanreialwfkpeelltevkpnpnlye
>d1lwxc_ 4.34.6.1.2 Nucleoside diphosphate kinases {(Dictyostelium discodeum)}
vnkertflavkpdgvarglvgeiiaryekkgfvlvglkqlvptkdlaeshyaehkerpff
gglvsfitsgpvvamvfegkgvvasarlmigvtnplasapgsirgdfgvdvgraiihgsd
svesanreialwfkpeelltevkpnpnlye
>d1lxa__ 2.63.1.1.1 UDP N-acetylglucosamine acyltransferase {(Escherichia coli) gene lpxA}
midksafvhptaiveegasiganahigpfcivgphveigegtvlkshvvvnghtkigrdn
eiyqfasigevnqdlkyageptrveigdrnriresvtihrgtvqgggltkvgsdnllmin
ahiahdctvgnrcilannatlaghvsvddfaiiggmtavhqfciigahvmvggcsgvaqd
vppyviaqgnhatpfgvnieglkrrgfsreaitairnaykliyrsgktldevkpeiaela
etypevkaftdffarstrglir
>d1lxda_ 4.11.3.1.2 Rbd of Ral guanosine-nucleotide exchange factor, RalGDS {Rat (Rattus norvegicus)}
gdcciirvsldvdngnmyksilvtsqdkaptvirkamdkhnldedepedyellqiisedh
klkipenanvfyamnsaanydfilkkr
>d1lxdb_ 4.11.3.1.2 Rbd of Ral guanosine-nucleotide exchange factor, RalGDS {Rat (Rattus norvegicus)}
gdcciirvsldvdngnmyksilvtsqdkaptvirkamdkhnldedepedyellqiisedh
klkipenanvfyamnsaanydfilkkr
>d1lxl__ 6.1.4.1.1 Apoptosis regulator Bcl-xL {Human (Homo sapiens)}
msmamsqsnrelvvdflsyklsqkgyswsqfsdveenrteapegtesemetpsaingnps
whladspavngatghsssldarevipmaavkqalreagdefelryrrafsdltsqlhitp
gtayqsfeqvvnelfrdgvnwgrivaffsfggalcvesvdkemqvlvsriaawmatylnd
hlepwiqenggwdtfvelygnnaaaesrkgqerlehhhhhh
>d1lxta1 3.72.1.1.1 (1-190) Phosphoglucomutase, first 3 domains {rabbit (Oryctolagus cuniculus)}
vkivtvktkaypdqkpgtsglrkrvkvfqsstnyaenfiqsiistvepaqrqeatlvvgg
dgrfymkeaiqlivriaaangigrlvigqngilstpavsciirkikaiggiiltashnpg
gpngdfgikfnisnggpapeaitdkifqisktieeyaicpdlkvdlgvlgkqqfdlenkf
kpftveivds
>d1lxta2 3.72.1.1.1 (191-303) Phosphoglucomutase, first 3 domains {rabbit (Oryctolagus cuniculus)}
veayatmlrnifdfnalkellsgpnrlkiridamhgvvgpyvkkilceelgapansavnc
vpledfgghhpdpnltyaadlvetmksgehdfgaafdgdgdrnmilgkhgffv
>d1lxta3 3.72.1.1.1 (304-420) Phosphoglucomutase, first 3 domains {rabbit (Oryctolagus cuniculus)}
npsdsvaviaanifsipyfqqtgvrgfarsmptsgaldrvanatkialyetptgwkffgn
lmdasklslcgeesfgtgsdhirekdglwavlawlsilatrkqsvedilkdhwhkfg
>d1lxta4 4.79.2.1.1 (421-561) Phosphoglucomutase, the C-terminal domain {rabbit (Oryctolagus cuniculus)}
rnfftrydyeeveaegatkmmkdlealmfdrsfvgkqfsandkvytvekadnfeyhdpvd
gsvsknqglrlifadgsriifrlsgtgsagatirlyidsyekdnakinqdpqvmlaplis
ialkvsqlqertgrtaptvit
>d1lxtb1 3.72.1.1.1 (1-190) Phosphoglucomutase, first 3 domains {rabbit (Oryctolagus cuniculus)}
vkivtvktkaypdqkpgtsglrkrvkvfqsstnyaenfiqsiistvepaqrqeatlvvgg
dgrfymkeaiqlivriaaangigrlvigqngilstpavsciirkikaiggiiltashnpg
gpngdfgikfnisnggpapeaitdkifqisktieeyaicpdlkvdlgvlgkqqfdlenkf
kpftveivds
>d1lxtb2 3.72.1.1.1 (191-303) Phosphoglucomutase, first 3 domains {rabbit (Oryctolagus cuniculus)}
veayatmlrnifdfnalkellsgpnrlkiridamhgvvgpyvkkilceelgapansavnc
vpledfgghhpdpnltyaadlvetmksgehdfgaafdgdgdrnmilgkhgffv
>d1lxtb3 3.72.1.1.1 (304-420) Phosphoglucomutase, first 3 domains {rabbit (Oryctolagus cuniculus)}
npsdsvaviaanifsipyfqqtgvrgfarsmptsgaldrvanatkialyetptgwkffgn
lmdasklslcgeesfgtgsdhirekdglwavlawlsilatrkqsvedilkdhwhkfg
>d1lxtb4 4.79.2.1.1 (421-561) Phosphoglucomutase, the C-terminal domain {rabbit (Oryctolagus cuniculus)}
rnfftrydyeeveaegatkmmkdlealmfdrsfvgkqfsandkvytvekadnfeyhdpvd
gsvsknqglrlifadgsriifrlsgtgsagatirlyidsyekdnakinqdpqvmlaplis
ialkvsqlqertgrtaptvit
>e1lya.1a 2.38.1.2.12 Cathepsin D {human (Homo sapiens)}
gpipevlknymdaqyygeigigtppqcftvvfdtgssnlwvpsihcklldiacwihhkyn
sdksstyvkngtsfdihygsgslsgylsqdtvsvpcq
>e1lya.1b 2.38.1.2.12 Cathepsin D {human (Homo sapiens)}
ggvkverqvfgeatkqpgitfiaakfdgilgmayprisvnnvlpvfdnlmqqklvdqnif
sfylsrdpdaqpggelmlggtdskyykgslsylnvtrkaywqvhldqvevasgltlckeg
ceaivdtgtslmvgpvdevrelqkaigavpliqgeymipcekvstlpaitlklggkgykl
spedytlkvsqagktlclsgfmgmdipppsgplwilgdvfigryytvfdrdnnrvgfaea
a
>e1lya.2c 2.38.1.2.12 Cathepsin D {human (Homo sapiens)}
gpipevlknymdaqyygeigigtppqcftvvfdtgssnlwvpsihcklldiacwihhkyn
sdksstyvkngtsfdihygsgslsgylsqdtvsvpcq
>e1lya.2d 2.38.1.2.12 Cathepsin D {human (Homo sapiens)}
ggvkverqvfgeatkqpgitfiaakfdgilgmayprisvnnvlpvfdnlmqqklvdqnif
sfylsrdpdaqpggelmlggtdskyykgslsylnvtrkaywqvhldqvevasgltlckeg
ceaivdtgtslmvgpvdevrelqkaigavpliqgeymipcekvstlpaitlklggkgykl
spedytlkvsqagktlclsgfmgmdipppsgplwilgdvfigryytvfdrdnnrvgfaea
a
>e1lyb.1a 2.38.1.2.12 Cathepsin D {human (Homo sapiens)}
gpipevlknymdaqyygeigigtppqcftvvfdtgssnlwvpsihcklldiacwihhkyn
sdksstyvkngtsfdihygsgslsgylsqdtvsvpcq
>e1lyb.1b 2.38.1.2.12 Cathepsin D {human (Homo sapiens)}
ggvkverqvfgeatkqpgitfiaakfdgilgmayprisvnnvlpvfdnlmqqklvdqnif
sfylsrdpdaqpggelmlggtdskyykgslsylnvtrkaywqvhldqvevasgltlckeg
ceaivdtgtslmvgpvdevrelqkaigavpliqgeymipcekvstlpaitlklggkgykl
spedytlkvsqagktlclsgfmgmdipppsgplwilgdvfigryytvfdrdnnrvgfaea
a
>e1lyb.2c 2.38.1.2.12 Cathepsin D {human (Homo sapiens)}
gpipevlknymdaqyygeigigtppqcftvvfdtgssnlwvpsihcklldiacwihhkyn
sdksstyvkngtsfdihygsgslsgylsqdtvsvpcq
>e1lyb.2d 2.38.1.2.12 Cathepsin D {human (Homo sapiens)}
ggvkverqvfgeatkqpgitfiaakfdgilgmayprisvnnvlpvfdnlmqqklvdqnif
sfylsrdpdaqpggelmlggtdskyykgslsylnvtrkaywqvhldqvevasgltlckeg
ceaivdtgtslmvgpvdevrelqkaigavpliqgeymipcekvstlpaitlklggkgykl
spedytlkvsqagktlclsgfmgmdipppsgplwilgdvfigryytvfdrdnnrvgfaea
a
>d1lyd__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d1lye__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvivk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1lyf__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvisk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1lyg__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvink
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1lyh__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvigk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1lyi__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvidk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1lyj__ 4.2.1.3.1 Phage T4 lysozyme {(Escherichia coli infected with bacteriophage T4)}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngviak
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1lyla1 2.29.4.1.4 (14-153) Lysyl-tRNA synthetase (LysRS) {(Escherichia coli, lysU) gene}
fndelrnrreklaalrqqgvafpndfrrdhtsdqlheefdakdnqeleslnievsvagrm
mtrrimgkasfvtlqdvggriqlyvardslpegvyndqfkkwdlgdiigargtlfktqtg
elsihctelrlltkalrplp
>d1lyla2 4.61.1.1.2 (161-502) Lysyl-tRNA synthetase (LysRS) {(Escherichia coli, LysU) gene}
dqevryrqryldliandksrqtfvvrskilaairqfmvargfmevetpmmqvipggasar
pfithhnaldldmylriapelylkrlvvggfervfeinrnfrnegisvrhnpeftmmely
mayadyhdlielteslfrtlaqevlgttkvtygehvfdfgkpfekltmreaikkyrpetd
madldnfdaakalaesigitvekswglgrivteifdevaeahliqptfiteypaevspla
rrndvnpeitdrfeffiggreigngfselndaedqaerfqeqvnakaagddeamfydedy
vtaleyglpptaglgigidrmimlftnshtirdvilfpamrp
>d1lylb1 2.29.4.1.4 (14-153) Lysyl-tRNA synthetase (LysRS) {(Escherichia coli, lysU) gene}
fndelrnrreklaalrqqgvafpndfrrdhtsdqlheefdakdnqeleslnievsvagrm
mtrrimgkasfvtlqdvggriqlyvardslpegvyndqfkkwdlgdiigargtlfktqtg
elsihctelrlltkalrplp
>d1lylb2 4.61.1.1.2 (154-502) Lysyl-tRNA synthetase (LysRS) {(Escherichia coli, LysU) gene}
dkfhglqdqevryrqryldliandksrqtfvvrskilaairqfmvargfmevetpmmqvi
pggasarpfithhnaldldmylriapelylkrlvvggfervfeinrnfrnegisvrhnpe
ftmmelymayadyhdlielteslfrtlaqevlgttkvtygehvfdfgkpfekltmreaik
kyrpetdmadldnfdaakalaesigitvekswglgrivteifdevaeahliqptfiteyp
aevsplarrndvnpeitdrfeffiggreigngfselndaedqaerfqeqvnakaagddea
mfydedyvtaleyglpptaglgigidrmimlftnshtirdvilfpamrp
>d1lylc1 2.29.4.1.4 (14-153) Lysyl-tRNA synthetase (LysRS) {(Escherichia coli, lysU) gene}
fndelrnrreklaalrqqgvafpndfrrdhtsdqlheefdakdnqeleslnievsvagrm
mtrrimgkasfvtlqdvggriqlyvardslpegvyndqfkkwdlgdiigargtlfktqtg
elsihctelrlltkalrplp
>d1lylc2 4.61.1.1.2 (161-502) Lysyl-tRNA synthetase (LysRS) {(Escherichia coli, LysU) gene}
dqevryrqryldliandksrqtfvvrskilaairqfmvargfmevetpmmqvipggasar
pfithhnaldldmylriapelylkrlvvggfervfeinrnfrnegisvrhnpeftmmely
mayadyhdlielteslfrtlaqevlgttkvtygehvfdfgkpfekltmreaikkyrpetd
madldnfdaakalaesigitvekswglgrivteifdevaeahliqptfiteypaevspla
rrndvnpeitdrfeffiggreigngfselndaedqaerfqeqvnakaagddeamfydedy
vtaleyglpptaglgigidrmimlftnshtirdvilfpamrp
>d1lyna_ 1.18.1.1.1 Lysin {red abalone (Haliotis rufescens)}
flnkafevalkvqiiagfdrglvkwlrvhgrtlstvqkkalyfvnrrymqthwanymlwi
nkkidalgrtpvvgdytrlgaeigrridmayfydflkdknmipkylpymeeinrmrpadv
pvkym
>d1lynb_ 1.18.1.1.1 Lysin {red abalone (Haliotis rufescens)}
flnkafevalkvqiiagfdrglvkwlrvhgrtlstvqkkalyfvnrrymqthwanymlwi
nkkidalgrtpvvgdytrlgaeigrridmayfydflkdknmipkylpymeeinrmrpadv
pvkym
>d1lyo__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1lysa_ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1lysb_ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1lyy__ 4.2.1.2.8 Lysozyme {human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcnhgktpgavnachlscsallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1lyz__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1lz1__ 4.2.1.2.8 Lysozyme {human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1lz2__ 4.2.1.2.2 Lysozyme {turkey (Meleagris gallopavo)}
kvygrcelaaamkrlgldnyrgyslgnwvcaakfesnfnthatnrntngstdygilqins
rwwcdngrtpgsrnlcnipcsallssditasvncakkiasggdgmnawvawrnrckgtdv
hawirgcrl
>d1lz3__ 4.2.1.2.2 Lysozyme {turkey (Meleagris gallopavo)}
kvygrcelaaamkrlgldnyrgyslgnwvcaakfesnfdthatnrntdgstdygilqins
rwwcndgrtpgsknlcnipcsallssditasvncakkiasggdgmnawvawrnrckgtdv
hawirgcrl
>d1lz4__ 4.2.1.2.8 Lysozyme {human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnaahlscsallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1lz5__ 4.2.1.2.8 Lysozyme {human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavrgdsnachlscsallqdniadavacakrvvrdpqgirawvawrnrc
qnrdvrqyvqgcgv
>d1lz6__ 4.2.1.2.8 Lysozyme {human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavtgrgdspanachlscsallqdniadavacakrvvrdpqgirawvaw
rnrcqnrdvrqyvqgcgv
>d1lza__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1lzb__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1lzc__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1lzd__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rywcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1lze__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rywcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1lzg__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rfwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1lzha_ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1lzhb_ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1lzr__ 4.2.1.2.8 Lysozyme {human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1lzsa_ 4.2.1.2.8 Lysozyme {human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1lzsb_ 4.2.1.2.8 Lysozyme {human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1lzt__ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1lzy__ 4.2.1.2.2 Lysozyme {turkey (Meleagris gallopavo)}
kvygrcelaaamkrlgldnyrgyslgnwvcaakfesnfnthatnrntdgstdygilqins
rwwcndgrtpgsknlcnipcsallssditasvncakkiasggngmnawvawrnrckgtdv
hawirgcrl
>d1maca_ 2.21.1.2.3 Bacillus 1-3,1-4-beta-glucanase {(Bacillus macerans)}
gsvfweplsyfnpstwekadgysnggvfnctwrannvnftndgklklgltssaynkfdca
eyrstniygyglyevsmkpakntgivssfftytgpahgtqwdeidieflgkdttkvqfny
ytngvgghekvislgfdaskgfhtyafdwqpgyikwyvdgvlkhtatanipstpgkimmn
lwngtgvddwlgsynganplyaeydwvkytsn
>d1macb_ 2.21.1.2.3 Bacillus 1-3,1-4-beta-glucanase {(Bacillus macerans)}
gsvfweplsyfnpstwekadgysnggvfnctwrannvnftndgklklgltssaynkfdca
eyrstniygyglyevsmkpakntgivssfftytgpahgtqwdeidieflgkdttkvqfny
ytngvgghekvislgfdaskgfhtyafdwqpgyikwyvdgvlkhtatanipstpgkimmn
lwngtgvddwlgsynganplyaeydwvkytsn
>d1maeh_ 2.51.2.1.2 Methylamine dehydrogenase, H-chain {gram negative methylotrophic bacteria (thiobacillus versutus)}
ssasaaaaaaaaalaagaadgptndeapgadgrrsyinlpahhsaiiqqwvldagsgsil
ghvnggflpnpvaahsgsefalastsfsriakgkrtdyvevfdpvtflpiadielpdapr
fdvgpyswmnantpnnadllffqfaagpavglvvqggssddqllssptcyhihpgapstf
yllcaqgglaktdhaggaagaglvgamltaaqnlltqpaqanksgrivwpvysgkilqad
isaagatnkapidalsggrkadtwrpggwqqvaylkssdgiylltseqsawklhaaakev
tsvtglvgqtssqislghdvdaisvaqdggpdlyalsagtevlhiydagagdqdqstvel
gsgpqvlsvmnea
>d1mael_ 7.20.1.1.2 Methylamine dehydrogenase {gram negative methylotrophic bacteria (thiobacillus versutus)}
vdprakwqpqdndiqacdywrhcsidgnicdcsggsltncppgtklataswvascynptd
gqsyliayrdccgynvsgrcpclntegelpvyrpefandiiwcfgaeddamtyhctispi
vgka
>d1mafh_ 2.51.2.1.2 Methylamine dehydrogenase, H-chain {gram negative methylotrophic bacteria (thiobacillus versutus)}
ssasaaaaaaaaalaagaadgptndeapgadgrrsyinlpahhsaiiqqwvldagsgsil
ghvnggflpnpvaahsgsefalastsfsriakgkrtdyvevfdpvtflpiadielpdapr
fdvgpyswmnantpnnadllffqfaagpavglvvqggssddqllssptcyhihpgapstf
yllcaqgglaktdhaggaagaglvgamltaaqnlltqpaqanksgrivwpvysgkilqad
isaagatnkapidalsggrkadtwrpggwqqvaylkssdgiylltseqsawklhaaakev
tsvtglvgqtssqislghdvdaisvaqdggpdlyalsagtevlhiydagagdqdqstvel
gsgpqvlsvmnea
>d1mafl_ 7.20.1.1.2 Methylamine dehydrogenase {gram negative methylotrophic bacteria (thiobacillus versutus)}
vdprakwqpqdndiqacdywrhcsidgnicdcsggsltncppgtklataswvascynptd
gqsyliayrdccgynvsgrcpclntegelpvyrpefandiiwcfgaeddamtyhctispi
vgka
>d1maha_ 3.56.1.1.3 Acetylcholinesterase {Murine (Mus musculus)}
edpqllvrvrggqlrgirlkapggpvsaflgipfaeppvgsrrfmppepkrpwsgvldat
tfqnvcyqyvdtlypgfegtemwnpnrelsedclylnvwtpyprpasptpvliwiygggf
ysgaasldvydgrflaqvegavlvsmnyrvgtfgflalpgsreapgnvglldqrlalqwv
qeniaafggdpmsvtlfgesagaasvgmhilslpsrslfhravlqsgtpngpwatvsage
arrratllarlvgcppggaggndteliaclrtrpaqdlvdhewhvlpqesifrfsfvpvv
dgdflsdtpealintgdfqdlqvlvgvvkdegsyflvygvpgfskdneslisraqflagv
rigvpqasdlaaeavvlhytdwlhpedpthlrdamsavvgdhnvvcpvaqlagrlaaqga
rvyayifehrastltwplwmgvphgyeiefifglpldpslnytteerifaqrlmkywtnf
artgdpndprdskspqwppyttaaqqyvslnlkplevrrglraqtcafwnrflpkllsat
>d1mahf_ 7.6.1.1.3 Fasciculin {green mamba (Dendroaspis angusticeps)}
tmcyshtttsrailtncgenscyrksrrhppkmvlgrgcgcppgddnlevkcctspdkcn
y
>d1mai__ 2.41.1.1.1 Phospholipase C delta-1 {Rat (Rattus norvegicus)}
glqddpdlqallkgsqllkvkssswrrerfyklqedcktiwqesrkvmrspesqlfsied
iqevrmghrteglekfardipedrcfsivfkdqrntldliapspadaqhwvqglrkiih
>d1maj__ 2.1.1.1.18 Immunoglobulin (variable domains of L and H chains) {Fab 26-10 (mouse), kappa L chain}
dvvmtqtplslpvslgdqasiscrssqslvhsngntylnwylqkagqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgiyfcsqtthvpptfgggtkleikr
>d1mak__ 2.1.1.1.18 Immunoglobulin (variable domains of L and H chains) {Fab 26-10 (mouse), kappa L chain}
dvvmtqtplslpvslgdqasiscrssqslvhsngntylnwylqkagqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgiyfcsqtthvpptfgggtkleikr
>d1mal__ 6.7.1.2.1 Maltoporin (also LamB protein) {(Escherichia coli)}
vdfhgyarsgigwtgsggeqqcfqttgaqskyrlgnecetyaelklgqevwkegdksfyf
dtnvaysvaqqndweatdpafreanvqgknliewlpgstiwagkrfyqrhdvhmidfyyw
disgpgaglenidvgfgklslaatrsseaggsssfasnniydytnetandvfdvrlaqme
inpggtlelgvdygranlrdnyrlvdgaskdgwlftaehtqsvlkgfnkfvvqyatdsmt
sqgkglsqgsgvafdnekfayninnnghmlrildhgaismgdnwdmmyvgmyqdinwdnd
ngtkwwtvgirpmykwtpimstvmeigydnvesqrtgdknnqykitlaqqwqagdsiwsr
pairvfatyakwdekwgydytgnadnnanfgkavpadfnggsfgrgdsdewtfgaqmeiw
w
>d1mamh1 2.1.1.1.29 (1-119) Immunoglobulin (variable domains of L and H chains) {Fab Yst9.1 (mouse), kappa L chain}
evklvesggglvqpggslrlscatsgftftdyymswvrqppgkalewlgfirnkadgytt
eysasvkgrftisrdnsqsilylqmntlraedsatyyctrdpygpaaywgqgtlvtvsa
>d1mamh2 2.1.1.2.37 (120-217) Immunoglobulin (constant domains of L and H chains) {Fab Yst9.1 (mouse), kappa L chain}
akttppsvyplapgcgdttgssvtlgclvkgyfpesvtvtwnsgslsssvhtfpallqsg
lytmsssvtvpsstwpsqtvtcsvahpassttvdkkle
>d1maml1 2.1.1.1.29 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab Yst9.1 (mouse), kappa L chain}
diqmtqttsslsaslgdrvtiscrasqdiynylnwyqqkpdgtvklliyytsrlhsgvps
rfsgsgsgtdysltisnlnqedmatyicqqgntlpftfgsgtkleikr
>d1maml2 2.1.1.2.37 (109-214) Immunoglobulin (constant domains of L and H chains) {Fab Yst9.1 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1map__ 3.54.1.1.1 Aspartate aminotransferase {chicken (Gallus gallus) mitochondria}
sswwshvemgppdpilgvteafkrdtnskkmnlgvgayrddngkpyvlncvrkaeamiaa
kkmdkeylpiagladftrasaelalgenseafksgryvtvqgisgtgslrvganflqrff
kfsrdvylpkpswgnhtpifrdaglqlqayryydpktcsldftgamediskipeksiill
hacahnptgvdprqeqwkelasvvkkrnllayfdmayqgfasgdinrdawalrhfieqgi
dvvlsqsyaknmglygeragaftvicrdaeeakrvesqlkilirpmysnppmngariasl
ilntpelrkewlvevkgmadriismrtqlvsnlkkegsshnwqhitdqigmfcftglkpe
qverltkefsiymtkdgrisvagvassnvgylahaihqvtk
>d1maq__ 3.54.1.1.1 Aspartate aminotransferase {chicken (Gallus gallus) mitochondria}
sswwshvemgppdpilgvteafkrdtnskkmnlgvgayrddngkpyvlncvrkaeamiaa
kkmdkeylpiagladftrasaelalgenseafksgryvtvqgisgtgslrvganflqrff
kfsrdvylpkpswgnhtpifrdaglqlqayryydpktcsldftgamediskipeksiill
hacahnptgvdprqeqwkelasvvkkrnllayfdmayqgfasgdinrdawalrhfieqgi
dvvlsqsyaknmglygeragaftvicrdaeeakrvesqlkilirpmysnppmngariasl
ilntpelrkewlvevkgmadriismrtqlvsnlkkegsshnwqhitdqigmfcftglkpe
qverltkefsiymtkdgrisvagvassnvgylahaihqvtk
>d1mar__ 3.1.5.1.2 Aldose reductase (aldehyde reductase) {human (Homo sapiens)}
asrlllnngakmpilglgtwksppgqvteavkvaidvgyrhidcahvyqnenevgvaiqe
klreqvvkreelfivsklwctyhekglvkgacqktlsdlkldyldlylihwptgfkpgke
ffpldesgnvvpsdtnildtwaameelvdeglvkaigisnfnhlqvemilnkpglkykpa
vnqiechpyltqekliqycqskgivvtaysplgspdrpwakpedpslledprikaiaakh
nkttaqvlirfpmqrnlvvipksvtperiaenfkvfdfelssqdmttllsynrnwrvcal
lsctshkdypfheef
>d1masa_ 3.57.1.1.1 Inosine-uridine nucleoside N-ribohydrolase, IU-NH {(Crithidia fasciculata)}
akkiildcdpglddavaillahgnpeiellaittvvgnqtlakvtrnaqlvadiagitgv
piaagcdkplvrkimtaghihgesgmgtvaypaefknkvderhavnliidlvmshepkti
tlvptggltniamaarleprivdrvkevvlmgggyhegnatsvaefniiidpeaahivfn
eswqvtmvgldlthqalatppilqrvkevdtnparfmleimdyytkiyqsnrymaaaavh
dpcavayvidpsvmttervpvdieltgkltlgmtvadfrnprpehchtqvavkldfekfw
glvldalerigdpq
>d1masb_ 3.57.1.1.1 Inosine-uridine nucleoside N-ribohydrolase, IU-NH {(Crithidia fasciculata)}
akkiildcdpglddavaillahgnpeiellaittvvgnqtlakvtrnaqlvadiagitgv
piaagcdkplvrkimtaghihgesgmgtvaypaefknkvderhavnliidlvmshepkti
tlvptggltniamaarleprivdrvkevvlmgggyhegnatsvaefniiidpeaahivfn
eswqvtmvgldlthqalatppilqrvkevdtnparfmleimdyytkiyqsnrymaaaavh
dpcavayvidpsvmttervpvdieltgkltlgmtvadfrnprpehchtqvavkldfekfw
glvldalerigdpq
>d1mat__ 4.77.1.1.2 Methionine aminopeptidase {(Escherichia coli)}
aisiktpediekmrvagrlaaevlemiepyvkpgvstgeldricndyivneqhavsaclg
yhgypksvcisinevvchgipddakllkdgdivnidvtvikdgfhgdtskmfivgkptim
gerlcritqeslylalrmvkpginlreigaaiqkfveaegfsvvreycghgigrgfheep
qvlhydsretnvvlkpgmtftiepmvnagkkeirtmkdgwtvktkdrslsaqyehtivvt
dngceiltlrkddtipaiishde
>d1max__ 2.35.1.2.1 Trypsin(ogen) {bovine (Bos taurus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1may__ 2.35.1.2.1 Trypsin(ogen) {bovine (Bos taurus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1maz__ 6.1.4.1.1 Apoptosis regulator Bcl-xL {Human (Homo sapiens)}
msqsnrelvvdflsyklsqkgyswsqfsdveenrteapegtesemetpsaingnpswhla
dspavngatghsssldarevipmaavkqalreagdefelryrrafsdltsqlhitpgtay
qsfeqvvnelfrdgvnwgrivaffsfggalcvesvdkemqvlvsriaawmatylndhlep
wiqenggwdtfvelyg
>d1mba__ 1.1.1.1.5 Myoglobin {sea hare (Aplysia limacina)}
xslsaaeadlagkswapvfanknangldflvalfekfpdsanffadfkgksvadikaspk
lrdvssriftrlnefvnnaanagkmsamlsqfakehvgfgvgsaqfenvrsmfpgfvasv
aappagadaawtklfgliidalkaaga
>d1mbb_1 4.90.1.2.1 (3-200) Uridine diphospho-N-Acetylenolpyruvylglucosamine reductase (MurB), N-terminal domain {(Escherichia coli)}
hslkpwntfgidhnaqhivcaedeqqllnawqyataegqpvlilgegsnvlfledyrgtv
iinrikgieihdepdawylhvgagenwhrlvkytlqegmpglenlalipgcvgsspiqni
gaygvelqrvcayvdsvelatgkqvrltakecrfgyrdsifkheyqdrfaivavglrlpk
ewqpvltygdltrldptt
>d1mbb_2 4.91.1.1.1 (201-342) Uridine diphospho-N-Acetylenolpyruvylglucosamine reductase, MurB, C-terminal domain {(Escherichia coli)}
vtpqqvfnavchmrttklpdpkvngnagsffknpvvsaetakallsqfptapnypqadgs
vklaagwlidqcqlkgmqiggaavhrqqalvlinednaksedvvqlahhvrqkvgekfnv
wlepevrfigasgevsavetis
>d1mbc__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgyqg
>d1mbd__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgyqg
>d1mbe__ 1.4.1.3.2 c-Myb, DNA-binding domain {mouse (Mus musculus)}
lgktrwtreedeklkklveqngtddwkvianylpnrtdvqcqhrwqkvlnpe
>d1mbf__ 1.4.1.3.2 c-Myb, DNA-binding domain {mouse (Mus musculus)}
lgktrwtreedeklkklveqngtddwkvianylpnrtdvqcqhrwqkvlnpe
>d1mbg__ 1.4.1.3.2 c-Myb, DNA-binding domain {mouse (Mus musculus)}
likgpwtkeedqrvielvqkygpkrwsviakhlkgrigkqcrerwhnhlnpe
>d1mbh__ 1.4.1.3.2 c-Myb, DNA-binding domain {mouse (Mus musculus)}
likgpwtkeedqrvielvqkygpkrwsviakhlkgrigkqcrerwhnhlnpe
>d1mbi__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgyqg
>d1mbj__ 1.4.1.3.2 c-Myb, DNA-binding domain {mouse (Mus musculus)}
vkktswteeedriiyqahkrlgnrwaeiakllpgrtdnaiknhwnstmrrkv
>d1mbk__ 1.4.1.3.2 c-Myb, DNA-binding domain {mouse (Mus musculus)}
vkktswteeedriiyqahkrlgnrwaeiakllpgrtdnaiknhwnstmrrkv
>d1mbla_ 5.4.1.1.4 beta-Lactamase, class A {(Bacillus licheniformis)}
ddfakleeqfdaklgifaldtgtnrtvayrpderfafastikaltvgvllqqksiedlnq
ritytrddlvnynpitekhvdtgmtlkeladaslrysdnaaqnlilkqiggpeslkkelr
kigdevtnperfapelnevnpgetqdtstaralvtslrafaledklpsekrellidwmkr
nttgdaliragvpdgwevadktgaasygtrndiaiiwppkgdpvvlavlssrdkkdakyd
dkliaeatkvvmkaln
>d1mblb_ 5.4.1.1.4 beta-Lactamase, class A {(Bacillus licheniformis)}
ddfakleeqfdaklgifaldtgtnrtvayrpderfafastikaltvgvllqqksiedlnq
ritytrddlvnynpitekhvdtgmtlkeladaslrysdnaaqnlilkqiggpeslkkelr
kigdevtnperfapelnevnpgetqdtstaralvtslrafaledklpsekrellidwmkr
nttgdaliragvpdgwevadktgaasygtrndiaiiwppkgdpvvlavlssrdkkdakyd
dkliaeatkvvmkaln
>d1mbn__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgyqg
>d1mbo__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgyqg
>d1mbs__ 1.1.1.1.6 Myoglobin {common seal (Phoca vitulina)}
glsdgewhlvlnvwgkvetdlaghgqevlirlfkshpetlekfdkfkhlkseddmrrsed
lrkhgntvltalggilkkkghheaelkplaqshatkhkipikylefiseaiihvlhskhp
aefgadaqaamkkalelfrndiaakykelgfhg
>d1mbt_1 4.90.1.2.1 (3-200) Uridine diphospho-N-Acetylenolpyruvylglucosamine reductase (MurB), N-terminal domain {(Escherichia coli)}
hslkpwntfgidhnaqhivcaedeqqllnawqyataegqpvlilgegsnvlfledyrgtv
iinrikgieihdepdawylhvgagenwhrlvkytlqegmpglenlalipgcvgsspiqni
gaygvelqrvcayvdsvelatgkqvrltakecrfgyrdsifkheyqdrfaivavglrlpk
ewqpvltygdltrldptt
>d1mbt_2 4.91.1.1.1 (201-342) Uridine diphospho-N-Acetylenolpyruvylglucosamine reductase, MurB, C-terminal domain {(Escherichia coli)}
vtpqqvfnavchmrttklpdpkvngnagsffknpvvsaetakallsqfptapnypqadgs
vklaagwlidqcqlkgmqiggaavhrqqalvlinednaksedvvqlahhvrqkvgekfnv
wlepevrfigasgevsavetis
>d1mcba1 2.1.1.1.117 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvpdrfsgs
ksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mcba2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mcbb1 2.1.1.1.117 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvpdrfsgs
ksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mcbb2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mcca1 2.1.1.1.117 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvpdrfsgs
ksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mcca2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mccb1 2.1.1.1.117 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvpdrfsgs
ksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mccb2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mcda1 2.1.1.1.117 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvpdrfsgs
ksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mcda2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mcdb1 2.1.1.1.117 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvpdrfsgs
ksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mcdb2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mcea1 2.1.1.1.117 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvpdrfsgs
ksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mcea2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mceb1 2.1.1.1.117 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvpdrfsgs
ksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mceb2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mcfa1 2.1.1.1.117 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvpdrfsgs
ksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mcfa2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mcfb1 2.1.1.1.117 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvpdrfsgs
ksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mcfb2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mcha1 2.1.1.1.117 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvpdrfsgs
ksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mcha2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mchb1 2.1.1.1.117 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvpdrfsgs
ksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mchb2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mcia1 2.1.1.1.117 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvpdrfsgs
ksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mcia2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mcib1 2.1.1.1.117 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvpdrfsgs
ksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mcib2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mcja1 2.1.1.1.117 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvpdrfsgs
ksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mcja2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mcjb1 2.1.1.1.117 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvpdrfsgs
ksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mcjb2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mcka1 2.1.1.1.117 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvpdrfsgs
ksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mcka2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mckb1 2.1.1.1.117 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvpdrfsgs
ksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mckb2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mcla1 2.1.1.1.117 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvpdrfsgs
ksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mcla2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mclb1 2.1.1.1.117 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvpdrfsgs
ksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mclb2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mcna1 2.1.1.1.117 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvpdrfsgs
ksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mcna2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mcnb1 2.1.1.1.117 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvpdrfsgs
ksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mcnb2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mcoh1 2.1.1.1.116 (1-117) Immunoglobulin (variable domains of L and H chains) {Intact antibody (lambda) MCG (human)}
plvlqesgpglvkpsealsltctvsgdsintilyywswirqppgkglewigyiyysgsty
gnpslksrvtisvntsknqfysklssvtaadtavyycarvplvvnpwgqgtlvtvss
>d1mcoh2 2.1.1.2.104 (118-219) Immunoglobulin (constant domains of L and H chains) {Intact antibody (lambda) MCG (human)}
astkgpsvfplapsskstsggtaalgclvkdyfpqpvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkrvapel
>d1mcoh3 2.1.1.2.104 (220-327) Immunoglobulin (constant domains of L and H chains) {Intact antibody (lambda) MCG (human)}
lggpsvflfppkpkdtlmisrtpevtcvvvdvshedpqvkfnwyvdgvqvhnaktkpreq
qynstyrvvsvltvlhqnwldgkeykckvsnkalpapiektiskakgq
>d1mcoh4 2.1.1.2.104 (328-428) Immunoglobulin (constant domains of L and H chains) {Intact antibody (lambda) MCG (human)}
prepqvytlppsreemtknqvsltclvkgfypsdiavewesngqpennykttppvldsdg
sfflyskltvdksrwqqgnvfscsvmhealhnhytqkslsl
>d1mcol1 2.1.1.1.116 (1-111) Immunoglobulin (variable domains of L and H chains) {Intact antibody (lambda) MCG (human)}
psaltqppsasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgv
pdrfsgsksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mcol2 2.1.1.2.104 (112-216) Immunoglobulin (constant domains of L and H chains) {Intact antibody (lambda) MCG (human)}
qpkanptvtlfppsseelqankatevclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mcph1 2.1.1.1.25 (1-121) Immunoglobulin (variable domains of L and H chains) {Fab MCPC603 (human), kappa L chain}
evklvesggglvqpggslrlscatsgftfsdfymewvrqppgkrlewiaasrnkgnkytt
eysasvkgrfivsrdtsqsilylqmnalraedtaiyycarnyygstwyfdvwgagttvtv
s
>d1mcph2 2.1.1.2.33 (122-222) Immunoglobulin (constant domains of L and H chains) {Fab MCPC603 (human), kappa L chain}
sesarnptiypltlppalssdpviigclihdyfpsgtmnvtwgksgkdittvnfppalas
ggrytmsnqltlpavecpegesvkcsvqhdsnpvqeldvnc
>d1mcpl1 2.1.1.1.25 (1-114) Immunoglobulin (variable domains of L and H chains) {Fab MCPC603 (human), kappa L chain}
divmtqspsslsvsagervtmsckssqsllnsgnqknflawyqqkpgqppklliygastr
esgvpdrftgsgsgtdftltissvqaedlavyycqndhsypltfgagtkleikr
>d1mcpl2 2.1.1.2.33 (115-220) Immunoglobulin (constant domains of L and H chains) {Fab MCPC603 (human), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1mcqa1 2.1.1.1.117 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvpdrfsgs
ksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mcqa2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mcqb1 2.1.1.1.117 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvpdrfsgs
ksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mcqb2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mcra1 2.1.1.1.117 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvpdrfsgs
ksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mcra2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mcrb1 2.1.1.1.117 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvpdrfsgs
ksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mcrb2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mcsa1 2.1.1.1.117 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvpdrfsgs
ksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mcsa2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mcsb1 2.1.1.1.117 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvpdrfsgs
ksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mcsb2 2.1.1.2.105 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mcta_ 2.35.1.2.2 Trypsin(ogen) {porcine (Sus scrofa)}
ivggytcaansipyqvslnsgshfcggslinsqwvvsaahcyksriqvrlgehnidvleg
neqfinaakiithpnfngntldndimliklsspatlnsrvatvslprscaaagteclisg
wgntkssgssypsllqclkapvlsnssckssypgqitgnmicvgflqggkdscqgdsggp
vvcngqlqgivswgygcaqknkpgvytkvcnyvnwiqqtiaan
>d1mcti_ 7.3.2.1.1 Trypsin inhibitor {bitter gourd (Momordica charantia, linn. cucurbitaceae) seed}
ricpriwmectrdsdcmakcicvaghcg
>d1mcwm1 2.1.1.1.118 (1-111) Immunoglobulin (variable domains of L and H chains) {Heterologous L chain dimer MCG-WEIR hybrid (human)}
xsaltqppsasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgv
pdrfsgsksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mcwm2 2.1.1.2.106 (112-216) Immunoglobulin (constant domains of L and H chains) {Heterologous L chain dimer MCG-WEIR hybrid (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mcww1 2.1.1.1.118 (1-111) Immunoglobulin (variable domains of L and H chains) {Heterologous L chain dimer MCG-WEIR hybrid (human)}
xsaltqpasvsgspgqsitvscaghtsdvadsnsiswfqqhpdkapklliyavtfrpsgi
plrfsgsksgntasltisgllpddeadyfcmsylsdasfvfgsgtkvtvlr
>d1mcww2 2.1.1.2.106 (112-216) Immunoglobulin (constant domains of L and H chains) {Heterologous L chain dimer MCG-WEIR hybrid (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspveagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1mcy__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdifirlfkshpetlekfdrfkhlkteaemkase
dlkkqgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgdfgadaqgamnkalelfrkdiaakykelgyqg
>d1mdaa_ 2.5.1.1.1 Amicyanin {(Paracoccus denitrificans)}
atipsespfaaaevadgaivvdiakmkyetpelhvkvgdtvtwinreamphnvhfvagvl
geaalkgpmmkkeqaysltfteagtydyhctphpfmrgkvvve
>d1mdab_ 2.5.1.1.1 Amicyanin {(Paracoccus denitrificans)}
atipsespfaaaevadgaivvdiakmkyetpelhvkvgdtvtwinreamphnvhfvagvl
geaalkgpmmkkeqaysltfteagtydyhctphpfmrgkvvve
>d1mdah_ 2.51.2.1.1 Methylamine dehydrogenase, H-chain {(Paracoccus denitrificans)}
ekskvagsaaaasaaaasdgsscdhgpgaisrrshitlpayfagttenwvscagcgvtlg
hslgaflslavaghsgsdfalastsfarsakgkrtdyvevfdpvtflpiadielpdaprf
svgprvhiigncassacllfflfgssaaaglsvpgasddqltksascfhihpgaaathyl
gscpaslaasdlaaapaaagivgaqctgaqncssqaaqanypgmlvwavassilqgdipa
agatmkaaidgnesgrkadnfrsagfqmvaklkntdgimiltvehsrsclaaaentssvt
asvgqtsgpisnghdsdaiiaaqdgasdnyansagtevldiydaasdqdqssveldkgpe
slsvqnea
>d1mdaj_ 2.51.2.1.1 Methylamine dehydrogenase, H-chain {(Paracoccus denitrificans)}
ekskvagsaaaasaaaasdgsscdhgpgaisrrshitlpayfagttenwvscagcgvtlg
hslgaflslavaghsgsdfalastsfarsakgkrtdyvevfdpvtflpiadielpdaprf
svgprvhiigncassacllfflfgssaaaglsvpgasddqltksascfhihpgaaathyl
gscpaslaasdlaaapaaagivgaqctgaqncssqaaqanypgmlvwavassilqgdipa
agatmkaaidgnesgrkadnfrsagfqmvaklkntdgimiltvehsrsclaaaentssvt
asvgqtsgpisnghdsdaiiaaqdgasdnyansagtevldiydaasdqdqssveldkgpe
slsvqnea
>d1mdal_ 7.20.1.1.1 Methylamine dehydrogenase {(Paracoccus denitrificans)}
vdprakwqpqdndiqacdywrhcsiagnicdcsagsltscppgtlvasgswvgscynppd
pnkyitayrdccgynvsgrcaclntegelpvynkdandiiwcfggedgmtyhcsispvsg
a
>d1mdam_ 7.20.1.1.1 Methylamine dehydrogenase {(Paracoccus denitrificans)}
vdprakwqpqdndiqacdywrhcsiagnicdcsagsltscppgtlvasgswvgscynppd
pnkyitayrdccgynvsgrcaclntegelpvynkdandiiwcfggedgmtyhcsispvsg
a
>d1mdc__ 2.45.1.2.4 Fatty acid-binding protein {tobacco hornworm (Manduca sexta l.)}
xsylgkvyslvkqenfdgflksaglsddkiqalvsdkptqkmeangdsysntstggggak
tvsfksgvefddvigagdsvksmytvdgnvvthvvkgdagvatfkkeyngddlvvtitss
nwdgvarryyka
>d1mdia_ 3.38.1.1.4 Thioredoxin {human (Homo sapiens)}
mvkqiesktafqealdaagdklvvvdfsatwcgpakmikpffhslsekysnviflevdvd
daqdvaseaevkatptfqffkkgqkvgefsgankekleatinelv
>d1mdja_ 3.38.1.1.4 Thioredoxin {human (Homo sapiens)}
mvkqiesktafqealdaagdklvvvdfsatwcgpakmikpffhslsekysnviflevdvd
daqdvaseaevkatptfqffkkgqkvgefsgankekleatinelv
>d1mdka_ 3.38.1.1.4 Thioredoxin {human (Homo sapiens)}
mvkqiesktafqealdaagdklvvvdfsatwcgpakmikpffhslsekysnviflevdvd
daqdvaseaevkatptfqffkkgqkvgefsgankekleatinelv
>d1mdl_1 3.1.6.2.2 (133-359) Mandelate racemase {(Pseudomonas putida)}
pvqaydshsldgvklateravtaaelgfravktrigypaldqdlavvrsirqavgddfgi
mvdynqsldvpaaikrsqalqqegvtwieeptlqhdyeghqriqsklnvpvqmgenwlgp
eemfkalsigacrlampdamkiggvtgwirasalaqqfgipmsshlfqeisahllaatpt
ahwlerldlagsvieptltfeggnavipdlpgvgiiwrekeigkylv
>d1mdl_2 4.32.1.1.4 (3-132) Mandelate racemase {(Pseudomonas putida)}
evlitglrtravnvplaypvhtavgtvgtaplvlidlatsagvvghsylfaytpvalksl
kqllddmaamivneplapvsleamlakrfclagytglirmaaagidmaawdalgkvhetp
lvkllganar
>d1mdp1_ 3.82.1.1.6 D-maltodextrin-binding protein {(Escherichia coli)}
kieegklviwingdkgynglaevgkkfekdtgikvtvehpdkleekfpqvaatgdgpdii
fwahdrfggyaqsgllaeitpdkafqdklypftwdavryngkliaypiavealsliynkd
llpnppktweeipdpgksalmfnlqepyftwpliaadggyafkyengkydikdvgvdnag
akagltflvdliknkhmnadtdysiaeaafnkgetamtingpwawsnidtskvnygvtvl
ptfkgqpskpfvgvlsaginaaspnkelakeflenylltdegleavnkdkplgavalksy
eeelakdpriaatmenaqkgeimpnipqmsafwyavrtavinaasgrqtvdealkdaqtr
itk
>d1mdp2_ 3.82.1.1.6 D-maltodextrin-binding protein {(Escherichia coli)}
kieegklviwingdkgynglaevgkkfekdtgikvtvehpdkleekfpqvaatgdgpdii
fwahdrfggyaqsgllaeitpdkafqdklypftwdavryngkliaypiavealsliynkd
llpnppktweeipdpgksalmfnlqepyftwpliaadggyafkyengkydikdvgvdnag
akagltflvdliknkhmnadtdysiaeaafnkgetamtingpwawsnidtskvnygvtvl
ptfkgqpskpfvgvlsaginaaspnkelakeflenylltdegleavnkdkplgavalksy
eeelakdpriaatmenaqkgeimpnipqmsafwyavrtavinaasgrqtvdealkdaqtr
itk
>d1mdq__ 3.82.1.1.6 D-maltodextrin-binding protein {(Escherichia coli)}
kieegklviwingdkgynglaevgkkfekdtgikvtvehpdkleekfpqvaatgdgpdii
fwahdrfggyaqsgllaeitpdkafqdklypftwdavryngkliaypiavealsliynkd
llpnppktweeipaldkelkakgksalmfnlqepyftwpliaadggyafkyengkydikd
vgvdnagakagltflvdliknkhmnadtdysiaeaafnkgetamtingpwawsnidtskv
nygvtvlptfkgqpskpfvgvlsaginaaspnkelakeflenylltdegleavnkdkplg
gsvalksyeeelakdpriaatmenaqkgeimpnipqmsafwyavrtavinaasgrqtvde
alkdaqtritk
>d1mdr_1 3.1.6.2.2 (133-359) Mandelate racemase {(Pseudomonas putida)}
pvqaydshsldgvklateravtaaelgfravktkigypaldqdlavvrsirqavgddfgi
mvdynqsldvpaaikrsqalqqegvtwieeptlqhdyeghqriqsklnvpvqmgenwlgp
eemfkalsigacrlampdamkiggvtgwirasalaqqfgipmsshlfqeisahllaatpt
ahwlerldlagsvieptltfeggnavipdlpgvgiiwrekeigkylv
>d1mdr_2 4.32.1.1.4 (3-132) Mandelate racemase {(Pseudomonas putida)}
evlitglrtravnvplaypvhtavgtvgtaplvlidlatsagvvghsylfaytpvalksl
kqllddmaamivneplapvsleamlakrfclagytglirmaaagidmaawdalgkvhetp
lvkllganar
>d1mdta1 2.2.1.1.1 (381-535) Diphtheria toxin, C-terminal domain {(Corynebacterium diphtheriae)}
spghktqpflhdgyavswntvedsiirtgfqgesghdikitaentplpiagvllptipgk
ldvnkskthisvngrkirmrcraidgdvtfcrpkspvyvgngvhanlhvafhrsssekih
sneissdsigvlgyqktvdhtkvnsklslffeiks
>d1mdta2 4.103.1.1.3 (1-187) Diphtheria toxin, N-terminal domain {(Corynebacterium diphtheriae)}
gaddvvdssksfvmenfssyhgtkpgyvdsiqkgiqkpksgtqgnydddwkgfystdnky
daagysvdnenplsgkaggvvkvtypgltkvlalkvdnaetikkelglslteplmeqvgt
eefikrfgdgasrvvlslpfaegsssveyinnweqakalsveleinfetrgkrgqdamye
ymaqaca
>d1mdta3 6.1.2.1.1 (200-380) Diphtheria toxin, middle domain {(Corynebacterium diphtheriae)}
scinldwdvirdktktkieslkehgpiknkmsespnktvseekakqyleefhqtalehpe
lselktvtgtnpvfaganyaawavnvaqvidsetadnlekttaalsilpgigsvmgiadg
avhhnteeivaqsialsslmvaqaiplvgelvdigfaaynfvesiinlfqvvhnsynrpa
y
>d1mdtb1 2.2.1.1.1 (381-535) Diphtheria toxin, C-terminal domain {(Corynebacterium diphtheriae)}
spghktqpflhdgyavswntvedsiirtgfqgesghdikitaentplpiagvllptipgk
ldvnkskthisvngrkirmrcraidgdvtfcrpkspvyvgngvhanlhvafhrsssekih
sneissdsigvlgyqktvdhtkvnsklslffeiks
>d1mdtb2 4.103.1.1.3 (1-187) Diphtheria toxin, N-terminal domain {(Corynebacterium diphtheriae)}
gaddvvdssksfvmenfssyhgtkpgyvdsiqkgiqkpksgtqgnydddwkgfystdnky
daagysvdnenplsgkaggvvkvtypgltkvlalkvdnaetikkelglslteplmeqvgt
eefikrfgdgasrvvlslpfaegsssveyinnweqakalsveleinfetrgkrgqdamye
ymaqaca
>d1mdtb3 6.1.2.1.1 (200-380) Diphtheria toxin, middle domain {(Corynebacterium diphtheriae)}
scinldwdvirdktktkieslkehgpiknkmsespnktvseekakqyleefhqtalehpe
lselktvtgtnpvfaganyaawavnvaqvidsetadnlekttaalsilpgigsvmgiadg
avhhnteeivaqsialsslmvaqaiplvgelvdigfaaynfvesiinlfqvvhnsynrpa
y
>d1mdya_ 1.36.1.1.3 Myod B/HLH domain {mouse (Mus musculus)}
melkrkttnadrrkaatmrerrrlskvneafetlkrstssnpnqrlpkveilrnairyie
glqallrd
>d1mdyb_ 1.36.1.1.3 Myod B/HLH domain {mouse (Mus musculus)}
ttnadrrkaatmrerrrlskvneafetlkrstssnpnqrlpkveilrnairyieglqall
rd
>d1mdyc_ 1.36.1.1.3 Myod B/HLH domain {mouse (Mus musculus)}
ttnadrrkaatmrerrrlskvneafetlkrstssnpnqrlpkveilrnairyieglqall
rd
>d1mdyd_ 1.36.1.1.3 Myod B/HLH domain {mouse (Mus musculus)}
ttnadrrkaatmrerrrlskvneafetlkrstssnpnqrlpkveilrnairyieglqall
rd
>d1mea__ 7.35.1.1.1 Methionyl-tRNA synthetase (MetRS), Zn-domain {(Escherichia coli)}
gsdrfvkgtcpkckspdqygdncevcga
>d1mec1_ 2.8.1.4.11 Mengo virus {Host: monkey brain; middle size plaque variant}
gvenaekgvtentdatadfvaqpvylpenqtkvaffydrsspigrfavksgslesgfapf
snkacpnsviltpgpqfdpaydqlrpqrlteiwgngneetsevfplktkqdysfclfspf
vyykcdlevtlsphtsgahgllvrwcptgtptkpttqvlhevsslsegrtpqvysagpgt
snqisfvvpynsplsvlpavwynghkrfdntgdlgiapnsdfgtlffagtkpdikftvyl
ryknmrvfcprptvffpwptsgdkidmtpragvl
>d1mec2_ 2.8.1.4.11 Mengo virus {Host: monkey brain; middle size plaque variant}
dqnteemenlsdrvsqdtagntvtntqstvgrlvgygtvhdgehpascadtasekilave
ryytfkvndwtstqkpfeyiriplphvlsgedggvfgatlrrhylvktgwrvqvqcnasq
fhagsllvfmapeyptldvfamdnrwskdnlpngtrtqtnrkgpfamdhqnfwqwtlyph
qflnlrtnttvdlevpyvniaptsswtqhaswtlviavvapltystgastslditasiqp
vrpvfnglrhevlsrq
>d1mec3_ 2.8.1.4.11 Mengo virus {Host: monkey brain; middle size plaque variant}
spipvtirehagtwystlpdstvpiygktpvapanymvgeykdfleiaqiptfignkmpn
avpyieasntavktqplavyqvtlscsclantflaalsrnfaqyrgslvytfvftgtamm
kgkfliaytppgagkptsrdqamqatyaiwdlglnssysftvpfispthfrmvgtdqani
tnvdgwvtvwqltpltyppgcptsakiltmvsagkdfslkmpispapwspq
>d1med__ 7.35.1.1.1 Methionyl-tRNA synthetase (MetRS), Zn-domain {(Escherichia coli)}
gsdrfvkgtcpkckspdqygdncevcga
>d1meea_ 3.33.1.1.8 Messentericopeptidase {(Bacillus mesentericus)}
aqsvpygisqikapalhsqgytgsnvkvavidsgidsshpdlnvrggasfvpsetnpyqd
gsshgthvagtiaalnnsigvlgvapsaslyavkvldstgsgqyswiingiewaisnnmd
vinmslggptgstalktvvdkavssgivvaaaagnegssgststvgypakypstiavgav
nsanqrasfssagseldvmapgvsiqstlpggtygayngtsmatphvagaaalilskhpt
wtnaqvrdrlestatylgssfyygkglinvqaaaq
>d1meei_ 4.22.1.1.1 Eglin C {leech (Hirudo medicinalis)}
lksfpevvgktvdqareyftlhypqynvyflpegspvtldlrynrvrvfynpgtnvvnhv
phvg
>d1mef__ 2.29.4.5.1 Major cold shock protein {(Escherichia coli)}
msgkmtgivkwfnadkgfgfitpddgskdvfvhfsaiqndgyksldegqkvsftiesgak
gpaagnvtsl
>d1meg__ 4.3.1.1.3 Caricain (protease omega) {papaya (Carica papaya)}
lpenvdwrkkgavtpvrhqgscgscwafsavatveginkirtgklvelseqelvdcerrs
hgckggyppyaleyvakngihlrskypykakqgtcrakqvggpivktsgvgrvqpnnegn
llnaiakqpvsvvveskgrpfqlykggifegpcgtkvehavtavgygksggkgyilikns
wgtawgekgyirikrapgnspgvcglykssyyptkn
>d1mek__ 3.38.1.2.1 Protein disulfide isomerase, N-terminal domain {human (Homo sapiens)}
dapeeedhvlvlrksnfaealaahkyllvefyapwcghckalapeyakaagklkaegsei
rlakvdateesdlaqqygvrgyptikffrngdtaspkeytagreaddivnwlkkrtgpaa
>d1mela_ 2.1.1.1.106 Immunoglobulin (variable domains of L and H chains) {camel (Camelus dromedarius) single-domain VH antibody fragment}
vqlqasgggsvqaggslrlscaasgytigpycmgwfrqapgkeregvaainmgggityya
dsvkgrftisqdnakntvyllmnslepedtaiyycaadstiyasyyecghglstggygyd
swgqgtqvtvss
>d1melb_ 2.1.1.1.106 Immunoglobulin (variable domains of L and H chains) {camel (Camelus dromedarius) single-domain VH antibody fragment}
vqlqasgggsvqaggslrlscaasgytigpycmgwfrqapgkeregvaainmgggityya
dsvkgrftisqdnakntvyllmnslepedtaiyycaadstiyasyyecghglstggygyd
swgqgtqvtvss
>d1mell_ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgc
>d1melm_ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgc
>d1mema_ 4.3.1.1.12 Cathepsin K {Human (Homo sapiens)}
apdsvdyrkkgyvtpvknqgqcgscwafssvgalegqlkkktgkllnlspqnlvdcvsen
dgcgggymtnafqyvqknrgidsedaypyvgqeescmynptgkaakcrgyreipegneka
lkravarvgpvsvaidasltsfqfyskgvyydescnsdnlnhavlavgygiqkgnkhwii
knswgenwgnkgyilmarnknnacgianlasfpkm
>d1mera_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvnvigrnlltqigctlnf
>d1merb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvnvigrnlltqigctlnf
>d1mesa_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvnvigrnlltqigctlnf
>d1mesb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvnvigrnlltqigctlnf
>d1meta_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpfniigrnlltqigctlnf
>d1metb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpfniigrnlltqigctlnf
>d1meua_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpfnvigrnlltqigctlnf
>d1meub_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpfnvigrnlltqigctlnf
>d1mf2h1 2.1.1.1.86 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab F11.2.32 (mouse), kappa L chain}
dvqlvesggglvqpggsrklscaasgftfmrfgmhwvrqapekglewvayissgsstiyy
adtvkgrftisrdnpkntlflqmtslrsedtalyycarsggierydgtyyvmdywgqgts
vtvss
>d1mf2h2 2.1.1.2.88 (114-209) Immunoglobulin (constant domains of L and H chains) {Fab F11.2.32 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpssprpsetvtcnvahpasstkvdkkivprd
>d1mf2l1 2.1.1.1.86 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab F11.2.32 (mouse), kappa L chain}
dtvltqspaslavslgqratiscrasesvdyygksfmnwfqqkpgqppklliyaasnqgs
gvparfsgsgsgtdfslhihpmeeddsamyfcqqskevpwtfgggtkleik
>d1mf2l2 2.1.1.2.88 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab F11.2.32 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1mf2m1 2.1.1.1.86 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab F11.2.32 (mouse), kappa L chain}
dtvltqspaslavslgqratiscrasesvdyygksfmnwfqqkpgqppklliyaasnqgs
gvparfsgsgsgtdfslhihpmeeddsamyfcqqskevpwtfgggtkleik
>d1mf2m2 2.1.1.2.88 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab F11.2.32 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1mf2n1 2.1.1.1.86 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab F11.2.32 (mouse), kappa L chain}
dvqlvesggglvqpggsrklscaasgftfmrfgmhwvrqapekglewvayissgsstiyy
adtvkgrftisrdnpkntlflqmtslrsedtalyycarsggierydgtyyvmdywgqgts
vtvss
>d1mf2n2 2.1.1.2.88 (114-209) Immunoglobulin (constant domains of L and H chains) {Fab F11.2.32 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpssprpsetvtcnvahpasstkvdkkivprd
>d1mfa_1 2.1.1.1.30 (1l-111l) Immunoglobulin (variable domains of L and H chains) {Fab SE155-4 (mouse), lambda L chain}
qivvtqesalttspgetvtltcrsstgtvtsgnhanwvqekpdhlftgligdtnnrapgv
parfsgsligdkaaltitgaqpedeaiyfcalwsnnhwifgggtkltvlgq
>d1mfa_2 2.1.1.1.30 (251h-367h) Immunoglobulin (variable domains of L and H chains) {Fab SE155-4 (mouse), lambda L chain}
evqvqqsgtvvarpgasvkmsckasgytftnywmhwikqrpgqglewigaiypgnsatfy
nhkfraktkltavtstttaymelssltsedsavyyctrgghgyygdywgqgasltvs
>d1mfbh1 2.1.1.1.30 (251-367) Immunoglobulin (variable domains of L and H chains) {Fab SE155-4 (mouse), lambda L chain}
evqvqqsgtvlarpgasvkmsckasgytftnywmhwikqrpgqglewigaiypgnsatfy
nhkfraktkltavtstitaymelssltnedsavyyctrgghgyygdywgqgasltvs
>d1mfbh2 2.1.1.2.38 (368-468) Immunoglobulin (constant domains of L and H chains) {Fab SE155-4 (mouse), lambda L chain}
sakttppsvyplapgsaaqtdsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqs
dlytlsssvtvpsstwpsetvtcnvahpasstkvdkkivpr
>d1mfbl1 2.1.1.1.30 (1-111) Immunoglobulin (variable domains of L and H chains) {Fab SE155-4 (mouse), lambda L chain}
qavvtqesalttspgetvtltcrsstgtvtsgnhanwvqekpdhlftgligdtnnrapgv
parfsgsligdkaaltitgaqpedeaiyfcalwcnnhwifgggtkltvlgq
>d1mfbl2 2.1.1.2.38 (112-212) Immunoglobulin (constant domains of L and H chains) {Fab SE155-4 (mouse), lambda L chain}
pksspsvtlfppsseeletnkatlvctitdfypgvvtvdwkvdgtpvtqgmettqpskqs
nnkymassyltltarawerhssyscqvtheghtvekslsra
>d1mfch1 2.1.1.1.30 (251-367) Immunoglobulin (variable domains of L and H chains) {Fab SE155-4 (mouse), lambda L chain}
evqvqqsgtvlarpgasvkmsckasgytftnywmhwikqrpgqglewigaiypgnsatfy
nhkfraktkltavtstitaymelssltnedsavyyctrgghgyygdywgqgasltvs
>d1mfch2 2.1.1.2.38 (368-468) Immunoglobulin (constant domains of L and H chains) {Fab SE155-4 (mouse), lambda L chain}
sakttppsvyplapgsaaqtdsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqs
dlytlsssvtvpsstwpsetvtcnvahpasstkvdkkivpr
>d1mfcl1 2.1.1.1.30 (1-111) Immunoglobulin (variable domains of L and H chains) {Fab SE155-4 (mouse), lambda L chain}
qavvtqesalttspgetvtltcrsstgtvtsgnhanwvqekpdhlftgligdtnnrapgv
parfsgsligdkaaltitgaqpedeaiyfcalwcnnhwifgggtkltvlgq
>d1mfcl2 2.1.1.2.38 (112-212) Immunoglobulin (constant domains of L and H chains) {Fab SE155-4 (mouse), lambda L chain}
pksspsvtlfppsseeletnkatlvctitdfypgvvtvdwkvdgtpvtqgmettqpskqs
nnkymassyltltarawerhssyscqvtheghtvekslsra
>d1mfdh1 2.1.1.1.30 (251-367) Immunoglobulin (variable domains of L and H chains) {Fab SE155-4 (mouse), lambda L chain}
evqvqqsgtvlarpgasvkmsckasgytftnywmhwikqrpgqglewigaiypgnsatfy
nhkfraktkltavtstitaymelssltnedsavyyctrgghgyygdywgqgasltvs
>d1mfdh2 2.1.1.2.38 (368-468) Immunoglobulin (constant domains of L and H chains) {Fab SE155-4 (mouse), lambda L chain}
sakttppsvyplapgsaaqtdsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqs
dlytlsssvtvpsstwpsetvtcnvahpasstkvdkkivpr
>d1mfdl1 2.1.1.1.30 (1-111) Immunoglobulin (variable domains of L and H chains) {Fab SE155-4 (mouse), lambda L chain}
qavvtqesalttspgetvtltcrsstgtvtsgnhanwvqekpdhlftgligdtnnrapgv
parfsgsligdkaaltitgaqpedeaiyfcalwcnnhwifgggtkltvlgq
>d1mfdl2 2.1.1.2.38 (112-212) Immunoglobulin (constant domains of L and H chains) {Fab SE155-4 (mouse), lambda L chain}
pksspsvtlfppsseeletnkatlvctitdfypgvvtvdwkvdgtpvtqgmettqpskqs
nnkymassyltltarawerhssyscqvtheghtvekslsra
>d1mfeh1 2.1.1.1.30 (251-367) Immunoglobulin (variable domains of L and H chains) {Fab SE155-4 (mouse), lambda L chain}
evqvqqsgtvlarpgasvkmsckasgytftnywmhwikqrpgqglewigaiypgnsatfy
nhkfraktkltavtstitaymelssltnedsavyyctrgghgyygdywgqgasltvs
>d1mfeh2 2.1.1.2.38 (368-468) Immunoglobulin (constant domains of L and H chains) {Fab SE155-4 (mouse), lambda L chain}
sakttppsvyplapgsaaqtdsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqs
dlytlsssvtvpsstwpsetvtcnvahpasstkvdkkivpr
>d1mfel1 2.1.1.1.30 (1-111) Immunoglobulin (variable domains of L and H chains) {Fab SE155-4 (mouse), lambda L chain}
xavvtqesalttspgetvtltcrsstgtvtsgnhanwvqekpdhlftgligdtnnrapgv
parfsgsligdkaaltitgaqpedeaiyfcalwcnnhwifgggtkltvlgq
>d1mfel2 2.1.1.2.38 (112-211) Immunoglobulin (constant domains of L and H chains) {Fab SE155-4 (mouse), lambda L chain}
pksspsvtlfppsseeletnkatlvctitdfypgvvtvdwkvdgtpvtqgmettqpskqs
nnkymassyltltarawerhssyscqvtheghtvekslsr
>d1mfn_1 2.1.2.1.4 (1-92) Fibronectin, different Fn3 modules {Mouse (Mus musculus)}
gldsptgfdssditansftvhwvaprapitgyiirhhaehsvgrprqdrvppsrnsitlt
nlnpgteyvvsiiavngreesppligqqatvs
>d1mfn_2 2.1.2.1.4 (93-184) Fibronectin, different Fn3 modules {Mouse (Mus musculus)}
diprdleviastptsllisweppavsvryyritygetggnspvqeftvpgskstatinni
kpgadytitlyavtgrgdspasskpvsinykt
>d1mfs__ 7.34.1.1.2 HIV-1 nucleocapsid {human immunodeficiency virus type 1 (Mn isolate)}
mqkgnfrnqrktvkcfncgkeghiakncraprkkgcwkcgkeghqmkdcterqan
>d1mgn__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkygvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1mgsa_ 4.7.1.1.4 Melanoma growth stimulating activity (MGSA) {human (Homo sapiens)}
asvatelrcqclqtlqgihpkniqsvnvkspgphcaqteviatlkngrkaclnpaspivk
kiiekmlnsdksn
>d1mgsb_ 4.7.1.1.4 Melanoma growth stimulating activity (MGSA) {human (Homo sapiens)}
asvatelrcqclqtlqgihpkniqsvnvkspgphcaqteviatlkngrkaclnpaspivk
kiiekmlnsdksn
>d1mh1__ 3.29.1.4.2 Rac1 {Human (Homo sapiens)}
gspqaikcvvvgdgavgktcllisyttnafpgeyiptvfdnysanvmvdgkpvnlglwdt
agqedydrlrplsypqtdvslicfslvspasfenvrakwypevrhhcpntpiilvgtkld
lrddkdtieklkekkltpitypqglamakeigavkylecsaltqrglktvfdeairavlc
ppp
>d1mhca1 2.1.1.2.13 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain {mouse (Mus musculus) h2-m3}
adppkahvahhprpkgdvtlrcwalgfypaditltwqkdeedltqdmelvetrpsgdgtf
qkwaavvvpsgeeqrytcyvhheglteplalkwrs
>d1mhca2 4.15.1.1.17 (1-181) MHC class I, alpha-1 and alpha-2 domains {mouse h2-m3}
gshslryfhtavsrpgrgepqyisvgyvddvqfqrcdsieeiprmeprapwmekerpeyw
kelklkvkniaqsaranlrtllryynqseggshilqwmvscevgpdmrllgahyqaaydg
sdyitlnedlsswtavdmvsqitksrlesagtaeyfrayvegeclellhrflrngkeilq
r
>d1mhcd1 2.1.1.2.13 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain {mouse (Mus musculus) h2-m3}
adppkahvahhprpkgdvtlrcwalgfypaditltwqkdeedltqdmelvetrpsgdgtf
qkwaavvvpsgeeqrytcyvhheglteplalkwrs
>d1mhcd2 4.15.1.1.17 (1-181) MHC class I, alpha-1 and alpha-2 domains {mouse h2-m3}
gshslryfhtavsrpgrgepqyisvgyvddvqfqrcdsieeiprmeprapwmekerpeyw
kelklkvkniaqsaranlrtllryynqseggshilqwmvscevgpdmrllgahyqaaydg
sdyitlnedlsswtavdmvsqitksrlesagtaeyfrayvegeclellhrflrngkeilq
r
>e1mhi.1a 7.1.1.1.2 Insulin {human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1mhi.1b 7.1.1.1.2 Insulin {human (Homo sapiens)}
fvnqhlcgdhlvealylvcgergffytpkt
>e1mhj.1a 7.1.1.1.2 Insulin {human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1mhj.1b 7.1.1.1.2 Insulin {human (Homo sapiens)}
fvnqhlcgshlvealylvcgergfytpkt
>e1mhl.1a 1.72.1.2.1 Myeloperoxidase {human (Homo sapiens)}
cpeqdkyrtitgmcnnrrsptlgasnrafvrwlpaeyedgfslpygwtpgvkrngfpval
aravsneivrfptdqltpdqerslmfmqwgqlldhdldftpepa
>e1mhl.1c 1.72.1.2.1 Myeloperoxidase {human (Homo sapiens)}
vncetscvqqppcfplkippndpriknqadcipffrscpacpgsnitirnqinaltsfvd
asmvygseeplarnlrnmsnqlgllavnqrfqdngrallpfdnlhddpclltnrsaripc
flagdtrssempeltsmhtlllrehnrlatelkslnprwdgerlyqearkivgamvqiit
yrdylplvlgptamrkylptyrsyndsvdprianvftnafryghtliqpfmfrldnryqp
mepnprvplsrvffaswrvvleggidpilrglmatpaklnrqnqiavdeirerlfeqvmr
igldlpalnmqrsrdhglpgynawrrfcglpqpetvgqlgtvlrnlklarklmeqygtpn
nidiwmggvseplkrkgrvgpllaciigtqfrklrdgdrfwwenegvfsmqqrqalaqis
lpriicdntgittvsknnifmsnsyprdfvncstlpalnlaswrea
>e1mhl.2b 1.72.1.2.1 Myeloperoxidase {human (Homo sapiens)}
cpeqdkyrtitgmcnnrrsptlgasnrafvrwlpaeyedgfslpygwtpgvkrngfpval
aravsneivrfptdqltpdqerslmfmqwgqlldhdldftpepa
>e1mhl.2d 1.72.1.2.1 Myeloperoxidase {human (Homo sapiens)}
vncetscvqqppcfplkippndpriknqadcipffrscpacpgsnitirnqinaltsfvd
asmvygseeplarnlrnmsnqlgllavnqrfqdngrallpfdnlhddpclltnrsaripc
flagdtrssempeltsmhtlllrehnrlatelkslnprwdgerlyqearkivgamvqiit
yrdylplvlgptamrkylptyrsyndsvdprianvftnafryghtliqpfmfrldnryqp
mepnprvplsrvffaswrvvleggidpilrglmatpaklnrqnqiavdeirerlfeqvmr
igldlpalnmqrsrdhglpgynawrrfcglpqpetvgqlgtvlrnlklarklmeqygtpn
nidiwmggvseplkrkgrvgpllaciigtqfrklrdgdrfwwenegvfsmqqrqalaqis
lpriicdntgittvsknnifmsnsyprdfvncstlpalnlaswrea
>d1mhta_ 3.53.1.5.1 DNA methylase HhaI, coenzyme-binding domain {(Haemophilus haemolyticus)}
mieikdkqltglrfidlfaglggfrlalescgaecvysnewdkyaqevyemnfgekpegd
itqvnektipdhdilcagfpcqafsisgkqkgfedsrgtlffdiarivrekkpkvvfmen
vknfashdngntlevvkntmneldysfhakvlnaldygipqkreriymicfrndlniqnf
qfpkpfelntfvkdlllpdsevehlvidrkdlvmtnqeieqttpktvrlgivgkggqger
iystrgiaitlsaygggifaktggylvngktrklhprecarvmgypdsykvhpstsqayk
qfgnsvvinvlqyiaynigsslnfkpy
>d1mhu__ 7.38.1.1.1 Metallothionein {(human)}
ksccsccpvgcakcaqgcickgasdkcscca
>d1mhyb_ 1.25.1.2.2 Methane monooxygenase hydrolase, beta and alpha subunits {(Methylosinus trichosporium)}
krgltdperaaiiaaavpdhaldtqrkyhyfiqprwkplseyeqlscyaqpnpdwiaggl
dwgdwtqkfhggrpswgnestelrttdwyrhrdparrwhhpyvkdkseearytqrflaay
ssegsirtidpywrdeilnkyfgallyseyglfnahssvgrdclsdtirqtavfaaldkv
dnaqmiqmerlfiaklvpgfdastdvpkkiwttdpiysgaratvqeiwqgvqdwneilwa
ghavydatfgqfarreffqrlatvygdtltpfftaqsqtyfqttrgaiddlfvyclands
efgahnrtflnawtehylassvaalkdfvglyakvekvagatdsagvsealqrvfgdwki
dyadkigfrvdvdqkvdavlagy
>d1mhyd_ 1.25.1.2.2 Methane monooxygenase hydrolase, beta and alpha subunits {(Methylosinus trichosporium)}
nrapvgvepqevhkwlqsfnwdfkenrtkyptkyhmanetkeqfkviakeyarmeaakde
rqfgtlldgltrlgagnkvhprwgetmkvisnflevgeynaiaasamlwdsataaeqkng
ylaqvldeirhthqcafinhyyskhyhdpaghndarrtraigplwkgmkrvfadgfisgd
avecsvnlqlvgeacftnplivavtewasangdeitptvflsvetdelrhmangyqtvvs
iandpasakflntdlnnafwtqqkyftpvlgylfeygskfkvepwvktwnrwvsedwggi
wigrlgkygvesprslrdakrdaywahhdlalaayamwplgfarlalpdeedqawfeany
pgwadhygkifnewkklgyedpksgfipyqwllanghdvyidrvsqvpfipslakgtgsl
rvhefngkkhsltddwgerqwlieperyechnvfeqyegrelseviaeghgvrsdgktli
aqphtrgdnlwtledikragcvfpdplakf
>d1mhyg_ 1.23.1.1.2 Methane monooxygenase hydrolase, gamma subunit {(Methylosinus trichosporium)}
akrepihdnsirteweakiakltsvdqatkfiqdfrlaytspfrksydidvdyqyierki
eeklsvlkteklpvadlitkattgedaaaveatwiakikaakskyeaeaihiefrqlykp
pvlpvnvflrtdaalgtvlmeirntdyygtpleglrkergvkvlhlq
>d1mhzb_ 1.25.1.2.2 Methane monooxygenase hydrolase, beta and alpha subunits {(Methylosinus trichosporium)}
krgltdperaaiiaaavpdhaldtqrkyhyfiqprwkplseyeqlscyaqpnpdwiaggl
dwgdwtqkfhggrpswgnestelrttdwyrhrdparrwhhpyvkdkseearytqrflaay
ssegsirtidpywrdeilnkyfgallyseyglfnahssvgrdclsdtirqtavfaaldkv
dnaqmiqmerlfiaklvpgfdastdvpkkiwttdpiysgaratvqeiwqgvqdwneilwa
ghavydatfgqfarreffqrlatvygdtltpfftaqsqtyfqttrgaiddlfvyclands
efgahnrtflnawtehylassvaalkdfvglyakvekvagatdsagvsealqrvfgdwki
dyadkigfrvdvdqkvdavlagy
>d1mhzd_ 1.25.1.2.2 Methane monooxygenase hydrolase, beta and alpha subunits {(Methylosinus trichosporium)}
nrapvgvepqevhkwlqsfnwdfkenrtkyptkyhmanetkeqfkviakeyarmeaakde
rqfgtlldgltrlgagnkvhprwgetmkvisnflevgeynaiaasamlwdsataaeqkng
ylaqvldeirhthqcafinhyyskhyhdpaghndarrtraigplwkgmkrvfadgfisgd
avecsvnlqlvgeacftnplivavtewasangdeitptvflsvetdelrhmangyqtvvs
iandpasakflntdlnnafwtqqkyftpvlgylfeygskfkvepwvktwnrwvsedwggi
wigrlgkygvesprslrdakrdaywahhdlalaayamwplgfarlalpdeedqawfeany
pgwadhygkifnewkklgyedpksgfipyqwllanghdvyidrvsqvpfipslakgtgsl
rvhefngkkhsltddwgerqwlieperyechnvfeqyegrelseviaeghgvrsdgktli
aqphtrgdnlwtledikragcvfpdplakf
>d1mhzg_ 1.23.1.1.2 Methane monooxygenase hydrolase, gamma subunit {(Methylosinus trichosporium)}
akrepihdnsirteweakiakltsvdqatkfiqdfrlaytspfrksydidvdyqyierki
eeklsvlkteklpvadlitkattgedaaaveatwiakikaakskyeaeaihiefrqlykp
pvlpvnvflrtdaalgtvlmeirntdyygtpleglrkergvkvlhlq
>d1mi2a_ 4.7.1.1.12 Macrophage inflammatory protein-2 {Mouse (Mus musculus)}
avvaselrcqclktlprvdfkniqslsvtppgphcaqteviatlkggqkvcldpeaplvq
kiiqkilnkgkan
>d1mi2b_ 4.7.1.1.12 Macrophage inflammatory protein-2 {Mouse (Mus musculus)}
avvaselrcqclktlprvdfkniqslsvtppgphcaqteviatlkggqkvcldpeaplvq
kiiqkilnkgkan
>d1mifa_ 4.41.1.3.1 Microphage migration inhibition factor (MIF) {Human (Homo sapiens)}
pmfivntnvprasvpdgflseltqqlaqatgkppqyiavhvvpdqlmafggssepcalcs
lhsigkiggaqnrsyskllcgllaerlrispdrvyinyydmnaasvgwnnstfa
>d1mifb_ 4.41.1.3.1 Microphage migration inhibition factor (MIF) {Human (Homo sapiens)}
pmfivntnvprasvpdgflseltqqlaqatgkppqyiavhvvpdqlmafggssepcalcs
lhsigkiggaqnrsyskllcgllaerlrispdrvyinyydmnaasvgwnnstfa
>d1mifc_ 4.41.1.3.1 Microphage migration inhibition factor (MIF) {Human (Homo sapiens)}
pmfivntnvprasvpdgflseltqqlaqatgkppqyiavhvvpdqlmafggssepcalcs
lhsigkiggaqnrsyskllcgllaerlrispdrvyinyydmnaasvgwnnstfa
>d1mika_ 2.47.1.1.1 Cyclophilin A {human (Homo sapiens)}
mvnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgf
mcqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictakte
wldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1mil__ 4.53.1.1.9 Shc adaptor protein {human (Homo sapiens)}
gsqlrgepwfhgklsrreaeallqlngdflvrestttpgqyvltglqsgqpkhlllvdpe
gvvrtkdhrfesvshlisyhmdnhlpiisagselclqqpverkl
>d1mimh1 2.1.1.1.77 (1-115) Immunoglobulin (variable domains of L and H chains) {Fab CHI621 (mouse), kappa L chain}
qlqqsgtvlarpgasvkmsckasgysftrywmhwikqrpgqglewigaiypgnsdtsynq
kfegkakltavtsastaymelsslthedsavyycsrdygyyfdfwgqgttltvss
>d1mimh2 2.1.1.2.80 (116-215) Immunoglobulin (constant domains of L and H chains) {Fab CHI621 (mouse), kappa L chain}
astkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkrvep
>d1miml1 2.1.1.1.77 (1-105) Immunoglobulin (variable domains of L and H chains) {Fab CHI621 (mouse), kappa L chain}
qivstqspaimsaspgekvtmtcsasssrsymqwyqqkpgtspkrwiydtsklasgvpar
fsgsgsgtsysltissmeaedaatyychqrssytfgggtkleikr
>d1miml2 2.1.1.2.80 (106-210) Immunoglobulin (constant domains of L and H chains) {Fab CHI621 (mouse), kappa L chain}
tvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqds
kdstyslsstltlskadyekhkvyacevthqglsspvtksfnrge
>d1mioa_ 3.75.1.1.1 Nitrogenase iron-molybdenum protein {(Clostridium pasteurianum)}
senlkdeilekyipktkktrsghivikteetpnpeivantrtvpgiitargcayagckgv
vmgpikdmvhithgpigcsfytwggrrfkskpengtglnfneyvfstdmqesdivfggvn
klkdaiheayemfhpaaigvyatcpvgligddilavaataskeigipvhafscegykgvs
qsaghhianntvmtdiigkgnkeqkkysinvlgeyniggdawemdrvlekigyhvnatlt
gdatyekvqnadkadlnlvqchrsinyiaemmetkygipwikcnfigvdgivetlrdmak
cfddpeltkrteeviaeeiaaiqddldyfkeklqgktaclyvggsrshtymnmlksfgvd
slvagfefahrddyegreviptikidadsknipeitvtpdeqkyrvvipedkveelkkag
vplssyggmmkemhdgtiliddmnhhdmevvleklkpdmffagikekfviqkggvlskql
hsydyngpyagfrgvvnfghelvngiytpawkmitppwkkasses
>d1miob_ 3.75.1.1.1 Nitrogenase iron-molybdenum protein {(Clostridium pasteurianum)}
ldatpkeiverkalrinpaktcqpvgamyaalgihnclphshgsqgccsyhrtvlsrhfk
epamastssftegasvfgggsniktavknifslynpdiiavhttclsetlgddlptyisq
medagsipegklvihtntpsyvgshvtgfanmvqgivnylsentgakngkinvipgfvgp
admreikrlfeamdipyimfpdtsgvldgpttgeykmypeggtkiedlkdtgnsdltlsl
gsyasdlgaktlekkckvpfktlrtpigvsatdefimalseatgkevpasieeergqlid
lmidaqqylqgkkvallgdpdeiialskfiielgaipkyvvtgtpgmkfqkeidamlaea
giegskvkvegdffdvhqwiknegvdllisntygkfiareenipfvrfgfpimdryghyy
npkvgykgairlveeitnvildkierecteedfevvr
>d1mioc_ 3.75.1.1.1 Nitrogenase iron-molybdenum protein {(Clostridium pasteurianum)}
senlkdeilekyipktkktrsghivikteetpnpeivantrtvpgiitargcayagckgv
vmgpikdmvhithgpigcsfytwggrrfkskpengtglnfneyvfstdmqesdivfggvn
klkdaiheayemfhpaaigvyatcpvgligddilavaataskeigipvhafscegykgvs
qsaghhianntvmtdiigkgnkeqkkysinvlgeyniggdawemdrvlekigyhvnatlt
gdatyekvqnadkadlnlvqchrsinyiaemmetkygipwikcnfigvdgivetlrdmak
cfddpeltkrteeviaeeiaaiqddldyfkeklqgktaclyvggsrshtymnmlksfgvd
slvagfefahrddyegreviptikidadsknipeitvtpdeqkyrvvipedkveelkkag
vplssyggmmkemhdgtiliddmnhhdmevvleklkpdmffagikekfviqkggvlskql
hsydyngpyagfrgvvnfghelvngiytpawkmitppwkkasses
>d1miod_ 3.75.1.1.1 Nitrogenase iron-molybdenum protein {(Clostridium pasteurianum)}
ldatpkeiverkalrinpaktcqpvgamyaalgihnclphshgsqgccsyhrtvlsrhfk
epamastssftegasvfgggsniktavknifslynpdiiavhttclsetlgddlptyisq
medagsipegklvihtntpsyvgshvtgfanmvqgivnylsentgakngkinvipgfvgp
admreikrlfeamdipyimfpdtsgvldgpttgeykmypeggtkiedlkdtgnsdltlsl
gsyasdlgaktlekkckvpfktlrtpigvsatdefimalseatgkevpasieeergqlid
lmidaqqylqgkkvallgdpdeiialskfiielgaipkyvvtgtpgmkfqkeidamlaea
giegskvkvegdffdvhqwiknegvdllisntygkfiareenipfvrfgfpimdryghyy
npkvgykgairlveeitnvildkierecteedfevvr
>d1mira_ 4.3.1.1.6 (Pro)cathepsin B {Rat (Rattus norvegicus)}
sddminyinkqnttwqagrnfynvdisylkklcgtvlggpklpervgfsedinlpesfda
reqwsncptiaqirdqgscgsswafgaveamsdricihtngrvnvevsaedlltccgiqc
gdgcnggypsgawnfwtrkglvsggvynshigclpytippcehhvngarppctgegdtpk
cnkmceagystsykedkhygytsysvsdsekeimaeiykngpvegaftvfsdfltyksgv
ykheagdvmgghairilgwgiengvpywlvanswnadwgdngffkilrgenhcgieseiv
agiprtqqywgrf
>d1mirb_ 4.3.1.1.6 (Pro)cathepsin B {Rat (Rattus norvegicus)}
sddminyinkqnttwqagrnfynvdisylkklcgtvlggpklpervgfsedinlpesfda
reqwsncptiaqirdqgscgsswafgaveamsdricihtngrvnvevsaedlltccgiqc
gdgcnggypsgawnfwtrkglvsggvynshigclpytippcehhvngarppctgegdtpk
cnkmceagystsykedkhygytsysvsdsekeimaeiykngpvegaftvfsdfltyksgv
ykheagdvmgghairilgwgiengvpywlvanswnadwgdngffkilrgenhcgieseiv
agiprtqqywgrf
>d1mit__ 4.22.1.1.3 Trypsin inhibitor V {pumpkin (Cucurbita maxima)}
gsscpgksswphlvgvggsvakaiierqnpnvkavileegtpvtkdfrcnrvriwvnkrg
lvvspprig
>d1mjc__ 2.29.4.5.1 Major cold shock protein {(Escherichia coli)}
sgkmtgivkwfnadkgfgfitpddgskdvfvhfsaiqndgyksldegqkvsftiesgakg
paagnvtsl
>d1mjka_ 1.41.1.2.1 Met repressor {(Escherichia coli)}
aewsgeyispyaehgkkseqvkkitvsiplkvlkiltdertrrkvnnlrhatnsellcea
flhaftgqplpddadlrkersdeipeaakeimremginpetwey
>d1mjkb_ 1.41.1.2.1 Met repressor {(Escherichia coli)}
aewsgeyispyaehgkkseqvkkitvsiplkvlkiltdertrrkvnnlrhatnsellcea
flhaftgqplpddadlrkersdeipeaakeimremginpetwey
>d1mjla_ 1.41.1.2.1 Met repressor {(Escherichia coli)}
aewsgeyispyaehgkkseqvkkitvsiplkvlkiltdertrrkvnnlrhatnsellcea
flhaftgqplpddadlrkersdeipeaakeimremginpetwey
>d1mjlb_ 1.41.1.2.1 Met repressor {(Escherichia coli)}
aewsgeyispyaehgkkseqvkkitvsiplkvlkiltdertrrkvnnlrhatnsellcea
flhaftgqplpddadlrkersdeipeaakeimremginpetwey
>d1mjwa_ 2.29.5.1.2 Inorganic pyrophosphatase {(Escherichia coli)}
sllnvpagkdlpediyvvieipanadpikyeidkesgalfvnrfmstamfypcnygyinh
tlsldgdpvdvlvptpyplqpgsvircrpvgvlkmtdeagedaklvavphsklskeydhi
kdvndlpellkaqiahffehykdlekgkwvkvegwenaeaakaeivasferaknk
>d1mjwb_ 2.29.5.1.2 Inorganic pyrophosphatase {(Escherichia coli)}
sllnvpagkdlpediyvvieipanadpikyeidkesgalfvnrfmstamfypcnygyinh
tlsldgdpvdvlvptpyplqpgsvircrpvgvlkmtdeagedaklvavphsklskeydhi
kdvndlpellkaqiahffehykdlekgkwvkvegwenaeaakaeivasferaknk
>d1mjxa_ 2.29.5.1.2 Inorganic pyrophosphatase {(Escherichia coli)}
sllnvpagkdlpediyvvieipanadpikyeidkesgalfvdrfmstamfypcnygyinh
tlslngdpvdvlvptpyplqpgsvircrpvgvlkmtdeagedaklvavphsklskeydhi
kdvndlpellkaqiahffehykdlekgkwvkvegwenaeaakaeivasferaknk
>d1mjxb_ 2.29.5.1.2 Inorganic pyrophosphatase {(Escherichia coli)}
sllnvpagkdlpediyvvieipanadpikyeidkesgalfvdrfmstamfypcnygyinh
tlslngdpvdvlvptpyplqpgsvircrpvgvlkmtdeagedaklvavphsklskeydhi
kdvndlpellkaqiahffehykdlekgkwvkvegwenaeaakaeivasferaknk
>d1mjya_ 2.29.5.1.2 Inorganic pyrophosphatase {(Escherichia coli)}
sllnvpagkdlpediyvvieipanadpikyeidkesgalfvdrfmstamfypcnygyinh
tlsldgdpvnvlvptpyplqpgsvtrcrpvgvlkmtdeagedaklvavphsklskeydhi
kdvndlpellkaqiahffehykdlekgkwvkvegwenaeaakaeivasferaknk
>d1mjyb_ 2.29.5.1.2 Inorganic pyrophosphatase {(Escherichia coli)}
sllnvpagkdlpediyvvieipanadpikyeidkesgalfvdrfmstamfypcnygyinh
tlsldgdpvnvlvptpyplqpgsvtrcrpvgvlkmtdeagedaklvavphsklskeydhi
kdvndlpellkaqiahffehykdlekgkwvkvegwenaeaakaeivasferaknk
>d1mjz__ 2.29.5.1.2 Inorganic pyrophosphatase {(Escherichia coli)}
sllnvpagkdlpediyvvieipanadpikyeidkesgalfvdrfmstamfypcnygyinh
tlsldgdpvdvlvptpyplqpgsvircrpvgvlkmtneagedaklvavphsklskeydhi
kdvndlpellkaqiahffehykdlekgkwvkvegwenaeaakaeivasferaknk
>d1mkaa_ 4.21.1.1.1 beta-Hydroxydecanol thiol ester dehydrase {(Escherichia coli)}
vdkresytkedllasgrgelfgakgpqlpapnmlmmdrvvkmtetggnfdkgyveaeldi
npdlwffgchfigdpvmpgclgldamwqlvgfylgwlggegkgralgvgevkftgqvlpt
akkvtyrihfkrivnrrlimgladgevlvdgrliytasdlkvglfqdtsaf
>d1mkab_ 4.21.1.1.1 beta-Hydroxydecanol thiol ester dehydrase {(Escherichia coli)}
vdkresytkedllasgrgelfgakgpqlpapnmlmmdrvvkmtetggnfdkgyveaeldi
npdlwffgchfigdpvmpgclgldamwqlvgfylgwlggegkgralgvgevkftgqvlpt
akkvtyrihfkrivnrrlimgladgevlvdgrliytasdlkvglfqdtsaf
>d1mkba_ 4.21.1.1.1 beta-Hydroxydecanol thiol ester dehydrase {(Escherichia coli)}
vdkresytkedllasgrgelfgakgpqlpapnmlmmdrvvkmtetggnfdkgyveaeldi
npdlwffgchfigdpvmpgclgldamwqlvgfylgwlggegkgralgvgevkftgqvlpt
akkvtyrihfkrivnrrlimgladgevlvdgrliytasdlkvglfqdtsaf
>d1mkbb_ 4.21.1.1.1 beta-Hydroxydecanol thiol ester dehydrase {(Escherichia coli)}
vdkresytkedllasgrgelfgakgpqlpapnmlmmdrvvkmtetggnfdkgyveaeldi
npdlwffgchfigdpvmpgclgldamwqlvgfylgwlggegkgralgvgevkftgqvlpt
akkvtyrihfkrivnrrlimgladgevlvdgrliytasdlkvglfqdtsaf
>d1mks__ 1.103.1.2.11 Phospholipase A2 {bovine (Bos taurus l.) pancreas}
alwqfngmikckipsseplldfnnygcycglggsgtpvddldrccqthdncfkqakklds
ckvlvdnpytnnfsyscsnneitcssennaceaficncnrnaaicfskvpynkehknldk
knc
>d1mkt__ 1.103.1.2.11 Phospholipase A2 {bovine (Bos taurus l.) pancreas}
alwqfngmikckipsseplldfnnygcycglggsgtpvddldrccqthdncykqakklds
ckvlvdnpytnnysyscsnneitcssennaceaficncdrnaaicfskvpynkehknldk
knc
>d1mku__ 1.103.1.2.11 Phospholipase A2 {bovine (Bos taurus l.) pancreas}
alwqfngmikckipsseplldfnnygcycglggsgtpvddldrccqthdncfkqakklds
ckvlvdnpytnnfsyscsnneitcssennaceaficncnrnaaicfskvpynkehknldk
knc
>d1mkv__ 1.103.1.2.11 Phospholipase A2 {bovine (Bos taurus l.) pancreas}
alwqfngmikckipsseplldfnnygcycglggsgtpvddldrccqthdncykqakklds
ckvlvdnpytnnysyscsnneitcssennaceaficncdrnaaicfskvpynkehknldk
knc
>e1mkw.1h 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
ivegqdaevglspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftvddll
vrigkhsrtryerkvekismldkiyihprynwkenldrdiallklkrpielsdyihpvcl
pdkqtaakllhagfkgrvtgwgnrretwttsvaevqpsvlqvvnlplverpvckastrir
itdnmfcagykpgegkrgdacegdsggpfvmkspynnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvid
>e1mkw.1l 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
eadcglrplfekkqvqdqtekelfesyie
>d1mkwk_ 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
geadcglrplfekkqvqdqtekelfesyiegrivegqdaevglspwqvmlfrkspqellc
gaslisdrwvltaahcllyppwdknftvddllvrigkhsrtryerkvekismldkiyihp
rynwkenldrdiallklkrpielsdyihpvclpdkqtaakllhagfkgrvtgwgnrretw
ttsvaevqpsvlqvvnlplverpvckastriritdnmfcagykpgegkrgdacegdsggp
fvmkspynnrwyqmgivswgegcdrdgkygfythvfrlkkwiqkvid
>e1mkx.1h 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
ivegqdaevglspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftvddll
vrigkhsrtryerkvekismldkiyihprynwkenldrdiallklkrpielsdyihpvcl
pdkqtaakllhagfkgrvtgwgnrretwttsvaevqpsvlqvvnlplverpvckastrir
itdnmfcagykpgegkrgdacegdsggpfvmkspynnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvid
>e1mkx.1l 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
eadcglrplfekkqvqdqtekelfesyie
>d1mkxk_ 2.35.1.2.11 Thrombin {bovine (Bos taurus)}
geadcglrplfekkqvqdqtekelfesyiegrivegqdaevglspwqvmlfrkspqellc
gaslisdrwvltaahcllyppwdknftvddllvrigkhsrtryerkvekismldkiyihp
rynwkenldrdiallklkrpielsdyihpvclpdkqtaakllhagfkgrvtgwgnrretw
ttsvaevqpsvlqvvnlplverpvckastriritdnmfcagykpgegkrgdacegdsggp
fvmkspynnrwyqmgivswgegcdrdgkygfythvfrlkkwiqkvid
>d1ml1a_ 3.1.11.1.4 Triosephosphate isomerase {(Trypanosoma brucei brucei)}
skpqpiaaanwksgspdslselidlfnstsinhdvqcvvastfvhlamtkerlshpkfvi
aaqnagnadalaslkdfgvnwivlghserrwyygetneivadkvaaavasgfmviacige
tlqeresgrtavvvltqiaaiakklkkadwakvviayepvwaigtgkvatpqqaqeahal
irswvsskigadvagelrilyggsvngknartlyqqrdvngflvggaslkpefvdiikat
q
>d1ml1c_ 3.1.11.1.4 Triosephosphate isomerase {(Trypanosoma brucei brucei)}
skpqpiaaanwksgspdslselidlfnstsinhdvqcvvastfvhlamtkerlshpkfvi
aaqnagnadalaslkdfgvnwivlghserrwyygetneivadkvaaavasgfmviacige
tlqeresgrtavvvltqiaaiakklkkadwakvviayepvwaigtgkvatpqqaqeahal
irswvsskigadvagelrilyggsvngknartlyqqrdvngflvggaslkpefvdiikat
q
>d1ml1e_ 3.1.11.1.4 Triosephosphate isomerase {(Trypanosoma brucei brucei)}
skpqpiaaanwksgspdslselidlfnstsinhdvqcvvastfvhlamtkerlshpkfvi
aaqnagnadalaslkdfgvnwivlghserrwyygetneivadkvaaavasgfmviacige
tlqeresgrtavvvltqiaaiakklkkadwakvviayepvwaigtgkvatpqqaqeahal
irswvsskigadvagelrilyggsvngknartlyqqrdvngflvggaslkpefvdiikat
q
>d1ml1g_ 3.1.11.1.4 Triosephosphate isomerase {(Trypanosoma brucei brucei)}
skpqpiaaanwksgspdslselidlfnstsinhdvqcvvastfvhlamtkerlshpkfvi
aaqnagnadalaslkdfgvnwivlghserrwyygetneivadkvaaavasgfmviacige
tlqeresgrtavvvltqiaaiakklkkadwakvviayepvwaigtgkvatpqqaqeahal
irswvsskigadvagelrilyggsvngknartlyqqrdvngflvggaslkpefvdiikat
q
>d1ml1i_ 3.1.11.1.4 Triosephosphate isomerase {(Trypanosoma brucei brucei)}
skpqpiaaanwksgspdslselidlfnstsinhdvqcvvastfvhlamtkerlshpkfvi
aaqnagnadalaslkdfgvnwivlghserrwyygetneivadkvaaavasgfmviacige
tlqeresgrtavvvltqiaaiakklkkadwakvviayepvwaigtgkvatpqqaqeahal
irswvsskigadvagelrilyggsvngknartlyqqrdvngflvggaslkpefvdiikat
q
>d1ml1k_ 3.1.11.1.4 Triosephosphate isomerase {(Trypanosoma brucei brucei)}
skpqpiaaanwksgspdslselidlfnstsinhdvqcvvastfvhlamtkerlshpkfvi
aaqnagnadalaslkdfgvnwivlghserrwyygetneivadkvaaavasgfmviacige
tlqeresgrtavvvltqiaaiakklkkadwakvviayepvwaigtgkvatpqqaqeahal
irswvsskigadvagelrilyggsvngknartlyqqrdvngflvggaslkpefvdiikat
q
>d1mla_1 3.13.1.1.1 (3-127,198-307) Catalytic domain of malonyl-CoA ACP transacylase {(Esherichia coli)}
qfafvfpgqgsqtvgmladmaasypiveetfaeasaalgydlwaltqqgpaeelnktwqt
qpalltasvalyrvwqqqggkapammaghslgeysalvcagvidfadavrlvemrgkfmq
eavpeXvpshcalmkpaadklavelakitfnaptvpvvnnvdvkcetngdairdalvrql
ynpvqwtksveymaaqgvehlyevgpgkvltgltkrivdtltasalnepsamaaal
>d1mla_2 4.34.19.1.1 (128-197) Probable ACP-binding domain of malonyl-CoA ACP transacylase {(Esherichia coli)}
gtgamaaiiglddasiakaceeaaegqvvspvnfnspgqvviaghkeaveragaackaag
akralplpvs
>d1mlba1 2.1.1.1.57 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab D44.1 (mouse), kappa L chain}
dieltqspatlsvtpgdsvslscrasqsisnnlhwyqqkshesprllikyvsqsssgips
rfsgsgsgtdftlsinsvetedfgmyfcqqsnswprtfgggtkleikr
>d1mlba2 2.1.1.2.62 (109-214) Immunoglobulin (constant domains of L and H chains) {Fab D44.1 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1mlbb1 2.1.1.1.57 (1-118) Immunoglobulin (variable domains of L and H chains) {Fab D44.1 (mouse), kappa L chain}
qvqlqesgaevmkpgasvkisckatgytfstywiewvkqrpghglewigeilpgsgstyy
nekfkgkatftadtssntaymqlssltsedsavyycargdgnygywgqgttltvssas
>d1mlbb2 2.1.1.2.62 (119-218) Immunoglobulin (constant domains of L and H chains) {Fab D44.1 (mouse), kappa L chain}
ttppsvfplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsdly
tlsssvtvpssprpsetvtcnvahpasstkvdkkivprdc
>d1mlca1 2.1.1.1.57 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab D44.1 (mouse), kappa L chain}
dieltqspatlsvtpgdsvslscrasqsisnnlhwyqqkshesprllikyvsqsssgips
rfsgsgsgtdftlsinsvetedfgmyfcqqsnswprtfgggtkleikr
>d1mlca2 2.1.1.2.62 (109-214) Immunoglobulin (constant domains of L and H chains) {Fab D44.1 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1mlcb1 2.1.1.1.57 (1-118) Immunoglobulin (variable domains of L and H chains) {Fab D44.1 (mouse), kappa L chain}
qvqlqesgaevmkpgasvkisckatgytfstywiewvkqrpghglewigeilpgsgstyy
nekfkgkatftadtssntaymqlssltsedsavyycargdgnygywgqgttltvssas
>d1mlcb2 2.1.1.2.62 (119-218) Immunoglobulin (constant domains of L and H chains) {Fab D44.1 (mouse), kappa L chain}
ttppsvfplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsdly
tlsssvtvpssprpsetvtcnvahpasstkvdkkivprdc
>d1mlcc1 2.1.1.1.57 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab D44.1 (mouse), kappa L chain}
dieltqspatlsvtpgdsvslscrasqsisnnlhwyqqkshesprllikyvsqsssgips
rfsgsgsgtdftlsinsvetedfgmyfcqqsnswprtfgggtkleikr
>d1mlcc2 2.1.1.2.62 (109-214) Immunoglobulin (constant domains of L and H chains) {Fab D44.1 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1mlcd1 2.1.1.1.57 (1-118) Immunoglobulin (variable domains of L and H chains) {Fab D44.1 (mouse), kappa L chain}
qvqlqesgaevmkpgasvkisckatgytfstywiewvkqrpghglewigeilpgsgstyy
nekfkgkatftadtssntaymqlssltsedsavyycargdgnygywgqgttltvssas
>d1mlcd2 2.1.1.2.62 (119-218) Immunoglobulin (constant domains of L and H chains) {Fab D44.1 (mouse), kappa L chain}
ttppsvfplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsdly
tlsssvtvpssprpsetvtcnvahpasstkvdkkivprdc
>d1mlce_ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1mlcf_ 4.2.1.2.1 Lysozyme {chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1mlda1 3.22.1.5.1 (1-144) Malate dehydrogenase {porcine (Sus scrofa)}
akvavlgasggigqplslllknsplvsrltlydiahtpgvaadlshietratvkgylgpe
qlpdclkgcdvvvipagvprkpgmtrddlfntnativatltaacaqhcpdamiciisnpv
nstipitaevfkkhgvynpnkifg
>d1mlda2 4.100.1.1.1 (145-313) Malate dehydrogenase {porcine (Sus scrofa)}
vttldivranafvaelkgldparvsvpvigghagktiiplisqctpkvdfpqdqlstltg
riqeagtevvkakagagsatlsmayagarfvfslvdamngkegvvecsfvksqetdcpyf
stplllgkkgieknlgigkispfeekmiaeaipelkasikkgeefvknm
>d1mldb1 3.22.1.5.1 (1-144) Malate dehydrogenase {porcine (Sus scrofa)}
akvavlgasggigqplslllknsplvsrltlydiahtpgvaadlshietratvkgylgpe
qlpdclkgcdvvvipagvprkpgmtrddlfntnativatltaacaqhcpdamiciisnpv
nstipitaevfkkhgvynpnkifg
>d1mldb2 4.100.1.1.1 (145-313) Malate dehydrogenase {porcine (Sus scrofa)}
vttldivranafvaelkgldparvsvpvigghagktiiplisqctpkvdfpqdqlstltg
riqeagtevvkakagagsatlsmayagarfvfslvdamngkegvvecsfvksqetdcpyf
stplllgkkgieknlgigkispfeekmiaeaipelkasikkgeefvknm
>d1mldc1 3.22.1.5.1 (1-144) Malate dehydrogenase {porcine (Sus scrofa)}
akvavlgasggigqplslllknsplvsrltlydiahtpgvaadlshietratvkgylgpe
qlpdclkgcdvvvipagvprkpgmtrddlfntnativatltaacaqhcpdamiciisnpv
nstipitaevfkkhgvynpnkifg
>d1mldc2 4.100.1.1.1 (145-313) Malate dehydrogenase {porcine (Sus scrofa)}
vttldivranafvaelkgldparvsvpvigghagktiiplisqctpkvdfpqdqlstltg
riqeagtevvkakagagsatlsmayagarfvfslvdamngkegvvecsfvksqetdcpyf
stplllgkkgieknlgigkispfeekmiaeaipelkasikkgeefvknm
>d1mldd1 3.22.1.5.1 (1-144) Malate dehydrogenase {porcine (Sus scrofa)}
akvavlgasggigqplslllknsplvsrltlydiahtpgvaadlshietratvkgylgpe
qlpdclkgcdvvvipagvprkpgmtrddlfntnativatltaacaqhcpdamiciisnpv
nstipitaevfkkhgvynpnkifg
>d1mldd2 4.100.1.1.1 (145-313) Malate dehydrogenase {porcine (Sus scrofa)}
vttldivranafvaelkgldparvsvpvigghagktiiplisqctpkvdfpqdqlstltg
riqeagtevvkakagagsatlsmayagarfvfslvdamngkegvvecsfvksqetdcpyf
stplllgkkgieknlgigkispfeekmiaeaipelkasikkgeefvknm
>d1mlf__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtaltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1mlg__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtaltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1mlh__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtaltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1mli__ 4.34.4.1.1 Muconalactone isomerase {(Pseudomonas putida)}
mlfhvkmtvklpvdmdpakatqlkadekelaqrlqregtwrhlwriaghyanysvfdvps
vealhdtlmqlplfpymdievdglcrhpssihsddr
>d1mlj__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtfltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1mlk__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtfltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1mll__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtfltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1mlm__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtiltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1mln__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtiltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1mlo__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtiltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1mlq__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtlltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1mlr__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtlltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1mls__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtlltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1mlu__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkggvtaltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1mma_1 2.24.3.1.2 (34-79) Myosin S1 fragment, N-terminal domain {(Dictyostelium discoideum)}
yiwynpdpkerdsyecgeivsetsdsftfktsdgqdrqvkkddanq
>d1mma_2 3.29.1.5.2 (2-33,80-759) Myosin S1, motor domain {Slime mold (Dictyostelium discoideum)}
npihdrtsdyhkylkvkqgdsdlfkltvsdkrXrnpikfdgvedmselsylnepavfhnl
rvrynqdliytysglflvavnpfkripiytqemvdifkgrrrnevaphifaisdvayrsm
lddrqnqsllitgesgagktentkkviqylasvagrnqangsgvleqqilqanpileafg
nakttrnnnssrfgkfieiqfnnagfisgasiqsylleksrvvfqseternyhifyqlla
gataeekkalhlagpesfnylnqsgcvdikgvsdseefkitrqamdivgfsqeeqmsifk
iiagilhlgnikfekgagegavlkdktalnaastvfgvnpsvlekalmeprilagrdlva
qhlnvekssssrdalvkalygrlflwlvkkinnvlcqerkayfigvldisgfeifkvnsf
eqlcinytneklqqffnhhmfkleqeeylkekinwtfidfgldsqatidlidgrqppgil
alldeqsvfpnatdntlitklhshfskknakyeeprfsktefgvthyagqvmyeiqdwle
knkdplqqdlelcfkdssdnvvtklfndpniasrakkganfitvaaqykeqlaslmatle
ttnphfvrciipnnkqlpakledkvvldqlrcngvlegiritrkgfpnriiyadfvkryy
llapnvprdaedsqkatdavlkhlnidpeqfrfgitkiffragqlarieeare
>d1mmb__ 4.52.1.7.2 Neutrophil collagenase (MMP-8) {Human (Homo sapiens)}
npkwertnltyrirnytpqlseaeveraikdafelwsvaspliftrisqgeadiniafyq
rdhgdnspfdgpngilahafqpgqgiggdahfdaeetwtntsanynlflvaahefghslg
lahssdpgalmypnyafretsnyslpqddidgiqaiyg
>d1mmc__ 7.3.1.2.1 Antimicrobial peptide 2, AC-AMP2 {Tassel (Amaranthus caudatus)}
vgecvrgrcpsgmccsqfgycgkgpkycgr
>d1mmd_1 2.24.3.1.2 (34-79) Myosin S1 fragment, N-terminal domain {(Dictyostelium discoideum)}
yiwynpdpderdsyecgeivsetsdsftfktvdgqdrqvkkddanq
>d1mmd_2 3.29.1.5.2 (2-33,80-759) Myosin S1, motor domain {Slime mold (Dictyostelium discoideum)}
npihdrtsdyhkylkvkqgdsdlfkltvsdkrXrnpikfdgvedmselsylnepavfhnl
rvrynqdliytysglflvavnpfkripiytqemvdifkgrrrnevaphifaisdvayrsm
lddrqnqsllitgesgagktentkkviqylasvagrnqangsgvleqqilqanpileafg
nakttrnnnssrfgkfieiqfnnagfisgasiqsylleksrvvfqseternyhifyqlla
gataeekkalhlagpesfnylnqsgcvdikgvsdedefkitrqamdivgfsqeeqmsifk
iiagilhlgnikfekgagegavlkdktalnaastvfgvnpsvlekalmeprilagrdlva
qhlnvekssssrdalvkalygrlflwlvkkinnvlcseraayfigvldisgfeifkvnsf
eqlcinytneklqqffnhhmfkveqeeylkekinwtfidfgldsqatidlidgrqppgil
alldeqsvfpnatdntlitklhshfskknakyeeprfsktefgvthyagqvmyeiqdwle
knkdplqqdlelcfkdssdnvvtklfndpniasrakkganfitvaaqykeqlaslmatle
ttnphfvrciipnnkqlpakledkvvldqlrcngvlegiritrkgfpnriiyadfvkryy
llapnvprdaedsqkatdavlkhlnidpeqyrfgitkiffragqlarieeare
>d1mmg_1 2.24.3.1.2 (34-79) Myosin S1 fragment, N-terminal domain {(Dictyostelium discoideum)}
yiwynpdpkerdsyecgeivsetsdsftfktsdgqdrqvkkddanq
>d1mmg_2 3.29.1.5.2 (2-33,80-759) Myosin S1, motor domain {Slime mold (Dictyostelium discoideum)}
npihdrtsdyhkylkvkqgdsdlfkltvsdkrXrnpikfdgvedmselsylnepavfhnl
rvrynqdliytysglflvavnpfkripiytqemvdifkgrrrnevaphifaisdvayrsm
lddrqnqsllitgesgagktentkkviqylasvagrnqangsgvleqqilqanpileafg
nakttrnnnssrfgkfieiqfnnagfisgasiqsylleksrvvfqstternyhifyqlla
gataeekkalhlagpesfnylnqsgcvdikgvsdedefkitrqamdivgfsqeeqmsifk
iiagilhlgnikfekgagegavlkdktalnaastvfgvnpsvlekalmeprilagrdlva
qhlnvekssssrdalvkalygrlflwlvkkinnvlcserkayfigvldisgfeifkvnsf
eqlcinytneklqqffnhhmfkveqeeylkekinwtfidfgldsqatidlidgrqppgil
alldeqsvfpnatdntlitklhshfskknakyeeprfsktefgvthyagqvmyeiqdwle
knkdplqqdlelcfkdssdnvvtklfndpniasrakkganfltvaaqykeqlaslmatle
ttnphfvrciipnnkqlpakledkvvldqlrcngvleairitrkgfpnriiyadfvkryy
dlapnvprdaedsqkatdavlkhlnidpeqfrfgitkiffragqlarieeare
>d1mml__ 5.9.1.2.1 MMLV reverse transcriptase {(Moloney murine leukemia virus)}
twlsdfpqawaetggmglavrqapliiplkatstpvsikqypmsqearlgikphiqrlld
qgilvpcqspwntpllpvkkpgtndyrpvqdlrevnkrvedihptvpnpynllsglppsh
qwytvldlkdaffclrlhptsqplfafewrdpemgisgqltwtrlpqgfknsptlfdeal
hrdladfriqhpdlillqyvddlllaatseldcqqgtrallqtlgnlgyrasakkaqicq
kqvkylgyllk
>d1mmn_1 2.24.3.1.2 (34-79) Myosin S1 fragment, N-terminal domain {(Dictyostelium discoideum)}
yiwynpdpkerdsyecgeivsetsdsftfktsdgqdrqvkkddanq
>d1mmn_2 3.29.1.5.2 (2-33,80-759) Myosin S1, motor domain {Slime mold (Dictyostelium discoideum)}
npihdrtsdyhkylkvkqgdsdlfkltvsdkrXrnpikfdgvedmselsylnepavfhnl
rvrynqdliytysglflvavnpfkripiytqemvdifkgrrrnevaphifaisdvayrsm
lddrqnqsllitgesgagktentkkviqylasvagrnqangsgvleqqilqanpileafg
nakttrnnnssrfgkfieiqfnnagfisgasiqsylleksrvvfqstternyhifyqlla
gataeekkalhlagpesfnylnqsgcvdikgvsdeeefkitrqamdivgfsqeeqmsifk
iiagilhlgnikfekgagegavlkdktalnaastvfgvnpsvlekalmeprilagrdlva
qhlnvekssssrdalvkalygrlflwlvkkinnvlcserkayfigvldisgfeifkvnsf
eqlcinytneklqqffnhhmfkveqeeylkekinwtfidfgldsqatidlidgrqppgil
alldeqsvfpnatdntlitklhshfskknakyeeprfsktefgvthyagqvmyeiqdwle
knkdplqqdlelcfkdssdnvvtklfndpniasrakkganfitvaaqykeqlaslmatle
ttnphfvrciipnnkqlpakledkvvldqlrcngvlegiritrkgfpnriiyadfvkryy
dlapnvprdaedsqkatdavlkhlnidpeqfrfgitkiffragqlarieeare
>d1mmob_ 1.25.1.2.1 Methane monooxygenase hydrolase, beta and alpha subunits {(Methylococcus capsulatus)}
errrgltdpemaavilkalpeapldgnnkmgyfvtprwkrlteyealtvyaqpnadwiag
gldwgdwtqkfhggrpswgnettelrtvdwfkhrdplrrwhapyvkdkaeewrytdrflq
gysadgqiramnptwrtsscnrywgaflfneyglfnahsqgarealsdvtrvslafwgfd
kidiaqmiqlergflakivpgfdestavpkaewtngevyksarlaveglwqevfdwnesa
fsvhavydalfgqfvrreffqrlaprfgdnltpffinqaqtyfqiakqgvqdlyynclgd
dpefsdynrtvmrnwtgkwleptiaalrdfmglfaklpagttdkeeitaslyrvvddwie
dyasaidfkadrdqivkavlaglk
>d1mmoc_ 1.25.1.2.1 Methane monooxygenase hydrolase, beta and alpha subunits {(Methylococcus capsulatus)}
errrgltdpemaavilkalpeapldgnnkmgyfvtprwkrlteyealtvyaqpnadwiag
gldwgdwtqkfhggrpswgnettelrtvdwfkhrdplrrwhapyvkdkaeewrytdrflq
gysadgqiramnptwrtsscnrywgaflfneyglfnahsqgarealsdvtrvslafwgfd
kidiaqmiqlergflakivpgfdestavpkaewtngevyksarlaveglwqevfdwnesa
fsvhavydalfgqfvrreffqrlaprfgdnltpffinqaqtyfqiakqgvqdlyynclgd
dpefsdynrtvmrnwtgkwleptiaalrdfmglfaklpagttdkeeitaslyrvvddwie
dyasaidfkadrdqivkavlaglk
>d1mmod_ 1.25.1.2.1 Methane monooxygenase hydrolase, beta and alpha subunits {(Methylococcus capsulatus)}
aanraptsvnaqevhrwlqsfnwdfknnrtkyatkykmanetkeqfkliakeyarmeavk
derqfgslqvaltrlnagvrvhpkwnetmkvvsnflevgeynaiaatgmlwdsaqaaeqk
ngylaqvldeirhthqcayvnyyfakngqdpaghndarrtrtigplwkgmkrvfsdgfis
gdavecslnlqlvgeacftnplivavtewaaangdeitptvflsietdelrhmangyqtv
vsiandpasakylntdlnnafwtqqkyftpvlgmlfeygskfkvepwvktwdrwvyedwg
giwigrlgkygvesprslkdakqdaywahhdlyllayalwptgffrlalpdqeemewfea
nypgwydhygkiyeewrargcedpssgfiplmwfiennhpiyidrvsqvpfcpslakgas
tlrvheyngemhtfsdqwgermwlaeperyecqnifeqyegrelseviaelhglrsdgkt
liaqphvrgdklwtlddikrlncvfknpvkaf
>d1mmoe_ 1.25.1.2.1 Methane monooxygenase hydrolase, beta and alpha subunits {(Methylococcus capsulatus)}
aanraptsvnaqevhrwlqsfnwdfknnrtkyatkykmanetkeqfkliakeyarmeavk
derqfgslqvaltrlnagvrvhpkwnetmkvvsnflevgeynaiaatgmlwdsaqaaeqk
ngylaqvldeirhthqcayvnyyfakngqdpaghndarrtrtigplwkgmkrvfsdgfis
gdavecslnlqlvgeacftnplivavtewaaangdeitptvflsietdelrhmangyqtv
vsiandpasakylntdlnnafwtqqkyftpvlgmlfeygskfkvepwvktwdrwvyedwg
giwigrlgkygvesprslkdakqdaywahhdlyllayalwptgffrlalpdqeemewfea
nypgwydhygkiyeewrargcedpssgfiplmwfiennhpiyidrvsqvpfcpslakgas
tlrvheyngemhtfsdqwgermwlaeperyecqnifeqyegrelseviaelhglrsdgkt
liaqphvrgdklwtlddikrlncvfknpvkaf
>d1mmog_ 1.23.1.1.1 Methane monooxygenase hydrolase, gamma subunit {(Methylococcus capsulatus)}
lgihsndtrdawvnkiahvntlekaaemlkqfrmdhttpfrnsyeldndylwieakleek
vavlkarafnevdfrhktafgedaksvldgtvakmnaakdkweaekihigfrqaykppim
pvnyfldgerqlgtrlmelrnlnyydtpleelrkqrgvrvvh
>d1mmoh_ 1.23.1.1.1 Methane monooxygenase hydrolase, gamma subunit {(Methylococcus capsulatus)}
lgihsndtrdawvnkiahvntlekaaemlkqfrmdhttpfrnsyeldndylwieakleek
vavlkarafnevdfrhktafgedaksvldgtvakmnaakdkweaekihigfrqaykppim
pvnyfldgerqlgtrlmelrnlnyydtpleelrkqrgvrvvh
>d1mmpa_ 4.52.1.7.5 Matrilysin (MMP-9) {Human (Homo sapiens)}
yslfpnspkwtskvvtyrivsytrdlphitvdrlvskalnmwgkeiplhfrkvvwgtadi
migfargahgdsypfdgpgntlahafapgtglggdahfdederwtdgsslginflyaath
elghslgmghssdpnavmyptygngdpqnfklsqddikgiqklygk
>d1mmpb_ 4.52.1.7.5 Matrilysin (MMP-9) {Human (Homo sapiens)}
yslfpnspkwtskvvtyrivsytrdlphitvdrlvskalnmwgkeiplhfrkvvwgtadi
migfargahgdsypfdgpgntlahafapgtglggdahfdederwtdgsslginflyaath
elghslgmghssdpnavmyptygngdpqnfklsqddikgiqklygk
>d1mmq__ 4.52.1.7.5 Matrilysin (MMP-9) {Human (Homo sapiens)}
yslfpnspkwtskvvtyrivsytrdlphitvdrlvskalnmwgkeiplhfrkvvwgtadi
migfargahgdsypfdgpgntlahafapgtglggdahfdederwtdgsslginflyaath
elghslgmghssdpnavmyptygngdpqnfklsqddikgiqklygk
>d1mmr__ 4.52.1.7.5 Matrilysin (MMP-9) {Human (Homo sapiens)}
yslfpnspkwtskvvtyrivsytrdlphitvdrlvskalnmwgkeiplhfrkvvwgtadi
migfargahgdsypfdgpgntlahafapgtglggdahfdederwtdgsslginflyaath
elghslgmghssdpnavmyptygngdpqnfklsqddikgiqklygkr
>d1mn1__ 1.72.1.1.4 Manganese peroxidase {Basidomycetos fungus (Phanerochaete chrysosporium)}
avcpdgtrvshaaccafiplaqdlqetifqnecgedahevirltfhdaiaisrsqgpkag
ggadgsmllfptvepnfsanngiddsvnnlipfmqkhntisaadlvqfagavalsncpga
prleflagrpnktiaavdglipepqdsvtkilqrfedaggftpfevvsllashsvarank
vdqtidaapfdstpftfdtqvflevllkgvgfpgsanntgevasplplgsgsdtgemrlq
sdfalahdprtaciwqgfvneqafmaasfraamsklavlghnrnslidcsdvvpvpkpat
gqpamfpastgpqdlelscpserfptlttqpgasqsliahcpdgsmscpgvqfngpa
>d1mn2__ 1.72.1.1.4 Manganese peroxidase {Basidomycetos fungus (Phanerochaete chrysosporium)}
avcpdgtrvshaaccafiplaqdlqetifqnecgqdahevirltfhdaiaisrsqgpkag
ggadgsmllfptvepnfsanngiddsvnnlipfmqkhntisaadlvqfagavalsncpga
prleflagrpnktiaavdglipepqdsvtkilqrfedaggftpfevvsllashsvarank
vdqtidaapfdstpftfdtqvflevllkgvgfpgsanntgevasplplgsgsdtgemrlq
sdfalahdprtaciwqgfvneqafmaasfraamsklavlghnrnslidcsdvvpvpkpat
gqpamfpastgpqdlelscpserfptlttqpgasqsliahcpdgsmscpgvqfngpa
>d1mnc__ 4.52.1.7.2 Neutrophil collagenase (MMP-8) {Human (Homo sapiens)}
gpkwertnltyrirnytpqlseaeveraikdafelwsvaspliftgisqgeadiniafyq
rdhgdgspfdgpngilahafqpgqgiggdahfdaeetwtntsanynlflvaahefghslg
lahssdpgalmypnyafretsnyslpqddidgiqaiyg
>d1mnd_1 2.24.3.1.2 (34-79) Myosin S1 fragment, N-terminal domain {(Dictyostelium discoideum)}
yiwynpdpderdsyecgeivsetsdsftfktvdgqdrqvkkddanq
>d1mnd_2 3.29.1.5.2 (2-33,80-690) Myosin S1, motor domain {Slime mold (Dictyostelium discoideum)}
npihdrtsdyhkylkvkqgdsdlfkltvsdkrXrnpikfdgvedmselsylnepavfhnl
rvrynqdliytysglflvavnpfkripiytqemvdifkgrrrnevaphifaisdvayrsm
lddrqnqsllitgesgagktentkkviqylasvagrnqangsgvleqqilqanpileafg
nakttrnnnssrfgkfieiqfnnagfisgasiqsylleksrvvfqseternyhifyqlla
gataeekkalhlagpesfnylnqsgcvdikgvsdedefkitrqamdivgfsqeeqmsifk
iiagilhlgnikfekgagegavlkdktalnaastvfgvnpsvlekalmeprilagrdlva
qhlnvekssssrdalvkalygrlflwlvkkinnvlcseraayfigvldisgfeifkvnsf
eqlcinytneklqqffnhhmfkveqeeylkekinwtfidfgldsqatidlidgrqppgil
alldeqsvfpnatdntlitklhshfskknakyeeprfsktefgvthyagqvmyeiqdwle
knkdplqqdlelcfkdssdnvvtklfndpniasrakkganfitvaaqykeqlaslmatle
ttnphfvrciipnnkqlpakledkvvldqlrcngvlegiritrk
>d1mne_1 2.24.3.1.2 (34-79) Myosin S1 fragment, N-terminal domain {(Dictyostelium discoideum)}
yiwynpdpderdsyecgeivsetsdsftfktvdgqdrqvkkddanq
>d1mne_2 3.29.1.5.2 (2-33,80-759) Myosin S1, motor domain {Slime mold (Dictyostelium discoideum)}
npihdrtsdyhkylkvkqgdsdlfkltvsdkrXrnpikfdgvedmselsylnepavfhnl
rvrynqdliytysglflvavnpfkripiytqemvdifkgrrrnevaphifaisdvayrsm
lddrqnqsllitgesgagktentkkviqylasvagrnqangsgvleqqilqanpileafg
nakttrnnnssrfgkfieiqfnnagfisgasiqsylleksrvvfqseternyhifyqlla
gataeekkalhlagpesfnylnqsgcvdikgvsdedefkitrqamdivgfsqeeqmsifk
iiagilhlgnikfekgagegavlkdktalnaastvfgvnpsvlekalmeprilagrdlva
qhlnvekssssrdalvkalygrlflwlvkkinnvlcseraayfigvldisgfeifkvnsf
eqlcinytneklqqffnhhmfkveqeeylkekinwtfidfgldsqatidlidgrqppgil
alldeqsvfpnatdntlitklhshfskknakyeeprfsktefgvthyagqvmyeiqdwle
knkdplqqdlelcfkdssdnvvtklfndpniasrakkganfitvaaqykeqlaslmatle
ttnphfvrciipnnkqlpakledkvvldqlrcngvlegiritrkgfpnriiyadfvkryy
llapnvprdaedsqkatdavlkhlnidpeqyrfgitkiffragqlarieeare
>d1mnga1 1.2.4.1.6 (1-92) Mn superoxide dismutase (SOD) {(Thermus thermophilus)}
pypfklpdlgypyealephidaktmeihhqkhhgayvtnlnaalekypylhgvevevllr
hlaalpqdiqtavrnnggghlnhslfwrlltp
>d1mnga2 4.26.1.1.2 (93-203) Mn superoxide dismutase (SOD) {(Thermus thermophilus)}
ggakepvgelkkaideqfggfqalkekltqaamgrfgsgwawlvkdpfgklhvlstpnqd
npvmegftpivgidvwehayylkyqnrradylqaiwnvlnwdvaeeffkka
>d1mngb1 1.2.4.1.6 (1-92) Mn superoxide dismutase (SOD) {(Thermus thermophilus)}
pypfklpdlgypyealephidaktmeihhqkhhgayvtnlnaalekypylhgvevevllr
hlaalpqdiqtavrnnggghlnhslfwrlltp
>d1mngb2 4.26.1.1.2 (93-203) Mn superoxide dismutase (SOD) {(Thermus thermophilus)}
ggakepvgelkkaideqfggfqalkekltqaamgrfgsgwawlvkdpfgklhvlstpnqd
npvmegftpivgidvwehayylkyqnrradylqaiwnvlnwdvaeeffkka
>d1mnh__ 1.1.1.1.7 Myoglobin {pig (Sus scrofa)}
glsdgewqlvlnvwgkveadvaghgqevlirlfkghpetlekfdkfkhlksedemkased
lkkvgnrvltalggilkkkghheaeltplaqshatkhkipvkylefiseaiiqvlqskhp
gdfgadaqgamskalelfrndmaakykelgfqg
>d1mnia_ 1.1.1.1.9 Myoglobin {human (Homo sapiens)}
glsdgewqlvlnvwgkveadvaghgqevlirlfkghpetlekfdkfkhlksedemkased
lkkvgnthltalggilkkkghheaeltplaqshatkhkipvkylefiseaiiqvlqskhp
gdfgadaqgamskalelfrndmaakykelgfqg
>d1mnib_ 1.1.1.1.9 Myoglobin {human (Homo sapiens)}
glsdgewqlvlnvwgkveadvaghgqevlirlfkghpetlekfdkfkhlksedemkased
lkkvgnthltalggilkkkghheaeltplaqshatkhkipvkylefiseaiiqvlqskhp
gdfgadaqgamskalelfrndmaakykelgfqg
>d1mnja_ 1.1.1.1.9 Myoglobin {human (Homo sapiens)}
glsdgewqlvlnvwgkveadvaghgqevlirlfkghpetlekfdkfkhlksedemkased
lkkvgntiltalggilkkkghheaeltplaqshatkhkipvkylefiseaiiqvlqskhp
gdfgadaqgamskalelfrndmaakykelgfqg
>d1mnjb_ 1.1.1.1.9 Myoglobin {human (Homo sapiens)}
glsdgewqlvlnvwgkveadvaghgqevlirlfkghpetlekfdkfkhlksedemkased
lkkvgntiltalggilkkkghheaeltplaqshatkhkipvkylefiseaiiqvlqskhp
gdfgadaqgamskalelfrndmaakykelgf
>d1mnka_ 1.1.1.1.9 Myoglobin {human (Homo sapiens)}
glsdgewqlvlnvwgkveadvaghgqevlirlfkghpetlekfdkfkhlksedemkased
lkkvgnttltalggilkkkghheaeltplaqshatkhkipvkylefiseaiiqvlqskhp
gdfgadaqgamskalelfrndmaakykelgf
>d1mnkb_ 1.1.1.1.9 Myoglobin {human (Homo sapiens)}
glsdgewqlvlnvwgkveadvaghgqevlirlfkghpetlekfdkfkhlksedemkased
lkkvgnttltalggilkkkghheaeltplaqshatkhkipvkylefiseaiiqvlqskhp
gdfgadaqgamskalelfrndmaakykelgf
>d1mnma_ 4.49.1.1.2 MCM1 transcriptional regulator {Baker's yeast (Saccharomyces cerevisiae)}
qkerrkieikfienktrrhvtfskrkhgimkkafelsvltgtqvlllvvsetglvytfst
pkfepivtqqegrnliqaclnapdd
>d1mnmb_ 4.49.1.1.2 MCM1 transcriptional regulator {Baker's yeast (Saccharomyces cerevisiae)}
rrkieikfienktrrhvtfskrkhgimkkafelsvltgtqvlllvvsetglvytfstpkf
epivtqqegrnliqaclnapd
>d1mnmc_ 1.4.1.1.3 mat alpha2 Homeodomain {baker's yeast (Saccharomyces cerevisiae)}
glvfnvvtqdminkstkpyrghrftkenvrileswfaknienpyldtkglenlmkntsls
riqiknwvsnrrrkekt
>d1mnmd_ 1.4.1.1.3 mat alpha2 Homeodomain {baker's yeast (Saccharomyces cerevisiae)}
glvfnvvtqdminkstkpyrghrftkenvrileswfaknienpyldtkglenlmkntsls
riqiknwvsnrrrkekt
>d1mnp__ 1.72.1.1.4 Manganese peroxidase {Basidomycetos fungus (Phanerochaete chrysosporium)}
avcpdgtrvshaaccafiplaqdlqetifqnecgedahevirltfhdaiaisrsqgpkag
ggadgsmllfptvepnfsanngiddsvnnlipfmqkhntisaadlvqfagavalsncpga
prleflagrpnktiaavdglipepqdsvtkilqrfedaggftpfevvsllashsvaradk
vdqtidaapfdstpftfdtqvflevllkgvgfpgsanntgevasplplgsgsdtgemrlq
sdfalahdprtaciwqgfvneqafmaasfraamsklavlghnrnslidcsdvvpvpkpat
gqpamfpastgpqdlelscpserfptlttqpgasqsliahcpdgsmscpgvqfngpa
>d1mns_1 3.1.6.2.2 (133-359) Mandelate racemase {(Pseudomonas putida)}
pvqaydshsldgvklateravtaaelgfravktkigypaldqdlavvrsirqavgddfgi
mvdynqsldvpaaikrsqalqqegvtwieeptlqhdyeghqriqsklnvpvqmgenwlgp
eemfkalsigacrlampdamkiggvtgwirasalaqqfgipmsshlfqeisahllaatpt
ahwlerldlagsvieptltfeggnavipdlpgvgiiwrekeigkylv
>d1mns_2 4.32.1.1.4 (3-132) Mandelate racemase {(Pseudomonas putida)}
evlitglrtravnvplaypvhtavgtvgtaplvlidlatsagvvghsylfaytpvalksl
kqllddmaamivneplapvsleamlakrfclagytglirmaaagidmaawdalgkvhetp
lvkllganar
>d1mnta_ 1.41.1.1.2 Mnt repressor {(Salmonella )bacteriophage P22}
arddphfnfrmpmevreklkfraeangrsmnsellqivqdalskpspvtgyrndaerlad
eqselv
>d1mntb_ 1.41.1.1.2 Mnt repressor {(Salmonella )bacteriophage P22}
arddphfnfrmpmevreklkfraeangrsmnsellqivqdalskpspvtgyrndaerlad
eqselv
>d1moa__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdifirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1mob__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkggvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1moc__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkktgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1mod__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkktgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1moh__ 1.1.1.1.2 Hemoglobin I {clam (Lucina pectinata)}
sleaaqksnvtsswakasaawgtagpeffmalfdahddvfakfsglfsgaakgtvkntpe
maaqaqsfkglvsnwvdnldnagalegqcktfaanhkargisagqleaafkvlsgfmksy
ggdegawtavagalmgeiepdm
>d1mola_ 4.13.1.1.1 Monellin, B & A chains together {serendipity berry (Dioscoreophyllum cumminsii diels)}
geweiidigpftqnlgkfavdeenkigqygrltfnkvirpcmkktiyenereikgyeyql
yvyasdklfradisedyktrgrkllrfngpvppp
>d1molb_ 4.13.1.1.1 Monellin, B & A chains together {serendipity berry (Dioscoreophyllum cumminsii diels)}
geweiidigpftqnlgkfavdeenkigqygrltfnkvirpcmkktiyenereikgyeyql
yvyasdklfradisedyktrgrkllrfngpvppp
>d1mom__ 4.102.1.1.3 alpha-Momorcharin (momordin) {bitter melon (Momordica charantia)}
dvsfrlsgadprsygmfikdlrnalpfrekvyniplllpsvsgagryllmhlfnydgkti
tvaldvtnvyimgyladttsyffnepaaelasqyvfrdarrkitlpysgnyerlqiaagk
prekipiglpaldsaistllhydstaaagallvliqttaeaarfkyieqqiqerayrdev
pslatislenswsglskqiqlaqgnngifrtpivlvdnkgnrvqitnvtskvvtsniqll
lntrni
>d1mpah1 2.1.1.1.79 (1-121) Immunoglobulin (variable domains of L and H chains) {Bactericidal Fab (mouse), kappa L chain}
evnlqqsgtvlarpgasvrmsckasgysftsywlhwikqrpgqglewiggiypgnrdtry
tqrfkdkakltavtsantaymelssltnedsavyycsiiyfdyadfimdywgqgttvtvs
s
>d1mpah2 2.1.1.2.82 (122-225) Immunoglobulin (constant domains of L and H chains) {Bactericidal Fab (mouse), kappa L chain}
akttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsd
lytlsssvtvtsstwpsqsitcnvahpasstkvdkkieprgpti
>d1mpal1 2.1.1.1.79 (1-112) Immunoglobulin (variable domains of L and H chains) {Bactericidal Fab (mouse), kappa L chain}
divmtqtplslpvslgdkasiscrssqalvhsngntylhwylqkpgqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvffcsqsthvprtfgggtkleik
>d1mpal2 2.1.1.2.82 (113-219) Immunoglobulin (constant domains of L and H chains) {Bactericidal Fab (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1mpb__ 3.82.1.1.6 D-maltodextrin-binding protein {(Escherichia coli)}
kieegklviwingdkgynglaevgkkfekdtgikvtvehpdkleekfpqvaatgdgpdii
fwahdrfggyaqsgllaeitpdkafqdklypftwdavryngkliaypiavealsliynkd
llpnppktweeipaldkelkakgksalmfnlqepyftwpliaadggyafkyengkydikd
vgvdnagakagltflvdliknkhmnadtdysiaeaafnkgetamtingprawsnidtskv
nygvtvlptfkgqpskpfvgvlsaginaaspnkelakeflenylltdegleavnkdkplg
avalksyeeelakdpriaatmenaqkgeimpnipqmsafwyavrtavinaasgrqtvdea
lkdaqtritk
>d1mpc__ 3.82.1.1.6 D-maltodextrin-binding protein {(Escherichia coli)}
kieegklviwingdkgynglaevgkkfekdtgikvtvehpdkleekfpqvaatgdgpdii
fwahdrfggyaqsgllaeitpdkafqdklypftwdavryngkliaypiavealsliynkd
llpnppktweeipaldkelkakgksalmfnlqepyftwpliaadggyafkyengkydikd
vgvdnagakagltflvdliknkhmnadtdysiaeaafnkgetamtingprawsnidtskv
nygvtvlptfkgqpskpfvgvlsaginaaspnkelakeflenylltdegleavnkdkplg
avalksyeeelakdpriaatmenaqkgeimpnipqmsafwyavrtavinaasgrqtvdea
lkdaqtritk
>d1mpd__ 3.82.1.1.6 D-maltodextrin-binding protein {(Escherichia coli)}
kieegklviwingdkgynglaevgkkfekdtgikvtvehpdkleekfpqvaatgdgpdii
fwahdrfggyaqsgllaeitpdkafqdklypftwdavryngkliaypiavealsliynkd
llpnppktweeipaldkelkakgksalmfnlqepyftwpliaadggyafkyengkydikd
vgvdnagakagltflvdliknkhmnadtdysiaeaafnkgetamtingprawsnidtskv
nygvtvlptfkgqpskpfvgvlsaginaaspnkelakeflenylltdegleavnkdkplg
avalksyeeelakdpriaatmenaqkgeimpnipqmsafwyavrtavinaasgrqtvdea
lkdaqtritk
>d1mpf__ 6.7.1.1.1 Porin {(Escherichia coli)}
aeiynkdgnkvdlygkavglhyfskgngensyggngdmtyarlgfkgetqinsdltgygq
weynfqgnnsegadaqtgnktrlafaglkyadvgsfdygrnygvvydalgytdmlpefdg
dtaysddffvgrvggvatyrnsnffglvdglnfavqylgknerdtarrsngdgvggsisy
eyegfgivgaygaadrtnlqeaqplgngkkaeqwatglkydanniylaanygetrnatpi
tnkftntsgfanktqdvllvaqyqfdfglrpsiaytkskakdvegigdvdlvnyfevgat
yyfnknmstyvdyiinqidsdnklgvgsddtvavgivyqf
>d1mpga1 1.74.1.2.1 (100-282) 3-Methyladenine DNA glycosylase II (gene alkA or aidA), 2 C-terminal domains {(Escherichia coli)}
aarpglrlpgcvdafeqgvrailgqlvsvamaakltarvaqlygerlddfpeyicfptpq
rlaaadpqalkalgmplkraealihlanaalegtlpmtipgdveqamktlqtfpgigrwt
anyfalrgwqakdvflpddylikqrfpgmtpaqirryaerwkpwrsyallhiwytegwqp
dea
>d1mpga2 4.79.1.2.1 (1-99) 3-Methyladenine DNA glycosylase II (gene alkA or aidA), N-terminal domain {(Escherichia coli)}
mytlnwqppydwswmlgflaaravssvetvadsyyarslavgeyrgvvtaipdiarhtlh
inlsaglepvaaeclakmsrlfdlqcnpqivngalgrlg
>d1mpgb1 1.74.1.2.1 (100-282) 3-Methyladenine DNA glycosylase II (gene alkA or aidA), 2 C-terminal domains {(Escherichia coli)}
aarpglrlpgcvdafeqgvrailgqlvsvamaakltarvaqlygerlddfpeyicfptpq
rlaaadpqalkalgmplkraealihlanaalegtlpmtipgdveqamktlqtfpgigrwt
anyfalrgwqakdvflpddylikqrfpgmtpaqirryaerwkpwrsyallhiwytegwqp
dea
>d1mpgb2 4.79.1.2.1 (1-99) 3-Methyladenine DNA glycosylase II (gene alkA or aidA), N-terminal domain {(Escherichia coli)}
mytlnwqppydwswmlgflaaravssvetvadsyyarslavgeyrgvvtaipdiarhtlh
inlsaglepvaaeclakmsrlfdlqcnpqivngalgrlg
>d1mph__ 2.41.1.1.2 beta-spectrin {mouse (Mus musculus) brain}
megflnrkheweahnkkassrswhnvycvinnqemgfykdaksaasgipyhsevpvslke
aicevaldykkkkhvfklrlsdgneylfqakddeemntwiqaissa
>e1mpj.1a 7.1.1.1.3 Insulin {pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e1mpj.1b 7.1.1.1.3 Insulin {pig (Sus scrofa)}
vnqhlcgshlvealylvcgergffytpk
>e1mpj.2c 7.1.1.1.3 Insulin {pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e1mpj.2d 7.1.1.1.3 Insulin {pig (Sus scrofa)}
fvnqhlcgshlvealylvcgergffytpka
>d1mpma_ 6.7.1.2.1 Maltoporin (also LamB protein) {(Escherichia coli)}
vdfhgyarsgigwtgsggeqqcfqttgaqskyrlgnecetyaelklgqevwkegdksfyf
dtnvaysvaqqndweatdpafreanvqgknliewlpgstiwagkrfyqrhdvhmidfyyw
disgpgaglenidvgfgklslaatrsseaggsssfasnniydytnetandvfdvrlaqme
inpggtlelgvdygranlrdnyrlvdgaskdgwlftaehtqsvlkgfnkfvvqyatdsmt
sqgkglsqgsgvafdnekfayninnnghmlrildhgaismgdnwdmmyvgmyqdinwdnd
ngtkwwtvgirpmykwtpimstvmeigydnvesqrtgdknnqykitlaqqwqagdsiwsr
pairvfatyakwdekwgydytgnadnnanfgkavpadfnggsfgrgdsdewtfgaqmeiw
w
>d1mpmb_ 6.7.1.2.1 Maltoporin (also LamB protein) {(Escherichia coli)}
vdfhgyarsgigwtgsggeqqcfqttgaqskyrlgnecetyaelklgqevwkegdksfyf
dtnvaysvaqqndweatdpafreanvqgknliewlpgstiwagkrfyqrhdvhmidfyyw
disgpgaglenidvgfgklslaatrsseaggsssfasnniydytnetandvfdvrlaqme
inpggtlelgvdygranlrdnyrlvdgaskdgwlftaehtqsvlkgfnkfvvqyatdsmt
sqgkglsqgsgvafdnekfayninnnghmlrildhgaismgdnwdmmyvgmyqdinwdnd
ngtkwwtvgirpmykwtpimstvmeigydnvesqrtgdknnqykitlaqqwqagdsiwsr
pairvfatyakwdekwgydytgnadnnanfgkavpadfnggsfgrgdsdewtfgaqmeiw
w
>d1mpmc_ 6.7.1.2.1 Maltoporin (also LamB protein) {(Escherichia coli)}
vdfhgyarsgigwtgsggeqqcfqttgaqskyrlgnecetyaelklgqevwkegdksfyf
dtnvaysvaqqndweatdpafreanvqgknliewlpgstiwagkrfyqrhdvhmidfyyw
disgpgaglenidvgfgklslaatrsseaggsssfasnniydytnetandvfdvrlaqme
inpggtlelgvdygranlrdnyrlvdgaskdgwlftaehtqsvlkgfnkfvvqyatdsmt
sqgkglsqgsgvafdnekfayninnnghmlrildhgaismgdnwdmmyvgmyqdinwdnd
ngtkwwtvgirpmykwtpimstvmeigydnvesqrtgdknnqykitlaqqwqagdsiwsr
pairvfatyakwdekwgydytgnadnnanfgkavpadfnggsfgrgdsdewtfgaqmeiw
w
>d1mpna_ 6.7.1.2.1 Maltoporin (also LamB protein) {(Escherichia coli)}
vdfhgyarsgigwtgsggeqqcfqttgaqskyrlgnecetyaelklgqevwkegdksfyf
dtnvaysvaqqndweatdpafreanvqgknliewlpgstiwagkrfyqrhdvhmidfyyw
disgpgaglenidvgfgklslaatrsseaggsssfasnniydytnetandvfdvrlaqme
inpggtlelgvdygranlrdnyrlvdgaskdgwlftaehtqsvlkgfnkfvvqyatdsmt
sqgkglsqgsgvafdnekfayninnnghmlrildhgaismgdnwdmmyvgmyqdinwdnd
ngtkwwtvgirpmykwtpimstvmeigydnvesqrtgdknnqykitlaqqwqagdsiwsr
pairvfatyakwdekwgydytgnadnnanfgkavpadfnggsfgrgdsdewtfgaqmeiw
w
>d1mpnb_ 6.7.1.2.1 Maltoporin (also LamB protein) {(Escherichia coli)}
vdfhgyarsgigwtgsggeqqcfqttgaqskyrlgnecetyaelklgqevwkegdksfyf
dtnvaysvaqqndweatdpafreanvqgknliewlpgstiwagkrfyqrhdvhmidfyyw
disgpgaglenidvgfgklslaatrsseaggsssfasnniydytnetandvfdvrlaqme
inpggtlelgvdygranlrdnyrlvdgaskdgwlftaehtqsvlkgfnkfvvqyatdsmt
sqgkglsqgsgvafdnekfayninnnghmlrildhgaismgdnwdmmyvgmyqdinwdnd
ngtkwwtvgirpmykwtpimstvmeigydnvesqrtgdknnqykitlaqqwqagdsiwsr
pairvfatyakwdekwgydytgnadnnanfgkavpadfnggsfgrgdsdewtfgaqmeiw
w
>d1mpnc_ 6.7.1.2.1 Maltoporin (also LamB protein) {(Escherichia coli)}
vdfhgyarsgigwtgsggeqqcfqttgaqskyrlgnecetyaelklgqevwkegdksfyf
dtnvaysvaqqndweatdpafreanvqgknliewlpgstiwagkrfyqrhdvhmidfyyw
disgpgaglenidvgfgklslaatrsseaggsssfasnniydytnetandvfdvrlaqme
inpggtlelgvdygranlrdnyrlvdgaskdgwlftaehtqsvlkgfnkfvvqyatdsmt
sqgkglsqgsgvafdnekfayninnnghmlrildhgaismgdnwdmmyvgmyqdinwdnd
ngtkwwtvgirpmykwtpimstvmeigydnvesqrtgdknnqykitlaqqwqagdsiwsr
pairvfatyakwdekwgydytgnadnnanfgkavpadfnggsfgrgdsdewtfgaqmeiw
w
>d1mpoa_ 6.7.1.2.1 Maltoporin (also LamB protein) {(Escherichia coli)}
vdfhgyarsgigwtgsggeqqcfqttgaqskyrlgnecetyaelklgqevwkegdksfyf
dtnvaysvaqqndweatdpafreanvqgknliewlpgstiwagkrfyqrhdvhmidfyyw
disgpgaglenidvgfgklslaatrsseaggsssfasnniydytnetandvfdvrlaqme
inpggtlelgvdygranlrdnyrlvdgaskdgwlftaehtqsvlkgfnkfvvqyatdsmt
sqgkglsqgsgvafdnekfayninnnghmlrildhgaismgdnwdmmyvgmyqdinwdnd
ngtkwwtvgirpmykwtpimstvmeigydnvesqrtgdknnqykitlaqqwqagdsiwsr
pairvfatyakwdekwgydytgnadnnanfgkavpadfnggsfgrgdsdewtfgaqmeiw
w
>d1mpob_ 6.7.1.2.1 Maltoporin (also LamB protein) {(Escherichia coli)}
vdfhgyarsgigwtgsggeqqcfqttgaqskyrlgnecetyaelklgqevwkegdksfyf
dtnvaysvaqqndweatdpafreanvqgknliewlpgstiwagkrfyqrhdvhmidfyyw
disgpgaglenidvgfgklslaatrsseaggsssfasnniydytnetandvfdvrlaqme
inpggtlelgvdygranlrdnyrlvdgaskdgwlftaehtqsvlkgfnkfvvqyatdsmt
sqgkglsqgsgvafdnekfayninnnghmlrildhgaismgdnwdmmyvgmyqdinwdnd
ngtkwwtvgirpmykwtpimstvmeigydnvesqrtgdknnqykitlaqqwqagdsiwsr
pairvfatyakwdekwgydytgnadnnanfgkavpadfnggsfgrgdsdewtfgaqmeiw
w
>d1mpoc_ 6.7.1.2.1 Maltoporin (also LamB protein) {(Escherichia coli)}
vdfhgyarsgigwtgsggeqqcfqttgaqskyrlgnecetyaelklgqevwkegdksfyf
dtnvaysvaqqndweatdpafreanvqgknliewlpgstiwagkrfyqrhdvhmidfyyw
disgpgaglenidvgfgklslaatrsseaggsssfasnniydytnetandvfdvrlaqme
inpggtlelgvdygranlrdnyrlvdgaskdgwlftaehtqsvlkgfnkfvvqyatdsmt
sqgkglsqgsgvafdnekfayninnnghmlrildhgaismgdnwdmmyvgmyqdinwdnd
ngtkwwtvgirpmykwtpimstvmeigydnvesqrtgdknnqykitlaqqwqagdsiwsr
pairvfatyakwdekwgydytgnadnnanfgkavpadfnggsfgrgdsdewtfgaqmeiw
w
>d1mpp__ 2.38.1.2.11 Pepsin {(Mucor pusillus)}
gsvdtpglydfdleeyaipvsigtpgqdfyllfdtgssdtwvphkgcdnsegcvgkrffd
psssstfketdynlnitygtggangiyfrdsitvggatvkqqtlayvdnvsgptaeqspd
selfldgifgaaypdntameaeygdtyntvhvnlykqglisspvfsvymntndgggqvvf
ggvnntllggdiqytdvlksrggyffwdapvtgvkidgsdavsfdgaqaftidtgtnffi
apssfaekvvkaalpdatesqqgytvpcskyqdskttfslvlqksgsssdtidvsvpisk
mllpvdksgetcmfivlpdggnqfivgnlflrffvnvydfgknrigfaplasgyend
>d1mpqa_ 6.7.1.2.1 Maltoporin (also LamB protein) {(Escherichia coli)}
vdfhgyarsgigwtgsggeqqcfqttgaqskyrlgnecetyaelklgqevwkegdksfyf
dtnvaysvaqqndweatdpafreanvqgknliewlpgstiwagkrfyqrhdvhmidfyyw
disgpgaglenidvgfgklslaatrsseaggsssfasnniydytnetandvfdvrlaqme
inpggtlelgvdygranlrdnyrlvdgaskdgwlftaehtqsvlkgfnkfvvqyatdsmt
sqgkglsqgsgvafdnekfayninnnghmlrildhgaismgdnwdmmyvgmyqdinwdnd
ngtkwwtvgirpmykwtpimstvmeigydnvesqrtgdknnqykitlaqqwqagdsiwsr
pairvfatyakwdekwgydytgnadnnanfgkavpadfnggsfgrgdsdewtfgaqmeiw
w
>d1mpqb_ 6.7.1.2.1 Maltoporin (also LamB protein) {(Escherichia coli)}
vdfhgyarsgigwtgsggeqqcfqttgaqskyrlgnecetyaelklgqevwkegdksfyf
dtnvaysvaqqndweatdpafreanvqgknliewlpgstiwagkrfyqrhdvhmidfyyw
disgpgaglenidvgfgklslaatrsseaggsssfasnniydytnetandvfdvrlaqme
inpggtlelgvdygranlrdnyrlvdgaskdgwlftaehtqsvlkgfnkfvvqyatdsmt
sqgkglsqgsgvafdnekfayninnnghmlrildhgaismgdnwdmmyvgmyqdinwdnd
ngtkwwtvgirpmykwtpimstvmeigydnvesqrtgdknnqykitlaqqwqagdsiwsr
pairvfatyakwdekwgydytgnadnnanfgkavpadfnggsfgrgdsdewtfgaqmeiw
w
>d1mpqc_ 6.7.1.2.1 Maltoporin (also LamB protein) {(Escherichia coli)}
vdfhgyarsgigwtgsggeqqcfqttgaqskyrlgnecetyaelklgqevwkegdksfyf
dtnvaysvaqqndweatdpafreanvqgknliewlpgstiwagkrfyqrhdvhmidfyyw
disgpgaglenidvgfgklslaatrsseaggsssfasnniydytnetandvfdvrlaqme
inpggtlelgvdygranlrdnyrlvdgaskdgwlftaehtqsvlkgfnkfvvqyatdsmt
sqgkglsqgsgvafdnekfayninnnghmlrildhgaismgdnwdmmyvgmyqdinwdnd
ngtkwwtvgirpmykwtpimstvmeigydnvesqrtgdknnqykitlaqqwqagdsiwsr
pairvfatyakwdekwgydytgnadnnanfgkavpadfnggsfgrgdsdewtfgaqmeiw
w
>d1mpra_ 6.7.1.2.2 Maltoporin (also LamB protein) {(Salmonella typhimurium)}
vdfhgyarsgigwtgsggeqqcfqatgaqskyrlgnecetyaelklgqevwkegdksfyf
dtnvaysvnqqndwestdpafreanvqgknliewlpgstiwagkrfyqrhdvhmidfyyw
disgpgagienidlgfgklslaatrsteaggsytfssqniydevkdtandvfdvrlaglq
tnpdgvlelgvdygranttdgykladgaskdgwmftaehtqsmlkgynkfvvqyatdamt
tqgkgqargsdgsssfteelsdgtkinyankvinnngnmwrildhgaislgdkwdlmyvg
myqnidwdnnlgtewwtvgvrpmykwtpimstllevgydnvksqqtgdrnnqykitlaqq
wqagdsiwsrpairifatyakwdekwgyikdgdnisryaaatnsgistnsrgdsdewtfg
aqmeiww
>d1mprb_ 6.7.1.2.2 Maltoporin (also LamB protein) {(Salmonella typhimurium)}
vdfhgyarsgigwtgsggeqqcfqatgaqskyrlgnecetyaelklgqevwkegdksfyf
dtnvaysvnqqndwestdpafreanvqgknliewlpgstiwagkrfyqrhdvhmidfyyw
disgpgagienidlgfgklslaatrsteaggsytfssqniydevkdtandvfdvrlaglq
tnpdgvlelgvdygranttdgykladgaskdgwmftaehtqsmlkgynkfvvqyatdamt
tqgkgqargsdgsssfteelsdgtkinyankvinnngnmwrildhgaislgdkwdlmyvg
myqnidwdnnlgtewwtvgvrpmykwtpimstllevgydnvksqqtgdrnnqykitlaqq
wqagdsiwsrpairifatyakwdekwgyikdgdnisryaaatnsgistnsrgdsdewtfg
aqmeiww
>d1mprc_ 6.7.1.2.2 Maltoporin (also LamB protein) {(Salmonella typhimurium)}
vdfhgyarsgigwtgsggeqqcfqatgaqskyrlgnecetyaelklgqevwkegdksfyf
dtnvaysvnqqndwestdpafreanvqgknliewlpgstiwagkrfyqrhdvhmidfyyw
disgpgagienidlgfgklslaatrsteaggsytfssqniydevkdtandvfdvrlaglq
tnpdgvlelgvdygranttdgykladgaskdgwmftaehtqsmlkgynkfvvqyatdamt
tqgkgqargsdgsssfteelsdgtkinyankvinnngnmwrildhgaislgdkwdlmyvg
myqnidwdnnlgtewwtvgvrpmykwtpimstllevgydnvksqqtgdrnnqykitlaqq
wqagdsiwsrpairifatyakwdekwgyikdgdnisryaaatnsgistnsrgdsdewtfg
aqmeiww
>d1mpt__ 3.33.1.1.9 M-proteinase {(Bacillus sp. ksm-k16)}
aqsvpwgisrvqapaahnrgltgsgvkvavldtgisthpdlnirggasfvpgepstqdgn
ghgthvagtiaalnnsigvlgvapsaelyavkvlgasgsgsvssiaqglewagnngmhva
nlslgspspsatleqavnsatsrgvlvvaasgnsgagsisyparyanamavgatdqnnnr
asfsqygagldivapgvnvqstypgstyaslngtsmatphvagvaalvkqknpswsnvqi
rnhlkntatglgntnlygsglvnaeaatr
>d1mra_1 3.1.6.2.2 (133-359) Mandelate racemase {(Pseudomonas putida)}
pvqaydshsldgvklateravtaaelgfravktkigypaldqdlavvrsirqavgddfgi
mvdynqsldvpaaikrsqalqqegvtwieeptlqhdyeghqriqsklnvpvqmgenwlgp
eemfkalsigacrlampnamkiggvtgwirasalaqqfgipmsshlfqeisahllaatpt
ahwlerldlagsvieptltfeggnavipdlpgvgiiwrekeigkylv
>d1mra_2 4.32.1.1.4 (3-132) Mandelate racemase {(Pseudomonas putida)}
evlitglrtravnvplaypvhtavgtvgtaplvlidlatsagvvghsylfaytpvalksl
kqllddmaamivneplapvsleamlakrfclagytglirmaaagidmaawdalgkvhetp
lvkllganar
>d1mrb__ 7.38.1.1.2 Metallothionein {(rabbit )}
ksccsccppgcakcaqgcickgasdkcscca
>d1mrch1 2.1.1.1.48 (1-115) Immunoglobulin (variable domains of L and H chains) {Fab Jel 103 (mouse), kappa L chain}
qvqlqqsgaelvkpgasvklsckasgytftsywmqwvkqrpgqglewigeidpsdsytny
nqkfkgkatltvdtssstaymqlssltsedsavyycanlrgyfdywgqgttltvssak
>d1mrch2 2.1.1.2.55 (116-227) Immunoglobulin (constant domains of L and H chains) {Fab Jel 103 (mouse), kappa L chain}
ttppsvyplapgcgdttgssvtlgclvkgyfpesvtvtwnsgslsssvhtfpallqsgly
tmsssvtvpsstwpsqtvtcsvahpassttvdkklep
>d1mrcl1 2.1.1.1.48 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab Jel 103 (mouse), kappa L chain}
dvvmtqtplslpvslgdqasiscrssqslvhsngntylhwylqkpgqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyfcsqsthvprtfgggtkleikr
>d1mrcl2 2.1.1.2.55 (109-211) Immunoglobulin (constant domains of L and H chains) {Fab Jel 103 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgkerqngvlnswtdqns
kdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1mrdh1 2.1.1.1.48 (2-115) Immunoglobulin (variable domains of L and H chains) {Fab Jel 103 (mouse), kappa L chain}
vqlqqsgaelvkpgasvklsckasgytftsywmqwvkqrpgqglewigeidpsdsytnyn
qkfkgkatltvdtssstaymqlssltsedsavyycanlrgyfdywgqgttltvssak
>d1mrdh2 2.1.1.2.55 (116-227) Immunoglobulin (constant domains of L and H chains) {Fab Jel 103 (mouse), kappa L chain}
ttppsvyplapgcgdttgssvtlgclvkgyfpesvtvtwnsgslsssvhtfpallqsgly
tmsssvtvpsstwpsqtvtcsvahpassttvdkklep
>d1mrdl1 2.1.1.1.48 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab Jel 103 (mouse), kappa L chain}
dvvmtqtplslpvslgdqasiscrssqslvhsngntylhwylqkpgqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyfcsqsthvprtfgggtkleikr
>d1mrdl2 2.1.1.2.55 (109-211) Immunoglobulin (constant domains of L and H chains) {Fab Jel 103 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgkerqngvlnswtdqns
kdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1mreh1 2.1.1.1.48 (1-115) Immunoglobulin (variable domains of L and H chains) {Fab Jel 103 (mouse), kappa L chain}
qvqlqqsgaelvkpgasvklsckasgytftsywmqwvkqrpgqglewigeidpsdsytny
nqkfkgkatltvdtssstaymqlssltsedsavyycanlrgyfdywgqgttltvssak
>d1mreh2 2.1.1.2.55 (116-227) Immunoglobulin (constant domains of L and H chains) {Fab Jel 103 (mouse), kappa L chain}
ttppsvyplapgcgdttgssvtlgclvkgyfpesvtvtwnsgslsssvhtfpallqsgly
tmsssvtvpsstwpsqtvtcsvahpassttvdkklep
>d1mrel1 2.1.1.1.48 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab Jel 103 (mouse), kappa L chain}
dvvmtqtplslpvslgdqasiscrssqslvhsngntylhwylqkpgqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyfcsqsthvprtfgggtkleikr
>d1mrel2 2.1.1.2.55 (109-213) Immunoglobulin (constant domains of L and H chains) {Fab Jel 103 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgkerqngvlnswtdqns
kdstysmsstltltkdeyerhnsytceathktstspivksfnrne
>d1mrfh1 2.1.1.1.48 (2-115) Immunoglobulin (variable domains of L and H chains) {Fab Jel 103 (mouse), kappa L chain}
vqlqqsgaelvkpgasvklsckasgytftsywmqwvkqrpgqglewigeidpsdsytnyn
qkfkgkatltvdtssstaymqlssltsedsavyycanlrgyfdywgqgttltvssak
>d1mrfh2 2.1.1.2.55 (116-227) Immunoglobulin (constant domains of L and H chains) {Fab Jel 103 (mouse), kappa L chain}
ttppsvyplapgcgdttgssvtlgclvkgyfpesvtvtwnsgslsssvhtfpallqsgly
tmsssvtvpsstwpsqtvtcsvahpassttvdkklep
>d1mrfl1 2.1.1.1.48 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab Jel 103 (mouse), kappa L chain}
dvvmtqtplslpvslgdqasiscrssqslvhsngntylhwylqkpgqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyfcsqsthvprtfgggtkleikr
>d1mrfl2 2.1.1.2.55 (109-211) Immunoglobulin (constant domains of L and H chains) {Fab Jel 103 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgkerqngvlnswtdqns
kdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1mrg__ 4.102.1.1.3 alpha-Momorcharin (momordin) {bitter melon (Momordica charantia)}
dvsfrlsgadprsygmfikdlrnalpfrekvyniplllpsvsgagryllmhlfnrdgkti
tvavdvtniyimgyladttsyffnepaaelasqyvfrdarrkitlpysgdyerlqiaagk
prekipiglpaldsaistllhydstaaagallvliqttaeaarfkyieqqiqerayrdev
pslatislenswsglskqiqlaqgnngifrtpivlvdnkgnrvqitnvtskvvtsniqll
lntrni
>d1mrh__ 4.102.1.1.3 alpha-Momorcharin (momordin) {bitter melon (Momordica charantia)}
dvsfrlsgadprsygmfikdlrnalpfrekvyniplllpsvsgagryllmhlfnrdgkti
tvavdvtnvyimgyladttsyffnepaaelasqyvfrdarrkitlpysgdyerlqiaagk
prekipiglpaldsaistllhydstaaagallvliqttaeaarfkyieqqiqerayrdev
pslatislenswsglskqiqlaqgnngifrtpivlvdnkgnrvqitnvtskvvtsniqll
lntrni
>d1mri__ 4.102.1.1.3 alpha-Momorcharin (momordin) {bitter melon (Momordica charantia)}
dvsfrlsgadprsygmfikdlrnalpfrekvyniplllpsvsgagryllmhlfnrdgkti
tvavdvtnvyimgyladttsyffnepaaelasqyvfrdarrkitlpysgdyerlqiaagk
prekipiglpaldsaistllhydstaaagallvliqttaeaarfkyieqqiqerayrdev
pslatislenswsglskqiqlaqgnngifrtpivlvdnkgnrvqitnvtskvvtsniqll
lntrni
>d1mrj__ 4.102.1.1.1 alpha-Trichosanthin {Mongolian snake gourd (Trichosanthes Kirillowii maxim)}
dvsfrlsgatsssygvfisnlrkalpnerklydipllrsslpgsqryalihltnyadeti
svaidvtnvyimgyragdtsyffneasateaakyvfkdamrkvtlpysgnyerlqtaagk
ireniplglpaldsaittlfyynansaasalmvliqstseaarykfieqqigkrvdktfl
pslaiislenswsalskqiqiastnngqfespvvlinaqnqrvtitnvdagvvtsniall
lnrnnma
>d1mrk__ 4.102.1.1.1 alpha-Trichosanthin {Mongolian snake gourd (Trichosanthes Kirillowii maxim)}
dvsfrlsgatsssygvfisnlrkalpnerklydipllrsslpgsqryalihltnyadeti
svaidvtnvyimgyragdtsyffneasateaakyvfkdamrkvtlpysgnyerlqtaagk
ireniplglpaldsaittlfyynansaasalmvliqstseaarykfieqqigkrvdktfl
pslaiislenswsalskqiqiastnngqfespvvlinaqnqrvtitnvdagvvtsniall
lnrnnma
>d1mrp__ 3.82.1.1.7 Ferric-binding protein {(Haemophilus influenzae)}
ditvyngqhkeaatavakafeqetgikvtlnsgkseqlagqlkeegdktpadvfyteqta
tfadlseagllapiseqtiqqtaqkgvplapkkdwialsgrsrvvvydhtklsekdmeks
vldyatpkwkgkigyvstsgafleqvvalskmkgdkvalnwlkglkengklyaknsvalq
avengevpaalinnyywynlakekgvenlksrlyfvrhqdpgalvsysgaavlkasknqa
eaqkfvdflaskkgqealvaaraeyplradvvspfnlepyekleapvvsattaqdkehai
klieeaglk
>d1mrra_ 1.25.1.2.3 Ribonucleotide reductase R2 {(Escherichia coli)}
ayttfsatkndqlkepmffgqpvqvarydqqkydifekliekqlsffwrpeevdvsrdri
dyqalpehekhifisnlkyqtlldsiqgrspnvallplisipeletwvetwafsetihsr
sythiirnivndpsvvfddivtneqiqkraegissyydeliemtsywhllgegthtvngk
tvtvslrelkkklylclmsvnaleairfyvsfacsfafaerelmegnakiirliardeal
hltgtqhmlnllrsgaddpemaeiaeeckqecydlfvqaaqqekdwadylfrdgsmigln
kdilcqyveyitnirmqavgldlpfntrsnpipwintwlv
>d1mrrb_ 1.25.1.2.3 Ribonucleotide reductase R2 {(Escherichia coli)}
ayttfsatkndqlkepmffgqpvqvarydqqkydifekliekqlsffwrpeevdvsrdri
dyqalpehekhifisnlkyqtlldsiqgrspnvallplisipeletwvetwafsetihsr
sythiirnivndpsvvfddivtneqiqkraegissyydeliemtsywhllgegthtvngk
tvtvslrelkkklylclmsvnaleairfyvsfacsfafaerelmegnakiirliardeal
hltgtqhmlnllrsgaddpemaeiaeeckqecydlfvqaaqqekdwadylfrdgsmigln
kdilcqyveyitnirmqavgldlpfntrsnpipwintwlv
>d1mrt__ 7.38.1.1.3 Metallothionein {(rat )}
ksccsccpvgcakcsqgcickeasdkcscca
>d1msaa_ 2.60.1.1.1 Lectin (agglutinin) {Snowdrop (Galanthus nivalis)}
dnilysgetlstgeflnygsfvfimqedcnlvlydvdkpiwatntgglsrscflsmqtdg
nlvvynpsnkpiwasntggqngnyvcilqkdrnvviygtdrwatgthtg
>d1msab_ 2.60.1.1.1 Lectin (agglutinin) {Snowdrop (Galanthus nivalis)}
dnilysgetlstgeflnygsfvfimqedcnlvlydvdkpiwatntgglsrscflsmqtdg
nlvvynpsnkpiwasntggqngnyvcilqkdrnvviygtdrwatgthtg
>d1msac_ 2.60.1.1.1 Lectin (agglutinin) {Snowdrop (Galanthus nivalis)}
dnilysgetlstgeflnygsfvfimqedcnlvlydvdkpiwatntgglsrscflsmqtdg
nlvvynpsnkpiwasntggqngnyvcilqkdrnvviygtdrwatgthtg
>d1msad_ 2.60.1.1.1 Lectin (agglutinin) {Snowdrop (Galanthus nivalis)}
dnilysgetlstgeflnygsfvfimqedcnlvlydvdkpiwatntgglsrscflsmqtdg
nlvvynpsnkpiwasntggqngnyvcilqkdrnvviygtdrwatgthtg
>d1msba_ 4.105.1.1.5 Mannose-binding protein A, lectin domain {rat (Rattus rattus)}
sgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevteg
qfmyvtggrltysnwkkdepndhgsgedcvtivdnglwndiscqashtavcefpa
>d1msbb_ 4.105.1.1.5 Mannose-binding protein A, lectin domain {rat (Rattus rattus)}
sgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevteg
qfmyvtggrltysnwkkdepndhgsgedcvtivdnglwndiscqashtavcefpa
>d1msc__ 4.46.1.1.1 MS2 virus coat protein {(bacteriophage MS2)}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvtcsvrqssaqnrkyti
kvevpkvatqtvggvelpvaarrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1msda1 1.2.4.1.4 (1-83) Mn superoxide dismutase (SOD) {human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaayvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1msda2 4.26.1.1.3 (84-198) Mn superoxide dismutase (SOD) {human (Homo sapiens)}
ngggepkgelleaikrdfgsfdkfkekltaasvgvqgsgwgwlgfnkerghlqiaacpnq
dplqgttglipllgidvwehayylqyknvrpdylkaiwnvinwenvterymackk
>d1msdb1 1.2.4.1.4 (1-83) Mn superoxide dismutase (SOD) {human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaayvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1msdb2 4.26.1.1.3 (84-198) Mn superoxide dismutase (SOD) {human (Homo sapiens)}
ngggepkgelleaikrdfgsfdkfkekltaasvgvqgsgwgwlgfnkerghlqiaacpnq
dplqgttglipllgidvwehayylqyknvrpdylkaiwnvinwenvterymackk
>d1msec1 1.4.1.3.2 (89-143) c-Myb, DNA-binding domain {mouse (Mus musculus)}
mlikgpwtkeedqrviklvqkygpkrwsviakhlkgrigkqcrerwhnhlnpevk
>d1msec2 1.4.1.3.2 (144-193) c-Myb, DNA-binding domain {mouse (Mus musculus)}
ktswteeedriiyqahkrlgnrwaeiakllpgrtdnaiknhwnstmrrkv
>d1msfc1 1.4.1.3.2 (89-143) c-Myb, DNA-binding domain {mouse (Mus musculus)}
mlikgpwtkeedqrviklvqkygpkrwsviakhlkgrigkqcrerwhnhlnpevk
>d1msfc2 1.4.1.3.2 (144-193) c-Myb, DNA-binding domain {mouse (Mus musculus)}
ktswteeedriiyqahkrlgnrwaeiakllpgrtdnaiknhwnstmrrkv
>d1msga_ 4.7.1.1.4 Melanoma growth stimulating activity (MGSA) {human (Homo sapiens)}
asvatelrcqclqtlqgihpkniqsvnvkspgphcaqteviatlkngrkaclnpaspivk
kiiekmlnsdks
>d1msgb_ 4.7.1.1.4 Melanoma growth stimulating activity (MGSA) {human (Homo sapiens)}
asvatelrcqclqtlqgihpkniqsvnvkspgphcaqteviatlkngrkaclnpaspivk
kiiekmlnsdks
>d1msha_ 4.7.1.1.4 Melanoma growth stimulating activity (MGSA) {human (Homo sapiens)}
asvatelrcqclqtlqgihpkniqsvnvkspgphcaqteviatlkngrkaclnpaspivk
kiiekmlnsdks
>d1mshb_ 4.7.1.1.4 Melanoma growth stimulating activity (MGSA) {human (Homo sapiens)}
asvatelrcqclqtlqgihpkniqsvnvkspgphcaqteviatlkngrkaclnpaspivk
kiiekmlnsdks
>d1msi__ 2.66.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus)}
aaqasvvanqlipintaltlvmmrsevvtpvgipaediprlvsmqvnravplgttlmpdm
vkgyaa
>d1msk__ 4.109.1.1.1 Methionine synthase (activation domain) {(Escherichia coli)}
tppvtleaardndfafdwqaytppvahrlgvqeveasietlrnyidwtpffmtwslagky
priledevvgveaqrlfkdandmldklsaektlnprgvvglfpanrvgddieiyrdetrt
hvinvshhlrqqtektgfanycladfvapklsgkadyigafavtggleedaladafeaqh
ddynkimvkaladrlaeafaeylhervrkvywgyapnenlsneelirenyqgirpapgyp
acpehtekatiwellevekhtgmkltesfamwpgasvsgwyfshpdskyyavaqiqrdqv
edyarrkgmsvteverwlapnlgydad
>d1mspa_ 2.1.8.2.1 Major sperm protein, alpha isoform (recombinant), ph 4.6 {Pig roundworm (Ascaris suum)}
svppgdintqpsqkivfnapyddkhtyhikitnaggrrigwaikttnmrrlsvdppcgvl
dpkekvlmavscdtfnaatedlnndritiewtntpdgaakqfrrewfqgdgmvrrknlpi
eynl
>d1mspb_ 2.1.8.2.1 Major sperm protein, alpha isoform (recombinant), ph 4.6 {Pig roundworm (Ascaris suum)}
ppgdintqpsqkivfnapyddkhtyhikitnaggrrigwaikttnmrrlsvdppcgvldp
kekvlmavscdtfnaatedlnndritiewtntpdgaakqfrrewfqgdgmvrrknlpiey
nl
>d1mssa_ 3.1.11.1.4 Triosephosphate isomerase {(Trypanosoma brucei brucei)}
skpqpiaaanwkcngsqqslselidlfnstsinhdvqcvvastsshlamtkerlshpkfv
iaaqnagnadalaslkdfgvnwivlghserrayygetneivadkvaaavasgfmviacig
etlqeresgrtavvvltqiaaiakklkkadwakvviayepvwaigtgkvatpqqaqeaha
lirswvsskigadvagelrilyggsvngknartlyqqrdvngflvggaslkpefvdiika
tq
>d1mssb_ 3.1.11.1.4 Triosephosphate isomerase {(Trypanosoma brucei brucei)}
skpqpiaaanwkcngsqqslselidlfnstsinhdvqcvvastsshlamtkerlshpkfv
iaaqnagnadalaslkdfgvnwivlghserrayygetneivadkvaaavasgfmviacig
etlqeresgrtavvvltqiaaiakklkkadwakvviayepvwaigtgkvatpqqaqeaha
lirswvsskigadvagelrilyggsvngknartlyqqrdvngflvggaslkpefvdiika
tq
>d1msta_ 4.46.1.1.1 MS2 virus coat protein {(bacteriophage MS2)}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvtcsvrqssaqnrkyti
kvevpkvatqtvggvdlpvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1mstb_ 4.46.1.1.1 MS2 virus coat protein {(bacteriophage MS2)}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvtcsvrqssaqnrkyti
kvevpkvatqtvggvdlpvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1mstc_ 4.46.1.1.1 MS2 virus coat protein {(bacteriophage MS2)}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvtcsvrqssaqnrkyti
kvevpkvatqtvggvdlpvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1mti__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrlkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1mtj__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrvkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1mtk__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrvkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>e1mtn.1b 2.35.1.2.7 (alpha, gamma-)chymotrypsin(ogen) {bovine (Bos taurus)}
ivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgvttsdvvvagefdqgs
ssekiqklkiakvfknskynsltinnditllklstaasfsqtvsavclpsasddfaagtt
cvttgwgltry
>e1mtn.1c 2.35.1.2.7 (alpha, gamma-)chymotrypsin(ogen) {bovine (Bos taurus)}
antpdrlqqaslpllsntnckkywgtkikdamicagasgvsscmgdsggplvckkngawt
lvgivswgsstcststpgvyarvtalvnwvqqtlaan
>e1mtn.2f 2.35.1.2.7 (alpha, gamma-)chymotrypsin(ogen) {bovine (Bos taurus)}
ivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgvttsdvvvagefdqgs
ssekiqklkiakvfknskynsltinnditllklstaasfsqtvsavclpsasddfaagtt
cvttgwgltry
>e1mtn.2g 2.35.1.2.7 (alpha, gamma-)chymotrypsin(ogen) {bovine (Bos taurus)}
antpdrlqqaslpllsntnckkywgtkikdamicagasgvsscmgdsggplvckkngawt
lvgivswgsstcststpgvyarvtalvnwvqqtlaan
>d1mtnd_ 7.7.1.1.1 Pancreatic trypsin inhibitor {bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d1mtnh_ 7.7.1.1.1 Pancreatic trypsin inhibitor {bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d1mtra_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwkrplvtiriggqlkealldtgaddtvieemnlpgkwkpkmiggiggfikvrqyd
qipveixghkaigtvlvgptpvniigrnlltqigxtlnf
>d1mtrb_ 2.38.1.1.1 Human immunodeficiency virus type 1 protease {(HIV-1)}
pqitlwkrplvtiriggqlkealldtgaddtvieemnlpgkwkpkmiggiggfikvrqyd
qipveixghkaigtvlvgptpvniigrnlltqigxtlnf
>d1mts__ 2.35.1.2.1 Trypsin(ogen) {bovine (Bos taurus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1mtu__ 2.35.1.2.3 Trypsin(ogen) {rat (Rattus rattus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1mtv__ 2.35.1.2.3 Trypsin(ogen) {rat (Rattus rattus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1mtw__ 2.35.1.2.3 Trypsin(ogen) {rat (Rattus rattus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1mtx__ 7.3.6.2.1 Margatoxin {scorpion (Centruroides margaritatus)}
tiinvkctspkqclppckaqfgqsagakcmngkckcyph
>d1mtyb_ 1.25.1.2.1 Methane monooxygenase hydrolase, beta and alpha subunits {(Methylococcus capsulatus)}
errrgltdpemaavilkalpeapldgnnkmgyfvtprwkrlteyealtvyaqpnadwiag
gldwgdwtqkfhggrpswgnettelrtvdwfkhrdplrrwhapyvkdkaeewrytdrflq
gysadgqiramnptwrdefinrywgaflfneyglfnahsqgarealsdvtrvslafwgfd
kidiaqmiqlergflakivpgfdestavpkaewtngevyksarlaveglwqevfdwnesa
fsvhavydalfgqfvrreffqrlaprfgdnltpffinqaqtyfqiakqgvqdlyynclgd
dpefsdynrtvmrnwtgkwleptiaalrdfmglfaklpagttdkeeitaslyrvvddwie
dyasridfkadrdqivkavlaglk
>d1mtyc_ 1.25.1.2.1 Methane monooxygenase hydrolase, beta and alpha subunits {(Methylococcus capsulatus)}
errrgltdpemaavilkalpeapldgnnkmgyfvtprwkrlteyealtvyaqpnadwiag
gldwgdwtqkfhggrpswgnettelrtvdwfkhrdplrrwhapyvkdkaeewrytdrflq
gysadgqiramnptwrdefinrywgaflfneyglfnahsqgarealsdvtrvslafwgfd
kidiaqmiqlergflakivpgfdestavpkaewtngevyksarlaveglwqevfdwnesa
fsvhavydalfgqfvrreffqrlaprfgdnltpffinqaqtyfqiakqgvqdlyynclgd
dpefsdynrtvmrnwtgkwleptiaalrdfmglfaklpagttdkeeitaslyrvvddwie
dyasridfkadrdqivkavlaglk
>d1mtyd_ 1.25.1.2.1 Methane monooxygenase hydrolase, beta and alpha subunits {(Methylococcus capsulatus)}
aanraptsvnaqevhrwlqsfnwdfknnrtkyatkykmanetkeqfkliakeyarmeavk
derqfgslqvaltrlnagvrvhpkwnetmkvvsnflevgeynaiaatgmlwdsaqaaeqk
ngylaqvldeirhthqcayvnyyfakngqdpaghndarrtrtigplwkgmkrvfsdgfis
gdavecslnlqlvgeacftnplivavtewaaangdeitptvflsietdelrhmangyqtv
vsiandpasakylntdlnnafwtqqkyftpvlgmlfeygskfkvepwvktwdrwvyedwg
giwigrlgkygvesprslkdakqdaywahhdlyllayalwptgffrlalpdqeemewfea
nypgwydhygkiyeewrargcedpssgfiplmwfiennhpiyidrvsqvpfcpslakgas
tlrvheyngemhtfsdqwgermwlaeperyecqnifeqyegrelseviaelhglrsdgkt
liaqphvrgdklwtlddikrlncvfknpvkaf
>d1mtye_ 1.25.1.2.1 Methane monooxygenase hydrolase, beta and alpha subunits {(Methylococcus capsulatus)}
aanraptsvnaqevhrwlqsfnwdfknnrtkyatkykmanetkeqfkliakeyarmeavk
derqfgslqvaltrlnagvrvhpkwnetmkvvsnflevgeynaiaatgmlwdsaqaaeqk
ngylaqvldeirhthqcayvnyyfakngqdpaghndarrtrtigplwkgmkrvfsdgfis
gdavecslnlqlvgeacftnplivavtewaaangdeitptvflsietdelrhmangyqtv
vsiandpasakylntdlnnafwtqqkyftpvlgmlfeygskfkvepwvktwdrwvyedwg
giwigrlgkygvesprslkdakqdaywahhdlyllayalwptgffrlalpdqeemewfea
nypgwydhygkiyeewrargcedpssgfiplmwfiennhpiyidrvsqvpfcpslakgas
tlrvheyngemhtfsdqwgermwlaeperyecqnifeqyegrelseviaelhglrsdgkt
liaqphvrgdklwtlddikrlncvfknpvkaf
>d1mtyg_ 1.23.1.1.1 Methane monooxygenase hydrolase, gamma subunit {(Methylococcus capsulatus)}
lgihsndtrdawvnkiahvntlekaaemlkqfrmdhttpfrnsyeldndylwieakleek
vavlkarafnevdfrhktafgedaksvldgtvakmnaakdkweaekihigfrqaykppim
pvnyfldgerqlgtrlmelrnlnyydtpleelrkqrgvrvvh
>d1mtyh_ 1.23.1.1.1 Methane monooxygenase hydrolase, gamma subunit {(Methylococcus capsulatus)}
lgihsndtrdawvnkiahvntlekaaemlkqfrmdhttpfrnsyeldndylwieakleek
vavlkarafnevdfrhktafgedaksvldgtvakmnaakdkweaekihigfrqaykppim
pvnyfldgerqlgtrlmelrnlnyydtpleelrkqrgvrvvh
>d1mua__ 2.56.1.1.2 Carbonic anhydrase {human (Homo sapiens) erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttpallecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasf
>d1muca1 3.1.6.2.1 (131-372) Muconate-lactonizing enzyme {(Pseudomonas putida)}
rvrdslevawtlasgdtardiaearhmleirrhrvfklkiganpveqdlkhvvtikrelg
dsasvrvdvnqywdesqairacqvlgdngidlieqpisrinrggqvrlnqrtpapimade
siesvedafslaadgaasifalkiaknggpravlrtaqiaeaagiglyggtmlegsigtl
asahafltlrqltwgtelfgplllteeivneppqyrdfqlhiprtpglgltldeqrlarf
ar
>d1muca2 4.32.1.1.3 (4-130) Muconate-lactonizing enzyme (cis muconate cycloisomerase) {(Pseudomonas putida)}
alieridaiivdlptirphklamhtmqqqtlvvlrvrcsdgvegigeattigglaygyes
pegikanidahlapaliglaadninaamlkldklakgntfaksgiesalldaqgkrlglp
vsellgg
>d1mucb1 3.1.6.2.1 (131-372) Muconate-lactonizing enzyme {(Pseudomonas putida)}
rvrdslevawtlasgdtardiaearhmleirrhrvfklkiganpveqdlkhvvtikrelg
dsasvrvdvnqywdesqairacqvlgdngidlieqpisrinrggqvrlnqrtpapimade
siesvedafslaadgaasifalkiaknggpravlrtaqiaeaagiglyggtmlegsigtl
asahafltlrqltwgtelfgplllteeivneppqyrdfqlhiprtpglgltldeqrlarf
ar
>d1mucb2 4.32.1.1.3 (4-130) Muconate-lactonizing enzyme (cis muconate cycloisomerase) {(Pseudomonas putida)}
alieridaiivdlptirphklamhtmqqqtlvvlrvrcsdgvegigeattigglaygyes
pegikanidahlapaliglaadninaamlkldklakgntfaksgiesalldaqgkrlglp
vsellgg
>d1muga_ 3.12.1.2.1 G:T/U mismatch-specific DNA glycosylase {(Escherichia coli)}
mvedilapglrvvfcginpglssagtgfpfahpanrfwkviyqagftdrqlkpqeaqhll
dyrcgvtklvdrptvqanevskqelhaggrkliekiedyqpqalailgkqayeqgfsqrg
aqwgkqtltigstqiwvlpnpsglsrvsleklveayreldqalvv
>d1mup__ 2.45.1.1.9 Major urinary protein {mouse (Mus musculus)}
eeasstgrnfnvekingewhtiilasdkrekiedngnfrlfleqihvlenslvlkfhtvr
deecselsmvadktekageysvtydgfntftipktdydnflmahlinekdgetfqlmgly
grepdlssdikerfaqlceehgilreniidlsnanrc
>d1mut__ 4.66.1.1.1 Nucleoside triphosphate pyrophosphorylase (MutT) {(Escherichia coli)}
mkklqiavgiirnenneifitrraadahmanklefpggkiemgetpeqavvrelqeevgi
tpqhfslfekleyefpdrhitlwfwlverwegepwgkegqpgewmslvglnaddfppane
pviaklkrl
>d1mvaa_ 4.46.1.1.1 MS2 virus coat protein {(bacteriophage MS2)}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvacsvrqssaqnrkyti
kvevpkvatqtvggvelpvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1mvab_ 4.46.1.1.1 MS2 virus coat protein {(bacteriophage MS2)}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvacsvrqssaqnrkyti
kvevpkvatqtvggvelpvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1mvac_ 4.46.1.1.1 MS2 virus coat protein {(bacteriophage MS2)}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvacsvrqssaqnrkyti
kvevpkvatqtvggvelpvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1mvba_ 4.46.1.1.1 MS2 virus coat protein {(bacteriophage MS2)}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvtcsvrqssaqnrkysi
kvevpkvatqtvggvelpvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1mvbb_ 4.46.1.1.1 MS2 virus coat protein {(bacteriophage MS2)}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvtcsvrqssaqnrkysi
kvevpkvatqtvggvelpvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1mvbc_ 4.46.1.1.1 MS2 virus coat protein {(bacteriophage MS2)}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvtcsvrqssaqnrkysi
kvevpkvatqtvggvelpvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1mvi__ 7.3.5.1.4 Conotoxin {sea snail (Conus magus) M VIIa}
ckgkgakcsrlmydcctgscrsgkc
>d1mvj__ 7.3.5.1.5 Conotoxin {(Conus striatus) S VIb}
cklkgqscrktsydccsgscgrsgkc
>d1mvma_ 2.8.1.4.6 MVM coat protein {(Murine minute virus), strain i}
gvgvstgsydnqthyrflgdgwveitalatrlvhlnmpksenycrirvhnttdtsvkgnm
akddaheqiwtpwslvdanawgvwlqpsdwqyicntmsqlnlvsldqeifnvvlktvteq
dsggqaikiynndltacmmvavdsnnilpytpaansmetlgfypwkptiaspyryyfcvd
rdlsvtyenqegtiehnvmgtpkgmnsqfftientqqitllrtgdefatgtyyfdtnpvk
lthtwqtnrqlgqppllstfpeadtdagtltaqgsrhgatqmevnwvseairtrpaqvgf
cqphndfeasragpfaapkvpadvtqgmdreangsvrysygkqhgenwaahgpaperytw
detnfgsgrdtrdgfiqsaplvvppplngiltnanpigtkndihfsnvfnsygplttfsh
pspvypqgqiwdkeldlehkprlhitapfvcknnapgqmlvrlgpnltdqydpngatlsr
ivtygtffwkgkltmraklranttwnpvyqvsvedngnsymsvtkwlptatgnmqsvpli
trpvarnty
>d1mvpa_ 2.38.1.1.5 Myeloblastosis-associated viral protease {(Myeloblastosis associated virus)}
lamtmehkdrplvrviltntgshpvkqrsvyitalldsgaditiiseedwptdwpvmeaa
npqihgigggipmrksrdmievgvinrdgslerplllfpavamvrgsilgrdclqglglr
ltnl
>d1mvpb_ 2.38.1.1.5 Myeloblastosis-associated viral protease {(Myeloblastosis associated virus)}
lamtmehkdrplvrviltntgshpvkqrsvyitalldsgaditiiseedwptdwpvmeaa
npqihgigggipmrksrdmievgvinrdgslerplllfpavamvrgsilgrdclqglglr
ltnl
>d1mwe__ 2.50.1.1.2 Influenza neuraminidase {(influenza virus A), different strains}
rdfnnltkglctinswhiygkdnavrigedsdvlvtrepyvscdpdecrfyalsqgttir
gkhsngtihdrsqyraliswplsspptvynsrvecigwsstschdgktrmsicisgpnnn
asaviwynrrpvteintwarnilrtqesecvchngvcpvvftdgsatgpaetriyyfkeg
kilkweplagtakhieecscygeraeitctcrdnwqgsnrpviridpvamthtsqyicsp
vltdnprpndptvgkcndpypgnnnngvkgfsyldgvntwlgrtisiasrsgyemlkvpn
altddkskptqgqtivlntdwsgysgsfmdywaegecyracfyvelirgrpkedkvwwts
nsivsmcssteflgqwdwpdgakieyfl
>d1mxa_1 4.80.1.1.1 (1-101) S-adenosylmethionine synthetase. MAT {(Escherichia coli)}
akhlftsesvseghpdkiadqisdavldaileqdpkarvacetyvktgmvlvggeittsa
wvdieeitrntvreigyvhsdmgfdanscavlsaigkqspd
>d1mxa_2 4.80.1.1.1 (108-231) S-adenosylmethionine synthetase. MAT {(Escherichia coli)}
radpleqgagdqglmfgyatnetdvlmpapityahrlvqrqaevrkngtlpwlrpdaksq
vtfqyddgkivgidavvlstqhseeidqkslqeavmeeiikpilpaewltsatkffinpt
grfv
>d1mxa_3 4.80.1.1.1 (232-383) S-adenosylmethionine synthetase. MAT {(Escherichia coli)}
iggpmgdcgltgrkiivdtyggmarhgggafsgkdpskvdrsaayaaryvaknivaagla
drceiqvsyaigvaeptsimvetfgtekvpseqltllvreffdlrpygliqmldllhpiy
ketaayghfgrehfpwektdkaqllrdaaglk
>d1mxb_1 4.80.1.1.1 (1-101) S-adenosylmethionine synthetase. MAT {(Escherichia coli)}
akhlftsesvseghpdkiadqisdavldaileqdpkarvacetyvktgmvlvggeittsa
wvdieeitrntvreigyvhsdmgfdanscavlsaigkqspd
>d1mxb_2 4.80.1.1.1 (108-231) S-adenosylmethionine synthetase. MAT {(Escherichia coli)}
radpleqgagdqglmfgyatnetdvlmpapityahrlvqrqaevrkngtlpwlrpdaksq
vtfqyddgkivgidavvlstqhseeidqkslqeavmeeiikpilpaewltsatkffinpt
grfv
>d1mxb_3 4.80.1.1.1 (232-383) S-adenosylmethionine synthetase. MAT {(Escherichia coli)}
iggpmgdcgltgrkiivdtyggmarhgggafsgkdpskvdrsaayaaryvaknivaagla
drceiqvsyaigvaeptsimvetfgtekvpseqltllvreffdlrpygliqmldllhpiy
ketaayghfgrehfpwektdkaqllrdaaglk
>d1mxc_1 4.80.1.1.1 (1-101) S-adenosylmethionine synthetase. MAT {(Escherichia coli)}
akhlftsesvseghpdkiadqisdavldaileqdpkarvacetyvktgmvlvggeittsa
wvdieeitrntvreigyvhsdmgfdanscavlsaigkqspd
>d1mxc_2 4.80.1.1.1 (108-231) S-adenosylmethionine synthetase. MAT {(Escherichia coli)}
radpleqgagdqglmfgyatnetdvlmpapityahrlvqrqaevrkngtlpwlrpdaksq
vtfqyddgkivgidavvlstqhseeidqkslqeavmeeiikpilpaewltsatkffinpt
grfv
>d1mxc_3 4.80.1.1.1 (232-383) S-adenosylmethionine synthetase. MAT {(Escherichia coli)}
iggpmgdcgltgrkiivdtyggmarhgggafsgkdpskvdrsaayaaryvaknivaagla
drceiqvsyaigvaeptsimvetfgtekvpseqltllvreffdlrpygliqmldllhpiy
ketaayghfgrehfpwektdkaqllrdaaglk
>d1myf__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgyqg
>d1myga_ 1.1.1.1.7 Myoglobin {pig (Sus scrofa)}
glsdgewqlvlnvwgkveadvaghgqevlirlfkghpetlekfdkfkhlksedemkased
lkkhgntvltalggilkkkghheaeltplaqshatkhkipvkylefiseaiiqvlqskhp
gdfgadaqgamskalelfrndmaakykelgfqg
>d1mygb_ 1.1.1.1.7 Myoglobin {pig (Sus scrofa)}
glsdgewqlvlnvwgkveadvaghgqevlirlfkghpetlekfdkfkhlksedemkased
lkkhgntvltalggilkkkghheaeltplaqshatkhkipvkylefiseaiiqvlqskhp
gdfgadaqgamskalelfrndmaakykelgfqg
>d1myha_ 1.1.1.1.7 Myoglobin {pig (Sus scrofa)}
glsdgewqlvlnvwgkveadvaghgqevlirlfkghpetlekfdrfkhlksedemkased
lkkhgntvltalggilkkkghheaeltplaqshatkhkipvkylefiseaiiqvlqskhp
gdfgadaqgamskalelfrndmaakykelgfqg
>d1myhb_ 1.1.1.1.7 Myoglobin {pig (Sus scrofa)}
glsdgewqlvlnvwgkveadvaghgqevlirlfkghpetlekfdrfkhlksedemkased
lkkhgntvltalggilkkkghheaeltplaqshatkhkipvkylefiseaiiqvlqskhp
gdfgadaqgamskalelfrndmaakykelgfqg
>d1myia_ 1.1.1.1.7 Myoglobin {pig (Sus scrofa)}
glsdgewqlvlnvwgkveadvaghgqevlirlfkghpetlekfdsfkhlksedemkased
lkkhgntvltalggilkkkghheaeltplaqshatkhkipvkylefiseaiiqvlqskhp
gdfgadaqgamskalelfrndmaakykelgfqg
>d1myib_ 1.1.1.1.7 Myoglobin {pig (Sus scrofa)}
glsdgewqlvlnvwgkveadvaghgqevlirlfkghpetlekfdsfkhlksedemkased
lkkhgntvltalggilkkkghheaeltplaqshatkhkipvkylefiseaiiqvlqskhp
gdfgadaqgamskalelfrndmaakykelgfqg
>d1myja_ 1.1.1.1.7 Myoglobin {pig (Sus scrofa)}
glsdgewqlvlnvwgkveadvaghgqevlirlfkghpetlekfdkfkhlksedemkased
lkkhgnttltalggilkkkghheaeltplaqshatkhkipvkylefiseaiiqvlqskhp
gdfgadaqgamskalelfrndmaakykelgfqg
>d1myjb_ 1.1.1.1.7 Myoglobin {pig (Sus scrofa)}
glsdgewqlvlnvwgkveadvaghgqevlirlfkghpetlekfdkfkhlksedemkased
lkkhgnttltalggilkkkghheaeltplaqshatkhkipvkylefiseaiiqvlqskhp
gdfgadaqgamskalelfrndmaakykelgfqg
>d1myka_ 1.41.1.1.1 Arc repressor {(Salmonella )bacteriophage P22}
kmlqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegrig
>d1mykb_ 1.41.1.1.1 Arc repressor {(Salmonella )bacteriophage P22}
kmlqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegr
>d1myla_ 1.41.1.1.1 Arc repressor {(Salmonella )bacteriophage P22}
kmpqfnlrwprevldlvrkvaeengmsvnsyiyqlvmesfkkegr
>d1mylb_ 1.41.1.1.1 Arc repressor {(Salmonella )bacteriophage P22}
mpqfnlrwprevldlvrkvaeengmsvnsyiyqlvmesfk
>d1mylc_ 1.41.1.1.1 Arc repressor {(Salmonella )bacteriophage P22}
mpqfnlrwprevldlvrkvaeengmsvnsyiyqlvmesfkkegri
>d1myld_ 1.41.1.1.1 Arc repressor {(Salmonella )bacteriophage P22}
mpqfnlrwprevldlvrkvaeengmsvnsyiyqlvmesfkkegri
>d1myle_ 1.41.1.1.1 Arc repressor {(Salmonella )bacteriophage P22}
mpqfnlrwprevldlvrkvaeengmsvnsyiyqlvmesfkk
>d1mylf_ 1.41.1.1.1 Arc repressor {(Salmonella )bacteriophage P22}
mpqfnlrwprevldlvrkvaeengmsvnsyiyqlvmesfk
>d1mym__ 1.1.1.1.4 Myoglobin {sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrvkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1myn__ 7.3.6.3.1 Drosomycin {Fruit fly (Drosophila melanogaster)}
dclsgrykgpcavwdnetcrrvckeegrssghcspslkcwcegc
>e1myp.1a 1.72.1.2.2 Myeloperoxidase {dog (Canis familiaris)}
cpeqdkyrtitgmcnnrrsptlgasnrafvrwlpaeyedgfslpygwtpgvkrngfpval
aravsneivrfptdqltpdqerslmfmqwgqlldhdldftpepa
>e1myp.1c 1.72.1.2.2 Myeloperoxidase {dog (Canis familiaris)}
ncetscvqqppcfplkippndpriknqadcipffrscpacpgsnitirnqinaltsfvda
smvygseeplarnlrnmsnqlgllavnqrfqdngrallpfdnlhddpclltnrsaripcf
lagdtrssempeltsmhtlllrehnrlatelkslnprwdgerlyqearkivgamvqiity
rdylplvlgptamrkylptyrsyndsvdprianvftnafryghtliqpfmfrldnryqpm
epnprvplsrvffaswrvvleggidpilrglmatpaklnrqnqiavdeirerlfeqvmri
gldlpalnmqrsrdhglpgynawrrfcglpqpetvgqlgtvlrnlklarklmeqygtpnn
idiwmggvseplkrkgrvgpllaciigtqfrklrdgdrfwwenegvfsmqqrqalaqisl
priicdntgittvsknnifmsnsyprdfvncstlpalnlasw
>e1myp.2b 1.72.1.2.2 Myeloperoxidase {dog (Canis familiaris)}
cpeqdkyrtitgmcnnrrsptlgasnrafvrwlpaeyedgfslpygwtpgvkrngfpval
aravsneivrfptdqltpdqerslmfmqwgqlldhdldftpepa
>e1myp.2d 1.72.1.2.2 Myeloperoxidase {dog (Canis familiaris)}
ncetscvqqppcfplkippndpriknqadcipffrscpacpgsnitirnqinaltsfvda
smvygseeplarnlrnmsnqlgllavnqrfqdngrallpfdnlhddpclltnrsaripcf
lagdtrssempeltsmhtlllrehnrlatelkslnprwdgerlyqearkivgamvqiity
rdylplvlgptamrkylptyrsyndsvdprianvftnafryghtliqpfmfrldnryqpm
epnprvplsrvffaswrvvleggidpilrglmatpaklnrqnqiavdeirerlfeqvmri
gldlpalnmqrsrdhglpgynawrrfcglpqpetvgqlgtvlrnlklarklmeqygtpnn
idiwmggvseplkrkgrvgpllaciigtqfrklrdgdrfwwenegvfsmqqrqalaqisl
priicdntgittvsknnifmsnsyprdfvncstlpalnlasw
>d1myr__ 3.1.1.4.1 Myrosinase {white mustard (Sinapis alba)}
eitcqennpftcgntdglnsssfeadfifgvassayqiegtigrglniwdgfthrypdks
gpdhgngdttcdsfsywqkdidvldelnatgyrfsiawsriiprgkrsrgvnqkgidyyh
glidglikkgitpfvtlfhwdlpqtlqdeyegfldpqiiddfkdyadlcfeefgdsvkyw
ltinqlysvptrgygsaldapgrcsptvdpscyagnsstepyivahhqllahakvvdlyr
knythqggkigptmitrwflpyndtdrhsiaatermkqfflgwfmgpltngtypqimidt
vgarlptfspeetnlvkgsydflglnyyftqyaqpspnpvnatnhtammdagakltyina
sghyigplfesdggdgssniyyypkgiysvmdyfknkyynpliyvtengistpgsenrke
smldytridylcshlcflnkvikekdvnvkgylawalgdnyefnngftvrfglsyinwnn
vtdrdlkksgqwyqkfisp
>d1myt__ 1.1.1.1.12 Myoglobin {yellowfin tuna (Thunnus albacares)}
adfdavlkcwgpveadyttmgglvltrlfkehpetqklfpkfagiaqadiagnaaisahg
atvlkklgellkakgshaailkplanshatkhkipinnfklisevlvkvmhekagldagg
qtalrnvmgiiiadleanykelgfsg
>d1mzl__ 1.47.1.1.4 plant non-specific lipid-transfer protein (ns-LTP) {maize (Zea mays)}
aiscgqvasaiapcisyargqgsgpsagccsgvrslnnaarttadrraacnclknaaagv
sglnagnaasipskcgvsipytiststdcsrvn
>d1mzm__ 1.47.1.1.4 plant non-specific lipid-transfer protein (ns-LTP) {maize (Zea mays)}
aiscgqvasaiapcisyargqgsgpsagccsgvrslnnaarttadrraacnclknaaagv
sglnagnaasipskcgvsipytiststdcsrvn
>d1n2ca_ 3.75.1.1.2 Nitrogenase iron-molybdenum protein {(Azotobacter vinelandii)}
msreevesliqevlevypekarkdrnkhlavndpavtqskkciisnkksqpglmtirgca
yagskgvvwgpikdmihishgpvgcgqysragrrnyyigttgvnafvtmnftsdfqekdi
vfggdkklaklidevetlfplnkgisvqsecpigligddiesvskvkgaelsktivpvrc
egfrgvsqslghhiandavrdwvlgkrdedttfastpydvaiigdyniggdawssrille
emglrcvaqwsgdgsiseieltpkvklnlvhcyrsmnyisrhmeekygipwmeynffgpt
ktieslraiaakfdesiqkkceeviakykpeweavvakyrprlegkrvmlyigglrprhv
igayedlgmevvgtgyefahnddydrtmkemgdstllyddvtgyefeefvkrikpdligs
gikekfifqkmgipfremhswdysgpyhgfdgfaifardmdmtlnnpcwkklqapwea
>d1n2cb_ 3.75.1.1.2 Nitrogenase iron-molybdenum protein {(Azotobacter vinelandii)}
sqqvdkikasyplfldqdykdmlakkrdgfeekypqdkidevfqwtttkeyqelnfqrea
ltvnpakacqplgavlcalgfektmpyvhgsqgcvayfrsyfnrhfrepvscvsdsmted
aavfggqqnmkdglqnckatykpdmiavsttcmaevigddlnafinnskkegfipdefpv
pfahtpsfvgshvtgwdnmfegiaryftlksmddkvvgsnkkinivpgfetylgnfrvik
rmlsemgvgysllsdpeevldtpadgqfrmyaggttqeemkdapnalntvllqpwhlekt
kkfvegtwkhevpklnipmgldwtdeflmkvseisgqpipasltkergrlvdmmtdshtw
lhgkrfalwgdpdfvmglvkfllelgcepvhilchngnkrwkkavdailaaspygknatv
yigkdlwhlrslvftdkpdfmignsygkfiqrdtlhkgkefevplirigfpifdrhhlhr
sttlgyegamqilttlvnsilerldeetrgmqatdynhdlvr
>d1n2cc_ 3.75.1.1.2 Nitrogenase iron-molybdenum protein {(Azotobacter vinelandii)}
msreevesliqevlevypekarkdrnkhlavndpavtqskkciisnkksqpglmtirgca
yagskgvvwgpikdmihishgpvgcgqysragrrnyyigttgvnafvtmnftsdfqekdi
vfggdkklaklidevetlfplnkgisvqsecpigligddiesvskvkgaelsktivpvrc
egfrgvsqslghhiandavrdwvlgkrdedttfastpydvaiigdyniggdawssrille
emglrcvaqwsgdgsiseieltpkvklnlvhcyrsmnyisrhmeekygipwmeynffgpt
ktieslraiaakfdesiqkkceeviakykpeweavvakyrprlegkrvmlyigglrprhv
igayedlgmevvgtgyefahnddydrtmkemgdstllyddvtgyefeefvkrikpdligs
gikekfifqkmgipfremhswdysgpyhgfdgfaifardmdmtlnnpcwkklqapwea
>d1n2cd_ 3.75.1.1.2 Nitrogenase iron-molybdenum protein {(Azotobacter vinelandii)}
sqqvdkikasyplfldqdykdmlakkrdgfeekypqdkidevfqwtttkeyqelnfqrea
ltvnpakacqplgavlcalgfektmpyvhgsqgcvayfrsyfnrhfrepvscvsdsmted
aavfggqqnmkdglqnckatykpdmiavsttcmaevigddlnafinnskkegfipdefpv
pfahtpsfvgshvtgwdnmfegiaryftlksmddkvvgsnkkinivpgfetylgnfrvik
rmlsemgvgysllsdpeevldtpadgqfrmyaggttqeemkdapnalntvllqpwhlekt
kkfvegtwkhevpklnipmgldwtdeflmkvseisgqpipasltkergrlvdmmtdshtw
lhgkrfalwgdpdfvmglvkfllelgcepvhilchngnkrwkkavdailaaspygknatv
yigkdlwhlrslvftdkpdfmignsygkfiqrdtlhkgkefevplirigfpifdrhhlhr
sttlgyegamqilttlvnsilerldeetrgmqatdynhdlvr
>d1n2ce_ 3.29.1.6.3 Nitrogenase iron protein {(Azotobacter vinelandii)}
amrqcaiygkggigkstttqnlvaalaemgkkvmivgcdpkadstrlilhskaqntimem
aaeagtvedleledvlkagyggvkcvesggpepgvgcagrgvitainfleeegayeddld
fvfydvlgdvvcggfampirenkaqeiyivcsgemmamyaanniskgivkyansgsvrlg
glicnsrntdredeliialanklgtqmihfvprdnvvqraeirrmtvieydpkakqadey
ralarkvvdnkllvipnpitmdeleellmefgim
>d1n2cf_ 3.29.1.6.3 Nitrogenase iron protein {(Azotobacter vinelandii)}
amrqcaiygkggigkstttqnlvaalaemgkkvmivgcdpkadstrlilhskaqntimem
aaeagtvedleledvlkagyggvkcvesggpepgvgcagrgvitainfleeegayeddld
fvfydvlgdvvcggfampirenkaqeiyivcsgemmamyaanniskgivkyansgsvrlg
glicnsrntdredeliialanklgtqmihfvprdnvvqraeirrmtvieydpkakqadey
ralarkvvdnkllvipnpitmdeleellmefgim
>d1n2cg_ 3.29.1.6.3 Nitrogenase iron protein {(Azotobacter vinelandii)}
amrqcaiygkggigkstttqnlvaalaemgkkvmivgcdpkadstrlilhskaqntimem
aaeagtvedleledvlkagyggvkcvesggpepgvgcagrgvitainfleeegayeddld
fvfydvlgdvvcggfampirenkaqeiyivcsgemmamyaanniskgivkyansgsvrlg
glicnsrntdredeliialanklgtqmihfvprdnvvqraeirrmtvieydpkakqadey
ralarkvvdnkllvipnpitmdeleellmefgim
>d1n2ch_ 3.29.1.6.3 Nitrogenase iron protein {(Azotobacter vinelandii)}
amrqcaiygkggigkstttqnlvaalaemgkkvmivgcdpkadstrlilhskaqntimem
aaeagtvedleledvlkagyggvkcvesggpepgvgcagrgvitainfleeegayeddld
fvfydvlgdvvcggfampirenkaqeiyivcsgemmamyaanniskgivkyansgsvrlg
glicnsrntdredeliialanklgtqmihfvprdnvvqraeirrmtvieydpkakqadey
ralarkvvdnkllvipnpitmdeleellmefgim
>d1nag__ 7.7.1.1.1 Pancreatic trypsin inhibitor {bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrgnfksaedcmrtcg
>d1nah__ 3.22.1.2.1 Uridine diphosphogalactose-4-epimerase (UDP-galactose 4-epimerase) {(Escherichia coli)}
mrvlvtggsgyigshtcvqllqnghdviildnlcnskrsvlpvierlggkhptfvegdir
nealmteilhdhaidtvihfaglkavgesvqkpleyydnnvngtlrlisamraanvknfi
fsssatvygdnpkipyvesfptgtpqspygksklmveqiltdlqkaqpdwsiallryfnp
vgahpsgdmgedpqgipnnlmpyiaqvavgrrdslaifgndyptedgtgvrdyihvmdla
dghvvameklankpgvhiynlgagvgnsvldvvnafskacgkpvnyhfaprregdlpayw
adaskadrelnwrvtrtldemaqdtwhwqsrhpqgypd
>d1nai__ 3.22.1.2.1 Uridine diphosphogalactose-4-epimerase (UDP-galactose 4-epimerase) {(Escherichia coli)}
mrvlvtggsgyigshtcvqllqnghdviildnlcnskrsvlpvierlggkhptfvegdir
nealmteilhdhaidtvihfaglkavgesvqkpleyydnnvngtlrlisamraanvknfi
fsssatvygdnpkipyvesfptgtpqspygksklmveqiltdlqkaqpdwsiallryfnp
vgahpsgdmgedpqgipnnlmpyiaqvavgrrdslaifgndyptedgtgvrdyihvmdla
dghvvameklankpgvhiynlgagvgnsvldvvnafskacgkpvnyhfaprregdlpayw
adaskadrelnwrvtrtldemaqdtwhwqsrhpqgypd
>d1nal1_ 3.1.3.1.1 N-acetylneuraminate lyase {(Escherichia coli)}
nlrgvmaalltpfdqqqaldkaslrrlvqfniqqgidglyvggstgeafvqslsereqvl
eivaeegkgkikliahvgcvttaesqqlaasakrygfdavsavtpfyypfsfeehcdhyr
aiidsadglpmvvynipalsgvkltldqintlvtlpgvgalkqtsgdlyqmeqirrehpd
lvlyngydeifasgllagadggigstynimgwryqgivkalkegdiqtaqklqtecnkvi
dlliktgvfrglktvlhymdvvsvplcrkpfgpvdekyqpelkalaqqlmq
>d1nal2_ 3.1.3.1.1 N-acetylneuraminate lyase {(Escherichia coli)}
nlrgvmaalltpfdqqqaldkaslrrlvqfniqqgidglyvggstgeafvqslsereqvl
eivaeegkgkikliahvgcvttaesqqlaasakrygfdavsavtpfyypfsfeehcdhyr
aiidsadglpmvvynipalsgvkltldqintlvtlpgvgalkqtsgdlyqmeqirrehpd
lvlyngydeifasgllagadggigstynimgwryqgivkalkegdiqtaqklqtecnkvi
dlliktgvfrglktvlhymdvvsvplcrkpfgpvdekyqpelkalaqqlmq
>d1nal3_ 3.1.3.1.1 N-acetylneuraminate lyase {(Escherichia coli)}
nlrgvmaalltpfdqqqaldkaslrrlvqfniqqgidglyvggstgeafvqslsereqvl
eivaeegkgkikliahvgcvttaesqqlaasakrygfdavsavtpfyypfsfeehcdhyr
aiidsadglpmvvynipalsgvkltldqintlvtlpgvgalkqtsgdlyqmeqirrehpd
lvlyngydeifasgllagadggigstynimgwryqgivkalkegdiqtaqklqtecnkvi
dlliktgvfrglktvlhymdvvsvplcrkpfgpvdekyqpelkalaqqlmq
>d1nal4_ 3.1.3.1.1 N-acetylneuraminate lyase {(Escherichia coli)}
nlrgvmaalltpfdqqqaldkaslrrlvqfniqqgidglyvggstgeafvqslsereqvl
eivaeegkgkikliahvgcvttaesqqlaasakrygfdavsavtpfyypfsfeehcdhyr
aiidsadglpmvvynipalsgvkltldqintlvtlpgvgalkqtsgdlyqmeqirrehpd
lvlyngydeifasgllagadggigstynimgwryqgivkalkegdiqtaqklqtecnkvi
dlliktgvfrglktvlhymdvvsvplcrkpfgpvdekyqpelkalaqqlmq
>d1napa_ 4.7.1.1.10 Neutrophil-activating peptide-2 (NAP-2) {Human (Homo sapiens)}
aelrclcikttsgihpkniqslevigkgthcnqveviatlkdgrkicldpdaprikkivq
kklagd
>d1napb_ 4.7.1.1.10 Neutrophil-acti