>d1sctb_ 1.1.1.1.1 Hemoglobin I [ark clam (Scapharca inaequivalvis)]
KVAELANAVVSNADQKDLLRMSWGVLSVDMEGTGLMLMANLFKTSPSAKGKFARLGDVSAGKDNSKLRGHSITLMYALQNFVDALDDVERLKCVVEKFAVNHINRQISADEFGEIVGPLRQTLKARMGNYFDEDTVAAWASLVAVVQASL
>d1scta_ 1.1.1.1.1 Hemoglobin I [ark clam (Scapharca inaequivalvis)]
VDAAVAKVCGSEAIKANLRRSWGVLSADIEATGLMLMSNLFTLRPDTKTYFTRLGDVQKGKANSKLRGHAITLTYALNNFVDSLDDPSRLKCVVEKFAVNHINRKISGDAFGAIVEPMKETLKARMGNYYSDDVAGAWAALVGVVQAAL
>d3sdha_ 1.1.1.1.1 Hemoglobin I [ark clam (Scapharca inaequivalvis)]
SVYDAAAQLTADVKKDLRDSWKVIGSDKKGNGVALMTTLFADNQETIGYFKRLGNVSQGMANDKLRGHSITLMYALQNFIDQLDNPDDLVCVVEKFAVNHITRKISAAEFGKINGPIKKVLASKNFGDKYANAWAKLVAVVQAAL
>d1emy__ 1.1.1.1.10 Myoglobin [asian elephant (Elephas maximus)]
GLSDGEWELVLKTWGKVEADIPGHGETVFVRLFTGHPETLEKFDKFKHLKTEGEMKASEDLKKQGVTVLTALGGILKKKGHHEAEIQPLAQSHATKHKIPIKYLEFISDAIIHVLQSKHPAEFGADAQGAMKKALELFRNDIAAKYKELGFQG
>d1lht__ 1.1.1.1.11 Myoglobin [Loggerhead sea turtle (Caretta caretta)]
GLSDDEWNHVLGIWAKVEPDLSAHGQEVIIRLFQLHPETQERFAKFKNLTTIDALKSSEEVKKHGTTVLTALGRILKQKNNHEQELKPLAESHATKHKIPVKYLEFICEIIVKVIAEKHPSDFGADSQAAMKKALELFRNDMASKYKEFGFQG
>d1myt__ 1.1.1.1.12 Myoglobin [yellowfin tuna (Thunnus albacares)]
ADFDAVLKCWGPVEADYTTMGGLVLTRLFKEHPETQKLFPKFAGIAQADIAGNAAISAHGATVLKKLGELLKAKGSHAAILKPLANSHATKHKIPINNFKLISEVLVKVMHEKAGLDAGGQTALRNVMGIIIADLEANYKELGFSG
>d1eca__ 1.1.1.1.13 Erythrocruorin [Midge (Chironomous thummi thummi), Fraction III]
LSADQISTVQASFDKVKGDPVGILYAVFKADPSIMAKFTQFAGKDLESIKGTAPFETHANRIVGFFSKIIGELPNIEADVNTFVASHKPRGVTHDQLNNFRAGFVSYMKAHTDFAGAEAAWGATLDTFFGMIFSKM
>d1lh1__ 1.1.1.1.14 Leghemoglobin [yellow lupin (Lupinus luteus l)]
GALTESQAALVKSSWEEFNANIPKHTHRFFILVLEIAPAAKDLFSFLKGTSEVPQNNPELQAHAGKVFKLVYEAAIQLEVTGVVVTDATLKNLGSVHVSKGVADAHFPVVKEAILKTIKEVVGAKWSEELNSAWTIAYDELAIVIKKEMDDAA
>d1fsla_ 1.1.1.1.15 Leghemoglobin [Soybean (Glycine max), isoform A]
VAFTEKQDALVSSSFEAFKANIPQYSVVFYTSILEKAPAAKDLFSFLANGVDPTNPKLTGHAEKLFALVRDSAGQLKASGTVVADAALGSVHAQKAVTDPQFVVVKEALLKTIKAAVGDKWSDELSRAWEVAYDELAAAIKKA
>d1baba_ 1.1.1.1.16 Hemoglobin, alpha-chain [human (Homo sapiens)]
MELSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHGKKVADALTNAVAHVDDMPNALSALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKYR
>d2mhba_ 1.1.1.1.17 Hemoglobin, alpha-chain [horse (Equus caballus)]
VLSAADKTNVKAAWSKVGGHAGEYGAEALERMFLGFPTTKTYFPHFDLSHGSAQVKAHGKKVGDALTLAVGHLDDLPGALSDLSNLHAHKLRVDPVNFKLLSHCLLSTLAVHLPNDFTPAVHASLDKFLSSVSTVLTSKYR
>d1hdsa_ 1.1.1.1.18 Hemoglobin, alpha-chain [deer (Odocoileus virginianus)]
VLSAANKSNVKAAWGKVGGNAPAYGAQALQRMFLSFPTTKTYFPHFDLSHGSAQQKAHGQKVANALTKAQGHLNDLPGTLSNLSNLHAHKLRVNPVNFKLLSHSLLVTLASHLPTNFTPAVHANLNKFLANDSTVLTSKYR
>d1hdaa_ 1.1.1.1.19 Hemoglobin, alpha-chain [bovine (Bos taurus)]
VLSAADKGNVKAAWGKVGGHAAEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHGAKVAAALTKAVEHLDDLPGALSELSDLHAHKLRVDPVNFKLLSHSLLVTLASHLPSDFTPAVHASLDKFLANVSTVLTSKYR
>d1flp__ 1.1.1.1.2 Hemoglobin I [clam (Lucina pectinata)]
SLEAAQKSNVTSSWAKASAAWGTAGPEFFMALFDAHDDVFAKFSGLFSGAAKGTVKNTPEMAAQAQSFKGLVSNWVDNLDNAGALEGQCKTFAANHKARGISAGQLEAAFKVLSGFMKSYGGDEGAWTAVAGALMGEIEPDM
>d2pgha_ 1.1.1.1.20 Hemoglobin, alpha-chain [pig (Sus scrofa)]
VLSAADKANVKAAWGKVGGQAGAHGAEALERMFLGFPTTKTYFPHFNLSHGSDQVKAHGQKVADALTKAVGHLDDLPGALSALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHHPDDFNPSVHASLDKFLANVSTVLTSKYR
>d1outa_ 1.1.1.1.21 Hemoglobin, alpha-chain [trout (Oncorhyncus mykiss)]
SLTAKDKSVVKAFWGKISGKADVVGAEALGRMLTAYPQTKTYFSHWADLSPGSGPVKKHGGIIMGAIGKAVGLMDDLVGGMSALSDLHAFKLRVDPGNFKILSHNILVTLAIHFPSDFTPEVHIAVDKFLAAVSAALADKYR
>d1hbha_ 1.1.1.1.22 Hemoglobin, alpha-chain [antarctic fish (Pagothenia bernacchii)]
SLSDKDKAAVRALWSKIGKSADAIGNDALSRMIVVYPQTKTYFSHWPDVTPGSPHIKAHGKKVMGGIALAVSKIDDLKTGLMELSEQHAYKLRVDPANFKILNHCILVVISTMFPKEFTPEAHVSLDKFLSGVALALAERYR
>d1spga_ 1.1.1.1.23 Hemoglobin, alpha-chain [teleost fish leiostomus xanthurus]
SLSATDKARVKALWDKIEGKSAELGAEALGRMLVSFPQTKIYFSEWGQDLGPQTPQVRNHGAVIMAAVGKAVKSIDNLVGGLSQLSELHAFKLRVDPANFKILAHNIILVISMYFPGDFTPEVHLSVDKFLACLALALSEKYR
>d1babb_ 1.1.1.1.24 Hemoglobin, beta-chain [human (Homo sapiens)]
VHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH
>d1fdhg_ 1.1.1.1.25 Hemoglobin, beta-chain [human fetus (Homo sapiens), gamma-chain]
GHFTEEDKATITSLWGKVNVEDAGGETLGRLLVVYPWTQRFFDSFGNLSSASAIMGNPKVKAHGKKVLTSLGDAIKHLDDLKGTFAQLSELHCDKLHVDPENFKLLGNVLVTVLAIHFGKEFTPEVQASWQKMVTGVASALSSRYH
>d2mhbb_ 1.1.1.1.26 Hemoglobin, beta-chain [horse (Equus caballus)]
VQLSGEEKAAVLALWDKVNEEEVGGEALGRLLVVYPWTQRFFDSFGDLSNPGAVMGNPKVKAHGKKVLHSFGEGVHHLDNLKGTFAALSELHCDKLHVDPENFRLLGNVLVVVLARHFGKDFTPELQASYQKVVAGVANALAHKYH
>d1hdsb_ 1.1.1.1.27 Hemoglobin, beta-chain [deer (Odocoileus virginianus)]
MLTAEEKAAVTGFWGKVDVDVVGAQALGRLLVVYPWTQRFFQHFGNLSSAGAVMNNPKVKAHGKRVLDAFTQGLKHLDDLKGAFAQLSGLHCNKLHVNPQNFRLLGNVLALVVARNFGGQFTPNVQALFQKVVAGVANALAHKYH
>d1hdab_ 1.1.1.1.28 Hemoglobin, beta-chain [bovine (Bos taurus)]
MLTAEEKAAVTAFWGKVKVDEVGGEALGRLLVVYPWTQRFFESFGDLSTADAVMNNPKVKAHGKKVLDSFSNGMKHLDDLKGTFAALSELHCDKLHVDPENFKLLGNVLVVVLARNFGKEFTPVLQADFQKVVAGVANALAHRYH
>d2pghb_ 1.1.1.1.29 Hemoglobin, beta-chain [pig (Sus scrofa)]
VHLSAEEKEAVLGLWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSNADAVMGNPKVKAHGKKVLQSFSDGLKHLDNLKGTFAKLSELHCDQLHVDPENFRLLGNVIVVVLARRLGHDFNPDVQAAFQKVVAGVANALAHKYH
>d1hbg__ 1.1.1.1.3 Glycera globin [marine bloodworm (Glycera dibranchiata)]
GLSAAQRQVIAATWKDIAGADNGAGVGKKCLIKFLSAHPQMAAVFGFSGASDPGVAALGAKVLAQIGVAVSHLGDEGKMVAQMKAVGVRHKGYGNKHIKAQYFEPLGASLLSAMEHRIGGKMNAAAKDAWAAAYADISGALISGLQS
>d1outb_ 1.1.1.1.30 Hemoglobin, beta-chain [trout (Oncorhyncus mykiss)]
VEWTDAEKSTISAVWGKVNIDEIGPLALARVLIVYPWTQRYFGSFGNVSTPAAIMGNPKVAAHGKVVCGALDKAVKNMGNILATYKSLSETHANKLFVDPDNFRVLADVLTIVIAAKFGASFTPEIQATWQKFMKVVVAAMGSRYF
>d1hbhb_ 1.1.1.1.31 Hemoglobin, beta-chain [antartic fish (Pagothenia bernacchii)]
VEWTDKERSIISDIFSHMDYDDIGPKALSRCLIVYPWTQRHFSGFGNLYNAEAIIGNANVAAHGIKVLHGLDRGVKNMDNIAATYADLSTLHSEKLHVDPDNFKLLSDCITIVLAAKMGHAFTAETQGAFQKFLAVVVSALGKQYH
>d1spgb_ 1.1.1.1.32 Hemoglobin, beta-chain [teleost fish leiostomus xanthurus]
VDWTDAERAAIKALWGKIDVGEIGPQALSRLLIVYPWTQRHFKGFGNISTNAAILGNAKVAEHGKTVMGGLDRAVQNMDNIKNVYKQLSIKHSEKIHVDPDNFRLLGEIITMCVGAKFGPSAFTPEIHEAWQKFLAVVVSALGRQYH
>d2lhb__ 1.1.1.1.33 Lamprey globin [sea lamprey (Petromyzon marinus)]
PIVDTGSVAPLSAAEKTKIRSAWAPVYSTYETSGVDILVKFFTSTPAAQEFFPKFKGLTTADELKKSADVRWHAERIINAVDDAVASMDDTEKMSMKLRNLSGKHAKSFQVDPEYFKVLAAVIADTVAAGDAGFEKLMSMICILLRSAY
>d1ash__ 1.1.1.1.34 Ascaris hemoglobin, domain 1 [pig roundworm (Ascaris suum)]
ANKTRELCMKSLEHAKVDTSNEARQDGIDLYKHMFENYPPLRKYFKSREEYTAEDVQNDPFFAKQGQKILLACHVLCATYDDRETFNAYTRELLDRHARDHVHMPPEVWTDFWKLFEEYLGKKTTLDEPTKQAWHEIGREFAKEINK
>d1itha_ 1.1.1.1.35 Hemoglobin [innkeeper worm (Urechis caupo)]
GLTAAQIKAIQDHWFLNIKGCLQAAADSIFFKYLTAYPGDLAFFHKFSSVPLYGLRSNPAYKAQTLTVINYLDKVVDALGGNAGALMKAKVPSHDAMGITPKHFGQLLKLVGGVFQEEFSADPTTVAAWGDAAGVLVAAMK
>d1hlb__ 1.1.1.1.36 Hemoglobin [sea cucumber (Caudina (Molpadia) arenicola)]
GGTLAIQAQGDLTLAQKKIVRKTWHQLMRNKTSFVTDVFIRIFAYDPSAQNKFPQMAGMSASQLRSSRQMQAHAIRVSSIMSEYVEELDSDILPELLATLARTHDLNKVGADHYNLFAKVLMEALQAELGSDFNEKTRDAWAKAFSVVQAVLLVKHG
>d1hlm__ 1.1.1.1.36 Hemoglobin [sea cucumber (Caudina (Molpadia) arenicola)]
GATQSFQSVGDLTPAEKDLIRSTWDQLMTHRTGFVADVFIRIFHNDPTAQRKFPQMAGLSPAELRTSRQMHAHAIRVSALMTTYIDEMDTEVLPELLATLTRTHDKNHVGKKNYDLFGKVLMEAIKAELGVGFTKQVHDAWAKTFAIVQGVLITKHAS
>d1mbd__ 1.1.1.1.4 Myoglobin [sperm whale (Physeter catodon)]
VLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPETLEKFDRFKHLKTEAEMKASEDLKKHGVTVLTALGAILKKKGHHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHPGDFGADAQGAMNKALELFRKDIAAKYKELGYQG
>d1mba__ 1.1.1.1.5 Myoglobin [sea hare (Aplysia limacina)]
SLSAAEADLAGKSWAPVFANKNANGLDFLVALFEKFPDSANFFADFKGKSVADIKASPKLRDVSSRIFTRLNEFVNNAANAGKMSAMLSQFAKEHVGFGVGSAQFENVRSMFPGFVASVAAPPAGADAAWTKLFGLIIDALKAAGA
>d1mbs__ 1.1.1.1.6 Myoglobin [common seal (Phoca vitulina)]
GLSDGEWHLVLNVWGKVETDLAGHGQEVLIRLFKSHPETLEKFDKFKHLKSEDDMRRSEDLRKHGNTVLTALGGILKKKGHHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSKHPAEFGADAQAAMKKALELFRNDIAAKYKELGFHG
>d1myga_ 1.1.1.1.7 Myoglobin [pig (Sus scrofa)]
GLSDGEWQLVLNVWGKVEADVAGHGQEVLIRLFKGHPETLEKFDKFKHLKSEDEMKASEDLKKHGNTVLTALGGILKKKGHHEAELTPLAQSHATKHKIPVKYLEFISEAIIQVLQSKHPGDFGADAQGAMSKALELFRNDMAAKYKELGFQG
>d1hrm__ 1.1.1.1.8 Myoglobin [horse (Equus caballus)]
GLSDGEWQQVLNVWGKVEADIAGHGQEVLIRLFTGHPETLEKFDKFKHLKTEAEMKASEDLKKHGTVVLTALGGILKKKGHHEAELKPLAQSYATKHKIPIKYLEFISDAIIHVLHSKHPGDFGADAQGAMTKALELFRNDIAAKYKELGFQG
>d2mm1__ 1.1.1.1.9 Myoglobin [human (Homo sapiens)]
GLSDGEWQLVLNVWGKVEADIPGHGQEVLIRLFKGHPETLEKFDRFKHLKSEDEMKASEDLKKHGATVLTALGGILKKKGHHEAEIKPLAQSHATKHKIPVKYLEFISEAIIQVLQSKHPGDFGADAQGAMNKALELFRKDMASNYKELGFQG
>d1phnb_ 1.1.1.2.1 Phycocyanin [red alga (Cyanidium caldarium]
MLDAFAKVVAQADARGEFLSNTQLDALSKMVSEGNKRLDVVNRITSNASAIVTNAARALFSEQPQLIQPGGAYTNRRMAACLRDMEIILRYVSYAIIAGDSSILDDRCLNGLRETYQALGVPGASVAVGIEKMKDSAIAIANDPSGITTGDCSALMAEVGTYFDRAATAVQ
>d1phna_ 1.1.1.2.1 Phycocyanin [red alga (Cyanidium caldarium]
MKTPITEAIAAADNQGRFLSNTELQAVNGRYQRAAASLEAARSLTSNAERLINGAAQAVYSKFPYTSQMPGPQYASSAVGKAKCARDIGYYLRMVTYCLVVGGTGPMDEYLIAGLEEINRTFDLSPSWYVEALNYIKANHGLSGQAANEANTYIDYAINALS
>d1cpcb_ 1.1.1.2.2 C-phycocyanin [cyanobacterium (Fremyella diplosiphon)]
MLDAFAKVVSQADARGEYLSGSQIDALSALVADGNKRMDVVNRITGNSSTIVANAARSLFAEQPQLIAPGGNAYTSRRMAACLRDMEIILRYVTYAIFAGDASVLDDRCLNGLKETYLALGTPGSSVAVGVQKMKDAALAIAGDTNGITRGDCASLMAEVASYFDKAASAVA
>d1cpca_ 1.1.1.2.2 C-phycocyanin [cyanobacterium (Fremyella diplosiphon)]
MKTPLTEAVAAADSQGRFLSSTEIQTAFGRFRQASASLAAAKALTEKASSLASGAANAVYSKFPYTTSQNGPNFASTQTGKDKCVRDIGYYLRMVTYCLVVGGTGPLDDYLIGGIAEINRTFDLSPSWYVEALKYIKANHGLSGDPAVEANSYIDYAINALS
>d1allb_ 1.1.1.2.3 Allophycocyanin [(Spirulina platensis)]
MQDAITSVINSSDVQGKYLDASAIQKLKAYFATGELRVRAATTISANAANIVKEAVAKSLLYSDVTRPGGNMYTTRRYAACIRDLDYYLRYATYAMLAGDPSILDERVLNGLKETYNSLGVPIGATVQAIQAMKEVTAGLVGGGAGKEMGIYFDYICSGLS
>d1alla_ 1.1.1.2.3 Allophycocyanin [(Spirulina platensis)]
SIVTKSIVNADAEARYLSPGELDRIKSFVTSGERRVRIAETMTGARERIIKQAGDQLFGKRPDVVSPGGNAYGADMTATCLRDLDYYLRLITYGIVAGDVTPIEEIGVVGVREMYKSLGTPIEAIAEGVRAMKSVATSLLSGADAAEAGSYFDYLIGAMS
>d1liab_ 1.1.1.2.4 R-phycoerythrin [red algae (Polysiphonia urceolata)]
MLDAFSRVVVNSDSKAAYVSGSDLQALKTFINDGNKRLDAVNYIVSNSSCIVSDAISGMICENPGLITPGGNCYTNRRMAACLRDGEIILRYVSYALLAGDASVLEDRCLNGLKETYIALGVPTNSTVRAVSIMKAAAVCFISNTASQRKVEVIEGDCSALASEVASYCDRVVAAVS
>d1liaa_ 1.1.1.2.4 R-phycoerythrin [red algae (Polysiphonia urceolata)]
MKSVITTTISAADAAGRYPSTSDLQSVQGNIQRAAARLEAAEKLGSNHEAVVKEAGDACFSKYGYNKNPGEAGENQEKINKCYRDIDHYMRLINYTLVVGGTGPLDEWGIAGAREVYRTLNLPSAAYIAAFVFTRDRLCIPRDMSAQAGVEFCTALDYLINSLS
>d1erc__ 1.10.1.1.1 ER-1 [Euplotes raikovi]
DACEQAAIQCVESACESLCTEGEDRTGCYMYIYSNCPPYV
>d1erd__ 1.10.1.1.2 ER-2 [Euplotes raikovi]
DPMTCEQAMASCEHTMCGYCQGPLYMTCIGITTDPECGLP
>d1erp__ 1.10.1.1.3 ER-10 [Euplotes raikovi]
DLCEQSALQCNEQGCHNFCSPEDKPGCLGMVWNPELCP
>d1ery__ 1.10.1.1.4 ER-11 [Euplotes raikovi]
DECANAAAQCSITLCNLYCGPLIEICELTVMQNCEPPFS
>d1aca__ 1.11.1.1.1 Acyl-CoA binding protein [bovine (Bos taurus)]
SQAEFDKAAEEVKHLKTKPADEEMLFIYSHYKQATVGDINTERPGMLDFKGKAKWDAWNELKGTSKEDAMKAYIDKVEELKKKYGI
>d1lre__ 1.13.1.1.1 alpha-2-Macroglobulin receptor associated protein (RAP) domain 1 [human (Homo sapiens)]
GEEFRMEKLNQLWEKAQRLHLPPVRLAELHADLKIQERDELAWKKLKLDGLDEDGEKEARLIRNLNVILAKYGLDGKKDAR
>d1vii__ 1.14.1.1.1 Thermostable subdomain from chicken villin headpiece [chicken (Gallus gallus)]
MLSDEDFKAVFGMTRSAFANLPLWKQQNLKKEKGLF
>d1ail__ 1.15.1.1.1 N-terminal, RNA-binding domain of nonstructural protein NS1 [Influenza A virus]
MDSNTVSSFQVDCFLWHVRKQVVDQELGDAPFLDRLRRDQKSLRGRGSTLGLNIEAATHVGKQIVEKILK
>d2end__ 1.16.1.1.1 T4 endonuclease V [Escherichia coli bacteriophage T4]
TRINLTLVSELADQHLMAEYRELPRVFGAVRKHVANGKRVRDFKISPTFILGAGHVTFFYDKLEFLRKRQIELIAECLKRGFNIKDTTVQDISDIPQEFRGDYIPHEASIAISQARLDEKIAQRPTWYKYYGKAIYA
>d1lis__ 1.17.1.1.1 Lysin [red abalone (Haliotis rufescens)]
HYVEPKFLNKAFEVALKVQIIAGFDRGLVKWLRVHGRTLSTVQKKALYFVNRRYMQTHWANYMLWINKKIDALGRTPVVGDYTRLGAEIGRRIDMAYFYDFLKDKNMIPKYLPYMEEINRMRPADVPVKYM
>d1bmfg_ 1.18.1.1.1 ATP syntase (F1-ATPase), gamma subunit [Bovine (Bos taurus)]
ATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKPARVYLCGAIHSSVAKQMKLANIIYYSLKESTTSEQSARMTAMDNASKNASEMIDKLTLTFNRTRQAVITKELIEIISGAAAL
>d1lbu_1 1.19.1.1.1 (1-83) Zn2+ DD-carboxypeptidase, the N-terminal domain [Streptomyces albus G]
DGCYTWSGTLSEGSSGEAVRQLQIRVAGYPGTGAQLAIDGQFGPATKAAVQRFQSAYGLAADGIAGPATFNKIYQLQDDDCTP
>d1grj_1 1.2.1.1.1 (1-78) GreA transcript cleavage protein, N-terminal domain [Escherichia coli]
QAIPMTLRGAEKLREELDFLKSVRRPEIIAAIAEAREHGDLKENAEYHAAREQQGFCEGRIKDIEAKLSNAQVIDVTK
>d1hdj__ 1.2.2.1.1 HSP40 [Human (Homo sapiens)]
MGKDYYQTLGLARGASDEEIKRAYRRQALRYHPDKNKEPGAEEKFKEIAEAYDVLSDPRKREIFDRYGEEGLKGSGC
>d1xbl__ 1.2.2.1.2 DnaJ chaperone, N-terminal (J) domain [Escherichia coli]
AKQDYYEILGVSKTAEEREIRKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDSQKRAAYDQYGHAAFEQ
>d1seta1 1.2.3.1.1 (1-110) Seryl-tRNA synthetase (SerRS), N-terminal domain [Thermus thermophilus, strain hb27]
MVDLKRLRQEPEVFHRAIREKGVALDLEALLALDREVQELKKRLQEVQTERNQVAKRVPKAPPEEKEALIARGKALGEEAKRLEEALREKEARLEALLLQVPLPPWPGAP
>d1idsa1 1.2.4.1.1 (1-84) Fe superoxide dismutase (SOD) [Mycobacterium tuberculosis]
AEYTLPDLDWDYGALEPHISGQINELHHSKHHATYVKGANDAVAKLEEARAKEDHSAILLNEKNLAFNLAGHVNHTIWWKNLSP
>d3sdpa1 1.2.4.1.2 (1-79) Fe superoxide dismutase (SOD) [Pseudomonas ovalis]
PPLPYAHDALQPHISKETLEYHHDKHHNTYVVNLNNLVPGTPEFEGKTLEEIVKSSSGGIFNNAAQVWNHTFYWNCLSP
>d1isaa1 1.2.4.1.3 (1-82) Fe superoxide dismutase (SOD) [Escherichia coli]
SFELPALPYAKDALAPHISAETIEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEIIRSSEGGVFNNAAQVWNHTFYWNCLAP
>d1abma1 1.2.4.1.4 (1-83) Mn superoxide dismutase (SOD) [human (Homo sapiens)]
KHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAKGDVTAQIALQPALKFNGGGHINHSIFWTNLSP
>d1mnga1 1.2.4.1.5 (1-92) Mn superoxide dismutase (SOD) [Thermus thermophilus]
PYPFKLPDLGYPYEALEPHIDAKTMEIHHQKHHGAYVTNLNAALEKYPYLHGVEVEVLLRHLAALPQDIQTAVRNNGGGHLNHSLFWRLLTP
>d1hme__ 1.20.1.1.1 HMG1, fragments A and B [rat/hamster (Rattus norvegicus/Cricetulus griseus)]
FKDPNAPKRPPSAFFLFCSEYRPKIKGEHPGLSIGDVAKKLGEMWNNTAADDKQPYEKKAAKLKEKYEKDIAAYRAK
>d1aab__ 1.20.1.1.1 HMG1, fragments A and B [rat/hamster (Rattus norvegicus/Cricetulus griseus)]
GKGDPKKPRGKMSSYAFFVQTSREEHKKKHPDASVNFSEFSKKCSERWKTMSAKEKGKFEDMAKADKARYEREMKTYIPPKGE
>d2ezda_ 1.20.1.1.2 HMG1, fragments A and B [human (Homo sapiens) HMG-I(Y)]
VPTPKRPRGRPKGSKNKGAAK
>d2ezea_ 1.20.1.1.2 HMG1, fragments A and B [human (Homo sapiens) HMG-I(Y)]
VPTPKRPRGRPKGSKNKGAAKTRKT
>d1hma__ 1.20.1.1.3 HMG-D [Drosophila melanogaster]
SDKPKRPLSAYMLWLNSARESIKRENPGIKVTEVAKRGGELWRAMKDKSEWEAKAAKAKDDYDRAVKEFEANG
>d1hrza_ 1.20.1.1.4 SRY [Human (Homo sapiens)]
DRVKRPMNAFIVWSRDQRRKMALENPRMRNSEISKQLGYQWKMLTEAEKWPFFQEAQKLQAMHREKYPNYKYR
>d1lefa_ 1.20.1.1.6 Lymphoid enhancer-binding factor, LEF1 [mouse (Mus musculus)]
MHIKKPLNAFMLYMKEMRANVVAESTLKESAAINQILGRRWHALSREEQAKYYELARKERQLHMQLYPGWSARDNYGKKKKRKREK
>d1bfma_ 1.21.1.2.1 Histone B [Methanothermus fervidus]
MELPIAPIGRIIKDAGAERVSDDARITLAKILEEMGRDIASEAIKLARHAGRKTIKAEDIELAVRRFKK
>d1tafa_ 1.21.1.3.1 TAFii42 [Fruit fly (Drosophila melanogaster)]
PKDAQVIMSILKELNVQEYEPRVVNQLLEFTFRYVTSILDDAKVYANHARKKTIDLDDVRLATEVTLD
>d1tafb_ 1.21.1.3.2 TAFii62 [Fruit fly (Drosophila melanogaster)]
MLYGSSISAESMKVIAESIGVGSLSDDAAKELAEDVSIKLKRIVQDAAKFMNHAKRQKLSVRDIDMSLKV
>d1mmog_ 1.22.1.1.1 Methane monooxygenase hydrolase, gamma subunit [Methylococcus capsulatus]
LGIHSNDTRDAWVNKIAHVNTLEKAAEMLKQFRMDHTTPFRNSYELDNDYLWIEAKLEEKVAVLKARAFNEVDFRHKTAFGEDAKSVLDGTVAKMNAAKDKWEAEKIHIGFRQAYKPPIMPVNYFLDGERQLGTRLMELRNLNYYDTPLEELRKQRGVRVVH
>d1mhyg_ 1.22.1.1.2 Methane monooxygenase hydrolase, gamma subunit [Methylosinus trichosporium]
AKREPIHDNSIRTEWEAKIAKLTSVDQATKFIQDFRLAYTSPFRKSYDIDVDYQYIERKIEEKLSVLKTEKLPVADLITKATTGEDAAAVEATWIAKIKAAKSKYEAEAIHIEFRQLYKPPVLPVNVFLRTDAALGTVLMEIRNTDYYGTPLEGLRKERGVKVLHLQ
>d1lpe__ 1.23.1.1.1 Apolipoprotein E3 [human (Homo sapiens)]
GQRWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQELRALMDETMKELKAYKSELEEQLTPVAEETRARLSKELQAAQARLGADMEDVCGRLVQYRGEVQAMLGQSTEELRVRLASHLRKLRKRLLRDADDLQKRLAVYQAGA
>d2asr__ 1.23.2.1.1 Aspartate receptor, ligand-binding domain [Escherichia coli]
KSFVVSNQLREQQGELTSTWDLMLQTRINLSRSAVRMMMDSSNQQSNAKVELLDSARKTLAQAATHYKKFKSMAPLPEMVATSRNIDEKYKNYYTALTELIDYLDYGNTGAYFAQPTQGMQNAMGERFAQYALSSEKLYRDI
>d2liga_ 1.23.2.1.2 Aspartate receptor, ligand-binding domain [Salmonella typhimurium]
MGGLLFSSLQHCQQGFVISNELRQQQSELTSTWDLMLQTRINLSRSAARMMMDASNQQSSAKTDLLQNAKTTLAQAAAHYANFKNMTPLPAMAEASANVDEKYQRYQAALAELIQFLDNGNMDAYFAQPTQGMQNALGEALGNYARVSENLYRQTFD
>d256ba_ 1.23.3.1.1 Cytochrome b562 [Escherichia coli]
ADLEDNMETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLANEGKVKEAQAAAEQLKTTRNAYHQKYR
>d2ccya_ 1.23.3.2.1 Cytochrome c' [Rhodospirillum molischianum]
QSKPEDLLKLRQGLMQTLKSQWVPIAGFAAGKADLPADAAQRAENMAMVAKLAPIGWAKGTEALPNGETKPEAFGSKSAEFLEGWKALATESTKLAAAAKAGPDALKAQAAATGKVCKACHEEFKQD
>d1bbha_ 1.23.3.2.2 Cytochrome c' [Chromatium vinosum]
AGLSPEEQIETRQAGYEFMGWNMGKIKANLEGEYNAAQVEAAANVIAAIANSGMGALYGPGTDKNVGDVKTRVKPEFFQNMEDVGKIAREFVGAANTLAEVAATGEAEAVKTAFGDVGAACKSCHEKYRAK
>d1cgo__ 1.23.3.2.4 Cytochrome c' [Alcaligenes sp.]
XFAKPEDAVKYRQSALTLMASHFGRMTPVVKGQAPYDAAQIKANVEVLKTLTALPWAAFGPGTEGGDARPEIWSDAASFKQKQQAFQDNIVKLSAAADAGDLDKLRAAFGDVGASCKACHDAYRK
>d1cpq__ 1.23.3.2.5 Cytochrome c' [(Rhodobacter capsulatus)]
ADTKEVLEAREAYFKSLGGSMKAMTGVAKAFDAEAAKVEAAKLEKILATDVAPLFPAGTSSTDLPGQTEAKAAIWANMDDFGAKGKAMHEAGGAVIAAANAGDGAAFGAALQKLGGTCKACHDDYREED
>d2hmqa_ 1.23.4.1.1 Hemerythrin [sipunculid worm (Themiste dyscrita)]
GFPIPDPYCWDISFRTFYTIVDDEHKTLFNGILLLSQADNADHLNELRRCTGKHFLNEQQLMQASQYAGYAEHKKAHDDFIHKLDTWDGDVTYAKNWLVNHIKTIDFKYRGKI
>d1hrb__ 1.23.4.1.2 Hemerythrin [Phascolopsis gouldi]
GFPIPDPYVWDPSFRTFYSIIDDEHKTLFNGIFHLAIDDNADNLGELRRCTGKHFLNQEVLMEASQYQFYDEHKKEHDGFINALDNWKGDVKWAKAWLVNHIKTIDFKYKGKI
>d2mhr__ 1.23.4.1.4 Myohemerythin [sipunculan worm (Themiste zostericola)]
GWEIPEPYVWDESFRVFYEQLDEEHKKIFKGIFDCIRDNSAPNLATLVKVTTNHFTHEEAMMDAAKYSEVVPHKKMHKDFLEKIGGLSAPVDAKNVDYCKEWLVNHIKGTDFKYKGKL
>d2tmvp_ 1.23.5.1.1 Tobacco mosaic virus coat protein [tobacco mosaic virus (Vulgare strain)]
SYSITTPSQFVFLSSAWADPIELINLCTNALGNQFQTQQARTVVQRQFSEVWKPSPQVTVRFPDSDFKVYRYNAVLDPLVTALLGAFDTRNRIIEVENQANPTTAETLDATRRVDDATVAIRSAINNLIVELIRGTGSYNRSSFESSSGLVWTS
>d1vtmp_ 1.23.5.1.1 Tobacco mosaic virus coat protein [tobacco mosaic virus (Vulgare strain)]
PYTINSPSQFVYLSSAYADPVELINLCTNALGNQFQTQQARTTVQQQFADAWKPSPVMTVRFPASDFYVYRYNSTLDPLITALLNSFDTRNRIIEVNNQPAPNTTEIVNATQRVDDATVAIRASINNLANELVRGTGMFNQAGFETASGLVWTTTPAT
>d1cgme_ 1.23.5.1.2 Cucumber green mottle mosaic virus [cucumber green mottle mosaic virus, watermelon strain]
AYNPITPSKLIAFSASYVPVRTLLNFLVASQGTAFQTQAGRDSFRESLSALPSSVVDINSRFPDAGFYAFLNGPVLRPIFVSLLSSTDTRNRVIEVVDPSNPTTAESLNAVKRTDDASTAARAEIDNLIESISKGFDVYDRASFEAAFSVVWSEATTSKA
>d1rmva_ 1.23.5.1.3 Ribgrass mosaic virus [Ribgrass mosaic virus]
SYNITNSNQYQYFAAVWAEPTPMLNQCVSALSQSYQTQAGRDTVRQQFANLLSTIVAPNQRFPDTGFRVYVNSAVIKPLYEALMKSFDTRNRIIETEEESRPSASEVANATQRVDDATVAIRSQIQLLLNELSNGHGYMNRAEFEAILPWTTAPAT
>d1buca1 1.23.6.1.1 (233-383) Butyryl-CoA dehydrogenase [Megasphaera elsdenii]
GKGFKIAMMTLDGGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTVDAAIAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTGGALLR
>d3mdda1 1.23.6.1.2 (232-385) Medium chain acyl-CoA dehydrogenase [Pig (Sus scrofa)]
GAGFKIAMGTFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLLAEHQGISFLLADMAMKVELARLSYQRAAWEIDSGRRNTYYASIAKAYAADIANQLATDAVQVFGGNGFNTEYPVEKLMRDAKIYQIYEGTAQIQRIIIAREHIGRYK
>d1egda1 1.23.6.1.3 (233-387) Medium chain acyl-CoA dehydrogenase [human homo sapiens]
GAGFKVAMGAFDKERPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYGGTSQIQRLIVAREHIDKYKN
>d1fapb_ 1.23.7.1.1 FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP) [human (Homo sapiens)]
RVAILWHEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLTQAWDLYYHVFRRIS
>d1ryt_1 1.24.1.1.1 (1-146) Rubrerythrin, N-terminal domain [Desulfovibrio vulgaris]
KSLKGSRTEKNILTAFAGESQARNRYNYFGGQAKKDGFVQISDIFAETADQEREHAKRLFKFLEGGDLEIVAAFPAGIIADTHANLIASAAGEHHEYTEMYPSFARIAREEGYEEIARVFASIAVAEEFHEKRFLDFARNIKEGRV
>d1bcfa_ 1.24.1.1.2 Bacterioferritin (cytochrome b1) [Escherichia coli]
MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRLNDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIGEDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMMIEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG
>d1fha__ 1.24.1.1.3 (Apo)ferritin [human (Homo sapiens), H chain]
TSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIQKPDCDDWESGLNAMECALHLEKNVNQSLLELHKLATDKNDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLG
>d1hrs__ 1.24.1.1.4 (Apo)ferritin [horse (Equus caballus), L chain]
SSQIRQNYSTEVEAAVNRLVNLYLRASYTYLSLGFYFDRDDVALEGVCHFFRELAEEKREGAERLLKMQNQRGGRALFQDLQKPSQDEWGTTLDAMKAAIVLEKSLNQALLDLHALGSAQADPHLCDFLESHFLDEEVKLIKKMGDHLTNIQRLVGSQAGLGEYLFERLTLKHD
>d1rcd__ 1.24.1.1.5 (Apo)ferritin [bullfrog (Rana catesbeiana)]
SQVRQNFHQDCEAGLNRTVNLKFHSSYVYLSMASYFNRDDVALSNFAKFFRERSEEEKEHAEKLIEYQNQRGGRVFLQSVEKPERDDWANGLEALQTALKLQKSVNQALLDLHAVAADKSDPHMTDFLESPYLSESVETIKKLGDHITSLKKLWSSHPGMAEYLFNKHTLG
>d1mmod_ 1.24.1.2.1 Methane monooxygenase hydrolase, beta and alpha subunits [Methylococcus capsulatus]
AANRAPTSVNAQEVHRWLQSFNWDFKNNRTKYATKYKMANETKEQFKLIAKEYARMEAVKDERQFGSLQVALTRLNAGVRVHPKWNETMKVVSNFLEVGEYNAIAATGMLWDSAQAAEQKNGYLAQVLDEIRHTHQCAYVNYYFAKNGQDPAGHNDARRTRTIGPLWKGMKRVFSDGFISGDAVECSLNLQLVGEACFTNPLIVAVTEWAAANGDEITPTVFLSIETDELRHMANGYQTVVSIANDPASAKYLNTDLNNAFWTQQKYFTPVLGMLFEYGSKFKVEPWVKTWDRWVYEDWGGIWIGRLGKYGVESPRSLKDAKQDAYWAHHDLYLLAYALWPTGFFRLALPDQEEMEWFEANYPGWYDHYGKIYEEWRARGCEDPSSGFIPLMWFIENNHPIYIDRVSQVPFCPSLAKGASTLRVHEYNGEMHTFSDQWGERMWLAEPERYECQNIFEQYEGRELSEVIAELHGLRSDGKTLIAQPHVRGDKLWTLDDIKRLNCVFKNPVKAF
>d1mmob_ 1.24.1.2.1 Methane monooxygenase hydrolase, beta and alpha subunits [Methylococcus capsulatus]
ERRRGLTDPEMAAVILKALPEAPLDGNNKMGYFVTPRWKRLTEYEALTVYAQPNADWIAGGLDWGDWTQKFHGGRPSWGNETTELRTVDWFKHRDPLRRWHAPYVKDKAEEWRYTDRFLQGYSADGQIRAMNPTWRTSSCNRYWGAFLFNEYGLFNAHSQGAREALSDVTRVSLAFWGFDKIDIAQMIQLERGFLAKIVPGFDESTAVPKAEWTNGEVYKSARLAVEGLWQEVFDWNESAFSVHAVYDALFGQFVRREFFQRLAPRFGDNLTPFFINQAQTYFQIAKQGVQDLYYNCLGDDPEFSDYNRTVMRNWTGKWLEPTIAALRDFMGLFAKLPAGTTDKEEITASLYRVVDDWIEDYASAIDFKADRDQIVKAVLAGLK
>d1mhyb_ 1.24.1.2.2 Methane monooxygenase hydrolase, beta and alpha subunits [Methylosinus trichosporium]
KRGLTDPERAAIIAAAVPDHALDTQRKYHYFIQPRWKPLSEYEQLSCYAQPNPDWIAGGLDWGDWTQKFHGGRPSWGNESTELRTTDWYRHRDPARRWHHPYVKDKSEEARYTQRFLAAYSSEGSIRTIDPYWRDEILNKYFGALLYSEYGLFNAHSSVGRDCLSDTIRQTAVFAALDKVDNAQMIQMERLFIAKLVPGFDASTDVPKKIWTTDPIYSGARATVQEIWQGVQDWNEILWAGHAVYDATFGQFARREFFQRLATVYGDTLTPFFTAQSQTYFQTTRGAIDDLFVYCLANDSEFGAHNRTFLNAWTEHYLASSVAALKDFVGLYAKVEKVAGATDSAGVSEALQRVFGDWKIDYADKIGFRVDVDQKVDAVLAGY
>d1mhyd_ 1.24.1.2.2 Methane monooxygenase hydrolase, beta and alpha subunits [Methylosinus trichosporium]
NRAPVGVEPQEVHKWLQSFNWDFKENRTKYPTKYHMANETKEQFKVIAKEYARMEAAKDERQFGTLLDGLTRLGAGNKVHPRWGETMKVISNFLEVGEYNAIAASAMLWDSATAAEQKNGYLAQVLDEIRHTHQCAFINHYYSKHYHDPAGHNDARRTRAIGPLWKGMKRVFADGFISGDAVECSVNLQLVGEACFTNPLIVAVTEWASANGDEITPTVFLSVETDELRHMANGYQTVVSIANDPASAKFLNTDLNNAFWTQQKYFTPVLGYLFEYGSKFKVEPWVKTWNRWVSEDWGGIWIGRLGKYGVESPRSLRDAKRDAYWAHHDLALAAYAMWPLGFARLALPDEEDQAWFEANYPGWADHYGKIFNEWKKLGYEDPKSGFIPYQWLLANGHDVYIDRVSQVPFIPSLAKGTGSLRVHEFNGKKHSLTDDWGERQWLIEPERYECHNVFEQYEGRELSEVIAEGHGVRSDGKTLIAQPHTRGDNLWTLEDIKRAGCVFPDPLAKF
>d1riba_ 1.24.1.2.3 Ribonucleotide reductase R2 [Escherichia coli]
AYTTFSATKNDQLKEPMFFGQPVQVARYDQQKYDIFEKLIEKQLSFFWRPEEVDVSRDRIDYQALPEHEKHIFISNLKYQTLLDSIQGRSPNVALLPLISIPELETWVETWAFSETIHSRSYTHIIRNIVNDPSVVFDDIVTNEQIQKRAEGISSYYDELIEMTSYWHLLGEGTHTVNGKTVTVSLRELKKKLYLCLMSVNALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHLTGTQHMLNLLRSGADDPEMAEIAEECKQECYDLFVQAAQQEKDWADYLFRDGSMIGLNKDILCQYVEYITNIRMQAVGLDLPFNTRSNPIPWINTWLV
>d1xsm__ 1.24.1.2.4 Ribonucleotide reductase R2 [mouse (Mus musculus)]
NPSVEDEPLLRENPRRFVVFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWEALKPDERHFISHVLAFFAASDGIVNENLVERFSQEVQVTEARCFYGFQIAMENIHSEMYSLLIDTYIKDPKEREYLFNAIETMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPAEQRVREIITNAVRIEQEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFNKIFRVENPFDFME
>d1afra_ 1.24.1.2.5 delta 9-stearoyl-acyl carrier protein desaturase [Castor bean (Ricinus communis)]
MPPREVHVQVTHSMPPQKIEIFKSLDNWAEENILVHLKPVEKCWQPQDFLPDPASDGFDEQVRELRERAKEIPDDYFVVLVGDMITEEALPTYQTMLNTLDGVRDETGASPTSWAIWTRAWTAEENRHGDLLNKYLYLSGRVDMRQIEKTIQYLIGSGMDPRTENSPYLGFIYTSFQERATFISHGNTARQAKEHGDIKLAQICGTIAADEKRHETAYTKIVEKLFEIDPDGTVLAFADMMRKKISMPAHLMYDGRDDNLFDHFSAVAQRLGVYTAKDYADILEFLVGRWKVDKLTGLSAEGQKAQDYVCRLPPRIRRLEERAQGRAKEAPTMPFSWIFDRQVKL
>d1rhga_ 1.25.1.1.1 Granulocyte-colony stimulating factor (G-CSF) [human (Homo sapiens)]
LPQSFLLKCLEQVRKIQGDGAALQEKLCATYKLCHPEELVLLGHSLGIPWAPLLAGCLSQLHSGLFLYQGLLQALEGISPELGPTLDTLQLDVADFATTIWQQMEELGMMPAFASAFQRRAGGVLVASHLQSFLEVSYRVLRHLA
>d1bgc__ 1.25.1.1.2 Granulocyte-colony stimulating factor (G-CSF) [Bovine (Bos taurus)]
SLPQSFLLKCLEQVRKIQADGAELQERLCAAHKLCHPEELMLLRHSLGIPQAPLSSCSSQSLQLRGCLNQLHGGLFLYQGLLQALAGISPELAPTLDTLQLDVTDFATNIWLQMEDLGAAPAMPTFTSAFQRRAGGVLVASQLHRFLELAYRGLRYLA
>d1bgea_ 1.25.1.1.3 Granulocyte-colony stimulating factor (G-CSF) [canine (Canis familiaris)]
PLPQSFLLKCLEQMRKVQADGTALQETLCATHQLCHPEELVLLGHALGIPQPPLSSCSSQALQLMGCLRQLHSGLFLYQGLLQALAGISPELAPTLDTLQLDTTDFAINIWQQMEDLGMAPTMPAFTSAFQRRAGGVLVASNLQSFLELAYRALRHFAK
>d1lki__ 1.25.1.1.4 Leukemia inhibitory factor (LIF) [mouse (Mus musculus)]
NATCAIRHPCHGNLMNQIKNQLAQLNGSANALFISYYTAQGEPFPNNVEKLCAPNMTDFPSFHGNGTEKTKLVELYRMVAYLSASLTNITRDQKVLNPTAVSLQVKLNATIDVMRGLLSNVLCRLCNKYRVGHVDVPPVPDHSDKEAFQRKKLGCQLLGTYKQVISVVVQAF
>d1huw__ 1.25.1.1.5 Growth hormone, somatotropin [human (Homo sapiens)]
FPTIPLSRLADNAWLRADRLNQLAFDTYQEFEEAYIPKEQIHSFWWNPQTSLCPSESIPTPSNKEETQQKSNLELLRISLLLIQSWLEPVQFLRSVFANSLVYGASDSNVYDLLKDLEEGIQTLMGRLEALLKNYGLLYCFNKDMSKVSTYLRTVQCRSVEGSCGF
>d1hgu__ 1.25.1.1.5 Growth hormone, somatotropin [human (Homo sapiens)]
PTIPLSRLFQNAMLRAHRLHQLAFDTYEEFEEAYIQKYSFLQAPQASLCFSESIPTPSNREQAQQKSNLQLLRISLLLIQSWLEPVGFLRSVFANSLVYGASDSDVYDLLKDLEEGIQTLMGRLEDGSPRTGQAFKQTYAKFDANSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCG
>d3hhra_ 1.25.1.1.5 Growth hormone, somatotropin [human (Homo sapiens)]
FPTIPLSRLFDNAMLRAHRLHQLAFDTYQEFEEAYIPKEQKYSFLQNPQTSLCFSESIPTPSNREETQQKSNLELLRISLLLIQSWLEPVQFLRSVFANSLVYGASDSNVYDLLKDLEEGIQTLMGRLEDGSPRTGQIFKQTYSKFDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCG
>d1cnt1_ 1.25.1.1.6 Ciliary neurotrophic factor (CNTF) [Human (Homo sapiens)]
PHRRDLCSRSIWLARKIRSDLTALTESYVKHQGLWSELTEAERLQENLQAYRTFHVLLARLLEDQQVHFTPTEGDFHQAIHTLLLQVAAFAYQIEELMILLEYKIPRNEADGMLFEKKLWGLKVLQELSQWTVRSIHDLRFISSHQTGIP
>d1csga_ 1.25.1.2.1 Granulocyte-macrophage colony-stimulating factor (GM-SCF) [human (Homo sapiens)]
SPSPSTQPWEHVNAIQEARRLLNLSRDTAAEMNETVEVISEMFDLQEPTCLQTRLELYKQGLRGSLTKLKGPLTMMASHYKQHCPPTPETSCATQIITFESFKENLKDFLLVIPFDCWEP
>d2int__ 1.25.1.2.2 Interleukin-4 (IL-4) [human (Homo sapiens)]
HKCDITLQEIIKTLNSLTEQKTLCTELTVTDIFAASKNTTEKETFCRAATVLRQFYSHHEKDTRCLGATAQQFHRHKQLIRFLKRLDRNLWGLAGLNSCPVKEANQSTLENFLERLKTIMREKYSKCSS
>d1hula_ 1.25.1.2.3 Interleukin-5 [human (Homo sapiens)]
IPTSALVKETLALLSTHRTLLIANETLRIPVPVHKNHQLCTEEIFQGIGTLESQTVQGGTVERLFKNLSLIKKYIDGQKKKCGEERRRVNQFLDYLQEFLGVMNTEWI
>d1hmca_ 1.25.1.2.4 Macrophage colony-stimulating factor (M-CSF) [human (Homo sapiens)]
SEYCSHMIGSGHLQSLQRLIDSQMETSCQITFEFVDQEQLKDPVCYLKKAFLLVQDIMEDTMRFRDNTPNAIAIVQLQELSLRLKSCFTKDYEEHDKACVRTFYETPLQLLEKVKNVFNETKNLLDKDWNIFSKNCNNSFAECSSQGH
>d3inkc_ 1.25.1.2.5 Interleukin-2 (IL-2) [human (Homo sapiens)]
STKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKCEYADETATIVEFLNRWITFAQSIISTLT
>d1jli__ 1.25.1.2.6 Interleukin-3 (IL-3) [human (Homo sapiens)]
ANCSIMIDEIIHHLKRPPNPLLDPNNLNSEDMDILMERNLRTPNLLAFVRAVKHLENASAIESILKNLLPCLPLATAAPTRHPIHIKDGDWNEFRRKLTFYLKTLENAQAQQ
>d1ilk__ 1.25.1.3.1 Interleukin-10 (cytokine synthesis inhibitory factor, CSIF) [human (Homo sapiens)]
NSCTHFPGNLPNMLRDLRDAFSRVKTFFQMKDQLDNLLLKESLLEDFKGYLGCQALSEMIQFYLEEVMPQAENQDPDIKAHVNSLGENLKTLRLRLRRCHRFLPCENKSKAVEQVKNAFNKLQEKGIYKAMSEFDIFINYIEAYMTMKIRN
>d1vlk__ 1.25.1.3.2 Interleukin-10 (cytokine synthesis inhibitory factor, CSIF) [Epstein-Barr virus, EBV]
CDNFPQMLRDLRDAFSRVKTFFQTKDEVDNLLLKESLLEDFKGYLGCQALSEMIQFYLEEVMPQAENQDPEAKDHVNSLGENLKTLRLRLRRCHRFLPCENKSKAVEQIKNAFNKLQEKGIYKAMSEFDIFINYIEAYMTIK
>d1rmi__ 1.25.1.3.3 Interferon-beta [mouse (Mus musculus)]
INYKQLQLQERTNIRKCQELLEQLNGKINLTYRADFKIPMEMTEKMQKSYTAFAIQEMLQNVFLVFRNNFSSTGWNETIVVRLLDELHQQTVFLKTVLEEKQEERLTWEMSSTALHLKSYYWRVQRYLKLMKYNSYAWMVVRAEIFRNFLIIRRLTRNFQ
>d1rfba_ 1.25.1.3.4 Interferon-gamma [bovine (Bos taurus)]
QGQFFREIENLKEYFNASSPDVAKGGPLFSEILKNWKDESDKKIIQSQIVSFYFKLFENLKDNQVIQRSMDIIKQDMFQKFLNGSSEKLEDFKKLIQIPVDDLQIQRKAINELIKVMND
>d1higa_ 1.25.1.3.5 Interferon-gamma [human (Homo sapiens)]
QDPYVKEAENLKKYFNAGHSDVADNGTLFLGILKNWKEESDRKIMQSQIVSFYFKLFKNFKDDQSIQKSVETIKEDMNVKFFNSNKKKRDDFEKLTNYSVTDLNVQRKAIHELIQVMAELSPA
>d2rig__ 1.25.1.3.6 Interferon-gamma [rabbit (Oryctolagus cuniculus)]
QDTLTRETEHLKAYLKANTSDVANGGPLFLNILRNWKEESDNKIIQSQIVSFYFKLFDNLKDHEVIKKSMESIKEDIFVKFFNSNLTKMDDFQNLTRISVDDRLVQRKAVSELSNVLNF
>d1acp__ 1.26.1.1.1 Acyl carrier protein [Escherichia coli]
STIEERVKKIIGEQLGVKQEEVTNNASFVEDLGADSLDTVELVMALEEEFDTEIPDEEAEKITTVQAAIDYINGHQA
>d1af8__ 1.26.1.1.2 Actinorhodin polyketide synthase acyl carrier protein, ACT ACP [Streptomyces coelicolor A3(2)]
MATLLTTDDLRRALVECAGETDGTDLSGDFLDLRFEDIGYDSLALMETAARLESRYGVSIPDDVAGRVDTPRELLDLINGALAEAA
>d1cei__ 1.26.2.1.1 ImmE7 protein [Escherichia coli]
LKNSISDYTEAEFVQLLKEIEKENVAATDDVLDVLLEHFVKITEHPDGTDLIYYPSDNRDDSPEGIVKEIKEWRAANGKPGFKQG
>d1imq__ 1.26.2.1.2 ImE9 protein [Escherichia coli]
MELKHSISDYTEAEFLQLVTTICNADTSSEEELVKLVTHFEEMTEHPSGSDLIYYPKEGDDDSPSGIVNTVKQWRAANGKSGFKQG
>d1rpo__ 1.27.1.1.1 ROP protein [Escherichia coli]
MTKQEKTALNMARFIRSQTLTLLEKLNELADAADEQADICESLHDHADELYRSCLARFGDD
>d1ytfb1 1.28.1.1.1 Transcription factor IIA (TFIIA), N-terminal domain [Baker's yeast (Schaccharomyces cerevisiae)]
SNAEASRVYEIIVESVVNEVREDFENAGIDEQTLQDLKNIWQKKLT
>d1ytfd1 1.28.1.1.1 (1-50) Transcription factor IIA (TFIIA), N-terminal domain [Baker's yeast (Schaccharomyces cerevisiae)]
GYYELYRRSTIGNSLVDALDTLISDGRIEASLAMRVLETFDKVVAETLKD
>d1ecia_ 1.29.1.1.1 Ectatomin, A & B chains [ant (Ectatomma tuberculatum) venom]
GVIPKKIWETVCPTVEPWAKKCSGDIATYIKRECGKL
>d1ecib_ 1.29.1.1.1 Ectatomin, A & B chains [ant (Ectatomma tuberculatum) venom]
WSTIVKLTICPTLKSMAKKCEGSIATMIKKKCDK
>d1ctj__ 1.3.1.1.1 Cytochrome c6 (synonym: cytochrome c553) [(Monoraphidium braunii)]
EADLALGKAVFDGNCAACHAGGGNNVIPDHTLQKAAIEQFLDGGFNIEAIVYQIENGKGAMPAWDGRLDEDEIAGVAAYVYDQAAGNKW
>d1c2ra_ 1.3.1.1.10 Cytochrome c2 [Rhodobacter capsulatus]
GDAAKGEKEFNKCKTCHSIIAPDGTEIVKGAKTGPNLYGVVGRTAGTYPEFKYKDSIVALGASGFAWTEEDIATYVKDPGAFLKEKLDDKKAKTGMAFKLAKGGEDVAAYLASVVK
>d2cxba_ 1.3.1.1.11 Cytochrome c2 [Rhodobacter spaeroides]
EGDPEAGAKAFNQCQTCHVIVDDSGTTIAGRNAKTGPNLYGVVGRTAGTQADFKGYGEGMKEAGAKGLAWDEEHFVQYVQDPTKFLKEYTGDAKAKGKMTFKLKKEADAHNIWAYLQQVAVRP
>d1cry__ 1.3.1.1.12 Cytochrome c2 [Rhodopseudomonas viridis]
QDAASGEQVFKQCLVCHSIGPGAKNKVGPVLNGLFGRHSGTIEGFAYSDANKNSGITWTEEVFREYIRDPKAKIPGTKMIFAGVKDEQKVSDLIAYIKQFNADGSKK
>d1hroa_ 1.3.1.1.13 Cytochrome c2 [(Rhodopila globiformis)]
SAPPGDPVEGKHLFHTICITCHTDIKGANKVGPSLYGVVGRHSGIEPGYNYSEANIKSGIVWTPDVLFKYIEHPQKIVPGTKMGYPGQPDPQKRADIIAYLETLK
>d155c__ 1.3.1.1.14 Cytochrome c2 [Paracoccus denitrificans]
NEGDAAKGEKEFNKCKACHMIQAPDGTDIKGGKTGPNLYGVVGRKIASEEGFKYGEGILEVAEKNPDLTWTEANLIEYVTDPKPLVKKMTDDKGAKTKMTFKMGKNQADVVAFLAQDDPDAXXXXXXXXXXXXX
>d1cot__ 1.3.1.1.14 Cytochrome c2 [Paracoccus denitrificans]
DGDAAKGEKEFNKCKACHMIQAPDGTDIIKGGKTGPNLYGVVGRKIASEEGFKYGEGILEVAEKNPDLTWTEADLIEYVTDPKPWLVKMTDDKGAKTKMTFKMGKNQADVVAFLAQNSPDA
>d1cc5__ 1.3.1.1.15 Cytochrome c5 [Azotobacter vinelandii]
GGGARSGDDVVAKYCNACHGTGLLNAPKVGDSAAWKTRADAKGGLDGLLAQSLSGLNAMPPKGTCADCSDDELKAAIGKMSGL
>d1cch__ 1.3.1.1.16 Cytochrome c551 [Pseudomonas stutzeri]
QDGEALFKSKPCAACHSVDTKMVGPALKEVAAKNAGVEGAADTLALHIKNGSQGVWGPIPMPPNPVTEEEAKILAEWVLSLK
>d1cor__ 1.3.1.1.16 Cytochrome c551 [Pseudomonas stutzeri]
XDGEALFKSKPCAACHSIDAKLVGPAFKEVAAKYAGQDGAADLLAGHIKNGSQGVWGPIPMPPNPVTEEEAKILAEWILSQK
>d351c__ 1.3.1.1.17 Cytochrome c551 [Pseudomonas aeruginosa]
EDPEVLFKNKGCVACHAIDTKMVGPAYKDVAAKFAGQAGAEAELAQRIKNGSQGVWGPIPMPPNAVSDDEAQTLAKWVLSQK
>d2mtac_ 1.3.1.1.18 Cytochrome c551 [Paracoccus denitrificans]
APQFFNIIDGSPLNFDDAMEEGRDTEAVKHFLETGENVYNEDPEILPEAEELYAGMCSGCHGHYAEGKIGPGLNDAYWTYPGNETDVGLFSTLYGGATGQMGPMWGSLTLDEMLRTMAWVRHLYTGDPKDASWLTDEQKAGFTPFQP
>d1gks__ 1.3.1.1.19 Cytochrome c551 [(Ectothiorhodospira halophila)]
DGESIYINGTAPTCSSCHDRGVAGAPELNAPEDWADRPSSVDELVESTLAGKGAMPAYDGRADREDLVKAIEYMLSTL
>d1dvh__ 1.3.1.1.2 Cytochrome c6 (synonym: cytochrome c553) [Desulfovibrio vulgaris, strain miyazaki f]
ADGAALYKSCIGCHGADGSKAAMGSAKPVKGQGAEELYKKMKGYADGSYGGERKAMMTNAVKKYSDEELKALADYMSKL
>d1c53__ 1.3.1.1.2 Cytochrome c6 (synonym: cytochrome c553) [Desulfovibrio vulgaris, strain miyazaki f]
ADGAALYKSCVGCHGADGSKQAMGVGHAVKGQKADELFKKLKGYADGSYGGEKKAVMTNLVKRYSDEEMKAMADYMSKL
>d1cyi__ 1.3.1.1.3 Cytochrome c6 (synonym: cytochrome c553) [Chlamydomonas reinhardtii]
ADLALGAQVFNGNCAACHMGGRNSVMPEKTLDKAALEQYLDGGFKVESIIYQVENGKGAMPAWADRLSEEEIQAVAEYVFKQATDAAWK
>d1yeb__ 1.3.1.1.4 Mitochondrial cytochrome c [baker's yeast (Saccharomyces cerevisiae)]
TEFKAGSAKKGATLFKTRCQQCHTIEEGGPNKVGPNLHGIFGRHSGQVKGYSYTDANINKNVKWDEDSMSEYLTNPKKYIPGTKMAFGGLKKEKDRNDLITYLKKACE
>d1ycc__ 1.3.1.1.4 Mitochondrial cytochrome c [baker's yeast (Saccharomyces cerevisiae)]
TEFKAGSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGRHSGQAEGYSYTDANIKKNVLWDENNMSEYLTNPKKYIPGTKMAFGGLKKEKDRNDLITYLKKACE
>d1yea__ 1.3.1.1.4 Mitochondrial cytochrome c [baker's yeast (Saccharomyces cerevisiae)]
AKESTGFKPGSAKKGATLFKTRCQQCHTIEEGGPNKVGPNLHGIFGRHSGQVKGYSYTDANINKNVKWDEDSMSEYLTNPKKYIPGTKMAFAGLKKEKDRNDLITYMTKAAK
>d1hrc__ 1.3.1.1.5 Mitochondrial cytochrome c [horse (Equus caballus)]
GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWKEETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE
>d1ccr__ 1.3.1.1.6 Mitochondrial cytochrome c [rice embryos (Oryza sativa l)]
ASFSEAPPGNPKAGEKIFKTKCAQCHTVDKGAGHKQGPNLNGLFGRQSGTTPGYSYSTADKNMAVIWEENTLYDYLLNPKKYIPGTKMVFPGLKKPQERADLISYLKEATS
>d5cytr_ 1.3.1.1.7 Mitochondrial cytochrome c [albacore tuna (Thunnus alalunga)]
GDVAKGKKTFVQKCAQCHTVENGGKHKVGPNLWGLFGRKTGQAEGYSYTDANKSKGIVWNNDTLMEYLENPKKYIPGTKMIFAGIKKKGERQDLVAYLKSATS
>d3c2c__ 1.3.1.1.9 Cytochrome c2 [Rhodospirillum rubrum]
EGDAAAGEKVSKKCLACHTFDQGGANKVGPNLFGVFENTAAHKDNYAYSESYTEMKAKGLTWTEANLAAYVKNPKAFVLEKSGDPKAKSKMTFKLTKDDEIENVIAYLKTLK
>d1aofa1 1.3.1.2.1 (1-98) N-terminal (heme c) domain of cytochrome cd1-nitrite reductase [Thiosphaera pantotropha]
DVAAPGAPEGVTALSDAQYNEANKIYFERCAGCHGVLRKGATGKALTPDLTRDLGFDYLQSFITYASPAGMPNWGTSGELSAEQVDLMANYLLLDPAA
>d1etpa2 1.3.1.3.1 (93-190) Cytochrome c4 [Pseudomonas stutzeri]
GYADPALAKQGEKLFRGGKLDQGMPACTGCHAPNGVGNDLAGFPKLGGQHAAYTAKQLTDFREGNRTNDGDTMIMRGVAAKLSNKDIEALSSYIQGLH
>d1etpa1 1.3.1.3.1 (1-92) Cytochrome c4 [Pseudomonas stutzeri]
AGDAEAGQGKVAVCGACHGVDGNSPAPNFPKLAGQGERYLLKQLQDIKAGSTPGAPEGVGRKVLEMTGMLDPLSDQDLEDIAAYFSSQKGSV
>d1fcdc2 1.3.1.3.2 (81-174) Flavocytochrome c sulfide dehydrogenase, FCSD, cytochrome subunit [Purple phototrophic bacterium (Cromatium vinosum)]
AKQSFDTALADTGAKLHDKYCEKCHVEGGKPLADEEDYHILAGQWTPYLQYAMSDFREERRPMEKKMASKLRELLKAEGDAGLDALFAFYASQQ
>d1fcdc1 1.3.1.3.2 (1-80) Flavocytochrome c sulfide dehydrogenase, FCSD, cytochrome subunit [Purple phototrophic bacterium (Cromatium vinosum)]
EPTAEMLTNNCAGCHGTHGNSVGPASPSIAQMDPMVFVEVMEGFKSGEIASTIMGRIAKGYSTADFEKMAGYFKQQTYQP
>d1octc2 1.30.1.1.1 (1-71) Oct-1 POU-specific domain [human (Homo sapiens)]
DLEELEQFAKTFKQRRIKLGFTQGDVGLAMGKLYGNDFSQTTISRFEALNLSFKNMCKLKPLLEKWLNDAE
>d1llia_ 1.30.1.2.1 lambda C1 repressor, DNA-binding domain [Escherichia coli bacteriophage Lambda]
KKPLTQEQLEDARRLKAIYEKKKNELGLSQESLADKLGMGQSGIGALFNGINALNAYNAALLAKILKVSVEEFSPSIAREIYEMYEAVS
>d1r69__ 1.30.1.2.2 434 C1 repressor, DNA-binding domain [Escherichia coli phage 434]
SISSRVKSKRIQLGLNQAELAQKVGTTQQSIEQLENGKTKRPRFLPELASALGVSVDWLLNGT
>d2cro__ 1.30.1.2.3 cro 434 [bacteriophage 434]
MQTLSERLKKRRIALKMTQTELATKAGVKQQSIQLIEAGVTKRPRFLFEIAMALNCDPVWLQYGT
>d1adr__ 1.30.1.2.4 p22 C2 repressor, DNA-binding domain [Salmonella bacteriophage P22]
MNTQLMGERIRARRKKLKIRQAALGKMVGVSNVAISQWERSETEPNGENLLALSKALQCSPDYLLKGDLSQTNVAY
>d1copd_ 1.30.1.2.5 cro lambda repressor [Escherichia coli bacteriophage Lambda]
MEQRITLKDYAMRFGQTKTAKDLGVYQSAINKAIHAGRKIFLTINADGSVYAEEVKPFPSNKKTTA
>d1ner__ 1.30.1.2.6 NER [Bacteriophage mu]
CSNEKARDWHRADVIAGLKKRKLSLSALSRQFGYAPTTLANALERHWPKGEQIIANALETKPEVIWPSRYQAGE
>d1pnra1 1.30.1.3.1 (1-56) Purine repressor (PurR), N-terminal domain [Escherichia coli]
TIKDVAKRANVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKVNH
>d1lcca_ 1.30.1.3.2 Lac repressor (LacR), N-terminal domain [Escherichia coli, strain bmh 74-12]
MKPVTLYDVAEYAGVSYQTVSRVVNQASHVSAKTREKVEAAMAELNYIPNR
>d1uxd__ 1.30.1.3.3 Fructose repressor (FruR), N-terminal domain [Escherichia coli]
MKLDEIARLAGVSRTTASYVINGKAKQYRVSDKTVEKVMAVVREHNYHPNAVAAGLRLQ
>d2tct_1 1.31.1.1.1 (1-66) Tetracyclin repressor (Tet-repressor, TetR), N-terminal domain [Escherichia coli]
ARLNRESVIDAALELLNETGIDGLTTRKLAQKLGIEQPTLYWHVKNKRALLDALAVEILARHHDYS
>d1rnl_1 1.31.1.2.1 (139-200) Nitrate/nitrite response regulator (NARL), receiver domain [Escherichia coli]
QLTPRERDILKLIAQGLPNKMIARRLDITESTVKVHVKHMLKKMKLKSRVEAAVWVHQERIF
>d1coo__ 1.32.1.1.1 the C-terminal domain of RNA polymerase alpha subunit [Escherichia coli]
FDPILLRPVDDLELTVRSANCLKAEAIHYIGDLVQRTEVELLKTPNLGKKSLTEIKDVLASRGLSLGMRLENWPPASIADE
>d1an2a_ 1.33.1.1.1 Max protein [mouse (Mus musculus)]
ADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQVRALEKARS
>d1mdya_ 1.33.1.1.2 Myod B/HLH domain [mouse (Mus musculus)]
MELKRKTTNADRRKAATMRERRRLSKVNEAFETLKRSTSSNPNQRLPKVEILRNAIRYIEGLQALLRD
>d1an4a_ 1.33.1.1.3 Usf B/HLH domain [human (Homo sapiens)]
MDEKRRAQHNEVERRRRDKINNWIVQLSKIIPDSSMESTKSGQSKGGILSKASDYIQELRQSNHR
>d4icb__ 1.34.1.1.1 Calbindin D9K [bovine (Bos taurus)]
MKSPEELKGIFEKYAAKEGDPNQLSKEELKLLLQTEFPSLLKGPSTLDELFEELDKNGDGEVSFEEFQVLVKKISQ
>d1cb1__ 1.34.1.1.2 Calbindin D9K [porcine (Sus scrofa)]
SAQKSPAELKSIFEKYAAKEGDPNQLSKEELKQLIQAEFPSLLKGPRTLDDLFQELDKNGDGEVSFEEFQVLVKKISQ
>d1cnpa_ 1.34.1.2.1 Calcyclin (S100) [Rabbit (Oryctolagus cuniculus)]
MASPLDQAIGLLIGIFHKYSGKEGDKHTLSKKELKELIQKELTIGSKLQDAEIVKLMDDLDRNKDQEVNFQEYITFLGALAMIYNEALKG
>d1syma_ 1.34.1.2.2 Calcyclin (S100) [rat (Rattus norvegicus)]
MSELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMETLDEDGDGECDFQEFMAFVSMVTTACHEFFEHE
>d1sra__ 1.34.1.3.1 The C-terminal (EC) domain of BM-40/SPARC/osteonectin [human (Homo sapiens)]
PPCLDSELTEFPLRMRDWLKNVLVTLYERDEDNNLLTEKQKLRVKKIHENEKRLEAGDHPVELLARDFEKNYNMYIFPVHWQFGQLDQHPIDGYLSHTELAPLRAPLIPMEHCTTRFFETCDLDNDKYIALDEWAGCFGIKQKDIDKDLVI
>d1rro__ 1.34.1.4.1 Oncomodulin [rat (Rattus norvegicus), Sprague-dawley strain]
SITDILSAEDIAAALQECQDPDTFEPQKFFQTSGLSKMSASQVKDIFRFIDNDQSGYLDGDELKYFLQKFQSDARELTESETKSLMDAADNDGDGKIGADEFQEMVHS
>d4cpv__ 1.34.1.4.2 Parvalbumin [carp (Cyprinus carpio)]
AFAGVLNDADIAAALEACKAADSFNHKAFFAKVGLTSKSADDVKKAFAIIDQDKSGFIEEDELKLFLQNFKADARALTDGETKTFLKAGDSDGDGKIGVDEFTALVKA
>d1pvaa_ 1.34.1.4.3 Parvalbumin [pike (Esox lucius)]
AAKDLLKADDIKKALDAVKAEGSFNHKKFFALVGLKAMSANDVKKVFKAIDADASGFIEEEELKFVLKSFAADGRDLTDAETKAFLKAADKDGDGKIGIDEFETLVHEA
>d1pvb__ 1.34.1.4.3 Parvalbumin [pike (Esox lucius)]
SFAGLKDADVAAALAACSAADSFKHKEFFAKVGLASKSLDDVKKAFYVIDQDKSGFIEEDELKLFLQNFSPSARALTDAETKAFLADGDKDGDGMIGVDEFAAMIKA
>d5pal__ 1.34.1.4.4 Parvalbumin [leopard shark (Triakis semifasciata)]
PMTKVLKADDINKAISAFKDPGTFDYKRFFHLVGLKGKTDAQVKEVFEILDKDQSGFIEEEELKGVLKGFSAHGRDLNDTETKALLAAGDSDHDGKIGADEFAKMVAQA
>d1rtp1_ 1.34.1.4.5 Parvalbumin [rat (Rattus rattus)]
SMTDLLSAEDIKKAIGAFTAADSFDHKKFFQMVGLKKKSADDVKKVFHILDKDKSGFIEEDELGSILKGFSSDARDLSAKETKTLMAAGDKDGDGKIGVEEFSTLVAES
>d1top__ 1.34.1.5.1 Troponin C [chicken (Gallus gallus)]
ASMTDQQAEARAFLSEEMIAEFKAAFDMFDADGGGDISTKELGTVMRMLGQNPTKEELDAIIEEVDEDGSGTIDFEEFLVMMVRQMKEDAKGKSEEELANCFRIFDKNADGFIDIEELGEILRATGEHVTEEDIEDLMKDSDKNNDGRIDFDEFLKMMEGVQ
>d1ctaa_ 1.34.1.5.1 Troponin C [chicken (Gallus gallus)]
KSEEELANAFRIFDKNADGYIDIEELGEILRATG
>d1osa__ 1.34.1.5.11 Calmodulin [Paramecium tetraurelia]
AEQLTEEQIAEFKEAFALFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLSLMARKMKEQDSEEELIEAFKVFDRDGNGLISAAELRHVMTNLGEKLTDDEVDEMIREADIDGDGHINYEEFVRMMVSK
>d1scmb_ 1.34.1.5.12 Myosin Essential Chain [bay scallop (Aequipecten irradians)]
LPQKQIQEMKEAFSMIDVDRDGFVSKEDIKAISEQLGRAPDDKELTAMLKEAPGPLNFTMFLSIFSDKLSGTDSEETIRNAFAMFDEQETKKLNIEYIKDLLENMGDNFNKDEMRMTFKEAPVEGGKFDYVKFTAMIK
>d2mysb_ 1.34.1.5.13 Myosin Essential Chain [chicken (Gallus gallus)]
FDETEIEDFKEAFTVIDQNADGIIDKDDLRETFAAMGRLNVKNEELDAMIKEASGPINFTVFLTMFGEKLKGADPEDVIMGAFKVLDPDGKGSIKKSFLEELLTTGGGFTPEEIKNMWAAFPVDYKNICYVITHGEDA
>d1scmc_ 1.34.1.5.14 Myosin Regulatory Chain [bay scallop (Aequipecten irradians)]
SQDEIDDLKDVFELFDFWDGRDGAVDAFKLGDVCRCLGINPRNEDVFAVGGTHKMGEKSLPFEEFLPAYEGLMDCEQGTFADYMEAFKTFDREGQGFISGAELRHVLTALGERLSDEDVDEIIKLTDLQEDLEGNVKYEDFVKKVMAGP
>d2mysc_ 1.34.1.5.15 Myosin Regulatory Chain [chicken (Gallus gallus)]
AAADDFKEAFLLFDRTGDAKITASQVGDIARALGQNPTNAEINKIAAITFEEFLPMLQAAANNKDQGTFEDFVEGLRVFDKEGNGTVMGAELRHVLATLGEKMTEEEVEELMKGQEDSNGCINYEAFVKHIMSV
>d1tcob_ 1.34.1.5.16 Calcineurin regulatory subunit (B-chain) [Bovine (Bos taurus)]
GNEASYPLEMCSHFDADEIKRLGKRFKKLDLDNSGSLSVEEFMSLPELQQNPLVQRVIDIFDTDGNGEVDFKEFIEGVSQFSVKGDKEQKLRFAFRIYDMDKDGYISNGELFQVLKMMVGNNLKDTQLQQIVDKTIINADKDGDGRISFEEFCAVVGGLDIHKKMVVDV
>d1rec__ 1.34.1.5.18 Recoverin [bovine (Bos taurus)]
LSKEILEELQLNTKFTEEELSSWYQSFLKECPSGRITRQEFQTIYSKFFPEADPKAYAQHVFRSFGTLDFKEYVIALHMTSAGKTNQKLEWAFSLYDVDGNGTISKNEVLEIVTAIFKMISPEDTKHLPEDENTPEKRAEKIWGFFGKKDDDKLTEKEFIEGTLANKEILRLIQFEPQKVKEKLK
>d2scpa_ 1.34.1.5.3 Sarcoplasmic calcium-binding protein [sandworm (Nereis diversicolor)]
SDLWVQKMKTYFNRIDFDKDGAITRMDFESMAERFAKESEMKAEHAKVLMDSLTGVWDNFLTAVAGGKGIDETTFINSMKEMVKNPEAKSVVEGPLPLFFRAVDTNEDNNISRDEYGIFFGMLGLDKTMAPASFDAIDTNNDGLLSLEEFVIAGSDFFMNDGDSTNKVFWGPLV
>d2sas__ 1.34.1.5.4 Sarcoplasmic calcium-binding protein [amphioxus (Branchiostoma lanceolatum)]
GLNDFQKQKIKFTFDFFLDMNHDGSIQDNDFEDMMTRYKEVNKGSLSDADYKSMQASLEDEWRDLKGRADINKDDVVSWEEYLAMWEKTIATCKSVADLPAWCQNRIPFLFKGMDVSGDGIVDLEEFQNYCKNFQLQCADVPAVYNVITDGGKVTFDLNRYKELYYRLLTSPAADAGNTLMGQKP
>d1cdma_ 1.34.1.5.6 Calmodulin [bovine (Bos taurus)]
LTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMAEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMT
>d1djxa1 1.34.1.6.1 (1-82) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) [Rat (Rattus norvegicus)]
EIETFYKMLTQRAEIDRAFEEAAGSAETLSVERLVTFLQHQQREEEAGPALALSLIERYEPSETAKAQRQMTKDGFLMYLLS
>d1cpo_2 1.34.2.1.1 (120-298) Cloroperoxidase [Fungus (Caldariomyces fumago)]
NSNDFIDNRNFDAETFQTSLDVVAGKTHFDYADMNEIRLQRESLSNELDFPGWFTESKPIQNVESGFIFALVSDFNLPDNDENPLVRIDWWKYWFTNESFPYHLGWHPPSPAREIEFVTSASSAVLAASVTSTPSSLPSGAIGPGAEAVPLSFASTMTPFLLATNAPYYAQDPTLGPND
>d1cpo_1 1.34.2.1.1 (1-119) Cloroperoxidase [Fungus (Caldariomyces fumago)]
EPGSGIGYPYDNNTLPYVAPGPTDSRAPCPALNALANHGYIPHDGRAISRETLQNAFLNHMGIANSVIELALTNAFVVCEYVTGSDCGDSLVNLTLLAEPHAFEHDHSFSRKDYKQGVA
>d1pax_1 1.35.1.1.1 (1-135) A domain of poly(ADP-ribose) polymerase [Chicken (Gallus gallus)]
KSKLAKPIQDLIKMIFDVESMKKAMVEFEIDLQKMPLGKLSKRQIQSAYSILNEVQQAVSDGGSESQILDLSNRFYTLIPHDFGMKKPPLLSNLEYIQAKVQMLDNLLDIEVAYSLLRGGNEDGDKDPIDINYEK
>d1myla_ 1.36.1.1.1 Arc repressor [Salmonella bacteriophage P22]
KMPQFNLRWPREVLDLVRKVAEENGMSVNSYIYQLVMESFKKEGR
>d1myka_ 1.36.1.1.1 Arc repressor [Salmonella bacteriophage P22]
KMLQFNLRWPREVLDLVRKVAEENGRSVNSEIYQRVMESFKKEGRIG
>d1mnta_ 1.36.1.1.2 Mnt repressor [Salmonella bacteriophage P22]
ARDDPHFNFRMPMEVREKLKFRAEANGRSMNSELLQIVQDALSKPSPVTGYRNDAERLADEQSELV
>d1cmba_ 1.36.1.2.1 Met repressor [Escherichia coli]
AEWSGEYISPYAEHGKKSEQVKKITVSIPLKVLKILTDERTRRQVNNLRHATNSELLCEAFLHAFTGQPLPDDADLRKERSDEIPEAAKEIMREMGINPETWEY
>d1dsba1 1.37.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain [Escherichia coli]
GGDLGKDLTQAWAVAMALGVEDKVTVPLFEGVQKTQTIRSASDIRDVFINAGIKGEEYDAAWNS
>d1bed_1 1.37.1.1.2 (63-126) Disulphide-bond formation facilitator (DSBA), insertion domain [Vibrio cholerae]
GNMGQAMSKAYATMIALEVEDKMVPVMFNRIHTLRKPPKDEQELRQIFLDEGIDAAKFDAAYNG
>d2gsta1 1.38.1.1.1 (85-217) Glutathione S-transferase [rat (Rattus rattus), class mu]
LCGETEEERIRADIVENQVMDNRMQLIMLCYNPDFEKQKPEFLKTIPEKMKLYSEFLGKRPWFAGDKVTYVDFLAYDILDQYHIFEPKCLDAFPNLKDFLARFEGLKKISAYMKSSRYLSTPIFSKLAQWSNK
>d1glqa1 1.38.1.1.2 (79-209) Glutathione S-transferase [mouse (Mus musculus)]
YGKNQREAAQMDMVNDGVEDLRGKYVTLIYTNYENGKNDYVKALPGHLKPFETLLSQNQGGKAFIVGDQISFADYNLLDLLLIHQVLAPGCLDNFPLLSAYVARLSARPKIKAFLSSPEHVNRPINGNGKQ
>d2gsra1 1.38.1.1.3 (77-207) Glutathione S-transferase [pig (Sus scrofa)]
YGKDQKEAALVDMVNDGVEDLRCKYATLIYTNYEAGKEKYVKELPEHLKPFETLLSQNQGGQAFVVGSQISFADYNLLDLLRIHQVLNPSCLDAFPLLSAYVARLSARPKIKAFLASPEHVNRPINGNGKQ
>d1gssa1 1.38.1.1.4 (79-209) Glutathione S-transferase [human (Homo sapiens), class pi]
YGKDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVKALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLIHEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVNLPINGNGKQ
>d1hna_1 1.38.1.1.5 (85-217) Glutathione S-transferase [human (Homo sapiens), class mu]
LCGESEKEQIREDILENQFMDSRMQLAKLCYDPDFEKLKPEYLQALPEMLKLYSQFLGKQPWFLGDKITFVDFIAYDVLERNQVFEPSCLDAFPNLKDFISRFEGLEKISAYMKSSRFLPRPVFTKMAVFGNK
>d1gsea1 1.38.1.1.6 (80-221) Glutathione S-transferase [human (Homo sapiens), class alpha]
LYGKDIKERALIDMYIEGIADLGEMILLLPVCPPEEKDAKLALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLVELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPGSPRKPPMDEKSLEEARKIFRF
>d1gsq_1 1.38.1.1.7 (76-202) Glutathione S-transferase [Squid (Ommastrephes sloani pacificus)]
LDGKTSLEKYRVDEITETLQDIFNDVVKIKFAPEAAKEAVQQNYEKSCKRLAPFLEGLLVSNGGGDGFFVGNSMTLADLHCYVALEVPLKHTPELLKDCPKIVALRKRVAECPKIAAYLKKRPVRDF
>d1gta_1 1.38.1.1.8 (81-218) Glutathione S-transferase [Schistosoma japonicum]
MLGGCPKERAEISMLEGAVLDIRYGVSRIAYSKDFETLKVDFLSKLPEMLKMFEDRLCHKTYLNGDHVTHPDFMLYDALDVVLYMDPMCLDAFPKLVCFKKRIEAIPQIDKYLKSSKYIAWPLQGWQATFGGGDHPPK
>d1gnwa1 1.38.1.1.9 (85-210) Glutathione S-transferase [mouse-ear cress (Arabidopsis thaliana)]
LQTDSKNISQYAIMAIGMQVEDHQFDPVASKLAFEQIFKSIYGLTTDEAVVAEEEAKLAKVLDVYEARLKEFKYLAGETFTLTDLHHIPAIQYLLGTPTKKLFTERPRVNEWVAEITKRPASEKVQ
>d1bmta1 1.39.1.1.1 (1-90) Methionine synthase domain [Escherichia coli]
QAEWRSWEVNKRLEYSLVKGITEFIEQDTEEARQQATRPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSARVMKQAVAYLEPFIEASK
>d1tpt_1 1.39.2.1.1 (1-70) Thymidine phosphorylase, N-terminal domain [Escherichia coli]
LFLAQEIIRKKRDGHALSDEEIRFFINGIRDNTISEGQIAALAMTIFFHDMTMPERVSLTMAMRDSGTVL
>d1enh__ 1.4.1.1.1 engrailed Homeodomain [Drosophila melanogaster]
RPRTAFSSEQLARLKREFNENRYLTERRRQQLSSELGLNEAQIKIWFQNKRAKI
>d1vnd__ 1.4.1.1.10 VND/NK-2 protein [fruit fly (Drosophila melanogaster)]
ASDGLPNKKRKRRVLFTKAQTYELERRFRQQRYLSAPEREHLASLIRLTPTQVKIWFQNHRYKTKRAQNEKGYEGHP
>d1fjla_ 1.4.1.1.11 Paired protein [fruit fly (Drosophila melanogaster)]
KQRRSRTTFSASQLDELERAFERTQYPDIYTREELAQRTNLTEARIQVWFQNRRARLRKQHTSVS
>d1yrna_ 1.4.1.1.2 mat A1/alpha2 Homeodomain [brewer's yeast (Saccharomyces cerevisiae)]
ISPQARAFLEQVFRRKQSLNSKEKEEVAKKCGITPLQVRVWFINKRMRS
>d1yrnb_ 1.4.1.1.2 mat A1/alpha2 Homeodomain [brewer's yeast (Saccharomyces cerevisiae)]
TKPYRGHRFTKENVRILESWFAKNIENPYLDTKGLENLMKNTSLSRIQIKNWVSNRRRKEKTITIAPELADLLSGEPL
>d1lfb__ 1.4.1.1.3 Transcription factor LFB1 [rat (Rattus rattus)]
RFKWGPASQQILFQAYERQKNPSKEERETLVEECNRAECIQRGVSPSQAQGLGSNLVTEVRVYNWFANRRKEEAFRH
>d1octc1 1.4.1.1.4 (72-131) Oct-1 POU Homeodomain [human (Homo sapiens)]
RKKRTSIETNIRVALEKSFLENQKPTSEEITMIADQLNMEKEVIRVWFCNRRQKEKRINP
>d1ftt__ 1.4.1.1.5 Thyroid transcription factor 1 homeodomain [rat (Rattus rattus)]
MRRKRRVLFSQAQVYELERRFKQQKYLSAPEREHLASMIHLTPTQVKIWFQNHRYKMKRQAKDKAAQQ
>d1hdp__ 1.4.1.1.6 Oct-2 POU Homeodomain [human (Homo sapiens)]
RRKKRTSIETNVRFALEKSFLANQKPTSEEILLIAEQLHMEKEVIRVWFCNRRQKEKRINP
>d1ocp__ 1.4.1.1.7 Oct-3 POU Homeodomain [mouse (Mus musculus)]
METLVQARKRKRTSIENRVRWSLETMFLKCPKPSLQQITHIANQLGLEKDVVRVWFCNRRQKGKRSS
>d1ahdp_ 1.4.1.1.8 antennapedia Homeodomain [Drosophila melanogaster]
MRKRGRQTYTRYQTLELEKEFHFNRYLTRRRRIEIAHALSLTERQIKIWFQNRRMKWKKENKTKGEPG
>d1ftz__ 1.4.1.1.9 Fushi Tarazu protein [fruit fly (Drosophila melanogaster)]
MDSKRTRQTYTRYQTLELEKEFHFNRYITRRRRIDIANALSLSERQIKIWFQNRRMKSKKDRTLDSSPEH
>d1hcra_ 1.4.1.2.1 HIN recombinase (DNA-binding domain) [synthetic]
GRPRAINKHEQEQISRLLEKGHPRQQLAIIFGIGVSTLYRYFPASSIKKRMN
>d1res__ 1.4.1.2.2 gamma,delta resolvase (C-terminal domain) [Escherichia coli]
GRKRKIDRDAVLNMWQQGLGASHISKTMNIARSTVYKVINESN
>d1mbf__ 1.4.1.3.2 c-Myb, DNA-binding domain [mouse (Mus musculus)]
LGKTRWTREEDEKLKKLVEQNGTDDWKVIANYLPNRTDVQCQHRWQKVLNPE
>d1msec2 1.4.1.3.2 (56-105) c-Myb, DNA-binding domain [mouse (Mus musculus)]
KTSWTEEEDRIIYQAHKRLGNRWAEIAKLLPGRTDNAIKNHWNSTMRRKV
>d1msec1 1.4.1.3.2 (1-55) c-Myb, DNA-binding domain [mouse (Mus musculus)]
MLIKGPWTKEEDQRVIKLVQKYGPKRWSVIAKHLKGRIGKQCRERWHNHLNPEVK
>d1pdnc_ 1.4.1.4.1 Paired protein (prd) [Fruit fly (Drosophila melanogaster)]
QGRVNQLGGVFINGRPLPNNIRLKIVEMAADGIRPCVISRQLRVSHGCVSKILNRYQETGSIRPGVIGGSKPRIATPEIENRIEEYKRSSPGMFSWEIREKLIREGVCDRSTAPSVSAISRLV
>d1igna1 1.4.1.5.1 (1-86) DNA-binding domain of rap1 [baker's yeast (Saccharomyces cerevisiae)]
KASFTDEEDEFILDVVRKNPTRRTTHTLYDEISHYVPNHTGNSIRHRFRVYLSKRLEYVYEVDKFGKLVRDDDGNLIKTKVLPPSI
>d1igna2 1.4.1.5.1 (87-189) DNA-binding domain of rap1 [baker's yeast (Saccharomyces cerevisiae)]
KRKFSADEDYTLAIAVKKQFYRDLFQIDPDTGRSLIRTQSRRGPIAREFFKHFAEEHAAHTENAWRDRFRKFLLAYGIDDYISYYEAEEPMKNLTPTPGNYNS
>d1sfe_1 1.4.2.1.1 (82-165) Ada DNA repair protein, C-terminal domain [Escherichia coli]
GTAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIVIPCHRVVRGDGSLSGYRWGVSRKAQLLRREAEN
>d1bia_1 1.4.3.1.1 (1-63) Biotin repressor, N-terminal domain [Escherichia coli]
MKDNTVPLKLIALLANGEFHSGEQLGETLGMSRAAINKHIQTLRDWGVDVFTVPGKGYSLPEP
>d1hks__ 1.4.3.10.1 Heat-shock transcription factor [Drosophila melanogaster]
GSGVPAFLAKLWRLVDDADTNRLICWTKDGQSFVIQNQAQFAKELLPLNYKHNNMASFIRQLNMYGFHKITSIDNGGLRFDRDEIEFSHPFFKRNSPFLLDQIKRK
>d2hts__ 1.4.3.10.2 Heat-shock transcription factor [Milk yeast (Kluyveromyces lactis)]
ARPAFVNKLWSMVNDKSNEKFIHWSTSGESIVVPNRERFVQEVLPKYFKHSNFASFVRQLNMYGWHKVQDVKSGSNDSRWEFENERHA
>d1dpra1 1.4.3.11.1 (1-62) Diphtheria toxin repressor (DtxR) [Corynebacterium diphtheriae]
DLVDTTEMYLRTIYELEEEGVTPLRARIAERLEQSGPTVSQTVARMERDGLVVVASDRSLQM
>d1xgsa1 1.4.3.12.1 (195-271) Methionine aminopeptidase, insert domain [Pyrococcus furiosus]
GQVIEVPPTLIYMYVRDVPVRVAQARFLLAKIKREYGTLPFAYRWLQNDMPEGQLKLALKTLEKAGAIYGYPVLKEI
>d1lea__ 1.4.3.2.1 LexA repressor, N-terminal DNA-binding domain [Escherichia coli]
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEE
>d1aoy__ 1.4.3.3.1 Arginine repressor (ArgR), N-terminal DNA-binding domain [Escherichia coli]
MRSSAKQEELVKAFKALLKEEKFSSQGEIVAALQEQGFDNINQSKVSRMLTKFGAVRTRNAKMEMVYCLPAELGVPTT
>d1cgpa1 1.4.3.4.1 (130-197) Catabolite gene activator protein (CAP), C-terminal domain [Escherichia coli]
DVTGRIAQTLLNLAKQPDAMTHPDGMQIKITRQEIGQIVGCSRETVGRILKMLEDQNLISAHGKTIVV
>d1opc__ 1.4.3.5.1 OMPR C-terminal DNA-binding domain [Escherichia coli]
VIAFGKFKLNLGTREMFREDEPMPLTSGEFAVLKALVSHPREPLSRDKLMNLARGREYSAMERSIDVQISRLRRMVEEDPAHPRYIQTVWGLGYVFVPD
>d1hsta_ 1.4.3.7.1 Histone H5, globular domain [chicken (Gallus gallus)]
SHPTYSEMIAAAIRAEKSRGGSSRQSIQKYIKSHYKVGHNADLQIKLSIRRLLAAGVLKQTKGVGASGSFRLAK
>d1ghc__ 1.4.3.7.2 Histone H1, globular domain [chicken (Gallus gallus)]
MAGPSVTELITKAVSASKERKGLSLAALKKALAAGGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFRLSK
>d1flia_ 1.4.3.9.1 Fli-1 [Human (Homo sapiens)]
PGSGQIQLWQFLLELLSDSANASCITWEGTNGEFKMTDPDEVARRWGERKSKPNMNYDKLSRALRYYYDKNIMTKVHGKRYAYKFDFHGIAQALQPHP
>d1etd__ 1.4.3.9.2 ETS-1 transcription factor, residues 331-440 [Murine (Mus musculus)]
IQLWQFLLELLTDKSCQSFISWTGDGWEFKLSDPDEVARRWGKRKNKPKMNYEKLSRGLRYYYDKNIIHKTAGKRYVYRFVCDLQSLLGYTPEELHAMLDVKPDAD
>d1puee_ 1.4.3.9.4 transcription factor PU.1, residues 171-259 [Murine (Mus musculus)]
KIRLYQFLLDLLRSGDMKDSIWWVDKDKGTFQFSSKHKEALAHRWGIQKGNRKKMTYEKMARALRNYGKTGEVKKVKKKLTYQFSGEV
>d1fow__ 1.4.4.1.1 Ribosomal protein L11, the C-terminal domain [Bacillus stearothermophilus]
MTFITKTPPAAVLLKKAAGIESGSGEPNRNKVATIKRDKVREIAELKMPDLNAASIEAAMRMIEGTARSMGIVVED
>d1kjs__ 1.40.1.1.1 C5a anaphylotoxin [human (Homo sapiens)]
MLQKKIEEIAAKYKHSVVKKCCYDGACVNNDETCEQRAARISLGPRCIKAFTECCVVASQLRANISHKDMQLGR
>d1c5a__ 1.40.1.1.2 C5a anaphylotoxin [pig (Sus scrofa domestica)]
MLQKKIEEEAAKYKYAMLKKCCYDGAYRNDDETCEERAARIKIGPKCVKAFKDCCYIANQVRAEQ
>d1occh_ 1.41.1.1.1 Cytochrome c oxidase subunit h [bovine (Bos taurus)]
YQTAPFDSRFPNQNQTRNCWQNYLDFHRCEKAMTAKGGDVSVCEWYRRVYKSLCPISWVSTWDDRRAEGTFPGKI
>d1hyp__ 1.42.1.1.1 Soybean hydrophobic protein [soybean (Glycine max)]
PSCPDLSICLNILGGSLGTVDDCCALIGGLGDIEAIVCLCIQLRALGILNLNRNLQLILNSCGRSYPSNATCPRT
>d1lpt__ 1.42.1.1.2 plant non-specific lipid-transfer protein (ns-LTP) [wheat (Triticum aestivum) L. seeds]
IDCGHVDSLVRPCLSYVQGGPGPSGQCCDGVKNLHNQARSQSDRQSACNCLKGIARGIHNLNEDNARSIPPKCGVNLPYTISLNIDCSRV
>d1lip__ 1.42.1.1.3 plant non-specific lipid-transfer protein (ns-LTP) [Barley (Hordeum vulgare)]
LNCGQVDSKMKPCLTYVQGGPGPSGECCNGVRDLHNQAQSSGDRQTVCNCLKGIARGIHNLNLNNAASIPSKCNVNVPYTISPDIDCSRIY
>d1mzm__ 1.42.1.1.4 plant non-specific lipid-transfer protein (ns-LTP) [maize (Zea mays)]
AISCGQVASAIAPCISYARGQGSGPSAGCCSGVRSLNNAARTTADRRAACNCLKNAAAGVSGLNAGNAASIPSKCGVSIPYTISTSTDCSRVN
>d1bip__ 1.42.1.2.1 Trypsin/alpha-amylase inhibitor RBI [Ragi (Eleusine coracana caertneru) seeds]
SVGTSCIPGMAIPHNPLDSCRWYVSTRTCGVGPRLATQEMKARCCRQLEAIPAYCRCEAVRILMDGVVTSSGQHEGRLLQDLPGCPRQVQRAFAPKLVTEVECNLATIHGGPFCLSLLGAGE
>d1pnb.1 1.42.1.3.1 (a,b) Napin BNIb [rape (Brassica napus]
QPQKCQREFQQEQHLRACQQWIRQQLAGSPFTLKQAAKSVRVQGQHGPFQSTRIYQIAKNLPNVCNMKQIGTCPFIAIQPQKCQREFQQEQHLRACQQWIRQQLAGSPFTLKQAAKSVRVQGQHGPFQSTRIYQIAKNLPNVCNMKQIGTCPFIAI
>d1bpya1 1.43.1.1.1 (1-82) DNA polymerase beta, N-terminal (8 kD)-domain [Human (Homo sapiens)]
TLNGGITDMLTELANFEKNVSQAIHKYNAYRKAASVIAKYPHKIKSGAEAKKLPGVGTKIAEKIDEFLATGKLRKLEKIRQD
>d1olga_ 1.44.1.1.1 p53 tetramerization domain [human (Homo sapiens)]
KKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPG
>d1adt_1 1.45.1.1.1 (1-90) A domain of early E2A DNA-binding protein, ADDBP [Adenovirus type 5]
PIVSAWEKGMEAARALMDKYHVDNDLKANFKLLPDQVEALAAVCKTWLNEEHRGLQLTFTSNKTFVTMMGRFLQAYLQSFAEVTYKHHEP
>d1ihfb_ 1.46.1.1.1 Integration host factor (IHF) [Escherichia coli]
MTKSELIERLATQQSHIPAKTVEDAVKEMLEHMASTLAQGERIEIRGFGSFSLHYRAPRTGRNPKTGDKVELEGKYVPHFKPGKELRDRANIYG
>d1ihfa_ 1.46.1.1.1 Integration host factor (IHF) [Escherichia coli]
ALTKAEMSEYLFDKLGLSKRDAKELVELFFEEIRRALENGEQVKLSGFGNFDLRDKNQRPGRNPKTGEDIPITARRVVTFRPGQKLKSRVENASPK
>d1hnr__ 1.46.1.1.2 DNA-binding domain of H1 protein, (H-NS) [Escherichia coli]
AQRPAKYSYVDENGETKTWTGQGRTPAVIKKAMDEQGKSLDDFLIKQ
>d1huea_ 1.46.1.1.3 HU protein [Bacillus stearothermophilus]
MNKTELINAVAETSGLSKKDATKAVDAVFDSITEALRKGDKVQLIGFGNFEVRERAARKGRNPQTGEEMEIPASKVPAFKPGKALKDAVK
>d1wtua_ 1.46.1.1.4 Transcription factor 1, TF1 [Bacillus subtilis phage SPO1]
MNKTELIKAIAQDTELTQVSVSKMLASFEKITTETVAKGDKVQLTGFLNIKPVARQARKGFNPQTQEALEIAPSVGVSVKPGESLKKAAEGLKYEDFAK
>d1alo_1 1.47.1.1.1 (81-193) Aldehyde oxidoreductase, domain 2 [(Desulfovibrio gigas)]
QPENLHPLQKAWVLHGGAQCGFCSPGFIVSAKGLLDTNADPSREDVRDWFQKHRNACRCTGYKPLVDAVMDAAAVINGKKPETDLEFKMPADGRIWGSKYPRPTAVAKVTGTL
>d1ab3__ 1.48.1.1.1 Ribosomal protein S15 from [Thermus thermophilus]
PITKEEKQKVIQEFARFPGDTGSTEVQVALLTLRINRLSEHLKVHKKDHHSHRGLLMMVGQRRRLLRYLQREDPERYRALIEKLGIRG
>d1aep__ 1.49.1.1.1 Apolipophorin-III [african locust (Locusta migratoria)]
NIAEAVQQLNHTIVNAAHELHETLGLPTPDEALNLLTEQANAFKTKIAEVTTSLKQEAEKHQGSVAEQLNAFARNLNNSIHDAATSLNLQDQLNSLQSALTNVGHQWQDIATKTQASAQEAWAPVQSALQEAAEKTKEAAANLQNSIQSAVQK
>d1cuk_1 1.5.1.1.1 (143-190) DNA helicase RuvA subunit, C-terminal domain [Escherichia coli]
TDDAEQEAVARLVALGYKPQEASRMVSKIARPDASSETLIREALRAAL
>d1nkl__ 1.50.1.1.1 NK-lysin [pig (Sus scrofa)]
GYFCESCRKIIQKLEDMVGPQPNEDTVTQAASQVCDKLKILRGLCKKIMRSFLRRISWDILTGKKPQAICVDIKICKE
>d1axn__ 1.51.1.1.1 Annexin III [human (Homo sapiens)]
SASIWVGHRGTVRDYPDFSPSVDAEAIQKAIRGIGTDEKMLISILTERSNAQRQLIVKEYQAAYGKELKDDLKGDLSGHFEHLMVALVTPPAVFDAKQLKKSMKGAGTNEDALIEILTTRTSRQMKDISQAYYTVYKKSLGDDISSETSGDFRKALLTLADGRRDESLKVDEHLAKQDAQILYKAGENRWGTDEDKFTEILCLRSFPQLKLTFDEYRNISQKDIVDSIKGELSGHFEDLLLAIVNCVRNTPAFLAERLHRALKGIGTDEFTLNRIMVSRSEIDLLDIRTEFKKHYGYSLYSAIKSDTSGDYEITLLKICGGDD
>d1ala__ 1.51.1.1.2 Annexin V [chicken (Gallus gallus)]
KYTRGTVTAFSPFDARADAEALRKAMKGMGTDEETILKILTSRNNAQRQEIASAFKTLFGRDLVDDLKSELTGKFETLMVSLMRPARIFDAHALKHAIKGAGTNEKVLTEILASRTPAEVQNIKQVYMQEYEANLEDKITGETSGHFQRLLVVLLQANRDPDGRVEEALVEKDAQVLFRAGELKWGTDEETFITILGTRSVSHLRRVFDKYMTISGFQIEETIDRETSGDLEKLLLAVVKCIRSVPAYFAETLYYSMKGAGTDDDTLIRVMVSRSEIDLLDIRHEFRKNFAKSLYQMIQKDTSGDYRKALLLLCGG
>d1hvd__ 1.51.1.1.3 Annexin V [human (Homo sapiens)]
VLRGTVTDFPGFDGRADAETLRKAMKGLGTDEESILTLLTSRSNAQRQEISAAFKTLFGRDLLDDLKSELTGKFEKLIVALMKPSRLYDAYELKHALKGAGTNEKVLTEIIASRTPEELRAIKQVYEEEYGSSLEDDVVGDTSGYYQRMLVVLLQANRDPDAGIDEAQVEQDAQALFQAGELKWGTDEEKFITIFGTRSVSHLRKVFDKYMTISGFQIEETIDRETSGNLEQLLLAVVKSIRSIPAYLAETLYYAMKGAGTDDHTLIRVMVSRSEIDLFNIRKEFRKNFATSLYSMIKGDTSGDYKKALLLLC
>d2ran__ 1.51.1.1.4 Annexin V [Rat (Rattus norvegicus)]
ALRGTVTDFSGFDGRADAEVLRKAMKGLGTDEDSILNLLTARSNAQRQQIAEEFKTLFGRDLVNDMKSELTGKFEKLIVALMKPSRLYDAYELKHALKGAGTDEKVLTEIIASRTPEELRAIKQAYEEEYGSNLEDDVVGDTSGYYQRMLVVLLQANRDPDTAIDDAQVELDAQALFQAGELKWGTDEEKFITILGTRSVSHLRRVFDKYMTISGFQIEETIDRETSGNLENLLLAVVKSIRSIPAYLAETLYYAMKGAGTDDHTLIRVIVSRSEIDLFNIRKEFRKNFATSLYSMIKGDTSGDYKKALLLLCGGE
>d1ann__ 1.51.1.1.5 Annexin IV [bovine (Bos taurus)]
GGTVKAASGFNAAEDAQTLRKAMKGLGTDEDAIINVLAYRSTAQRQEIRTAYKTTIGRDLMDDLKSELSGNFEQVILGMMTPTVLYDVQELRKAMKGAGTDEGCLIEILASRTPEEIRRINQTYQLQYGRSLEDDIRSDTSFMFQRVLVSLSAGGRDESNYLDDALMRQDAQDLYEAGEKKWGTDEVKFLTVLCSRNRNHLLHVFDEYKRIAQKDIEQSIKSETSGSFEDALLAIVKCMRNKSAYFAERLYKSMKGLGTDDDTLIRVMVSRAEIDMLDIRANFKRLYGKSLYSFIKGDTSGDYRKVLLILCGGDD
>d1aeia_ 1.51.1.1.6 Annexin XII [hydra (Hydra attenuata)]
VVQGTVKPHASFNSREDAETLRKAMKGIGTDEKSITHILATRSNAQRQQIKTDYTTLFGKHLEDELKSELSGNYEAAALALLRKPDEFLAEQLHAAMKGLGTDENALIDILCTQSNAQIHAIKAAFKLLYKEDLEKEIISETSGNFQRLLVSMLQGGRKEDEPVNAAHAAEDAAAIYQAGEGQIGTDESRFNAVLATRSYPQLHQIFHEYSKISNKTILQAIENEFSGDIKNGLLAIVKSVENRFAYFAERLHHAMKGLGTSDKTLIRILVSRSEIDLANIKETFQAMYGKSLYEFIADDCSGDYKDLLLQITGH
>d1ain__ 1.51.1.1.7 Annexin I [human (Homo sapiens)]
GSAVSPYPTFNPSSDVAALHKAIMVKGVDEATIIDILTKRNNAQRQQIKAAYLQETGKPLDETLKKALTGHLEEVVLALLKTPAQFDADELRAAMKGLGTDEDTLIEILASRTNKEIRDINRVYREELKRDLAKDITSDTSGDFRNALLSLAKGDRSEDFGVNEDLADSDARALYEAGERRKGTDVNVFNTILTTRSYPQLRRVFQKYTKYSKHDMNKVLDLELKGDIEKCLTAIVKCATSKPAFFAEKLHQAMKGVGTRHKALIRIMVSRSEIDMNDIKAFYQKMYGISLCQAILDETKGDYEKILVALCGGN
>d1tada1 1.52.1.1.1 (31-151) Transducin (alpha subunit), insertion domain [bovine (Bos taurus)]
YSLEECLEFIAIIYGNTLQSILAIVRAMTTLNIQYGDSARQDDARKLMHMADTIEEGTMPKEMSDIIQRLWKDSGIQACFDRASEYQLNDSAGYYLSDLERLVTPGYVPTEQDVLRSRVKT
>d1gota1 1.52.1.1.2 (55-170) Transducin (alpha subunit), insertion domain [rat (Rattus rattus)]
ECLEFIAIIYGNTLQSILAIVRATTLNIQYGDSARQDDARKLHADTIEEGTPKESDIIQRLWKDSGIQACFDRASEYQLNDSAGYYLSDLERLVTPGYVPTEQDVLRSRVKTTGII
>d1gia_1 1.52.1.1.2 (28-148) Transducin (alpha subunit), insertion domain [rat (Rattus rattus)]
YSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDAARADDARQLFVLAGAAEEGFMTAELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKT
>d1ezm_1 1.53.1.1.1 (154-298) Elastase [Pseudomonas aeruginosa]
IYRGQSGGMNEAFSDMAGEAAEFYMRGKNDFLIGYDIKKGSGALRYMDQPSRDGRSIDNASQYYNGIDVHHSSGVYNRAFYLLANSPGWDTRKAFEVFVDANRYYWTATSNYNSGACGVIRSAQNRNYSAADVTRAFSTVGVTCP
>d8tlne1 1.53.1.1.2 (156-316) Thermolysin [Bacillus thermoproteolyticus]
IYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGDSLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTHYGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTSQEVASVKQAFDAVGVK
>d1npc_1 1.53.1.1.3 (157-317) Neutral protease [Bacillus cereus, strain dsm 3101]
IYQNESGALNEAISDIFGTLVEFYDNRNPDWEIGEDIYTPGKAGDALRSMSDPTKYGDPDHYSKRYTGSSDNGGVHTNSGIINKQAYLLANGGTHYGVTVTGIGKDKLGAIYYRANTQYFTQSTTFSQARAGAVQAAADLYGANSAEVAAVKQSFSAVGVN
>d2ts1_1 1.54.1.1.1 (226-317) Tyrosyl-tRNA synthetase, middle domain [Bacillus stearothermophilus nca 1503]
GTKFGKTESGTIWLDKEKTSPYEFYQFWINTDDRDVIRYLKYFTFLSKEEIEALEQELREAPEKRAAQKTLAEEVTKLVHGEEALRQAIRIS
>d1bmfa1 1.55.1.1.1 (357-487) The C-terminal domain of alpha and beta subunits of F1 ATP synthase [bovine (Bos taurus)]
TRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVISQHQALLGKIRTDGKISEESDAKLKEIVTNFLAGFEA
>d1bmfd1 1.55.1.1.1 (350-467) The C-terminal domain of alpha and beta subunits of F1 ATP synthase [bovine (Bos taurus)]
MDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAE
>d1abv__ 1.56.1.1.1 N-terminal domain of the delta subunit of the F1F0-ATP synthase [Escherichia coli]
SEFITVARPYAKAAFDFAVEHQSVERWQDMLAFAAEVTKNEQMAELLSGALAPETLAESFIAVCGEQLDENGQNLIRVMAENGRLNALPDVLEQFIHLRAVSEAT
>d1ak4c_ 1.57.1.1.1 HIV-1 capsid protein, N-terminal core domain [Human immunodeficiency virus type 1 (HIV-1)]
PIVQNLQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTHNPPIPVGEIYKRWIILGLNKIVRMY
>d2hmx__ 1.58.1.1.1 HIV-1 matrix protein (HIV-1 MA, HIVp17, p17, MA) [Human immunodeficiency virus type 1 (HIV-1)]
HMGARASVLSGGELDKWEKIRLRPGGKKQYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTIAVLYCVHQRIDVKDTKEALDKIEEEQNKSKKKAQQAAADTGNNSQVSQNY
>d1tam__ 1.58.1.1.1 HIV-1 matrix protein (HIV-1 MA, HIVp17, p17, MA) [Human immunodeficiency virus type 1 (HIV-1)]
MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEALDKIEEEQNKSKKKAQQAAA
>d1jvr__ 1.58.1.2.1 HTLV-II matrix protein [TTLV-II (Human t-cell leukemia virus type II)]
HMGQIHGLSPTPIPKAPRGLSTHHWLNFLQAAYRLQPGPSDFDFQQLRRFLKLALKTPIWLNPIDYSLLASLIPKGYPGRVVEIINILVKNQVSPSAPAAPVPTPICPTTTPPPPPPPSPEAHVPPPYVEPTTTQCF
>d1vin_2 1.59.1.1.2 (129-252) Cyclin A [Bovine (Bos taurus)]
PTINQFLTQYFLHQQPANCKVESLAMFLGELSLIDADPYLKYLPSVIAAAAFHLALYTVTGQSWPESLVQKTGYTLETLKPCLLDLHQTYLRAPQHAQQSIREKYKNSKYHGVSLLNPPETLNL
>d1vin_1 1.59.1.1.2 (1-128) Cyclin A [Bovine (Bos taurus)]
DIHTYLREMEVKCKPKVGYMKKQPDITNSMRAILVDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQLVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRMEHLVLKVLAFDLAA
>d1jkw_2 1.59.1.1.3 (152-277) Cyclin h (mcs2) [human (Homo sapiens)]
NPYRPFEGFLIDLKTRYPILENPEILRKTADDFLNRIALTDAYLLYTPSQIALTAILSSASRAGITMESYLSESLMLKENRTCLSQLLDIMKSMRNLVKKYEPPRSEEVAVLKQKLDRCHSAELAL
>d1jkw_1 1.59.1.1.3 (1-151) Cyclin h (mcs2) [human (Homo sapiens)]
WTFSSEEQLARLRADANRKFRCKAVANGKVLPNDPVFLEPHEEMTLCKYYEKRLLEFCSVFKPAMPRSVVGTACMYFKRFYLNNSVMEYHPRIIMLTCAFLACKVDEFNVSSPQFVGNLRESPLGQEKALEQILEYELLLIQQLNFHLIVH
>d1vola1 1.59.1.2.1 (1-95) Transcription factor IIB (TFIIB), the core domain [Human (Homo sapiens)]
AMMNAFKEITTMADRINLPRNKVDRTNNLFRQAYEQKSLKGRANDAIASACLYIACRQEGVPRTFKEICAVSRISKKEIGRCFKLILKALETSVD
>d1vola2 1.59.1.2.1 (96-204) Transcription factor IIB (TFIIB), the core domain [Human (Homo sapiens)]
LITTGDFMSRFCSNLCLPKQVQMAATHIARKAVELDLVPGRSPISVAAAAIYMASQASAEKRTQKEIGDIAGVADVTIRQSYRLIYPRAPDLFPTDFKFDTPVDKLPQL
>d1aisb1 1.59.1.2.2 (1-98) Transcription factor IIB (TFIIB), the core domain [Pyrococcus woesei]
NLAFALSELDRITAQLKLPRHVEEEAARLYREAVRKGLIRGRSIESVMAACVYAACRLLKVPRTLDEIADIARVDKKEIGRSYRFIARNLNLTPKKLF
>d1aisb2 1.59.1.2.2 (99-193) Transcription factor IIB (TFIIB), the core domain [Pyrococcus woesei]
VKPTDYVNKFADELGLSEKVRRRAIEILDEAYKRGLTSGKSPAGLVAAALYIASLLEGEKRTQREVAEVARVTEVTVRNRYKELVEKLKIKVPIA
>d1tns__ 1.6.1.1.1 Mu transposase, DNA-binding domain [Mu bacteriophage]
MELWVSPKELANLPGLPKTSAGVIYVAKKQGWQNRTRAGVKGGKAIEYNANSLPVEAKAALLLRQGEIETSLGYFE
>d1cuk_2 1.60.1.1.1 (65-142) DNA helicase RuvA subunit, the middle domain [Escherichia coli]
NKQERTLFKELIKTNGVGPKLALAILSGMSAQQFVNAVEREEVGALVKLPGIGKKTAERLIVEMKDRFKGLHGDLFTP
>d1dpra2 1.61.1.1.1 (63-134) Diphtheria toxin repressor (DtxR) dimerization domain [Corynebacterium diphtheriae]
TPTGRTLATAVMRKHRLAERLLTDIIGLDINKVHDEACRWEHVMSDEVERRLVKVLKDVSRSPFGNPIPGLD
>d1ngr__ 1.62.1.1.1 p75 low affinity neurotrophin receptor [rat (Rattus norvegicus)]
GNLYSSLPLTKREEVEKLLNGDTWRHLAGELGYQPEHIDSFTHEACPVRALLASWGAQDSATLDALLAALRRIQRADIVESLCSE
>d1crka1 1.63.1.1.1 (1-98) Creatine kinase, N-terminal domain [chicken (Gallus gallus) mitochondria]
TVHEKRKLFPPSADYPDLRKHNNCMAECLTPAIYAKLRDKLTPNGYSLDQCIQTGVDNPGHPFIKTVGMVAGDEESYEVFAEIFDPVIKARHNGYDPR
>d1agre_ 1.64.1.1.1 Regulator of G-protein signalling 4, RGS4 [rat (Rattus norvegicus)]
VSQEEVKKWAESLENLINHECGLAAFKAFLKSEYSEENIDFWISCEEYKKIKSPSKLSPKAKKIYNEFISVQATKEVNLDSCTREETSRNMLEPTITCFDEAQKKIFNLMEKDSYRRFLKSRFYLDLT
>d1qpaa_ 1.65.1.1.1 Lignin peroxidase [white rot basidiomycete (Phanerochaete chrysosporium)]
VACPDGVHTASNAACCAWFPVLDDIQQNLFHGGQCGAEAHEALRMVFHDSIAISPKLQSQGKFGGGGADGSIITFSSIETTYHPNIGLDEVVAIQKPFIAKHGVTPGDFIAFAGAVGVSNCPGAPQMQFFLGRPEATQAAPDGLVPEPFHTIDQVLARMLDAGGFDEIETVLLSAHSIAAANDVDPTISGLPFDSTPGQFDSQFFVETQLRGTAFPGKTGIQGTVMSPLKGEMRLQTDHLFARDSRTACEWQSFVNNQTKLQEDFQFIFTALSTLGHDMNAMIDCSEVIPAPKPVNFGPSFFPAGKTHADIEQACASTPFPTLITAPGPSASVARIPPPPSPN
>d1lgaa_ 1.65.1.1.1 Lignin peroxidase [white rot basidiomycete (Phanerochaete chrysosporium)]
ATCANGKTVGDASCCAWFDVLDDIQANMFHGGQCGAEAHESIRLVFHDSIAISPAMEAKGKFGGGGADGSIMIFDTIETAFHPNIGLDEVVAMQKPFVQKHGVTPGDFIAFAGAVALSNCPGAPQMNFFTGRKPATQPAPDGLVPEPFHTVDQIIARVNDAGEFDELELVWMLSAHSVAAVNDVDPTVQGLPFDSTPGIFDSQFFVETQFRGTLFPGSGGNQGEVESGMAGEIRIQTDHTLARDSRTACEWQSFVGNQSKLVDDFQFIFLALTQLGQDPNAMTDCSDVIPLSKPIPGNGPFSFFPPGKSHSDIEQACAETPFPSLVTLPGPATSVARIPPHKA
>d1aru__ 1.65.1.1.2 Peroxidase [Arthromyces ramous]
SVTCPGGQSTSNSQCCVWFDVLDDLQTNFYQGSKCESPVRKILRIVFHDAIGFSPALTAAGQFGGGGADGSIIAHSNIELAFPANGGLTDTIEALRAVGINHGVSFGDLIQFATAVGMSNCPGSPRLEFLTGRSNSSQPSPPSLIPGPGNTVTAILDRMGDAGFSPDEVVDLLAAHSLASQEGLNSAIFRSPLDSTPQVFDTQFYIETLLKGTTQPGPSLGFAEELSPFPGEFRMRSDALLARDSRTACRWQSMTSSNEVMGQRYRAAMAKMSVLGFDRNALTDCSDVIPSAVSNNAAPVIPGGLTVDDIEVSCPSEPFPEIATASGPLPSLAPAP
>d2cyp__ 1.65.1.1.3 Cytochrome c peroxidase [baker's yeast (Saccharomyces cerevisiae)]
TPLVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHTSGTWDKHDNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTPEDTTPDNGRLPDADKDADYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAANNVFTNEFYLNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQDPKYLSIVKEYANDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL
>d1mnp__ 1.65.1.1.4 Manganese peroxidase [Basidomycetos fungus (Phanerochaete chrysosporium)]
AVCPDGTRVSHAACCAFIPLAQDLQETIFQNECGEDAHEVIRLTFHDAIAISRSQGPKAGGGADGSMLLFPTVEPNFSANNGIDDSVNNLIPFMQKHNTISAADLVQFAGAVALSNCPGAPRLEFLAGRPNKTIAAVDGLIPEPQDSVTKILQRFEDAGGFTPFEVVSLLASHSVARADKVDQTIDAAPFDSTPFTFDTQVFLEVLLKGVGFPGSANNTGEVASPLPLGSGSDTGEMRLQSDFALAHDPRTACIWQGFVNEQAFMAASFRAAMSKLAVLGHNRNSLIDCSDVVPVPKPATGQPAMFPASTGPQDLELSCPSERFPTLTTQPGASQSLIAHCPDGSMSCPGVQFNGPA
>d1apxa_ 1.65.1.1.5 Ascorbate peroxidase [Pea (Pisum sativum)]
GKSYPTVSPDYQKAIEKAKRKLRGFIAEKKCAPLILRLAWHSAGTFDSKTKTGGPFGTIKHQAELAHGANNGLDIAVRLLEPIKEQFPIVSYADFYQLAGVVAVEITGGPEVPFHPGREDKPEPPPEGRLPDATKGSDHLRDVFGKAMGLSDQDIVALSGGHTIGAAHKERSGFEGPWTSNPLIFDNSYFTELLTGEKDGLLQLPSDKALLTDSVFRPLVEKYAADEDVFFADYAEAHLKLSELGFAEA
>d1scha_ 1.65.1.1.6 Peroxidase [Peanut (Arachis hypogaea)]
LSSNFYATKCPNALSTIKSAVNSAVAKEARMGASLLRLHFHDCFVQGCDASVLLDDTSNFTGEKTAGPNANSIRGFEVIDTIKSQVESLCPGVVSCADILAVAARDSVVALGGASWNVLLGRRDSTTASLSSANSDLPAPFFNLSGLISAFSNKGFTTKELVTLSGAHTIGQAQCTAFRTRIYNESNIDPTYAKSLQANCPSVGGDTNLSPFDVTTPNKFDNAYYINLRNKKGLLHSDQQLFNGVSTDSQVTAYSNNAATFNTDFGNAMIKMGNLSPLTGTSGQIRTNCRKTN
>d1mhl.1 1.65.1.2.1 (a,c) Myeloperoxidase [human (Homo sapiens)]
CPEQDKYRTITGMCNNRRSPTLGASNRAFVRWLPAEYEDGFSLPYGWTPGVKRNGFPVALARAVSNEIVRFPTDQLTPDQERSLMFMQWGQLLDHDLDFTPEPALKIPPNDPRIKNQADCIPFFRSCPACPGSNITIRNQINALTSFVDASMVYGSEEPLARNLRNMSNQLGLLAVNQRFQDNGRALLPFDNLHDDPCLLTNRSARIPCFLAGDTRSSEMPELTSMHTLLLREHNRLATELKSLNPRWDGERLYQEARKIVGAMVQIITYRDYLPLVLGPTAMRKYLPTYRSYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNRYQPMEPNPRVPLSRVFFASWRVVLEGGIDPILRGLMATPAKLNRQNQIAVDEIRERLFEQVMRIGLDLPALNMQRSRDHGLPGYNAWRRFCGLPQPETVGQLGTVLRNLKLARKLMEQYGTPNNIDIWMGGVSEPLKRKGRVGPLLACIIGTQFRKLRDGDRFWWENEGVFSMQQRQALAQISLPRIICDNTGITTVSKNNIFMSNSYPRDFVNCSTLPALNLASWREACPEQDKYRTITGMCNNRRSPTLGASNRAFVRWLPAEYEDGFSLPYGWTPGVKRNGFPVALARAVSNEIVRFPTDQLTPDQERSLMFMQWGQLLDHDLDFTPEPALKIPPNDPRIKNQADCIPFFRSCPACPGSNITIRNQINALTSFVDASMVYGSEEPLARNLRNMSNQLGLLAVNQRFQDNGRALLPFDNLHDDPCLLTNRSARIPCFLAGDTRSSEMPELTSMHTLLLREHNRLATELKSLNPRWDGERLYQEARKIVGAMVQIITYRDYLPLVLGPTAMRKYLPTYRSYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNRYQPMEPNPRVPLSRVFFASWRVVLEGGIDPILRGLMATPAKLNRQNQIAVDEIRERLFEQVMRIGLDLPALNMQRSRDHGLPGYNAWRRFCGLPQPETVGQLGTVLRNLKLARKLMEQYGTPNNIDIWMGGVSEPLKRKGRVGPLLACIIGTQFRKLRDGDRFWWENEGVFSMQQRQALAQISLPRIICDNTGITTVSKNNIFMSNSYPRDFVNCSTLPALNLASWREA
>d1prha1 1.65.1.2.3 (42-554) Prostaglandin H2 synthase-1 [Sheep (Ovis aries)]
IWTWLRTTLRPSPSFIHFLLTHGRWLWDFVNATFIRDTLMRLVLTVRSNLIPSPPTYNIAHDYISWESFSNVSYYTRILPSVPRDCPTPMGTKGKKQLPDAEFLSRRFLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTSGKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLFKDGKLKYQMLNGEVYPPSVEEAPVLMHYPRGIPPQSQMAVGQEVFGLLPGLMLYATIWLREHQRVCDLLKAEHPTWGDEQLFQTAKLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGAQFQYRNRIAMEFNQLYHWHPLMPDSFRVGPQDYSYEQFLFNTSMLVDYGVEALVDAFSRQPAGRIGGGRNIDHHILHVAVDVIKESRVLRLQPFNEYRKRFGMKPYTSFQELTGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESMIEMGAPFSLKGLLGNPICSPEYWKASTFGGEVGFNLVKTATLKKLVCLNTKTCPYVSFHVPDPR
>d2abk__ 1.66.1.1.1 Endonuclease III [Escherichia coli]
MNKAKRLEILTRLRENNPHPTTELNFSSPFELLIAVLLSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTIGLYNSKAENIIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAPGKNVEQVEEKLLKVVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLCEYKEKVDI
>d1gln_1 1.67.1.1.1 (306-468) Anticodon-binding (C-terminal) domain of glutamyl-tRNA synthetase (GluRS) [Thermus thermophilus]
DLEKLRWMNGKYIREVLSLEEVAERVKPFLREAGLSWESEAYLRRAVELMRPRFDTLKEFPEKARYLFTEDYPVSEKAQRKLEEGLPLLKELYPRLRAQEEWTEAALEALLRGFAAEKGVKLGQVAQPLRAALTGSLETPGLFEILALLGKERALRRLERALA
>d1rlr_1 1.68.1.1.1 (1-212) R1 subunit of ribonucleotide reductase, N-terminal domain [Escherichia coli]
RDGSTERINLDKIHRVLDWAAEGLHNVSISQVELRSHIQFYDGIKTSDIHETIIKAAADLISRDAPDYQYLAARLAIFHLRKKAYGQFEPPALYDHVVKMVEMGKYDNHLLEDYTEEEFKQMDTFIDHDRDMTFSYAAVKQLEGKYLVQNRVTGEIYESAQFLYILVAACLFSNYPRETRLQYVKRFYDAVSTFKISLPTPIMSGVRTPTRQ
>d1dnpa1 1.69.1.1.1 (201-469) FAD-binding (C-terminal) domain of DNA photolyase [Escherichia coli]
PVEEKAAIAQLRQFCQNGAGEYEQQRDFPAVEGTSRLSASLATGGLSPRQCLHRLLAEQPQALDGGAGSVWLNELIWREFYRHLITYHPSLCKHRPFIAWTDRVQWQSNPAHLQAWQEGKTGYPIVDAAMRQLNSTGWMHNRLRMITASFLVKDLLIDWREGERYFMSQLIDGDLAANNGGWQWAASTGTDAAPYFRIFNPTTQGEKFDHEGEFIRQWLPELRDVPGKVVHEPWKWAQKAGVTLDYPQPIVEHKEARVQTLAAYEAARK
>d1aj3__ 1.7.1.1.1 Spectrin (one repeat unit) [drosophila spectrin]
HQFFRDMDDEESWIKEKKLLVSSEDYGRDLTGVQNLRKKHKRLEAELAAHEPAIQGVLDTGKKLSDDNTIGKEEIQQRLAQFVDHWKELKQLAAARGQ
>d2spca_ 1.7.1.1.1 Spectrin (one repeat unit) [drosophila spectrin]
QNLDLQLYMRDCELAESWMSAREAFLNADDDANAGGNVEALIKKHEDFDKAINGHEQKIAALQTVADQLIAQNHYASNLVDEKRKQVLERWRHLKEGLIEKRSRLGD
>d1lla_1 1.70.1.1.1 (1-359) Hemocyanin, N-terminal and middle domains [Limulus polyphemus]
LHDKQIRICHLFEQLSSATHSDRLKNVGKLQPGAIFSCFHPDHLEEARHLYEVFWEAGDFNDFIEIAKEARTFVNEGLFAFAAEVAVLHRDDCKGLYVPPVQEIFPDKFIPSAAINEAFKKESPILVDVTGNILDPEYRLAYYREDVGINAHHWHWHLVYPSTWNPKYFGKKKDRKGELFYYMHQQMCARYDCERLSNGMHRMLPFNNFDEPLAGYAPHLTHVASGKYYSPRPDGLKLRDLGDIEISEMVRMRERILDSIHLGYVISEDGSHKTLDELHGTDILGALVESSYESVNHEYYGNLHNWGHVTMARIHDPDGRFHEEPGVMSDTSTSLRDPIFYNWHRFIDNIFHEYKNTLK
>d1hc2_1 1.70.1.1.2 (1-390) Hemocyanin, N-terminal and middle domains [spiny lobster (Panulirus interruptus)]
TGNAQKQQDINHLLDKIYEPTKYPDLKDIAENFNPLGDTSIYNDHGAAVETLMKELNDHRLLEQRHWYSLFNTRQRKEALMLFAVLNQCKEWYCFRSNAAYFRERMNEGEFVYALYVSVIHSKLGDGIVLPPLYQITPHMFTNSEVIDKAYSAKMTQKPGTFNVSFKNREQRVAYFGEDIGMNIHHVTWHMDFPFWWEDSYGYHLDRKGELFFWVHHQLTARFDFERLSNWLDPVDELHWDRIIREGFAPLTSYKYGGEFPVRPDNIHFEDVDGVAHVHDLEITESRIHEAIDHGYITDSDGHTIDIRQPKGIELLGDIIESSKYSSNVQYYGSLHNTAHVMLGRQGDPHGKFNLPPGVMEHFETATRDPSFFRLHKYMDNIFKKHTDSF
>d2pgd_1 1.71.1.1.1 (177-473) 6-phosphogluconate dehydrogenase (6PGD) [sheep (Ovis orientalis aries)]
GAGHFVKMVHNGIEYGDMQLICEAYHLMKDVLGLGHKEMAKAFEEWNKTELDSFLIEITASILKFQDADGKHLLPKIRDSAGQKGTGKWTAISALEYGVPVTLIGEAVFARCLSSLKDERIQASKKLKGPQNIPFEGDKKSFLEDIRKALYASKIISYAQGFMLLRQAATEFGWTLNYGGIALMWRGGCIIRSVFLGKIKDAFDRNPGLQNLLLDDFFKSAVENCQDSWRRAISTGVQAGIPMPCFTTALSFYDGYRHAMLPANLIQAQRDYFGAHTYELLAKPGQFIHTNWTGHGG
>d1yvei1 1.71.1.2.1 (226-513) Acetohydroxy acid isomeroreductase, ketoacid reductoisomerase (KARI) [spinach (Spinacia oleracea)]
LEQEYKSDIFGERGILLGAVHGIVECLFRRYTESGMSEDLAYKNTVECITGVISKTISTKGMLALYNSLSEEGKKDFQAAYSASYYPSMDILYECYEDVASGSEIRSVVLAGRRFYEKEGLPAFPMGKIDQTRMWKVGEKVRSVRPAGDLGPLYPFTAGVYVALMMAQIEILRKKGHSYSEIINESVIEAVDSLNPFMHARGVSFMVDNCSTTARLGSRKWAPRFDYILSQQALVAVDNGAPINQDLISNFLSDPVHEAIGVCAQLRPSVDISVTADADFVRPELRQA
>d1utg__ 1.72.1.1.1 Uteroglobin [Rabbit (Oryctolagus cuniculus)]
GICPRFAHVIENLLLGTPSSYETSLKEFEPDDTMKDAGMQMKKVLDSLPQTTRENIMKLTEKIVKSPLCM
>d1ccd__ 1.72.1.1.2 Clara cell 17kDa protein [rat (Rattus rattus)]
SSDICPGFLQVLEALLLGSESNYEAALKPFNPASDLQNAGTQLKRLVDTLPQETRINIVKLTEKILTSPLCEQDLRV
>d1glm__ 1.73.1.1.1 Glucoamylase [Aspergillus awamori, variant x100]
ATLDSWLSNEATVARTAILNNIGADGAWVSGADSGIVVASPSTDNPDYFYTWTRDSGLVIKTLVDLFRNGDTDLLSTIEHYISSQAIIQGVSNPSGDLSSGGLGEPKFNVDETAYTGSWGRPQRDGPALRATAMIGFGQWLLDNGYTSAATEIVWPLVRNDLSYVAQYWNQTGYDLWEEVNGSSFFTIAVQHRALVEGSAFATAVGSSCSWCDSQAPQILCYLQSFWTGSYILANFDSSRSGKDTNTLLGSIHTFDPEAGCDDSTFQPCSPRALANHKEVVDSFRSIYTLNDGLSDSEAVAVGRYPEDSYYNGNPWFLCTLAAAEQLYDALYQWDKQGSLEITDVSLDFFKALYSGAATGTYSSSSSTYSSIVSAVKTFADGFVSIVETHAASNGSLSEQFDKSDGDELSARDLTWSYAALLTANNRRNSVVPPSWGETSASSVPGTCAATSASGTYSSVTVTSWPSIVA
>d1cem__ 1.73.1.2.1 CelA cellulase [Clostridium thermocellum]
AGVPFNTKYPYGPTSIADNQSEVTAMLKAEWEDWKSKRITSNGAGGYKRVQRDASTNYDTVSEGMGYGLLLAVCFNEQALFDDLYRYVKSHFNGNGLMHWHIDANNNVTSHDGGDGAATDADEDIALALIFADKQWGSSGAINYGQEARTLINNLYNHCVEHGSYVLKPGDRWGGSSVTNPSYFAPAWYKVYAQYTGDTRWNQVADKCYQIVEEVKKYNNGTGLVPDWCTASGTPASGQSYDYKYDATRYGWRTAVDYSWFGDQRAKANCDMLTKFFARDGAKGIVDGYTIQGSKISNNHNASFIGPVAAASMTGYDLNFAKELYRETVAVKDSEYYGYYGNSLRLLTLLYITGNFPNPLSDL
>d1tf4a1 1.73.1.2.2 (1-460) Endo/exocellulase:cellobiose E-4, N-terminal domain [Thermomonospora fusca]
EPAFNYAEALQKSMFFYEAQRSGKLPENNRVSWRGDSGLNDGADVGLDLTGGWYDAGDHVKFGFPMAFTATMLAWGAIESPEGYIRSGQMPYLKDNLRWVNDYFIKAHPSPNVLYVQVGDGDADHKWWGPAEVMPMERPSFKVDPSCPGSDVAAETAAAMAASSIVFADDDPAYAATLVQHAKQLYTFADTYRGVYSDCVPAGAFYNSWSGYQDELVWGAYWLYKATGDDSYLAKAEYEYDFLSTEQQTDLRSYRWTIAWDDKSYGTYVLLAKETGKQKYIDDANRWLDYWTVGVNGQRVPYSPGGMAVLDTWGALRYAANTAFVALVYAKVIDDPVRKQRYHDFAVRQINYALGDNPRNSSYVVGFGNNPPRNPHHRTAHGSWTDSIASPAENRHVLYGALVGGPGSPNDAYTDDRQDYVANEVATDYNAGFSSALAMLVEEYGGTPLADFPPTEEPDG
>d1clc_1 1.73.1.2.3 (101-541) CelD cellulase [Clostridium thermocellum]
AMNVYEDAFKTAMLGMYLLRCGTSVSATYNGIHYSHGPCHTNDAYLDYINGQHTKKDSTKGWHDAGDYNKYVVNAGITVGSMFLAWEHFKDQLEPVALEIPEKNNSIPDFLDELKYEIDWILTMQYPDGSGRVAHKVSTRNFGGFIMPENEHDERFFVPWSSAATADFVAMTAMAARIFRPYDPQYAEKCINAAKVSYEFLKNNPANVFANQSGFSTGEYATVSDADDRLWAAAEMWETLGDEEYLRDFENRAAQFSKKIEADFDWDNVANLGMFTYLLSERPGKNPALVQSIKDSLLSTADSIVRTSQNHGYGRTLGTTYYWGCNGTVVRQTMILQVANKISPNNDYVNAALDAISHVFGRNYYNRSYVTGLGINPPMNPHDRRSGADGIWEPWPGYLVGGGWPGPKDWVDIQDSYQTNEIAINWNAALIYALAGFVNYN
>d5eas_1 1.73.2.1.1 (1-197) 5-Epi-aristolochene synthase, N-terminal domain [Tobacco (Nicotiana tabacum)]
LWGDQFLSFSIDNQVAEKYAQEIEALKEQTRSMLLATGRKLADTLNLIDIIERLGISYHFEKEIDEILDQIYNQNSNCNDLCTSALQFRLLRQHGFNISPEIFSKFQDENGKFKESLASDVLGLLNLYEASHVRTHADDILEDALAFSTIHLESAAPHLKSPLREQVTHALEQCLHKGVPRVETRFFISSIYDKEQS
>d4csc__ 1.74.1.1.1 Citrate synthase [chicken (Gallus gallus)]
ASSTNLKDVLAALIPKEQARIKTFRQQHGGTALGQITVDMSYGGMRGMKGLVYETSVLDPDEGIRFRGFSIPECQKLLPKGGGGEPLPEGLFWLLVTGQIPTGAQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGILRTKYWEMVYESAMDLIAKLPCVAAKIYRNLYRAGSSIGAIDSKLDWSHNFTNMLGYTDAQFTELMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLGWLAQLQKAAGADASLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPGDPMFKLVAQLYKIVPNVLLEQGAAANPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTDGLIAL
>d1csh__ 1.74.1.1.1 Citrate synthase [chicken (Gallus gallus)]
STNLKDVLASLIPKEQARIKTFRQQHGNTAVGQITVDMSYGGMRGMKGLIYETSVLDPDEGIRFRGFSIPECQKLLPKAGGGEEPLPEGLFWLLVTGQIPTPEQVSWVSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGINRTKYWEFVYEDAMDLIAKLPCVAAKIYRNLYRAGSSIGAIDSKLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLLWLSQLQKDLGADASDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPSDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTAGLEKLSAGG
>d2cts__ 1.74.1.1.2 Citrate synthase [pig (Sus scrofa)]
ASSTNLKDILADLIPKEQARIKTFRQQHGNTAVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAKGGEEPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGIHRTKYWELIYEDCMDLIAKLPCVAAKIYRNLYREGSSIGAIDSKLDWSHNFTNMLGYTDAQFTELMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPHDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTDGLIKLVDSK
>d1phb__ 1.75.1.1.1 Cytochrome P450 [Pseudomonas putida]
NLAPLPPHVPEHLVFDFDMYNPSNLSAGVQEAWAVLQESNVPDLVWTRCNGGHWIATRGQLIREAYEDYRHFSSECPFIPREAGEAYDFIPTSMDPPEQRQFRALANQVVGMPVVDKLENRIQELACSLIESLRPQGQCNFTEDYAEPFPIRIFMLLAGLPEEDIPHLKYLTDQMTRPDGSMTFAEAKEALYDYLIPIIEQRRQKPGTDAISIVANGQVNGRPITSDEAKRMCGLLLVGGLDTVVNFLSFSMEFLAKSPEHRQELIERPERIPAACEELLRRFSLVADGRILTSDYEFHGVQLKKGDQILLPQMLSGLDERENACPMHVDFSRQKVSHTTFGHGSHLCLGQHLARREIIVTLKEWLTRIPDFSIAPGAQIQHKSGIVSGVQALPLVWDPATTKAV
>d2bmha_ 1.75.1.1.2 Cytochrome P450 [Bacillus megaterium]
TIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLSSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDDENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL
>d1rom__ 1.75.1.1.3 Cytochrome P450-NOR, nitric reductase [fungus (Fusarium oxysporum)]
APSFPFSRASGPEPPAEFAKLRATNPVSQVKLFDGSLAWLVTKHKDVCFVATSEKLSKVRTRQGFPELSASGKQAAKAKPTFVDMDPPEHMHQRSMVEPTFTPEAVKNLQPYIQRTVDDLLEQMKQKGCANGPVDLVKEFALPVPSYIIYTLLGVPFNDLEYLTQQNAIRTNGSSTAREASAANQELLDYLAILVEQRLVEPKDDIISKLCTEQVKPGNIDKSDAVQIAFLLLVAGNATMVNMIALGVATLAQHPDQLAQLKANPSLAPQFVEELCRYHTASALAIKRTAKEDVMIGDKLVRANEGIIASNQSANRDEEVFENPDEFNMNRKWPPQDPLGFGFGDHRCIAEHLAKAELTTVFSTLYQKFPDLKVAVPLGKINYTPLNRDVGIVDLPVIF
>d1oxa__ 1.75.1.1.4 Cytochrome P450-ERYF [Saccarapolyspora erythraea]
ATVPDLESDSFHVDWYSTYAELRETAPVTPVRFLGQDAWLVTGYDEAKAALSDLRLSSDPKKKYPGVEVEFPAYLGFPEDVRNYFATNMGTSDPPTHTRLRKLVSQEFTVRRVEAMRPRVEQITAELLDEVGDSGVVDIVDRFAHPLPIKVICELLGVDEAARGAFGRWSSEILVMDPERAEQRGQAAREVVNFILDLVERRRTEPGDDLLSALISVQDDDDGRLSADELTSIALVLLLAGFEASVSLIGIGTYLLLTHPDQLALVRADPSALPNAVEEILRYIAPPETTTRFAAEEVEIGGVAIPQYSTVLVANGAANRDPSQFPDPHRFDVTRDTRGHLSFGQGIHFCMGRPLAKLEGEVALRALFGRFPALSLGIDADDVVWRRSLLLRGIDHLPVRLDG
>d1cpt__ 1.75.1.1.5 Cytochrome P450-TERP [Pseudomonas sp.]
MDARATIPEHIARTVILPQGYADDEVIYPAFKWLRDEQPLAMAHIEGYDPMWIATKHADVMQIGKQPGLFSNAEGSEILYDQNNEAFMRSISGGCPHVIDSLTSMDPPTHTAYRGLTLNWFQPASIRKLEENIRRIAQASVQRLLDFDGECDFMTDCALYYPLHVVMTALGVPEDDEPLMLKLTQDFFGVEAARRFHETIATFYDYFNGFTVDRRSCPKDDVMSLLANSKLDGNYIDDKYINAYYVAIATAGHDTTSSSSGGAIIGLSRNPEQLALAKSDPALIPRLVDEAVRWTAPVKSFMRTALADTEVRGQNIKRGDRIMLSYPSANRDEEVFSNPDEFDITRFPNRHLGFGWGAHMCLGQHLAKLEMKIFFEELLPKLKSVELSGPPRLVATNFVGGPKNVPIRFTKA
>d1fipa_ 1.76.1.1.1 FIS protein [Escherichia coli]
PLRDSVKQALKNYFAQLNGQDVNDLYELVLAEVEQALLDMVMQYTRGNQTRAALMMGINRGTLRKKLKKYGMN
>d1prcc_ 1.77.1.1.1 Photosynthetic reaction centre (cytochrome subunit) [Rhodopseudomonas viridis]
CFEPPPATTTQTGFRGLSMGEVLHPATVKAKKERDAQYPPALAAVKAEGPPVSQVYKNVKVLGNLTEAEFLRTMTAITEWVSPQEGCTYCHDENNLASEAKYPYVVARRMLEMTRAINTNWTQHVAQTGVTCYTCHRGTPLPPYVRYLEPTLPLNNRETPTHVERVETRSGYVVRLAKYTAYSALNYDPFTMFLANDKRQVRVVPQTALPLVGVSRGKERRPLSDAYATFALMMSISDSLGTNCTFCHNAQTFESWGKKSTPQRAIAWWGIRMVRDLNMNYLAPLNASLPASRLGRQGEAPQADCRTCHQGVTKPLFGASRLKDYPELGPIK
>d2wrpr_ 1.78.1.1.1 Trp repressor [Escherichia coli]
SPYSAAMAEQRHQEWLRFVDLLKNAYQNDLHLPLLNLMLTPDEREALGTRVRIVEELLRGEMSQRELKNELGAGIATITRGSNSLKAAPVELRQWLEEVLLKSD
>d1aora1 1.79.1.1.1 (211-605) Aldehyde ferredoxin oxidoreductase, C-terminal domains [Pyrococcus furiosis]
IADKQKFMLVVREKVNKLRNDPVAGGGLPKYGTAVLVNIINENGLYPVKNFQTGVYPYAYEQSGEAMAAKYLVRNKPCYACPIGCGRVNRLPTVGETEGPEYESVWALGANLGINDLASIIEANHMCDELGLDTISTGGTLATAMELYEKGHIKDEELGDAPPFRWGNTEVLHYYIEKIAKREGFGDKLAEGSYRLAESYGHPELSMTVKKLELPAYDPRGAEGHGLGYATNNRGGCHIKNYMISPEILGYPYKMDPHDVSDDKIKMLILFQDLTALIDSAGLCLFTTFGLGADDYRDLLNAALGWDFTTEDYLKIGERIWNAERLFNLKAGLDPARDDTLPKRFLEEPMPEGPNKGHTVRLKEMLPRYYKLRGWTEDGKIPKEKLEELGIAEFY
>d1edi__ 1.8.1.1.1 Immunoglobulin-binding protein A modules [Staphylococcus aureus]
AQHDEAQQNAFYQVLNMPNLNADQRNGFIQSLKDDPSQSANVLGEAQKLNDSQAPK
>d1fc2c_ 1.8.1.1.1 Immunoglobulin-binding protein A modules [Staphylococcus aureus]
FNKEQQNAFYEILHLPNLNEEQRNGFIQSLKDDPSQSANLLAE
>d1spzz_ 1.8.1.1.1 Immunoglobulin-binding protein A modules [Staphylococcus aureus]
VDNKFNKEQQNAFYEILHLPNLNEEQRNAFIQSLKDDPSQSANLLAEAKKLNDAQAPK
>d1gab__ 1.8.1.2.1 An albumin-binding domain [Peptostreptococcus magnus]
TIDQWLLKNAKEDAIAELKKAGITSDFYFNAINKAKTVEEVNALKNEILKAHA
>d1vnc__ 1.80.1.1.1 Vanadium-containing chloroperoxidase [Curvularia inaequalis]
SVTPIPLPKIDEPEEYNTNYILFWNHVGLELNRVTHTVGGPLTGPPLSARALGMLHLAIHDAYFSICPPTDFTTFLSPDTENAAYRLPSPNGANDARQAVAGAALKMLSSLYMKPVEQPNPNPGANISDNAYAQLGLVLDRSVLEAPGGVDRESASFMFGEDVADVFFALLNDPRGASQEGYHPTPGRYKFDDEPTHPVVLIPVDPNNPNGPKMPFRQYHAPFYGKTTKRFATQSEHFLADPPGLRSNADETAEYDDAVRVAIAMGGAQALNSTKRSPWQTAQGLYWAYDGSNLIGTPPRFYNQIVRRIAVTYKKEEDLANSEVNNADFARLFALVDVACTDAGIFSWKEKWEFEFWRPLSGVRDDGRPDHGDPFWLTLGAPATNTNDIPFKPPFPAYPSGHATFGGAVFQMVRRYYNGRVGTWKDDEPDNIAIDMMISEELNGVNRDLRQPYDPTAPIEDQPGIVRTRIVRHFDSAWELMFENAISRIFLGVHWRFDAAAARDILIPTTTKDVYAVDNNGATVFQNVEDIRYTTRGTREDEEGLFPIGGVPLGIEIADEIFNNGLKPTPPEIQPM
>d1sig__ 1.81.1.1.1 A sigma70 subunit fragment from RNA polymerase [Escherichia coli]
MEGEIDIAKRIEDGINQVQCSVAEYPEAITYLLEQYNRVEAEEARLSDLITGFVDDLAPTATHVGSELSQEDLDIDPELAREKFAELRAQYVVTRDTIKAHATAQEEILKLSEVFKQFRLVPKQFDYLVNSMRVMMDRVRTQERLIMKLCVEQCKMPKKNFITLFTGNETSDTWFNAAIAMNKPWSEKLHDVSEEVHRALQKLQQIEEETGLTIEQVKDINRRMSIGEAKARRAKKEMVEANLRLVISIAKKYTNRGLQFLDLIQEGNIGLMKAVDKFEYRRGYKFSTYATWWIRQAITRSIADQ
>d1bvp11 1.82.1.1.1 (1-120,255-349) Bluetongue virus coat protein vp7 (BTV-10 vp7), alpha-helical domain [Bluetongue virus]
MDTIAARALTVMRACATLQEARIVLEANVMEILGIAINRYNGLTLRGVTMRPTSLAQRNEMFFMCLDMMLSAAGINVGPISPDYTQHMATIGVLATPEIPFTTEAANEIARVTGETSTW
>d1rgp__ 1.83.1.1.1 p50 RhoGAP domain [human (Homo sapiens)]
PRPPLPNQQFGVSLQHLQEKNPEQEPIPIVLRETVAYLQAHALTTEGIFRRSANTQVVREVQQKYNMGLPVDFDQYNELHLPAVILKTFLRELPEPLLTFDLYPHVVGFLNIDESQRVPATLQVLQTLPEENYQVLRFLTAFLVQISAHSDQNKMTNTNLAVVFGPNLLWINPINTFTKFLLDHQGELF
>d1pbwa_ 1.83.1.1.2 p85 alpha subunit RhoGAP domain [human (Homo sapiens)]
LPDLAEQFAPPDIAPPLLIKLVEAIEKKGLECSTLYRTQSSSNLAELRQLLDCDTPSVDLEMIDVHVLADAFKRYLLDLPNPVIPAAVYSEMISLAPEVQSSEEYIQLLKKLIRSPSIPHQYWLTLQYLLKHFFKLSQTSSKNLLNARVLSEIFSPMLFRFSAASSDNTENLIKVIEILISTEW
>d2bct__ 1.84.1.1.1 beta-Catenin [Mouse (Mus musculus)]
TRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSED
>d1lrv__ 1.84.2.1.1 A leucine-rich repeat variant [Azotobacter vinelandii]
TPIGDCRVCSFRMSLLLTGRCTPGDACVAVESGRQIDRFFRNNPHLAVQYLADPFWERRAIAVRYSPVEALTPLIRDSDEVVRRAVAYRLPREQLSALMFDEDREVRITVADRLPLEQLEQMAADRDYLVRAYVVQRIPPGRLFRFMRDEDRQVRKLVAKRLPEESLGLMTQDPEPEVRRIVASRLRGDDLLELLHDPDWTVRLAAVEHASLEALRELDEPDPEVRLAIAGRL
>d1sly_1 1.84.4.1.1 (1-450) Soluble lytic transglycosylase (SLT), suprhelical domain [Escherichia coli]
DSLDEQRSRYAQIKQAWDNRQMDVVEQMMPGLKDYPLYPYLEYRQITDDLMNQPAVTVTNFVRANPTLPPARTLQSRFVNELARREDWRGLLAFSPEKPGTTEAQCNYYYAKWNTGQSEEAWQGAKELWLTGKSQPNACDKLFSVWRASGKQDPLAYLERIRLAMKAGNTGLVTVLAGQMPADYQTIASAIISLANNPNTVLTFARTTGATDFTRQMAAVAFASVARQDAENARLMIPSLAQAQQLNEDQIQELRDIVAWRLMGNDVTDEQAKWRDDAIMRSQSTSLIERRVRMALGTGDRRGLNTWLARLPMEAKEKDEWRYWQADLLLERGREAEAKEILHQLMQQRGFYPMVAAQRIGEEYELKIDKAPQNVDSALTQGPEMARVRELMYWNLDNTARSEWANLVKSKSKTEQAQLARYAFNNQWWDLSVQATIAGKLWDHLEERFP
>d1occe_ 1.84.7.1.1 Cytochrome c oxidase subunit e [bovine (Bos taurus)]
SHGSHETDEEFDARWVTYFNKPDIDAWELRKGMNTLVGYDLVPEPKIIDAALRACRRLNDFASAVRILEVVKDKAGPHKEIYPYVIQELRPTLNELGISTPEELGLDKV
>d2sblb1 1.85.1.1.1 (125-807) Lipoxigenase, C-terminal domain [Soybean (Glycine max), isozyme L1]
VPSETPAPLVSYREEELKSLRGNGTGERKEYDRIYDYDVYNDLGNPDKSEKLARPVLGGSSTFPYPRRGRTGRGPTVTDPNTEKQGEVFYVPRDENLGHLKSKDALEIGTKSLSQIVQPAFESAFDLKSTPIEFHSFQDVHDLYEGGIKLPRDVISTIIPLPVIKELYRTDGQHILKFPQPHVVQVSQSAWMTDEEFAREMIAGVNPCVIRGLEEFPPKSNLDPAIYGDQSSKITADSLDLDGYTMDEALGSRRLFMLDYHDIFMPYVRQINQLNSAKTYATRTILFLREDGTLKPVAIELSLPAAVSQVVLPAKEGVESTIWLLAKAYVIVNDSCYHQLMSHWLNTHAAMEPFVIATHRHLSVLHPIYKLLTPHYRNNMNINALARQSLINANGIIETTFLPSKYSVEMSSAVYKNWVFTDQALPADLIKRGVAIKDPSTPHGVRLLIEDYPYAADGLEIWAAIKTWVQEYVPLYYARDDDVKNDSELQHWWKEAVEKGHGDLKDKPWWPKLQTLEDLVEVCLIIIWIASALHAAVNFGQYPYGGLIMNRPTASRRLLPEKGTPEYEEMINNHEKAYLRTITSKLPTLISLSVIEILSTHASDEVYLGQRDNPHWTSDSKALQAFQKFGNKLKEIEEKLVRRNNDPSLQGNRLGPVQLPYTLLYPSSEEGLTFRGIPNSISI
>d1lnh_1 1.85.1.1.2 (129-836) Lipoxigenase, C-terminal domain [Soybean (Glycine max), isozyme L3]
YNAKLFKSDRIFFANQTYLPSETPAPLVKYREEELHNLRGDGTGERKEWERIYDYDVYNDLGDPDKGENHARPVLGGNDTFPYPRRGRTGRKPTRKDPNSESRSNDVYLPRDEAFGHLKSSDFLTYGLKSVSQNVLPLLQSAFDLNFTPREFDSFDEVHGLYSGGIKLPTDIISKISPLPVLKEIFRTDGEQALKFPPPKVIQVSKSAWMTDEEFAREMLAGVNPNLIRCLKDFPPRSKLDSQVYGDHTSQITKEHLEPNLEGLTVDEAIQNKRLFLLDHHDPIMPYLRRINATSTKAYATRTILFLKNDGTLRPLAIELSLPHPQGDQSGAFSQVFLPADEGVESSIWLLAKAYVVVNDSCYHQLVSHWLNTHAVVEPFIIATNRHLSVVHPIYKLLHPHYRDTMNINGLARLSLVNDGGVIEQTFLWGRYSVEMSAVVYKDWVFTDQALPADLIKRGMAIEDPSCPHGIRLVIEDYPYTVDGLEIWDAIKTWVHEYVFLYYKSDDTLREDPELQACWKELVEVGHGDKKNEPWWPKMQTREELVEACAIIIWTASALHAAVNFGQYPYGGLILNRPTLSRRFMPEKGSAEYEELRKNPQKAYLKTITPKFQTLIDLSVIEILSRHASDEVYLGERDNPNWTSDTRALEAFKRFGNKLAQIENKLSERNNDEKLRNRCGPVQMPYTLLLPSSKEGLTFRGIPNSISI
>d2tct_2 1.86.1.1.1 (67-198) Tetracyclin repressor (Tet-repressor, TetR), C-terminal domain [Escherichia coli]
LPAAGESWQSFLRNNAMSFRRALLRYRDGAKVHLGTRPDEKQYDTVETQLRFMTENGFSLRDGLYAISAVSHFTLGAVLEQQEHTAALNLPPLLREALQIMDSDDGEQAFLHGLESLIRGFEVQLTALLQIV
>d1lbd__ 1.87.1.1.1 retinoid-X receptor (RXR-alpha) [Human (Homo sapiens)]
SANEDMPVERILEAELAVEPKTETYVEANMGLNPSSPNDPVTNICQAADKQLFTLVEWAKRIPHFSELPLDDQVILLRAGWNELLIASFSHRSIAVKDGILLATGLHVHRNSAHSAGVGAIFDRVLTELVSKMRDMQMDKTELGCLRAIVLFNPDSKGLSNPAEVEALREKVYASLEAYCKHKYPEQPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQMT
>d1bbl__ 1.9.1.1.2 E3-binding domain of dihydrolipoamide succinyltransferase [Escherichia coli]
LSPAIRRLLAEHNLDASAIKGTGVGGRLTREDVEKHL
>d1bal__ 1.9.1.1.2 E3-binding domain of dihydrolipoamide succinyltransferase [Escherichia coli]
YASLEEQNNDALSPAIRRLLAEHNLDASAIKGTGVGGRLTREDVEKHLAKA
>d2pde__ 1.9.1.1.3 E3/E1 binding domain of dihydrolipoyl acetyltransferase [Bacillus stearothermophilus]
VIAMPSVRKYAREKGVDIRLVQGTGKNGRVLKEDIDAFLAGGA
>d1jswa_ 1.90.1.1.1 L-aspartate ammonia lyase [Escherichia coli]
MSNNIRIEEDLLGTREVPADAYYGVHTLRAIENFYISNNKISDIPEFVRGMVMVKKAAAMANKELQTIPKSVANAIIAACDEVLNNGKCMDQFPVDVYQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIAVYSSLIKLVDAINQLREGFERKAVEFQDILKMGRTQLQDAVPMTLGQEFRAFSILLKEEVKNIQRTAELLLEVNLGATAIGTGLNTPKEYSPLAVKKLAEVTGFPCVPAEDLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIMPAKVNPVVPEVVNQVCFKVIGNDTTVTMAAEAGQLQLNVMEPVIGQAMFESVHILTNACYNLLEKCINGITANKEVCEGYVYNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLERGLLTEAELDDIFSV
>d1fura_ 1.90.1.2.1 Fumarase C [Escherichia coli]
VRSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPTSLIHALALTKRAAAKVNEDLGLLSEEKASAIRQAADEVLAGQHDDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAALLALRKQLIPQLKTLTQTLNEKSRAFADIVKIGRTNLQDATPLTLGQEISGWVAMLEHNLKHIEYSLPHVAELALGGTAVGTGLNTHPEYARRVADELAVITCAPFVTAPNKFEALATCDALVQAHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPGKVNPTQCEALTMLCCQVMGNDVAINMGGASGNFELNVFRPMVIHNFLQSVRLLADGMESFNKHCAVGIEPNRERINQLLNESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKAAALALGYLSEAEFDSWVRPEQM
>d1fps__ 1.91.1.1.1 Farnesyl diphosphate synthase [Chicken (Gallus gallus)]
SPVVVEREREEFVGFFPQIVRDLTEDGIGHPEVGDAVARLKEVLQYNAPGGKCNRGLTVVAAYRELSGPGQKDAESLRCALAVGWCIELFQAFFLVADDIMDQSLTRRGQLCWYKKEGVGLDAINDSFLLESSVYRVLKKYCRQRPYYVHLLELFLQTAYQTELGQMLDLITAPVSKVDLSHFSEERYKAIVKYKTAFYSFYLPVAAAMYMVGIDSKEEHENAKAILLEMGEYFQIQDDYLDCFGDPALTGKVGTDIQDNKCSWLVVQCLQRVTPEQRQLLEDNYGRKEPEKVAKVKELYEAVGMRAAFQQYEESSYRRLQELIEKHSNRLPKEIFLGLAQKIYKRQK
>d5eas_2 1.91.1.2.1 (198-514) 5-Epi-aristolochene synthase, C-terminal domain [Tobacco (Nicotiana tabacum)]
KNNVLLRFAKLDFNLLQMLHKQELAQVSRWWKDLDFVTTLPYARDRVVECYFWALGVYFEPQYSQARVMLVKTISMISIVDDTFDAYGTVKELEAYTDAIQRWDINEIDRLPDYMKISYKAILDLYKDYEKELSSAGRSHIVCHAIERMKEVVRNYNVESTWFIEGYTPPVSEYLSNALATTTYYYLATTSYLGMKSATEQDFEWLSKNPKILEASVIICRVIDDTATYEVEKSRGQIATGIECCMRDYGISTKEAMAKFQNMAETAWKDINEGLLRPTPVSTEFLTPILNLARIVEVTYIVLKPHIINLLVDSIKI
>d1grl_1 1.92.1.1.1 (1-131,405-518) GroEL, the ATPase domain [Escherichia coli)]
VKFGNDAGVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIITEGLKAVAAGMNPMDLKRGIDKAVTVAVEELKALS
>d1ecma_ 1.93.1.1.1 Chorismate mutase domain of P-protein [Escherichia coli)]
NPLLALREKISALDEKLLALLAERRELAVEVGKAKLLSHRPVRDIDRERDLLERLITLGKAHHLDAHYITRLFQLIIEDSVLTQQALLQQH
>d1csma_ 1.93.1.2.1 Allosteric chorismate mutase [Saccharomyces cerevisiae)]
MDFTKPETVLNLQNIRDELVRMEDSIIFKFIERSHFATCPSVYEANHPGLEIPNFKGSFLDWALSNLEIAHSRIRRFESPDETPFFPDKIQKSFLPSINYPQILAPYAPEVNYNDKIKKVYIEKIIPLISKRDGDDKNNFGSVATRDIECLQSLSRRIHFGKFVAEAKFQSDIPLYTKLIKSKDVEGIMKNITNSAVEEKILERLTKKAEVYGVDPTERRIIPEYLVKIYKEIVIPITKEVEVEYLLRRLEE
>d1pprm2 1.94.1.1.1 (157-312) Peridinin-chlorophyll protein [dinoflagellate (Amphidinium carterae)]
PATVPSGDKIGVAAQQLSEASYPFLKEIDWLSDVYMKPLPGVSAQQSLKAIDKMIVMGAQADGNALKAAAEAHHKAIGSIDATGVTSAADYAAVNAALGRVIASVPKSTVMDVYNAMAGVTDTSIPLNMFSKVNPLDANAAAKAFYTFKDVVQAAQ
>d1pprm1 1.94.1.1.1 (1-156) Peridinin-chlorophyll protein [dinoflagellate (Amphidinium carterae)]
DEIGDAAKKLGDASYAFAKEVDWNNGIFLQAPGKLQPLEALKAIDKMIVMGAAADPKLLKAAAEAHHKAIGSISGPNGVTSRADWDNVNAALGRVIASVPENMVMDVYDSVSKITDPKVPAYMKSLVNGADAEKAYEGFLAFKDVVKKSQVTSAAG
>d1beo__ 1.96.1.1.1 beta-cryptogein [Phytophthora cryptogea]
TACTATQQTAAYKTLVSILSDASFNQCSTDSGYSMLTAKALPTTAQYKLMCASTACNTMIKKIVTLNPPNCDLTVPTSGLVLNVYSYANGFSNKCSSL
>d1rtm11 1.97.1.1.1 (1-32) Mannose-binding protein A, triple coiled-coil domain [rat (Rattus rattus)]
AIEVKLANMEAEINTLKSKLELTNKLHAFSMG
>d1hup_1 1.97.1.1.2 (1-24) Mannose-binding protein A, triple coiled-coil domain [human (Homo sapiens)]
AASERKALQTEMARIKKWLTFSLG
>d1zika_ 1.97.2.1.1 GCN4 [Yeast Saccharomyces cerevisiae]
RMKQLEDKVEELLSKKYHLENEVARLKKLV
>d2dgca_ 1.97.2.1.1 GCN4 [Yeast Saccharomyces cerevisiae]
ALKRARNTEAARRSRARKLQRMKQLEDKVEELLSKNYHLENEVARLKKL
>d1zima_ 1.97.2.1.1 GCN4 [Yeast Saccharomyces cerevisiae]
RMKQLEDKVEELLSKQYHLENEVARLKKLVGE
>d1gcla_ 1.97.2.1.1 GCN4 [Yeast Saccharomyces cerevisiae]
RMKQIEDKLEEILSKLYHIENELARIKKLLG
>d1gcma_ 1.97.2.1.1 GCN4 [Yeast Saccharomyces cerevisiae]
RMKQIEDKIEEILSKIYHIENEIARIKKLIG
>d2ztaa_ 1.97.2.1.1 GCN4 [Yeast Saccharomyces cerevisiae]
RMKQLEDKVEELLSKNYHLENEVARLKKLVG
>d1d66a1 1.97.2.1.2 (42-57) CD2-Gal4 [Yeast Saccharomyces cerevisiae]
LTRAHLTEVESRLERL
>d1pyia1 1.97.2.1.3 (43-88) PPR1 [Yeast Saccharomyces cerevisiae]
VPRSYVFFLEDRLAVMMRVLKEYGVDPTKIRGNIPATSDDEPFDLK
>d1ajya1 1.97.2.1.4 (38-71) PUT3 [Yeast Saccharomyces cerevisiae]
KKIVVSTKYLQQLQKDLNDKTEENNRLKALLLER
>d1fose_ 1.97.2.1.5 C-fos [Human (Homo sapiens)]
KRRIRRERNKMAAAKSRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEKLEFILA
>d1fosf_ 1.97.2.1.6 C-jun [Human (Homo sapiens)]
RKRMRNRIAASKSRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVM
>d1ifj__ 1.97.3.1.1 Inovirus (filamentous phage) major coat protein [strain fd]
AEGDDPAKAAFDSLQASATEYIGYAWAMVVVIVGATIGIKLFKKFTSKAS
>d1ifm__ 1.97.3.1.2 Inovirus (filamentous phage) major coat protein [strain pf1]
GVIDTSAVESAITDGQGDMKAIGGYIVGALVILAVAGLIYSMLRKA
>d1ifk__ 1.97.3.1.3 Inovirus (filamentous phage) major coat protein [strain if1]
ADDATSQAKAAFDSLTAQATEMSGYAWALVVLVVGATVGIKLFKKFVSRAS
>d1ifl__ 1.97.3.1.4 Inovirus (filamentous phage) major coat protein [strain ike]
AEPNAATNYATEAMDSLKTQAIDLISQTWPVVTTVVVAGLVIRLFKKFSSKAV
>d2ifo__ 1.97.3.1.5 Inovirus (filamentous phage) major coat protein [strain xf]
SGGGGVDVGDVVSAIQGAAGPIAAIGGAVLTVMVGIKVYKWVRRAM
>d1vdfa_ 1.97.5.1.1 Assembly domain of cartilage oligomeric matrix protein [rat (Rattus norvegicus)]
MDLAPQMLRELQETNAALQDVRELLRQQVKEITFLKNTVMECDACG
>d1dkga1 1.97.6.1.1 (1-99) The coiled-coil domain of nucleotide exchange factor GrpE [Escherichia coli]
AEQVDPRDEKVANLEAQLAEAQTRERDGILRVKAEMENLRRRTELDIEKAHKFALEKFINELLPVIDSLDRALEVAMSAMVEDIELTLKSMLDVVRKFG
>d1dipa_ 1.97.7.1.1 Delta-sleep-iducing peptide immunoreactive peptide [Pig (Sus scrofa)]
MDLVKNHLMYAVREEVEILKEQIRELVEKNSQLERENTLLKTLASPEQLEKFQSRLSPEEPAPETPEAPEAPGGSAV
>d1neu__ 2.1.1.1.1 Myelin membrane adhesion molecule P0 [rat (Rattus norvegicus)]
IVVYTDREVYGAVGSQVTLHCSFWSSEWVSDDISFTWRYQPEGGRDAISIFHYAKGQPYIDEVGTFKERIQWVGDPSWKDGSIVIHNLDYSDNGTFTCDVKNVGKTSQVTLYVFE
>d1bafh1 2.1.1.1.10 (1-115) Immunoglobulin (variable domains of L and H chains) [Fab ANO2 (mouse), kappa L chain]
DVQLQESGPGLVKPSQSQSLTCTVTGYSITSDYAWNWIRQFPGNKLEWMGYMSYSGSTRYNPSLRSRISITRDTSKNQFFLQLKSVTTEDTATYFCARGWPLAYWGQGTQVSVSE
>d1bafl1 2.1.1.1.10 (1-108) Immunoglobulin (variable domains of L and H chains) [Fab ANO2 (mouse), kappa L chain]
QIVLTQSPAIMSASPGEKVTMTCSASSSVYYMYWYQQKPGSSPRLLIYDTSNLASGVPVRFSGSGSGTSYSLTISRMEAEDAATYYCQQWSSYPPITFGVGTKLELKR
>d1ao7e1 2.1.1.1.100 (1-115) T-cell antigen receptor [human (Homo sapiens), beta-chain]
GVTQTPKFQVLKTGQSMTLQCAQDMNHEYMSWYRQDPGMGLRLIHYSVGAGITDQGEVPNGYNVSRSTTEDFPLRLLSAAPSQTSVYFCASRPGLAGGRPEQYFGPGTRLTVTED
>d1bbdh1 2.1.1.1.11 (1-119) Immunoglobulin (variable domains of L and H chains) [Fab 8F5 (mouse), kappa L chain]
EVQLQQSGAELVRPGASVKLSCTTSGFNIKDIYIHWVKQRPEQGLEWIGRLDPANGYTKYDPKFQGKATITVDTSSNTAYLHLSSLTSEDTAVYYCDGYYSYYDMDYWGPGTSVTVSSA
>d1bbdl1 2.1.1.1.11 (1-114) Immunoglobulin (variable domains of L and H chains) [Fab 8F5 (mouse), kappa L chain]
DIVMTQSPSSLTVTTGEKVTMTCKSSQSLLNSRTQKNYLTWYQQKPGQSPKLLIYWASTRESGVPDRFTGSGSGTDFTLSISGVQAEDLAVYYCQNNYNYPLTFGAGTKLELKR
>d1bbjl1 2.1.1.1.12 (1-109) Immunoglobulin (variable domains of L and H chains) [Fab B72.3 (mouse/human chimera), kappa L chain]
DIQMTQSPASLSVSVGETVTITCRASENIYSNLAWYQQKQGKSPQLLVYAATNLADGVPSRFSGSGSGTQYSLKINSLQSEDFGSYYCQHFWGTPYTFGGGTRLEIKRA
>d1bbjh1 2.1.1.1.12 (1-115) Immunoglobulin (variable domains of L and H chains) [Fab B72.3 (mouse/human chimera), kappa L chain]
XVQLQQSDAELVKPGASVKISCKASGYTFTDHAIHWAKQKPEQGLEWIGYISPGNDDIKYNEKFKGKATLTADKSSSTAYMQLNSLTSEDSAVYFCKRSYYGHWGQGTTLTVSSA
>d1hilb1 2.1.1.1.13 (1-119) Immunoglobulin (variable domains of L and H chains) [Fab 17/9 (mouse), kappa L chain]
EVQLVESGGDLVKPGGSLKLSCAASGFSFSSYGMSWVRQTPDKRLEWVATISNGGGYTYYPDSVKGRFTISRDNAKNTLYLQMSSLKSEDSAMYYCARRERYDENGFAYWGQGTLVTVS
>d1hila1 2.1.1.1.13 (1-114) Immunoglobulin (variable domains of L and H chains) [Fab 17/9 (mouse), kappa L chain]
DIVMTQSPSSLTVTAGEKVTMSCTSSQSLFNSGKQKNYLTWYQQKPGQPPKVLIYWASTRESGVPDRFTGSGSGTDFTLTISSVQAEDLAVYYCQNDYSNPLTFGGGTKLELKR
>d1dbbh1 2.1.1.1.14 (1-118) Immunoglobulin (variable domains of L and H chains) [Fab DB3 (mouse), kappa L chain]
QIQLVQSGPELKKPGETVKISCKASGYAFTNYGVNWVKEAPGKELKWMGWINIYTGEPTYVDDFKGRFAFSLETSASTAYLEINNLKNEDTATYFCTRGDYVNWYFDVWGAGTTVTVS
>d1dfbl1 2.1.1.1.15 (1-106) Immunoglobulin (variable domains of L and H chains) [Fab 3D6 (human), kappa L chain]
DIQMTQSPSTLSASVGDRVTITCRASQSISRWLAWYQQKPGKVPKLLIYKASSLESGVPSRFSGSGSGTEFTLTISSLQPDDFATYYCQQYNSYSFGPGTKVDIKR
>d1dfbh1 2.1.1.1.15 (1-126) Immunoglobulin (variable domains of L and H chains) [Fab 3D6 (human), kappa L chain]
EVQLVESGGGLVQPGRSLRLSCAASGFTFNDYAMHWVRQAPGKGLEWVSGISWDSSSIGYADSVKGRFTISRDNAKNSLYLQMNSLRAEDMALYYCVKGRDYYDSGGYFTVAFDIWGQGTMVTVSS
>d1igfl1 2.1.1.1.16 (1-112) Immunoglobulin (variable domains of L and H chains) [Fab B13I2 (mouse), kappa L chain]
DVLMTQTPLSLPVSLGDQASISCRSNQTILLSDGDTYLEWYLQKPGQSPKLLIYKVSNRFSGVPDRFSGSGSGTDFTLKISRVEAEDLGVYYCFQGSHVPPTFGGGTKLEIK
>d1igfh1 2.1.1.1.16 (1-119) Immunoglobulin (variable domains of L and H chains) [Fab B13I2 (mouse), kappa L chain]
EVQLVESGGDLVKPGGSLKLSCAASGFTFSRCAMSWVRQTPEKRLEWVAGISSGGSYTFYPDTVKGRFIISRNNARNTLSLQMSSLRSEDTAIYYCTRYSSDPFYFDYWGQGTTLTVSS
>d1igih1 2.1.1.1.17 (1-119) Immunoglobulin (variable domains of L and H chains) [Fab 26-10 (mouse), kappa L chain]
VQLQQSGPELVKPGASVRMSCKSSGYIFTDFYMNWVRQSHGKSLDYIGYISPYSGVTGYNQKFKGKATLTVDKSSSTAYMELRSLTSEDSAVYYCAGSSGNKWAMDYWGHGASVTVSSA
>d1igmh_ 2.1.1.1.18 Immunoglobulin (variable domains of L and H chains) [Fv POT (human) Ig-M, kappa L chain]
EVHLLESGGNLVQPGGSLRLSCAASGFTFNIFVMSWVRQAPGKGLEWVSGVFGSGGNTDYADAVKGRFTITRDNSKNTLYLQMNSLRAEDTAIYYCAKHRVSYVLTGFDSWGQGTLVTVSSGSASAPTL
>d1igml_ 2.1.1.1.18 Immunoglobulin (variable domains of L and H chains) [Fv POT (human) Ig-M, kappa L chain]
DIQMTQSPSSLSASVGDRVTITCQASQDISNYLAWYQQKPGKAPELRIYDASNLETGVPSRFSGSGSGTDFTFTISSLQPEDIATYYCQQYQNLPLTFGPGTKVDIKRTVAAPSV
>d1indl1 2.1.1.1.19 (1-108) Immunoglobulin (variable domains of L and H chains) [Fab Cha255 (mouse), lambda L chain]
AVVTQESALTTSPGETVTLTCRSSTGAVTTSNYANWVQEKPDHLFTGLIGGTNNRAPGVPARFSGSLIGDKAALTITGAQTEDEARYFCALWYSNLWVFGGGTKLTVL
>d1cd8__ 2.1.1.1.2 CD8 [human (Homo sapiens)]
SQFRVSPLDRTWNLGETVELKCQVLLSNPTSGCSWLFQPRGAAASPTFLLYLSQNKPKAAEGLDTQRFSGKRLGDTFVLTLSDFRRENEGYYFCSALSNSIMYFSHFVPVFLPA
>d1faih1 2.1.1.1.20 (1-123) Immunoglobulin (variable domains of L and H chains) [Fab R19.9 (mouse), kappa L chain]
QVQLQQSGAELVRAGSSVKMSCKASGYTFTSYGVNWVKQRPGQGLEWIGYINPGKGYLSYNEKFKGKTTLTVDRSSSTAYMQLRSLTSEDAAVYFCARSFYGGSDLAVYYFDSWGQGTTLTVS
>d2fb4h1 2.1.1.1.21 (1-127) Immunoglobulin (variable domains of L and H chains) [Fab KOL (human), lambda L chain]
EVQLVQSGGGVVQPGRSLRLSCSSSGFIFSSYAMYWVRQAPGKGLEWVAIIWDDGSDQHYADSVKGRFTISRNDSKNTLFLQMDSLRPEDTGVYFCARDGGHGFCSSASCFGPDYWGQGTPVTVSSA
>d2fb4l1 2.1.1.1.21 (1-111) Immunoglobulin (variable domains of L and H chains) [Fab KOL (human), lambda L chain]
QSVLTQPPSASGTPGQRVTISCSGTSSNIGSSTVNWYQQLPGMAPKLLIYRDAMRPSGVPDRFSGSKSGASASLAIGGLQSEDETDYYCAAWDVSLNAYVFGTGTKVTVLG
>d2fbjl1 2.1.1.1.22 (1-109) Immunoglobulin (variable domains of L and H chains) [Fab J539 (mouse), kappa L chain]
EIVLTQSPAITAASLGQKVTITCSASSSVSSLHWYQQKSGTSPKPWIYEISKLASGVPARFSGSGSGTSYSLTINTMEAEDAAIYYCQQWTYPLITFGAGTKLELKRAD
>d2fbjh1 2.1.1.1.22 (1-118) Immunoglobulin (variable domains of L and H chains) [Fab J539 (mouse), kappa L chain]
EVKLLESGGGLVQPGGSLKLSCAASGFDFSKYWMSWVRQAPGKGLEWIGEIHPDSGTINYTPSLKDKFIISRDNAKNSLYLQMSKVRSEDTALYYCARLHYYGYNAYWGQGTLVTVSA
>d1fgvl_ 2.1.1.1.23 Immunoglobulin (variable domains of L and H chains) [Fab H52 (synthetic, humanised version), kappa L chain]
DIQMTQSPSSLSASVGDRVTITCRASQDINNYLNWYQQKPGKAPKLLIYYTSTLESGVPSRFSGSGSGTDYTLTISSLQPEDFATYYCQQGNTLPPTFGAGTKVEIK
>d1fgvh_ 2.1.1.1.23 Immunoglobulin (variable domains of L and H chains) [Fab H52 (synthetic, humanised version), kappa L chain]
EVQLVESGGGLVQPGGSLRLSCATSGYTFTEYTMHWMRQAPGKGLEWVAGINPKNGGTSYADSVKGRFTISVDKSKNTLYLQMNSLRAEDTAVYYCARWRGLDVRYFDVWGQGTLVTVSS
>d2fgwh1 2.1.1.1.23 (1-116) Immunoglobulin (variable domains of L and H chains) [Fab H52 (synthetic, humanised version), kappa L chain]
EVQLVESGGGLVQPGGSLRLSCATSGYTFTEYTMHWMRQAPGKGLEWVAGINPKNGGTSHNQRFMDRFTISVDKSTSTAYMQMNSLRAEDTAVYYCARWRRYFDVWGQGTLVTVSS
>d1mcph1 2.1.1.1.24 (1-121) Immunoglobulin (variable domains of L and H chains) [Fab MCPC603 (human), kappa L chain]
EVKLVESGGGLVQPGGSLRLSCATSGFTFSDFYMEWVRQPPGKRLEWIAASRNKGNKYTTEYSASVKGRFIVSRDTSQSILYLQMNALRAEDTAIYYCARNYYGSTWYFDVWGAGTTVTVS
>d2imn__ 2.1.1.1.24 Immunoglobulin (variable domains of L and H chains) [Fab MCPC603 (human), kappa L chain]
DIVMTQSPSSLSVSAGERVTMSCKSSQSLLYKDGKNFLAWYQQKPGQPPKLLIYGASTRESGVPDRFTGSGSGTDFTLTISSVQAEDLAVYYCQNDHSYPLTFGAGTKLELKR
>d1fvcb_ 2.1.1.1.25 Immunoglobulin (variable domains of L and H chains) [Fab 4D5 (synthetic, humanised version), kappa L chain]
EVQLVESGGGLVQPGGSLRLSCAASGFNIKDTYIHWVRQAPGKGLEWVARIYPTNGYTRYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCSRWGGDGFYAMDYWGQGTLVTVSS
>d1fvca_ 2.1.1.1.25 Immunoglobulin (variable domains of L and H chains) [Fab 4D5 (synthetic, humanised version), kappa L chain]
DIQMTQSPSSLSASVGDRVTITCRASQDVNTAVAWYQQKPGKAPKLLIYSASFLYSGVPSRFSGSRSGTDFTLTISSLQPEDFATYYCQQHYTTPPTFGQGTKVEIKRT
>d1ggbl1 2.1.1.1.26 (1-111) Immunoglobulin (variable domains of L and H chains) [Fab 50.1 (mouse), kappa L chain]
DIVLTQSPGSLAVSLGQRATISCRASESVDDDGNSFLHWYQQKPGQPPKLLIYRSSNLISGIPDRFSGSGSRTDFTLTINPVEADDVATYYCQQSNEDPLTFGAGTKLEIK
>d1ggbh1 2.1.1.1.26 (1-114) Immunoglobulin (variable domains of L and H chains) [Fab 50.1 (mouse), kappa L chain]
QVQLQESGPGILQPSQTLSLTCSFSGFSLSTYGMGVSWIRQPSGKGLEWLAHIFWDGDKRYNPSLKSRLKISKDTSNNQVFLKITSVDTADTATYYCVQEGYIYWGQGTSVTVS
>d1acyh1 2.1.1.1.27 (1-120) Immunoglobulin (variable domains of L and H chains) [Fab 59.1 (mouse), kappa L chain]
QVKLQESGPAVIKPSQSLSLTCIVSGFSITRTNYCWHWIRQAPGKGLEWMGRICYEGSIYYSPSIKSRSTISRDTSLNKFFIQLISVTNEDTAMYYCSRENHMYETYFDVWGQGTTVTVS
>d1acyl1 2.1.1.1.27 (1-112) Immunoglobulin (variable domains of L and H chains) [Fab 59.1 (mouse), kappa L chain]
DIVMTQSPASLVVSLGQRATISCRASESVDSYGKSFMHWYQQKPGQPPKVLIYIASNLESGVPARFSGSGSRTDFTLTIDPVEADDAATYYCQQNNEDPPTFGAGTKLEMRR
>d1mamh1 2.1.1.1.28 (1-119) Immunoglobulin (variable domains of L and H chains) [Fab Yst9.1 (mouse), kappa L chain]
EVKLVESGGGLVQPGGSLRLSCATSGFTFTDYYMSWVRQPPGKALEWLGFIRNKADGYTTEYSASVKGRFTISRDNSQSILYLQMNTLRAEDSATYYCTRDPYGPAAYWGQGTLVTVSA
>d1maml1 2.1.1.1.28 (1-108) Immunoglobulin (variable domains of L and H chains) [Fab Yst9.1 (mouse), kappa L chain]
DIQMTQTTSSLSASLGDRVTISCRASQDIYNYLNWYQQKPDGTVKLLIYYTSRLHSGVPSRFSGSGSGTDYSLTISNLNQEDMATYICQQGNTLPFTFGSGTKLEIKR
>d1mfel1 2.1.1.1.29 (1-111) Immunoglobulin (variable domains of L and H chains) [Fab SE155-4 (mouse), lambda L chain]
XAVVTQESALTTSPGETVTLTCRSSTGTVTSGNHANWVQEKPDHLFTGLIGDTNNRAPGVPARFSGSLIGDKAALTITGAQPEDEAIYFCALWCNNHWIFGGGTKLTVLGQ
>d3cd4_1 2.1.1.1.3 (1-97) CD4 [human (Homo sapiens)]
KKVVLGKKGDTVELTCTASQKKSIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRADSRRSLWDQGNFPLIIKNLKIEDSDTYICEVEDQKEEVQLLV
>d1cbvh1 2.1.1.1.30 (1-122) Immunoglobulin (variable domains of L and H chains) [Fab BV04-01 (mouse), kappa L chain]
EVQPVETGGGLVQPKGSLKLSCAASGFSFNTNAMNWVRQAPGKGLEWVARIRSKSNNYATYYADSVKDRFTISRDDSQNMLYLQMNNLKTEDTAMYYCVRDQTGTAWFAYWGQGTLVTVSAA
>d1teth1 2.1.1.1.31 (1-115) Immunoglobulin (variable domains of L and H chains) [Fab TE33 (mouse), kappa L chain]
QIQLVQSGPELKTPGETVRISCKASGYTFTTYGMSWVKQTPGKGFKWMGWINTYSGVPTYADDFKGRFAFSLETSASTAYLQINNLKNEDTATYFCARRSWYFDVWGTGTTVTVS
>d1tetl1 2.1.1.1.31 (1-112) Immunoglobulin (variable domains of L and H chains) [Fab TE33 (mouse), kappa L chain]
DVLMTQTPLSLPVSLGDQASISCKSSQSIVHSSGNTYFEWYLQKPGQSPKLLIYKVSNRFSGVPDRFSGSGSGTDFTLKISRVEAEDLGVYYCFQGSHIPFTFGSGTKLEIK
>d1flrh1 2.1.1.1.32 (1-116) Immunoglobulin (variable domains of L and H chains) [Fab 4-4-20 (mouse), kappa L chain]
EVKLDETGGGLVQPGRPMKLSCVASGFTFSDYWMNWVRQSPEKGLEWVAQIRNKPYNYETYYSDSVKGRFTISRDDSSVYLQMNNLRVEDMGIYYCTGSYYGMDYWGQGTSVTVSS
>d6fabl1 2.1.1.1.33 (1-108) Immunoglobulin (variable domains of L and H chains) [Fab 36-71 (mouse), kappa L chain]
DIQMTQIPSSLSASLGDRVSISCRASQDINNFLNWYQQKPDGTIKLLIYFTSRSQSGVPSRFSGSGSGTDYSLTISNLEQEDIATYFCQQGNALPRTFGGGTKLEIKR
>d6fabh1 2.1.1.1.33 (1-121) Immunoglobulin (variable domains of L and H chains) [Fab 36-71 (mouse), kappa L chain]
EVQLQQSGVELVRAGSSVKMSCKASGYTFTSNGINWVKQRPGQGLEWIGYNNPGNGYIAYNEKFKGKTTLTVDKSSSTAYMQLRSLTSEDSAVYFCARSEYYGGSYKFDYWGQGTTLTVSS
>d1gigh1 2.1.1.1.34 (1-120) Immunoglobulin (variable domains of L and H chains) [Fab HC19 (mouse), lambda L chain]
QVQLKESGPGLVAPSQSLSITCTVSGFLLISNGVHWVRQPPGKGLEWLGVIWAGGNTNYNSALMSRVSISKDNSKSQVFLKMKSLQTDDTAMYYCARDFYDYDVFYYAMDYWGQGTSVTV
>d2cgrh1 2.1.1.1.35 (1-117) Immunoglobulin (variable domains of L and H chains) [Fab, anti-sweetener (mouse), kappa L chain]
RVQLLESGAELMKPGASVQISCKATGYTFSEYWIEWVKERPGHGLEWIGEILPGSGRTNYREKFKGKATFTADTSSNTAYMQLSSLTSEDSAVYYCTRGYSSMDYWGQGTSVTVSAA
>d2cgrl1 2.1.1.1.35 (1-112) Immunoglobulin (variable domains of L and H chains) [Fab, anti-sweetener (mouse), kappa L chain]
ELVMTQSPLSLPVSLGDQASISCRPSQSLVHSNGNTYLHWYLQKPGQSPKLLIYRVSNRFSGVPDRFSGSGSGTAFTLKISRVEAEDLGVYFCSQGTHVPYTFGGGTKLELK
>d1figh1 2.1.1.1.36 (1-119) Immunoglobulin (variable domains of L and H chains) [Fab 1F7 (mouse), kappa L chain]
DVQLQQSGPELEKPGASVKISCKASGFSLPGHNINWIVQRNGKSLEWIGNIDPYYGGTNFNPKFKGKATLTVDKSSSTLYMHLTSLQSEDSAVYYCARRRDGNYGFTYWGQGTLVTVSA
>d1figl1 2.1.1.1.36 (1-109) Immunoglobulin (variable domains of L and H chains) [Fab 1F7 (mouse), kappa L chain]
ENVLTQSPAIMSASPGEKVTMACRASSSVSSTYLHWYQQKSGASPKLLIYSTSNLASGVPARFSGSGSGTSYSLTISSVEAEDAATYYCQQYSGYPLTFGAGTKLELKR
>d1frgh1 2.1.1.1.37 (1-119) Immunoglobulin (variable domains of L and H chains) [Fab 26/9 (mouse), kappa L chain]
EVLLVESGGDLVKPGGFLKLSCAASGFTFSSFGMSWVRHTPDKRLEWVATISNGGGYTYYQDSVKGRFTISRDNAKNTLFLEMTSLKSEDAGLYYCARRERYDEKGFAYWGRGTLVTVS
>d1vfba_ 2.1.1.1.38 Immunoglobulin (variable domains of L and H chains) [Fab D1.3 (mouse), kappa L chain]
DIVLTQSPASLSASVGETVTITCRASGNIHNYLAWYQQKQGKSPQLLVYYTTTLADGVPSRFSGSGSGTQYSLKINSLQPEDFGSYYCQHFWSTPRTFGGGTKLEIK
>d1vfbb_ 2.1.1.1.38 Immunoglobulin (variable domains of L and H chains) [Fab D1.3 (mouse), kappa L chain]
QVQLQESGPGLVAPSQSLSITCTVSGFSLTGYGVNWVRQPPGKGLEWLGMIWGDGNTDYNSALKSRLSISKDNSKSQVFLKMNSLHTDDTARYYCARERDYRLDYWGQGTTLTVSS
>d1jhlh_ 2.1.1.1.39 Immunoglobulin (variable domains of L and H chains) [Fv D11.15 (mouse), kappa L chain]
QVQLQQSGAELVRPGASVKLSCKASGYTFISYWINWVKQRPGQGLEWIGNIYPSDSYTNYNQKFKDKATLTVDKSSSTAYMQLSSPTSEDSAVYYCTRDDNYGAMDYWGQGTTVTV
>d1jhll_ 2.1.1.1.39 Immunoglobulin (variable domains of L and H chains) [Fv D11.15 (mouse), kappa L chain]
DIELTQSPSYLVASPGETITINCRASKSISKSLAWYQEKPGKTNNLLIYSGSTLQSGIPSRFSGSGSGTDFTLTISSLEPEDFAMYICQQHNEYPWTFGGGTKLEIKR
>d1cid_1 2.1.1.1.4 (1-105) CD4 [rat (Rattus rattus)]
TSITAYKSEGESAEFSFPLNLGEESLQGELRWKAEKAPSSQSWITFSLKNQKVSVQKSTSNPKFQLSETLPLTLQIPQVSLQFAGSGNLTLTLDRGILYQEVNLV
>d2iffl1 2.1.1.1.40 (1-106) Immunoglobulin (variable domains of L and H chains) [Fab HyHEL-5 (mouse), kappa L chain]
DIVLTQSPAIMSASPGEKVTMTCSASSSVNYMYWYQQKSGTSPKRWIYDTSKLASGVPVRFSGSGSGTSYSLTISSMETEDAATYYCQQWGRNPTFGGGTKLEIKR
>d2iffh1 2.1.1.1.40 (1-115) Immunoglobulin (variable domains of L and H chains) [Fab HyHEL-5 (mouse), kappa L chain]
VQLQQSGAELMKPGASVKISCKASGYTFSDYWIEWVKQRPGHGLEWIGEILPGSGSTNYHERFKGKATFTADTSSSTAYMQLNSLTSEDSGVYYCLHGNYDFDGWGQGTTLTVSS
>d3hfmh1 2.1.1.1.41 (1-113) Immunoglobulin (variable domains of L and H chains) [Fab HyHEL-10 (mouse), kappa L chain]
DVQLQESGPSLVKPSQTLSLTCSVTGDSITSDYWSWIRKFPGNRLEYMGYVSYSGSTYYNPSLKSRISITRDTSKNQYYLDLNSVTTEDTATYYCANWDGDYWGQGTLVTVSA
>d1jell1 2.1.1.1.42 (1-113) Immunoglobulin (variable domains of L and H chains) [Fab JE142 (mouse), kappa L chain]
DVLMTQTPLSLPVSLGDQASISCRSSQSIVHGNGNTYLEWYLQKPGQSPKLLIYSISSRFSGVPDRFSGSGSGTDFTLKISRVQAEDLGVYYCFQGSHVPYTFGGGTKLEIKR
>d1jelh1 2.1.1.1.42 (1-118) Immunoglobulin (variable domains of L and H chains) [Fab JE142 (mouse), kappa L chain]
QVQLQQSGPELVRPGSSVKISCKGSGYTFTTYAMHWVKQSHAKSLEWIGLISPSSGYTSYNGEFKGKATMTVDKSSSTAYMELARLTSEDSAIYYCARVMGEQYFDVWGAGTTVTVSS
>d1ncal1 2.1.1.1.43 (1-108) Immunoglobulin (variable domains of L and H chains) [Fab NC41 (mouse), kappa L chain]
DIVMTQSPKFMSTSVGDRVTITCKASQDVSTAVVWYQQKPGQSPKLLIYWASTRHIGVPDRFAGSGSGTDYTLTISSVQAEDLALYYCQQHYSPPWTFGGGTKLEIKR
>d1ncah1 2.1.1.1.43 (1-120) Immunoglobulin (variable domains of L and H chains) [Fab NC41 (mouse), kappa L chain]
QIQLVQSGPELKKPGETVKISCKASGYTFTNYGMNWVKQAPGKGLKWMGWINTNTGEPTYGEEFKGRFAFSLETSASTANLQINNLKNEDTATFFCARGEDNFGSLSDYWGQGTTVTVSS
>d1forl1 2.1.1.1.44 (1-107) Immunoglobulin (variable domains of L and H chains) [Fab 17-Ia (mouse), kappa L chain]
QIVLTQSPAIMSAFPGEKVTITCSATSSVNYMHWFQQKPGTSPKLWIYSSSNLASGVPARFSGSGSGTSYSLTISRMEAEDAATYYCQQRSSYPITFGSGTKLEIKR
>d1forh1 2.1.1.1.44 (1-120) Immunoglobulin (variable domains of L and H chains) [Fab 17-Ia (mouse), kappa L chain]
QGQLQQSGAELVRPGSSVKISCKASGYAFSSFWVNWVKQRPGQGLEWIGQIYPGDGDNKYNGKFKGKATLTADKSSTTAYMQLYSLTSEDSAVYFCARSGNYPYAMDYWGQGTSVTVSSA
>d1knob1 2.1.1.1.45 (1-119) Immunoglobulin (variable domains of L and H chains) [Fab CNJ206 (mouse), kappa L chain]
DVKLVESGGGLVQPGGSRKLSCAASGFTFSSFGMHWVRQAPEKGLEWVAYISSGSSTIYYADTVKGRFTISRDNPKNTLFLQMTSLRSEDTAMYYCARGDYYGSRGAYWGQGTLVTVSA
>d1knoa1 2.1.1.1.45 (1-108) Immunoglobulin (variable domains of L and H chains) [Fab CNJ206 (mouse), kappa L chain]
QIQMTQSPSSLSASLGERVSLTCRASQEISGYLSWLQQKPDGTIKRLIYAASTLDSGVPKRFSGSRSGSDYSLTISSLESEDFADYYCLQYASSPYTFGGGTKLEILR
>d1eapa1 2.1.1.1.46 (1-106) Immunoglobulin (variable domains of L and H chains) [Fab 17E8 (mouse), kappa L chain]
DIELTQSPSSLSASLGGKVTITCKASQDIKKYIGWYQHKPGKGPRLLIHYTSTLLPGIPSRFRGSGSGRDYSFSISNLEGGDIATYYCLQYYNLRTFGGGTKLEIK
>d1eapb1 2.1.1.1.46 (1-119) Immunoglobulin (variable domains of L and H chains) [Fab 17E8 (mouse), kappa L chain]
EVQLQESGTELVKPGASVKISCKASGYISTDHAIHWVKQRPEQGLEWIGYISPGNGDIKYNEKFKVKATLTADQSSSTAYMQLNSLTSEDSAVYFCKRSYYGSSYVDYWGQGTTLTVSS
>d1mrdl1 2.1.1.1.47 (1-113) Immunoglobulin (variable domains of L and H chains) [Fab Jel 103 (mouse), kappa L chain]
DVVMTQTPLSLPVSLGDQASISCRSSQSLVHSNGNTYLHWYLQKPGQSPKLLIYKVSNRFSGVPDRFSGSGSGTDFTLKISRVEAEDLGVYFCSQSTHVPRTFGGGTKLEIKR
>d1mrdh1 2.1.1.1.47 (1-114) Immunoglobulin (variable domains of L and H chains) [Fab Jel 103 (mouse), kappa L chain]
VQLQQSGAELVKPGASVKLSCKASGYTFTSYWMQWVKQRPGQGLEWIGEIDPSDSYTNYNQKFKGKATLTVDSTAYMQLSSLTSEDSAVYYCANLRGYFDYWGQGTTLTVSSAK
>d1fbih1 2.1.1.1.48 (1-121) Immunoglobulin (variable domains of L and H chains) [Fab F9.13.7 (mouse), kappa L chain]
QVQLQQPGAELVKPGASVKLSCKASGYTFTSYWMHWVKQGPGQGLEWIGEIDPSDSYPNYNEKFKGKATLTVDKSSSTAYMQLSSLTSEDSAVYYCASLYYYGTSYGVLDYWGQGTSVTVS
>d1rmfh1 2.1.1.1.49 (1-119) Immunoglobulin (variable domains of L and H chains) [Fab R6.5 (mouse), kappa L chain]
QVQLQQSGPELVRPGVSVKISCKGSGYTFIDYAIHWVKESHAKSLEWIGVISAYSGDTNYNQKFKGKATMTVDKSSNTAYLELARLTSEDSAIYYCARGGWLLLSFDYWGQGTTLTVSS
>d1hnf_1 2.1.1.1.5 (1-101) CD2 [human (Homo sapiens)]
TNALETWGALGQDINLDIPSFQMSDDIDDIKWEKTSDKKKIAQFRKEKETFKEKDTYKLFKNGTLKIKHLKTDDQDIYKVSIYDTKGKNVLEKIFDLKIQE
>d1fpth1 2.1.1.1.50 (1-120) Immunoglobulin (variable domains of L and H chains) [Fab C3(?), neutralizing type 1 poliovirus, (mouse), kapppa L chain]
QVQLQQSGAELVRPGTSVKVSCKASGYAFTNYLIQWIKQRPGQGLEWIGVINPGSGGTDYNANFKGKATLTADKSSSIVYMQLSSLTSDDSAVYFCARDFYDYDVGFDYWGQGTTLTVSS
>d1ikfl1 2.1.1.1.51 (1-107) Immunoglobulin (variable domains of L and H chains) [Fab, anti-cyclosporin A, (mouse), kappa L chain]
DIQMTQTTSSLSASLGDRVTISCRASQDISTYLNWYQQKPDGTVKLLIFYTSRLRSGVPSRFSGSGSGTDYSLTISNLEQEDIATYFCQQGSRIPPTFGGGTKLEIL
>d1lmka1 2.1.1.1.52 (1-126) Immunoglobulin (variable domains of L and H chains) [scFv dimer (L5MK16 diabody), based on: (mouse), kappa L chain]
VQLQQSGTELMKPGRSLKISCKTTGYIFSNYWIEWVKQRPGHGLEWIGKILPGGGSNTYNDKFKGKATFTADTSSNIAYMQLSSLTSEDSAVYYCARGEDYYAYWYVLDYWGQGTTVTVSSGGGGS
>d1lmka2 2.1.1.1.52 (127-238) Immunoglobulin (variable domains of L and H chains) [scFv dimer (L5MK16 diabody), based on: (mouse), kappa L chain]
DIELTQSPLSLPVSLGDQASISCRSSQSLVHSNGNTSLHWYLKKPGQSPKLLIYKVSTRFSGVPDRFSGSGSGTDFTLKISRVEAEDLGVYFCSQSTHVPFTFGSGTKLELK
>d1nqba1 2.1.1.1.53 (1-119) Immunoglobulin (variable domains of L and H chains) [scFv trivalent antibody, based on: (mouse), kappa L chain]
VQLQQSGAELVKPGASVKLSCKASGYTFTSYWMHWVKQRPGRGLEWIGRIDPNSGGTKYNEKFKSKATLTVDKPSSTAYMQLSSLTSEDSAVYYCARYDYYGSSYFDYWGQGTTVTVSS
>d1nqba2 2.1.1.1.53 (120-232) Immunoglobulin (variable domains of L and H chains) [scFv trivalent antibody, based on: (mouse), kappa L chain]
DIELTQTPLSLPVSLGDQASISCRSSQSIVHSNGNTYLEWYLQKPGQSPKLLIYKVSNRFSGVPDRFSGSGSGTDFTLKISRVEAEDLGVYYCFQGSHVPYTFGGGTKLEIKR
>d1igch1 2.1.1.1.54 (1-119) Immunoglobulin (variable domains of L and H chains) [Fab MoPC21 (mouse), kappa L chain]
DVQLVESGGGLVQPGGSRKLSCAASGFTFSSFGMHWVRQAPEKGLEWVAYISSGSSTLHYADTVKGRFTISRDNPKNTLFLQMTSLRSEDTGMYYCARWGNYPYYAMDYWGQGTSVTVS
>d1igcl1 2.1.1.1.54 (1-108) Immunoglobulin (variable domains of L and H chains) [Fab MoPC21 (mouse), kappa L chain]
NIVMTQSPKSMSMSVGERVTLTCKASENVVTYVSWYQQKPEQSPKLLIYGASNRYTGVPDRFTGSGSATDFTLTISSVQAEDLADYHCGQGNSYPYTFGGGTKLEIKR
>d1ibgl1 2.1.1.1.55 (1-110) Immunoglobulin (variable domains of L and H chains) [Fab 40-50 (mouse), kappa L chain]
IVLTQSPASLAVSLGQRATISCRASKSVSTSGYSHIHWYQQKPGQPPKLLIYLASILESGVPARFSGSGSGTDFTLNIHPVEEEDAATYYCQHSREYPLTFGAGTELELK
>d1ibgh1 2.1.1.1.55 (1-120) Immunoglobulin (variable domains of L and H chains) [Fab 40-50 (mouse), kappa L chain]
VHLVQSGPGLVAPSQSLSITCTVSGFSLTTYGVHWFRQPPGKGLEWLGLIWAGGNTDYNSALMSRLSINKDNSKSQVFLKMNSLQADDTAMYYCARFRFASYYDYAVDYWGQGTSVTVSS
>d1mlbb1 2.1.1.1.56 (1-118) Immunoglobulin (variable domains of L and H chains) [Fab D44.1 (mouse), kappa L chain]
QVQLQESGAEVMKPGASVKISCKATGYTFSTYWIEWVKQRPGHGLEWIGEILPGSGSTYYNEKFKGKATFTADTSSNTAYMQLSSLTSEDSAVYYCARGDGNYGYWGQGTTLTVSSAS
>d1nmbh_ 2.1.1.1.57 Immunoglobulin (variable domains of L and H chains) [Fab NC10 (mouse), kappa L chain]
QVQLQQPGAELVKPGASVRMSCKASGYTFTNYNMYWVKQSPGQGLEWIGIFYPGNGDTSYNQKFKDKATLTADKSSNTAYMQLSSLTSEDSAVYYCARSGGSYRYDGGFDYWGQGTTLTVSS
>d1nmbl_ 2.1.1.1.57 Immunoglobulin (variable domains of L and H chains) [Fab NC10 (mouse), kappa L chain]
DIQMTQTTSSLSASLGDRVTISCRASQDISNYLNWYQQNPDGTVKLLIYYTSNLHSEVPSRFSGSGSGTDYSLTISNLEQEDIATYFCQQDFTLPFTFGGGTKLEIRRA
>d1opgl1 2.1.1.1.58 (1-107) Immunoglobulin (variable domains of L and H chains) [Fab OPG2 (mouse), kappa L chain]
DELLTQSPATLSVTPGDSVSLSCRASQSISNNLHWYQQKSHESPRLLIKYASQSISGIPSRFSGSGSGTDFTLSINSVETEDFGMYFCQQSNSWPLTFGGGSKLEIK
>d1opgh1 2.1.1.1.58 (1-125) Immunoglobulin (variable domains of L and H chains) [Fab OPG2 (mouse), kappa L chain]
EVQLVQSGGGLVNPGRSLKLSCAASGFTFSSYGMSWVRQTPEKRLEWVAAISGGGTYIHYPDSVKGRFTISRDNAKNNLYLQMSSLRSEDTALYYCTRHPFYRYDGGNYYAMDHWGQGTSVTVSA
>d1nsnh1 2.1.1.1.59 (1-114) Immunoglobulin (variable domains of L and H chains) [Fab N10 (mouse), kappa L chain]
DVQLQESGPGLVKPSQSLSLTCTVTGYSITSDYAWNWIRQFPGNKLEWMGYITYSGTTSYNPSLKSRISISRDTSKNQFFMQLNSVTTEDTGTFYCTRGNGDWGQGTTLTVSSA
>d1nsnl1 2.1.1.1.59 (1-111) Immunoglobulin (variable domains of L and H chains) [Fab N10 (mouse), kappa L chain]
DIVLTQSPSSLAVSLGQRATISCRASQSVSTSSFRYMHWYQQKPGQPPRLLIKYASNLESGVPARFSGSGSGTDFTLNIHPVEEEDTATYYCQHSWEIPYTFGGGTKLEIK
>d1cdcb_ 2.1.1.1.6 CD2 [rat (Rattus rattus)]
GTVWGALGHGINLNIPNFQMTDDIDEVRWERGSTLVAEFKRKMKPFLKSGAFEILANGDLKIKNLTRDDSGTYNVTVYSTNGTRILDKALDLRILE
>d1iaih1 2.1.1.1.60 (1-121) Immunoglobulin (variable domains of L and H chains) [Fab 730.1.4 (mouse), kappa L chain]
QIQLVQSGPELKKPGETVKISCKASGYTFTNYGMNWVKQAPGKGLKWMAWINTYTGEPTYADDFKGRFAFSLETSASTAYLQINNLKNEDTATYFCARDGYYENYYAMDYWGQGTSVTVSS
>d1iail1 2.1.1.1.60 (1-108) Immunoglobulin (variable domains of L and H chains) [Fab 730.1.4 (mouse), kappa L chain]
DIVMTQSHKFMSTSVGDRVSITCKASQDVSTAVAWYQQKPGQSPKLLIYSASYQYTGVPDRFTGSGSRTDFTFTINSVQAEDLAVYYCHQHYSTPFTFGSGTKLEIKR
>d1iaii1 2.1.1.1.61 (1-121) Immunoglobulin (variable domains of L and H chains) [Fab 409.5.3 (mouse), kappa L chain]
EVKLQESGGGLVQPGGSMKLSCVASGFTFNNYWMSWVRQSPEKGLEWVAEIRLNSDNFATHYAESVKGKFIISRDDSKSRLYLQMNSLRAEDTGIYYCVLRPLFYYAVDYWGQGTSVTVSS
>d1iaim1 2.1.1.1.61 (1-109) Immunoglobulin (variable domains of L and H chains) [Fab 409.5.3 (mouse), kappa L chain]
DIQLTQSPAFMAASPGEKVTITCSVSSSISSSNLHWYQQKSETSPKPWIYGTSNLASGVPVRFSGSGSGTSYSLTISSMEAEDAATYYCQQWNSYPYTFGGGTKLEIKR
>d1plgh1 2.1.1.1.62 (1-117) Immunoglobulin (variable domains of L and H chains) [Polysialic acid-binding Fab (mouse), kappa L chain]
QIQLQQSGPELVRPGASVKISCKASGYTFTDYYIHWVKQRPGEGLEWIGWIYPGSGNTKYNEKFKGKATLTVDTSSSTAYMQLSSLTSEDSAVYFCARGGKFAMDYWGQGTSVTVSS
>d1gafh1 2.1.1.1.63 (1-114) Immunoglobulin (variable domains of L and H chains) [Fab 48G7 (mouse/human), kappa L chain]
QVQLQQSGAELVKPGASVKLSCTASGFNIKDTYMHWVKQRPKQGLEWIGRIDPANVDTKYDPKFQDKATITADTSSKTTYLQLSSLTSEDTAVYYCASYYGIYWGQGTTLTVSS
>d1gafl1 2.1.1.1.63 (1-109) Immunoglobulin (variable domains of L and H chains) [Fab 48G7 (mouse/human), kappa L chain]
DIQMTQSPSSLSASLGERVSLTCRASQEINGYLGWLQQKPDGTIKRLIYAASTLHSGVPKRFSGSRSGSDYSLTISSLESEDFADYYCLQYASYPRTFGGGTKVEIKRT
>d1ngph1 2.1.1.1.64 (1-120) Immunoglobulin (variable domains of L and H chains) [Fab N1G9 (mouse). lambda L chain]
QVQLQQPGAELVKPGASVKLSCKASGYTFTSYWMHWVKQRPGRGLEWIGRIDPNSGGTKYNEKFKSKATLTVDKPSSTAYMQLSSLTSEDSAVYYCARYDYYGSSYFDYWGQGTTLTVSS
>d1vgel1 2.1.1.1.65 (1-107) Immunoglobulin (variable domains of L and H chains) [Fab TR1.9 (mouse/human), kappa L chain]
ELVMTQSPSSLSASVGDRVNIACRASQGISSALAWYQQKPGKAPRLLIYDASNLESGVPSRFSGSGSGTDFTLTISSLQPEDFAIYYCQQFNSYPLTFGGGTKVEIK
>d1vgeh1 2.1.1.1.65 (1-122) Immunoglobulin (variable domains of L and H chains) [Fab TR1.9 (mouse/human), kappa L chain]
QVKLLEQSGAEVKKPGASVKVSCKASGYSFTSYGLHWVRQAPGQRLEWMGWISAGTGNTKYSQKFRGRVTFTRDTSATTAYMGLSSLRPEDTAVYYCARDPYGGGKSEFDYWGQGTLVTVSS
>d1yuhh1 2.1.1.1.66 (1-118) Immunoglobulin (variable domains of L and H chains) [Fab anti-nitrophenol (mouse), lambda L chain]
QVQFQQSGAELVKPGASVKLSCKASGYTFTSYLMHWIKQRPGRGLEWIGRIDPNNVVTKFNEKFKSKATLTVDKPSSTAYMELSSLTSEDSAVYYCARYAYCRPMDYWGQGTTVTVSS
>d1clyl1 2.1.1.1.67 (1-111) Immunoglobulin (variable domains of L and H chains) [Fab CBR96 (mouse/human), kappa L chain]
LMTQIPVSLPVSLGDQASISCRSSQIIVHNNGNTYLEWYLQKPGQSPQLLIYKVSNRFSGVPDRFSGSGSGTDFTLKISRVEAEDLGVYYCFQGSHVPFTFGSGTKLEIKR
>d1clyh1 2.1.1.1.67 (1-119) Immunoglobulin (variable domains of L and H chains) [Fab CBR96 (mouse/human), kappa L chain]
EVNLVESGGGLVQPGGSLKVSCVTSGFTFSDYYMYWVRQTPEKRLEWVAYISQGGDITDYPDTVKGRFTISRDNAKNSLYLQMSRLKSEDTAMYYCARGLDDGAWFAYWGQGTLVTVSV
>d1clzh1 2.1.1.1.68 (1-119) Immunoglobulin (variable domains of L and H chains) [Fab MBR96 (mouse), kappa L chain]
EVNLVESGGGLVQPGGSLKVSCVTSGFTFSDYYMYWVRQTPEKRLEWVAYISQGGDITDYPDTVKGRFTISRDNAKNSLYLQMSRLKSEDTAMYYCARGLDDGAWFAYWGQGTLVTVSV
>d1dvfd_ 2.1.1.1.69 Immunoglobulin (variable domains of L and H chains) [Fv E5.2 (mouse), kappa L chain]
QVQLQQSGTELVKSGASVKLSCTASGFNIKDTHMNWVKQRPEQGLEWIGRIDPANGNIQYDPKFRGKATITADTSSNTAYLQLSSLTSEDTAVYYCATKVIYYQGRGAMDYWGQGTTLTVS
>d1dvfc_ 2.1.1.1.69 Immunoglobulin (variable domains of L and H chains) [Fv E5.2 (mouse), kappa L chain]
DIQLTQSPSSLSASLGDRVTISCRASQDISNYLNWYQQKPDGTVKLLIYYTSRLHSGVPSRFSGSGSGTDYSLTISNLEQEDIATYFCQQGNTLPWTFGGGTKLEIK
>d1igtb1 2.1.1.1.7 (1-119) Immunoglobulin (variable domains of L and H chains) [Intact IgG2a antidody Mab231 (mouse), kappa L chain]
EVKLQESGGGLVQPGGSLKLSCATSGFTFSDYYMYWVRQTPEKRLEWVAYISNGGGSTYYPDTVKGRFTISRDNAKNTLYLQMSRLKSEDTAMYYCARHGGYYAMDYWGQGTTVTVSSA
>d1igta1 2.1.1.1.7 (1-108) Immunoglobulin (variable domains of L and H chains) [Intact IgG2a antidody Mab231 (mouse), kappa L chain]
DIVLTQSPSSLSASLGDTITITCHASQNINVWLSWYQQKPGNIPKLLIYKASNLHTGVPSRFSGSGSGTGFTLTISSLQPEDIATYYCQQGQSYPLTFGGGTKLEIKR
>d1ghfh1 2.1.1.1.70 (1-114) Immunoglobulin (variable domains of L and H chains) [Fab GH1002 (mouse), kappa L chain]
VQLQQSGPELKKPGETVKISCKLWYTFTDYGMNWVKQAPGKGLKWMGWIQTNTEEPTYGAEFKGRFAFSLETSAFTAYKQINNLKNEDMATYFCARVEAGFDYWAQGTTLTVSS
>d1nldh1 2.1.1.1.71 (1-112) Immunoglobulin (variable domains of L and H chains) [Fab1583, against an epitope of gp41 of HIV-1, (mouse), kappa L chain]
QVKLQQSGPGLVQPSQSLSITCTVSGFSLTCYGVHWVRQSPGKGLEWLGVIWSGGDTDYNAAFISRLSITKDNSKSQVFFKMNSLQPNDRAIYYCARRGGDFWGQGTTVTVS
>d1nldl1 2.1.1.1.71 (1-112) Immunoglobulin (variable domains of L and H chains) [Fab1583, against an epitope of gp41 of HIV-1, (mouse), kappa L chain]
DVVMTQTPLTLSVTIGQPASISCKSSQSLLDSDGKTYLNWLLQRPGQSPKRLIYLVSKLDSGVPDRFTGSGSGTDFTLKISRVEAEDLGVYYCWQGTHFPRTFGGGTKLEIK
>d1kelh1 2.1.1.1.72 (1-115) Immunoglobulin (variable domains of L and H chains) [Fab 28B4 (mouse), kappa L chain]
EVKLVESGGGLGQPGGSLRLSCATSGFTFTDYYFNWARQPPGKALEWLGFIRNKAKGYTTEYSASVKGRFTISRDNSQGILYLQMNTLRAEDSATYYCARWGSYAMDYWGQGTSV
>d1ospl1 2.1.1.1.73 (1-108) Immunoglobulin (variable domains of L and H chains) [Fab 184.1 (mouse), kappa L chain]
DIQMSQSSSSFSVSLGDRVTITCKASEDIYSRLAWYQQKPGNAPRLLISGATSLETWVPSRFSGSDSGKDYTLSITSLQTEDVATYFCQQYWSPPPTFGGGTKLEIKR
>d1osph1 2.1.1.1.73 (1-121) Immunoglobulin (variable domains of L and H chains) [Fab 184.1 (mouse), kappa L chain]
EVQLQESGPSLVKPSQTLSLTCSVTGEPITSGFWDWIRKFPGNKLEFMGYIRYGGGTYYNPSLKSPISITRDTSKNHYYLQLNSVVTEDTATYYCARSRDYYGSSGFAFWGEGTLVTVSAA
>d1clol1 2.1.1.1.74 (1-106) Immunoglobulin (variable domains of L and H chains) [Fab A5B7 (mouse), kappa L chain]
QTVLSQSPAILSASPGEKVTMTCRASSSVTYIHWYQQKPGSSPKSWIYATSNLASGVPARFSGSGSGTSYSLTISRVEAEDAATYYCQHWSSKPPTFGGGTKLEIK
>d1cloh1 2.1.1.1.74 (1-121) Immunoglobulin (variable domains of L and H chains) [Fab A5B7 (mouse), kappa L chain]
EVKLVESGGGLVQPGGSLRLSCATSGFTFTDYYMNWVRQPPGKALEWLGFIGNKANGYTTEYSASVKGRFTISRDKSQSILYLQMNTLRAEDSATYYCTRDRGLRFYFDYWGQGTTLTVSS
>d1mimh1 2.1.1.1.75 (1-115) Immunoglobulin (variable domains of L and H chains) [Fab CHI621 (mouse), kappa L chain]
QLQQSGTVLARPGASVKMSCKASGYSFTRYWMHWIKQRPGQGLEWIGAIYPGNSDTSYNQKFEGKAKLTAVTSASTAYMELSSLTHEDSAVYYCSRDYGYYFDFWGQGTTLTVSS
>d1miml1 2.1.1.1.75 (1-105) Immunoglobulin (variable domains of L and H chains) [Fab CHI621 (mouse), kappa L chain]
QIVSTQSPAIMSASPGEKVTMTCSASSSRSYMQWYQQKPGTSPKRWIYDTSKLASGVPARFSGSGSGTSYSLTISSMEAEDAATYYCHQRSSYTFGGGTKLEIKR
>d1afvl1 2.1.1.1.76 (1-112) Immunoglobulin (variable domains of L and H chains) [Fab 25.3 (mouse), kappa L chain]
DIVLTQSPASLAVSLGQRATISCRASESVDNYGISFMNWFQQKPGQPPKLLIYAASNLGSGVPARFSGSGSGTDFSLNIHPMEEEDTAMYFCQQSKEVPLTFGAGTKVELKR
>d1afvh1 2.1.1.1.76 (1-120) Immunoglobulin (variable domains of L and H chains) [Fab 25.3 (mouse), kappa L chain]
QVQLQQPGSVLVRPGASVKLSCKASGYTFTSSWIHWAKQRPGQGLEWIGEIHPNSGNTNYNEKFKGKATLTVDTSSSTAYVDLSSLTSEDSAVYYCARWRYGSPYYFDYWGQGTTLTVSS
>d1mpah1 2.1.1.1.77 (1-121) Immunoglobulin (variable domains of L and H chains) [Bactericidal Fab (mouse), kappa L chain]
EVNLQQSGTVLARPGASVRMSCKASGYSFTSYWLHWIKQRPGQGLEWIGGIYPGNRDTRYTQRFKDKAKLTAVTSANTAYMELSSLTNEDSAVYYCSIIYFDYADFIMDYWGQGTTVTVSS
>d1pskl1 2.1.1.1.78 (1-106) Immunoglobulin (variable domains of L and H chains) [Fab against a ganglioside (mouse), kappa L chain]
QIVLTQSPAIMSASPGEKVTITCSASSSVSNIHWFQQKPGTFPKLWIYSTSTLASGVPGRFSGSGSGTSYSLTISRMGAEDAATYYCQQRSGYPFTFGSGTKLEIK
>d1pskh1 2.1.1.1.78 (1-114) Immunoglobulin (variable domains of L and H chains) [Fab against a ganglioside (mouse), kappa L chain]
EVQLQQSGPELVKPGASVKISCKTSGYTFTKYTMHWVKQSHGKSLEWIGDINPNNGGTNYNQKFKGTATLTVHKSSTTAYMELRSLTSEDSAVYYCTSKSFDYWGQGTTLTVSS
>d1yecl1 2.1.1.1.79 (1-112) Immunoglobulin (variable domains of L and H chains) [Fab D2.3 (mouse), kappa L chain]
DIVMTQSPLTLSVTIGQPASISCKSSQSLLYSNGKTYLNWLLQRPGQSPKRLIHLVSKLDSGVPDRITGSGSGTDFTLKISRVEAADLGVYYCVQGTHFPYTFGGGTKLEIL
>d1yech1 2.1.1.1.79 (1-123) Immunoglobulin (variable domains of L and H chains) [Fab D2.3 (mouse), kappa L chain]
EMQLQQSGAELLRPGTSVKLSCKTSGYIFTSYWIHWVKQRSGQGLEWIARIYPGTGSTYYNEKFKGKATLTADKSSSTAYMQLSTLKSEDSAVYFCTRWGFIPVREDYVMDYWGQGTLVTVSS
>d8faba1 2.1.1.1.8 (1-103) Immunoglobulin (variable domains of L and H chains) [Fab HIL (human), lambda L chain]
ELTQPPSVSVSPGQTARITCSANALPNQYAYWYQQKPGRAPVMVIYKDTQRPSGIPQRFSSSTSGTTVTLTISGVQAEDEADYYCQAWDNSASIFGGGTKLTV
>d8fabb1 2.1.1.1.8 (1-121) Immunoglobulin (variable domains of L and H chains) [Fab HIL (human), lambda L chain]
AVKLVQAGGGVVQPGRSLRLSCIASGFTFSNYGMHWVRQAPGKGLEWVAVIWYNGSRTYYGDSVKGRFTISRDNSKRTLYMQMNSLRTEDTAVYYCARDPDILTAFSFDYWGQGVLVTVSS
>d1yeeh1 2.1.1.1.81 (1-123) Immunoglobulin (variable domains of L and H chains) [Fab D2.5 (mouse), kappa L chain]
EVKLQESGAELVRPGASVKLSCKTSGYIFTSYWIHWVKQRAAAGLEWIARIYPGTGSSYYNVKFKGKATLTADKSSSTAYMQLSSLKSDDSAVYFCVRWGFIPVREDYVLDYWGQGTLVTVSS
>d1cfvh_ 2.1.1.1.82 Immunoglobulin (variable domains of L and H chains) [Fv 4155 (mouse), kappa L chain]
QVQLQESGGGLVNLGGSMTLSCVASGFTFNTYYMSWVRQTPEKTLELVAAINSDGEPIYYPDTLKGRVTISRDNAKKTLYLQMSSLNFEDTALYYCARLNYAVYGMDYWGQGTTVTVSS
>d1cfvl_ 2.1.1.1.82 Immunoglobulin (variable domains of L and H chains) [Fv 4155 (mouse), kappa L chain]
DIELTQSPPSLPVSLGDQVSISCRSSQSLVSNNRRNYLHWYLQKPGQSPKLVIYKVSNRFSGVPDRFSGSGSGTDFTLKISRVAAEDLGLYFCSQSSHVPLTFGSGTKLEIKR
>d1vhp__ 2.1.1.1.83 Immunoglobulin (variable domains of L and H chains) [VH-P8 domain (human), camelised monomer]
EVQLVESGGGLVQPGGSLRLSCAASGFTFSSYAMSWVRQAPGKEREIVSAVSGSGGSTYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARLKKYAFDYWGQGTLVTVSS
>d1mela_ 2.1.1.1.84 Immunoglobulin (variable domains of L and H chains) [camel (Camelus dromedarius) single-domain VH antibody fragment]
VQLQASGGGSVQAGGSLRLSCAASGYTIGPYCMGWFRQAPGKEREGVAAINMGGGITYYADSVKGRFTISQDNAKNTVYLLMNSLEPEDTAIYYCAADSTIYASYYECGHGLSTGGYGYDSWGQGTQVTVSS
>d1hcv__ 2.1.1.1.85 Immunoglobulin (variable domains of L and H chains) [llama lama glama VH domain]
VQLQESGGGLVQAGGSLRLSCAASGRTGSTYDMGWFRQAPGKERESVAAINWDSARTYYASSVRGRFTISRDNAKKTVYLQMNSLKPEDTAVYTCGAGEGGTWDSWGQGTQVTVSS
>d1ivla_ 2.1.1.1.86 Immunoglobulin (variable domains of L and H chains) [VL domain (kappa) of antibody M29B, dimer (synthetic)]
DIELTQSPATLSVTPGNSVSISCRASQSIGNRLFWYQQKSHESPRLLIKYASQSISGIPSRFSGSGSGTDFTLSINSVETEDLAVYFCQQVSEWPFTFGGGTKLEIK
>d1reia_ 2.1.1.1.87 Immunoglobulin (variable domains of L and H chains) [Bence-Jones VL (kappa) dimer REI (human)]
DIQMTQSPSSLSASVGDRVTITCQASQDIIKYLNWYQQTPGKAPKLLIYEASNLQAGVPSRFSGSGSGTDYTFTISSLQPEDIATYYCQQYQSLPYTFGQGTKLQIT
>d2rhe__ 2.1.1.1.88 Immunoglobulin (variable domains of L and H chains) [Bence-Jones VL (lambda) dimer RHE (human)]
ESVLTQPPSASGTPGQRVTISCTGSATDIGSNSVIWYQQVPGKAPKLLIYYNDLLPSGVSDRFSASKSGTSASLAISGLESEDEADYYCAAWNDSLDEPGFGGGTKLTVLGQPK
>d1bjma_ 2.1.1.1.89 Immunoglobulin (variable domains of L and H chains) [Bence-Jones VL (lambda) dimer LOC (human)]
XSVLTQPPSASGTPGQRVTISCSGSSSNIGENSVTWYQHLSGTAPKLLIYEDNSRASGVSDRFSASKSGTSASLAISGLQPEDETDYYCAAWDDSLDVAVFGTGTKVTVLGQPKANPTVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADGSPVKAGVETTKPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS
>d7fabl1 2.1.1.1.9 (1-103) Immunoglobulin (variable domains of L and H chains) [Fab NEW (human), lambda L chain]
ASVLTQPPSVSGAPGQRVTISCTGSSSNIGAGHNVKWYQQLPGTAPKLLIFHNNARFSVSKSGTSATLAITGLQAEDEADYYCQSYDRSLRVFGGGTKLTVLR
>d7fabh1 2.1.1.1.9 (1-116) Immunoglobulin (variable domains of L and H chains) [Fab NEW (human), lambda L chain]
AVQLEQSGPGLVRPSQTLSLTCTVSGTSFDDYYWTWVRQPPGRGLEWIGYVFYTGTTLLDPSLRGRVTMLVNTSKNQFSLRLSSVTAADTAVYYCARNLIAGGIDVWGQGSLVTVS
>d1wtla_ 2.1.1.1.90 Immunoglobulin (variable domains of L and H chains) [Bence-Jones VL (kappa) dimer WAT (human)]
DIQMTQSPSSLSASVGDRVTITCRASQDITNYVNWFQQRPGQAPKVLIYGASILETGVPSRFSGSGSGTDFTFTISSLQPEDIATYYCQQYDTLPLTFGGGTKVDIKR
>d1brea_ 2.1.1.1.91 Immunoglobulin (variable domains of L and H chains) [Bence-Jones VL (kappa) dimer BRE (human)]
DIQMTQSPSSLSASVGDRVTITCQASQDISDYLIWYQQKLGKAPNLLIYDASTLETGVPSRFSGSGSGTEYTFTISSLQPEDIATYYCQQYDDLPYTFGQGTKVEIK
>d1lvd__ 2.1.1.1.92 Immunoglobulin (variable domains of L and H chains) [Bence-Jones VL (kappa) domain LEN (human)]
DIVMTQSPNSLAVSLGERATINCKSSQSVLYSSNSKNYLAWYQQKPGQPPKLLIYWASTRESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQYYSTPYSFGQGTKLEIK
>d1lila1 2.1.1.1.93 (1-107) Immunoglobulin (variable domains of L and H chains) [Bence-Jones lambda L chain dimer CLE (human)]
YEVTQPPSLSVSPGQTARITCSGEKLGDAYVCWYQQRPGQSPVVVIYQDNRRPSGIPERFSGSSSGNTATLTISGTQTLDEADYYCQVWDSNASVVFGGGTKLTVLG
>d1mcba1 2.1.1.1.95 (1-111) Immunoglobulin (variable domains of L and H chains) [Lambda L chain dimer MCG (human)]
PSALTQPPSASGSLGQSVTISCTGTSSDVGGYNYVSWYQQHAGKAPKVIIYEVNKRPSGVPDRFSGSKSGNTASLTVSGLQAEDEADYYCSSYEGSDNFVFGTGTKVTVLG
>d1mcww1 2.1.1.1.96 (1-111) Immunoglobulin (variable domains of L and H chains) [Heterologous L chain dimer MCG-WEIR hybrid (human)]
XSALTQPASVSGSPGQSITVSCAGHTSDVADSNSISWFQQHPDKAPKLLIYAVTFRPSGIPLRFSGSKSGNTASLTISGLLPDDEADYFCMSYLSDASFVFGSGTKVTVLR
>d1tcra1 2.1.1.1.97 (1-112) T-cell antigen receptor [Mouse (Mus musculus), alpha-chain]
QSVTQPDARVTVSEGASLQLRCKYSYSATPYLFWYVQYPRQGLQLLLKYYSGDPVVQGVNGFEAEFSKSNSSFHLRKASVHWSDSAVYFCAVSGFASALTFGSGTKVIVLPY
>d1ao7d_ 2.1.1.1.98 T-cell antigen receptor [human (Homo sapiens), alpha-chain]
KEVEQNSGPLSVPEGAIASLNCTYSDRGSQSFFWYRQYSGKSPELIMSIYSNGDKEDGRFTAQLNKASQYVSLLIRDSQPSDSATYLCAVTTDSWGKLQFGAGTQVVVTPDIQNP
>d1bec_1 2.1.1.1.99 (1-113) T-cell antigen receptor [Mouse (Mus musculus), beta-chain]
AVTQSPRNKVAVTGGKVTLSCQQTNNHNNMYWYRQDTGHGLRLIHYSYGAGSTEKGDIPDGYKASRPSQEQFSLILELATPSQTSVYFCASGGGRGSYAEQFFGPGTRLTVLE
>d1frua1 2.1.1.2.1 (179-269) Fc (IgG) receptor, alpha-3 domain and beta subunit [rat (Rattus norvegicus)]
KEPPSMRLKARPGNSGSSVLTCAAFSFYPPELKFRFLRNGLASGSGNCSTGPNGDGSFHAWSLLEVKRGDEHHYQCQVEHEGLAQPLTVDL
>d1frub1 2.1.1.2.1 Fc (IgG) receptor, alpha-3 domain and beta subunit [rat (Rattus norvegicus)]
IQKTPQIQVYSRHPPENGKPNFLNCYVSQFHPPQIEIELLKNGKKIPNIEMSDLSFSKDWSFYILAHTEFTPTETDVYACRVKHVTLKEPKTVTWDRDM
>d1hoca1 2.1.1.2.10 (182-272) Class I MHC, beta2-microglobulin and alpha-3 domain [mouse (Mus musculus) h-2d (B)]
TDSPKAHVTHHPRSKGEVTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTFQKWASVVVPLGKEQNYTCRVYHEGLPEPLTL
>d1mhca1 2.1.1.2.11 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain [mouse (Mus musculus) h2-m3]
ADPPKAHVAHHPRPKGDVTLRCWALGFYPADITLTWQKDEEDLTQDMELVETRPSGDGTFQKWAAVVVPSGEEQRYTCYVHHEGLTEPLALKWRS
>d1mhcb1 2.1.1.2.11 Class I MHC, beta2-microglobulin and alpha-3 domain [mouse (Mus musculus) h2-m3]
IQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKDWSFYILAHTEFTPTETDTYACRVKHDSMAEPKTVYWDRDM
>d1igta2 2.1.1.2.12 (109-214) Immunoglobulin (constant domains of L and H chains) [Intact IgG2a antidody Mab231 (mouse), kappa L chain]
ADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>d1igtb2 2.1.1.2.12 (120-223) Immunoglobulin (constant domains of L and H chains) [Intact IgG2a antidody Mab231 (mouse), kappa L chain]
KTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEPRGPTIK
>d1igtb3 2.1.1.2.12 (224-342) Immunoglobulin (constant domains of L and H chains) [Intact IgG2a antidody Mab231 (mouse), kappa L chain]
PCPPCKCPAPNLLGGPSVFIFPPKIKDVLMISLSPIVTCVVVDVSEDDPDVQISWFVNNVEVHTAQTQTHREDYNSTLRVVSALPIQHQDWMSGKEFKCKVNNKDLPAPIERTISKPKG
>d1igtb4 2.1.1.2.12 (343-444) Immunoglobulin (constant domains of L and H chains) [Intact IgG2a antidody Mab231 (mouse), kappa L chain]
SVRAPQVYVLPPPEEEMTKKQVTLTCMVTDFMPEDIYVEWTNNGKTELNYKNTEPVLDSDGSYFMYSKLRVEKKNWVERNSYSCSVVHEGLHNHHTTKSFSR
>d8fabb2 2.1.1.2.13 (122-214) Immunoglobulin (constant domains of L and H chains) [Fab HIL (human), lambda L chain]
ASTKGPSVFPLAPTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPK
>d8faba2 2.1.1.2.13 (104-206) Immunoglobulin (constant domains of L and H chains) [Fab HIL (human), lambda L chain]
LGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPIKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAP
>d7fabh2 2.1.1.2.14 (117-209) Immunoglobulin (constant domains of L and H chains) [Fab NEW (human), lambda L chain]
SASTKGPSVFPLAPTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEP
>d7fabl2 2.1.1.2.14 (104-204) Immunoglobulin (constant domains of L and H chains) [Fab NEW (human), lambda L chain]
QPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADGSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHKSYSCQVTHEGSTVEKTVAP
>d1bafl2 2.1.1.2.15 (109-214) Immunoglobulin (constant domains of L and H chains) [Fab ANO2 (mouse), kappa L chain]
ADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>d1bafh2 2.1.1.2.15 (116-217) Immunoglobulin (constant domains of L and H chains) [Fab ANO2 (mouse), kappa L chain]
AKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKIVPRDC
>d1bbdh2 2.1.1.2.16 (120-213) Immunoglobulin (constant domains of L and H chains) [Fab 8F5 (mouse), kappa L chain]
KTTAPSVYPLAPVCSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEPR
>d1bbdl2 2.1.1.2.16 (115-219) Immunoglobulin (constant domains of L and H chains) [Fab 8F5 (mouse), kappa L chain]
ADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNE
>d1bbjl2 2.1.1.2.17 (110-211) Immunoglobulin (constant domains of L and H chains) [Fab B72.3 (mouse/human chimera), kappa L chain]
DAAPTVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNR
>d1bbjh2 2.1.1.2.17 (116-212) Immunoglobulin (constant domains of L and H chains) [Fab B72.3 (mouse/human chimera), kappa L chain]
STKGPSVFPLAPCSRSTSESTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTKTYTCNVDHKPSNTKVDKRV
>d1hilb2 2.1.1.2.18 (120-214) Immunoglobulin (constant domains of L and H chains) [Fab 17/9 (mouse), kappa L chain]
AAKTTAPSVYPLAPVSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEPR
>d1hila2 2.1.1.2.18 (115-217) Immunoglobulin (constant domains of L and H chains) [Fab 17/9 (mouse), kappa L chain]
ADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNR
>d1dbbh2 2.1.1.2.19 (119-219) Immunoglobulin (constant domains of L and H chains) [Fab DB3 (mouse), kappa L chain]
SAKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKIVPR
>d1bmg__ 2.1.1.2.2 Class I MHC, beta2-microglobulin and alpha-3 domain [bovine (Bos taurus)]
IQRPPKIQVYSRHPPEDGKPNYLNCYVYGFHPPQIEIDLLKNGEKIKSEQSDLSFSKDWSFYLLSHAEFTPNSKDQYSCRVKHVTLEQPRIVKWDRDL
>d1dfbh2 2.1.1.2.20 (126-229) Immunoglobulin (constant domains of L and H chains) [Fab 3D6 (human), kappa L chain]
SASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC
>d1dfbl2 2.1.1.2.20 (106-212) Immunoglobulin (constant domains of L and H chains) [Fab 3D6 (human), kappa L chain]
RTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
>d1igfl2 2.1.1.2.21 (113-219) Immunoglobulin (constant domains of L and H chains) [Fab B13I2 (mouse), kappa L chain]
RADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>d1igfh2 2.1.1.2.21 (120-218) Immunoglobulin (constant domains of L and H chains) [Fab B13I2 (mouse), kappa L chain]
AKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKIVP
>d1igih2 2.1.1.2.22 (119-217) Immunoglobulin (constant domains of L and H chains) [Fab 26-10 (mouse), kappa L chain]
AKTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEP
>d1indl2 2.1.1.2.23 (109-211) Immunoglobulin (constant domains of L and H chains) [Fab Cha255 (mouse), lambda L chain]
GQPKSSPSVTLFPPSSEELETNKATLVCTIIDFYPGVVTVDWKVDGTPVTQGMETTQPSKQSNNKYMASSYLTLTAREWERHSSYSCQVTHEGHTVEKSLSRA
>d1faih2 2.1.1.2.24 (124-221) Immunoglobulin (constant domains of L and H chains) [Fab R19.9 (mouse), kappa L chain]
SAKTTPPSVYPLAPGCGDTTGSSVTLGCLVKGYFPESVTVTWNSGSLSSSVHTFPALLQSALYTMSSSVTVPSSTWPSQTVTCSVAHPASSTTVDKKL
>d2fb4l2 2.1.1.2.25 (112-216) Immunoglobulin (constant domains of L and H chains) [Fab KOL (human), lambda L chain]
QPKANPTVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADGSPVKAGVETTKPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS
>d2fb4h2 2.1.1.2.25 (128-229) Immunoglobulin (constant domains of L and H chains) [Fab KOL (human), lambda L chain]
STKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPQPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSC
>d2fbjh2 2.1.1.2.26 (119-220) Immunoglobulin (constant domains of L and H chains) [Fab J539 (mouse), kappa L chain]
ESARNPTIYPLTLPPALSSDPVIIGCLIHDYFPSGTMNVTWGKSGKDITTVNFPPALASGGRYTMSNQLTLPAVECPEGESVKCSVQHDSNPVQELDVNCSG
>d2fbjl2 2.1.1.2.26 (110-213) Immunoglobulin (constant domains of L and H chains) [Fab J539 (mouse), kappa L chain]
AAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>d2fgwh2 2.1.1.2.27 (117-220) Immunoglobulin (constant domains of L and H chains) [Fab H52 (synthetic, humanised version), kappa L chain]
ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCD
>d1mcph2 2.1.1.2.28 (122-222) Immunoglobulin (constant domains of L and H chains) [Fab MCPC603 (human), kappa L chain]
SESARNPTIYPLTLPPALSSDPVIIGCLIHDYFPSGTMNVTWGKSGKDITTVNFPPALASGGRYTMSNQLTLPAVECPEGESVKCSVQHDSNPVQELDVNC
>d1ggbl2 2.1.1.2.30 (112-215) Immunoglobulin (constant domains of L and H chains) [Fab 50.1 (mouse), kappa L chain]
RADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNR
>d1ggbh2 2.1.1.2.30 (115-215) Immunoglobulin (constant domains of L and H chains) [Fab 50.1 (mouse), kappa L chain]
SAKTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEPR
>d1acyh2 2.1.1.2.31 (121-221) Immunoglobulin (constant domains of L and H chains) [Fab 59.1 (mouse), kappa L chain]
SAKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKIVPR
>d1acyl2 2.1.1.2.31 (113-215) Immunoglobulin (constant domains of L and H chains) [Fab 59.1 (mouse), kappa L chain]
ADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNR
>d1mamh2 2.1.1.2.32 (120-217) Immunoglobulin (constant domains of L and H chains) [Fab Yst9.1 (mouse), kappa L chain]
AKTTPPSVYPLAPGCGDTTGSSVTLGCLVKGYFPESVTVTWNSGSLSSSVHTFPALLQSGLYTMSSSVTVPSSTWPSQTVTCSVAHPASSTTVDKKLE
>d1maml2 2.1.1.2.32 (109-214) Immunoglobulin (constant domains of L and H chains) [Fab Yst9.1 (mouse), kappa L chain]
ADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>d1mfel2 2.1.1.2.33 (112-211) Immunoglobulin (constant domains of L and H chains) [Fab SE155-4 (mouse), lambda L chain]
PKSSPSVTLFPPSSEELETNKATLVCTITDFYPGVVTVDWKVDGTPVTQGMETTQPSKQSNNKYMASSYLTLTARAWERHSSYSCQVTHEGHTVEKSLSR
>d1cbvh2 2.1.1.2.34 (123-219) Immunoglobulin (constant domains of L and H chains) [Fab BV04-01 (mouse), kappa L chain]
KTTPPSVYPLAPGCGDTTGSSVTLGCLVKGYFPESVTVTWNSGSLSSSVHTFPALLQSGLYTMSSSVTVPSSTWPSQTVTCSVAHPASSTTVDKKLE
>d1tetl2 2.1.1.2.35 (113-216) Immunoglobulin (constant domains of L and H chains) [Fab TE33 (mouse), kappa L chain]
RADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYEWHNSYTCEATHKTSTSPIVKSFNR
>d1teth2 2.1.1.2.35 (116-209) Immunoglobulin (constant domains of L and H chains) [Fab TE33 (mouse), kappa L chain]
SAKTTPPSVYPLAPSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKIVPR
>d1flrh2 2.1.1.2.36 (117-216) Immunoglobulin (constant domains of L and H chains) [Fab 4-4-20 (mouse), kappa L chain]
AKTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEPR
>d6fabh2 2.1.1.2.37 (122-222) Immunoglobulin (constant domains of L and H chains) [Fab 36-71 (mouse), kappa L chain]
AKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKIVPRD
>d6fabl2 2.1.1.2.37 (109-214) Immunoglobulin (constant domains of L and H chains) [Fab 36-71 (mouse), kappa L chain]
ADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>d1gigh2 2.1.1.2.38 (121-221) Immunoglobulin (constant domains of L and H chains) [Fab HC19 (mouse), lambda L chain]
SSAKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSTWPSETVTCNVAHPASSTKVDKKIVP
>d2cgrh2 2.1.1.2.39 (118-214) Immunoglobulin (constant domains of L and H chains) [Fab, anti-sweetener (mouse), kappa L chain]
KTTPPSVYPLAPGCGDTTGSSVTLGCLVKGYFPESVTVTWNSGSLSSSVHTFPALLQSGLYTMSSSVTVPSSTWPSQTVTCSVAHPASSTTVDKKLE
>d2cgrl2 2.1.1.2.39 (113-219) Immunoglobulin (constant domains of L and H chains) [Fab, anti-sweetener (mouse), kappa L chain]
RADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>d1figh2 2.1.1.2.40 (120-216) Immunoglobulin (constant domains of L and H chains) [Fab 1F7 (mouse), kappa L chain]
AKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSTWPSETVTCNVAHPASSTKVDKKI
>d1figl2 2.1.1.2.40 (109-215) Immunoglobulin (constant domains of L and H chains) [Fab 1F7 (mouse), kappa L chain]
RADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>d1frgh2 2.1.1.2.41 (120-220) Immunoglobulin (constant domains of L and H chains) [Fab 26/9 (mouse), kappa L chain]
AAKTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEPR
>d2iffl2 2.1.1.2.43 (107-212) Immunoglobulin (constant domains of L and H chains) [Fab HyHEL-5 (mouse), kappa L chain]
ADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>d2iffh2 2.1.1.2.43 (116-214) Immunoglobulin (constant domains of L and H chains) [Fab HyHEL-5 (mouse), kappa L chain]
AKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKIVP
>d3hfmh2 2.1.1.2.44 (114-215) Immunoglobulin (constant domains of L and H chains) [Fab HyHEL-10 (mouse), kappa L chain]
AKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKIVPRDC
>d1jell2 2.1.1.2.45 (114-217) Immunoglobulin (constant domains of L and H chains) [Fab JE142 (mouse), kappa L chain]
ADAAPTVSIFPPSSEQLTAGGASVVCFLNNFYPKDINVKWKIGDEARQGGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNAA
>d1jelh2 2.1.1.2.45 (119-215) Immunoglobulin (constant domains of L and H chains) [Fab JE142 (mouse), kappa L chain]
AATTPPSVYPLAPGSAAGTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQGDLYTLSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKI
>d1ncal2 2.1.1.2.46 (109-214) Immunoglobulin (constant domains of L and H chains) [Fab NC41 (mouse), kappa L chain]
ADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>d1ncah2 2.1.1.2.46 (121-221) Immunoglobulin (constant domains of L and H chains) [Fab NC41 (mouse), kappa L chain]
AKTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEPRG
>d1forh2 2.1.1.2.47 (121-219) Immunoglobulin (constant domains of L and H chains) [Fab 17-Ia (mouse), kappa L chain]
KTTAPSVYPLAPVCGGTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSGLYTLSSSVTVTSSTWPSQTITCNVAHPASSTKVDKKIEPR
>d1forl2 2.1.1.2.47 (108-210) Immunoglobulin (constant domains of L and H chains) [Fab 17-Ia (mouse), kappa L chain]
ADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNR
>d1knob2 2.1.1.2.48 (120-220) Immunoglobulin (constant domains of L and H chains) [Fab CNJ206 (mouse), kappa L chain]
AKTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEPRG
>d1knoa2 2.1.1.2.48 (109-214) Immunoglobulin (constant domains of L and H chains) [Fab CNJ206 (mouse), kappa L chain]
ADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>d1eapa2 2.1.1.2.49 (107-213) Immunoglobulin (constant domains of L and H chains) [Fab 17E8 (mouse), kappa L chain]
RADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERAQGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>d1eapb2 2.1.1.2.49 (120-216) Immunoglobulin (constant domains of L and H chains) [Fab 17E8 (mouse), kappa L chain]
AKTTPPSVYPLAPGCGDTTGSSVTLGCLVKGYFPESVTVTWNSGGLSSSVHTFPALLQSGLYTMSSSVTVPGGGWPSATVTCSVAHPASSTTVDKKL
>d1mrdh2 2.1.1.2.50 (115-208) Immunoglobulin (constant domains of L and H chains) [Fab Jel 103 (mouse), kappa L chain]
TTPPSVYPLAPGTTGSSVTLGCLVKGYFPESVTVTWNSGSLSSSVHTFPALLQSGLYTMSSSVTVPSSTWPSQTVTCSVAHPASSTTVDKKLEP
>d1mrdl2 2.1.1.2.50 (114-216) Immunoglobulin (constant domains of L and H chains) [Fab Jel 103 (mouse), kappa L chain]
ADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGKERQNGVLNSWTDQNSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNR
>d1fbih2 2.1.1.2.51 (122-221) Immunoglobulin (constant domains of L and H chains) [Fab F9.13.7 (mouse), kappa L chain]
SAKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKIVP
>d1rmfh2 2.1.1.2.52 (120-216) Immunoglobulin (constant domains of L and H chains) [Fab R6.5 (mouse), kappa L chain]
AKTTAPSVTPLAPVCGDTTGSSVTLGVLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKI
>d1fpth2 2.1.1.2.53 (121-220) Immunoglobulin (constant domains of L and H chains) [Fab C3(?), neutralizing type 1 poliovirus, (mouse), kapppa L chain]
AKTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEPR
>d1ikfl2 2.1.1.2.54 (108-214) Immunoglobulin (constant domains of L and H chains) [Fab, anti-cyclosporin A, (mouse), kappa L chain]
RADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRAAC
>d1igch2 2.1.1.2.55 (120-222) Immunoglobulin (constant domains of L and H chains) [Fab MoPC21 (mouse), kappa L chain]
SAKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKIVPRDC
>d1igcl2 2.1.1.2.55 (109-213) Immunoglobulin (constant domains of L and H chains) [Fab MoPC21 (mouse), kappa L chain]
ADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>d1ibgl2 2.1.1.2.56 (111-217) Immunoglobulin (constant domains of L and H chains) [Fab 40-50 (mouse), kappa L chain]
RADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>d1ibgh2 2.1.1.2.56 (121-217) Immunoglobulin (constant domains of L and H chains) [Fab 40-50 (mouse), kappa L chain]
AKTTPPSVYPLAPGCGDTTGSSVTSGCLVKGYFPEPVTVTWNSGSLSSSVHTFPALLQSGLYTMSSSVTVPSSTWPSQTVTCSVAHPASSTTVDKKL
>d1mlbb2 2.1.1.2.57 (119-218) Immunoglobulin (constant domains of L and H chains) [Fab D44.1 (mouse), kappa L chain]
TTPPSVFPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKIVPRDC
>d1opgh2 2.1.1.2.58 (126-227) Immunoglobulin (constant domains of L and H chains) [Fab OPG2 (mouse), kappa L chain]
AKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKIVPRDC
>d1opgl2 2.1.1.2.58 (108-214) Immunoglobulin (constant domains of L and H chains) [Fab OPG2 (mouse), kappa L chain]
RADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>d1nsnh2 2.1.1.2.59 (115-210) Immunoglobulin (constant domains of L and H chains) [Fab N10 (mouse), kappa L chain]
KTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKI
>d1nsnl2 2.1.1.2.59 (112-217) Immunoglobulin (constant domains of L and H chains) [Fab N10 (mouse), kappa L chain]
RADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNE
>d1hsaa1 2.1.1.2.6 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain [human (Homo sapiens) hla-b2705]
ADPPKTHVTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDRTFQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEP
>d1iaih2 2.1.1.2.60 (122-219) Immunoglobulin (constant domains of L and H chains) [Fab 730.1.4 (mouse), kappa L chain]
AKTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTTPSQSITCNVAHPASSTKVDKKID
>d1iail2 2.1.1.2.60 (109-214) Immunoglobulin (constant domains of L and H chains) [Fab 730.1.4 (mouse), kappa L chain]
ADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>d1iaim2 2.1.1.2.61 (110-215) Immunoglobulin (constant domains of L and H chains) [Fab 409.5.3 (mouse), kappa L chain]
ADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>d1iaii2 2.1.1.2.61 (122-218) Immunoglobulin (constant domains of L and H chains) [Fab 409.5.3 (mouse), kappa L chain]
AKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSTWRPSETVTCNVAHPASSTKVDKKI
>d1plgh2 2.1.1.2.62 (118-215) Immunoglobulin (constant domains of L and H chains) [Polysialic acid-binding Fab (mouse), kappa L chain]
AKTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIE
>d1gafh2 2.1.1.2.63 (115-217) Immunoglobulin (constant domains of L and H chains) [Fab 48G7 (mouse/human), kappa L chain]
ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC
>d1gafl2 2.1.1.2.63 (110-214) Immunoglobulin (constant domains of L and H chains) [Fab 48G7 (mouse/human), kappa L chain]
VAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
>d1ngph2 2.1.1.2.64 (121-215) Immunoglobulin (constant domains of L and H chains) [Fab N1G9 (mouse/human), kappa L chain]
AKTTPPSVYPLAPGSSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSPWPSETVTCNVAHPASSTKVDKKIVPR
>d1vgeh2 2.1.1.2.65 (123-225) Immunoglobulin (constant domains of L and H chains) [Fab TR1.9 (mouse/human), kappa L chain]
ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC
>d1vgel2 2.1.1.2.65 (108-214) Immunoglobulin (constant domains of L and H chains) [Fab TR1.9 (mouse/human), kappa L chain]
RTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
>d1yuhh2 2.1.1.2.66 (119-218) Immunoglobulin (constant domains of L and H chains) [Fab anti-nitrophenol (mouse/human), lambda L chain]
AATTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGALSSGVHTFPAVLQSDLYTLSSSVTVPASTWPSGTVTCNVAHPASSTAVDKKIVPR
>d1clyh2 2.1.1.2.67 (120-219) Immunoglobulin (constant domains of L and H chains) [Fab CBR96 (mouse/human), kappa L chain]
ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPQPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEP
>d1clyl2 2.1.1.2.67 (112-217) Immunoglobulin (constant domains of L and H chains) [Fab CBR96 (mouse/human), kappa L chain]
TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
>d1clzh2 2.1.1.2.68 (120-218) Immunoglobulin (constant domains of L and H chains) [Fab MBR96 (mouse), kappa L chain]
TTTAPSVYPLVPGCSDTSGSSVTLGCLVKGYFPEPVTVKWNYGALSSGVRTVSSVLQSGFYSLSSLVTVPSSTWPSQTVICNVAHPASKTELIKRIEPR
>d1ghfh2 2.1.1.2.69 (115-212) Immunoglobulin (constant domains of L and H chains) [Fab GH1002 (mouse), kappa L chain]
AKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKII
>d1hsba1 2.1.1.2.7 (182-270) Class I MHC, beta2-microglobulin and alpha-3 domain [human (Homo sapiens) hla-aw68]
TDAPKTHMTHHAVSDHEATLRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDGTFQKWVAVVVPSGQEQRYTCHVQHEGLPKPL
>d1hsbb1 2.1.1.2.7 Class I MHC, beta2-microglobulin and alpha-3 domain [human (Homo sapiens) hla-aw68]
IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
>d1nldh2 2.1.1.2.70 (113-215) Immunoglobulin (constant domains of L and H chains) [Fab1583, against an epitope of gp41 of HIV-1, (mouse), kappa L chain]
SASTTAPSVYPLAPVSGDQTNSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSPWPSETITCNVAHPASSTKVDKKIEPRGC
>d1nldl2 2.1.1.2.70 (113-219) Immunoglobulin (constant domains of L and H chains) [Fab1583, against an epitope of gp41 of HIV-1, (mouse), kappa L chain]
RADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>d1kelh2 2.1.1.2.71 (116-218) Immunoglobulin (constant domains of L and H chains) [Fab 28B4 (mouse), kappa L chain]
TVSSAKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKIVP
>d1osph2 2.1.1.2.72 (122-218) Immunoglobulin (constant domains of L and H chains) [Fab 184.1 (mouse), kappa L chain]
KTTPPSVYPLAPGCGDTTGSSVTLGCLVKGYFPESVTVTWNSGSLSSSVHTFPALLQSGLYTMSSSVTVPSSTWPSQTVTCSVAHPASSTTVDKKLE
>d1ospl2 2.1.1.2.72 (109-214) Immunoglobulin (constant domains of L and H chains) [Fab 184.1 (mouse), kappa L chain]
ADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>d1cloh2 2.1.1.2.73 (122-222) Immunoglobulin (constant domains of L and H chains) [Fab A5B7 (mouse), kappa L chain]
AKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKIVPRD
>d1clol2 2.1.1.2.73 (107-213) Immunoglobulin (constant domains of L and H chains) [Fab A5B7 (mouse), kappa L chain]
RADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>d1miml2 2.1.1.2.74 (106-210) Immunoglobulin (constant domains of L and H chains) [Fab CHI621 (mouse), kappa L chain]
TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGE
>d1mimh2 2.1.1.2.74 (116-215) Immunoglobulin (constant domains of L and H chains) [Fab CHI621 (mouse), kappa L chain]
ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEP
>d1afvl2 2.1.1.2.75 (113-217) Immunoglobulin (constant domains of L and H chains) [Fab 25.3 (mouse), kappa L chain]
ADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNE
>d1afvh2 2.1.1.2.75 (121-220) Immunoglobulin (constant domains of L and H chains) [Fab 25.3 (mouse), kappa L chain]
AKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSTWPSETVTCNVAHPASSTKVDKKIVPK
>d1mpah2 2.1.1.2.76 (122-225) Immunoglobulin (constant domains of L and H chains) [Bactericidal Fab (mouse), kappa L chain]
AKTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEPRGPTI
>d1pskl2 2.1.1.2.77 (107-213) Immunoglobulin (constant domains of L and H chains) [Fab against a ganglioside (mouse), kappa L chain]
RADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>d1pskh2 2.1.1.2.77 (115-198) Immunoglobulin (constant domains of L and H chains) [Fab against a ganglioside (mouse), kappa L chain]
AKTTAPSVYPLAPVAVTLGCLVKGYFPEPVTLTWNSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDK
>d1yecl2 2.1.1.2.78 (113-219) Immunoglobulin (constant domains of L and H chains) [Fab D2.3 (mouse), kappa L chain]
RGDAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>d1yech2 2.1.1.2.78 (124-222) Immunoglobulin (constant domains of L and H chains) [Fab D2.3 (mouse), kappa L chain]
AKTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEP
>d1agda1 2.1.1.2.8 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain [human hla-b0801]
ADPPKTHVTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDRTFQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEP
>d1yeeh2 2.1.1.2.80 (124-222) Immunoglobulin (constant domains of L and H chains) [Fab D2.5 (mouse), kappa L chain]
AKTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEP
>d1lila2 2.1.1.2.81 (108-212) Immunoglobulin (constant domains of L and H chains) [Bence-Jones lambda L chain dimer CLE (human)]
QPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS
>d1mcba2 2.1.1.2.83 (112-216) Immunoglobulin (constant domains of L and H chains) [Lambda L chain dimer MCG (human)]
QPKANPTVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADGSPVKAGVETTKPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS
>d1mcww2 2.1.1.2.84 (112-216) Immunoglobulin (constant domains of L and H chains) [Heterologous L chain dimer MCG-WEIR hybrid (human)]
QPKANPTVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADGSPVEAGVETTKPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS
>d1fc1a2 2.1.1.2.85 (105-206) Immunoglobulin (constant domains of L and H chains) [Fc (human) IgG1 class]
QPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSL
>d1fc1a1 2.1.1.2.85 (1-104) Immunoglobulin (constant domains of L and H chains) [Fc (human) IgG1 class]
PSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPQVKFNWYVDGVQVHNAKTKPREQQYNSTYRVVSVLTVLHQNWLDGKEYKCKVSNKALPAPIEKTISKAKG
>d1pfc__ 2.1.1.2.87 Immunoglobulin (constant domains of L and H chains) [Fc' (guinea pig)]
RTISKAKGPPRIPEVYLLPPPRNELSKKKVSLTCMITGFYPADINVEWDSSEPSDYKNTPPVFDTDGSFFLYSRLKVDTDAWNNGESFTCSVMHEALPNHVIQKSISRSPG
>d1tcra2 2.1.1.2.88 (113-202) T-cell antigen receptor [Mouse (Mus musculus), alpha-chain]
IQNPEPAVYALKDPRSQDSTLCLFTDFDSQINVPKTMESGTFITDATVLDMKAMDSKSNGAIAWSNQTSFTCQDIFKETNATYPSSDVPC
>d1bec_2 2.1.1.2.89 (114-238) T-cell antigen receptor [Mouse (Mus musculus), beta-chain]
DLRQVTPPKVSLFEPSKAEIANKQKATLVCLARGFFPDHVELSWWVNGKEVHSGVSTDPQAYKESNYSYCLSSRLRVSATFWHNPRNHFRCQVQFHGLSEEDKWPEGSPKPVTQNISAEAWGRAD
>d2mhaa1 2.1.1.2.9 (182-270) Class I MHC, beta2-microglobulin and alpha-3 domain [mouse (Mus musculus) h-2k (B)]
TDSPKAHVTHHSRPEDKVTLRCWALGFYPADITLTWQLNGEELIQDMELVETRPAGDGTFQKWASVVVPLGKEQYYTCHVYHQGLPEPL
>d1ao7e2 2.1.1.2.90 (116-209) T-cell antigen receptor [human (Homo sapiens), beta-chain]
LKNVFPPEVAVFLVCLATGFYPDHVELSWWVNGKEVHSGVSTDPQPLYALSSRLRVSATFWQNPRNHFRCQVQFYGLAKPVTQIVSAEAWGRAD
>d1cd1a1 2.1.1.2.91 (180-273) CD1, beta2-microglobulin and alpha-3 domain [Mouse (Mus musculus)]
QEKPVAWLSSVPSSAHGHRQLVCHVSGFYPKPVWVMWMRGDQEQQGTHRGDFLPNADETWYLQATLDVEAGEEAGLACRVKHSSLGGQDIILYW
>d1dlha1 2.1.1.2.92 (80-180) Class II MHC, C-terminal domains of alpha and beta chains [human hla-dr1]
ITNVPPEVTVLTNSPVELREPNVLICFIDKFTPPVVNVTWLRNGKPVTTGVSETVFLPREDHLFRKFHYLPFLPSTEDVYDCRVEHWGLDEPLLKHWEFDA
>d1dlhb1 2.1.1.2.92 (91-188) Class II MHC, C-terminal domains of alpha and beta chains [human hla-dr1]
RRVEPKVTVYPSKTQPLQHHNLLVCSVSGFYPGSIEVRWFRNGQEEKAGVVSTGLIQNGDWTFQTLVMLETVPRSGEVYTCQVEHPSVTSPLTVEWRA
>d1vcaa1 2.1.1.3.1 (91-199) The second domain of vascular cell adhesion molecule-1 (VCAM-1) [human (Homo sapiens)]
FPKDPEIHLSGPLEAGKPITVKCSVADVYPFDRLEIDLLKGDHLMKSQEFLEDADRKSLETKSLEVTFTPVIEDIGKVLVCRAKLHIDEMDSVPTVRQAVKELQVYISP
>d1zxq_1 2.1.1.3.2 (87-192) The second domain of intercellular cell adhesion molecule-2 (ICAM-2) [human (Homo sapiens)]
PPRQVILTLQPTLVAVGKSFTIECRVPTVEPLDSLTLFLFRGNETLHYETFGKAAPAPQEATATFNSTADREDGHRNFSCLAVLDLMSRGGNIFHKHSAPKMLEIY
>d3cd4_2 2.1.1.3.3 (98-178) CD4 [human (Homo sapiens)]
FGLTANSDTHLLQGQSLTLTLESPPGSSPSVQCRSPRGKNIQGGKTLSVSQLELQDSGTWTCTVLQNQKKVEFKIDIVVLA
>d1cid_2 2.1.1.3.4 (106-177) CD4 [rat (Rattus rattus)]
VMKVTQPDSNTLTCEVMGPTSPKMRLILKQENQEARVSRQEKVIQVQAPEAGVWQCLLSEGEEVKMDSKIQV
>d1hnf_2 2.1.1.3.5 (102-179) CD2 [human (Homo sapiens)]
RVSKPKISWTCINTTLTCEVMNGTDPELNLYQDGKHLKLSQRVITHKWTTSLSAKFKCTAGNKVSKESSVEPVSCPEK
>d1vcaa2 2.1.1.4.1 (1-90) N-terminal domain of vascular cell adhesion molecule-1 (VCAM-1) [human (Homo sapiens)]
FKIETTPESRYLAQIGDSVSLTCSTTGCESPFFSWRTQIDSPLNGKVTNEGTTSTLTMNPVSFGNEHSYLCTATCESRKLEKGIQVEIYS
>d1zxq_2 2.1.1.4.2 (1-86) N-terminal domain of intracellular adhesion molecule-2, ICAM-2 [human (Homo sapiens)]
KVFEVHVRPKKLAVEPKGSLEVNCSTTCNQPEVGGLETSLNKILLDEQAQWKHYLVSNISHDTVLQCHFTCSGKQESMNSNVSVYQ
>d1tlk__ 2.1.1.4.3 Telokin [turkey (Meleagris gallopavo)]
VAEEKPHVKPYFTKTILDMDVVEGSAARFDCKVEGYPDPEVMWFKDDNPVKESRHFQIDYDEEGNCSLTISEVCGDDDAKYTCKAVNSLGEATCTAELLVETM
>d2ncm__ 2.1.1.4.4 N-terminal domain of neural cell adhesion molecule (NCAM) [human (Homo sapiens)]
RVLQVDIVPSQGEISVGESKFFLCQVAGDAKDKDISWFSPNGEKLSPNQQRISVVWNDDDSSTLTIYNANIDDAGIYKCVVTAEDGTQSEATVNVKIFQ
>d1tnm__ 2.1.1.4.5 Titin [Human (Homo sapiens), module M5]
RILTKPRSMTVYEGESARFSCDTDGEPVPTVTWLRKGQVLSTSARHQVTTTKYKSTFEISSVQASDEGNYSVVVENSEGKQEAEFTLTIQK
>d1wiu__ 2.1.1.4.6 Twitchin [Nematode (Caenorhabditis elegans)]
LKPKILTASRKIKIKAGFTHNLEVDFIGAPDPTATWTVGDSGAALAPELLVDAKSSTTSIFFPSAKRADSGNYKLKVKNELGEDEAIFEVIVQ
>d1koa_1 2.1.1.4.6 (351-447) Twitchin [Nematode (Caenorhabditis elegans)]
QPRFIVKPYGTEVGEGQSANFYCRVIASSPPVVTWHKDDRELKQSVKYMKRYNGNDYGLTINRVKGDDKGEYTVRAKNSYGTKEEIVFLNVTRHSEP
>d1tiu__ 2.1.1.4.7 Twitchin [Human (Homo sapiens), Ig repeat 27]
LIEVEKPLYGVEVFVGETAHFEIELSEPDVHGQWKLKGQPLTASPDCEIIEDGKKHILILHNCQLGMTGEVSFQAANAKSAANLKVKEL
>d1gof_1 2.1.1.5.1 (538-639) Galactose oxidase, C-terminal domain [Dactylium dendroides]
GNLATRPKITRTSTQSVKVGGRITISTDSSISKASLIRYGTATHTVNTDQRRIPLTLTNNGGNSYSFQVPSDSGVALPGYWMLFVMNSAGVPSVASTIRVTQ
>d1clc_2 2.1.1.5.10 (1-100) CelD cellulase, N-terminal domain [Clostridium thermocellum]
IETKVSAAKITENYQFDSRIRLNSIGFIPNHSKKATIAANCSTFYVVKEDGTIVYTGTATSMFDNDTKETVYIADFSSVNEEGTYYLAVPGVGKSVNFKI
>d1ctn_1 2.1.1.5.11 (1-109) Chitinase A, N-terminal domain [Serratia marcescens]
AAPGKPTIAWGNTKFAIVEVDQAATAYNNLVKVKNAADVSVSWNLWNGDTGTTAKILLNGKEAWSGPSTGSSGTANFKVNKGGRYQMQVALCNADGCTASDATEIVVAD
>d1ggta1 2.1.1.5.12 (1-171) Transglutaminase factor XIII, N-terminal domain [Human (Homo sapiens) blood]
FGGRRAVPPNNSNAAEDDLPTVEEFLNVTSVHLFKERWDTNKVDHHTDKYENNKLIVRRGQSFYVQIDFSRPYDPRRDLFRVEYVIGRYPQENKGTYIPVPIVSELQSGKWGAKIVMREDRSVRLSIQSSPKCIVGKFRMYVAVWTPYGVLRTSRNPETDTYILFNPWCED
>d1ksr__ 2.1.1.5.14 The F-actin cross-linking gelation factor (ABP-120), one repeat (ROD 4) [slime mold (Dictyostelium discoideum)]
ADPEKSYAEGPGLDGGECFQPSKFKIHAVDPDGVHRTDGGDGFVVTIEGPAPVDPVMVDNGDGTYDVEFEPKEAGDYVINLTLDGDNVNGFPKTVTVKPA
>d1rhoa_ 2.1.1.5.15 Rho GDP-dissociation inhibitor 1, RhoGDI [human (Homo sapiens)]
VAVSADPNVPNVVVTGLTLVCSSAPGPLELDLTGDLESFKKQSFVLKEGVEYRIKISFRVNREIVSGKYIEHTYRKGVKIDKTDYVGSYGPRAEEYEFLTPVEEAPKGLARGSYSIKSRFTDDDKTDHLSWEWNLTIKKDWK
>d1svcp1 2.1.1.5.16 (209-311) p50 subunit of NF-kappa B transcription factor, C-terminal domain [human (Homo sapiens)]
LKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDINITKPASVFVQLRRKSDLETSEPKPFLYYPE
>d1qba_1 2.1.1.5.2 (754-858) Bacterial chitobiase, c-terminal domain [(Serratia marcescens)]
GETHFVDTQALEKDWLRFANILGQRELAKLDKGGVAYRLPVPGARVAGGKLEANIALPGLGIEYSTDGGKQWQRYDAKAKPAVSGEVQVRSVSPDGKRYSRAEKV
>d1svb_1 2.1.1.5.3 (304-395) Envelope glycoprotein, domain III (C-terminal) [Tick-borne encephalitis virus, (TBE)]
YTMCDKTKFTWKRAPTDSGHDTVVMEVTFSGTKPCRIPVRAVAHGSPDVNVAMLITPNPTIENNGGGFIEMQLPPGDNIIYVGELSHQWFQK
>d1cdg_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E [Bacillus circulans]
TATPTIGHVGPMMAKPGVTITIDGRGFGSSKGTVYFGTTAVSGADITSWEDTQIKVKIPAVAGGNYNIKVANAAGTASNVYDNFEV
>d1cgt_1 2.1.1.5.4 (495-579) Cyclodextrin glycosyltransferase, domain E [Bacillus circulans]
ETTPTIGHVGPVMGKPGNVVTIDGRGFGSTKGTVYFGTTAVTGAAITSWEDTQIKVTIPSVAAGNYAVKVAASGVNSNAYNNFTI
>d1cyg_1 2.1.1.5.5 (492-574) Cyclodextrin glycosyltransferase, domain E [Bacillus stearothermophylus]
ESTPIIGHVGPMMGQVGHQVTIDGEGFGTNTGTVKFGTTAANVVSWSNNQIVVAVPNVSPGKYNITVQSSSGQTSAAYDNFEV
>d1pama1 2.1.1.5.6 (497-582) Cyclodextrin glycosyltransferase, domain E [alkalophilic Bacillus sp. 1011]
TTPIIGNVGPMMAKPGVTITIDGRGFGSGKGTVYFGTTAVTGADIVAWEDTQIQVKIPAVPGGIYDIRVANAAGAASNIYDNFEVL
>d1ciu_1 2.1.1.5.7 (496-578) Cyclodextrin glycosyltransferase, domain E [Thermoanaerobacterium thermosulfurigenes EM1]
SNSPLIGHVGPTMTKAGQTITIDGRGFGTTSGQVLFGSTAGTIVSWDDTEVKVKVPSVTPGKYNISLKTSSGATSNTYNNINI
>d1lla_2 2.1.1.5.8 (360-600) Hemocyanin, C-terminal domain [Horseshoe crab(Limulus polyphemus) hemolymph]
PYDHDVLNFPDIQVQDVTLHARVDNVVHTFMREQELELKHGINPGNARSIKARYYHLDHEPFSYAVNVQNNSASDKHATVRIFLAPKYDELGNEIKADELRRTAIELDKFKTDLHPGKNTVVRHSLDSSVTLSHQPTFEDLLHGVGLSEYCSCGWPSHLLVPKGNIKGMEYHLFVMLTDWDKDKVSVACVDAVSYCGARDHKYPDKKPMGFPFDRPIHTEHISDFLTNNMFIKDIKIKFHE
>d1hc2_2 2.1.1.5.9 (391-634) Hemocyanin, C-terminal domain [spiny lobster (Panulirus interruptus)]
PPYTHDNLEFSGMVVNGVAIDGELITFFDEFQYSLINAVDSGENIEDVEINARVHRLNHNEFTYKITMSNNNDGERLATFRIFLCPIEDNNGITLTLDEARWFCIELDKFFQKVPSGPETIERSSKDSSVTVPDMPSFQSLKEQADNAVNGGLDLSAYERSCGIPDRMLLPKSKPEGMEFNLYVAVTDGDKDTEGHHAQCGVHGEAYPDNRPLGYPLERRIPDERVIDGVSNIKHVVVKIVHHL
>d2hft_2 2.1.2.1.1 (103-205) Extracellular region of human tissue factor [human (Homo sapiens)]
NLGQPTIQSFEQVGTKVNVTVEDERTLVRRNNTFLSLRDVFGKDLIYTLYYWKSSGKKTAKTNTNEFLIDVDKGENYCFSVQAVIPSRTVNRKSTDSPVECMG
>d2hft_1 2.1.2.1.1 (1-102) Extracellular region of human tissue factor [human (Homo sapiens)]
SGTTNTVAAYNLTWKSTNFKTILEWEPKPVNQVYTVQISTKSGDWKSKCFYTTDTECDLTDEIVKDVKQTYLARVFSYPAGNVESTEPLYENSPEFTPYLET
>d1fna__ 2.1.2.1.2 Fibronectin, fifferent Fn3 modules [human (Homo sapiens)]
GSLEVVAATPTSLLISWDAPAVTVRYYRITYGETGGNSPVQEFTVPGSKSTATISGLKPGVDYTITVYAVTGRGDSPASSKPISINYRTEI
>d1ten__ 2.1.2.1.3 Tenascin, a Fn3 repeat [human (Homo sapiens)]
LDAPSQIEVKDVTDTTALITWFKPLAEIDGIELTYGIKDVPGDRTTIDLTEDENQYSIGNLKPDTEYEVSLISRRGDMSSNPAKETFTT
>d1cfb_1 2.1.2.1.4 (1-100) Neuroglian, the two amino proximal Fn3 repeats [Drosophila melanogaster]
IVQDVPNAPKLTGITCQADKAEIHWEQQGDNRSPILHYTIQFNTSFTPASWDAAYEKVPNTDSSFVVQMSPWANYTFRVIAFNKIGASPPSAHSDSCTTQ
>d3hhrb2 2.1.2.1.5 (92-195) Growth hormone receptor [human (Homo sapiens)]
PDPPIALNWTLLNVSLTGIHADIQVRWEAPRNADIQKGWMVLEYELQYKEVNETKWKMMDPILTTSVPVYSLKVDKEYEVRVRSKQRNSGNYGEFSEVLYVTLP
>d3hhrb1 2.1.2.1.5 (1-91) Growth hormone receptor [human (Homo sapiens)]
EPKFTKCRSPERETFSCHWTDEVHGPIQLFYTRRNEWTQEWKECPDYVSAGENSCYFNSSFTSIWIPYCIKLTSNGGTVDEKCFSVDEIVQ
>d1ebpa_ 2.1.2.1.6 Erythropoietin (EPO) receptor [human homo sapiens]
KFESKAALLAARGPEELLCFTERLEDLVCFWEEAASAGVGPGNYSFSYQLEDEPWKLCRLHQAPTARGAVRFWCSLPTADTSSFVPLELRVTAASGAPRYHRVIHINEVVLLDAPVGLVARLADESGHVVLRWLPPPETPMTSHIRYEVDVSAGNGAGSVQRVEILEGRTECVLSNLRGRTRYTFAVRARMAEPSFGGFWSAWSEPVSLLT
>d1cto__ 2.1.2.1.8 Granulocyte colony-stimulating factor (GC-SF) receptor [mouse (Mus musculus)]
GSSLEPPMLQALDIGPDVVSHQPGCLWLSWKPWKPSEYMEQECELRYQPQLKGANWTLVFHLPSSKDQFELCGLHQAPVYTLQMRCIRSSLPGFWSPWSPGLQLRPTMK
>d1bgla2 2.1.3.1.1 (624-728) beta-Galactosidase, domains 2 and 4 [Escherichia coli]
FFQFRLSGQTIEVTSEYLFRHSDNELLHWMVALDGKPLASGEVPLDVAPQGKQLIELPELPQPESAGQLWLTVRVVQPNATAWSEAGHISAWQQWRLAENLSVTL
>d1bgla1 2.1.3.1.1 (218-331) beta-Galactosidase, domains 2 and 4 [Escherichia coli]
TQISDFHVATRFNDDFSRAVLEAEVQMCGELRDYLRVTVSLWQGETQVASGTAPFGGEIIDERGGYADRVTLRLNVENPKLWSAEIPNLYRAVVELHTADGTLIEAEACDVGFR
>d1bhga1 2.1.3.1.2 (205-307) beta-Glucuronidase [human (Homo sapiens)]
TYIDDITVTTSVEQDSGLVNYQISVKGSNLFKLEVRLLDAENKVVANGTGTQGQLKVPGVSLWWPYLMHERPAYLYSLEVQLTAQTSLGPVSDFYTLPVGIRT
>d1ggta3 2.1.4.1.1 (609-710) Coagulation factor XIII, two C-terminal domains [Human (Homo sapiens) blood]
TIPEIIIKVRGTQVVGSDMTVTVEFTNPLKETLRNVWVHLDGPGVTRPMKKMFREIRPNSTVQWEEVCRPWVSGHRKLIASMSSDSLRHVYGELDVQIQRRP
>d1ggta2 2.1.4.1.1 (497-608) Coagulation factor XIII, two C-terminal domains [Human (Homo sapiens) blood]
SNVDMDFEVENAVLGKDFKLSITFRNNSHNRYTITAYLSANITFYTGVPKAEFKKETFDVTLEPLSFKKEAVLIQAGEYMGQLLEQASLHFFVTARINETRDVLAKQKSTVL
>d1ncia_ 2.1.5.1.1 N-cadherin (uvomorulin), domain 1 [Mouse (Mus musculus)]
GSDWVIPPINLPENSRGPFPQELVRIRSGRDKNLSLRYSVTGPGADQPPTGIFIINPISGQLSVTKPLDRELIARFHLRAHAVDINGNQVENPIDIVINVID
>d1edha_ 2.1.5.1.2 E-CADHERIN DOMAINS 1 AND 2 [mouse (Mus musculus)]
VIPPISCPENEKGEFPKNLVQIKSNRDKETKVFYSITGQGADKPPVGVFIIERETGWLKVTQPLDREAIAKYILYSHAVSSNGEAVEDPMEIVITVTDQNDNRPEFTQEVFEGSVAEGAVPGTSVMKVSATDADDDVNTYNAAIAYTIVSQDPELPHKNMFTVNRDTGVISVLTSGLDRESYPTYTLVVQAADLQGEGLSTTAKAVITVKD
>d2mcm__ 2.1.6.1.1 Macromycin [Streptomyces macromomyceticus]
APGVTVTPATGLSNGQTVTVSATGLTPGTVYHVGQCAVVEPGVIGCDATTSTDVTADAAGKITAQLKVHSSFQAVVGADGTPWGTVNCKVVSCSAGLGSDSGEGAAQAITFA
>d1noa__ 2.1.6.1.2 Neocarzinostatin [Streptomyces carzinostaticis]
AAPTATVTPSSGLSDGTVVKVAGAGLQAGTAYDVGQCAWVDTGVLACNPADFSSVTADANGSASTSLTVRRSFEGFLFDGTRWGTVDCTTAACQVGLSDAAGNGPEGVAISFN
>d1acx__ 2.1.6.1.3 Actinoxantin [Actinomyces globisporus, number 1131]
APAFSVSPASGASDGQSVSVSVAAAGETYYIAQCAPVGGQDACNPATATSFTTDASGAASFSFTVRKSYAGQTPSGTPVGSVDCATDACNLGAGNSGLNLGHVALTFG
>d1akp__ 2.1.6.1.4 Kedarcidin (apo form) [Actimomycete strain L585-6]
ASAAVSVSPATGLADGATVTVSASGFATSTSATALQCAILADGRGACNVAEFHDFSLSGGEGTTSVVVRRSFTGYVMPDGPEVGAVDCDTAPGGCEIVVGGNTGEYGNAAISFG
>d1sxca_ 2.1.7.1.1 Cu,Zn superoxide dismutase, SOD [bovine (Bos taurus)]
ATKAVCVLKGDGPVQGTIHFEAKGDTVVVTGSITGLTEGDHGFHVHQFGDNTQGCTSAGPHFNPLSKKHGGPKDEERHVGDLGNVTADKNGVAIVDIVDPLISLSGEYSIIGRTMVVHEKPDDLGRGGNEESTKTGNAGSRLACGVIGIAK
>d1sosa_ 2.1.7.1.2 Cu,Zn superoxide dismutase, SOD [human (Homo sapiens)]
ATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERHVGDLGNVTADKDGVADVSIEDSVISLSGDHSIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
>d1xsoa_ 2.1.7.1.3 Cu,Zn superoxide dismutase, SOD [African clawed frog (Xenopus laevis)]
VKAVCVLAGSGDVKGVVHFEQQDEGAVSVEGKIEGLTDGLHGFHIHVFGDNTNGCMSAGSHFNPENKNHGAPGDTDRHVGDLGNVTAEGGVAQFKITDSLISLKGPNSIIGRTAVVHEKADDLGKGGNDESLKTGNAGGRLACGVIGYSP
>d1srda_ 2.1.7.1.4 Cu,Zn superoxide dismutase, SOD [spinach (Spinacea oleracea)]
ATKKAVAVLKGTSNVEGVVTLTQEDDGPTTVNVRISGLAPGKHGFHLHEFGDTTNGCMSTGPHFNPDKKTHGAPEDEVRHAGDLGNIVANTDGVAEATIVDNQIPLTGPNSVVGRALVVHELEDDLGKGGHELSPTTGNAGGRLACGVVGLTPV
>d1sdya_ 2.1.7.1.5 Cu,Zn superoxide dismutase, SOD [yeast (Saccharomyces cerevisiae)]
VQAVAVLKGDAGVSGVVKFEQASESEPTTVSYEIAGNSPNAERGFHIHEFGDATNGCVSAGPHFNPFKKTHGAPTDEVRHVGDMGNVKTDENGVAKGSFKDSLIKLIGPTSVVGRSVVIHAGQDDLGKGDTEESLKTGNAGPRPACGVIGLTN
>d1yaia_ 2.1.7.1.6 Cu,Zn superoxide dismutase, SOD [Photobacterium leiognathi]
QDLTVKMTDLQTGKPVGTIELSQNKYGVVFTPELADLTPGMHGFHIHQNGSCASSEKDGKVVLGGAAGGHYDPEHTNKHGFPWTDDNHKGDLPALFVSANGLATNPVLAPRLTLKELKGHAIMIHAGGDNHSDMPKALGGGGARVACGVIQ
>d3dpa_1 2.1.8.1.1 (1-119) Pilus chaperone PapD, N-domain [Escherichia coli]
AVSLDRTRAVFDGSEKSMTLDISNDNKQLPYLAQAWIENENQEKIITGPVIATPPVQRLDPGAKSMVRLSTTPDISKLPQDRESLFYFNLREIPPRSEKANVLQIALQTKIKLFYRPAA
>d1mspa_ 2.1.8.2.1 Major sperm protein, alpha isoform (recombinant), ph 4.6 [Pig roundworm (Ascaris suum)]
SVPPGDINTQPSQKIVFNAPYDDKHTYHIKITNAGGRRIGWAIKTTNMRRLSVDPPCGVLDPKEKVLMAVSCDTFNAATEDLNNDRITIEWTNTPDGAAKQFRREWFQGDGMVRRKNLPIEYNL
>d4kbpa1 2.1.9.1.1 (1-112) Purple acid phosphatase, N-terminal domain [Kidney bean (Phaseolus vulgaris)]
RDMPLDSDVFRVPPGYNAPQQVHITQGDLVGRAMIISWVTMDEPGSSAVRYWSEKNGRKRIAKGKMSTYRFFNYSSGFIHHTTIRKLKYNTKYYYEVGLRNTTRRFSFITPP
>d2sblb2 2.10.1.1.1 (1-124) Lipoxigenase, N-terminal domain [Soybean (Glycine max), isozyme L1]
KIKGTVVLMPKNELELNAFLGRSVSLQLISATKADAHGKGKVGKDTFLEGINLGAGESAFNIHFEWDGSMGIPGAFYIKNYMQVEFFLKSLTLEAITIRFVCNSWVYNTKLYKSVRIFFANHTY
>d1lnh_2 2.10.1.1.2 (1-128) Lipoxigenase, N-terminal domain [Soybean (Glycine max), isozyme L3]
GHKIKGTVVLMRKNVLDVNSVTSVTLDTLTAFLGRSVSLQLISATKADANGKGKLGKATFLEGIITSLPTLGAGQSAFKINFEWDDGSGIPGAFYIKNFMQTEFFLVSLTLEDIPNHGSIHFVCNSWI
>d1hpla1 2.10.2.1.1 (338-449) Pancreatic lipase, C-terminal domain [horse (Equus caballus)]
RWRYRVDVTLSGKKVTGHVLVSLFGNKGNSRQYEIFQGTLKPDNTYSNEFDSDVEVGDLEKVKFIWYNNVINLTLPKVGASKITVERNDGSVFNFCSEETVREDVLLTLTAC
>d1etha1 2.10.2.1.2 (337-448) Pancreatic lipase, C-terminal domain [pig (Sus scrofa)]
ARWRYKVSVTLSGKKVTGHILVSLFGNEGNSRQYEIYKGTLQPDNTHSDEFDSDVEVGDLQKVKFIWYNVINPTLPRVGASKITVERNDGKVYDFCSQETVREEVLLTLNPC
>d1lpbb1 2.10.2.1.3 (338-449) Pancreatic lipase, C-terminal domain [human (Homo sapience)]
RWRYKVSVTLSGKKVTGHILVSLFGNKGNSKQYEIFKGTLKPDSTHSNEFDSDVDVGDLQMVKFIWYNNVINPTLPRVGASKIIVETNVGKQFNFCSPETVREEVLLTLTPC
>d1gpl_1 2.10.2.1.4 (321-432) Pancreatic lipase, C-terminal domain [Guinea pig (Cavia porcellus)]
RWRYKVSVTLSGKKVTGHILVSLFGNKGNSKQYEIFKGTLKPDSTHSNEFDSDVDVGDLQMVKFIWYNNVINPTLPRVGASKIIVETNVGKQFNFCSPETVREEVLLTLTPC
>d1pgs_1 2.11.1.1.1 (1-137) Peptide:N-glycosidase F (PNGase F) [Flavobacterium meningosepticum]
DNTVNIKTFDKVKNAFGDGLSQSAEGTFTFPADVTTVKTIKMFIKNECPNKTCDEWDRYANVYVKNKTTGEWYEIGRFITPYWVGTEKLPRGLEIDVTDFKSLLSGNTELKIYTETWLAKGREYSVDFDIVYGTPDY
>d1pgs_2 2.11.1.1.1 (138-311) Peptide:N-glycosidase F (PNGase F) [Flavobacterium meningosepticum]
KYSAVVPVIQYNKSSIDGVPYGKAHTLGLKKNIQLPTNTEKAYLRTTISGWGHAKPYDAGSRGCAEWCFRTHTIAINNANTFQHQLGALGCSANPINNQSPGNWTPDRAGWCPGMAVPTRIDVLNNSLTGSTFSYEYKFQSWTNNGTNGDAFYAISSFVIAKSNTPISAPVVTN
>d1slua_ 2.12.1.1.1 Ecotin, trypsin inhibitor [Escherichia coli]
IAPYPQAEKGMKRQVIQLTPQEDESTLKVELLIGQTLEVDCNLHRLGGKLENKTLEGWGYDYYVFDKVSSPVSTMMHCPDKEKKFVTAYLGDAGMLRYNSKLPIVVYTPDNVDVKYRVWKAEEKIDNAVVR
>d1gof_2 2.13.1.1.1 (1-150) Galactose oxidase, N-terminal domain [Dactylium dendroides]
ASAPIGSAISRNNWAVTCDSAQSGNECNKAIDGNKDTFWHTFYGANGDPKPPHTYTIDMKTTQNVNGLSMLPRQDGNQNGWIGRHEVYLSSDGTNWGSPVASGSWFADSTTKYSNFETRPARYVRLVAITEANGQPWTSIAEINVFQASS
>d1dlc_1 2.13.1.2.1 (440-584) delta-Endotoxin, C-terminal domain [Bacillus thuringiensis tenebrionis, CRYIIIA (BT13)]
FFNMIDSKKITQLPLVKAYKLQSGASVVAGPRFTGGDIIQCTENGSAATIYVTPDVSYSQKYRARIHYASTSQITFTLSLDGAPFNQYYFDKTINKGDTLTYNSFNLASFSTPFELSGNNLQIGVTGLSAGDKVYIDKIEFIPVN
>d1ciy_1 2.13.1.2.2 (430-577) delta-Endotoxin, C-terminal domain [(Bacillus thuringiensis), CRYIA (A)]
NNIIPSSQITQIPLTKSTNLGSGTSVVKGPGFTGGDILRRTSPGQISTLRVNITAPLSQRYRVRIRYASTTNLQFHTSIDGRPINQGNFSATMSSGSNLQSGSFRTVGFTTPFNFSNGSSVFTLSAHVFNSGNEVYIDRIEFVPAEVT
>d1bgla3 2.13.1.3.1 (1-217) beta-Galactosidase [Escherichia coli]
ITDSLAVVLQRRDWENPGVTQLNRLAAHPPFASWRNSEEARTDRPSQQLRSLNGEWRFAWFPAPEAVPESWLECDLPEADTVVVPSNWQMHGYDAPIYTNVTYPITVNPPFVPTENPTGCYSLTFNVDESWLQEGQTRIIFDGVNSAFHLWCNGRWVGYGQDSRLPSEFDLSAFLRAGENRLAVMVLRWSDGSYLEDQDMWRMSGIFRDVSLLHKPT
>d1bhga2 2.13.1.3.2 (1-204) beta-Glucuronidase [human (Homo sapiens)]
GLQGGMLYPQESPSRECKELDGLWSFRADFSDNRRRGFEEQWYRRPLWESGPTVDMPVPSSFNDISQDWRLRHFVGWVWYEREVILPERWTQDLRTRVVLRIGSAHSYAIVWVNGVDTLEHEGGYLPFEADISNLVQVGPLPSRLRITIAINNTLTPTTLPPGTIQYLTDTSKYPKGYFVQNTYFDFFNYAGLQRSVLLYTTPT
>d1ulo__ 2.13.1.4.1 Cellulose-binding domain [Cellulomonas fimi]
ASPIGEGTFDDGPEGWVAYGTDGPLDTSTGALCVAVPAGSAQYGVGVVLNGVAIEEGTTYTLRYTATASTDVTVRALVGQNGAPYGTVLDTSPALTSEPRQVTETFTASATYPATPAADDPEGQIAFQLGGFSADAWTLCLDDVALDSEVEL
>d1bvp12 2.14.1.1.1 (121-254) Virus coat protein vp7 (BTV-10 vp7), central (top) domain [Bluetongue virus]
PARQPYGFFLETEETFQPGRWFMRAAQAVTAVVCGPDMIQVSLNAGARGDVQQIFQGRNDPMMIYLVWRRIENFAMAQGNSQQTQAGVTVSVGGVDMRAGRIIAWDGQAALHVHNPTQQNAMVQIQVVFYISMD
>d1ahsa_ 2.14.1.1.2 Virus coat protein vp7 (BTV-10 vp7), central (top) domain [African horse sickness virus]
TGPYAGAVEVQQSGRYYVPQGRTRGGYINSNIAEVCMDAGAAGQVNALLAPRRGDAVMIYFVWRPLRIFCDPQGASLESAPGTFVTVDGVNVAAGDVVAWNTIAPVNVGNPGARRSILQFEVLWYT
>d1hgea_ 2.14.1.2.1 Hemagglutinin, headpiece [influenza virus (Strain x-31)]
QDLPGNDNSTATLCLGHHAVPNGTLVKTITDDQIEVTNATELVQSSSTGKICNNPHRILDGIDCTLIDALLGDPHCDVFQNETWDLFVERSKAFSNCYPYDVPDYASLRSLVASSGTLEFITEGFTWTGVTQNGRSNACKRGPGSGFFSRLNWLTKSGSTYPVLNVTMPNNDNFDKLYIWGIHHPSTNQEQTSLYVQASGRVTVSTRRSQQTIIPNIGSRPWVRGLSSRISIYWTIVKPGDVLVINSNGNLIAPRGYFKMRTGKSSIMRSDAPIDTCISECITPNGSIPNDKPFQNVNKITYGACPKYVKQNTLKLATGMRNVPEKQT
>d1aol__ 2.15.1.1.1 F-MuLV receptor-binding domain [Friend murine leukemia virus, F-MuLV]
QVYNITWEVTNGDRETVWAISGNHPLWTWWPVLTPDLCMLALSGPPHWGLEYQAPYSSPPGPPCCSGSSGSSAGCSRDCDEPLTSLTPRCNTAWNRLKLDQVTHKSSEGFYVCPGSHRPREAKSCGGPDSFYCASWGCETTGRVYWKPSSSWDYITVDNNLTTSQAVQVCKDNKWCNPLAIQFTNAGKQVTSWTTGHYWGLRLYVSGRDPGLTFGIRLRYQNLGPRVP
>d1knb__ 2.16.1.1.1 Adenovirus type 5 fiber protein, knob domain [Adenovirus type 5]
NDKLTLWTTPAPSPNCRLNAEKDAKLTLVLTKCGSQILATVSVLAVKGSLAPISGTVQSAHLIIRFDENGVLLNNSFLDPEYWNFRNGDLTEGTAYTNAVGFMPNLSAYPKSHGKTAKSNIVSQVYLNGDKTKPVTLTITLNGTQETGDTTPSAYSMSFSWDWSGHNYINEIFATSSYTFSYIAQE
>d1aly__ 2.17.1.1.1 Extracellular domain of CD40 ligand [human (Homo sapiens)]
GDQNPQIAAHVISEASSKTTSVLQWAEKGYYTMSNNLVTLENGKQLTVKRQGLYYIYAQVTFCSNREASSQAPFIASLCLKSPGRFERILLRAANTHSSAKPCGQQSIHLGGVFELQPGASVFVNVTDPSQVSHGTGFTSFGLLKL
>d1tnfa_ 2.17.1.1.2 Tumor necrosis factor (TNF) [human (Homo sapiens)]
RTPSDKPVAHVVANPQAEGQLQWLNRRANALLANGVELRDNQLVVPSEGLYLIYSQVLFKGQGCPSTHVLLTHTISRIAVSYQTKVNLLSAIKSPCQRETPEGAEAKPWYEPIYLGGVFQLEKGDRLSAEINRPDYLLFAESGQVYFGIIAL
>d1tnra_ 2.17.1.1.2 Tumor necrosis factor (TNF) [human (Homo sapiens)]
KPAAHLIGDPSKQNSLLWRANTDRAFLQDGFSLSNNSLLVPTSGIYFVYSQVVFSGKAYSPKATSSPLYLAHEVQLFSSQYPFHVPLLSSQKMVYPGLQEPWLHSMYHGAAFQLTQGDQLSTHTDGIPHLVLSPSTVFFGAFAL
>d1thw__ 2.18.1.1.1 Thaumatin [ketemfe (Thaumatococcus daniellii benth)]
ATFEIVNRCSYTVWAAASKGDAALDAGGRQLNSGESWTINVEPGTKGGKIWARTDCYFDDSGSGICKTGDCGGLLRCKRFGRPPTTLAEFSLNQYGKDYIDISNIKGFNVPMDFSPTTRGCRGVRCAADIVGQCPAKLKAPGGGCNDACTVFQTSEYCCTTGKCGPTEYSRFFKRLCPDAFSYVLDKPTTVTCPGSSNYRVTFCPTA
>d2cna__ 2.19.1.1.1 Concanavalin A [jack bean (Canavalia ensiformis)]
ADTIVAVELDTYPNTDIGDPSYPHIGIDIKSVRSKKTAKWNMQDGKVGTAHIIYNSVDKRLSAVVSYPNADATSVSYDVDLNDVLPEWVRVGLSASTGLYKETNTILSWSFTSKLKSNSTHQTDALHFMFNQFSKDQKDLILQGDATTGTDGNLELTRVSSNGSPEGSSVGRALFYAPVHIWESSATVSAFEATFAFLIKSPDSHPADGIAFFISNIDSSIPSGSTGRLLGLFPDAN
>d1scs__ 2.19.1.1.1 Concanavalin A [jack bean (Canavalia ensiformis)]
ADTIVAVELDTYPNTDIGDPSYPHIGIDIKSVRSKKTAKWNMQNGKVGTAHIIYNSVDKRLSAVVSYPNADSATVSYDVDLDNVLPEWVRVGLSASTGLYKETNTILSWSFTSKLKSNSTHETNALHFMFNQFSKDQKDLILQGDATTGTDGNLELTRVSSNGSPQGSSVGRALFYAPVHIWESSAVVASFEATFTFLIKSPDSHPADGIAFFISNIDSSIPSGSTGRLLGLFPDAN
>d1fata_ 2.19.1.1.10 Phytohemagglutinin-L, PHA-L, also arcelin [Kidney bean (Phaseolus vulgaris)]
SNDIYFNFQRFNETNLILQRDASVSSSGQLRLTNLNNGEPRVGSLGRAFYSAPIQIWDNTTGTVASFATSFTFNIQVPNNAGPADGLAFALVPVGSQPKDKGGFLGLFDGSNSNFHTVAVEFDTLYNKDWDPTERHIGIDVNSIRSIKTTRWDFVNGENAEVLITYDSSTNLLVASLVYPSQKTSFIVSDTVDLKSVLPEWVSVGFSATTGINKGNVETNDVLSWSFASKLS
>d1ioaa_ 2.19.1.1.11 Phytohemagglutinin-L, PHA-L, also arcelin [Kidney bean (Phaseolus vulgaris) G02771, arcelin-5a]
ATETSFNFPNFHTDDKLILQGNATISSKGQLQLTGVGSNELPRVDSLGRAFYSDPIQIKDSNNVASFNTNFTFIIRAKNQSISAYGLAFALVPVNSPPQKKQEFLGIFNTNNPEPNARTVAVVFNTFKNRIDFDKNFIKPYVNENCDFHKYNGEKTDVQITYDSSNNDLRVFLHFTVSQVKCSVSATVHLEKEVDEWVSVGFSPTSGLTEDTTETHDVLSWSFSSKFR
>d2ltn.1 2.19.1.1.2 (a,b) Lectin [garden pea (Pisum sativum)]
TETTSFLITKFSPDQQNLIFQGDGYTTKEKLTLTKAVKNTVGRALYSSPIHIWDRETGNVANFVTSFTFVINAPNSYNVADGFTFFIAPVDTKPQTGGGYLGVFNSAEYDKTTQTVAVEFDTFYNAAWDPSNRDRHIGIDVNSIKSVNTKSWKLQNGEEANVVIAFNAATNVLTVSLTYPNTETTSFLITKFSPDQQNLIFQGDGYTTKEKLTLTKAVKNTVGRALYSSPIHIWDRETGNVANFVTSFTFVINAPNSYNVADGFTFFIAPVDTKPQTGGGYLGVFNSAEYDKTTQTVAVEFDTFYNAAWDPSNRDRHIGIDVNSIKSVNTKSWKLQNGEEANVVIAFNAATNVLTVSLTYPN
>d1lesb_ 2.19.1.1.3 Lectin [common lentil (Lens culinaris)]
VTSYTLNEVVPLKDVVPEWVRIGFSATTGAEFAAHEVHSWSFHSQLG
>d1lesa_ 2.19.1.1.3 Lectin [common lentil (Lens culinaris)]
TETTSFSITKFSPDQQNLIFQGDGYTTKGKLTLTKAVKSTVGRALYSTPIHIWDRDTGNVANFVTSFTFVIDAPSSYNVADGFTFFIAPVDTKPQTGGGYLGVFNSKEYDKTSQTVAVEFDTFYNAAWDPSNKERHIGIDVNSIKSVNTKSWNLQNGERANVVIAFNAATNVLTVTLTYPN
>d1lec__ 2.19.1.1.4 Lectin [the west-central african legume (Griffonia simplicifolia)]
XNTVNFTYPDFWSYSLKNGTEITFLGDATRIPGALQLTKTDANGNPVRSSAGQASYSEPVFLWDSTGKAASFYTSFTFLLKNYGAPTADGLAFFLAPVDSSVKDYGGFLGLFRHETAADPSKNQVVAVEFDTWINKDWNDPPYPHIGIDVNSIVSVATTRWENDDAYGSSIATAHITYDARSKILTVLLSYEHGRDYILSHVVDLAKVLPQKVRIGFSAGVGYDEVTYILSWHFFSTLDGTNK
>d1lte__ 2.19.1.1.5 Lectin [coral tree (Erythrina corallodendron)]
VETISFSFSEFEPGNDNLTLQGASLITQSGVLQLTKINQNGMPAWDSTGRTLYAKPVHIWDMTTGTVASFETRFSFSIEQPYTRPLPADGLVFFMGPTKSKPAQGYGYLGIFNQSKQDNSYQTLGVEFDTFSNPWDPPQVPHIGIDVNSIRSIKTQPFQLDNGQVANVVIKYDASSKLLHAVLVYPSSGAIYTIAEIVDVKQVLPEWVDVGLSGATGAQRDAAETHDVYSWSFQASLPE
>d1loe.1 2.19.1.1.6 (a,b) Lectin [Isolectin I from Lathyrus ochrus]
TETTSFSITKFGPDQQNLIFQGDGYTTKERLTLTKAVRNTVGRALYSSPIHIWDSKTGNVANFVTSFTFVIDAPNSYNVADGFTFFIAPVDTKPQTGGGYLGVFNSKDYDKTSQTVAVEFDTFYNTAWDPSNGDRHIGIDVNSIKSINTKSWALQNGKEANVVIAFNAATNVLTVSLTYPTETTSFSITKFGPDQQNLIFQGDGYTTKERLTLTKAVRNTVGRALYSSPIHIWDSKTGNVANFVTSFTFVIDAPNSYNVADGFTFFIAPVDTKPQTGGGYLGVFNSKDYDKTSQTVAVEFDTFYNTAWDPSNGDRHIGIDVNSIKSINTKSWALQNGKEANVVIAFNAATNVLTVSLTYP
>d2pela_ 2.19.1.1.8 Lectin [peanut (Arachis hypogaea)]
AETVSFNFNSFSEGNPAINFQGDVTVLSNGNIQLTNLNKVNSVGRVLYAMPVRIWSSATGNVASFLTSFSFEMKDIKDYDPADGIIFFIAPEDTQIPAGSIGGGTLGVSDTKGAGHFVGVEFDTYSNSEYNDPPTDHVGIDVNSVDSVKTVPWNSVSGAVVKVTVIYDSSTKTLSVAVTNDNGDITTIAQVVDLKAKLPERVKFGFSASGSLGGRQIHLIRSWSFTSTLITT
>d1sba__ 2.19.1.1.9 Lectin [Soybean (Glycine max)]
AETVSFSWNKFVPKQPNMILQGDAIVTSSGKLQLNKVDENGTPKPSSLGRALYSTPIHIWDKETGSVASFAASFNFTFYAPDTKRLADGLAFFLAPIDTKPQTHAGYLGLFNENESGDQVVAVEFDTFRNSWDPPNPHIGINVNSIRSIKTTSWDLANNKVAKVLITYDASTSLLVASLVYPSQRTSNILSDVVDLKTSLPEWVRIGFSAATGLDIPGESHDVLSWSFASNLPH
>d1gbg__ 2.19.1.2.1 Bacillus 1-3,1-4-beta-glucanase [Bacillus licheniformis]
QTGGSFYEPFNNYNTGLWQKADGYSNGNMFNCTWRANNVSMTSLGEMRLSLTSPSYNKFDCGENRSVQTYGYGLYEVNMKPAKNVGIVSSFFTYTGPTDGTPWDEIDIEFLGKDTTKVQFNYYTNGVGNHEKIVNLGFDAANSYHTYAFDWQPNSIKWYVDGQLKHTATTQIPQTPGKIMMNLWNGAGVDEWLGSYNGVTPLYAHYNWVRYTKR
>d1cpn__ 2.19.1.2.3 Bacillus 1-3,1-4-beta-glucanase [Bacillus macerans]
FDCAEYRSTNIYGYGLYEVSMKPAKNTGIVSSFFTYTGPAHGTQWDEIDIEFLGKDTTKVQFNYYTNGVGGHEKVISLGFDASKGFHTYAFDWQPGYIKWYVDGVLKHTATANIPSTPGKIMMNLWNGTGVDDWLGSYNGANPLYAEYDWVKYTSNGSVFWEPKSYFNPSTWEKADGYSNGGVFNCTWRANNVNFTNDGKLKLGLTSS
>d1slaa_ 2.19.1.3.1 S-lectin (galectin-1) [bovine (Bos taurus)]
ACGLVASNLNLKPGECLRVRGEVAADAKSFLLNLGKDDNNLCLHFNPRFNAHGDVNTIVCNSKDAGAWGAEQRESAFPFQPGSVVEVCISFNQTDLTIKLPDGYEFKFPNRLNLEAINYLSAGGDFKIKCVAFE
>d1hlca_ 2.19.1.3.2 S-lectin (galectin-1) [human (Homo sapiens)]
ELEVKNMDMKPGSTLKITGSIADGTDGFVINLGQGTDKLNLHFNPRFSESTIVCNSLDGSNWGQEQREDHLCFSPGSEVKFTVTFESDKFKVKLPDGHELTFPNRLGHSHLSYLSVRGGFNMSSFKLKE
>d1gana_ 2.19.1.3.3 S-lectin (galectin-1) [toad (Bufo arenarum)]
ASAGVAVTNLNLKPGHCVEIKGSIPPDCKGFAVNLGEDASNFLLHFNARFDLHGDVNKIVCNSKEADAWGSEQREGVFPFQQGAEVMVCFEYQTDKIIIKFSSGDQFSFPVRKVLPSIPFLSLEGLQFKSITTE
>d1lcl__ 2.19.1.3.4 Charcot-Leyden crystal (CLC) protein [human (Homo sapiens)]
SLLPVPYTEAASLSTGSTVTIKGRPLVCFLNEPYLQVDFHTEMKEESDIVFHFQVCFGRRVVMNSREYGAWKQQVESKNMPFQDGQEFELSISVLPDKYQVMVNGQSSYTFDHRIKPEAVKMVQVWRDISLTKFNVSYLKR
>d1saca_ 2.19.1.4.1 Serum amyloid P component (SAP) [human (Homo sapiens)]
HTDLSGKVFVFPRESVTDHVNLITPLEKPLQNFTLCFRAYSDLSRAYSLFSYNTQGRDNELLVYKERVGEYSLYIGRHKVTSKVIEKFPAPVHICVSWESSSGIAEFWINGTPLVKKGLRQGYFVEAQPKIVLGQEQDSYGGKFDRSQSFVGEIGDLYMWDSVLPPENILSAYQGTPLPANILDWQALNYEIRGYVIIKPLVWV
>d1gnha_ 2.19.1.4.2 C-reactive protein (CRP) [Human (Homo sapiens)]
QTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFYTELSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGSEILFEVPEVTVAPVHICTSWESASGIVEFWVDGKPRVRKSLKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVNMWDFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFTKPQLWP
>d1kit_1 2.19.1.6.1 (1-192) Vibrio cholerae sialidase, N-terminal and insertion domains [Vibrio cholerae]
ALFDYNATGDTEFDSPAKQGWMQDNTNNGSGVLTNADGMPAWLVQGIGGRAQWTYSLSTNQHAQASSFGWRMTTEMKVLSGGMITNYYANGTQRVLPIISLDSSGNLVVEFEGQTGRTVLATGTAATEYHKFELVFLPGSNPSASFYFDGKLIRDNIQPTASKQNMIVWGNGSSNTDGVAAYRDIKFEIQGD
>d1kit_2 2.19.1.6.1 (323-519) Vibrio cholerae sialidase, N-terminal and insertion domains [Vibrio cholerae]
DVTDQVKERSFQIAGWGGSELYRRNTSLNSQQDWQSNAKIRIVDGAANQIQVADGSRKYVVTLSIDESGGLVANLNGVSAPIILQSEHAKVHSFHDYELQYSALNHTTTLFVDGQQITTWAGEVSQENNIQFGNADAQIDGRLHVQKIVLTQQGHNLVEFDAFYLAQQTPEVEKDLEKLGWTKIKTGNTMSLYGNAS
>d1cela_ 2.19.1.7.1 Cellobiohydrolase I (cellulase) [Trichoderma reesei]
XSACTLQSETHPPLTWQKCSSGGTCTQQTGSVVIDANWRWTHATNSSTNCYDGNTWSSTLCPDNETCAKNCCLDGAAYASTYGVTTSGNSLSIGFVTQSAQKNVGARLYLMASDTTYQEFTLLGNEFSFDVDVSQLPCGLNGALYFVSMDADGGVSKYPTNTAGAKYGTGYCDSQCPRDLKFINGQANVEGWEPSSNNANTGIGGHGSCCSEMDIWEANSISEALTPHPCTTVGQEICEGDGCGGTYSDNRYGGTCDPDGCDWNPYRLGNTSFYGPGSSFTLDTTKKLTVVTQFETSGAINRYYVQNGVTFQQPNAELGSYSGNELNDDYCTAEEAEFGGSSFSDKGGLTQFKKATSGGMVLVMSLWDDYYANMLWLDSTYPTNETSSTPGAVRGSCSTSSGVPAQVESQSPNAKVTFSNIKFGPIGSTGNPSG
>d1eg1a_ 2.19.1.7.2 Endoglucanase I [Trichoderma reesei]
QPGTSTPEVHPKLTTYKCTKSGGCVAQDTSVVLDWNYRWMHDANYNSCTVNGGVNTTLCPDEATCGKNCFIEGVDYAASGVTTSGSSLTMNQYMPSSSGGYSSVSPRLYLLDSDGEYVMLKLNGQELSFDVDLSALPCGENGSLYLSQMDENGGANQYNTAGANYGSGYCDAQCPVQTWRNGTLNTSHQGFCCNEMDILEGNSRANALTPHSCTATACDSAGCGFNPYGSGYKSYYGPGDTVDTSKTFTIITQFNTDNGSPSGNLVSITRKYQQNGVDIPSAQPGGDTISSCPSASAYGGLATMGKALSSGMVLVFSIWNDNSQYMNWLDSGNAGPCSSTEGNPSNILANNPNTHVVFSNIRWGDIGSTT
>d1xnb__ 2.19.1.8.1 Xylanase II [Bacillus circulans]
ASTDYWQNWTDGGGIVNAVNGSGGNYSVNWSNTGNFVVGKGWTTGSPFRTINYNAGVWAPNGNGYLTLYGWTRSPLIEYYVVDSWGTYRPTGTYKGTVKSDGGTYDIYTTTRYNAPSIDGDRTTFTQYWSVRQSKRPTGSNATITFTNHVNAWKSHGMNLGSNWAYQVMATEGYQSSGSSNVTVW
>d1xnd__ 2.19.1.8.2 Xylanase II [Trichoderma harzianum]
QTIGPGTGYSNGYYYSYWNDGHAGVTYTNGGGGSFTVNWSNSGNFVAGKGWQPGTKNKVINFSGSYNPNGNSYLSIYGWSRNPLIEYYIVENFGTYNPSTGATKLGEVTSDGSVYDIYRTQRVNQPSIIGTATFYQYWSVRRNHRSSGSVNTANHFNAWASHGLTLGTMDYQIVAVEGYFSSGSASITVS
>d1xyn__ 2.19.1.8.3 Xylanase II [Trichoderma reesei xynI]
ASINYDQNYQTGGQVSYSPSNTGFSVNWNTQDDFVVGVGWTTGSSAPINFGGSFSVNSGTGLLSVYGWSTNPLVEYYIMEDNHNYPAQGTVKGTVTSDGATYTIWENTRVNEPSIQGTATFNQYISVRNSPRTSGTVTVQNHFNAWASLGLHLGQMNYQVVAVEGWGGSGSASQSVSN
>d1enxa_ 2.19.1.8.4 Xylanase II [Trichoderma reesei xynII]
XTIQPGTGYNNGYFYSYWNDGHGGVTYTNGPGGQFSVNWSNSGNFVGGKGWQPGTKNKVINFSGSYNPNGNSYLSVYGWSRNPLIEYYIVENFGTYNPSTGATKLGEVTSDGSVYDIYRTQRVNQPSIIGTATFYQYWSVRRNHRSSGSVNTANHFNAWAQQGLTLGTMDYQIVAVEGYFSSGSASITVS
>d1yna__ 2.19.1.8.5 Xylanase II [Thermomyces lanuginosus]
TTPNSEGWHDGYYYSWWSDGGAQATYTNLEGGTYEISWGDGGNLVGGKGWNPGLNARAIHFEGVYQPNGNSYLAVYGWTRNPLVEYYIVENFGTYDPSSGATDLGTVECDGSIYRLGKTTRVNAPSIDGTQTFDQYWSVRQDKRTSGTVQTGCHFDAWARAGLNVNGDHYYQIVATEGYFSSGYARITVADVG
>d1ddt_1 2.2.1.1.1 (369-523) Diphtheria toxin, C-terminal domain [Corynebacterium diphtheriae]
SPGHKTQPFLHDGYAVSWNTVEDSIIRTGFQGESGHDIKITAENTPLPIAGVLLPTIPGKLDVNKSKTHISVNGRKIRMRCRAIDGDVTFCRPKSPVYVGNGVHANLHVAFHRSSSEKIHSNEISSDSIGVLGYQKTVDHTKVNSKLSLFFEIKS
>d1exg__ 2.2.2.1.1 Exo-1,4-beta-D-glycanase (cellulase, xylanase) [Cellumonas fimi]
ASSGPAGCQVLWGVNQWNTGFTANVTVKNTSSAPVDGWTLTFSFPSGQQVTQAWSSTVTQSGSAVTVRNAPWNGSIPAGGTAQFGFNGSHTGTNAAPTAFSLNGTPCTVG
>d1nbca_ 2.2.2.2.1 Cellusomal scaffolding protein A, scafoldin [Clostridium thermocellum]
NLKVEFYNSNPSDTTNSINPQFKVTNTGSSAIDLSKLTLRYYYTVDGQKDQTFWCDHAAIIGSNGSYNGITSNVKGTFVKMSSSTNNADTYLEISFTGGTLEPGAHVQIQGRFAKNDWSNYTQSNDYSFKSASQFVEWDQVTAYLNGVLVWGKEP
>d1tf4a2 2.2.2.2.2 (461-605) Endo/exocellulase:cellobiose E-4, C-terminal domain [Thermomonospora fusca]
PEIFVEAQINTPGTTFTEIKAMIRNQSGWPARMLDKGTFRYWFTLDEGVDPADITVSSAYNQCATPEDVHHVSGDLYYVEIDCTGEKIFPGGQSEHRREVQFRIAGGPGWDPSNDWSFQGIGNELAPAPYIVLYDDGVPVWGTAP
>d1anu__ 2.2.2.2.3 Cohesin-2 domain of the cellulosome [Clostridium thermocellum]
VVVEIGKVTGSVGTTVEIPVYFRGVPSKGIANCDFVFRYDPNVLEIIGIDPGDIIVDPNPTKSFDTAIYPDRKIIVFLFAEDSGTGAYAITKDGVFAKIRATVKSSAPGYITFDEVGGFADNDLVEQKVSFIDGGVNV
>d1qba_2 2.2.2.3.1 (1-173) Bacterial chitobiase, n-terminal domain [(Serratia marcescens)]
DQQLVDQLSQLKLNVKMLDNRAGENGVDCAALGADWASCNRVLFTLSNDGQAIDGKDWVIYFHSPRQTLRVDNDQFKIAHLTGDLYKLEPTAKFSGFPAGKAVEIPVVAEYWQLFRNDFLPRWYATSGDAKPKMLANTDTENLDQFVAPFTGDQWKRTKDDKNILMTPASRFV
>d1tupa_ 2.2.3.1.1 p53 tumor supressor, DNA-binding domain [Human (Homo sapiens)]
SSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENL
>d1nfa__ 2.2.3.1.2 Transcription factor NFATC, DNA-binding domain [human (Homo sapiens)]
MKDWQLPSHSGPYELRIEVQPKSHHRAHYETEGSRGAVKASAGGHPIVQLHGYLENEPLMLQLFIGTADDRLLRPHAFYQVHRITGKTVSTTSHEAILSNTKVLEIPLLPENSMRAVIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHVPQPSGRTLSLQVASNPIECSQRS
>d1svcp2 2.2.3.1.3 (1-208) p50 subunit of NF-kappa B (NFKB), N-terminal domain [human (Homo sapiens)]
PYLQILEQPKQRGFRFRYVAEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDGICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACIRGYNPGLLVHPDLAYLQAEGGGDRQLGDREKELIRQAALQQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSKAPNASN
>d1ctm_1 2.2.4.1.1 (1-167,231-250) Cytochrome f, large domain [turnip (Brassica rapa)]
YPIFAQQNYENPREATGRIVCANCHLASKPVDIEVPQAVLPDTVFEAVVKIPYDMQLKQVLANGKKGALNVGAVLILPEGFELAPPDRISPEMKEKIGNLSFQNYRPNKKNILVIGPVPGQKYSEITFPILAPDPATNKDVHFLKYPIYVGGNRGRGQIYPDGSKS
>d1bgla4 2.20.1.1.1 (729-1021) beta-Galactosidase, domain 5 [Escherichia coli]
PAASHAIPHLTTSEMDFCIELGNKRWQFNRQSGFLSQMWIGDKKQLLTPLRDQFTRAPLDNDIGVSEATRIDPNAWVERWKAAGHYQAEAALLQCTADTLADAVLITTAHAWQHQGKTLFISRKTYRIDGSGQMAITVDVEVASDTPHPARIGLNCQLAQVAERVNWLGLGPQENYPDRLTAACFDRWDLPLSDMYTPYVFPSENGLRCGTRELNYGPHQWRGDFQFNISRYSQQQLMETSHRHLLHAEEGTWLNIDGFHMGIGGDDSWSPSVSAEFQLSAGRYHYQLVWCQK
>d1oaca1 2.20.2.1.1 (297-719) Copper amine oxidase, domain 4 (catalytic) [Escherichia coli]
PAVKPMQIIEPEGKNYTITGDMIHWRNWDFHLSMNSRVGPMISTVTYNDNGTKRKVMYEGSLGGMIVPYGDPDIGWYFKAYLDSGDYGMGTLTSPIARGKDAPSNAVLLNETIADYTGVPMEIPRAIAVFERYAGPEYKHQEMGQPNVSTERRELVVRWISTVGNDYIFDWIFHENGTIGIDAGATGIEAVKGVKAKTMHDETAKDDTRYGTLIDHNIVGTTHQHIYNFRLDLDVDGENNSLVAMDPVVKPNTAGGPRTSTMQVNQYNIGNEQDAAQKFDPGTIRLLSNPNKENRMGNPVSYQIIPYAGGTHPVAKGAQFAPDEWIYHRLSFMDKQLWVTRYHPGERFPEGKYPNRSTHDTGLGQYSKDNESLDNTDAVVWMTTGTTHVARAEEWPIMPTEWVHTLLKPWNFFDETPTLGALK
>d1bia_2 2.21.1.1.1 (246-292) Biotin repressor/biotin holoenzyme synthetase, C-terminal domain [Escherichia coli]
FINRPVKLIIGDKEIFGISRGIDKQGALLLEQDGIIKPWMGGEISLR
>d1umua_ 2.21.1.2.1 UmuD' [Escherichia coli]
DYVEQRIDLNQLLIQHPSATYFVKASGDSIDGGISDGDLLIVDSAITASHGDIVIAAVDGEFTVKKLQLRPTVQLIPNSAYSPITISSEDTLDVFGVVIHVVK
>d1ckaa_ 2.21.2.1.1 C-Crk, N-terminal SH3 domain [mouse (Mus musculus)]
AEYVRALFDFNGNDEEDLPFKKGDILRIRDKPEEQWWNAEDSEGKRGMIPVPYVEKY
>d1sema_ 2.21.2.1.10 Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains [Caenorhabditis elegans SEM-5]
ETKFVQALFDFNPQESGELAFKRGDVITLINKDDPNWWEGQLNNRRGIFPSNYVCPYN
>d1hsq__ 2.21.2.1.11 Phospholipase C, SH3 domain [human (Homo sapiens)]
GSPTFKCAVKALFDYKAQREDELTFIKSAIIQNVEKQEGGWWRGDYGGKKQLWFPSNYVEEMVNPEGIHRD
>d1prmc_ 2.21.2.1.12 Src kinase, SH3 domain [chicken (Gallus gallus)]
TFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLTTGQTGYIPSNYVAPS
>d1cska_ 2.21.2.1.13 Src kinase, SH3 domain [human (Homo sapiens)]
GTECIAKYNFHGTAEQDLPFCKGDVLTIVAVTKDPNWYKAKNKVGREGIIPANYVQKR
>d1shfa_ 2.21.2.1.2 Fyn, SH3 domain [human (Homo sapiens)]
VTLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAPVD
>d1aboa_ 2.21.2.1.3 Abl tyrosine kinase, SH3 domain [Mouse (Mus musculus)]
NLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNS
>d1pht__ 2.21.2.1.4 Phosphatidylinositol 3-kinase (p85-alpha subunit, pi3k), SH3 domain [human (Homo sapiens)]
AEGYQYRALYDYKKEREEDIDLHLGDILTVNKGSLVALGFSDGQEARPEEIGWLNGYNETTGERGDFPGTYVEYIGRKKISPP
>d1shg__ 2.21.2.1.6 alpha-Spectrin, SH3 domain [chicken (Gallus gallus)]
KELVLALYDYQEKSPREVTMKKGDILTLLNSTNKDWWKVEVNDRQGFVPAAYVKKLD
>d2hcka1 2.21.2.1.7 (1-63) Hemapoetic cell kinase Hck [human (Homo sapiens)]
EDIIVVALYDYEAIHHEDLSFQKGDQMVVLEESGEWWKARSLATRKEGYIPSNYVARVDSLET
>d1gfc__ 2.21.2.1.8 Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains [human (Homo sapiens)]
GSTYVQALFDFDPQEDGELGFRRGDFIHVMDNSDPNWWKGACHGQTGMFPRNYVTPVNR
>d1gbra_ 2.21.2.1.9 Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains [mouse (Mus musculus)]
GSRRASVGSMEAIAKYDFKATADDELSFKRGDILKVLNEECDQNWYKAELNGKDGFIPKNYIEMKPHPEFIVTD
>d2mysa1 2.21.3.1.1 (29-69) Myosin S1 fragment, N-terminal domain [chicken (Gallus gallus) pectoral muscle]
ASSVFVVHPKQSFVGTIQSEGGVTVTEGGETLTVKEDQVFS
>d1mmd_1 2.21.3.1.2 (33-78) Myosin S1 fragment, N-terminal domain [Dictyostelium discoideum]
YIWYNPDPDERDSYECGEIVSETSDSFTFKTVDGQDRQVKKDDANQ
>d1vie__ 2.21.4.1.1 R67 dihydrofolate reductase [Escherichia coli plasmid PLZ1]
PSNATFGMGDRVRKKSGAAWQGQIVGWYCTNLTPEGYAVESEAHPGSVQIYPVAALERIN
>d1pse__ 2.21.5.1.1 Photosystem I accessory protein E (PSAE) [Cyanobacterium synechococcus Sp. strain PCC 7002]
AIERGSKVKILRKESYWYGDVGTVASIDKSGIIYPVIVRFNKVNYNGFSGSAGGLNTNNFAEHELEVVG
>d1ihwa_ 2.21.6.1.1 DNA-binding domain of HIV-1 integrase [human immunodeficiency virus, HIV-1]
MIQNFRVYYRDSRDPVWKGPAKLLWKGEGAVVIQDNSDIKVVPRRKAKIIRD
>d1aono_ 2.22.1.1.1 Chaperonin-10 (GroES) [(Escherichia coli)]
MNIRPLHDRVIVKRKEVETKSAGGIVLTGSAAAKSTRGEVLAVGNGRILENGEVKPLDVKVGDIVIFNDGYGVKSEKIDNEEVLIMSESDILAIVEA
>d1lepa_ 2.22.1.1.2 Chaperonin-10 (GroES) [(Mycobacterium leprae)]
AKVKIKPLEDKILVQAEKPQEGTVVAVGPGRWDEDGAKRIPVDVSEGDIVIYSKYGGTEIKYNGEEYLILSARDVLAVVSK
>d7adh_1 2.22.1.2.1 (1-174,325-374) Alcohol dehydrogenase [horse (Equus caballus)]
STAGXVIXCXAAVLWEEXXPFSIEEVEVAPPXAHEVRIXMVATGICRSDDHVVSGTLVTPLPVIAGHEAAGIVESIGEGVTTVRPGDXVIPLFTPQCGXCRVCKHPEGNFCLXNDLSMPRGTMQDGTSRFTCRGXPIHHFLGTSTFSQYTVVDEISVAXIDAASPLEXVCLIG
>d2ohxa1 2.22.1.2.1 (1-174,325-374) Alcohol dehydrogenase [horse (Equus caballus)]
STAGKVIKCKAAVLWEEKKPFSIEEVEVAPPKAHEVRIKMVATGICRSDDHVVSGTLVTPLPVIAGHEAAGIVESIGEGVTTVRPGDKVIPLFTPQCGKCRVCKHPEGNFCLKNDLSMPRGTMQDGTSRFTCRGKPIHHFLGTSTFSQYTVVDEISVAKIDAASPLEKVCLIG
>d1cdoa1 2.22.1.2.1 (1-175,325-374) Alcohol dehydrogenase [horse (Equus caballus)]
ATVGKVIKCKAAVAWEANKPLVIEEIEVDVPHANEIRIKIIATGVCHTDLYHLFEGKHKDGFPVVLGHEGAGIVESVGPGVTEFQPGEKVIPLFISQCGECRFCQSPKTNQCVKGWANESPDVMSPKETRFTCKGRKVLQFLGTSTFSQYTVVNQIAVAKIDPSAPLDTVCLLG
>d1agna1 2.22.1.2.2 (1-173,324-373) Alcohol dehydrogenase [human (Homo sapiens)]
GTAGKVIKCKAAVLWEQKQPFSIEEIEVAPPKTKEVRIKILATGICRTDDHVIKGTMVSKFPVIVGHEATGIVESIGEGVTTVKPGDKVIPLFLPQCRECNACRNPDGNLCIRSDITGRGVLADGTTRFTCKGKPVHHFMNTSTFTEYTVVDESSVAKIDDAAPPEKVCLIG
>d1htba1 2.22.1.2.2 (1-174,325-374) Alcohol dehydrogenase [human (Homo sapiens)]
STAGKVIKCKAAVLWEVKKPFSIEDVEVAPPKAYEVRIKMVAVGICRTDDHVVSGNLVTPLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLFTPQCGKCRVCKNPESNYCLKNDLGNPRGTLQDGTRRFTCRGKPIHHFLGTSTFSQYTVVDENAVAKIDAASPLEKVCLIG
>d1teha1 2.22.1.2.2 (1-173,324-373) Alcohol dehydrogenase [human (Homo sapiens)]
ANEVIKCKAAVAWEAGKPLSIEEIEVAPPKAHEVRIKIIATAVCHTDAYTLSGADPEGCFPVILGHEGAGIVESVGEGVTKLKAGDTVIPLYIPQCGECKFCLNPKTNLCQKIRVTQGKGLMPDGTSRFTCKGKTILHYMGTSTFSEYTVVADISVAKIDPLAPLDKVCLLG
>d1keva1 2.22.1.2.3 (1-150,315-351) Bacterial secondary alcohol dehydrogenase [Clostridium beijerinckii]
MKGFAMLGINKLGWIEKERPVAGSYDAIVRPLAVSPCTSDIHTVFEGALGDRKNMILGHEAVGEVVEVGSEVKDFKPGDRVIVPCTTPDWRSLEVQAGFQQHSNGMLAGWKFSNFKDGVFGEYFHVNDADMNLAILPKDMPLENAVMIT
>d1qora1 2.22.1.2.4 (1-134,265-326) Quinone oxidoreductase [Escherichia coli]
ATRIEFHKHGGPEVLQAVEFTPADPAENEIQVENKAIGINFIDTYIRSGLYPPPSLPSGLGTEAAGIVSKVGSGVKHIKAGDRVVYAQSALGAYSSVHNIIADKAAILPAAISFEQAAASFLKGLTVYYLLRK
>d1pdr__ 2.23.1.1.1 Discs large protein homolog [human homo sapiens]
ITREPRKVVLHRGSTGLGFNIVGGEDGEGIFISFILAGGPADLSGELRKGDRIISVNSVDLRAASHEQAAAALKNAGQAVTIVAQYRPEEYSRQHA
>d1fgp__ 2.24.1.1.1 Membrane penetration domain of the minor coat protein g3p [fd phage (bacteriophage fd)]
ETVESCLAKPHTENSFTNVWKDDKTLDRYANYEGCLWNATGVVVCTGDETQCYGTWVPIGLAIPENAAAH
>d1whi__ 2.25.1.1.1 Ribosomal protein L14 [Bacillus stearothermophilus]
MIQQESRLKVADNSGAREVLVIKVLGGSGRRYANIGDVVVATVKDATPGGVVKKGQVVKAVVVRTKRGVRRPDGSYIRFDENACVIIRDDKSPRGTRIFGPVARELRDKDFMKIISLAPEVI
>d1sty__ 2.26.1.1.1 Staphylococcal nuclease [Staphylococcal aureus]
KLHKEPATLIKAIDGDTVKLMYKGQPMTFRLLLVDTPETKHPKKGVEKYGPEASAFTKKMVENAKKIEVEFDKGQRTDKYGRGLAYIYADGKMVNEALVRQGLAKVAYVYKPNNTHEQHLRGKSEAQAKKEKLNIWS
>d1ltsd_ 2.26.2.1.1 Heat-labile toxin [Escherichia coli type IB]
APQTITELCSEYRNTQIYTINDKILSYTESMAGKREMVIITFKSGETFQVEVPGSQHIDSQKKAIERMKDTLRITYLTETKIDKLCVWNNKTPNSIAAISMKN
>d1tiid_ 2.26.2.1.2 Heat-labile toxin [Escherichia coli type IIB]
GASQFFKDNCNRTTASLVEGVELTKYISDINNNTDGMYVVSSTGGVWRISRAKDYPDNVMTAEMRKIAMAAVLSGMRVNMCASPASSPNVIWAIELEA
>d1chbd_ 2.26.2.1.3 Cholera toxin [Vibrio cholerae)]
TPQNITDLCAEYHNTQIHTLNNKIFSYTESLAGKREMAIITFKNGATFQVEVPGSQHIDSQKKAIERMKNTLRIAYLTEAKVEKLCVWNNKTPHAIAAISMAN
>d1bova_ 2.26.2.1.4 Verotoxin-1 [Escherichia coli]
TPDCVTGKVEYTKYNDDDTFTVKVGDKELFTNRWNLQSLLLSAQITGMTVTIKTNACHNGGGFSEVIFR
>d1prtc1 2.26.2.1.6 (85-196) Pertussis toxin S2/S3 subunits, C-terminal domain [Bordetella pertussis]
ITTIYKTGQPAADHYYSKVTATRLLASTNSRLCAVFVRDGQSVIGACASPYEGRYRDMYDALRRLLYMIYMSGLAVRVHVSKEEQYYDYEDATFQTYALTGISLCNPAASIC
>d1prtb1 2.26.2.1.6 (85-196) Pertussis toxin S2/S3 subunits, C-terminal domain [Bordetella pertussis]
IMTTRNTGQPATDHYYSNVTATRLLSSTNSRLCAVFVRSGQPVIGACTSPYDGKYWSMYSRLRKMLYLIYVAGISVRVHVSKEEQYYDYEDATFETYALTGISICNPGSSLC
>d1prtd_ 2.26.2.1.7 Pertussis toxin S4 subunit [Bordetella pertussis]
DVPYVLVKTNMVVTSVAMKPYEVTPTRMLVCGIAAKLGAAASSPDAHVPFCFGKDLKRPGSSPMEVMLRAVFMQQRPLRMFLGPKQLTFEGKPALELIRMVECSGKQDCP
>d1prtf_ 2.26.2.1.8 Pertussis toxin S5 subunit [Bordetella pertussis]
LPTHLYKNFTVQELALKLKGKNQEFCLTAFMSGRSLVRACLSDAGHEHDTWFDTMLGFAISAYALKSRIALTVEDSPYPGTPGDLLELQICPLNGYCE
>d1esfa1 2.26.2.2.1 (1-116) Staphylococcal enterotoxin A, SEA [Staphylococcus aureus]
SEKSEEINEKDLRKKSELQGTALGNLKQIYYYNEKAKTENKESHDQFLQHTILFKGFFTYNDLLVDFDSKDIVDKYKGKKVDLYGAYYGYQCAGGTPNKTACMYGGVTLHDNNRLT
>d1ste_1 2.26.2.2.2 (1-120) Staphylococcal enterotoxin C2, SEC2 [Staphylococcus aureus]
ESQPDPTPDELHKSSEFTGTMGNMKYLYDDHYVSATKVMSVDKFLAHDLIYNISDKKLKNYDKVKTELLNEDLAKKYKDEVVDVYGSNYYVNCYFSSKDNVGKVTGGKTCMYGGITKHEG
>d1tssa1 2.26.2.2.3 (1-93) Toxic shock syndrome toxin-1 (TSST-1) [Staphylococcus aureus]
STNDNIKDLLDWYSSGSDTFTNSEVLDNSLGSMRIKNTDGSISLIIFPSPYYSPAFTKGEKVDLNTKRTKKSQHTSEGTYIHFQISGVTNTEK
>d1se4_1 2.26.2.2.4 (1-121) Staphylococcal enterotoxin B, SEB [Staphylococcus aureus]
ESQPDPKPDELHKSSKFTGLMENMKVLYDDNHVSAINVKSIDQFLYFDLIYSIKDTKLGNYDNVRVEFKNKDLADKYKDKYVDVFGANYYYQCYFSKKTNDINSHQTDKRKTCMYGGVTEH
>d1asya1 2.26.4.1.1 (1-137) Aspartyl-tRNA synthetase (AspRS) [Yeast (Saccharomyces cerevisiae)]
EDTAKDNYGKLPLIQSRDSDRTGQKRVKFVDLDEAKDSDKEVLFRARVHNTRQQGATLAFLTLRQQASLIQGLVKANKEGTISKNMVKWAGSLNLESIVLVRGIVKKVDEPIKSATVQNLEIHITKIYTISETPEAL
>d1krt__ 2.26.4.1.3 Lysyl-tRNA synthetase (LysRS) [Escherichia coli, lysS gene]
FRRDHTSDQLHAEFDGKENEELEALNIEVAVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDDLPEGVYNEQFKKWDLGDILGAKGKLFKTKTGELSIHCTELRLLTKA
>d1lyla1 2.26.4.1.4 (1-140) Lysyl-tRNA synthetase (LysRS) [Escherichia coli, lysU gene]
FNDELRNRREKLAALRQQGVAFPNDFRRDHTSDQLHEEFDAKDNQELESLNIEVSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEGVYNDQFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLP
>d1cuk_3 2.26.4.2.1 (1-64) DNA helicase RuvA subunit, N-terminal domain [Escherichia coli]
MIGRLRGIIIEKQPPLVLIEVGGVGYEVHMPMTCFYELPEAGQEAIVFTHFVVREDAQLLYGFN
>d3ulla_ 2.26.4.3.1 ssDNA-binding protein [human (Homo sapiens) mitochondria]
LERSLNRVHLLGRVGQDPVLRQVEGKNPVTIFSLATNEMWRSDVSQKTTWHRISVFRPGLRDVAYQYVKKGSRIYLEGKIDYGEYMDKNNVRRQATTIIADNIIFL
>d1jmca1 2.26.4.3.3 (1-116) Replication protein A fragment [human (Homo sapiens)]
KVVPIASLTPYQSKWTICARVTNKSQIRTWSNSRGEGKLFSLELVDESGEIRATAFNEQVDKFFPLIEVNKVYYFSKGTLKIANKQFTAVKNDYEMTFNNETSVMPCEDDHHLPTV
>d1jmca2 2.26.4.3.3 (117-238) Replication protein A fragment [human (Homo sapiens)]
QFDFTGIDDLENKSKDSLVDIIGICKSYEDATKITVRSNNREVAKRNIYLMDTSGKVVTATLWGEDADKFDGSRQPVLAIKGARVSDFGGRSLSVLSSSTIIANPDIPEAYKLRGWFDAEGQ
>d1mjc__ 2.26.4.4.1 Major cold shock protein [Escherichia coli]
SGKMTGIVKWFNADKGFGFITPDDGSKDVFVHFSAIQNDGYKSLDEGQKVSFTIESGAKGPAAGNVTSL
>d1csp__ 2.26.4.4.2 Major cold shock protein [Bacillus subtilis]
MLEGKVKWFNSEKGFGFIEVEGQDDVFVHFSAIQGEGFKTLEEGQAVSFEIVEGNRGPQAANVTKEA
>d1sro__ 2.26.4.4.3 S1 RNA-binding domain of polyribonucleotide phosphorylase, PNP [Escherichia coli]
AEIEVGRVYTGKVTRIVDFGAFVAIGGGKEGLVHISQIADKRVEKVTDYLQMGQEVPVKVLEVDRQGRIRLSIKEA
>d1ah9__ 2.26.4.4.4 Translational initiation factor 1, IF1 [Escherichia coli]
AKEDNIEMQGTVLETLPNTMFRVELENGHVVTAHISGKMRKNYIRILTGDKVTVELTPYDLSKGRIVFRSR
>d1ckma1 2.26.4.5.1 (229-317) RNA guanylyltransferase (mRNA capping enzyme) [Chlorella virus PBCV-1]
THHTIDFIIMSEDGTIGIFDPNLRKNVPVGKLDGYYNKGSIVECGFADGTWKYIQGRSDKNQANDRLTYEKTLLNIEENITIDELLDLF
>d1rip__ 2.26.4.6.1 Ribosomal S17 protein [Bacillus stearothermophilus]
QRKVYVGRVVSDKMDKTITVLVETYKKHPLYGKRVKYSKKYKAHDEHNEAKVGDIVKIMETRPLSATKRFRLVEIVEKAVR
>d1yhb__ 2.26.4.7.1 Gene V protein [Bacteriophage f1]
MIKVEIKPSQAQFTTRSGVSRQGKPYSLNEQLCYVDLGNEFPVLVKITLDEGQPAYAPGLYTVHLSSFKVGQFGSLMIDRLRLVPAK
>d1pfsa_ 2.26.4.7.2 Gene V protein [Pseudomonas phage pf3]
MNIQITFTDSVRQGTSAKGNPYTFQEGFLHLEDKPHPLQCQFFVESVIPAGSYQVPYRINVNNGRPELAFDFKAMKRA
>d1gpc__ 2.26.4.7.3 Gene 32 protein (GP32) core [bacteriophage T4]
GFSSEDKGEWKLKLDNAGNGQAVIRFLPSKNDEQAPFAILVNHGFKKNGKWYIETCSSTHGDYDSCPVCQYISKNDLYNTDNKEYSLVKRKTSYWANILVVKDPAAPENEGKVFKYRFGKKIWDKINAMIAVDVEMGETPVDVTCPWEGANFVLKVKQVSGFSNYDESKFLNQSAIPNIDDESFQKELFEQMVDLSEMTSKDKFKSFEELNTKFGQVM
>d1pyp__ 2.26.5.1.1 Inorganic pyrophosphatase [baker's yeast (Saccharomyces cerevisiae)]
TYTTRQIGAKNTLEYKVYIEKDGKPVSAFHDIPLYADKEDNIFNMVVEIPRWTNAKLEITKEETLNPIIQNTKGKLRFVRNCFPHHGYIHNYGAFPQTWEDPNVSHPETKAVGDNNPIDVLQIGETIAYTGQVKEVKALGIMALLDEGETDWKVIAIDINDPLAPKLNDIEDVEKYFPGLLRATDEWFRIYKIPDGKPENQFAFSGEAKNKKYALDIIKETHNSWKQLIAGKSSDSKGIDLTNVTLPDTPTYSKAASDAIPPASPKADAPIDKSIDKWFF
>d1igp__ 2.26.5.1.2 Inorganic pyrophosphatase [Escherichia coli]
SLLNVPAGKDLPEDIYVVIEIPANADPIKYEIDKESGALFVDRFMSTAMFYPCNYGYINHTLSLDGDPVDVLVPTPYPLQPGSVTRCRPVGVLKMTDEAGEDAKLVAVPHSKLSKEYDHIKDVNDLPELLKAQIAHFFEHYKDLEKGKWVKVEGWENAEAAKAEIVASFERAKNK
>d2prd__ 2.26.5.1.3 Inorganic pyrophosphatase [Thermus thermophilus.]
ANLKSLPVGDKAPEVVHMVIEVPRGSGNKYEYDPDLGAIKLDRVLPGAQFYPGDYGFIPSTLAEDGDPLDGLVLSTYPLLPGVVVEVRVVGLLLMEDEKGGDAKVIGVVAEDQRLDHIQDIGDVPEGVKQEIQHFFETYKALEAKKGKWVKVTGWRDRKAALEEVRACIARYKG
>d1prch1 2.27.1.1.1 (37-258) Photosynthetic reaction centre [Rhodopseudomonas viridis]
RREGYPLVEPLGLVKLAPEDGQVYELPYPKTFVLPHGGTVTVPRRRPETRELKLAQTDGFEGAPLQPTGNPLVDAVGPASYAERAEVVDATVDGKAKIVPLRVATDFSIAEGDVDPRGLPVVAADGVEAGTVTDLWVDRSEHYFRYLELSVAGSARTALIPLGFCDVKKDKIVVTSILSEQFANVPRLQSRDQITLREEDKVSAYYAGGLLYATPERAESLL
>d1pcrh1 2.27.1.1.2 (26-240) Photosynthetic reaction centre [Rhodobacter sphaeroides]
MREGYPLENEDGTPAANQGPFPLPKPKTFILPHGRGTLTVPGPESEDRPIALARTAVSEGFPHAPTGDPMKDGVGPASWVARRDLPELDGHGHNKIKPMKAAAGFHVSAGKNPIGLPVRGCDLEIAGKVVDIWVDIPEQMARFLEVELKDGSTRLLPMQMVKVQSNRVHVNALSSDLFAGIPTIKSPTEVTLLEEDKICGYVAGGLMYAAPKRKS
>d2fgf__ 2.28.1.1.1 Basic FGF [human (Homo sapiens)]
DPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHIKLQLQAEERGVVSIKGVCANRYLAMKEDGRLLASKCVTDECFFFERLESNNYNTYRSRKYTSWYVALKRTGQYKLGSKTGPGQKAILFLPMSA
>d1bara_ 2.28.1.1.2 Acidic FGF [bovine (Bos taurus)]
PKLLYCSNGGYFLRILPDGTVDGTKDRSDQHIQLQLAAESIGEVYIKSTETGQFLAMDTDGLLYGSQTPNEECLFLERLEENGYNTYISKKHAEKHWFVGLKKNGRSKLGPRTHFGQKAILFLPLPV
>d2afga_ 2.28.1.1.3 Acidic FGF [human (Homo sapiens)]
KPKLLYCSNGGHFLRILPDGTVDGTRDRSDQHIQLQLSAESVGEVYIKSTETGQYLAMDTDGLLYGSQTPNEECLFLERLEENHYNTYISKKHAEKNWFVGLKKNGSCKRGPRTHYGQKAILFLPLPVS
>d1i1b__ 2.28.1.2.1 Interleukin-1beta [human (Homo sapiens)]
VRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFVQGEESNDKIPVALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKMEKRFVFNKIEINNKLEFESAQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS
>d2mib__ 2.28.1.2.2 Interleukin-1beta [mouse (Mus musculus)]
IRQLHYRLRDEQQKSLVLSDPYELKALHLNGQNINQQVIFSMSFVQGEPSNDKIPVALGLKGKNLYLSCVMKDGTPTLQLESVDPKQYPKKKMEKRFVFNKIEVKSKVEFESAEFPNWYISTSQAEHKPVFLGNNSGQDIIDFTMESVS
>d1ilr1_ 2.28.1.2.3 Interleukin-1 receptor antagonist protein [Human Homo sapiens]
SKMQAFRIWDVNQKTFYLRNNQLVAGYLQGPNVNLEEKIDVVPIEPHALFLGIHGGKMCLSCVKSGDETRLQLEAVNITDLSENRKQDKRFAFIRSDSGPTTSFESAACPGWFLCTAMEADQPVSLTNMPDEGVMVTKFYFQEDE
>d2ila__ 2.28.1.2.4 Interleukin-1alpha [human (Homo sapiens)]
NVKYNFMRIIKYEFILNDALNQSIIRANAQYLTAAALHNLDEAVKFDMGAYKSSAKITVILRISKTQLYVTAQDEDQPVLLKEMPEIPKTITGSETNLLFFWETHGTKNYFTSVAHPNLFIATKQDYWVCLAGGPPSITDFQILE
>d2aaib2 2.28.2.1.1 (136-262) Plant cytotoxin B-chain (lectin) [castor bean (Ricinus communis); Ricin]
NTQPFVTTIVGLYGLCLQANSGQVWIEDCSSEKAEQQWALYADGSIRPQQNRDNCLTSDSNIRETVVKILSCGPASSGQRWMFKNDGTILNLYSGLVLDVRASDPSLKQIILYPLHGDPNQIWLPLF
>d2aaib1 2.28.2.1.1 (1-135) Plant cytotoxin B-chain (lectin) [castor bean (Ricinus communis); Ricin]
ADVCMDPEPIVRIVGRNGLCVDVRDGRFHNGNAIQLWPCKSNTDANQLWTLKRDNTIRSNGKCLTTYGYSPGVYVMIYDCNTAATDATRWQIWDNGTIINPRSSLVLAATSGNSGTTLTVQTNIYAVSQGWLPTN
>d1abrb2 2.28.2.1.2 (141-267) Plant cytotoxin B-chain (lectin) [Abrus precatorius; Abrin]
NTSPFVTSISGYSDLCMQAQGSNVWMADCDSNKKEQQWALYTDGSIRSVQNTNNCLTSKDHKQGSTILLMGCSNGWASQRWVFKNDGSIYSLYDDMVMDVKGSDPSLKQIILWPYTGKPNQIWLTLF
>d1abrb1 2.28.2.1.2 (1-140) Plant cytotoxin B-chain (lectin) [Abrus precatorius; Abrin]
IVEKSKICSSRYEPTVRIGGRDGMCVDVYDNGYHNGNRIIMWKCKDRLEENQLWTLKSDKTIRSNGKCLTTYGYAPGSYVMIYDCTSAVAEATYWEIWDNGTIINPKSALVLSAESSSMGGTLTVQTNEYLMRQGWRTGN
>d1wba__ 2.28.3.1.1 Winged bean albumin 1 [goa bean (Psophocarpus tetragonolobus)]
DDPVYDAEGNKLVNRGKYTIVSFSDGAGIDVVATGNENPEDPLSIVKSTRNIMYATSISSEDKTPPQPRNILENMRLKINFATDPHKGDVWSVVDFQPDGQQLKLAGRYPNQVKGAFTIQKGSNTPRTYKLLFCPVGSPCKNIGISTDPEGKKRLVVSYQSDPLVVKFHRH
>d1tie__ 2.28.3.1.2 Erythrina cafra trypsin inhibitor [Erythrina caffra]
VLLDGNGEVVQNGGTYYLLPQVWAQGGGVQLAKTGEETCPLTVVQSPNELSDGKPIRIESRLRSAFIPDDDKVRIGFAYAPKCAPSPWWTVVEGLSVKLSEDESTQFDYPFKFEQVSDQLHSYKLLYCEGKHEKCASIGINRDQKGYRRLVVTEDYPLTVVLKKDE
>d1wbc__ 2.28.3.1.3 chymotrypsin inhibitor WCI [winged bean (Psophocarpus tetragonolobus)]
DDDLVDAEGNLVENGGTYYLLPHIWAHGGGIETAKTGNEPCPLTVVRSPNEVSKGEPIRISSQFLSLFIPRGSLVALGFANPPSCAASPWWTVVDSPQGPAVKLSQQKLPEKDILVFKFEKVSHSNIHVYKLLYCQHDEEDVKCDQYIGIHRDRNGNRRLVVTEENPLELVLLKAKSETASSH
>d1hcd__ 2.28.4.1.1 Histidine-rich actin-binding protein (hisactophilin) [Dictyostelium discoideum]
MGNRAFKSHHGHFLSAEGEAVKTHHGHHDHHTHFHVENHGGKVALKTHCGKYLSIGDHKQVYLSHHLHGDHSLFHLEHHGGKVSIKGHHHHYISADHHGHVSTKEHHDHDTTFEEIII
>d1fnb_1 2.29.1.1.1 (1-136) Ferredoxin reductase [spinach (Spinacia oleracea)]
HSKKMEEGITVNKFKPKTPYVGRCLLNTKITGDDAPGETWHMVFSHEGEIPYREGQSVGVIPDGEDKNGKPHKLRLYSIASSALGDFGDAKSVSLCVKRLIYTNDAGETIKGVCSNFLCDLKPGAEVKLTGPVGKE
>d1quf_1 2.29.1.1.2 (1-134) Ferredoxin reductase [cyanobacterium (Anabaena pcc 7119)]
ADVPVNLYRPNAPFIGKVISNEPLVKEGGIGIVQHIKFDLTGGNLKYIEGQSIGIIPPGVDKNGKPEKLRLYSIASTRHGDDVDDKTISLCVRQLEYKHPESGETVYGVCSTYLTHIEPGSEVKITGPVGKEML
>d2cnd_1 2.29.1.1.3 (1-114) Nitrate reductase [corn (Zea mays)]
GRIHCRLVAKKELSRDVRLFRFSLPSPDQVLGLPIGKHIFVCATIEGKLCMRAYTPTSMVDEIGHFDLLVKVYFKNEHPKFPNGGLMTQYLDSLPVGSYIDVKGPLGHVEYTGR
>d1ndh_1 2.29.1.1.4 (1-123) cytochrome b5 reductase [pig (Sus scrofa) liver]
PAITLENPDIKYPLRLIDKEVVNHDTRRFRFALPSPEHILGLPVGQHIYLSARIDGNLVIRPYTPVSSDDDKGFVDLVIKVYFKDTHPKFPAGGKMSQYLESMKIGDTIEFRGPNGLLVYQGK
>d1fdr_1 2.29.1.1.5 (1-96) Flavodoxin reductase [Escherichia coli]
ADWVTGKVTKVQNWTDALFSLTVHAPVLPFTAGQFTKLGLEIRVQRAYSYVNSPDNPDLEFYLVTVPDGKLSPRLAALKPGDEVQVVSEAAGFFVL
>d2pia_1 2.29.1.2.1 (1-103) Phthalate dioxygenase reductase [Pseudomonas cepacia db01]
TTPQEDGFLRLKIASKEKIARDIWSFELTDPQGAPLPPFEAGANLTVAVPNGSRRTYSLCNDSQERNRYVIAVKRDSNGRGGSISFIDDTSEGDAVEVSLPRN
>d1fuia1 2.29.2.1.1 (356-591) L-fucose isomerase, C-terminal domain [Escherichia coli]
AQVFADVRTYWSPEAIERVTGHKLDGLAEHGIIHLINSGSAALDGSCKQRDSEGNPTMKPHWEISQQEADACLAATEWCPAIHEYFRGGGYSSRFLTEGGVPFTMTRVNIIKGLGPVLQIAEGWSVELPKDVHDILNKRTNSTWPTTWFAPRLTGKGPFTDVYSVMANWGANHGVLTIGHVGADFITLASMLRIPVCMHNVEETKVYRPSAWAAHGMDIEGQDYRACQNYGPLYKR
>d1eft_1 2.29.3.1.2 (213-312) Elongation factor Tu (EF-Tu), domain 2 [Thermus aquaticus]
PVRDVDKPFLMPVEDVFTITGRGTVATGRIERGKVKVGDEVEIVGLAPETRKTVVTGVEMHRKTLQEGIAGDNVGLLLRGVSREEVERGQVLAKPGSITP
>d1dar_1 2.29.3.1.4 (255-372) Elongation factor G (EF-G), domain II [Thermus thermophilus]
PLDIPPIKGTTPEGEVVEIHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHANHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILE
>d1cgt_2 2.3.1.1.1 (580-684) Cyclodextrin glycosyltransferase, C-terminal domain [Bacillus circulans]
LTGDQVTVRFVVNNASTTLGQNLYLTGNVAELGNWSTGSTAIGPAFNQVIHQYPTWYYDVSVPAGKQLEFKFFKKNGSTITWESGSNHTFTTPASGTATVTVNWQ
>d1cdg_2 2.3.1.1.1 (582-686) Cyclodextrin glycosyltransferase, C-terminal domain [Bacillus circulans]
LSGDQVSVRFVVNNATTALGQNVYLTGSVSELGNWDPAKAIGPMYNQVVYQYPNWYYDVSVPAGKTIEFKFLKKQGSTVTWEGGSNHTFTAPSSGTATINVNWQP
>d1cyg_2 2.3.1.1.2 (575-680) Cyclodextrin glycosyltransferase, C-terminal domain [Bacillus stearothermophilus]
LTNDQVSVRFVVNNATTNLGQNIYIVGNVYELGNWDTSKAIGPMFNQVVYSYPTWYIDVSVPEGKTIEFKFIKKDSQGNVTWESGSNHVYTTPTNTTGKIIVDWQN
>d1pama2 2.3.1.1.3 (583-686) Cyclodextrin glycosyltransferase, C-terminal domain [alkalophilic Bacillus sp. 1011]
TGDQVTVRFVINNATTALGQNVFLTGNVSELGNWDPNNAIGPMYNQVVYQYPTWYYDVSVPAGQTIEFKFLKKQGSTVTWEGGANRTFTTPTSGTATVNVNWQP
>d1ciu_2 2.3.1.1.4 (579-683) Cyclodextrin glycosyltransferase, C-terminal domain [Thermoanaerobacterium thermosulfurigenes EM1]
LTGNQICVRFVVNNASTVYGENVYLTGNVAELGNWDTSKAIGPMFNQVVYQYPTWYYDVSVPAGTTIQFKFIKKNGNTITWEGGSNHTYTVPSSSTGTVIVNWQQ
>d1kul__ 2.3.1.1.5 Glucoamilase, granular starch-binding domain [Aspergillus niger]
CTTPTAVAVTFDLTATTTYGENIYLVGSISQLGDWETSDGIALSADKYTSSDPLWYVTVTLPAGESFEYKFIRIESDDSVEWESDPNREYTVPQACGTSTATVTDTWR
>d1eta1_ 2.3.2.1.1 Transthyretin (synonym: prealbumin) [human (Homo sapiens)]
GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE
>d1tfpa_ 2.3.2.1.2 Transthyretin (synonym: prealbumin) [Chicken (Gallus gallus)]
CPLMVKVLDAVRGSPAANVAVKVFKKAADGTWQDFATGKTTEFGEIHELTTEEQFVEGVYRVEFDTSSYWKGLGLSPFHEYADVVFTANDSGHRHYTIAALLSPFSYSTTAVVS
>d2pcda_ 2.3.3.1.1 Protocatechuate-3,4-dioxygenase, alpha chain [Pseudomonas aeruginosa]
PIELLPETPSQTAGPYVHIGLALEAAGNPTRDQEIWNRLAKPDAPGEHILLLGQVYDGNGHLVRDSFLEVWQADANGEYQDAYNLENAFNSFGRTATTFDAGEWTLHTVKPGVVNNAAGVPMAPHINISLFARGINIHLHTRLYFDDEAQANAKCPVLNLIEQPQRRETLIAKRCEVDGKTAYRFDIRIQGEGETVFFDF
>d2pcdm_ 2.3.3.1.2 Protocatechuate-3,4-dioxygenase, beta chain [Pseudomonas aeruginosa]
PAQDNSRFVIRDRNWHPKALTPDYKTSIARSPRQALVSIPQSISETTGPNFSHLGFGAHDHDLLLNFGLPIGERIIVAGRVVDQYGKPVPNTLVEMWQANAGGRYRHKNDRYLAPLDPNFGGVGRCLTDSDGYYSFRTIKPGPYPWRNGPNDWRPAHIHFGISGPSIATKLITQLYFEGDPLIPMCPIVKSIANPEAVQQLIAKLDMNNANPMDCLAYRFDIVLRGQRKTHFE
>d1eft_2 2.30.1.1.2 (313-405) Elongation factor Tu (EF-Tu), the C-terminal domain [Thermus aquaticus]
HTKFEASVYVLKKEEGGRHTGFFSGYRPQFYFRTTDVTGVVRLPQGVEMVMPGDNVTFTVELIKPVALEEGLRFAIREGGRTVGAGVVTKILE
>d1arb__ 2.31.1.1.1 Achromobacter protease [Achromobacter lyticus, strain m497-1]
GVSGSCNIDVVCPEGDGRRDIIRAVGAYSKSGTLACTGSLVNNTANDRKMYFLTAHHCGMGTASTAASIVVYWNYQNSTCRAPNTPASGANGDGSMSQTQSGSTVKATYATSDFTLLELNNAANPAFNLFWAGWDRRDQNYPGAIAIHHPNVAEKRISNSTSPTSFVAWGGGAGTTHLNVQWQPSGGVTEPGSSGSPIYSPEKRVLGQLHGGPSSCSATGTNRSDQYGRVFTSWTGGGAAASRLSDWLDPASTGAQFIDGLDS
>d2alp__ 2.31.1.1.2 alpha-Lytic protease [Lysobacter enzymogenes 495]
ANIVGGIEYSINNASLCSVGFSVTRGATKGFVTAGHCGTVNATARIGGAVVGTFAARVFPGNDRAWVSLTSAQTLLPRVANGSSFVTVRGSTEAAVGAAVCRSGRTTGYQCGTITAKNVTANYAEGAVRGLTQGNACMGRGDSGGSWITSAGQAQGVMSGGNVQSNGNNCGIPASQRSSLFERLQPILSQYGLSLVTG
>d1sgc__ 2.31.1.1.3 Protease A [Streptomyces griseus, strain k1]
IAGGEAITTGGSRCSLGFNVSVNGVAHALTAGHCTNISASWSIGTRTGTSFPNNDYGIIRHSNPAAADGRVYLYNGSYQDITTAGNAFVGQAVQRSGSTTGLRSGSVTGLNATVNYGSSGIVYGMIQTNVCAQPGDSGGSLFAGSTALGLTSGGSGNCRTGGTTFYQPVTEALSAYGATVL
>d1hpga_ 2.31.1.1.4 Glutamic acid-specific protease [Streptomyces griseus]
VLGGGAIYGGGSRCSAAFNVTKGGARYFVTAGHCTNISANWSASSGGSVVGVREGTSFPTNDYGIVRYTDGSSPAGTVDLYNGSTQDISSAANAVVGQAIKKSGSTTKVTSGTVTAVNVTVNYGDGPVYNMVRTTACSAGGDSGGAHFAGSVALGIHSGSSGCSGTAGSAIHQPVTEALSAYGVTVY
>d1sgt__ 2.31.1.1.5 Trypsin [Streptomyces griseus, strain k1]
VVGGTRAAQGEFPFMVRLSMGCGGALYAQDIVLTAAHCVSGSGNNTSITATGGVVDLQSGAAVKVRSTKVLQAPGYNGTGKDWALIKLAQPINQPTLKIATTTAYNQGTFTVAGWGANREGGSQQRYLLKANVPFVSDAACRSAYGNELVANEEICAGYPDTGGVDTCQGDSGGPMFRKDNADEWIQVGIVSWGYGCARPGYPGVYTEVSTFASAIASAARTL
>d2sfa__ 2.31.1.1.6 Serine proteinase [Streptomyces fradiae]
IAGGEAIYAAGGGRCSLGFNVRSSSGATYALTAGHCTEIASTWYTNSGQTSLLGTRAGTSFPGNDYGLIRHSNASAADGRVYLYNGSYRDITGAGNAYVGQTVQRSGSTTGLHSGRVTGLNATVNYGGGDIVSGLIQTNVCAEPGDSGGALFAGSTALGLTSGGSGNCRTGGTTFFQPVTEALSAYGVSIL
>d1sgpe_ 2.31.1.1.7 Protease B [Streptomyces griseus, strain k1]
ISGGDAIYSSTGRCSLGFNVRSGSTYYFLTAGHCTDGATTWWANSARTTVLGTTSGSSFPNNDYGIVRYTNTTIPKDGTVGGQDITSAANATVGMAVTRRGSTTGTHSGSVTALNATVNYGGGDVVYGMIRTNVCAEPGDSGGPLYSGTRAIGLTSGGSGNCSSGGTTFFQPVTEALVAYGVSVY
>d1agja_ 2.31.1.1.8 Epidermolytic toxin A [Staphylococcus aureus]
EVSAEEIKKHEEKWNKYYGVNAFNLPKELFSKVDEKDRQKYPYNTIGNVFVKGQTSATGVLIGKNTVLTNRHIAKFANGDPSKVSFRPSINTDDNGNTETPYGEYEVKEILQEPFGAGVDLALIRLKPDQNGVSLGDKISPAKIGTSNDLKDGDKLELIGYPFDHKVNQMHRSEIELTTLSRGLRYYGFTVPGNSGSGIFNSNGELVGIHSSKVSHLDREHQINYGVGIGNYVKRIINEKNE
>d1bty__ 2.31.1.2.1 Trypsin(ogen) [bovine (Bos taurus)]
IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRLGEDNINVVEGNEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRVASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKSAYPGQITSNMFCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQTIASN
>d1etr.1 2.31.1.2.10 (l,h) Thrombin [bovine (Bos taurus)]
TFGAGEADCGLRPLFEKKQVQDQTEKELFESYIEGRQELLCGASLISDRWVLTAAHCLLYPPWDKNFTVDDLLVRIGKHSRTRYERKVEKISMLDKIYIHPRYNWKENLDRDIALLKLKRPIELSDYIHPVCLPDKQTAAKLLHAGFKGRVTGWGNRRETWTTSVAEVQPSVLQVVNLPLVERPVCKASTRIRITDNMFCAGYKPGEGKRGDACEGDSGGPFVMKSPYNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDRLGSTFGAGEADCGLRPLFEKKQVQDQTEKELFESYIEGRQELLCGASLISDRWVLTAAHCLLYPPWDKNFTVDDLLVRIGKHSRTRYERKVEKISMLDKIYIHPRYNWKENLDRDIALLKLKRPIELSDYIHPVCLPDKQTAAKLLHAGFKGRVTGWGNRRETWTTSVAEVQPSVLQVVNLPLVERPVCKASTRIRITDNMFCAGYKPGEGKRGDACEGDSGGPFVMKSPYNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDRLGS
>d1fona_ 2.31.1.2.11 Procarboxypeptidase A-S6 subunit III (zymogen E) [bovine (Bos taurus)]
SWSWQVSLQYEKDGAFHHTCGGSLIAPDWVVTAGHCISTSRTYQVVLGEYDRSVLEGSEQVIPINAGDLFVHPLWNSNCVACGNDIALVKLSRSAQLGDKVQLANLPPAGDILPNEAPCYISGWGRLYTGGPLPDKLQQALLPTVDYEHCSQWDWWGITVKKTMVCAGGDTRSGCNGDSGGPLNCPAADGSWQVHGVTSFVSAFGCNTIKKPTVFTRVSAFIDWIDETIASN
>d1ppfe_ 2.31.1.2.12 Elastase [human (Homo sapiens)]
IVGGRRARPHAWPFMVSLQLRGGHFCGATLIAPNFVMSAAHCVANVNVRAVRVVLGAHNLSRREPTRQVFAVQRIFENGYDPVNLLNDIVILQLNGSATINANVQVAQLPAQGRRLGNGVQCLAMGWGLLGRNRGIASVLQELNVTVVTSLCRRSNVCTLVRGRQAGVCFGDSGSPLVCNGLIHGIASFVRGGCASGLYPDAFAPVAQFVNWIDSIIQ
>d1elg__ 2.31.1.2.13 Elastase [porcine (Sus scrofa)]
VVGGTEAQRNSWPSQISLQYRSGSSWAHTCGGTLIRQNWVMTAAHCVDRELTFRVVVGEHNLNQNNGTEQYVGVQKIVVHPYWNTDDVAAGYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGQLAQTLQQAYLPTVDYAICSSSSYWGSTVKNSMVCAGGDGVRSGCQGDSGGPLHCLVNGQYAVHGVTSFVSRLGCNVTRKPTVFTRVSAYISWINNVIASN
>d1elt__ 2.31.1.2.14 Elastase [Salmon (Salmo salar)]
VVGGRVAQPNSWPWQISLQYKSGSSYYHTCGGSLIRQGWVMTAAHCVDSARTWRVVLGEHNLNTNEGKEQIMTVNSVFIHSGWNSDDVAGGYDIALLRLNTQASLNSAVQLAALPPSNQILPNNNPCYITGWGKTSTGGPLSDSLKQAWLPSVDHATCSSSGWWGSTVKTTMVCAGGGANSGCNGDSGGPLNCQVNGSYYVHGVTSFVSSSGCNASKKPTVFTRVSAYISWMNGIM
>d1cgha_ 2.31.1.2.15 Cathepsin G [human homo sapiens]
IIGGRESRPHSRPYMAYLQIQSPAGQSRCGGFLVREDFVLTAAHCWGSNINVTLGAHNIQRRENTQQHITARRAIRHPQYNQRTIQNDIMLLQLSRRVRRNRNVNPVALPRAQEGLRPGTLCTVAGWGRVSMRRGTDTLREVQLRVQRDRQCLRIFGSYDPRRQICVGDRRERKAAFKGDSGGPLLCNNVAHGIVSYGKSSGVPPEVFTRVSSFLPWIRTTMRS
>d1danh_ 2.31.1.2.16 Coagulation factor VIIa [human (Homo sapiens)]
IVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP
>d3rp2a_ 2.31.1.2.17 Proteinase II [rat (Rattus rattus)]
IIGGVESIPHSRPYMAHLDIVTEKGLRVICGGFLISRQFVLTAAHCKGREITVILGAHDVRKRESTQQKIKVEKQIIHESYNSVPNLHDIMLLKLEKKVELTPAVNVVPLPSPSDFIHPGAMCWAAGWGKTGVRDPTSYTLREVELRIMDEKACVDYRYYEYKFQVCVGSPTTLRAAFMGDSGGPLLCAGVAHGIVSYGHPDAKPPAIFTRVSTYVPWINAVIN
>d2pka.1 2.31.1.2.18 (a,b) Kallikrein A [porcine (Sus scrofa)]
IIGGRECEKNSHPWQVAIYHYSSFQCGGVLVNPKWVLTAAHCKNDNYEVWLGRHNLFENENTAQFFGVTADFPHPGFNLSTCEASGWGSIEPGPDDFEFPDEIQCVQLTLLQNTFCADAHPDKVTESMLCAGYLPGGKDTCMGDSGGPLICNGMWQGITSWGHTPCGSANKPSIYTKLIFYLDWIDDTITENPIIGGRECEKNSHPWQVAIYHYSSFQCGGVLVNPKWVLTAAHCKNDNYEVWLGRHNLFENENTAQFFGVTADFPHPGFNLSTCEASGWGSIEPGPDDFEFPDEIQCVQLTLLQNTFCADAHPDKVTESMLCAGYLPGGKDTCMGDSGGPLICNGMWQGITSWGHTPCGSANKPSIYTKLIFYLDWIDDTITENP
>d1ton__ 2.31.1.2.19 Tonin [rat (Rattus rattus)]
IVGGYKCEKNSQPWQVAVINEYLCGGVLIDPSWVITAAHCYSNNYQVLLGRNNLFKDEPFAQRRLVRQSFRHPDYIPLPVHDHSNDLMLLHLSEPADITGGVKVIDLPTKEPKVGSTCLASGWGSTNPSEMVVSHDLQCVNIHLLSNEKCIETYKDNVTDVMLCAGEMEGGKDTCAGDSGGPLICDGVLQGITSGGATPCAKPKTPAIYAKLIKFTSWIKKVMKENP
>d1mcta_ 2.31.1.2.2 Trypsin(ogen) [porcine (Sus scrofa)]
IVGGYTCAANSIPYQVSLNSGSHFCGGSLINSQWVVSAAHCYKSRIQVRLGEHNIDVLEGNEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRSCAAAGTECLISGWGNTKSSGSSYPSLLQCLKAPVLSNSSCKSSYPGQITGNMICVGFLQGGKDSCQGDSGGPVVCNGQLQGIVSWGYGCAQKNKPGVYTKVCNYVNWIQQTIAAN
>d1dst__ 2.31.1.2.20 Factor D [Human (Homo sapiens)]
ILGGREAEAHARPYMASVQLNGAHLCGGVLVAEQWVLSAAHCLEDAADGKVQVLLGAHSLSQPEPSKRLYDVLRAVPHPDYQPDTIDHDLLLLQLSEKATLGPAVRPLPWQRVDRDVAPGTLCDVAGWGIVNHAGRRPDSLQHVLLPVLDRATCNRRTHHDGAITERLMCAESNRRDSCKGDSGGPLVCGGVLEGVVSWGSRVCGNRKKPGIYTRVASYAAWIDSVLA
>d1ao5a_ 2.31.1.2.22 Kallikrein-13 [mouse (Mus musculus)]
VVGGFNCEKNSQPWQVAVYYQKEHICGGVLLDRNWVLTAAHCYVDQYEVWLGKNKLFQEEPSAQHRLVSKSFPHPGFNMSLLMLQTIPPGADFSDDLMLLRLSKPADITDVVKPIALPTKEPKPGSKCLASGWGSITPTWQKPDDLQCVFITLLPNENCAKVYLQKVTDVMLCAGEMGGGKDTCRDDSGGPLICDGILQGTTSYGPVPCGKPGVPAIYTNLIKFNSWIKDTMMKNA
>d1hcga_ 2.31.1.2.23 Coagulation factor Xa (Chrismas factor), protease domain [Human (Homo sapiens)]
IVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDSGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAK
>d1autc_ 2.31.1.2.24 Activated protein c (autoprothrombin IIa) [human (Homo sapiens)]
LIDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDESKKLLVRLGEYDLRRWEKWELDLDIKEVFVHPNYSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGLAERELNQAGQETLVTGWGYHSSREKEAKRNRTFVLNFIKIPVVPHNECSEVMSNMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWIHGHIRD
>d1fuja_ 2.31.1.2.25 Myeloblastin, PR3 [human (Homo sapiens)]
IVGGHEAQPHSRPYMASLQMRGNPGSHFCGGTLIHPSFVLTAAHCLRDIPQRLVNVVLGAHNVRTQEPTQQHFSVAQVFLNNYDAENKLNDILLIQLSSPANLSASVATVQLPQQDQPVPHGTQCLAMGWGRVGAHDPPAQVLQELNVTVVTFFCRPHNICTFVPRRKAGICFGDSGGPLICDGIIQGIDSFVIWGCATRLFPDFFTRVALYVDWIRSTLR
>d1pfxc_ 2.31.1.2.26 Coagulation factor IXa, protease domain [Pig (Sus scrofa)]
IVGGENAKPGQFPWQVLLNGKIDAFCGGSIINEKWVVTAAHCIEPGVKITVVAGEYNTEETEPTEQRRNVIRAIPHHSYNATVNKYSHDIALLELDEPLTLNSYVTPICIADKEYTNIFLKFGSGYVSGWGRVFNRGRSATILQYLKVPLVDRATCLRSTKFTIYSNMFCAGFHEGGKDSCQGDSGGPHVTEVEGTSFLTGIISWGEECAVKGKYGIYTKVSRYVNWIKEKTKLT
>d1brbe_ 2.31.1.2.3 Trypsin(ogen) [rat (Rattus rattus)]
IVGGYTCQENSVPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKSRIQVRLGEHNINVLEGNEQFVNAAKIIKHPNFDRKTLNNDIMLIKLSSPVKLNARVATVALPSSCAPAGTQCLISGWGNTLSSGVNEPDLLQCLDAPLLPQADCEASYPGKITDNMVCVGFLEGGKGSCQGDSGGPVVCNGELQGIVSWGYGCALPDNPDVYTKVCNYVDWIQDTIAAN
>d1trna_ 2.31.1.2.4 Trypsin(ogen) [human (Homo sapiens)]
IVGGYNCEENSVPYQVSLNSGYHFCGGSLINEQWVVSAGHCYKSRIQVRLGEHNIEVLEGNEQFINAAKIIRHPQYDRKTLNNDIMLIKLSSRAVINARVSTISLPTAPPATGTKCLISGWGNTASSGADYPDELQCLDAPVLSQAKCEASYPGKITSNMFCVGFLEGGKDSCQGDSGGPVVCNGQLQGVVSWGDGCAQKNKPGVYTKVYNYVKWIKNTIAANS
>d2tbs__ 2.31.1.2.5 Trypsin(ogen) [north atlantic salmon (Salmo salar)]
IVGGYECKAYSQAHQVSLNSGYHFCGGSLVNENWVVSAAHCYKSRVEVRLGEHNIKVTEGSEQFISSSRVIRHPNYSSYNIDNDIMLIKLSKPATLNTYVQPVALPTSCAPAGTMCTVSGWGNTMSSTADSDKLQCLNIPILSYSDCNDSYPGMITNAMFCAGYLEGGKDSCQGDSGGPVVCNGELQGVVSWGYGCAEPGNPGVYAKVCIFSDWLTSTMASY
>d1try__ 2.31.1.2.6 Trypsin(ogen) [mold (Fusarium oxysporum)]
IVGGTSASAGDFPFIVSISRNGGPWCGGSLLNANTVLTAAHCVSGYAQSGFQIRAGSLSRTSGGITSSLSSVRVHPSYSGNNNDLAILKLSTSIPSGGNIGYARLAASGSDPVAGSSATVAGWGATSEGGSSTPVNLLKVTVPIVSRATCRAQYGTSAITNQMFCAGVSSGGKDSCQGDSGGPIVDSSNTLIGAVSWGNGCARPNYSGVYASVGALRSFIDTYA
>d1pytd_ 2.31.1.2.7 (alpha, gamma-)chymotrypsin(ogen) [bovine (Bos taurus)]
CGAPIFQPNLSARVVGGEDAIPHSWPWQISLQYLRDNTWRHTCGGTLITPNHVLTAAHCISNTLTYRVALGKNNLEVEDEAGSLYVGVDTIFVHEKWNSFLVRNDIALIKLAETVELGDTIQVACLPSEGSLLPQDYPCFVTGWGRLYTNGPIAAELQQGLQPVVDYATCSQRDWWGTTVKETMVCAGGDGVISACNGDSGGPLNCQADGQWDVRGIVSFGSGLSCNTFKKPTVFTRVSAYIDWINQKLQL
>d1gcta_ 2.31.1.2.7 (alpha, gamma-)chymotrypsin(ogen) [bovine (Bos taurus)]
CGVPAIQPVLIVNGEEAVPGSWPWQVSLQDKTGFHFCGGSLINENWVVTAAHCGVTTSDVVVAGEFDQGSSSEKIQKLKIAKVFKNSKYNSLTINNDITLLKLSTAASFSQTVSAVCLPSASDDFAAGTTCVTTGWGLTRYTPDRLQQASLPLLSNTNCKKYWGTKIKDAMICAGASGVSSCMGDSGGPLVCKKNGAWTLVGIVSWGSSTCSTSTPGVYARVTALVNWVQQTLAAN
>d1hyla_ 2.31.1.2.8 HL collagenase [Common cattle grub (Hypoderma lineatum)]
IINGYEAYTGLFPYQAGLDITLQDQRRVWCGGSLIDNKWILTAAHCVHDAVSVVVYLGSAVQYEGEAVVNSERIISHSMFNPDTYLNDVALIKIPHVEYTDNIQPIRLPSGEELNNKFENIWATVSGWGQSNTDTVILQYTYNLVIDNDRCAQEYPPGIIVESTICGDTSDGKSPCFGDSGGPFVLSDKNLLIGVVSFVSGAGCESGKPVGFSRVTSYMDWIQQNTGIKF
>d1hbt.1 2.31.1.2.9 (l,h) Thrombin [human (Homo sapiens)]
ADCGLRPLFEKKSLEDKTERELLESYIISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKEGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQFADCGLRPLFEKKSLEDKTERELLESYIISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKEGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQF
>d2snv__ 2.31.1.3.1 viral capsid protein [sindbis virus]
RLFDVKNEDGDVIGHALAMEGKVMKPLHVKGTIDHPVLSKLKFTKSSAYDMEFAQLPVNMRSEAFTYTSEHPEGFYNWHHGAVQYSGGRFTIPRGVGGRGDSGRPIMDNSGRVVAIVLGGADEGTRTALSVVTWNSKGKTIKTTPEGTEEW
>d1vcpa_ 2.31.1.3.2 viral capsid protein [(Semliki forest virus)]
CIFEVKHEGKVTGYACLVGDKVMKPAHVKGVIDNADLAKLAFKKSSKYDLECAQIPVHMRSDASKYTHEKPEGHYNWHHGAVQYSGGRFTIPTGAGKPGDSGRPIFDNKGRVVAIVLGGANEGSRTALSVVTWNKDMVTRVTPEGSEEW
>d1hava_ 2.31.1.4.2 3C cysteine protease (picornain 3C) [Human hepatitis A virus]
STLEIAGLVRKNLVQFGVGEKNGSVRWVMNALGVKDDWLLVPSHAYKFEKDYEMMEFYFNRGGTYYSISAGNVVIQSLDVGFQDVVLMKVPTIPKFRDITQHFIKKGDVPRALNRLATLVTTVNGTPMLISEGPLKMEEKATYVHKKNDGTTVDLTVDQAWRGKGEGLPGMCGGALVSSNQSIQNAILGIHVAGGNSILVAKLVTQEMFQNIDKKI
>d1bco_1 2.32.1.1.1 (216-295) Mu transposase, C-terminal domain [Bacteriophage mu]
TEEQKRMLLLPAEAVNVSRKGEFTLKVGGSLKGAKNVYYNMALMNAGVKKVVVRFDPQQLHSTVYCYTLDGRFICEAECL
>d1bmfd2 2.33.1.1.1 (1-73) The N-terminal domain of alpha and beta subunits of F1 ATP synthase [bovine (Bos taurus)]
TTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAP
>d1bmfa2 2.33.1.1.1 (1-71) The N-terminal domain of alpha and beta subunits of F1 ATP synthase [bovine (Bos taurus)]
DLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAI
>d1sfta1 2.33.2.1.1 (1-10,244-382) Alanine racemase, C-terminal domain [Bacillus stearothermophilus]
NDFHRDTWAEHFHVLVDGQKAPIVGRICMDQCMIRLPGPLPVGTKVTLIGRQGDEVISIDDVARHLETINYEVPCTISYRVPRIFFRHKRIMEVRNAIGA
>d4hvpa_ 2.34.1.1.1 Human immunodeficiency virus type 1 protease [HIV-1]
PQITLWQRPLVTIRIGGQLKEALLDTGADDTVLEEMNLPGKWKPKMIGGIGGFIKVRQYDQIPVEIGHKAIGTVLVGPTPVNIIGRNLLTQIGTLNF
>d1hiha_ 2.34.1.1.1 Human immunodeficiency virus type 1 protease [HIV-1]
PQITLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMSLPGRWKPKMIGGIGGFIKVRQYDQILIEICGHKAIGTVLVGPTPVNIIGRNLLTQIGCTLNF
>d1fiva_ 2.34.1.1.2 Feline immunodeficiency virus (FIV) protease [Feline (Felis catus) immunodeficiency virus]
VGTTTTLEKRPEILIFVNGYPIKFLLDTGADITILNRRDFQVKNSIENGRQNMIGVGGGKRGTNYINVHLEIRDENYKTQCIFGNVCVLEDNSLIQPLLGRDNMIKFNIRLVM
>d1idaa_ 2.34.1.1.3 Human immunodeficiency virus type 2 protease [HIV-2 (rod isolate)]
PQFSLWKRPVVTAYIEGQPVEVLLDTGADDSIVAGIELGNNYSPKIVGGIGGFINTKEYKNVEIEVLNKKVRATIMTGDTPINIFGRNILTALGMSLNL
>d2rspa_ 2.34.1.1.4 Rous sarcoma virus protease [rous sarcoma virus (Strain pr-C)]
LAMTMEHKDRPLVRVILTNTGSHPVKQRSVYITALLDSGADITIISEEDWPTDWPVMEAAGIPMRKSRDMIELGVINRDGSLERPLLLFPAVAMVRGSILGRDCLQGLGLRLTNL
>d2sam__ 2.34.1.1.6 Simian immunodeficiency virus (SIV) protease [simian immunodeficiency virus (Mac251 isolate)]
PQFHLWKRPVVTAHIEGQPVEVLLDTGADDSIVTGIELGPHYTPKIVGGIGGFINTKEYKNVEIEVLGKRIKGTIMTGDTPINIFGRNLLTALGMSLNF
>d1fmb__ 2.34.1.1.7 EIAV protease [Equine infection anemia virus, EIAV]
VTYNLEKRPTTIVLINDTPLNVLLDTGADTSVLTTAHYNRLKYRGRKYQGTGIGGVGGNVETFSTPVTIKKKGRHIKTRMLVADIPVTILGRDILQDLGAKLVL
>d1epne_ 2.34.1.2.1 Endothiapepsin [chestnut blight fungus (Endothia parasitica)]
STGSATTTPIDSLDDAYITPVQIGTPAQTLNLDFDTGSSDLWVFSSETTASEVDGQTIYTPSKSTTAKLLSGATWSISYGDGSSSSGDVYTDTVSVGGLTVTGQAVESAKKVSSSFTEDSTIDGLLGLAFSTLNTVSPTQQKTFFDNAKASLDSPVFTADLGYHAPGTYNFGFIDTTAYTGSITYTAVSTKQGFWEWTSTGYAVGSGTFKSTSIDGIADTGTTLLYLPATVVSAYWAQVSGAKSSSSVGGYVFPCSATLPSFTFGVGSARIVIPGDYIDFGPISTGSSSCFGGIQSSAGIGINIFGDVALKAAFVVFNGATTPTLGFASK
>d1lya.1 2.34.1.2.10 (a,b) Cathepsin D [human (Homo sapiens)]
GPIPEVLKNYMDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLDIACWIHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLSQDTVSVPCQAAKFDGILGMAYPRISVNNVLPVFDNLMQQKLVDQNIFSFYLSRDPDAQPGGELMLGGTDSKYYKGSLSYLNVTRKAYWQVHLDQVEVASGLTLCKEGCEAIVDTGTSLMVGPVDEVRELQKAIGAVPLIQGEYMIPCEKVSTLPAITLKLGGKGYKLSPEDYTLKVSQAGKTLCLSGFMGMDIPPPSGPLWILGDVFIGRYYTVFDRDNNRVGFAEAAGPIPEVLKNYMDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLDIACWIHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLSQDTVSVPCQAAKFDGILGMAYPRISVNNVLPVFDNLMQQKLVDQNIFSFYLSRDPDAQPGGELMLGGTDSKYYKGSLSYLNVTRKAYWQVHLDQVEVASGLTLCKEGCEAIVDTGTSLMVGPVDEVRELQKAIGAVPLIQGEYMIPCEKVSTLPAITLKLGGKGYKLSPEDYTLKVSQAGKTLCLSGFMGMDIPPPSGPLWILGDVFIGRYYTVFDRDNNRVGFAEAA
>d3cms__ 2.34.1.2.11 Chymosin (synonim: renin) [bovine (Bos taurus)]
GEVASVPLTNYLDSQYFGKIYLGTPPQEFTVLFDTGSSDFWVPSIYCKSNACKNHQRFDPRKSSTFQNLGKPLSIHYGTGSMQGILGYDTVTVSNIVDIQQTVGLSTQEPGDFFTYAEFDGILGMAYPSLASEYSIPVFDNMMNRHLVAQDLFSVYMDRNGQESMLTLGAIDPSYYTGSLHWVPVTVQQYWQFTVDSVTISGVVVACEGGCQAILDTGTSKLVGPSSDILNIQQAIGATQNQYGEFDIDCDNLSYMPTVVFEINGKMYPLTPSAYTSQDQGFCTSGFQSEQKWILGDVFIREYYSVFDRANNLVGLAKAI
>d1hrna_ 2.34.1.2.12 Chymosin (synonim: renin) [human (Homo sapiens)]
GNTTSSVILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSNVWVPSSKCSRLYTACVYHKLFDASDSSSYKHNGTELTLRYSTGTVSGFLSQDIITVGGITVTQMFGEVTEMPALPFMLAEFDGVVGMGFIEQAIGRVTPIFDNIISQGVLKEDVFSFYYNRDSESLGGQIVLGGSDPQHYEGNFHYINLIKTGVWQIQMKGVSVGSSTLLCEDGCLALVDTGASYISGSTSSIEKLMEALGAKKRLFDYVVKCNEGPTLPDISFHLGGKEYTLTSADYVFQESYSSKKLCTLAIHAMDIPPPTGPTWALGATFIRKFYTEFDRRNNRIGFALAR
>d1smra_ 2.34.1.2.13 Chymosin (synonim: renin) [mouse (Mus musculus)]
TDLISPVVLTNYLNSQYYGEIGIGTPPQTFKVIFDTGSANLWVPSTKCSRLYLACGIHSLYESSDSSSYMENGDDFTIHYGSGRVKGFLSQDSVTVGGITVTQTFGEVTQLPLIPFMLAQFDGVLGMGFPAQAVGGVTPVFDHILSQGVLKEKVFSVYYNRGPHLLGGEVVLGGSDPQHYQGDFHYVSLSKTDSWQITMKGVSVGSSTLLCEEGCEVVVDTGSSFISAPTSSLKLIMQALGAKEKRLHEYVVSCSQVPTLPDISFNLGGRAYTLSSTDYVLQRDKLCTVALHAMDIPPPTGPVWVLGATFIRKFYTEFDRHNNRIGFALAR
>d1smea_ 2.34.1.2.14 Plasmepsin ii (a hemoglobin-degrading enzyme) [(Plasmodium falciparum)]
SSNDNIELVDFQNIMFYGDAEVGDNQQPFTFILDTGSANLWVPSVKCTTAGCLTKHLYDSSKSRTYEKDGTKVEMNYVSGTVSGFFSKDLVTVGNLSLPYKFIEVIDTNGFEPTYTASTFDGILGLGWKDLSIGSVDPIVVELKNQNKIENALFTFYLPVHDKHTGFLTIGGIEERFYEGPLTYEKLNHDLYWQITLDAHVGNIMLEKANCIVDSGTSAITVPTDFLNKMLQNLDVIKVPFLPFYVTLCNNSKLPTFEFTSENGKYTLEPEYYLQHIEDVGPGLCMLNIIGLDFPVPTFILGDPFMRKYFTVFDYDNHSVGIALAKKNL
>d1ppme_ 2.34.1.2.2 Acid protease [fungus (Penicillium janthinellum)]
AASGVATNTPTANDEEYITPVTIGGTTLNLNFDTGSADLWVFSTELPASQQSGHSVYNPSATGKELSGYTWSISYGDGSSASGNVFTDSVTVGGVTAHGQAVQAAQQISAQFQQDTNNDGLLGLAFSSINTVQPQSQTTFFDTVKSSLAQPLFAVALKHQQPGVYDFGFIDSSKYTGSLTYTGVDNSQGFWSFNVDSYTAGSQSGDGFSGIADTGTTLLLLDDSVVSQYYSQVSGAQQDSNAGGYVFDCSTNLPDFSVSISGYTATVPGSLINYGPSGDGSTCLGGIQSNSGIGFSIFGDIFLKSQYVVFDSDGPQLGFAPQA
>d2apr__ 2.34.1.2.3 Acid protease [bread mold (Rhizopus chinensis)]
AGVGTVPMTDYGNDIEYYGQVTIGTPGKKFNLDFDTGSSDLWIASTLCTNCGSGQTKYDPNQSSTYQADGRTWSISYGDGSSASGILAKDNVNLGGLLIKGQTIELAKREAASFASGPNDGLLGLGFDTITTVRGVKTPMDNLISQGLISRPIFGVYLGKAKNGGGGEYIFGGYDSTKFKGSLTTVPIDNSRGWWGITVDRATVGTSTVASSFDGILDTGTTLLILPNNIAASVARAYGASDNGDGTYTISCDTSAFKPLVFSINGASFQVSPDSLVFEEFQGQCIAGFGYGNWGFAIIGDTFLKNNYVVFNQGVPEVQIAPVAE
>d2asi__ 2.34.1.2.4 Acid protease [Rhizomucor miehei]
GSVDTPGYYDFDLEEYAIPVSIGTPGQDFLLLFDTGSSDTWVPHKGCTKSEGCVGSRFFDPSASSTFKATNYNLNITYGTGANGLYFEDSIAIGDITVTKQILAYVDNVRGPTAEQSPNADIFLDGLFGAAYPDNTAMEAEYGSTYNTVHVNLYKQGLISSPLFSVYMNTNSGTGEVVFGGVNNTLLGGDIAYTDVMSRYGGYYFWDAPVTGITVDGSAAVRFSRPQAFTIDTGTNFFIMPSSAASKIVKAALPDATETQQGWVVPCASYQNSKSTISIVMQKSGSSSDTIEISVPVSKMLLPVDQSNETCMFIILPDGGNQYIVGNLFLRFFVNVYDFGNNRIGFAPLASAYENE
>d1eaga_ 2.34.1.2.5 Acid protease [yeast (Candida albicans)]
QAVPVTLHNEQVTYAADITVGSNNQKLNVIVDTGSSDLWVPDVNVDCQVTYSDQTADFCKQKGTYDPSGSSASQDLNTPFKIGYGDGSSSQGTLYKDTVGFGGVSIKNQVLADVDSTSIDQGILGVGYKTNEAGGSYDNVPVTLKKQGVIAKNAYSLYLNSPDAATGQIIFGGVDNAKYSGSLIALPVTSDRELRISLGSVEVSGKTINTDNVDVLLDSGTTITYLQQDLADQIIKAFNGKLTQDSNGNSFYEVDCNLSGDVVFNFSKNAKISVPASEFAASLDGQPYDKCQLLFDVNDANILGDNFLRSAYIVYDLDDNEISLAQVKYTSASSISALT
>d3psg__ 2.34.1.2.6 Pepsin(ogen) [pig (Sus scrofa)]
LVKVPLVRKKSLRQNLIKDGKLKDFLKTHKHNPASKYFPEAAALIGDEPLENYLDTEYFGTIGIGTPAQDFTVIFDTGSSNLWVPSVYCSSLACSDHNQFNPDDSSTFEATSQELSITYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSISASGATPVFDNLWDQGLVSQDLFSVYLSGSVVLLGGIDSSYYTGSLNWVPVSVEGYWQITLDSITMDGETIACSGGCQAIVDTGTSLLTGPTSAIANIQSDIGASENSDGEMVISCSSIDSLPDIVFTIDGVQYPLSPSAYILQDDDSCTSGFEGMDVPTSSGELWILGDVFIRQYYTVFDRANNKVGLAPVA
>d1psoe_ 2.34.1.2.7 Pepsin(ogen) [human (Homo sapiens) 3A]
VDEQPLENYLDMEYFGTIGIGTPAQDFTVVFDTGSSNLWVPSVYCSSLACTNHNRFNPEDSSTYQSTSETVSITYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSISSSGATPVFDNIWNQGLVSQDLFSVYLSADDQSGSVVIFGGIDSSYYTGSLNWVPVTVEGYWQITVDSITMNGEAIACAEGCQAIVDTGTSLLTGPTSPIANIQSDIGASENSDGDMVVSCSAISSLPDIVFTINGVQYPVPPSAYILQSEGSCISGFQGMNLPTESGELWILGDVFIRQYFTVFDRANNQVGLAPVA
>d1htr.1 2.34.1.2.8 (p,b) Pepsin(ogen) [human (Homo sapiens) progastricsin (pepsinogen C)]
AVVKVPLKKFKSIRETMKEKGLLGEFLRTHKYDPAWKYRFGDLEISIGTPPQNFLVLFDTGSSNLWVPSVYCQSQACTSHSRFNPSESSTYSTNGQTFSLQYGSGSLTGFFGYDTLTVQSIQVPNQEFGLSENEPGTNFVYAQFDGIMGLAYPALSVDEATTAMQGMVQEGALTSPVFSVYLSNQQGSSGGAVVFGGVDSSLYTGQIYWAPVTQELYWQIGIEEFLIGGQASGWCSEGCQAIVDTGTSLLTVPQQYMSALLQATGAQEDEYGQFLVNCNSIQNLPSLTFIINGVEFPLPPSSYILSNNGYCTVGVEPTYLSSQNGQPLWILGDVFLRSYYSVYDLGNNRVGFATAAAVVKVPLKKFKSIRETMKEKGLLGEFLRTHKYDPAWKYRFGDLEISIGTPPQNFLVLFDTGSSNLWVPSVYCQSQACTSHSRFNPSESSTYSTNGQTFSLQYGSGSLTGFFGYDTLTVQSIQVPNQEFGLSENEPGTNFVYAQFDGIMGLAYPALSVDEATTAMQGMVQEGALTSPVFSVYLSNQQGSSGGAVVFGGVDSSLYTGQIYWAPVTQELYWQIGIEEFLIGGQASGWCSEGCQAIVDTGTSLLTVPQQYMSALLQATGAQEDEYGQFLVNCNSIQNLPSLTFIINGVEFPLPPSSYILSNNGYCTVGVEPTYLSSQNGQPLWILGDVFLRSYYSVYDLGNNRVGFATAA
>d1mpp__ 2.34.1.2.9 Pepsin [Mucor pusillus]
GSVDTPGLYDFDLEEYAIPVSIGTPGQDFYLLFDTGSSDTWVPHKGCDNSEGCVGKRFFDPSSSSTFKETDYNLNITYGTGGANGIYFRDSITVGGATVKQQTLAYVDNVSGPTAEQSPDSELFLDGIFGAAYPDNTAMEAEYGDTYNTVHVNLYKQGLISSPVFSVYMNTNDGGGQVVFGGVNNTLLGGDIQYTDVLKSRGGYFFWDAPVTGVKIDGSDAVSFDGAQAFTIDTGTNFFIAPSSFAEKVVKAALPDATESQQGYTVPCSKYQDSKTTFSLVLQKSGSSSDTIDVSVPISKMLLPVDKSGETCMFIVLPDGGNQFIVGNLFLRFFVNVYDFGKNRIGFAPLASGYEND
>d2eng__ 2.35.1.1.1 Endoglucanase V [Humicola insolens]
ADGRSTRYWDCCKPSCGWAKKAPVNQPVFSCNANFQRITDFDAKSGCEPGGVAYSCADQTPWAVNDDFALGFAATSIAGSNEAGWCCACYELTFTSGPVAGKKMVVQSTSTSNHFDLNIPGGGVGIFDGCTPQFGGLPGQRYGGISSRNECDRFPDALKPGCYWRFDWFKNADNPSFSFRQVQCPAELVARTGCRRNDDGNFPAV
>d1bw3__ 2.35.1.2.1 Barwin [barley (Hordeum vulgare)]
EQANDVRATYHYYRPAQNNWDLGAPAVSAYCATWDASKPLSWRSKYGWTAFCGPAGPRGQAACGKCLRVTNPATGAQITARIVDQCANGGLDLDWDTVFTKIDTNGIGYQQGHLNVNYQFVDCRD
>d1cxsa1 2.35.2.1.1 (614-768) Dimethylsulfoxide reductase (DMSO reductase) [Rhodobacter sphaeroides]
ERLGGAGAKYPLHVVASHPKSRLHSQLNGTSLRDLYAVAGHEPCLINPADAAARGIADGDVLRVFNDRGQILVGAKVSDAVMPGAIQIYEGGWYDPLDPSEEGTLDKYGDVNVLSLDVGTSKLAQGNCGQTILADVEKYAGAPVTVTVFDTPKGA
>d1fdo_1 2.35.2.1.2 (564-714) Formate dehydrogenase H [Escherichia coli]
PIDKLTDEYPMVLSTVREVGHYSCRSMTGNCAALAALADEPGYAQINTEDAKRLGIEDEALVWVHSRKGKIITRAQVSDRPNKGAIYMTYQWWIGACNELVTENLSPITKTPEYKYCAVRVEPIADQRAAEQYVIDEYNKLKTRLREAALA
>d1gtra1 2.36.1.1.1 (332-529) Gln-tRNA synthetase (GlnRS), C-terminal (anticodon-binding) domain [Escherichia coli]
APRAMAVIDPVKLVIENYQGEGEMVTMPNHPNKPEMGSRQVPFSGEIWIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDAEGNITTIFCTYDADTLGVIHWVSAAHALPVEIRLYDRLFSVPNPGAADDFLSVINPESLVIKQGFAEPSLKDAVAGKAFQFEREGYFCLDSRHSTAEKPVFNRTVGLRDT
>d1mai__ 2.37.1.1.1 Phospholipase C delta-1 [Rat (Rattus norvegicus)]
GLQDDPDLQALLKGSQLLKVKSSSWRRERFYKLQEDCKTIWQESRKVMRSPESQLFSIEDIQEVRMGHRTEGLEKFARDIPEDRCFSIVFKDQRNTLDLIAPSPADAQHWVQGLRKIIH
>d1btn__ 2.37.1.1.2 beta-spectrin [mouse (Mus musculus) brain]
MEGFLNRKHEWEAHNKKASSRSWHNVYCVINNQEMGFYKDAKSAASGIPYHSEVPVSLKEAICEVALDYKKKKHVFKLRLSDGNEYLFQAKDDEEMNTWIQAISSA
>d1dro__ 2.37.1.1.3 beta-spectrin [fruit fly (Drosophila melanogaster)]
GSGTGAGEGHEGYVTRKHEWDSTTKKASNRSWDKVYMAAKAGRISFYKDQKGYKSNPELTFRGEPSYDLQNAAIEIASDYTKKKHVLRVKLANGALFLLQAHDDTEMSQWVTSLKAQSDSTA
>d1dyna_ 2.37.1.1.4 Dynamin [Human (Homo sapiens)]
ILVIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKDYRQLELACETQEEVDSWKASFLRAGVYPERV
>d1btka_ 2.37.1.1.5 Bruton's tyrosine kinase [Human (Homo sapiens)]
AAVILESIFLKRSQQKKKTSPLNFKKCLFLLTVHKLSYYEYDFERGRRGSKKGSIDVEKITCVETVVPEKNPPPERQIMEQISIIERFPYPFQVVYDEGPLYVFSPTEELRKRWIHQLKNVIRYNSDLVQKYHPCFWIDGQYLCCSQTAKNAMGCQILEN
>d1pls__ 2.37.1.1.6 Pleckstrin, N-terminal domain [Human (Homo sapiens)]
MEPKRIREGYLVKKGSVFNTWKPMWVVLLEDGIEFYKKKSDNSPKGMIPLKGSTLTSPCQDFGKRMFVFKITTTKQQDHFFQAAFLEERDAWVRDINKAIKCIEGLEHHHHHH
>d1pms__ 2.37.1.1.7 Son of sevenless 1 (sos1) [mouse (Mus musculus)]
SKQLAIKKMNEIQKNIDGWEGKDIGQCCNEFIMEGTLTRVGAKHERHIFLFDGLMICCKSNHGQPRLPGASSAEYRLKEKFFMRKVQINDKDDTSEYKHAFEIILKDGNSVIFSAKSAEEKNNWMAALISLQYRS
>d1irsa_ 2.37.1.2.1 Insulin receptor substrate 1, IRS-1 [human (Homo sapiens)]
MGPAFKEVWQVILKPKGLGQTKNLIGIYRLCLTSKTISFVKLNSEAAAVVLQLMNIRRCGHSENFFFIEVGRSAVTGPGEFWMQVDDSVVAQNMHETILEAMRAMSDEFRPR
>d1shca_ 2.37.1.2.2 The adaptor protein Shc [Human (Homo sapiens)]
GSHMGQLGGEEWTRHGSFVNKPTRGWLHPNDKVMGPGVSYLVRYMGCVEVLQSMRALDFNTRTQVTREAISLVCEAVPGAKGATRRRKPCSRPLSSILGRSNLKFAGMPITLTVSTSSLNLMAADCKQIIANHHMQSISFASGGDPDTAEYVAYVAKDPVNQRACHILECPEGLAQDVISTIGQAFELRFKQYLR
>d1ytfc1 2.38.1.1.1 Transcription factor IIA (TFIIA), N-terminal domain [Baker's yeast (Schaccharomyces cerevisiae)]
ENLMLCLYDKVTRTKARWKCSLKDGVVTINRNDYTFQKAQVEAEWV
>d1ytfd2 2.38.1.1.1 (51-100) Transcription factor IIA (TFIIA), N-terminal domain [Baker's yeast (Schaccharomyces cerevisiae)]
NTQSKLTVKGNLDTYGFCDDVWTFIVKNCQVTVESVISVDKLRIVACNSK
>d1wpoa_ 2.39.1.1.1 Human cytomegalovirus protease [Human cytomegalovirus), hCMV]
QAVAPVYVGGFLARYDQSLLPRDVVEHWLHAVALPLNINHDDTAVVGHVAAQSVRDGLFCLGCVTSPRFLEIVRRASEKSELVSRGPVSPLQPDKVVEFLSGSYAGLSLSSTPFKHVALCSVGRRRGTLAVYGRDPEWVQRFPDLTAADRDGLRAQWQRGDPFRSDSYGLLGNSVDAYIRERLPKLRYDKQLVGVTERESYVKA
>d1hoe__ 2.4.1.1.1 HOE-467A [Streptomyces tendae 4158]
DTTVSEPAPSCVTLYQSWRYSQADNGCAETVTVKVVYEDDTEGLCYAVAPGQITTVGDGYIGSHGHARYLARCL
>d1pkm_1 2.40.1.1.2 (105-206) Pyruvate kinase [cat (Felis domestica)]
PEIRTGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENVLWLDYKNICKVVEVGSKVYVDDGLISLLVKEKGADFLVTEVENGGSLGSKKGVNLPGAAVDL
>d1pkya1 2.40.1.1.3 (70-167) Pyruvate kinase [Escherichia coli]
PEIRTMKLEGGNDVSLKAGQTFTFTTDKSVIGNSEMVAVTYEGFTTDLSVGNTVLVDDGLIGMEVTAIEGNKVICKVLNNGDLGENKGVNLPGVSIAL
>d1hbp__ 2.41.1.1.1 Retinol binding protein [bovine (Bos taurus)]
ERDCRVSSFRVKENFDKARFAGTWYAMAKKDPEGLFLQDNIVAEFSVDENGHMSATAKGRVRLLNNWDVCADMVGTFTDTEDPAKFKMKYWGVASFLQKGNDDHWIIDTDYETFAVQYSCRLLNLDGTCADSYSFVFARDPSGFSPEVQKIVRQRQEELCLARQYRLIPHNGYC
>d1rbp__ 2.41.1.1.2 Retinol binding protein [human (Homo sapiens)]
ERDCRVSSFRVKENFDKARFSGTWYAMAKKDPEGLFLQDNIVAEFSVDETGQMSATAKGRVRLLNNWDVCADMVGTFTDTEDPAKFKMKYWGVASFLQKGNDDHWIVDTDYDTYAVQYSCRLLNLDGTCADSYSFVFSRDPNGLPPEAQKIVRQRQEELCLARQYRLIVHNGYC
>d1obpa_ 2.41.1.1.4 Odorant-binding protein [Bovine (Bos taurus)]
QEEEAEQNLSELSGPWRTVYIGSTNPEKIQENGPFRTYFRELVFDDEKGTVDFYFSVKRDGKWKNVHVKATKQDDGTYVADYEGQNVFKIVSLSRTHLVAHNINVDKHGQTTELTGLFVKLNVEDEDLEKFWKLTEDKGIDKKNVVNFLENEDHPHPE
>d1beba_ 2.41.1.1.5 beta-Lactoglobulin [Bovine (Bos taurus)]
QTMKGLDIQKVAGTWYSLAMAASDISLLDAQSAPLRVYVEELKPTPEGDLEILLQKWENGECAQKKIIAEKTKIPAVFKIDALNENKVLVLDTDYKKYLLFCMENSAEPEQSLVCQCLVRTPEVDDEALEKFDKALKALPMHIRLSFNPTQLEEQC
>d1bbpa_ 2.41.1.1.6 Bilin-binding protein [cabbage butterfly (Pieris brassicae)]
NVYHDGACPEVKPVDNFDWSNYHGKWWEVAKYPNSVEKYGKCGWAEYTPEGKSVKVSNYHVIHGKEYFIEGTAYPVGDSKIGKIYHKLTYGGVTKENVFNVLSTDNKNYIIGYYCKYDEDKKGHQDFVWVLSRSKVLTGEAKTAVENYLIGSPVVDSQKLVYSDFSEAACKVN
>d1epba_ 2.41.1.1.7 Retinoic acid-binding protein [rat (Rattus norvegicus, albino)]
VKDFDISKFLGFWYEIAFASKMGTPGLAHKEEKMGAMVVELKENLLALTTTYYSEDHCVLEKVTATEGDGPAKFQVTRLSGKKEVVVEATDYLTYAIIDITSLVAGAVHRTMKLYSRSLDDNGEALYNFRKITSDHGFSETDLYILKHDLTCVKVLQSAA
>d1mup__ 2.41.1.1.8 Major urinary protein [mouse (Mus musculus)]
EEASSTGRNFNVEKINGEWHTIILASDKREKIEDNGNFRLFLEQIHVLENSLVLKFHTVRDEECSELSMVADKTEKAGEYSVTYDGFNTFTIPKTDYDNFLMAHLINEKDGETFQLMGLYGREPDLSSDIKERFAQLCEEHGILRENIIDLSNANRC
>d1hms__ 2.41.1.2.1 Muscle fatty acid binding protein (m-fabp) [human (Homo sapiens)]
VDAFLGTWKLVDSKNFDDYMKSLGVGFATRQVASMTKPTTIIEKNGDILTLKTHSTFKNTEISFKLGVEFDETTADDRKVKSIVTLDGGKLVHLQKWDGQETTLVRELIDGKLILTLTHGTAVCTRTYEKE
>d1pmpa_ 2.41.1.2.10 P2 myelin protein [bovine (Bos taurus)caudal spinal root myelin]
SNKFLGTWKLVSSENFDEYMKALGVGLATRKLGNLAKPRVIISKKGDIITIRTESPFKNTEISFKLGQEFEETTADNRKTKSTVTLARGSLNQVQKWNGNETTIKRKLVDGKMVVECKMKDVVCTRIYEKV
>d1eal__ 2.41.1.2.11 Ileal lipid binding protein [pig (Sus scrofa)]
AFTGKYEIESEKNYDEFMKRLALPSDAIDKARNLKIISEVKQDGQNFTWSQQYPGGHSITNTFTIGKECDIETIGGKKFKATVQMEGGKVVVNSPNYHHTAEIVDGKLVEVSTVGGVSYERVSKKLA
>d1ifc__ 2.41.1.2.2 Intestinal fatty acid binding protein [rat (Rattus rattus)]
AFDGTWKVDRNENYEKFMEKMGINVVKRKLGAHDNLKLTITQEGNKFTVKESSNFRNIDVVFELGVDFAYSLADGTELTGTWTMEGNKLVGKFKRVDNGKELIAVREISGNELIQTYTYEGVEAKRIFKKE
>d1lib__ 2.41.1.2.3 Adipocite lipid-binding protein, ALBP [mouse (Mus musculus)]
CDAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDLVTIRSESTFKNTEISFKLGVEFDEITADDRKVKSIITLDGGALVQVQKWDGKSTTIKRKRDGDKLVVECVMKGVTSTRVYERA
>d1mdc__ 2.41.1.2.4 Fatty acid-binding protein [tobacco hornworm (Manduca sexta l.)]
SYLGKVYSLVKQENFDGFLKSAGLSDDKIQALVSDKPTQKMEANGDSYSNTSTGGGGAKTVSFKSGVEFDDVIGAGDSVKSMYTVDGNVVTHVVKGDAGVATFKKEYNGDDLVVTITSSNWDGVARRYYKA
>d1ftpa_ 2.41.1.2.5 Fatty acid-binding protein [desert locust (Schistocerca gregaria)]
VKEFAGIKYKLDSQTNFEEYMKAIGVGAIERKAGLALSPVIELEILDGDKFKLTSKTAIKNTEFTFKLGEEFDEETLDGRKVKSTITQDGPNKLVHEQKGDHPTIIIREFSKEQCVITIKLGDLVATRIYKAQ
>d1cbs__ 2.41.1.2.6 Cellular retinoic-acid-binding protein (CRABP) [Human (Homo sapiens) CRABP-II]
PNFSGNWKIIRSENFEELLKVLGVNVMLRKIAVAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPCKSLVKWESENKMVCEQKLLKGEGPKTSWTRELTNDGELILTMTADDVVCTRVYVRE
>d1cbia_ 2.41.1.2.7 Cellular retinoic-acid-binding protein (CRABP) [bovine/murine (identical sequences) (Bos taurus/Mus musculus) CRABP-I]
PNFAGTWKMRSSENFDELLKALGVNAMLRKVAVAAASKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEGFEEETVDGRKCRSLPTWENENKIHCTQTLLEGDGPKTYWTRELANDELILTFGADDVVCTRIYVRE
>d1opaa_ 2.41.1.2.8 Cellular retinol-binding protein II (CRBP) [rat (Rattus rattus)]
TKDQNGTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKIIVQDGDNFKTKTNSTFRNYDLDFTVGVEFDEHTKGLDGRNVKTLVTWEGNTLVCVQKGEKENRGWKQWVEGDKLYLELTCGDQVCRQVFKKK
>d1crb__ 2.41.1.2.8 Cellular retinol-binding protein II (CRBP) [rat (Rattus rattus)]
PVDFNGYWKMLSNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDLTGIDDRKCMTTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRAEGVTCKQVFKKVH
>d1lfo__ 2.41.1.2.9 Liver fatty acid binding protein [rat (Rattus norvegicus)]
MNFSGKYQVQSQENFEPFMKAMGLPEDLIQKGKDIKGVSEIVHEGKKVKLTITYGSKVIHNEFTLGEEELETMTGEKVKAVVKMEGDNKMVTTFKGIKSVTEFNGDTITNTMTLGDIVYKRVSKRI
>d1sria_ 2.42.1.1.1 Streptavidin [Streptomyces avidinii]
AEAGITGTWYNQLGSTFIVTAGADGALTGTYESAVGNAESRYVLTGRYDSAPASGTALGWTVAWKNNYRNAHSATTWSGQYVGGAEARINTQWLLTSGTTEANAWKSTLVGHDTFTKV
>d2avia_ 2.42.1.1.2 Avidin [hen (Gallus gallus)]
KCSLTGKWTNDLGSNMTIGAVNSRGEFTGTYTTAVTATSNEIKESPLHGTENTINKRTQPTFGFTVNWKFSESTTVFTGQCFIDRNGKEVLKTMWLLRSSVNDIGDDWKATRVGINIFTRL
>d1smpi_ 2.42.2.1.1 Metalloprotease inhibitor [Erwina chrysantemi]
SSLRLPSAAELSGQWVLSGAEQHCDIRLNTDVLDGTTWKLAGDTACLQKLLPEAPVGWRPTPDGLTLTQADGSAVAFFSRNRDRYEHKLVDGSVRTLKKK
>d2cpl__ 2.43.1.1.1 Cyclophilin A [human (Homo sapiens)]
VNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIADCGQLE
>d2rmca_ 2.43.1.1.2 Cyclophilin C [Mouse (Mus musculus)]
KRGPSVTDKVFFDVRIGDKDVGRIVIGLFGNVVPKTVENFVALATGEKGYGYKGSIFHRVIKDFMIQGGDFTARDGTGGMSIYGETFPDENFKLKHYGIGWVSMANAGPDTNGSQFFITLTKPTWLDGKHVVFGKVLDGMTVVHSIELQATDGHDRPLTDCTIVNSGKIDVKTPFVVEVPDW
>d1cyna_ 2.43.1.1.3 Cyclophilin B [Human (Homo sapiens)]
GPKVTVKVYFDLRIGDEDVGRVIFGLFGKTVPKTVDNFVALATGEKGFGYKNSKFHRVIKDFMIQGGDFTRGDGTGGKSIYGERFPDENFKLKHYGPGWVSMANAGKDTNGSQFFITTVKTAWLDGKHVVFGKVLEGMEVVRKVESTKTDSRDKPLKDVIIADCGKIEVEKPFAIAKE
>d1clh__ 2.43.1.1.4 Cyclophilin [Escherichia coli]
AKGDPHVLLTTSAGNIELELDKQKAPVSVQNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQQKKPNPPIKNEADNGLRNTRGTIAMARTADKDSATSQFFINVADNAFLDHGQRDFGYAVFGKVVKGMDVADKISQVPTHDVGPYQNVPSKPVVILSAKVLP
>d1lopa_ 2.43.1.1.4 Cyclophilin [Escherichia coli]
MVTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKEPIKNEANNGLKNTRGTLAMARTQAPHSATAQFFINVVDNDFLNFSGESLQGWGYCVFAEVVDGMDEVDKIKGVATGRSGMHQDVPKEDVIIESVTVSE
>d1hxn__ 2.44.1.1.1 Hemopexin, C-terminal domain [Rabbit (Oryctolagus cuniculus)]
ESTRCDPDLVLSAMVSDNHGATYVFSGSHYWRLDTNRDGWHSWPIAHQWPQGPSTVDAAFSWEDKLYLIQDTKVYVFLTKGGYTLVNGYPKRLEKELGSPPVISLEAVDAAFVCPGSSRLHIMAGRRLWWLDLKSGAQATWTELPWPHEKVDGALCMEKPLGPNSCSTSGPNLYLIHGPNLYCYRHVDKLNAAKNLPQPQRVSRLLGCTH
>d1gen__ 2.44.1.1.2 Gelatinase A (MMP-2), C-terminal domain [human (Homo sapiens)]
LGPVTPEICKQDIVFDGIAQIRGEIFFFKDRFIWRTVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSASTLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC
>d1fbl_1 2.44.1.1.3 (173-367) Collagenase, C-terminal domain [Porcine (Sus scroffa)]
PQTPQVCDSKLTFDAITTLRGELMFFKDRFYMRTNSFYPEVELNFISVFWPQVPNGLQAAYEIADRDEVRFFKGNKYWAVRGQDVLYGYPKDIHRSFGFPSTVKNIDAAVFEEDTGKTYFFVAHECWRYDEYKQSMDTGYPKMIAEEFPGIGNKVDAVFQKDGFLYFFHGTRQYQFDFKTKRILTLQKANSWFNC
>d1pex__ 2.44.1.1.4 Collagenase-3 (MMP-13), C-terminal domain [human (Homo sapiens)]
TPDKCDPSLSLDAITSLRGETMIFKDRFFWRLHPQQVDAELFLTKSFWPELPNRIDAAYEHPSHDLIFIFRGRKFWALNGYDILEGYPKKISELGLPKEVKKISAAVHFEDTGKTLLFSGNQVWRYDDTNHIMDKDYPRLIEEDFPGIGDKVDAVYEKNGYIYFFNGPIQFEYSIWSNRIVRVMPANSILWC
>d2sil__ 2.45.1.1.1 Salmonella sialidase [Salmonella typhimurium, strain lt2]
TVEKSVVFKAEGEHFTDQKGNTIVGSGSGGTTKYFRIPAMCTTSKGTIVVFADARHNTASDQSFIDTAAARSTDGGKTWNKKIAIYNDRVNSKLSRVMDPTCIVANIQGRETILVMVGKWNNNDKTWGAYRDKAPDTDWDLVLYKSTDDGVTFSKVETNIHDIVTKNGTISAMLGGVGSGLQLNDGKLVFPVQMVRTKNITTVLNTSFIYSTDGITWSLPSGYCEGFGSENNIIEFNASLVNNIRNSGLRRSFETKDFGKTWTEFPPMDKKVDNRNHGVQGSTITIPSGNKLVAAHSSAQNKNNDYTRSDISLYAHNLYSGEVKLIDDFYPKVGNASGAGYSCLSYRKNVDKETLYVVYEANGSIEFQDLSRHLPVIKSYN
>d2bat__ 2.45.1.1.2 Influenza neuraminidase [influenza virus A, different strains]
VEYRNWSKPQCQITGFAPFSKDNSIRLSAGGDIWVTREPYVSCDPVKCYQFALGQGTTLDNKHSNDTVHDRIPHRTLLMNELGVPFHLGTRQVCIAWSSSSCHDGKAWLHVCITGDDKNATASFIYDGRLVDSIGSWSQNILRTQESECVCINGTCTVVMTDGSASGRADTRILFIEEGKIVHISPLAGSAQHVEECSCYPRYPGVRCICRDNWKGSNRPVVDINMEDYSIDSSYVCSGLVGDTPRNDDRSSNSNCRNPNNERGTQGVKGWAFDNGNDLWMGRTISKDLRSGYETFKVIGGWSTPNSKSQINRQVIVDSDNRSGYSGIFSVEGKSCINRCFYVELIRGRKQETRVWWTSNSIVVFCGTSGTYGTGSWPDGANINFMPI
>d3nn9__ 2.45.1.1.2 Influenza neuraminidase [influenza virus A, different strains]
RDFNNLTKGLCTINSWHIYGKDNAVRIGEDSDVLVTREPYVSCDPDECRFYALSQGTTIRGKHSNGTIHDRSQYRALISWPLSSPPTVYNSRVECIGWSSTSCHDGKTRMSICISGPNNNASAVIWYNRRPVTEINTWARNILRTQESECVCHNGVCPVVFTDGSATGPAETRIYYFKEGKILKWEPLAGTAKHIEECSCYGERAEITCTCRDNWQGSNRPVIRIDPVAMTHTSQYICSPVLTDNPRPDDPTVGKCNDPYPGNNNNGVKGFSYLDGVNTWLGRTISIASRSGYEMLKVPNALTDDKSKPTQGQTIVLNTDWSGYSGSFMDYWAEGECYRACFYVELIRGRPKEDKVWWTSNSIVSMCSSTEFLGQWDWPDGAKIEYFL
>d1inv__ 2.45.1.1.3 Influenza neuraminidase [influenza virus B, different strains]
EPEWTYPRLSCQGSTFQKALLISPHRFGEIKGNSAPLIIREPFVACGPKECRHFALTHYAAQPGGYYNGTRKDRNKLRHLVSVKLGKIPTVENSIFHMAAWSGSACHDGREWTYIGVDGPDNDALVKIKYGEAYTDTYHSYAHNILRTQESACNCIGGDCYLMITDGSASGISKCRFLKIREGRIIKEILPTGRVEHTEECTCGFASNKTIECACRDNSYTAKRPFVKLNVETDTAEIRLMCTKTYLDTPRPDDGSIAGPCESNGDKWLGGIKGGFVHQRMASKIGRWYSRTMSKTNRMGMELYVRYDGDPWTDSDALTLSGVMVSIEEPGWYSFGFEIKDKKCDVPCIGIEMVHDGGKDTWHSAATAIYCLMGSGQLLWDTVTGVDMAL
>d1nsca_ 2.45.1.1.3 Influenza neuraminidase [influenza virus B, different strains]
EPEWTYPRLSCQGSTFQKALLISPHRFGEARGNSAPLIIREPFIACGPKECKHFALTHYAAQPGGYYNGTREDRNKLRHLISVKLGKIPTVENSIFHMAAWSGSACHDGREWTYIGVDGPDSNALIKIKYGEAYTDTYHSYANNILRTQESACNCIGGDCYLMITDGSASGISKCRFLKIREGRIIKEIFPTGRVEHTEECTCGFASNKTIECACRDNSYTAKRPFVKLNVETDTAEIRLMCTETYLDTPRPDDGSITGPCESNGDKGRGGIKGGFVHQRMASKIGRWYSRTMSKTERMGMELYVRYDGDPWTDSDALAHSGVMVSMKEPGWYSFGFEIKDKKCDVPCIGIEMVHDGGKKTWHSAATAIYCLMGSGQLLWDTVTGVDMAL
>d1eur__ 2.45.1.1.4 Micromonospora sialidase, N-terminal domain [Micromonospora viridifaciens]
GEPLYTEQDLAVNGREGFPNYRIPALTVTPDGDLLASYDGRPTGIDAPGPNSILQRRSTDGGRTWGEQQVVSAGQTTAPIKGFSDPSYLVDRETGTIFNFHVYSQRQGFAGSRPGTDPADPNVLHANVATSTDGGLTWSHRTITADITPDPGWRSRFAASGEGIQLRYGPHAGRLIQQYTIINAAGAFQAVSVYSDDHGRTWRAGEAVGVGMDENKTVELSDGRVLLNSRDSARSGYRKVAVSTDGGHSYGPVTIDRDLPDPTNNASIIRAFPDAPAGSARAKVLLFSNAASQTSRSQGTIRMSCDDGQTWPVSKVFQPGSMSYSTLTALPDGTYGLLYEPGTGIRYANFNLAWLGGICAP
>d1kit_3 2.45.1.1.5 (193-322,520-757) Vibrio cholerae sialidase [Vibrio cholerae]
VIFRGPDRIPSIVASSVTPGVVTAFAEKRVGGGDPGALSNTNDIITRTSRDGGITWDTELNLTEQINVSDEFDFSDPRPIYDPSSNTVLVSYARWPTDAAQNGDRIKPWMPNGIFYSVYDVASGNWQAPINWQTGSTLPIPFRWKSSSILETLEPSEADMVELQNGDLLLTARLDFNQIVNGVNYSPRQQFLSKDGGITWSLLEANNANVFSNISTGTVDASITRFEQSDGSHFLLF
>d1gof_3 2.46.1.1.1 (151-537) Galactose oxidase, central domain [Dactylium dendroides]
YTAPQPGLGRWGPTIDLPIVPAAAAIEPTSGRVLMWSSYRNDAFGGSPGGITLTSSWDPSTGIVSDRTVTVTKHDMFCPGISMDGNGQIVVTGGNDAKKTSLYDSSSDSWIPGPDMQVARGYQSSATMSDGRVFTIGGSWSGGVFEKNGEVYSPSSKTWTSLPNAKVNPMLTADKQGLYRSDNHAWLFGWKKGSVFQAGPSTAMNWYYTSGSGDVKSAGKRQSNRGVAPDAMCGNAVMYDAVKGKILTFGGSPDYQDSDATTNAHIITLGEPGTSPNTVFASNGLYFARTFHTSVVLPDGSTFITGGQRRGIPFEDSTPVFTPEIYVPEQDTFYKQNPNSIVRVYHSISLLLPDGRVFNGGGGLCGDCTTNHFDAQIFTPNYLYNSN
>d1mdah_ 2.46.2.1.1 Methylamine dehydrogenase, H-chain [Paracoccus denitrificans]
EKSKVAGSAAAASAAAASDGSSCDHGPGAISRRSHITLPAYFAGTTENWVSCAGCGVTLGHSLGAFLSLAVAGHSGSDFALASTSFARSAKGKRTDYVEVFDPVTFLPIADIELPDAPRFSVGPRVHIIGNCASSACLLFFLFGSSAAAGLSVPGASDDQLTKSASCFHIHPGAAATHYLGSCPASLAASDLAAAPAAAGIVGAQCTGAQNCSSQAAQANYPGMLVWAVASSILQGDIPAAGATMKAAIDGNESGRKADNFRSAGFQMVAKLKNTDGIMILTVEHSRSCLAAAENTSSVTASVGQTSGPISNGHDSDAIIAAQDGASDNYANSAGTEVLDIYDAASDQDQSSVELDKGPESLSVQNEA
>d2bbkh_ 2.46.2.1.1 Methylamine dehydrogenase, H-chain [Paracoccus denitrificans]
DEPRILEAPAPDARRVYVNDPAHFAAVTQQFVIDGEAGRVIGMIDGGFLPNPVVADDGSFIAHASTVFSRIARGERTDYVEVFDPVTLLPTADIELPDAPRFLVGTYPWMTSLTPDGKTLLFYQFSPAPAVGVVDLEGKAFKRMLDVPDCYHIFPTAPDTFFMHCRDGSLAKVAFGTEGTPEITHTEVFHPEDEFLINHPAYSQKAGRLVWPTYTGKIHQIDLSSGDAKFLPAVEALTEAERADGWRPGGWQQVAYHRALDRIYLLVDQRDEWRHKTASRFVVVLDAKTGERLAKFEMGHEIDSINVSQDEKPLLYALSTGDKTLYIHDAESGEELRSVNQLGHGPQVITTADMG
>d2madh_ 2.46.2.1.2 Methylamine dehydrogenase, H-chain [gram negative methylotrophic bacteria (thiobacillus versutus)]
SSASAAAAAAAAALAAGAADGPTNDEAPGADGRRSYINLPAHHSAIIQQWVLDAGSGSILGHVNGGFLPNPVAAHSGSEFALASTSFSRIAKGKRTDYVEVFDPVTFLPIADIELPDAPRFDVGPYSWMNANTPNNADLLFFQFAAGPAVGLVVQGGSSDDQLLSSPTCYHIHPGAPSTFYLLCAQGGLAKTDHAGGAAGAGLVGAMLTAAQNLLTQPAQANKSGRIVWPVYSGKILQADISAAGATNKAPIDALSGGRKADTWRPGGWQQVAYLKSSDGIYLLTSEQSAWKLHAAAKEVTSVTGLVGQTSSQISLGHDVDAISVAQDGGPDLYALSAGTEVLHIYDAGAGDQDQSTVELGSGPQVLSVMNEA
>d2trcb_ 2.46.3.1.1 beta1-subunit of the signal-transducing G protein heterotrimer [Bovine (Bos taurus)]
MSELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGRIQMRTRRTLRGHLAKIYAMHWGTDSRLLLSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNYVACGGLDNICSIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSGDTTCALWDIETGQQTTTFTGHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTFTGHESDINAICFFPNGNAFATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSGRLLLAGYDDFNCNVWDALKADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN
>d4aaha_ 2.47.1.1.1 Methanol dehydrogenase, heavy chain [methylophilis w3a1]
DADLDKQVNTAGAWPIATGGYYSQHNSPLAQINKSNVKNVKAAWSFSTGVLNGHEGAPLVIGDMMYVHSAFPNNTYALNLNDPGKIVWQHKPKQDASTKAVMCCDVVDRGLAYGAGQIVKKQANGHLLALDAKTGKINWEVEVCDPKVGSTLTQAPFVAKDTVLMGCSGAELGVRGAVNAFDLKTGELKWRAFATGSDDSVRLAKDFNSANPHYGQFGLGTKTWEGDAWKIGGGTNWGWYAYDPKLNLFYYGSGNPAPWNETMRPGDNKWTMTIWGRDLDTGMAKWGYQKTPHDEWDFAGVNQMVLTDQPVNGKMTPLLSHIDRNGILYTLNRENGNLIVAEKVDPAVNVFKKVDLKTGTPVRDPEFATRMDHKGTNICPSAMGFHNQGVDSYDPESRTLYAGLNHICMDWEPFMLPYRAGQFFVGATLAMYPGPNGPTKKEMGQIRAFDLTTGKAKWTKWEKFAAWGGTLYTKGGLVWYATLDGYLKALDNKDGKELWNFKMPSGGIGSPMTYSFKGKQYIGSMYGVGGWPGVGLVFDLTDPSAGLGAVGAFRELQNHTQMGGGLMVFSL
>d1aofa2 2.47.2.1.1 (99-532) C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase [Triosphaera pantotropha]
PPEFGMKEMRESWKVHVAPEDRPTQQMNDWDLENLFSVTLRDAGQIALIDGSTYEIKTVLDTGYAVHISRLSASGRYLFVIGRDGKVNMIDLWMKEPTTVAEIKIGSEARSIETSKMEGWEDKYAIAGAYWPPQYVIMDGETLEPKKIQSTRGMTYDEQEYHPEPRVAAILASHYRPEFIVNVKETGKILLVDYTDLNNLKTTEISAERFLHDGGLDGSHRYFITAANARNKLVVIDTKEGKLVAIEDTGGQTPHPGRGANFVHPTFGPVWATSHMGDDSVALIGTDPEGHPDNAWKILDSFPALGGGSLFIKTHPNSQYLYVDATLNPEAEISGSVAVFDIKAMTGDGSDPEFKTLPIAEWAGITEGQPRVVQGEFNKDGTEVWFSVWNGKDQESALVVVDDKTLELKHVIKDERLVTPTGKFNVYNTMTDTY
>d1bplb1 2.48.1.1.1 (182-290) Bacterial alpha-Amylase (BLA) [Bacillus licheniformis]
QREIPALKHKIEPILKARKQYAYGAQHDYFDHHDIVGWTREGDSSVANSGLAALITDGPGGAKRMYVGRQNAGETWHDITGNRSEPVVINSEGWGEFHVNGGSVSIYVQ
>d1jdc_1 2.48.1.1.10 (358-418) G4-amylase (1,4-alpha-D-glucan maltotetrahydrolase [Pseudomonas stutzeri]
RADSAISFHSGYSGLVATVSGSQQTLVVALNSDLGNPGQVASGSFSEAVNASNGQVRVWRS
>d1amy_1 2.48.1.1.11 (347-403) plant alpha-amylase [Barley (Hordeum vulgare) seeds, AMY2 isozyme]
HNESKLQIIEADADLYLAEIDGKVIVKLGPRYDVGNLIPGGFKVAAHGNDYAVWEKI
>d1cgt_3 2.48.1.1.2 (383-494) Cyclodextrin glycosyltransferase [Bacillus circulans]
KSTTAFNVISKLAPLRKSNPAIAYGSTQQRWINNDVYVYERKFGKSVAVVAVNRNLSTSASITGLSTSLPTGSYTDVLGGVLNGNNITSTNGSINNFTLAAGATAVWQYTTA
>d1cdg_3 2.48.1.1.2 (383-495) Cyclodextrin glycosyltransferase [Bacillus circulans]
TSTTAYQVIQKLAPLRKCNPAIAYGSTQERWINNDVLIYERKFGSNVAVVAVNRNLNAPASISGLVTSLPQGSYNDVLGGLLNGNTLSVGSGGAASNFTLAAGGTAVWQYTAA
>d1cyg_3 2.48.1.1.3 (379-491) Cyclodextrin glycosyltransferase [Bacillus sterothermophilus]
KNTRAYQVIQKLSSLRRNNPALAYGDTEQRWINGDVYVYERQFGKDVVLVAVNRSSSSNYSITGLFTALPAGTYTDQLGGLLDGNTIQVGSNGSVNAFDLGPGEVGVWAYSAT
>d1pama3 2.48.1.1.4 (384-496) Cyclodextrin glycosyltransferase [alkalophilic Bacillus sp. 1011]
TTTAYQVIQKLAPLRKSNPAIAYGSTHERWINNDVIIYERKFGNNVAVVAINRNMNTPASITGLVTSLPRGSYNDVLGGILNGNTLTVGAGGAASNFTLAPGGTAVWQYTTDA
>d1ciu_3 2.48.1.1.5 (383-495) Cyclodextrin glycosyltransferase [Thermoanaerobacterium thermosulfurigenes EM1]
TSTTAYNVIKKLAPLRKSNPAIAYGTTQQRWINNDVYIYERKFGNNVALVAINRNLSTSYNITGLYTALPAGTYTDVLGGLLNGNSISVASDGSVTPFTLSAGEVAVWQYVSS
>d1ppi_1 2.48.1.1.6 (404-496) Mammalian alpha-amylase [porcine (Sus scrofa)]
EPFANWWDNGSNQVAFGRGNRGFIVFNNDDWQLSSTLQTGLPGGTYCDVISGDKVGNSCTGIKVYVSSDGTAQFSISNSAEDPFIAIHAESKL
>d1smd_1 2.48.1.1.7 (403-495) Mammalian alpha-amylase [human (Homo sapiens)]
QPFTNWYDNGSNQVAFGRGNRGFIVFNNDDWTFSLTLQTGLPAGTYCDVISGDKINGNCTGIKIYVSDDGKAHFSISNSAEDPFIAIHAESKL
>d2aaa_1 2.48.1.1.8 (374-476) Fungal alpha-amylase [Aspergillus niger, acid amylase]
AADSAYITYANDAFYTDSNTIAMAKGTSGSQVITVLSNKGSSGSSYTLTLSGSGYTSGTKLIEAYTCTSVTVDSSGDIPVPMASGLPRVLLPASVVDSSSLCG
>d6taa_1 2.48.1.1.9 (374-476) Fungal alpha-amylase [Aspergillus oryzae, Taka-amylase]
SKDTGFVTYKNWPIYKDDTTIAMRKGTDGSQIVTILSNKGASGDSYTLSLSGAGYTAGQQLTEVIGCTTVTVGSDGNVPVPMAGGLPRVLYPTEKLAGSKICS
>d1dkga2 2.49.1.1.1 (100-158) The head domain of nucleotide exchange factor GrpE [Escherichia coli]
VEVIAETNVPLDPNVHQAIAMVESDDVAPGNVLGIMQKGYTLNGRTIRAAMVTVAKAKA
>d1aaj__ 2.5.1.1.1 Amicyanin [Paracoccus denitrificans]
DKATIPSESPFAAAEVADGAIVVDIAKMKYETPELHVKVGDTVTWINREAMPHNVHFVAGVLGEAALKGPMMKKEQAYSLTFTEAGTYDYHCTPHPFMRGKVVVE
>d1pmy__ 2.5.1.1.10 Pseudoazurin [Methylobacterium extorquens, strain am1]
DEVAVKMLNSGPGGMMVFDPALVRLKPGDSIKFLPTDKGHNVETIKGMAPDGADYVKTTVGQEAVVKFDKEGVYGFKCAPHYMMGMVALVVVGDKRDNLEAAKSVQHNKLTQKRLDPLFAQIQ
>d1zia__ 2.5.1.1.11 Pseudoazurin [Achromobacter cycloclastes]
ADFEVHMLNKGKDGAMVFEPASLKVAPGDTVTFIPTDKGHNVETIKGMIPDGAEAFKSKINENYKVTFTAPGVYGVKCTPHYGMGMVGVVQVGDAPANLEAVKGAKNPKKAQERLDAALAALGN
>d1adwa_ 2.5.1.1.12 Pseudoazurin [Thiosphaera pantotropha]
ATHEVHMLNKGESGAMVFEPAFVRAEPGDVINFVPTDKSHNVEAIKEILPEGVESFKSKINESYTLTVTEPGLYGVKCTPHFGMGMVGLVQVGDAPENLDAAKTAKMPKKARERMDAELAQVN
>d2cbp__ 2.5.1.1.13 Cucumber basic protein [cucumber (Cucumis sativus)]
AVYVVGGSGGWTFNTESWPKGKRFRAGDILLFNYNPSMHNVVVVNQGGFSTCNTPAGAKVYTSGRDQIKLPKGQSYFICNFPGHCQSGMKIAVNAL
>d1aiza_ 2.5.1.1.14 Azurin [Alcaligenes denitrificans]
AQCEATIESNDAMQYNLKEMVVDKSCKQFTVHLKHVGKMAKVAMGHNWVLTKEADKQGVATDGMNAGLAQDYVKAGDTRVIAHTKVIGGGESDSVTFDVSKLTPGEAYAYFCSFPGHWAMMKGTLKLSN
>d1arn__ 2.5.1.1.15 Azurin [Alcaligenes xylosoxidans xylosoxidans NCIMB (11015), isoform II]
AQCEATVESNDAMQYNVKEIVVDKSCKQFTMHLKHVGKMAKVAMGHNLVLTKDADKQAVATDGMGAGLAQDYVKAGDTRVIAHTKVIGGGESDSVTFDVSKIAAGENYAYFCSFPGHWAMMKGTLKLGS
>d2azua_ 2.5.1.1.16 Azurin [Pseudomonas aeruginosa]
AQCSVDIQGNDQMQFNTNAITVDKSCKQFTVNLSLPGNLPKNVMGHNWVLSTAADMQGVVTDGMASGLDKDYLKPDDSRVIAHTKLIGSGEKDSVTFDVSKLKEGEQYMFFCTFPGHSALMKGTLTLK
>d1cur__ 2.5.1.1.17 Rusticyanin [Thiobacillus ferooxidans]
GTLDTTWKEATLPQVKAMLEKDTGKVSGDTVTYSGKTVHVVAAAVLPGFPFPSFEVHDKKNPTLEIPAGATVDVTFINTNKGFGHSFDITKKGPPYAVMPVIDPIVAGTGFSPVPKDGKFGYTDFTWHPTAGTYYYVCQIPGHAATGMFGKIVVK
>d1jer__ 2.5.1.1.18 Stellacyanin [cucumber (Cucumis sativus)]
MQSTVHIVGDNTGWSVPSSPNFYSQWAAGKTFRVGDSLQFNFPANAHNVHEMETKQSFDACNFVNSDNDVERTSPVIERLDELGMHYFVCTVGTHCSNGQKLSINVVAAN
>d1plc__ 2.5.1.1.2 Plastocyanin [poplar (Populus nigra variant italica)]
IDVLLGADDGSLAFVPSEFSISPGEKIVFKNNAGFPHNIVFDEDSIPSGVDASKISMSEEDLLNAKGETFEVALSNKGEYSFYCSPHQGAGMVGKVTVN
>d9pcy__ 2.5.1.1.3 Plastocyanin [french bean (Phaseolus vulgaris)]
LEVLLGSGDGSLVFVPSEFSVPSGEKIVFKNNAGFPHNVVFDEDEIPAGVDAVKISMPEEELLNAPGETYVVTLDTKGTYSFYCSPHQGAGMVGKVTVN
>d1plb__ 2.5.1.1.4 Plastocyanin [parsley (Petroselinum crispum)]
AEVKLGSDDGGLVFSPSSFTVAAGEKITFKNNAGFPHNIVFDEDEVPAGVNAEKISQPEYLNGAGETYEVTLTEKGTYKFYCEPHAGAGMKGEVTVN
>d1iuz__ 2.5.1.1.5 Plastocyanin [sea lettuce (Ulva pertusa)]
AQIVKLGGDDGSLAFVPSKISVAAGEAIEFVNNAGFPHNIVFDEDAVPAGVDADAISYDDYLNSKGETVVRKLSTPGVYGVYCEPHAGAGMKMTITVQ
>d2plt__ 2.5.1.1.6 Plastocyanin [green alga (Chlamydomonas reinhardtii)]
DATVKLGADSGALEFVPKTLTIKSGETVNFVNNAGFPHNIVFDEDAIPSGVNADAISRDDYLNAPGETYSVKLTAAGEYGYYCEPHQGAGMVGKIIVQ
>d7pcy__ 2.5.1.1.7 Plastocyanin [green alga (Enteromorpha prolifera)]
AAIVKLGGDDGSLAFVPNNITVGAGESIEFINNAGFPHNIVFDEDAVPAGVDADAISAEDYLNSKGQTVVRKLTTPGTYGVYCDPHSGAGMKMTITVQ
>d1nin__ 2.5.1.1.8 Plastocyanin [(Anabaena variailis)]
ETYTVKLGSDKGLLVFEPAKLTIKPGDTVEFLNNKVPPHNVVFDAALNPAKSADLAKSLSHKQLLMSPGQSTSTTFPADAPAGEYTFYCEPHRGAGMVGKITVAG
>d1paz__ 2.5.1.1.9 Pseudoazurin [Alcaligenes faecalis, strain s-6]
ENIEVHMLNKGAEGAMVFEPAYIKANPGDTVTFIPVDKGHNVESIKDMIPEGAEKFKSKINENYVLTVTQPGAYLVKCTPHYAMGMIALIAVGDSPANLDQIVSAKKPKIVQERLEKVIA
>d1cyx__ 2.5.1.2.1 Quinol oxidase (CYOA) [Escherichia coli]
KPITIEVVSMDWKWFFIYPEQGIATVNEIAFPANTPVYFKVTSNSVMHSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGICAEICGPGHSGMKFKAIATPDRAAFDQWVAKAKQSPNTMSDMAAFEKLAAPSEYNQVEYFSNVKPDLFADVINKFM
>d1occb1 2.5.1.2.2 (91-227) Cytochrome c oxidase [bovine (Bos taurus)]
NNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSELKPGELRLLEVDNRVVLPMEMTIRMLVSSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSSRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML
>d1nif_2 2.5.1.3.1 (160-333) Nitrite reductase, NIR [Achromobacter cycloclastes]
GQPLTYDKIYYVGEQDFYVPKDEAGNYKKYETPGEAYEDAVKAMRTLTPTHIVFNGAVGALTGDHALTAAVGERVLVVHSQANRDTRPHLIGGHGDYVWATGKFRNPPDLDQETWLIPGGTAGAAFYTFRQPGVYAYVNHNLIEAFELGAAGHFKVTGEWNDDLMTSVVKPASM
>d1nif_1 2.5.1.3.1 (1-159) Nitrite reductase, NIR [Achromobacter cycloclastes]
DISTLPRVKVDLVKPPFVHAHDQVAKTGPRVVEFTMTIEEKKLVIDREGTEIHAMTFNGSVPGPLMVVHENDYVELRLINPDTNTLLHNIDFHAATGALGGGALTQVNPGEETTLRFKATKPGVFVYHCAPEGMVPWHVTSGMNGAIMVLPRDGLKDEK
>d2afna2 2.5.1.3.2 (159-331) Nitrite reductase, NIR [Alcaligenes faecalis, strain s-6]
GKALTYDKIYYVGEQDFYVPRDENGKYKKYEAPGDAYEDTVKVMRTLTPTHVVFNGAVGALTGDKAMTAAVGEKVLIVHSQANRDTRPHLIGGHGDYVWATGKFNTPPDVDQETWFIPGGAAGAAFYTFQQPGIYAYVNHNLIEAFELGAAAHFKVTGEWNDDLMTSVLAPSG
>d2afna1 2.5.1.3.2 (1-158) Nitrite reductase, NIR [Alcaligenes faecalis, strain s-6]
IAALPRQKVELVDPPFVHAHSQVAEGGPKVVEFTMVIEEKKIVIDDAGTEVHAMAFNGTVPGPLMVVHQDDYLELTLINPETNTLMHNIDFHAATGALGGGGLTEINPGEKTILRFKATKPGVFVYHCAPPGMVPWHVVSGMNGAIMVLPREGLHDGK
>d1ndsa2 2.5.1.3.3 (157-330) Nitrite reductase, NIR [Alcaligenes xylosoxidans]
GAALAYDRVYTIGESDLYVPKAADGNYSDYPALASAYADTVAVMRTLTPSHAVFNGAVGALTGANALTAAVGESVLIIHSQANRDSRPHLIGGHGDWVWTTGKFANPPQLNMETWFIPGGSAAAALYTFKQPGTYAYLSHNLIEAMELGAAAQASVEGQWDDDLMTSVAAPGPA
>d1ndsa1 2.5.1.3.3 (1-156) Nitrite reductase, NIR [Alcaligenes xylosoxidans]
GLPRVAVDLVAPPLVHPHSQVAAGAPKVVQFRMSIEEKKMVADDDGTTAQAMTFNGSVPGPTLVVHEGDYIELTLVNPATNSMPHNVDFHAATGALGGAGLTQVVPGQEAVLRFKADRSGTFVYHCAPAGMVPWHVVSGMNGALMVLPRDGLRDAA
>d1aoza3 2.5.1.3.4 (339-552) Ascorbate oxidase [zucchini (Cucurbita pepo medullosa)]
PPVKFNRRIFLLNTQNVINGYVKWAINDVSLALPPTPYLGAMKYNLLHAFDQNPPPEVFPEDYDIDTPPTNEKTRIGNGVYQFKIGEVVDVILQNANMMKENLSETHPWHLHGHDFWVLGYGDGKFSAEEESSLNLKNPPLRNTVVIFPYGWTAIRFVADNPGVWAFHCHIEPHLHMGMGVVFAEGVEKVGRIPTKALACGGTAKSLINNPKNP
>d1aoza1 2.5.1.3.4 (1-129) Ascorbate oxidase [zucchini (Cucurbita pepo medullosa)]
SQIRHYKWEVEYMFWAPNCNENIVMGINGQFPGPTIRANAGDSVVVELTNKLHTEGVVIHWHGILQRGTPWADGTASISQCAINPGETFFYNFTVDNPGTFFYHGHLGMQRSAGLYGSLIVDPPQGKKE
>d1aoza2 2.5.1.3.4 (130-338) Ascorbate oxidase [zucchini (Cucurbita pepo medullosa)]
PFHYDGEINLLLSDWWHQSIHKQEVGLSSKPIRWIGEPQTILLNGRGQFDCSIAAKYDSNLEPCKLKGSESCAPYIFHVSPKKTYRIRIASTTALAALNFAIGNHQLLVVEADGNYVQPFYTSDIDIYSGESYSVLITTDQNPSENYWVSVGTRARHPNTPPGLTLLNYLPNSVSKLPTSPPPQTPAWDDFDRSKNFTYRITAAMGSPK
>d1kcw_4 2.5.1.3.5 (538-689) Ceruloplasmin [Human (Homo sapiens)]
DVDKEFYLFPTVFDENESLLLEDNIRMFTTAPDQVDKEDEDFQESNKMHSMNGFMYGNQPGLTMCKGDSVVWYLFSAGNEADVHGIYFSGNTYLWRGERRDTANLFPQTSLTLHMWPDTEGTFNVECLTTDHYTGGMKQKYTVNQCRRQSED
>d1kcw_6 2.5.1.3.5 (869-1017) Ceruloplasmin [Human (Homo sapiens)]
RRKLEFALLFLVFDENESWYLDDNIKTYSDHPEKVNKDDEEFIESNKMHAINGRMFGNLQGLTMHVGDEVNWYLMGMGNEIDLHTVHFHGHSFQYKHRGVYSSDVFDIFPGTYQTLEMFPRTPGIWLLHCHVTDHIHAGMETTYTVLQN
>d1kcw_3 2.5.1.3.5 (339-537) Ceruloplasmin [Human (Homo sapiens)]
IRGKHVRHYYIAAEEIIWNYAPSGIDIFTKENLTAPGSDSAVFFEQGTTRIGGSYKKLVYREYTDASFTNRKERGPEEEHLGILGPVIWAEVGDTIRVTFHNKGAYPLSIEPIGVRFNKNNEGTYYSPVPPSASHVAPTETFTYEWTVPKEVGPTNADPVCLAKMYYSAVDPTKDIFTGLIGPMKICKKGSLHANGRQK
>d1kcw_1 2.5.1.3.5 (1-192) Ceruloplasmin [Human (Homo sapiens)]
KEKHYYIGIIETTWDYASDHGEKKLISVDTEHSNIYLQNGPDRIGRLYKKALYLQYTDETFRTTIEKPVWLGFLGPIIKAETGDKVYVHLKNLASRPYTFHSHGITYYKEHEGAIYPDNTTDFQRADDKVYPGEQYTYMLLATEEQSPGEGDGNCVTRIYHSHIDAPKDIASGLIGPLIICKKDSLDKEKEK
>d1kcw_2 2.5.1.3.5 (193-338) Ceruloplasmin [Human (Homo sapiens)]
HIDREFVVMFSVVDENFSWYLEDNIKTYCSEPEKVDKDNEDFQESNRMYSVNGYTFGSLPGLSMCAEDRVKWYLFGMGNEVDVHAAFFHGQALTNKNYRIDTINLFPATLFDAYMVAQNPGEWMLSCQNLNHLKAGLQAFFQVQEC
>d1kcw_5 2.5.1.3.5 (690-868) Ceruloplasmin [Human (Homo sapiens)]
STFYLGERTYYIAAVEVEWDYSPQREWEKELHHLQEQNVSNAFLDKGEFYIGSKYKKVVYRQYTDSTFRVPVERKAEEEHLGILGPQLHADVGDKVKIIFKNMATRPYSIHAHGVQTESSTVTPTLPGETLTYVWKIPERSGAGTEDSACIPWAYYSTVDQVKDLYSGLIGPLIVCRRP
>d1hcb__ 2.50.1.1.1 Carbonic anhydrase [human (Homo sapiens) erythrocytes, isozyme I]
PDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVLKGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQKVLDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAVPMQHNNRPTQPLKGRTVRASF
>d2cba__ 2.50.1.1.2 Carbonic anhydrase [human (Homo sapiens) erythrocytes, isozyme II]
HHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK
>d1znca_ 2.50.1.1.3 Carbonic anhydrase [human (Homo sapiens) isozyme IV]
WCYEVQAESSNYPCLVPVKWGGNCQKDRQSPINIVTTKAKVDKKLGRFFFSGYDKKQTWTVQNNGHSVMMLLENKASISGGGLPAPYQAKQLHLHWSDLPYKGSEHSLDGEHFAMEMHIVHEKEKGTSRNVKEAQDPEDEIAVLAFLVEAGTQVNEGFQPLVEALSNIPKPEMSTTMAESSLLDLLPKEEKLRHYFRYLGSLTTPTCDEKVVWTVFREPIQLHREQILAFSQKLYYDKEQTVSMKDNVRPLQQLGQRTVIKS
>d1dmya_ 2.50.1.1.4 Carbonic anhydrase [Murine (Mus musculus) liver, isozyme V]
GTRQSPINIQWKDSVYDPQLAPLRVSYDAASCRYLWNTGYFFQVEFDDSCEDSGISGGPLGNHYRLKQFHFHWGATDEWGSEHAVDGHTYPAELHLVHWNSTKYENYKKASVGENGLAVIGVFLKLGAHHQALQKLVDVLPEVRHKDTQVAMGPFDPSCLMPACRDYWTYPGSLTTPPLAESVTWIVQKTPVEVSPSQLSMFRTLLFSGRGEEEDVMVNNYRPLQPLRDRKLRSSFR
>d3bcl__ 2.51.1.1.1 Bacteriochlorophyl A protein [Prosthecochloris aestuarii, strain 2k]
VSABSAYKIILZGGASSWGZVAGAASVSVPASIPLBPTBCSIKIBASPSTVKFTVAIASTIBATABTLSVATSIABSAASKRIATGAGSVAVGSFAHAFSFMGSTTBMYYSGSSATARBIPBPIYMZGRZFHBIBMKVPLBBGBLTSTWKGFSAASBFGBWIRBFWFIGPAFAAIBZGGZRISPVTTBSASTZGPBGTTRWSFSHAGSGVVBSISRWTZLFPTAKLSKPAAIZGGFSSBSAGISVAVAGSLPGVSKSAGGGBKKILBHPBIPLTHHGMTGKFBSFSSBTABKITLPKGYAISYAAPAHSSKBBZAYKWAGGAYARWVZHVCKGGTGZHZTLYAA
>d1ospo_ 2.52.1.1.1 Outer surface protein A [lyme disease spirochete (Borrelia burgdorferi)]
SLDEKNSVSVDLPGEMKVLVSKEKNKDGKYDLIATVDKLELKGTSDKNNGSGVLEGVKADKCKVKLTISDDLGQTTLEVFKEDGKTLVSKKVTSKDKSSTEEKFNEKGEVSEKIITRADGTRLEYTGIKSDGSGKAKEVLKGYVLEGTLTAEKTTLVVKEGTVTLSKNISKSGEVSVELNDTDSSAATKKTAAWNSGTSTLTITVNSKKTKDLVFTKENTITVQQYDSNGTKLEGSAVEITKLDEIKNALK
>d1vmoa_ 2.53.1.1.1 Vitelline membrane outer protein-I (VMO-I) [hen (Gallus gallus)]
RTREYTSVITVPNGGHWGKWGIRQFCHSGYANGFALKVEPSQFGRDDTALNGIRLRCLDGSVIESLVGKWGTWTSFLVCPTGYLVSFSLRSEKSQGGGDDTAANNIQFRCSDEAVLVGDGLSWGRFGPWSKRCKICGLQTKVESPQGLRDDTALNNVRFFCCK
>d1dlc_2 2.53.2.1.1 (230-439) delta-Endotoxin (insectocide), middle domain [Bacillus thuringiensis tenebrionis, CRYIIIA (BT13)]
LYPKEVKTELTRDVLTDPIVGVNNLRGYGTTFSNIENYIRKPHLFDYLHRIQFHTRFQPGYYGNDSFNYWSGNYVSTRPSIGSNDIITSPFYGNKSSEPVQNLEFNGEKVYRAVANTNLAVWPSAVYSGVTKVEFSQYNDQTDEASTQTYDSKRNVGAVSWDSIDQLPPETTDEPLEKGYSHQLNYVMCFLMQGSRGTIPVLTWTHKSVD
>d1ciy_2 2.53.2.1.2 (224-429) delta-Endotoxin (insectocide), middle domain [(Bacillus thuringiensis), CRYIA(A)]
PIRTVSQLTREIYTNPVLENFDGSFRGMAQRIEQNIRQPHLMDILNSITIYTDVHRGFNYWSGHQITASPVGFSGPEFAFPLFGNAGNAAPPVLVSLTGLGIFRTLSSPLYRRIILGSGPNNQELFVLDGTEFSFASLTTNLPSTIYRQRGTVDSLDVIPPQDNSVPPRAGFSHRLSHVTMLSQAAGAVYTLRAPTFSWQHRSAEF
>d1msaa_ 2.54.1.1.1 Lectin (agglutinin) [Snowdrop (Galanthus nivalis)]
DNILYSGETLSTGEFLNYGSFVFIMQEDCNLVLYDVDKPIWATNTGGLSRSCFLSMQTDGNLVVYNPSNKPIWASNTGGQNGNYVCILQKDRNVVIYGTDRWATGTHTG
>d1kapp1 2.55.1.1.1 (247-470) Metalloprotease, C-terminal domain [Pseudomonas aeruginosa (alkaline protease)]
GANLTTRTGDTVYGFNSNTERDFYSATSSSSKLVFSVWDAGGNDTLDFSGFSQNQKINLNEKALSDVGGLKGNVSIAAGVTVENAIGGSGSDLLIGNDVANVLKGGAGNDILYGGLGADQLWGGAGADTFVYGDIAESSAAAPDTLRDFVSGQDKIDLSGLDAFVNGGLVLQYVDAFAGKAGQAILSYDAASKAGSLAIDFSGDAHADFAINLIGQATQADIVV
>d1sat_1 2.55.1.1.2 (244-468) Metalloprotease, C-terminal domain [Serratia marcescens]
GANLSTRTGDTVYGFNSNTGRDFLSTTSNSQKVIFAAWDAGGNDTFDFSGYTANQRINLNEKSFSDVGGLKGNVSIAAGVTIENAIGGSGNDVIVGNAANNVLKGGAGNDVLFGGGGADELWGGAGKDIFVFSAASDSAPGASDWIRDFQKGIDKIDLSFFDKEANSSSFIHFVDHFSGTAGEALLSYNASSNVTDLSVNIGGHAAPDFLVKIVGQVDVATDFIV
>d2pec__ 2.56.1.1.1 Pectate lyase [Erwinia chrysanthemi type C]
ATDTGGYAATAGGNVTGAVSKTATSMQDIVNIIDAARLDANGKKVKGGAYPLVITYTGNEDSLINAAAANICGQWSKDPRGVEIKEFTKGITIIGANGSSANFGIWIKKSSDVVVQNMRIGYLPGGAKDGDMIRVDDSPNVWVDHNELFAANHECDGTPDNDTTFESAVDIKGASNTVTVSYNYIHGVKKVGLDGSSSSDTGRNITYHHNYYNDVNARLPLQRGGLVHAYNNLYTNITGSGLNVRQNGQALIENNWFEKAINPVTSRYDGKNFGTWVLKGNNITKPADFSTYSITWTADTKPYVNADSWTSTGTFPTVAYNYSPVSAQCVKDKLPGYAGVGKNLATLTSTAC
>d1pcl__ 2.56.1.1.2 Pectate lyase [Erwinia chrysanthemi type E]
AVETDAATTGWATQNGGTTGGAKAAKAVEVKNISDFKKALNGTDSSAKIIKVTGPIDISGGKAYTSFDDQKARSQISIPSNTTIIGVGSNGKFTNGSLVIKGVKNVILRNLYIETPVDVAPHYESGDGWNAEWDAAVIDNSTNVWVDHVTISDGSFTDDKYTTKDGEKYVQHDGALDIKKGSDYVTISYSRFELHDKTILIGHSDSNGSQDSGKLRVTFHNNVFDRVTERAPRVRFGSIHAYNNVYLGDVKHSVYPYLYSFGLGTSGSILSESNSFTLSNLKSIDGKNPECSIVKQFNSKVFSDKGSLVNGSTTTKLDTCGLTAYKPTLPYKYSAQTMTSSLATSINNNAGYGKL
>d1idk__ 2.56.1.2.1 Pectin lyase A [Aspergillus niger]
VGVSGSAEGFAKGVTGGGSATPVYPDTIDELVSYLGDDEARVIVLTKTFDFTDSEGTTTGTGCAPWGTASACQVAIDQDDWCENYEPDAPSVSVEYYNAGTLGITVTSNKSLIGEGSSGAIKGKGLRIVSGAENIIIQNIAVTDINPKYVWGGDAITLDDCDLVWIDHVTTARIGRQHYVLGTSADNRVSLTNNYIDGVSDYSATCDGYHYWAIYLDGDADLVTMKGNYIYHTSGRSPKVQDNTLLHAVNNYWYDISGHAFEIGEGGYVLAEGNVFQNVDTVLETYEGEAFTVPSSTAGEVCSTYLGRDCVINGFGSSGTFSEDSTSFLSDFEGKNIASASAYTSVASRVVANAGQGNL
>d1tsp__ 2.56.2.1.1 P22 tailspike protein [Salmonella typhimurium phage P22]
YSIEADKKFKYSVKLSDYPTLQDAASAAVDGLLIDRDYNFYGGETVDFGGKVLTIECKAKFIGDGNLIFTKLGKGSRIAGVFMESTTTPWVIKPWTDDNQWLTDAAAVVATLKQSKTDGYQPTVSDYVKFPGIETLLPPNAKGQNITSTLEIRECIGVEVHRASGLMAGFLFRGCHFCKMVDANNPSGGKDGIITFENLSGDWGKGNYVIGGRTSYGSVSSAQFLRNNGGFERDGGVIGFTSYRAGESGVKTWQGTVGSTTSRNYNLQFRDSVVIYPVWDGFDLGADTDRPGDYPITQYPLHQLPLNHLIDNLLVRGALGVGFGMDGKGMYVSNITVEDCAGSGAYLLTHESVFTNIAIIDTNTKDFQANQIYISGACRVNGLRLIGIRSSLTIDAPNSTVSGITGMVDPSRINVANLAEEGLGNIRANSFGYDSAAIKLRIHKLSKTLDSGALYSHINGGAGSGSAYTQLTAISGSTPDAVSLKVNHKDCRGAEIPFVPDIASDDFIKDSSCFLPYWENNSTSLKALVKKPNGELVRLTLATL
>d1lxa__ 2.57.1.1.1 UDP N-acetylglucosamine acyltransferase [Escherichia coli gene lpxA]
MIDKSAFVHPTAIVEEGASIGANAHIGPFCIVGPHVEIGEGTVLKSHVVVNGHTKIGRDNEIYQFASIGEVNQDLKYAGEPTRVEIGDRNRIRESVTIHRGTVQGGGLTKVGSDNLLMINAHIAHDCTVGNRCILANNATLAGHVSVDDFAIIGGMTAVHQFCIIGAHVMVGGCSGVAQDVPPYVIAQGNHATPFGVNIEGLKRRGFSREAITAIRNAYKLIYRSGKTLDEVKPEIAELAETYPEVKAFTDFFARSTRGLIR
>d1tdta_ 2.57.1.2.1 Tetrahydrodipicolinate-N-succinlytransferase, THDP-succinlytransferase, DapD [Mycobacterium bovis]
MQQLQNVIESAFERRADITPANVDTVTREAVNQVIGLLDSGALRVAEKIDGQWVTHQWLKKAVLLSFRINDNKVMDGAETRYYDKVPMKFADYDEARFQKEGFRVVPPATVRQGAFIARNTVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGVGIGGVLEPLQANPTIIEDNCFIGARSEVVEGVIVEEGSVISMGVYLGQSTRIYDRETGEIHYGRVPAGSVVVSGNLPSKDGSYSLYCAVIVKKV
>d1thja_ 2.57.1.3.1 Carbonic anhydrase [Arhaeon (Methanosarcina thermophila)]
MQEITVDEFSNIRENPVTPWNPEPSAPVIDPTAYIDPEASVIGEVTIGANVMVSPMASIRSDEGMPIFVGDRSNVQDGVVLHALETINEEGEPIEDNIVEVDGKEYAVYIGNNVSLAHQSQVHGPAAVGDDTFIGMQAFVFKSKVGNNCVLEPRSAAIGVTIPDGRYIPAGMVVTSQAEADKLPEVTDDYAYSHTNEAVVYVNVHLAEGYKET
>d2phla1 2.58.1.1.1 (1-200) Phaseolin [french bean (Phaseolus vulgaris)]
DNPFYFNSDNSWNTLFKNQYGHIRVLQRFDQQSKRLQNLEDYRLVEFRSKPETLLLPQQADAELLLVVRSGSAILVLVKPDDRREYFFLTSDNPIFSDHQKIPAGTIFYLVNPDPKEDLRIIQLAMPVNNPQIHEFFLSSTEAQQSYLQEFSKHILEASFNSKFEEINRVLFEEEGQQEGVIVNIDSEQIKELSKHAKSS
>d2phla2 2.58.1.1.1 (201-360) Phaseolin [french bean (Phaseolus vulgaris)]
NTIGNEFGNLTERTDNSLNVLISSIEMEEGALFVPHYYSKAIVILVVNEGEAHVELVGPKGETLEYESYRAELSKDDVFVIPAAYPVAIKATSNVNFTGFGINANNNNRNLLAGKTDNVISSIGRALDGKDVLGLTFSGSGDEVMKLINKQSGSYFVDAH
>d1caub_ 2.58.1.1.2 Canavalin 7S vicilin [jack bean plant (Canavalia ensiformis)]
TLSSQDKPFNLRSRDPIYSNNYGKLYEITPEKNSQLRDLDILLNCLQMNEGALFVPHYNSRATVILVANEGRAEVELVGLEQQQQQGLESMQLRRYAATLSEGDIIVIPSSFPVALKAASDLNMVGIGVNAENNERNFLAGHKENVIRQIPRQVSDLTFPGSGEEVEELLENQKESYFVDGQPR
>d1caua_ 2.58.1.1.2 Canavalin 7S vicilin [jack bean plant (Canavalia ensiformis)]
AQNNPYLFRSNKFLTLFKNQHGSLRLLQRFNEDTEKLENLRDYRVLEYCSKPNTLLLPHHSDSDLLVLVLEGQAILVLVNPDGRDTYKLDQGDAIKIQAGTPFYLINPDNNQNLRILKFAITFRRPGTVEDFFLSSTKRLPSYLSAFSKNFLEASYDSPYDEIEQTLLQEEQEGVIVKMPK
>d1pmi__ 2.58.2.1.1 Phosphomannose isomerase [yeast (Candida albicans)]
SSEKLFRIQCGYQNYDWGKIGSSSAVAQFVHNSDPSITIDETKPYAELWMGTHPSVPSKAIDLNNQTLRDLVTAKPQEYLGESIITKFGSSKELPFLFKVLSIEKVLSIQAHPDKKLGAQLHAADPKNYPDDNHKPEMAIAVTDFEGFCGFKPLDQLAKTLATVPELNEIIGQELVDEFISGIKLPAEVGSQDDVNNRKLLQKVFGKLMNTDDDVIKQQTAKLLERTDREPQVFKDIDSRLPELIQRLNKQFPNDIGLFCGCLLLNHVGLNKGEAMFLQAKDPHAYISGDIIECMAASDNVVRAGFTPKFKDVKNLVEMLTYSYESVEKQKMPLQEFPRSKGDAVKSVLYDPPIAEFSVLQTIFDKSKGGKQVIEGLNGPSIVIATNGKGTIQITGDDSTKQKIDTGYVFFVAPGSSIELTADSANQDQDFTTYRAFVEA
>d1cgpa2 2.58.3.1.1 (1-129) Catabolite gene activator protein, N-terminal domain, [Escherichia coli]
PTLEWFLSHCHIHKYPSKSTLIHQGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFEEGQERSAWVRAKTACEVAEISYKKFRQLIQVNPDILMRLSAQMARRLQVTSEKVGNLAFL
>d1rgs_1 2.58.3.2.1 (1-130) Regulatory subunit of Protein kinase A [Bovine (Bos taurus)]
RKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFDAMFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNEWATSVGEGGSFGELALIYGTPRAATVKAKTNVKLWGIDRDSYRRILMGSTLRKRK
>d1rgs_2 2.58.3.2.1 (131-264) Regulatory subunit of Protein kinase A [Bovine (Bos taurus)]
MYEEFLSKVSILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGSAAVLQRRSENEEFVEVGRLGPSDYFGEIALLMNRPRAATVVARGPLKCVKLDRPRFERVLGPCSDILKRNIQQYNSFVS
>d2arca_ 2.58.4.1.1 Regulatory protein AraC [Escherichia coli]
DPLLPGYSFNAHLVAGLTPIEANGYLDFFIDRPLGMKGYILNLTIRGQGVVKNQGREFVCRPGDILLFPPGEIHHYGRHPEAREWYHQWVYFRPRAYWHEWLNWPSIFANTGFFRPDEAHQPHFSDLFGQIINAGQGEGRYSELLAINLLEQLLLRRMEAI
>d1wapa_ 2.58.5.1.1 Trp RNA-binding attenuation protein (TRAP) [Bacillus subtilis]
DFVVIKAVEDGVNVIGLTRGTDTKFHHSEKLDKGEVIIAQFTEHTSAIKVRGEALIQTAYGEMKSEKK
>d1bdo__ 2.59.1.1.1 biotinyl domain of acetyl-CoA carboxylase [Escherichia coli]
EISGHIVRSPMVGTFYRTPSPDAKAFIEVGQKVNVGDTLCIVEAMKMMNQIEADKSGTVKAILVESGQPVEFDEPLVVIE
>d1htp__ 2.59.1.1.2 Protein H of glycine cleavage system [Pea (Pisum sativum)]
SNVLDGLKYAPSHEWVKHEGSVATIGITDHAQDHLGEVVFVELPEPGVSVTKGKGFGAVESVKATSDVNSPISGEVIEVNTGLTGKPGLINSSPYEDGWMIKIKPTSPDELESLLGAKEYTKFCEEEDAAH
>d1lac__ 2.59.1.1.3 The ipoyl domain of dihydrolipoamide acetyltransferase [Bacillus stearothermophilus]
AFEFKLPDIGEGIHEGEIVKWFVKPGDEVNEDDVLCEVQNDKAVVEIPSPVKGKVLEILVPEGTVATVGQTLITLDAPGY
>d1iyu__ 2.59.1.1.4 The ipoyl domain of dihydrolipoamide acetyltransferase [azotobacter vinelandii]
SEIIRVPDIGGDGEVIELLVKTGDLIEVEQGLVVLESAKASMEVPSPKAGVVKSVSVKLGDKLKEGDAIIELEPAAGAR
>d1fyc__ 2.59.1.1.5 The ipoyl domain of dihydrolipoamide acetyltransferase [human (Homo sapiens)]
GSNMSYPPHMQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKEADISAFADYRPTEVTDLK
>d1ghk__ 2.59.1.1.6 The lipoyl domain of the 2-oxoglutarate dehydrogenase complex [(Azotobacter vinelandii)]
AIDIKAPTFPESIADGTVATWHKKPGEAVKRDELIVDIETDKVVMEVLAEADGVIAEIVKNEGDTVLSGELLGKLTEGG
>d1bnca1 2.59.2.1.1 (318-433) Biotin carboxylase subunit of acetyl-CoA carboxylase, C-terminal domain [Escherichia coli]
RGHAVECRINAEDPNTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVAIARMKNALQELIIDGIKTNVDLQIRIMNDENFQHGGTNIHYLEKKLGL
>d1ctm_2 2.59.2.2.1 (168-230) Cytochrome f, small domain [turnip (Brassica rapa)]
NTVYNATAGGIISKILRKEKGGYEITIVDASNERQVIDIIPRGLELLVSEGESIKLDQPLTSN
>d1gpr__ 2.59.3.1.1 Glucose permease IIa domain [Bacillus subtilis]
EPLQNEIGEEVFVSPITGEIHPITDVPDQVFSGKMMGDGFAILPSEGIVVSPVRGKILNVFPTKHAIGLQSDGGREILIHFGIDTVSLKGEGFTSFVSEGDRVEPGQKLLEVDLDAVKPNVPSLMTPIVFTNLAEGETVSIKASGSVNREQEDIVKIE
>d1glaf_ 2.59.3.1.2 Glucose-specific factor III (glsIII) [Escherichia coli]
GLFDKLKSLVSTIEIIAPLSGEIVNIEDVPDVVFAEKIVGDGIAIKPTGNKMVAPVDGTIGKIFETNHAFSIESDSGVELFVHFGIDTVELKGEGFKRIAEEGQRVKVGDTVIEFDLPLLEEKAKSTLTPVVISNMDEIKELIKLSGSVTVGETPVIRIKK
>d1djxa2 2.6.1.1.1 (383-513) PI-specific phospholipase C isozyme D1 (PLC-D1), C-terminal domain [Rat (Rattus norvegicus)]
WRPERLRVRIISGQQLPKVNKNKNSIVDPKVIVEIHGVGRDTGSRQTAVITNNGFNPRWDMEFEFEVTVPDLALVRFMVEDYDSSSKNDFIGQSTIPWNSLKQGYRHVHLLSKNGDQHPSATLFVKISIQD
>d1rsy__ 2.6.1.2.1 Synaptogamin I, first C2 domain [Rat (Rattus norvegicus)]
GGGILDSMVEKLGKLQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPYVKVFLLPDKKKKFETKVHRKTLNPVFNEQFTFKVPYSELGGKTLVMAVYDFDRFSKHDIIGEFKVPMNTVDFGHVTEEWRDLQSA
>d3dpa_2 2.6.2.1.1 (120-218) PapD, C-domain [Escherichia coli]
IKTRPNEVWQDQLILNKVSGGYRIENPTPYYVTVIGLGGSEKQAEEGEFETVMLSPRSEQTVKSANYNTPYLSYINDYGGRPVLSFICNGSRCSVKKEK
>d1who__ 2.6.3.1.1 Pollen allergen PHL P 2 [timothy grass (Phleum pratense)]
VPKVTFTVEKGSNEKHLAVLVKYEGDTMAEVELREHGSDEWVAMTKGEGGVWTFDSEEPLQGPFNFRFLTEKGMKNVFDDVVPEKYTIGATYAP
>d1gzi__ 2.60.1.1.1 Antifreeze protein type III [Ocean pout (Macrozoarces americanus)]
NQASVVANQLIPINTALTLVMMRSEVVTPVGIPAEDIPRLVSMQVNRAVPLGTTLMPDMVKGYAA
>d2kaub_ 2.60.2.1.1 Urease, beta-subunit [Klebsiella aerogenes]
MIPGEYHVKPGQIALNTGRATCRVVVENHGDRPIQVGSHYHFAEVNPALKFDRQQAAGYRLNIPAGTAVRFEPGQKREVELVAFAGHRAVFGFRGEVMGPL
>d1dupa_ 2.60.3.1.1 Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) [Escherichia coli]
MMKKIDVKILDPRVGKEFPLPTYATSGSAGLDLRACLNDAVELAPGDTTLVPTGLAIHIADPSLAAMMLPRSGLGHKHGIVLGNLVGLIDSDYQGQLMISVWNRGQDSFTIQPGERIAQMIFVPVVQAEFNLVEDF
>d1duta_ 2.60.3.1.2 Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) [FIV (Feline immunodeficiency virus)]
MIIEGDGILDKRSEDAGYDLLAAKEIHLLPGEVKVIPTGVKLMLPKGYWGLIIGKSSIGSKGLDVLGGVIDEGYRGEIGVIMINVSRKSITLMERQKIAQLIILPCKHEVLEQGKVV
>d1tul__ 2.60.4.1.1 ACMNPV telokin-like protein [Baculovirus (Autographa californica nuclear polyhedrosis virus)]
GTPDIIVNAQINSEDENVLDFIIEDEYYLKKRGVGAHIIKVASSPQLRLLYKNAYSTVSCGNYGVLCNLVQNGEYDLNAIMFNCAEIKLNKGQMLFQTKIWR
>d2kauc1 2.61.1.1.1 (1-128,422-474) alpha-Subunit of urease, composite domain [Klebsiella aerogenes]
SNISRQAYADMFGPTVGDKVRLADTELWIEVEDDLTTYGEEVKFGGGKVIRDGMGQGQMLAADCVDLVLTNALIVDHWGIVKADIGVKDGRIFAIGKAGNPDIQPNVTIPIGAATEVIAAEGKIVTA
>d1npoa_ 2.7.1.1.1 Neurophysin II [bovine (Bos taurus)]
LELRQCLPCGPGGKGRCFGPSICCGDELGCFVGTAEALRCQEENYLPSPCQSGQKPCGSGGRCAAAGICCNDESCVTEPEC
>d2bpa1_ 2.8.1.1.1 Bacteriophage capsid proteins [bacteriophage phiX174]
SNIQTGAERMPHDLSHLGFLAGQIGRLITISTTPVIAGDSFEMDAVGALRLSPLRRGLAIDSTVDIFTFYVPHRHVYGEQWIKFMKDGVNATPLPTVNTTGYIDHAAFLGTINPDTNKIPKHLFQGYLNIYNNYFKAPWMPDRTEANPNELNQDDARYGFRCCHLKNIWTAPLPPETELSRQMTTSTTSIDIMGLQAAYANLHTDQERDYFMQRYRDVISSFGGKTSYDADNRPLLVMRSNLWASGYDVDGTDQTSLGQFSGRVQQTYKHSVPRFFVPEHGTMFTLALVRFPPTATKEIQYLNAKGALTYTDIAGDPVLYGNLPPREISMKDVFRSGDSSKKFKIAEGQWYRYAPSYVSPAYHLLEGFPFIQEPPSGDLQERVLIRHHDYDQCFQSVQLLQWNSQVKFNVTVYRNLPTTRDSIMTS
>d2bpa2_ 2.8.1.1.1 Bacteriophage capsid proteins [bacteriophage phiX174]
MFQTFISRHNSNFFSDKLVLTSVTPASSAPVLQTPKATSSTLYFDSLTVNAGNGGFLHCIQMDTSVNAANQVVSVGADIAFDADPKFFACLVRFESSSVPTTLPTAYDVYPLNGRHDGGYYTVKDCVTIDVLPRTPGNNVYVGFMVWSNFTATKCRGLVSLNQVIKEIICLQPLK
>d1gff2_ 2.8.1.1.2 Bacteriophage capsid proteins [bacteriophage G4]
MFQKFISKHNAPINSTQLAATKTPAVAAPVLSVPNLSRSTILINATTTAVTTHSGLCHVVRIDETNPTNHHALSIAGSLSNVPADMIAFAIRFEVADGVVPTAVPALYDVYPIETFNNGKAISFKDAVTIDSHPRTVGNDVYAGIMLWSNAWTASTISGVLSVNQVNREATVLQPLK
>d1gff1_ 2.8.1.1.2 Bacteriophage capsid proteins [bacteriophage G4]
VPHDLSHLVFEAGKIGRLKTISWTPVVAGDSFECDMVGAIRLSPLRRGLAVDSRVDIFSFYIPHRHIYGQQWINFMKDGVNASPLPPVTCSSGWDSAAYLGTIPSSTLKVPKFLHQGYLNIYNNYFKPPWSDDLTYANPSNMPSEDYKWGVRVANLKSIWTAPLPPDTRTSENMTTGTSTIDIMGLQAAYAKLHTEQERDYFMTRYRDIMKEFGGHTSYDGDNRPLLLMRSEFWASGYDVDGTDQSSLGQFSGRVQQTFNHKVPRFYVPEHGVIMTLAVTRFPPTHEMEMHYLVGKENLTYTDIACDPALMANLPPREVSLKEFFHSSPDSAKFKIAEGQWYRTQPDRVAFPYNALDGFPFYSALPSTDLKDRVLVNTNNYDEIFQSMQLAHWNMQTKFNINVYRHMPTTRDSIMTS
>d1stma_ 2.8.1.2.1 SPMV coat protein [Sattelite panicum mosaic virus]
AAATSLVYDTCYVTLTERATTSFQRQSFPTLKGMGDRAFQVVAFTIQGVSAAPLMYNARLYNPGDTDSVHATGVQLMGTVPRTVRLTPRVGQNNWFFGNTEEAETILAIDGLVSTKGANAPSNTVIVTGCFRLAPSELQSS
>d2stv__ 2.8.1.2.2 STNV coat protein [satellite tobacco necrosis virus]
TMRAVKRMINTHLEHKRFALINSGNTNATAGTVQNLSNGIIQGDDINQRSGDQVRIVSHKLHVRGTAITVSQTFRFIWFRDNMNRGTTPTVLEVLNTANFMSQYNPITLQQKRFTILKDVTLNCSLTGESIKDRIINLPGQLVNYNGATAVAASNGPGAIFMLQIGDSLVGLWDSSYEAVYTDA
>d1smva_ 2.8.1.2.3 SMV coat potein [sesbania mosaic virus]
GAITVLHCELTAEIGVTDSIVVSSELVMPYTVGTWLRGVADNWSKYSWLSVRYTYIPSCPSSTAGSIHMGFQYDMADTVPVSVNKLSNLRGYVSGQVWSGSAGLCFINNSRCSDTSTAISTTLDVSELGKKWYPYKTSADYATAVGVDVNIATDLVPARLVIALLDGSSSTAVAAGRIYDTYTIQMIEPTASALNL
>d1bmv2_ 2.8.1.2.4 BPMV coat protein [Bean pod mottle virus]
METNLFKLSLDDVETPKGSMLDLKISQSKIALPKNTVGGTILRSDLLANFLTEGNFRASVDLQRTHRIKGMIKMVATVGIPENTGIALACAMNSSIRGRASSDIYTICSQDCELWNPACTKAMTMSFNPNPCSDAWSLEFLKRTGFHCDIICVTGWTATPMQDVQVTIDWFISSQECVPRTYCVLNPQNPFVLNRWMGKLTFPQGTSRSVKRMPLSIGGGAGAKSAILMNMPNAVLSMWRYFVGDLVFEVSKMTSPYIKCTVSFFIAFGNLADDTINFEAFPHKLVQFGEIQEKVVLKFSQEEFLTAWSTQVRPATTLLADGCPYLYAMVHDSSVSTIPGDFVIGVKLTIIENMCAYGLNPGISGSRLLGTIPQ
>d1bmv1_ 2.8.1.2.4 BPMV coat protein [Bean pod mottle virus]
SISQQTVWNQMATVRTPLNFDSSKQSFCQFSVDLLGGGISVDKTGDWITLVQNSPISNLLRVAAWKKGCLMVKVVMSGNAAVKRSDWASLVQVFLTNSNSTEHFDACRWTKSEPHSWELIFPIEVCGPNNGFEMWSSEWANQTSWHLSFLVDNPKQSTTFDVLLGISQNFEIAGNTLMPAFSVPQ
>d4sbva_ 2.8.1.2.5 SBMV coat protein [southern bean mosaic virus (Cow pea strain)]
SSMDVTILSHCELSTELAVTVTIVVTSELVMPFTVGTWLRGVAQNWSKYAWVAIRYTYLPSCPTTTSGAIHMGFQYDMADTLPVSVNQLSNLKGYVTGPVWEGQSGLCFVNNTKCPDTSRAITIALDTNEVSEKRYPFKTATDYATAVGVNANIGNILVPARLVTAMEGGSSKTAVNTGRLYASYTIRLIEPIAAALNL
>d2tbva_ 2.8.1.2.6 TBSV coat protein [tomato bushy stunt virus]
GVTVTSHREYLTQVNNSSGFVVNGGIVGNSLQLNPSNGTLFSWLPALASNFDQYSFNSVVLDYVPLCGTTEVGRVALYFDKDSQDPEPADRVELANFGVLKETAPWAEAMLRIPTDKVKRYCNDSATVDQKLIDLGQLGIATYGGAGADAVGELFLARSVTLYFPQPTNTLLSSKRLDLTGSLADATGPGYLVLTRTPTVLTHTFRATGTFNLSGGLRCLTSLTLGATGAVVINDILAIDNVGTASDYFLNCTVSSLPATVTFTVSGVAAGILLVGRARANVVNLL
>d1cwpa_ 2.8.1.2.7 Cowpea chlorotic mottle virus [host: cowpea (Vigna unguiculta) (L.)]
KAIKAWTGYSVSKWTASCAAAEAKVTSAITISLPNELSSERNKQLKVGRVLLWLGLLPSVSGTVKSCVTETQTTAAASFQVALAVADNSKDVVAAMYPEAFKGITLEQLAADLTIYLYSSAALTEGDVIVHLEVEHVRPTFDDSFTPVY
>d2bbva_ 2.8.1.3.1 Black beetle virus (BBV) capsid protein [Black beetle virus: grown in (Drosophila melanogaster)]
LTRLSQPGLAFLKCAFAPPDFNTDPGKGIPDRFEGKVVTRKDVLNQSINFTANRDTFILIAPTPGVAYWVADVPAGTFPISTTTFNAVNFPGFNSMFGNAAASRSDQVSSFRYASMNVGIYPTSNLMQFAGSITVWKCPVKLSNVQFPVATTPATSALVHTLVGLDGVLAVGPDNFSESFIKGVFSQSVCNEPDFEFSDILEGIQTLPPANVTVATSGQPFNLAAGAEAVSGIVGWGNMDTIVIRVSAPTGAVNSAILKTWACLEYRPNPNAMLYQFGHDSPPCDEVALQEYRTVARSLPVAVIAAQN
>d1sida_ 2.8.1.4.1 Murine polyomavirus coat protein vp1 [Murine poluomavirus (Strain small-plaque 16)]
KACPRPAPVPKLLIKGGMEVLDLVTGPDSVTEIEAFLNPRMGQPPTPESLTEGGQYYGWSRGINLATSDTEDSPGNNTLPTWSMAKLQLPMLNEDLTCDTLQMWEAVSVKTEVVGSGSLLDVHGFNKPTDTVNTKGISTPVEGSQYHVFAVGGEPLDLQGLVTDARTKYKEEGVVTIKTITKKDMVNKDQVLNPISKAKLDKDGMYPVEIWHPDPAKNENTRYFGNYTGGTTTPPVLQFTNTLTTVLLDENGVGPLCKGEGLYLSCVDIMGWRVTRNYDVHHWRGLPRYFKITLRKRWVKNPYPMASLISSLFNNMLPQVQGQPMEGENTQVEEVRVYDGTEPVPGDPDMTRYVDRFGKTKTVFPG
>d2mev1_ 2.8.1.4.10 Mengo virus [Host: monkey brain; middle size plaque variant]
GVENAEKGVTENTDATADFVAQPVYLPENQTKVAFFYDRSSPIGAFAVKSGSLESGFAPFSNKACPNSVILTPGPQFDPAYDQLRPQRLTEIWGNGNEETSEVFPLKTKQDYSFCLFSPFVYYKCDLEVTLSPHTSGAHGLLVRWCPTGTPTKPTTQVLHEVSSLSEGRTPQVYSAGPGTSNQISFVVPYNSPLSVLPAVWYNGHKRFDNTGDLGIAPNSDFGTLFFAGTKPDIKFTVYLRYKNMRVFCPRPTVFFPWPTSGDKIDMT
>d2mev3_ 2.8.1.4.10 Mengo virus [Host: monkey brain; middle size plaque variant]
SPIPVTIREHAGTWYSTLPDSTVPIYGKTPVAPANYMVGEYKDFLEIAQIPTFIGNKVPNAVPYIEASNTAVKTQPLAVYQVTLSCSCLANTFLAALSRNFAQYRGSLVYTFVFTGTAMMKGKFLIAYTPPGAGKPTSRDQAMQATYAIWDLGLNSSYSFTVPFISPTHFRMVGTDQANITNVDGWVTVWQLTPLTYPPGCPTSAKILTMVSAGKDFSLKMPISPAPWSPQ
>d2mev2_ 2.8.1.4.10 Mengo virus [Host: monkey brain; middle size plaque variant]
ENLSDRVSQDTAGNTVTNTQSTVGRLVGYGTVHDGEHPASCADTASEKILAVERYYTFKVNDWTSTQKPFEYIRIPLPHVLSGEDGGVFGATLRRHYLVKTGWRVQVQCNASQFHAGSLLVFMAPEYPTLDVFAMDNRWSKDNLPNGTRTQTNRKGPFAMDHQNFWQWTLYPHQFLNLRTNTTVDLEVPYVNIAPTSSWTQHASWTLVIAVVAPLTYSTGASTSLDITASIQPVRPVFNGLRHEVLSRQ
>d1cov2_ 2.8.1.4.11 Coxsackievirus B3 [Host: human (Homo sapiens)]
GYSDRVRSITLGNSTITTQECANVVVGYGVWPDYLKDSEATAEDQPTQPDVATCRFYTLDSVQWQKTSPGWWWKLPDALSNLGLFGQNMQYHYLGRTGYTIHVQCNASKFHQGCLLVVCVPEAEMGCATLNNTPSSAELLGGDTAKEFADKPVASGSNKLVQRVVYNAGMGVGVGNLTIFPHQWINLRTNNSATIVMPYTNSVPMDNMFRHNNVTLMVIPFVPLDYCPGSTTYVPITVTIAPMCAEYNGLRLAGHQ
>d1cov3_ 2.8.1.4.11 Coxsackievirus B3 [Host: human (Homo sapiens)]
GLPTMNTPGSCQFLTSDDFQSPSAMPQYDVTPEMRIPGEVKNLMEIAEVDSVVPVQNVGEKVNSMEAYQIPVRSNEGSGTQVFGFPLQPGYSSVFSRTLLGEILNYYTHWSGSIKLTFMFCGSAMATGKFLLAYSPPGAGAPTKRVDAMLGTHVVWDVGLQSSCVLCIPWISQTHYRYVASDEYTAGGFITCWYQTNIVVPADAQSSCYIMCFVSACNDFSVRLLKDTPFISQENFFQ
>d1cov1_ 2.8.1.4.11 Coxsackievirus B3 [Host: human (Homo sapiens)]
RVADTVGTGPTNSEAIPALTAAETGHTSQVVPSDTMQTRHVKNYHSRSESTIENFLCRSACVYFTEYENSGAKRYAEWVITPRQAAQLRRKLEFFTYVRFDLELTFVITSTQQPSTTQNQDAQILTHQIMYVPPGGPVPDKVDSYVWQTSTNPSVFWTEGNAPPRMSVPFLSIGNAYSNFYDGWSEFSRNGVYGINTLNNMGTLYARHVNAGSTGPIKSTIRIYFKPKHVKAWIPRPPRLCQYEKAKNVNFQPSGVTTTRQSITTMTNT
>d1tme1_ 2.8.1.4.12 Theiler's murine encephalomyelitis virus [theiler's murine encephalomyelitis virus (Strain da)]
GSDNAEKGKVSNDDASVDFVAEPVKLPENQTRVAFFYDRAVPIGMLRPGQNIESTFVYQENDLRLNCLLLTPLPSFCPDSTSGPVKTKAPVQWRWVRSGGTTNFPLMTKQDYAFLCFSPFTYYKCDLEVTVSALGTDTVASVLRWAPTGAPADVTDQLIGYTPSLGETRNPHMWLVGAGNTQISFVVPYNSPLSVLPAAWFNGWSDFGNTKDFGVAPNADFGRLWIQGNTSASVRIRYKKMKVFCPRPTLFFPWPV
>d1tme2_ 2.8.1.4.12 Theiler's murine encephalomyelitis virus [theiler's murine encephalomyelitis virus (Strain da)]
DRVASDKAGNSATNTQSTVGRLCGYGEAHHGEHPASCADTATDKVLAAERYYTIDLASWTTTQEAFSHIRIPLPHVLAGEDGGVFGATLRRHYLCKTGWRVQVQCNASQFHAGSLLVFMAPEFYTGKGTKTGDMEPTDPFTMDTTWRAPQGAPTGYRYDSRTGFFAMNHQNQWQWTVYPHQILNLRTNTTVDLEVPYVNIAPTSSWTQHANWTLVVAVFSPLQYASGSSSDVQITASIQPVNPVFNGLRHETVIA
>d1tmf1_ 2.8.1.4.12 Theiler's murine encephalomyelitis virus [theiler's murine encephalomyelitis virus (Strain da)]
GVDNAEKGKVSNDDASVDFVAEPVKLPENQTRVAFFYDRAVPIGMLRPGQNMETTFNYQENDYRLNCLLLTPLPSFCPDSSSGPQKTKAPVQWRWVRSGGVNGANFPLMTKQDYAFLCFSPFTFYKCDLEVTVSALGTDTVASVLRWAPTGAPADVTDQLIGYTPSLGETRNPHMWLVGAGNSQVSFVVPYNSPLSVLPAAWFNGWSDFGNTKDFGVAPNADFGRLWIQGNTSASVRIRYKKMKVFCPRPTLFFPWPTPTTTKINADNPVPILELE
>d1tme3_ 2.8.1.4.12 Theiler's murine encephalomyelitis virus [theiler's murine encephalomyelitis virus (Strain da)]
SPIAVTVREHKGCFYSTNPDTTVPIYGKTISTPNDYMCGEFSDLLELCKLPTFLGNPNSNNKRYPYFSATNSVPTTSLVDYQVALSCSCMCNSMLAAVARNFNQYRGSLNFLFVFTGAAMVKGKFLIAYTPPGAGKPTTRDQAMQATYAIWDLGLNSSFVFTAPFISPTHYRQTSYTSAASVDGWVTVWQLTPLTYPSGTPVNSDILTLVSAGDDFTLRMPISPTKWVPQ
>d1tmf2_ 2.8.1.4.12 Theiler's murine encephalomyelitis virus [theiler's murine encephalomyelitis virus (Strain da)]
DQNTEEMENLSDRVASDKAGNSATNTQSTVGRLCGYGKSHHGEHPASCADTATDKVLAAERYYTIDLASWTTSQEAFSHIRIPLPHVLAGEDGGVFGATLRRHYLCKTGWRVQVQCNASQFHAGSLLVFMAPEFYTGKGTKTGTMEPSDPFTMDTEWRSPQGAPTGYRYDSRTGFFATNHQNQWQWTVYPHQILNLRTNTTVDLEVPYVNVAPSSSWTQHANWTLVVAVLSPLQYATGSSPDVQITASLQPVNPVFNGLRHETVIAQ
>d1sva1_ 2.8.1.4.14 Simian virus 40 (SV40) coat protein [Simian virus 40, SV40]
PKKPKEPVQVPKLVIKGGIEVLGVKTGVDSFTEVECFLNPQMGNPDEHQKGLSKSLAAEKQFTDDSPDKEQLPCYSVARIPLPNINEDLTCGNILMWEAVTVKTEVIGVTAMLNLHSGTQKTHENGAGKPIQGSNFHFFAVGGEPLELQGVLANYRTKYPAQTVTPKNATVDSQQMNTDHKAVLDKDNAYPVECWVPDPSKNENTRYFGTYTGGENVPPVLHITNTATTVLLDEQGVGPLCKADSLYVSAVDICGLFTNTSGTQQWKGLPRYFKITLRKRSVKNPYPISFLLSDLINRRTQRVDGQPMIGMSSQVEEVRVYEDTEELPGDPDMIRYIDEFGQTTTRMQ
>d1dhx__ 2.8.1.4.15 Adenovirus type 2 hexon [Host: human (Homo sapiens)]
FRNPTVAPTHDVTTDRSQRLTLRFIPVDREDTAYSYKARFTLAVGDNRVLDMASTYFDIRGVLDRGPTFKPYSGTAYNALAPKGAPNSCEWEQTEDSGRAVAEDEEEEDEDEEEEEEEQNARDQATKKTHVYAQAPLSGETITKSGLQIGSDNAETQAKPVYADPSYQPEPQIGESQWNEADANAAGGRVLKKTTPMKPCYGSYARPTNPFGGQSVLVPDEKGVPLPKVKPKVVLYSEDVNMETPDTHLSYKPGKGDENSKAMLGQQSMPNRPNYIAFRDNFIGLMYYNSTGNMGVLAGQASQLNAVVDLQDRNTELSYQLLLDSIGDRTRYFSMWNQAVDSYDPDVRIIENHGTEDELPNYCFPLGGIGVTDTYQAIKANGNGSGDNGDTTWTKDETFATRNEIGVGNNFAMEINLNANLWRNFLYSNIALYLPDKLKYNPTNVEISDNPNTYDYMNKRVVAPGLVDCYINLGARWSLDYMDNVNPFNHHRNAGLRYRSMLLGNGRYVPFHIQVPQKFFAIKNLLLLPGSYTYEWNFRKDVNMVLQSSLGNDLRVDGASIKFDSICLYATFFPMAHNTASTLEAMLRNDTNDQSFNDYLSAANMLYPIPANATNVPISIPSRNWAAFRGWAFTRLKTKETPSLGSGYDPYYTYSGSIPYLDGTFYLNHTFKKVAITFDSSVSWPGNDRLLTPNEFEIKRSVDGEGYNVAQCNMTKDWFLVQMLANYNIGYQGFYIPESYKDRMYSFFRNFQPMSRQVVDDTKYKEYQQVGILHQHNNSGFVGYLAPTMREGQAYPANVPYPLIGKTAVDSITQKKFLCDRTLWRIPFSSNFMSMGALTDLGQNLLYANSAHALDMTFEVDPMDEPTLLYVLFEVFDVVRVHQPHRGVIETVYLRTPFSAGNATT
>d1fmd2_ 2.8.1.4.2 Foot-and-mouth desease virus [foot-and-mouth disease virus (Strain bfs, 1860)]
DKKTEETTLLEDRILTTRNGHTTSTTQSSVGVTFGYATAEDSTSGPNTSALETRVHQAERFFKMALFDWVPSQNFGHMHKVVLPHEPKGVYGGLVKSYAYMRNGWDVEVTAVGNQFNGGCLLVALVPEMGDISDREKYQLTLYPHQFINPRTNMTAHITVPYVGVNRYDQYKQHRPWTLVVMVVAPLTTNTAGAQQIKVYANIAPTNVHVAGELPSKE
>d1bbt3_ 2.8.1.4.2 Foot-and-mouth desease virus [foot-and-mouth disease virus (Strain bfs, 1860)]
GIFPVACSDGYGGLVTTDPKTADPVYGKVFNPPRNQLPGRFTNLLDVAEACPTFLRFEGGVPYVTTKTDSDRVLAQFDMSLAAKHMSNTFLAGLAQYYTQYSGTINLHFMFTGPTDAKARYMVAYAPPGMEPPKTPEAAAHCIHAEWDTGLNSKFTFSIPYLSAADYTYTASDVAETTNVQGWVCLFQITHGKADGDALVVLASAGKDFELRLPVDARAE
>d1fmd1_ 2.8.1.4.2 Foot-and-mouth desease virus [foot-and-mouth disease virus (Strain bfs, 1860)]
TTTTGESADPVTTTVENYGGETQVQRRHHTDVAFVLDRFVKVTVSDNQHTLDVMQAHKDNIVGALLRAATYYFSDLEIAVTHTGKLTWVPNGAPVSALNNTTNPTAYHKGPVTRLALPYTAPHRVLATAYTGAHLPTSFNFGAVKAETITELLVRMKRAELYCPRPILPIQPTGDRHKQPLVAPAKQ
>d1bbt2_ 2.8.1.4.2 Foot-and-mouth desease virus [foot-and-mouth disease virus (Strain bfs, 1860)]
LLEDRILTTRNGHTTSTTQSSVGVTYGYATAEDFVSGPNTSGLETRVVQAERFFKTHLFDWVTSDSFGRCHLLELPTDHKGVYGSLTDSYAYMRNGWDVEVTAVGNQFNGGCLLVAMVPELCSIQKRELYQLTLFPHQFINPRTNMTAHITVPFVGVNRYDQYKVHKPWTLVVMVVAPLTVNTEGAPQIKVYANIAPTNVHVAGEFPSKE
>d1bbt1_ 2.8.1.4.2 Foot-and-mouth desease virus [foot-and-mouth disease virus (Strain bfs, 1860)]
TTSAGESADPVTTTVENYGGETQIQRRQHTDVSFIMDRFVKVTPQNQINILDLMQVPSHTLVGGLLRASTYYFSDLEIAVKHEGDLTWVPNGAPEKALDNTTNPTAYHKAPLTRLALPYTAPHRVLATVYNGECRTLPTSFNYGAIKATRVTELLYRMKRAETYCPRPLLAIHPTEARHKQKIVAP
>d1fmd3_ 2.8.1.4.2 Foot-and-mouth desease virus [foot-and-mouth disease virus (Strain bfs, 1860)]
GIFPVACSDGYGNMVTTDPKTADPAYGKVYNPPRTALPGRFTNYLDVAEACPTFLMFENVPYVSTRTDGQRLLAKFDVSLAAKHMSNTYLAGLAQYYTQYTGTINLHFMFTGPTDAKARYMVAYVPPGMDAPDNPEEAAHCIHAEWDTGLNSKFTFSIPYISAADYTYTASHEAETTCVQGWVCVYQITHGKADADALVVSASAGKDFELRLPVDARQQ
>d1pov3_ 2.8.1.4.3 Poliovirus [poliovirus (type 1, mahoney strain)]
GLPVMNTPGSNQYLTADNFQSPCALPEFDVTPPIDIPGEVKNMMELAEIDTMIPFDLSATKKNTMEMYRVRLSDKPHTDDPILCLSLSPASDPRLSHTMLGEILNYYTHWAGSLKFTFLFCGSMMATGKLLVSYAPPGADPPKKRKEAMLGTHVIWDIGLQSSCTMVVPWISNTTYRQTIDDSFTEGGYISVFYQTRIVVPLSTPREMDILGFVSACNDFSVRLLRDTTHIEQKALAQ
>d1pov1_ 2.8.1.4.3 Poliovirus [poliovirus (type 1, mahoney strain)]
QHRSRSESSIESFFARGACVTIMTVDNPASTTNKDKLFAVWKITYKDTVQLRRKLEFFTYSRFDMELTFVVTANFTETNNGHALNQVYQIMYVPPGAPVPEKWDDYTWQTSSNPSIFYTYGTAPARISVPYVGISNAYSHFYDGFSKVPLKDQSAALGDSLYGAASLNDFGILAVRVVNDHNPTKVTSKIRVYLKPKHIRVWCPRPPRAVAYYGPGVDYKDGTLTPLSTKDLTTY
>d1pov0_ 2.8.1.4.3 Poliovirus [poliovirus (type 1, mahoney strain)]
GAQVSSQKVGAHINYTTINYYRDSASNAASKQIKDVLIKTAPMLNSPNIEACGYLQLTLGNSTITTQEAANSVVAYGRWPEYLRDVAACRFYTLDTVSWTKESRGWWWKLPDALRDMGLFGQNMYYHYLGRSGYTVHVQCNASKFHQGALGVFAVPEMCLAGDSNTTTMHTSYQNANPGEKGGTFTGTFTPDNNQTSPARRFCPVDYLLGNGTLLGNAFVFPHQIINLRTNNCATLVLPYVNSLSIDSMVKHNNWGIAILPLAPLNFASESSPEIPITLTIAPMCCEFNGLRNITLPRLQ
>d1pvc2_ 2.8.1.4.4 Poliovirus [poliovirus (type 3, sabin strain)]
ACGYSDRVLQLTLGNSTITTQEAANSVVAYGRWPEFIRDDEANPVDQPTEPDVATCRFYTLDTVMWGKESKGWWWKLPDALRDMGLFGQNMYYHYLGRSGYTVHVQCNASKFHQGALGVFAIPEYCLAGDSDKQRYTSYANANPGERGGKFYSQFNKDNAVTSPKREFCPVDYLLGCGVLLGNAFVYPHQIINLRTNNSATIVLPYVNALAIDSMVKHNNWGIAILPLSPLDFAQDSSVEIPITVTIAPMCSEFNGLRNVTAPKFQ
>d1pvc1_ 2.8.1.4.4 Poliovirus [poliovirus (type 3, sabin strain)]
QDSLPDTKASGPAHSKEVPALTAVETGATNPLAPSDTVQTRHVVQRRSRSESTIESFFARGACVAIIEVDNEQPTTRAQKLFAMWRITYKDTVQLRRKLEFFTYSRFDMEFTFVVTANFTNANNGHALNQVYQIMYIPPGAPTPKSWDDYTWQTSSNPSIFYTYGAAPARISVPYVGLANAYSHFYDGFAKVPLKTDANDQIGDSLYSAMTVDDFGVLAVRVVNDHNPTKVTSKVRIYMKPKHVRVWCPRPPRAVPYYGPGVDYRNNLDPLSEKGLTTY
>d1pvc3_ 2.8.1.4.4 Poliovirus [poliovirus (type 3, sabin strain)]
GLPVLNTPGSNQYLTSDNHQSPCAIPEFDVTPPIDIPGEVKNMMELAEIDTMIPLNLESTKRNTMDMYRVTLSDSADLSQPILCLSLSPAFDPRLSHTMLGEVLNYYTHWAGSLKFTFLFCGSMMATGKILVAYAPPGAQPPTSRKEAMLGTHVIWDLGLQSSCTMVVPWISNVTYRQTTQDSFTEGGYISMFYQTRIVVPLSTPKSMSMLGFVSACNDFSVRLLRDTTHISQSA
>d2cas__ 2.8.1.4.5 Parvovirus capsid [Host: canine (Canis familiaris)]
GVGISTGTFNNQTEFKFLENGWVEITANSSRLVHLNMPESENYRRVVVNNMDKTAVNGNMALDDIHAQIVTPWSLVDANAWGVWFNPGDWQLIVNTMSELHLVSFEQEIFNVVLKTVSESATQPPTKVYNNDLTASLMVALDSNNTMPFTPAAMRSETLGFYPWKPTIPTPWRYYFQWDRTLIPSHTGTSGTPTNIYHGTDPDDVQFYTIENSVPVHLLRTGDEFATGTFFFDCKPCRLTHTWQTNRALGLPPFLNSLPQSEGATNFGDIGVQQDKRRGVTQMGNTNYITEATIMRPAEVGYSAPYYSFEASTQGPFKTPIAAGRGGAQTDENQAADGNPRYAFGRQHGQKTTTTGETPERFTYIAHQDTGRYPEGDWIQNINFNLPVTNDNVLLPTDPIGGKTGINYTNIFNTYGPLTALNNVPPVYPNGQIWDKEFDTDLKPRLHVNAPFVCQNNCPGQLFVKVAPNLTNEYDPDASANMSRIVTYSDFWWKGKLVFKAKLRASHTWNPIQQMSINVDNQFNYVPSNIGGMKIVYEKSQLAPRKLY
>d1r091_ 2.8.1.4.6 Rhinovirus coat protein [Human (Homo sapiens) rhinovirus 14]
TVASISSGPKHTQKVPILTANETGATMPVLPSDSIETRTTYMHFNGSETDVECFLGRAACVHVTEIQNKDATGIDNHREAKLFNDWKINLSSLVQLRKKLELFTYVRFDSEYTILATASQPDSANYSSNLVVQAMYVPPGAPNPKEWDDYTWQSASNPSVFFKVGDTSRFSVPYVGLASAYNCFYDGYSHDDAETQYGITVLNHMGSMAFRIVNEHDEHKTLVKIRVYHRAKHVEAWIPRAPRALPYTSIGRTNYPKNTEPVIKKRKGDIKSY
>d1r093_ 2.8.1.4.6 Rhinovirus coat protein [Human (Homo sapiens) rhinovirus 14]
GLPTTTLPGSGQFLTTDDRQSPSALPNYEPTPRIHIPGKVHNLLEIIQVDTLIPMNNTHTKDEVNSYLIPLNANRQNEQVFGTNLFIGDGVFKTTLLGEIVQYYTHWSGSLRFSLMYTGPALSSAKLILAYTPPGARGPQDRREAMLGTHVVWDIGLQSTIVMTIPWTSGVQFRYTDPDTYTSAGFLSCWYQTSLILPPETTGQVYLLSFISACPDFKLRLMKDTQTISQTVALTE
>d1r092_ 2.8.1.4.6 Rhinovirus coat protein [Human (Homo sapiens) rhinovirus 14]
GYSDRVQQITLGNSTITTQEAANAVVCYAEWPEYLPDVDASDVNKTSKPDTSVCRFYTLDSKTWTTGSKGWCWKLPDALKDMGVFGQNMFFHSLGRSGYTVHVQCNATKFHSGCLLVVVIPEHQLASHEGGNVSVKYTFTHPGERGIDLSSANEVGGPVKDVLYNMNGTLLGNLLIFPHQFINLRTNNTATIVIPYINSVPIDSMTRHNNVSLMVIPIAPLTVPTGATPSLPITVTIAPMCTEFSGIRSKSIVPQ
>d2rhn3_ 2.8.1.4.7 Rhinovirus coat protein [Human (Homo sapiens) rhinovirus 16]
GLPVYVTPGSGQFMTTDDMQSPCALPWYHPTKEIFIPGEVKNLIEMCQVDTLIPINSTQSNIGNVSMYTVTLSPQTKLAEEIFAIKVDIASHPLATTLIGEIASYFTHWTGSLRFSFMFCGTANTTLKVLLAYTPPGIGKPRSRKEAMLGTHVVWDVGLQSTVSLVVPWISASQYRFTTPDTYSSAGYITCWYQTNFVVPPNTPNTAEMLCFVSGCNHFCLRMARDTDLHKQTGPITQ
>d2rhn2_ 2.8.1.4.7 Rhinovirus coat protein [Human (Homo sapiens) rhinovirus 16]
DRIIQITRGDSTITSQDVANAVVGYGVWPHYLTPQDATAIDKPTQPDTSSNRFYTLDSKMWNSTSKGWWWKLPDALKDMGIFGENMFYHFLGRSGYTVHVQCNASKFHQGTLLVVMIPEHQLATVNKGNVNAGYKYTHPGEAGREVGTQVENEKQPSDDNWLNFDGTLLGNLLIFPHQFINLRSNNSATLIVPYVNAVPMDSMVRHNNWSLVIIPVCQLQSNNISNIVPITVSISPMCAEFSGARAKTV
>d2rhn1_ 2.8.1.4.7 Rhinovirus coat protein [Human (Homo sapiens) rhinovirus 16]
RYVDEVLNEVLVVPNINQSHPTTSNAAPVLDAAETGHTNKIQPEDTIETRYVQSSQTLDEMSVESFLGRSGCIHESVLDIVDNYNDQSFTKWNINLQEMAQIRRKFEMFTYARFDSEITMVPSVAAKDGHIGHIVMQYMYVPPGAPIPTTRDDYAWQSGTNASVFWQHGQPFPRFSLPFLSIASAYYMFYDGYDGDTYKSRYGTVVTNDMGTLCSRIVTSEQLHKVKVVTRIYHKAKHTKAWCPRPPRAVQYSHTHTTNYKLSSEVHNDVAIRPRTNLTT
>d1r1a3_ 2.8.1.4.8 Rhinovirus coat protein [Human (Homo sapiens) rhinovirus 1A]
GLPVYITPGSGQFMTTDDMQSPCALPWYHPTKEISIPGEVKNLIEMCQVDTLIPVNNVGNNVGNVSMYTVQLGNQTGMAQKVFSIKVDITSTPLATTLIGEIASYYTHWTGSLRFSFMFCGTANTTLKLLLAYTPPGIDEPTTRKDAMLGTHVVWDVGLQSTISLVVPWVSASHFRLTADNKYSMAGYITCWYQTNLVVPPSTPQTADMLCFVSACKDFCLRMARDTDLHIQSGPIEQ
>d1r1a2_ 2.8.1.4.8 Rhinovirus coat protein [Human (Homo sapiens) rhinovirus 1A]
DRIMQITRGDSTISSDDVANAVVGYGVWPHYLTPQDATAINKPTQPDTSSNRFYTLESKHWNGSSKGWWWKLPDALKDMGIFGENMYYHFLGRSGYTVHVQCNASKFHQGTLLVAMIPEHQLASAKHGSVTAGYKLTHPGEAGRDVSQERDASLRQPSDDSWLNFDGTLLGNLLIFPHQFINLRSNNSATLIVPYVNAVPMDSMLRHNNWCLVIIPISPLRSETTSSNIVPITVSISPMCAEFSGARAKNIKQ
>d1r1a1_ 2.8.1.4.8 Rhinovirus coat protein [Human (Homo sapiens) rhinovirus 1A]
NYIDEVLNEVLVVPNIKESHHTTSNSAPLLDAAETGHTSNVQPEDAIETRYVITSQTRDEMSIESFLGRSGCVHISRIKVDYTDYNGQDINFTKWKITLQEMAQIRRKFELFTYVRFDSEITLVPCIAGRGDDIGHIVMQYMYVPPGAPIPSKRNDFSWQSGTNMSIFWQHGQPFPRFSIPFLSIASAYYMFYDGYDGDNTSSKYGSVVTNDMGTICSRIVTEKQKLSVVITTHIYHKAKHTKAWCPRPPRAVPYTHSHVTNYMPETGDVTTAIVRRNTITTA
>d1rhi3_ 2.8.1.4.9 Rhinovirus coat protein [Human (Homo sapiens) rhinovirus 3]
GLPTTTLPGSGQFLTTDDRQSPSALPSYEPTPRIHIPGKVRNLLEIIQVGTLIPMNNTGTNDNVTNYLIPLHADRQNEQIFGTKLYIGDGVFKTTLLGEIAQYYTHWSGSLRISLMYTGPALSSAKIILAYTPPGTRGPEDKKEAMLGTHVVWDIGLQSTIVMTIPWTSGVQFRYTDPDTYTSAGYLSCWYLTSLILPPQTSGQVYLLSFISACPDFKLRLMKDTQTISQTDALTE
>d1rhi2_ 2.8.1.4.9 Rhinovirus coat protein [Human (Homo sapiens) rhinovirus 3]
GYSDRVQQITLGNSTITTQEARNAIVCYAEWPEYLSDNDASDVNKTSKPDISVCRFYTLDSKTWKATSKGWCWKLPDALKDMGVFGQNMFYHSLGRTGYTIHVQCNATKFHSGCLLVVVIPEHQLASHEGGTVSVKYKYTHPGDRGIDLDTVEVAGGPTSDAIYNMDGTLLGNLLIFPHQFINMRTNNTATIVVPYINSVPIDSMTRHNNVSLMVVPIAPLNAPTGSSPTLPVTVTIAPMCTEFTGIRSRSIVPQ
>d1rhi1_ 2.8.1.4.9 Rhinovirus coat protein [Human (Homo sapiens) rhinovirus 3]
QTLASVSSGPKHTQSVPALTANETGATLPTRPSDNVETRTTYMHFNGSETDVESFLGRAACVHVTEIKNKNAAGLDNHRKEGLFNDWKINLSSLVQLRKKLELFTYVRFDSEYTILATASQPEASSYSSNLTVQAMYVPPGAPNPKEWDDYTWQSASNPSVFFKVGETSRFSVPFVGIASAYNCFYDGYSHDDPDTPYGITVLNHMGSMAFRVVNEHDVHTTIVKIRVYHRAKHVEAWIPRAPRALPYVSIGRTNYPRDSKTIVKKRTNIKTY
>d4gcr_1 2.9.1.1.1 (1-85) gamma-Crystallin [bovine (Bos taurus) isoform II (B)]
GKITFYEDRGFQGHCYECSSDCPNLQPYFSRCNSIRVDSGCWMLYERPNYQGHQYFLRRGDYPDYQQWMGFNDSIRSCRLIPQHT
>d4gcr_2 2.9.1.1.1 (86-174) gamma-Crystallin [bovine (Bos taurus) isoform II (B)]
GTFRMRIYERDDFRGQMSEITDDCPSLQDRFHLTEVHSLNVLEGSWVLYEMPSYRGRQYLLRPGEYRRYLDWGAMNAKVGSLRRVMDFY
>d1elpa1 2.9.1.1.2 (1-85) gamma-Crystallin [bovine (Bos taurus) isoform IIIb (D)]
GKITFYEDRGFQGRHYECSSDHSNLQPYLGRCNSVRVDSGCWMIYEQPNYLGPQYFLRRGDYPDYQQWMGLNDSIRSCRLIPHAG
>d1elpa2 2.9.1.1.2 (86-173) gamma-Crystallin [bovine (Bos taurus) isoform IIIb (D)]
SHRLRLYEREDYRGQMIEITEDCSSLQDRFHFNEIHSLNVLEGSWVLYELPNYRGRQYLLRPGEYRRYHDWGAMNAKVGSLRRVIDIY
>d2gcr_2 2.9.1.1.3 (85-173) gamma-Crystallin [bovine (Bos taurus) isoform IVa]
SSHRLRIYEREDYRGQMVEITEDCSSLQDRFHFSDIHSFHVMEGYWVLYEMPNYRGRQYLLRPGDYRRYLDWGAANARVGSLRRAVDFY
>d2gcr_1 2.9.1.1.3 (1-84) gamma-Crystallin [bovine (Bos taurus) isoform IVa]
GKITFYEDRGFQGRHYECSSDHSNLQPYFSRCNSIRVDSGCWMLYEQPNFTGCQYFLRRGDYPDYQQWMGFSDSVRSCRLIPHT
>d2bb2_1 2.9.1.1.4 (2-90) beta-Crystallin [bovine (Bos taurus)]
NPKIIIFEQENFQGHSHELNGPCPNLKETGVEKAGSVLVQAGPWVGYEQANCKGEQFVFEKGEYPRWDSWTSSRRTDSLSSLRPIKVDS
>d2bb2_2 2.9.1.1.4 (91-181) beta-Crystallin [bovine (Bos taurus)]
QEHKITLYENPNFTGKKMEVIDDDVPSFHAHGYQEKVSSVRVQSGTWVGYQYPGYRGLQYLLEKGDYKDSGDFGAPQPQVQSVRRIRDMQW
>d1prr_2 2.9.1.2.1 (91-173) Protein S [Myxococcus xantus]
PRARFFYKEQFDGKEVDLPPGQYTQAELERYGIDNNTISSVKPQGLAVVLFKNDNFSGDTLPVNSDAPTLGAMNNNTSSIRIS
>d1prr_1 2.9.1.2.1 (1-90) Protein S [Myxococcus xantus]
MANITVFYNEDFQGKQVDLPPGNYTRAQLAALGIENNTISSVKVPPGVKAILYQNDGFAGDQIEVVANAEELGPLNNNVSSIRVISVPVQ
>d1wkt__ 2.9.1.3.1 Yeast killer toxin [Williopsis mrakii]
GDGYLIMCKNCDPNTGSCDWKQNWNTCVGIGANVHWMVTGGSTDGKQGCATIWEGSGCVGRSTTMCCPANTCCNINTGFYIRSYRRVE
>d1bpl.1 3.1.1.1.1 (a,b:1-181) Bacterial alpha-amylase (BLA) [Bacillus licheniformis]
LNGTLMQYFEWYMPNDGQHWKRLQNDSAYLAEHGITAVWIPPAYKGTSQADVGYGAYDLYDLGEFHQKGTVRTKYGTKGELQSAIKSLHSRDINVYGDVVINHKGGADATEDVTAVEVDPADRNRVISGEHLIKAWTHFHFPGRGSTYSDFKWHWYHFDGTDWDESRKLNRIYKFQGKAYDYLMYADIDYDHPDVAAEIKRWGTWYANELQLDGFRLDAVKHIKFSFLRDWVNHVREKTGKEMFTVAEYWQNDLGALENYLNKTNFNHSVFDVPLHYQFHAASTQGGGYDMRKLLNSTVVSKHPLKAVTFVDNHDTQPGQSLESTVQTWFKPLAYAFILTRESGYPQVFYGDMYGTKGDSLNGTLMQYFEWYMPNDGQHWKRLQNDSAYLAEHGITAVWIPPAYKGTSQADVGYGAYDLYDLGEFHQKGTVRTKYGTKGELQSAIKSLHSRDINVYGDVVINHKGGADATEDVTAVEVDPADRNRVISGEHLIKAWTHFHFPGRGSTYSDFKWHWYHFDGTDWDESRKLNRIYKFQGKAYDYLMYADIDYDHPDVAAEIKRWGTWYANELQLDGFRLDAVKHIKFSFLRDWVNHVREKTGKEMFTVAEYWQNDLGALENYLNKTNFNHSVFDVPLHYQFHAASTQGGGYDMRKLLNSTVVSKHPLKAVTFVDNHDTQPGQSLESTVQTWFKPLAYAFILTRESGYPQVFYGDMYGTKGDS
>d1jdc_2 3.1.1.1.10 (1-357) G4-amylase (1,4-alpha-D-glucan maltotetrahydrolase) [Pseudomonas stutzeri]
DQAGKSPNAVRYHGGDEIILQGFHWNVVREAPNDWYNILRQQAATIAADGFSAIWMPVPWRDFSSWSDGSKSGGGEGYFWHDFNKNGRYGSDAQLRQAASALGGAGVKVLYDVVPNHMNRGYPDKEINLPAGQGFWRNDCADPGNYPNDCDDGDRFIGGDADLNTGHPQVYGMFRDEFTNLRSQYGAGGFRFDFVRGYAPERVNSWMTDSADNSFCVGQLWKGPSEYPNWDWRNTASWQQIIKDWSDRAKCPVFDFALKERMQNGSIADWKHGLNGNPDPRWREVAVTFVDNHDTGYSPGQNGGQHHWALQDGLIRQAYAYILTSPGTPVVYWDHMYDWGYGDFIRQLIQVRRAAGV
>d1amy_2 3.1.1.1.11 (1-346) Plant alpha-amylase [Barley (Hordeum vulgare) seeds, AMY2 isozyme]
QVLFQGFNWESWKHNGGWYNFLMGKVDDIAAAGITHVWLPPASQSVAEQGYMPGRLYDLDASKYGNKAQLKSLIGALHGKGVKAIADIVINHRTAEHKDGRGIYCIFEGGTPDARLDWGPHMICRDDRPYADGTGNPDTGADFGAAPDIDHLNLRVQKELVEWLNWLKADIGFDGWRFDFAKGYSADVAKIYIDRSEPSFAVAEIWTSLAYGGDGKPNLNQDQHRQELVNWVDKVGGKGPATTFDFTTKGILNVAVEGELWRLRGTDGKAPGMIGWWPAKAVTFVDNHDTGSTQHMWPFPSDRVMQGYAYILTHPGTPCIFYDHFFDWGLKEEIDRLVSVRTRHGI
>d1cgt_4 3.1.1.1.2 (1-382) Cyclodextrin glycosyltransferase [Bacillus circulans]
DPDTAVTNKQSFSTDVIYQVFTDRFLDGNPSNNPTGAAYDATCSNLKLYCGGDWQGLINKINDNYFSDLGVTALWISQPVENIFATINYSGVTNTAYHGYWARDFKKTNPYFGTMADFQNLITTAHAKGIKIVIDFAPNHTSPAMETDTSFAENGRLYDNGTLVGGYTNDTNGYFHHNGGSDFSSLENGIYKNLYDLADFNHNNATIDKYFKDAIKLWLDMGVDGIRVDAVKHMPLGWQKSWMSSIYAHKPVFTFGEWFLGSAASDADNTDFANKSGMSLLDFRFNSAVRNVFRDNTSNMYALDSMINSTATDYNQVNDQVTFIDNHDMDRFKTSAVNNRRLEQALAFTLTSRGVPAIYYGTEQYLTGNGDPDNRAKMPSFS
>d1cdg_4 3.1.1.1.2 (1-382) Cyclodextrin glycosyltransferase [Bacillus circulans]
APDTSVSNKQNFSTDVIYQIFTDRFSDGNPANNPTGAAFDGTCTNLRLYCGGDWQGIINKINDGYLTGMGVTAIWISQPVENIYSIINYSGVNNTAYHGYWARDFKKTNPAYGTIADFQNLIAAAHAKNIKVIIDFAPNHTSPASSDQPSFAENGRLYDNGTLLGGYTNDTQNLFHHNGGTDFSTTENGIYKNLYDLADLNHNNSTVDVYLKDAIKMWLDLGIDGIRMDAVKHMPFGWQKSFMAAVNNYKPVFTFGEWFLGVNEVSPENHKFANESGMSLLDFRFAQKVRQVFRDNTDNMYGLKAMLEGSAADYAQVDDQVTFIDNHDMERFHASNANRRKLEQALAFTLTSRGVPAIYYGTEQYMSGGTDPDNRARIPSFS
>d1cyg_4 3.1.1.1.3 (1-378) Cyclodextrin glycosyltransferase [Bacillus stearothermophilus]
AGNLNKVNFTSDVVYQIVVDRFVDGNTSNNPSGALFSSGCTNLRKYCGGDWQGIINKINDGYLTDMGVTAIWISQPVENVFSVMNDASGSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPASETNPSYMENGRLYDNGTLLGGYTNDANMYFHHNGGTTFSSLEDGIYRNLFDLADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAVKHMPFGWQKSLMDEIDNYRPVFTFGEWFLSENEVDANNHYFANESGMSLLDFRFGQKLRQVLRNNSDNWYGFNQMIQDTASAYDEVLDQVTFIDNHDMDRFMIDGGDPRKVDMALAVLLTSRGVPNIYYGTEQYMTGNGDPNNRKMMSSFN
>d1pama4 3.1.1.1.4 (1-383) Cyclodextrin glycosyltransferase [alkalophilic Bacillus sp. 1011]
APDTSVSNKQNFSTDVIYQIFTDRFSDGNPANNPTGAAFDGSCTNLRLYCGGDWQGIINKINDGYLTGMGITAIWISQPVENIYSVINYSGVNNTAYHGYWARDFKKTNPAYGTMQDFKNLIDTAHAHNIKVIIDFAPNHTSPASSDDPSFAENGRLYDNGNLLGGYTNDTQNLFHHYGGTDFSTIENGIYKNLYDLADLNHNNSSVDVYLKDAIKMWLDLGVDGIRVDAVKHMPFGWQKSFMATINNYKPVFTFGEWFLGVNEISPEYHQFANESGMSLLDFRFAQKARQVFRDNTDNMYGLKAMLEGSEVDYAQVNDQVTFIDNHDMERFHTSNGDRRKLEQALAFTLTSRGVPAIYYGSEQYMSGGNDPDNRARLPSFST
>d1ciu_4 3.1.1.1.5 (1-382) Cyclodextrin glycosyltransferase [Thermoanaerobacterium thermosulfurigenes EM1]
ASDTAVSNVVNYSTDVIYQIVTDRFVDGNTSNNPTGDLYDPTHTSLKKYFGGDWQGIINKINDGYLTGMGVTAIWISQPVENIYAVLPDSTFGGSTSYHGYWARDFKRTNPYFGSFTDFQNLINTAHAHNIKVIIDFAPNHTSPASETDPTYAENGRLYDNGTLLGGYTNDTNGYFHHYGGTDFSSYEDGIYRNLFDLADLNQQNSTIDSYLKSAIKVWLDMGIDGIRLDAVKHMPFGWQKNFMDSILSYRPVFTFGEWFLGTNEIDVNNTYFANESGMSLLDFRFSQKVRQVFRDNTDTMYGLDSMIQSTASDYNFINDMVTFIDNHDMDRFYNGGSTRPVEQALAFTLTSRGVPAIYYGTEQYMTGNGDPYNRAMMTSFN
>d1ppi_2 3.1.1.1.6 (1-403) Mammalian alpha-amylase [porcine (Sus scrofa)]
QYAPQTQSGRTSIVHLFEWRWVDIALECERYLGPKGFGGVQVSPPNENVVVTNPSRPWWERYQPVSYKLCTRSGNENEFRDMVTRCNNVGVRIYVDAVINHMCGSGAAAGTGTTCGSYCNPGSREFPAVPYSAWDFNDGKCKTASGGIESYNDPYQVRDCQLVGLLDLALEKDYVRSMIADYLNKLIDIGVAGFRIDASKHMWPGDIKAVLDKLHNLNTNWFPAGSRPFIFQEVIDLGGEAIKSSEYFGNGRVTEFKYGAKLGTVVRKWSGEKMSYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGSSILTFWDARLYKVAVGFMLAHPYGFTRVMSSYRWARNFVNGEDVNDWIGPPNNNGVIKEVTINADTTCGNDWVCEHRWREIRNMVWFRNVVDG
>d1smd_2 3.1.1.1.7 (1-402) Mammalian alpha-amylase [human (Homo sapiens)]
YSSNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENVAIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGNAVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLSGLLDLALGKDYVRSKIAEYMNHLIDIGVAGFRIDASKHMWPGDIKAILDKLHNLNSNWFPEGSKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWPRYFENGKDVNDWVGPPNDNGVTKEVTINPDTTCGNDWVCEHRWRQIRNMVNFRNVVDG
>d2aaa_2 3.1.1.1.8 (1-353) Fungal alpha-amylases [Aspergillus niger, acid amylase]
LSAASWRTQSIYFLLTDRFGRTDNSTTATCNTGNEIYCGGSWQGIIDHLDYIEGMGFTAIWISPITEQLPQDTADGEAYHGYWQQKIYDVNSNFGTADNLKSLSDALHARGMYLMVDVVPDHMGYAGNGNDVDYSVFDPFDSSSYFHPYCLITDWDNLTMVEDCWEGDTIVSLPDLDTTETAVRTIWYDWVADLVSNYSVDGLRIDSVLEVQPDFFPGYNKASGVYCVGEIDNGNPASDCPYQKVLDGVLNYPIYWQLLYAFESSSGSISNLYNMIKSVASDCSDPTLLGNFIENHDNPRFAKYTSDYSQAKNVLSYIFLSDGIPIVYAGEEQHYAGGKVPYNREATWLSGYD
>d6taa_2 3.1.1.1.9 (1-353) Fungal alpha-amylases [Aspergillus oryzae, Taka-amylase]
ATPADWRSQSIYFLLTDRFARTDGSTTATCNTADQKYCGGTWQGIIDKLDYIQGMGFTAIWITPVTAQLPQTTAYGDAYHGYWQQDIYSLNENYGTADDLKALSSALHERGMYLMVDVVANHMGYDGAGSSVDYSVFKPFSSQDYFHPFCFIQNYEDQTQVEDCWLGDNTVSLPDLDTTKDVVKNEWYDWVGSLVSNYSIDGLRIDTVKHVQKDFWPGYNKAAGVYCIGEVLDGDPAYTCPYQNVMDGVLNYPIYYPLLNAFKSTSGSMDDLYNMINTVKSDCPDSTLLGTFVENHDNPRFASYTNDIALAKNVAAFIILNDGIPIIYAGQEQHYAGGNDPANREATWLSGYP
>d1byb__ 3.1.1.2.1 beta-Amylase [soybean (Glycine max)]
SNMLLNYVPVYVMLPLGVVNVDNVFEDPDGLKEQLLQLRAAGVDGVMVDVWWGIIELKGPKQYDWRAYRSLFQLVQECGLTLQAIMSFHQCGGNVGDIVNIPIPQWVLDIGESNHDIFYTNRSGTRNKEYLTVGVDNEPIFHGRTAIEIYSDYMKSFRENMSDFLESGLIIDIEVGLGPAGELRYPSYPQSQGWEFPRIGEFQCYDKYLKADFKAAVARAGHPEWELPDDAGKYNDVPESTGFFKSNGTYVTEKGKFFLTWYSNKLLNHGDQILDEANKAFLGCKVKLAIKVSGIHWWYKVENHAAELTAGYYNLNDRDGYRPIARMLSRHHAILNFTCLEMRDSEQPSDAKSGPQELVQQVLSGGWREDIRVAGENALPRYDATAYNQIILNAKPQGVNNNGPPKLSMFGVTYLRLSDDLLQKSNFNIFKKFVLKMHADQDYCANPQKYNHAITPLKPSAPKIPIEVLLEATKPTLPFPWLPETDMKVD
>d1xyza_ 3.1.1.3.1 Xylanase XynZ (family F) [Clostridium thermocellum]
NALRDYAEARGIKIGTCVNYPFYNNSDPTYNSILQREFSMVVCENEMKFDALQPRQNVFDFSKGDQLLAFAERNGMQMRGHTLIWHNQNPSWLTNGNWNRDSLLAVMKNHITTVMTHYKGKIVEWDVANECMDDSGNGLRSSIWRNVIGQDYLDYAFRYAREADPDALLFYNDYNIEDLGPKSNAVFNMIKSMKERGVPIDGVGFQCHFINGMSPEYLASIDQNIKRYAEIGVIVSFTEIDIRIPQSENPATAFQVQANNYKELMKICLANPNCNTFVMWGFTDKYTWIPGTFPGYGNPLIYDSNYNPKPAYNAIKEALM
>d1xas__ 3.1.1.3.10 Xylanase A, catalytic core [Streptomyces lividans]
LGAAAAQSGRYFGTAIASGRLSDSTYTSIAGREFNMVTAENEMKIDATEPQRGQFNFSSADRVYNWAVQNGKQVRGHTLAWHSQQPGWMQSLSGRPLRQAMIDHINGVMAHYKGKIVQWDVVNEAFADGSSGARRDSNLQRSGNDWIEVAFRTARAADPSAKLCYNDYNVENWTWAKTQAMYNMVRDFKQRGVPIDCVGFQSHFNSGSPYNSNFRTTLQNFAALGVDVAITELDIQGAPASTYANVTNDCLAVSRCLGITVWGVRDSDSWRSEQTPLLFNNDGSKKAAYTAVLDA
>d1clxa_ 3.1.1.3.11 Xylanase A, catalytic core [Pseudomonas fluorescens]
GLASLADFPIGVAVAASGGNADIFTSSARQNIVRAEFNQITAENIMKMSYMYSGSNFSFTNSDRLVSWAAQNGQTVHGHALVWHPSYQLPNWASDSNANFRQDFARHIDTVAAHFAGQVKSWDVVNEALFDSADDPDGRGSANGYRQSVFYRQFGGPEYIDEAFRRARAADPTAELYYNDFNTEENGAKTTALVNLVQRLLNNGVPIDGVGFQMHVMNDYPSIANIRQAMQKIVALSPTLKIKITELDVRLNNPYDGNSSNDYTNRNDCAVSCAGLDRQKARYKEIVQAYLEVVPPGRRGGITVWGIADPDSWLYTHQNLPDWPLLFNDNLQPKPAYQGVVEALS
>d1edg__ 3.1.1.3.2 Endoglucanase CelA [Clostridium cellulolyticum]
MYDASLIPNLQIPQKNIPNNDGMNFVKGLRLGWNLGNTFDAFNGTNITNELDYETSWSGIKTTKQMIDAIKQKGFNTVRIPVSWHPHVSGSDYKISDVWMNRVQEVVNYCIDNKMYVILNTHHDVDKVKGYFPSSQYMASSKKYITSVWAQIAARFANYDEHLIFEGMNEPRLVGHANEWWPELTNSDVVDSINCINQLNQDFVNTVRATGGKNASRYLMCPGYVASPDGATNDYFRMPNDISGNNNKIIVSVHAYCPWNFAGLAMADGGTNAWNINDSKDQSEVTWFMDNIYNKYTSRGIPVIIGECGAVDKNNLKTRVEYMSYYVAQAKARGILCILWDNNNFSGTGELFGFFDRRSCQFKFPEIIDGMVKYAFGLIN
>d2exo__ 3.1.1.3.3 beta-1,4-glycanase Cex, catalytic domain [Cellulomonas fimi ATCC 484]
ATTLKEAADGAGRDFGFALDPNRLSEAQYKAIADSEFNLVVAENAMKWDATEPSQNSFSFGAGDRVASYAADTGKELYGHTLVWHSQLPDWAKNLNGSAFESAMVNHVTKVADHFEGKVASWDVVNEAFADGGGRRQDSAFQQKLGNGYIETAFRAARAADPTAKLCINDYNVEGINAKSNSLYDLVKDFKARGVPLDCVGFQSHLIVGQVPGDFRQNLQRFADLGVDVRITELDIRMRTPSDATKLATQAADYKKVVQACMQVTRCQGVTVWGITDKYSWVPDVFPGEGAALVWDASYAKKPAYAAVMEAF
>d1cec__ 3.1.1.3.4 Endoglucanase CelC [Clostridium thermocellum]
VSFKAGINLGGWISQYQVFSKEHFDTFITEKDIETIAEAGFDHVRLPFDYPIIESDDNVGEYKEDGLSYIDRCLEWCKKYNLGLVLDMHHAPGSTLFEDPNQQKRFVDIWRFLAKRYINEREHIAFELLNEVVEPDSTRWNKLMLECIKAIREIDSTMWLYIGGNNYNSPDELKNLADIDDDYIVYNFHFYNPFFFTHQKAHWSESAMAYNRTVKYPGQYEGIEEFVKNNPKYSFMMELNNLKLNKELLRKDLKPAIEFREKKKCKLYCGEFGVIAIADLESRIKWHEDYISLLEEYDIGGAVWNYKKMDFEIYNEDRKPVSQELVNILAR
>d1ecea_ 3.1.1.3.5 Endocellulase E1 [Acidothermus cellulolyticus]
AGGGYWHTSGREILDANNVPVRIAGINWFGFETCNYVVHGLWSRDYRSMLDQIKSLGYNTIRLPYSDDILKPGTMPNSINFYQMNQDLQGLTSLQVMDKIVAYAGQIGLRIILDRHRPDCSGQSALWYTSSVSEATWISDLQALAQRYKGNPTVVGFDLHNEPHDPACWGCGDPSIDWRLAAERAGNAVLSVNPNLLIFVEGVQSYNGDSYWWGGNLQGAGQYPVVLNVPNRLVYSAHDYATSVYPQTWFSDPTFPNNMPGIWNKNWGYLFNQNIAPVWLGEFGTTLQSTTDQTWLKTLVQYLRPTAQYGADSFQWTFWSWNPDSGDTGGILKDDWQTVDTVKDGYLAPIKSSIFDPV
>d1ghsa_ 3.1.1.3.6 plant beta-glucanases [barley (Hordeum vulgare) 1,3-beta-glucanase]
IGVCYGVIGNNLPSRSDVVQLYRSKGINGMRIYFADGQALSALRNSGIGLILDIGNDQLANIAASTSNAASWVQNNVRPYYPAVNIKYIAAGNEVQGGATQSILPAMRNLNAALSAAGLGAIKVSTSIRFDEVANSFPPSAGVFKNAYMTDVARLLASTGAPLLANVYPYFAYRDNPGSISLNYATFQPGTTVRDQNNGLTYTSLFDAMVDAVYAALEKAGAPAVKVVVSESGWPSAGGFAASAGNARTYNQGLINHVGGGTPKKREALETYIFAMFNENQKTGDATERSFGLFNPDKSPAYNIQF
>d1ghr__ 3.1.1.3.7 plant beta-glucanases [barley (Hordeum vulgare) 1,3-1,4-beta-glucanase]
IGVCYGMSANNLPAASTVVSMFKSNGIKSMRLYAPNQAALQAVGGTGINVVVGAPNDVLSNLAASPAAAASWVKSNIQAYPKVSFRYVCVGNEVAGGATRNLVPAMKNVHGALVAAGLGHIKVTTSVSQAILGVFSPPSAGSFTGEAAAFMGPVVQFLARTNAPLMANIYPYLAWAYNPSAMDMGYALFNASGTVVRDGAYGYQNLFDTTVDAFYTAMGKHGGSSVKLVVSESGWPSGGGTAATPANARFYNQHLINHVGRGTPRHPGAIETYIFAMFNENQKDSGVEQNWGLFYPNMQHVYPINF
>d1bgla5 3.1.1.3.8 (332-623) beta-Galactosidase, domain 3 [Escherichia coli]
EVRIENGLLLLNGKPLLIRGVNRHEHHPLHGQVMDEQTMVQDILLMKQNNFNAVRCSHYPNHPLWYTLCDRYGLYVVDEANIETHGMVPMNRLTDDPRWLPAMSERVTRMVQRDRNHPSVIIWSLGNESGHGANHDALYRWIKSVDPSRPVQYEGGGADTTATDIICPMYARVDEDQPFPAVPKWSIKKWLSLPGETRPLILCEYAHAMGNSLGGFAKYWQAFRQYPRLQGGFVWDWVDQSLIKYDENGNPWSAYGGDFGDTPNDRQFCMNGLVFADRTPHPALTEAKHQQQ
>d1bhga3 3.1.1.3.9 (308-611) beta-Glucuronidase, domain 3 [human (Homo sapiens)]
VAVTKSQFLINGKPFYFHGVNKHEDADIRGKGFDWPLLVKDFNLLRWLGANAFRTSHYPYAEEVMQMCDRYGIVVIDECPGVGLALPQFFNNVSLHHHMQVMEEVVRRDKNHPAVVMWSVANEPASHLESAGYYLKMVIAHTKSLDPSRPVTFVSNSNYAADKGAPYVDVICLNSYYSWYHDYGHLELIQLQLATQFENWYKKYQKPIIQSEYGAETIAGFHQDPPLMFTEEYQKSLLEQYHLGLDQKRRKYVVGELIWNFADFMTEQSPTRVLGNKKGIFTRQRQPKSAAFLLRERYWKIANE
>d2myr__ 3.1.1.4.1 Myrosinase [white mustard (Sinapis alba)]
EITCQENNPFTCGNTDGLNSSSFEADFIFGVASSAYQIEGTIGRGLNIWDGFTHRYPDKSGPDHGNGDTTCDSFSYWQKDIDVLDELNATGYRFSIAWSRIIPRGKRSRGVNQKGIDYYHGLIDGLIKKGITPFVTLFHWDLPQTLQDEYEGFLDPQIIDDFKDYADLCFEEFGDSVKYWLTINQLYSVPTRGYGSALDAPGRCSPTVDPSCYAGNSSTEPYIVAHHQLLAHAKVVDLYRKNYTHQGGKIGPTMITRWFLPYNDTDRHSIAATERMKQFFLGWFMGPLTNGTYPQIMIDTVGARLPTFSPEETNLVKGSYDFLGLNYYFTQYAQPSPNPVNATNHTAMMDAGAKLTYINASGHYIGPLFESDGGDGSSNIYYYPKGIYSVMDYFKNKYYNPLIYVTENGISTPGSENRKESMLDYTRIDYLCSHLCFLNKVIKEKDVNVKGYLAWALGDNYEFNNGFTVRFGLSYINWNNVTDRDLKKSGQWYQKFISP
>d1cbg__ 3.1.1.4.2 Cyanogenic beta glucosidase [Creeping white clover (Trfolium repens)]
FKPLPISFDDFSDLNRSCFAPGFVFGTASSAFQYEGAAFEDGKGPSIWDTFTHKYPEKIKDRTNGDVAIDEYHRYKEDIGIMKDMNLDAYRFSISWPRVLPKGKLSGGVNREGINYYNNLINEVLANGMQPYVTLFHWDVPQALEDEYRGFLGRNIVDDFRDYAELCFKEFGDRVKHWITLNEPWGVSMNAYAYGTFAPGRCSDWLKLNCTGGDSGREPYLAAHYQLLAHAAAARLYKTKYQASQNGIIGITLVSHWFEPASKEKADVDAAKRGLDFMLGWFMHPLTKGRYPESMRYLVRKRLPKFSTEESKELTGSFDFLGLNYYSSYYAAKAPRIPNARPAIQTDSLINATFEHNGKPLGPMAASSWLCIYPQGIRKLLLYVKNHYNNPVIYITENGRNEFNDPTLSLQESLLDTPRIDYYYRHLYYVLTAIGDGVNVKGYFAWSLFDNMEWDSGYTVRFGLVFVDFKNNLKRHPKLSAHWFKSFLKK
>d1pbga_ 3.1.1.4.3 6-phospho-beta-D-galactosidase, PGAL [Lactococcus lactis]
MTKTLPKDFIFGGATAAYQAEGATHTDGKGPVAWDKYLEDNYWYTAEPASDFYHKYPVDLELAEEYGVNGIRISIAWSRIFPTGYGEVNEKGVEFYHKLFAECHKRHVEPFVTLHHFDTPEALHSNGDFLNRENIEHFIDYAAFCFEEFPEVNYWTTFNEIGPIGDGQYLVGKFPPGIKYDLAKVFQSHHNMMVSHARAVKLYKDKGYKGEIGVVHALPTKYPYDPENPADVRAAELEDIIHNKFILDATYLGHYSDKTMEGVNHILAENGGELDLRDEDFQALDAAKDLNDFLGINYYMSDWMQAFDGETEIIKYQIKGVGRRVAPDYVPRWIIYPEGLYDQIMRVKNDYPNYKKIYITENGLGYKDEFVDNTVYDDGRIDYVKQHLEVLSDAIADGANVKGYFIWSLMDVFSWSNGYEKRYGLFYVDFDTQERYPKKSAHWYKKLAETQVIE
>d1gowa_ 3.1.1.4.4 beta-Glycosidase [Sulfolobus solfataricus]
MYSFPNSFRFGWSQAGFQSEMGTPGSEDPNTDWYKWVHDPENMAAGLVSGDLPENGPGYWGNYKTFHDNAQKMGLKIARLNSEWSRQFPNPLPRPQNFDESKQDVTEVEINENELKRLDEYANKDALNHYREIFKDLKSRGLYFIQNMYHWPLPLWLHDPIRVRRGDFTGPSGWLSTRTVYEFARFSAYTAWKFDDLVDEYSTMNEPNVVGGLGYVGVKSGFPPGYLSFELSRRAMYNIIQAHARAYDGIKSVSKKPVGIIYANSSFQPLTDKDMEAVEMAENDNRWWFFDAIIRGEITRGNEKIVRDDLKGRLDWIGVNYYTRTVVKRTEKGYVSLGGYGHGCERNSVSLAGLPTSDFGWEFFPEGLYDVLTKYWNRYHLYMYVTENGIADDADYQRPYYLVSHVYQVHRAINSGADVRGYLHWSLADNYEWASGFSMRFGLLKVDYNTKRLYWRPSALVYREIATNGAITDEIEHLNSVPPVKPLRH
>d1hvq__ 3.1.1.5.1 Hevamine A (chitinase/lysozyme) [Para rubber tree Hevea brasiliensis]
GGIAIYWGQNGNEGTLTQTCSTRKYSYVNIAFLNKFGNGQTPQINLAGHCNPAAGGCTIVSNGIRSCQIQGIKVMLSLGGGIGSYTLASQADAKNVADYLWNNFLGGKSSSRPLGDAVLDGIDFDIEHGSTLYWDDLARYLSAYSKQGKKVYLTAAPQCPFPDRYLGTALNTGLFDYVWVQFYNNPPCQYSSGNINNIINSWNRWTTSINAGKIFLGLPAAPEAAGSGYVPPDVLISRILPEIKKSPKYGGVMLWSKFYDDKNGYSSSILDSV
>d1nar__ 3.1.1.5.2 Seed storage protein [Vicia narbonensis l., Narbonin]
PKPIFREYIGVKPNSTTLHDFPTEIINTETLEFHYILGFAIESYYESGKGTGTFEESWDVELFGPEKVKNLKRRHPEVKVVISIGGRGVNTPFDPAEENVWVSNAKESLKLIIQKYSDDSGNLIDGIDIHYEHIRSDEPFATLMGQLITELKKDDDLNINVVSIAPSENNSSHYQKLYNAKKDYINWVDYQFSNQQKPVSTDDAFVEIFKSLEKDYHPHKVLPGFSTDPLDTKHNKITRDIFIGGCTRLVQTFSLPGVFFWNANDSVIPKRDGDKPFIVELTLQQLLAA
>d1cnv__ 3.1.1.5.3 Seed storage protein [jack bean (Canavalia ensiformis), Concanavalin B]
DISSTEIAVYWGQREDGLLRDTCKTNNYKIVFISFLDKFGCEIRKPELELEGVCGPSVGNPCSFLESQIKECQRMGVKVFLALGGPKGTYSACSADYAKDLAEYLHTYFLSERREGPLGKVALDGIHFDIQKPVDELNWDNLLEELYQIKDVYQSTFLLSAAPGCLSPDEYLDNAIQTRHFDYIFVRFYNDRSCQYSTGNIQRIRNAWLSWTKSVYPRDKNLFLELPASQATAPGGGYIPPSALIGQVLPYLPDLQTRYAGIALWNRQADKETGYSTNIIRYL
>d2ebn__ 3.1.1.5.4 Endo-beta-N-acetylglucosaminidase [Flavobacterium meningosepticum, endoglycosidase F1]
TTKANIKLFSFTEVNDTNPLNNLNFTLKNSGKPLVDMVVLFSANINYDAANDKVFVSNNPNVQHLLTNRAKYLKPLQDKGIKVILSILGNHDRSGIANLSTARAKAFAQELKNTCDLYNLDGVFFDDEYSAYQTPPPSGFVTPSNNAAARLAYETKQAMPNKLVTVYVYSRTSSFPTAVDGVNAGSYVDYAIHDYGGSYDLATNYPGLAKSGMVMSSQEFNQGRYATAQALRNIVTKGYGGHMIFAMDPNRSNFTSGQLPALKLIAKELYGDELVYSNTPYSKDW
>d1edt__ 3.1.1.5.5 Endo-beta-N-acetylglucosaminidase [Streptomyces plicatus, endoglycosidase H]
KQGPTSVAYVEVNNNSMLNVGKYTLADGGGNAFDVAVIFAANINYDTGTKTAYLHFNENVQRVLDNAVTQIRPLQQQGIKVLLSVLGNHQGAGFANFPSQQAASAFAKQLSDAVAKYGLDGVDFDDEYAEYGNNGTAQPNDSSFVHLVTALRANMPDKIISLYNIGPAASRLSYGGVDVSDKFDYAWNPYYGTWQVPGIALPKAQLSPAAVEIGRTSRSTVADLARRTVDEGYGVYLTYNLDGGDRTADVSAFTRELYGSEAVRT
>d1ctn_2 3.1.1.5.6 (110-418,493-538) Chitinase A, central domain [Serratia marcescens]
TDGSHLAPLKEPLLEKNKPYKQNSGKVVGSYFVEWGVYGRNFTVDKIPAQNLTHLLYGFIPICGGNGINDSLKEIEGSFQALQRSCQGREDFKISIHDPFAALQKAQKGVTAWDDPYKGNFGQLMALKQAHPDLKILPSIGGWTLSDPFFFMGDKVKRDRFVGSVKEFLQTWKFFDGVDIDWEFPGGKGANPNLGSPQDGETYVLLMKELRAMLDQLSTETGRKYELTSAISAGKDKIDKVAYNVAQNSMDHIFLMSYDFYGAFDLKNLGHQTALNAPAWKPDTAYTTVNGVNALLAQGVKPGKIVVG
>d1qba_3 3.1.1.6.1 (311-753) Bacterial chitobiase, catalytic domain [(Serratia marcescens)]
FPYRGIFLDVARNFHKKDAVLRLLDQMAAYKLNKFHFHLSDDEGWRIEIPGLPELTEVGGQRCHDLSETTCLLPQYGQGPDVYGGFFSRQDYIDIIKYAQARQIEVIPEIDMPAHARAAVVSMEARYKKLHAAGKEQEANEFRLVDPTDTSNTTSVQFFNRQSYLNPCLDSSQRFVDKVIGEIAQMHKEAGQPIKTWHFGGDEAKNIRLGAGYTDKAKPEPGKGIIDQGNEDKPWAKSQVCQTMIKEGKVADMEHLPSYFGQEVSKLVKAHGIDRMQAWQDGLKDAESSKAFATSRVGVNFWDTLYWGGFDSVNDWANKGYEVVVSNPDYVYMDFPYEVNPDERGYYWGTRFSDERKVFSFAPDNMPQNAETSVDRDGNHFNAKSDKPWPGAYGLSAQLWSETQRTDPQMEYMIFPRALSVAERSWHRAGWEQDYRAGREYKG
>d3rubl1 3.1.10.1.1 (122-441) Ribulose 1,5-bisphosphate carboxylase-oxygenase [tobacco (Nicotiana tabacum) variant turkish samsun]
FQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDFVEQDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGMTLGHPWGNAPGAVANRVALEACVKARNEGRDLAQEGNEIIREACKWSPELAAACEVWKEIVF
>d1ausl1 3.1.10.1.2 (129-439) Ribulose 1,5-bisphosphate carboxylase-oxygenase [spinach (Spinacia oleracea)]
FQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTCEDMMKRAVFARELGVPIVMHDYLTGGFTANTTLSHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHIHSGTVVERDITLGFVDLLRDDYTEKDRSRGIYFTQSWVSTPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNTIIREATKWSPELAAACEVWK
>d1rbla1 3.1.10.1.3 (140-467) Ribulose 1,5-bisphosphate carboxylase-oxygenase [Synechococcus, strain pcc 6301]
FQGPPHGIQVERDLLNKYGRPMLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENINSQPFQRWRDRFLFVADAIHKSQAETGEIKGHYLNVTAPTCEEMMKRAEFAKELGMPIIMHDFLTAGFTANTTLAKWCRDNGVLLHIHRAMHAVIDRQRNHGIHFRVLAKCLRLSGGDHLHSGTVVGKLEGDKASTLGFVDLMREDHIEADRSRGVFFTQDWASMPGVLPVASGGIHVWHMPALVEIFGDDSVLQFGGGTLGHPWGNAPGATANRVALEACVQARNEGRDLYREGGDILREAGKWSPELAAALDLWKEIKFEFETMDKL
>d5ruba1 3.1.10.1.4 (126-436) Ribulose 1,5-bisphosphate carboxylase-oxygenase [Rhodospirillum rubrum]
GPSVNISALWKVLGRPEVDGGLVVGTIIKPKLGLRPKPFAEACHAFWLGGDFIKNDEPQGNQPFAPLRDTIALVADAMRRAQDETGEAKLFSANITADDPFEIIARGEYVLETFGENASHVALLVDGYVAGAAAITTARRRFPDNFLHYHRAGHGAVTSPQSKRGYTAFVHCKMARLQGASGIHTGTSSDRAIAYMLTQDEAQGPFYRQSWGGMKACTPIISGGMNALRMPGFFENLGNANVILTAGGGAFGHIDGPVAGARSLRQAWQAWRDGVPVLDYAREHKELARAFESFPGDADQIYPGWRKALGV
>d1tph1_ 3.1.11.1.1 Triosephosphate isomerase [chicken (Gallus gallus)]
RKFFVGGNWKMNGDKKSLGELIHTLNGAKLSADTEVVCGAPSIYLDFARQKLDAKIGVAAQNCYKVPKGAFTGEISPAMIKDIGAAWVILGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKAIADNVKDWSKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKTHVSDAVAQSTRIIYGGSVTGGNCKELASQHDVDGFLVGGASLKPEFVDIINAKH
>d1htia_ 3.1.11.1.2 Triosephosphate isomerase [Human (Homo sapiens)]
APSRKFFVGGNWKMNGRKQSLGELIGTLNAAKVPADTEVVCAPPTAYIDFARQKLDPKIAVAAQNCYKVTNGAFTGEISPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPEFVDIINAKQ
>d7tima_ 3.1.11.1.3 Triosephosphate isomerase [yeast (Saccharomyces cerevisiae)]
ARTFFVGGNFKLNGSKQSIKEIVERLNTASIPENVEVVICPPATYLDYSVSLVKKPQVTVGAQNAYLKASGAFTGENSVDQIKDVGAKWVILGHSERRSYFHEDDKFIADKTKFALGQGVGVILCIGETLEEKKAGKTLDVVERQLNAVLEEVKDWTNVVVAYEPVWAIGTGLAATPEDAQDIHASIRKFLASKLGDKAASELRILYGGSANGSNAVTFKDKADVDGFLVGGASLKPEFVDIINSRN
>d1tpfa_ 3.1.11.1.4 Triosephosphate isomerase [Trypanosoma brucei brucei]
MSKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCVVASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSLPILKDFGVNWIVLGHSERRAYYGETNEIVADKVAAAVASGFMVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWAKVVIAYEPVWAIGTGKVATPQQAQEAHALIRSWVSSKIGADVAGELRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKPEFVDIIKATQ
>d1tmha_ 3.1.11.1.6 Triosephosphate isomerase [hybrid between Escherichia coli and chicken TIM]
MRHPLVMGNWKLNGSRHMVHELVSNLRKELAGVAGCAVAIAPPEMYIDMAKREAEGSHIMLGAQNVDLNLSGAFTGETSAAMLKDIGAQYIIIGHSERRTYHKESDELIAKKFAVLKEQGLTPVLCIGETEAENEAGKTEEVCARQIDAVLKTQGAAAFEGAVIAYEPVWAIGTGKSATPAQAQAVHKFIRDHIAKVDANIAEQVIIQYGGSVNASNAAELFAQHDVDGFLVGGASLKPEFVDIINAAEAAKQA
>d1btma_ 3.1.11.1.7 Triosephosphate isomerase [Bacillus stearothermophilus]
RKPIIAGNWKMHKTLAEAVQFVEDVKGHVPPADEVISVVCAPFLFLDRLVQAADGTDLKIGAQTMHFADQGAYTGEVSPVMLKDLGVTYVILGHSERRQMFAETDETVNKKVLAAFTRGLIPIICCGESLEEREAGQTNAVVASQVEKALAGLTPEQVKQAVIAYEPIWAIGTGKSSTPEDANSVCGHIRSVVSRLFGPEAAEAIRIQYGGSVKPDNIRDFLAQQQIDGPLVGGASLEPASFLQLVEAGRH
>d1ydva_ 3.1.11.1.8 Triosephosphate isomerase [Plasmodium falciparum]
RKYFVAANWKCNGTLESIKSLTNSFNNLDFDPSKLDVVVFPVSVHYDHTRKLLQSKFSTGIQNVSKFGNGSYTGEVSAEIAKDLNIEYVIIGHFERRKYFHETDEDVREKLQASLKNNLKAVVCFGESLEQREQNKTIEVITKQVKAFVDLIDNFDNVILVYEPLWAIGTGKTATPEQAQLVHKEIRKIVKDTCGEKQANQIRILYGGSVNTENCSSLIQQEDIDGFLVGNASLKESFVDIIKSAM
>d2gyia_ 3.1.12.1.3 D-xylose isomerase [streptomyces olivochromogenes]
YQPTPEDRFTFGLWTVGWQGRDPFGDATRPALDPVETVQRLAELGAHGVTFHDDDLIPFGSSDTERESHIKRFRQALDATGMTVPMATTNLFTHPVFKDGGFTANDRDVRRYALRKTIRNIDLAVELGAKTYVAWGGREGAESGAAKDVRVALDRMKEAFDLLGEYVTSQGYDTRFAIEPKPNEPRGDILLPTVGHALAFIERLERPELYGVNPEVGHEQMAGLNFPHGIAQALWAGKLFHIDLNGQSGIKYDQDLRFGAGDLRAAFWLVDLLESAGYEGPRHFDFKPPRTEDIDGVWASAAGCMRNYLILKERAAAFRADPEVQEALRASRLDELAQPTAADGVQELLADRTAFEDFDVDAAAARGMAFERLDQLAMDHLLGAR
>d2xis__ 3.1.12.1.4 D-xylose isomerase [streptomyces rubiginosus]
YQPTPEDRFTFGLWTVGWQGRDPFGDATRRALDPVESVRRLAELGAHGVTFHDDDLIPFGSSDSEREEHVKRFRQALDDTGMKVPMATTNLFTHPVFKDGGFTANDRDVRRYALRKTIRNIDLAVELGAETYVAWGGREGAESGGAKDVRDALDRMKEAFDLLGEYVTSQGYDIRFAIEPKPNEPRGDILLPTVGHALAFIERLERPELYGVNPEVGHEQMAGLNFPHGIAQALWAGKLFHIDLNGQNGIKYDQDLRFGAGDLRAAFWLVDLLESAGYSGPRHFDFKPPRTEDFDGVWASAAGCMRNYLILKERAAAFRADPEVQEALRASRLDELARPTAADGLQALLDDRSAFEEFDVDAAAARGMAFERLDQLAMDHLLGAR
>d1xlaa_ 3.1.12.1.5 D-xylose isomerase [Arthrobacter strain b3728]
VQPTPADHFTFGLWTVGWTGADPFGVATRKNLDPVEAVHKLAELGAYGITFHDNDLIPFDATEAEREKILGDFNQALKDTGLKVPMVTTNLFSHPVFKDGGFTSNDRSIRRFALAKVLHNIDLAAEMGAETFVMWGGREGSEYDGSKDLAAALDRMREGVDTAAGYIKDKGYNLRIALEPKPNEPRGDIFLPTVGHGLAFIEQLEHGDIVGLNPETGHEQMAGLNFTHGIAQALWAEKLFHIDLNGQRGIKYDQDLVFGHGDLTSAFFTVDLLENGFPNGGPKYTGPRHFDYKPSRTDGYDGVWDSAKANMSMYLLLKERALAFRADPEVQEAMKTSGVFELGETTLNAGESAADLMNDSASFAGFDAEAAAERNFAFIRLNQLAIEHLLGSR
>d1xima_ 3.1.12.1.6 D-xylose isomerase [Actinoplanes missouriensis]
VQATREDKFSFGLWTVGWQARDAFGDATRTALDPVEAVHKLAEIGAYGITFHDDDLVPFGSDAQTRDGIIAGFKKALDETGLIVPMVTTNLFTHPVFKDGGFTSNDRSVRRYAIRKVLRQMDLGAELGAKTLVLWGGREGAEYDSAKDVSAALDRYREALNLLAQYSEDRGYGLRFAIEPKPNEPRGDILLPTAGHAIAFVQELERPELFGINPETGHEQMSNLNFTQGIAQALWHKKLFHIDLNGQHGPKFDQDLVFGHGDLLNAFSLVDLLENGPDGAPAYDGPRHFDYKPSRTEDYDGVWESAKANIRMYLLLKERAKAFRADPEVQEALAASKVAELKTPTLNPGEGYAELLADRSAFEDYDADAVGAKGFGFVKLNQLAIEHLLGAR
>d1luca_ 3.1.13.1.1 Bacterial luciferase [Vibrio harveyi]
MKFGNFLLTYQPPELSQTEVMKRLVNLGKASEGCGFDTVWLLEHHFTEFGLLGNPYVAAAHLLGATETLNVGTAAIVLPTAHPVRQAEDVNLLDQMSKGRFRFGICRGLYDKDFRVFGTDMDNSRALMDCWYDLMKEGFNEGYIAADNEHIKFPKIQLNPSAYTQGGAPVYVVAESASTTEWAAERGLPMILSWIINTHEKKAQLDLYNEVATEHGYDVTKIDHCLSYITSVDHDSNRAKDICRNFLGHWYDSYVNATKIFRIDYSYEINPVGTPEECIAIIQQDIDATGIDNICCGFEANGSEEEIIASMKLFQSDVMPYLKEKQ
>d1lucb_ 3.1.13.1.1 Bacterial luciferase [Vibrio harveyi]
MKFGLFFLNFMNSKRSSDQVIEEMLDTAHYVDQLKFDTLAVYENHFSNNGVVGAPLTVAGFLLGMTKNAKVASLNHVITTHHPVRVAEEACLLDQMSEGRFAFGFSDCEKSADMRFFNRPTDSQFQLFSECHKIINDAFTTGYCHPNNDFYSFPKISVNPHAFTEGGPAQFVNATSKEVVEWAAKLGLPLVFRWDDSNAQRKEYAGLYHEVAQAHGVDVSQVRHKLTLLVNQNVDGEAARAEARVYLEEFVRESYSNTDFEQKMGELLSENAIGTYEESTQAARVAIECCGAADLLMSFESMEDKAQQRAVIDVVNANIV
>d1nfp__ 3.1.13.2.1 non-fluorescent flavoprotein (luxF, FP390) [Photobacterium leiognathi]
MTKWNYGVFFLNFYHVGQQEPSLTMSNALETLRIIDEDTSIYDVVAFSEHHIDKSYNDETKLAPFVSLGKQIHVLATSPETVVKAAKYGMPLLFKWDDSQQKRIELLNHYQAAAAKFNVDIANVRHRLMLFVNVNDNPTQAKAELSIYLEDYLSYTQAETSIDEIINSNAAGNFDTCLHHVAEMAQGLNNKVDFLFCFESMKDQENKKSLMINFDKRVINYRKEHNLN
>d1fvpa_ 3.1.13.2.2 non-fluorescent flavoprotein (luxF, FP390) [Photobacterium phosphoreum]
MNKWNYGVFFVNFYNKGQQEPSKTMNNALETLRIIDEDTSIYDVINIDDHYLVKKDSEDKKLAPFITLGEKLYVLATSENTVDIAAKYALPLVFKWDDINEERLKLLSFYNASASKYNKNIDLVRHQLMLHVNVNEAETVAKEELKLYIENYVACTQPSNFNGSIDSIIQSNVTGSYKDCLSYVANLAGKFDNTVDFLLCFESMQDQNKKKSVMIDLNNQVIKFRQDNNLI
>d1qapa1 3.1.14.1.1 (123-289) quinolinic acid phosphoribosyltransferase, C-terminal domain [Salmonella typhimurium]
VASEVRRYVGLLAGTQTQLLDTRKTLPGLRTALKYAVLCGGGANHRLGLTDAFLIKENHIIASGSVRQAVEKAFWLHPDVPVEVEVENLDELDDALKAGADIIMLDNFNTDQMREAVKRVNGQARLEVSGNVTAETLREFAETGVDFISVGALTKHVRALDLSMRFC
>d1djxa3 3.1.15.1.1 (100-363) Phospholipase C isozyme D1 (PLC-D1) [Rat (Rattus norvegicus)]
DQPLSHYLVSSSHNTYLLEDQLTGPSSTEAYIRALCKGCRCLELDCWDGPNQEPIIYHGYTFTSKILFCDVLRAIRDYAFKASPYPVILSLENHCSLEQQRVMARHLRAILGPILLDQPLDGVTTSLPSPEQLKGKILLKGKKLKLVPELSDMIIYCKSVHFGGFSSPGTSGQAFYEMASFSESRALRLLQESGNGFVRHNVSCLSRIYPAGWRTDSSNYSPVEMWNGGCQIVALNFQTPGPEMDVYLGCFQDNGGCGYVLKPA
>d1gym__ 3.1.15.2.1 Phosphatidylinositol-specific phospholipase C [Bacillus cereus]
ASSVNELENWSKWMQPIPDSIPLARISIPGTHDSGTFKLQNPIKQVWGMTQEYDFRYQMDHGARIFDIRGRLTDDNTIVLHHGPLYLYVTLHEFINEAKQFLKDNPSETIIMSLKKEYEDMKGAEDSFSSTFEKKYFVDPIFLKTEGNIKLGDARGKIVLLKRYSGSNEPGGYNNFYWPDNETFTTTVNQNANVTVQDKYKVSYDEKVKSIKDTMDETMNNSEDLNHLYINFTSLSSGGTAWNSPYYYASYINPEIANYIKQKNPARVGWVIQDYINEKWSPLLYQEVIRANKSLI
>d1reqa1 3.1.16.1.1 (1-559) Methylmalonyl-CoA mutase, alpha and beta subunits [Propionibacterium freudenreichii shermani]
STLPRFDSVDLGNAPVPADAARRFEELAAKAGTGEAWETAEQIPVGTLFNEDVYKDMDWLDTYAGIPPFVHGPYATMYAFRPWTIRQYAGFSTAKESNAFYRRNLAAGQKGLSVAFDLPTHRGYDSDNPRVAGDVGMAGVAIDSIYDMRELFAGIPLDQMSVSMTMNGAVLPILALYVVTAEEQGVKPEQLAGTIQNDILKEFMVRNTYIYPPQPSMRIISEIFAYTSANMPKWNSISISGYHMQEAGATADIEMAYTLADGVDYIRAGESVGLNVDQFAPRLSFFWGIGMNFFMEVAKLRAARMLWAKLVHQFGPKNPKSMSLRTHSQTSGWSLTAQDVYNNVVRTCIEAMAATQGHTQSLHTNSLDEAIALPTDFSARIARNTQLFLQQESGTTRVIDPWSGSAYVEELTWDLARKAWGHIQEVEKVGGMAKAIEKGIPKMRIEEAAARTQARIDSGRQPLIGVNKYRLEHEPPLDVLKVDNSTVLAEQKAKLVKLRAERDPEKVKAALDKITWAAGNPDDKDPDRNLLKLCIDAGRAMATVGEMSDALEKVFGRYT
>d1reqb1 3.1.16.1.1 (1-456) Methylmalonyl-CoA mutase, alpha and beta subunits [Propionibacterium freudenreichii shermani]
TLSLAGDFPKATEEQWEREVEKVLNRGRPPEKQLTFAECLKRLTVHTVDGIDIVPMYRPKDAPKKLGYPGVAPFTRGTTVRNGDMDAWDVRALHEDPDEKFTRKAILEGLERGVTSLLLRVDPDAIAPEHLDEVLSDVLLEMTKVEVFSRYDQGAAAEALVSVYERSDKPAKDLALNLGLDPIGFAALQGTEPDLTVLGDWVRRLAKFSPDSRAVTIDANIYHNAGAGDVAELAWALATGAEYVRALVEQGFTATEAFDTINFRVTATHDQFLTIARLRALREAWARIGEVFGVDEDKRGARQNAITSWRELTREDPYVNILRGSIATFSASVGGAESITTLPFTQALGLPEDDFPLRIARNTGIVLAEEVNIGRVNDPAGGSYYVESLTRSLADAAWKEFQEVEKLGGMSKAVMTEHVTKVLDACNAERAKRLANRKQPITAVSEFPMIGARSIE
>d1pud__ 3.1.17.1.1 tRNA-guanine transglycosylase [Zymomonas mobilis]
RPRFSFSIAAREGKARTGTIEMKRGVIRTPAFMPVGTAATVKALKPETVRATGADIILGNTYHLMLRPGAERIAKLGGLHSFMGWDRPILTDSGGYQVMSLSSLTKQSEEGVTFKSHLDGSRHMLSPERSIEIQHLLGSDIVMAFDECTPYPATPSRAASSMERSMRWAKRSRDAFDSRKEQAENAALFGIQQGSVFENLRQQSADALAEIGFDGYAVGGLAVGEGQDEMFRVLDFSVPMLPDDKPHYLMGVGKPDDIVGAVERGIDMFDCVLPTRSGRNGQAFTWDGPINIRNARFSEDLKPLDSECHCAVCQKWSRAYIHHLIRAGEILGAMLMTEHNIAFYQQLMQKIRDSISEGRFSQFAQDFRARYF
>d1sfta2 3.1.18.1.1 (1-243) Alanine racemase, N-terminal domain [Bacillus stearothermophilus]
NDFHRDTWAEVDLDAIYDNVENLRRLLPDDTHIMAVVKANAYGHGDVQVARTALEAGASRLAVAFLDEALALREKGIEAPILVLGASRPADAALAAQQRIALTVFRSDWLEEASALYSGPFPIHFHLKMDTGMGRLGVKDEEETKRIVALIERHPHFVLEGLYTHFATADEVNTDYFSYQYTRFLHMLEWLPSRPPLVHCANSAASLRFPDRTFNMVRFGIAMYGLAPSPGIKPLLPYPLKEA
>d1add__ 3.1.2.1.1 Adenosine deaminase [mouse (Mus musculus)]
TPAFNKPKVELHVHLDGAIKPETILYFGKKRGIALPADTVEELRNIIGMDKPLSLPGFLAKFDYYMPVIAGCREAIKRIAYEFVEMKAKEGVVYVEVRYSPHLLANSKVDPMPWNQTEGDVTPDDVVDLVNQGLQEGEQAFGIKVRSILCCMRHQPSWSLEVLELCKKYNQKTVVAMDLAGDETIEGSSLFPGHVEAYEGAVKNGIHRTVHAGEVGSPEVVREAVDILKTERVGHGYHTIEDEALYNRLLKENMHFEVCPWSSYLTGAWDPKTTHAVVRFKNDKANYSLNTDDPLIFKSTLDTDYQMTKKDMGFTEEEFKRLNINAAKSSFLPEEEKKELLERLYREYQ
>d2kauc2 3.1.2.2.1 (129-421,475-566) alpha-subunit of urease, catalytic domain [Klebsiella aerogenes]
GIDTHIHWICPQQAEEALVSGVTTMVGGGTGPAAGTHATTCTPGPWYISRMLQAADSLPVNIGLLGKGNVSQPDALREQVAAGVIGLKIHEDWGATPAAIDCALTVADEMDIQVALHSDTLNESGFVEDTLAAIGGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPTLPYTLNTIDEHLDMLMVCHHLDPDIAEDVAFAESRIRRETIAAEDVLHDLGAFSLTSSDSQAMGRVGEVILRTWQVAHRMKVQRGALAEETGDNDNFRVKRYIAKYTINPALTHGIAHEV
>d1pta__ 3.1.2.3.1 Phosphotriesterase [Pseudomonas diminuta]
RINTVRGPITISEAGFTLTHEHICGSSAGFLRAWPEFFGSRKALAEKAVRGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAADVHIVAATGLWFDPPLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQELVLKAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIGHSDDTDDLSYLTALAARGYLIGLDHIPHSAIALLGIRSWQTRALLIKALIDQGYMKQILVSNDWLFGFSSYVTNIMDVMDRVNPDGMAFIPLRVIPFLREKGVPQETLAGITVTNPARFLSPTL
>d1nal1_ 3.1.3.1.1 N-acetylneuraminate lyase [Escherichia coli]
NLRGVMAALLTPFDQQQALDKASLRRLVQFNIQQGIDGLYVGGSTGEAFVQSLSEREQVLEIVAEEGKGKIKLIAHVGCVTTAESQQLAASAKRYGFDAVSAVTPFYYPFSFEEHCDHYRAIIDSADGLPMVVYNIPALSGVKLTLDQINTLVTLPGVGALKQTSGDLYQMEQIRREHPDLVLYNGYDEIFASGLLAGADGGIGSTYNIMGWRYQGIVKALKEGDIQTAQKLQTECNKVIDLLIKTGVFRGLKTVLHYMDVVSVPLCRKPFGPVDEKYQPELKALAQQLMQ
>d1ald__ 3.1.3.1.2 Fructose-1,6-bisphosphate aldolase [human (Homo sapiens)]
PYQYPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKFSHEEIAMATVTALRRTVPPAVTGITFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALANSLACQGKYTPSGQAGAAASESLFVSNHAY
>d1fbaa_ 3.1.3.1.3 Fructose-1,6-bisphosphate aldolase [Drosophila melanogaster, strain sevelen (Wild type, pupea)]
TTYFNYPSKELQDELREIAQKIVAPGKGILAADESGPTMGKRLQDIGVENTEDNRRAYRQLLFSTDPKLAENISGVILFHETLYQKADDGTPFAEILKKKGIILGIKVDKGVVPLFGSEDEVTTQGLDDLAARCAQYKKDGCDFAKWRCVLKIGKNTPSYQSILENANVLARYASICQSQRIVPIVEPEVLPDGDHDLDRAQKVTETVLAAVYKALSDHHVYLEGTLLKPNMVTAGQSAKKNTPEEIALATVQALRRTVPAAVTGVTFLSGGQSEEEATVNLSAINNVPLIRPWALTFSYGRALQASVLRAWAGKKENIAAGQNELLKRAKANGDAAQGKYVAGSAGAGSGSLFVANHAY
>d1dhpa_ 3.1.3.1.4 Dihidrodipicolinate synthase [Escherichia coli]
MFTGSIVAIVTPMDEKGNVCRASLKKLIDYHVASGTSAIVSVGTTGESATLNHDEHADVVMMTLDLADGRIPVIAGTGANATAEAISLTQRFNDSGIVGCLTVTPYYNRPSQEGLYQHFKAIAEHTDLPQILYNVPSRTGCDLLPETVGRLAKVKNIIGIKEATGNLTRVNQIKELVSDDFVLLSGDDASALDFMQLGGHGVISVTANVAARDMAQMCKLAAEGHFAEARVINQRLMPLHNKLFVEPNPIPVKWACKELGLVATDTLRLPMTPITDSGRETVRAALKHAGLL
>d1ucwa_ 3.1.3.2.1 Transaldolase [Escherichia coli]
TDKLTSLRQYTTVVADTGDIAAMKLYQPQDATTNPSLILNAAQIPEYRKLIDDAVAWAKQQSNDRAQQIVDATDKLAVNIGLEILKLVPGRISTEVDARLSYDTEASIAKAKRLIKLYNDAGISNDRILILASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAEAGVFLISPFVGRILDWYKANTDKKEYAPAEDPGVVSVSEIYQYYKEHGYETVVMGASFRNIGEILELAGCDRLTIAPALLKELAESEGAIERKLSYTGEVKARPARITESEFLWQHNQDPMAVDKLAEGIRKFAIDQEKLEKMIGDLL
>d1dosa_ 3.1.4.1.1 Fructose-bisphosphate aldolase [Escherichia coli]
SKIFDFVKPGVITGDDVQKVFQVAKENNFALPAVNCVGTDSINAVLETAAKVKAPVIVQFSNGGASFIAGKGVKSDVPQGAAILGAISGAHHVHQMAEHYGVPVILHTDHCAKKLLPWIDGLLDAGEKHFAATGKPLFSSHMIDLSEESLQENIEICSKYLERMSKIGMTLEIELGCTGGEEDGVDNSHMDASALYTQPEDVDYAYTELSKISPRFTIAASFGNVHGVYKAGNVVLTPTILRDSQEYVSKKHNLPHNSLNFVFHGGSGSTAQEIKDSVSYGVVKMNIDTDTQWATWEGVLNYYKANEAYLQGQLGNPKGEDQPNKKYYDPRVWLRAGQTSMIARLEKAFQELNAIDVL
>d1frb__ 3.1.5.1.1 FR-1 (fibroblast growth factor-induced) protein [mouse (Mus musculus)]
ATFVELSTKAKMPIVGLGTWKSPPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKIKEKAVQREDLFIVSKLWPTCFEKKLLKEAFQKTLTDLKLDYLDLYLIHWPQGLQPGKELFPKDDQGRILTSKTTFLEAWEGMEELVDQGLVKALGVSNFNHFQIERLLNKPGLKHKPVTNQVECHPYLTQEKLIQYCHSKGISVTAYSPLGSPDRPSAKPEDPSLLEDPKIKEIAAKHEKTSAQVLIRFHIQRNVVVIPKSVTPSRIQENIQVFDFQLSDEEMATILSFNRNWRACLLPETVNMEEYPYDAEY
>d1dlaa_ 3.1.5.1.2 Aldose reductase [human (Homo sapiens)]
SHLVLYTGAKMPILGLGTWKSPPGKVTEAVKVAIDLGYRHIDCAHVYQNENEVGLGLQEKLQGQVVKREDLFIVSKLWCTDHEKNLVKGACQTTLRDLKLDYLDLYLIHWPTGFKPGKDPFPLDGDGNVVPDESDFVETWEAMEELVDEGLVKAIGVSNFNHLQVEKILNKPGLKYKPAVNQIEVHPYLTQEKLIEYCKSKGIVVTAYSPLGSPDRPWASLLEDPRIKAIAAKYNKTTAQVLIRFPMQRNLIVIPKSVTPERIAENFQVFDFELSPEDMNTLLSYNRNWRVCALMSCASHKDYPFHEEY
>d2acr__ 3.1.5.1.2 Aldose reductase [human (Homo sapiens)]
ASRLLLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLWCTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEFFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKHNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVCALLSCTSHKDYPFHEEF
>d1ral__ 3.1.5.1.3 3-alpha-hydroxysteroid dehydrogenase [rat (Rattus norvegicus) sprague-dawley strain]
MDSISLRVALNDGNFIPVLGFGTTVPEKVAKDEVIKATKIAIDNGFRHFDSAYLYEVEEEVGQAIRSKIEDGTVKREDIFYTSKLWSTFHRPELVRTCLEKTLKSTQLDYVDLYIIHFPMALQPGDIFFPRDEHGKLLFETVDICDTWEAMEKCKDAGLAKSIGVSNFNCRQLERILNKPGLKYKPVCNQVECHLYLNQSKMLDYCKSKDIILVSYCTLGSSRDKTWVDQKSPVLLDDPVLCAIAKKYKQTPALVALRYQLQRGVVPLIRSFNAKRIKELTQVFEFQLASEDMKALDGLNRNFRYNNA
>d2alr__ 3.1.5.1.4 Aldehyde reductase ALR1 [Human (Homo sapiens)]
AASCVLLHTGQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEDVGPGKAVPREELFVTSKLWNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNADGTICYDSTHYKETWKALEALVAKGLVQALGLSNFNSRQIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGVLLEEPVVLALAEKYGRSPAQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKNWRYIVPMLTVDGKRVPRDAGHPLYPFNDPY
>d1ak5__ 3.1.5.2.1 Inosine monophosphate dehydrogenase (IMPDH) [Tritrichomonas foetus]
AKYYNEPCHTFNEYLLIPGLSTVDCIPSNVNLSTPLVKFQKGQQSEINLKIPLVSAIMQSVSGEKMAIALAREGGISFIFGSQSIESQAAMVHAVKNFKAHNELVDSQKRYLVGAGINTRDFRERVPALVEAGADVLCIDSSDGFSEWQKITIGWIREKYGDKVKVGAGNIVDGEGFRYLADAGADFIKIGIGRGQATAVIDVVAERNKYFEETGIYIPVCSDGGIVYDYHMTLALAMGADFIMLGRYFARFEESPTRKVTINGSVMKEYWGEGSSRGVDSYVPYAGKLKDNVEASLNKVKSTMCNCGALTIPQLQSKAKITLVSSVSI
>d1ebha1 3.1.6.1.1 (142-436) Enolase [baker's yeast (Saccharomyces cerevisiae)]
SPYVLPVPFLNVLNGGSHAGGALALQEFMIAPTGAKTFAEALRIGSEVYHNLKSLTKKRYGASAGNVGDEGGVAPNIQTAEEALDLIVDAIKAAGHDGKVKIGLDCASSEFFKDGKYDLDFKNPNSDKSKWLTGPQLADLYHSLMKRYPIVSIEDPFAEDDWEAWSHFFKTAGIQIVADDLTVTNPKRIATAIEKKAADALLLKVNQIGTLSESIKAAQDSFAAGWGVMVSHRSGETEDTFIADLVVGLRTGQIKTGAPARSERLAKLNQLLRIEEELGDNAVFAGENFHHGDKL
>d1pdz_1 3.1.6.1.2 (140-433) Enolase [Lobster (Homarus vulgaris)]
DEVILPVPAFNVINGGSHAGNKLAMQEFMILPTGATSFTEAMRMGTEVYHHLKAVIKARFGLDATAVGDEGGFAPNILNNKDALDLIQEAIKKAGYTGKIEIGMDVAASEFYKQNNIYDLDFKTANNDGSQKISGDQLRDMYMEFCKDFPIVSIEDPFDQDDWETWSKMTSGTTIQIVGDDLTVTNPKRITTAVEKKACKCLLLKVNQIGSVTESIDAHLLAKKNGWGTMVSHRSGETEDCFIADLVVGLCTGQIKTGAPCRSERLAKYNQILRIEEELGSGAKFAGKNFRAPS
>d1muca1 3.1.6.2.1 (119-360) Muconate-lactonizing enzyme [Pseudomonas putida]
RVRDSLEVAWTLASGDTARDIAEARHMLEIRRHRVFKLKIGANPVEQDLKHVVTIKRELGDSASVRVDVNQYWDESQAIRACQVLGDNGIDLIEQPISRINRGGQVRLNQRTPAPIMADESIESVEDAFSLAADGAASIFALKIAKNGGPRAVLRTAQIAEAAGIGLYGGTMLEGSIGTLASAHAFLTLRQLTWGTELFGPLLLTEEIVNEPPQYRDFQLHIPRTPGLGLTLDEQRLARFAR
>d2mnr_1 3.1.6.2.2 (131-357) Mandelate racemase [Pseudomonas putida]
PVQAYDSHSLDGVKLATERAVTAAELGFRAVKTKIGYPALDQDLAVVRSIRQAVGDDFGIMVDYNQSLDVPAAIKRSQALQQEGVTWIEEPTLQHDYEGHQRIQSKLNVPVQMGENWLGPEEMFKALSIGACRLAMPDAMKIGGVTGWIRASALAQQFGIPMSSHLFQEISAHLLAATPTAHWLERLDLAGSVIEPTLTFEGGNAVIPDLPGVGIIWREKEIGKYLV
>d2chr_1 3.1.6.2.3 (127-370) Chlormuconate cycloisomerase [Alcaligenes eutrophus]
PLRSAIPIAWTLASGDTKRDLDSAVEMIERRRHNRFKVKLGFRSPQDDLIHMEALSNSLGSKAYLRVDVNQAWDEQVASVYIPELEALGVELIEQPVGRENTQALRRLSDNNRVAIMADESLSTLASAFDLARDRSVDVFSLKLCNMGGVSATQKIAAVAEASGIASYGGTMLDSTIGTSVALQLYSTVPSLPFGCELIGPFVLADTLSHEPLEIRDYELQVPTGVGHGMTLDEDKVRQYARVS
>d1dora_ 3.1.7.1.1 Dihydroorotate dehydrogenase A [Lactococcus lactis]
MLNTTFANAKFANPFMNASGVHCMTIEDLEELKASQAGAYITKSSTLEKREGNPLPRYVDLELGSINSMGLPNLGFDYYLDYVLKNQKENAQEGPIFFSIAGMSAAENIAMLKKIQESDFSGITELNLSCPNVPGKPQLAYDFEATEKLLKEVFTFFTKPLGVKLPPYFDLVHFDIMAEILNQFPLTYVNSVNSIGNGLFIDPEAESVVIKPKDGFGGIGGAYIKPTALANVRAFYTRLKPEIQIIGTGGIETGQDAFEHLLCGATMLQIGTALHKEGPAIFDRIIKELEEIMNQKGYQSIADFHGKLKSL
>d1oya__ 3.1.7.1.2 Old yellow enzyme (OYE) [Brewer's yeast (Saccharomyces carlsbergensis)]
SFVKDFKPQALGDTNLFKPIKIGNNELLHRAVIPPLTRMRALHPGNIPNRDWAVEYYTQRAQRPGTMIITEGAFISPQAGGYDNAPGVWSEEQMVEWTKIFNAIHEKKSFVWVQLWVLGWAAFPDNLARDGLRYDSASDNVFMDAEQEAKAKKANNPQHSLTKDEIKQYIKEYVQAAKNSIAAGADGVEIHSANGYLLNQFLDPHSNTRTDEYGGSIENRARFTLEVVDALVEAIGHEKVGLRLSPYGVFNSMSGGAETGIVAQYAYVAGELEKRAKAGKRLAFVHLVEPRVTNPFLTEGEGEYEGGSNDFVYSIWKGPVIRAGNFALHPEVVREEVKDKRTLIGYGRFFISNPDLVDRLEKGLPLNKYDRDTFYQMSAHGYIDYPTYEEALKLGWDKK
>d1gox__ 3.1.7.1.3 Glycolate oxidase [spinach (Spinacia oleracea)]
MEITNVNEYEAIAKQKLPKMVYDYYASGAEDQWTLAENRNAFSRILFRPRILIDVTNIDMTTTILGFKISMPIMIAPTAMQKMAHPEGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYKDRNVVAQLVRRAERAGFKAIALTVDTPRLGRREADIKNRFVLPPFLTLKNFEGIDLGLSSYVAGQIDRSLSWKDVAWLQTITSLPILVKGVITAEDARLAVQHGAAGIIVSNHGARQLDYVPATIMALEEVVKAAQGRIPVFLDGGVRRGTDVFKALALGAAGVFIGRPVVFSLAAEGEAGVKKVLQMMRDEFELTMALSGCRSLKEISRSHIAADWD
>d2tmda1 3.1.7.1.4 (1-340) Trimethylamine dehydrogenase, N-terminal domain [Escherichia coli]
ARDPKHDILFEPIQIGPKTLRNRFYQVPHCIGAGSDKPGFQSAHRSVKAEGGWAALNTEYCSINPESDDTHRLSARIWDEGDVRNLKAMTDEVHKYGALAGVELWYGGAHAPNMESRATPRGPSQYASEFETLSYCKEMDLSDIAQVQQFYVDAAKRSRDAGFDIVYVYGAHSYLPLQFLNPYYNKRTDKYGGSLENRARFWLETLEKVKHAVGSDCAIATRFGVDTVYGPGQIEAEVDGQKFVEMADSLVDMWDITIGDIAEWGEDAGPSRFYQQGHTIPWVKLVKQVSKKPVLGVGRYTDPEKMIEIVTKGYADIIGCARPSIADPFLPQKVEQGRYD
>d1ltda1 3.1.7.1.5 (89-481) Flavocytochrome b2, C-terminal domain [yeast (Saccharomyces cerevisiae)]
APGETKEDIARKEQLKSLLPPLDNIINLYDFEYLASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATALCKLGNPLEGEKDVARGCGQGVTKVPQMISTLASCSPEEIIEAAPSDKQIQWYQLYVNSDRKITDDLVKNVEKLGVKALFVTVDAPSLGQREKDMKLKFSNALSKFIDPSLTWKDIEELKKKTKLPIVIKGVQRTEDVIKAAEIGVSGVVLSNHGGRQLDFSRAPIEVLAETMPILEQRNLKDKLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPFLYANSCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAELKPDLLDLSTLKARTVGVPNDVLYNEVYEGPTLTEFEDA
>d1pii_1 3.1.8.1.1 (1-254) N-(5'phosphoribosyl)antranilate (PRA)isomerase [Escherichia coli]
MQTVLAKIVADKAIWVEARKQQQPLASFQNEVQPSTRHFYDALQGARTAFILECKKASPSKGVIRDDFDPARIAAIYKHYASAISVLTDEKYFQGSFNFLPIVSQIAPQPILCKDFIIDPYQIYLARYYQADACLLMLSVLDDDQYRQLAAVAHSLEMGVLTEVSNEEEQERAIALGAKVVGINNRDLRDLSIDLNRTRELAPKLGHNVTVISESGINTYAQVRELSHFANGFLIGSALMAHDDLHAAVRRVLL
>d1nsj__ 3.1.8.1.2 N-(5'phosphoribosyl)antranilate (PRA)isomerase [Thermotoga maritima]
MVRVKICGITNLEDALFSVESGADAVGFVFYPKSKRYISPEDARRISVELPPFVFRVGVFVNEEPEKILDVASYVQLNAVQLHGEEPIELCRKIAERILVIKAVGVSNERDMERALNYREFPILLDTKTPEYGGSGKTFDWSLILPYRDRFRYLVLSGGLNPENVRSAIDVVRPFAVDVSSGVEAFPGKKDHDSIKMFIKNAKGL
>d1pii_2 3.1.8.1.3 (255-452) Indole-3-glycerophosphate (IGP) synthase [Escherichia coli]
GENKVCGLTRGQDAKAAYDAGAIYGGLIFVATSPRCVNVEQAQEVMAAAPLQYVGVFRNHDIADVVDKAKVLSLAAVQLHGNEEQLYIDTLREALPAHVAIWKALSVGETLPAREFQHVDKYVLDNGQGGSGQRFDWSLLNGQSLGNVLLAGGLGADNCVEAAQTGCAGLDFNSAVESQPGIKDARLLASVFQTLRAY
>d1igs__ 3.1.8.1.4 Indole-3-glycerophosphate (IGP) synthase [(Sulfolobus solfataricus)]
PRYLKGWLKDVVQLSLRRPSFRASRQRPIISLNERILEFNKRNITAIIAEYKRKSPSGLDVERDPIEYSKFMERYAVGLSILTEEKYFNGSYETLRKIASSVSIPILMKDFIVKESQIDDAYNLGADTVLLIVKILTERELESLLEYARSYGMEPLIEINDENDLDIALRIGARFIGINSRDLETLEINKENQRKLISMIPSNVVKVAESGISERNEIEELRKLGVNAFLIGSSLMRNPEKIKEFIL
>d1wsya_ 3.1.8.1.5 Trp synthase alpha-subunit [Salmonella typhimurium]
MERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSADGPTIQNANLRAFAAGVTPAQCFEMLALIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADDDLLRQVASYGRGYTYLLPLHHLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKIIEKNLASPKQMLAELRSFVSAMKAA
>d1pkm_2 3.1.9.1.1 (1-104,207-384) Pyruvate kinase, N-terminal domain [cat muscle (Felis domestica)]
IQTQQLHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVEILKEMIKSGMNVARLNFSHGTHEYHAETIKNVRAATESFASDPIRYRPVAVALDTKGEQDVDMVFASFIRKASDVHEVRKVLGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKV
>d1pkya2 3.1.9.1.3 (1-69,168-344) Pyruvate kinase, N-terminal domain [Escherichia coli]
MKKTKIVCTIGPKTESEEMLAKMLDAGMNVMRLNFSHGDYAEHGQRIQNLRNVMSKTGKTAAILLDTKGISKIENQEGLNNFDEILEASDGIMVARGDLGVEIPVEEVIFAQKMMIEKCIRARKVVITATMMLDSMIKNPRPTRAEAGDVANAILDGTDAVMLSGESAKGKYPLEA
>d1dik_1 3.1.9.2.1 (505-869) Pyruvate phosphate dikinase, C-terminal domain [Escherichia coli]
IETQEASVSGSFERIMVWADKFRTLKVRTNADTPEDTLNAVKLGAEGIGLCRTEHMFFEADRIMKIRKMILSDSVEAREEALNELIPFQKGDFKAMYKALEGRPMTVRYLDPPLHEFVPHTEEEQAELAKNMGLTLAEVKAKVDELHEFNPMMGHRGCRLAVTYPEIAKMQTRAVMEAAIEVKEETGIDIVPEIMIPLVGEKKELKFVKDVVVEVAEQVKKEKGSDMQYHIGTMIEIPRAALTADAIAEEAEFFSFGTNDLTQMTFGFSRDDAGKFLDSYYKAKIYESDPFARLDQTGVGQLVEMAVKKGRQTRPGLKCGICGEHGGDPSSVEFCHKVGLNYVSCSPFRVPIARLAAAQAALNNK
>d1pau.1 3.10.1.1.1 (a,b) Apopain [Human (Homo sapiens)]
DNSYKMDYPEMGLCIIINNKNFHKSTGMTSRSGTDVDAANLRETFRNLKYEVRNKNDLTREEIVELMRDVSKEDHSKRSSFVCVLLSHGEEGIIFGTNGPVDLKKITNFFRGDRCRSLTGKPKLFIIQACRGTELDCGIEQYADKLEFMHILTRVNRKVATEFESFSFDATFHAKKQIPCIVSMLTKELYFYDNSYKMDYPEMGLCIIINNKNFHKSTGMTSRSGTDVDAANLRETFRNLKYEVRNKNDLTREEIVELMRDVSKEDHSKRSSFVCVLLSHGEEGIIFGTNGPVDLKKITNFFRGDRCRSLTGKPKLFIIQACRGTELDCGIEQYADKLEFMHILTRVNRKVATEFESFSFDATFHAKKQIPCIVSMLTKELYFY
>d1ice.1 3.10.1.1.2 (a,b) Interleukin-1beta converting enzyme (a cysteine protease) [Human (Homo sapiens)]
GNVKLCSLEEAQRIWKQKSAEIYPIMDKSSRTRLALIICNEEFDSIPRRTGAEVDITGMTMLLQNLGYSVDVKKNLTASDMTTELEAFAHRPEHKTSDSTFLVFMSHGIREGICGKKHSEQVPDILQLNAIFNMLNTKNCPSLKDKPKVIIIQACRGDSPGVVWFKDAFCSSTPDNVSWRHPTMGSVFIGRLIEHMQEYACSCDVEEIFRKVRFSFEQPDGRAQMPTTERVTLTRCFYLFPGHGNVKLCSLEEAQRIWKQKSAEIYPIMDKSSRTRLALIICNEEFDSIPRRTGAEVDITGMTMLLQNLGYSVDVKKNLTASDMTTELEAFAHRPEHKTSDSTFLVFMSHGIREGICGKKHSEQVPDILQLNAIFNMLNTKNCPSLKDKPKVIIIQACRGDSPGVVWFKDAFCSSTPDNVSWRHPTMGSVFIGRLIEHMQEYACSCDVEEIFRKVRFSFEQPDGRAQMPTTERVTLTRCFYLFPGH
>d1akz__ 3.11.1.1.1 Uracil-DNA glycosylase [Human (Homo sapiens)]
MEFFGESWKKHLSGEFGKPYFIKLMGFVAEERKHYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVPPPPSLENIYKELSTDIEDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLWGSYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGCRHFSKTNELLQKSGKKPIDWKEL
>d1udg__ 3.11.1.1.2 Uracil-DNA glycosylase [Herpes simplex virus type-1 (HSV1)]
LDWTTFRRVFLIDDAWRPLMEPELANPLTAHLLAEYNRRCQTEEVLPPREDVFSWTRYCTPDEVRVVIIGQDPYHHPGQAHGLAFSVRANVPPPPSLRNVLAAVKNCYPEARMSGHGCLEKWARDGVLLLNTTLTVKRGAAASHSRIGWDRFVGGVIRRLAARRPGLVFMLWGTHAQNAIRPDPRVHCVLKFSHPSPLSKVPFGTCQHFLVANRYLETRSISPIDWSV
>d1mla_1 3.12.1.1.1 (1-125,196-305) Catalytic domain of malonyl-CoA ACP transacylase [Esherichia coli]
QFAFVFPGQGSQTVGMLADMAASYPIVEETFAEASAALGYDLWALTQQGPAEELNKTWQTQPALLTASVALYRVWQQQGGKAPAMMAGHSLGEYSALVCAGVIDFADAVRLVEMRGKFMQEAVP
>d1ipha1 3.13.1.1.2 (572-727) Catalase, C-terminal domain [Escherichia coli HPII]
VKGRVVAILLNDEVRSADLLAILKALKAKGVHAKLLYSRMGEVTADDGTVLPIAATFAGAPSLTVDAVIVPCGNIADIADNGDANYYLMEAYKHLKPIALAGDARKFKATIKIADQGEEGIVEADSADGSFMDELLTLMAAHRVWSRIPKIDKIPA
>d3chy__ 3.13.2.1.1 CheY protein [Escherichia coli]
ADKELKFLVVDDFSTMRRIVRNLLKELGFNNVEEAEDGVDALNKLQAGGYGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEKLGM
>d1hey__ 3.13.2.1.1 CheY protein [Escherichia coli]
DKELKFLVVGNGGTGKSTVRNLLKELGFNNVEDAEDGVDALNKLQAGGYGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEKLGM
>d1rnl_2 3.13.2.1.3 (1-138) Nitrate/nitrite response regulator (NARL), receiver domain [Escherichia coli]
EPATILLIDDHPMLRTGVKQLISMAPDITVVGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGRIVVFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKALHQAAAGEMVLSEALTPVLAASL
>d1ntr__ 3.13.2.1.4 NTRC receiver domain [Salmonella typhimurium]
MQRGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLAALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQE
>d1srra_ 3.13.2.1.5 Sporulation response regulator Spo0F [Bacillus subtilis]
NEKILIVDDQSGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTAYGELDMIQESKELGALTHFAKPFDIDEIRDAVKKYLPL
>d1scua1 3.13.3.1.1 (122-288) Succinyl-CoA synthetase, alpha-chain, C-terminal domain [Escherichia coli]
NCPGVITPGECKIGIQPGHIHKPGKVGIVSRSGTLTYEAVKQTTDYGFGQSTCVGIGGDPIPGSNFIDILEMFEKDPQTEAIVMIGEIGGSAEEEAAAYIKEHVTKPVVGYIAGVTAPKGKRMGHAGAIIAGGKGTADEKFAALEAAGVKTVRSLADIGEALKTVLK
>d1scub1 3.13.3.1.2 (245-388) Succinyl-CoA synthetase, beta-chain, C-terminal domain [Escherichia coli]
AAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKVKAVLVNIFGGIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAAKGLTDAAQQVVAAVEGK
>d2fcr__ 3.13.4.1.1 Flavodoxin [Chondrus crispus]
KIGIFFSTSTGNTTEVADFIGKTLGAKADAPIDVDDVTDPQALKDYDLLFLGAPTWNTGADTERSGTSWDEFLYDKLPEVDMKDLPVAIFGLGDAEGYPDNFCDAIEEIHDCFAKQGAKPVGFSNPDDYDYEESKSVRDGKFLGLPLDMVNDQIPMEKRVAGWVEAVVSETGV
>d2fx2__ 3.13.4.1.2 Flavodoxin [Desulfovibrio vulgaris]
AKALIVYGSTTGNTEYTAETIARELADAGYEVDSRDAASVEAGGLFEGFDLVLLGCSTWGDDSIELQDDFIPLFDSLEETGAQGRKVACFGCGDSSYEYFCGAVDAIEEKLKNLGAEIVQDGLRIDGDPRAARDDIVGWAHDVRGAI
>d1rcf__ 3.13.4.1.3 Flavodoxin [Anabaena 7120]
SKKIGLFYGTQTGKTESVAEIIRDEFGNDVVTLHDVSQAEVTDLNDYQYLIIGCPTWNIGELQSDWEGLYSELDDVDFNGKLVAYFGTGDQIGYADNFQDAIGILEEKISQRGGKTVGYWSTDGYDFNDSKALRNGKFVGLALDEDNQSDLTDDRIKSWVAQLKSEFGL
>d1ofv__ 3.13.4.1.5 Flavodoxin [Anacystis nidulans]
AKIGLFYGTQTGVTQTIAESIQQEFGGESIVDLNDIANADASDLNAYDYLIIGCPTWNVGELQSDWEGIYDDLDSVNFQGKKVAYFGAGDQVGYSDNFQDAMGILEEKISSLGSQTVGYWPIEGYDFNESKAVRNNQFVGLAIDEDNQPDLTKNRIKTWVSQLKSEFGL
>d5nul__ 3.13.4.1.6 Flavodoxin [Clostridium beijerinckii]
MKIVYWSGTGNTEKMAELIAKGIIESGKDVNTINVSDVNIDELLNEDILILGCSAMTDEVLEESEFEPFIEEISTKISGKKVALFGSYGWGDGKWMRDFEERMNGYGCVVVETPLIVQNEPDEAEQDCIEFGKKIANI
>d1qrda_ 3.13.4.2.1 NAD(P)H:quinone reductase [Murine (Mus musculus)]
AVRRALIVLAHAERTSFNYAMKEAAVEALKKKGWEVVESDLYAMNFNPLISRNDITGEPKDSENFQYPVESSLAYKEGRLSPDIVAEQKKLEAADLVIFQFPLYWFGVPAILKGWFERVLVAGFAYTYATMYDKGPFQNKKTLLSITTGGSGSMYSLQGVHGDMNVILWPIQSGILRFCGFQVLEPQLVYSIGHTPPDARVQVLEGWKKRLETVWEESPLYFAPSSLFDLNFQAGFLLKKEVQEEQKKNKFGLSVGHHLGKSIPADNQIKARK
>d1bmta2 3.13.5.1.1 (91-246) Methionine synthase, C-terminal domain [Escherichia coli]
EQGKTNGKMVIATVKGDVHDIGKNIVGVVLQCNNYEIVDLGVMVPAEKILRTAKEVNADLIGLSGLITPSLDEMVNVAKEMERQGFTIPLLIGGATTSKAHTAVKIEQNYSGPTVYVQNASRTVGVVAALLSDTQRDDFVARTRKEYETVRIQHGR
>d1reqb2 3.13.5.2.1 (457-619) Methylmalonyl-CoA mutase, alpha and beta subunits [Propionibacterium freudenreichii shermani]
TKPFPAAPARKGLAWHRDSEVFEQLMDRSTSVSERPKVFLACLGTRRDFGGREGFSSPVWHIAGIDTPQVEGGTTAEIVEAFKKSGAQVADLCSSAKVYAQQGLEVAKALKAAGAKALYLSGAFKEFGDDAAEAEKLIDGRLFMGMDVVDTLSSTLDILGVAK
>d1reqa2 3.13.5.2.1 (560-727) Methylmalonyl-CoA mutase, alpha and beta subunits [Propionibacterium freudenreichii shermani]
AQIRTISGVYSKEVKNTPEVEEARELVEEFEQAEGRRPRILLAKMGQDGHDRGQKVIATAYADLGFDVDVGPLFQTPEETARQAVEADVHVVGVSSLAGGHLTLVPALRKELDKLGRPDILITVGGVIPEQDFDELRKDGAVEIYTPGTVIPESAISLVKKLRASLDA
>d1orda1 3.13.6.1.1 (1-107) Ornithine decarboxylase N-terminal "wing" domain [Lactobacillus 30a]
SSSLKIASTQEARQYFDTDRVVVDAVGSDFTDVGAVIAMDYETDVIDAADATKFGIPVFAVTKDAQAISADELKKIFHIIDLENKFDATVNAREIETAVNNYEDSIL
>d1cus__ 3.13.7.1.1 Cutinase [fungus (Fusarium solani, subsp. pisi)]
RTTRDDLINGNSASCADVIFIYARGSTETGNLGTLGPSIASNLESAFGKDGVWIQGVGGAYRATLGDNALPRGTSSAAIREMLGLFQQANTKCPDATLIAGGYSQGAALAAASIEDLDSAIRDKIAGTVLFGYTKNLQNRGRIPNYPADRTKVFCNTGDLVCTGSLIVAAPHLAYGPDARGPAPEFLIEKVRAVRGS
>d1esc__ 3.13.8.1.1 Esterase [Streptomyces scabies]
DPVPTVFFGDSYTANFGIAPVTNQDSERGWCFQAKENYPAVATRSLADKGITLDVQADVSCGGALIHHFWEKQELPFGAGELPPQQDALKQDTQLTVGSLGGNTLGFNRILKQCSDELRKPSLLPGDPVDGDEPAAKCGEFFGTGDGKQWLDDQFERVGAELEELLDRIGYFAPDAKRVLVGYPRLVPEDTTKCLTAAPGQTQLPFADIPQDALPVLDQIQKRLNDAMKKAAADGGADFVDLYAGTGANTACDGADRGIGGLLEDSQLELLGTKIPWYAHPNDKGRDIQAKQVADKIEEILN
>d2naca1 3.13.9.1.1 (1-147,336-374) Formate dehydrogenase [Pseudomonas sp. 101]
AKVLCVLYDDPVDGYPKTYARDDLPKIDHYPGGQTLPTPKAIDFTPGQLLGSVSGELGLRKYLESNGHTLVVTSDKDGPDSVFERELVDADVVISQPFWPAYLTPERIAKAKNLKLALTAGIGSDHVDLQSAIDRNVTVAEVTYCN
>d1dxy_1 3.13.9.1.2 (1-100) D-2-hydroxyisocaproate dehydrogenase [Lactobacillus casei]
MKIIAYGARVDEIQYFKQWAKDTGNTLEYHTEFLDENTVEWAKGFDGINSLQTTPYAAGVFEKMHAYGIKFLTIRNVGTDNIDMTAMKQYGIRLSNVPAY
>d1gdha1 3.13.9.1.3 (1-99,291-320) D-glycerate dehydrogenase [Hyphomicrobium methylovorum]
KKKILITWPLPEAAMARARESYDVIAHGDDPKITIDEMIETAKSVDALLITLNEKCRKEVIDRIPENIKCISTYSIGFDHIDLDACKARGIKVGNAPH
>d1psda1 3.13.9.1.4 (1-101,290-320) Phosphoglycerate dehydrogenase [Escherichia coli]
EKDKIKFLLVEGVHQKALESLRAAGYTNIEFHKGALDDEQLKESIRDAHFIGLRSRTHLTEDVINAAEKLVAIGCFCIGTNQVDLDAAAKRGIPVFNAPF
>d2dlda1 3.13.9.1.5 (1-103) D-lactate dehydrogenase [Lactobacillus helveticus]
MTKVFAYAIRKDEEPFLNEWKEAHKDIDVDYTDKLLTPETAKLAKGADGVVVYQQLDYTADTLQALADAGVTKMSLRNVGVDNIDMDKAKELGFQITNVPVYS
>d1fnb_2 3.14.1.1.1 (137-296) Ferredoxin reductase [spinach (Spinacia oleracea)]
MLMPKDPNATIIMLGTGTGIAPFRSFLWKMFFEKHDDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPDNFRLDFAVSREQTNEKGEKMYIQTRMAQYAVELWEMLKKDNTYVYMCGLKGMEKGIDDIMVSLAAAEGIDWIEYKRQLKKAEQWNVEVY
>d1quf_2 3.14.1.1.2 (135-296) Ferredoxin reductase [cyanobacterium (Anabaena pcc 7119)]
LPDDPEANVIMLATGTGIAPMRTYLWRMFKDAERAANPEYQFKGFSWLVFGVPTTPNILYKEELEEIQQKYPDNFRLTYAISREQKNPQGGRMYIQDRVAEHADQLWQLIKNEKTHTYICGLRGMEEGIDAALSAAAAKEGVTWSDYQKDLKKAGRWHVETY
>d1fdr_2 3.14.1.1.3 (97-244) Ferredoxin reductase [Escherichia coli]
DEVPHCETLWMLATGTAIGPYLSILRLGKDLDRFKNLVLVHAARYAADLSYLPLMQELEKRYEGKLRIQTVVSRETAAGSLTGRIPALIESGELESTIGLPMNKETSHVMLCGNPQMVRDTQQLLKETRQMTKHLRRRPGHMTAEHYW
>d2cnd_2 3.14.1.1.4 (115-260) Nitrate reductase [corn (Zea mays)]
GSFVINGKQRNARRLAMICGGSGITPMYQIIQAVLRDQPEDHTEMHLVYANRTEDDILLRDELDRWAAEYPDRLKVWYVIDQVKRPEEGWKYSVGFVTEAVLREHVPEGGDDTLALACGPPPMIQFAISPNLEKMKYDMANSFVVF
>d1ndh_2 3.14.1.1.5 (124-270) cytochrome b5 reductase [pig (Sus scrofa) liver]
GKFAIRPDKKSSPVIKTVKSVGMIAGGTGITPMLQVIRAIMKDPDDHTVCHLLFANQTEKDILLRPELEELRNEHSARFKLWYTVDRAPEAWDYSQGFVNEEMIRDHLPPPEEEPLVLMCGPPPMIQYACLPNLERVGHPKERCFAF
>d2pia_2 3.14.1.2.1 (104-223) Phthalate dioxygenase reductase [Pseudomonas cepacia db01]
EFPLDKRAKSFILVAGGIGITPMLSMARQLRAEGLRSFRLYYLTRDPEGTAFFDELTSDEWRSDVKIHHDHGDPTKAFDFWSVFEKSKPAQHVYCCGPQALMDTVRDMTGHWPSGTVHFE
>d2ts1_2 3.15.1.1.1 (1-215) Tyrosyl-tRNA synthetase (TyrRS) [Bacillus stearothermophilus /nca 1503]
MDLLAELQWRGLVNQTTDEDGLRKLLNEERVTLYCGFDPTADSLHIGHLATILTMRRFQQAGHRPIALVGGATGLIGDPSGKKSERTLNAKETVEAWSARIKEQLGRFLDFEADGNPAKIKNNYDWIGPLDVITFLRDVGKHFSVNYMMAKESVQSRIETGISFTEFSYMMLQAYDFLRLYETEGCRLQIGGSDQWGNITAGLELIRKTKGRAFG
>d1gtra2 3.15.1.1.2 (1-331) Glutaminyl-tRNA synthetase (GlnRS) [Escherichia coli]
TNFIRQIIDEDLASGKHTTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYKGQCNLRFDDTNPVKEDIEYVESIKNDVEWLGFHWSGNVRYSSDYFDQLHAYAIELINKGLAYVDELTPEQIREYRGTLTQPGKNSPYRDRSVEENLALFEKMRAGGFEEGKACLRAKIDMASPFIVMRDPVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPVHPRQYEFSRLNLEYTVMSKRKLNLLVTDKHVEGWDDPRMPTISGLRRRGYTAASIREFCKRIGVTKQDNTIEMASLESCIREDLNEN
>d1gln_2 3.15.1.1.3 (1-305) Glutamyl-tRNA synthetase (GluRS) [Thermus thermophilus]
MVVTRIAPSPTGDPHVGTAYIALFNYAWARRNGGRFIVRIEDTDRARYVPGAEERILAALKWLGLSYDEGPDVAAPTGPYRQSERLPLYQKYAEELLKRGWAYRAFETPEELEQIRKEKGGYDGRARNIPPEEAEERARRGEPHVIRLKVPRPGTTEVKDELRGVVVYDNQEIPDVVLLKSDGYPTYHLANVVDDHLMGVTDVIRAEEWLVSTPIHVLLYRAFGWEAPRFYHMPLLRNPDKTKISKRKSHTSLDWYKAEGFLPEALRNYLCLMGFSMPDGREIFTLEEFIQAFTWERVSLGGPVF
>d1gpma1 3.15.2.1.1 (206-380) GMP synthetase, central domain [Escherichia coli]
WTPAKIIDDAVARIREQVGDDKVILGLSGGVDSSVTAMLLHRAIGKNLTCVFVDNGLLRLNEAEQVLDMFGDHFGLNIVHVPAEDRFLSALAGENDPEAKRKIIGRVFVEVFDEEALKLEDVKWLAQGTIYPDVIESAAKMGLVEPLKELFKDEVRKIGLELGLPYDMLYRHPFP
>d1nsya_ 3.15.2.1.2 NH3-dependent NAD+-synthetase [Bacillus subtilis]
SMQEKIMRELHVKPSIDPKQEIEDRVNFLKQYVKKTGAKGFVLGISGGQDSTLAGRLAQLAVESIREEGGDAQFIAVRLPHGTQQDEDDAQLALKFIKPDKSWKFDIKSTVSAFSDQYQQETGDQLTDFNKGNVKARTRMIAQYAIGGQEGLLVLGTDHAAEAVTGFFTKYGDGGADLLPLTGLTKRQGRTLLKELGAPERLYLKEPTADLLDEKPQQSDETELGISYDEIDDYLEGKEVSAKVSEALEKRYSMTEHKRQVPASMFDDWWK
>d1tpt_2 3.16.1.1.1 (71-335) Thymidine phosphorylase, middle domain [Escherichia coli]
DWKSLHLNGPIVDKHSTGGVGDVTSLMLGPMVAACGGYIPMISGRGLGHTGGTLDKLESIPGFDIFPDDNRFREIIKDVGVAIIGQTSSLAPADKRFYATRDITATVDSIPLITASILAKKLAEGLDALVMDVKVGSGAFMPTYELSEALAEAIVGVANGAGVRTTALLTDMNQVLASSAGNAVEVREAVQFLTGEYRNPRLFDVTMALCVEMLISGKLAKDDAEARAKLQAVLDNGKAAEVFGRMVAAQKGPTDFVENYAKYLP
>d1dnpa2 3.17.1.1.1 (1-200) N-terminal domain of DNA photolyase [Escherichia coli]
TTHLVWFRQDLRLHDNLALAAACRNSSARVLALYIATPRQWATHNMSPRQAELINAQLNGLQIALAEKGIPLLFREVDDFVASVEIVKQVCAENSVTHLFYNYQYEVNERARDVEVERALRNVVCEGFDDSVILPPGAVMTGNHEMYKVFTPFKNAWLKRLREGMPECVAAPKVRSSGSIEPSPSITLNYPRQSFDTAHF
>d2tmda3 3.18.1.1.1 (341-489,646-729) Trimethylamine dehydrogenase, middle, ADP-binding domain [Escherichia coli]
DIRVCIGCNVCISRWEIGGPPMICTQNATAGEEYRRGWHPEKFRQTKNKDSVLIVGAGPSGSEAARVLMESGYTVHLTDTAEKIGGHLNQVAALPGLGEWSYHRDYRETQITKLLKKNKESQLALGQKPMTADDVLQYGADKVIIATG
>d1kifa1 3.18.1.2.1 (1-194,288-339) D-amino acid oxidase, N-terminal domain [Pig (Sus scrofa)]
MRVVVIGAGVIGLSTALCIHERYHSVLQPLDVKVYADRFTPFTTTDVAAGLWQPYTSEPSNPQEANWNQQTFNYLLSHIGSPNAANMGLTPVSGYNLFREAVPDPYWKDMVLGFRKLTPRELDMFPDYRYGWFNTSLILEGRKYLQWLTERLTERGVKFFLRKVESFEEVARGGADVIINCTGVWAGVLQPDP
>d1cdoa2 3.19.1.1.1 (176-324) Alcohol dehydrogenase [horse (Equus caballus)]
GVSTGFGAAVNTAKVEPGSTCAVFGLGAVGLAAVMGCHSAGAKRIIAVDLNPDKFEKAKVFGATDFVNPNDHSEPISQVLSKMTNGGVDFSLECVGNVGVMRNALESCLKGWGVSVLVGWTDLHDVATRPIQLIAGRTWKGSMFGGFKG
>d7adh_2 3.19.1.1.1 (175-324) Alcohol dehydrogenase [horse (Equus caballus)]
GFSTGYGSAVXVAXVTQGSTCAVFGLGGVGLSVIMGCXAAGAARIIGVDINXDXFAXAKEVGATECVNPQDYXKPIQEVLTEMSNGGVDFSFEVIGRLDTMVTALSCCQEAYGVSVIVGVPPDSQNLSMNPMLLLSGRTWKGAIFGGFKS
>d2ohxa2 3.19.1.1.1 (175-324) Alcohol dehydrogenase [horse (Equus caballus)]
GFSTGYGSAVKVAKVTQGSTCAVFGLGGVGLSVIMGCKAAGAARIIGVDINKDKFAKAKEVGATECVNPQDYKKPIQEVLTEMSNGGVDFSFEVIGRLDTMVTALSCCQEAYGVSVIVGVPPDSQNLSMNPMLLLSGRTWKGAIFGGFKS
>d1agna2 3.19.1.1.2 (174-323) Alcohol dehydrogenase [human (Homo sapiens), different isozymes]
GFSTGYGAAVKTGKVKPGSTCVVFGLGGVGLSVIMGCKSAGASRIIGIDLNKDKFEKAMAVGATECISPKDSTKPISEVLSEMTGNNVGYTFEVIGHLETMIDALASCHMNYGTSVVVGVPPSAKMLTYDPMLLFTGRTWKGCVFGGLKS
>d1htba2 3.19.1.1.2 (175-324) Alcohol dehydrogenase [human (Homo sapiens), different isozymes]
GFSTGYGSAVNVAKVTPGSTCAVFGLGGVGLSAVMGCKAAGAARIIAVDINKDKFAKAKELGATECINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPASQNLSINPMLLLTGRTWKGAVYGGFKS
>d1teha2 3.19.1.1.2 (174-323) Alcohol dehydrogenase [human (Homo sapiens), different isozymes]
GISTGYGAAVNTAKLEPGSVCAVFGLGGVGLAVIMGCKVAGASRIIGVDINKDKFARAKEFGATECINPQDFSKPIQEVLIEMTDGGVDYSFECIGNVKVMRAALEACHKGWGVSVVVGVAASGEEIATRPFQLVTGRTWKGTAFGGWKS
>d1keva2 3.19.1.1.3 (151-314) Bacterial secondary alcohol dehydrogenase [Clostridium beijerinckii]
MMTTGFHGAELADIQMGSSVVVIGIGAVGLMGIAGAKLRGAGRIIGVGSRPICVEAAKFYGATDILNYKNGHIVDQVMKLTNGKGVDRVIMAGGGSETLSQAVSMVKPGGIISNINYHGSGDALLIPRVEWGCGMAHKTIKGGLCPGGRLRAEMLRDMVVYNRV
>d1qora2 3.19.1.1.4 (135-264) Quinone oxidoreductase [Escherichia coli]
YEIKPDEQFLFHAAAGGVGLIACQWAKALGAKLIGTVGTAQKAQSALKAGAWQVINYREEDLVERLKEITGGKKVRVVYDSVGRDTWERSLDCLQRRGLMVSFGNSSGAVTGVNLGILNQKGSLYVTRPS
>d1xel__ 3.19.1.2.1 Uridine diphosphogalactose-4-epimerase (UDP-galactose 4-epimerase) [Escherichia coli]
MRVLVTGGSGYIGSHTCVQLLQNGHDVIILDNLCNSKRSVLPVIERLGGKHPTFVEGDIRNEALMTEILHDHAIDTVIHFAGLKAVGESVQKPLEYYDNNVNGTLRLISAMRAANVKNFIFSSSATVYGDNPKIPYVESFPTGTPQSPYGKSKLMVEQILTDLQKAQPDWSIALLRYFNPVGAHPSGDMGEDPQGIPNNLMPYIAQVAVGRRDSLAIFGNDYPTEDGTGVRDYIHVMDLADGHVVAMEKLANKPGVHIYNLGAGVGNSVLDVVNAFSKACGKPVNYHFAPRREGDLPAYWADASKADRELNWRVTRTLDEMAQDTWHWQSRHPQGYPD
>d1ybva_ 3.19.1.2.11 1,3,8-trihydroxynaphtalene reductase (THNR, naphtol reductase) [Rice blast fungus (Magnaporthe grisea)]
DAIPGPLGPQSASLEGKVALVTGAGRGIGREMAMELGRRGCKVIVNYANSTESAEEVVAAIKKNGSDAACVKANVGVVEDIVRMFEEAVKIFGKLDIVCSNSGVVSFGHVKDVTPEEFDRVFTINTRGQFFVAREAYKHLEIGGRLILMGSITGQAKAVPKHAVYSGSKGAIETFARCMAIDMADKKITVNVVAPGGIKTDMYHAVCREYIPNGENLSNEEVDEYAAVQWSPLRRVGLPIDIARVVCFLASNDGGWVTGKVIGIDGGACM
>d1cyda_ 3.19.1.2.2 Carbonyl reductase [Mouse (Mus musculus)]
LNFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKECPGIEPVCVDLGDWDATEKALGGIGPVDLLVNNAALVIMQPFLEVTKEAFDRSFSVNLRSVFQVSQMVARDMINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGYLAS
>d1fds__ 3.19.1.2.3 Human estrogenic 17beta-hydroxysteroid dehydrogenase [Human (Homo sapiens)]
ARTVVLITGCSSGIGLHLAVRLASDPSQSFKVYATLRDLKTQGRLWEAARALACPPGSLETLQLDVRDSKSVAAARERVTEGRVDVLVCNAGLGLLGPLEALGEDAVASVLDVNVVGTVRMLQAFLPDMKRRGSGRVLVTGSVGGLMGLPFNDVYCASKFALEGLCESLAVLLLPFGVHLSLIECGPVHTVLGSPEEVLDRTDIHTFHRFYQYLAHSKQVFREAAQNPEEVAEVFLTALRAPKPTLRYFTTERFLPLLRMRLDDPSGSNYVTAMHREVFGDV
>d1fmca_ 3.19.1.2.4 7-alpha-hydroxysteroid dehydrogenase [Escherichia coli]
MFNSDNLRLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGGQAFACRCDITSEQELSALADFAISKLGKVDILVNNAGGGGPKPFDMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDALKSVITPEIEQKMLQHTPIRRLGQPQDIANAALFLCSPAASWVSGQILTVSGGGVQELN
>d1hdca_ 3.19.1.2.5 3-alpha,20-beta-hydroxysteroid dehydrogenase [Streptomyces hydrogenans]
NDLSGKTVIITGGARGLGAEAARQAVAAGARVVLADVLDEEGAATARELGDAARYQHLDVTIEEDWQRVVAYAREEFGSVDGLVNNAGISTGMFLETESVERFRKVVEINLTGVFIGMKTVIPAMKDAGGGSIVNISSAAGLMGLALTSSYGASKWGVRGLSKLAAVELGTDRIRVNSVHPGMTYTPMTAETGIRQGEGNYPNTPMGRVGEPGEIAGAVVKLLSDTSSYVTGAELAVDGGWTTGPTVKYVMGQ
>d1dhr__ 3.19.1.2.6 Dihydropteridin reductase [rat (Rattus norvegicus)]
EARRVLVYGGRGALGSRCVQAFRARNWWVASIDVVENEEASASVIVKMTDSFTEQADQVTAEVGKLLGDQKVDAILCVAGGWAGGNAKSKSLFKNCDLMWKQSIWTSTISSHLATKHLKEGGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLAGKNSGMPSGAAAIAVLPVTLDTPMNRKSMPEADFSSWTPLEFLVETFHDWITGNKRPNSGSLIQVVTTDGKTELTPAYF
>d1eno__ 3.19.1.2.8 Enoyl-ACP reductase [Oil seed rape (Brassica napus)]
LPIDLRGKRAFIAGIADDNGYGWAVAKSLAAAGAEILVGTWVPALNIFETSLRRGKFDQSRVLPDGSLMEIKKVYPLDAVFDNPEDVPEDVKANKRYAGSSNWTVQEAAECVRQDFGSIDILVHSLANGPEVSKPLLETSRKGYLAAISASSYSFVSLLSHFLPIMNPGGASISLTYIASERIIPGYGGGMSSAKAALESDTRVLAFEAGRKQNIRVNTISAGPLGSRAAKAIGFIDTMIEYSYNNAPIQKTLTADEVGNAAAFLVSPLASAITGATIYVDNGLNSMGVALDSPVFK
>d1eny__ 3.19.1.2.9 Enoyl-ACP reductase [Mycobacterium tuberculosis, gene InhA]
AGLLDGKRILVSGIITDSSIAFHIARVAQEQGAQLVLTGFDRLRLIQRITDRLPAKAPLLELDVQNEEHLASLAGRVTEAIGAGNKLDGVVHSIGFMPQTGMGINPFFDAPYADVSKGIHISAYSYASMAKALLPIMNPGGSIVGMDFDPSRAMPAYNWMTVAKSALESVNRFVAREAGKYGVRSNLVAAGPIRTLAMSAIVGGALGEEAGAQIQLLEEGWDQRAPIGWNMKDATPVAKTVCALLSDWLPATTGDIIYADGGAHTQLL
>d1gado1 3.19.1.3.1 (2-148,313-330) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) [Escherichia coli]
IKVGINGFGRIGRIVFRAAQKRSDIEIVAINDLLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDNTPMFVKGANFDKYAGQDIVSNA
>d1dih_1 3.19.1.3.10 (1-129,240-272) Dihydrodipicolinate reductase [Escherichia coli]
HDANIRVAIAGAGGRMGRQLIQAALALEGVQLGAALEREGSSLLGSDAGELAGAGKTGVTVQSSLDAVKDDFDVFIDFTRPEGTLNHLAFCRQHGKGMVIGTTGFDEAGKQAIRDAAADIAIVFAANF
>d1ofga1 3.19.1.3.11 (1-160,323-381) glucose-fructose oxidoreductase, N-terminal domain [Zymomonas mobilis]
ATLPAGASQVPTTPAGRPMPYAIRPMPEDRRFGYAIVGLGKYALNQILPGFAGCQHSRIEALVSGNAEKAKIVAAEYGVDPRKIYDYSNFDKIAKDPKIDAVYIILPNSLHAEFAIRAFKAGKHVMCEKPMATSVADCQRMIDAAKAANKKLMIGYRCH
>d1dpga1 3.19.1.3.12 (1-181,413-426) glucose 6-phosphate dehydrogenase, N-terminal domain [Leuconostoc mesenteroides]
VSEIKTLVTFFGGTGDLAKRKLYPSVFNLYKKGYLQKHFAIVGTARQALNDDEFKQLVRDCIKDFTDDQAQAEAFIEHFSYRAHDVTDAASYAVLKEAIEEAADKFDIDGNRIFYMSVAPRFFGTIAKYLKSEGLLADTGYNRLMIEKPFGTSYDTAAELQNDLENAFDDNQLFRIDHYL
>d1gd1o1 3.19.1.3.2 (2-150,314-334) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) [Bacillus stearothermophilus /nca 1503]
VKVGINGFGRIGRNVFRAALKNPDIEVVAVNDLTDANTLAHLLKYDSVHGRLDAEVSVNGNNLVVNGKEIIVKAERDPENLAWGEIGVDIVVESTGRFTKREDAAKHLEAGAKKVIISAPAKNEDITIVMGVNQDKYDPKAHHVISNA
>d1cero1 3.19.1.3.3 (1-148,311-331) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) [Thermus aquaticus]
MKVGINGFGRIGRQVFRILHSRGVEVALINDLTDNKTLAHLLKYDSIYHRFPGEVAYDDQYLYVDGKAIRATAVKDPKEIPWAEAGVGVVIESTGVFTDADKAKAHLEGGAKKVIITAPAKGEDITIVMGVNHEAYDPSRHHIISNA
>d1hdgo1 3.19.1.3.4 (1-150,314-332) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) [Thermotoga maritima]
ARVAINGFGRIGRLVYRIIYERKNPDIEVVAINDLTDTKTLAHLLKYDSVHKKFPGKVEYTENSLIVDGKEIKVFAEPDPSKLPWKDLGVDFVIESTGVFRNREKAELHLQAGAKKVIITAPAKGEDITVVIGCNEDQLKPEHTIISCA
>d1ggao1 3.19.1.3.5 (1-164,334-358) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) [Trypanosoma brucei brucei, glycosome]
TIKVGINGFGRIGRMVFQALCDDGLLGNEIDVVAVVDMNTDARYFAYQMKYDSVHGKFKHSVSTTKSKPSVAKDDTLVVNGHRILCVKAQRNPADLPWGKLGVEYVIESTGLFTVKSAAEGHLRGGARKVVISAPASGGAKTFVMGVNHNNYNPREQHVVSNA
>d1gypa1 3.19.1.3.6 (1-165,335-358) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) [Leishmania mexicana]
APIKVGINGFGRIGRMVFQAICDQGLIGTEIDVVAVVDMSTNAEYFAYQMKHDTVHGRPKYTVEAVKSSPSVETADVLVVNGHRIKCVKAQRNPADLPWGKLGVDYVIESTGLFTDKLKAEGHIKGGAKKVVISAPASGGAKTIVMGVNQHEYSPASHHVVSNA
>d1gpdg1 3.19.1.3.7 (1-147,312-333) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) [lobster (Homarus americanus)]
SKIGINGFGRIGRLVLRAALSCGAQVVAVNDPFIALEYMVYMFKYDSTHGVFKGEVKMEDGALVVDGKKITVFNEMKPENIPWSKAGAEYIVESTGVFTTIEKASAHFKGGAKKVVISAPSADAPMFVCGVNLEKYSKDMTVVSNA
>d3gpdr1 3.19.1.3.8 (1-150,315-334) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) [human (Homo sapiens)]
GKVKVGVDGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLHYMVYMFQYDSTHGKFHGTVKAEDGKLVIDGKAITIFQERDPENIKWGDAGTAYVVESTGVFTTMEKAGAHLKGGAKRIVISAPSADAPMFVMGVNHFKYANSLKIISNA
>d1dapa1 3.19.1.3.9 (1-118,269-320) Diaminopimelic acid dehydrogenase (DAPDH) [Corynebacterium glutamicum]
MTNIRVAIVGYGNLGRSVEKLIAKQPDMDLVGIFSRRATLDTKTPVFDVADVDKHADDVDVLFLCMGSATDIPEQAPKFAQFACTVDTYDNHRDIPRHRQVMNEAATAAGNVALVST
>d2naca2 3.19.1.4.1 (148-335) Formate dehydrogenase [Pseudomonas sp. 101]
ISVAEHVVMMILSLVRNYLPSHEWARKGGWNIADCVSHAYDLEAMHVGTVAAGRIGLAVLRRLAPFDVHLHYTDRHRLPESVEKELNLTWHATREDMYPVCDVVTLNCPLHPETEHMINDETLKLFKRGAYIVNTARGKLCDRDAVARALESGRLAGYAGDVWFPQPAPKDHPWRTMPYNGMTPHISG
>d1dxy_2 3.19.1.4.2 (101-330) D-2-hydroxyisocaproate dehydrogenase [Lactobacillus casei]
SPAAIAEFALTDTLYLLRNMGKVQAQLQAGDYEKAGTFIGKELGQQTVGVMGTGHIGQVAIKLFKGFGAKVIAYDPYPMKGDHPDFDYVSLEDLFKQSDVIDLHVPGIEQNTHIINEAAFNLMKPGAIVINTARPNLIDTQAMLSNLKSGKLAGVGIDTYEYETEDLLNLAKHGSFKDPLWDELLGMPNVVLSPHIAYYTETAVHNMVYFSLQHLVDFLTKGETSTEVTG
>d1gdha2 3.19.1.4.3 (100-290) D-glycerate dehydrogenase [Hyphomicrobium methylovorum]
VTVATAEIAMLLLLGSARRAGEGEKMIRTRSWPGWEPLELVGEKLDNKTLGIYGFGSIGQALAKRAQGFDMDIDYFDTHRASSSDEASYQATFHDSLDSLLSVSQFFSLNAPSTPETRYFFNKATIKSLPQGAIVVNTARGDLVDNELVVAALEAGRLAYAGFDVFAGEPNINEGYYDLPNTFLFPHIGSA
>d1psda2 3.19.1.4.4 (102-289) Phosphoglycerate dehydrogenase [Escherichia coli]
NTRSVAELVIGELLLLLRGVPEANAKAHRGVWNKLAAGSFEARGKKLGIIGYGHIGTQLGILAESLGMYVYFYDIENKLPLGNATQVQHLSDLLNMSDVVSLHVPENPSTKNMMGAKEISLMKPGSLLINASRGTVVDIPALCDALASKHLAGAAIDVFPTEPATNSDPFTSPLCEFDNVLLTPHIGG
>d2dlda2 3.19.1.4.5 (104-300) D-lactate dehydrogenase [Lactobacillus helveticus]
PNAIAEHAAIQAARVLRQDKRMDEKMAKRDLRWAPTIGREVRDQVVGVVGTGHIGQVFMRIMEGFGAKVIAYDIFKNPELEKKGYYVDSLDDLYKQADVISLHVPDVPANVHMINDKSIAEMKDGVVIVNCSRGRLVDTDAVIRGLDSGKIFGFVMDTYEDEVGVFNKDWEGKEFPDKRLADLIDRPNVLVTPHTAF
>d4mdha1 3.19.1.5.1 (1-154) Malate dehydrogenase [porcine (Sus scrofa)]
SEPIRVLVTGAAGQIAYSLLYSIGNGSVFGKDQPIILVLLDITPMMGVLDGVLMELQDCALPLLKDVIATDKEEIAFKDLDVAILVGSMPRRDGMERKDLLKANVKIFKCQGAALDKYAKKSVKVIVVGNPANTNCLTASKSAPSIPKENFSCL
>d1mlda1 3.19.1.5.1 (1-144) Malate dehydrogenase [porcine (Sus scrofa)]
AKVAVLGASGGIGQPLSLLLKNSPLVSRLTLYDIAHTPGVAADLSHIETRATVKGYLGPEQLPDCLKGCDVVVIPAGVPRKPGMTRDDLFNTNATIVATLTAACAQHCPDAMICIISNPVNSTIPITAEVFKKHGVYNPNKIFG
>d1ldb_1 3.19.1.5.10 (1-138) Lactate dehydrogenase [Bacillus stearothermophilus]
MKNNGGARVVVIGAGFVGASYVFALMNQGIADEIVLIDANESKAIGDAMDFNHGKVFAPKPVDIWDYDDCRDADLVVICAGANDLVDKNIAIFRSIVESVMASGFQGLFLVATNPVDILTYATWKFSGLPHERVIGSG
>d1ldna1 3.19.1.5.10 (1-148) Lactate dehydrogenase [Bacillus stearothermophilus]
MKNNGGARVVVIGAGFVGASYVFALMNQGIADEIVLIDANESKAIGDAMDFNHGKVFAPKPVDIWHGDYDDCRDADLVVICAGANQKPGETRLDLVDKNIAIFRSIVESVMASGFQGLFLVATNPVDILTYATWKFSGLPHERVIGSG
>d1llc_1 3.19.1.5.11 (1-149) Lactate dehydrogenase [Lactobacillus casei]
ASITDKDHQKVILVGDGAVGSSYAFAMVLQGIAQEIGIVDIFKDKTKGDAIDLSNALPFTSPKKIYSAEYSDAKDADLVVITAGAPKQPGETRLDLVNKNLKILKSIVDPIVDSGFNLIFLVAANPVDILTYATWKLSGFPKNRVVGSG
>d1llda1 3.19.1.5.12 (1-143) Lactate dehydrogenase [Bifidobacterium longum, strain am101-2]
PTKLAVIGAGAVGSTLAFAAAQRGIAREIVLEDIAKERVEAEVLDMQHGSSFYPTVSIDGSDDPEICRDADMVVITAGPRQKPGQSRLELVGATVNILKAIMPNLVKVAPNAIYMLITNPVDIATHVAQKLTGLPENQIFGSG
>d2cmd_1 3.19.1.5.2 (1-145) Malate dehydrogenase [Escherichia coli]
MKVAVLGAAGGIGQALALLLKTQLPSGSELSLYDIAPVTPGVAVDLSHIPTAVKIKGFSGEDATPALEGADVVLISAGVRRKPGMDRSDLFNVNAGIVKNLVQQVAKTCPKACIGIITNPVNTTVAIAAEVLKKAGVYDKNKLFG
>d1bdma1 3.19.1.5.3 (2-145) Malate dehydrogenase [Thermus flavus]
KAPVRVAVTGAAGQIGYSLLFRIAAGEMLGKDQPVILQLLEIPQAMKALEGVVMELEDCAFPLLAGLEATDDPDVAFKDADYALLVGAAPLQVNGKIFTEQGRALAEVAKKDVKVLVVGNPANTNALIAYKNAPGLNPRNFTAM
>d1hlpa1 3.19.1.5.4 (1-128) Malate dehydrogenase [Haloarcula marismortui]
TKVSVVGAAGTVGAAAGYNIALRDIADEVVFVDIPDKEDDTVGQAADTNHGIAYDSNTRVRQGGYEDTAGSDVVVITAGIPRQPGQTRIDLAGDNAPIMEDIQSSLDEHNDDYISLTTSNPVDLLNRH
>d1hyha1 3.19.1.5.5 (1-139) L-2-hydroxyisocapronate dehydrogenase, L-HICDH [Lactobacillus confusus]
ARKIGIIGLGNVGAAVAHGLIAQGVADDYVFIDANEAKVKADQIDFQDAMANLEAHGNIVINDWAALADADVVISTLGNIKLQQFAELKFTSSMVQSVGTNLKESGFHGVLVVISNPVDVITALFQHVTGFPAHKVIGT
>d9ldta1 3.19.1.5.6 (1-159) Lactate dehydrogenase [porcine (Sus scrofa)]
ATLKDQLIHNLLKEEHVPHNKITVVGVGAVGMACAISILMKELADEIALVDVMEDKLKGEMMDLQHGSLFLRTPKIVSGKDYNVTANSRLVVITAGARQQEGESRLNLVQRNVNIFKFIIPNIVKYSPNCKLLVVSNPVDILTYVAWKISGFPKNRVIG
>d5ldh_1 3.19.1.5.6 (1-160) Lactate dehydrogenase [porcine (Sus scrofa)]
ATLKEKLIAPVAQQETTIPDNKITVVGVGQVGMACAISILGKSLTDELALVDVLEDKLKGEMMDLQHGSLFLQTPKIVANKDYSVTANSKIVVVTAGVRQQEGESRLNLVQRNVNVFKFIIPQIVKYSPNCIIIVVSNPVDILTYVAWKLSGLPKHRVIG
>d2ldx_1 3.19.1.5.7 (1-159) Lactate dehydrogenase [mouse (Mus musculus)]
STVKEQLIQNLVPEDKLSRCKITVVGVGDVGMACAISILLKGLADELALVDADTDKLRGEALDLQHGSLFLSTPKIVFGKDYNVSANSKLVIITAGARMVSGQTRLDLLQRNVAIMKAIVPGVIQNSPDCKIIVVTNPVDILTYVVWKISGFPVGRVIG
>d1ldm_1 3.19.1.5.8 (1-160) Lactate dehydrogenase [dogfish (Squalus acanthias)]
ATLKDKLIGHLATSQEPRSYNKITVVGVGAVGMACAISILMKDLADEVALVDVMEDKLKGEMMDLQHGSLFLHTAKIVSGKDYSVSAGSKLVVITAGARQQEGESRLNLVQRNVNIFKFIIPNIVKHSPDCIILVVSNPVDVLTYVAWKLSGLPMHRIIG
>d1ldg_1 3.19.1.5.9 (1-149) Lactate dehydrogenase [malarial parasite (Plasmodium falciparum)]
APKAKIVLVGSGMIGGVMATLIVQKNLGDVVLFDIVKNMPHGKALDTSHTNVMAYSNCKVSGSNTYDDLAGSDVVIVTAGFTKAPGKSDKEWNRLDLLPLNNKIMIEIGGHIKKNCPNAFIIVVTNPVDVMVQLLHQHSGVPKNKIIGL
>d1yvei2 3.19.1.6.1 (1-225) Acetohydroxy acid isomeroreductase, ketoacid reductoisomerase (KARI) [spinach (Spinacia oleracea)]
ATTFDFDSSVFKKEKVTLSGHDEYIVRGGRNLFPLLPDAFKGIKQIGVIGWGSQAPAQAQNLKDSLTEAKSDVVVKIGLRKGSNSFAEARAAGFSEENGTLGDMWETISGSDLVLLLISDSAQADNYEKVFSHMKPNSILGLSHGFLLGHLQSLGQDFPKNISVIAVCPKGMGPSVRRLYVQGKEVNGAGINSSFAVHQDVDGRATDVALGWSIALGSPFTFATT
>d2pgd_2 3.19.1.6.2 (1-176) 6-phosphogluconate dehydrogenase [sheep (Ovis orientalis aries)]
AQADIALIGLAVMGQNLILNMNDHGFVVCAFNRTVSKVDDFLANEAKGTKVLGAHSLEEMVSKLKKPRRIILLVKAGQAVDNFIEKLVPLLDIGDIIIDGGNSEYRDTMRRCRDLKDKGILFVGSGVSGGEDGARYGPSLMPGGNKEAWPHIKAIFQGIAAKVGTGEPCCDWVGDD
>d1hrda1 3.19.1.7.1 (195-449) Glutamate dehydrogenase, C-terminal domain [Clostridium symbiosum]
KARSFGGSLVRPEATGYGSVYYVEAVMKHENDTLVGKTVALAGFGNVAWGAAKKLAELGAKAVTLSGPDGYIYDPEGITTEEKINYMLEMRASGRNKVQDYADKFGVQFFPGEKPWGQKVDIIMPCATQNDVDLEQAKKIVANNVKYYIEVANMPTTNEALRFLMQQPNMVVAPSKAVNAGGVLVSGFEMSQNSERLSWTAEEVDSKLHQVMTDIHDGSAAAAERYGLGYNLVAGANIVGFQKIADAMMAQGIAW
>d1gtma1 3.19.1.7.2 (179-417) Glutamate dehydrogenase, C-terminal domain [Pyrococcus furiosis]
GGSLGRIEATARGASYTIREAAKVLGWDTLKGKTIAIQGYGNAGYYLAKIMSEDFGMKVVAVSDSKGGIYNPDGLNADEVLKWKNEHGSVKDFPGATNITNEELLELEVDVLAPAAIEEVITKKNADNIKAKIVAEVANGPVTPEADEILFEKGILQIPDFLCNAGGVTVSYFEWVQNITGYYWTIEEVRERLDKKMTKAFYDVYNIAKEKNIHMRDAAYVVAVQRVYQAMLDRGWVKH
>d1leha1 3.19.1.7.3 (135-364) Leucine dehydrogenase, C-terminal domain [Bacillus sphaericus]
GISPAFGSSGNPSPVTAYGVYRGMKAAAKEAFGSDSLEGLAVSVQGLGNVAKALCKKLNTEGAKLVVTDVNKAAVSAAVAEEGADAVAPNAIYGVTCDIFAPCALGAVLNDFTIPQLKAKVIAGSADNQLKDPRHGKYLHELGIVYAPDYVINAGGVINVADELYGYNRTRAMKRVDGIYDSIEKIFAISKRDGVPSYVAADRMAEERIAKVAKARSQFLQDQRNILNGR
>d1scua2 3.19.1.8.1 (1-121) Succinyl-CoA synthetase, alpha-chain, N-terminal (CoA-binding) domain [Escherichia coli]
SILIDKNTKVICQGFTGSQGTFHSEQAIAYGTKMVGGVTPGKGGTTHLGLPVFNTVREAVAATGATASVIYVPAPFCKDSILEAIDAGIKLIITITEGIPTLDMLTVKVKLDEAGVRMIGP
>d1tml__ 3.2.1.1.1 Cellulase E2 [Thermomonospora fusca, strain yx]
NDSPFYVNPNMSSAEWVRNNPNDPRTPVIRDRIASVPQGTWFAHHNPGQITGQVDALMSAAQAAGKIPILVVYNAPGRDCGNHSSGGAPSHSAYRSWIDEFAAGLKNRPAYIIVEPDLISLMSSCMQHVQQEVLETMAYAGKALKAGSSQARIYFDAGHSAWHSPAQMASWLQQADISNSAHGIATNTSNYRWTADEVAYAKAVLSAIGNPSLRAVIDTSRNGNGPAGNEWCDPSGRAIGTPSTTNTGDPMIDAFLWIKLPGEADGCIAGAGQFVPQAAYEMAIAA
>d1cb2a_ 3.2.1.1.2 Cellobiohydrolase II [Trichoderma reesei]
TATYSGNPFVGVTPWANAYYASEVSSLAIPSLTGAMATAAAAVAKVPSFMWLDTLDKTPLMEQTLADIRTANKNGGNYAGQFVVFDLPDRDCAALASNGEYSIADGGVAKYKNYIDTIRQIVVEYSDIRTLLVIEPDSLANLVTNLGTPKCANAQSAYLECINYAVTQLNLPNVAMYLDAGHAGWLGWPANQDPAAQLFANVYKNASSPRALRGLATNVANYNGWNITSPPSYTQGNAVYNEKLYIHAIGPLLANHGWSNAFFITDQGRSGKQPTGQQQWGDWCNVIGTGFGIRPSANTGDSLLDSFVWVKPGGECDGTSDSSAPRFDSHCALPDALQPAPQAGAWFQAYFVQLLTNANPSFL
>d1bnca2 3.20.1.1.1 (1-114) Biotin carboxylase subunit of acetyl-CoA carboxylase [Escherichia coli]
MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHPGYGFLSENANFAEQVERSGFIFIGPKAETIRLMG
>d2dln_1 3.20.1.2.1 (1-96) D-Ala-D-Ala ligase, N-terminal domain [Escherichia coli, gene ddlB]
MTDKIAVLLGGTSAEREVSLNSGAAVLAGLREGGIDAYPVDPKEVDVTQLKSMGFQKVFIALHGRGGEDGTLQGMLELMGLPYTGSGVMASALSMD
>d2glt_1 3.20.1.3.1 (1-122) Glutathione synthetase, N-terminal domain [Escherichia coli]
MIKLGIVMDPIANINIKKDSSFAMLLEAQRRGYELHYMEMGDLYLINGEARAHTRTLNVKQNYEEWFSFVGEQDLPLADLDVILMRKDPPFDTEFIYATYILERAEEKGTLIVNKPQSLRDC
>d1pvda1 3.21.1.1.2 (173-341) Pyruvate decarboxylase [baker's yeast (Saccharomyces cerevisiae)]
QTPIDMSLKPNDAESEKEVIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLTQFPAFVTPMGKGSISEQHPRYGGVYVGTLSKPEVKEAVESADLILSVGALLSDKTKNIVEFHSDHMKIRNATFPGVQMKFVLQKLLTNIADAAKGYKPVAVPARTPANAAVP
>d1poxa1 3.21.1.1.3 (175-357) Pyruvate oxidase [Lactobacillus plantarum]
YASANNYQTPLLPEPDVQAVTRLTQTLLAAERPLIYYGIGARKAGKELEQLSKTLKIPLMSTYPAKGIVADRYPAYLGSANRVAQKPANEALAQADVVLFVGNNYPFAEVSKAFKNTRYFLQIDIDPAKLGKRHKTDIAVLADAQKTLAAILAQVSERESTPWWQANLANVKNWRAYLASLED
>d1nbaa_ 3.22.1.1.1 N-carbamoylsarcosine amidohydrolase [Arthrobacter sp.]
TFNDIEARLAAVLEEAFEAGTSIYNERGFKRRIGYGNRPAVIHIDLANAWTQPGHPFSCPGMETIIPNVQRINEAARAKGVPVFYTTNVYRNRDASSGTNDMGLWYSKIPTETLPADSYWAQIDDRIAPADGEVVIEKNRASAFPGTNLELFLTSNRIDTLIVTGATAAGCVRHTVEDAIAKGFRPIIPRETIGDRVPGVVQWNLYDIDNKFGDVESTDSVVQYLDALPQFEDTVPKTLSDPQPEVEAPADPV
>d1deaa_ 3.23.1.1.1 Glucosamine 6-phosphate deaminase [Escherichia coli]
MRLIPLTTAEQVGKWAARHIVNRINAFKPTADRPFVLGLPTGGTPMTTYKALVEMHKAGQVSFKHVVTFNMDEYVGLPKEHPESYYSFMHRNFFDHVDIPAENINLLNGNAPDIDAECRQYEEKIRSYGKIHLFMGGVGNDGHIAFNEPASSLASRTRIKTLTHDTRVANSRFFDNDVNQVPKYALTVGVGTLLDAEEVMILVLGSQKALALQAAVEGCVNHMWTISCLQLHPKAIMVCDEPSTMELKVKTLRYFNELEAENIKGL
>d1pvda2 3.24.1.1.2 (1-172) Pyruvate decarboxylase [baker's yeast (Saccharomyces cerevisiae)]
SEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGMSCIITTFGVGELSALNGIAGSYAEHVGVLHVVGVPSISHHTLGNGDFTVFHRMSANISETTAMITDIATAPAEIDRCIRTTYVTQRPVYLGLPANLVDLNVPAKLL
>d1pvda3 3.24.1.1.2 (342-537) Pyruvate decarboxylase [baker's yeast (Saccharomyces cerevisiae)]
ASTPLKQEWMWNQLGNFLQEGDVVIAETGTSAFGINQTTFPNNTYGISQVLWGSIGFTTGATLGAAFAAEEIDPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTIEKLIHGPKAQYNEIQGWDHLSLLPTFGAKDYETHRVATTGEWDKLTQDKSFNDNSKIRMIEIMLPVFDAPQNLVKQAKLT
>d1poxa2 3.24.1.1.3 (1-174) Pyruvate oxidase [Lactobacillus plantarum]
TNILAGAAVIKVLEAWGVDHLYGIPGGSINSIMDALSAERDRIHYIQVRHEEVGAMAAAADAKLTGKIGVCFGSAGPGGTHLMNGLYDAREDHVPVLALIGQFGTTGMNMDTFQEMNENPIYADVADYNVTAVNAATLPHVIDEAIRRAYAHQGVAVVQIPVDLPWQQISAEDW
>d1poxa3 3.24.1.1.3 (358-545) Pyruvate oxidase [Lactobacillus plantarum]
KQEGPLQAYQVLRAVNKIAEPDAIYSIDVGDINLNANRHLKLTPSNRHITSNLFATMGVGIPGAIAAKLNYPERQVFNLAGDGGASMTMQDLVTQVQYHLPVINVVFTNCQYGFIKDEQEDTNQNDFIGVEFNDIDFSKIADGVHMQAFRVNKIEQLPDVFEQAKAIAQHEPVLIDAVITGDRPLPAE
>d1trka2 3.24.1.2.1 (336-532) Transketolase [baker's yeast (Saccharomyces cerevisiae)]
LPANWESKLPTYTAKDSAVATRKLSETVLEDVYNQLPELIGGSADLTPSNLTRWKEALDFQPPSSGSGNYSGRYIRYGIREHAMGAIMNGISAFGANYKPYGGTFLNFVSYAAGAVRLSALSGHPVIWVATHDSIGVGEDGPTHQPIETLAHFRSLPNIQVWRPADGNEVSAAYKNSLESKHTPSIIALSRQNLPQL
>d1trka1 3.24.1.2.1 (1-335) Transketolase [baker's yeast (Saccharomyces cerevisiae)]
QFTDIDKLAVSTIRILAVDTVSKANSGHPGAPLGMAPAAHVLWSQMRMNPTNPDWINRDRFVLSNGHAVALLYSMLHLTGYDLSIEDLKQFRQLGSRTPGHPEFELPGVEVTTGPLGQGISNAVGMAMAQANLAATYNKPGFTLSDNYTYVFLGDGCLQEGISSEASSLAGHLKLGNLIAIYDDNKITIDGATSISFDEDVAKRYEAYGWEVLYVENGNEDLAGIAKAIAQAKLSKDKPTLIKMTTTIGYGSLHAGSHSVHGAPLKADDVKQLKSKFGFNPDKSFVVPQEVYDHYQKTILKPGVEANNKWNKLFSEYQKKFPELGAELARRLSGQ
>d1gky__ 3.25.1.1.1 Guanylate kinase [baker's yeast (Saccharomyces cerevisiae)]
SRPIVISGPSGTGKSTLLKKLFAEYPDSFGFSVSSTTRTPRAGEVNGKDYNFVSVDEFKSMIKNNEFIEWAQFSGNYYGSTVASVKQVSKSGKTCILDIDMQGVKSVKAIPELNARFLFIAPPSVEDLKKRLEGRGTETEESINKRLSAAQAELAYAETGAHDKVIVNDDLDKAYKELKDFIFAEK
>d1zin_1 3.25.1.1.10 (1-125,161-217) Adenylate kinase [Bacillus stearothermophilus]
MNLVLMGLPGAGKGTQAEKIVAAYGIPHISTGDMFRAAMKEGTPLGLQAKQYMDRGDLVPDEVTIGIVRERLSKDDCQNGFLLDGFPRTVAQAEALETMLADIGRKLDYVIHIDVRQDVLMERL
>d1ukz__ 3.25.1.1.2 Uridylate kinase [Saccharomyces serevisiae]
PAFSPDQVSVIFVLGGPGAGKGTQCEKLVKDYSFVHLSAGDLLRAEQGRAGSQYGELIKNCIKEGQIVPQEITLALLRNAISDNVKANKHKFLIDGFPRKMDQAISFERDIVESKFILFFDCPEDIMLERLLERGKTSGRSDDNIESIKKRFNTFKETSMPVIEYFETKSKVVRVRCDRSVEDVYKDVQDAIRDSL
>d1deka_ 3.25.1.1.3 Deoxynucleoside monophosphate kinase complexed with deoxy-gmp [(Bacteriophage t4)]
MKLIFLSGVKRSGKDTTADFIMSNYSAVKYQLAGPIKDALAYAWGVFAANTDYPLTRKEFEGIDYDRETNLNLTKLEVITIMEQAFCYLNGKSPIKGVFVFDDEGKESVNFVAFNKITDVINNIEDQWSVRRLMQALGTDLIVNNFDRMYWVKLFALDYLDKFNSGYDYYIVPDTRQDHEMDAARAMGATVIHVVRPGQKSNDTHITEAGLPIRDGDLVITNDGSLEELFSKIKNTLKVL
>d1ukd__ 3.25.1.1.4 UMP/CMP kinase [Dictyostelium discodeum]
EKSKPNVVFVLGGPGSGKGTQCANIVRDFGWVHLSAGDLLRQEQQSGSKDGEMIATMIKNGEIVPSIVTVKLLKNAIDANQGKNFLVDGFPRNEENNNSWEENMKDFVDTKFVLFFDCPEEVMTQRLLKRGESSGRSDDNIESIKKRFNTFNVQTKLVIDHYNKFDKVKIIPANRDVNEVYNDVENLFKSMGF
>d1vtk__ 3.25.1.1.5 Thymidine kinase [Herpes simplex virus type 1, HSV1]
MPTLLRVYIDGPHGMGKTTTTQLLVALGSRDDIVYVPEPMTYWRVLGASETIANIYTTQHRLDQGEISAGDAAVVMTSAQITMGMPYAVTDAVLAPHIGGEAGSPPPALTLIFDRHPIAALLCYPAARYLMGSMTPQAVLAFVALIPPTLPGTNIVLGALPEDRHIDRLAKRQRPGERLDLAMLAAIRRVYGLLANTVRYLQCGGSWREDWGQLSGPRPHIGDTLFTLFRAPELLAPNGDLYNVFAWALDVLAKRLRSMHVFILDYDQSPAGCRDALLQLTSGMVQTHVTTPGSIPTICDLARTFAREMGEAN
>d3adk__ 3.25.1.1.6 Adenylate kinase [porcine (Sus scrofa)]
MEEKLKKSKIIFVVGGPGSGKGTQCEKIVQKYGYTHLSTGDLLRAEVSSGSARGKMLSEIMEKGQLVPLETVLDMLRDAMVAKVDTSKGFLIDGYPREVKQGEEFERKIGQPTLLLYVDAGPETMTKRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAFYEKRGIVRKVNAEGSVDDVFSQVCTHLDTLK
>d1ak2__ 3.25.1.1.7 Adenylate kinase [bovine (Bos taurus) izozymes]
PKGVRAVLLGPPGAGKGTQAPKLAKNFCVCHLATGDMLRAMVASGSELGKKLKATMDAGKLVSDEMVLELIEKNLETPPCKNGFLLDGFPRTVRQAEMLDDLMEKRKEKLDSVIEFSIPDSLLIRRITGRLIHPQSGRSYHEEFNPPKEPMKDDITGEPLIRRSDDNKKALKIRLEAYHTQTTPLVEYYSKRGIHSAIDASQTPDVVFASILAAFSKATS
>d2ak3a_ 3.25.1.1.7 Adenylate kinase [bovine (Bos taurus) izozymes]
GASARLLRAAIMGAPGSGKGTVSSRITKHFELKHLSSGDLLRDNMLRGTEIGVLAKTFIDQGKLIPDDVMTRLVLHELKNLTQYNWLLDGFPRTLPQAEALDRAYQIDTVINLNVPFEVIKQRLTARWIHPGSGRVYNIEFNPPKTMGIDDLTGEPLVQREDDRPETVVKRLKAYEAQTEPVLEYYRKKGVLETFSGTETNKIWPHVYAFLQTKLPQRSQETSVTP
>d1aky__ 3.25.1.1.8 Adenylate kinase [baker's yeast (Saccharomyces cerevisiae)]
ESIRMVLIGPPGAGKGTQAPNLQERFHAAHLATGDMLRSQIAKGTQLGLEAKKIMDQGGLVSDDIMVNMIKDELTNNPACKNGFILDGFPRTIPQAEKLDQMLKEQGTPLEKAIELKVDDELLVARITGRLIHPASGRSYHKIFNPPKEDMKDDVTGEALVQRSDDNADALKKRLAAYHAQTEPIVDFYKKTGIWAGVDASQPPATVWADILNKLGKN
>d1akea_ 3.25.1.1.9 Adenylate kinase [Escherichia coli]
MRIILLGAPGAGKGTQAQFIMEKYGIPQISTGDMLRAAVKSGSELGKQAKDIMDAGKLVTDELVIALVKERIAQEDCRNGFLLDGFPRTIPQADAMKEAGINVDYVLEFDVPDELIVDRIVGRRVHAPSGRVYHVKFNPPKVEGKDDVTGEELTTRKDDQEETVRKRLVEYHQMTAPLIGYYSKEAEAGNTKYAKVDGTKPVAEVRADLEKILG
>d5p21__ 3.25.1.3.1 cH-p21 Ras protein [human (Homo sapiens)]
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQH
>d1guaa_ 3.25.1.3.10 Rap1A [Human (Homo sapiens)]
MREYKLVVLGSGGVGKSALTVQFVQGIFVDEYDPTIEDSYRKQVEVDCQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDERVVGKEQGQNLARQWCNCAFLESSAKSKINVNEIFYDLVRQINR
>d1tada2 3.25.1.3.2 (1-30,152-316) Transducin (alpha subunit) [bovine (Bos taurus)]
ARTVKLLLLGAGESGKSTIVKQMKIIHQDGWIHCFEGVTCIIFIAALSAYDMVLVEDDEVNRMHESLHLFNSICNHRYFATTSIVLFLNKKDVFSEKIKKAHLSICFPDYNGPNTYEDAGNYIKVQFLELNMRRDVKEIYSHMTCATDTQNVKFVFDAVTDIII
>d1gia_2 3.25.1.3.3 (1-27,149-310) Transducin (alpha subunit) [rat (Rattus rattus)]
VKLLLLGAGESGKSTIVKQMKIIHEAGCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVI
>d1gota2 3.25.1.3.3 (1-54,171-326) Transducin (alpha subunit) [rat (Rattus rattus)]
SAEEKHSRELEKKLKEDAEKDARTVKLLLLGAGESGKSTIVKQKIIHQDGYSLEFKDLNFRFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEENRHESKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNT
>d1hura_ 3.25.1.3.4 ADP-ribosylation factor 1 (ARF1) [human (Homo sapiens)]
GNIFANLFKGLFGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLSNQLRNQK
>d1etu__ 3.25.1.3.6 Elongation factor Tu (EF-Tu), the N-terminal (G) domain [Escherichia coli]
FERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGDAEWEAKILELAGFLDSYIP
>d1eft_3 3.25.1.3.7 (1-212) Elongation factor Tu (EF-Tu), the N-terminal (G) domain [Thermus aquaticus]
AKGEFIRTKPHVNVGTIGHVDHGKTTLTAALTFVTAAENPNVEVKDYGDIDKAPEERARGITINTAHVEYETAKRHYSHVDCPGHADYIKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFMNKVDMVDDPELLDLVEMEVRDLLNQYEFPGDEVPVIRGSALLALEEMHKNPKTKRGENEWVDKIWELLDAIDEYIPT
>d1dar_2 3.25.1.3.9 (1-254) Elongation factor G (EF-G), the N-terminal (G) domain [Thermus thermophilus]
MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRAAVTTCFWKDHRINIIDTPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSETVWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDVLRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEEELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPS
>d2mysa2 3.25.1.4.1 (1-28,70-669) Myosin S1, motor domain [chicken (Gallus gallus) pectoral muscle]
DAEMAAFGEAAPYLRSEKERIEAQNPFDMIYTYSGLFCVTVNPYWLPVYNPVVLAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTRVIQYFATIAASGEGTLEDQIISANPLLEAFGNATVRNDNSSRFGFIRIHFGATGKLASADIETYLLESRVTFQLPAERSYHIFYQIMSNPELIDMLLITTNPYDYHYVSEGEITVPSIDDQEELMATDSAIDILGFSADETAIYLTGAVMHYGNLKFQQREEQAEPDGTEVADAAYLMGLNSAELLKALCYPRVGVGNEAVTGETVSEVHNSVGALAAVYEMFLWMVIRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNELQQFFNHHMFVLEQEEYEGIEWEFIDFGMDLAACIELIEPMGIFSILEEECMFPKATDTSFNLYDEHLGKSNNFQKPKPAAEAHFSLVHYAGTVDYNISGWLENDPLNETVIGLYQSSVTLALLFATYQTVSALFRENLNLMANLRSTHPHFVRCIIPNETTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRVLYADFKQRYRVLNASAMDSKKASEKLLGG
>d1mmd_2 3.25.1.4.2 (1-32,79-743) Myosin S1, motor domain [Dictyostelium discoideum]
NPIHDRTSDYHKYLKVKQGDSDLFKLTVSDKRRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGESGAGKTENTKKVIQYLASVAGRNQAGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNNAGFISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIKGVSDEDEFKITRQAMDIVGFSQEEQMSIFKIIAGILHLGNIKFEKGAGEGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSSSSRDALVKALYGRLFLWLVKKINNVLCSERAAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKVEQEEYLKEKINLDSQATIDLIDGRQPPGILALLDEQSVFPNATDNTLITKLHSHFSKKNAKYEEPRFSKTEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIASRAFITVAAQYKEQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRDAEDSQKATDAVLKHLNIDPEQYRFGITKIFFRAGQLAR
>d1dts__ 3.25.1.5.1 Dethiobiotin synthetase [Escherichia coli]
SKRYFVTGTDTEVGKTVASCALLQAAKAAGYRTAGYKPVASGSEKTPEGLRNSDALALQRNSSLQLDYATVNPYTFAEPTSPHIISAQEGRPIESLVMSAGLRALEQQADWVLVEGAGGWFTPLSDTFTFADWVTQEQLPVILVVGVKLGCINHAMLTAQVIQHAGLTLAGWVANDVTPPGKRHAEYMTTLTRMIPAPLLGEIPWLAEAATGKYINLALL
>d1adea_ 3.25.1.5.2 Adenylosuccinate synthetase (gene purA product) [Escherichia coli]
GNNVVVLGTQWGDEGKGKIVDLLTERAKYVVRYQGGHNAGHTLVINGEKTVLHLIPSGILRENVTSIIGNGVVLSPAALMKEMKELEDRGIPVRERLLLSEACPLILDYHVALDNAREKARGAKAIGTTGRGIGPAYEDKVARRGLRVGDLFDKETFAEKLKEVMEYHNFQLVNYYKAEAVDYQKVLDDTMAVADILTSMVVDVSDLLDQARQRGDFVMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVATGSGLGPRYVDYVLGILKAYSTRVGAGPFPTELFDETGEFLCKQGNEFGATTGRRRRTGWLDTVAVRRAVQLNSLSGFCLTKLDVLDGLKEVKLCVAYRMPDGREVTTTPLAADDWKGVEPIYETMPGWSESTFGVKDRSGLPQAALNYIKRIEELTGVPIDIISTGPDRTETMILRDPFDA
>d1nipa_ 3.25.1.5.3 Nitrogenase iron protein [Azotobacter vinelandii]
AMRQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHSKAQNTIMEMAAEAGTVEDLELEDVLKAGYGGVKCVESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYDVLGDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAANNISKGIVKYANSGSVRLGGLICNSRNTDREDELIIALANKLGTQMIHFVPRDNVVQRAEIRRMTVIEYDPKAKQADEYRALARKVVDNKLLVIPNPITMDELEELLMEFGIMEVEDESIVG
>d2reb_1 3.25.1.6.1 (1-243) RecA protein, ATPase-domain [Escherichia coli]
DENKQKALAAALGQIEKQFGKGSIMRLGEDRSMDVETISTGSLSLDIALGAGGLPMGRIVEIYGPESSGKTTLTLQVIAAAQREGKTCAFIDAEHALDPIYARKLGVDIDNLLCSQPDTGEQALEICDALARSGAVDVIVVDSVAALTPKAEIEGLAARMMSQAMRKLAGNLKQSNTLLIFINQTGGNALKFYASVRLDIRRIGAVKEGENVVGSETRVKVVKNKIAAPFKQAEFQILYGEGI
>d1bmfa3 3.25.1.6.2 (72-356) central domain of alpha and beta subunits of F1 ATP synthase [bovine (Bos taurus)]
VDVPVGEELLGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQ
>d1bmfd3 3.25.1.6.2 (74-349) central domain of alpha and beta subunits of F1 ATP synthase [bovine (Bos taurus)]
IRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRI
>d1ble__ 3.26.1.1.1 Fructose permease, subunit IIb [Bacillus subtilis]
MNIVLARIDDRFIHGQILTRWIKVHAADRIIVVSDDIAQDEMRKTLILSVAPSNVKASAVSVSKMAKAFHSPRYEGVTAMLLFENPSDIVSLIEAGVPIKTVNVGGMRFENHRRQITKSVSVTEQDIKAFETLSDKGVKLELRQLPSDASEDFVQILRNVT
>d1chd__ 3.27.1.1.1 CheB methylesterase domain (C-terminal residues 152-349) [Salmonella typhimurium]
LLSSEKLIAIGASTGGTEAIRHVLQPLPLSSPAVIITQHMPPGFTRSFAERLNKLCQISVKEAEDGERVLPGHAYIAPGDKHMELARSGANYQIKIHDGPPVNRHRPSVDVLFHSVAKHAGRNAVGVILTGMGNDGAAGMLAMYQAGAWTIAQNEASCVVFGMPREAINMGGVSEVVDLSQVSQQMLAKISAGQAIRI
>d1csee_ 3.28.1.1.1 Subtilisin Carlsberg [Bacillus subtilis]
AQTVPYGIPLIKADKVQAQGFKGANVKVAVLDTGIQASHPDLNVVGGASFVAGEAYNTDGNGHGTHVAGTVAALDNTTGVLGVAPSVSLYAVKVLNSSGSGSYSGIVSGIEWATTNGMDVINMSLGGASGSTAMKQAVDNAYARGVVVVAAAGNSGNSGSTNTIGYPAKYDSVIAVGAVDSNSNRASFSSVGAELEVMAPGAGVYSTYPTNTYATLNGTSMASPHVAGAAALILSKHPNLSASQVRNRLSSTATYLGSSFYYGKGLINVEAAAQ
>d1thm__ 3.28.1.1.3 Thermitase [Thermoactinomyces vulgaris]
YTPNDPYFSSRQYGPQKIQAPQAWDIAEGSGAKIAIVDTGVQSNHPDLAGKVVGGWDFVDNDSTPQNGNGHGTHCAGIAAAVTNNSTGIAGTAPKASILAVRVLDNSGSGTWTAVANGITYAADQGAKVISLSLGGTVGNSGLQQAVNYAWNKGSVVVAAAGNAGNTAPNYPAYYSNAIAVASTDQNDNKSSFSTYGSWVDVAAPGSSIYSTYPTSTYASLSGTSMATPHVAGVAGLLASQGRSASNIRAAIENTADKISGTGTYWAKGRVNAYKAVQY
>d1st3__ 3.28.1.1.5 Subtilisin BL [Bacillus lentus]
GQSVPWGISRVQAPAAHNRGLTGSGVKVAVLDTGISTHPDLNIRGGASFVPGEPSTQDGNGHGTHVAGTIAALNNSIGVLGVAPSAELYAVKVLGADGRGAISSIAQGLEWAGNNGMHVANLSLGSPSPSATLEQAVNSATSRGVLVVAASGNSGASSISYPARYANAMAVGATDQNNNRASFSQYGAGLDIVAPGVNVQSTYPGSTYASLNGTSMATPHVAGAAALVKQKNPSWSNVQIRNHLKNTATSLGSTNLYGSGLVNAEAATR
>d1sup__ 3.28.1.1.6 Subtilisin Novo/PBN' [Bacillus amyloliquefaciens]
AQSVPYGVSQIKAPALHSQGYTGSNVKVAVIDSGIDSSHPDLKVAGGASMVPSETNPFQDNNSHGTHVAGTVAALNNSIGVLGVAPSASLYAVKVLGADGSGQYSWIINGIEWAIANNMDVINMSLGGPSGSAALKAAVDKAVASGVVVVAAAGNEGTSGSSSTVGYPGKYPSVIAVGAVDSSNQRASFSSVGPELDVMAPGVSIQSTLPGNKYGAYNGTSMASPHVAGAAALILSKHPNWTNTQVRSSLENTTTKLGDSFYYGKGLINVQAAAQ
>d2pkc__ 3.28.1.1.7 Proteinase K [fungus (Tritirachium album limber)]
AAQTNAPWGLARISSTSPGTSTYYYDESAGQGSCVYVIDTGIEASHPEFEGRAQMVKTYYYSSRDGNGHGTHCAGTVGSRTYGVAKKTQLFGVKVLDDNGSGQYSTIIAGMDFVASDKNNRNCPKGVVASLSLGGGYSSSVNSAAARLQSSGVMVAVAAGNNNADARNYSPASEPSVCTVGASDRYDRRSSFSNYGSVLDIFGPGTSILSTWIGGSTRSISGTSMATPHVAGLAAYLMTLGKTTAASACRYIADTANKGDLSNIPFGTVNLLAYNNYQA
>d1meea_ 3.28.1.1.8 Messentericopeptidase [Bacillus mesentericus]
AQSVPYGISQIKAPALHSQGYTGSNVKVAVIDSGIDSSHPDLNVRGGASFVPSETNPYQDGSSHGTHVAGTIAALNNSIGVLGVAPSASLYAVKVLDSTGSGQYSWIINGIEWAISNNMDVINMSLGGPTGSTALKTVVDKAVSSGIVVAAAAGNEGSSGSTSTVGYPAKYPSTIAVGAVNSANQRASFSSAGSELDVMAPGVSIQSTLPGGTYGAYNGTSMATPHVAGAAALILSKHPTWTNAQVRDRLESTATYLGSSFYYGKGLINVQAAAQ
>d1rlaa_ 3.29.1.1.1 Arginase [rat (Rattus norvegicus)]
KPIEIIGAPFSKGQPRGGVEKGPAALRKAGLVEKLKETEYNVRDHGDLAFVDVPNDSPFQIVKNPRSVGKANEQLAAVVAETQKNGTISVVLGGDHSMAIGSISGHARVHPDLCVIWVDAHTDINTPLTTSSGNLHGQPVAFLLKELKGKFPDVPGFSWVTPCISAKDIVYIGLRDVDPGEHYIIKTLGIKYFSMTEVDKLGIGKVMEETFSYLLGRKKRPIHLSFDVDGLDPVFTPATGTPVVGGLSYREGLYITEEIYKTGLLSGLDIMEVNPTLGKTPEEVTRTVNTAVALTLSCFGTKREGNHKPETDYL
>d1rlr_2 3.3.1.1.1 (212-737) R1 subunit of ribonucleotide reductase, C-terminal domain [Escherichia coli]
QFSSCVLIECGDSLDSINATSSAIVKYVSQRAGIGINAGRIRALGSPIRGGEAFHTGCIPFYKHFQTAVKSCSQGGVRGGAATLFYPMWHLEVESLLVLKNNRGVEGNRVRHMDYGVQINKLMYTRLLKGEDITLFSPSDVPGLYDAFFADQEEFERLYTKYEKDDSIRKQRVKAVELFSLMMQERASTGRIYIQNVDHCNTHSPFDPAIAPVRQSNLCLEIALPTKPLNDVNDENGEIALCTLSAFNLGAINNLDELDELAILAVRALDALLDYQDYPIPAAKRGAMGRRTLGIGVINFAYYLAKHGKRYSDGSANNLTHKTFEAIQYYLLKASNELAKEQGACPWFNETTYAKGILPIDTYKKDLDTIANEPLHYDWEALRESIKTHGLRNSTLSALMPSETSSQISNATNGIEPPRGYVSIKASKDGILRQVVPDYEHLHDAYELLWEMPGNDGYLQLVGIMQKFIDQSISANTNYDPSRFPSGKVPMQQLLKDLLTAYKFGVKTLYYQNTRDDIDDLSNFQL
>d3cla__ 3.30.1.1.1 Chloramphenicol acetyltransferase [Escherichia coli]
MNYTKFDVKNWVRREHFEFYRHRLPCGFSLTSKIDITTLKKSLDDSAYKFYPVMIYLIAQAVNQFDELRMAIKDDELIVWDSVDPQFTVFHQETETFSALSCPYSSDIDQFMVNYLSVMERYKSDTKLFPQGVTPENHLNISALPWVNFDSFNLNVANFTDYFAPIITMAKYQQEGDRLLLPLSVQVHHAVCDGFHVARFINRLQELCNSKLK
>d1eaf__ 3.30.1.1.3 Dihydrolipoamide acetyltransferase [Azotobacter vinelandii]
IPPIPPVDFAKYGEIEEVPMTRLMQIGATNLHRSWLNVPHVTQFESADITELEAFRVAQKAVAKKAGVKLTVLPLLLKACAYLLKELPDFNSSLAPSGQALIRKKYVHIGFAVDTPDGLLVPVIRNVDQKSLLQLAAEAAELAEKARSKKLGADAMQGACFTISSLGHIGGTAFTPIVNAPEVAILGVSKASMQPVWDGKAFQPRLMLPLSLSYDHRVINGAAAARFTKRLGDLLADIRAILL
>d1phr__ 3.31.1.1.1 Tyrosine phosphatase [bovine (Bos taurus)]
VTKSVLFVCLGNICRSPIAEAVFRKLVTDQNISDNWVIDSGAVSDWNVGRSPDPRAVSCLRNHGINTAHKARQVTKEDFVTFDYILCMDESNLRDLNRKSNQVKNCRAKIELLGSYDPQKQLIIEDPYYGNDADFETVYQQCVRCCRAFLEKVR
>d1e2b__ 3.31.2.1.1 Enzyme IIB-cellobiose [Escherichia coli]
MEKKHIYLFSSAGMSTSLLVSKMRAQAEKYEVPVIIEAFPETLAGEKGQNADVVLLGPQIAYMLPEIQRLLPNKPVEVIDSLLYGKVDGLGVLKAAVAAIKKAAAN
>d1vhra_ 3.32.1.1.1 VH1-related dual-specificity phosphatase, VHR [human (Homo sapiens)]
SVQDLNDLLSDGSGCYSLPSQPCNEVTPRIYVGNASVAQDIPKLQKLGITHVLNAAEGRSFMHVNTNANFYKDSGITYLGIKANDTQEFNLSAYFERAADFIDQALAQKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSIVRQNREIGPNDGFLAQLCQLNDRLAKEGKLKP
>d2hnp__ 3.32.1.2.1 Tyrosine phosphatase [Human (Homo sapiens) 1B]
KEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIM
>d1yfoa_ 3.32.1.2.2 Tyrosine phosphatase [mouse (Mus musculus)]
KYPPLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNVRVSVEDVTVLVDYTVRKFCIQQQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKACNPQYAGAIVVHCSAGVGRTGTFVVIDAMLDMMHSERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLY
>d1ypta_ 3.32.1.2.3 Tyrosine phosphatase [Yersinia enterocolitica]
PEARAELSSRLTTLRNTLAPATNDPRYLQACGGEKLNRFRDIQCRRQTAVRADLNANYIQVGNTRTIACQYPLQSQLESHFRMLAENRTPVLAVLASSSEIANQRFGMPDYFRQSGTYGSITVESKMTQQVGLGDGIMADMYTLTIREAGQKTISVPVVHVGNWPDQTAVSSEVTKALASLVDQTAETKRNMYESKGSSAVADDSKLRPVIHCRAGVGRTAQLIGAMCMNDSRNSQLSVEDMVSQMRVQRNGIMVQKDEQLDVLIKLAEGQGRPLLNS
>d2trxa_ 3.33.1.1.1 Thioredoxin [Escherichia coli]
SDKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVGALSKGQLKEFLDANLA
>d1thx__ 3.33.1.1.2 Thioredoxin [Anabaena sp.]
SKGVITITDAEFESEVLKAEQPVLVYFWASWCGPCQLMSPLINLAANTYSDRLKVVKLEIDPNPTTVKKYKVEGVPALRLVKGEQILDSTEGVISKDKLLSFLDTHLN
>d1tof__ 3.33.1.1.3 Thioredoxin [(Chlamydomonas reinhardtii)]
GGSVIVIDSKAAWDAQLAKGKEEHKPIVVDFTATWCGPCKMIAPLFETLSNDYAGKVIFLKVDVDAVAAVAEAAGITAMPTFHVYKDGVKADDLVGASQDKLKALVAKHAAA
>d1mdia_ 3.33.1.1.4 Thioredoxin [human (Homo sapiens)]
MVKQIESKTAFQEALDAAGDKLVVVDFSATWCGPAKMIKPFFHSLSEKYSNVIFLEVDVDDAQDVASEAEVKATPTFQFFKKGQKVGEFSGANKEKLEATINELV
>d1erw__ 3.33.1.1.4 Thioredoxin [human (Homo sapiens)]
MVKQIESKTAFQEALDAAGDKLVVVDFSATWSGPSKMIKPFFHSLSEKYSNVIFLEVDVDDCQDVASECEVKCMPTFQFFKKGQKVGEFSGANKEKLEATINELV
>d1ego__ 3.33.1.1.5 Glutaredoxin [bacteriophage t4]
MQTVIFGRSGCPYCVRAKDLAEKLSNERDDFQYQYVDIRAEGITKEDLQQKAGKPVETVPQIFVDQQHIGGYTDFAAWVKENLDA
>d1aba__ 3.33.1.1.5 Glutaredoxin [bacteriophage t4]
MFKVYGYDSNIHKCGPCDNAKRLLTVKKQPFEFINIMPEKGVFDDEKIAELLTKLGRDTQIGLTMPQVFAPDGSHIGGFDQLREYFK
>d1kte__ 3.33.1.1.6 thioltransferase [Pig (Sus scrofa)]
AQAFVNSKIQPGKVVVFIKPTCPFCRKTQELLSQLPFKEGLLEFVDITATSDTNEIQDYLQQLTGARTVPRVFIGKECIGGCTDLESMHKRGELLTRLQQVGAVK
>d1mek__ 3.33.1.2.1 Protein disulfide isomerase, N-terminal domain [human (Homo sapiens)]
DAPEEEDHVLVLRKSNFAEALAAHKYLLVEFYAPWCGHCKALAPEYAKAAGKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFRNGDTASPKEYTAGREADDIVNWLKKRTGPAA
>d1dsba2 3.33.1.3.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) [Escherichia coli]
AQYEDGKQYTTLEKPVAGAPQVLEFFSFFCPHCYQFEEVLHISDNVKKKLPEGVKMTKYHVNF
>d1gp1a_ 3.33.1.4.1 Glutathione peroxidase [bovine (Bos taurus)]
RTVYAFSARPLAGGEPFNLSSLRGKVLLIENVASLGTTVRDYTQMNDLQRRLGPRGLVVLGFPCNQFGHQENAKNEEILNCLKYVRPGGGFEPNFMLFEKCEVNGEKAHPLFAFLREVLPTPSDDATALMTDPKFITWSPVCRNDVSWNFEKFLVGPDGVPVRRYSRRFLTIDIEPDIETLLS
>d2gsta2 3.33.1.5.1 (1-84) Glutathione S-transferase [rat (Rattus rattus)]
PMILGYWNVRGLTHPIRLLLEYTDSSYEEKRYAMGDAPDYDRSQWLNEKFKLGLDFPNLPYLIDGSRKITQSNAIMRYLARKHH
>d1glqa2 3.33.1.5.2 (1-78) Glutathione S-transferase [mouse (Mus musculus) class pi]
PPYTIVYFPVRGRCEAMRMLLADQGQSWKEEVVTIDTWMQGLLKPTCLYGQLPKFEDGDLTLYQSNAILRHLGRSLGL
>d2gsra2 3.33.1.5.3 (1-76) Glutathione S-transferase [pig (Sus scrofa) class pi]
PPYTITYFPVRGRCEAMRMLLADQDQSWKEEVVTMETWPPLKPSCLFRQLPKFQDGDLTLYQSNAILRHLGRSFGL
>d1gssa2 3.33.1.5.4 (1-78) Glutathione S-transferase [human (Homo sapiens) class pi]
PPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEGSLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGL
>d1hna_2 3.33.1.5.5 (1-84) Glutathione S-transferase [human (Homo sapiens) class mu]
PMTLGYWNIRGLAHSIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNLPYLIDGTHKITQSNAILRYIARKHN
>d1gsea2 3.33.1.5.6 (1-79) Glutathione S-transferase [human (Homo sapiens) class alpha]
AEKPKLHYFNARGKMESTRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQQVPMVEIDGMKLVQTRAILNYIASKYN
>d1gsq_2 3.33.1.5.7 (1-75) Glutathione S-transferase [Squid (Ommastrephes sloani pacificus)]
PKYTLHYFPLMGRAELCRFVLAAHGEEFTDRVVEMADWPNLKATMYSNAMPVLDIDGTKMSQSMCIARHLAREFG
>d1gta_2 3.33.1.5.8 (1-80) Glutathione S-transferase [Schistosoma japonicum]
MSPILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKWRNKKFELGLEFPNLPYYIDGDVKLTQSMAIIRYIADKHN
>d1gnwa2 3.33.1.5.9 (1-84) Glutathione S-transferase [mouse-ear cress (Arabidopsis thaliana)]
GIKVFGHPASIATRRVLIALHEKNLDFELVHVELKDGEHKKEPFLSRNPFGQVPAFEDGDLKLFESRAITQYIAHRYENQGTNL
>d2trcp_ 3.33.2.1.1 Phosducin [rat rattus norvegicus]
EGQATHTGPKGVINDWRKFKLESEDGDSIPPSKKEILRQMSSPQSRDDKDSKERSRKSIQEYELIHQDKEDEGCLRKYRRQCQDHQKLSFGPRYGFVYELETGEQFLETIEKEQKVTTIVVNIYEDGVRGCDALNSSLECLAAEYPVKFCKIRASNTGAGDRFSSDVLPTLLVYKGGELISNFISVAEQFAEDFFAADVESFLNEYGLLPER
>d1trka3 3.34.1.1.1 (533-678) Transketolase, C-terminal domain [baker's yeast (Saccharomyces cerevisiae)]
EGSSIESASKGGYVLQDVANPDIILVATGSEVSLSVEAAKTLAAKNIKARVVSLPDFFTFDKQPLEYRLSVLPDNVPIMSVEVLATTCWGKYAHQSFGIDRFGASGKAPEVFKFFGFTPEGVAERAQKTIAFYKGDKLISPLKKAF
>d1pkm_3 3.35.1.1.1 (385-519) Pyruvate kinase, C-terminal domain [cat (Felis domestica)]
ELVRGSSHSTDLMEAMAMGSVEASYKCLAAALIVLTESGRSAHQVARYRPRAPIIAVTRNHQTARQAHLYRGIFPVVCKDPVQEAWAEDVDLRVNLAMNVGKARGFFKHGDVVIVLTGWRPGSGFTNTMRVVPVP
>d1pkya3 3.35.1.1.3 (345-464) Pyruvate kinase, C-terminal domain [Escherichia coli]
KLRITEAVCRGAVETAEKLDAPLIVVATQGGKSARAVRKYFPDATILALTTNEKTAHQLVLSKGVVPQLVKEITSTDDFYRLGKELALQSGLAHKGDVVVMVSGALVPSGTTNTASVHVL
>d1lam_1 3.36.1.1.1 (1-159) Leucine aminopeptidase, N-terminal domain [bovine (Bos taurus)]
TKGLVLGIYSKEKEEDEPQFTSAGENFNKLVSGKLREILNISGPPLKAGKTRTFYGLHEDFPSVVVVGLGKKTAGIDEQENWHEGKENIRAAVAAGCRQIQDLEIPSVEVDPCGDAQAAAEGAVLGLYEYDDLKQKRKVVVSAKLHGSEDQEAWQRGVL
>d1htta1 3.37.1.1.1 (268-366) Histidyl-tRNA synthetase (HisRS), C-terminal domain [Escherichia coli]
DPVVDIYLVASGADTQSAAMALAERLRDELPGVKLMTNHGGGNFKKQFARADKWGARVAVVLGESEVANGTAVVKDLRSGEQTAVAQDSVAAHLRTLLG
>d1adja1 3.37.1.1.2 (325-420) Histidyl-tRNA synthetase (HisRS), C-terminal domain [Thermus thermophilus]
EKGPDLYLIPLTEEAVAEAFYLAEALRPRLRAEYALAPRKPAKGLEEALKRGAAFAGFLGEDELRAGEVTLKRLATGEQVRLSREEVPGYLLQALG
>d1atia1 3.37.1.1.3 (327-437) Glycyl-tRNA synthetase (GlyRS), C-terminal domain [Thermus thermophilus]
QLAPIKVAVIPLVKNRPEITEYAKRLKARLLALGLGRVLYEDTGNIGKAYRRHDEVGTPFAVTVDYDTIGQSKDGTTRLKDTVTVRDRDTMEQIRLHVDELEGFLRERLRW
>d1eria_ 3.38.1.1.1 Restriction endonuclease EcoRI [Escherichia coli]
SQGVIGIFGDYAKAHDLAVGEVSKLVKKALSNEYPQLSFRYRDSIKKTEINEALKKIDPDLGGTLFVSNSSIKPDGGIVEVKDDYGEWRVVLVAEAKHQGKDIINIRNGLLVGKRGDQDLMAAGNAIERSHKNISEIANFMLSESHFPYVLFLEGSNFLTENISITRPDGRVVNLEYNSGILNRLDRLTAANYGMPINSNLCINKFVNHKDKSIMLQAASIYTQGDGREWDSKIMFEIMFDISTTSLRVLGRDLFEQLTSK
>d1rvaa_ 3.38.1.2.1 Restriction endonuclease EcoRV [Escherichia coli]
SLRSDLINALYDENQKYDVCGIISAEGKIYPLGSDTKVLSTIFELFSRPIINKIAEKHGYIVEEPKQQNHYPDFTLYKPSEPNKKIAIDIKTTYTNKENEKIKFTLGGYTSFIRNNTKNIVYPFDQYIAHWIIGYVYTRVATRKSSLKTYNINELNEIPKPYKGVKVFLQDKWVIAGDLAGSGNTTNIGSIHAHYKDFVEGKGIFDSEDEFLDYWRNYERTSQLRNDKYNNISEYRNWIYRGRK
>d1bam__ 3.38.1.3.1 Restriction endonuclease BamHI [Bacillus amyloliquefaciens]
MEVEKEFITDEAKELLSKDKLIQQAYNEVKTSICSPIWPATSKTFTINNTEKNCNGVVPIKELCYTLLEDTYNWYREKPIDVYKEFIENSELKRVGMEFETGNISSAHRSMNKLLLGLKHGEIDLAIILMPIKQLAYYLTDRVTNFEELEPYFELTEGQPFIFIGFNAEAYNSNVPLIPKGSDGMSKRSIKKWKDKVENK
>d1pvua_ 3.38.1.4.1 Restriction endonuclease PvuII [Proteus vulgaris]
SHPDLNKLLELWPHIQEYQDLALKHGINDIFQDNGGKLLQVLLITGLTVLPGGNDAVDNAGQEYELKSINIDLTKGFSTHHHMNPVIIAKYRQVPWIFAIYRGIAIEAIYRLEPKDLEFYYDKWERKWYSDGHKDINNPKIPVKYVMEHGTKIY
>d1cfr__ 3.38.1.5.1 Restriction endonuclease Cfr10I [Citrobacter freundii]
MDIISKSGEGNKYTINSAIAFVAYASHIDINTTEFSKVLSGLRDFINDEAIRLGGKISDGSFNKCNGDWYEWLIGIRAIEFFLESETNFIVVKMPNATSFDVMSIYKSCLSEFIYDLRSKLSLNNVNLITSNPDFSIIDIRGRREELKSMLKDISFSNISLSTISEIDNLYKNFIDYAELEHIKSFLSVKTTFRPDRRLQLAHEGSLMKALYTHLQTRTWTINPTGIRYYAAATSIGNADVIGLKTVATHSITDVKSLPQSAVDEIFKINSVLDVDSCLSHIL
>d2rsla_ 3.39.1.1.1 gamma,delta resolvase, large fragment [Escherichia coli]
MRLFGYARVSTSQQSLDIQVRALKDAGVKANRIFTDKRKGLDLLRMKVEEGDVILVKKLDRLGRDTADMIQLIKEFDAQGVSIRFIDDGISTDGEMGKMVVTILSAVAQAERQRI
>d2tmda2 3.4.1.1.1 (490-645) Trimethylamine dehydrogenase, C-terminal domain [Escherichia coli]
RWNTDGTNCLTHDPIPGADASLPDQLTPEQVMDGKKKIGKRVVILNADTYFMAPSLAEKLATAGHEVTIVSGVHLANYMHFTLEYPNMMRRLHELHVEELGDHFCSRIEPGRMEIYNIWGDGSKRTYRGPGVSPRDANTSHRWIEFDSLVLVTGRH
>d1coy_1 3.4.1.2.1 (1-315) Cholesterol oxidase [Brevibacterium sterolicum]
RTLADGDRVPALVIGSGYGGAVAALRLTQAGIPTQIVEMGRSWDTPGSDGKIFCGMLNPDKRSMWLADKTDQPVSNFMGFGINKSIDRYVGVLDSERFSGIKVYQGRGVGGGSLVNGGMAVTPKRNYFEEILPSVDSNEMYNKYFPRANTGLGVNNIDQAWFESTEWYKFARTGRKTAQRSGFTTAFVPNVYDFEYMKKEAAGQVTKSGLGGEVIYGNNAGKKSLDKTYLAQAAATGKLTITTLHRVTKVAPATGSGYSVTMEQIDEQGNVVATKVVTADRVFFAAGSVGTSKLLVSMKAQGHLPNLSSQVGEGW
>d1pbe_1 3.4.1.2.2 (1-173,276-391) p-Hydroxybenzoate hydroxylase (PHBH) [Pseudomonas fluorescens]
MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFAGQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREACGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDGFHGISRQSIPAE
>d1gal_1 3.4.1.2.4 (1-322) Glucose oxidase [Aspergillus niger]
GIEASLLTDPKDVSGRTVDYIIAGGGLTGLTTAARLTENPNISVLVIESGSYESDRGPIIEDLNAYGDIFGSSVDHAYETVELATNNQTALIRSGNGLGGSTLVNGGTWTRPHKAQVDSWETVFGNEGWNWDNVAAYSLQAERARAPNAKQIAAGHYFNASCHGVNGTVHAGPRDTGDDYSPIVKALMSAVEDRGVPTKKDFGCGDPHGVSMFPNTLHEDQVRSDAAREWLLPNYQRPNLQVLTGQYVGKVLLSQNGTTPRAVGVEFGTHKGNTHNVYAKHEVLLAAGSAVSPTILEYSGIGMKSILEPLGIDTVVDLPVGL
>d1gnd_1 3.4.1.3.1 (1-291,389-430) Guanine nucleotide dissosiation inhibitor, GDI [Bovine (Bos taurus)]
MDEEYDVIVLGTGLTECILSGIMSVNGKKVLHMDRNPYYGGESSSITPLEELYKRFQLLEGPPETMGRGRDWNVDLIPKFLMANGQLVKMLLYTEVTRYLDFKVVEGSFVYKGGKIYKVPSTETEALASNLMGMFEKRRFRKFLVFVANFDENDPKTFEGVDPQNTSMRDVYRKFDLGQDVIDFTGHALALYRTDDYLDQPCLETINRIKLYSESLARYGKSPYLYPLYGLGELPQGFARLSAIYGGTYMLNKPVDDIIMENGKVVGVKSEGEVARCKQLICDPSYVPDR
>d3grs_2 3.4.1.4.1 (149-273) Glutathione reductase [human (Homo sapiens)]
SQIPGASLGITSDGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVKEVKKTLSGLEVSMVTAVPGRLPVMTMIPDVDCLLWAIG
>d3grs_1 3.4.1.4.1 (1-148,274-346) Glutathione reductase [human (Homo sapiens)]
VASYDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDHADYGFPSCEGKFNWRVIKEKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTSDPKPTIEVSGKKYTAPHILIATGGMPSTPH
>d1ojt_1 3.4.1.4.10 (1-159,285-354) Dihydrolipoamide dehydrogenase [Neisseria meningitidis]
GSADAEYDVVVLGGGPGGYSAAFAAADEGLKVAIVERYKTLGGVCLNVGCIPSKALLHNAAVIDEVRHLAANGIKYPEPELDIDMLRAYKDGVVSRLTGGLAGMAKSRKVDVIQGDGQFLDPHHLEVSLTAGDAYEQAAPTGEKKIVAFKNCIIAAGS
>d1ojt_2 3.4.1.4.10 (160-284) Dihydrolipoamide dehydrogenase [Neisseria meningitidis]
VTKLPFIPEDPRIIDSSGALALKEVPGKLLIIGGGIIGLEMGTVYSTLGSRLDVVEMMDGLMQGADRDLVKVWQKQNEYRFDNIMVNTKTVAVEPKEDGVYVTFEGANAPKEPQRYDAVLVAAGR
>d1fcda1 3.4.1.4.11 (1-114,256-327) Flavocytochrome c sulfide dehydrogenase, FCSD, flavin-binding subunit [Purple phototrophic bacterium (Chromatium vinosum)]
AGRKVVVVGGGTGGATAAKYIKLADPSIEVTLIEPNTDYYTCYLSNEVIGGDRKLESIKHGYDGLRAHGIQVVHDSATGIDPDKKLVKTAGGAEFGYDRCVVAPGIELIYDKI
>d1fcda2 3.4.1.4.11 (115-255) Flavocytochrome c sulfide dehydrogenase, FCSD, flavin-binding subunit [Purple phototrophic bacterium (Chromatium vinosum)]
GYSEEAAAKLPHAWKAGEQTAILRKQLEDMADGGTVVIAPPAAPFRCPPGPYERASQVAYYLKAHKPMSKVIILDSSQTFSKQSQFSKGWERLYGFGTENAMIEWHPGPDSAVVKVDGGEMMVETAFGDEFKADVINLIPP
>d1gesa1 3.4.1.4.2 (1-144,261-333) Glutathione reductase [Escherichia coli]
KHYDYIAIGGGSGGIASINRAAMYGQKCALIEAKELGGTCVNVGCVPKKVMWHAAQIREAIHMYGPDYGFDTTINKFNWETLIASRTAYIDRIHTSYENVLGKNNVDVIKGFARFVDAKTLEVNGETITADHILIATGGRPSH
>d1gesa2 3.4.1.4.2 (145-260) Glutathione reductase [Escherichia coli]
DIPGVEYGIDSDGFFALPALPERVAVVGAGYIGVELGGVINGLGAKTHLFEMFDAPLPSFDPMISETLVEVMNAEGPQLHTNAIPKAVVKNTDGSLTLELEDGRSETVDCLIWAIG
>d1ndaa2 3.4.1.4.3 (167-283) Trypanothione reductase [Crithidia fasciculata]
PGIEHCISSNEAFYLPEPPRRVLTVGGGFISVEFAGIFNAYKPKDGQVTLCYRGEMILRGFDHTLREELTKQLTANGIQILTKENPAKVELNADGSKSVTFESGKKMDFDLVMMAIG
>d2tpra2 3.4.1.4.3 (169-285) Trypanothione reductase [Crithidia fasciculata]
EGDDLCITSNEAFYLDEAPKRALCVGGGYISIEFAGIFNAYKARGGQVDLAYRGDMILRGFDSELRKQLTEQLRANGINVRTHENPAKVTKNADGTRHVVFESGAEADYDVVMLAIG
>d2tpra1 3.4.1.4.3 (1-168,286-357) Trypanothione reductase [Crithidia fasciculata]
SRAYDLVVIGAGSGGLEAGWNAASLHKKRVAVIDLQKHHGPPHYAALGGTCVNVGCVPKKLMVTGANYMDTIRESAGFGWELDRESVRPNWKALIAAKNKAVSGINDSYEGMFADTEGLTFHQGFGALQDNHTVLVRESADPNSAVLETLDTEYILLATGSWPQHLG
>d1ndaa1 3.4.1.4.3 (1-166,284-354) Trypanothione reductase [Crithidia fasciculata]
IFDLVVIGAGSGGLEAAWNAATLYKKRVAVIDVQMVHGPPFFSALGGTCVNVGCVPKKLMVTGAQYMEHLRESAGFGWEFDRTTLRAEWKKLIAVKDEAVLNINKSYEEMFRDTEGLEFFLGWGSLESKNVVNVRESADPASAVKERLETENILLASGSWPHMPN
>d1tde_1 3.4.1.4.5 (1-118,245-316) Thioredoxin reductase [Escherichia coli]
GTTKHSKLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNDLTGPLLMERMHEHATKFETEIIFDHINKVDLQNRPFRLNGDNGEYTCDALIIATGASAR
>d1tde_2 3.4.1.4.5 (119-244) Thioredoxin reductase [Escherichia coli]
LGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDGFRAEKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQNSDNIESLDVAGLFVAIG
>d1vdc_2 3.4.1.4.6 (123-252) Thioredoxin reductase [mouse-ear cress (Arabidopsis thaliana)]
RLSFVGSGEVLGGFWNRGISACAVCDGAAPIFRNKPLAVIGGGDSAMEEANFLTKYGSKVYIIHRRDAFRASKIMQQRALSNPKIDVIWNSSVVEAYGDGERDVLGGLKVKNVVTGDVSDLKVSGLFFAI
>d1vdc_1 3.4.1.4.6 (1-122,253-322) Thioredoxin reductase [mouse-ear cress (Arabidopsis thaliana)]
LETHNTRLCIVGSGPAAHTAAIYAARAELKPLLFEGWMANDIAPGGQLTTTTDVENFPGFPEGILGVELTDKFRKQSERFGTTIFTETVTKVDFSSKPFKLFTDSKAILADAVILAIGAVA
>d1nhp_2 3.4.1.4.7 (120-242) NADH peroxidase [Streptococcus (Enterococcus) faecalis]
IPGKDLDNIYLMRGRQWAIKLKQKTVDPEVNNVVVIGSGYIGIEAAEAFAKAGKKVTVIDILDRPLGVYLDKEFTDVLTEEMEANNITIATGETVERYEGDGRVQKVVTDKNAYDADLVVVAV
>d1nhp_1 3.4.1.4.7 (1-119,243-321) NADH peroxidase [Streptococcus (Enterococcus) faecalis]
MKVIVLGSSHGGYEAVEELLNLHPDAEIQWYEKGDFISFLSAGMQLYLEGKVKDVNSVRYMTGEKMESRGVNVFSNTEITAIQPKEHQVTVKDLVSGEERVENYDKLIISPGAVPFEL
>d1lvl_1 3.4.1.4.8 (1-150,266-335) Dihydrolipoamide dehydrogenase [Pseudomonas putida]
QQTIQTTLLIIGGGPGGYVAAIRAGQLGIPTVLVEGQALGGTCLNIGCIPSKALIHVAEQFHQASRFTEPSPLGISVASPRLDIGQSVAWKDGIVDRLTTGVAALLKKHGVKVVHGWAKVLDGKQVEVDGQRIQCEHLLLATGSSSVEL
>d3lada2 3.4.1.4.8 (159-277) Dihydrolipoamide dehydrogenase [Pseudomonas putida]
PAPVDQDVIVDSTGALDFQNVPGKLGVIGAGVIGLELGSVWARLGAEVTVLEAMDKFLPAVDEQVAKEAQKILTKQGLKILLGARVTGTEVKNKQVTVKFVDAEGEKSQAFDKLIVAVG
>d1lpfa2 3.4.1.4.8 (159-277) Dihydrolipoamide dehydrogenase [Pseudomonas putida]
PAPLSDDIIVDSTGALEFQAVPKKLGVIGAGVIGLELGSVWARLGAEVTVLEALDKFLPAADEQIAKEALKVLTKQGLNIRLGARVTASEVKKKQVTVTFTDANGEQKETFDKLIVAVG
>d1lpfa1 3.4.1.4.8 (1-158,278-348) Dihydrolipoamide dehydrogenase [Pseudomonas putida]
SQKFDVVVIGAGPGGYVAAIRAAQLGLKTACIEKYIGKEGKVALGGTCLNVGCIPSKALLDSSYKYHEAKEAFKVHGIEAKGVTIDVPAMVARKANIVKNLTGGIATLFKANGVTSFEGHGKLLANKQVEVTGLDGKTQVLEAENVIIASGSRPVEI
>d3lada1 3.4.1.4.8 (1-158,278-348) Dihydrolipoamide dehydrogenase [Pseudomonas putida]
SQKFDVIVIGAGPGGYVAAIKSAQLGLKTALIEKYKGKEGKTALGGTCLNVGCIPSKALLDSSYKFHEAHESFKLHGISTGEVAIDVPTMIARKDQIVRNLTGGVASLIKANGVTLFEGHGKLLAGKKVEVTAADGSSQVLDTENVILASGSKPVEI
>d1lvl_2 3.4.1.4.8 (151-265) Dihydrolipoamide dehydrogenase [Pseudomonas putida]
MLPLGGPVISSTEALAPKALPQHLVVVGGGYIGLELGIAYRKLGAQVSVVEARERILPTYDSELTAPVAESLKKLGIALHLGHSVEGYENGCLLANDGKGGQLRLEADRVLVAVG
>d1ebda2 3.4.1.4.9 (149-265) Dihydrolipoamide dehydrogenase [Bacillus stearothermophilus]
PNFKFSNRILDSTGALNLGEVPKSLVVIGGGYIGIELGTAYANFGTKVTILEGAGEILSGFEKQMAAIIKKRLKKKGVEVVTNALAKGAEEREDGVTVTYEANGETKTIDADYVLVT
>d1ebda1 3.4.1.4.9 (1-148,266-340) Dihydrolipoamide dehydrogenase [Bacillus stearothermophilus]
AIETETLVVGAGPGGYVAAIRAAQLGQKVTIVEKGNLGGVCLNVGCIPSKALISASHRYEQAKHSEEMGIKAENVTIDFAKVQEWKASVVKKLTGGVEGLLKGNKVEIVKGEAYFVDANTVRVVNGDSAQTYTFKNAIIATGSRPIE
>d1pdo__ 3.40.1.1.1 The IIA domain of mannose transporter, IIA-Man [Escherichia coli]
TIAIVIGTHGWAAEQLLKTAEMLLGEQENVGWIDFVPGENAETLIEKYNAQLAKLDTTKGVLFLVDTWGGSPFNAASRIVVDKEHYEVIAGVNIPMLVETLMARDDDPSFDELVALAVETGREGVKALK
>d1hpm_2 3.41.1.1.1 (186-378) Heat shock protein 70kDa, ATPase fragment [bovine (Bos taurus)]
VGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILS
>d1hpm_1 3.41.1.1.1 (1-185) Heat shock protein 70kDa, ATPase fragment [bovine (Bos taurus)]
GPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKK
>d1dkgd_ 3.41.1.1.2 Heat shock protein 70kDa, ATPase fragment [Escherichia coli, gene dnaK]
KIIGIDLGTTNSCVAIMDGTTPRVLENAEGDRTTPSIIAYTQDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEEVQRDVSIMPFKIIAADNGDAWVEVKGQKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAGLEVKRIINEPTAAALAYGLDKTGNRTIAVYDLGGGTFDISIIEIDEKTFEVLATNGDTHLGGEDFDSRLINYLVEEFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDLVNRSIELLKVALQDAGLSVSDIDDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQGGVLT
>d1atna1 3.41.1.1.3 (2-147) Actin [bovine (Bos taurus) pancreas]
DEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASG
>d1atna2 3.41.1.1.3 (148-373) Actin [bovine (Bos taurus) pancreas]
RTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVHR
>d2btfa2 3.41.1.1.3 (146-374) Actin [bovine (Bos taurus) pancreas]
RTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
>d2btfa1 3.41.1.1.3 (1-145) Actin [bovine (Bos taurus) pancreas]
DDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASG
>d2yhx_1 3.41.1.2.1 (1-201) Hexokinase BIII [baker's yeast (Saccharomyces cerevisiae)]
AAAXDXSLVEVHXXVFIVPPXILQAVVSILTTRXDDXDSSAASIPMVPGWVLKQVSGAQAGSFLAIVMGGGDLEVILISLAGRQESSIXASRSLAAAMSTTAIPSDLWGNXAXSNAAFSSXEFSSXAGSVPLGFTFXEAGAKEXVIKGQITXQAXAFSLAXLXKLISAMXNAXFPAGDXXXSVADIXDSHGILXXVNYTDA
>d2yhx_2 3.41.1.2.1 (202-457) Hexokinase BIII [baker's yeast (Saccharomyces cerevisiae)]
XIKMGIIFGSGVNAAYWCDSTXIGDAADGGXXGGAGXMXICCDQSSFRKAFPSLPQIXYLXTLNXXSPXAXKTFXKNSXAKNXGQSLRDVLMXFKXXGQXHXXXAXSFXAANVENTSYPAKIQKLPHFDLRXXXDLFXGDQGIAXKTXMKXVVRRXLFLIAAYAFRLVVCXIXAICQKKGYSSGHIAAXGSXRSYSGFSXNSATXNXNIYGWPQSAXXSKPIXITPAIDGXGAASXVIXSIASAXXSXAXXSAXXA
>d1hkg_1 3.41.1.2.2 (1-201) Hexokinase A [yeast (Saccharomyces cerevisiae)]
AASXDXSLVEVHXXVFIVPPXILQAVVSIATTRXDDXDSAAASIPMVPGWVLKQVXGSQAGSFLAIVMGGGDLEVILIXLAGYQESSIXASRSLAASMXTTAIPSDLWGNXAXSNAAFSSXEFSSXAGSVPLGFTFXEAGAKEXVIKGQITXQAXAFSLAXLXKLISAMXNAXFPAGDXXXXVADIXDSHGILXXVNYTDA
>d1hkg_2 3.41.1.2.2 (202-457) Hexokinase A [yeast (Saccharomyces cerevisiae)]
XIKMGIIFGSGVNAAYWCDSTXIADAADAGXXGGAGXMXVCCXQDSFRKAFPSLPQIXYXXTLNXXSPXAXKTFEKNSXAKNXGQSLRDVLMXYKXXGQXHXXXAXDFXAANVENSSYPAKIQKLPHFDLRXXXDLFXGDQGIAXKTXMKXVVRRXLFLIAAYAFRLVVCXIXAICQKKGYSSGHIAAXGSXRDYSGFSXNSATXNXNIYGWPQSAXXSKPIXITPAIDGEGAAXXVIXSIASSQXXXAXXSAXXA
>d1glag1 3.41.1.3.1 (1-243) Glycerate kinase [Escherichia coli]
KYIVALDQGTTSSRAVVMDHDANIISVSQREFEQIYPKPGWVEHDPMEIWATQSSTLVEVLAKADISSDQIAAIGITNQRETTIVWEKETGKPIYNAIVWQCRRTAEICEHLKRDGLEDYIRSNTGLVIDPYFSGTKVKWILDHVEGSRERARRGELLFGTVDTWLIWKMTQGRVHVTDYTNASRTMLFNIHTLDWDDKMLEVLDIPREMLPEVRRSSEVYGQTNIIPISGIAGDQQAALFGQ
>d1glag2 3.41.1.3.1 (244-489) Glycerate kinase [Escherichia coli]
LCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIACGPTGEVNYALEGAVFMAGASIQWLRDEMKLINDAYDSEYFATKVQNTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNANHIIRATLESIAYQTRDVLEAMQADSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQNLDELQEKAVIEREFRPGIETTERNYRYAGWKKAVKRAMAWEEH
>d1chma1 3.41.2.1.1 (1-155) Creatinase, N-terminal domain [Pseudomonas putida]
QMPKTLRIRNGDKVRSTFSAQEYANRQARLRAHLAAENIDAAIFTSYHNINYYSDFLYCSFGRPYALVVTEDDVISISANIDGGQPWRRTVGTDNIVYTDWQRDNYFAAIQQALPKARRIGIEHDHLNLQNRDKLAARYPDAELVDVAAACMRMR
>d2rn2__ 3.41.3.1.1 RNase H [Escherichia coli]
MLKQVEIFTDGSCLGNPGPGGYGAILRYRGREKTFSAGYTRTTNNRMELMAAIVALEALKEHCEVILSTDSQYVRQGITQWIHNWKKRGWKTADKKPVKNVDLWQRLDAALGQHQIKWEWVKGHAGHPENERCDELARAAAMNPTLEDTGYQVEV
>d1ril__ 3.41.3.1.3 RNase H [Thermus thermophilus]
RKRVALFTDGACLGNPGPGGWAALLRFHAHEKLLSGGEACTTNNRMELKAAIEGLKALKEPCEVDLYTDSHYLKKAFTEGWLEGWRKRGWRTAEGKPVKNRDLWEALLLAMAPHRVRFHFVKGHTGHPENERVDREARRQAQSQAKT
>d1hrha_ 3.41.3.1.4 HIV RNase H (Domain of reverse transcriptase) [human immunodeficiency virus type I]
YQLEKEPIVGAETFYVDGAANRETKLGKAGYVTNKGRQKVVPLTNTTNQKTELQAIYLALQDSGLEVNIVTDSQYALGIIQAQPDKSESELVNQIIEQLIKKEKVYLAWVPGGNEQVDKLVSAGI
>d1asu__ 3.41.3.2.1 ASV integrase, catalytic domain [Avian sarcoma virus (Rous sarcoma virus), Schmidt-Ruppin strain B]
PLREPRGLGPLQIWQTDFTLEPRMAPRSWLAVTVDTASSAIVVTQHGRVTSVAAQHHWATAIAVLGRPKAIKTDNGSCFTSKSTREWLARWGIAHTTGIPGNSQGQAMVERANRLLKDKIRVLAEGDGFMKRIPTSKQGELLAKAMYALNHFERGENTKTNL
>d1itg__ 3.41.3.2.2 HIV integrase, catalytic domain [human immunodeficiency virus]
DCSPGIWQLDCTHLEGKVILVAVHVASGYIEAEVIPAETGQETAYFLLKLAGRWPVKTVHTDNGSNFTSTTVKAACWWAGIKQEFGMNKELKKIIGQVRDQAEHLKTAVQMAVFIHNKKRKGGIGGYSAGERIVDIIATDIQ
>d1bco_2 3.41.3.3.1 (1-215) Mu transposase, core domain [Bacteriophage mu]
EHLDAMQWINGDGYLHNVFVRWFNGDVIRPKTWFWQDVKTRKILGWRCDVSENIDSIRLSFMDVVTRYGIPEDFHITIDNTRGAANKWLTGGAPNRYRFKVKEDDPKGLFLLMGAKMHWTSVVAGKGWGQAKPVERAFGVGGLEEYVDKHPALAGAYTGPYGDRAVDAELFLKTLAEGVAMFNARTGRETEMCGGKLSFDDVFEREYARTIVRKP
>d1kfd_1 3.41.3.4.1 (1-195) Exonuclease domain of DNA polymerase KF [Escherichia coli]
VISYDNYVTILDEETLKAWIAKLEKAPVFAFDTETDSLDNISANLVGLSFAIEPGVAAYIPVAHDYLDAPDQISRERALELLKPLLEDEKALKVGQNLKYDRGILANYGIELRGIAFDTMLESYILNSVAGRHDMDSLAERWLKHKTITFEEIAGKGKNQLTFNQIALEEAGRYAAEDADVTLQLHLKMWPDLQK
>d1taq_1 3.41.3.4.2 (265-425) Exonuclease domain of DNA polymerase KF [Thermus aquaticus]
SPKALEEAPWPPPEGAFVGFVLSRKEPMWADLLALAAARGGRVHRAPEPYKALRDLKEARGLLAKDLSVLALREGLGLPPGDDPMLLAYLLDPSNTTPEGVARRYGGEWTEEAGERAALSERLFANLWGRLEGEERLLWLYREVERPLSAVLAHMEATGVR
>d1noya_ 3.41.3.5.1 3'-5' exonuclease domain of T4 DNA polymerase [Bacteriophage T4]
DEFYISIETVGNNIVERYIDENGKERTREVEYLPTMFRHCKEESKYKDIYGKNCAPQKFPSMKDARDWMKRMEDIGLEALGMNDFKLAYISDTYGSEIVYDRKFVRVANCDIEVTGDKFPDPMKAEYEIDAITHYDSIDDRFYVFDLLNSMYGSVSKWDAKLAAKLDCEGGDEVPQEILDRVIYMPFDNERDMLMEYINLWEQKRPAIFTGWNIEGFDVPYIMNRVKMILGERSMKRFSPIGRVKSKLLQNMYGSKEIYSIDGVSILDYLDLYKKFAFTNLPSFSLESVAQHETKKGKLPYDGPINKLRETNHQRYISYNIIDVESVQAIDKIRGFIDLVLSMSYYAKMPFSGVMSPIKTWDAIIFNSLKGE
>d1hjra_ 3.41.3.6.1 RuvC resolvase [Escherichia coli]
AIILGIDPGSRVTGYGVIRQVGRQLSYLGSGCIRTKVDDLPSRLKLIYAGVTEIITQFQPDYFAIEQVFMAKNADSALKLGQARGVAIVAAVNQELPVFEYAARQVKQTVVGIGSAEKSQVQHMVRTLLKLPANPQADAADALAIAITHCHVSQNAMQ
>d1sfe_2 3.41.4.1.1 (1-81) Ada DNA repair protein, the middle domain [Escherichia coli]
LAVRYALADCELGRCLVAESERGICAILLGDDDATLISELQQMFPAADNAPADLMFQQHVREVIASLNQRDTPLTLPLDIR
>d1tfr__ 3.42.1.1.1 T4 RNase H [bacteriophage T4]
KEGICLIDFSQIALSTALVNFPDKEKINLSMVRHLILNSIKFNVKKAKTLGYTKIVLCIDNAKSGYWRRDFAYYYKKTWDWEGYFESSHKVIDELKAYMPYIVMDIDKYEADDHIAVLVKKFSLEGHKILIISSDGDFTQLHKYPNVKQWSPMHKKWVKIGSAEIDCMTKILKGDKKDNVASVKVRSDFWFTRVEGERTPSMKTSIVEAIANDREQAKVLLTESEYNRYKENLVLIDFDYIPDNIASNIVNYYNSYKLPPRGKIYSYFVKAGLSKLTNSINEF
>d1taq_2 3.42.1.2.1 (1-264) 5' to 3' exonuclease domain of DNA polymerase Taq [Thermus aquaticus]
PKGRVLLVDGHHLAYRTFHALKGLTTSRGEPVQAVYGFAKSLLKALKEDGDAVIVVFDARAPTPEDFPRQLALIKELVDLLGLARLEVPGYEADDVLASLAKKAEKEGYEVRILTADKDLYQLLSDRIHVLHPEGYLITPAWLWEKYGLRPDQWADYRALTGDESDNLPGVKGIGEKTARKLLEEWGSLEALLKNLDRLKPAIREKILAHMDDLKLSWDLAKVRTDLPLEVDFAKRREPDRERLRAFLERLEFGSLLHEFGLLE
>d1exna_ 3.42.1.3.1 T5 5'-exonuclease [bacteriophage T5]
RNLIVDGTNLGFRFKHNNSKKPFASSYVSTIQSLAKSYSARTTIVLGDKGKSVFRLEHLPEYKGNRDEKYAQRTEEEKALDEQFFEYLKDAFELCKTTFPTFTIRGVEADDAAYIVKLIGHLYDHVWLISTDGDWDTLLTDKVSRFSFTTRREYHLRDYEHHNVDDVEQFISLKAIGDLGDNIRGVEGIGAKRGYNIIREFGNVLDIIDQLPLPGKQKYIQNLNASEELLFRNLILVDLPTYCVDAIAAVGQDVLDKFTKDILEIAE
>d3pgm__ 3.43.1.1.1 Phosphoglycerate mutase [baker's yeast (Saccharomyces cerevisiae)]
PKLVLVRHGQSEWNEKNLFTGWVDVKLSAKGQQEAARAGELLKEKGVNVLVDYTSKLSRAIQTANIALEKADRLWIPVNRSWRLNERHYGDLQGKDKAQTLKKFGEEKFNTYRRSFDVPPPPIDASSPFSQKGDERYKYVDPNVLPETESLALVIDRLLPYWQDVIAKLVGKTSMIAAHGNSLRGLVKHLEGISDADIAKLNIPPGTILVFELDENLKPSKPSYYLDPEA
>d1rpa__ 3.43.1.2.1 Acid phosphatase [rat (Rattus norvegicus)]
KELKFVTLVFRHGDRGPIETFPNDPIKESSWPQGFGQLTKWGMGQHYELGSYIRRRYGRFLNNSYKHDQVYIRSTDVDRTLMSAMTNLAALFPPEGNSIWNPRLLWQPIPVHTVSLSEDRLLYLPFRDCPRFQELKSETLKSEEFLKRLQPYKSFIDTLPSLSGFEDQDLFEIWSRLYDPLYCESVHNFTLPTWATEDAMTKLKELSELSLLSLYGIHKQKEKSRLQGGVLVNEILKNMKLATQPQKARKLIMYSAHDTTVSGLQMALDVYNGLLPPYASCHIMELYQDNGGHFVEMYYRNETQNEPYPLTLPGCTHSCPLEKFAELLDPVIPQDWATECMG
>d1fbta_ 3.43.1.3.1 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, phosphatase domain [Rat (Rattus norvegicus)]
RSIYLCRHGESELNLRGRIGGDSGLSARGKQYAYALANFIRSQGISSLKVWTSHKRTIQTAEALGVPYEQWKALNEIDAGVCEETYEEIQEHYPEEFALRDQDKYRYRYPKGESYEDLVQRLEPVIELERQENVLVICHQAVRCLLAYFLDKSSDELPYLKCPLHTVLKLTPVAYGCRVESIYLNV
>d1nula_ 3.44.1.1.1 Xantine-guanine PRTase (XPRTase) [Escherichia coli]
EKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVPGALLARELGIRHVDTVCISSLKVLKRAEGDGEGFIVIDDLVDTGGTAVAIREMYPKAHFVTIFAKPAGRPLVDDYVVDIPQDTWIEQPWDMGVVFVPPISGR
>d1hgxa_ 3.44.1.1.2 Hypoxantine-guanine-xanthine PRTase [(Tritrichomonas foetus)]
MDDLERVLYNQDDIQKRIRELAAELTEFYEDKNPVMICVLTGAVFFYTDLLKHLDFQLEPDYIICSSLTISKDLKTNIEGRHVLVVEDIIDTGLTMYQLLNNLQMRKPASLKVCTLCDKDIGKKAYDVPIDYCGFVVENRYIIGYGFDFHNKYRNLPVIGILKE
>d1gph11 3.44.1.1.3 (235-465) Glutamine PRPP amidotransferase, C-terminal domain [Bacillus subtilis]
ICSMEYIYFSRPDSNIDGINVHSARKNLGKMLAQESAVEADVVTGVPDSSISAAIGYAEATGIPYELGLIKNRYVGRTFIQPSQALREQGVRMKLSAVRGVVEGKRVVMVDDSIVRGTTSRRIVTMLREAGATEVHVKISSPPIAHPCFYGIDTSTHEELIASSHSVDEIRQEIGADTLSFLSVEGLLKGIGRKYDDSNCGQCLACFTGKYPTEIYQDTVLPHVKEAVLTK
>d1ecfa1 3.44.1.1.4 (250-469) Glutamine PRPP amidotransferase, C-terminal domain [Escherichia coli]
NPCLFEYVYFARPDSFIDKISVYSARVNMGTKLGEKIAREWEDLDIDVVIPIPETSCDIALEIARILGKPYRQGFVKNRYVGRTFIMPGQQLRRKSVRRKLNANRAEFRDKNVLLVDDSIVRGTTSEQIIEMAREAGAKKVYLASAAPEIRFPNVYGIDMPSATELIAHGREVDEIRQIIGADGLIFQDLNDLIDAVRAENPDIQQFECSVFNGVYVTKD
>d1hmpa_ 3.44.1.1.5 Hypoxantine-guanine PRTase [Human (Homo sapiens)]
SPGVVISDDEPGYDLDLFCIPNHYAEDLERVFIPHGLIMDRTERLARDVMKEMGGHHIVALCVLKGGYKFFADLLDYIKALNRNSDRSIPMTVDFIRLKSYCNDQSTGDIKVIGGDDLSTLTGKNVLIVEDIIDTGKTMQTLLSLVRQYNPKMVKVASLLVKRTPRSVGYKPDFVGFEIPDKFVVGYALDYNEYFRDLNHVCVISETGKAKYKA
>d1opr__ 3.44.1.1.6 Orotate PRTase [Salmonella typhimurium]
MKPYQRQFIEFALNKQVLKFGEFTLKSGRKSPYFFNAGLFNTGRDLALLGRFYAEALVDSGIEFDLLFGPAYKGIPIATTTAVALAEHHDKDLPYCFNRKEAKDHGEGGSLVGSALQGRVMLVDDVITAGTAIRESMEIIQAHGATLAGVLISLDRQERGRGEISAIQEVERDYGCKVISIITLKDLIAYLEEKPDMAEHLAAVRAYREEFGV
>d1lfaa_ 3.45.1.1.1 Integrin CD11a/CD18 (LFA-1) [Human (Homo sapiens)]
GNVDLVFLFDGSMSLQPDEFQKILDFMKDVMKKLSNTSYQFAAVQFSTSYKTEFDFSDYVKRKDPDALLKHVKHMLLLTNTFGAINYVATEVFREELGARPDATKVLIIITDGEATDSGNIDAAKDIIRYIIGIGKHFQTKESQETLHKFASKPASEFVKILDTFEKLKDLFTELQKKIYVIE
>d1ido__ 3.45.1.1.2 Integrin CR3 (CD11b/CD18), alpha subunit [Human (Homo sapiens)]
DSDIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLKKSKTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPITQLLGRTHTATGIRKVVRELFNITNGARKNAFKILVVITDGEKFGDPLGYEDVIPEADREGVIRYVIGVGDAFRSEKSRQELNTIASKPPRDHVFQVNNFEALKTIQNQLREK
>d1gara_ 3.46.1.1.1 Glycinamide ribonucleotide transformylase [Escherichia coli, k12 strain tx635, with plasmid pjs167]
MNIVVLISGNGSNLQAIIDACKTNKIKGTVRAVFSNKADAFGLERARQAGIATHTLIASAFDSREAYDRELIHEIDMYAPDVVVLAGFMRILSPAFVSHYAGRLLNIHPSLLPKYPGLHTHNGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGDSEDDITARVQTQEHAIYPLVISWFADGRLKMHENAAWLDGQRLPPQGYA
>d1vid__ 3.47.1.1.1 Catechol O-methyltransferase, COMT [rat (Rattus norvegicus)]
TKEQRILRYVQQNAKPGDPQSVLEAIDTYCTQKEWAMNVGDAKGQIMDAVIREYSPSLVLELGAYCGYSAVRMARLLQPGARLLTMEMNPDYAAITQQMLNFAGLQDKVTILNGASQDLIPQLKKKYDVDTLDMVFLDHWKDRYLPDTLLLEKCGLLRKGTVLLADNVIVPGTPDFLAYVRGSSSFECTHYSSYLEYMKVVDGLEKAIYQGPS
>d1xvaa_ 3.47.1.2.1 Glycine N-methyltransferase [Rat (Rattus norvegicus)]
VDSVYRTRSLGVAAEGIPDQYADGEAARVWQLYIGDTRSRTAEYKAWLLGLLRQHGCHRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYALKERWNRRKEPAFDKWVIEEANWLTLDKDVPAGDGFDAVICLGNSFAHLPDSKGDQSEHRLALKNIASMVRPGGLLVIDHRNYDYILSTGCAPPGKNIYYKSDLTKDITTSVLTVNNKAHMVTLDYTVQVPGAGRDGAPGFSKFRLSYYPHCLASFTELVQEAFGGRCQHSVLGDFKPYRPGQAYVPCYFIHVLKKTG
>d1v39__ 3.47.1.3.1 Polymerase regulatory subunit VP39 [Vaccinia virus]
MDVVSLDKPFMYFEEIDNELDYEPESANEVAKKLPYQGQLKLLLGELFFLSKLQRHGILDGATVVYIGSAPGTHIRYLRDHFYNLGVIIKWMLIDGRHHDPILNGLRDVTLVTRFVDEEYLRSIKKQLHPSKIILISDVRSPSTADLLSNYALQNVMISILNPVASSLKWRCPFPDQWIKDFYIPHGNKMLQPFAPSYSAEMRLLSIYTGENMRLTRVTKSDAVNYEKKMYYLNKIVRNKVVVNFDYPNQEYDYFHMYFMLRTVYCNKTFPTTKAKVLFLQQSIFRFLNIP
>d1hmy__ 3.47.1.4.1 DNA methylase HhaI, coenzyme-binding domain [Haemophilus haemolyticus]
MIEIKDKQLTGLRFIDLFAGLGGFRLALESCGAECVYSNEWDKYAQEVYEMNFGEKPEGDITQVNEKTIPDHDILCAGFPCQAFSISGKQKGFEDSRGTLFFDIARIVREKKPKVVFMENVKNFASHDNGNTLEVVKNTMNELDYSFHAKVLNALDYGIPQKRERIYMICFRNDLNIQNFQFPKPFELNTFVKDLLLPDSEVEHLVIDRKDLVMTNQEIEQTTPKTVRLGIVGKGGQGERIYSTRGIAITLSAYGGGIFAKTGGYLVNGKTRKLHPRECARVMGYPDSYKVHPSTSQAYKQFGNSVVINVLQYIAYNIGSSLNFKPY
>d2adma_ 3.47.1.4.2 DNA methylase TaqI, coenzyme-binding domain [Thermophilus aquaticus ]
VETPPEVVDFMVSLAEAPRGGRVLEPACAHGPFLRAFREAHGTGYRFVGVEIDPKALDLPPWAEGILADFLLWEPGEAFDLILGNPPYGIVGVFKAVKDLYKKAFSTWKGKYNLYGAFLEKAVRLLKPGGVLVFVVPATWLVLEDFALLREFLAREGKTSVYYLGEVFPQKKVSAVVIRFQKSGKGLSLWDTQESESGFTPILWAEYPHWEGEIIRFETEETRKLEISGMPLGDLFHIRFAARSPEFKKHPAVRKEPGPGLVPVLTGRNLKPGWVDYEKNHSGLWMPKERAKELRDFYATPHLVVAHTKGTRVVAAWDERAYPWREEFHLLPKEGVRLDPSTLVQWLNSEAMQKHVRTLYRDFVPHLTLRMLERLPVRREYGFHT
>d1dcta_ 3.47.1.4.3 DNA methylase HaeIII, coenzyme-binding domain [Haemophilus aegyptius ]
MNLISLFSGAGGLDLGFQKAGFRIICANEYDKSIWKTYESNHSAKLIKGDISKISSDEFPKCDGIIGGPPCQSWSEGGSLRGIDDPRGKLFYEYIRILKQKKPIFFLAENVKGMMAQRHNKAVQEFIQEFDNAGYDVHIILLNANDYGVAQDRKRVFYIGFRKELNINYLPPIPHLIKPTFKDVIWDLKDNPIPALDKNKTNGNKCIYPNHEYFIGSYSTIFMSRNRVRQWNEPAFTVQASGRQCQLHPQAPVMLKVSKNLNKFVEGKEHLYRRLTVRECARVQGFPDDFIFHYESLNDGYKMIGNAVPVNLAYEIAKTIKSAL
>d7aata_ 3.48.1.1.1 Aspartate aminotransferase [chicken (Gallus gallus) mitochondria]
SSWWSHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLNCVRKAEAMIAAKKMDKEYLPIAGLADFTRASAELALGENSEAFKSGRYVTVQGISGTGSLRVGANFLQRFFKFSRDVYLPKPSWGNHTPIFRDAGLQLQAYRYYDPKTCSLDFTGAMEDISKIPEKSIILLHACAHNPTGVDPRQEQWKELASVVKKRNLLAYFDMAYQGFASGDINRDAWALRHFIEQGIDVVLSQSYAKNMGLYGERAGAFTVICRDAEEAKRVESQLKILIRPMYSNPPMNGARIASLILNTPELRKEWLVEVKGMADRIISMRTQLVSNLKKEGSSHNWQHITDQIGMFCFTGLKPEQVERLTKEFSIYMTKDGRISVAGVASSNVGYLAHAIHQVTK
>d2csta_ 3.48.1.1.2 Aspartate aminotransferase [chicken (Gallus gallus), cytosolic form]
AASIFAAVPRAPPVAVFKLTADFREDGDSRKVNLGVGAYRTDEGQPWVLPVVRKVEQLIAGDGSLNHEYLPILGLPEFRANASRIALGDDSPAIAQKRVGSVQGLGGTGALRIGAEFLRRWYNGNNNTATPVYVSSPTWENHNSVFMDAGFKDIRTYRYWDAAKRGLDLQGLLDDMEKAPEFSIFILHACAHNPTGTDPTPDEWKQIAAVMKRRCLFPFFDSAYQGFASGSLDKDAWAVRYFVSEGFELFCAQSFSKNFGLYNERVGNLSVVGKDEDNVQRVLSQMEKIVRTTWSNPPSQGARIVATTLTSPQLFAEWKDNVKTMADRVLLMRSELRSRLESLGTPGTWNHITDQIGMFSFTGLNPKQVEYMIKEKHIYLMASGRINMCGLTTKNLDYVAKSIHEAVTKIQ
>d1ajsa_ 3.48.1.1.3 Aspartate aminotransferase [pig sus scrofa, cytosolic form]
APPSVFAEVPQAQPVLVFKLIADFREDPDPRKVNLGVGAYRTDDCQPWVLPVVRKVEQRIANNSSLNHEYLPILGLAEFRTCASRLALGDDSPALQEKRVGGVQSLGGTGALRIGAEFLARWYNGTNNKDTPVYVSSPTWENHNGVFTTAGFKDIRSYRYWDTEKRGLDLQGFLSDLENAPEFSIFVLHACAHNPTGTDPTPEQWKQIASVMKRRFLFPFFDSAYQGFASGNLEKDAWAIRYFVSEGFELFCAQSFSKNFGLYNERVGNLTVVAKEPDSILRVLSQMQKIVRVTWSNPPAQGARIVARTLSDPELFHEWTGNVKTMADRILSMRSELRARLEALKTPGTWNHITDQIGMFSFTGLNPKQVEYLINQKHIYLLPSGRINMCGLTTKNLDYVATSIHEAVTKIQ
>d1art__ 3.48.1.1.4 Aspartate aminotransferase [Escherichia coli]
MFENITAAPADPILGLADLFRADERPGKINLGIGVYKDETGKTPVLTSVKKAEQYLLENETTKNYLGIDGIPEFGRCTQELLFGKGSALINDKRARTAQTPGGTGALRVAADFLAKNTSVKRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFDALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIVASSYSKNFGLYNERVGACTLVAADSETVDRAFSQMKAAIRANYSNPPAHGASVVATILSNDALRAIWEQELTDMRQRIQRMRQLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLRLREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVLD
>d1tpla_ 3.48.1.2.1 Tyrosine phenol-lyase [Citrobacter intermedius]
MNYPAEPFRIKSVETVSMIPRDERLKKMQEAGYNTFLLNSKDIYIDLLTDSGTNAMSDKQWAGMMMGDEAYAGSENFYHLERTVQELFGFKHIVPTHQGRGAENLLSQLAIKPGQYVAGNMYKNGAVFVDIVRDEAHDAGLNIAFKGDIDLKKLQKLIDEKGAENIAYICLAVTVNLAGGQPVSMANMRAVRELTAAHGIKVFYDATRCVENAYFIKEQEQGFENKSIAEIVHEMFSYADGCTMSGKKDCLVNIGGFLCMNDDEMFSSAKELVVVYEGMPSYGGLAGRDMEAMAIGLREAMQYEYIEHRVKQVRYLGDKLKAAGVPIVEPVGGHAVFLDARRFCEHLTQDEFPAQSLAASIYVETGVRSMERGIKLETVRLTIPRRVYTYAHMDVVADGIIKLYQHKEDIRGLKFIYFFTARFDYI
>d2dkb__ 3.48.1.3.1 Dialkylglycine decarboxylase [Pseudomonas cepacia]
LNDDATFWRNARHHLVRYGGTFEPMIIERAKGSFVYDADGRAILDFTSGQMSAVLGHCHPEIVSVIGEYAGKLDHLFSEMLSRPVVDLATRLANITPPGLDRALLLSTGAESNEAAIRMAKLVTGKYEIVGFAQSWHGMTGAAASATYSAGRKGVGPAAVGSFAIPAPFTYRPRFERNGAYDYLAELDYAFDLIDRQSSGNLAAFIAEPILSSGGIIELPDGYMAALKRKCEARGMLLILDEAQTGVGRTGTMFACQRDGVTPDILTLSKTLGAGLPLAAIVTSAAIEERAHELGYLFYTTHVSDPLPAAVGLRVLDVVQRDGLVARANVMGDRLRRGLLDLMERFDCIGDVRGRGLLLGVEIVKDRRTKEPADGLGAKITRECMNLGLSMNIVQLPGMGGVFRIAPPLTVSEDEIDLGLSLLGQAIERAL
>d1orda2 3.48.1.4.1 (108-569) Ornithine decarboxylase major domain [Lactobacillus 30a]
PPFFKSLKEYVSRGLIQFDCPGHQGGQYYRKHPAGREFYDFFGETVFRADLCNADVALGDLLIHEGPAVAAEKHAARVYNADKTYFVLGGSSNANNTVTSALVSNGDLVLFDRNNHKSVYNSALAMAGGRPVYLQTNRNPYGFIGGIYDSDFDEKKIRELAAKVDPERAKWKRPFRLAVIQLGTYDGTIYNAHEVVKRIGHLCDYIEFDSAWVGYEQFIPMMRNSSPLLIDDLGPEDPGIIVVQSVHKQQAGFSQTSQIHKKDSHIKGQLRYCDHKHFNNSFNLFMSTSPFYPMYAALDVNAAMQEGEAGRKLWHDLLITTIEARKKLIKAGSMFRPFVPPVVNGKKWEDGDTEDMANNIDYWRFEKGAKWHAYEGYGDNQYYVDPNKFMLTTPGINPETGDYEDFGVPATIVANYLRDHGIIPEKSDLNSILFLMTPAETPAKMNNLITQLLQLQRLIEED
>d1gpma2 3.49.1.1.1 (1-205) GMP synthetase [Escherichia coli]
ENIHKHRILILDFGSQYTQLVARRVRELGVYCELWAWDVTEAQIRDFNPSGIILSGGPESTTEENSPRAPQYVFEAGVPVFGVCYGMQTMAMQLGGHVEASNEREFGYAQVEVVNDSALVRGIEDALTADGKPLLDVWMSHGDKVTAIPSDFITVASTESCPFAIMANEEKRFYGVQFHPEVTHTRQGMRMLERFVRDICQCEAL
>d1dik_2 3.5.1.1.1 (376-504) Pyruvate phosphate dikinase, central domain [Escherichia coli]
LHPTFNPAALKAGEVIGSALPASPGAAAGKVYFTADEAKAAHEKGERVILVRLETSPEDIEGMHAAEGILTVRGGMTSHAAVVARGMGTCCVSGCGEIKINEEAKTFELGGHTFAEGDYISLDGSTGKI
>d1zyma_ 3.5.1.2.1 N-terminal domain of enzyme I of the PEP:sugar phosphotransferase system [Escherichia coli]
SGILASPGIAFGKALLLKEDEIVIDRKKISADQVDQEVERFLSGRAKASAQLETIKTKAGETFGEEKEAIFEGHIMLLEDEELEQEIIALIKDKHMTADAAAHEVIEGQASALEELDDEYLKERAADVRDIGKRLLRNILGLKIIDLSAIQDEVILVAADLTPSETAQLNLKKVLGFITDAGGRTSHTSIMARSLELPAIVGTGSVTSQVKNDDYLILDAVNNQVYVNPTNEVIDKMRAVQEQVASE
>d1aco_1 3.5.2.1.2 (528-753) Aconitase, C-terminal domain [bovine (Bos taurus)]
VDVSPTSQRLQLLEPFDKWDGKDLEDLQILIKVKGKCTTDHISAAGPWLKFRGHLDNISNNLLIGAINSENRKANSVRNAVTQEFGPVPDTARYYKQHGIRWVVIGDENYGEGSSREHSALEPRFLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYNKIHPVDKLTIQGLKDFAPGKPLTCIIKHPNGTQETILLNHTFNETQIEWFRAGSALNRMKELQQK
>d1grl_2 3.5.3.1.1 (186-361) the apical domain of GroEL [Escherichia coli]
EGMQFDRGYLSPYFINKPETGAVELESPFILLADKKISNIREMLPVLEAVAKAGKPLLIIAEDVEGEALATAVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISEEIGMELEKATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGRVAQIRQQIEEATSDYDREKLQ
>d1acj__ 3.50.1.1.1 Acetylcholinesterase [Electric ray (Torpedo californica)]
SELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPPVGNMRFRRPEPKKPWSGVWNASTYPNNCQQYVDEQFPGFSGSEMWNPNREMSEDCLYLNIWVPSPRPKSTTVMVWIYGGGFYSGSSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALHGSQEAPGNVGLLDQRMALQWVHDNIQFFGGDPKTVTIFGESAGGASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAEGRRRAVELGRNLNCNLNSDEELIHCLREKKPQELIDVEWNVLPFDSIFRFSFVPVIDGEFFPTSLESMLNSGNFKKTQILLGVNKDEGSFFLLYGAPGFSKDSESKISREDFMSGVKLSVPHANDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNVICPLMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYEIEFVFGLPLVKELNYTAEEEALSRRIMHYWATFAKTGNPNEPSKWPLFTTKEQKFIDLNTEPMKVHQRLRVQMCVFWNQFLPKLLNAT
>d1maha_ 3.50.1.1.3 Acetylcholinesterase [Murine (Mus musculus)]
EDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSAT
>d1yasa_ 3.50.1.10.1 Hydroxynitrile lyase [Rubber tree (Hevea brasiliensis)]
AFAHFVLIHTICHGAWIWHKLKPLLEALGHKVTALDLAASGVDPRQIEEIGSFDEYSEPLLTFLEALPPGEKVILVGESCGGLNIAIAADKYCEKIAAAVFHNSVLPDTEHCPSYVVDKLMEVFPDWKDTTYFTYTKDGKEITGLKLGFTLLRENLYTLCGPEEYELAKMLTRKGSLFQNILAKRPFFTKEGYGSIKKIYVWTDQDEIFLPEFQLWQIENYKPDKVYKVEGGDHKLQLTKTKEIAEILQEVADTYN
>d1wht.1 3.50.1.2.1 (a,b) Serine carboxypeptidase II [wheat (Triticum vulgaris)]
GHAADRIARLPGQPAVDFDMYSGYITVDEGAGRSLFYLLQEAPEDAQPAPLVLWLNGGPGCSSVAYGASEELGAFRVKPRGAGLVLNEYRWNKVANVLFLDSPAGVGFSYTNTSSDIYTSGDNRTAHDSYAFLAKWFERFPHYKYRDFYIAGESYAGHYVPELSQLVHRSKNPVINLKGFMVGNGLIDDYHDYVGTFEFWWNHGIVSDDTYRRLKEACLHDSFIHPSPACDAATDVATAEQGNIDMYSLYTPVCNITHWHDAPRSMLPIYRELIAAGLRIWVFSGDTDAVVPLTATRYSIGALGLPTTTSWYPWYDDQEVGGWSQVYKGLTLVSVRGAGHEVPLHRPRQALVLFQYFLQGKPMPGQGHAADRIARLPGQPAVDFDMYSGYITVDEGAGRSLFYLLQEAPEDAQPAPLVLWLNGGPGCSSVAYGASEELGAFRVKPRGAGLVLNEYRWNKVANVLFLDSPAGVGFSYTNTSSDIYTSGDNRTAHDSYAFLAKWFERFPHYKYRDFYIAGESYAGHYVPELSQLVHRSKNPVINLKGFMVGNGLIDDYHDYVGTFEFWWNHGIVSDDTYRRLKEACLHDSFIHPSPACDAATDVATAEQGNIDMYSLYTPVCNITHWHDAPRSMLPIYRELIAAGLRIWVFSGDTDAVVPLTATRYSIGALGLPTTTSWYPWYDDQEVGGWSQVYKGLTLVSVRGAGHEVPLHRPRQALVLFQYFLQGKPMPGQ
>d1cpy__ 3.50.1.2.2 Serine carboxypeptidase II [yeast (Saccharomyces cerevisiae)]
KIKDPKILGIDPNVTQYTGYLDVEDEDKHFFFWTFESRNDPAKDPVILWLNGGPGCSSLTGLFFALGPSSIGPDLKPIGNPYSWNSNATVIFLDQPVNVGFSYSGSSGVSNTVAAGKDVYNFLELFFDQFPEYVNKGQDFHIAGASYAGHYIPVFASEILSHKDRNFNLTSVLIGNGLTDPLTQYNYYEPMACGEGGEPSVLPSEECSAMEDSLERCLGLIESCYDSQSVWSCVPATIYCNNAQLAPYQRTGRNVYDIRKDCEGGNLCYPTLQDIDDYLNQDYVKEAVGAEVDHYESCNFDINRNFLFAGDWMKPYHTAVTDLLNQDLPILVYAGDKDFICNWLGNKAWTDVLPWKYDEEFASQKVRNWTASITDEVAGEVKSYKHFTYLRVFNGGHMVPFDVPENALSMVNEWIHGGFSL
>d1ac5__ 3.50.1.2.3 Serine carboxypeptidase II [yeast (Saccharomyces cerevisiae), kex1(delta)p]
LPSSEEYKVAYELLPGLSEVPDPSNIPQMHAGHIPLRSEDADEQDSSDLEYFFWKFTNNDSNGNVDRPLIIWLNGGPGCSSMDGALVESGPFRVNSDGKLYLNEGSWISKGDLLFIDQPTGTGFSVEQNKDEGKIDKNKFDEDLEDVTKHFMDFLENYFKIFPEDLTRKIILSGESYAGQYIPFFANAILNHNKFSKIDGDTYDLKALLIGNGWIDPNTQSLSYLPFAMEKKLIDESNPNFKHLTNAHENCQNLINSASTDEAAHFSYQECENILNLLLSYTRESSQKGTADCLNMYNFNLKDSYPSCGMNWPKDISFVSKFFSTPGVIDSLHLDSDKIDHWKECTNSVGTKLSNPISKPSIHLLPGLLESGIEIVLFNGDKDLICNNKGVLDTIDNLKWGGIKGFSDDAVSFDWIHKSKSTDDSEEFSGYVKYDRNLTFVSVYNASHMVPFDKSLVSRGIVDIYSNDVMIIDNNGKNVMITT
>d1ivya_ 3.50.1.2.4 human 'protective protein', HPP [Homo sapiens]
APDQDEIQRLPGLAKQPSFRQYSGYLKSSGSKHLHYWFVESQKDPENSPVVLWLNGGPGCSSLDGLLTEHGPFLVQPDGVTLEYNPYSWNLIANVLYLESPAGVGFSYSDDKFYATNDTEVAQSNFEALQDFFRLFPEYKNNKLFLTGESYAGIYIPTLAVLVMQDPSMNLQGLAVGNGLSSYEQNDNSLVYFAYYHGLLGNRLWSSLQTHCCSQNKCNFYDNKDLECVTNLQEVARIVGNSGLNIYNLYAPCAGGVPSHFRYEKDTVVVQDLGNIFTRLPLKRMWHQALLRSGDKVRMDPPCTNTTAASTYLNNPYVRKALNIPEQLPQWDMCNFLVNLQYRRLYRSMNSQYLKLLSSQKYQILLYNGDVDMACNFMGDEWFVDSLNQKMEVQRRPWLVKYGDSGEQIAGFVKEFSHIAFLTIKGAGHMVPTDKPLAAFTMFSRFLNKQPY
>d1ede__ 3.50.1.3.1 Haloalkane dehalogenase [Xanthobacter autotrophicus]
MINAIRTPDQRFSNLDQYPFSPNYLDDLPGYPGLRAHYLDEGNSDAEDVFLCLHGEPTWSYLYRKMIPVFAESGARVIAPDFFGFGKSDKPVDEEDYTFEFHRNFLLALIERLDLRNITLVVQDWGGFLGLTLPMADPSRFKRLIIMNACLMTDPVTQPAFSAFVTQPADGFTAWKYDLVTPSDLRLDQFMKRWAPTLTEAEASAYAAPFPDTSYQAGVRKFPKMVAQRDQACIDISTEAISFWQNDWNGQTFMAIGMKDKLLGPDVMYPMKALINGCPEPLEIADAGHFVQEFGEQVAREALKHFAETE
>d1din__ 3.50.1.4.1 Dienelactone hydrolase [Pseudomonas sp. B13]
MLTEGISIQSYDGHTFGALVGSPAKAPAPVIVIAQEIFGVNAFMRETVSWLVDQGYAAVCPDLYARQAPGTALDPQDERQREQAYKLWQAFDMEAGVGDLEAAIRYARHQPYSNGKVGLVGYCLGGALAFLVAAKGYVDRAVGYYGVGLEKQLNKVPEVKHPALFHMGGQDHFVPAPSRQLITEGFGANPLLQVHWYEEAGHSFARTSSSGYVASAAALANERTLDFLAPLQS
>d1broa_ 3.50.1.5.1 Bromoperoxidase A2 [Streptomyces aureofaciens]
PFITVGQENSTSIDLYYEDHGTGQPVVLIHGFPLSGHSWERQSAALLDAGYRVITYDRRGFGQSSQPTTGYDYDTFAADLNTVLETLDLQDAVLVGFSMGTGEVARYVSSYGTARIAKVAFLASLEPFLLKTDDNPDGAAPQEFFDGIVAAVKADRYAFYTGFFNDFYNLDENLGTRISEEAVRNSWNTAASGGFFAAAAAPTTWYTDFRADIPRIDVPALILHGTGDRTLPIENTARVFHKALPSAEYVEVEGAPHGLLWTHAEEVNTALLAFLAK
>d1thta_ 3.50.1.6.1 Myristoyl-ACP-specific thioesterase [Vibrio harveyi]
QCKTIAHVLRVNNGQELHVWETPPKENVPFKNNTILIASGFARRMDHFAGLAEYLSTNGFHVFRYDSLHHVEFTMTTGKNSLCTVYHWLQTKGTQNIGLIAASLSARVAYEVISDLELSFLITAVGVVNLRDTLEKALGFDYLSLPIDELPNDLDFEGHKLGSEVFVRDCFEHHWDTLDSTLDKVANTSVPLIAFTANNDDWVKQEEVYDMLAHIRTGHCKLYSLLGSSHDLGENLVVLRNFYQSVTKAAIAMDGGSLEIDVDFIEPDFEQLTIATVNERRLKAEIENRTPEMA
>d1tca__ 3.50.1.7.1 Triacylglycerol lipase [yeast (Candida antarctica) form b]
LPSGSDPAFSQPKSVLDAGLTCQGASPSSVSKPILLVPGTGTTGPQSFDSNWIPLSTQLGYTPCWISPPPFMLNDTQVNTEYMVNAITALYAGSGNNKLPVLTWSQGGLVAQWGLTFFPSIRSKVDRLMAFAPDYKGTVLAGPLDALAVSAPSVWQQTTGSALTTALRNAGGLTQIVPTTNLYSATDEIVQPQVSNSPLDSSYLFNGKNVQAQAVCGPLFVIDHAGSLTSQFSYVVGRSALRSTTGQARSADYGITDCNPLPANDLTPEQKVAAAALLAPAAAAIVAGPKQNCEPDLMPYARPFAVGKRTCSGIVTP
>d3tgl__ 3.50.1.7.2 Triacylglycerol lipase [Rhizomucor miehei]
GIRAATSQEINELTYYTTLSANSYCRTVIPGATWDCIHCDATEDLKIIKTWSTLIYDTNAMVARGDSEKTIYIVFRGSSSIRNWIADLTFVPVSYPPVSGTKVHKGFLDSYGEVQNELVATVLDQFKQYPSYKVAVTGHSLGGATVLLCALDLYQREEGLSSSNLFLYTQGQPRVGDPAFANYVVSTGIPYRRTVNERDIVPHLPPAAFGFLHAGEEYWITDNSPETVQVCTSDLETSDCSNSIVPFTSVLDHLSYFGINTGLCT
>d1tia__ 3.50.1.7.3 Triacylglycerol lipase [Penicillium caembertii]
DVSTSELDQFEFWVQYAAASYYEADYTAQVGDKLSCSKGNCPEVEATGATVSYDFSDSTITDTAGYIAVDHTNSAVVLAFRGSYSVRNWVADATFVHTNPGLCDGCLAELGFWSSWKLVRDDIIKELKEVVAQNPNYELVVVGHSLGAAVATLAATDLRGKGYPSAKLYAYASPRVGNAALAKYITAQGNNFRFTHTNDPVPKLPLLSMGYVHVSPEYWITSPNNATVSTSDIKVIDGDVSFDGNTGTGLPLLTDFEAHIWYFVQVDAGKG
>d1tib__ 3.50.1.7.4 Triacylglycerol lipase [Humicola lanuginosa]
EVSQDLFNQFNLFAQYSAAAYCGKNNDAPAGTNITCTGNACPEVEKADATFLYSFEDSGVGDVTGFLALDNTNKLIVLSFRGSRSIENWIGNLNFDLKEINDICSGCRGHDGFTSSWRSVADTLRQKVEDAVREHPDYRVVFTGHSLGGALATVAGADLRGNGYDIDVFSYGAPRVGNRAFAEFLTVQTGGTLYRITHTNDIVPRLPPREFGYSHSSPEYWIKSGTLVPVTRNDIVKIEGIDATGGNNQPNIPDIPAHLWYFGLIGTCL
>d1lgya_ 3.50.1.7.5 Triacylglycerol lipase [Rhizopus niveus]
KVVAATTAQIQEFTKYAGIAATAYCRSVVPGNKWDCVQCQKWVPDGKIITTFTSLLSDTNGYVLRSDKQKTIYLVFRGTNSFRSAITDIVFNFSDYKPVKGAKVHAGFLSSYEQVVNDYFPVVQEQLTAHPTYKVIVTGHSLGGAQALLAGMDLYQREPRLSPKNLSIFTVGGPRVGNPTFAYYVESTGIPFQRTVHKRDIVPHVPPQSFGFLHPGVESWIKSGTSNVQICTSEIETKDCSNSIVPFTSILDHLSYFDINEGSCL
>d1thg__ 3.50.1.7.7 type-B carboxylesterase/lipase [fungus (Geotrichum candidum) strain atcc 34614]
XAPTAVLNGNEVISGVLEGKVDTFKGIPFADPPLNDLRFKHPQPFTGSYQGLKANDFSPACMQLDPGNSLTLLDKALGLAKVIPEEFRGPLYDMAKGTVSMNEDCLYLNVFRPAGTKPDAKLPVMVWIYGGAFVYGSSAAYPGNSYVKESINMGQPVVFVSINYRTGPFGFLGGDAITAEGNTNAGLHDQRKGLEWVSDNIANFGGDPDKVMIFGESAGAMSVAHQLIAYGGDNTYNGKKLFHSAILQSGGPLPYHDSSSVGPDISYNRFAQYAGCDTSASANDTLECLRSKSSSVLHDAQNSYDLKDLFGLLPQFLGFGPRPDGNIIPDAAYELFRSGRYAKVPYISGNQEDEGTAFAPVALNATTTPHVKKWLQYIFYDASEASIDRVLSLYPQTLSVGSPFRTGILNALTPQFKRVAAILSDMLFQSPRRVMLSATKDVNRWTYLSTHLHNLVPFLGTFHGNELIFQFNVNIGPANSYLRYFISFANHHDPNVGTNLLQWDQYTDEGKEMLEIHMTDNVMRTDDYRIEGISNFETDVNLYG
>d1lpp__ 3.50.1.7.8 type-B carboxylesterase/lipase [fungus (Candida rugosa, formerly cylindracea)]
APTATLANGDTITGLNAIINEAFLGIPFAEPPVGNLRFKDPVPYSGSLDGQKFTSYGPSCMQQNPEGTYEENLPKAALDLVMQSKVFEAVSPSSEDCLTINVVRPPGTKAGANLPVMLWIFGGGFEVGGTSTFPPAQMITKSIAMGKPIIHVSVNYRVSSWGFLAGDEIKAEGSANAGLKDQRLGMQWVADNIAAFGGDPTKVTIFGESAGSMSVMCHILWNDGDNTYKGKPLFRAGIMQSGAMVPSDAVDGIYGNEIFDLLASNAGCGSASDKLACLRGVSSDTLEDATNNTPGFLAYSSLRLSYLPRPDGVNITDDMYALVREGKYANIPVIIGDQNDEGTFFGTSSLNVTTDAQAREYFKQSFVHASDAEIDTLMTAYPGDITQGSPFDTGILNALTPQFKRISAVLGDLGFTLARRYFLNHYTGGTKYSFLSKQLSGLPVLGTFHSNDIVFQDYLLGSGSLIYNNAFIAFATDLDPNTAGLLVKWPEYTSSSQSGNNLMMINALGLYTGKDNFRTAGYDALFSNPPSFFV
>d1clea_ 3.50.1.7.9 type-B carboxylesterase/lipase [Candida cylindracea), cholesterol esterase]
APTAKLANGDTITGLNAIINEAFLGIPFAEPPVGNLRFKDPVPYSGSLNGQKFTSYGPSCMQQNPEGTFEENLGKTALDLVMQSKVFQAVLPQSEDCLTINVVRPPGTKAGANLPVMLWIFGGGFEIGSPTIFPPAQMVTKSVLMGKPIIHVAVNYRVASWGFLAGDDIKAEGSGNAGLKDQRLGMQWVADNIAGFGGDPSKVTIFGESAGSMSVLCHLIWNDGDNTYKGKPLFRAGIMQSGAMVPSDPVDGTYGNEIYDLFVSSAGCGSASDKLACLRSASSDTLLDATNNTPGFLAYSSLRLSYLPRPDGKNITDDMYKLVRDGKYASVPVIIGDQNDEGTVFGLSSLNVTTNAQARAYFKQSFIHASDAEIDTLMAAYPQDITQGSPFDTGIFNAITPQFKRISAVLGDLAFIHARRYFLNHFQGGTKYSFLSKQLSGLPIMGTFHANDIVWQDYLLGSGSVIYNNAFIAFATDLDPNTAGLLVNWPKYTSSSQSGNNLMMINALGLYTGKDNFRTAGYDALMTNPSSFFV
>d1tahb_ 3.50.1.8.1 Bacterial lipase [Pseudomonas glumae, also known as Pseudomonas gladioli]
DTYAATRYPVILVHGLAGTDKFANVVDYWYGIQSDLQSHGAKVYVANLSGFQSDDGPNGRGEQLLAYVKQVLAATGATKVNLIGHSQGGLTSRYVAAVAPQLVASVTTIGTPHRGSEFADFVQDVLKTDPTGLSSTVIAAFVNVFGTLVSSSHNTDQDALAALRTLTTAQTATYNRNFPSAGLGAPGSCQTGAATETVGGSQHLLYSWGGTAIQPTSTVLGVTGATDTSTGTLDVANVTDPSTLALLATGAVMINRASGQNDGLVSRCSSLFGQVISTSYHWNHLDEINQLLGVRGANAEDPVAVIRTHVNRLKLQGV
>d3lip__ 3.50.1.8.2 Bacterial lipase [Pseudomonas cepacia]
ADNYAATRYPIILVHGLTGTDKYAGVLEYWYGIQEDLQQRGATVYVANLSGFQSDDGPNGRGEQLLAYVKTVLAATGATKVNLVGHSQGGLTSRYVAAVAPDLVASVTTIGTPHRGSEFADFVQGVLAYDPTGLSSTVIAAFVNVFGILTSSSNNTNQDALAALKTLTTAQAATYNQNYPSAGLGAPGSCQTGAPTETVGGNTHLLYSWAGTAIQPTISVFGVTGATDTSTIPLVDPANALDPSTLALFGTGTVMVNRGSGQNDGVVSKCSALYGQVLSTSYKWNHLDEINQLLGVRGANAEDPVAVIRTHANRLKLAGV
>d1hpla2 3.50.1.9.1 (1-337) Pancreatic lipase, N-terminal domain [horse (Equus caballus)]
NEVCYERLGCFSDDSPWAGIVERPLKILPWSPEKVNTRFLLYTNENPDNFQEIVADPSTIQSSNFNTGRKTRFIIHGFIDKGEESWLSTMCQNMFKVESVNCICVDWKSGSRTAYSQASQNVRIVGAEVAYLVGVLQSSFDYSPSNVHIIGHSLGSHAAGEAGRRTNGAVGRITGLDPAEPCFQGTPELVRLDPSDAQFVDVIHTDIAPFIPNLGFGMSQTAGHLDFFPNGGKEMPGCQKNVLSQIVDIDGIWQGTRDFAACNHLRSYKYYTDSILNPDGFAGFSCASYSDFTANKCFPCSSEGCPQMGHYADRFPGRTKGVGQLFYLNTGDASNFA
>d1etha2 3.50.1.9.2 (1-336) Pancreatic lipase, N-terminal domain [pig (Sus scrofa)]
SEVCFPRLGCFSDDAPWAGIVQRPLKILPWSPKDVDTRFLLYTNQNQNNYQELVADPSTITNSNFRMDRKTRFIIHGFIDKGEEDWLSNICKNLFKVESVNCICVDWKGGSRTGYTQASQNIRIVGAEVAYFVEVLKSSLGYSPSNVHVIGHSLGSHAAGEAGRRTNGTIERITGLDPAEPCFQGTPELVRLDPSDAKFVDVIHTDAAPIIPNLGFGMSQTVGHLDFFPNGGKQMPGCQKNILSQIVDIDGIWEGTRDFVACNHLRSYKYYADSILNPDGFAGFPCDSYNVFTANKCFPCPSEGCPQMGHYADRFPGKTNGVSQVFYLNTGDASNF
>d1lpbb2 3.50.1.9.3 (1-337) Pancreatic lipase, N-terminal domain [human (Homo sapience)]
KEVCYERLGCFSDDSPWSGITERPLHILPWSPKDVNTRFLLYTNENPNNFQEVAADSSSISGSNFKTNRKTRFIIHGFIDKGEENWLANVCKNLFKVESVNCICVDWKGGSRTGYTQASQNIRIVGAEVAYFVEFLQSAFGYSPSNVHVIGHSLGAHAAGEAGRRTNGTIGRITGLDPAEPCFQGTPELVRLDPSDAKFVDVIHTDGAPIVPNLGFGMSQVVGHLDFFPNGGVEMPGCKKNILSQIVDIDGIWEGTRDFAACNHLRSYKYYTDSIVNPDGFAGFPCASYNVFTANKCFPCPSGGCPQMGHYADRYPGKTNDVGQKFYLDTGDASNFA
>d1gpl_2 3.50.1.9.4 (1-320) Pancreatic lipase, N-terminal domain [Guinea pig (Cavia porcellus)]
AEVCYSHLGCFSDEKPWAGTSQRPIKSLPSDPKKINTRFLLYTNENQNSYQLITATDIATIKASNFNLNRKTRFIIHGFTDSGENSWLSDMCKNMFQVEKVNCICVDWKGGSKAQYSQASQNIRVVGAEVAYLVQVLSTSLNYAPENVHIIGHSLGAHTAGEAGKRLNGLVGRITGLDPAEPYFQDTPEEVRLDPSDAKFVDVIHTDISPILPSLGFGMSQKVGHMDFFPNGGKDMPGCKTGISCNHHRSIEYYHSSILNPEGFLGYPCASYDEFQESGCFPCPAKGCPKMGHFADQYPGKTNAVEQTFFLNTGASDNFT
>d2masa_ 3.51.1.1.1 Inosine-uridine nucleoside N-ribohydrolase, IU-NH [(Crithidia fasciculata)]
AKKIILDCDPGLDDAVAILLAHGNPEIELLAITTVVGNQTLAKVTRNAQLVADIAGITGVPIAAGCDKPLVRKIMTAGHIHGESGMGTVAYPAEFKNKVDERHAVNLIIDLVMSHEPKTITLVPTGGLTNIAMAARLEPRIVDRVKEVVLMGGGYHEGNATSVAEFNIIIDPEAAHIVFNESWQVTMVGLDLTHQALATPPILQRVKEVDTNPARFMLEIMDYYTKIYQSNRYMAAAAVHDPCAVAYVIDPSVMTTERVPVDIELTGKLTLGMTVADFRNPRPEHCHTQVAVKLDFEKFWGLVLDALERIGDP
>d1ulb__ 3.52.1.1.1 Purine nucleoside phosphorylase, PNP [human (Homo sapiens)]
MENGYTYEDYKNTAEWLLSHTKHRPQVAIICGSGLGGLTDKLTQAQIFDYSEIPNFPRSTVPGHAGRLVFGFLNGRACVMMQGRFHMYEGYPLWKVTFPVRVFHLLGVDTLVVTNAAGGLNPKFEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPAMSDAYDRTMRQRALSTWKQMGEQRELQEGTYVMVAGPSFETVAECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVIMDYESLEKANHEEVLAAGKQAAQKLEQFVSILMASIPLPDKAS
>d1pbn__ 3.52.1.1.2 Purine nucleoside phosphorylase, PNP [Bovine (Bos taurus)]
MANGYTYEDYQDTAKWLLSHTEQRPQVAVICGSGLGGLVNKLTQAQTFDYSEIPNFPESTVPGHAGRLVFGILNGRACVMMQGRFHMYEGYPFWKVTFPVRVFRLLGVETLVVTNAAGGLNPNFEVGDIMLIRDHINLPGFSGENPLRGPNEERFGVRFPAMSDAYDRDMRQKAHSTWKQMGEQRELQEGTYVMLGGPNFETVAECRLLRNLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVIMDTESQGKANHEEVLEAGKQAAQKLEQFVSLLMASIPVSGHTG
>d1ecpa_ 3.52.1.1.3 Purine nucleoside phosphorylase, PNP [Escherichia coli]
ATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITDFGVKKIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFYSPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLGDK
>d2ctb__ 3.52.3.1.1 Carboxypeptidase A [bovine (Bos taurus)]
ARSTNTFNYATYHTLDEIYDFMDLLVAEHPQLVSKLQIGRSYEGRPIYVLKFSTGGSNRPAIWIDLGIHSREWITQATGVWFAKKFTEDYGQDPSFTAILDSMDIFLEIVTNPDGFAFTHSQNRLWRKTRSVTSSSLCVGVDANRNWDAGFGKAGASSSPCSETYHGKYANSEVEVKSIVDFVKDHGNFKAFLSIHSYSQLLLYPYGYTTQSIPDKTELNQVAKSAVEALKSLYGTSYKYGSIITTIYQASGGSIDWSYNQGIKYSFTFELRDTGRYGFLLPASQIIPTAQETWLGVLTIMEHTLNN
>d1pca_1 3.52.3.1.2 (1-402) Carboxypeptidase A [porcine (Sus scrofa)]
KEDFVGHQVLRISVDDEAQVQKVKELEDLEHLQLDFWRGPARPGFPIDVRVPFPSIQAVKVFLEAHGIRYTIMIEDVQLLLDEEQEQMFASQGRARTTSTFNYATYHTLEEIYDFMDILVAEHPALVSKLQIGRSYEGRPIYVLKFSTGGSNRPAIWIDSGIHSREWITQASGVWFAKKITENYGQNSSFTAILDSMDIFLEIVTNPNGFAFTHSDNRLWRKTRSKASGSLCVGSDSNRNWDAGFGGAGASSSPCAETYHGKYPNSEVEVKSITDFVKNNGNIKAFISIHSYSQLLLYPYGYKTQSPADKSELNQIAKSAVAALKSLYGTSYKYGSIITVIYQASGGVIDWTYNQGIKYSFSFELRDTGRRGFLLPASQIIPTAQETWLALLTIMEHTLNNSV
>d1cpb__ 3.52.3.1.3 Carboxypeptidase B [bovine (Bos taurus)]
TTGHSYEKYNNWETIEAWTEQVASENPDLISRSAIGTTFLGNTIYLLKVGKPGSNKPAVFMDCGFHAREWISPAFCQWFVREEIHMTEFLDKLDFYVLPVVNIDGYIYTWTTNRMWRKTRSTRAGSSCTGTDLNRNFDAGWCSIGASNNPCSETYCGSAAESEKESKAVADFIRNHLSSIKAYLTIHSYSQMMLYPYSYDYKLPKNNVELNTLAKGAVKKLASLHGTTYSYGPGATTIYPASGGSDDWAYDQGIKYSFTFELRDKGRYGFVLPESQIQPTCEETMLAIKYVTSYVLEHL
>d1obr__ 3.52.3.2.1 Carboxypeptidase T [Thermoactinomyces vulgaris]
DFPSYDSGYHNYNEMVNKINTVASNYPNIVKKFSIGKSYEGRELWAVKISDNVGTDENEPEVLYTALHHAREHLTVEMALYTLDLFTQNYNLDSRITNLVNNREIYIVFNINPDGGEYDISSGSYKSWRKNRQPNSGSSYVGTDLNRNYGYKWGCCGGSSGSPSSETYRGRSAFSAPETAAMRDFINSRVVGGKQQIKTLITFHTYSELILYPYGYTYTDVPSDMTQDDFNVFKTMANTMAQTNGYTPQQASDLYITDGDMTDWAYGQHKIFAFTFEMYPTSYNPGFYPPDEVIGRETSRNKEAVLYVAEKADCPYSVIGKSC
>d1lam_2 3.52.3.3.1 (160-484) Leucine aminopeptidase, C-terminal domain [bovine (Bos taurus)]
FASGQNLARRLMETPANEMTPTKFAEIVEENLKSASIKTDVFIRPKSWIEEQEMGSFLSVAKGSEEPPVFLEIHYKGSPNASEPPLVFVGKGITFDSGGISIKAAANMDLMRADMGGAATICSAIVSAAKLDLPINIVGLAPLCENMPSGKANKPGDVVRARNGKTIQVDNTDAEGRLILADALCYAHTFNPKVIINAATLTGAMDIALGSGATGVFTNSSWLWNKLFEASIETGDRVWRMPLFEHYTRQVIDCQLADVNNIGKYRSAGACTAAAFLKEFVTHPKWAHLDIAGVMTNKDEVPYLRKGMAGRPTRTLIEFLFRFSQ
>d1amp__ 3.52.3.4.1 Aminopeptidase [Aeromonas proteolytica]
MPPITQQATVTAWLPQVDASQITGTISSLESFTNRFYTTTSGAQASDWIASEWQALSASLPNASVKQVSHSGYNQKSVVMTITGSEAPDEWIVIGGHLDSTIGSHTNEQSVAPGADDDASGIAAVTEVIRVLSENNFQPKRSIAFMAYAAEEVGLRGSQDLANQYKSEGKNVVSALQLDMTNYKGSAQDVVFITDYTDSNFTQYLTQLMDEYLPSLTYGFDTCGYACSDHASWHNAGYPAAMPFESKFNDYNPRIHTTQDTLANSDPTGSHAKKFTQLGLAYAIEMGSATG
>d1xjo__ 3.52.3.4.2 Aminopeptidase [Streptomyces griseus]
APDIPLANVKAHLTQLSTIAANNGGNRAHGRPGYKASVDYVKAKLDAAGYTTTLQQFTSGGATGYNLIANWPGGDPNKVLMAGAHLDSVSSGAGINDNGSGSAAVLETALAVSRAGYQPDKHLRFAWWGAEELGLIGSKFYVNNLPSADRSKLAGYLNFDIGSPNPGYFVYDDDPVIEKTFKNYFAGLNVPTEIRSDHAPFKNVGVPVGGLFTGAGYTKSAAQAQKWGGTAGQAFDRCYHSSCDSLSNINDTALDRNSDAAAHAIWTLSS
>d1draa_ 3.53.1.1.1 Dihydrofolate reductase, prokaryotic type [Escherichia coli]
MISLIAALAVDRVIGMENAMPWNLPAELAWFKRNTLDKPVIMGRHTWESIGRPLPGRKNIILSSQPGTDDRVTWVKSVDEAIAACGDVPEIMVIGGGRVYEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILERR
>d3dfr__ 3.53.1.1.2 Dihydrofolate reductase, prokaryotic type [Lactobacillus casei]
TAFLWAQNRNGLIGKDGHLPWHLPDDLHYFRAQTVGKIMVVGRRTYESFPKRPLPERTNVVLTHQEDYQAQGAVVVHDVAAVFAYAKQHLDQELVIAGGAQIFTAFKDDVDTLLVTRLAGSFEGDTKMIPLNWDDFTKVSSRTVEDTNPALTHTYEVWQKKA
>d8dfr__ 3.53.1.1.3 Dihydrofolate reductases, eukaryotic type [chicken (Gallus gallus)]
VRSLNSIVAVCQNMGIGKDGNLPWPPLRNEYKYFQRMTSTSHVEGKQNAVIMGKKTWFSIPEKNRPLKDRINIVLSRELKEAPKGAHYLSKSLDDALALLDSPELKSKVDMVWIVGGTAVYKAAMEKPINHRLFVTRILHEFESDTFFPEIDYKDFKLLTEYPGVPADIQEEDGIQYKFEVYQKSV
>d1dls__ 3.53.1.1.4 Dihydrofolate reductases, eukaryotic type [human (Homo sapiens)]
VGSLNCIVAVSQNMGIGKNGDYPWPPLRNEFRYFQRMTTTSSVEGKQNLVIMGKKTWFSIPEKNRPLKGRINLVLSRELKEPPQGAHFLSRSLDDALKLTEQPELANKVDMVWIVGGSSVYKEAMNHPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLPEYPGVLSDVQEEKGIKYKFEVYEKND
>d1dyr__ 3.53.1.1.5 Dihydrofolate reductases, eukaryotic type [fungus (Pneumocystis carinii)]
NQQKSLTLIVALTTSYGIGRSNSLPWKLKKEISYFKRVTSFVPTFDSFESMNVVLMGRKTWESIPLQFRPLKGRINVVITRNESLDLGNGIHSAKSLDHALELLYRTYGSESSVQINRIFVIGGAQLYKAAMDHPKLDRIMATIIYKDIHCDVFFPLKFRDKEWSSVWKKEKHSDLESWVGTKVPHGKINEDGFDYEFEMWTRDL
>d1hrda2 3.54.1.1.1 (1-194) Glutamate dehydrogenase, N-terminal domain [Clostridium symbiosum]
SKYVDRVIAEVEKKYADEPEFVQTVEEVLSSLGPVVDAHPEYEEVALLERMVIPERVIEFRVPWEDDNGKVHVNTGYRVQFNGAIGPYKGGLRFAPSVNLSIMKFLGFEQAFKDSLTTLPMGGAKGGSDFDPNGKSDREVMRFCQAFMTELYRHIGPDIDVPAGDLGVGAREIGYMYGQYRKIVGGFYNGVLTG
>d1gtma2 3.54.1.1.2 (1-178) Glutamate dehydrogenase, N-terminal domain [Pyrococcus furiosis]
ADPYEIVIKQLERAAQYMEISEEALEFLKRPQRIVEVTIPVEMDDGSVKVFTGFRVQHNWARGPTKGGIRWHPEETLSTVKALAAWMTWKTAVMDLPYGGGKGGIIVDPKKLSDREKERLARGYIRAIYDVISPYEDIPAPDVYTNPQIMAWMMDEYETISRRKTPAFGIITGKPLSI
>d1leha2 3.54.1.1.3 (1-134) Leucine dehydrogenase, N-terminal domain [Bacillus sphaericus]
MEIFKYMEKYDYEQLVFCQDEASGLKAVIAIHDTTLGPALGGARMWTYNAEEEAIEDALRLARGMTYKNAAAGLNLGGGKTVIIGDPFADKNEDMFRALGRFIQGLNGRYITAEDVGTTVDDMDLIHQETDYVT
>d1fua__ 3.55.1.1.1 L-fuculose-1-phospate aldolase [Escherichia coli]
MERNKLARQIIDTCLEMTRLGLNQGTAGNVSVRYQDGMLITPTGIPYEKLTESHIVFIDGNGKHEEGKLPSSEWRFHMAAYQSRPDANAVVHNHAVHCTAVSILNRSIPAIHYMIAAAGGNSIPCAPYATFGTRELSEHVALALKNRKATLLQHHGLIACEVNLEKALWLAHEVEVLAQLYLTTLAITDPVPVLSDEEIAVVLEKF
>d2anha_ 3.56.1.1.1 Alkaline phosphatase [Escherichia coli]
MPVLENRAAQGDITAPGGARRLTGDQTAALRDSLSDKPAKNIILLIGDGMGDSEITAARNYAEGAGGFFKGIDALPLTGQYTHYALNKKTGKPDYVTDSAASATAWSTGVKTYNGALGVDIHEKDHPTILEMAKAAGLATGNVSTAELQHATPAALVAHVTSRKCYGPSATSEKCPGNALEKGGKGSITEQLLNARADVTLGGGAKTFAETATAGEWQGKTLREQAQARGYQLVSDAASLNSVTEANQQKPLLGLFADGNMPVRWLGPKATYHGNIDKPAVTCTPNPQRNDSVPTLAQMTDKAIELLSKNEKGFFLQVEGASIDKQDHAANPCGQIGETVDLDEAVQRALEFAKKEGNTLVIVTADHAHASQIVAPDTKAPGLTQALNTKDGAVMVMSYGNSEEDSQEHTGSQLRIAAYGPHAANVVGLTDQTDLFYTMKAALGLK
>d1idm__ 3.57.1.1.1 3-isopropylmalate dehydrogenase [Thermus thermophilus, strain HB8]
MKVAVLPGDGIGPEVTEAALKVLRALDEAEGLGLAYEVFPFGGAAIDAFGEPFPEPTRKGVEEAEAVLLGSVGGPKWGTGSVRPEQGLLSLRKSQDLFANLRPAKVFPGLERLSPLKEEIARGVDVLIVRELTGGIYFGEPRGMSEAEAWNTERYSKPEVERVARVAFEAARKRRKHVVSVDKANVLEVGEFWRKTVEEVGRGYPDVALEHQYVDAMAMHLVRSPARFDVVVTGNIFGDILSDLASVLPGSLGLLPSASLGRGTPVFEPVHGSAPDIAGKGIANPTAAILSAAMMLEHAFGLVELARKVEDAVAKALLETPPPDLGGSAGTEAFTATVLRHLA
>d1xac__ 3.57.1.1.2 3-isopropylmalate dehydrogenase [chimera (Thermus thermophilus/Bacillus subtilis)]
MKVAVLPGDGIGPEVTEAALKVLRALDEAEGLGLAYEVFPFGGAAIDAFGEPFPEPTRKGVEEAEAVLLGSVGGPKWDQNPRELRPEKGLLSIRKQLDLFANLRPVKVFESLSDASPLKKEYIDNVDFVIVRELTGGIYFGEPRGMSEAEAWNTERYSKPEVERVARVAFEAARKRRKHVVSVDKANVLEVGEFWRKTVEEVGRGYPDVALEHQYVDAMAMHLVRSPARFDVVVTGNIFGDILSDLASVLPGSLGLLPSASLGRGTPVFEPVHGSAPDIAGKGIANPTAAILSAAMMLEHAFGLVELARKVEDAVAKALLETPPPDLGGSAGTEAFTATVLRHLA
>d7icd__ 3.57.1.1.3 Isocitrate dehydrogenase [Escherichia coli]
SKVVVPAQGKKITLQNGKLNVPENPIIPYIEGDGIGVDVTPAMLKVVDAAVEKAYKGERKISWMEIYTGEKSTQVYGQDVWLPAETLDLIREYRVAIKGPLTTPVGGGIRELNVALRQELDLYICLRPVRYYQGTPSPVKHPELTDMVIFRENSEDIYAGIEWKADSADAEKVIKFLREEMGVKKIRFPEHCGIGIKPCSEEGTKRLVRAAIEYAIANDRDSVTLVHKGNIMKFTEGAFKDWGYQLAREEFGGELIDGGPWLKVKNPNTGKEIVIKDVIADAFLQQILLRPAEYDVIACMNLNGDYISDALAAQVGGIGIAPGANIGDECALFEATHGTAPKYAGQDKVNPGSIILSAEMMLRHMGWTEAADLIVKGMEGAINAKTVTYDFERLMDGAKLLKCSEFGDAIIENM
>d1raaa2 3.58.1.1.1 (151-310) Aspartate carbamoyltransferase [Escherichia coli]
RLDNLHVAMVGDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPQYILDMLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEYANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKTPHAWYFQQAGNGIFARQALLALVLNRDLVL
>d1raaa1 3.58.1.1.1 (1-150) Aspartate carbamoyltransferase [Escherichia coli]
ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLKHKVIASCFFEASTRTRLSFETSMHRLGASVVGFSDSANTSLGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSGNVPVLNAGDGSNQHPTQTLLDLFTIQETQG
>d2at2a1 3.58.1.1.2 (1-144) Aspartate carbamoyltransferase [Bacillus subtilis]
MKHLTTMSELSTEEIKDLLQTAQELKSGKTDNQLTGKFAANLFFEPSTRTRFSFEVAEKKLGMNVLNLDGTSTSVQKGETLYDTIRTLESIGVDVCVIRHSEDEYYEELVSQVNIPILNAGDGCGQHPTQSLLDLMTIYEEFNT
>d2at2a2 3.58.1.1.2 (145-295) Aspartate carbamoyltransferase [Bacillus subtilis]
FKGLTVSIHGDIKHSRVARSNAEVLTRLGARVLFSGPSEWQDEENTFGTYVSMDEAVESSDVVMLLRIQNERHQSAVSQEGYLNKYGLTVERAERMKRHAIIMHPAPVNRGVEIDDSLVESEKSRIFKQMKNGVFIRMAVIQCALQTNVKR
>d1orta1 3.58.1.1.3 (1-150) Ornithine transcarbamoylase [(Pseudomonas aeruginosa)]
AFNMHNRNLLSLMHHSTRELRYLLDLSRDLKRAKYTGTEQQHLKRKNIALIFEKTSTRTRCAFEVAAYDQGANVTYIDPNSSQIGHKESMKDTARVLGRMYDAIGYRGFKQEIVEELAKFAGVPVFNGLTDEYHPTQMLADVLTMREHSD
>d1orta2 3.58.1.1.3 (151-335) Ornithine transcarbamoylase [(Pseudomonas aeruginosa)]
KPLHDISYAYLGDARNNMGNSLLLIGAKLGMDVRIAAPKALWPHDEFVAQCKKFAEESGAKLTLTEDPKEAVKGVDFVHTDVWVSMGEPVEAWGERIKELLPYQVNMEIMKATGNPRAKFMHCLPAFHNSETKVGKQIAEQYPNLANGIEVTEDVFESPYNIAFEQAENRMHTIKAILVSTLADI
>d1wsyb_ 3.59.1.1.1 Tryptophan synthase, beta-subunit [Salmonella typhimurium]
FGEFGGMYVPQILMPALNQLEEAFVRAQKDPEFQAQFADLLKNYAGRPTALTKCQNITAGTRTTLYLKREDLLHGGAHKTNQVLGQALLAKRMGKSEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRLMGAEVIPVHSGSATLKDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIVREFQRMIGEETKAQILDKEGRLPDAVIACVGGGSNAIGMFADFINDTSVGLIGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTADGQIEESYSISAGLDFPSVGPQHAYLNSIGRADYVSITDDEALEAFKTLCRHEGIIPALESSHALAHALKMMREQPEKEQLLVVNLSGRGDKDIFTVHDILKA
>d1brsd_ 3.6.1.1.1 Barstar (barnase inhibitor) [Bacillus amyloliquefaciens]
KKAVINGEQIRSISDLHQTLKKELALPEYYGENLDALWDALTGWVEYPLVLEWRQFEQSKQLTGAESVLQVFREAKAEGADITIILS
>d1orb_1 3.60.1.1.1 (1-149) Rhodanese [bovine (Bos taurus)]
VHQVLYRALVSTKWLAESVRAGKVGPGLRVLDASWYSPGTREARKEYLERHVPGASFFDIEECRDKASPYEVMLPSEAGFADYVGSLGISNDTHVVVYDGDDLGSFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEGHPVTSEPSRPEP
>d1orb_2 3.60.1.1.1 (150-293) Rhodanese [bovine (Bos taurus)]
AIFKATLNRSLLKTYEQVLENLESKRFQLVDSRAQGRYLGTQPEPDAVGLDSGHIRGSVNMPFMNFLTEDGFEKSPEELRAMFEAKKVDLTKPLIATCRKGVTACHIALAAYLCGKPDVAIYDGSWFEWFHRAPPETWVSQGKG
>d1cxsa2 3.61.1.1.1 (1-613) Dimethylsulfoxide reductase (DMSO reductase) [Rhodobacter sphaeroides]
EGLANGEVMSGCHWGVFKARVENGRAVAFEPWDKDPAPSHQLPGVLDSIYSPTRIKYPMVRREFLEKGVNADRSTRGNGDFVRVTWDEALDLVARELKRVQESYGPTGTFGGSYGWKSPGRLHNCQVLMRRALNLAGGFVNSSGDYSTAAAQIIMPHVMGTLEVYEQQTAWPVVVENTDLMVFWAADPMKTNEIGWVIPDHGAYAGMKALKEKGTRVICINPVRTETADYFGADVVSPRPQTDVALMLGMAHTLYSEDLHDKDFLENCTTGFDLFAAYLTGESDGTPKTAEWAAEICGLPAEQIRELARSFVAGRTMLAAGWSIQRMHHGEQAHWMLVTLASMIGQIGLPGGGFGLSYHYSNGGSPTSDGPALGGISDGGWATSIPCARVVDMLLNPGGEFQFNGATATYPDVKLAYWAGGNPFAHHQDRNRMLKAWEKLETFIVQDFQWTATARHADIVLPATTSYERNDIESVGDYSNRAILAMKKVVDPLYEARSDYDIFAALAERLGKGAEFTEGRDEMGWISSFYEAAVKQAEFKNVAMPSFEDFWSEGIVEFPITEGANFVRYADFREDPLFNPLGTPSGLIEIYSKNIEKMGYDDCPAHPTWMEPA
>d1fdo_2 3.61.1.1.2 (1-563) Formate dehydrogenase H [Escherichia coli]
MKKVVTVCPYCASGCKINLVVDNGKIVRAEAAQGKTNQGTLCLKGYYGWDFINDTQILTPRLKTPMIRRQRGGKLEPVSWDEALNYVAERLSAIKEKYGPDAIQTTGSSRGTGNETNYVMQKFARAVIGTNNVDCCARVHGPSVAGLHQSVGNGAMSNAINEIDNTDLVFVFGYNPADSHPIVANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAMGHVIIEENLYDKAFVASRTEGFEEYRKIVEGYTPESVEDITGVSASEIRQAARMYAQAKSAAILWGMGVTQFYQGVETVRSLTSLAMLTGNLGKPHAGVNPVRGQNNVQGACDMGALPDTYPGYQYVKDPANREKFAKAWGVESLPAHTGYRISELPHRAAHGEVRAAYIMGEDPLQTDAELSAVRKAFEDLELVIVQDIFMTKTASAADVILPSTSWGEHEGVFTAADRGFQRFFKAVEPKWDLKTDWQIISEIATRMGYPMHYNNTQEIWDELRHLCPDFYGATYEKMGELGFIQWPCRDTSDADQGTSYLFKEKFDTPNGLAQFFTCDWVA
>d1ad3a_ 3.62.1.1.1 Aldehyde reductase (class III enzyme) [rat (Rattus norvegicus)]
SISDTVKRAREAFNSGKTRSLQFRIQQLEALQRMINENLKSISGALASDLGKNEWTSYYEEVAHVLEELDTTIKELPDWAEDEPVAKTRQTQQDDLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAVAAGNAVILKPSEVSGHMADLLATLIPQYMDQNLYLVVKGGVPETTELLKERFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKDFYGEDAKQSRDYGRIINDRHFQRVKGLIDNQKVAHGGTWDQSSRYIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLEEAIQFINQREKPLALYVFSNNEKVIKKMIAETSSGGVTANDVIVHITVPTLPFGGVGNSGMGAYHGKKSFETFSHRRSCLVKSLLNEEAHKARYPPSPA
>d1ag8a_ 3.62.1.1.2 Aldehyde reductase (class III enzyme) [bovine (Bos taurus) mitochondria]
VPTPNQQPEVLYNQIFINNEWHDAVSKKTFPTVNPSTGDVICHVAEGDKADVDRAVKAARAAFQLGSPWRRMDASERGRLLNRLADLIERDRTYLAALETLDNGKPYIISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDYFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNVIPGFGPTAGAAIASHEDVDKVAFTGSTEVGHLIQVAAGKSNLKRVTLEIGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYAEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKVLGYIKSGKEEGLKLLCGGGAAADRGYFIQPTVFGDLQDGMTIAKEEIFGPVMQILKFKSMEEVVGRANNSKYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKLSGSGRELGEYGLQAYTEVKTVTVRVPQKNS
>d1aco_2 3.63.1.1.2 (1-527) Aconitase, first 3 domains [bovine (Bos taurus)]
RAKVAMSHFEPHEYIRYDLLEKNIDIVRKRLNRPLTLSEKIVYGHLDDPANQEIERGKTYLRLRPDRVAMQDATAQMAMLQFISSGLPKVAVPSTIHCDHLIEAQLGGEKDLRRAKDINQEVYNFLATAGAKYGVGFWRPGSGIIHQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRADIANLADEFKDHLVPDSGCHYDQLIEINLSELKPHINGPFTPDLAHPVAEVGSVAEKEGWPLDIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGLKCKSQFTITPGSEQIRATIERDGYAQVLRDVGGIVLANACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRNDANPETHAFVTSPEIVTALAIAGTLKFNPETDFLTGKDGKKFKLEAPDADELPRAEFDPGQDTYQHPPKDSSGQR
>d3pmga1 3.64.1.1.1 (1-190) Phosphoglucomutase, first 3 domains [rabbit (Oryctolagus cuniculus)]
VKIVTVKTKAYPDQKPGTSGLRKRVKVFQSSTNYAENFIQSIISTVEPAQRQEATLVVGGDGRFYMKEAIQLIVRIAAANGIGRLVIGQNGILSTPAVSCIIRKIKAIGGIILTASHNPGGPNGDFGIKFNISNGGPAPEAITDKIFQISKTIEEYAICPDLKVDLGVLGKQQFDLENKFKPFTVEIVDS
>d3pmga3 3.64.1.1.1 (304-420) Phosphoglucomutase, first 3 domains [rabbit (Oryctolagus cuniculus)]
NPSDSVAVIAANIFSIPYFQQTGVRGFARSMPTSGALDRVANATKIALYETPTGWKFFGNLMDASKLSLCGEESFGTGSDHIREKDGLWAVLAWLSILATRKQSVEDILKDHWHKFG
>d3pmga2 3.64.1.1.1 (191-303) Phosphoglucomutase, first 3 domains [rabbit (Oryctolagus cuniculus)]
VEAYATMLRNIFDFNALKELLSGPNRLKIRIDAMHGVVGPYVKKILCEELGAPANSAVNCVPLEDFGGHHPDPNLTYAADLVETMKSGEHDFGAAFDGDGDRNMILGKHGFFV
>d1fuia2 3.65.1.1.1 (1-355) L-fucose isomerase, N-terminal and second domains [Escherichia coli]
MKKISLPKIGIRPVIDGRRMGVRESLEEQTMNMAKATAALLTEKLRHACGAAVECVISDTCIAGMAEAAACEEKFSSQNVGLTITVTPCWCYGSETIDMDPTRPKAIWGFNGTERPGAVYLAAALAAHSQKGIPAFSIYGHDVQDADDTSIPADVEEKLLRFARAGLAVASMKGKSYLSLGGVSMGIAGSIVDHNFFESWLGMKVQAVDMTELRRRIDQKIYDEAELEMALAWADKNFRYGEDENNKQYQRNAEQSRAVLRESLLMAMCIRDMMQGNSKLADIGRVEESLGYNAIAAGFQGQRHWTDQYPNGDTAEAILNSSFDWNGVREPFVVATENDSLNGVAMLMGHQLTGT
>d3pgk__ 3.66.1.1.1 Phosphoglycerate kinase [baker's yeast (Saccharomyces cerevisiae)]
SLSSKLSVQDLDLKDKRVFIRVDFNVPLDGKKITSNQRIVAALPTIKYVLEHHPRYVVLASHLGRPNGERNEKYSLAPVAKELQSLLGKDVTFLNDCVGPEVEAAVKASAPGSVILLENLRYHIEEEGSRKVDGQKVKASKEDVQKFRHELSSLADVYINDAFGTAHRAHSSMVGFDLPQRAAGFLLEKELKYFGKALENPTRPFLAILGGAKVADKIQLIDNLLDKVDSIIIGGGMAFTFKKVLENTEIGDSIFDKAVGPEIAKLMEKAKAKGVEVVLPVDFIIADAFSASANTKTVTDKEGIPAGWQGLDNGPESRKLFAATVAKATVILWNGPPGVFEFEKFAAGTKALLDEVVKSSAAGNTVIIGGGDTATVAKKYGVTDKISHVSTGGGASLELLEGKELPGVAFLSEKK
>d1php__ 3.66.1.1.3 Phosphoglycerate kinase [Bacillus stearothermophilus]
MNKKTIRDVDVRGKRVFCRVDFNVPMEQGAITDDTRIRAALPTIRYLIEHGAKVILASHLGRPKGKVVEELRLDAVAKRLGELLERPVAKTNEAVGDEVKAAVDRLNEGDVLLLENVRFYPGEEKNDPELAKAFAELADLYVNDAFGAAHRAHASTEGIAHYLPAVAGFLMEKELEVLGKALSNPDRPFTAIIGGAKVKDKIGVIDNLLEKVDNLIIGGGLAYTFVKALGHDVGKSLLEEDKIELAKSFMEKAKEKGVRFYMPVDVVVADRFANDANTKVVPIDAIPADWSALDIGPKTRELYRDVIRESKLVVWNGPMGVFEMDAFAHGTKAIAEALAEALDTYSVIGGGDSAAAVEKFGLADKMDHISTGGGASLEFMEGKQLPGVVALEDK
>d1mioa_ 3.67.1.1.1 Nitrogenase iron-molybdenum protein [Clostridium pasteurianum]
SENLKDEILEKYIPKTKKTRSGHIVIKTEETPNPEIVANTRTVPGIITARGCAYAGCKGVVMGPIKDMVHITHGPIGCSFYTWGGRRFKSKPENGTGLNFNEYVFSTDMQESDIVFGGVNKLKDAIHEAYEMFHPAAIGVYATCPVGLIGDDILAVAATASKEIGIPVHAFSCEGYKGVSQSAGHHIANNTVMTDIIGKGNKEQKKYSINVLGEYNIGGDAWEMDRVLEKIGYHVNATLTGDATYEKVQNADKADLNLVQCHRSINYIAEMMETKYGIPWIKCNFIGVDGIVETLRDMAKCFDDPELTKRTEEVIAEEIAAIQDDLDYFKEKLQGKTACLYVGGSRSHTYMNMLKSFGVDSLVAGFEFAHRDDYEGREVIPTIKIDADSKNIPEITVTPDEQKYRVVIPEDKVEELKKAGVPLSAYGGMMKEMHDGTILIDDMNHHDMEVVLEKLKPDMFFAGIKEKFVIQKGGVLSKQLHSYDYNGPYAGFRGVVNFGHELVNGIYTPAWKMITPPWKKASSES
>d1miob_ 3.67.1.1.1 Nitrogenase iron-molybdenum protein [Clostridium pasteurianum]
LDATPKEIVERKALRINPAKTCQPVGAMYAALGIHNCLPHSHGSQGCCSYHRTVLSRHFKEPAMASTSSFTEGASVFGGGSNIKTAVKNIFSLYNPDIIAVHTTCLSETLGDDLPTYISQMEDAGSIPEGKLVIHTNTPSYVGSHVTGFANMVQGIVNYLSENTGAKNGKINVIPGFVGPADMREIKRLFEAMDIPYIMFPDTSGVLDGPTTGEYKMYPEGGTKIEDLKDTGNSDLTLSLGSYASDLGAKTLEKKCKVPFKTLRTPIGVSATDEFIMALSEATGKEVPASIEEERGQLIDLMIDAQQYLQGKKVALLGDPDEIIALSKFIIELGAIPKYVVTGTPGMKFQKEIDAMLAEAGIEGSKVKVEGDFFDVHQWIKNEGVDLLISNTYGKFIAREENIPFVRFGFPIMDRYGHYYNPKVGYKGAIRLVEEITNVILDKIERECTEEDFEVVR
>d2mina_ 3.67.1.1.2 Nitrogenase iron-molybdenum protein [Azotobacter vinelandii]
SREEVESLIQEVLEVYPEKARKDRNKHLAVNCIISNKKSQPGLMTIRGCAYAGSKGVVWGPIKDMIHISHGPVGCGQYSRAGRRNYYIGTTGVNAFVTMNFTSDFQEKDIVFGGDKKLAKLIDEVETLFPLNKGISVQSECPIGLIGDDIESVSKVKGAELSKTIVPVRCEGFRGVSQSLGHHIANDAVRDWVLGKRDEDTTFASTPYDVAIIGDYNIGGDAWSSRILLEEMGLRCVAQWSGDGSISEIELTPKVKLNLVHCYRSMNYISRHMEEKYGIPWMEYNFFGPTKTIESLRAIAAKFDESIQKKCEEVIAKYKPEWEAVVAKYRPRLEGKRVMLYIGGLRPRHVIGAYEDLGMEVVGTGYEFAHNDDYDRTMKEMGDSTLLYDDVTGYEFEEFVKRIKPDLIGSGIKEKFIFQKMGIPFREMHSWDYSGPYHGFDGFAIFARDMDMTLNNPCWKKLQAPWE
>d2minb_ 3.67.1.1.2 Nitrogenase iron-molybdenum protein [Azotobacter vinelandii]
SQQVDKIKASYPLFLDQDYKDMLAKKRDGFEEKYPQDKIDEVFQWTTTKEYQELNFQREALTVNPAKACQPLGAVLCALGFEKTMPYVHGSQGCVAYFRSYFNRHFREPVSCVSDSMTEDAAVFGGQQNMKDGLQNCKATYKPDMIAVSTTCMAEVIGDDLNAFINNSKKEGFIPDEFPVPFAHTPSFVGSHVTGWDNMFEGIARYFTLKSMDDKVVGSNKKINIVPGFETYLGNFRVIKRMLSEMGVGYSLLSDPEEVLDTPADGQFRMYAGGTTQEEMKDAPNALNTVLLQPWHLEKTKKFVEGTWKHEVPKLNIPMGLDWTDEFLMKVSEISGQPIPASLTKERGRLVDMMTDSHTWLHGKRFALWGDPDFVMGLVKFLLELGCEPVHILCHNGNKRWKKAVDAILAASPYGKNATVYIGKDLWHLRSLVFTDKPDFMIGNSYGKFIQRDTLHKGKEFEVPLIRIGFPIFDRHHLHRSTTLGYEGAMQILTTLVNSILERLDEETRGMQATDYNHDLVR
>d2bgu__ 3.68.1.1.1 beta-Glucosyltransferase (DNA-modifying) [Bacteriophage T4]
MKIAIINMGNNVINFKTVPSSETIYLFKVISEMGLNVDIISLKNGVYTKSFDEVDVNDYDRLIVVNSNLAILSAQKFMAKYKSKIYYLFTDIRLPFSQSEEELLIKSPIKVISQGINLDIAKAAHKKVDNVIEFEYFPIEQYKIHMNDFQLSKPTKKTLDVIYGGSFRSGQRESKMVEFLFDTGLNIEFFGNAREKQFKNPKYPWTKAPVFTGKIPMNMVSEKNSQAIAALIIGDKNYNDNFITLRVWETMASDAVMLIDEEFDTKHRIINDARFYVNNRAELIDRVNELKHSDVLRKEMLSIQHDILNKTRAKKAEWQDAFKKAIDL
>d1gpb__ 3.68.1.2.1 Glycogen phosphorylase [rabbit (Oryctolagus cuniculus)]
AGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDEATYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNDFNLKDFNVGGYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSSKFGCRDPVRTNFDAFPDKVAIQLNDTHPSLAIPELMRVLVDLERLDWDKAWEVTVKTCAYTNHTVIPEALERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDVDRLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEIIAERIGEEYISDLDQLRKLLSYVDDEAFIRDVAKVKQENKLKFAAYLEREYKVHINPNSLFDVQVKRIHEYKRQLLNCLHVITLYNRIKKEPNKFVVPRTVMIGGKAAPGYHMAKMIIKLITAIGDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVEDVDRLDQRGYNAQEYYDRIPELRQIIEQLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYEEYVKCQERVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSRQRLPAPDEKI
>d1ygpa_ 3.68.1.2.2 Glycogen phosphorylase [Baker's yeast (Saccharomyces cerevisiae)]
TRRLTGFLPQEIKSIDTMIPLLSRALWNKHQVKKFNKAEDFQDRFIDHVETTLARSLYNCDDMVAYEAASMSIRDNLVIDWNKTQQKFTTRDPKRVYYLSLEFLMGRALDNALINMKIPREMIKGALDELGFKLEDVLDQEPDAGLGNGGLGRLAACFVDSMATEGIPAWGYGLRYEYGIFAQKIIDGYQVETPDYWLNSGNPWEIERNEVQIPVTFYGYVDRPTTLSASQWIGGERVLAVAYDFPVPGFKTSNVNNLRLWQARPTTEFDLNKFNNGDYKNSVAQQQRAESITAVLYPNDNFAQGKELRLKQQYFWCAASLHDILRRFKKSKRPWTEFPDQVAIQLNDTHPTLAIVELQRVLVDLEKLDWHEAWDIVTKTFAYTNHTVMQEALEKWPRRLFGHLLPRHLEIIYDINWFFLEDVAKKFPKDVDLLSRISIIEENSPERQIRMAFLAIVGSHKVNGVVELHSELIKTTIFKDFIKFYGPSKFVNVTNGITPRRWLKQANPSLAKLISETLNDPTEEYLLDMAKLTQLEKYVEDKEFLKKWNQVKLNNKIRLVDLIKKENDGVDIINREYLDDTLFDMQVKRIHEYKRQQLNVFGIIYRYLAMKNMLKNGASIEEVARKYPRKVSIFGGKSAPGYYMAKLIIKLINCVADIVNNDESIEHLLKVVFVADYNVSKAEIIIPASDLSEHISTAGTEASGTSNMKFVMNGGLIIGTVDGANVEITREIGEDNVFLFGNLSENVEELRYNHQYHPQDLPSSLDSVLSYIEQFSPENPNEFKPLVDSIKYHGDYYLVSDDFESYLATHELVDQEFHNQRSEWLKKSVLSLANVGFFSSDRCIEEYSDTIWNVEPVT
>d1ahpa_ 3.68.1.2.3 Maltodextrin phosphorylase (MALP) [Escherichia coli]
SQPIFNDKQFQEALSRQWQRYGLNSAAEMTPRQWWLAVSEALAEMLRAQPFAKPVANQRHVNYISMEFLIGRLTGNNLLNLGWYQDVQDSLKAYDINLTDLLEEEIDPALGAGGLGRLAACFLDSMATVGQSATGYGLNYQYGLFRQSFVDGKQVEAPDDWHRSNYPWFRHNEALDVQVGIGGAVTKDGRWEPEFTITGQAWDLPVVGYRNGVAQPLRLWQATHAHPFDLTKFNDGDFLRAEQQGINAEKLTKVLYPNDNHTAGKKLRLMQQYFQCACSVADILRRHHLAGRELHELADYEVIQLNDTHPTIAIPELLRVLIDEHQMSWDDAWAITSKTFAYTNHTLMPEALERWDVKLVKGLLPRHMQIINEINTRFKTLVEKTWPGDEKVWAKLAVVHDKQVHMANLCVVGGFAVNGVAALHSDLVVKDLFPEYHQLWPNKFHNVTNGITPRRWIKQCNPALAALLDKSLQKEWANDLDQLINLVKLADDAKFRDLYRVIKQANKVRLAEFVKVRTGIDINPQAIFDIQIKRLHEYKRQHLNLLRILALYKEIRENPQADRVPRVFLFGAKAAPGYYLAKNIIFAINKVADVINNDPLVGDKLKVVFLPDYCVSAAEKLIPAADISEQISTAGKEASGTGNMKLALNGALTVGTLDGANVEIAEKVGEENIFIFGHTVKQVKAILAKGYDPVKWRKKDKVLDAVLKELESGKYSDGDKHAFDQMLHSIGKQGGDPYLVMADFAAYVEAQKQVDVLYRDQEAWTRAAILNTARCGMFSSDRSIRDYQARIWQAAR
>d3ecaa_ 3.69.1.1.1 Asparaginase type II [Escherichia coli]
LPNITILATGGTIAGGGDSATKSNYTVGKVGVENLVNAVPQLKDIANVKGEQVVNIGSQDMNDNVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLDLTVKCDKPVVMVGAMRPSTSMSADGPFNLYNAVVTAADKASANRGVLVVMNDTVLDGRDVTKTNTTDVATFKSVNYGPLGYIHNGKIDYQRTPARKHTSDTPFDVSKLNELPKVGIVYNYANASDLPAKALVDAGYDGIVSAGVGNGNLYKSVFDTLATAAKTGTAVVRSSRVPTGATTQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQTKDPQQIQQIFNQY
>d1wsaa_ 3.69.1.1.2 Asparaginase type II [Wolinella succinogenes]
KPQVTILATGGTIAGYSAGAVTVDKLLAAVPAINDLATIKGEQISSIGSQEMTGKVWLKLAKRVNELLAQKETEAVIITHGTDTMEETAFFLNLTVKSQKPVVLVGAMRPGSSMSADGPMNLYNAVNVAINKASTNKGVVIVMNDEIHAAREATKLNTTAVNAFASPNTGKIGTVYYGKVEYFTQSVRPHTLASEFDISKIEELPRVDILYAHPDDTDVLVNAALQAGAKGIIHAGMGNGNPFPLTQNALEKAAKSGVVVARSSRVGSGSTTQEAEVDDKKLGFVATESLNPQKARVLLMLALTKTSDREAIQKIFSTY
>d1agx__ 3.69.1.1.3 Glutaminase-asparaginase [Acinetobacter glutaminasificans]
KNNVVIVATGGTIAGAGASSTNSATYSAAKVPVDALIKAVPQVNDLANITGIQALQVASESITDKELLSLARQVNDLVKKPSVNGVVITHGTDTMEETAFFLNLVVHTDKPIVLVGSMRPSTALSADGPLNLYSAVALASSNEAKNKGVMVLMNDSIFAARDVTKGINIHTHAFVSQWGALGTLVEGKPYWFRSSVKKHTNNSEFNIEKIQGDALPGVQIVYGSDNMMPDAYQAFAKAGVKAIIHAGTGNGSMANYLVPEVRKLHDEQGLQIVRSSRVAQGFVLRNAEQPDDKYGWIAAHDLNPQKARLLMALALTKTNDAKEIQNMFWNY
>d3pga1_ 3.69.1.1.4 Glutaminase-asparaginase [Pseudomonas 7A]
KLANVVILATGGTIAGAGASAANSATYQAAKVGVDKLIAGVPELADLANVRGEQVMQIASESITNDDLLKLGKRVAELADSNDVDGIVITHGTDTLEETAYFLDLTLNTDKPIVVVGSMRPGTAMSADGMLNLYNAVAVASNKDSRGKGVLVTMNDEIQSGRDVSKSINIKTEAFKSAWGPLGMVVEGKSYWFRLPAKRHTVNSEFDIKQISSLPQVDIAYSYGNVTDTAYKALAQNGAKALIHAGTGNGSVSSRLTPALQTLRKTGTQIIRSSHVNQGGFVLRNAEQPDDKNDWVVAHDLNPEKARILVELAMVKTQDSKELQRIFWEY
>d1dfji_ 3.7.1.1.1 Ribonuclease inhibitor [pig (Sus scrofa)]
MNLDIHCEQLSDARWTELLPLLQQYEVVRLDDCGLTEEHCKDIGSALRANPSLTELCLRTNELGDAGVHLVLQGLQSPTCKIQKLSLQNCSLTEAGCGVLPSTLRSLPTLRELHLSDNPLGDAGLRLLCEGLLDPQCHLEKLQLEYCRLTAASCEPLASVLRATRALKELTVSNNDIGEAGARVLGQGLADSACQLETLRLENCGLTPANCKDLCGIVASQASLRELDLGSNGLGDAGIAELCPGLLSPASRLKTLWLWECDITASGCRDLCRVLQAKETLKELSLAGNKLGDEGARLLCESLLQPGCQLESLWVKSCSLTAACCQHVSLMLTQNKHLLELQLSSNKLGDSGIQELCQALSQPGTTLRVLCLGDCEVTNSGCSSLASLLLANRSLRELDLSNNCVGDPGVLQLLGSLEQPGCALEQLVLYDTYWTEEVEDRLQALEGSKPGLRVIS
>d1pfka_ 3.70.1.1.1 Phosphofructokinase [Escherichia coli]
MIKKIGVLTSGGDAPGMNAAIRGVVRSALTEGLEVMGIYDGYLGLYEDRMVQLDRYSVSDMINRGGTFLGSARFPEFRDENIRAVAIENLKKRGIDALVVIGGDGSYMGAMRLTEMGFPCIGLPGTIDNDIKGTDYTIGFFTALSTVVEAIDRLRDTSSSHQRISVVEVMGRYCGDLTLAAAIAGGCEFVVVPEVEFSREDLVNEIKAGIAKGKKHAIVAITEHMCDVDELAHFIEKETGRETRATVLGHIQRGGSPVPYDRILASRMGAYAIDLLLAGYGGRCVGIQNEQLVHHDIIDAIENMKRPFKGDWLDCAKKLY
>d3pfk__ 3.70.1.1.2 Phosphofructokinase [Bacillus stearothermophilus]
MKRIGVLTSGGDSPGMNAAIRSVVRKAIYHGVEVYGVYHGYAGLIAGNIKKLEVGDVGDIIHRGGTILYTARCPEFKTEEGQKKGIEQLKKHGIQGLVVIGGDGSYQGAKKLTEHGFPCVGVPGTIDNDIPGTDFTIGFDTALNTVIDAIDKIRDTATSHERTYVIEVMGRHAGDIALWSGLAGGAETILIPEADYDMNDVIARLKRGHERGKKHSIIIVAEGVGSGVDFGRQIQEATGFETRVTVLGHVQRGGSPTAFDRVLASRLGARAVELLLEGKGGRCVGIQNNQLVDHDIAEALANKHTIDQRMYALSKELSI
>d1ayl__ 3.71.1.1.1 Phosphoenolpyruvate carboxykinase (ATP-oxaloacetate carboxy-liase) [Escherichia coli]
MRVNNGLTPQELEAYGISDVHDIVYNPSYDLLYQEELDPSLTGYERGVLTNLGAVAVDTGIFTGRSPKDKYIVRDDTTRDTFWWADKGKGKNDNKPLSPETWQHLKGLVTRQLSGKRLFVVDAFCGANPDTRLSVRFITEVAWQAHFVKNMFIRPSDEELAGFKPDFIVMNGAKCTNPQWKEQGLNSENFVAFNLTERMQLIGGTWYGGEMKKGMFSMMNYLLPLKGIASMHCSANVGEKGDVAVFFGLSGTGKTTLSTDPKRRLIGDDEHGWDDDGVFNFEGGCYAKTIKLSKEAEPEIYNAIRRDALLENVTVREDGTIDFDDGSKTENTRVSYPIYHIDNIVKPVSKAGHATKVIFLTADAFGVLPPVSRLTADQTQYHFLSGFTAKLAPTPTFSACFGAAFLSLHPTQYAEVLVKRMQAAGAQAYLVNTGWNGTGKRISIKDTRAIIDAILNGSLDNAETFTLPMFNLAIPTELPGVDTKILDPRNTYASPEQWQEKAETLAKLFIDNFDKYTDTPAGAALVAAGPKL
>d2dri__ 3.72.1.1.1 D-ribose-binding protein [Escherichia coli, strain k-12]
KDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAHKFNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSDVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQIGAKGVETADKVLKGEKVQAKYPVDLKLVVKQ
>d8abp__ 3.72.1.1.2 L-arabinose-binding protein [Escherichia coli]
NLKLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKIAVPDGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGYDMKVIAVDDQFVNAKGKPMDTVPLVMLAATKIGERQGQELYKEMQKRGWDVKESAVMAITANELDTARRRTTGSMDALKAAGFPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKHWLIVGMNDSTVLGGVRATEGQGFKAADIIGIGINGVDAVSELSKAQATGFYGSLLPSPDVHGYKSSEMLYNWVAKDVEPPKFTEVTDVVLITRDNFKEELEKKGLGGK
>d2gbp__ 3.72.1.1.3 Galactose/glucose-binding protein [Escherichia coli b]
ADTRIGVTIYKYDDNFMSVVRKAIEQDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKEPSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWAANQGWDLNKDGQIQFVLLKGEPGHPDAEARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNANKIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLADGKGAADGTNWKIDNKVVRVPYVGVDKDNLAEFSKK
>d1gca__ 3.72.1.1.4 Galactose/glucose-binding protein [Salmonella typhimurium, strain lt2]
ADTRIGVTIYKYDDNFMSVVRKAIEKDGKSAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKEPSRKALDSYDKAYYVGTDSKESGVIQGDLIAKHWQANQGWDLNKDGKIQYVLLKGEPGHPDAEARTTYVVKELNDKGIQTEQLALDTAMWDTAQAKDKMDAWLSGPNANKIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVDALPEALALVKSGAMAGTVLNDANNQAKATFDLAKNLAEGKGAADGTSWKIENKIVRVPYVGVDKDNLSEFTQK
>d1pea__ 3.72.1.1.5 Amide receptor/negative regulator of the amidase operon (AmiC) [Pseudomonas aeruginosa]
PLIGLLFSETGVTADIERSQRYGALLAVEQLNREGGVGGRPIETLSQDPGGDPDRYRLCAEDFIRNRGVRFLVGCYMSHTRKAVMPVVERADALLCYPTPYEGFEYSPNIVYGGPAPNQNSAPLAAYLIRHYGERVVFIGSDYIYPRESNHVMRHLYRQHGGTVLEEIYIPLYPSDDDLQRAVERIYQARADVVFSTVVGTGTAELYRAIARRYGDGRRPPIASLTTSEAEVAKMESDVAEGQVVVAPYFSSIDTPASRAFVQACHGFFPENATITAWAEAAYWQTLLLGRAAQAAGNWRVEDVQRHLYDIDIDAPQGPVRVERQNNHSRLSSRIAEIDARGVFQVRWQSPEPIRPDPYVVVHNLDDW
>d1pnra2 3.72.1.1.6 (57-338) Purine repressor (PurR), C-terminal domain [Escherichia coli]
TKSIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLAMLEEYRHIPMVVMDWGEAKADFTDAVIDNAFEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPESWIVQGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSLGETAFNMLLDRIVNKREEPQSIEVHPRLIERRSVADGPFRDYR
>d2liv__ 3.72.1.1.7 Leucine-,isoleucine-,valine-binding (LIV) protein [Escherichia coli]
EDIKVAVVGAMSGPVAQYGDQEFTGAEQAVADINAKGGIKGNKLQIAKYDDACDPKQAVAVANKVVNDGIKYVIGHLCSSSTQPASDIYEDEGILMITPAATAPELTARGYQLILRTTGLDSDQGPTAAKYILEKVKPQRIAIVHDKQQYGEGLARAVQDGLKKGNANVVFFDGITAGEKDFSTLVARLKKENIDFVYYGGYHPEMGQILRQARAAGLKTQFMGPEGVANVSLSNIAGESAEGLLVTKPKNYDQVPANKPIVDAIKAKKQDPSGAFVWTTYAALQSLQAGLNQSDDPAEIAKYLKANSVDTVMGPLTWDEKGDLKGFEFGVFDWHANGTATDAK
>d1tlfa_ 3.72.1.1.8 Lac-repressor (lacR) core (C-terminal domain) [Escherichia coli]
SLLIGVATSSLALHAPSQIVAAIKSRADQLGASVVVSMVERSGVEACKAAVHNLLAQRVSGLIINYPLDDQDAIAVEAACTNVPALFLDVSDQTPINSIIFSHEDGTRLGVEHLVALGHQQIALLAGPLSSVSARLRLAGWHKYLTRNQIQPIAEREGDWSAMSGFQQTMQMLNEGIVPTAMLVANDQMALGAMRAITESGLRVGADISVVGYDDTEDSSCYIPPLTTIKQDFRLLGQTSVDRLLQLSQGQAVKGNQLLPVSLVKRKTTLAPNTQTASPRALADSLMQLARQVSRL
>d2lbp__ 3.72.1.1.9 Leucine-binding protein [Escherichia coli]
DDIKVAVVGAMSGPIAQWGIMEFNGAEQAIKDINAKGGIKGDKLVGVEYDDACDPKQAVAVANKIVNDGIKYVIGHLCSSSTQPASDIYEDEGILMISPGATAPELTQRGYQHIMRTAGLDSSQGPTAAKYILETVKPQRIAIIHDKQQYGEGLARSVQDGLKAANANVVFFDGITAGEKDFSALIARLKKENIDFVYYGGYYPEMGQMLRQARSVGLKTQFMGPEGVGNASLSNIAGDAAEGMLVTMPKRYDQDPANQGIVDALKADKKDPSGPYVWITYAAVQSLATALERTGSDEPLALVKDLKANGANTVIGPLNWDEKGDLKGFDFGVFQWHADGSSTKAK
>d2olba_ 3.73.1.1.1 Oligo-peptide binding protein (OPPA) [Salmonella typhimurium]
ADVPAGVQLADKQTLVRNNGSEVQSLDPHKIEGVPESNVSRDLFEGLLISDVEGHPSPGVAEKWENKDFKVWTFHLRENAKWSDGTPVTAHDFVYSWQRLADPNTASPYASYLQYGHIANIDDIIAGKKPATDLGVKALDDHTFEVTLSEPVPYFYKLLVHPSVSPVPKSAVEKFGDKWTQPANIVTNGAYKLKNWVVNERIVLERNPQYWDNAKTVINQVTYLPISSEVTDVNRYRSGEIDMTYNNMPIELFQKLKKEIPNEVRVDPYLCTYYYEINNQKAPFNDVRVRTALKLALDRDIIVNKVKNQGDLPAYSYTPPYTDGAKLVEPEWFKWSQQKRNEEAKKLLAEAGFTADKPLTFDLLYNTSDLHKKLAIAVASIWKKNLGVNVNLENQEWKTFLDTRHQGTFDVARAGWCADYNEPTSFLNTMLSDSSNNTAHYKSPAFDKLIADTLKVADDTQRSELYAKAEQQLDKDSAIVPVYYYVNARLVKPWVGGYTGKDPLDNIYVKNLYIIKH
>d1pot__ 3.73.1.1.11 Spermidine/putrescine-binding protein POTD [Escherichia coli]
NNTLYFYNWTEYVPPGLLEQFTKETGIKVIYSTYESNETMYAKLKTYKDGAYDLVVPSTYYVDKMRKEGMIQKIDKSKLTNFSNLDPDMLNKPFDPNNDYSIPYIWGATAIGVNGDAVDPKSVTSWADLWKPEYKGSLLLTDDAREVFQMALRKLGYSGNTTDPKEIEAAYNELKKLMPNVAAFNSDNPANPYMEGEVNLGMIWNGSAFVARQAGTPIDVVWPKEGGIFWMDSLAIPANAKNKEGALKLINFLLRPDVAKQVAETIGYPTPNLAARKLLSPEVANDKTLYPDAETIKNGEWQNDVGAASSIYEEYYQKLKAG
>d1ggga_ 3.73.1.1.12 Glutamine-binding protein [Escherichia coli]
LVVATDTAFVPFEFKQGDLYVGFDVDLWAAIAKELKLDYELKPMDFSGIIPALQTKNVDLALAGITITDERKKAIDFSDGYYKSGLLVMVKANNNDVKSVKDLDGKVVAVKSGTGSVDYAKANIKTKDLRQFPNIDNAYMELGTNRADAVLHDTPNILYFIKTAGNGQFKAVGDSLEAQQYGIAFPKGSDELRDKVNGALKTLRENGTYNEIYKKWFGTE
>d1pda_1 3.73.1.1.2 (1-208) Porphobilinogen deaminase (hydroxymethylbilane synthase), N-terminal domain [Escherichia coli]
DNVLRIATRQSPLALWQAHYVKDKLMASHPGLVVELVPMVTRGDVIGKGLFVKELEVALLENRADIAVHSMKDVPVEFPQGLGLVTICEREDPRDAFVSNNYDSLDALPAGSIVGTSSLRRQCQLAERRPDLIIRSLRGNVGTRLSKLDNGEYDAIILAVAGLKRLGLESRIRAALPPEISLPAVGQGAVGIECRLDDSRTRELLAAL
>d1lst__ 3.73.1.1.3 Lysine-,arginine-,ornithine-binding (LAO) protein [Salmonella typhimurium]
ALPQTVRIGTDTTYAPFSSKDAKGEFIGFDIDLGNEMCKRMQVKCTWVASDFDALIPSLKAKKIDAIISSLSITDKRQQEIAFSDKLYAADSRLIAAKGSPIQPTLESLKGKHVGVLQGSTQEAYANDNWRTKGVDVVAYANQDLIYSDLTAGRLDAALQDEVAASEGFLKQPAGKEYAFAGPSVKDKKYFGDGTGVGLRKDDTELKAAFDKALTELRQDGTYDKMAKKYFDFNVYGDK
>d1sbp__ 3.73.1.1.4 Sulphate-binding protein [Salmonella typhimurium]
KDIQLLNVSYDPTRELYEQYNKAFSAHWKQETGDNVVIDQSHGGSGKQATSVINGIEADTVTLALAYDVNAIAERGRIDKNWIKRLPDDSAPYTSTIVFLVRKGNPKQIHDWNDLIKPGVSVITPNPKSSGGARWNYLAAWGYALHHNNNDQAKAEDFVKALFKNVEVLDSGARGSTNTFVERGIGDVLIAWENEALLATNELGKDKFEIVTPSESILAEPTVSVVDKVVEKKDTKAVAEAYLKYLYSPEGQEIAAKNFYRPRDADVAKKYDDAFPKLKLFTIDEVFGGWAKAQKDHFADGGTFDQISK
>d1pbp__ 3.73.1.1.5 Phosphate-binding protein [Escherichia coli]
EASLTGAGATFPAPVYAKWADTYQKETGNKVNYQGIGSSGGVKQIIANTVDFGASDAPLSDEKLAQEGLFQFPTVIGGVVLAVNIPGLKSGELVLDGKTLGDIYLGKIKKWDDEAIAKLNPGLKLPSQNIAVVRRADGSGDSFVFTSYLAKVNEEWKNNVGTGSTVKWPIGLGGKGNDGIAAFVQRLPGAIGYVEYAYAKQNNLAYTKLISADGKPVSPTEENFANAAKGADWSKTFAQDLTNQKGEDAWPITSTTFILIHKDQKKPEQGTEVLKFFDWAYKTGAKQANDLDYASLPDSVVEQVRAAWKTNIKDSSGKPLY
>d1mpb__ 3.73.1.1.7 D-maltodextrin-binding protein [escherichia coli]
KIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPRAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTRITK
>d1dppa_ 3.73.1.1.8 Dipeptide-binding protein [Escherichia coli]
KTLVYCSEGSPEGFNPQLFTSGTTYDASSVPLYNRLVEFKIGTTEVIPGLAEKWEVSEDGKTYTFHLRKGVKWHDNKEFKPTRELNADDVVFSFDRQKNAQNPYHKVSGGSYEYFEGMGLPELISEVKKVDDNTVQFVLTRPEAPFLADLAMDFASILSKEYADAMMKAGTPEKLDLNPIGTGPFQLQQYQKDSRIRYKAFDGYWGTKPQIDTLVFSITPDASVRYAKLQKNECQVMPYPNPADIARMKQDKSINLMEMPGLNVGYLSYNVQKKPLDDVKVRQALTYAVNKDAIIKAVYQGAGVSAKNLIPPTMWGYNDDVQDYTYDPEKAKALLKEAGLEKGFSIDLWAMPVQRPYNPNARRMAEMIQADWAKVGVQAKIVTYEWGEYLKRAKDGEHQTVMMGWTGDNGDPDNFFATLFSCAASEQGSNYSKWCYKPFEDLIQPARATDDHNKRVELYKQAQVVMHDQAPALIIAHSTVFEPVRKEVKGYVVDPLGKHHFENVSIE
>d1hsla_ 3.73.1.1.9 Histidine-binding protein [Escherichia coli, strain k-12]
AIPQKIRIGTDPTYAPFESKNAQGELVGFDIDLAKELCKRINTQCTFVENPLDALIPSLKAKKIDAIMSSLSITEKRQQEIAFTDKLYAADSRLVVAKNSDIQPTVASLKGKRVGVLQGTTQETFGNEHWAPKGIEIVSYQGQDNIYSDLTAGRIDAAFQDEVAASEGFLKQPVGKDYKFGGPAVKDEKLFGVGTGMGLRKEDNELREALNKAFAEMRADGTYEKLAKKYFDFDVYGG
>d1lct__ 3.73.1.2.1 Lactoferrin [human (Homo sapiens)]
RSVQWCAVSNPEATKCFQWQRNMRKVRGPPVSCIKRDSPIQCIQAIAENRADAVTLDGGFIYEAGLAPYKLRPVAAEVYGTERQPRTHYYAVAVVKKGGSFQLNELQGLKSCHTGLRRTAGWNVPIGTLRPFLNWTGPPEPIEAAVARFFSASCVPGADKGQFPNLCRLCAGTGENKCAFSSQEPYFSYSGAFKCLRDGAGDVAFIRESTVFEDLSDEAERDEYELLCPDNTRKPVDKFKDCHLARVPSHAVVARSVNGKEDAIWNLLRQAQEKFGKDKSPKFQLFGSPSGQKDLLFKDSAIGFSRVPPRIDSGLYLGSGYFTA
>d1ovb__ 3.73.1.2.2 Ovotransferrin [Duck (Anas platyrhynchos)]
SYYAVAVVKKGTDFMIKDLRGKTSCHTGLGRSAGWNIPIGTLIHREDIEWEGIESGSVEQAVAKFFSASCVPGATIEQKLCRQCKGDAKTKCLRNAPYSGYSGAFQCLKDGKGDVAFVKHTTVQENAPEEKDEYELLCLDGSRQPVDSYKTCNWARVAA
>d1ovt_1 3.73.1.2.3 (1-330) Ovotransferrin [Chicken (Gallus gallus)]
SVIRWCTISSPEEKKCNNLRDLTQQERISLTCVQKATYLDCIKAIANNEADAISLDGGQAFEAGLAPYKLKPIAAEVYEHTEGSTTSYYAVAVVKKGTEFTVNDLQGKTSCHTGLGRSAGWNIPIGTLLHRGAIEWEGIESGSVEQAVAKFFSASCVPGATIEQKLCRQCKGDPKTKCARNAPYSGYSGAFHCLKDGKGDVAFVKHTTVNENAPDQKDEYELLCLDGSRQPVDNYKTCNWARVAAHAVVARDDNKVEDIWSFLSKAQSDFGVDTKSDFHLFGPPGKKDPVLKDLLFKDSAIMLKRVPSLMDSQLYLGFEYYSAIQSMRKD
>d1ovt_2 3.73.1.2.3 (331-682) Ovotransferrin [Chicken (Gallus gallus)]
QLTPSPRENRIQWCAVGKDEKSKCDRWSVVSNGDVECTVVDETKDCIIKIMKGEADAVALDGGLVYTAGVCGLVPVMAERYDDESQCSKTDERPASYFAVAVARKDSNVNWNNLKGKKSCHTAVGRTAGWVIPMGLIHNRTGTCNFDEYFSEGCAPGSPPNSRLCQLCQGSGGIPPEKCVASSHEKYFGYTGALRCLVEKGDVAFIQHSTVEENTGGKNKADWAKNLQMDDFELLCTDGRRANVMDYRECNLAEVPTHAVVVRPEKANKIRDLLERQEKRFGVNGSEKSKFMMFESQNKDLLFKDLTKCLFKVREGTTYKEFLGDKFYTVISSLKTCNPSDILQMCSFLEGK
>d1tfd__ 3.73.1.2.4 Transferrin [rabbit (Oryctolagus cuniculus)]
VRWCAVNDHEASKCANFRDSMKKVLPEDGPRIICVKKASYLDCIKAIAAHEADAVTLDAGLVHEAGLTPNNLKPVVAEFYGSKENPKTFYYAVALVKKGSNFQLNELQGKKSCHTGLGRSAGWNIPIGLLYCDLPEPRKPLEKAVASFFSGSCVPCADQLCQLCPGCGCSSSQPYFGYSGAFKCLKDGLGDVAFVKQETIFENLPSKDERDQYELLCLDNTRKPVDEYEQCHLARVPSHAVVARSVDGKEDLIWELLNQAQEHFGKDKSGDFQLFSSPHGKNLLFKDSAYGFFK
>d1pxta2 3.74.1.1.1 (220-343) Thiolase [yeast (Saccharomyces serevisiae)]
LNLPVLGRYIDFQTVGVPPEIMGVGPAYAIPKVLEATGLQVQDIDIFEINEAFAAQALYCIHKLGIDLNKVNPRGGAIALGHPLGCTGARQVATILRELKKDQIGVVSMCIGTGMGAAAIFIKE
>d1pxta1 3.74.1.1.1 (1-219) Thiolase [yeast (Saccharomyces serevisiae)]
LLEKRPEDVVIVAANRSAIGKGFKGAFKDVNTDYLLYNFLNEFIGRFPEPLRADLNLIEEVACGNVLNVGAGATEHRAACLASGIPYSTPFVALNRQCSSGLTAVNDIANKIKVGQIDIGLALGVESMTNNYKNQKNREAKKCLIPMGITNENRKDQDEFAANSYQKAYKAKNEGLFEDEILPIKLPDGSICQSDEGPRPQVSDGVAGVLLARRSVANQ
>d1ctt_2 3.75.1.1.1 (151-294) Cytidine deaminase [Escherichia coli]
GREAHALRDYLPDAFGPKDLEIKTLLMDEQDHGYALTGDALSQAAIAAANRSHMPYSKSPSGVALECKDGRIFSGSYAENAAFNPTLPPLQGALILLNLKGYDYPDIQRAVLAEKADAPLIQWDATSATLKALGCHSIDRVLLA
>d1ctt_1 3.75.1.1.1 (1-150) Cytidine deaminase [Escherichia coli]
MHPRFQTAFAQLADNLQSALEPILADKYFPALLTGEQVSSLKSATGLDEDALAFALLPLAAACARTPLSNFNVGAIARGVSGTWYFGANMEFIGATMQQTVHAEQSAISHAWLSGEKALAAITVNYTPCGHCRQFMNELNSGLDLRIHLP
>d1nzya_ 3.8.1.1.1 4-Chlorobenzoyl-CoA dehalogenase [Pseidomonas sp. strain CBS-3]
MYEAIGHRVEDGVAEITIKLPRHRNALSVKAMQEVTDALNRAEEDDSVGAVMITGAEDAFCAGFYLREIPLDKGVAGVRDHFRIAALWWHQMIHKIIRVKRPVLAAINGVAAGGGLGISLASDMAICADSAKFVCAWHTIGIGNDTATSYSLARIVGMRRAMELMLTNRTLYPEEAKDWGLVSRVYPKDEFREVAWKVARELAAAPTHLQVMAKERFHAGWMQPVEECTEFEIQNVIASVTHPHFMPCLTRFLDGHRADRPQVELPAGV
>d1duba_ 3.8.1.1.2 Enoyl-CoA hydratase [Rat (Rattus norvegicus)]
ANFQYIITEKKGKNSSVGLIQLNRPKALNALCNGLIEELNQALETFEEDPAVGAIVLTGGEKAFAAGADIKEMQNRTFQDCYSGKFLSHWDHITRIKKPVIAAVNGYALGGGCELAMMCDIIYAGEKAQFGQPEILLGTIPGAGGTQRLTRAVGKSLAMEMVLTGDRISAQDAKQAGLVSKIFPVETLVEEAIQCAEKIANNSKIIVAMAKESVNAAFEMTLTEGNKLEKKLFYSTFATDDRREGMSAFVEKRKANFKDH
>d1rvva_ 3.9.1.1.1 beta-subunit (capsid) of the lumazine synthase/riboflavin synthase complex [Bacillus subtilis]
MNIIQGNLVGTGLKIGIVVGRFNDFITSKLLSGAEDALLRHGVDTNDIDVAWVPGAFEIPFAAKKMAETKKYDAIITLGTVIRGATTHYDYVCNEAAKGIAQAANTTGVPVIFGIVTTENIEQAIERAGTKAGNKGVDCAVSAIEMANLNRSFE
>d1gmpa_ 4.1.1.1.1 RNase Sa [Streptomyces aureofaciens]
DVSGTVCLSALPPEATDTLNLIASDGPFPYSQDGVVFQNRESVLPTQSYGYYHEYTVITPGARTRGTRRIICGEATQEDYYTGDHYATFSLIDQTC
>d1fus__ 4.1.1.1.2 RNase F1 [Fusarium moniliforme]
XSATTCGSTNYSASQVRAAANAACQYYQNDDTAGSSTYPHTYNNYEGFDFPVDGPYQEFPIKSGGVYTGGSPGADRVVINTNCEYAGAITHTGASGNNFVGCSGTN
>d9rnt__ 4.1.1.1.3 RNase T1 [Aspergillus oryzae]
ACDYTCGSNCYSSSDVSTAQAAGYKLHEDGETVGSNSYPHKYNNYEGFDFSVSSPYYEWPILSSGDVYSGGSPGADRVVFNENNQLAGVITHTGASGNNFVECT
>d1rtu__ 4.1.1.1.4 RNase U2 [Ustilago sphaerogena]
CDIPQSTNCGGNVYSNDDINTAIQGALDDVANGDRPDNYPHQYYEASEDITLCCGSGPWSEFPLVYNGPYYSSRDNYVSPGPDRVIYQTNTGEFCATVTHTGAASYDGFTQCS
>d1brnl_ 4.1.1.1.5 Barnase/Binase [Bacillus amyloliquefaciens]
VINTFDGVADYLQTYHKLPDNYITKSEAQALGWVASKGNLADVAPGKSIGGDIFSNREGKLPGKSGRTWREADINYTSGFRNSDRILYSSDWLIYKTTDHYQTFTKIR
>d2rbia_ 4.1.1.1.6 Barnase/Binase [Bacillus intermedius]
VINTFDGVADYLIRYKRLPDNYITKSQASALGWVASKGNLAEVAPGKSIGGDVFSNREGRLPSASGRTWREADINYVSGFRNADRLVYSSDWLIYKTTDNYATFTRIR
>d1rms__ 4.1.1.1.7 RNase Ms [molsin (Aspergillus saitoi)]
ESCEYTCGSTCYWSSDVSAAKAKGYSLYESGDTIDDYPHEYHDYEGFDFPVSGTYYEYPIMSDYDVYTGGSPGADRVIFNGDDELAGVITHTGASGDDFVACSSS
>d1kpaa_ 4.10.1.1.2 Protein kinase C inhibitor-1, PKCI-1 [human (Homo sapiens)]
GGDTIFGKIIRKEIPAKIIFEDDRCLAFHDISPQAPTHFLVIPKKHISQISVAEDDDESLLGHLMIVGKKCAADLGLNKGYRMVVNEGSDGGQSVYHVHLHVLGGRQMHWPPG
>d1hxpa1 4.10.1.2.1 (1-169) Galactose-1-phosphate uridylyltransferase [Escherichia coli]
TQFNPVDHPHRRYNPLTGQWILVSPHRAKRPWEGAVLPAHDPDCFLCAGNVRVTGDKNPDYTGTYVFTNDFAALMSDTPDAPESHDPLMRCQSARGTSRVICFSPDHSKTLPELSVAALTEIVKTWQEQTAELGKTYPWVQVFENKGAAMGCSNPHPHGQIWANSFLPN
>d1hxpa2 4.10.1.2.1 (170-340) Galactose-1-phosphate uridylyltransferase [Escherichia coli]
EAEREDRLQKEYFAEQKSPMLVDYVQRELADGSRTVVETEHWLAVVPYWAAWPFETLLLPKAHVLRITDLTDAQRSDLALALKKLTSRYDNLFQCSFPYSMGWHGAPFNGEENQHWQLHAHFYPPLLRSATVRKFMVGYEMLAETQRDLTAEQAAERLRAVSDIHFRESGV
>d1pmd_3 4.100.1.1.1 (1-188) Penicillin-binding protein 2x (pbp-2x), N-terminal domain [Streptococcus pneumoniae]
RGTIYDRNGVPIAEDATSYNVYAVIDENYKSATGKILYVEKTQFNKVAEVFHKYLDMEESYVREQLSQPNLKQVSFGAKGNGITYANMMSIKKELEAAEVKGIDFTTSPNRSYPNGQFASSFIGLAQLHENEDGSKSLLGTSGMESSLNSILAGTDGIITYEKDRLGNIVPGTEQVSQRTMDGKDVYT
>d1dar_3 4.11.1.1.1 (403-525) Elongation factor G (EF-G), domain IV [Thermus thermophilus]
GKPQVAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIPAVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYHEVDSSEMAFKIAGSMAIKEAVQKGDP
>d1pkp_1 4.11.1.1.2 (75-145) Ribosomal S5 protein, the C-terminal domain [Bacillus stearothermophilus]
GTTIPHEVIGHFGAGEIILKPASEGTGVIAGGPARAVLELAGISDILSKSIGSNTPINMVRATFDGLKQLK
>d1pgb__ 4.12.1.1.1 Immunoglobulin-binding protein G, separate domains [group G streptococcus (Streptomyces griseus)]
MTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTE
>d1igd__ 4.12.1.1.1 Immunoglobulin-binding protein G, separate domains [group G streptococcus (Streptomyces griseus)]
MTPAVTTYKLVINGKTLKGETTTKAVDAETAEKAFKQYANDNGVDGVWTYDDATKTFTVTE
>d1fccc_ 4.12.1.1.1 Immunoglobulin-binding protein G, separate domains [group G streptococcus (Streptomyces griseus)]
TTYKLVINGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTE
>d2ptl__ 4.12.1.1.2 Immunoglobulin light chain-binding domain of protein L [Peptostreptococcus magnus]
ENKEETPETPETDSEEEVTIKANLIFANGSTQTAEFKGTFEKATSEAYAYADTLKKDNGEYTVDVADKGYTLNIKFAG
>d1ubi__ 4.12.2.1.1 Ubiquitin [human (Homo sapiens)]
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG
>d1guab_ 4.12.3.1.1 c-Raf1, Ras-binding domain [Human (Homo sapiens)]
NTIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLHEHKGKKARLDWNTDAASLIGEELQVDFL
>d1frd__ 4.12.4.1.1 2Fe-2S ferredoxin [Cyanobacterium (Anabaena sp.)]
ASYQVRLINKKQDIDTTIEIDEETTILDGAEENGIELPFSCHSGSCSSCVGKVVEGEVDQSDQIFLDDEQMGKGFALLCVTYPRSNCTIKTHQEPYLA
>d1fxaa_ 4.12.4.1.1 2Fe-2S ferredoxin [Cyanobacterium (Anabaena sp.)]
ATFKVTLINEAEGTKHEIEVPDDEYILDAAEEQGYDLPFSCRAGACSTCAGKLVSGTVDQSDQSFLDDDQIEAGYVLTCVAYPTSDVVIQTHKEEDLY
>d1put__ 4.12.4.1.10 Putidaredoxin [Pseudomonas putida]
SKVVYVSHDGTRRQLDVADGVSLMQAAVSNGIYDIVGDCGGSASCATCHVYVNEAFTDKVPAANEREIGMLECVTAELKPNSRLCCQIIMTPELDGIVVDVPDRQW
>d4fxc__ 4.12.4.1.2 2Fe-2S ferredoxin [Spirulina platensis]
ATYKVTLINEAEGINETIDCDDDTYILDAAEEAGLDLPYSCRAGACSTCAGTITSGTIDQSDQSFLDDDQIEAGYVLTCVAYPTSDCTIKTHQEEGLY
>d1fxia_ 4.12.4.1.3 2Fe-2S ferredoxin [cyanobacterium (Aphanothece sacrum)]
ASYKVTLKTPDGDNVITVPDDEYILDVAEEEGLDLPYSCRAGACSTCAGKLVSGPAPDEDQSFLDDDQIQAGYILTCVAYPTGDCVIETHKEEALY
>d1dox__ 4.12.4.1.4 2Fe-2S ferredoxin [(Synechocystis sp. PCC 6803)]
ASYTVKLITPDGESSIECSDDTYILDAAEEAGLDLPYSCRAGACSTCAGKITAGSVDQSDQSFLDDDQIEAGYVLTCVAYPTSDCTIETHKEEDLY
>d1roe__ 4.12.4.1.5 2Fe-2S ferredoxin [(Synechococcus elongatus)]
ATYKVTLVRPDGSETTIDVPEDEYILDVAEEQGLDLPFSCRAGACSTCAGKLLEGEVDQSDQSFLDDDQIEKGFVLTCVAYPRSDCKILTNQEEELY
>d1frra_ 4.12.4.1.6 2Fe-2S ferredoxin [Equisetum arvense]
AYKTVLKTPSGEFTLDVPEGTTILDAAEEAGYDLPFSCRAGACSSCLGKVVSGSVDESEGSFLDDGQMEEGFVLTCIAIPESDLVIETHKEEELF
>d1doi__ 4.12.4.1.7 2Fe-2S ferredoxin [(Haloarcula marismortui)]
PTVEYLNYEVVDDNGWDMYDDDVFGEASDMDLDDEDYGSLEVNEGEYILEAAEAQGYDWPFSCRAGACANCAAIVLEGDIDMDMQQILSDEEVEDKNVRLTCIGSPDADEVKIVYNAKHLDYLQNRVI
>d1alo_2 4.12.4.1.8 (1-80) Aldehyde oxidoreductase, N-terminal domain [(Desulfovibrio gigas)]
MIQKVITVNGIEQNLFVDAEALLSDVLRQQLGLTGVKVGCEQGQCGACSVILDGKVVRACVTKMKRVADGAQITTIEGVG
>d2pia_3 4.12.4.1.9 (224-321) Phthalate dioxygenase reductase, C-terminal domain [Pseudomonas cepacia db01]
SFGATNTNARENTPFTVRLSRSGTSFEIPANRSILEVLRDANVRVPSSCESGTCGSCKTALCSGEADHRDMVLRDDEKGTQIMVCVSRAKSAELVLDL
>d1esfa2 4.12.5.1.1 (117-229) Staphylococcal enterotoxin A, SEA [Staphylococcus aureus]
EEKKVPINLWLDGKQNTVPLETVKTNKKNVTVQELDLQARRYLQEKYNLYNSDVFDGKVQRGLIVFHTSTEPSVNYDLFGAQGQYSNTLLRIYRDNKTINSENMHIDIYLYTS
>d1ste_2 4.12.5.1.2 (121-238) Staphylococcal enterotoxin C2, SEC2 [Staphylococcus aureus]
NHFDNGNLQNVLIRVYENKRNTISFEVQTDKKSVTAQELDIKARNFLINKKNLYEFNSSPYETGYIKFIENNGNTFWYDMMPAPGDKFDQSKYLMMYNDNKTVDSKSVKIEVHLTTKN
>d1tssa2 4.12.5.1.3 (94-194) Toxic shock syndrome toxin-1 (TSST-1) [Staphylococcus aureus]
LPTPIELPLKVKVHGKDSPLKYWPKFDKKQLAISTLDFEIRHQLTQIHGLYRSSDKTGGYWKITMNDGSTYQSDLSKKFEYNTEKPPINIDEIKTIEAEIN
>d1se4_2 4.12.5.1.4 (122-239) Staphylococcal enterotoxin B, SEB [Staphylococcus aureus]
NGNQLDKYRSITVRVFEDGKNLLSFDVQTNKKKVTAQELDYLTRHYLVKNKKLYEFNNSPYETGYIKFIENENSFWYDMMPAPGDKFDQSKYLMMYNDNKMVDSKDVKIEVYLTTKKK
>d1tif__ 4.12.6.1.1 Translation initiation factor IF3, N-terminal domain [Bacillus stearothermophilus]
KDFIINEQIRAREVRLIDQNGDQLGIKSKQEALEIAARRNLDLVLVAPNAKPPVCRIMDYGKFRFEQQKKEKEARK
>d1lgr_1 4.12.7.1.1 (1-94) Glutamine synthetase, N-terminal domain [Salmonella typhimurium]
SAEHVLTMLNEHEVKFVDLRFTDTKGKEQHVTIPAHQVNAEFFEEGKMFDGSSIGGWDMVLMPDASTAVIDPFFADSTLIIRCDILEPGTLQGY
>d1coy_2 4.13.1.1.1 (316-445) Cholesterol oxidase [Brevibacterium sterolicum]
GNNGNIMVGRANHMWDATGSKQATIPTMGIDNWADPTAPIFAEIAPLPAGLETYVSLYLAITKNPERARFQFNSGTGKVDLTWAQSQNQKGIDMAKKVFDKINQKEGTIYRTDLFYYKTWGDDFTYHPLG
>d1pbe_2 4.13.1.2.1 (174-275) p-Hydroxybenzoate hydroxylase [Pseudomonas fluorescens]
LKVFERVYPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYYVQVPLTEKVEDWSDERFWTELKARLPAEVAEKLVTGPSLEKSIAPLRSFVVEP
>d1kifa2 4.13.1.3.1 (195-287) D-amino acid oxidase [Pig (Sus scrofa)]
LQPGRGQIIKVDAPWLKNFIITHDLERGIYNSPYIIPGLQAVTLGGTFQVGNWNEINNIQDHNTIWEGCCRLEPTLKDAKIVGEYTGFRPVRP
>d1gal_2 4.13.1.4.1 (516-581) Glucose oxidase [Aspergillus niger]
VGTCSMMPKEMGGVVDNAARVYGVQGLRVIDGSIPPTQMSSHVMTVFYAMALKISDAILEDYASMQ
>d1gnd_2 4.13.1.5.1 (292-388) Guanine nucleotide dissosiation inhibitor, GDI [Bovine (Bos taurus)]
RKAGQVIRIICILSHPIKNTNDANSCQIIIPQNQVNRKSDIYVCMISYAHNVAAQGKYIAIASTTVETTDPEKEVEPALELLEPIDQKFVAISDLYE
>d1mola_ 4.14.1.1.1 Monellin, B & A chains together [serendipity berry (Dioscoreophyllum cumminsii diels)]
GEWEIIDIGPFTQNLGKFAVDEENKIGQYGRLTFNKVIRPCMKKTIYENEREIKGYEYQLYVYASDKLFRADISEDYKTRGRKLLRFNGPVPPP
>d1cewi_ 4.14.1.2.1 Cystatin [chicken (Gallus gallus)]
GAPVPVDENDEGLQRALQFAMAEYNRASNDKYSSRVVRVISAKRQLVSGIKYILQVEIGRTTCPKSSGDLQSCEFHDEPEMAKYTTCTFVVYSIPWLNQIKLLESKCQ
>d1cyu__ 4.14.1.2.2 Cystatin A (stefin A) [human (Homo sapiens)]
MIPGGLSEAKPATPEIQEIVDKVKPQLEEKTNETYGKLEAVQYKTQVVAGTNYYIKVRAGDNKYLHLKVFKSLPGQNEDLVLTGYQVDKNKDDELTGF
>d1stfi_ 4.14.1.2.3 Cystatin B (stefin B) [human (Homo sapiens)]
MMSGAPSATQPATAETQHIADQVRSQLEEKYNKKFPVFKAVSFKSQVVAGTNYFIKVHVGDEDFVHLRVFQSLPHENKPLTLSNYQTNKAKHDELTYF
>d1oaca3 4.14.2.1.1 (182-296) Copper amine oxidase, domains 2 and 3 [Escherichia coli]
MVLLDDFASVQNIINNSEEFAAAVKKRGITDAKKVITTPLTVGYFDGKDGLKQDARLLKVISYLDVGDGNYWAHPIENLVAVVDLEQKKIVKIEEGPVVPVPMTARPFDGRDRVA
>d1oaca2 4.14.2.1.1 (87-181) Copper amine oxidase, domains 2 and 3 [Escherichia coli]
KRPHPLNALTADEIKQAVEIVKASADFKPNTRFTEISLLPPDKEAVWAFALENKPVDQPRKADVIMLDGKHIIEAVVDLQNNKLLSWQPIKDAHG
>d1std__ 4.14.3.1.1 Scytalone dehydratase [fungus Magnaporthe grisea]
DEITFSDYLGLMTCVYEWADSYDSKDWDRLRKVIAPTLRIDYRSFLDKLWEAMPAEEFVGMVSSKQVLGDPTLRTQHFIGGTRWEKVSEDEVIGYHQLRVPHQRYKDTTMKEVTMKGHAHSANLHWYKKIDGVWKFAGLKPDIRWGEFDFDRIFEDGRETFG
>d1ouna_ 4.14.3.2.1 Nuclear transport factor-2 (NTF2) [Human (Homo sapiens)]
GDKPIWEQIGSSFIQHYYQLFDNDRTQLGAIYIDASCLTWEGQQFQGKAAIVEKLSSLPFQKIQHSITAQDHQPTPDSCIISMVVGQLKADEDPIMGFHQMFLLKNINDAWVCTNDMFRLALHNF
>d1udii_ 4.14.4.1.1 Uracil-DNA glycosylase inhibitor protein [Herpes simplex virus type-1 (HSV1)]
TNLSDIIEKETGKQLVIQESILMLPEEVEEVIGNKPESDILVHTAYDESTDENVMLLTSDAPEYKPWALVIQDSNGENKIKML
>d1frua2 4.15.1.1.1 (1-178) Fc (IgG) receptor, alpha-1 and alpha-2 domains [rat (Rattus norvegicus)]
AEPRLPLMYHLAAVSDLSTGLPSFWATGWLGAQQYLTYNNLRQEADPCGAWIWENQVSWYWEKETTDLKSKEQLFLEAIRTLENQINGTFTLQGLLGCELAPDNSSLPTAVFALNGEEFMRFNPRTGNWSGEWPETDIVGNLWMKQPEAARKESEFLLTSCPERLLGHLERGRQNLEW
>d1agda2 4.15.1.1.10 (1-181) MHC class I, alpha-1 and alpha-2 domains [human hla-b0801]
GSHSMRYFDTAMSRPGRGEPRFISVGYVDDTQFVRFDSDAASPREEPRAPWIEQEGPEYWDRNTQIFKTNTQTDRESLRNLRGYYNQSEAGSHTLQSMYGCDVGPDGRLLRGHNQYAYDGKDYIALNEDLRSWTAADTAAQITQRKWEAARVAEQDRAYLEGTCVEWLRRYLENGKDTLER
>d2mhaa2 4.15.1.1.11 (1-181) MHC class I, alpha-1 and alpha-2 domains [mouse h-2k (B)]
GPHSLRYFVTAVSRPGLGEPRYMEVGYVDDTEFVRFDSDAENPRYEPRARWMEQEGPEYWERETQKAKGNEQSFRVDLRTLLGYYNQSKGGSHTIQVISGCEVGSDGRLLRGYQQYAYDGCDYIALNEDLKTWTAADMAALITKHKWEQAGEAERLRAYLEGTCVEWLRRYLKNGNATLLR
>d1hoca2 4.15.1.1.12 (1-181) MHC class I, alpha-1 and alpha-2 domains [mouse h-2d (B)]
GPHSMRYFETAVSRPGLEEPRYISVGYVDNKEFVRFDSDAENPRYEPRAPWMEQEGPEYWERETQKAKGQEQWFRVSLRNLLGYYNQSAGGSHTLQQMSGCDLGSDWRLLRGYLQFAYEGRDYIALNEDLKTWTAADMAAQITRRKWEQSGAAEHYKAYLEGECVEWLHRYLKNGNATLLR
>d1mhca2 4.15.1.1.13 (1-181) MHC class I, alpha-1 and alpha-2 domains [mouse h2-m3]
GSHSLRYFHTAVSRPGRGEPQYISVGYVDDVQFQRCDSIEEIPRMEPRAPWMEKERPEYWKELKLKVKNIAQSARANLRTLLRYYNQSEGGSHILQWMVSCEVGPDMRLLGAHYQAAYDGSDYITLNEDLSSWTAVDMVSQITKSRLESAGTAEYFRAYVEGECLELLHRFLRNGKEILQR
>d1cd1a2 4.15.1.1.2 (1-179) CD1, alpha-1 and alpha-2 domains [Mouse (Mus musculus)]
NYTFRCLQMSSFANRSWSRTDSVVWLGDLQTHRWSNDSATISFTKPWSQGKLSNQQWEKLQHMFQVYRVSFTRDIQELVKMMSPKEDYPIEIQLSAGCEMYPGNASESFLHVAFQGKYVVRFWGTSWQTVPGAPSWLDLPIKVLNADQGTSATVQMLLNDTCPLFVRGLLEAGKSDLEK
>d1dlha2 4.15.1.1.3 (1-79) MHC class II, N-terminal domains of alpha and beta chains [human hla-dr1]
EEHVIIQAEFYLNPDQSGEFMFDFDGDEIFHVDMAKKETVWRLEEFGRFASFEAQGALANIAVDKANLEIMTKRSNYTP
>d1dlhb2 4.15.1.1.3 (1-90) MHC class II, N-terminal domains of alpha and beta chains [human hla-dr1]
TRPRFLWQLKFECHFFNGTERVRLLERCIYNQEESVRFDSDVGEYRAVTELGRPDAEYWNSQKDLLEQRRAAVDTYCRHNYGVGESFTVQ
>d1ieaa1 4.15.1.1.4 (1-81) MHC class II, N-terminal domains of alpha and beta chains [mouse I-EK]
IKEEHTIIQAEFYLLPDKRGEFMFDFDGDEIFHVDIEKSETIWRLEEFAKFASFEAQGALANIAVDKANLDVMKERSNNTP
>d1iebb1 4.15.1.1.4 (1-118) MHC class II, N-terminal domains of alpha and beta chains [mouse I-EK]
RDRMVNHFIAEFKRKGGSLVPRGSGGGGSRPWFLEYCKSECHFYNGTQRVRLLVRYFYNLEENLRFDSDVGEFRAVTELGRPDAENWNSQPEFLEQKRAEVDTVCRHNYEIFDNFLVP
>d1ieab1 4.15.1.1.4 (31-118) MHC class II, N-terminal domains of alpha and beta chains [mouse I-EK]
PWFLEYCKSECHFYNGTQRVRLLVRYFYNLEENLRFDSDVGEFRAVTELGRPDAENWNSQPEFLEQKRAEVDTVCRHNYEIFDNFLVP
>d1hsaa2 4.15.1.1.8 (1-181) MHC class I, alpha-1 and alpha-2 domains [human hla-b2705]
GSHSMRYFHTSVSRPGRGEPRFITVGYVDDTLFVRFDSDAASPREEPRAPWIEQEGPEYWDRETQICKAKAQTDREDLRTLLRYYNQSEAGSHTLQNMYGCDVGPDGRLLRGYHQDAYDGKDYIALNEDLSSWTAADTAAQITQRKWEAARVAEQLRAYLEGECVEWLRRYLENGKETLQR
>d1hsba2 4.15.1.1.9 (1-181) MHC class I, alpha-1 and alpha-2 domains [human hla-aw68]
GSHSMRYFYTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEYWDRNTRNVKAQSQTDRVDLGTLRGYYNQSEAGSHTIQMMYGCDVGSDGRFLRGYRQDAYDGKDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQWRAYLEGTCVEWLRRYLENGKETLQR
>d1aak__ 4.16.1.1.1 Ubiquitin conjugating enzyme [Arabidopsis thaliana]
MSTPARKRLMRDFKRLQQDPPAGISGAPQDNNIMLWNAVIFGPDDTPWDGGTFKLSLQFSEDYPNKPPTVRFVSRMFHPNIYADGSICLDILQNQWSPIYDVAAILTSIQSLLCDPNPNSPANSEAARMYSESKREYNRRVRDVVEQSWT
>d2uce__ 4.16.1.1.2 Ubiquitin conjugating enzyme [yeast (Saccharomyces cerevisiae) ubc4]
MSSSKRIAKELSDLERDPPTSCSAGPVGDDLYHWQASIMGPADSPYAGGVFFLSIHFPTDYPFKPPKISFTTKIYHPNINANGNICLDILKDQWSPALTLSKVLLSICSLLTDANPDDPLVPEIAHIYKTDRPKYEATAREWTKKYAV
>d1ucz__ 4.16.1.1.3 Ubiquitin conjugating enzyme [yeast (Saccharomyces cerevisiae) ubc7]
KTAQKRLLKELQQLIKDSPPGIVAGPKSENNIFIWDCLIQGPPDTPYADGVFNAKLEFPKDYPLSPPKLTFTPSILHPNIYPNGEVCISILHSPGDDPNMYELAEERWSPVQSVEKILLSVMSMLSEPNIESGANIDACILWRDNRPEFERQVKLSILKSLGF
>d1u9b__ 4.16.1.1.4 Ubiquitin conjugating enzyme [human/mouse (Homo sapiens/Mus musculus) ubc9]
NMSGIALSRLAQERKAWRKDHPFGFVAVPTKNPDGTMNLMNWECAIPGKKGTPWEGGLFKLRMLFKDDYPSSPPKCKFEPPLFHPNVYPSGTVCLSILEEDKDWRPAITIKQILLGIQELLNEPNIQDPAQAEAYTIYCQNRVEYEKRVRAQAKKFAPS
>d1ema__ 4.17.1.1.1 Green fluorescent protein [Jellyfish (Aequorea victoria)]
SKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTFVQCFSRYPDHKRHDFFKSAPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSALSKDPNEKRDHVLLEFVTAAGI
>d1fkd__ 4.19.1.1.1 FK-506 binding protein (FKBP12), an immunophilin [Human (Homo sapiens)]
GVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFDVELLKLE
>d1yat__ 4.19.1.1.3 FK-506 binding protein (FKBP12), an immunophilin [yeast]
SEVIEGNVKIDRISPGDGATFPKTGDLVTIHYTGTLENGQKFDSSVDRGSPFQCNIGVGQVIKGWDVGIPKLSVGEKARLTIPGPYAYGPRGFPGLIPPNSTLVFDVELLKVN
>d1pbk__ 4.19.1.1.4 FKBP25 [Human (Homo sapiens)]
PKYTKSVLKKGDKTNFPKKGDVVHCWYTGTLQDGTVFDTNIQTSAKKKKNAKPLSFKVGVGKVIRGWDEALLTMSKGEKARLEIEPEWAYGKKGQPDAKIPPNAKLTFEVELVDID
>d1rou__ 4.19.1.1.5 FKBP59-I, the N-terminal domain [Rabbit (Oryctolagus cuniculus)]
GVDISPKQDEGVLKVIKREGTGTETPMIGDRVFVHYTGWLLDGTKFDSSLDRKDKFSFDLGKGEVIKAWDIAVATMKVGELCRITCKPEYAYGSAGSPPKIPPNATLVFEVELFEFKG
>d1ctn_3 4.19.3.1.1 (419-492) Chitinase A, insertion domain [Serratia marcescens]
AMYGRGWTGVNGYQNNIPFTGTATGPVKGTWENGIVDYRQIAGQFMSGEWQYTYDATAEAPYVFKPSTGDLITF
>d1grj_2 4.19.4.1.1 (79-151) GreA transcript cleavage factor, C-terminal domain [Escherichia coli]
MPNNGRVIFGATVTVLNLDSDEEQTYRIVGDDEADFKQNLISVNSPIARGLIGKEEDDVVVIVEFEVIKVEYL
>d2baa__ 4.2.1.1.1 Barley endochitinase [pearled barley (Hordeum vulgare l.)]
SVSSIVSRAQFDRMLLHRNDGACQAKGFYTYDAFVAAAAAFPGFGTTGSADAQKREVAAFLAQTSHETTGGWATAPDGAFAWGYCFKQERGASSDYCTPSAQWPCAPGKRYYGRGPIQLSHNYNYGPAGRAIGVDLLANPDLVATDATVGFKTAIWFWMTAQPPKPSSHAVIAGQWSPSGADRAAGRVPGFGVITNIINGGIECGHGQDSRVADRIGFYKRYCDILGVGYGNNLDCYSQRPFA
>d193l__ 4.2.1.2.1 Lysozyme [chicken (Gallus gallus)]
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>d1jug__ 4.2.1.2.10 Lysozyme [Australian echidna (Tachyglossus aculeatus)]
KILKKQELCKNLVAQGMNGYQHITLPNWVCTAFHESSYNTRATNHNTDGSTDYGILQINSRYWCHDGKTPGSKNACNISCSKLLDDDITDDLKCAKKIAGEAKGLTPWVAWKSKCRGHDLSKFKC
>d1lmn__ 4.2.1.2.11 Lysozyme [rainbow trout (Oncorhynchus mykiss)]
KVYDRCELARALKASGMDGYAGNSLPNWVCLSKWESSYNTQATNRNTDGSTDYGIFQINSRYWCDDGRTPGAKNVCGIRCSQLLTDDLTVAIRCAKRVVLDPNGIGAWVAWRLHCQNQDLRSYVAGCGV
>d1alc__ 4.2.1.2.13 alpha-Lactalbumin [baboon (Papio cynocephalus)]
KQFTKCELSQNLYDIDGYGRIALPELICTMFHTSGYDTQAIVENDESTEYGLFQISNALWCKSSQSPQSRNICDITCDKFLDDDITDDIMCAKKILDIKGIDYWIAHKALCTEKLEQWLCEK
>d1hml__ 4.2.1.2.14 alpha-Lactalbumin [human (Homo sapiens)]
KQFTKCELSQLLKDIDGYGGIALPELICTMFHTSGYDTQAIVENNESTEYGLFQISNKLWCKSSQVPQSRNICDISCDKFLDDDITDDIMCAKKILDIKGIDYWLAHKALCTEKLEQWLCEKL
>d1hfx__ 4.2.1.2.15 alpha-Lactalbumin [guinea pig (Gavia porcellus)]
KQLTKCALSHELNDLAGYRDITLPEWLCIIFHISGYDTQAIVKNSDHKEYGLFQINDKDFCESSTTVQSRNICDISCDKLLDDDLTDDIMCVKKILDIKGIDYWLAHKPLCSDKLEQWYCEAQ
>d1hfya_ 4.2.1.2.16 alpha-Lactalbumin [goat (Capra hircus)]
EQLTKCEVFQKLKDLKDYGGVSLPEWVCTAFHTSGYDTQAIVQNNDSTEYGLFQINNKIWCKDDQNPHSRNICNISCDKFLDDDLTDDIVCAKKILDKVGINYWLAHKALCSEKLDQWLC
>d1hfza_ 4.2.1.2.17 alpha-Lactalbumin [bovine (Bos taurus)]
MEQLTKCEVFRELKDLKGYGGVSLPEWVCTTFHTSGYDTQAIVQNNDSTEYGLFQINNKIWCKDDQNPHSSNICNISCDKFLDDDLTDDIVCVKKILDKVGINYWLAHKALCSEKLDQWLCEK
>d1lzy__ 4.2.1.2.2 Lysozyme [turkey (Meleagris gallopavo)]
KVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKFESNFNTHATNRNTDGSTDYGILQINSRWWCNDGRTPGSKNLCNIPCSALLSSDITASVNCAKKIASGGNGMNAWVAWRNRCKGTDVHAWIRGCRL
>d1hhl__ 4.2.1.2.3 Lysozyme [guinea fowl (Numida meleagris)]
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNSQATNRNTDGSTDYGVLQINSRWWCNDGRTPGSRNLCNIPCSALQSSDITATANCAKKIVSDGDGMNAWVAWRKHCKGTDVRVWIKGCRL
>d1ghla_ 4.2.1.2.4 Lysozyme [pheasant (Phasianus colchicus)]
GKVYGRCELAAAMKRMGLDNYRGYSLGNWVCAAKFESNFNTGATNRNTDGSTDYGILQINSRWWCNDGRTPGSKNLCHIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRKHCKGTDVNVWIRGCRL
>d1lzr__ 4.2.1.2.8 Lysozyme [human (Homo sapiens)]
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
>d2eql__ 4.2.1.2.9 Lysozyme [Horse (Equus caballus) milk]
KVFSKCELAHKLKAQEMDGFGGYSLANWVCMAEYESNFNTRAFNGKNANGSSDYGLFQLNNKWWCKDNKRSSSNACNIMCSKLLDENIDDDISCAKRVVRDPKGMSAWKAWVKHCKDKDLSEYLASCNL
>d192l__ 4.2.1.3.1 Phage T4 lysozyme [Escherichia coli infected with bacteriophage T4]
MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLAAAKAALAAAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWAAAAAALAKSRWYNQTPNRAKRVITTFRTGTWDAYK
>d174la_ 4.2.1.3.1 Phage T4 lysozyme [Escherichia coli infected with bacteriophage T4]
MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLAAAADLAAAKAALAAAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYKNL
>d119l__ 4.2.1.3.1 Phage T4 lysozyme [Escherichia coli infected with bacteriophage T4]
MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLSKSRWYNQTPNRAKRVITTFRTGTWDAYK
>d191l__ 4.2.1.3.1 Phage T4 lysozyme [Escherichia coli infected with bacteriophage T4]
MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRACAGAITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRMLQQKRWDAAAAALAKSRWYNQTPNRAKRVITTFRTGTWDAYK
>d169la_ 4.2.1.3.1 Phage T4 lysozyme [Escherichia coli infected with bacteriophage T4]
MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRMLQQKRWDAAAAALAAAAWAAATPNRAKRVITTFRTGTWDAYK
>d189l__ 4.2.1.3.1 Phage T4 lysozyme [Escherichia coli infected with bacteriophage T4]
MNLFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPDLNVAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILRNPKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTDSLRMLQQKRWDEAAANLAKSRWYNQTPDRAKRVITTFRTGTWDAYKNL
>d1gbs__ 4.2.1.4.2 Lysozyme [Australian black swan (Cygnus atratus)]
RTDCYGNVNRIDTTGASCKTAKPEGLSYCGVPASKTIAERDLKAMDRYKTIIKKVGEKLCVEPAVIAGIISRESHAGKVLKNGWGDRGNGFGLMQVDKRSHKPQGTWNGEVHITQGTTILTDFIKRIQKKFPSWTKDQQLKGGISAYNAGAGNVRSYARMDIGTTHDDYANDVVARAQYYKQHGY
>d1sly_2 4.2.1.5.1 (451-618) Soluble lytic transglycosylase, SLT [Escherichia coli]
LAYNDLFKRYTSGKEIPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHTVKMFSIPGYSSPGQLLDPETNINIGTSYLQYVYQQFGNNRIFSSAAYNAGLGRVRTWLGNSAGRIDAVAFVESIPFSETRGYVKNVLAYDAYYRYFMGDKPTLMSATEWGRRY
>d1chka_ 4.2.1.6.1 Endochitosanase [(Streptomyces sp.)]
AGAGLDDPHKKEIAMELVSSAENSSLDWKAQYKYIEDIGDGRGYTGGIIGFCSGTGDMLELVQHYTDLEPGNILAKYLPALKKVNGSASHSGLGTPFTKDWATAAKDTVFQQAQNDERDRVYFDPAVSQAKADGLRALGQFAYYDAIVMHGPGNDPTSFGGIRKTAMKKARTPAQGGDETTYLNGFLDARKAAMLTEAAHDDTSRVDTEQRVFLKAGNLDLNPPLKWKTYGDPYVINS
>d1froa_ 4.20.1.1.1 Glyoxalase I [human (Homo sapiens)]
GGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKMATLM
>d1dhy_2 4.20.1.3.1 (133-278) 2,3-Dihydroxybiphenyl dioxygenase (DHDB, BPHC enzyme) [Pseudomonas sp.]
VSGFVTGDQGIGHFVRCVPDTAKAMAFYTEVLGFVLSDIIDIVPAHFLHCNGRHHTIALAAFPIPKRIHHFMLQANTIDDVGYAFDRLDAAGRITSLLGRHTNDQTLSFYADTPSPMIEVEFGWGPRTVWTVARHSRTAMWGHKSV
>d1dhy_1 4.20.1.3.1 (1-132) 2,3-Dihydroxybiphenyl dioxygenase (DHDB, BPHC enzyme) [Pseudomonas sp.]
SIERLGYLGFAVKDVPAWDHFLTKSVGLMAAGSAGDAALYRADQRAWRIAVQPGELDDLAYAGLEVDDAAALERMADKLRQAGVAFTRGDEALMQQRKVMGLLCLQDPFGLPLEIYYGPAEIFHEPFLPSAP
>d1han_1 4.20.1.3.2 (1-131) 2,3-Dihydroxybiphenyl dioxygenase (DHDB, BPHC enzyme) [Pseudomonas cepacia]
SIRSLGYMGFAVSDVAAWRSFLTQKLGLMEAGTTDNGDLFRIDSRAWRIAVQQGEVDDLAFAGYEVADAAGLAQMADKLKQAGIAVTTGDASLARRRGVTGLITFADPFGLPLEIYYGASEVFEKPFLPGA
>d1han_2 4.20.1.3.2 (132-287) 2,3-Dihydroxybiphenyl dioxygenase (DHDB, BPHC enzyme) [Pseudomonas cepacia]
AVSGFLTGEQGLGHFVRCVPDSDKALAFYTDVLGFQLSDVIDMKMGPDVTVPAYFLHCNERHHTLAIAAFPLPKRIHHFMLEVASLDDVGFAFDRVDADGLITSTLGRHTNDHMVSFYASTPSGVEVEYGWSARTVDRSWVVVRHDSPSMWGHKSV
>d1mkaa_ 4.21.1.1.1 beta-Hydroxydecanol thiol ester dehydrase [(Escherichia coli)]
VDKRESYTKEDLLASGRGELFGAKGPQLPAPNMLMMDRVVKMTETGGNFDKGYVEAELDINPDLWFFGCHFIGDPVMPGCLGLDAMWQLVGFYLGWLGGEGKGRALGVGEVKFTGQVLPTAKKVTYRIHFKRIVNRRLIMGLADGEVLVDGRLIYTASDLKVGLFQDTSAF
>d1csei_ 4.22.1.1.1 Eglin C [leech (Hirudo medicinalis)]
KSFPEVVGKTVDQAREYFTLHYPQYNVYFLPEGSPVTLDLRYNRVRVFYNPGTNVVNHVPHVG
>d1ypci_ 4.22.1.1.2 Chymotrypsin inhibitor CI-2 [barley (Hordeum vulgare), hiproly strain]
MKTEWPELVGKSVAAAKKVILQDKPEAQIIVLPVGTIVTMEYRIDRVRLFVDKLDNIAQVPRVG
>d1coai_ 4.22.1.1.2 Chymotrypsin inhibitor CI-2 [barley (Hordeum vulgare), hiproly strain]
MKTEWPELVGKSVEEAKKVILQDKPEAQIIVLPVGTIVTMEYRIDRVRLFVDKLDNVAEVPRVG
>d3ci2__ 4.22.1.1.2 Chymotrypsin inhibitor CI-2 [barley (Hordeum vulgare), hiproly strain]
LKTEWPELVGKSVEEAKKVILQDKPEAQIIVLPVGTIVTMEYRIDRVRLFVDKLDNIAQVPRVG
>d1tin__ 4.22.1.1.3 Trypsin inhibitor V [pumpkin (Cucurbita maxima)]
SSCPGKSSWPHLVGVGGSVAKAIIERQNPNVKAVILEEGTPVTKDFRCNRVRIWVNKRGLVVSPPRIG
>d1alo_3 4.23.1.1.1 (194-310) Aldehyde oxidoreductase, domain 3 [(Desulfovibrio gigas)]
DYGADLGLKMPAGTLHLAMVQAKVSHANIKGIDTSEALTMPGVHSVITHKDVKGKNRITGLITFPTNKGDGWDRPILCDEKVFQYGDCIALVCADSEANARAAAEKVKVDLEELPAY
>d1qapa2 4.23.2.1.1 (1-122) Quinolinic acid phosphoribosyltransferase, N-terminal domain [Salmonella typhimurium]
DDRRDALLERINLDIPAAVAQALREDLGGEVDAGNDITAQLLPADTQAHATVITREDGVFCGKRWVEEVFIQLAGDDVRLTWHVDDGDAIHANQTVFELQGPARVLLTGERTALNFVQTLSG
>d1tpt_3 4.23.3.1.1 (335-440) Thymidine phosphorylase, C-terminal domain [Escherichia coli]
PTAMLTKAVYADTEGFVSEMDTRALGMAVVAMGGGRRQASDTIDYSVGFTDMARLGDQVDGQRPLAVIHAKDENNWQEAAKAVKAAIKLADKAPESTPTVYRRISE
>d1efub1 4.24.1.1.1 (1-139) Elongation factor Ts (EF-Ts), dimerisation domain [Escherichia coli]
AEITASLVKELRERTGAGMMDCKKALTEANGDIELAIENMRKSGAIKAAKKAGNVAADGVIKTKIDGNYGIILEVNCQTDFVAKDAGFQAFADKVLDAAVAGKITDVEVLKAQFEEERVALVAKIGENINIRRVAALEG
>d1efub2 4.24.1.1.1 (140-282) Elongation factor Ts (EF-Ts), dimerisation domain [Escherichia coli]
DVLGSYQHGARIGVLVAAKGADEELVKHIAMHVAASKPEFIKPEDVSAEVVEKEYQVQLDIAMQSGKPKEIAEKMVEGRMKKFTGEVSLTGQPFVMEPSKTVGQLLKEHNAEVTGFIRFEVGEGIEKVETDFAAEVAAMSKQS
>d1tfe__ 4.24.1.1.2 Elongation factor Ts (EF-Ts), dimerisation domain [Thermus termophilus]
AREGIIGHYIHHNQRVGVLVELNCETDFVARNELFQNLAKDLAMHIAMMNPRYVSAEEIPAEELEKERQIYIQAALNEGKPQQIAEKIAEGRLKKYLEEVVLLEQPFVKDDKVKVKELIQQAIAKIGENIVVRRFCRFELGA
>d1mnga2 4.25.1.1.1 (93-203) Mn superoxide dismutase (SOD) [Thermus thermophilus]
GGAKEPVGELKKAIDEQFGGFQALKEKLTQAAMGRFGSGWAWLVKDPFGKLHVLSTPNQDNPVMEGFTPIVGIDVWEHAYYLKYQNRRADYLQAIWNVLNWDVAEEFFKKA
>d1abma2 4.25.1.1.2 (84-198) Mn superoxide dismutase (SOD) [human (Homo sapiens)]
NGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERGHLQIAACPNQDPLQGTTGLIPLLGIDVWEHAYYLQYKNVRPDYLKAIWNVINWENVTERYMACKK
>d3sdpa2 4.25.1.1.3 (80-186) Fe superoxide dismutase (SOD) [Pseudomonas ovalis]
DAGGQPTGALADAINAAFGSFDKFKEEFTKTSVGTFGSGWAWLVKADGSLALCSTIGAGAPLTSGDTPLLTCDVWEHAYYIDYRNLRPKYVEAFWNLVNWAFVAEEG
>d1isaa2 4.25.1.1.4 (83-192) Fe superoxide dismutase (SOD) [Escherichia coli]
NAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNSDGKLAIVSTSNAGTPLTTDATPLLTVDVWEHAYYIDYRNARPGYLEHFWALVNWEFVAKNLAA
>d1idsa2 4.25.1.1.5 (85-198) Fe superoxide dismutase (SOD) [Mycobacterium tuberculosis]
NGGDKPTGELAAAIADAFGSFDKFRAQFHAAATTVQGSGWAALGWDTLGNKLLIFQVYDHQTNFPLGIVPLLLLDMWEHAFYLQYKNVKVDFAKAFWNVVNWADVQSRYAAATS
>d1ctf__ 4.26.1.1.1 Ribosomal protein L7/12, C-terminal fragment [Escherichia coli]
EFDVILKAAGANKVAVIKAVRGATGLGLKEAKDLVESAPAALKEGVSKDDAEALKKALEEAGAEVEVK
>d2reb_2 4.27.1.1.1 (244-303) RecA protein, C-terminal domain [Escherichia coli]
NFYGELVDLGVKEKLIEKAGAWYSYKGEKIGQGKANATAWLKDNPETAKEIEKKVRELLL
>d1stu__ 4.28.1.1.1 Staufen, domain III [fruit fly (Drosophila melanogaster]
PISQVHEIGIKRNMTVHFKVLREEGPAHMKNFITACIVGSIVTEGEGNGKKVSKKRAAEKMLVELQKL
>d1pkp_2 4.28.1.2.1 (1-74) Ribosomal S5 protein, the N-terminal domain [Bacillus stearothermophilus]
INPNKLELEERVVAVNRVAKVVKGGRRLRFSALVVVGDKNGHVGFGTGKAQEVPEAIRKAIEDAKKNLIEVPIV
>d1pda_2 4.28.2.1.1 (209-296) Porphobilinogen deaminase (hydroxymethylbilane synthase), C-terminal domain [Escherichia coli]
NHHETALRVTAERAMNTRLEGGCQVPIGSYAELIDGEIWLRALVGAPDGSQIIRGERRGAPQDAEQMGISLAEELLNNGAREILAEVY
>d1vig__ 4.29.1.1.1 Vigilin, repeat 6 [Human (Homo sapiens)]
INRMDYVEINIDHKFHRHLIGKSGANINRIKDQYKVSVRIPPDSEKSNLIRIEGDPQGVQQAKRELLELAS
>d1aec__ 4.3.1.1.1 Actinidin [chinese gooseberry or kiwifruit (Actinidia chinensis)]
LPSYVDWRSAGAVVDIKSQGECGGCWAFSAIATVEGINKIVTGVLISLSEQELIDCGRTQNTRGCNGGYITDGFQFIINNGGINTEENYPYTAQDGECNVDLQNEKYVTIDTYENVPYNNEWALQTAVTYQPVSVALDAAGDAFKQYSSGIFTGPCGTAIDHAVTIVGYGTEGGIDYWIVKNSWDTTWGEEGYMRILRNVGGAGTCGIATMPSYPVKY
>d2act__ 4.3.1.1.1 Actinidin [chinese gooseberry or kiwifruit (Actinidia chinensis)]
LPSYVDWRSAGAVVDIKSQGECGGCWAFSAIATVEGINKITSGSLISLSEQELIDCGRTQNTRGCDGGYITDGFQFIINDGGINTEENYPYTAQDGDCDVALQDQKYVTIDTYENVPYNNEWALQTAVTYQPVSVALDAAGDAFKQYASGIFTGPCGTAVDHAIVIVGYGTEGGVDYWIVKNSWDTTWGEEGYMRILRNVGGAGTCGIATMPSYPVKY
>d1cjl__ 4.3.1.1.10 (Pro)cathepsin L [Human (Homo sapiens)]
DHSLEAQWTKWKAMHNRLYGMNEEGWRRAVWEKNMKMIELHNQEYREGKHSFTMAMNAFGDMTSEEFRQVMNGLQNRKPRKGKVFQEPLFYEAPRSVDWREKGYVTPVKNQGQCGSSWAFSATGALEGQMFRKTGRLISLSEQNLVDCSGPEGNEGCNGGLMDYAFQYVQDNGGLDSEESYPYEATEESCKYNPKYSVANDAGFVDIPKQEKALMKAVATVGPISVAIDAGHESFLFYKEGIYFEPDCSSEDMDHGVLVVGYGFESNKYWLVKNSWGEEWGMGGYVKMAKDRRNHCGIASAASYPTV
>d1ppd__ 4.3.1.1.2 Papain [papaya (Carica papaya)]
IPEYVDWRQKGAVTPVKNQGSCGSCWAFSAVVTIEGIIKIRTGNLNQYSEQELLDCDRRSYGCNGGYPWSALQLVAQYGIHYRNTYPYEGVQRYCRSREKGPYAAKTDGVRQVQPYNQGALLYSIANQPVSVVLQAAGKDFQLYRGGIFVGPCGNKVDHAVAAVGYGPNYILIKNSWGTGWGENGYIRIKRGTGNSYGVCGLYTSSFYPVKN
>d1ppo__ 4.3.1.1.3 Caricain (protease omega) [papaya (Carica papaya)]
LPENVDWRKKGAVTPVRHQGSCGSCWAFSAVATVEGINKIRTGKLVELSEQELVDCERRSHGCKGGYPPYALEYVAKNGIHLRSKYPYKAKQGTCRAKQVGGPIVKTSGVGRVQPNNEGNLLNAIAKQPVSVVVESKGRPFQLYKGGIFEGPCGTKVDHAVTAVGYGKSGGKGYILIKNSWGTAWGEKGYIRIKRAPGNSPGVCGLYKSSYYPTKN
>d1yal__ 4.3.1.1.4 Chymopapain [papaya (Carica papaya)]
YPQSIDWRAKGAVTPVKNQGACGSWAFSTIATVEGINKIVTGNLLELSEQELVDCDKHSYGCKGGYQTTSLQYVANNGVHTSKVYPYQAKQYKCRATDKPGPKVKITGYKRVPSNETSFLGALANQPLSVLVEAGGKPFQLYKSGVFDGPCGTKLDHAVTAVGYGTSDGKNYIIIKNSWGPNWGEKGYMRLKRQSGNSQGTCGVYKSSYYPFKGFA
>d1huc.1 4.3.1.1.5 (a,b) (Pro)cathepsin B [Human (Homo sapiens)]
LPASFDAREQWPQCPTIKEIRDQGSCGSCWAFGAVEAISDRICIHTNCCGSMCGDGCNGGYPAEAWNFWTRKGLVSGGLYESHVGCRPYSIPPCEHHVNGSRPPCTGEGDTPKCSKICEPGYSPTYKQDKHYGYNSYSVSNSEKDIMAEIYKNGPVEGAFSVYSDFLLYKSGVYQHVTGEMMGGHAIRILGWGVENGTPYWLVANSWNTDWGDNGFFKILRGQDHCGIESEVVAGIPRTDLPASFDAREQWPQCPTIKEIRDQGSCGSCWAFGAVEAISDRICIHTNCCGSMCGDGCNGGYPAEAWNFWTRKGLVSGGLYESHVGCRPYSIPPCEHHVNGSRPPCTGEGDTPKCSKICEPGYSPTYKQDKHYGYNSYSVSNSEKDIMAEIYKNGPVEGAFSVYSDFLLYKSGVYQHVTGEMMGGHAIRILGWGVENGTPYWLVANSWNTDWGDNGFFKILRGQDHCGIESEVVAGIPRTD
>d1ctea_ 4.3.1.1.6 (Pro)cathepsin B [Rat (Rattus norvegicus)]
LPESFDAREQWSNCPTIAQIRDQGSCGSCWAFGAVEAMSDRICIHTNGRVNVEVSAEDLLTCCGIQCGDGCNGGYPSGAWNFWTRKGLVSGGVYNSHIGCLPYTIPPCEHHVNGARPPCTGEGDTPKCNKMCEAGYSTSYKEDKHYGYTSYSVSDSEKEIMAEIYKNGPVEGAFTVFSDFLTYKSGVYKHEAGDVMGGHAIRILGWGIENGVPYWLVANSWNADWGDNGFFKILRGENHCGIESEIVAGIPRT
>d1gece_ 4.3.1.1.7 Glycyl endopeptidase [papaya (Carica papaya)]
LPESVDWRAKGAVTPVKHQGYCESCWAFSTVATVEGINKIKTGNLVELSEQELVDCDLQSYGCNRGYQSTSLQYVAQNGIHLRAKYPYIAKQQTCRANQVGGPKVKTNGVGRVQSNNEGSLLNAIAHQPVSVVVESAGRDFQNYKGGIFEGSCGTKVDHAVTAVGYGKSGGKGYILIKNSWGPGWGENGYIRIRRASGNSPGVCGVYRSSYYPIKN
>d1gcb__ 4.3.1.1.8 Bleomycin hydrolase, Gal6 [Baker's yeast (Saccharomyces cerevisiae)]
SSSIDISKINSWNKEFQSDLTHQLATTVLKNYNADDALLNKTRLQKQDNRVFNTVVSTDSTPVTNQKSSGRCWLFAATNQLRLNVLSELNLKEFELSQAYLFFYDKLEKANYFLDQIVSSADQDIDSRLVQYLLAAPTEDGGQYSMFLNLVKKYGLIPKDLYGDLPYSTTASRKWNSLLTTKLREFAETLRTALKERSADDSIIVTLREQMQREIFRLMSLFMDIPPVQPNEQFTWEYVDKDKKIHTIKSTPLEFASKYAKLDPSTPVSLINDPRHPYGKLIKIDRLGNVLGGDAVIYLNVDNETLSKLVVKRLQNNKAVFFGSHTPKFMDKKTGVMDIELWNYPAIGYNLPQQKASRIRYHESLMTHAMLITGCHVDETSKLPLRYRVENSWGKDSGKDGLYVMTQKYFEEYCFQIVVDINELPKELASKFTSGKEEPIVLPIWDPMGALA
>d1aim__ 4.3.1.1.9 Cruzain [Trypanosoma cruzi]
APAAVDWRARGAVTAVKDQGQCGSCWAFSAIGNVECQWFLAGHPLTNLSEQMLVSCDKTDSGCSGGLMNNAFEWIVQENNGAVYTEDSYPYASGEGISPPCTTSGHTVGATITGHVELPQDEAQIAAWLAVNGPVAVAVDASSWMTYTGGVMTSCVSEALDHGVLLVGYNDSAAVPYWIIKNSWTTQWGEEGYIRIAKGSNQCLVKEEASSAVVG
>d1ggta4 4.3.1.2.1 (172-496) Coagulation factor XIII, catalytic domain [Human (Homo sapiens) blood]
DAVYLDNEKEREEYVLNDIGVIFYGEVNDIKTRSWSYGQFEDGILDTCLYVMDRAQMDLSGRGNPIKVSRVGSAMVNAKDDEGVLVGSWDNIYAYGVPPSAWTGSVDILLEYRSSENPVRYGQCWVFAGVFNTFLRCLGIPARIVTNYFSAHDNDANLQMDIFLEEDGNVNSKLTKDSVWNYHCWNEAWMTRPDLPVGFGGWQAVDSTPQENSDGMYRCGPASVQAIKHGHVCFQFDAPFVFAEVNSDLIYITAKKDGTHVVENVDATHIGKLIVTKQIGGDGMMDITDTYKFQEGQEEERLALETALMYGAKKPLNTEGVMKSR
>d1gpma3 4.30.1.1.1 (381-501) GMP synthetase, the C-terminal, dimerisation domain [Escherichia coli]
GPGLGVRVLGEVKKEYCDLLRRADAIFIEELRKADLYDKVSQAFTVFLPVRSVGVMGDGRKYDWVVSLRAVETIDFMTAHWAHLPYDFLGRVSNRIINEVNGISRVVYDISGKPPATIEWE
>d1ebha2 4.31.1.1.1 (1-141) Enolase [baker's yeast (Saccharomyces cerevisiae)]
AVSKVYARSVYDSRGNPTVEVELTTEKGVFRSIVPSGASTGVHEALEMRDGDKSKWMGKGVLHAVKNVNDVIAPAFVKANIDVKDQKAVDDFLISLDGTANKSKLGANAILGVSLAASRAAAAEKNVPLYKHLADLSKSKT
>d1pdz_2 4.31.1.1.2 (1-139) Enolase [Lobster (Homarus vulgaris)]
SITKVFARTIFDSRGNPTVEVDLYTSKGLFRAAVPSGASTGVHEALEMRDGDKSKYHGKSVFNAVKNVNDVIVPEIIKSGLKVTQQKECDEFMCKLDGTENKSSLGANAILGVSLAICKAGAAELGIPLYRHIANLANY
>d1muca2 4.31.1.1.3 (1-118) Muconate-lactonizing enzyme (cis muconate cycloisomerase) [(Pseudomonas putida)]
ALIERIDAIIVDLPTIRQQQTLVVLRVRCSDGVEGIGEATTIGGLAYGYESPEGIKANIDAHLAPALIGLAADNINAAMLKLDKLAKGNTFAKSGIESALLDAQGKRLGLPVSELLGG
>d2mnr_2 4.31.1.1.4 (1-130) Mandelate racemase [Pseudomonas putida]
EVLITGLRTRAVNVPLAYPVHTAVGTVGTAPLVLIDLATSAGVVGHSYLFAYTPVALKSLKQLLDDMAAMIVNEPLAPVSLEAMLAKRFCLAGYTGLIRMAAAGIDMAAWDALGKVHETPLVKLLGANAR
>d2chr_2 4.31.1.1.5 (1-126) Chlormuconate cycloisomerase [Alcaligenes eutrophus]
MKIDAIEAVIVDVPTKRPIQMSITTVHQQSYVIVRVYSEGLVGVGEGGSVGGPVWSAECAETIKIIVERYLAPHLLGTDAFNVSGALQTMARAVTGNASAKAAVEMALLDLKARALGVSIAELLGG
>d1fxd__ 4.33.1.1.1 Ferredoxin II [Desulfovibrio gigas]
PIEVNDDCMACEACVEICPDVFEMNEEGDKAVVINPDSDLDCVEEAIDSCPAEAIVRS
>d1fdx__ 4.33.1.1.2 Ferredoxin II [Peptococcus aerogenes]
AYVINDSCIACGACKPECPVNIIQGSIYAIDADSCIDCGSCASVCPVGAPNPED
>d1fdn__ 4.33.1.1.3 Ferredoxin II [Closridium acidiurici]
AYVINEACISCGACEPECPVNAISSGDDRYVIDADTCIDCGACAGVCPVDAPVQA
>d1fca__ 4.33.1.1.3 Ferredoxin II [Closridium acidiurici]
AYVINEACISCGACEPECPVDAISQGGSRYVIDADTCIDCGACAGVCPVDAPVQA
>d1clf__ 4.33.1.1.4 Ferredoxin II [Closridium pasteurianum]
AYKIADSCVSCGACASECPVNAISQGDSIFVIDADTCIDCGNCANVCPVGAPVQE
>d1blu__ 4.33.1.1.5 Ferredoxin II [Cromatium vinosum]
ALMITDECINCDVCEPECPNGAISQGDETYVIEPSLCTECVGHYETSQCVEVCPVDCIIKDPSHEETEDELRAKYERITG
>d1fd2__ 4.33.1.2.1 Ferredoxin [Azotobacter vinelandii ]
AFVVTDNCIKCKYTDCVEVAPVDCFYEGPNFLVIHPDECIDCALCEPECPAQAIFSEDEVPEDMQEFIQLNAELAEVWPNITEKKDPLPDAEDWDGVKGKLQHLER
>d1xer__ 4.33.1.3.1 Ferredoxin [Sulfolobus sp.]
GIDPNYRTNRQVVGEHSGHKVYGPVEPPVLGIHGTIVGVDFDLCIADGSCINACPVNVFQWYDTPGHPASEKKADPVNEQACIFCMACVNVCPVAAIDVKPP
>d1vjw__ 4.33.1.4.1 Ferredoxin [Thermatoga maritima]
MKVRVDADACIGCGVCENLCPDVFQLGDDGKAKVLQPETDLPCAKDAADSCPTGAISVE
>d1fxra_ 4.33.1.4.2 Ferredoxin I [Sulfate-reducing bacteria (Desulfovibrio africanus)]
ARKFYVDQDECIACESCVEIAPGAFAMDPEIEKAYVKDVEGASQEEVEEAMDTCPVQCIHWEDE
>d2fxb__ 4.33.1.4.3 Ferredoxin [Bacillus thermoproteolyticus]
PKYTIVDKETCIACGACGAAAPDIYDYDEDGIAYVTLDDNQGIVEVPDILIDDMMDAFEGCPTDSIKVADEPFDGDPNKFE
>d1aps__ 4.33.10.1.1 Acylphosphatase [horse (Equus caballus)]
STARPLKSVDYEVFGRVQGVCFRMYAEDEARKIGVVGWVKNTSKGTVTGQVQGPEEKVNSMKSWLSKVGSPSSRIDRTNFSNEKTISKLEYSNFSVRY
>d1ris__ 4.33.11.1.1 Ribosomal protein S6 [Thermus thermophilus]
MRRYEVNIVLNPNLDQSQLALEKEIIQRALENYGARVEKVEELGLRRLAYPIAKDPQGYFLWYQVEMPEDRVNDLARELRIRDNVRRVMVVKSQEPF
>d1dar_4 4.33.12.1.1 (526-615) Elongation factor G (EF-G), domain V [Thermus thermophilus]
VILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLRSKTQGRGSFVMFFDHYQEVPKQVQEKLIK
>d1afi__ 4.33.14.1.1 Mercuric ion binding protein MerP [shigella flexneri]
ATQTVTLAVPGMTCAACPITVKKALSKVEGVSKVDVGFEKREAVVTFDDTKASVQKLTKATADAGYPSSVKQ
>d1psda3 4.33.15.1.1 (321-404) Phosphoglycerate dehydrogenase, regulatory (C-terminal) domain [Escherichia coli]
FPEVSLPLHGGRRLMHIHENRPGVLTALNKIFAEQGVNIAAQYLQTSAQMGYVVIDIEADEDVAEKALQAMKAIPGTIRARLLY
>d1mla_2 4.33.17.1.1 (126-195) Probable ACP-binding domain of malonyl-CoA ACP transacylase [Esherichia coli]
GTGAMAAIIGLDDASIAKACEEAAEGQVVSPVNFNSPGQVVIAGHKEAVERAGAACKAAGAKRALPLPVS
>d1fwp__ 4.33.18.1.1 CheY-binding domain of CheA [Escherichia coli]
PRRIILSRLKAGEVDLLEEELGHLTTLTDVVKGADSLSAILPGDIAEDDITAVLCFVIEADQITFETVE
>d1regx_ 4.33.19.1.1 Translational regulator protein regA [Bacteriophage T4)]
MIEITLKKPEDFLKVKETLTRMGIANNKDKVLYQSCHILQKKGLYYIVHFKEMLRMDGRQVEMTEEDEVRRDSIAWLLEDWGLIEIVPGQRTFMKDLTNNFRVISFKQKHEWKLVPKYTIGN
>d1raab1 4.33.2.1.1 (1-100) Aspartate carbamoyltransferase [Escherichia coli]
MTHDNKLQVEAIKRGTVIDHIPAQIGFKLLSLFKLTETDQRITIGLNLPSGEMGRKDLIKIENTFLSEDQVDQLALYAPQATVNRIDNYEVVGKSRPSLP
>d2atcb1 4.33.2.1.1 (1-100) Aspartate carbamoyltransferase [Escherichia coli]
MTHNDKLQVAEIKRGTVINHIPAEIGFKLLSLFKLTETQDRITIGLNLPSGEMGRKDLIKIENTFLSEDEVDELALYAPQATVNRINDYEVVGKSRPSLP
>d1ab8a_ 4.33.20.1.1 Type II adenylyl cyclase C2 domain [rat (Rattus norvegicus)]
LYHQSYDCVCVMFASIPDFKEFYTESDVNKEGLECLRLLNEIIADFDDLLSKPKFSGVEKIKTIGSTYMAATGLSAIPSQQYMHIGTMVEFAYALVGKLDAINKHSFNDFKLRVGINHGPVIAGVIGAQKPQYDIWGNTVNVASRMDSTGVLDKIQVTEETSLILQTLGYTCTCFVN
>d1vaoa1 4.33.21.1.1 (264-550) Vanillyl-alcohol oxidase [Fungus (Penicillium simplicissimum)]
RGYQSYLITLPKDGDLKQAVDIIRPLRLGMALQNVPTIRHILLDAAVLGDKRSYSSRTEPLSDEELDKIAKQLNLGRWNFYGALYGPEPIRRVLWETIKDAFSAIPGVKFYFPEDTPENSVLRVRDKTMQGIPTYDELKWIDWLPNGAHLFFSPIAKVSGEDAMMQYAVTKKRCQEAGLDFIGTFTVGMREMHHIVCIVFNKKDLIQKRKVQWLMRTLIDDCAANGWGEYRTHLAFMDQIMETYNWNNSSFLRFNEVLKNAVDPNGIIAPGKSGVWPSQYSHVTWKL
>d1geo_1 4.33.22.1.1 (1-60) Sulfite reductase, domains 1 and 3 [Escherichia coli]
LLRCRLPGGVITTKQWQAIDKFAGENTIYGSIRLTNRQTFQFHGILPVHQMLHSVGLDAL
>d1geo_2 4.33.22.1.1 (234-313) Sulfite reductase, domains 1 and 3 [Escherichia coli]
IGWVKGIDDQWHLTLFIENGRILDYPARPLKTGLLEIAKIHKGDFRITANQNLIIAGVPESEKAKIEKIAKESGLMNAVT
>d1pca_2 4.33.3.1.1 (1-94) Carboxypeptidase A [porcine (Sus scrofa)]
KEDFVGHQVLRISVDDEAQVQKVKELEDLEHLQLDFWRGPARPGFPIDVRVPFPSIQAVKVFLEAHGIRYTIMIEDVQLLLDEEQEQMFASQGR
>d1pyta_ 4.33.3.1.2 Carboxypeptidase A [bovine (Bos taurus)]
KEDFVGHQVLRITAADEAEVQTVKELEDLEHLQLDFWRGPGQPGSPIDVRVPFPSLQAVKVFLEAHGIRYRIMIEDVQSLLDEEQEQMFASQSR
>d1pba__ 4.33.3.1.3 Carboxypeptidase B [porcine (Sus scrofa)]
HHSGEHFEGEKVFRVNVEDENDISELHELASTRQIDFWKPDSVTQIKPHSTVDFRVKAEDILAVEDFLEQNELQYEVLINN
>d1spbp_ 4.33.3.2.1 Subtilisin BPN' prosegment [Bacillus amyloliquifaciens]
EKKYIVGFKQTMSTMSAAKKKDVISEKGGKVQKQFKYVDAASATLNEKAVKELKKDPSVAYVEEDHVAHAY
>d1mli__ 4.33.4.1.1 Muconalactone isomerase [Pseudomonas putida]
MLFHVKMTVKLPVDMDPAKATQLKADEKELAQRLQREGTWRHLWRIAGHYANYSVFDVPSVEALHDTLMQLPLFPYMDIEVDGLCRHPSSIHSDDR
>d1pil__ 4.33.5.1.1 Signal transducing protein P2 (product of glnB) [Escherichia coli]
MKKIDAIIKPFKLDDVREALAEVGITGMTVTEVKGFGRQKGHTELYRGAEYMVDFLPKVKIEIVVPDDIVDTCVDTIIRTAQTGKIGDGKIFVFDVARVIRIRTGEEDDAAI
>d1nskr_ 4.33.6.1.1 Nucleoside diphosphate kinases [Human (Homo sapiens)]
MANLERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVAMKFLRASEEHLKQHYIDLKDRPFFPGLVKYMNSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGSDSVKSAEKEISLWFKPEELVDYKSCAHDWVY
>d1npk__ 4.33.6.1.2 Nucleoside diphosphate kinases [Dictyostelium discodeum]
VNKERTFLAVKPDGVARGLVGEIIARYEKKGFVLVGLKQLVPTKDLAESHYAEHKERPFFGGLVSFITSGPVVAMVFEGKGVVASARLMIGVTNPLASAPGSIRGDFGVDVGRNIIHGSDSVESANREIALWFKPEELLTEVKPNPNLYE
>d1nsqa_ 4.33.6.1.3 Nucleoside diphosphate kinases [Drosophila]
AANKERTFIMVKPDGVQRGLVGKIIERFEQKGFKLVALKFTWASKELLEKHYADLSARPFFPGLVNYMNSGPVVPMVWEGLNVVKTGRQMLGATNPADSLPGTIRGDFCIQVGRNIIHGSDAVESAEKEIALWFNEKELVTWTPAAKDWIYE
>d1nhkr_ 4.33.6.1.4 Nucleoside diphosphate kinases [Myxococcus xanthus]
AIERTLSIIKPDGLEKGVIGKIISRFEEKGLKPVAIRLQHLSQAQAEGFYAVHKARPFFKDLVQFMISGPVVLMVLEGENAVLANRDIMGATNPAQAAEGTIRKDFATSIDKNTVHGSDSLENAKIEIAYFFRETEIHSYPYQK
>d1up1_2 4.33.7.1.1 (87-170) Nuclear ribonucleoprotein A1, RNP A1, UP1 [human homo sapiens]
GAHLTVKKIFVGGIKEDTEEHHLRDYFEQYGKIEVIEIMTDRGSGKKRGFAFVTFDDHDSVDKIVIQKYHTVNGHNCEVRKALS
>d1up1_1 4.33.7.1.1 (1-86) Nuclear ribonucleoprotein A1, RNP A1, UP1 [human homo sapiens]
PKEPEQLRKLFIGGLSFETTDESLRSHFEQWGTLTDCVVMRDPNTKRSRGFGFVTYATVEEVDAAMNARPHKVDGRVVEPKRAVSR
>d1urna_ 4.33.7.1.2 U1A protein [human (Homo sapiens)]
AVPETRPNHTIYINNLNEKIKKDELKKSLHAIFSRFGQILDILVSRSLKMRGQAFVIFKEVSSATNALRSMQGFPFYDKPMRIQYAKTDSDIIAKM
>d2u1a__ 4.33.7.1.2 U1A protein [human (Homo sapiens)]
MAPAQPLSENPPNHILFLTNLPEETNELMLSMLFNQFPGFKEVRLVPGRHDIAFVEFDNEVQAGAARDALQGFKITQNNAMKISFAKK
>d1sxl__ 4.33.7.1.3 Sex-lethal protein (second RNA-binding domain) [Drosophila melanogaster]
MSYARPGGESIKDTNLYVTNLPRTITDDQLDTIFGKYGSIVQKNILRDKLTGRPRGVAFVRYNKREEAQEAISALNNVIPEGGSQPLSVRLAEEHGK
>d2bopa_ 4.33.8.1.1 Papillomavirus-1 E2 protein [bovine papillomavirus-1]
SCFALISGTANQVKCYRFRVKKNHRHRYENCTTTWFTVADNGAERQGQAQILITFGSPSQRQDFLKHVPLPPGMNISGFTASLDF
>d1dhma_ 4.33.8.1.2 Papillomavirus-1 E2 protein [(HUMAN PAPILLOMAVIRUS-31)]
MATTPIIHLKGDANILKCLRYRLSKYKQLYEQVSSTWHWTCTDGKHKNAIVTLTYISTSQRDDFLNTVKIPNTVSVSTGYMTI
>d1vhia_ 4.33.8.1.3 Epstein barr virus nuclear antigen-1 (ebna1) [Epstein-Barr virus]
MGQGGSNPKFENIAEGLRALLARSHVERTTDEGTWVAGVFVYGGSKTSLYNLRRGTALAIPQCRLTPLSRLPFGMAPGPGPQPGPLRESIVCYFMVFLQTHIFAEVLKDAIKDLVMTKPAPTCNIRVTVCSFDDGVDLP
>d3rubl2 4.33.9.1.1 (1-121) Ribulose 1,5-bisphosphate carboxylase-oxygenase [tobacco (Nicotiana tabacum) variant turkish samsun]
LTYYTPEYQTKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTVWTDGLTSLDRYKGRCYRIERVVGEKDQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYVKT
>d1ausl2 4.33.9.1.2 (1-128) Ribulose 1,5-bisphosphate carboxylase-oxygenase [spinach (Spinacia oleracea)]
YKLTYYTPEYETLDTDILAAFRVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTNLDRYKGRCYHIEPVAGEENQYICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPVAYVKT
>d1rbla2 4.33.9.1.3 (1-139) Ribulose 1,5-bisphosphate carboxylase-oxygenase [Synechococcus, strain pcc 6301]
SAAGYKAGVKDYKLTYYTPDYTPKDTDLLAAFRFSPQPGVPADEAGAAIAAESSTGTWTTVWTDLLTDMDRYKGKCYHIEPVAGEENSYFAFIAYPLDLFEEGSVTNILTSIVGNVFGFKAIRSLRLEDIRFPVALVKT
>d5ruba2 4.33.9.1.4 (1-125) Ribulose 1,5-bisphosphate carboxylase-oxygenase [Rhodospirillum rubrum]
DQSSRYVNLALKEEDLIAGGEHVLCAYIMKPKAGYGYVATAAHFAAESSTGTRGVDALVYEVDEARELTKIAYPVALFDRNITDGKAMIASFLTLTMGNNQGMGDVEYAKMHDFYVPEAYRALFD
>d1lbu_2 4.34.1.1.1 (84-213) Zn2+ DD-carboxypeptidase, the C-terminal, catalytic domain [Streptomyces albus G]
VNFTYAELNRCNSDWSGGKVSAATARANALVTMWKLQAMRHAMGDKPITVNGGFRSVTCNSNVGGASNSRHMYGHAADLGAGSQGFCALAQAARNHGFTEILGPGYPGHNDHTHVAGGDGRFWSAPSCGI
>d1vhh__ 4.34.1.2.1 Sonic hedgehog [Murine (Mus musculus)]
KLTPLAYKQFIPNVAEKTLGASGRYEGKITRNSERFKELTPNYNPDIIFKDEENTGADRLMTQRCKDKLNALAISVMNQWPGVKLRVTEGWDEDGHHSEESLHYEGRAVDITTSDRDRSKYGMLARLAVEAGFDWVYYESKAHIHCSVKAENSVAAK
>d1tig__ 4.35.1.1.1 Translation initiation factor IF3 [Bacillus stearothermophilus]
INVKEVRLSPTIEEHDFNTKLRNARKFLEKGDKVKATIRFKGRAITHKEIGQRVLDRLSEACADIAVVETAPKMDGRNMFLVLAPKND
>d1ife__ 4.35.1.1.2 Translation initiation factor IF3 [Escherichia coli, strain: JM83]
VIQVKEIKFRPGTDEGDYQVKLRSLIRFLEEGDKAKITLRFRGREMAHQQIGMEVLNRVKDDLQELAVVESFPTKIEGRQMIMVLAPKKKQ
>d1uae__ 4.35.2.1.1 UDP-N-acetylglucosamine enolpyruvyl transferase (EPT, MurA, MurZ) [Escherichia coli]
MDKFRVQGPTKLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDVDTSMKLLSQLGAKVERNGSVHIDARDVNVFCAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCTIGARPVDLHISGLEQLGATIKLEEGYVKASVDGRLKGAHIVMDKVSVGATVTIMCAATLAEGTTIIENAAREPEIVDTANFLITLGAKISGQGTDRIVIEGVERLGGGVYRVLPDRIETGTFLVAAAISRGKIICRNAQPDTLDAVLAKLRDAGADIEVGEDWISLDMHGKRPKAVNVRTAPHPAFPTDMQAQFTLLNLVAEGTGFITETVFENRFMHVPELSRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRGYERIEDKLRALGANIERVKG
>d1nawa_ 4.35.2.1.2 UDP-N-acetylglucosamine enolpyruvyl transferase (EPT, MurA, MurZ) [Enterobacter cloacae]
MDKFRVQGPTRLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVERNGSVWIDASNVNNFSAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLEEGYVKASVNGRLKGAHIVMDKVSVGATVTIMSAATLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTFLVAAAISGGKIVCRNAQPDTLDAVLAKLREAGADIETGEDWISLDMHGKRPKAVTVRTAPHPAFPTDMQAQFTLLNLVAEGTGVITETIFENRFMHVPELIRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRGYERIEDKLRALGANIERVKGE
>d1eps__ 4.35.2.1.3 5-enol-pyruvyl shikimate-3-phosphate(EPSP) synthase [Escherichia coli]
MESLTLQPIARVDGTINLPGSKTVSNRALLLAALAHGKTVLTNLLDSDDVRHMLNALTALGVSYTLSADRTRCEIIGNGGPLHAEGALELFLGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRLGGAKITYLEQENYPPLRLQGGFTGGNVDVDGSVSSQFLTALLMTAPLAPEDTVIRIKGDLVSKPYIDITLNLMKTFGVEIENQHYQQFVVKGGQSYQSPGTYLVEGDASSASYFLAAAAIKGGTVKVTGIGRNSMQGDIRFADVLEKMGATICWGDDYISCTRGELNAIDMDMNHIPDAAMTIATAALFAKGTTRLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDYIRITPPEKLNFAEIATYNDHRMAMCFSLVALSDTPVTILDPKCTAKTFPDYFEQLARISQAA
>d1kpta_ 4.36.1.1.1 Virally encoded KP4 toxin [Ustilago maydis P4 strain]
LGINCRGSSQCGLSGGNLMVRIRDQACGNQGQTWCPGERRAKVCGTGNSISAYVQSTNNCISGTEACRHLTNLVNHGCRVCGSDPLYAGNDVSRGQLTVNYVNSC
>d1kvd.1 4.36.1.2.1 (a,b) SMK toxin [halotolerant yeast Pichia farinosa]
WSLRWRMQKSTTIAAIAGCSGAATFGGLAGGIVGCIAAGILAILQGFEVNWHNGGGGDRSNPVMIKFSLAGGSNDPGGSPCSDDWSLRWRMQKSTTIAAIAGCSGAATFGGLAGGIVGCIAAGILAILQGFEVNWHNGGGGDRSNPVMIKFSLAGGSNDPGGSPCSDD
>d3rubs_ 4.37.1.1.1 Ribulose 1,5-bisphosphate carboxylase-oxygenase [tobacco (Nicotiana tabacum) variant turkish samsun]
MQVWPPINKKKYETLSYLPDLSQEQLLSEVEYLLKNGWVPCLEFETEHGFVYRENNKSPGYYDGRYWTMWKLPMFGCTDATQVLAEVEEAKKAYPQAWIRIIGFDNVRQVQCISFIAYKPEGY
>d1auss_ 4.37.1.1.2 Ribulose 1,5-bisphosphate carboxylase-oxygenase [spinach (Spinacia oleracea)]
MQVWPILNLKKYETLSYLPPLTTDQLARQVDYLLNNKWVPCLEFETDHGFVYREHHNSPGYYDGRYWTMWKLPMFGCTDPAQVLNELEECKKEYPNAFIRIIGFDSNREVQCISFIAYKPAGY
>d1burs_ 4.37.1.1.2 Ribulose 1,5-bisphosphate carboxylase-oxygenase [spinach (Spinacia oleracea)]
MQVWPILGMKKYETLSYLPPLTTEQLLAEVNYLLVNNWIPCLEFEVKDGFVYREHLKSPGYYDGRYWTMWKLPMFGCTDPAQVLNELEECKKAYPDAFIRIIGFDNKRQVQCISFIAYKPAGY
>d1rblm_ 4.37.1.1.3 Ribulose 1,5-bisphosphate carboxylase-oxygenase [Synechococcus, strain pcc 6301]
SMKTLPKERRFETFSYLPPLSDRQIAAQIEYMIEQGFHPLIEFNEHSNPEEFYWTMWKLPLFACAAPQQVLDEVRECRSEYGDCYIRVAGFDNIKECQTSSFIVHRPGR
>d1dcoa_ 4.38.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) [Rat (Rattus rattus]
HRLSAEERDQLLPNLRAVGWNELEGRDAIFKQFHFKDFNRAFGFMTRVALQAEKLDHHPEWFNVYNKVHITLSTHECAGLSERDINLASFIEQVAVSMT
>d1xxaa_ 4.38.2.1.1 C-terminal domain of arginine repressor [Escherichia coli]
LKNLVLDIDYNDAVVVIHTSPGAAQLIARLLDSLGKAEGILGTIAGDDTIFTTPANGFTVKDLYEAILELF
>d2chsa_ 4.39.1.1.1 Chorismate mutase [Bacillus subtilis]
MIRGIRGATTVERDTEEEILQKTKQLLEKIIEENHTKPEDVVQMLLSATPDLHAVFPAKAVRELSGWQYVPVTCMQEMDVTGGLKKCIRVMMTVQTDVPQDQIRHVYLEKAVVL
>d7rsa__ 4.4.1.1.1 Ribonuclease A (also ribonuclease B, S) [bovine (Bos taurus)]
KETAAAKFERQHMDSSTSAASSSNYCNQMMKSRNLTKDRCKPVNTFVHESLADVQAVCSQKNVACKNGQTNCYQSYSTMSITDCRETGSSKYPNCAYKTTQANKHIIVACEGNPYVPVHFDASV
>d1onc__ 4.4.1.1.2 P-30 protein [frog (Rana pipiens)]
XDWLTFQKKHITNTRDVDCDNIMSTNLFHCKDKNTFIYSRPEPVKAICKGIIASKNVLTTSEFYLSDCNVTSRPCKYKLKKSTNKFCVTCENQAPVHFVGVGSC
>d1bsra_ 4.4.1.1.3 Seminal ribonucleasease [bovine (Bos taurus)]
KESAAAKFERQHMDSGNSPSSSSNYCNLMMCCRKMTQGKCKPVNTFVHESLADVKAVCSQKKVTCKNGQTNCYQSKSTMRITDCRETGSSKYPNCAYKTTQVEKHIIVACGGKPSVPVHFDASV
>d1ang__ 4.4.1.1.4 Angiogenin [Human (Homo sapiens)]
QDNSRYTHFLTQHYDAKPQGRDDRYCESIMRRRGLTSPCKDINTFIHGNKRSIKAICENKNGNPHRENLRISKSSFQVTTCKLHGGSPWPPCQYRATAGFRNVVVACENGLPVHLDQSIFRRP
>d1agi__ 4.4.1.1.5 Angiogenin [Bovine (Bos taurus)]
AQDDYRYIHFLTQHYDAKPKGRNDEYCFNMMKNRRLTRPCKDRNTFIHGNKNDIKAICEDRNGQPYRGDLRISKSEFQITICKHKGGSSRPPCRYGATEDSRVIVVGCENGLPVHFDESFITPRH
>d1otfa_ 4.40.1.1.1 4-oxalocrotonate tautomerase [Pseudomonas sp.]
PIAQLYIIEGRTDEQKETLIRQVSEAMANSLDAPLERVRVLITEMPKNHFGIGGEPASK
>d1otga_ 4.40.1.2.1 5-carboxymethyl-2-hydroxymuconate isomerase (CHMI) [Escherichia coli]
PHFIVECSDNIREEADLPGLFAKVNPTLAATGIFPLAGIRSRVHWVDTWQMADGQHDYAFVHMTLKIGAGRSLESRQQAGEMLFELIKTHFAALMESRLLALSFEIEELHPTLNFKQNNVHALFK
>d1mifa_ 4.40.1.3.1 Microphage migration inhibition factor (MIF) [Human (Homo sapiens)]
PMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLMAFGGSSEPCALCSLHSIGKIGGAQNRSYSKLLCGLLAERLRISPDRVYINYYDMNAASVGWNNSTFA
>d1fim__ 4.40.1.3.2 Microphage migration inhibition factor (MIF) [Rat (Rattus norvegicus)]
PAFIVNTNVPRASVPEGFLSELTQQLAQATGKPAQYIAVHVVPDQLTFSGTSDPCALCSLHSIGKIGGAQNRNYSKLLCGLLSDRLHISPDRVYINYYDANA
>d1gado2 4.41.1.1.1 (149-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) [Escherichia coli]
CTTNCLAPLAKVINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYD
>d1gd1o2 4.41.1.1.2 (151-313) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) [Bacillus stearothermophilus /nca 1503]
CTTNCLAPFAKVLHEQFGIVRGMMTTVHSYTNDQRILDLPHKDLRRARAAAESIIPTTTGAAKAVALVLPELKGKLNGMAMRVPTPNVSVVDLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMVIDGKMVKVVSWYD
>d1cero2 4.41.1.1.3 (149-310) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) [Thermus aquaticus]
CTTNSLAPVMKVLEEAFGVEKALMTTVHSYTNDQRLLDLPHKDLRRARAAAINIIPTTTGAAKATALVLPSLKGRFDGMALRVPTATGSISDITALLKREVTAEEVNAALKAAAEGPLKGILAYTEDEIVLQDIVMDPHSSIVDAKLTKALGNMVKVFAWYD
>d1hdgo2 4.41.1.1.4 (151-332) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) [Thermotoga maritima]
CTTNSIAPIVKVLHEKFGIVSGMLTTVHSYTNDQRVLDLPHKDLRRARAAAVNIIPTTTGAAKAVALVVPEVKGKLDGMAIRVPTPDGSITDLTVLVEKETTVEEVNAVMKEATEGRLKGIIGYNDEPIVSSDIIGTTFSGIFDATITNVIGGKLVKVASWYDNEYGYSNRVVDTLELLLKM
>d1ggao2 4.41.1.1.5 (165-333) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) [Trypanosoma brucei brucei, glycosome]
CTTNCLAPLVHVLVKEGFGISTGLMTTVHSYTATQKTVDGVSVKDWRGGRAAALNIIPSTTGAAKAVGMVIPSTQGKLTGMAFRVPTADVSVVDLTFIATRDTSIKEIDAALKRASKTYMKNILGYTDEELVSADFISDSRSSIYDSKATLQNNLPNERRFFKIVSWYD
>d1gypa2 4.41.1.1.6 (166-334) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) [Leishmania mexicana]
CTTNCLAPIVHVLTKENFGIETGLMTTIHSYTATQKTVDGVSLKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDKAIKKAAQTYMKGILGFTDEELVSADFINDNRSSVYDSKATLQNNLPGEKRFFKVVSWYD
>d1gpdg2 4.41.1.1.7 (148-311) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) [lobster (Homarus americanus)]
CTTNCLAPVAKVLHENFEIVEGLMTTVHAVTATQKTVDGPSAKDWRGGRGAAQNIIPSSTGAAKAVGKVIPELDGKLTGMAFRVPTPDVSVVDLTVRLGKECSYDDIKAAMKTASEGPLQGFLGYTEDDVVSSDFIGDNRSSIFDAKAGIQLSKTFVKVVSWYD
>d3gpdr2 4.41.1.1.8 (151-314) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) [human (Homo sapiens)]
CTTNCLAPLAKVIHDHFGIVEGLMTTVHAITATQKTVDSPSGKLWRGGRGAAQNLIPASTGAAKAVGKVIPELDGKLTGMAFRVPTANVSVLDLTCRLEKPAKYDDIKKVVKEASEGPLKGILGYTEDEVVSDDFNGSNHSSIFDAGAGIELNDTFVKLVSWYD
>d1dapa2 4.41.1.2.1 (119-268) Diaminopimelic acid dehydrogenase (DAPDH) [Corynebacterium glutamicum]
WDPGMFSINRVYAAAVLAEHQQHTFWGPGLSQGHSDALRRIPGVQKAVQYTLPSEDALEKARRGEAGDLTGKQTHKRQCFVVADAADHERIENDIRTMPDYFVGYEVEVNFIDEATFDSEHTGMPHGGHVITTGDTGGFNHTVEYILKLD
>d1dih_2 4.41.1.2.2 (130-239) Dihydrodipicolinate reductase [Escherichia coli]
VGVNVMLKLLEKAAKVMGDYTDIEIIEAHHRHKVDAPSGTALAMGEAIAHALDKDLKDCAVYSREGHTGERVPGTIGFATVRAGDIVGEHTAMFADIGERLEITHKASSR
>d1ofga2 4.41.1.3.1 (161-322) Glucose-fructose oxidoreductase [Zymomonas mobilis]
DPMNRAAVKLIRENQLGKLGMVTTDNSDVMDQNDPAQQWRLRRELAGGGSLMDIGIYGLNGTRYLLGEEPIEVRAYTYSDPNDERFVEVEDRIIWQMRFRSGALSHGASSYSTTTTSRFSVQGDKAVLLMDPATGYYQNLISVQTPGHANQSMMPQFIMPAN
>d1dpga2 4.41.1.3.2 (182-412,427-485) glucose 6-phosphate dehydrogenase [Leuconostoc mesenteroides]
KEMVQNIAALRFGNPIFDAAWNKDYIKNVQVTLSEVLGVEERAGYYDTAGALLDMIQNHTMQIVGWLAMEKPESFTDKDIRAAKNAAFNALKIYDEAEVNKYFVRAQYGAGDSADFKPYLEELDVPADSKNNTFIAGELQFDLPRWEGVPFYVRSGKRLAAKQTRVDIVFKAGTFNFGSEQEAQEAVLSIIIDPKGAIELKLNAKSVEDAFNTRTIDLGWTVSDEDKKNT
>d1oaca4 4.42.1.1.1 (1-86) Copper amine oxidase, domain 1 [Escherichia coli]
AHMVPMDKTLKEFGADVQWDDYAQLFTLIKDGAYVKVKPGAQTAIVNGQPLALQVPVVMKDNKAWVSDTFINDVFQSGLDQTFQVE
>d1bp1_1 4.43.1.1.1 (1-217) Bactericidal permeability-increasing protein, BPI [human (Homo sapiens)]
VNPGVVVRISQKGLDYASQQGTAALQKELKRIKIPDYSDSFKIKHLGKGHYSFYSMDIREFQLPSSQISMVPNVGLKFSISNANIKISGKWKAQKRFLKMSGNFDLSIEGMSISADLKLGSNPTSGKPTITCSSCSSHINSVHVHISKSKVGWLIQLFHKKIESALRNKMNSQVCEKVTNSVSSKLQPYFQTLPVMTKIDSVAGINYGLVAPPATTA
>d1bp1_2 4.43.1.1.1 (218-456) Bactericidal permeability-increasing protein, BPI [human (Homo sapiens)]
ETLDVQMKGEFYSENHHNPPPFAPPVMEFPAAHDRMVYLGLSDYFFNTAGLVYQEAGVLKMTLRDDMIPKESKFRLTTKFFGTFLPEVAKKFPNMKIQIHVSASTPPHLSVQPTGLTFYPAVDVQAFAVLPNSALASLFLIGMHTTGSMEVSAESNRLVGELKLDRLLLELKHSNIGPFPVELLQDIMNYIVPILVLPRVNEKLQKGFPLPTPARVQLYNVVLQPHQNFLLFGADVVYK
>d2sici_ 4.44.1.1.2 Subtilisin inhibitor [Streptomyces albogriseolus, s-3253]
YAPSALVLTVGKGVSATTAAPERAVTLTCAPGPSGTHPAAGSACADLAAVGGDLNALTRGEDVMCPMVYDPVLLTVDGVWQGKRVSYERVFSNECEMNAHGSSVFAF
>d2ms2a_ 4.45.1.1.1 MS2 virus coat protein [bacteriophage MS2]
ASNFTQFVLVDNGGTGDVTVAPSNFANGVAEWISSNSRSQAYKVTCSVRQSSAQNRKYTIKVEVPKVATQTVGGVELPVAAWRSYLNMELTIPIFATNSDCELIVKAMQGLLKDGNPIPSAIAANSGIY
>d1unaa_ 4.45.1.1.2 GA coat protein [bacteriophage GA]
ATLHSFVLVDNGGTGNVTVVPVSNANGVAEWLSNNSRSQAYRVTASYRASGADKRKYTIKLEVPKIVELPVSAWKAYASIDLTIPIFAATDDVTVISKSLTGLFKVGNPIAEAISSQSGFYA
>d1frsa_ 4.45.1.1.3 fr coat protein [bacteriophage fr]
ASNFEEFVLVDNGGTGDVKVAPSNFANGVAEWISSNSRSQAYKVTCSVRQSSANNRKYTVKVEVPKVATQVQGGVELPVAAWRSYMNMELTIPVFATNDDCALIVKALQGTFKTGNPIATAIAANSGIY
>d1qbea_ 4.45.1.1.4 Qbeta coat protein [bacteriophage Qbeta]
AKLETVTLGNIGKDGKQTLVLNPRGVNPTNGVASLSQAGAVPALEKRVTVSVSQPNYKVQVKIQNPTACTCDPSVTRQAYADVTFSFTQYSTDEERAFVRTELAALLASPLLIDAIDQLNPAY
>d3grs_3 4.46.1.1.1 (347-461) Glutathione reductase [human (Homo sapiens)]
YNNIPTVVFSHPPIGTVGLTEDEAIHKYGIENVKTYSTSFTPMYHAVTKRKTKCVMKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTLR
>d1gesa3 4.46.1.1.2 (334-448) Glutathione reductase [Escherichia coli]
YSNIPTVVFSHPPIGTVGLTEPQAREQYGDDQVKVYKSSFTAMYTAVTTHRQPCRMKLVCVGSEEKIVGIHGIGFGMDEMLQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTMR
>d2tpra3 4.46.1.1.3 (358-482) Trypanothione reductase [Crithidia fasciculata]
HTKVACAVFSIPPMGVCGYVEEDAAKKYDQVAVYESSFTPLMHNISGSTYKKFMVRIVTNHADGEVLGVHMLGDSSPEIIQSVAICLKMGAKISDVYNTIGVHPTSAEELCSMRTPAYFYEKGKR
>d1ndaa3 4.46.1.1.3 (355-481) Trypanothione reductase [Crithidia fasciculata]
HTRVASAVFSIPPIGTCGLIEEVASKRYEVVAVYLSSFTPLMHNISGSKYKTFVAKIITNHSDGTVLGVHLLGDNAPEIIQGVGICLKLNAKISDFYNTIGVHPTSAEELCSMRTPSYYYVKGEKME
>d1nhp_3 4.46.1.1.5 (322-447) NADH peroxidase [Enterococcus faecalis]
GVQGSSGLAVFDYKFASTGINEVMAQKLGKETKAVTVVEDYLMDFNPDKQKAWFKLVYDPETTQILGAQLMSKADLTANINAISLAIQAKMTIEDLAYADFFFQPAFDKPWNIINTAALEAVKQER
>d3lada3 4.46.1.1.6 (349-472) Dihydrolipoamide dehydrogenase [Pseudomonas putida]
YDLIPAVIYTHPEIAGVGKTEQALKAEGVAINVGVFPFAASGRAMAANDTAGFVKVIADAKTDRVLGVHVIGPSAAELVQQGAIAMEFGTSAEDLGMMVFAHPALSEALHEAALAVSGHAIHVA
>d1lpfa3 4.46.1.1.6 (349-472) Dihydrolipoamide dehydrogenase [Pseudomonas putida]
YDLIPSVIYTHPEIAWVGKTEQTLKAEGVEVNVGTFPFAASGRAMAANDTTGLVKVIADAKTDRVLGVHVIGPSAAELVQQGAIGMEFGTSAEDLGMMVFSHPTLSEALHEAALAVNGHAIHIA
>d1lvl_3 4.46.1.1.6 (336-458) Dihydrolipoamide dehydrogenase [Pseudomonas putida]
PAAIAAVCFTDPEVVVVGKTPEQASQQGLDCIVAQFPFAANGRAMSLESKSGFVRVVARRDNHLILGWQAVGVAVSELSTAFAQSLEMGACLEDVAGTIHAHPTLGEAVQEAALRALGHALHI
>d1ebda3 4.46.1.1.7 (340-455) Dihydrolipoamide dehydrogenase [Bacillus stearothermophilus]
VAIPAVVFSDPECASVGYFEQQAKDEGIDVIAAKFPFAANGRALALNDTDGFLKLVVRKEDGVIIGAQIIGPNASDMIAELGLAIEAGMTAEDIALTIHAHPTLGEIAMEAAEVAL
>d1ojt_3 4.46.1.1.8 (355-482) Dihydrolipoamide dehydrogenase [Neisseria meningitidis]
ARVIPGVAYTSPEVAWVGETELSAKASARKITKANFPWAASGRAIANGCDKPFTKLIFDAETGRIIGGGIVGPNGGDMIGEVCLAIEMGCDAADIGKTIHPHPTLGESIGMAAEVALGTCTDLPPQKK
>d1fcda3 4.46.1.1.9 (328-401) Flavocytochrome c sulfide dehydrogenase, FCSD, flavin-binding subunit [Purple phototrophic bacterium (Chromatium vinosum)]
PGTPSYLNTCYSILAPAYGISVAAIYRPNADGSAIESVPDSGGVTPVDAPDWVLEREVQYAYSWYNNIVHDTFG
>d1srsa_ 4.47.1.1.1 Serum response factor (SRF) core [Human (Homo sapiens)]
TRGRVKIKMEFIDNKLRRYTTFSKRKTGIMKKAYELSTLTGTQVLLLVASETGHVYTFATRKLQPMITSETGKALIQTCLNSPD
>d1tbd__ 4.48.1.1.1 The origin DNA-binding domain of SV40 T-antigen [SV40 (Simian virus 40)]
GSKVEDPKDFPSELLSFLSHAVFSNRTLACFAIYTTKEKAALLYKKIMEKYSVTFISRHNSYNHNILFFLTPHRHRVSAINNYAQKLCTFSFLICKGVNKEYLMYSALTRDPFSVIEESLPGGLKEHDFNPESS
>d1nox__ 4.49.1.1.1 NADH oxidase [Thermus thermophilus HB8]
PVLDAKTAALKRRSIRRYRKDPVPEGLLREILEAALRAPSAWNLQPWRIVVVRDPATKRALREAAFGQAHVEEAPVVLVLYADLEDALAHLDEVIHPGVQGERREAQKQAIQRAFAAMGQEARKAWASGQSYILLGYLLLLLEAYGLGSVPMLGFDPERVRAILGLPSRAAIPALVALGYPAEEGYPSHRLPLERVVLWR
>d1ag2__ 4.5.1.1.1 Prion protein domain [mouse (Mus musculus)]
GLGGYMLGSAMSRPMIHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYY
>d1kuh__ 4.50.1.1.1 Zinc protease [Streptomyces caespitosus]
TVTVTYDPSNAPSFQQEIANAAQIWNSSVRNVQLRAGGNADFSYYEGNDSRGSYAQTDGHGRGYIFLDYQQNQQYDSTRVTAHETGHVLGLPDHYQGPCSELMSGGGPGPSCTNPYPNAQERSRVNALWANG
>d1ezm_2 4.50.1.2.1 (1-153) Elastase [Pseudomonas aeruginosa]
AEAGGPGGNQKIGKYTYGSDYGPLIVNDRCEMDDGNVITVDMNSSTDDSKTTPFRFACPTNTYKQVNGAYSPLNDAHFFGGVVFKLYRDWFGTSPLTHKLYMKVHYGRSVENAYWDGTAMLFGDGATMFYPLVSLDVAAHEVSHGFTEQNSGL
>d8tlne2 4.50.1.2.2 (1-155) Thermolysin [Bacillus thermoproteolyticus]
ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGDGIFTYDAKYRTTLPGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAIRSSVHYSQGYNNAFWNGSEMVYGDGDGQTFIPLSGGIDVVAHELTHAVTDYTAGL
>d1npc_2 4.50.1.2.3 (1-156) Neutral protease [Bacillus cereus, strain dsm 3101]
VTGTNKVGTGKGVLGDTKSLNTTLSGSSYYLQDNTRGATIFTYDAKNRSTLPGTLWADADNVFNAAYDAAAVDAHYYAGKTYDYYKATFNRNSINDAGAPLKSTVHYGSNYNNAFWNGSQMVYGDGDGVTFTSLSGGIDVIGHELTHAVTENSSNL
>d1lml__ 4.50.1.3.1 Leishmanolysin [Leishmania major]
VVRDVNWGALRIAVSTEDLTDPAYHCARVGQHVKDHAGAIVTCTAEDILTNEKRDILVKHLIPQAVQLHTERLKVQQVQGKWKVTDMVGDICGDFKVPQAHITEGFSNTDFVMYVASVPSEEGVLAWATTCQTFSDGHPAVGVINIPAANIASRYDQLVTRVVTHEMAHALGFSGPFFEDARIVANVPNVRGKNFDVPVINSSTAVAKAREQYGCDTLEYLEVEDQGGAGSAGSHIKMRNAQDELMAPAAAAGYYTALTMAIFQDLGFYQADFSKAEVMPWGQNAGCAFLTNKCMEQSVTQWPAMFCNAIRCPTSRLSLGACGVTRHPGLPPYWQYFTDPSLAGVSAFMDYCPVVVPYSDGSCTQRASEAHASLLPFNVFSDAARCIDGAFRPKASYAGLCANVQCDTATRTYSVQVHGSNDYTNCTPGLRVELSTVSNAFEGGGYITCPPYVEVCQGNVQAAKD
>d1ast__ 4.50.1.4.1 Astacin [The european fresh water crayfish (Astacus astacus L.)]
AAILGDEYLWSGGVIPYTFAGVSGADQSAILSGMQELEEKTCIRFVPRTTESDYVEIFTSGSGCWSYVGRISGAQQVSLQANGCVYHGTIIHELMHAIGFYHEHTRMDRDNYVTINYQNVDPSMTSNFDIDTYSRYVGEDYQYYSIMHYGKYSFSIQWGVLETIVPLQNGIDLTDPYDKAHMLQTDANQINNLYTNECSL
>d1iag__ 4.50.1.5.1 Snake venom metalloprotease [Adamalysin II: Eastern diamondback rattlesnake (Crotalus adamanteus)]
NLPQRYIELVVVADRRVFMKYNSDLNIIRTRVHEIVNIINKFYRSLNIRVSLTDLEIWSGQDFITIQSSSSNTLNSFGEWRERVLLIWKRHDNAQLLTAINFEGKIIGKAYTSSMCNPRSSVGIVKDHSPINLLVAVTMAHELGHNLGMEHDGKDCLRGASLCIMRPGLTPGRSYEFSDDSMGYYQKFLNQYKPQCILNKP
>d1atla_ 4.50.1.5.2 Snake venom metalloprotease [Atrolysin C: Western diamonback rattlesnake (Crotalus atrox)]
LPQRYIELVVVADHRVFMKYNSDLNTIRTRVHEIVNFINGFYRSLNIHVSLTDLEIWSNEDQINIQSASSDTLNAFAEWRETDLLNRKSHDNAQLLTAIELDEETLGLAPLGTMCDPKLSIGIVQDHSPINLLMGVTMAHELGHNLGMEHDGKDCLRGASLCIMRPGLTKGRSYEFSDDSMHYYERFLKQYKPQCILNKP
>d1kapp2 4.50.1.6.1 (1-239) Metallo protease, catalytic (N-terminal) domain [Pseudomonas aeruginosa (alkaline protease)]
GRSDAYTQVDNFLHAYARGGDELVNGHPSYTVDQAAEQILREQASWQKAPGDSVLTLSYSFLTKPNDFFNTPWKYVSDIYSLGKFSAFSAQQQAQAKLSLQSWSDVTNIHFVDAGQGDQGDLTFGNFSSSVGGAAFAFLPDVPDALKGQSWYLINSSYSANVNPANGNYGRQTLTHEIGHTLGLSHPGDYNAGEGDPTYADATYAEDTRAYSVMSYWEEQNTGQDFKGAYSSAPLLDDI
>d1sat_2 4.50.1.6.2 (1-236) Metallo protease, catalytic (N-terminal) domain [Serratia marcescens]
TGYDAVDDLLHYHERGNGIQINGKDSFSNEQAGLFITRENQTWNGYKVFGQPVKLTFSFPDYKFSSTNVAGDTGLSKFSAEQQQQAKLSLQSWADVANITFTEVAAGQKANITFGNYSQDRPGHYDYGTQAYAFLPNTIWQGQDLGGQTWYNVNQSNVKHPATEDYGRQTFTHEIGHALGLSHPGDYNAGEGDPTYADVTYAEDTRQFSLMSYWSETNTGGDNGGHYAAAPLLDDI
>d1hfc__ 4.50.1.7.1 Fibroblast collagenase [human (Homo sapiens)]
PRWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDERWTNNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSYTFSGDVQLAQDDIDGIQAIYGRS
>d1mnc__ 4.50.1.7.2 Neutrophil collagenase (MMP-8) [Human (Homo sapiens)]
GPKWERTNLTYRIRNYTPQLSEAEVERAIKDAFELWSVASPLIFTGISQGEADINIAFYQRDHGDGSPFDGPNGILAHAFQPGQGIGGDAHFDAEETWTNTSANYNLFLVAAHEFGHSLGLAHSSDPGALMYPNYAFRETSNYSLPQDDIDGIQAIYG
>d2srt__ 4.50.1.7.3 Stromelysin-1 (MMP-3) [human (Homo sapiens) fibroblast]
FRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRFRLSQDDINGIQSLYGPPPDSPET
>d1fbl_2 4.50.1.7.4 (1-172) Stromelysin-1 (MMP-3) [Porcine (Sus scroffa) fibroblast]
FVLTPGNPRWENTHLTYRIENYTPDLSREDVDRAIEKAFQLWSNVSPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDERWTKNFRDYNLYRVAAHELGHSLGLSHSTDIGALMYPNYIYTGDVQLSQDDIDGIQAIYGPSENPVQPSG
>d1mmq__ 4.50.1.7.5 Matrilysin (MMP-9) [Human (Homo sapiens)]
YSLFPNSPKWTSKVVTYRIVSYTRDLPHITVDRLVSKALNMWGKEIPLHFRKVVWGTADIMIGFARGAHGDSYPFDGPGNTLAHAFAPGTGLGGDAHFDEDERWTDGSSLGINFLYAATHELGHSLGMGHSSDPNAVMYPTYGNGDPQNFKLSQDDIKGIQKLYGK
>d1qba_4 4.50.2.1.1 (174-310) Bacterial chitobiase, Domain 2 [(Serratia marcescens)]
SNADLQTLPAGALRGKIVPTPMQVKVHAQDADLRKGVALDLSTLVKPAADVVSQRFALLGVPVQTNGYPIKTDIQPGKFKGAMAVSGAYELKIGKKEAQVIGFDQAGVFYGLQSILSLVPSDGSGKIATLDASDAPR
>d1lcja_ 4.51.1.1.1 p56-lck tyrosine kinase [human (Homo sapiens)]
EPEPWFFKNLSRKDAERQLLAPGNTHGSFLIRESESTAGSFSLSVRDFDQNQGEVVKHYKIRNLDNGGFYISPRITFPGLHELVRHYTNASDGLCTRLSRPCQT
>d1ab2__ 4.51.1.1.10 Proto-oncogen tyrosine kinase [Human (Homo sapiens)]
GSGNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRGIHRD
>d1csya_ 4.51.1.1.11 Syk tyrosine kinase [Human (Homo sapiens)]
GSRRASVGSHEKMPWFHGKISREESEQIVLIGSKTNGKFLIRARDNNGSYALCLLHEGKVLHYRIDKDKTGKLSIPEGKKFDTLWQLVEHYSYKADGLLRVLTVPCQKIGTQ
>d2plda_ 4.51.1.1.12 Phospholipase C-gamma-1 [bovine (Bos taurus)]
GSPGIHESKEWYHASLTRAQAEHMLMRVPRDGAFLVRKRNEPNSYAISFRAEGKIKHCRVQQEGQTVMLGNSEFDSLVDLISYYEKHPLYRKMKLRYPINEENSS
>d1blj__ 4.51.1.1.13 P55 Blk protein tyrosine kinase [mouse (Mus musculus)]
GSVAPVETLEVEKWFFRTISRKDAERQLLAPMNKAGSFLIRESESNKGAFSLSVKDITTQGEVVKHYKIRSLDNGGYYISPRITFPTLQALVQHYSKKGDGLCQKLTLPCVNLA
>d1shaa_ 4.51.1.1.2 v-src tyrosine kinase [rous sarcoma virus (Schmidt-ruppin strain a)]
AEEWYFGKITRRESERLLLNPENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFSSLQQLVAYYSKHADGLCHRLTNVCPT
>d1ayd__ 4.51.1.1.4 Tyrosine phosphatase SYP [mouse (Mus musculus)]
MRRWFHPNITGVEAENLLLTRGVDGSFLARPSKSNPGDFTLSVRRNGAVTHIKIQNTGDYYDLYGGEKFATLAELVQYYMEHHGQLKEKNGDVIELKYPLN
>d1tzee_ 4.51.1.1.5 Growth factor receptor-bound protein 2 (GRB2) [human (Homo sapiens)]
MKPHPWFFGKIPRAKAEEMLSKQRHDGAFLIRESESAPGDFSLSVKFGNDVQHFKVLRDGAGKYFLWVVKFNSLNELVDYHRSTSVSRNQQIFLRDIE
>d2hcka2 4.51.1.1.6 (64-166) Hemopoetic cell kinase Hck [human (Homo sapiens)]
EEWFFKGISRKDAERQLLAPGNMLGSFMIRDSETTKGSYSLSVRDYDPRQGDTVKHYKIRTLDNGGFYISPRSTFSTLQELVDHYKKGNDGLCQKLSVPCMSS
>d1tcea_ 4.51.1.1.7 Shc adaptor protein [human (Homo sapiens)]
AEQLRGEPWFHGKLSRREAEALLQLNGDFLVRESTTTPGQYVLTGSQSGQPKHLLLVDPEGVVRTKDHRFESVSHLISYHMDNHLPIISAGSELCLQQPVERKLLEH
>d2pnb__ 4.51.1.1.8 Phosphatidylinositol 3-kinase, p85-alpha subunit [bovine (Bos taurus)]
LQDAEWYWGDISREEVNEKLRDTADGTFLVRDASTKMHGDYTLTLRKGGNNKLIKIFHRDGKYGFSDPLTFNSVVELINHYRNESLAQYNPKLDVKLLYPVSKY
>d1pica_ 4.51.1.1.9 Phosphatidylinositol 3-kinase, p85-alpha subunit [human (Homo sapiens)]
GSPIPHHDEKTWNVGSSNRNKAENLLRGKRDGTFLVRESSKQGCYACSVVVDGEVKHCVINKTATGYGFAEPYNLYSSLKELVLHYQHTSLVQHNDSLNVTLAYPVYAQQRR
>d1spha_ 4.52.1.1.1 Histidine-containing phosphocarrier proteins (HPr) [Bacillus subtilis]
AQKTFKVTADSGIHARPATVLVQTASKYDADVNLEYNGKTVNLKDIMGVMSLGIAKGAEITISASGADENDALNALEETMKSEGLGE
>d1ptf__ 4.52.1.1.2 Histidine-containing phosphocarrier proteins (HPr) [Streptococcus faecalis]
MEKKEFHIVAETGIHARPATLLVQTASKFNSDINLEYKGKSVNLKSIMGVMSLGVGQGSDVTITVDGADEAEGMAAIVETLQKEGLA
>d1poh__ 4.52.1.1.3 Histidine-containing phosphocarrier proteins (HPr) [Escherichia coli]
MFQQEVTITAPNGLHTRPAAQFVKEAKGFTSEITVTSNGKSASAKSLFKLQTLGLTQGTVVTISAEGEDEQKAVEHLVKLMAELE
>d1pch__ 4.52.1.1.4 Histidine-containing phosphocarrier proteins (HPr) [Mycoplasma capricolum]
AKFSAIITDKVGLHARPASVLAKEASKFSSNITIIANEKQGNLKSIMNVMAMAIKTGTEITIQADGNDADQAIQAIKQTMIDTALIQG
>d1zer__ 4.52.1.1.5 Histidine-containing phosphocarrier proteins (HPr) [Staphylococcus aureus]
MEQNSYVIIDETGIHARPATMLVQTASKFDSDIQLEYNGKKVNLKSIMGVMSLGVGKDAEITIYADGSDESDAIQAISDVLSKEGLT
>d1iba__ 4.53.1.1.1 Glucose permease domain IIB [Escherichia coli]
MAPALVAAFGGKENITNLDACITRLRVSVADVSKVDQAGLKKLGAAGVVVAGSGVQAIFGTKSDNLKTEMDEYIRNFG
>d1af5__ 4.53.2.1.1 DNA endonuclease I-CreI [Chlamydomonas reinhardtii]
KYNKEFLLYLAGFVDGDGSIIAQIKPNQSYKFKHQLSLTFQVTQKTQRRWFLGKLVDEIGVGYVRDRGSVSDYILSEIKPLHNFLTQLQPFLKLKQKQANLVLKIIEQLPLEVCTWVDQIAALNDS
>d1gtpa_ 4.54.1.1.1 GTP cyclohydrolase I [Escherichia coli]
PSLSKEAALVHEALVARGLETPLRPPVHEMDNETRKSLIAGHMTEIMQLLNLDLADDSLMETPHRIAKMYVDEIFSGLDYANFPKITLIENKMKVDEMVTVRDITLTSTCEHHFVTIDGKATVAYIPKDSVIGLSKINRIVQFFAQRPQVQERLTQQILIALQTLLGTNNVAVSIDAVHYCVKARGIRDATSATTTTSLGGLFKSSQNTRHEFLRAVRHHN
>d1gtqa_ 4.54.1.2.1 6-pyruvoyl tetrahydropterin synthase [rat (Rattus rattus)]
LRRRARLSRLVSFSASHRLHSPSLSAEENLKVFGKCNNPNGHGHNYKVVVTIHGEIDPVTGMVMNLTDLKEYMEEAIMKPLDHKNLDLDVPYFADVVSTTENVAVYIWENLQRLLPVGALYKVKVYETDNNIVVYKGE
>d1scea_ 4.55.1.1.1 suc1 [Yeast (Saccharomyces pombe)]
VPRLLTASERERLEPFIDQIHYSPRYADDEYEYRHVMLPKAMLKAIPTDYFNPETGTLRILQEEEWRGLGITQSLGWEMYEVHVPEPHILLFKREKD
>d1cksa_ 4.55.1.1.2 CksHs2 [Human (Homo sapiens)]
AHKQIYYSDKYFDEHYEYRHVMLPRELSKQVPKTHLMSEEEWRRLGVQQSLGWVHYMIHEPEPHILLFRRPLPK
>d1dksa_ 4.55.1.1.3 CksHs1 [Human (Homo sapiens)]
SHKQIYYSDKYDDEEFEYRHVMLPKDIAKLVPKTHLMSESEWRNLGVQQSQGWVHYMIHEPEPHILLFRRPLPKKP
>d1efnb_ 4.57.1.1.1 Regulatory factor Nef [Human immunodeficiency virus type 1, HIV-1]
RPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIYHTQGYFPDWQNYTPGPGVRYPLTFGWCYKLVPVREVLEWRFDSRLAFHHVARELHPEYF
>d1cby__ 4.58.1.1.1 Mosquitocidal delta-endotoxin CytB [Bacillus thuringiensis, strain Kyushuensis]
CSAPIIRKPFKHIVLTVPSSDLDNFNTVFYVQPQYINQALHLANAFQGAIDPLNLNFNFEKALQIANGIPNSAIVKTLNQSVIQQTVEISVMVEQLKKIIQEVLGLVINSTSFWNSVEATIKGTFTNLDTQIDEAWIFWHSLSAHNTSYYYNILFSIQNEDTGAVMAVLPLAFEVSVDVEKQKVLFFTIKDSARYEVKMKALTLVQALHSSNAPIVDIFNVNNYNLY
>d1seta2 4.59.1.1.1 (111-421) Seryl-tRNA synthetase (SerRS) [Thermus thermophilus, strain hb27]
VGGEEANREIKRVGGPPEFSFPPLDHVALMEKNGWWEPRISQVSGSRSYALKGDLALYELALLRFAMDFMARRGFLPMTLPSYAREKAFLGTGHFPAYRDQVWAIAETDLYLTGTAEVVLNALHSGEILPYEALPLRYAGYAPAFRSEAGSFGKDVRGLMRVHQFHKVEQYVLTEASLEASDRAFQELLENAEEILRLLELPYRLVEVATGDMGPGKWRQVDIEVYLPSEGRYRETHSCSALLDWQARRANLRYRDPEGRVRYAYTLNNTALATPRILAMLLENHQLQDGRVRVPQALIPYMGKEVLEPCG
>d1lyla2 4.59.1.1.2 (141-482) Lysyl-tRNA synthetase (LysRS) [Escherichia coli, LysU gene]
DQEVRYRQRYLDLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFDFGKPFEKLTMREAIKKYRPETDMADLDNFDAAKALAESIGITVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFPAMRP
>d1htta2 4.59.1.1.3 (1-267) Histidyl-tRNA synthetase (HisRS) [Escherichia coli]
NIQAIRGMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIGEVTDVVEKEMYTFEDRNGDSLTLRPEGTAGCVRAGIEHGLLYNQEQRLWYIGPMFRHERPQKGRYRQFHQLGCEVFGLQGPDIDAELIMLTARWWRALGISEHVTLELNSIGSLEARANYLDEESREHFAGLCKLLESAGIAYTVNQRLVRGLDYYNRTVFEWVTNQGTVCAGGRYDGLVEQLGGRATPAVGFAMGLERLVLLVQAVNPEFKA
>d1adja2 4.59.1.1.4 (1-324) Histidyl-tRNA synthetase (HisRS) [Thermus thermophilus]
TARAVRGTKDLFGKELRMHQRIVATARKVLEAAGALELVTPIFEETQVFEKGVGAATDIVRKEMFTFQDRGGRSLTLRPEGTAAMVRAYLEHGMKVWPQPVRLWMAGPMFRAERPQKGRYRQFHQVNYEALGSENPILDAEAVVLLYECLKELGLRRLKVKLSSVGDPEDRARYNAYLREVLSPHREALSEDSKERLEENPMRILDSKSERDQALLKELGVRPMLDFLGEEARAHLKEVERHLERLSVPYELEPALVRGLDYYVRTAFEVHHEEIGAQSALGGGGRYDGLSELLGGPRVPGVGFAFGVERVALALEAEGFGLPE
>d1atia2 4.59.1.1.5 (1-326) Glycyl-tRNA synthetase (GlyRS) [Thermus thermophilus]
AASSLDELVALCKRRGFIFQSSEIYGGLQGVYDYGPLGVELKNNLKQAWWRRNVYERDDMEGLDASVLTHRLVLHYSGHEATFADPMVDNWTPPRYFNMMFQDLRGPRGGRGLLAYLRPETAQGIFVNFKNVLDATSRKLGFGIAQIGKAFRNEITPRNFIFRVREFEQMEIEYFVRPGEDEYWHRYWVEERLKWWQEMGLSRENLVPYQQPPESSAHYAKATVDILYRFPHGSLELEGIAQRTDFDLGSHTKDQEALGITARVLRNEHSTQRLAYRDPETGKWFVPYVIEPSAGVDRGVLALLAEAFTREELPNGEERIVLKLKP
>d1asya2 4.59.1.1.6 (138-490) Aspartyl-tRNA synthetase (AspRS) [Yeast (Saccharomyces serevisiae)]
PILLEDASRSEAEAEAAGLPVVNLDTRLDYRVIDLRTVTNQAIFRIQAGVCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQQLIVADFERVYEIGPVFRAENSNTHRHMTEFTGLDMEMAFEEHYHEVLDTLSELFVFIFSELPKRFAHEIELVRKQYPVEEFKLPKDGKMVRLTYKEGIEMLRAAGKEIGDFEDLSTENEKFLGKLVRDKYDTDFYILDKFPLEIRPFYTMPDPANPKYSNSYDFFMRGEEILSGAQRIHDHALLQERMKAHGLSPEDPGLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFPRDPKRLRP
>d1bia_3 4.59.1.2.1 (64-245) Biotin repressor/biotin holoenzyme synthetase, catalytic (central) domain [Escherichia coli]
IQLLNAKQILGQLDGGSVAVLPVIDSTNQYLLDRIGELKSGDACIAEYQQAGSPFGANLYLSMFWRLEQPAAAIGLSLVIGIVMAEVLRKLGADKVRVKWPNDLYLQDRKLAGILVELTGAAQIVIGAGINMAMWITLQEAGINLDRNTLAAMLIRELRAALELFEQEGLAPYLSRWEKLDN
>d2kaua_ 4.6.1.1.1 Urease, gamma-subunit [Klebsiella aerogenes]
MELTPREKDKLLLFTAALVAERRLARGLKLNYPESVALISAFIMEGARDGKSVASLMEEGRHVLTREQVMEGVPEMIPDIQVEATFPDGSKLVTVHNPII
>d2vik__ 4.60.1.1.1 Villin, domain 1 (res. 1-126) [chicken (Gallus gallus)]
VELSKKVTGKLDKTTPGIQIWRIENMEMVPVPTKSYGNFYEGDCYVLLSTRKTGSGFSYNIHYWLGKNSSQDEQGAAAIYTTQMDEYLGSVAVQHREVQGHESETFRAYFKQGLIYKQGGVASGMK
>d1svr__ 4.60.1.1.2 Severin, domain 2 [Dictyostelium discoideum]
EYKPRLLHISGDKNAKVAEVPLATSSLNSGDCFLLDAGLTIYQFNGSKSSPQEKNKAAEVARAIDAERKGLPKVEVFCETDSDIPAEFWKLLGG
>d1cfya_ 4.60.1.2.1 yeast cofilin, monoclinic crystal form [baker's yeast saccharomyces cerevisiae]
VAVADESLTAFNDLKLGKKYKFILFGLNDAKTEIVVKETSTDPSYDAFLEKLPENDCLYAIYDFEYEINGNEGKRSKIVFFTWSPDTAPVRSKMVYASSKDALRRALNGVSTDVQGTDFSEVSYDSVLERVSR
>d1ahq__ 4.60.1.2.2 Actophorin [amoeba (Acanthamoeba castellanii)]
GIAVSDDCVQKFNELKLGHQHRYVTFKMNASNTEVVVEHVGGPNATYEDFKSQLPERDCRYAIFDYEFQVDGGQRNKITFILWAPDSAPIKSKMMYTSTKDSIKKKLVGIQVEVQATDAAEISEDAVSERAKK
>d1ak7__ 4.60.1.2.3 Destrin [pig (Sus scrofa)]
TMITPSSGNSASGVQVADEVCRIFYDMKVRKCSTPEEIKKRKKAVIFCLSADKKCIIVEEGKEILVGDVGVTITDPFKHFVGMLPEKDCRYALYDASFETKESRKEELMFFLWAPELAPLKSKMIYASSKDAIKKKFQGIKHECQANGPEDLNRACIAEKLGGSLIVAFEGCPV
>d1pne__ 4.61.1.1.1 Profilin (actin-binding protein) [bovine (Bos taurus)]
AGWNAYIDNLMADGTCQDAAIVGYKDSPSVWAAVPGKTFVNITPAEVGILVGKDRSSFFVNGLTLGGQKCSVIRDSLLQDGEFTMDLRTKSTGGAPTFNITVTMTAKTLVLLMGKEGVHGGMINKKCYEMASHLRRSQY
>d1pfl__ 4.61.1.1.2 Profilin (actin-binding protein) [human (Homo sapiens)]
AGWNAYIDNLMADGTCQDAAIVGYKDSPSVWAAVPGKTFVNITPAEVGVLVGKDRSSFYVNGLTLGGQKCSVIRDSLLQDGEFSMDLRTKSTGGAPTFNVTVTKTDKTLVLLMGKEGVHGGLINKKCYEMASHLRRSQY
>d2acg__ 4.61.1.1.4 Profilin (actin-binding protein) [Acanthamoeba castellani]
SWQTYVDTNLVGTGAVTQAAIIGHDGNTWATSAGFAVSPANGAALANAFKDATAIRSNGFELAGTRYVTIRADDRSVYGKKGSAGVITVKTSKAILIGVYNEKIQPGTAANVVEKLADYLIGQGF
>d1acf__ 4.61.1.1.4 Profilin (actin-binding protein) [Acanthamoeba castellani]
SWQTYVDTNLVGTGAVTQAAILGLDGNTWATSAGFAVTPAQGTTLAGAFNNADAIRAGGFDLAGVHYVTLRADDRSIYGKKGSSGVITVKTSKAILVGVYNEKIQPGTAANVVEKLADYLIGQGF
>d1cqa__ 4.61.1.1.5 Profilin (actin-binding protein) [Birch (Betula verrucosa)]
SWQTYVDEHLMLAASAIVGHDGSVWAQSSSFPQFKPQEITGIMKDFEEPGHLAPTGLHLGGIKYMVIQGEAGAVIRGKKGSGGITIKKTGQALVFGIYEEPVTPGQCNMVVERLGDYLIDQGL
>d2phy__ 4.61.2.1.1 Photoactive yellow protein [Ectothiorhodospira halophila]
MEHVAFGSEDIENTLAKMDDGQLDGLAFGAIQLDGDGNILQYNAAEGDITGRDPKQVIGKNFFKDVAPCTDSPEFYGKFKEGVASGNLNTMFEYTFDYQMTPTKVKVHMKKALSGDSYWVFVKRV
>d1mut__ 4.62.1.1.1 Nucleoside triphosphate pyrophosphorylase (MutT) [Escherichia coli]
MKKLQIAVGIIRNENNEIFITRRAADAHMANKLEFPGGKIEMGETPEQAVVRELQEEVGITPQHFSLFEKLEYEFPDRHITLWFWLVERWEGEPWGKEGQPGEWMSLVGLNADDFPPANEPVIAKLKRL
>d1tys__ 4.63.1.1.1 Thymidylate synthase [Escherichia coli]
MKQYLELMQKVLDEGTQKNDRTGTGTLSIFGHQMRFNLQDGFPLVTTKRCHLRSIIHELLWFLQGDTNIAYLHENNVTIWDEWADENGDLGPVYGKQWRAWPTPDGRHIDQITTVLNQLKNDPDSRRIIVSAWNVGELDKMALAPSHAFFQFYVADGKLSCQLYQRSCDVFLGLPFNIASYALLVHMMAQQCDLEVGDFVWTGGDTHLYSNHMDQTHLQLSREPRPLPKLIIKRKPESIFDYRFEDFEIEGYDPHPGIKAPVAI
>d4tms__ 4.63.1.1.2 Thymidylate synthase [Lactobacillus casei ]
MLEQPYLDLAKKVLDEGHFKPDRTHTGTYSIFGHQMRFDLSKGFPLLTTKKVPFGLIKSELLWFLHGDTNIRFLLQHRNHIWDEWAFEKWVKSDEYHGPDMTDFGHRSQKDPEFAAVYHEEMAKFDDRVLHDDAFAAKYGDLGLVYGSQWRAWHTSKGDTIDQLGDVIEQIKTHPYSRRLIVSAWNPEDVPTMALPPCHTLYQFYVNDGKLSLQLYQRSADIFLGVPFNIASYALLTHLVAHECGLEVGEFIHTFGDAHLYVNHLDQIKEQLSRTPRPAPTLQLNPDKHDIFDFDMKDIKLLNYDPYPAIKAPVAV
>d1tis__ 4.63.1.1.3 Thymidylate synthase [Bacteriophage t4]
MKQYQDLIKDIFENGYETDDRTGTGTIALFGSKLRWDLTKGFPAVTTKKLAWKACIAELIWFLSGSTNVNDLRLIQHDSLIQGKTVWDENYENQAKDLGYHSGELGPIYGKQWRDFGGVDQIIEVIDRIKKLPNDRRQIVSAWNPAELKYMALPPCHMFYQFNVRNGYLDLQWYQRSVDVFLGLPFNIASYATLVHIVAKMCNLIPGDLIFSGGNTHIYMNHVEQCKEILRREPKELCELVISGLPYKFRYLSTKEQLKYVLKLRPKDFVLNNYVSHPPIKGKMAV
>d1lba__ 4.64.1.1.1 Bacteriophage T7 lysozyme (Zn amidase) [bacteriophage T7]
AKQRESTDAIFVHCSATKPSQNVGVREIRQWHKEQGWLDVGYHFIIKRDGTVEAGRDEMAVGSHAKGYNHNSIGVCLVGGIDDKGKFDANFTPAQMQSLRSLLVTLLAKYEGAVLRAHHEVAPKACPSFDLKRWWEKNELVTSDRG
>d3b5c__ 4.66.1.1.1 Cytochrome b5 [bovine (Bos taurus)]
AVKYYTLEEIQKHNNSKSTWLILHYKVYDLTKFLEEHPGGEEVLREQAGGDATENFEDVGHSTDARELSKTFIIGELHPDDRSKI
>d1b5m__ 4.66.1.1.2 Cytochrome b5 [rat (Rattus norvegicus)]
AVTYYRLEEVAKRNTAEETWMVIHGRVYDITRFLSEHPGGEEVLLEQAGADATESFEDVGHSPDAREMLKQYYIGDVHPNDLKP
>d1iet__ 4.66.1.1.2 Cytochrome b5 [rat (Rattus norvegicus)]
DKDVKYYTLEEIQKHKDSKSTWVILHHKVYDLTKFLEEHPGGEEVLREQAGGDATENFEDVGHSTDARELSKTYIIGELHPDDRSKIAKPSETL
>d1ltda2 4.66.1.1.3 (1-88) Flavocytochrome b2, N-terminal domain [yeast (Saccharomyces cerevisiae)]
KISPAEVAKHNKPDDCWVVINGYVYDLTRFLPNHPGGQDVIKFNAGKDVTAIFEPLHAPNVIDKYIAPEKKLGPLQGSMPPELVCPPY
>d1vcc__ 4.67.1.1.1 Vaccinia DNA topoisomerase I, the 9 kDa N-terminal fragment [Vaccinia virus, strain WR]
MRALFYKDGKLFTDNNFLNPVSDDNPAYEVLQHVKIPTHLTDVVVYEQTWEEALTRLIFVGSDSKGRRQYFYGKMHV
>d1yua_1 4.67.1.2.1 (1-65) Prokariotic DNA topoisomerase I, C-terminal domain [Escherichia coli]
MNGEVAPPKEDPVPLPELPCEKSDAYFVLRDGAAGVFLAANTFPKSRETRAPLVEELYRFRDRLP
>d1yua_2 4.67.1.2.1 (66-122) Prokariotic DNA topoisomerase I, C-terminal domain [Escherichia coli]
EKLRYLADAPQQDPEGNKTMVRFSRKTKQQYVSSEKDGKATGWSAFYVDGKWVEGKK
>d1ah6__ 4.68.1.1.1 HSP90 [yeast (Saccharomyces cerevisiae)]
ASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLSDPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSGTKAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWESNAGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFVAYPIQLVVTKEVE
>d3il8__ 4.7.1.1.1 Interleukin-8, IL-8 [human (Homo sapiens)]
LRCQCIKTYSKPFHPKFIKELRVIESGPHCANTEIIVKLSDGRELCLDPKENWVQRVVEKFLKRAENS
>d1napa_ 4.7.1.1.10 Neutrophil-activating peptide-2 (NAP-2) [Human (Homo sapiens)]
AELRCLCIKTTSGIHPKNIQSLEVIGKGTHCNQVEVIATLKDGRKICLDPDAPRIKKIVQKKLAGD
>d1plfa_ 4.7.1.1.2 Platelet factor 4, PF4 [bovine (Bos taurus)]
LQCVCLKTTSGINPRHISSLEVIGAGLHCPSPQLIATLKTGRKICLDQQNPLYKKIIKRLLKS
>d1rhpa_ 4.7.1.1.3 Platelet factor 4, PF4 [human (Homo sapiens)]
DLQCLCVKTTSQVRPRHITSLEVIKAGPHCPTAQLIATLKNGRKICLDLQAPLYKKIIKKLLES
>d1pfma_ 4.7.1.1.3 Platelet factor 4, PF4 [human (Homo sapiens)]
MSAKELRCQCVKTTSQVRPRHITSLEVIKAGPHCPTAQLIATLKNGRKICLDLQAPLYKKIIKKLLES
>d1msga_ 4.7.1.1.4 Melanoma growth stimulating activity (MGSA) [human (Homo sapiens)]
ASVATELRCQCLQTLQGIHPKNIQSVNVKSPGPHCAQTEVIATLKNGRKACLNPASPIVKKIIEKMLNSDKS
>d1roda_ 4.7.1.1.5 IL-8/MGSA chimeric protein CIL-8M [human (Homo sapiens)]
SAKELRCQCIKTYSKPFHPKFIKELRVIESGPHCANTEIIVKLSDGRELCLDPASPIVKKIIEKMLNSDKSN
>d1huma_ 4.7.1.1.6 Macrophage inflammatory protein 1-beta [human (Homo sapiens)]
APMGSDPPTACCFSYTARKLPRNFVVDYYETSSLCSQPAVVFQTKRSKQVCADPSESWVQEYVYDLELN
>d1rtoa_ 4.7.1.1.7 RANTES (regulated upon activation, normal T-cell expressed and secreted) [human (Homo sapiens)]
SPYSSDTTPCCFAYIARPLPRAHIKEYFYTSGKCSNPAVVFVTRKNRQVCANPEKKWVREYINSLEMS
>d1dona_ 4.7.1.1.8 Monocyte chemoattractant protein-1 (MCP-1, MCAF) [human (Homo sapiens)]
QPDAINAPVTCCYNFTNRKISVQRLASYRRITSSKCPKEAVIFKTIVAKEICADPKQKWVQDSMDHLDKQTQTPKT
>d1ncva_ 4.7.1.1.9 Monocyte chemoattractant protein-3 (MCP-3) [human (Homo sapiens)]
QPVGINTSTTCCYRFINKKIPKQRLESYRRTTSSHCPREAVIFKTKLDKEICADPTQKWVQDFMKHLDKKTQTPKL
>d1orda3 4.70.1.1.1 (570-730) Ornithine decarboxylase C-terminal domain [Lactobacillus 30a]
APLKQVLPSIYAANEERYNGYTIRELCQELHDFYKNNNTFTYQKRLFLREFFPEQGMLPYEARQEFIRNHNKLVPLNKIEGEIALEGALPYPPGVFCVAPGEKWSETAVKYFTILQDGINNFPGFAPEIQGVYFKQEGDKVVAYGEVYDAEVAKNDDRYNN
>d1smna_ 4.71.1.1.1 Endonuclease [Serratia marcescens]
SIDNCAVGCPTGGSSNVSIVRHAYTLNNNSTTKFANWVAYHITKDTPASGKTRNWKTDPALNPADTLAPADYTGANAALKVDRGHQAPLASLAGVSDWESLNYLSNITPQKSDLNQGAWARLEDQERKLIDRADISSVYTVTGPLYERDMGKLPGTQKAHTIPSAYWKVIFINNSPAVNHYAAFLFDQNTPKGADFCQFRVTVDEIEKRTGLIIWAGLPDDVQASLKSKPGVLPELMGCKN
>d1chma2 4.72.1.1.1 (156-401) Creatinase, catalytic (C-terminal) domain [Pseudomonas putida]
MIKSAEEHVMIRHGARIADIGGAAVVEALGDQVPEYEVALHATQAMVRAIADTFEDVELMDTWTWFQSGINTDGAHNPVTTRKVNKGDILSLNCFPMIAGYYTALERTLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIARELNEIFLKHDVLQYRTFGYGHSFGTLSHYYGREAGLELREDIDTVLEPGMVVSMEPMIMLPEGLPGAGGYREHDILIVNENGAENITKFPYGPEKNIIR
>d1mat__ 4.72.1.1.2 Methionine aminopeptidase [Escherichia coli]
AISIKTPEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVNEQHAVSACLGYHGYPKSVCISINEVVCHGIPDDAKLLKDGDIVNIDVTVIKDGFHGDTSKMFIVGKPTIMGERLCRITQESLYLALRMVKPGINLREIGAAIQKFVEAEGFSVVREYCGHGIGRGFHEEPQVLHYDSRETNVVLKPGMTFTIEPMVNAGKKEIRTMKDGWTVKTKDRSLSAQYEHTIVVTDNGCEILTLRKDDTIPAIISHDE
>d1xgsa2 4.72.1.1.3 (1-194,272-295) Methionine aminopeptidase [Pyrococcus furiosus]
MDTEKLMKAGEIAKKVREKAIKLARPGMLLLELAESIEKMIMELGGKPAFPVNLSINEIAAHYTPYKGDTTVLKEGDYLKIDVGVHIDGFIADTAVTVRVGMEEDELMEAAKEALNAAISVARAGVEIKELGKAIENEIRKRGFKPIVNLSGHKIERYKLHAGISIPNIYRPHDNYVLKEGDVFAIEPFATIG
>d1lgr_2 4.73.1.1.1 (95-445) Glutamine synthetase, C-terminal domain [Salmonella typhimurium]
DRDPRSIAKRAEDYLRATGIADTVLFGPEPEFFLFDDIRFGASISGSHVAIDDIEGAWNSSTKYEGGNKGHRPGVKGGYFPVPPVDSAQDIRSEMCLVMEQMGLVVEAHHHEVATAGQNEVATRFNTMTKKADEIQIYKYVVHNVAHRFGKTATFMPKPMFGDNGSGMHCHMSLAKNGTNLFSGDKYAGLSEQALYYIGGVIKHAKAINALANPTTNSYKRLVPPVMLAYSARNRSASIRIPVVASPKARRIEVRFPDPAANPYLCFAALLMAGLDGIKNKIHPGEPMDIPQVAGSLEEALNALDLDREFLKAGGVFTDEAIDAYIALRREEDDRVRMTPHPVEFELYYSV
>d1crka2 4.73.1.2.1 (99-380) Creatine kinase, C-terminal domain [chicken (Gallus gallus) mitochondria]
TMKHHTDLDASKITHGQFDERYVLSSRVRTGRSIRGLSLPPACSRAERREVENVVVTALAGLKGDLSGKYYSLTNMSERDQQQLIDDHFLFDKPVSPLLTCAGMARDWPDARGIWHNNDKTFLVWINEEDHTRVISMEKGGNMKRVFERFCRGLKEVERLIKERGWEFMWNERLGYVLTCPSNLGTGLRAGVHVKLPRLSKDPRFPKILENLRLQKRGTGGVDTAAVADVYDISNLDRMGRSEVELVQIVIDGVNYLVDCEKKLEKGQDIKVPPPLPQFGRK
>d1cdwa_ 4.74.1.1.1 TATA-box binding protein (TBP), C-terminal domain [Human (Homo sapiens)]
SGIVPQLQNIVSTVNLGCKLDLKTIALRARNAEYNPKRFAAVIMRIREPRTTALIFSSGKMVCTGAKSEENSRLAARKYARVVQKLGFPAKFLDFKIQNMVGSCDVKFPIRLEGLVLTHQQFSSYEPELFPGLIYRMIKPRIVLLIFVSGKVVLTGAKVRAEIYEAFENIYPILKGFRK
>d1voka1 4.74.1.1.2 (1-109) TATA-box binding protein (TBP), C-terminal domain [Arabidopsis thaliana]
EGSNPVDLSKHPSGIVPTLQNIVSTVNLDCKLDLKAIALQARNAEYNPKRFAAVIMRIREPKTTALIFASGKMVCTGAKSEDFSKMAARKYARIVQKLGFPAKFKDFKI
>d1voka2 4.74.1.1.2 (110-192) TATA-box binding protein (TBP), C-terminal domain [Arabidopsis thaliana]
QNIVGSCDVKFPIRLEGLAYSHAAFSSYEPELFPGLIYRMKVPKIVLLIFVSGKIVITGAKMRDETYKAFENIYPVLSEFRKI
>d1ytba1 4.74.1.1.3 (1-95) TATA-box binding protein (TBP), C-terminal domain [yeast (Saccharomyces cerevisiae)]
SGIVPTLQNIVATVTLGCRLDLKTVALHARNAEYNPKRFAAVIMRIREPKTTALIFASGKMVVTGAKSEDDSKLASRKYARIIQKIGFAAKFTDF
>d1ytba2 4.74.1.1.3 (96-180) TATA-box binding protein (TBP), C-terminal domain [yeast (Saccharomyces cerevisiae)]
KIQNIVGSCDVKFPIRLEGLAFSHGTFSSYEPELFPGLIYRMVKPKIVLLIFVSGKIVLTGAKQREEIYQAFEAIYPVLSEFRKM
>d1aisa2 4.74.1.1.4 (93-181) TATA-box binding protein (TBP), C-terminal domain [(Pyrococcus woesei)]
KFKRAPQIDVQNMVFSGDIGREFNLDVVALTLPNCEYEPEQFPGVIYRVKEPKSVILLFSSGKIVCSGAKSEADAWEAVRKLLRELDKY
>d1aisa1 4.74.1.1.4 (1-92) TATA-box binding protein (TBP), C-terminal domain [(Pyrococcus woesei)]
MVDMSKVKLRIENIVASVDLFAQLDLEKVLDLCPNSKYNPEEFPGIICHLDDPKVALLIFSSGKLVVTGAKSVQDIERAVAKLAQKLKSIGV
>d3pmga4 4.74.2.1.1 (421-561) Phosphoglucomutase, the C-terminal domain [rabbit (Oryctolagus cuniculus)]
RNFFTRYDYEEVEAEGATKMMKDLEALMFDRSFVGKQFSANDKVYTVEKADNFEYHDPVDGSVSKNQGLRLIFADGSRIIFRLSGTGSAGATIRLYIDSYEKDNAKINQDPQVMLAPLISIALKVSQLQERTGRTAPTVIT
>d1bv1__ 4.74.3.1.1 Major birch pollen allergen Bet v 1 [white birch (Betula verrucosa)]
GVFNYETETTSVIPAARLFKAFILDGDNLFPKVAPQAISSVENIEGNGGPGTIKKISFPEGLPFKYVKDRVDEVDHTNFKYNYSVIEGGPIGDTLEKISNEIKIVATPDGGSILKISNKYHTKGDHEVKAEQVKASKEMGETLLRAVESYLLAHSDAYN
>d1mxa_3 4.75.1.1.1 (226-377) S-adenosylmethionine synthetase. MAT [Escherichia coli]
IGGPMGDCGLTGRKIIVDTYGGMARHGGGAFSGKDPSKVDRSAAYAARYVAKNIVAAGLADRCEIQVSYAIGVAEPTSIMVETFGTEKVPSEQLTLLVREFFDLRPYGLIQMLDLLHPIYKETAAYGHFGREHFPWEKTDKAQLLRDAAGLK
>d1mxa_1 4.75.1.1.1 (1-101) S-adenosylmethionine synthetase. MAT [Escherichia coli]
AKHLFTSESVSEGHPDKIADQISDAVLDAILEQDPKARVACETYVKTGMVLVGGEITTSAWVDIEEITRNTVREIGYVHSDMGFDANSCAVLSAIGKQSPD
>d1mxa_2 4.75.1.1.1 (102-225) S-adenosylmethionine synthetase. MAT [Escherichia coli]
RADPLEQGAGDQGLMFGYATNETDVLMPAPITYAHRLVQRQAEVRKNGTLPWLRPDAKSQVTFQYDDGKIVGIDAVVLSTQHSEEIDQKSLQEAVMEEIIKPILPAEWLTSATKFFINPTGRFV
>d2pola1 4.76.1.1.1 (1-122) DNA polymerase III, beta subunit [Escherichia coli]
MKFTVEREHLLKPLQQVSGPLGGRPTLPILGNLLLQVADGTLSLTGTDLEMEMVARVALVQPHEPGATTVPARKFFDICRGLPEGAEIAVQLEGERMLVRSGRSRFSLSTLPAADFPNLDDW
>d2pola3 4.76.1.1.1 (245-366) DNA polymerase III, beta subunit [Escherichia coli]
RRVLPKNPDKHLEAGCDLLKQAFARAAILSNEKFRGVRLYVSENQLKITANNPEQEEAEEILDVTYSGAEMEIGFNVSYVLDVLNALKCENVRMMLTDSVSSVQIEDAASQSAAYVVMPMRL
>d2pola2 4.76.1.1.1 (123-244) DNA polymerase III, beta subunit [Escherichia coli]
QSEVEFTLPQATMKRLIEATQFSMAHQDVRYYLNGMLFETEGEELRTVATDGHRLAVCSMPIGQSLPSHSVIVPRKGVIELMRMLDGGDNPLRVQIGSNNIRAHVGDFIFTSKLVDGRFPDY
>d1plq_1 4.76.1.2.1 (1-126) Prolifirating cell nuclear antigen (PCNA) [yeast (Saccharomyces cerevisiae)]
MLEAKFEEASLFKRIIDGFKDCVQLVNFQCKEDGIIAQAVDDSRVLLVSLEIGVEAFQEYRCDHPVTLGMDLTSLSKILRCGNNTDTLTLIADNTPDSIILLFEDTKKDRIAEYSLKLMDIDADFL
>d1plq_2 4.76.1.2.1 (127-258) Prolifirating cell nuclear antigen (PCNA) [yeast (Saccharomyces cerevisiae)]
KIEELQYDSTLSLPSSEFSKIVRDLSQLSDSINIMITKETIKFVADGDIGSGSVIIKPFVDMEHPETSIKLEMDQPVDLTFGAKYLLDIIKGSSLSDRVGIRLSSEAPALFQFDLKSGFLQFFLAPKFNDEE
>d1alo_6 4.77.1.1.1 (558-735) Aldehyde oxidoreductase, molybdemum cofactor-binding domain [(Desulfovibrio gigas)]
DPLELRYKNAYRPGDTNPTGQEPEVFSLPDMIDQLRPKYQAALEKAQKESTATHKKGVGISIGVYGSGLDGPDASEAWAELNADGTITVHTAWEDHGQGADIGCVGTAHEALRPMGVAPEKIKFTWPNTATTPNSGPSGGSREQVMTGNAIRVACENLLKACEKPGGGYYTYDELKAA
>d1alo_7 4.77.1.1.1 (736-907) Aldehyde oxidoreductase, molybdemum cofactor-binding domain [(Desulfovibrio gigas)]
DKPTKITGNWTASGATHCDAVTGLGKPFVVYMYGVFMAEVTVDVATGQTTVDGMTLMADLGSLCNQLATDGQIYGGLAQGIGLALSEDFEDIKKHATLVGAGFPFIKQIPDKLDIVYVNHPRPDGPFGASGVGELPLTSPHAAIINAIKSATGVRIYRLPAYPEKVLEALKA
>d1alo_5 4.77.1.1.1 (443-557) Aldehyde oxidoreductase, molybdemum cofactor-binding domain [(Desulfovibrio gigas)]
PVHLRYNYQQQQQYTGKRSPWEMNVKFAAKKDGTLLAMESDWLVDHGPYSEFGDLLTLRGAQFIGAGYNIPNIRGLGRTVATNHVWGSAFRGYGAPQSMFASECLMDMLAEKLGM
>d1alo_4 4.77.1.1.1 (311-442) Aldehyde oxidoreductase, molybdemum cofactor-binding domain [(Desulfovibrio gigas)]
MSGPAAAAEDAIEIHPGTPNVYFEQPIVKGEDTGPIFASADVTVEGDFYVGRQPHMPIEPDVAFAYMGDDGKCYIHSKSIGVHLHLYMIAPGVGLEPDQLVLVANPMGGTFGYKFSPTSEALVAVAAMATGR
>d1geo_4 4.78.1.1.1 (314-458) Sulfite reductase hemoprotein (SiRHP), domains 2 and 4 [Escherichia coli]
PQRENSMACVSFPTCPLAMAEAERFLPSFIDNIDNLMAKHGVSDEHIVMRVTGCPNGCGRAMLAEVGLVGKAPGRYNLHLGGNRIGTRIPRMYKENITEPEILASLDELIGRWAKEREAGEGFGDFTVRAGIIRPVLDPARDLWD
>d1geo_3 4.78.1.1.1 (0-233) Sulfite reductase hemoprotein (SiRHP), domains 2 and 4 [Escherichia coli]
D
>d1hqi__ 4.79.1.1.1 Phenol hydroxylase P2 protein [Pseudomonas sp. CF600]
MSSLVYIAFQDNDNARYVVEAIIQDNPHAVVQHHPAMIRIEAEKRLEIRRETVEENLGRAWDVQEMLVDVITIGGNVDEDDDRFVLEWKN
>d1pmd_1 4.8.1.1.1 (545-617) Penicillin-binding protein 2x (pbp-2x), c-terminal domain [Streptococcus pneumoniae]
LQTTAKALEQVSQQSPYPMPSVKDISPGDLAEELRRNLVQPIVVGTGTKIKNSSAEEGKNLAPNQQVLILSDK
>d1pmd_2 4.8.1.1.1 (618-675) Penicillin-binding protein 2x (pbp-2x), c-terminal domain [Streptococcus pneumoniae]
AEEVPDMYGWTKETAETLAKWLNIELEFQGSGSTVQKQDVRANTAIKDIKKITLTLGD
>d1seia_ 4.80.1.1.1 Ribosomal protein S8 [Bacillus stearothermophilus]
VMTDPIADMLTAIRNANMVRHEKLEVPASKIKREIAEILKREGFIRDYEYIEDNKQGILRIFLKYGPNERVITGLKRISKPGLRVYVKAHEVPRVLNGLGIAILSTSQGVLTDKEARQKGTGGEIIAYVI
>d1div__ 4.82.1.1.1 Ribosomal protein L9 [Bacillus stearothermophilus]
MKVIFLKDVKGKGKKGEIKNVADGYANNFLFKQGLAIEATPANLKALEAQKQKEQRQAAEELANAKKLKEQLEKLTVTIPAKAGEGGRLFGSITSKQIAESLQAQHGLKLDKRKIELADAIRALGYTNVPVKLHPEVTATLKVHVTEQK
>d2glt_2 4.83.1.1.1 (123-296) Glutathione synthetase [Escherichia coli]
NEKLFTAWFSDLTPETLVTRNKAQLKAFWEKHSDIILKPLDASIFRVKEGDPNLGVIAETLTEHGTRYCMAQNYLPAIKDGDKRVLVVDGEPVPYCLARGEPRPLTESDWKIARQIGPTLKEKGLIFVGLDIIGDRLTEINVTSPTCIREIEAEFPVSITGMLMDAIEARLQQQ
>d2dln_2 4.83.1.1.2 (97-306) D-ala-D-ala ligase [Escherichia coli ddlB gene]
KLRSKLLWQGAGLPVAPWVALTRAEFEKGLSDKQLAEISALGLPVIVKPSREGSSVGMSKVVAENALQDALRLAFQHDEEVLIEKWLSGPEFTVAILGEEILPSIRIQPSGTFYDYEAKYLSDETQYFCPAGLEASQEANLQALVLKAWTTLGCKGWGRIDVMLDSDGQFYLLEANTSPGMTSHSLVPMAARQAGMSFSQLVVRILELAD
>d1bnca3 4.83.1.2.1 (115-317) Biotin carboxylase subunit of acetyl-CoA carboxylase [Escherichia coli]
DKVSAIAAMKKAGVPCVPGSDGPLGDDMDKNRAIAKRIGYPVIIKRGMRVVRGDAELAQSISMTRAEAKMVYMEKYLENPRHVEIQVLADGQGNAIYLAERDCSMQRRHQKVVEEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQPLSIKQEEVHV
>d1scub2 4.83.1.3.1 (1-244) Succinyl-CoA synthetase, beta-chain, N-terminal domain [Escherichia coli]
MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKRLVTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRRVVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQGRELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINPLVITKQGDLICLDGKLGADGNALFRQPDLREMRDQSQEDPREAQ
>d1dik_3 4.83.1.4.1 (1-375) Pyruvate phosphate dikinase, N-terminal domain [Escherichia coli]
AKWVYKFEEGNASMRNLLGGKGCNLAEMTILGMPIPQGFTVTTEACTEYYNSGKQITQEIQDQIFEAITWLEELNGKKFGDTEDPLLVSVRSAARASMPGMMDTILNLGLNDVAVEGFAKKTGNPRFAYDSYRRFIQMYSDVVMEVPKSHFEKIIDAMKEEKGVHFDTDLTADDLKELAEKFKAVYKEAMNGEEFPQEPKDQLMGAVKAVFRSWDNPRAIVYRRMNDIPGDWGTAVNVQTMVFGNKGETSGTGVAFTRNPSTGEKGIYGEYLINAQGEDVVAGVRTPQPITQLENDMPDCYKQFMDLAMKLEKHFRDMQDMEFTIEEGKLYFLQTRNGKRTAPAALQIACDLVDEGMITEEEAVVRIEAKSLDQL
>d1ckma2 4.83.2.2.1 (1-228) RNA guanylyltransferase (mRNA capping enzyme), N-terminal domain [Chlorella virus PBCV-1]
NITTERAVLTLNGLQIKLHKVVGESRDDIVAKMKDLAMDDHKFPRLPGPNPVSIERKDFEKLKQNKYVVSEKTDGIRFMMFFTRVFGFKVCTIIDRAMTVYLLPFKNIPRVLFQGSIFDGELCVDIVEKKFAFVLFDAVVVSGVTVSQMDLASRFFAMKRSLKEFKNVPEDPAILRYKEWIPLEHPTIIKDHLKKANAIYHTDGLIIMSVDEPVIYGRNFNLFKLKPG
>d1vaoa2 4.84.1.1.1 (1-263) Vanillyl-alcohol oxidase [Fungus (Penicillium simplicissimum)]
EFRPLTLPPKLSLSDFNEFIQDIIRIVGSENVEVISVDGSYMKPTHTHDPHHVMDQDYFLASAIVAPRNVADVQSIVGLANKFSFPLWPISIGRNSGYGGAAPRVSGSVVLDMGKNMNRVLEVNVEGAYCVVEPGVTYHDLHNYLEANNLRDKLWLDVPDLGGGSVLGNAVERGVGYTPYGDHWMMHSGMEVVLANGELLRTGMGALPDPKRPETMGLKPEDQPWSKIAHLFPYGFGPYIDGLFSQSNMGIVTKIGIWLMPNP
>d1mbb_1 4.84.1.2.1 (1-198) Uridine diphospho-N-Acetylenolpyruvylglucosamine reductase (MurB), N-terminal domain [Escherichia coli]
HSLKPWNTFGIDHNAQHIVCAEDEQQLLNAWQYATAEGQPVLILGEGSNVLFLEDYRGTVIINRIKGIEIHDEPDAWYLHVGAGENWHRLVKYTLQEGMPGLENLALIPGCVGSSPIQNIGAYGVELQRVCAYVDSVELATGKQVRLTAKECRFGYRDSIFKHEYQDRFAIVAVGLRLPKEWQPVLTYGDLTRLDPTT
>d1mbb_2 4.85.1.1.1 (199-340) Uridine diphospho-N-Acetylenolpyruvylglucosamine reductase, MurB, C-terminal domain [Escherichia coli]
VTPQQVFNAVCHMRTTKLPDPKVNGNAGSFFKNPVVSAETAKALLSQFPTAPNYPQADGSVKLAAGWLIDQCQLKGMQIGGAAVHRQQALVLINEDNAKSEDVVQLAHHVRQKVGEKFNVWLEPEVRFIGASGEVSAVETIS
>d1ako__ 4.86.1.1.1 DNA-repair enzyme exonuclease III [Escherichia coli]
MKFVSFNINGLRARPHQLEAIVEKHQPDVIGLQETKVHDDMFPLEEVAKLGYNVFYHGQKGHYGVALLTKETPIAVRRGFPGDDEEAQRRIIMAEIPSLLGNVTVINGYFPQGESRDHPIKFPAKAQFYQNLQNYLETELKRDNPVLIMGDMNISPTDLDIGIGEENRKRWLRTGKCSFLPEEREWMDRLMSWGLVDTFRHANPQTADRFSWFDYRSKGFDDNRGLRIDLLLASQPLAECCVETGIDYEIRSMEKPSDHAPVWATFRR
>d2dnja_ 4.86.1.1.2 Deoxyribonuclease I [bovine (Bos taurus)]
LKIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNQDDPNTYHYVVSEPLGRNSYKERYLFLFRPNKVSVLDTYQYDDDSFSREPAVVKFSSHSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKWHLNDVMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTTATSTNCAYDRIVVAGSLLQSSVVPGSAAPFDFQAAYGLSNEMALAISDHYPVEVTLT
>d1aora2 4.87.1.1.1 (1-210) Aldehyde ferredoxin oxidoreductase, N-terminal domains [Pyrococcus furiosis]
MYGNWGRFIRVNLSTGDIKVEEYDEELAKKWLGSRGLAIYLLLKEMDPTVDPLSPENKLIIAAGPLTGTSAPTGGRYNVVTKSPLTGFITMANSGGYFGAELKFAGYDAIVVEGKAEKPVYIYIKDEHIEIRDASHIWGKKVSETEATIRKEVGSEKVKIASIGPAGENLVKFAAIMNDGHRAAGRGGVGAVMGSKNLKAIAVEGSKTVP
>d1gdoa_ 4.88.1.1.1 Glucosamine 6-phosphate synthase, N-terminal domain [Escherichia coli]
CGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDAEGHMTRLRRLGKVQMLAQAAEEHPLHGGTGIAHTRWATHGEPSEVNAHPHVSEHIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAVLRAIPQLRGAYGTVIMDSRHPDTLLAARSGSPLVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEITRRSVNIFDKTGAEVKRQDIESNL
>d1gph12 4.88.1.1.2 (1-234) Glutamine PRPP amidotransferase, N-terminal domain [Bacillus subtilis]
CGVFGIWGHEEAPQITYYGLHSLQHRGQEGAGIVATDGEKLTAHKGQGLITEVFQNGELSKVKGKGAIGHVRYATAGGGGYENVQPLLFRSQNNGSLALAHNGNLVNATQLKQQLENQGSIFQTSSDTEVLAHLIKRSGHFTLKDQIKNSLSMLKGAYAFLIMTETEMIVALDPNGLRPLSIGMMGDAYVVASETCAFDVVGATYLREVEPGEMLIINDEGMKSERFSMNINRS
>d1ecfa2 4.88.1.1.3 (1-249) Glutamine PRPP amidotransferase, N-terminal domain [Escherichia coli]
CGIVGIAGVMPVNQSIYDALTVLQHRGQDAAGIITIDANNCFRLRKANGLVSDVFEARHMQRLQGNMGIGHVRYPTAGSSSASEAQPFYVNSPYGITLAHNGNLTNAHELRKKLFEEKRRHINTTSDSEILLNIFASELDNFRHYPLEADNIFAAIAATNRLIRGAYACVAMIIGHGMVAFRDPNGIRPLVLGKRDIDENRTEYMVASESVALDTLGFDFLRDVAPGEAIYITEEGQLFTRQCADNPVS
>d1pnk.1 4.88.1.2.1 (a,b) Penicillin acylase, catalytic domain [Escherichia coli]
SSSEIKIVRDEYGMPHIYANDTWHLFYGYGYVVAQDRLFQMEMARRSTQGTVAEVLGKDFVKFDKDIRRNYWPDAIRAQIAALSPEDMSILQGYADGMNAWIDKVNTNPETLLPKQFNTFGFTPKRWEPFDVAMIFVGTMANRFSDSTSEIDNLALLTALKDKYGVSQGMAVFNQLKWLVNPSAPTTIAVQESNTPFAYPGLVFGHNGVISWGSTAGFGDDVDIFAERLSAEKPGYYLHNGKWVKMLSREETITVKNGQAETFTVWRTVHGNILQTDQTTQTAYAKSRAWDGKEVASLLAWTHQMKAKNWQEWTQQAAKQALTINWYYADVNGNIGYVHTGAYPDRQSGHDPRLPVPGTGKWDWKGLLPFEMNPKVYNPQSGYIANWNNSPQKDYPASDLFAFLWGGADRVTEIDRLLEQKPRLTADQAWDVIRQTSRQDLNLRLFLPTLQAATSGLTQSDPRRQLVETLTRWDGINLLNDDGKTWQQPGSAILNVWLTSMLKRTVVAAVPMPFDKWYSASGYETTQDGPTGSLNISVGAKILYEAVQGDKSPIPQAVDLFAGKPQQEVVLAALEDTWETLSKRYGNNVSNWKTPAMALTFRANNFFGVPQAAAEETRHQAEYQNRGTENDMIVFSPTTSDRPVLAWDVVAPGQSGFIAPDGTVDKHYEDQLKMYENFGRKSLWLTKQDVEAHKESQEVLHVQRSSSEIKIVRDEYGMPHIYANDTWHLFYGYGYVVAQDRLFQMEMARRSTQGTVAEVLGKDFVKFDKDIRRNYWPDAIRAQIAALSPEDMSILQGYADGMNAWIDKVNTNPETLLPKQFNTFGFTPKRWEPFDVAMIFVGTMANRFSDSTSEIDNLALLTALKDKYGVSQGMAVFNQLKWLVNPSAPTTIAVQESNTPFAYPGLVFGHNGVISWGSTAGFGDDVDIFAERLSAEKPGYYLHNGKWVKMLSREETITVKNGQAETFTVWRTVHGNILQTDQTTQTAYAKSRAWDGKEVASLLAWTHQMKAKNWQEWTQQAAKQALTINWYYADVNGNIGYVHTGAYPDRQSGHDPRLPVPGTGKWDWKGLLPFEMNPKVYNPQSGYIANWNNSPQKDYPASDLFAFLWGGADRVTEIDRLLEQKPRLTADQAWDVIRQTSRQDLNLRLFLPTLQAATSGLTQSDPRRQLVETLTRWDGINLLNDDGKTWQQPGSAILNVWLTSMLKRTVVAAVPMPFDKWYSASGYETTQDGPTGSLNISVGAKILYEAVQGDKSPIPQAVDLFAGKPQQEVVLAALEDTWETLSKRYGNNVSNWKTPAMALTFRANNFFGVPQAAAEETRHQAEYQNRGTENDMIVFSPTTSDRPVLAWDVVAPGQSGFIAPDGTVDKHYEDQLKMYENFGRKSLWLTKQDVEAHKESQEVLHVQR
>d1pmab_ 4.88.1.3.1 Proteasome beta subunit (catalytic) [Thermoplasma acidophilum]
TTTVGITLKDAVIMATERRVTMENFIMHKNGKKLFQIDTYTGMTIAGLVGDAQVLVRYMKAELELYRLQRRVNMPIEAVATLLSNMLNQVKYMPYMVQLLVGGIDTAPHVFSIDAAGGSVEDIYASTGSGSPFVYGVLESQYSEKMTVDEGVDLVIRAISAAKQRDSASGGMIDVAVITRKDGYVQLPTDQIESRIRKLGLIL
>d1pmaa_ 4.88.1.3.2 Proteasome alpha subunit (non-catalytic) [Thermoplasma acidophilum]
TVFSPDGRLFQVEYAREAVKKGSTALGMKFANGVLLISDKKVRSRLIEQNSIEKIQLIDDYVAAVTSGLVADARVLVDFARISAQQEKVTYGSLVNIENLVKRVADQMQQYTQYGGVRPYGVSLIFAGIDQIGPRLFDCDPAGTINEYKATAIGSGKDAVVSFLEREYKENLPEKEAVTLGIKALKSSLEEGEELKAPEIASITVGNKYRIYDQEEVKKFL
>d1apy.1 4.88.1.4.1 (a,b) lysosomal aspartylglucosaminidase, AGA [Human (Homo sapiens)]
SPLPLVVNTWPFKNATEAAWRALASGGSALDAVESGCAMCEREQCDGSVGFGGSPDELGETTLDAMIMDGTTMDVGAVGDLRRIKNAIGVARKVLEHTTHTLLVGESATTFAQSMGFINEDLSTSASQALHSDWLARNCQPNYWRNVIPDPSKYCGPYKPPTNGIKFKIHGRVGDSPIPGAGAYADDTAGAAAATGNGDILMRFLPSYQAVEYMRRGEDPTIACQKVISRIQKHFPEFFGAVICANVTGSYGAACNKLSTFTQFSFMVYNSEKNQPTEEKVDCISPLPLVVNTWPFKNATEAAWRALASGGSALDAVESGCAMCEREQCDGSVGFGGSPDELGETTLDAMIMDGTTMDVGAVGDLRRIKNAIGVARKVLEHTTHTLLVGESATTFAQSMGFINEDLSTSASQALHSDWLARNCQPNYWRNVIPDPSKYCGPYKPPTNGIKFKIHGRVGDSPIPGAGAYADDTAGAAAATGNGDILMRFLPSYQAVEYMRRGEDPTIACQKVISRIQKHFPEFFGAVICANVTGSYGAACNKLSTFTQFSFMVYNSEKNQPTEEKVDCI
>d1pya.1 4.89.1.1.1 (a,b) Histidine decarboxylase [Lactobacillus sp., strain 30a]
SELDAKLNKLGVDRIAISPYKQWTRGYMEPGNIGNGYVTGLKVDAGVRDKSDDDVLDGIVSYDRAETKNAYIGQINMTTASYDAKPLQDALVEYFGTEQDRRHYPAPGSFIVCANKGVTAERPKNDADMKPGQGYGVWSAIAISFAKDPTKDSSMFVEDAGVWETPNEDELLEYLEGRRKAMAKSIAECGQDAHASFESSWIGFAYTMMEPGQIGNAITVAPYVSLPIDSIPGGSILTPDKDMEIMENLTMPEWLEKMGYKSLSANNALKYSELDAKLNKLGVDRIAISPYKQWTRGYMEPGNIGNGYVTGLKVDAGVRDKSDDDVLDGIVSYDRAETKNAYIGQINMTTASYDAKPLQDALVEYFGTEQDRRHYPAPGSFIVCANKGVTAERPKNDADMKPGQGYGVWSAIAISFAKDPTKDSSMFVEDAGVWETPNEDELLEYLEGRRKAMAKSIAECGQDAHASFESSWIGFAYTMMEPGQIGNAITVAPYVSLPIDSIPGGSILTPDKDMEIMENLTMPEWLEKMGYKSLSANNALKY
>d1sso__ 4.9.1.1.1 DNA-binding protein [Sulfolobus solfataricus]
ATVKFKYKGEEKQVDISKIKKVWRVGKMISFTYDEGGGKTGRGAVSEKDAPKELLQMLEKQK
>d1sap__ 4.9.1.1.2 DNA-binding protein [Sulfolobus acidocaldarius]
MVKVKFKYKGEEKEVDTSKIKKVWRVGKMVSFTYDDNGKTGRGAVSEKDAPKELLDMLARAEREKK
>d1bme__ 4.90.1.1.1 Zn metallo-beta-lactamase [Bacillus cereus]
TVIKNETGTISISQLNKNVWVHTELGSFNGEAVPSNGLVLNTSKGLVLVDSSWDDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGIKTLKERGIKAHSTALTAELAKKNGYEEPLGDLQTVTNLKFGNMKVETFYPGKGHTEDNIVVWLPQYNILVGGCLVKSTSAKDLGNVADAYVNEWSTSIENVLKRYRNINAVVPGHGEVGDKGLLLHTLDLLK
>d1znba_ 4.90.1.1.2 Zn metallo-beta-lactamase [(Bacteroides fragilis)]
KSVKISDDISITQLSDKVYTYVSLAEIEGMVPSNGMIVINNHQAALLDTPINDAQTETLVNWVADSLHAKVTTFIPNHWHGDCIGGLGYLQKKGVQSYANQMTIDLAKEKGLPVPEHGFTDSLTVSLDGMPLQCYYLGGGHATDNIVVWLPTENILFGGCMLKDNQATSIGNISDADVTAWPKTLDKVKAKFPSARYVVPGHGDYGGTELIEHTKQIVNQYIESTSKP
>d4kbpa2 4.91.1.1.1 (113-424) Purple acid phosphatase, catalytic domain [Kidney bean (Phaseolus vulgaris)]
QTGLDVPYTFGLIGDLGQSFDSNTTLSHYELSPKKGQTVLFVGDLSYADRYPNHDNVRWDTWGRFTERSVAYQPWIWTAGNHEIEFAPEINETEPFKPFSYRYHVPYEASQSTSPFWYSIKRASAHIIVLSSYSAYGRGTPQYTWLKKELRKVKRSETPWLIVLMHSPLYNSYNHHFMEGEAMRTKFEAWFVKYKVDVVFAGHVHAYERSERVSNIAYKITDGLCTPVKDQSAPVYITIGDAGNYGVIDSNMIQPQPEYSAFREASFGHGMFDIKNRTHAHFSWNRNQDGVAVEADSVWFFNRHWYPVDDST
>d1fjma_ 4.91.1.2.1 Protein phosphatase-1 (PP-1) [Rabbit (Oryctolagus cuniculus)]
LNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAD
>d1tcoa_ 4.91.1.2.2 Protein phosphatase-2B (PP-2B, calcineurin A subunit) [Bovine (Bos taurus)]
VPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKEGRLEETVALRIITEGASILRQEKNLLDIDAPVTVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMDAFDCLPLAALMNQQFLCVHGGLSPEINTLDDIRKLDRFKEPPAYGPMCDILWSDPLEDFGNEKTQEHFTHNTVRGCSYFYSYPAVCEFLQHNNLLSILRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLNIC
>d1mlda2 4.92.1.1.1 (145-313) Malate dehydrogenase [porcine (Sus scrofa)]
VTTLDIVRANAFVAELKGLDPARVSVPVIGGHAGKTIIPLISQCTPKVDFPQDQLSTLTGRIQEAGTEVVKAKAGAGSATLSMAYAGARFVFSLVDAMNGKEGVVECSFVKSQETDCPYFSTPLLLGKKGIEKNLGIGKISPFEEKMIAEAIPELKASIKKGEEFVKNM
>d4mdha2 4.92.1.1.1 (155-333) Malate dehydrogenase [porcine (Sus scrofa)]
TRLDHNRAKAQIALKLGVTSDDVKNVIIWGNHSSTQYPDVNHAKVKLQAKEVGVYEAVKDDSWLKGEFITTVQQRGAAVIKARKLSSAMSAAKAICDHVRDIWFGTPEGEFVSMGIISDGNSYGVPDDLLYSFPVTIKDKTWKIVEGLPINDFSREKMDLTAKELAEEKETAFEFLSSA
>d1ldna2 4.92.1.1.10 (149-316) Lactate dehydrogenase [Bacillus stearothermophilus]
TILDTARFRFLLGEYFSVAPQNVHAYIIGEHGDTELPVWSQAYIGVMPIRKLVESKGEEAQKDLERIFVNVRDAAYQIIEKKGATYYGIAMGLARVTRAILHNENAILTVSAYLDGLYGERDVYIGVPAVINRNGIREVIEIELNDDEKNRFHHSAATLKSVLARAFT
>d1ldb_2 4.92.1.1.10 (139-294) Lactate dehydrogenase [Bacillus stearothermophilus]
TILDTARFRFLLGEYFSVAPQNVHAYIIGEHGDTELPVWSQAYIGVMPIDLERIFVNVRDAAYQIIEKKGATYYGIAMGLARVTRAILHNENAILTVSAYLDGLYGERDVYIGVPAVINRNGIREVIEIELNDDEKNRFHHSAATLKSVLARAFTR
>d1llc_2 4.92.1.1.11 (150-320) Lactate dehydrogenase [Lactobacillus casei]
TSLDTARFRQSIAEMVNVDARSVHAYIMGEHGDTEFPVWSHANIGGVTIAEWVKAHPEIKEDKLVKMFEDVRDAAYEIIKLKGATFYGIATALARISKAILNDENAVLPLSVYMDGQYGINDLYIGTPAVINRNGIQNILEIPLTDHEEESMQKSASQLKKVLTDAFAKND
>d1llda2 4.92.1.1.12 (144-313) Lactate dehydrogenase [Bifidobacterium longum, strain am101-2]
TNLDSARLRFLIAQQTGVNVKNVHAYIAGEHGDSEVPLWESATIGGVPMSDWTPLPGHDPLDADKREEIHQEVKNAAYKIINGKGATNYAIGMSGVDIIEAVLHDTNRILPVSSMLKDFHGISDICMSVPTLLNRQGVNNTINTPVSDKELAALKRSAETLKETAAQFGF
>d2cmd_2 4.92.1.1.2 (146-312) Malate dehydrogenase [Escherichia coli]
VTTLDIIRSNTFVAELKGKQPGEVEVPVIGGHSGVTILPLLSQVPGVSFTEQEVADLTKRIQNAGTEVVEAKAGGGSATLSMGQAAARFGLSLVRALQGEQGVVECAYVEGDGQYARFFSQPLLLGKNGVEERKSIGTLSAFEQNALEGMLDTLKKDIALGQEFVNK
>d1bdma2 4.92.1.1.3 (146-317) Malate dehydrogenase [Thermus flavus]
TRLDHNRAKAQLAKKTGTGVDRIRRMTVWGNHSSIMFPDLFHAEVDGRPALELVDMEWYEKVFIPTVAQRGAAIIQARGASSAASAANAAIEHIRDWALGTPEGDWVSMAVPSQGEYGIPEGIVYSFPVTAKDGAYRVVEGLEINEFARKRMEITAQELLDEMEQVKALGLI
>d1hlpa2 4.92.1.1.4 (129-303) Malate dehydrogenase [Haloarcula marismortui]
LYEAGDRSREQVIGFGGRLDSARFRYVLSEEFDAPVQNVEGTILGEHGDAQVPVFSKVRVDGTDPEFSGDEKEQLLGDLQESAMDVIERKGATEWGPARGVAHMVEAILHDTGEVLPASVKLEGEFGHEDTAFGVPVRLGSNGVEEIVEWDLDDYEQDLMADAAEKLSDQYDKIS
>d1hyha2 4.92.1.1.5 (140-297) L-2-hydroxyisocapronate dehydrogenase, L-HICDH [Lactobacillus confusus]
GTLLDTARMQRAVGEAFDLDPRSVSGYNLGEHGNSQFVAWSTVRVMGQPIVTLIDLAAIEEEARKGGFTVLNGKGYTSYGVATSAIRIAKAVMADAHAELVVSNRRDDMGMYLSYPAIIGRDGVLAETTLDLTTDEQEKLLQSRDYIQQRFDEIVDTL
>d5ldh_2 4.92.1.1.6 (161-333) Lactate dehydrogenase [porcine (Sus scrofa)]
SGCNLDSARFRYLMGEKLGVHPSSCHGWILGEHGDSSVAVWSGVNVAGVVLQQLNPEMGTDNDSENWKEVHKMVVESAYEVIKLKGYTNWAIGLSVADLIESMLKNLSRIHPVSTMVQGMYGIENEVFLSLPCVLNARGLTSVINQKLKDDEVAQLKNSADTLWGIQKDLKDL
>d9ldta2 4.92.1.1.6 (160-331) Lactate dehydrogenase [porcine (Sus scrofa)]
SGCNLDSARFRYLMGERLGVHPLSCHGWILGEHGDSSVPVWSGVNVAGVSLKNLHPELGTDADKEHWKAVHKEVVDSAYEVIKLKGYTSWAIGLSVADLAESIMKNLRRVHPISTMIKGLYGIKENVFLSVPCILGQNGISDVVKVTLTPEEEAHLKKSADTLWGIQKELQF
>d2ldx_2 4.92.1.1.7 (160-331) Lactate dehydrogenase [mouse (Mus musculus)]
SGCNLDSARFRYLIGEKLGVNPTSCHGWVLGEHGDSSVPIWSGVNVAGVTLKSLNPAIGTDKNKQHWKNVHKQVVEGGYEVLDMKGYTSWAIGLSVTDLARSILKNLKRVHPVTTLVKGFHGIKEEVFLSIPCVLGESGITDFVKVNMTAEEEGLLKKSADTLWNMQKNLEL
>d1ldm_2 4.92.1.1.8 (161-329) Lactate dehydrogenase [dogfish (Squalus acanthias)]
SGCNLDSARFRYLMGERLGVHSCSCHGWVIGEHGDSVPSVWSGMNVASIKLHPLDGTNKDKQDWKKLHKDVVDSAYEVIKLKGYTSWAIGLSVADLAETIMKNLCRVHPVSTMVKDFYGIKDNVFLSLPCVLNDHGISNIVKMKLKPNEEQQLQKSATTLWDIQKDLKF
>d1ldg_2 4.92.1.1.9 (150-315) Lactate dehydrogenase [malarial parasite (Plasmodium falciparum)]
GGVLDTSRLKYYISQKLNVCPRDVNAHIVGAHGNKMVLLKRYITVGGIPLQEFINNKLISDAELEAIFDRTVNTALEIVNLHASPYVAPAAAIIEMAESYLKDLKKVLICSTLLEGQYGHSDIFGGTPVVLGANGVEQVIELQLNSEEKAKFDEAIAETKRMKALA
>d1aiha_ 4.93.1.1.1 Integrase [Bacteriophage HP1]
ETELAFLYERDIYRLLAECDNSRNPDLGLIVRICLATGARWSEAETLTQSQVMPYKITFTNTKSKKNRTVPISDELFDMLPKKRGRLFNDAYESFENAVLRAEIELPKGQLTHVLRHTFASHFMMNGGNILVLKEILGHSTIEMTMRYAHFAPSHLESAVKFNPLSNPAQ
>d1mrj__ 4.94.1.1.1 alpha-Trichosanthin [Mongolian snake gourd (Trichosanthes Kirillowii maxim)]
DVSFRLSGATSSSYGVFISNLRKALPNERKLYDIPLLRSSLPGSQRYALIHLTNYADETISVAIDVTNVYIMGYRAGDTSYFFNEASATEAAKYVFKDAMRKVTLPYSGNYERLQTAAGKIRENIPLGLPALDSAITTLFYYNANSAASALMVLIQSTSEAARYKFIEQQIGKRVDKTFLPSLAIISLENSWSALSKQIQIASTNNGQFESPVVLINAQNQRVTITNVDAGVVTSNIALLLNRNNMA
>d1mrg__ 4.94.1.1.2 alpha-Momorcharin (momordin) [bitter melon (Momordica charantia)]
DVSFRLSGADPRSYGMFIKDLRNALPFREKVYNIPLLLPSVSGAGRYLLMHLFNRDGKTITVAVDVTNIYIMGYLADTTSYFFNEPAAELASQYVFRDARRKITLPYSGDYERLQIAAGKPREKIPIGLPALDSAISTLLHYDSTAAAGALLVLIQTTAEAARFKYIEQQIQERAYRDEVPSLATISLENSWSGLSKQIQLAQGNNGIFRTPIVLVDNKGNRVQITNVTSKVVTSNIQLLLNTRNI
>d1abra_ 4.94.1.1.3 Abrin A-chain [Abrus precatorius]
EDRPIKFSTEGATSQSYKQFIEALRERLRGGLIHDIPVLPDPTTLQERNRYITVELSNSDTESIEVGIDVTNAYVVAYRAGTQSYFLRDAPSSASDYLFTGTDQHSLPFYGTYGDLERWAHQSRQQIPLGLQALTHGISFFRSGGNDNEEKARTLIVIIQMVAEAARFRYISNRVRVSIQTGTAFQPDAAMISLENNWDNLSRGVQESVQDTFPNQVTLTNIRNEPVIVDSLSHPTVAVLALMLFVCNPPN
>d1apa__ 4.94.1.1.4 Pokeweed antiviral protein alpha [pokeweed (Phytolacca americana)]
INTITFDVGNATINKYATFMKSIHNQAKDPTLKCYGIPMLPNTNLTPKYLLVTLQDSSLKTITLMLKRNNLYVMGYADTYNGKCRYHIFKDISNTTERNDVMTTLCPNPSSRVGKNINYDSSYPALEKKVGRPRSQVQLGIQILNSGIGKIYGVDSFTEKTEAEFLLVAIQMVSEAARFKYIENQVKTNFNRAFYPNAKVLNLEESWGKISTAIHNAKNGALTSPLELKNANGSKWIVLRVDDIEPDVGLLKYVNGTCQAT
>d1paga_ 4.94.1.1.4 Pokeweed antiviral protein alpha [pokeweed (Phytolacca americana)]
VNTIIYNVGSTTISKYATFLNDLRNEAKDPSLKCYGIPMLPNTNTNPKYVLVELQGSNKKTITLMLRRNNLYVMGYSDPFETNKCRYHIFNDISGTERQDVETTLCPNANSRVSKNINFDSRYPTLESKAGVKSRSQVQLGIQILDSNIGKISGVMSFTEKTEAEFLLVAIQMVSEAARFKYIENQVKTNFNRAFNPNPKVLNLQETWGKISTAIHDAKNGVLPKPLELVDASGAKWIVLRVDEIKPDVALLNYVGGSCQTT
>d1rtc__ 4.94.1.1.5 Ricin A-chain [castor bean (Ricinus communis)]
MIFPKQYPIINFTTAGATVQSYTNFIRAVRGRLTTGADVRHEIPVLPNRVGLPINQRFILVELSNHAELSVTLALDVTNAYVVGYRAGNSAYFFHPDNQEDAEAITHLFTDVQNRYTFAFGGNYDRLEQLAGNLRENIELGNGPLEEAISALYYYSTGGTQLPTLARSFIICIQMISEAARFQYIEGEMRTRIRYNRRSAPDPSVITLENSWGRLSTAIQESNQGAFASPIQLQRRNGSKFSVYDVSILIPIIALMVYRCAPPPSSQF
>d1lts.1 4.95.1.1.1 (a,c) Heat-labile toxin, A-chain [(Escherichia coli) type IB]
RLYRADSRPPDEIKRSGGLMPRGHNEYFDRGTQMNINLYDHARGTQTGFVRYDDGYVSTSLSLRSAHLAGQSILSGYSTYYIYVIATAPNMFNVNDVLGVYSPHPYEQEVSALGGIPYSQIYGWYRVNFGVIDERLHRNREYRDRYYRNLNIAPAEDGYRLAGFPPDHQAWREEPWIHHAPQGCGRLYRADSRPPDEIKRSGGLMPRGHNEYFDRGTQMNINLYDHARGTQTGFVRYDDGYVSTSLSLRSAHLAGQSILSGYSTYYIYVIATAPNMFNVNDVLGVYSPHPYEQEVSALGGIPYSQIYGWYRVNFGVIDERLHRNREYRDRYYRNLNIAPAEDGYRLAGFPPDHQAWREEPWIHHAPQGCG
>d1tii.1 4.95.1.1.2 (a,c) Heat-labile toxin, A-chain [(Escherichia coli) type IIB]
NDYFRADSRTPDEVRRSGGLIPRGQDEAYERGTPININLYDHARGTTGNTRYNDGYVSTTTTLRQAHLLGQNMLGGYNEYYIYVVAAAPNLFDVNGVLGRYSPYPSENEYAALGGIPLSQIIGWYRVSFGAIEGGMHRNRDYRRDLFRGLSAAPNEDGYRIAGFPDGFPAWEEVPWREFAPNSCLPNDYFRADSRTPDEVRRSGGLIPRGQDEAYERGTPININLYDHARGTTGNTRYNDGYVSTTTTLRQAHLLGQNMLGGYNEYYIYVVAAAPNLFDVNGVLGRYSPYPSENEYAALGGIPLSQIIGWYRVSFGAIEGGMHRNRDYRRDLFRGLSAAPNEDGYRIAGFPDGFPAWEEVPWREFAPNSCLP
>d1ddt_2 4.95.1.1.3 (1-187) Diphtheria toxin, N-terminal domain [Corynebacterium diphtheriae]
GADDVVDSSKSFVMENFSSYHGTKPGYVDSIQKGIQKPKSGTQGNYDDDWKGFYSTDNKYDAAGYSVDNENPLSGKAGGVVKVTYPGLTKVLALKVDNAETIKKELGLSLTEPLMEQVGTEEFIKRFGDGASRVVLSLPFAEGSSSVEYINNWEQAKALSVELEINFETRGKRGQDAMYEYMAQACA
>d1dmaa_ 4.95.1.1.4 Exotoxin A, C-terminal domain [Pseudomonas aeruginosa]
FLGDGGDVSFSTRGTQNWTVERLLQAHRQLEERGYVFVGYHGTFLEAAQSIVFGGVRAAIWRGFYIAGDPALAYGYAQDQEPDARGRIRNGALLRVYVPRSSLPGFYRTSLTLAAPEAAGEVERLIGHPLPLRLDAITGPEEEGGRLETILGWPLAERTVVIPSAIPTDPRNVGGDLDPSSIPDKEQAISALPDYASQPGKPPR
>d1prta_ 4.95.1.1.5 Pertussis toxin, S1 subunit [Bordetella pertussis]
DPPATVYRYDSRPPEDVFQNGFTAWGNNDNVLEHLTGRSCQVGSSNSAFVSTSSSRRYTEVYLEHRMQEAVEAERAGRGTGHFIGYIYEVRADNNFYGAASSYFEYVDTYGDNAGRILAGALATYQSEYLAHRRIPPENIRRVTRVYHNGITGETTTTEYSNARYVSQQTRANPNPYTSRRSVASIVGTLVRMAPVVGACMARQAESSEEAMVLVYYESIAYSF
>d1xtc.1 4.95.1.1.6 (a,c) Cholera toxin [Vibrio cholerae]
NDDKLYRADSRPPDEIKQSGGLMPRGQSEYFDRGTQMNINLYDHARGTQTGFVRHDDGYVSTSISLRSAHLVGQTILSGHSTYYLYVLATAPNMFNVNDVLGAYSPHPDEQEVSALGGIPYSQIYGWYRVHFGVLDEQLHRNRGYRDRYYSNLDIAPAADGYGLAGFPPEHRAWREEPWIHHAPPGCGNAPRNDDKLYRADSRPPDEIKQSGGLMPRGQSEYFDRGTQMNINLYDHARGTQTGFVRHDDGYVSTSISLRSAHLVGQTILSGHSTYYLYVLATAPNMFNVNDVLGAYSPHPDEQEVSALGGIPYSQIYGWYRVHFGVLDEQLHRNRGYRDRYYSNLDIAPAADGYGLAGFPPEHRAWREEPWIHHAPPGCGNAPR
>d1pax_2 4.95.1.2.1 (136-350) Poly(ADP-ribose) polymerase, C-terminal domain [Chicken (Gallus gallus)]
LRTDIKVVDKDSEEAKIIKQYVKNTHAATHNAYDLKVVEIFRIEREGESQRYKPFKQLHNRQLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQADPIGLILLGEVALGNMYELKNASHITKLPKGKHSVKGLGKTAPDPTATTTLDGVEVPLGNGISTGINDTCLLYNEYIVYDVAQVNLKYLLKLKFNYKT
>d1def__ 4.96.1.1.1 Peptide deformylase catalytic core [Escherichia coli]
SVLQVLHIPDERLRKVAKPVEEVNAEIQRIVDDMFETMYAEEGIGLAATQVDIHQRIIVIDVSENRDERLVLINPELLEKSGETGIEEGCLSIPEQRALVPRAEKVKIRALDRDGKPFELEADGLLAICIQHEMDHLVGKLFMDYLS
>d1lit__ 4.97.1.1.1 Lithostathine, inhibitor of stone formation [human (Homo sapiens)]
CPEGTNAYRSYCYYFNEDRETWVDADLYCQNMNSGNLVSVLTQAEGAFVASLIKESGTDDFNVWIGLHDPKKNRRWHWSSGSLVSYKSWGIGAPSSVNPGYCVSLTSSTGFQKWKDVPCEDKFSFVCKFKN
>d1esl_1 4.97.1.1.2 (1-118) E-selectin [human (Homo sapiens)]
WSYNTSTEAMTYDEASAYCQQRYTHLVAIQNKEEIEYLNSILSYSPSYYWIGIRKVNNVWVWVGTQKPLTEEAKNWAPGEPNNRQKDEDCVEIYIKREKDVGMWNDERCSKKKLALCY
>d1hup_2 4.97.1.1.3 (25-141) Mannose-binding protein A, lectin domain [human (Homo sapiens)]
KQVGNKFFLTNGEIMTFEKVKALCVKFQASVATPRNAAENGAIQNLIKEEAFLGITDEKTEGQFVDLTGNRLTYTNWNEGEPNNAGSDEDCVLLLKNGQWNDVPCSTSHLAVCEFPI
>d1rtm12 4.97.1.1.4 (33-149) Mannose-binding protein A, lectin domain [rat (Rattus rattus)]
KKSGKKFFVTNHERMPFSKVKALCSELRGTVAIPRNAEENKAIQEVAKTSAFLGITDEVTEGQFMYVTGGRLTYSNWKKDEPNDHGSGEDCVTIVDNGLWNDISCQASHTAVCEFPA
>d1rdl1_ 4.97.1.1.4 Mannose-binding protein A, lectin domain [rat (Rattus rattus)]
KYFMSSVRRMPLNRAKALCSELQGTVATPRNAEENRAIQNVAKDVAFLGITDQRTENVFEDLTGNRVRYTNWNEGEPNNVGSGENCVVLLTNGKWNDVPCSDSFLVVCEFS
>d1prtb2 4.97.1.2.1 (1-84) Pertussis toxin, S2/S3 subunits, N-terminal domain [Bordetella pertussis]
GIVIPPQEQITQHGSPYGRCANKTRALTVAELRGSGDLQEYLRHVTRGWSIFALYDGTYLGGEYGGVIKDGTPGGAFDLKTTFC
>d1prtc2 4.97.1.2.1 (1-84) Pertussis toxin, S2/S3 subunits, N-terminal domain [Bordetella pertussis]
GIVIPPKALFTQQGGAYGRCPNGTRALTVAELRGNAELQTYLRQITPGWSIYGLYDGTYLGQAYGGIIKDAPPGAGFIYRETFC
>d1prea1 4.97.1.2.2 (1-83) Proaerolysin, N-terminal domain [Aeromonas hydrophila]
EPVYPDQLRLFSLGQGVCGDKYRPVNREEAQSVKSNIVGMMGQWQISGLANGWVIMGPGYNGEIKPGTASNTWCYPTNPVTGE
>d1tsg__ 4.97.1.3.1 TSG-6, Link module [Human (Homo sapiens)]
GVYHREARSGKYKLTYAEAKAVCEFEGGHLATYKQLEAARKIGFHVCAAGWMAKGRVGYPIVKPGPNCGFGKTGIIDYGIRLNRSERWDAYCYNPHAK
>d3fib__ 4.98.1.1.1 gamma-Fibrinogen C-terminal fragment (residues 143-411) [human (Homo sapiens)]
QIHDITGKDCQDIANKGAKQSGLYFIKPLKANQQFLVYCEIDGSGNGWTVFQKRLDGSVDFKKNWIQYKEGFGHLSPTGTTEFWLGNEKIHLISTQSAIPYALRVELEDWNGRTSTADYAMFKVGPEADKYRLTYAYFAGGDAGDAFDGFDFGDDPSDKFFTSHNGMQFSTWDNDNDKFEGNCAEQDGSGWWMNKCHAGHLNGVYYQGGTYSKASTPNGYDNGIIWATWKTRWYSMKKTTMKIIPFNRL
>d1msk__ 4.99.1.1.1 Methionine synthase (activation domain) [Escherichia coli]
TPPVTLEAARDNDFAFDWQAYTPPVAHRLGVQEVEASIETLRNYIDWTPFFMTWSLAGKYPRILEDEVVGVEAQRLFKDANDMLDKLSAEKTLNPRGVVGLFPANRVGDDIEIYRDETRTHVINVSHHLRQQTEKTGFANYCLADFVAPKLSGKADYIGAFAVTGGLEEDALADAFEAQHDDYNKIMVKALADRLAEAFAEYLHERVRKVYWGYAPNENLSNEELIRENYQGIRPAPGYPACPEHTEKATIWELLEVEKHTGMKLTESFAMWPGASVSGWYFSHPDSKYYAVAQIQRDQVEDYARRKGMSVTEVERWLAPNLGYDAD
>d1hcl__ 5.1.1.1.1 Cyclin-dependent PK [Human (Homo sapiens)]
MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRTEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSFPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL
>d1ckia_ 5.1.1.1.10 Casein kinase-1, CK1 [rat (Rattus norvegicus)]
MELRVGNRYRLGRKIGSGSFGDIYLGTDIAAGEEVAIKLECVKTKHPQLHIESKIYKMMQGGVGIPTIRWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKYERISEKKMSTPIEVLCKGYPSEFATYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFGASR
>d1csn__ 5.1.1.1.11 Casein kinase-1, CK1 [Schizosaccharomyces pombe]
NVVGVHYKVGRRIGEGSFGVIFEGTNLLNNQQVAIKFEPRRSDAPQLRDEYRTYKLLAGCTGIPNVYYFGQEGLHNVLVIDLLGPSLEDLLDLCGRKFSVKTVAMAAKQMLARVQSIHEKSLVYRDIKPDNFLIGRPNSKNANMIYVVDFGMVKFYRDPVTKQHIPYREKKNLSGTARYMSINTHLGREQSRRDDLEALGHVFMYFLRGSLPWQGLKAATNKQKYERIGEKKQSTPLRELCAGFPEEFYKYMHYARNLAFDATPDYDYLQGLFSKVLERLNTTEDENFDWNLL
>d1apme_ 5.1.1.1.4 cAMP-dependent PK, catalytic subunit [mouse (Mus musculus)]
SEQESVKEFLAKAKEDFLKKWETPSQNTAQLDQFDRIKTLGTGSFGRVMLVKHKESGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVMEYVAGGEMFSHLRRIGRFAEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFTEF
>d1phk__ 5.1.1.1.5 gamma-subunit of glycogen phosphorylase kinase (Phk) [Rabbit (Oryctolagus cuniculus)]
FYENYEPKEILGRGVSSVVRRCIHKPTCKEYAVKIIDVTGGGSFSAEEVQELREATLKEVDILRKVSGHPNIIQLKDTYETNTFFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQLDPGEKLREVCGTPSYLAPEIIECSMNDNHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFGSPEWDDYSDTVKDLVSRFLVVQPQKRYTAEEALAHPFFQQYV
>d1koba_ 5.1.1.1.6 Twitchin, kinase domain [california sea hare aplysia californica, twk43]
INDYDKFYEDIWKKYVPQPVEVKQGSVYDYYDILEELGSGAFGVVHRCVEKATGRVFVAKFINTPYPLDKYTVKNEISIMNQLHHPKLINLHDAFEDKYEMVLILEFLSGGELFDRIAAEDYKMSEAEVINYMRQACEGLKHMHEHSIVHLDIKPENIMCETKKASSVKIIDFGLATKLNPDEIVKVTTATAEFAAPEIVDREPVGFYTDMWAIGVLGYVLLSGLSPFAGEDDLETLQNVKRCDWEFDEDAFSSVSPEAKDFIKNLLQKEPRKRLTVHDALEHPWLKGDHSNLTSRIPSSRYNKIRQKIKEKYADWPAPQPAIGRIANFSSLRKHRPQEYQIYDSYFDRKEAV
>d1koa_2 5.1.1.1.7 (1-350) Twitchin, kinase domain [Caenorhabditis elegans, pjk4]
YDNYVFDIWKQYYPQPVEIKHDHVLDHYDIHEELGTGAFGVVHRVTERATGNNFAAKFVMTPHESDKETVRKEIQTMSVLRHPTLVNLHDAFEDDNEMVMIYEFMSGGELFEKVADEHNKMSEDEAVEYMRQVCKGLCHMHENNYVHLDLKPENIMFTTKRSNELKLIDFGLTAHLDPKQSVKVTTGTAEFAAPEVAEGKPVGYYTDMWSVGVLSYILLSGLSPFGGENDDETLRNVKSCDWNMDDSAFSGISEDGKDFIRKLLLADPNTRMTIHQALEHPWLTPGNAPGRDSQIPSSRYTKIRDSIKTKYDAWPEPLPPLGRISNYSSLRKHRPQEYSIRDAFWDRSEA
>d1wfc__ 5.1.1.1.8 MAP kinase p38 [human (Homo sapiens)]
RPTFYRQELTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLEEFNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFTDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPGAELLKKISSESARNYIQSLTQMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPDDEPVADPYDQSFESRDLLIDEWKSLTYDEVISFVPP
>d1erk__ 5.1.1.1.9 MAP kinase Erk2 [rat Rattus norvegicus]
AAAAAAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNLNKVRVAIKKISPFEHQTYCQRTLREIKILLRFRHENIIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADPDHDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQYYDPSDEPIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGYRS
>d2hcka3 5.1.1.2.1 (167-437) Haemopoetic cell kinase Hck [human (Homo sapiens)]
KPQKPWEKDAWEIPRESLKLEKKLGAGQFGEVWMATYNKHTKVAVKTMKPGSMSVEAFLAEANVMKTLQHDKLVKLHAVVTKEPIYIITEFMAKGSLLDFLKSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYPGMSNPEVIRALERGYRMPRPENCPEELYNIMMRCWKNRPEERPTFEYIQSVLDDFYTATESQQQQP
>d1fgka_ 5.1.1.2.2 Fibroblast growth factor receptor 1 [human (Homo sapiens)]
ELPEDPRWELPRDRLVLGKPLGQVVLAEAIGLPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTS
>d1irk__ 5.1.1.2.3 insulin receptor [Human (Homo sapiens)]
SSVFVPDEWEVSREKITLLRELGQGSFGMVYEGNARDIIKGEAETRVAVKTVNESASLRERIEFLNEASVMKGFTCHHVVRLLGVVSKGQPTLVVMELMAHGDLKSYLRSLRPEAENNPGRPPPTLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQPYQGLSNEQVLKFVMDGGYLDQPDNCPERVTDLMRMCWQFNPKMRPTFLEIVNLLKDDLHPSFPEVSFFHSEENK
>d1bpya2 5.10.1.1.1 (83-326) DNA polymerase beta, catalytic (31 kD) fragment [Human (Homo sapiens)]
DTSSSINFLTRVSGIGPSAARKFVDEGIKTLEDLRKNEDKLNHHQRIGLKYFGDFEKRIPREEMLQMQDIVLNEVKKVDSEYIATVCGSFRRGAESSGDMDVLLTHPSFTSESTKQPKLLHQVVEQLQKVHFITDTLSKGETKFMGVCQLPSKNDEKEYPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEKGFTINEYTIRPLGVTGVAGEPLPVDSEKDIFDYIQWKYREPKDRSE
>d1rpl__ 5.10.1.1.2 DNA polymerase beta, catalytic (31 kD) fragment [rat (Rattus norvegicus)]
SSINFLTRVTGIGPSAARKLVDEGIKTLEDLRKNEDKLNHHQRIGLKYFEDFEKRIPREEMLQMQDIVLNEVKKLDPEYIATVCGSFRRGAESSGDMDVLLTHPNFTSESSKQPKLLHRVVEQLQKVRFITDTLSKGETKFMGVCQLPSENDENEYPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEKGFTINEYTIRPLGVTGVAGEPLPVDSEQDIFDYIQWRYREPKDRSE
>d1knya_ 5.10.1.2.1 Kanamycin nucleotidyltransferase (KNTase) [Staphylococcus aureus]
MNGPIIMTREERMKIVHEIKERILDKYGDDVKAIGVYGSLGRQTDGPYSDIEMMCVMSTEEAEFSHEWTTGEWKVEVNFYSEEILLDYASQVESDWPLTHGQFFSILPIYDSGGYLEKVYQTAKSVEAQTFHDAICALIVEELFEYAGKWRNIRVQGPTTFLPSLTVQVAMAGAMLIGLHHRICYTTSASVLTEAVKQSDLPSGYDHLCQFVMSGQLSDSEKLLESLENFWNGIQEWTERHGYIVDVSKRIPF
>d1ecl__ 5.11.1.1.1 DNA topoisomerase I, the 67K N-terminal domain [Escherichia coli]
GKALVIVESPAKAKTINKYLGSDYVVKSSVGHIRDLPDERGALVNRMGVDPWHNWEAHYEVLPGKEKVVSELKQLAEKADHIYLATDLDREGEAIAWHLREVIGGDDARYSRVVFNEITKNAIRQAFNKPGELNIDRVNAQQARRFMDRVVGYMVSPLLWKKIARGLSAGRVQSVAVRLVVEREREIKAFVPEEFWEVDASTTTPSGEALALQVTHQNDKPFRPVNKEQTQAAVSLLEKARYSVLEREDKPTTSKPGAPFITSTLQQAASTRLGFGVKKTMMMAQRLYEAGYITYMRTDSTNLSQDAVNMVRGYISDNFGKKYLPESPNQYAHEAIRPSDVNVMAESLKDMEADAQKLYQLIWRQFVACQMTPAKYDSTTLTVGAGDFRLKARGRILRFDGWTKVMPALRILPAVNKGDALTLVELTPAQHFTKPPARFSEASLVKELEKRGIGRPSTYASIISTIQDRGYVRVENRRFYAEKMGEIVTDRLEENFRELMNYDFTAQMENSLDQVANHEAEWKAVLDHFFSDFTQQLDKAEKDPEEGGMRPN
>d1ois__ 5.12.1.1.1 DNA topoisomerase I, N-terminal fragment [baker's yeast (Saccharomyces cerevisiae)]
DTIKWVTLKHNGVIFPPPYQPLPSHIKLYYDGKPVDLPPQAEEVAGFFAALLESDHAKNPVFQKNFFNDFLQVLKESGGPLNGIEIKEFSRCDFTKMFDYFQLQKEQKKQLEKKQIRLEREKFEEDYKFCELDGRREQVGNFKVEPPDLFRGRGAHPKTGKLKRRVNPEDIVLNLSKDAPVPPAPEGHKWGEIRHDNTVQWLAMWRENIFNSFKYVRLAA
>d1bgw__ 5.13.1.1.1 DNA topoisomerase II, the C-terminal fragment (residues 410-1202) [Saccharomyces cerevisiae]
RKSRITNYPKLEDANKAGTKEGYKCTLVLTEGDSALSLAVAGLAVVGRDYYGCYPLRGKMLNVREASADQILKNAEIQAIKKIMGLQHRKKYEDTKSLRYGHLMIMTDQDHDGSHIKGLIINFLESSFLGLLDIQGFLLEFITPIIKVSITKPTKNTIAFYNMPDYEKWREEESHKFTWKQKYYKGLGTSLAQEVREYFSNLDRHLKIFHSLQGLLFSLADNIRSIPNVLDGFKPGQRKVLYGCFKKNLKSELKVAQLAPYVSECTAYHHGEQSLAQTIIGLAQNFVGSNNIYLLLPNGAFGTRATGGKDAAAARYIYTELNKLTRKIFHPADDPLYKYIQEDEKTVEPEWYLPILPMILVNGAEGIGTGWSTYIPPFNPLEIIKNIRHLMNDEELEQMHPWFRGWTGTIEEIEPLRYRMYGRIEQIGDNVLEITELPARTWTSTIKEYLLLGLSGNDKIKPWIKDMEEQHDDNIKFIITLSPEEMAKTRKIGFYERFKLISPISLMNMVAFDPHGKIKKYNSVNEILSEFYYVRLEYYQKRKDHMSERLQWEVEKYSFQVKFIKMIIEKELTVTNKPRNAIIQELENLGFPRFNKEGKPYYGSPNDEIEELYGTYEYLLGMRIWSLTKERYQKLLKQKQEKETELENLLKLSAKDIWNTDLKAFEVGYQEFLQRDAEAR
>d1daaa_ 5.14.1.1.1 D-amino acid aminotransferase [Thermophilic bacillus strain YM-1]
GYTLWNDQIVKDEEVKIDKEDRGYQFGDGVYEVVKVYNGEMFTVNEHIDRLYASAEKIRITIPYTKDKFHQLLHELVEKNELNTGHIYFQVTRGTSPRAHQFPENTVKPVIIGYTKENPRPLENLEKGVKATFVEDIRWLRCDIKSLNLLGAVLAKQEAHEKGCYEAILHRNNTVTEGSSSNVFGIKDGILYTHPANNMILKGITRDVVIACANEINMPVKEIPFTTHEALKMDELFVTSTTSEITPVIEIDGKLIRDGKVGEWTRKLQKQFETKIP
>d1frvb_ 5.15.1.1.1 Nickel-iron hydrogenase, large subunit [Desulfovibrio gigas]
NKIVVDPITRIEGHLRIEVEVEGGKIKNAWSMSTLFRGLEMILKGRDPRDAQHFTQRACGVCTYVHALASVRAVDNCVGVKIPENATLMRNLTMGAQYMHDHLVHFYHLHALDWVNVANALNADPAKAARLANDLSPRKTTTESLKAVQAKVKALVESGQLGIFTNAYFLGGHPAYVLPAEVDLIATAHYLEALRVQVKAARAMAIFGAKNPHTQFTVVGGCTNYDSLRPERIAEFRKLYKEVREFIEQVYITDLLAVAGFYKNWAGIGKTSNFLTCGEFPTDEYDLNSRYTPQGVIWGNDLSKVDDFNPDLIEEHVKYSWYEGADAHHPYKGVTKPKWTEFHGEDRYSWMKAPRYKGEAFEVGPLASVLVAYAKKHEPTVKAVDLVLKTLGVGPEALFSTLGRTAARGIQCLTAAQEVEVWLDKLEANVKAGKDDLYTDWQYPTESQGVGFVNAPRGMLSHWIVQRGGKIENFQHVVPSTWNLGPRCAERKLSAVEQALIGTPIADPKRPVEILRTVHSYDPCIACGVH
>d1frva_ 5.16.1.1.1 Nickel-iron hydrogenase, small subunit [Desulfovibrio gigas]
AKKRPSVVYLHNAECTGCSESLLRTVDPYVDELILDVISMDYHETLMAGAGHAVEEALHEAIKGDFVCVIEGGIPMGDGGYWGKVGRRNMYDICAEVAPKAKAVIAIGTCATYGGVQAAKPNPTGTVGVNEALGKLGVKAINIAGCPPNPMNFVGTVVHLLTKGMPELDKQGRPVMFFGETVHDNCPRLKHFEAGEFATSFGSPEAKKGYCLYELGCKGPDTYNNCPKQLFNQVNWPVQAGHPCIACSEPNFWDLYSPFYSA
>d1dkza_ 5.17.1.1.1 DnaK [Escherichia coli]
VLLLDVTPLSLGIETMGGVMTTLIAKNTTIPTKHSQVFSTAEDNQSAVSIHVLQGERKRAADNKSLGQFNLDGINPAPRGMPQIEVTFDIDADGILHVSAKDKNSGKEQKITIKASSGLNEDEIQKMVRDAEANAEADRKFEELVQTRNQGDHLLHSTRKQVEEAGDKLPADDKTAIESALTALETALKGEDKAAIEAKMQELAQVSQKLMEIAQ
>d1jud__ 5.18.1.1.1 L-2-Haloacid dehalogenase [(Pseudomonas sp)]
YIKGIYFDLYGTLFDVHSVVGRCDEYFPGRGREISYLWRQKQLEYTWLRSLMNRYVNFQQYTEDYLRFTCRHLGLDLDYRTRSTLCDYYLRLYPFSEVPDSLRELKRRGLKLYILSNGSPQSIDYVVSHYGLRDGFDHLLSVDPVQVYKPDNRVYELYEQYLGLDRSYILFVSSNYWDYTGYRYFGFPTCWINRTGNVFEEMGQTPDWEVTSLRYVVELF
>d1lci__ 5.19.1.1.1 Luciferase [Firefly (Phontinus pyralis)]
AKNIKKGPAPFYPLEDGTAGEQLHKAMKRYALVPGTIAFTDAHIEVNITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMNISQPTVVFVSKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSMYTFVTSHLPPGFNEYDFVPESFDRDKTIALIMNSLPKGVALPHRTACVRFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILITPEGPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKLDARKIREILIKAKK
>d1hle.1 5.2.1.1.1 (a,b) Elastase inhibitor [horse (Equus caballus)]
MEQLSTANTHFAVDLFRALNESDPTGNIFISPLSISSALAMIFLGTRGNTAAQVSKALYFDTVEDIHSRFQSLNADINKPGAPYILKLANRLYGEKTYNFLADFLASTQKMYGAELASVDFQQAPEDARKEINEWVKGQTEGKIPELLVKGMVDNMTKLVLVNAIYFKGNWQQKFMKEATRDAPFRLNKKDTKTVKMMYQKKKFPYNYIEDLKCRVLELPYQGKELSMIILLPDDIEDESTGLEKIEKQLTLDKLREWTKPENLYLAEVNVHLPRFKLEESYDLTSHLARLGVQDLFNRGKADLSGMSGARDLFVSKIIHKSFVDLNEEGTEAAAATAGTILLAHNPSANILFLGRFSSPMEQLSTANTHFAVDLFRALNESDPTGNIFISPLSISSALAMIFLGTRGNTAAQVSKALYFDTVEDIHSRFQSLNADINKPGAPYILKLANRLYGEKTYNFLADFLASTQKMYGAELASVDFQQAPEDARKEINEWVKGQTEGKIPELLVKGMVDNMTKLVLVNAIYFKGNWQQKFMKEATRDAPFRLNKKDTKTVKMMYQKKKFPYNYIEDLKCRVLELPYQGKELSMIILLPDDIEDESTGLEKIEKQLTLDKLREWTKPENLYLAEVNVHLPRFKLEESYDLTSHLARLGVQDLFNRGKADLSGMSGARDLFVSKIIHKSFVDLNEEGTEAAAATAGTILLAHNPSANILFLGRFSSP
>d1ovaa_ 5.2.1.1.2 Ovalbumin [hen (Gallus domesticus)]
GSIGAASMEFCFDVFKELKVHHANENIFYCPIAIMSALAMVYLGAKDSTRTQINKVVRFDKLPGFGDSIEAQCGTSVNVHSSLRDILNQITKPNDVYSFSLASRLYAEERYPILPEYLQCVKELYRGGLEPINFQTAADQARELINSWVESQTNGIIRNVLQPSSVDSQTAMVLVNAIVFKGLWEKAFKDEDTQAMPFRVTEQESKPVQMMYQIGLFRVASMASEKMKILELPFASGTMSMLVLLPDEVSGLEQLESIINFEKLTEWTSSNVMEERKIKVYLPRMKMEEKYNLTSVLMAMGITDVFSSSANLSGISSAESLKISQAVHAAHAEINEAGREVVGSAEAGVDAASVSEEFRADHPFLFCIKHIATNAVLFFGRCVSP
>d2ach.1 5.2.1.1.3 (a,b) Antichymotrypsin, alpha-1 [human (Homo sapiens)]
LGLASANVDFAFSLYKQLVLKAPDKNVIFSPLSISTALAFLSLGAHNTTLTEILKGLKFNLTETSEAEIHQSFQHLLRTLNQSSDELQLSMGNAMFVKEQLSLLDRFTEDAKRLYGSEAFATDFQDSAAAKKLINDYVKNGTRGKITDLIKDLDSQTMMVLVNYIFFKAKWEMPFDPQDTHQSRFYLSKKKWVMVPMMSLHHLTIPYFRDEELSCTVVELKYTGNASALFILPDQDKMEEVEAMLLPETLKRWRDSLEFREIGELYLPKFSISRDYNLNDILLQLGIEEAFTSKADLSGITGARNLAVSQVVHKAVLDVFEEGTEASAATAVKITLLIFFMSKVTNPKQALGLASANVDFAFSLYKQLVLKAPDKNVIFSPLSISTALAFLSLGAHNTTLTEILKGLKFNLTETSEAEIHQSFQHLLRTLNQSSDELQLSMGNAMFVKEQLSLLDRFTEDAKRLYGSEAFATDFQDSAAAKKLINDYVKNGTRGKITDLIKDLDSQTMMVLVNYIFFKAKWEMPFDPQDTHQSRFYLSKKKWVMVPMMSLHHLTIPYFRDEELSCTVVELKYTGNASALFILPDQDKMEEVEAMLLPETLKRWRDSLEFREIGELYLPKFSISRDYNLNDILLQLGIEEAFTSKADLSGITGARNLAVSQVVHKAVLDVFEEGTEASAATAVKITLLIFFMSKVTNPKQA
>d9api.1 5.2.1.1.4 (a,b) Antitrypsin, alpha-1 [human (Homo sapiens)]
HPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMTKSPLFMGKVVNPTQKHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMTKSPLFMGKVVNPTQK
>d1atta_ 5.2.1.1.5 Antithrombin [bovine (Bos Taurus)]
VEDVCTAKPRDIPVNPMCIYRATEGQGSEQKIPGATNRRVWELSKANSHFATAFYQHLADSKNNNDNIFLSPLSISTAFAMTKLGACNNTLTQLMEVFKFDTISEKTSDQIHFFFAKLNCRLYRKANKSSELVSANRLFGDKSITFNETYQDISEVVYGAKLQPLDFKGNAEQSRLTINQWISNKTEGRITDVIPPQAINEFTVLVLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSVLMMYQESKFRYRRVAESTQVLELPFKGDDITMVLILPKLEKTLAKVEQELTPDMLQEWLDELTETLLVVHMPRFRIEDSFSVKEQLQDMGLEDLFSPEKSRLPGIVAEGRSDLYVSDAFHKAFLEVNEEGSEAAASTVISIAGRSRVTFKANRPFLVLIREVALNTIIFMGRVANPCVD
>d1atha_ 5.2.1.1.6 Antithrombin [human (Homo sapiens)]
ICTCIYRRRVWELSKANSRFATTFYQHLADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSDQIHFFFAKLNCRLYRSSKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAEQSRAAINKWVSNKTEGRITDVIPSEAINELTVLVLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRVAEGTQVLELPFKGDDITMVLILPKPEKSLAKVEKELTPEVLQEWLDELEEMMLVVHMPRFRIEDGFSLKEQLQDMGLVDLFSPEKSKLPGIVAEGRDDLYVSDAFHKAFLEVNEEGSEAAASTAVVIAGRSLNPNRVTFKANRPFLVFIREVPLNTIIFMGRVANPCV
>d1ad2__ 5.20.1.1.1 Ribosomal protein L1 [Thermus thermophilus]
KRYRALLEKVDPNKIYTIDEAAHLVKELATAKFDETVEVHAKLGIDPRRSDQNVRGTVSLPHGLGKQVRVLAIAKGEKIKEAEEAGADYVGGEEIIQKILDGWMDFDAVVATPDVMGAVGSKLGRILGPRGLLPNPKAGTVGFNIGEIIREIKAGRIEFRNDKTGAIHAPVGKACFPPEKLADNIRAFIRALEAHKPEGAKGTFLRSVYVTTTMGPSVRINPHS
>d1ecra_ 5.3.1.1.1 Replication terminator protein (Tus) [Escherichia coli]
DLVDRLNTTFRQMEQELAIFAAHLEQHKLLVARVFSLPEVKKEDEHNPLNRIEVKQHLGNDAQSLALRHFRHLFIQQQSENRSSKAAVRLPGVLCYQVDNLSQAALVSHIQHINKLKTTFEHIVTVESELPTAARFEWVHRHLPGLITLNAYRTLTVLHDPATLRFGWANKHIIKNLHRDEVLAQLEKSLKSPRSVAPWTREEWQRKLEREYQDIAALPQNAKLKIKRPVKVQPIARVWYKGDQKQVQHACPTPLIALINRDNGAGVPDVGELLNYDADNVQHRYKPQAQPLRLIIPRLHLYVAD
>d3pte__ 5.4.1.1.1 D-ala carboxypeptidase/transpeptidase [streptomyces R61]
ADLPAPDDTGLQAVLHTALSQGAPGAMVRVDDNGTIHQLSEGVADRATGRAITTTDRFRVGSVTKSFSAVVLLQLVDEGKLDLDASVNTYLPGLLPDDRITVRQVMSHRSGLYDYTNDMFAQTVPGFESVRNKVFSYQDLITLSLKHGVTNAPGAAYSYSNTNFVVAGMLIEKLTGHSVATEYQNRIFTPLNLTDTFYVHPDTVIPGTHANGYLTPDEAGGALVDSTEQTVSWAQSAGAVISSTQDLDTFFSALMSGQLMSAAQLAQMQQWTTVNSTQGYGLGLRRRDLSCGISVYGHTGTVQGYYTYAFASKDGKRSVTALANTSNNVNVLNTMARTLESAFCGKP
>d1btl__ 5.4.1.1.2 beta-Lactamase TEM-1 [Escherichia coli]
HPETLVKVKDAEDQLGARVGYIELDLNSGKILESFRPEERFPMMSTFKVLLCGAVLSRIDAGQEQLGRRIHYSQNDLVEYSPVTEKHLTDGMTVRELCSAAITMSDNTAANLLLTTIGGPKELTAFLHNMGDHVTRLDRWEPELNEAIPNDERDTTMPVAMATTLRKLLTGELLTLASRQQLIDWMEADKVAGPLLRSALPAGWFIADKSGAGERGSRGIIAALGPDGKPSRIVVIYTTGSQATMDERNRQIAEIGASLIKHW
>d3blm__ 5.4.1.1.3 beta-Lactamase, class A [Staphylococcus aureus]
KELNDLEKKYNAHIGVYALDTKSGKEVKFNSDKRFAYASTSKAINSAILLEQVPYNKLNKKVHINKDDIVAYSPILEKYVGKDITLKALIEASMTYSDNTANNKIIKEIGGIKKVKQRLKELGDKVTNPVRYEIELNYYSPKSKKDTSTPAAFGKTLNKLIANGKLSKENKKFLLDLMLNNKSGDTLIKDGVPKDYKVADKSGQAITYASRNDVAFVYPKGQSEPIVLVIFTNKDNKSDKPNDKLISETAKSVMKEF
>d4blma_ 5.4.1.1.4 beta-Lactamase, class A [Bacillus licheniformis]
DDFAKLEEQFDAKLGIFALDTGTNRTVAYRPDERFAFASTIKALTVGVLLQQKSIEDLNQRITYTRDDLVNYNPITEKHVDTGMTLKELADASLRYSDNAAQNLILKQIGGPESLKKELRKIGDEVTNPERFEPELNEVNPGETQDTSTARALVTSLRAFALEDKLPSEKRELLIDWMKRNTTGDALIRAGVPDGWEVADKTGAASYGTRNDIAIIWPPKGDPVVLAVLSSRDKKDAKYDDKLIAEATKVVMKALN
>d2blta_ 5.4.1.1.6 beta-Lactamase, class C [Cephalosporinase Enterobacter cloacae P99]
PVSEKQLAEVVANTITPLMKAQSVPGMAVAVIYQGKPHYYTFGKADIAANKPVTPQTLFELGSISKTFTGVLGGDAIARGEISLDDAVTRYWPQLTGKQWQGIRMLDLATYTAGGLPLQVPDEVTDNASLLRFYQNWQPQWKPGTTRLYANASIGLFGALAVKPSGMPYEQAMTTRVLKPLKLDHTWINVPKAEEAHYAWGYRDGKAVRVSPGMLDAQAYGVKTNVQDMANWVMANMAPENVADASLKQGIALAQSRYWRIGSMYQGLGWEMLNWPVEANTVVEGSDSKVALAPLPVAEVNPPAPPVKASWVHKTGSTGGFGSYVAFIPEKQIGIVMLANTSYPNPARVEAAYHILEAL
>d1pmd_4 5.4.1.1.7 (189-544) Penicillin-binding protein 2x (pbp-2x), transpeptidase domain [Streptococcus pneumoniae]
TISSPLQSFMETQMDAFQEKVKGKYMTATLVSAKTGEILATTQRPTFDADTKEGITEDFVWRDILYQSNYEPGSTMKVMMLAAAIDNNTFPGGEVFNSSELKIADATIRDWDVNEGLTGGRMMTFSQGFAHSSNVGMTLLEQKMGDATWLDYLNRFKFGVPTRFGLTDEYAGQLPADNIVNIAQSSFGQGISVTQTQMIRAFTAIANDGVMLEPKFISAIYDPNDQTARKSQKEIVGNPVSKDAASLTRTNMVLVGTDPVYGTMYNHSTGKPTVTVPGQNVALKSGTAQIADEKNGGYLVGLTDYIFSAVSMSPAENPDFILYVTVQQPEHYSGIQLGEFANPILERASAMKDSLN
>d1lbea_ 5.5.1.1.1 ADP ribosyl cyclase [sea hare (Aplysia californica)]
IVPTRELENVFLGRCKDYEITRYLDILPRVRSDCSALWKDFFKAFSFKNPCDLDLGSYKDFFTSAQQQLPKNKVMFWSGVYDEAHDYANTGRKYITLEDTLPGYMLNSLVWCGQRANPGFNEKVCPDFKTCPVQARESFWGMASSSYAHSAEGEVTYMVDGSNPKVPAYRPDSFFGKYELPNLTNKVTRVKVIVLHRLGEKIIEKCGAGSLLDLEKLVKAKHFAFDCVENPRAVLFLLCSDNPNARECRL
>d7cata_ 5.6.1.1.1 Catalase [beef (Bos taurus)]
NRDPASDQMKHWKEQRAAQKPDVLTTGGGNPVGDKLNSLTVGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITRYSKAKVFEHIGKRTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDALLFPSFIHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDRGIPDGHRHMDGYGSHTFKLVNADGEAVYCKFHYKTDQGIKNLSVEDAARLAHEDPDYGLRDLFNAIATGNYPSWTLYIQVMTFSEAEIFPFNPFDLTKVWPHGDYPLIPVGKLVLNRNPVNYFAEVEQLAFDPSNMPPGIEPSPDKMLQGRLFAYPDTHRHRLGPNYLQIPVNCPYRARVANYQRDGPMCMMDNQGGAPNYYPNSFSAPEHQPSALEHRTHFSGDVQRFNSANDDNVTQVRTFYLKVLNEEQRKRLCENIAGHLKDAQLFIQKKAVKNFSDVHPEYGSRIQALLDKYN
>d2cae__ 5.6.1.1.2 Catalase [Proteus mirabilis]
KKLTTAAGAPVVDNNNVITAGPRGPMLLQDVWFLEKLAHFDREVIPERRHAKGSGAFGTFTVTHDITKYTRAKIFSEVGKKTEMFARFSTVAGERGAADAERDIRGFALKFYTEEGNWDMVGNNTPVFYLRDPLKFPDLNHIVKRDPRTNMRNMAYKWDFFSHLPESLHQLTIDMSDRGLPLSYRFVHGFGSHTYSFINKDNERFWVKFHFRCQQGIKNLMDDEAEALVGKDRESSQRDLFEAIERGDYPRWKLQIQIMPEKEASTVPYNPFDLTKVWPHADYPLMDVGYFELNRNPDNYFSDVEQAAFSPANIVPGISFSPDKMLQGRLFSYGDAHRYRLGVNHHQIPVNAPKCPFHNYHRDGAMRVDGNSGNGITYEPNSGGVFQEQPDFKEPPLSIEGAADHWNHREDEDYFSQPRALYELLSDDEHQRMFARIAGELSQASKETQQRQIDLFTKVHPEYGAGVEKAIKVL
>d1ipha2 5.6.1.1.5 (1-571) Catalase [Escherichia coli PHII]
DSLAPEDGSHRPAAEPTPPGAQPTAPGSLKAPDTRNEKLNSLEDVRKGSENYALTTNQGVRIADDQNSLRAGSRGPTLLEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKSLSDITKADFLSDPNKITPVFVRFSTVQGGAGSADTVRDIRGFATKFYTEEGIFDLVGNNTPIFFIQDAHKFPDFVHAVKPEPHWAIPQGQSAHDTFWDYVSLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAEGKATFVRFHWKPLAGKASLVWDEAQKLTGRDPDFHRRELWEAIEAGDFPEYELGFQLIPEEDEFKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAENEQAAFHPGHIVPGLDFTNDPLLQGRLFSYTDTQISRLGGPNFHEIPINRPTCPYHNFQRDGMHRMGIDTNPANYEPNSINDNWPRETPPGPKRGGFESYQERVEGNKVRERSPSFGEYYSHPRLFWLSQTPFEQRHIVDGFSFELSKVVRPYIRERVVDQLAHIDLTLAQAVAKNLGIELTDDQLNITPPPDVNGLKKDPSLSLYAIPDGD
>d1buca2 5.7.1.1.1 (1-232) Butyryl-CoA dehydrogenase [Megasphaera elsdenii]
MDFNLTDIQQDFLKLAHDFGEKKLAPTVTERDHKGIYDKELIDELLSLGITGAYFEEKYGGSGDDGGDVLSYILAVEELAKYDAGVAITLSATVSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDGTYTLNGSKIFITNGGAADIYIVFAMTDKSKGNHGITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGEE
>d3mdda2 5.7.1.1.2 (1-231) Medium chain acyl-CoA dehydrogenase [Pig (Sus scrofa)]
GFSFELTEQQKEFQATARKFAREEIIPVAAEYDRTGEYPVPLLKRAWELGLMNTHIPESFGGLGLGIIDSCLITEELAYGCTGVQTAIEANTLGQVPLIIGGNYQQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPASKAFTGFIVEADTPGVQIGRKEINMGQRCSDTRGIVFEDVRVPKENVLTGE
>d1egda2 5.7.1.1.3 (1-232) Medium chain acyl-CoA dehydrogenase [human homo sapiens]
LGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGD
>d5fbpa_ 5.8.1.1.1 Fructose-1,6-bisphosphatase [pig (Sus scrofa)]
FDTNIVTLTRFVMEQGRKARGTGEMTQLLNSLCTAVKAISTAVRKAGIAKLDVLSNDLVINVLKSSFATCVLVTEEDKNAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKNSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMVNGVNCFMLDPAIGEFILVDRNVKIKKKGSIYSINEGYAKEFDPAITEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFMYPANKKSPKGKLRLLYECNPMAYVMEKAGGLATTGKEAVLDIVPTDIHQRAPIILGSPEDVTELLEIYQKHA
>d1ftaa_ 5.8.1.1.2 Fructose-1,6-bisphosphatase [human (Homo sapiens)]
DVVTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAVRKAGIAHLYGIAGVKKLDVLSNDLVMNMLKSSFATCVLVSEEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEAYAKDFDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAPIILGSPDDVLEFLKVYEKHS
>d1spia_ 5.8.1.1.3 Fructose-1,6-bisphosphatase [spinach (Spinacia oleracea)]
AATQTKARTRSKYEIETLTGWLLKQPMAGVIDAELTIVLSSISLACKQIASLVQRAKLDVVSNEVFSSCLRSSGRTGIIASEEEDVPVAVEESYSGNYIVVFDPLDGSSNIDAAVSTGSIFGIYSPNDECIVDSDHDDESQLSAEEQRCVVNVCQPGDNLLAAGYCMYSSSVIFVLTIGKGVYAFTLDPMYGEFVLTSEKIQIPKAGKIYSFNEGNYKMWPDKLKKYMDDLKEPGESQKPYSSRYIGSLVGDFHRTLLYGGIYGYPRDAKSKNGKLRLLYECAPMSFIVEQAGGKGSDGHQRILDIQPTEIHQRVPLYIGSVEEVEKLEKYLA
>d2hhma_ 5.8.1.2.1 Inositol monophosphatase [human (Homo sapiens)]
WQECMDYAVTLARQAGEVVCEAIKNEMNVMLKSSPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSILTDNPTWIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTELGSSRTPETVRMVLSNMEKLFCIPVHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDVAGAGIIVTEAGGVLMDVTGGPFDLMSRRVIAANNRILAERIAKEIQVIPLQRDDE
>d1inp__ 5.8.1.3.1 Inositol polyphosphate 1-phospatase [Bovine (Bos taurus) brain]
MSDILQELLRVSEKAANIARACRQQETLFQLLIEEKKEGEKNKKFAVDFKTLADVLVQEVIKENMENKFPGLGKKIFGEESNELTNDLGEKIIMRLGPTEEETVALLSKVLNGNKLASEALAKVVHQDVFFSDPALDSVEINIPQDILGIWVDPIDSTYQYIKGSADITPNQGIFPSGLQCVTVLIGVYDIQTGVPLMGVINQPFVSQDLHTRRWKGQCYWGLSYLGTNIHSLLPPVSTRSNSEAQSQGTQNPSSEGSCRFSVVISTSEKETIKGALSHVCGERIFRAAGAGYKSLCVILGLADIYIFSEDTTFKWDSCAAHAILRAMGGGMVDLKECLERNPDTGLDLPQLVYHVGNEGAAGVDQWANKGGLIAYRSEKQLETFLSRLLQHLAPVATHT
>d1kfd_2 5.9.1.1.1 (196-560) DNA polymerase I (Klenov fragment) [Escherichia coli]
HKGPLNVFENIEMPLVPVLSRIERNGVKIDPKVLHNHSEELTLRLAELEKKAHEIADYPLPKVILEYRGLAKLKSTYTDKLPLMINPKTGRVHTSYHQAVTATGRLSSTDPNLQNIPVRNEEGRRIRQAFIAPEDYVIVSADYSQIELRIMAHLSRDKGLLTAFAEGKDIHRATAAEVFGLPLETVTSEQRRSAKAINFGLIYGMSAFGLARQLNIPRKEAQKYMDLYFERYPGVLEYMERTRAQAKEQGYVETLDGRRLYLPDIKSSNGARRAAAERAAINAPMQGTAADIIKRAMIAVDAWLQAEQPRVRMIMQVHDELVFEVHKDDVDAVAKQIHQLMENCTRLDVPLLVEVGSGENWDQAH
>d1taq_3 5.9.1.1.2 (426-807) DNA polymerase I (Klenov fragment) [Thermus aquaticus]
LDVAYLRALSLEVAEEIARLEAEVFRLAGHPFNLNSRDQLERVLFDELGLPAIGKTEKTGKRSTSAAVLEALREAHPIVEKILQYRELTKLKSTYIDPLPDLIHPRTGRLHTRFNQTATATGRLCCCDPNLQNIPVRTPLGQRIRRGFIAEEGWLLVALDYSQIELRVLAHLSGDENLIRVFQEGRDIHTETASWMFGVPREAVDPLMRRAAKTINFGVLYGMSAHRLSQELAIPYEEAQAFIERYFQSFPKVRAWIEKTLEEGRRRGYVETLFGRRRYVPDLEARVKSVREAAERMAFNMPVQGTAADLMKLAMVKLFPRLEEMGARMLLQVHDELVLEAPKERAEAVARLAKEVMEGVYPLAVPLEVEVGIGEDWLSAKE
>d1mml__ 5.9.1.2.1 MMLV reverse transcriptase [Moloney murine leukemia virus)]
TWLSDFPQAWAETGGMGLAVRQAPLIIPLKATSTPVSIKQYPMSQEARLGIKPHIQRLLDQGILVPCQSPWNTPLLPVKKPGTNDYRPVQDLREVNKRVEDIHPTVPNPYNLLSGLPPSHQWYTVLDLKDAFFCLRLHPTSQPLFAFEWRDPEMGISGQLTWTRLPQGFKNSPTLFDEALHRDLADFRIQHPDLILLQYVDDLLLAATSELDCQQGTRALLQTLGNLGYRASAKKAQICQKQVKYLGYLLK
>d1har__ 5.9.1.2.2 HIV-1 reverse transcriptase [human immunodeficiency virus type 1 (Bh10 isolate)]
PISPIETVPVKLKPGMDGPKVAQWPLTAAKIAALVAICTEMEKEGKISKIGPENPYNTPVFAIWAKLVDFRELNKRTQDFWEVKSVTVLDVGDAYFSVPLDEDFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILAPFKAANPDIVIYQYMDDLYVGSDLAIGAHRTKIEELRQHLLRWGLTT
>d1hnib1 5.9.1.2.2 HIV-1 reverse transcriptase [human immunodeficiency virus type 1 (Bh10 isolate)]
PISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGPENPYNTPVFAIKKKDSTKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFRKQNPDIVIYQYMDDLYVGSDLEIGQHRTKIEELRQHLLRWGLTTPDKKHQKEPPFLWMGYELHPDKWTVQPIVLPEKDSWTVNDIQKLVGKLNWASQIYPGIKVRQLSKLLRGTKALTEVIPLTEEAELELAENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTGKYARTRGAHTNDVKQLTEAVQKITTESIVIWGKTPKFKLPIQKETWETWWTEYWQATWIPEWEFVNTPPLVKLWY
>d1cola_ 6.1.1.1.1 Colicin A [Escherichia coli]
AKDERELLEKTSELIAGMGDKIGEHLGDKYKAIAKDIADNIKNFQGKTIRSFDDAMASLNKITANPAMKINKADRDALVNAWKHVDAQDMANKLGNLSKAFKVADVVMKVEKVREKSIEGYETGNWGPLMLEVESWVLSGIASSVALGIFSATLGAYALSLGVPAIAVGIAGILLAAVVGALIDDKFADALNNEIIR
>d1ddt_3 6.1.2.1.1 (188-368) Diphtheria toxin, middle domain [Corynebacterium diphtheriae]
SCINLDWDVIRDKTKTKIESLKEHGPIKNKMSESPNKTVSEEKAKQYLEEFHQTALEHPELSELKTVTGTNPVFAGANYAAWAVNVAQVIDSETADNLEKTTAALSILPGIGSVMGIADGAVHHNTEEIVAQSIALSSLMVAQAIPLVGELVDIGFAAYNFVESIINLFQVVHNSYNRPAY
>d1dlc_3 6.1.3.1.1 (1-229) delta-Endotoxin (insectocide), N-terminal domain [Bacillus thuringiensis tenebrionis, CRYIIIA (BT13)]
TTKDVIQKGISVVGDLLGVVGFPFGGALVSFYTNFLNTIWPSEDPWKAFMEQVEALMDQKIADYAKNKALAELQGLQNNVEDYVSALSSWQKNPVSSRNPHSQGRIRELFSQAESHFRNSMPSFAISGYEVLFLTTYAQAANTHLFLLKDAQIYGEEWGYEKEDIAEFYKRQLKLTQEYTDHCVKWYNVGLDKLRGSSYESWVNFNRYRREMTLTVLDLIALFPLYDVR
>d1ciy_3 6.1.3.1.2 (1-223) delta-Endotoxin (insectocide), N-terminal domain [(Bacillus thuringiensis,) CRYIA (A)]
YTPIDISLSLTQFLLSEFVPGAGFVLGLVDIIWGIFGPSQWDAFLVQIEQLINQRIEEFARNQAISRLEGLSNLYQIYAESFREWEADPTNPALREEMRIQFNDMNSALTTAIPLLAVQNYQVPLLSVYVQAANLHLSVLRDVSVFGQRWGFDAATINSRYNDLTRLIGNYTDYAVRWYNTGLERVWGPDSRDWVRYNQFRRELTLTVLDIVALFSNYDSRRY
>d1af3__ 6.1.4.1.2 Apoptosis regulator Bcl-xL [rat (Rattus norvegicus)]
SQSNRELVVDFLSYKLSQKGYSWSQFSDVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIASWMATYLNDHLEPWIQENGGWDTFVDLYG
>d1svb_2 6.10.1.1.1 (1-302) Envelope glycoprotein, central and dimerisation domains [Tick-borne encephalitis virus, (TBE)]
SRCTHLENRDFVTGTQGTTRVTLVLELGGCVTITAEGKPSMDVWLDAIYQENPAKTREYCLHAKLSDTKVAARCPTMGPATLAEEHQGGTVCKRDQSDRGWGNHCGLFGKGSIVACVKAACEAKKKATGHVYDANKIVYTVKVEPHTGDYVAANETHSGRKTASFTISSEKTILTMGEYGDVSLLCRVASGVDLAQTVILELDKTVEHLPTAWQVHRDWFNDLALPWKHEGAQNWNNAERLVEFGAPHAVKMDVYNLGDQTGVLLKALAGVPVAHIEGTKYHLKSGHVTCEVGLEKLKMKGL
>d1htmb_ 6.2.1.1.1 Influenza hemagglutinin (stalk) [Influenza virus A]
STQAAIDQINGKLNRVIEKTNEKFHQIEKEFSEVEGRIQDLEKYVEDTKIDLWSYNAELLVALENQHTIDLTDSEMNKLFEKTRRQLRENAEEMGNGCFKIYHKCDNACIESIR
>d1aik.1 6.2.2.1.1 (n,c) HIV-1 gp41 protease-resistant core [human immunodeficiency virus type 1]
SGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARILNQQEKNEQELLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARILNQQEKNEQELL
>d1vsga_ 6.3.1.1.1 Variant surface glycoprotein (N-terminal domain) [Trypanosoma brucei]
AAEKGFKQAFWQPLCQVSEELDDQPKGALFTLQAAASKIQKMRDAALRASIYAEINHGTNRAKAAVIVANHYAMKADSGLEALKQTLSSQEVTATATASYLKGRIDEYLNLLLQTKESGTSGCMMDTSGTNTVTKAGGTIGGVPCKLQLSPIQPKRPAATYLGKAGYVGLTRQADAANNFHDNDAECRLASGHNTNGLGKSGQLSAAVTMAAGYVTVANSQTAVTVQALDALQEASGAAHQPWIDAWKAKKALTGAETAEFRNETAGIAGKTGVTKLVEEALLKKKDSEASEIQTELKKYFSGHENEQWTAIEKLISEQPVAQNLVGDNQPTKLGELEGNAKLTTILAYYRMETAGKFEVLT
>d1aa0__ 6.4.1.1.1 Fibritin deletion mutant E [Bacteriophage T4]
VSGLNNAVQNLQVEIGNNSAGIKGQVVALNTLVNGTNPNGSTVEERGLTNSIKANETNIASVTQEVNTAKGNISSLQGDVQALQEAGYIPEAPRDGQAYVRKDGEWVLLSTFL
>d1prcl1 6.5.1.1.1 Photosynthetic reaction centre, L-, M- and H-chains [rhodobacter viridis ]
ALLSFERKYRVRGGTLIGGDLFDFWVGPYFVGFFGVSAIFFIFLGVSLIGYAASQGPTWDPFAISINPPDLKYGLGAAPLLEGGFWQAITVCALGAFISWMLREVEISRKLGIGWHVPLAFCVPIFMFCVLQVFRPLLLGSWGHAFPYGILSHLDWVNNFGYQYLNWHYNPGHMSSVSFLFVNAMALGLHGGLILSVANPGDGDKVKTAEHENQYFRDVVGYSIGALSIHRLGLFLASNIFLTGAFGTIASGPFWTRGWPEWWGWWLDIPFWS
>d1prch2 6.5.1.1.1 (1-36) Photosynthetic reaction centre, L-, M- and H-chains [rhodobacter viridis ]
MYHGALAQHLDIAQLVWYAQWLVIWTVVLLYLRRED
>d1prcm1 6.5.1.1.1 Photosynthetic reaction centre, L-, M- and H-chains [rhodobacter viridis ]
ADYQTIYTQIQARGPHITVSGEWGDNDRVGKPFYSYWLGKIGDAQIGPIYLGASGIAAFAFGSTAILIILFNMAAEVHFDPLQFFRQFFWLGLYPPKAQYGMGIPPLHDGGWWLMAGLFMTLSLGSWWIRVYSRARALGLGTHIAWNFAAAIFFVLCIGCIHPTLVGSWSEGVPFGIWPHIDWLTAFSIRYGNFYYCPWHGFSIGFAYGCGLLFAAHGATILAVARFGGDREIEQITDRGTAVERAALFWRWTIGFNATIESVHRWGWFFSLMVMVSASVGILLTGTFVDNWYLWCVKHGAAPDYPAYLPATPDPASLPGAPK
>d1pcrm1 6.5.1.1.2 Photosynthetic reaction centre, L-, M- and H-chains [rhodobacter sphaeroides ]
AEYQNIFSQVQVRGPADLGMTEDVNLANRSGVGPFSTLLGWFGNAQLGPIYLGSLGVLSLFSGLMWFFTIGIWFWYQAGWNPAVFLRDLFFFSLEPPAPEYGLSFAAPLKEGGLWLIASFFMFVAVWSWWGRTYLRAQALGMGKHTAWAFLSAIWLWMVLGFIRPILMGSWSEAVPYGIFSHLDWTNNFSLVHGNLFYNPFHGLSIAFLYGSALLFAMHGATILAVSRFGGERELEQIADRGTAAERAALFWRWTMGFNATMEGIHRWAIWMAVLVTLTGGIGILLSGTVVDNWYVWGQNHG
>d1pcrl1 6.5.1.1.2 Photosynthetic reaction centre, L-, M- and H-chains [rhodobacter sphaeroides ]
ALLSFERKYRVPGGTLVGGNLFDFWVGPFYVGFFGVATFFFAALGIILIAWSAVLQGTWNPQLISVYPPALEYGLGGAPLAKGGLWQIITICATGAFVSWALREVEICRKLGIGYHIPFAFAFAILAYLTLVLFRPVMMGAWGYAFPYGIWTHLDWVSNTGYTYGNFHYNPAHMIAISFFFTNALALALHGALVLSAANPEKGKEMRTPDHEDTFFRDLVGYSIGTLGIHRLGLLLSLSAVFFSALCMIITGTIWFDQWVDWWQWWVKLPWWANIPGGING
>d1pcrh2 6.5.1.1.2 (1-25) Photosynthetic reaction centre, L-, M- and H-chains [rhodobacter sphaeroides ]
DLASLAIYSFWIFLAGLIYYLQTEN
>d1occb2 6.5.1.1.3 (1-90) Cytochrome c oxidase [bovine (Bos taurus)]
MAYPMQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEI
>d1occd1 6.5.1.1.3 Cytochrome c oxidase [bovine (Bos taurus)]
SVVKSEDYALPSYVDRRDYPLPDVAHVKNLSASQKALKEKEKASWSSLSIDEKVELYRLKFKESFAEMNRSTNEWKTVVGAAMFFIGFTALLLIWEKHYVYGPIPHTFEEEWVAKQTKRMLDMKVAPIQGFSAKWDYDKNEWKK
>d1occj1 6.5.1.1.3 Cytochrome c oxidase [bovine (Bos taurus)]
FENRVAEKQKLFQEDNGLPVHLKGGATDNILYRVTMTLCLGGTLYSLYCLGWASFP
>d1occk1 6.5.1.1.3 Cytochrome c oxidase [bovine (Bos taurus)]
APDFHDKYGNAVLASGATFCVAVWVYMATQIGIEWNPSPVGRVTPKEWR
>d1occl1 6.5.1.1.3 Cytochrome c oxidase [bovine (Bos taurus)]
SHYEEGPGKNIPFSVENKWRLLAMMTLFFGSGFAAPFFIVRHQLLKK
>d1occa1 6.5.1.1.3 Cytochrome c oxidase [bovine (Bos taurus)]
MFINRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVMITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFAIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTMWNTISSMGSFISLTAVMLMVFIIWEAFASKREVLTVDLTTTNLEWLNGCPPPYHTFEEPTYVNLK
>d1occg1 6.5.1.1.3 Cytochrome c oxidase [bovine (Bos taurus)]
ASAAKGDHGGTGARTWRFLTFGLALPSVALCTLNSWLHSGHRERPAFIPYHHLRIRTKPFSWGDGNHTFFHNPRVNPLPTGYEK
>d1occm1 6.5.1.1.3 Cytochrome c oxidase [bovine (Bos taurus)]
ITAKPAKTPTSPKEQAIGLSVTFLSFLLPAGWVLYHLDNYKKS
>d1occc1 6.5.1.1.3 Cytochrome c oxidase [bovine (Bos taurus)]
MTHQTHAYHMVNPSPWPLTGALSALLMTSGLTMWFHFNSMTLLMIGLTTNMLTMYQWWRDVIRESTFQGHHTPAVQKGLRYGMILFIISEVLFFTGFFWAFYHSSLAPTPELGGCWPPTGIHPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGDRKHMLQALFITITLGVYFTLLQASEYYEAPFTISDGVYGSTFFVATGFHGLHVIIGSTFLIVCFFRQLKFHFTSNHHFGFEAGAWYWHFVDVVWLFLYVSIYWWGS
>d1occi1 6.5.1.1.3 Cytochrome c oxidase [bovine (Bos taurus)]
STALAKPQMRGLLARRLRFHIVGAFMVSLGFATFYKFAVAEKRKKAYADFYRNYDSMKDFEEMRKAGIFQSAK
>d1kzub_ 6.6.1.1.1 Light-harvesting complex LH2 [Purple bacterium (Rhodopseudomonas acidophila)]
ATLTAEQSEELHKYVIDGTRVFLGLALVAHFLAFSATPWLH
>d1kzua_ 6.6.1.1.1 Light-harvesting complex LH2 [Purple bacterium (Rhodopseudomonas acidophila)]
NQGKIWTVVNPAIGIPALLGSVTVIAILVHLAILSHTTWFPAYWQGGV
>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
>d2omf__ 6.7.1.1.1 Porin [Escherichia coli]
AEIYNKDGNKVDLYGKAVGLHYFSKGNGENSYGGNGDMTYARLGFKGETQINSDLTGYGQWEYNFQGNNSEGADAQTGNKTRLAFAGLKYADVGSFDYGRNYGVVYDALGYTDMLPEFGGDTAYSDDFFVGRVGGVATYRNSNFFGLVDGLNFAVQYLGKNERDTARRSNGDGVGGSISYEYEGFGIVGAYGAADRTNLQEAQPLGNGKKAEQWATGLKYDANNIYLAANYGETRNATPITNKFTNTSGFANKTQDVLLVAQYQFDFGLRPSIAYTKSKAKDVEGIGDVDLVNYFEVGATYYFNKNMSTYVDYIINQIDSDNKLGVGSDDTVAVGIVYQF
>d1pho__ 6.7.1.1.1 Porin [Escherichia coli]
AEIYNKDGNKLDVYGKVKAMHYMSDNASKDGDQSYIRFGFKGETQINDQLTGYGRWEAEFAGNKAESDTAQQKTRLAFAGLKYKDLGSFDYGRNLGALYDVEAWTDMFPEFGGDSSAQTDNFMTKRASGLATYRNTDFFGVIDGLNLTLQYQGKNENRDVKKQNGDGFGTSLTYDFGGSDFAISGAYTNSDRTNEQNLQSRGTGKRAEAWATGLKYDANNIYLATFYSETRKMTPITGGFANKTQNFEAVAQYQFDFGLRPSLGYVLSKGKDIEGIGDEDLVNYIDVGATYYFNKNMSAFVDYKINQLDSDNKLNINNDDIVAVGMTYQF
>d2por__ 6.7.1.1.2 Porin [Rhodobacter capsulatus]
EVKLSGDARMGVMYNGDDWNFSSRSRVLFTMSGTTDSGLEFGASFKAHESVGAETGEDGTVFLSGAFGKIEMGDALGASEALFGDLYEVGYTDLDDRGGNDIPYLTGDERLTAEDNPVLLYTYSAGAFSVAASMSDGKVGETSEDDAQEMAVAAAYTFGNYTVGLGYEKIDSPDTALMADMEQLELAAIAKFGATNVKAYYADGELDRDFARAVFDLTPVAAAATAVDHKAYGLSVDSTFGATTVGGYVQVLDIDTIDDVTYYGLGASYDLGGGASIVGGIADNDLPNSDMVADLGVKFKF
>d1prn__ 6.7.1.1.3 Porin [Rhodopseudomonas blastica strain DSM2131]
EISLNGYGRFGLQYVEDRGVGLEDTIISSRLRINIVGTTETDQGVTFGAKLRMQWDDGDAFAGTAGNAAQFWTSYNGVTVSVGNVDTAFDSVALTYDSEMGYEASSFGDAQSSFFAYNSKYDASGALDNYNGIAVTYSISGVNLYLSYVDPDQTVDSSLVTEEFGIAADWSNDMISLAAAYTTDAGGIVDNDIAFVGAAYKFNDAGTVGLNWYDNGLSTAGDQVTLYGNYAFGATTVRAYVSDIDRAGADTAYGIGADYQFAEGVKVSGSVQSGFANETVADVGVRFDF
>d1mal__ 6.7.1.2.1 Maltoporin (also LamB protein) [Escherichia coli]
VDFHGYARSGIGWTGSGGEQQCFQTTGAQSKYRLGNECETYAELKLGQEVWKEGDKSFYFDTNVAYSVAQQNDWEATDPAFREANVQGKNLIEWLPGSTIWAGKRFYQRHDVHMIDFYYWDISGPGAGLENIDVGFGKLSLAATRSSEAGGSSSFASNNIYDYTNETANDVFDVRLAQMEINPGGTLELGVDYGRANLRDNYRLVDGASKDGWLFTAEHTQSVLKGFNKFVVQYATDSMTSQGKGLSQGSGVAFDNEKFAYNINNNGHMLRILDHGAISMGDNWDMMYVGMYQDINWDNDNGTKWWTVGIRPMYKWTPIMSTVMEIGYDNVESQRTGDKNNQYKITLAQQWQAGDSIWSRPAIRVFATYAKWDEKWGYDYTGNADNNANFGKAVPADFNGGSFGRGDSDEWTFGAQMEIWW
>d2mpra_ 6.7.1.2.2 Maltoporin (also LamB protein) [Salmonella typhimurium</i]
VDFHGYARSGIGWTGSGGEQQCFQATGAQSKYRLGNECETYAELKLGQEVWKEGDKSFYFDTNVAYSVNQQNDWESTDPAFREANVQGKNLIEWLPGSTIWAGKRFYQRHDVHMIDFYYWDISGPGAGIENIDLGFGKLSLAATRSTEAGGSYTFSSQNIYDEVKDTANDVFDVRLAGLQTNPDGVLELGVDYGRANTTDGYKLADGASKDGWMFTAEHTQSMLKGYNKFVVQYATDAMTTQGKGQARGSDGSSSFTEKINYANKVINNNGNMWRILDHGAISLGDKWDLMYVGMYQNIDWDNNLGTEWWTVGVRPMYKWTPIMSTLLEVGYDNVKSQQTGDRNNQYKITLAQQWQAGDSIWSRPAIRIFATYAKWDEKWGYIKDGDNISRYAAATNSGISTNSRGDSDEWTFGAQMEIWW
>d1prea2 6.9.1.1.1 (84-449) (Pro)aerolysin, the pore-forming lobe [Aeromonas hydrophila]
IPTLSALDIPDGDEVDVQWRLVHDSANFIKPTSYLAHYLGYAWVGGNHSQYVGEDMDVTRDGDGWVIRGNNDGGCDGYRCGDKTAIKVSNFAYNLDPDSFKHGDVTQSDRQLVKTVVGWAVNDPQSGYDVTLRYDTATNWSKTNTYGLSEKVTTKNKFKWPLVGETELSIEIAANQSWASQNGGSTTTSLSQSVRPTVPARSKIPVKIELYKADISYPYEFKADVSYDLTLSGFLRWGGNAWYTHPDNRPNWNHTFVIGPYKDKASSIRYQWDKRYIPGEVKWWDWNWTIQQNGLSTMQNNLARVLRPVRAGITGDFSAESQFAGNIEIGAPVPLGLRLEIPLDAQELSGLGFNNVSLSVTPAANQ