>d3sdha_ 1.1.1.1.1 Hemoglobin I {Ark clam (Scapharca inaequivalvis)}
svydaaaqltadvkkdlrdswkvigsdkkgngvalmttlfadnqetigyfkrlgnvsqgm
andklrghsitlmyalqnfidqldnpddlvcvvekfavnhitrkisaaefgkingpikkv
lasknfgdkyanawaklvavvqaal
>d1b0b__ 1.1.1.1.2 Hemoglobin I {Clam (Lucina pectinata)}
lsaaqkdnvksswakasaawgtagpeffmalfdahddvfakfsglfsgaakgtvkntpem
aaqaqsfkglvsnwvdnldnagalegqcktfaanhkargisagqleaafkvlagfmksyg
gdegawtavagalmgmirpdm
>d2hbg__ 1.1.1.1.3 Glycera globin {Marine bloodworm (Glycera dibranchiata)}
glsaaqrqviaatwkdiagadngagvgkkclikflsahpqmaavfgfsgasdpgvaalga
kvlaqigvavshlgdegkmvaqmkavgvrhkgygnkhikaqyfeplgasllsamehrigg
kmnaaakdawaaayadisgalisglqs
>d1a6m__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgy
>d1mba__ 1.1.1.1.5 Myoglobin {Sea hare (Aplysia limacina)}
xslsaaeadlagkswapvfanknangldflvalfekfpdsanffadfkgksvadikaspk
lrdvssriftrlnefvnnaanagkmsamlsqfakehvgfgvgsaqfenvrsmfpgfvasv
aappagadaawtklfgliidalkaaga
>d1eco__ 1.1.1.1.13 Erythrocruorin {Midge (Chironomous thummi thummi), fraction III}
lsadqistvqasfdkvkgdpvgilyavfkadpsimakftqfagkdlesikgtapfethan
rivgffskiigelpnieadvntfvashkprgvthdqlnnfragfvsymkahtdfagaeaa
wgatldtffgmifskm
>d2gdm__ 1.1.1.1.14 Leghemoglobin {Yellow lupin (Lupinus luteus)}
galtesqaalvkssweefnanipkhthrffilvleiapaakdlfsflkgtsevpqnnpel
qahagkvfklvyeaaiqlevtgvvvtdatlknlgsvhvskgvadahfpvvkeailktike
vvgakwseelnsawtiaydelaivikkemddaa
>d1baba_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
xmelspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkgh
gkkvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeft
pavhasldkflasvstvltskyr
>d1cg5a_ 1.1.1.1.25 Hemoglobin, alpha-chain {Cartilaginous fish akaei (Dasyatis akajei)}
vlssqnkkaieelgnlikanaeawgadalarlfelhpqtktyfskfsgfeacneqvkkhg
krvmnaladathhldnlhlhledlarkhgenllvdphnfhlfadcivvtlavnlqaftpv
thcavdkflelvayelsscyr
>d1babb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1cg5b_ 1.1.1.1.39 Hemoglobin, beta-chain {Cartilaginous fish akaei (Dasyatis akajei)}
vklsedqehyikgvwkdvdhkqitakalervfvvypwttrlfsklqglfsandigvqqha
dkvqralgeaiddlkkveinfqnlsgkhqeigvdtqnfkllgqtfmvelalhykktfrpk
ehaaaykffrlvaealssnyh
>d2lhb__ 1.1.1.1.43 Lamprey globin {Sea lamprey (Petromyzon marinus)}
pivdtgsvaplsaaektkirsawapvystyetsgvdilvkfftstpaaqeffpkfkgltt
adelkksadvrwhaeriinavddavasmddtekmsmklrnlsgkhaksfqvdpeyfkvla
aviadtvaagdagfeklmsmicillrsay
>d1ash__ 1.1.1.1.44 Ascaris hemoglobin, domain 1 {Pig roundworm (Ascaris suum)}
anktrelcmkslehakvdtsnearqdgidlykhmfenypplrkyfksreeytaedvqndp
ffakqgqkillachvlcatyddretfnaytrelldrhardhvhmppevwtdfwklfeeyl
gkkttldeptkqawheigrefakeink
>d1itha_ 1.1.1.1.45 Hemoglobin {Innkeeper worm (Urechis caupo)}
gltaaqikaiqdhwflnikgclqaaadsiffkyltaypgdlaffhkfssvplyglrsnpa
ykaqtltvinyldkvvdalggnagalmkakvpshdamgitpkhfgqllklvggvfqeefs
adpttvaawgdaagvlvaamk
>d1hlb__ 1.1.1.1.46 Hemoglobin {Sea cucumber (Caudina (Molpadia) arenicola)}
xggtlaiqaqgdltlaqkkivrktwhqlmrnktsfvtdvfirifaydpsaqnkfpqmagm
sasqlrssrqmqahairvssimseyveeldsdilpellatlarthdlnkvgadhynlfak
vlmealqaelgsdfnektrdawakafsvvqavllvkhg
>d1cqxa1 1.1.1.1.48 (1-150) Flavohemoglobin, N-terminal domain {Alcaligenes eutrophus}
mltqktkdivkatapvlaehgydiikcfyqrmfeahpelknvfnmahqeqgqqqqalara
vyayaeniedpnslmavlkniankhaslgvkpeqypivgehllaaikevlgnaatddiis
awaqaygnladvlmgmeselyersaeqpgg
>d1ew6a_ 1.1.1.1.49 Dehaloperoxidase {Marine worm (Amphitrite ornata)}
gfkqdiatirgdlrtyaqdiflaflnkypderryfknyvgksdqelksmakfgdhtekvf
nlmmevadratdcvplasdantlvqmkqhsslttgnfeklfvalveymrasgqsfdsqsw
drfgknlvsalssagmk
>d1phna_ 1.1.1.2.1 Phycocyanin {Red alga (Cyanidium caldarium)}
mktpiteaiaaadnqgrflsntelqavngryqraaasleaarsltsnaerlingaaqavy
skfpytsqmpgpqyassavgkakcardigyylrmvtyclvvggtgpmdeyliagleeinr
tfdlspswyvealnyikanhglsgqaaneantyidyainals
>d1alla_ 1.1.1.2.3 Allophycocyanin {Spirulina platensis}
sivtksivnadaearylspgeldriksfvtsgerrvriaetmtgareriikqagdqlfgk
rpdvvspggnaygadmtatclrdldyylrlitygivagdvtpieeigvvgvremykslgt
pieaiaegvramksvatsllsgadaaeagsyfdyligams
>d1qgwc_ 1.1.1.2.7 Phycoerythrin {Rhodomonas cs 24}
dafsrvvtnadskaayvggadlqalkkfisegnkrldsvnsivsnascivsdavsgmice
npslispsgxcytnrrmaaclrdgeiilryvsyallsgdasvledrclnglketysslgv
pansnaravsimkacavafvnntasqkklstpqgdcsglasevggyfdkvtaais
>d1grj_1 1.2.1.1.1 (2-79) GreA transcript cleavage protein, N-terminal domain {Escherichia coli}
qaipmtlrgaeklreeldflksvrrpeiiaaiaearehgdlkenaeyhaareqqgfcegr
ikdieaklsnaqvidvtk
>d1hdj__ 1.2.2.1.1 HSP40 {Human (Homo sapiens)}
mgkdyyqtlglargasdeeikrayrrqalryhpdknkepgaeekfkeiaeaydvlsdprk
reifdrygeeglkgsgc
>d1xbl__ 1.2.2.1.2 DnaJ chaperone, N-terminal (J) domain {Escherichia coli}
akqdyyeilgvsktaeereirkaykrlamkyhpdrnqgdkeaeakfkeikeayevltdsq
kraaydqyghaafeq
>d1du2a_ 1.2.3.1.1 Theta subunit of DNA polymerase III {Escherichia coli}
mlknlakldqtemdkvnvdlaaagvafkerynmpviaeavereqpehlrswfrerliahr
lasvnlsrlpyepklk
>d1cxzb_ 1.2.4.1.1 Effector domain of the protein kinase pkn/prk1 {Human (Homo sapiens)}
wslleqlglagadlaapgvqqqlelererlrreirkelklkegaenlrrattdlgrslgp
velllrgssrrldllhqqlqelhahv
>d1seta1 1.2.5.1.1 (1-110) Seryl-tRNA synthetase (SerRS) {Thermus thermophilus, strain hb27}
mvdlkrlrqepevfhrairekgvaldleallaldrevqelkkrlqevqternqvakrvpk
appeekealiargkalgeeakrleealrekearlealllqvplppwpgap
>d1eiya1 1.2.5.2.1 (6-84) Phenylalanyl-tRNA synthetase (PheRS) {Thermus thermophilus}
laaiqnardleelkalkarylgkkglltqemkglsalpleerrkrgqelnaikaaleaal
earekaleeaalkealere
>d1a36a1 1.2.6.1.1 (641-712) Eukaryotic DNA topoisomerase I, dispensable insert domain {Human (Homo sapiens)}
eksmmnlqtkidakkeqladarrdlksakadakvmkdaktkkvveskkkavqrleeqlmk
levqatdreenk
>d1aqt_1 1.2.7.1.1 (87-136) Epsilon subunit of F1F0-ATP synthase C-terminal domain {Escherichia coli}
qdldearameakrkaeehissshgdvdyaqasaelakaiaqlrvieltkk
>d1bsha1 1.2.7.1.1 (87-138) Epsilon subunit of F1F0-ATP synthase C-terminal domain {Escherichia coli}
qdldearameakrkaeehissshgdvdyaqasaelakaiaqlrvieltkkam
>d1bsna1 1.2.7.1.1 (87-138) Epsilon subunit of F1F0-ATP synthase C-terminal domain {Escherichia coli}
qdldearameakrkaeehissshgdvdyaqasaelakaiaqlrvieltkkam
>d1isaa1 1.2.8.1.3 (1-82) Fe superoxide dismutase (FeSOD) {Escherichia coli}
sfelpalpyakdalaphisaetieyhygkhhqtyvtnlnnlikgtafegksleeiirsse
ggvfnnaaqvwnhtfywnclap
>d1coja1 1.2.8.1.4 (2-90) Fe superoxide dismutase (FeSOD) {Aquifex pyrophilus}
vhklepkdhlkpqnlegisneqiephfeahykgyvakyneiqekladqnfadrskanqny
seyrelkveetfnymgvvlhelyfgmltp
>d1b06a1 1.2.8.1.6 (3-92) Fe superoxide dismutase (FeSOD) {Sulfolobus acidocaldarius}
viqlkryefpqlpykvdalepyiskdiidvhynghhkgyvnganslldrleklikgdlpq
gqydlqgilrgltfninghklhaiywnnma
>d1ap6a1 1.2.8.1.7 (1-83) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaafvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1d5na1 1.2.8.1.8 (1-90) Mn superoxide dismutase (MnSOD) {Escherichia coli}
sytlpslpyaydalephfdkqtmeihhtkhhqtyvnnanaaleslpefanlpveelitkl
dqlpadkktvlrnnagghanhslfwkglkk
>d1mnga1 1.2.8.1.9 (1-92) Mn superoxide dismutase (MnSOD) {Thermus thermophilus}
pypfklpdlgypyealephidaktmeihhqkhhgayvtnlnaalekypylhgvevevllr
hlaalpqdiqtavrnnggghlnhslfwrlltp
>d1bsma1 1.2.8.1.10 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1qnna1 1.2.8.1.11 (1-84) Cambialistic superoxide dismutase {Porphyromonas gingivalis}
mthelislpyavdalapvisketvefhhgkhlktyvdnlnkliigtefenadlntivqks
eggifnnagqtlnhnlyftqfrpg
>d1c75a_ 1.3.1.1.1 Cytochrome c6 (synonym: cytochrome c553) {Bacillus pasteurii}
vdaeavvqqkcischggdltgasapaidkaganyseeeildiilngqggmpggiakgaea
eavaawlaekk
>d1ctj__ 1.3.1.1.2 Cytochrome c6 (synonym: cytochrome c553) {Monoraphidium braunii}
eadlalgkavfdgncaachagggnnvipdhtlqkaaieqfldggfnieaivyqiengkga
mpawdgrldedeiagvaayvydqaagnkw
>d1c53__ 1.3.1.1.3 Cytochrome c6 (synonym: cytochrome c553) {Desulfovibrio vulgaris, different strains}
adgaalykscvgchgadgskqamgvghavkgqkadelfkklkgyadgsyggekkavmtnl
vkrysdeemkamadymskl
>d1c6s__ 1.3.1.1.5 Cytochrome c6 (synonym: cytochrome c553) {Cyanobacterium (Synechococcus elongatus)}
adlangakvfsgncaachmgggnvvmanktlkkealeqfgmysedaiiyqvqhgknampa
fagrltdeqiqdvaayvldqaakgwag
>d1c52__ 1.3.1.1.7 Cytochrome c552 {Thermus thermophilus}
qadgakiyaqcagchqqngqgipgafpplaghvaeilakeggreylilvllyglqgqiev
kgmkyngvmssfaqlkdeeiaavlnhiatawgdakkvkgfkpftaeevkklrakkltpqq
vlaerkklglk
>d1cnoa_ 1.3.1.1.8 Cytochrome c552 {Pseudomonas nautica}
agdieagkakaavcaachgqngisqvpiypnlagqkeqylvaalkaykagqrqggqapvm
qgqatalsdadianlaayyasnpaaa
>d1ql3a_ 1.3.1.1.9 Cytochrome c552 {Paracoccus denitrificans}
adpaagekvfgkckachkldgndgvgphlngvvgrtvagvdgfnysdpmkahggdwtpea
lqefltnpkavvkgtkmafaglpkiedranliaylegqq
>d1ayg__ 1.3.1.1.10 Cytochrome c552 {Hydrogenobacter thermophilus}
neqlakqkgcmachdlkakkvgpayadvakkyagrkdavdylagkikkggsgvwgsvpmp
pqnvtdaeakqlaqwilsik
>d1a56__ 1.3.1.1.11 Cytochrome c552 {Nitrosomonas europaea}
dadlakknnciachqvetkvvgpalkdiaakyadkddaatylagkikggssgvwgqipmp
pnvnvsdadakaladwiltlk
>d1ycc__ 1.3.1.1.12 Mitochondrial cytochrome c {Baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdanikk
nvlwdennmseyltnpkkyipgtkmafgglkkekdrndlitylkkace
>d3c2c__ 1.3.1.1.17 Cytochrome c2 {Rhodospirillum rubrum}
egdaaagekvskkclachtfdqggankvgpnlfgvfentaahkdnyaysesytemkakgl
twteanlaayvknpkafvleksgdpkakskmtfkltkddeienviaylktlk
>d1cxc__ 1.3.1.1.19 Cytochrome c2 {Rhodobacter spaeroides}
qegdpeagakafnqcqtchvivddsgttiagrnaktgpnlygvvgrtagtqadfkgygeg
mkeagakglawdeehfvqyvqdptkflkeytgdakakgkmtfklkkeadahniwaylqqv
avrp
>d1co6a_ 1.3.1.1.20 Cytochrome c2 {Rhodopseudomonas viridis}
qdaasgeqvfkqclvchsigpgaknkvgpvlnglfgrhsgtiegfaysdanknsgitwte
evfreyirdpkakipgtkmifagvkdeqkvsdliayikqfnadgskk
>d1hroa_ 1.3.1.1.21 Cytochrome c2 {Rhodopila globiformis}
sappgdpvegkhlfhticitchtdikgankvgpslygvvgrhsgiepgynyseaniksgi
vwtpdvlfkyiehpqkivpgtkmgypgqpdpqkradiiayletlk
>d1cot__ 1.3.1.1.22 Cytochrome c2 {Paracoccus denitrificans}
dgdaakgekefnkckachmiqapdgtdiikggktgpnlygvvgrkiaseegfkygegile
vaeknpdltwteadlieyvtdpkpwlvkmtddkgaktkmtfkmgknqadvvaflaqnspd
a
>d1cc5__ 1.3.1.1.23 Cytochrome c5 {Azotobacter vinelandii}
gggarsgddvvakycnachgtgllnapkvgdsaawktradakggldgllaqslsglnamp
pkgtcadcsddelkaaigkmsgl
>d451c__ 1.3.1.1.25 Cytochrome c551 {Pseudomonas aeruginosa}
edpevlfknkgcvachaidtkmvgpaykdvaakfagqagaeaelaqrikngsqgvwgpip
mppnavsddeaqtlakwvlsqk
>d2mtac_ 1.3.1.1.26 Cytochrome c551 {Paracoccus denitrificans}
apqffniidgsplnfddameegrdteavkhfletgenvynedpeilpeaeelyagmcsgc
hghyaegkigpglndaywtypgnetdvglfstlyggatgqmgpmwgsltldemlrtmawv
rhlytgdpkdaswltdeqkagftpfqp
>d1gks__ 1.3.1.1.27 Cytochrome c551 {Ectothiorhodospira halophila}
dgesiyingtaptcsschdrgvagapelnapedwadrpssvdelvestlagkgampaydg
radredlvkaieymlstl
>d1dw0a_ 1.3.1.1.29 SHP, an oxygen binding cytochrome c {Rhodobacter sphaeroides}
gdtspaqliagyeaaagapadaergralflstqtggkpdtpscttchgadvtragqtrtg
keiaplapsatpdrftdsarvekwlgrncnsvigrdctpgekadllawlaaq
>d1diqc_ 1.3.1.1.30 p-Cresol methylhydroxylase, cytochrome c subunit {Pseudomonas putida}
sqwgsgknlydkvcghchkpevgvgpvlegrglpeayikdivrngframpafpasyvdde
sltqvaeylsslpa
>d1qksa1 1.3.1.2.3 (9-135) N-terminal (heme c) domain of cytochrome cd1-nitrite reductase {Paracoccus denitrificans}
dpaaaledhktrtdnryepsldnlaqqdvaapgapegvtalsdaqyneankiyfercagc
hgvlrkgatgkaltpdltrdlgfdylqsfityaspagmpnwgtsgelsaeqvdlmanyll
ldpaapp
>d1etpa1 1.3.1.3.1 (1-92) Cytochrome c4 {Pseudomonas stutzeri}
agdaeagqgkvavcgachgvdgnspapnfpklagqgeryllkqlqdikagstpgapegvg
rkvlemtgmldplsdqdlediaayfssqkgsv
>d1etpa2 1.3.1.3.1 (93-190) Cytochrome c4 {Pseudomonas stutzeri}
gyadpalakqgeklfrggkldqgmpactgchapngvgndlagfpklggqhaaytakqltd
fregnrtndgdtmimrgvaaklsnkdiealssyiqglh
>d1fcdc1 1.3.1.3.2 (1-80) Flavocytochrome c sulfide dehydrogenase, FCSD, cytochrome subunit {Purple phototrophic bacterium (Cromatium vinosum)}
eptaemltnncagchgthgnsvgpaspsiaqmdpmvfvevmegfksgeiastimgriakg
ystadfekmagyfkqqtyqp
>d1fcdc2 1.3.1.3.2 (81-174) Flavocytochrome c sulfide dehydrogenase, FCSD, cytochrome subunit {Purple phototrophic bacterium (Cromatium vinosum)}
akqsfdtaladtgaklhdkycekchveggkpladeedyhilagqwtpylqyamsdfreer
rpmekkmasklrellkaegdagldalfafyasqq
>d1enh__ 1.4.1.1.1 Engrailed Homeodomain {Drosophila melanogaster}
rprtafsseqlarlkrefnenrylterrrqqlsselglneaqikiwfqnkraki
>d1hddc_ 1.4.1.1.1 Engrailed Homeodomain {Drosophila melanogaster}
rprtafsseqlarlkrefnenrylterrrqqlsselglneaqikiwfqnkrakikks
>d2hdda_ 1.4.1.1.1 Engrailed Homeodomain {Drosophila melanogaster}
rtafsseqlarlkrefnenrylterrrqqlsselglneaqikiwfknkrakikks
>d2hddb_ 1.4.1.1.1 Engrailed Homeodomain {Drosophila melanogaster}
krprtafsseqlarlkrefnenrylterrrqqlsselglneaqikiwfknkrakik
>d3hdda_ 1.4.1.1.1 Engrailed Homeodomain {Drosophila melanogaster}
rtafsseqlarlkrefnenrylterrrqqlsselglneaqikiwfqnkrakikks
>d3hddb_ 1.4.1.1.1 Engrailed Homeodomain {Drosophila melanogaster}
rprtafsseqlarlkrefnenrylterrrqqlsselglneaqikiwfqnkrakikk
>d1akha_ 1.4.1.1.2 Mating type protein A1 Homeodomain {Baker's yeast (Saccharomyces cerevisiae)}
ispqarafleevfrrkqslnskekeevakkcgitplqvrvwfinkrmrs
>d1yrna_ 1.4.1.1.2 Mating type protein A1 Homeodomain {Baker's yeast (Saccharomyces cerevisiae)}
ispqarafleqvfrrkqslnskekeevakkcgitplqvrvwfinkrmrs
>d1mnmc_ 1.4.1.1.3 mat alpha2 Homeodomain {Baker's yeast (Saccharomyces cerevisiae)}
glvfnvvtqdminkstkpyrghrftkenvrileswfaknienpyldtkglenlmkntsls
riqiknwvsnrrrkekt
>d1lfb__ 1.4.1.1.4 Transcription factor LFB1 {Rat (Rattus rattus)}
rfkwgpasqqilfqayerqknpskeeretlveecnraeciqrgvspsqaqglgsnlvtev
rvynwfanrrkeeafrhk
>d1octc1 1.4.1.1.5 (102-161) Oct-1 POU Homeodomain {Human (Homo sapiens)}
rkkrtsietnirvaleksflenqkptseeitmiadqlnmekevirvwfcnrrqkekrinp
>d1au7a1 1.4.1.1.6 (103-160) Pit-1 POU homeodomain {Rat (Rattus norvegicus)}
krrttisiaakdalerhfgehskpssqeimrmaeelnlekevvrvwfcnrrqrekrvk
>d1ftt__ 1.4.1.1.7 Thyroid transcription factor 1 homeodomain {Rat (Rattus rattus)}
mrrkrrvlfsqaqvyelerrfkqqkylsaperehlasmihltptqvkiwfqnhrykmkrq
akdkaaqq
>d1hdp__ 1.4.1.1.8 Oct-2 POU Homeodomain {Human (Homo sapiens)}
rrkkrtsietnvrfaleksflanqkptseeilliaeqlhmekevirvwfcnrrqkekrin
pcs
>d1ocp__ 1.4.1.1.9 Oct-3 POU Homeodomain {Mouse (Mus musculus)}
metlvqarkrkrtsienrvrwsletmflkcpkpslqqithianqlglekdvvrvwfcnrr
qkgkrss
>d1b72a_ 1.4.1.1.10 Homeobox protein hox-b1 {Human (Homo sapiens)}
artfdwmkvkrnppktakvsepglgspsglrtnfttrqltelekefhfnkylsrarrvei
aatlelnetqvkiwfqnrrmkqkkrere
>d1b72b_ 1.4.1.1.11 pbx1 {Human (Homo sapiens)}
rkrrnfnkqateilneyfyshlsnpypseeakeelakkcgitvsqvsnwfgnkrirykkn
igkfqeeaniyaa
>d1bw5__ 1.4.1.1.12 Insulin gene enhancer protein isl-1 {Rat (Rattus norvegicus)}
mkttrvrtvlnekqlhtlrtcyaanprpdalmkeqlvemtglsprvirvwfqnkrckdkk
rsimmk
>d9anta_ 1.4.1.1.13 Antennapedia Homeodomain {Drosophila melanogaster}
rqtytryqtlelekefhfnryltrrrrieiahalslterqikiwfqnrrmkwkken
>d1b8ia_ 1.4.1.1.14 Ultrabithorax (ubx) homeodomain {Drosophila melanogaster}
fypwmaiagtnglrrrgrqtytryqtlelekefhtnhyltrrrriemahalslterqiki
wfqnrrmklkkei
>d1ftz__ 1.4.1.1.16 Fushi Tarazu protein {Fruit fly (Drosophila melanogaster)}
mdskrtrqtytryqtlelekefhfnryitrrrridianalslserqikiwfqnrrmkskk
drtldsspeh
>d1nk3p_ 1.4.1.1.17 VND/NK-2 protein {Fruit fly (Drosophila melanogaster)}
kkrkrrvlftkaqtyelerrfrqqrylsaperehlaslirltptqvkiwfqnhryktkra
qne
>d1fjla_ 1.4.1.1.18 Paired protein {Fruit fly (Drosophila melanogaster)}
kqrrsrttfsasqldelerafertqypdiytreelaqrtnlteariqvwfqnrrarlrkq
htsvs
>d1hcra_ 1.4.1.2.1 HIN recombinase (DNA-binding domain) {Synthetic}
grprainkheqeqisrllekghprqqlaiifgigvstlyryfpassikkrmn
>d1gdta1 1.4.1.2.2 (141-183) gamma,delta resolvase (C-terminal domain) {Escherichia coli}
grkrkidrdavlnmwqqglgashisktmniarstvykvinesn
>d1gdtb1 1.4.1.2.2 (141-183) gamma,delta resolvase (C-terminal domain) {Escherichia coli}
grkrkidrdavlnmwqqglgashisktmniarstvykvinesn
>d1res__ 1.4.1.2.2 gamma,delta resolvase (C-terminal domain) {Escherichia coli}
grkrkidrdavlnmwqqglgashisktmniarstvykvinesn
>d1ret__ 1.4.1.2.2 gamma,delta resolvase (C-terminal domain) {Escherichia coli}
grkrkidrdavlnmwqqglgashisktmniarstvykvinesn
>d1tc3c_ 1.4.1.2.3 Transposase tc3a1-65 {Caenorhabditis elegans}
prgsalsdteraqldvmkllnvslhemsrkisrsrhcirvylkdpvsygts
>d2ezl__ 1.4.1.2.4 Ibeta subdomain of the mu end DNA-binding domain of phage mu transposase {Bacteriophage mu}
miarptleahdydrealwskwdnasdsqrrlaekwlpavqaademlnqgistktafatva
ghyqvsastlrdkyyqvqkfakpdwaaalvdgrgasrrn
>d2ezi__ 1.4.1.2.5 Transposase {Bacteriophage mu}
mnvhksefdedawqfliadylrpekpafrkcyerlelaarehgwsipsratafrriqqld
eamvvacregehalm
>d1idz__ 1.4.1.3.2 c-Myb, DNA-binding domain {Mouse (Mus musculus)}
mevkktswteeedrilyqahkrlgnrwaeiakllpgrtdnaiknhwnstmrrkv
>d1mbf__ 1.4.1.3.2 c-Myb, DNA-binding domain {Mouse (Mus musculus)}
lgktrwtreedeklkklveqngtddwkvianylpnrtdvqcqhrwqkvlnpe
>d1mbg__ 1.4.1.3.2 c-Myb, DNA-binding domain {Mouse (Mus musculus)}
likgpwtkeedqrvielvqkygpkrwsviakhlkgrigkqcrerwhnhlnpe
>d1mbj__ 1.4.1.3.2 c-Myb, DNA-binding domain {Mouse (Mus musculus)}
vkktswteeedriiyqahkrlgnrwaeiakllpgrtdnaiknhwnstmrrkv
>d1mbk__ 1.4.1.3.2 c-Myb, DNA-binding domain {Mouse (Mus musculus)}
vkktswteeedriiyqahkrlgnrwaeiakllpgrtdnaiknhwnstmrrkv
>d1msec2 1.4.1.3.2 (144-193) c-Myb, DNA-binding domain {Mouse (Mus musculus)}
ktswteeedriiyqahkrlgnrwaeiakllpgrtdnaiknhwnstmrrkv
>d1msfc2 1.4.1.3.2 (144-193) c-Myb, DNA-binding domain {Mouse (Mus musculus)}
ktswteeedriiyqahkrlgnrwaeiakllpgrtdnaiknhwnstmrrkv
>d1a5j_1 1.4.1.3.3 (1-55) b-Myb DNA binding domain {Chicken (Gallus gallus)}
gipdlvkgpwtkeedqkvielvkkygtkqwtliakhlkgrlgkqcrerwhnhlnp
>d1a5j_2 1.4.1.3.3 (56-110) b-Myb DNA binding domain {Chicken (Gallus gallus)}
evkksswteeedriifeahkvlgnrwaeiakllpgrtdnavknhwnstikrkvdt
>d1ba5__ 1.4.1.4.1 DNA-binding domain of human telomeric protein, htrf1 {Human (Homo sapiens)}
rkrqawlweedknlrsgvrkygegnwskillhykfnnrtsvmlkdrwrtmkkl
>d1pdnc_ 1.4.1.5.2 Paired protein (prd) {Fruit fly (Drosophila melanogaster)}
qgrvnqlggvfingrplpnnirlkivemaadgirpcvisrqlrvshgcvskilnryqetg
sirpgviggskpriatpeienrieeykrsspgmfsweirekliregvcdrstapsvsais
rlv
>d1igna1 1.4.1.6.1 (360-445) DNA-binding domain of rap1 {Baker's yeast (Saccharomyces cerevisiae)}
kasftdeedefildvvrknptrrtthtlydeishyvpnhtgnsirhrfrvylskrleyvy
evdkfgklvrdddgnliktkvlppsi
>d1igna2 1.4.1.6.1 (446-594) DNA-binding domain of rap1 {Baker's yeast (Saccharomyces cerevisiae)}
krkfsadedytlaiavkkqfyrdlfqidpdtgrslitdedtptaiarrnmtmdpnhvpgs
epnfaayrtqsrrgpiareffkhfaeehaahtenawrdrfrkfllaygiddyisyyeaek
aqnrepepmknltnrpkrpgvptpgnyns
>d1bw6a_ 1.4.1.7.1 DNA-binding domain of centromere binding protein B (CENP-B) {Human (Homo sapiens)}
mgpkrrqltfreksriiqeveenpdlrkgeiarrfnippstlstilknkrailase
>d1bl0a1 1.4.1.8.1 (9-62) MarA {Escherichia coli}
daitihsildwiednlesplslekvsersgyskwhlqrmfkketghslgqyirs
>d1bl0a2 1.4.1.8.1 (63-124) MarA {Escherichia coli}
rkmteiaqklkesnepilylaerygfesqqtltrtfknyfdvpphkyrmtnmqgesrflh
pl
>d1d5ya1 1.4.1.8.2 (3-56) Rob transcription factor, N-terminal domain {Escherichia coli}
qagiirdlliwleghldqplsldnvaakagyskwhlqrmfkdvtghaigayira
>d1d5ya2 1.4.1.8.2 (57-121) Rob transcription factor, N-terminal domain {Escherichia coli}
rrlsksavalrltarpildialqyrfdsqqtftrafkkqfaqtpalyrrspewsafgirp
plrlg
>d1sfe_1 1.4.2.1.1 (93-176) Ada DNA repair protein {Escherichia coli}
gtafqqqvwqalrtipcgetvsyqqlanaigkpkavravasacaanklaivipchrvvrg
dgslsgyrwgvsrkaqllrreaen
>d1qnta1 1.4.2.1.2 (92-176) O6-alkylguanine-DNA alkyltransferase {Human (Homo sapiens)}
esftrqvlwkllkvvkfgevisyqqlaalagnpkaaravggamrgnpvpilipchrvvcs
sgavgnysgglavkewllaheghrl
>d1mgta1 1.4.2.1.3 (89-169) O6-alkylguanine-DNA alkyltransferase {Pyrococcus kodakaraensis}
vtpfekkvyewltknvkrgsvitygdlakalntspravggamkrnpypivvpchrvvahd
gigyyssgieekkflleiegv
>d1c20a_ 1.4.3.1.1 DNA-binding domain from the dead ringer protein {Fruit fly (Drosophila melanogaster)}
gwsfeeqfkqvrqlyeinddpkrkeflddlfsfmqkrgtpinrlpimaksvldlyelynl
viargglvdvinkklwqeiikglhlpssitsaaftlrtqymkylypyecekknlstpael
qaaidgnr
>d1f1za1 1.4.4.1.1 (169-267) TnsA endonuclease, C-terminal domain {Escherichia coli}
npvvkeniewlysvkteevsaellaqlsplahilqekgdeniinvckqvdiaydlelgkt
lseiraltangfikfniyksfrankcadlcisqvvnmee
>d1bia_1 1.4.5.1.1 (1-63) Biotin repressor, N-terminal domain {Escherichia coli}
mkdntvplkliallangefhsgeqlgetlgmsraainkhiqtlrdwgvdvftvpgkgysl
pep
>d1lea__ 1.4.5.2.1 LexA repressor, N-terminal DNA-binding domain {Escherichia coli}
mkaltarqqevfdlirdhisqtgmpptraeiaqrlgfrspnaaeehlkalarkgvieivs
gasrgirllqee
>d1aoy__ 1.4.5.3.1 Arginine repressor (ArgR), N-terminal DNA-binding domain {Escherichia coli}
mrssakqeelvkafkallkeekfssqgeivaalqeqgfdninqskvsrmltkfgavrtrn
akmemvyclpaelgvptt
>d1b4aa1 1.4.5.3.2 (4-78) Arginine repressor (ArgR), N-terminal DNA-binding domain {Bacillus stearothermophilus}
gqrhikireiimsndietqdelvdrlreagfnvtqatvsrdikemqlvkvpmangrykys
lpsdqrfnplqklkr
>d2cgpa1 1.4.5.4.1 (138-207) Catabolite gene activator protein (CAP), C-terminal domain {Escherichia coli}
dvtgriaqtllnlakqpdamthpdgmqikitrqeigqivgcsretvgrilkmledqnlis
ahgktivvyg
>d1opc__ 1.4.5.5.1 OmpR, C-terminal DNA-binding domain {Escherichia coli}
viafgkfklnlgtremfredepmpltsgefavlkalvshpreplsrdklmnlargreysa
mersidvqisrlrrmveedpahpryiqtvwglgyvfvpd
>d1qqia_ 1.4.5.5.2 PhoB {Escherichia coli}
maveeviemqglsldptshrvmageeplemgptefkllhffmthpervysreqllnhvwg
tnvyvedrtvdvhirrlrkalepgghdrmvqtvrgtgyrfstrf
>d1smta_ 1.4.5.6.1 SmtB repressor {Cyanobacteria (Synechococcus), pcc7942}
elqaiapevaqslaeffavladpnrlrllsllarselcvgdlaqaigvsesavshqlrsl
rnlrlvsyrkqgrhvyyqlqdhhivalyqnaldhlqec
>d1bm9a_ 1.4.5.7.1 Replication terminator protein (RTP) {Bacillus subtilis}
eekrsstgflvkqraflklymitmteqerlyglkllevlrsefkeigfkpnhtevyrslh
ellddgilkqikvkkegaklqevvlyqfkdyeaaklykkqlkveldrckkliekalsdnf
>d1b9ma1 1.4.5.8.1 (-1-126) N-terminal domain of molybdate-dependent transcriptional regulator ModE {Escherichia coli}
hxqaeilltlklqqklfadprrisllkhialsgsisqgakdagisyksawdainexnqls
ehilveratggkggggavltrygqrliqlydllaqiqqkafdvlsdddalplnsllaais
rfslqts
>d1bjaa_ 1.4.5.9.1 Transcription factor MotA, activation domain {Bacteriophage T4}
skvtyiikasndvlnektatilitiakkdfitaaevrevhpdlgnavvnsnigvlikkgl
veksgdgliitgeaqdiisnaatlyaqenapellk
>d1repc1 1.4.5.10.1 (15-143) RepE54 {Escherichia coli mini-F plasmid}
sprivqsndlteaayslsrdqkrmlylfvdqirksdgtlqehdgiceihvakyaeifglt
saeaskdirqalksfagkevvfyrpeedagdekgyesfpwfikpahspsrglysvhinpy
lipffiglq
>d1repc2 1.4.5.10.1 (144-246) RepE54 {Escherichia coli mini-F plasmid}
nrftqfrlsetkeitnpyamrlyeslcqyrkpdgsgivslkidwiieryqlpqsyqrmpd
frrrflqvcvneinsrtpmrlsyiekkkgrqtthivfsfrdit
>d2foka1 1.4.5.11.1 (5-143) Restriction endonuclease FokI, N-terminal (recognition) domain {Flavobacterium okeanokoites}
irtfgwvqnpgkfenlkrvvqvfdrnskvhnevknikiptlvkeskiqkelvaimnqhdl
iytykelvgtgtsirseapcdaiiqatiadqgnkkgyidnwssdgflrwahalgfieyin
ksdsfvitdvglaysksad
>d2foka2 1.4.5.11.1 (144-286) Restriction endonuclease FokI, N-terminal (recognition) domain {Flavobacterium okeanokoites}
gsaiekeilieaissyppairiltlledgqhltkfdlgknlgfsgesgftslpegilldt
lanampkdkgeirnnwegssdkyarmiggwldklglvkqgkkefiiptlgkpdnkefish
afkitgeglkvlrrakgstkftr
>d2foka3 1.4.5.11.1 (287-386) Restriction endonuclease FokI, N-terminal (recognition) domain {Flavobacterium okeanokoites}
vpkrvywemlatnltdkeyvrtrralileilikagslkieqiqdnlkklgfdevietien
dikglintgifieikgrfyqlkdhilqfvipnrlgkpdlv
>d1hsta_ 1.4.5.12.1 Histone H5, globular domain {Chicken (Gallus gallus)}
shptysemiaaairaeksrggssrqsiqkyikshykvghnadlqiklsirrllaagvlkq
tkgvgasgsfrlak
>d1ghc__ 1.4.5.12.2 Histone H1, globular domain {Chicken (Gallus gallus)}
magpsvtelitkavsaskerkglslaalkkalaaggydveknnsriklglkslvskgtlv
qtkgtgasgsfrlsk
>d2hfh__ 1.4.5.14.1 Genesis {Rat (Rattus norvegicus)}
mvkppysyialitmailqspqkkltlsgicefisnrfpyyrekfpawqnsirhnlslndc
fvkiprepgnpgkgnywtldpqsedmfdngsfl
>d2bby__ 1.4.5.15.1 DNA-binding domain from rap30 {Human (Homo sapiens)}
raradkqhvldmlfsafekhqyynlkdlvditkqpvvylkeilkeigvqnvkgihkntwe
lkpeyrhyq
>d1cf7a_ 1.4.5.16.1 Cell cycle transcription factor e2f-dp {Human (Homo sapiens)}
srhekslgllttkfvsllqeakdgvldlklaadtlavrqkrriyditnvlegigliekks
knsiqwk
>d1cf7b_ 1.4.5.16.1 Cell cycle transcription factor e2f-dp {Human (Homo sapiens)}
gkglrhfsmkvcekvqrkgttsynevadelvseftnsnnhlaadsaydqknirrrvydal
nvlmamniiskekkeikwiglp
>d1d8ja_ 1.4.5.17.1 The central core domain of TFIIE beta {Human (Homo sapiens)}
alsgssgykfgvlakivnymktrhqrgdthpltldeildetqhldiglkqkqwlmtealv
nnpkievidgkyafkpkynvr
>d1qbja_ 1.4.5.18.1 Z-alpha domain of dsRNA-specific adenosine deaminase, ADAR1 {Human (Homo sapiens)}
siyqdqeqrilkfleelgegkattahdlsgklgtpkkeinrvlyslakkgklqkeagtpp
lwkia
>d1dp7p_ 1.4.5.19.1 MHC class II transcription factor RFX1 {Human (Homo sapiens)}
tvqwlldnyetaegvslprstlynhyllhsqeqklepvnaasfgklirsvfmglrtrrlg
trgnskyhyyglrika
>d1puee_ 1.4.5.20.4 Transcription factor PU.1, residues 171-259 {Murine (Mus musculus)}
kirlyqflldllrsgdmkdsiwwvdkdkgtfqfsskhkealahrwgiqkgnrkkmtyekm
aralrnygktgevkkvkkkltyqfsgev
>d1awca_ 1.4.5.20.5 GA binding protein (GABP) alpha {Mouse (Mus musculus)}
iqlwqfllelltdkdardciswvgdegefklnqpelvaqkwgqrknkptmnyeklsralr
yyydgdmickvqgkrfvykfvcdlktligysaaelnrlvieceqkklarm
>d1bc8c_ 1.4.5.20.6 Serum responce factor accessory protein 1a, SAP-1 {Human (Homo sapiens)}
mdsaitlwqfllqllqkpqnkhmicwtsndgqfkllqaeevarlwgirknkpnmnydkls
ralryyyvkniikkvngqkfvykfvsypeilnm
>d1hks__ 1.4.5.21.1 Heat-shock transcription factor {Drosophila melanogaster}
gsgvpaflaklwrlvddadtnrlicwtkdgqsfviqnqaqfakellplnykhnnmasfir
qlnmygfhkitsidngglrfdrdeiefshpffkrnspflldqikrk
>d2hts__ 1.4.5.21.2 Heat-shock transcription factor {Milk yeast (Kluyveromyces lactis)}
arpafvnklwsmvndksnekfihwstsgesivvpnrerfvqevlpkyfkhsnfasfvrql
nmygwhkvqdvksgsndsrwefenerha
>d2irfg_ 1.4.5.22.3 Interferon regulatory factor-2, IRF-2 {Mouse (Mus musculus)}
rmrmrpwleeqinsntipglkwlnkekkifqipwmhaarhgwdvekdaplfrnwaihtgk
hqpgidkpdpktwkanfrcamnslpdieevkdrsikkgnnafrvyrmlp
>d1bi1_1 1.4.5.23.1 (4-64) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
lvdttemylrtiyeleeegvtplrariaerleqsgptvsqtvarmerdglvvvasdrslq
m
>d1b1ba1 1.4.5.23.2 (1-64) Iron-dependent regulator {Mycobacterium tuberculosis}
mnelvdttemylrtiydleeegvtplrariaerldqsgptvsqtvsrmerdgllrvagdr
hlel
>d1xgsa1 1.4.5.24.1 (195-271) Methionine aminopeptidase, insert domain {Pyrococcus furiosus}
gqvievpptliymyvrdvpvrvaqarfllakikreygtlpfayrwlqndmpegqlklalk
tlekagaiygypvlkei
>d1b6a_1 1.4.5.24.2 (375-448) Methionine aminopeptidase, insert domain {Human (Homo sapiens)}
hddmecshymknfdvghvpirlprtkhllnvinenfgtlafcrrwldrlgeskylmalkn
lcdlgivdpypplc
>d1qpma_ 1.4.5.25.1 mu transposase, DNA-binding domain {Bacteriophage mu}
ksiwcspqeimaadgmpgsvagvhyranvqgwtkrkkegvkggkaveydvmsmptkereq
viahlglst
>d1tns__ 1.4.5.25.1 mu transposase, DNA-binding domain {Bacteriophage mu}
melwvspkelanlpglpktsagviyvakkqgwqnrtragvkggkaieynanslpveakaa
lllrqgeietslgyfe
>d1qa6a_ 1.4.6.1.1 Ribosomal protein L11, C-terminal domain {Bacillus stearothermophilus}
ktppaavllkkaagiesgsgepnrnkvatikrdkvreiaelkmpdlnaasieaamrmieg
tarsmgi
>d1mmsa1 1.4.6.1.2 (71-140) Ribosomal protein L11, C-terminal domain {Thermotoga maritima}
ktppasfllkkaagiekgssepkrkivgkvtrkqieeiaktkmpdlnansleaamkiieg
taksmgievv
>d1wjaa_ 1.4.7.1.1 N-terminal Zn binding domain of HIV integrase {Human immunodeficiency virus, type 1, HIV-1}
fldgidkaqeehekyhsnwramasdfnlppvvakeivascdkcqlkg
>d1wjab_ 1.4.7.1.1 N-terminal Zn binding domain of HIV integrase {Human immunodeficiency virus, type 1, HIV-1}
fldgidkaqeehekyhsnwramasdfnlppvvakeivascdkcqlkg
>d1wjba_ 1.4.7.1.1 N-terminal Zn binding domain of HIV integrase {Human immunodeficiency virus, type 1, HIV-1}
fldgidkaqeehekyhsnwramasdfnlppvvakeivascdkcqlkgeamhgqvd
>d1wjca_ 1.4.7.1.1 N-terminal Zn binding domain of HIV integrase {Human immunodeficiency virus, type 1, HIV-1}
fldgidkaqeehekyhsnwramasdfnlppvvakeivascdkcqlkg
>d1wjcb_ 1.4.7.1.1 N-terminal Zn binding domain of HIV integrase {Human immunodeficiency virus, type 1, HIV-1}
fldgidkaqeehekyhsnwramasdfnlppvvakeivascdkcqlkg
>d1wjea_ 1.4.7.1.1 N-terminal Zn binding domain of HIV integrase {Human immunodeficiency virus, type 1, HIV-1}
fldgidkaqeecekyhsnwramasdfnlppvvakeivascdkcqlk
>d1wjeb_ 1.4.7.1.1 N-terminal Zn binding domain of HIV integrase {Human immunodeficiency virus, type 1, HIV-1}
fldgidkaqeecekyhsnwramasdfnlppvvakeivascdkcqlk
>d1aub__ 1.4.7.1.2 N-terminal Zn binding domain of HIV integrase {Human immunodeficiency virus, type 2, HIV-2}
flekiepaqeehekyhsnvkelshkfgipnlvarqivnscaqcqqk
>d1ef4a_ 1.4.8.1.1 RNA polymerase subunit RPB10 {Methanobacterium thermoautotrophicum}
mipvrclscgkpvsayfneyqrrvadgedpkdvlddlglkryccrrmlishvetw
>d1bdxa1 1.5.1.1.1 (156-203) DNA helicase RuvA subunit, C-terminal domain {Escherichia coli}
tddaeqeavaalvalgykpqeasrmvskiarpdassetlirealraal
>d1bdxb1 1.5.1.1.1 (156-203) DNA helicase RuvA subunit, C-terminal domain {Escherichia coli}
tddaeqeavaalvalgykpqeasrmvskiarpdassetlirealraal
>d1bdxc1 1.5.1.1.1 (156-203) DNA helicase RuvA subunit, C-terminal domain {Escherichia coli}
tddaeqeavaalvalgykpqeasrmvskiarpdassetlirealraal
>d1bdxd1 1.5.1.1.1 (156-203) DNA helicase RuvA subunit, C-terminal domain {Escherichia coli}
tddaeqeavaalvalgykpqeasrmvskiarpdassetlirealraal
>d1cuk_1 1.5.1.1.1 (156-203) DNA helicase RuvA subunit, C-terminal domain {Escherichia coli}
tddaeqeavarlvalgykpqeasrmvskiarpdassetlirealraal
>d1hjp_1 1.5.1.1.1 (158-203) DNA helicase RuvA subunit, C-terminal domain {Escherichia coli}
daeqeavaalvalgykpqeasrmvskiarpdassetlirealraal
>d1bvsa1 1.5.1.1.2 (148-203) DNA helicase RuvA subunit, C-terminal domain {Mycobacterium leprae}
navrgsvvealvglgfaakqaeeatdqvldgelgkdgavatssalraalsllgktr
>d1bvsb1 1.5.1.1.2 (147-203) DNA helicase RuvA subunit, C-terminal domain {Mycobacterium leprae}
gnavrgsvvealvglgfaakqaeeatdqvldgelgkdgavatssalraalsllgktr
>d1bvsc1 1.5.1.1.2 (148-203) DNA helicase RuvA subunit, C-terminal domain {Mycobacterium leprae}
navrgsvvealvglgfaakqaeeatdqvldgelgkdgavatssalraalsllgktr
>d1bvsd1 1.5.1.1.2 (147-203) DNA helicase RuvA subunit, C-terminal domain {Mycobacterium leprae}
gnavrgsvvealvglgfaakqaeeatdqvldgelgkdgavatssalraalsllgktr
>d1bvse1 1.5.1.1.2 (148-203) DNA helicase RuvA subunit, C-terminal domain {Mycobacterium leprae}
navrgsvvealvglgfaakqaeeatdqvldgelgkdgavatssalraalsllgktr
>d1bvsf1 1.5.1.1.2 (147-203) DNA helicase RuvA subunit, C-terminal domain {Mycobacterium leprae}
gnavrgsvvealvglgfaakqaeeatdqvldgelgkdgavatssalraalsllgktr
>d1bvsg1 1.5.1.1.2 (148-203) DNA helicase RuvA subunit, C-terminal domain {Mycobacterium leprae}
navrgsvvealvglgfaakqaeeatdqvldgelgkdgavatssalraalsllgktr
>d1bvsh1 1.5.1.1.2 (147-203) DNA helicase RuvA subunit, C-terminal domain {Mycobacterium leprae}
gnavrgsvvealvglgfaakqaeeatdqvldgelgkdgavatssalraalsllgktr
>d1dv0a_ 1.5.2.1.1 C-terminal UBA domain of DNA repair protein {Human (Homo sapiens)}
qekeaierlkalgfpeslviqayfaceknenlaanfllsqnfdde
>d1aua_1 1.5.3.1.1 (4-96) N-terminal domain of phosphatidylinositol transfer protein sec14p {Baker's yeast (Saccharomyces cerevisiae)}
qqekeflesypqncppdalpgtpgnldsaqekalaelrklledagfierlddstllrflr
arkfdvqlakemfencekwrkdygtdtilqdfh
>d1enwa_ 1.5.4.1.1 Elongation factor TFIIS domain 2 {Yeast (Saccharomyces cerevisiae)}
gshmprnskndgvdtaiyhhklrdqvlkalydvlakesehppqsilhtakaiesemnkvn
ncdtneaaykaryriiysnvisknnpdlkhkiangditpeflatcdakdlapap
>d1pysb1 1.6.1.1.1 (1-38,152-190) Domains B1 and B5 of PheRS-beta, PheT {Thermus thermophilus (Thermus aquaticus)}
mrvpfswlkayvpelespevleerlaglgfetdriervXeevvldlevtpnrpdalgllg
lardlhalgyalvepeaa
>d1pysb2 1.6.1.1.1 (400-474) Domains B1 and B5 of PheRS-beta, PheT {Thermus thermophilus (Thermus aquaticus)}
ppeaipfrpeyanrllgtsypeaeqiailkrlgcrvegegptyrvtppshrldlrleedl
veevariqgyetipl
>d1d4ua1 1.6.1.2.1 (37-111) DNA repair factor XPA DNA- and RPA-binding domain, C-terminal subdomain {Human (Homo sapiens)}
dkhklitkteakqeyllkdcdlekrepplkfivkknphhsqwgdmklylklqivkrslev
wgsqealeeakevrq
>d2spca_ 1.7.1.1.1 Spectrin {Fruit fly (Drosophila melanogaster)}
qnldlqlymrdcelaeswmsareaflnadddanaggnvealikkhedfdkaingheqkia
alqtvadqliaqnhyasnlvdekrkqvlerwrhlkegliekrsrlgd
>d1cuna1 1.7.1.1.2 (7-115) Spectrin {Chicken (Gallus gallus)}
mvhqffrdmddeeswikekkllvssedygrdltgvqnlrkkhkrleaelaahepaiqsvl
dtgkklsddntigkeeiqqrlaqfvdhwkelkqlaaargqrleesleyq
>d1cuna2 1.7.1.1.2 (116-219) Spectrin {Chicken (Gallus gallus)}
qfvanveeeeawinekmtlvasedygdtlaaiqgllkkheafetdftvhkdrvndvcang
edlikknnhhvenitakmkglkgkvsdlekaaaqrkakldensa
>d1quua1 1.7.1.1.3 (1-124) alpha-actinin {Human (Homo sapiens)}
gssneirrlerlehlaekfrqkasthetwaygkeqillqkdyesasltevrallrkheaf
esdlaahqdrveqiaaiaqelneldyhdavnvndrcqkicdqwdrlgtltqkrrealerm
ekll
>d1quua2 1.7.1.1.3 (125-248) alpha-actinin {Human (Homo sapiens)}
etidqlhlefakraapfnnwmegamedlqdmfivhsieeiqslitaheqfkatlpeadge
rqsimaiqnevekviqsynirisssnpystvtmdelrtkwdkvkqlvpirdqslqeelar
qhan
>d1e2aa_ 1.7.2.1.1 Enzyme IIa from lactose specific PTS, IIa-lac {Lactococcus lactis}
mnreemtllgfeivayagdarskllealkaaengdfakadslvveagsciaeahssqtgm
lareasgeelpysvtmmhgqdhlmttillkdvihhlielykr
>d1chua1 1.7.3.1.1 (423-533) L-aspartate oxidase {Escherichia coli}
desrvenpdervviqhnwhelrlfmwdyvgivrttkrleralrritmlqqeideyyahfr
vsnnllelrnlvqvaelivrcammrkesrglhftldypellthsgpsi
>d1fuma1 1.7.3.1.2 (443-575) Fumarate reductase flavoprotein subunit {Escherichia coli}
dggenwakirdemglameegcgiyrtpelmqktidklaelqerfkrvritdtssvfntdl
lytielghglnvaecmahsamarkesrgahqrldegcterddvnflkhtlafrdadgttr
leysdvkittlpp
>d1qlaa1 1.7.3.1.3 (458-655) Fumarate reductase flavoprotein subunit {Wolinella succinogenes}
kgtedvfkiknrmkdvmddnvgifrdgphleksvkeleelykksknvgiknkrlhanpel
eeayrvpmmlkvalcvakgaldrtesrgahnredypkrddinwlnrtlaswpnpeqtlpt
leyealdvnemeiapryrgygakgnyienplsvkrqeeidkiqseleaagkdrhaiqeal
mpyelpakykarnerlgd
>d1qsda_ 1.7.4.1.1 beta-Tubulin binding post-chaperonin cofactor Rbl2p {Baker's yeast (Saccharomyces cerevisiae)}
tqldikvkalkrltkeegyyqqelkdqeahvaklkedksvdpydlkkqeevlddtkrllp
tlyekirefkedleqflktyqgtedvsdarsaitsaqellds
>d1deeg_ 1.8.1.1.1 Immunoglobulin-binding protein A modules {Staphylococcus aureus}
dqqsafyeilnmpnlneaqrngfiqslkddpsqstnvlgeakklnesqapk
>d1deeh_ 1.8.1.1.1 Immunoglobulin-binding protein A modules {Staphylococcus aureus}
fnkdqqsafyeilnmpnlneaqrngfiqslkddpsqstnvlgeakklnesqapk
>d1edj__ 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}
fnkeqqnafyeilhlpnlneeqrngfiqslkddpsqsanllaea
>d2spza_ 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
>d1prb__ 1.8.1.2.1 An albumin-binding domain {Peptostreptococcus magnus}
tidqwllknakedaiaelkkagitsdfyfnainkaktveevnalkneilkaha
>d1ebdc_ 1.9.1.1.1 E3-binding domain of dihydrolipoamide acetyltransferase {Bacillus stearothermophilus}
iampsvrkyarekgvdirlvqgtgkngrvlkedidaflagg
>d1bal__ 1.9.1.1.2 E3-binding domain of dihydrolipoamide succinyltransferase {Escherichia coli}
yasleeqnndalspairrllaehnldasaikgtgvggrltredvekhlaka
>d1bbl__ 1.9.1.1.2 E3-binding domain of dihydrolipoamide succinyltransferase {Escherichia coli}
lspairrllaehnldasaikgtgvggrltredvekhl
>d2pdd__ 1.9.1.1.3 E3/E1 binding domain of dihydrolipoyl acetyltransferase {Bacillus stearothermophilus}
viampsvrkyarekgvdirlvqgtgkngrvlkedidaflagga
>d2pde__ 1.9.1.1.3 E3/E1 binding domain of dihydrolipoyl acetyltransferase {Bacillus stearothermophilus}
viampsvrkyarekgvdirlvqgtgkngrvlkedidaflagga
>d1erc__ 1.10.1.1.1 ER-1 {Euplotes raikovi}
daceqaaiqcvesaceslctegedrtgcymyiysncppyv
>d2erl__ 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)}
sqaefdkaaeevkhlktkpadeemlfiyshykqatvgdinterpgmldfkgkakwdawne
lkgtskedamkayidkveelkkkygi
>d1ef1a1 1.11.2.1.1 (88-198) Moesin {Human (Homo sapiens)}
dvseeliqditqrlfflqvkegilnddiycppetavllasyavqskygdfnkevhksgyl
agdkllpqrvleqhklnkdqweeriqvwheehrgxlredavleylkiaqdl
>d1kdxa_ 1.12.1.1.1 Kix domain of CBP (creb binding protein) {Mouse (Mus musculus)}
gvrkgwhehvtqdlrshlvhklvqaifptpdpaalkdrrmenlvayakkvegdmyesans
rdeyyhllaekiykiqkelee
>d1lre__ 1.13.1.1.1 alpha-2-Macroglobulin receptor associated protein (RAP) domain 1 {Human (Homo sapiens)}
geefrmeklnqlwekaqrlhlppvrlaelhadlkiqerdelawkklkldgldedgekear
lirnlnvilakygldgkkdar
>d1qqva_ 1.14.1.1.1 Thermostable subdomain from chicken villin headpiece {Chicken (Gallus gallus)}
ptkletfpldvlvntaaedlprgvdpsrkenhlsdedfkavfgmtrsafanlplwkqqnl
kkekglf
>d1vii__ 1.14.1.1.1 Thermostable subdomain from chicken villin headpiece {Chicken (Gallus gallus)}
mlsdedfkavfgmtrsafanlplwkqqnlkkekglf
>d1tbaa_ 1.15.1.1.1 TAF(II)230 TBP-binding fragment {Fruit fly (Drosophila melanogaster)}
egsigngldltgilfgnidsegrllqdddgegrggtgfdaelrenigslsklgldsmlle
vidlkea
>d1ail__ 1.16.1.1.1 N-terminal, RNA-binding domain of nonstructural protein NS1 {Influenza virus A}
mdsntvssfqvdcflwhvrkqvvdqelgdapfldrlrrdqkslrgrgstlglnieaathv
gkqivekilk
>d1a32__ 1.16.1.2.1 Ribosomal protein S15 {Bacillus stearothermophilus}
ltqerkreiieqfkvhendtgspevqiailteqinnlnehlrvhkkdhhsrrgllkmvgk
rrrllaylrnkdvaryreiveklgl
>d1dk1a_ 1.16.1.2.2 Ribosomal protein S15 {Thermus thermophilus}
pitkeekqkvxqefarfpgdtgstevqvalltlrinrlsehlkvhkkdhhshrgllxxvg
qrrrllrylqredperyrxlieklgi
>d1d2da_ 1.16.1.3.1 Multifunctional Glu-Pro-tRNA synthase (EPRS) second repeated element {Chinese hamster (Cricetulus griseus)}
mvydkiaaqgevvrklkaekapkakvteavecllslkaeykektgkeyvpglehhh
>d2hp8__ 1.17.1.1.1 p8-MTCP1 {Human (Homo sapiens)}
mpqkdpcqkqaceiqkclqansymeskcqaviqelrkccaqypkgrsvvcsgfekeeeen
ltrksask
>d2end__ 1.18.1.1.1 T4 endonuclease V {bacteriophage T4, (Escherichia coli)}
trinltlvseladqhlmaeyrelprvfgavrkhvangkrvrdfkisptfilgaghvtffy
dkleflrkrqieliaeclkrgfnikdttvqdisdipqefrgdyipheasiaisqarldek
iaqrptwykyygkaiya
>d2lisa_ 1.19.1.1.1 Lysin {Red abalone (Haliotis rufescens)}
hyvepkflnkafevalkvqiiagfdrglvkwlrvhgrtlstvqkkalyfvnrrymqthwa
nymlwinkkidalgrtpvvgdytrlgaeigrridmayfydflkdknmipkylpymeeinr
mrpadvpvkym
>d1bmfg_ 1.20.1.1.1 ATP syntase (F1-ATPase), gamma subunit {Bovine (Bos taurus)}
atlkditrrlksikniqkitksmkmvaaakyaraerelkparvygvgslalyekadiktp
edkkkhliigvssdrglcgaihssvakqmkseaanlaaagkevkiigvgdkirsilhrth
sdqflvtfkevgrrpptfgdasvialellnsgyefdegsiifnrfrsvisykteekpifs
ldtissaesmsiyddidadvlrnyqeyslaniiyyslkesttseqsarmtamdnasknas
emidkltltfnrtrqavitkelieiisgaaal
>d1lbu_1 1.21.1.1.1 (1-83) Zn2+ DD-carboxypeptidase, N-terminal domain {Streptomyces albus G}
dgcytwsgtlsegssgeavrqlqirvagypgtgaqlaidgqfgpatkaavqrfqsaygla
adgiagpatfnkiyqlqdddctp
>d1ckta_ 1.22.1.1.1 HMG1, domains A and B {Rat/Hamster (Rattus norvegicus/Cricetulus griseus)}
kprgkmssyaffvqtcreehkkkhpdasvnfsefskkcserwktmsakekgkfedmakad
karyeremkty
>d1hsm__ 1.22.1.1.1 HMG1, domains A and B {Rat/Hamster (Rattus norvegicus/Cricetulus griseus)}
napkrppsafflfcseyrpkikgehpglsigdvakklgemwnntaaddkqpyekkaaklk
ekyekdiaayrakgkpdaa
>d2ezda_ 1.22.1.1.2 HMG1, domains A and B {Human (Homo sapiens), HMG-I(Y)}
vptpkrprgrpkgsknkgaak
>d2ezea_ 1.22.1.1.2 HMG1, domains A and B {Human (Homo sapiens), HMG-I(Y)}
vptpkrprgrpkgsknkgaaktrkt
>d1qrva_ 1.22.1.1.3 HMG-D {Drosophila melanogaster}
sdkpkrplsaymlwlnsaresikrenpgikvtevakrggelwramkdkseweakaakakd
dydravkefeang
>d1cg7a_ 1.22.1.1.4 NHP6a {Baker's yeast (Saccharomyces cerevisiae)}
mvtprepkkrttrkkkdpnapkralsaymffanenrdivrsenpditfgqvgkklgekwk
altpeekqpyeakaqadkkryesekelynatla
>d1hrya_ 1.22.1.1.5 SRY {Human (Homo sapiens)}
drvkrpmnafivwsrdqrrkmalenprmrnseiskqlgyqwkmlteaekwpffqeaqklq
amhrekypnykyr
>d2lefa_ 1.22.1.1.7 Lymphoid enhancer-binding factor, LEF1 {Mouse (Mus musculus)}
mhikkplnafmlymkemranvvaestlkesaainqilgrrwhalsreeqakyyelarker
qlhmqlypgwsardnygkkkkrkrek
>d1eqza_ 1.23.1.1.1 Histone H2A {Chicken (Gallus gallus), erythrocytes}
sgrgkqggkarakaksrssraglqfpvgrvhrllrkgnyaervgagapvylaavleylta
eilelagnaardnkktriiprhlqlairndeelnkllgkvtiaqggvlpniqavllpkkt
dshka
>d1eqzb_ 1.23.1.1.3 Histone H2B {Chicken (Gallus gallus), erythrocytes}
vtktqkkgdkkrkksrkesysiyvykvlkqvhpdtgisskamgimnsfvndiferiagea
srlahynkrstitsreiqtavrlllpgelakhavsegtkavtkytssk
>d1eqzc_ 1.23.1.1.5 Histone H3 {Chicken (Gallus gallus), erythrocytes}
apatggvkkphryrpgtvalreirryqkstellirklpfqrlvreiaqdfktdlrfqssa
vmalqeaseaylvglfedtnlcaihakrvtimpkdiqlarrirgera
>d1eqzd_ 1.23.1.1.7 Histone H4 {Chicken (Gallus gallus), erythrocytes}
gakrhrkvlrdniqgitkpairrlarrggvkrisgliyeetrgvlkvflenvirdavtyt
ehakrktvtamdvvyalkrqgrtlygfgg
>d1b67a_ 1.23.1.2.1 Histone A {Methanothermus fervidus}
gelpiapigriiknagaervsddarialakvleemgeeiaseavklakhagrktikaedi
elarkmfk
>d1b6wa_ 1.23.1.2.2 Histone B {Methanothermus fervidus}
elpiapigriikdagaervsddaritlakileexgrdiaseaiklarhagrktikaedie
lavrrfk
>d1tafa_ 1.23.1.3.1 TAF(II)42 {Fruit fly (Drosophila melanogaster)}
pkdaqvimsilkelnvqeyeprvvnqlleftfryvtsilddakvyanharkktidlddvr
latevtld
>d1tafb_ 1.23.1.3.2 TAF(II)62 {Fruit fly (Drosophila melanogaster)}
mlygssisaesmkviaesigvgslsddaakelaedvsiklkrivqdaakfmnhakrqkls
vrdidmslkv
>d1bh8a_ 1.23.1.3.3 TAF(II)18 {Human (Homo sapiens)}
lfskelrcmmygfgddqnpytesvdiledlviefitemthkamsi
>d1bh9a_ 1.23.1.3.3 TAF(II)18 {Human (Homo sapiens)}
lfskelrcmmygfgddqnpytesvdiledlviefitemthkamsi
>d1bh9b_ 1.23.1.3.4 TAF(II)28 {Human (Homo sapiens)}
fseeqlnryemyrrsafpkaaikrliqsitgtsvsqnvviamsgiskvfvgevveealdv
cekwgempplqpkhmreavrrlkskgqip
>d1diog_ 1.24.1.1.1 Diol dehydratase, gamma subunit {Klebsiella oxytoca}
sarvsdyplankhpewvktatnktlddftlenvlsnkvtaqdmritpetlrlqasiakda
grdrlamnferaaeltavpddrileiynalrpyrstkeellaiaddlesryqakicaafv
reaatlyverkklkgdd
>d1mtyg_ 1.24.2.1.1 Methane monooxygenase hydrolase, gamma subunit {Methylococcus capsulatus}
lgihsndtrdawvnkiahvntlekaaemlkqfrmdhttpfrnsyeldndylwieakleek
vavlkarafnevdfrhktafgedaksvldgtvakmnaakdkweaekihigfrqaykppim
pvnyfldgerqlgtrlmelrnlnyydtpleelrkqrgvrvvh
>d1om2a_ 1.24.3.1.1 Mitochondrial import receptor subunit Tom20 {Rat (Rattus norvegicus)}
raglsklpdlkdaeavqkffleeiqlgeellaqgdyekgvdhltnaiavcgqpqqllqvl
qqtlpppvfqmlltklptisqrivsaqslgeddve
>d1bz4a_ 1.25.1.1.1 Apolipoprotein E3 {Human (Homo sapiens)}
sgqrwelalgrfwdylrwvqtlseqvqeellssqvtqelralmdetmkelkaykseleeq
ltpvaeetrarlskelqaaqarlgadmedvcgrlvqyrgevqamlgqsteelrvrlashl
rklrkrllrdaddlqkrlavyqag
>d2liga_ 1.25.2.1.2 Aspartate receptor, ligand-binding domain {Salmonella typhimurium}
mggllfsslqhcqqgfvisnelrqqqseltstwdlmlqtrinlsrsaarmmmdasnqqss
aktdllqnakttlaqaaahyanfknmtplpamaeasanvdekyqryqaalaeliqfldng
nmdayfaqptqgmqnalgealgnyarvsenlyrqtfd
>d256ba_ 1.25.3.1.1 Cytochrome b562 {Escherichia coli}
adlednmetlndnlkviekadnaaqvkdaltkmraaaldaqkatppkledkspdspemkd
frhgfdilvgqiddalklanegkvkeaqaaaeqlkttrnayhqkyr
>d2ccya_ 1.25.3.2.1 Cytochrome c' {Rhodospirillum molischianum}
qskpedllklrqglmqtlksqwvpiagfaagkadlpadaaqraenmamvaklapigwakg
tealpngetkpeafgsksaeflegwkalatestklaaaakagpdalkaqaaatgkvckac
heefkqd
>d1bbha_ 1.25.3.2.2 Cytochrome c' {Chromatium vinosum}
aglspeeqietrqagyefmgwnmgkikanlegeynaaqveaaanviaaiansgmgalygp
gtdknvgdvktrvkpeffqnmedvgkiarefvgaantlaevaatgeaeavktafgdvgaa
ckschekyrak
>d1cgo__ 1.25.3.2.4 Cytochrome c' {Alcaligenes}
xfakpedavkyrqsaltlmashfgrmtpvvkgqapydaaqikanvevlktltalpwaafg
pgteggdarpeiwsdaasfkqkqqafqdnivklsaaadagdldklraafgdvgasckach
dayrk
>d1cpq__ 1.25.3.2.6 Cytochrome c' {Rhodobacter capsulatus}
adtkevleareayfkslggsmkamtgvakafdaeaakveaaklekilatdvaplfpagts
stdlpgqteakaaiwanmddfgakgkamheaggaviaaanagdgaafgaalqklggtcka
chddyreed
>d1a7va_ 1.25.3.2.7 Cytochrome c' {Rhodopseudomonas palustris}
qtdviaqrkailkqmgeatkpiaamlkgeakfdqavvqkslaaiaddskklpalfpadsk
tggdtaalpkiwedkakfddlfaklaaaataaqgtikdeaslkaniggvlgnckschddf
rakks
>d2hmza_ 1.25.4.1.1 Hemerythrin {Sipunculid worm (Themiste dyscrita)}
gfpipdpycwdisfrtfytivddehktlfngilllsqadnadhlnelrrctgkhflneqq
lmqasqyagyaehkkahddfihkldtwdgdvtyaknwlvnhiktidfkyrgki
>d2mhr__ 1.25.4.1.3 Myohemerythin {Sipunculan worm (Themiste zostericola)}
gweipepyvwdesfrvfyeqldeehkkifkgifdcirdnsapnlatlvkvttnhftheea
mmdaakysevvphkkmhkdflekigglsapvdaknvdyckewlvnhikgtdfkykgkl
>d1ei7a_ 1.25.5.1.1 Tobacco mosaic virus coat protein {Tobacco mosaic virus, Vulgare strain}
sysittpsqfvflssawadpielinlctnalgnqfqtqqartvvqrqfsevwkpspqvtv
rfpdsdfkvyrynavldplvtallgafdtrnriievenqanpttaetldatrrvddatva
irsainnlivelirgtgsynrssfesssglvwtsgpat
>d1cgme_ 1.25.5.1.2 Cucumber green mottle mosaic virus {Cucumber green mottle mosaic virus, watermelon strain}
xaynpitpskliafsasyvpvrtllnflvasqgtafqtqagrdsfreslsalpssvvdin
srfpdagfyaflngpvlrpifvsllsstdtrnrvievvdpsnpttaeslnavkrtddast
aaraeidnliesiskgfdvydrasfeaafsvvwseattska
>d3mdda1 1.25.6.1.2 (242-395) Medium chain acyl-CoA dehydrogenase {Pig (Sus scrofa)}
gagfkiamgtfdktrppvaagavglaqraldeatkyalerktfgkllaehqgisflladm
amkvelarlsyqraaweidsgrrntyyasiakayaadianqlatdavqvfggngfnteyp
veklmrdakiyqiyegtaqiqriiiarehigryk
>d1ivha1 1.25.6.1.4 (242-392) Isovaleryl-CoA dehydrogenase {Human (Homo sapiens)}
kgvyvlmsgldlerlvlaggplglmqavldhtipylhvreafgqkighfqlmqgkmadmy
trlmacrqyvynvakacdeghctakdcagvilysaecatqvaldgiqcfggngyindfpm
grflrdaklyeigagtsevrrlvigrafnad
>d1nsgb_ 1.25.7.1.1 FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP) {Human (Homo sapiens)}
vailwhemwhegleeasrlyfgernvkgmfevleplhammergpqtlketsfnqaygrdl
meaqewcrkymksgnvkdltqawdlyyhvfrris
>e1avo.1a 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
lrvqpeaqakvdvfredlctktenllgsyfpkkiseldaflkepalneanlsnlkapldi
>e1avo.1b 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
avncnekivvllqrlkpeikdvieqlnlvttwlqlqipriedgnnfgvavqekvfelmts
lhtklegfhtqiskyfsergdavtkaakqphvgdyrqlvheldeaeyrdirlmvmeirna
yavlydiilknfeklkkprg
>d2a0b__ 1.25.9.1.1 Aerobic respiration control sensor protein, ArcB {Escherichia coli}
sksealldipmleqylelvgpklitdglavfekmmpgyvsvlesnltaqdkkgiveeghk
ikgaagsvglrhlqqlgqqiqspdlpawednvgewieemkeewrhdvevlkawvakat
>d1c02a_ 1.25.9.2.1 Phosphorelay protein ypd1 {Yeast (Saccharomyces cerevisiae)}
stipseiinwtilneiismddddsdfskgliiqfidqaqttfaqmqrqldgeknlteldn
lghflkgssaalglqriawvceriqnlgrkmqhffpnktelvntlsdksiinginidedd
eeikiqvddkdensiyliliakalnqsrlefklarielskyyntnl
>d1ryt_1 1.26.1.1.1 (2-147) Rubrerythrin, N-terminal domain {Desulfovibrio vulgaris}
kslkgsrtekniltafagesqarnrynyfggqakkdgfvqisdifaetadqerehakrlf
kfleggdleivaafpagiiadthanliasaagehheytemypsfariareegyeeiarvf
asiavaeefhekrfldfarnikegrv
>d1bcfa_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d2fha__ 1.26.1.1.3 (Apo)ferritin {Human (Homo sapiens), H chain}
tsqvrqnyhqdseaainrqinlelyasyvylsmsyyfdrddvalknfakyflhqsheere
haeklmklqnqrggriflqdiqkpdcddwesglnamecalhleknvnqsllelhklatdk
ndphlcdfiethylneqvkaikelgdhvtnlrkmgapesglaeylfdkhtlg
>d1dpsa_ 1.26.1.1.6 Dodecameric ferritin homolog DPS {Escherichia coli}
skatnllytrndvsdsekkatvellnrqviqfidlslitkqahwnmrganfiavhemldg
frtalidhldtmaeravqlggvalgttqvinsktplksypldihnvqdhlkeladryaiv
andvrkaigeakdddtadiltaasrdldkflwfiecnie
>d1qgha_ 1.26.1.1.7 Dodecameric ferritin homolog DPS {Listeria innocua}
vdtkeflnhqvanlnvftvkihqihwymrghnfftlhekmddlysefgeqmdevaerlla
iggspfstlkeflenasveeapytkpktmdqlmedlvgtlellrdeykqgieltdkegdd
vtndmliafkasidkhiwmfkaflgkaple
>d1mtyb_ 1.26.1.2.1 Methane monooxygenase hydrolase, beta and alpha subunits {Methylococcus capsulatus}
errrgltdpemaavilkalpeapldgnnkmgyfvtprwkrlteyealtvyaqpnadwiag
gldwgdwtqkfhggrpswgnettelrtvdwfkhrdplrrwhapyvkdkaeewrytdrflq
gysadgqiramnptwrdefinrywgaflfneyglfnahsqgarealsdvtrvslafwgfd
kidiaqmiqlergflakivpgfdestavpkaewtngevyksarlaveglwqevfdwnesa
fsvhavydalfgqfvrreffqrlaprfgdnltpffinqaqtyfqiakqgvqdlyynclgd
dpefsdynrtvmrnwtgkwleptiaalrdfmglfaklpagttdkeeitaslyrvvddwie
dyasridfkadrdqivkavlaglk
>d1mtyd_ 1.26.1.2.1 Methane monooxygenase hydrolase, beta and alpha subunits {Methylococcus capsulatus}
aanraptsvnaqevhrwlqsfnwdfknnrtkyatkykmanetkeqfkliakeyarmeavk
derqfgslqvaltrlnagvrvhpkwnetmkvvsnflevgeynaiaatgmlwdsaqaaeqk
ngylaqvldeirhthqcayvnyyfakngqdpaghndarrtrtigplwkgmkrvfsdgfis
gdavecslnlqlvgeacftnplivavtewaaangdeitptvflsietdelrhmangyqtv
vsiandpasakylntdlnnafwtqqkyftpvlgmlfeygskfkvepwvktwdrwvyedwg
giwigrlgkygvesprslkdakqdaywahhdlyllayalwptgffrlalpdqeemewfea
nypgwydhygkiyeewrargcedpssgfiplmwfiennhpiyidrvsqvpfcpslakgas
tlrvheyngemhtfsdqwgermwlaeperyecqnifeqyegrelseviaelhglrsdgkt
liaqphvrgdklwtlddikrlncvfknpvkaf
>d1xika_ 1.26.1.2.3 Ribonucleotide reductase R2 {Escherichia coli}
ayttfsqtkndqlkepmffgqpvnvarydqqkydifekliekqlsffwrpeevdvsrdri
dyqalpehekhifisnlkyqtlldsiqgrspnvallplisipeletwvetwafsetihsr
sythiirnivndpsvvfddivtneqiqkraegissyydeliemtsywhllgegthtvngk
tvtvslrelkkklylclmsvnaleairfyvsfacsfafaerelmegnakiirliardeal
hltgtqhmlnllrsgaddpemaeiaeeckqecydlfvqaaqqekdwadylfrdgsmigln
kdilcqyveyitnirmqavgldlpfqtrsnpipwintwlv
>d1r2fa_ 1.26.1.2.4 Ribonucleotide reductase R2 {Salmonella typhimurium}
isainwnkiqddkdlevwnrltsnfwlpekvplsndipawqtlsaaeqqltirvftgltl
ldtiqniagapslmadaitpheeavlsnisfmeavharsyssifstlcqtkevdaayaws
eenpplqrkaqiilahyvsdeplkkkiasvflesflfysgfwlpmyfssrgkltntadli
rliirdeavhgyyigykyqialqklsaiereelklfaldllmelydneirytealyaetg
wvndvkaflcynankalmnlgyealfppemadvnpailaalsp
>d1xsm__ 1.26.1.2.5 Ribonucleotide reductase R2 {Mouse (Mus musculus)}
npsvedepllrenprrfvvfpieyhdiwqmykkaeasfwtaeevdlskdiqhwealkpde
rhfishvlaffaasdgivnenlverfsqevqvtearcfygfqiamenihsemysllidty
ikdpkereylfnaietmpcvkkkadwalrwigdkeatygervvafaavegiffsgsfasi
fwlkkrglmpgltfsnelisrdeglhcdfaclmfkhlvhkpaeqrvreiitnavrieqef
ltealpvkligmnctlmkqyiefvadrlmlelgfnkifrvenpfdfme
>d1afra_ 1.26.1.2.6 delta 9-stearoyl-acyl carrier protein desaturase {Castor bean (Ricinus communis)}
mpprevhvqvthsmppqkieifksldnwaeenilvhlkpvekcwqpqdflpdpasdgfde
qvrelrerakeipddyfvvlvgdmiteealptyqtmlntldgvrdetgasptswaiwtra
wtaeenrhgdllnkylylsgrvdmrqiektiqyligsgmdprtenspylgfiytsfqera
tfishgntarqakehgdiklaqicgtiaadekrhetaytkiveklfeidpdgtvlafadm
mrkkismpahlmydgrddnlfdhfsavaqrlgvytakdyadileflvgrwkvdkltglsa
egqkaqdyvcrlpprirrleeraqgrakeaptmpfswifdrqvkl
>d1bgc__ 1.27.1.1.2 Granulocyte-colony stimulating factor (G-CSF) {Bovine (Bos taurus)}
slpqsfllkcleqvrkiqadgaelqerlcaahklchpeelmllrhslgipqaplsscssq
slqlrgclnqlhgglflyqgllqalagispelaptldtlqldvtdfatniwlqmedlgaa
pavqptqgamptftsafqrraggvlvasqlhrflelayrglryla
>d1alu__ 1.27.1.1.4 Interleukin-6 {Human (Homo sapiens)}
ltsseridkqiryildgisalrketcnksnmcesskealaennlnlpkmaekdgcfqsgf
neetclvkiitgllefevyleylqnrfesseeqaravqmstkvliqflqkkaknldaitt
pdpttnaslltklqaqnqwlqdmtthlilrsfkeflqsslralrqm
>d1lki__ 1.27.1.1.5 Leukemia inhibitory factor (LIF) {Mouse (Mus musculus)}
natcairhpchgnlmnqiknqlaqlngsanalfisyytaqgepfpnnveklcapnmtdfp
sfhgngtektklvelyrmvaylsasltnitrdqkvlnptavslqvklnatidvmrgllsn
vlcrlcnkyrvghvdvppvpdhsdkeafqrkklgcqllgtykqvisvvvqaf
>d1huw__ 1.27.1.1.6 Growth hormone, somatotropin {Human (Homo sapiens)}
fptiplsrladnawlradrlnqlafdtyqefeeayipkeqihsfwwnpqtslcpsesipt
psnkeetqqksnlellrisllliqswlepvqflrsvfanslvygasdsnvydllkdleeg
iqtlmgrleallknygllycfnkdmskvstylrtvqcrsvegscgf
>d1cnt1_ 1.27.1.1.7 Ciliary neurotrophic factor (CNTF) {Human (Homo sapiens)}
phrrdlcsrsiwlarkirsdltaltesyvkhqglnkninldsadgmpvastdqwseltea
erlqenlqayrtfhvllarlledqqvhftptegdfhqaihtlllqvaafayqieelmill
eykiprneadgmpinvgdgglfekklwglkvlqelsqwtvrsihdlrfisshqtgip
>d1ax8__ 1.27.1.1.8 Leptin (obesity protein) {Human (Homo sapiens)}
iqkvqddtktliktivtrindishtqsvsskqkvtgldfipglhpiltlskmdqtlavyq
qiltsmpsrnviqisndlenlrdllhvlafskschlpeasgletldslggvleasgyste
vvalsrlqgslqdmlwqldlspgc
>d1eera_ 1.27.1.2.1 Erythropoietin {Human (Homo sapiens)}
apprlicdsrvlerylleakeaekittgcaehcslnekitvpdtkvnfyawkrmevgqqa
vevwqglallseavlrgqallvkssqpweplqlhvdkavsglrslttllralgaqkeais
nsdaasaaplrtitadtfrklfrvysnflrgklklytgeacrtgdr
>d2gmfa_ 1.27.1.2.2 Granulocyte-macrophage colony-stimulating factor (GM-CSF) {Human (Homo sapiens)}
rspspstqpwehvnaiqearrllnlsrdtaaemnetvevisemfdlqeptclqtrlelyk
qglrgsltklkgpltmmashykqhcpptpetscatqiitfesfkenlkdfllvipfdcwe
p
>d1iara_ 1.27.1.2.3 Interleukin-4 (IL-4) {Human (Homo sapiens)}
hkcditlqeiiktlnslteqktlcteltvtdifaaskntteketfcraatvlrqfyshhe
kdtrclgataqqfhrhkqlirflkrldrnlwglaglnscpvkeanqstlenflerlktim
rekyskcss
>d1hula_ 1.27.1.2.4 Interleukin-5 {Human (Homo sapiens)}
iptsalvketlallsthrtllianetlripvpvhknhqlcteeifqgigtlesqtvqggt
verlfknlslikkyidgqkkkcgeerrrvnqfldylqeflgvmntewi
>d1hmca_ 1.27.1.2.5 Macrophage colony-stimulating factor (M-CSF) {Human (Homo sapiens)}
seycshmigsghlqslqrlidsqmetscqitfefvdqeqlkdpvcylkkafllvqdimed
tmrfrdntpnaiaivqlqelslrlkscftkdyeehdkacvrtfyetplqllekvknvfne
tknlldkdwnifskncnnsfaecssqgh
>d1etea_ 1.27.1.2.6 Flt3 ligand {Human (Homo sapiens)}
tqdcsfqhspissdfavkirelsdyllqdypvtvasnlqddelcgglwrlvlaqrwmerl
ktvagskmqgllervnteihfvtkcafqpppsclrfvqtnisrllqetseqlvalkpwit
rqnfsrclelqcqp
>d3inkc_ 1.27.1.2.7 Interleukin-2 (IL-2) {Human (Homo sapiens)}
stkktqlqlehllldlqmilnginnyknpkltrmltfkfympkkatelkhlqcleeelkp
leevlnlaqsknfhlrprdlisninvivlelkgsettfmceyadetativeflnrwitfa
qsiistlt
>d1jli__ 1.27.1.2.8 Interleukin-3 (IL-3) {Human (Homo sapiens)}
ancsimideiihhlkrppnplldpnnlnsedmdilmernlrtpnllafvravkhlenasa
iesilknllpclplataaptrhpihikdgdwnefrrkltfylktlenaqaqq
>d2ilk__ 1.27.1.3.1 Interleukin-10 (cytokine synthesis inhibitory factor, CSIF) {Human (Homo sapiens)}
tqsenscthfpgnlpnmlrdlrdafsrvktffqmkdqldnlllkeslledfkgylgcqal
semiqfyleevmpqaenqdpdikahvnslgenlktlrlrlrrchrflpcenkskaveqvk
nafnklqekgiykamsefdifinyieaymtmkirn
>d1au1a_ 1.27.1.3.3 Interferon-beta {Human (Homo sapiens)}
msynllgflqrssnfqcqkllwqlngrleyclkdrmnfdipeeikqlqqfqkedaaltiy
emlqnifaifrqdssstgwnetivenllanvyhqinhlktvleeklekedftrgklmssl
hlkryygrilhylkakeyshcawtivrveilrnfyfinrltgylrn
>d1b5l__ 1.27.1.3.7 Interferon-tau {Sheep (Ovis aries)}
cylsrklmldarenlklldrmnrlsphsclqdrkdfglpqemvegdqlqkdqafpvlyem
lqqsfnlfytehssaawdttlleqlctglqqqldhldtcrgqvmgeedselgnmdpivtv
kkyfqgiydylqekgysdcaweivrvemmraltvsttlqkrltk
>d1d9ca_ 1.27.1.3.8 Interferon-gamma {Bovine (Bos taurus)}
qgqffreienlkeyfnasspdvakggplfseilknwkdesdkkiiqsqivsfyfklfenl
kdnqviqrsmdiikqdmfqkflngssekledfkkliqipvddlqiqrkainelikvmndl
s
>d1a8h_1 1.28.1.1.1 (349-500) Methionyl-tRNA synthetase (MetRS) {Thermus thermophilus}
laddlgnlvqrtramlfrfaegripepvageelaegtglagrlrplvrelkfhvaleeam
ayvkalnryinekkpwelfkkepeearavlyrvveglriasilltpampdkmaelrralg
lkeevrleeaerwglaeprpipeeapvlfpkk
>d1qqta1 1.28.1.1.2 (389-548) Methionyl-tRNA synthetase (MetRS) {Escherichia coli}
vvnlasrnagfinkrfdgvlaseladpalyktftdaaevigeawesrefgkavreimala
dlanryvdeqapwvvakqagrdadlqaicsmginlfrvlmtylkpvlpklteraeaflnt
eltwdgiqqpllghkvnpfkalynridmrqvealveaske
>d1ile_1 1.28.1.1.3 (642-821) Isoleucyl-tRNA synthetase (IleRS) {Thermus thermophilus}
yfltlwnvysffvtyanldrpdlknppppekrpemdrwllarmqdliqrvtealeaydpt
tsaralrdfvvedlsqwyvrrnrrrfwknedaldreaayatlyealvlvatlaapftpfl
aevlwqnlvrsvrleakesvhladwpeadpaladealvaqmravlkvvdlaraaraksgv
>d1qu2a1 1.28.1.1.4 (645-917) Isoleucyl-tRNA synthetase (IleRS) {Staphylococcus aureus}
yrkirntlrfmlgnindfnpdtdsipesellevdryllnrlreftastinnyenfdylni
yqevqnfinvelsnfyldygkdilyieqrdshirrsmqtvlyqilvdmtkllapilvhta
eevwshtphvkeesvhladmpkvvevdqalldkwrtfmnlrddvnraletarnekvigks
leakvtiasndkfnasefltsfdalhqlfivsqvkvvdklddqatayehgdiviehadge
kcercwnysedlgavdelthlcprcqqvvkslv
>d1bs2a1 1.28.1.1.5 (484-607) Arginyl-tRNA synthetase (ArgRS) {Baker's yeast (Saccharomyces cerevisiae)}
dtgpylqyahsrlrsvernasgitqekwinadfsllkepaakllirllgqypdvlrnaik
thepttvvtylfklthqvsscydvlwvagqteelatarlalygaarqvlyngmrllgltp
verm
>d1acp__ 1.29.1.1.1 Acyl carrier protein {Escherichia coli}
stieervkkiigeqlgvkqeevtnnasfvedlgadsldtvelvmaleeefdteipdeeae
kittvqaaidyinghqa
>d1af8__ 1.29.1.1.2 Actinorhodin polyketide synthase acyl carrier protein, ACT ACP {Streptomyces coelicolor, A3(2)}
matllttddlrralvecagetdgtdlsgdfldlrfedigydslalmetaarlesrygvsi
pddvagrvdtprelldlingalaeaa
>d1dnya_ 1.29.1.2.1 Peptidyl carrier protein (PCP), thioester domain {Bacillus brevis}
yvaptnavesklaeiwervlgvsgigildnffqigghslkamavaaqvhreyqvelplkv
lfaqptikalaqyvat
>d1unka_ 1.29.2.1.1 ImmE7 protein {Escherichia coli}
melknsisdyteaefvqllkeiekenvaatddvldvllehfvkitehpdgtdliyypsdn
rddspegivkeikewraangkpgfkqg
>d1bxia_ 1.29.2.1.3 ImE9 protein {Escherichia coli}
lkasisdyteaeflqlvtticnadtsseeelvklvthfeemtehpsgsdliyypkegddd
spsgivntvqqwraangksgfkq
>d2eiaa1 1.29.3.1.1 (148-222) EIAV capsid protein p26 {Equine infectious anemia virus, EIAV}
pkaqnirqgakepypefvdrllsqikseghpqeiskfltdtltiqnaneecrnamrhlrp
edtleekmyacrdig
>d1qrjb1 1.29.3.1.2 (131-214) HTLV-I capsid protein {Human t-cell leukemia virus, type I, HTLV-I}
pswasilqgleepyhafverlnialdnglpegtpkdpilrslaysnankecqkllqargh
tnsplgdmlracqtwtpkdktkvl
>d1a8o__ 1.29.3.1.3 HIV capsid protein, dimerisation domain {Human immunodeficiency virus, type 1, HIV-1}
dirqgpkepfrdyvdrfyktlraeqasqevknwxtetllvqnanpdcktilkalgpgatl
eexxtacqg
>d1bmx__ 1.29.3.1.3 HIV capsid protein, dimerisation domain {Human immunodeficiency virus, type 1, HIV-1}
csildirqgpkepfrdyvdrfyktlraeqas
>d1d1da1 1.29.3.1.4 (151-230) RSV capsid protein {Rous sarcoma virus, RSV}
gpwaditqgpsesfvdfanrlikavegsdlppsarapviidcfrqksqpdiqqliraaps
tlttpgeiikyvldrqkiap
>d1ffh_1 1.30.1.1.1 (2-88) Signal sequence recognition protein Ffh {Thermus aquaticus}
fqqlsarlqeaigrlrgrgriteedlkatlreirralmdadvnlevtrdfvervreealg
kqvlesltpaevilatvyealkealgg
>d1fts_1 1.30.1.1.2 (201-284) Signal recognition particle receptor, FtsY {Escherichia coli}
rsllktkenlgsgfislfrgkkidddlfeeleeqlliadvgvettrkiitnltegasrkq
lrdaealygllkeemgeilakvde
>d1b91a_ 1.30.2.1.1 P300/CAF histone acetyltransferase bromodomain {human (Homo sapiens)}
gshmskeprdpdqlystlksilqqvkshqsawpfmepvkrteapgyyevirspmdlktms
erlknryyvskklfmadlqrvftnckeynapeseyykcanilekfffskikeaglidk
>d1eqfa1 1.30.2.1.2 (1359-1497) TAFII250 double bromodomain module {Human (Homo sapiens)}
gttvhcdylnrphksihrrrtdpmvtlssilesiindmrdlpntypfhtpvnakvvkdyy
kiitrpmdlqtlrenvrkrlypsreefrehlelivknsatyngpkhsltqisqsmldlcd
eklkekedklarlekainp
>d1eqfa2 1.30.2.1.2 (1498-1625) TAFII250 double bromodomain module {Human (Homo sapiens)}
llddddqvafsfildnivtqkmmavpdswpfhhpvnkkfvpdyykvivnpmdletirkni
skhkyqsresflddvnlilansvkyngpesqytktaqeivnvcyqtlteydehltqlekd
ictakeaa
>d1b6q__ 1.31.1.1.1 ROP protein {Escherichia coli}
mtkqektalnmarfirsqtltlleklneldpdeqadiceslhdhadelyrsclarf
>d1gtoa_ 1.31.1.1.1 ROP protein {Escherichia coli}
gtkqektalnmarfirsqtltlleklnelgadeqadiceslhdhadelyrsclarfgddg
en
>d1nkd__ 1.31.1.1.1 ROP protein {Escherichia coli}
mtkqektalnmarfirsqtltlleklneladaadeqadiceslhdhadelyrsclarfg
>d1ropa_ 1.31.1.1.1 ROP protein {Escherichia coli}
mtkqektalnmarfirsqtltlleklneldadeqadiceslhdhadelyrsclarf
>d1joya_ 1.31.2.1.1 EnvZ histidine kinase {Escherichia coli}
maagvkqladdrtllmagvshdlrtpltrirlatemmseqdgylaesinkdieecnaiie
qfidylr
>d1b3qa1 1.31.2.1.2 (293-354) Histidine kinase CheA {Thermotoga maritima}
sqtvrvdiekldnlmdlmgelviarsriletlkkynikeldeslshlsritldlqnvvmk
ir
>d1r2aa_ 1.32.1.1.1 Dimerization-anchoring domain of cAMP-dependent type II PK regulatory subunit {Mouse (Mus musculus)}
hmghiqippgltellqgytvevlrqqppdlvdfaveyftrlrearr
>d1r2ab_ 1.32.1.1.1 Dimerization-anchoring domain of cAMP-dependent type II PK regulatory subunit {Mouse (Mus musculus)}
hmghiqippgltellqgytvevlrqqppdlvdfaveyftrlrearr
>d1ytfb1 1.33.1.1.1 Transcription factor IIA (TFIIA), N-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
snaeasrvyeiivesvvnevredfenagideqtlqdlkniwqkklt
>d1ytfd1 1.33.1.1.1 (5-54) Transcription factor IIA (TFIIA), N-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
gyyelyrrstignslvdaldtlisdgrieaslamrvletfdkvvaetlkd
>d1ecia_ 1.34.1.1.1 Ectatomin, A & B chains {Ant (Ectatomma tuberculatum), venom}
gvipkkiwetvcptvepwakkcsgdiatyikrecgkl
>d1ecib_ 1.34.1.1.1 Ectatomin, A & B chains {Ant (Ectatomma tuberculatum), venom}
wstivklticptlksmakkcegsiatmikkkcdk
>d1b0na1 1.35.1.1.1 (74-108) SinR repressor (dimerisation domain)-SinI anti-repressor complex {Bacillus subtilis}
ldseweklvrdamtsgvskkqfrefldyqkwrksq
>d1b0nb1 1.35.1.1.1 SinR repressor (dimerisation domain)-SinI anti-repressor complex {Bacillus subtilis}
feldqewvelmveakeanispeeirkyllln
>d1octc2 1.36.1.1.1 (5-75) Oct-1 {Human (Homo sapiens)}
dleeleqfaktfkqrriklgftqgdvglamgklygndfsqttisrfealnlsfknmcklk
pllekwlndae
>d1au7a2 1.36.1.1.2 (5-76) Pit-1 {Rat (Rattus norvegicus)}
gmraleqfanefkvrriklgytqtnvgealaavhgsefsqtticrfenlqlsfknacklk
ailskwleeaeq
>d1lmb3_ 1.36.1.2.1 lambda C1 repressor, DNA-binding domain {Bacteriophage lambda (Escherichia coli)}
pltqeqledarrlkaiyekkknelglsqesvadkmgmgqsgvgalfnginalnaynaall
akilkvsveefspsiareiyemyeavs
>d1r69__ 1.36.1.2.2 434 C1 repressor, DNA-binding domain {Phage 434 (Escherichia coli)}
sissrvkskriqlglnqaelaqkvgttqqsieqlengktkrprflpelasalgvsvdwll
ngt
>d2cro__ 1.36.1.2.3 cro 434 {Bacteriophage 434}
mqtlserlkkrrialkmtqtelatkagvkqqsiqlieagvtkrprflfeiamalncdpvw
lqygt
>d1adr__ 1.36.1.2.4 p22 C2 repressor, DNA-binding domain {Bacteriophage p22 (Salmonella)}
mntqlmgerirarrkklkirqaalgkmvgvsnvaisqwersetepngenllalskalqcs
pdyllkgdlsqtnvay
>d1d1la_ 1.36.1.2.5 cro lambda repressor {Bacteriophage lambda (Escherichia coli)}
meqritlkdyamrfgqtktakdlgvyqsainkaihagrkifltinadgsvyaeevkpwps
n
>d1orc__ 1.36.1.2.5 cro lambda repressor {Bacteriophage lambda (Escherichia coli)}
qritlkdyamrfgqtktakdlgvyqsainkaihagrkifltinadgsvyaeevkdgevkp
fpsn
>d1ner__ 1.36.1.2.6 Ner {Bacteriophage mu}
csnekardwhradviaglkkrklslsalsrqfgyapttlanalerhwpkgeqiianalet
kpeviwpsryqage
>d1b0na2 1.36.1.3.1 (1-68) SinR repressor, DNA-binding domain {Bacillus subtilis}
migqrikqyrkekgyslselaekagvaksylssiernlqtnpsiqflekvsavldvsvht
lldekhet
>d1bdha1 1.36.1.5.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslavnh
>d1bdia1 1.36.1.5.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkvnh
>d1pnra1 1.36.1.5.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkvnh
>d1pru__ 1.36.1.5.1 Purine repressor (PurR), N-terminal domain {Escherichia coli}
matikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkv
>d1prv__ 1.36.1.5.1 Purine repressor (PurR), N-terminal domain {Escherichia coli}
matikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkv
>d1qp0a1 1.36.1.5.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkvnh
>d1qp4a1 1.36.1.5.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkvnh
>d1qp7a1 1.36.1.5.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslavnh
>d1qpza1 1.36.1.5.1 (2-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
atikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkvnh
>d1qqaa1 1.36.1.5.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslavnh
>d1qqba1 1.36.1.5.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslavnh
>d1vpwa1 1.36.1.5.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarsmkvnh
>d1weta1 1.36.1.5.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkvnh
>d1zaya1 1.36.1.5.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkvnh
>d2puba1 1.36.1.5.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkvnh
>d2puca1 1.36.1.5.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkvnh
>d2puda1 1.36.1.5.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkvnh
>d2puea1 1.36.1.5.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkvnh
>d2pufa1 1.36.1.5.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkvnh
>d2puga1 1.36.1.5.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkvnh
>d1efaa1 1.36.1.5.2 (2-60) Lac repressor (LacR), N-terminal domain {Escherichia coli}
kpvtlydvaeyagvsyqtvsrvvnqashvsaktrekveaamaelnyipnrvaqqlagkq
>d1lcca_ 1.36.1.5.2 Lac repressor (LacR), N-terminal domain {Escherichia coli}
mkpvtlydvaeyagvsyqtvsrvvnqashvsaktrekveaamaelnyipnr
>d1lcda_ 1.36.1.5.2 Lac repressor (LacR), N-terminal domain {Escherichia coli}
mkpvtlydvaeyagvsyqtvsrvvnqashvsaktrekveaamaelnyipnr
>d1lqc__ 1.36.1.5.2 Lac repressor (LacR), N-terminal domain {Escherichia coli}
mkpvtlydvaeyagvsyqtvsrvvnqashvsaktrekveaamaelnyipnrvaqql
>d1uxc__ 1.36.1.5.3 Fructose repressor (FruR), N-terminal domain {Escherichia coli}
mkldeiarlagvsrttasyvingkakqyrvsdktvekvmavvrehnyhpn
>d1uxd__ 1.36.1.5.3 Fructose repressor (FruR), N-terminal domain {Escherichia coli}
mkldeiarlagvsrttasyvingkakqyrvsdktvekvmavvrehnyhpnavaaglrlq
>d2tct_1 1.37.1.1.1 (2-67) Tetracyclin repressor (Tet-repressor, TetR), N-terminal domain {Escherichia coli}
arlnresvidaalellnetgidglttrklaqklgieqptlywhvknkralldalaveila
rhhdys
>d1a04a1 1.37.1.2.1 (150-216) Nitrate/nitrite response regulator (NARL), effector domain {Escherichia coli}
erdvnqltprerdilkliaqglpnkmiarrlditestvkvhvkhmlkkmklksrveaavw
vhqerif
>d1dula_ 1.38.1.1.1 Signal sequence binding protein Ffh {Escherichia coli}
fdlndfleqkvlvrxeaiinsxtxkerakpeiikgsrkrriaagsgxqvqdvnrllkqfd
dxqrxxkk
>d2ffha2 1.38.1.1.2 (319-418) Signal sequence binding protein Ffh {Thermus aquaticus}
eapksakelsledflkqmqnlkrlgpfseilgllpgvpqglkvdekaikrleaivlsmtp
eerkdprilngsrrkriakgsgtsvqevnrfikafeemkalmkslek
>d1qb2a_ 1.38.1.1.3 SRP54M {Human (Homo sapiens)}
qftlrdmyeqfqnimkmgpfsqilgmipgfgtdfmskgneqesmarlkklmtimdsmndq
eldstdgakvfskqpgriqrvargsgvstrdvqelltqytkfaqmvk
>d1sknp_ 1.39.1.1.1 Binding domain of Skn-1 {Caenorhabditis elegans}
grqskdeqlasdnelpvsafqisemslselqqvlkneslseyqrqlirkirrrgknkvaa
rtcrqrrtdrhdkm
>d1hloa_ 1.40.1.1.1 Max protein {Human (Homo sapiens)}
nddievesdadkrahhnalerkrrdhikdsfhslrdsvpslqgekasraqildkateyiq
ymrrknhthqqdiddlkrqn
>d1mdya_ 1.40.1.1.3 Myod B/HLH domain {Mouse (Mus musculus)}
melkrkttnadrrkaatmrerrrlskvneafetlkrstssnpnqrlpkveilrnairyie
glqallrd
>d1an4a_ 1.40.1.1.4 Usf B/HLH domain {Human (Homo sapiens)}
mdekrraqhneverrrrdkinnwivqlskiipdssmestksgqskggilskasdyiqelr
qsnhr
>d1a0aa_ 1.40.1.1.5 Pho4 B/HLH domain {Baker's yeast (Saccharomyces cerevisiae)}
mkreshkhaeqarrnrlavalhelaslipaewkqqnvsaapskattveaacryirhlqqn
gst
>d1am9a_ 1.40.1.1.6 SREBP-1a {Human (Homo sapiens)}
qsrgekrtahnaiekryrssindkiielkdlvvgteaklnksavlrkaidyirflqhsnq
klkqenlslrtavhkskslk
>d1bod__ 1.41.1.1.1 Calbindin D9K {Bovine (Bos taurus)}
mkspeelkgifekydkegdgqlskeelklllqtefpsllkgmstldelfeeldkngdgev
sfeefqvlvkkisq
>d5icb__ 1.41.1.1.1 Calbindin D9K {Bovine (Bos taurus)}
kspeelkgifekyaakegdpnqlskeelklllqtefpsllkgpstldelfeeldkngdge
vsfeefqvlvkkisq
>d1a03a_ 1.41.1.2.1 Calcyclin (S100) {Rabbit (Oryctolagus cuniculus)}
maspldqaiglligifhkysgkegdkhtlskkelkeliqkeltigsklqdaeivklmddl
drnkdqevnfqeyitflgalamiynealkg
>d1mho__ 1.41.1.2.3 Calcyclin (S100) {Bovine (Bos taurus), s100b}
selekavvalidvfhqysgregdkhklkkselkelinnelshfleeikeqevvdkvmetl
dsdgdgecdfqefmafvamittacheff
>d1a4pa_ 1.41.1.2.5 Calcyclin (S100) {Human (Homo sapiens), P11 s100a10, calpactin}
psqmehametmmftfhkfagdkgyltkedlrvlmekefpgflenqkdplavdkimkdldq
crdgkvgfqsffsliagltiacndyfvvhmkq
>d1psra_ 1.41.1.2.6 Calcyclin (S100) {Human (Homo sapiens), psoriasin s100a7}
sntqaersiigmidmfhkytrrddkidkpslltmmkenfpnflsacdkkgtnyladvfek
kdknedkkidfseflsllgdiatdyhkqshgaapcsggsq
>d1qlsa_ 1.41.1.2.7 Calcyclin (S100) {Pig (Sus scrofa), calgizzarin s100c (s100a11)}
pteterciesliaifqkhagrdgnntkiskteflifmntelaaftqnqkdpgvldrmmkk
ldldsdgqldfqeflnligglaiachdsfikstqk
>d1mr8a_ 1.41.1.2.8 Calcyclin (S100) {Human (Homo sapiens), calgranulin s100a8, MRP8}
mltelekalnsiidvyhkyslikgnfhavyrddlkklletecpqyirkkgadvwfkeldi
ntdgavnfqeflilvikmgvaahkkshees
>d1sra__ 1.41.1.3.1 C-terminal (EC) domain of BM-40/SPARC/osteonectin {Human (Homo sapiens)}
ppcldseltefplrmrdwlknvlvtlyerdednnlltekqklrvkkihenekrleagdhp
vellardfeknynmyifpvhwqfgqldqhpidgylshtelaplraplipmehcttrffet
cdldndkyialdewagcfgikqkdidkdlvi
>d1rro__ 1.41.1.4.1 Oncomodulin {Rat (Rattus norvegicus), Sprague-dawley strain}
sitdilsaediaaalqecqdpdtfepqkffqtsglskmsasqvkdifrfidndqsgyldg
delkyflqkfqsdareltesetkslmdaadndgdgkigadefqemvhs
>d2pvba_ 1.41.1.4.3 Parvalbumin {Pike (Esox lucius)}
sfaglkdadvaaalaacsaadsfkhkeffakvglaskslddvkkafyvidqdksgfieed
elklflqnfspsaraltdaetkafladgdkdgdgmigvdefaamika
>d5pal__ 1.41.1.4.4 Parvalbumin {Leopard shark (Triakis semifasciata)}
pmtkvlkaddinkaisafkdpgtfdykrffhlvglkgktdaqvkevfeildkdqsgfiee
eelkgvlkgfsahgrdlndtetkallaagdsdhdgkigadefakmvaqa
>d1avsa_ 1.41.1.5.1 Troponin C {Chicken (Gallus gallus)}
qaearaflseemiaefkaafdmfdadgggdistkelgtvmrmlgqnptkeeldaiieevd
edgsgtidfeeflvmmvrqmk
>d1ctaa_ 1.41.1.5.1 Troponin C {Chicken (Gallus gallus)}
xkseeelanafrifdknadgyidieelgeilratg
>d1ctab_ 1.41.1.5.1 Troponin C {Chicken (Gallus gallus)}
xkseeelanafrifdknadgyidieelgeilratg
>d1ctda_ 1.41.1.5.1 Troponin C {Chicken (Gallus gallus)}
xkseeelanafrifdknadgyidieelgeilratg
>d1ctdb_ 1.41.1.5.1 Troponin C {Chicken (Gallus gallus)}
xkseeelanafrifdknadgyidieelgeilratg
>d1ggsa_ 1.41.1.5.1 Troponin C {Chicken (Gallus gallus)}
mvrcmkddskgkteeelsdlfrmfdknadgyidleelkimlqatgetiteddieelmkdg
dknndgridydeflefmkgve
>d1ncx__ 1.41.1.5.1 Troponin C {Chicken (Gallus gallus)}
asmtdqqaearaflseemiaefkaafdmfdadgggdistkelgtvmrmlgqnptkeelda
iieevdedgsgtidfeeflvmmvrqmkedakgkseeelancfrifdknadgfidieelge
ilratgehvteediedlmkdsdknndgridfdeflkmmegvq
>d1pona_ 1.41.1.5.1 Troponin C {Chicken (Gallus gallus)}
kseeelanafrifdknadgyidieelgeilratg
>d1ponb_ 1.41.1.5.1 Troponin C {Chicken (Gallus gallus)}
vteediedlmkdsdknndgridfdeflkmmegvq
>d1ap4__ 1.41.1.5.4 Troponin C {Human (Homo sapiens), cardiac isoform}
mddiykaaveqlteeqknefkaafdifvlgaedgcistkelgkvmrmlgqnptpeelqem
idevdedgsgtvdfdeflvmmvrcmkdds
>d2scpa_ 1.41.1.5.5 Sarcoplasmic calcium-binding protein {Sandworm (Nereis diversicolor)}
sdlwvqkmktyfnridfdkdgaitrmdfesmaerfakesemkaehakvlmdsltgvwdnf
ltavaggkgidettfinsmkemvknpeaksvvegplplffravdtnednnisrdeygiff
gmlgldktmapasfdaidtnndgllsleefviagsdffmndgdstnkvfwgplv
>d2sas__ 1.41.1.5.6 Sarcoplasmic calcium-binding protein {Amphioxus (Branchiostoma lanceolatum)}
glndfqkqkikftfdffldmnhdgsiqdndfedmmtrykevnkgslsdadyksmqasled
ewrdlkgradinkddvvsweeylamwektiatcksvadlpawcqnripflfkgmdvsgdg
ivdleefqnycknfqlqcadvpavynvitdggkvtfdlnrykelyyrlltspaadagntl
mgqkp
>d1ej3a_ 1.41.1.5.7 Aequorin {Jellyfish (Aequorea aequorea)}
ltsdfdnprwigrhkhmfnfldvnhngkisldemvykasdivinnlgatpeqakrhkdav
eaffggagmkygvetdwpayiegwkklatdelekyakneptliriwgdalfdivdkdqng
aitldewkaytkaagiiqssedceetfrvcdidesgqldvdemtrqhlgfwytmdpacek
lyggavp
>d1c7wa_ 1.41.1.5.8 Calcium vector protein {Amphioxus (Branchiostoma lanceolatum)}
eeeilrafkvfdangdgvidfdefkfimqkvgeepltdaeveeamkeadedgngvidipe
fmdlikks
>d1cll__ 1.41.1.5.9 Calmodulin {Human (Homo sapiens)}
lteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngti
dfpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevde
mireadidgdgqvnyeefvqmmta
>d1ak8__ 1.41.1.5.10 Calmodulin {Bovine (Bos taurus)}
madqlteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadg
ngtidfpefltmmark
>d1cmg__ 1.41.1.5.10 Calmodulin {Bovine (Bos taurus)}
mkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevdemireadidgdgq
vnyeefvqmmtak
>d1osa__ 1.41.1.5.15 Calmodulin {Paramecium tetraurelia}
aeqlteeqiaefkeafalfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgn
gtidfpeflslmarkmkeqdseeelieafkvfdrdgnglisaaelrhvmtnlgekltdde
vdemireadidgdghinyeefvrmmvsk
>d1wdcb_ 1.41.1.5.17 Myosin Essential Chain {Bay scallop (Aequipecten irradians)}
lpqkqiqemkeafsmidvdrdgfvskedikaiseqlgrapddkeltamlkeapgplnftm
flsifsdklsgtdseetirnafamfdeqetkklnieyikdllenmgdnfnkdemrmtfke
apveggkfdyvkftamikgsge
>d2mysb_ 1.41.1.5.18 Myosin Essential Chain {Chicken (Gallus gallus)}
fdeteiedfkeaftvidqnadgiidkddlretfaamgrlnvkneeldamikeasgpinft
vfltmfgeklkgadpedvimgafkvldpdgkgsikksfleellttgggrftpeeiknmwa
afppdvagnvdyknicyvithgeda
>d1wdcc_ 1.41.1.5.19 Myosin Regulatory Chain {Bay scallop (Aequipecten irradians)}
lsqdeiddlkdvfelfdfwdgrdgavdafklgdvcrclginprnedvfavggthkmgeks
lpfeeflpayeglmdceqgtfadymeafktfdregqgfisgaelrhvltalgerlsdedv
deiikltdlqedlegnvkyedfvkkvmagpyp
>d2mysc_ 1.41.1.5.20 Myosin Regulatory Chain {Chicken (Gallus gallus)}
aaaddfkeafllfdrtgdakitasqvgdiaralgqnptnaeinkilgnpskeemnaaait
feeflpmlqaaannkdqgtfedfveglrvfdkegngtvmgaelrhvlatlgekmteeeve
elmkgqedsngcinyeafvkhimsv
>d1auib_ 1.41.1.5.22 Calcineurin regulatory subunit (B-chain) {Human (Homo sapiens)}
syplemcshfdadeikrlgkrfkkldldnsgslsveefmslpelqqnplvqrvidifdtd
gngevdfkefiegvsqfsvkgdkeqklrfafriydmdkdgyisngelfqvlkmmvgnnlk
dtqlqqivdktiinadkdgdgrisfeefcavvggldihkkmvvdv
>d1rec__ 1.41.1.5.24 Recoverin {Bovine (Bos taurus)}
lskeileelqlntkfteeelsswyqsflkecpsgritrqefqtiyskffpeadpkayaqh
vfrsfdansdgtldfkeyvialhmtsagktnqklewafslydvdgngtisknevleivta
ifkmispedtkhlpedentpekraekiwgffgkkdddkltekefiegtlankeilrliqf
epqkvkeklk
>d1dgua_ 1.41.1.5.27 Calium- and integrin-binding protein, CIB {Human (Homo sapiens)}
skellaeyqdltfltkqeillahrrfcellpqeqrsvesslraqvpfeqilslpelkanp
fkericrvfstspakdslsfedfldllsvfsdtatpdikshyafrifdfdddgtlnredl
srlvncltgegedtrlsasemkqlidnileesdidrdgtinlsefqhvisrspdfassfk
ivl
>d1qjta_ 1.41.1.6.1 Eps15 {Mouse (Mus musculus)}
lsltqlssgnpvyekyyrqveagntgrvlaldaaaflkksglpdlilgkiwdladtdgkg
vlskqeffvalrlvacaqnglevslsslslavppprfhd
>d1eh2__ 1.41.1.6.2 Eps15 {Human (Homo sapiens)}
pwavkpedkakydaifdslspvngflsgdkvkpvllnsklpvdilgrvwelsdidhdgml
drdefavamflvycalekepvpmslppalvppskr
>d1qasa1 1.41.1.7.1 (205-298) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
ykmltqraeidrafeeaagsaetlsverlvtflqhqqreeeagpalalslieryepseta
kaqrqmtkdgflmyllsadgnafslahrrvyqdm
>d1alva_ 1.41.1.7.4 Calpain small (regulatory) subunit (domain VI) {Pig (Sus scrofa)}
eevrqfrrlfaqlagddmevsatelmnilnkvvtrhpdlktdgfgidtcrsmvavmdsdt
tgklgfeefkylwnnikkwqaiykqfdvdrsgtigsselpgafeaagfhlnehlysmiir
rysdeggnmdfdnfisclvrldamfrafksldkdgtgqiqvniqewlqltmys
>d2cbla1 1.41.1.7.7 (178-263) Cbl {Human (Homo sapiens)}
tfritkadaaefwrkafgektivpwksfrqalhevhpissgleamalkstidltcndyis
vfefdiftrlfqpwssllrnwnslav
>d1c3za_ 1.41.2.1.1 Thp12-carrier protein {Yellow meal worm (Tenebrio molitor)}
etpreklkqhsdackaesgvseeslnkvrnreevddpklkehafcilkragfidasgefq
ldhiktkfkensehpekvddlvakcavkkdtpqhssadffkcvhdnrs
>d1cpo_1 1.41.3.1.1 (1-119) Cloroperoxidase {Fungus (Caldariomyces fumago)}
epgsgigypydnntlpyvapgptdsrapcpalnalanhgyiphdgraisretlqnaflnh
mgiansvielaltnafvvceyvtgsdcgdslvnltllaephafehdhsfsrkdykqgva
>d1cpo_2 1.41.3.1.1 (120-298) Cloroperoxidase {Fungus (Caldariomyces fumago)}
nsndfidnrnfdaetfqtsldvvagkthfdyadmneirlqreslsneldfpgwfteskpi
qnvesgfifalvsdfnlpdndenplvridwwkywftnesfpyhlgwhppspareiefvts
assavlaasvtstpsslpsgaigpgaeavplsfastmtpfllatnapyyaqdptlgpnd
>d1bkra_ 1.42.1.1.1 beta-spectrin {Human (Homo sapiens)}
ksakdalllwcqmktagypnvnihnfttswrdgmafnalihkhrpdlidfdklkksnahy
nlqnafnlaeqhlgltklldpedisvdhpdeksiityvvtyyhyfskm
>d1aoa_1 1.42.1.1.2 (121-251) N-terminal actin-crosslinking domain from fimbrin {Human (Homo sapiens)}
yseeekyafvnwinkalendpdcrhvipmnpntddlfkavgdgivlckminlsvpdtide
rainkkkltpfiiqenlnlalnsasaigchvvnigaedlragkphlvlgllwqiikiglf
adielsrneal
>d1aoa_2 1.42.1.1.2 (260-375) N-terminal actin-crosslinking domain from fimbrin {Human (Homo sapiens)}
tleelmklspeelllrwanfhlensgwqkinnfsadikdskayfhllnqiapkgqkegep
ridinmsgfnetddlkraesmlqqadklgcrqfvtpadvvsgnpklnlafvanlfn
>d1bhda_ 1.42.1.1.3 Utrophin {Human (Homo sapiens)}
lqqtnsekillswvrqttrpysqvnvlnfttswtdglafnavlhrhkpdlfswdkvvkms
pierlehafskaqtylgieklldpedvavrlpdkksiimyltslfevl
>d1dxxa1 1.42.1.1.4 (9-119) Dystrophin {Human (Homo sapiens)}
dsyeredvqkktftkwvnaqfskfgkqhienlfsdlqdgrrlldllegltgqklpkekgs
trvhalnnvnkalrvlqnnnvdlvnigstdivdgnhkltlgliwniilhwq
>d1a26_1 1.43.1.1.1 (662-796) Domain of poly(ADP-ribose) polymerase {Chicken (Gallus gallus)}
ksklakpiqdlikmifdvesmkkamvefeidlqkmplgklskrqiqsaysilnevqqavs
dggsesqildlsnrfytliphdfgmkkppllsnleyiqakvqmldnlldievaysllrgg
nedgdkdpidinyek
>d1ycqa_ 1.44.1.1.1 MDM2 {African clawed frog (Xenopus laevis)}
eklvqptplllsllksagaqketftmkeviyhlgqyimakqlydekqqhivhcsndplge
lfgvqefsvkeprrlyamisrnlvsanv
>d1arqa_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1arqb_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1arra_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1arrb_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1b28a_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengmsvnsyiyqlvmesfkkegriga
>d1b28b_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengmsvnsyiyqlvmesfkkegriga
>d1baza_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
skmpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1bazb_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
kmpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfk
>d1bazc_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegrig
>d1bazd_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfk
>d1bdta_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegrig
>d1bdtb_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1bdtc_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegr
>d1bdtd_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegr
>d1bdva_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegrig
>d1bdvb_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1bdvc_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkeg
>d1bdvd_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegr
>d1myka_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
kmlqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegrig
>d1mykb_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
kmlqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegr
>d1myla_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
kmpqfnlrwprevldlvrkvaeengmsvnsyiyqlvmesfkkegr
>d1mylb_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mpqfnlrwprevldlvrkvaeengmsvnsyiyqlvmesfk
>d1mylc_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mpqfnlrwprevldlvrkvaeengmsvnsyiyqlvmesfkkegri
>d1myld_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mpqfnlrwprevldlvrkvaeengmsvnsyiyqlvmesfkkegri
>d1myle_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mpqfnlrwprevldlvrkvaeengmsvnsyiyqlvmesfkk
>d1mylf_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mpqfnlrwprevldlvrkvaeengmsvnsyiyqlvmesfk
>d1para_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegrig
>d1parb_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1parc_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegr
>d1pard_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1qtga_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqflnrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1qtgb_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqflnrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1mnta_ 1.45.1.1.2 Mnt repressor {Bacteriophage p22 (Salmonella)}
arddphfnfrmpmevreklkfraeangrsmnsellqivqdalskpspvtgyrndaerlad
eqselv
>d1b01a_ 1.45.1.2.1 Transcriptional repressor CopG {Streptococcus agalactiae}
mkkrltitlsesvlenlekmaremglsksamisvalenykkgq
>d1b01b_ 1.45.1.2.1 Transcriptional repressor CopG {Streptococcus agalactiae}
mkkrltitlsesvlenlekmaremglsksamisvalenykkgq
>d2cpga_ 1.45.1.2.1 Transcriptional repressor CopG {Streptococcus agalactiae}
mkkrltitlsesvlenlekmaremglsksamisvalenykkgq
>d2cpgb_ 1.45.1.2.1 Transcriptional repressor CopG {Streptococcus agalactiae}
mkkrltitlsesvlenlekmaremglsksamisvalenykkgqer
>d2cpgc_ 1.45.1.2.1 Transcriptional repressor CopG {Streptococcus agalactiae}
mkkrltitlsesvlenlekmaremglsksamisvalenykkg
>d1cmba_ 1.45.1.2.2 Met repressor, MetR {Escherichia coli}
aewsgeyispyaehgkkseqvkkitvsiplkvlkiltdertrrqvnnlrhatnsellcea
flhaftgqplpddadlrkersdeipeaakeimremginpetwey
>d1fvka1 1.46.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1bed_1 1.46.1.1.2 (63-126) Disulphide-bond formation facilitator (DSBA), insertion domain {Vibrio cholerae}
gnmgqamskayatmialevedkmvpvmfnrihtlrkppkdeqelrqifldegidaakfda
ayng
>d1glqa1 1.47.1.1.3 (79-209) Glutathione S-transferase {Mouse (Mus musculus), class pi}
ygknqreaaqmdmvndgvedlrgkyvtliytnyengkndyvkalpghlkpfetllsqnqg
gkafivgdqisfadynlldlllihqvlapgcldnfpllsayvarlsarpkikaflsspeh
vnrpingngkq
>d2gsta1 1.47.1.1.5 (85-217) Glutathione S-transferase {Rat (Rattus norvegicus), class mu}
lcgeteeeriradivenqvmdnrmqlimlcynpdfekqkpeflktipekmklyseflgkr
pwfagdkvtyvdflaydildqyhifepkcldafpnlkdflarfeglkkisaymkssryls
tpifsklaqwsnk
>d1gsea1 1.47.1.1.7 (81-222) Glutathione S-transferase {Human (Homo sapiens), class alpha}
lygkdikeralidmyiegiadlgemilllpvcppeekdaklalikekiknryfpafekvl
kshgqdylvgnklsradihlvellyyveeldsslissfpllkalktrisnlptvkkflqp
gsprkppmdeksleearkifrf
>d1ljra1 1.47.1.1.9 (80-244) Glutathione S-transferase {Human (Homo sapiens), class theta}
tpdhwypsdlqararvheylgwhadcirgtfgiplwvqvlgpligvqvpeekvernrtam
dqalqwledkflgdrpflagqqvtladlmaleelmqpvalgyelfegrprlaawrgrvea
flgaelcqeahsiilsileqaakktlptpspeayqamllriarip
>d1pd211 1.47.1.1.10 (76-199) Glutathione S-transferase {Rat (Rattus norvegicus), class sigma}
dlagkteleqcqvdavvdtlddfmslfpwaeenqdlkertfndlltrqaphllkdldtyl
gdkewfignyvtwadfywdicsttllvlkpdllgiyprlvslrnkvqaipaisawilkrp
qtkl
>d2gsq_1 1.47.1.1.11 (76-202) Glutathione S-transferase {Squid (Ommastrephes sloani pacificus), class sigma}
ldgktslekyrvdeitetlqdifndvvkikfapeaakeavqqnyeksckrlapflegllv
sngggdgffvgnsmtladlhcyvalevplkhtpellkdcpkivalrkrvaecpkiaaylk
krpvrdf
>d1duga1 1.47.1.1.12 (81-220) Glutathione S-transferase {Schistosoma japonicum}
lggcpkeraeismlegavldirygvsriayskdfetlkvdflsklpemlkmfedrlchkt
ylngdhvthpdfmlydaldvvlymdpmcldafpklvcfkkrieaipqidkylksskyiaw
plqgwqatfgggdhppksdp
>d1gnwa1 1.47.1.1.14 (86-211) Glutathione S-transferase {Mouse-ear cress (Arabidopsis thaliana)}
lqtdsknisqyaimaigmqvedhqfdpvasklafeqifksiyglttdeavvaeeeaklak
vldvyearlkefkylagetftltdlhhipaiqyllgtptkklfterprvnewvaeitkrp
asekvq
>d1aw9_1 1.47.1.1.16 (83-217) Glutathione S-transferase {Maize (Zea mays), type III}
gtdllpatasaaklevwleveshhfypnasplvfqllvrpllggapdaavvdkhaeqlak
vldvyeahlarnkylagdeftladanhasyllylsktpkaglvaarphvkawweaivarp
afqktvaaiplpppp
>d1a0fa1 1.47.1.1.17 (81-201) Glutathione S-transferase {Escherichia coli}
qllapvnsisryktiewlnyiatelhkgftplfrpdtpeeykptvraqlekklqyvneal
kdehwicgqrftiadaylftvlrwayavklnleglehiaafmqrmaerpevqdalsaegl
k
>d1f2ea1 1.47.1.1.19 (81-201) Glutathione S-transferase {Sphingomonas paucimobilis}
glapaegsldryrllsrlsflgsefhkafvplfapatsdeakaaaaesvknhlaaldkel
agrdhyagnafsvadiylyvmlgwpayvgidmaaypalgayagkiaqrpavgaalkaegl
a
>d1bmta1 1.48.1.1.1 (651-740) Methionine synthase domain {Escherichia coli}
qaewrswevnkrleyslvkgitefieqdteearqqatrpieviegplmdgmnvvgdlfge
gkmflpqvvksarvmkqavaylepfieask
>d2tpt_1 1.48.2.1.1 (1-70) Thymidine phosphorylase {Escherichia coli}
lflaqeiirkkrdghalsdeeirffingirdntisegqiaalamtiffhdmtmpervslt
mamrdsgtvl
>d1brwa1 1.48.2.1.2 (1-70) Pyrimidine nucleoside phosphorylase {Bacillus stearothermophilus}
mrmvdliakkrdgkaltkeeiewivrgytngdipdyqmsalamaiyfrgmteeetaaltm
amvqsgemld
>d1bg1a1 1.49.1.1.2 (136-321) STAT3b {Mouse (Mus musculus)}
vvtekqqmleqhlqdvrkrvqdleqkmkvvenlqddfdfnyktlksqgdmqdlngnnqsv
trqkmqqleqmltaldqmrrsivselagllsameyvqktltdeeladwkrrqqiaciggp
pnicldrlenwitslaesqlqtrqqikkleelqqkvsykgdpivqhrpmleerivelfrn
lmksaf
>d1ez3a_ 1.49.2.1.1 Syntaxin 1A N-terminal domain {Rat (Rattus norvegicus)}
rdrfmdeffeqveeirgfidkiaenveevkrkhsailaspnpdektkeeleelmsdikkt
ankvrsklksieqsieqeeglnrssadlrirktqhstlsrkfvevmseynatqsdyrerc
kgri
>d2cbla2 1.50.1.1.1 (47-177) N-terminal domain of cbl (N-cbl) {Human (Homo sapiens)}
ppgtvdkkmvekcwklmdkvvrlcqnpklalknsppyildllpdtyqhlrtilsryegkm
etlgeneyfrvfmenlmkktkqtislfkegkermyeensqprrnltklslifshmlaelk
gifpsglfqgd
>d1de4c1 1.50.2.1.1 (609-756) Transferrin receptor ectodomain, C-terminal domain {Human (Homo sapiens)}
ldyerynsqllsfvrdlnqyradikemglslqwlysargdffratsrlttdfgnaektdr
fvmkklndrvmrveyhflspyvspkespfrhvfwgsgshtlpallenlklrkqnngafne
tlfrnqlalatwtiqgaanalsgdvwdi
>d1eo0a_ 1.50.3.1.1 Transcription elongation factor TFIIS N-domain {Yeast (Saccharomyces cerevisiae)}
mdskevlvhvknleknksndaavleilhvldkefvptekllretkvgvevnkfkkstnve
isklvkkmisswkdain
>d1cfaa_ 1.51.1.1.1 C5a anaphylotoxin {Human (Homo sapiens)}
mlqkkieeiaakykhsvvkkccydgasvnndetceqraarislgprcikafteccvvasq
lranishkdmc
>d1c5a__ 1.51.1.1.2 C5a anaphylotoxin {Pig (Sus scrofa domestica)}
mlqkkieeeaakykyamlkkccydgayrnddetceeraarikigpkcvkafkdccyianq
vraeqs
>d2occh_ 1.52.1.1.1 Cytochrome c oxidase subunit h {Bovine (Bos taurus)}
kiknyqtapfdsrfpnqnqtrncwqnyldfhrcekamtakggdvsvcewyrrvykslcpi
swvstwddrraegtfpgki
>d1hyp__ 1.53.1.1.1 Soybean hydrophobic protein {Soybean (Glycine max)}
pscpdlsiclnilggslgtvddccaligglgdieaivclciqlralgilnlnrnlqliln
scgrsypsnatcprt
>d1rzl__ 1.53.1.1.5 Plant non-specific lipid-transfer protein (ns-LTP) {Rice (Oryza sativa)}
itcgqvnsavgpcltyarggagpsaaccsgvrslkaaasttadrrtacnclknaargikg
lnagnaasipskcgvsvpytisasidcsrvs
>d1hssa_ 1.53.1.2.1 0.19 alpha-amylase inhibitor {Wheat (Triticum aestivum)}
mcypgqafqvpalpacrpllrlqcngsqvpeavlrdccqqlahisewcrcgalysmldsm
ykehgaqegqagtgafprcrrevvkltaasitavcrlpivvdasgdgayvckdvaaypda
>d1bea__ 1.53.1.2.3 Hageman factor/amylase inhibitor {Maize (Zea mays)}
scvpgwaiphnplpscrwyvtsrtcgigprlpwpelkrrccreladipaycrctalsilm
dgaippgpdaqlegrledlpgcprevqrgfaatlvteaecnlatisgvaecpwilg
>e1pnb.1a 1.53.1.3.1 Napin BNIb {Rape (Brassica napus)}
qpqkcqrefqqeqhlracqqwirqqlagspf
>e1pnb.1b 1.53.1.3.1 Napin BNIb {Rape (Brassica napus)}
qsgpqqgpwlreqccnelyqedqvcvcptlkqaaksvrvqgqhgpfqstriyqiaknlpn
vcnmkqigtcpfiai
>d1a1ua_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
eyftlqirgrerfekireynealelkdaq
>d1a1uc_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
eyftlqirgrerfekireynealelkdaq
>d1aie__ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
eyftlqirgrerfemfrelnealelkdaqag
>d1c26a_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
geyftlqirgrerfemfrelnealelkdaqag
>d1olga_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1olgb_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1olgc_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1olgd_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1olha_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1olhb_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1olhc_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1olhd_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1pesa_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
geyftlqirgrerfemfrelnealelkdaqa
>d1pesb_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
geyftlqirgrerfemfrelnealelkdaqa
>d1pesc_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
geyftlqirgrerfemfrelnealelkdaqa
>d1pesd_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
geyftlqirgrerfemfrelnealelkdaqa
>d1peta_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
geyftlqirgrerfemfrelnealelkdaqa
>d1petb_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
geyftlqirgrerfemfrelnealelkdaqa
>d1petc_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
geyftlqirgrerfemfrelnealelkdaqa
>d1petd_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
geyftlqirgrerfemfrelnealelkdaqa
>d1saea_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1saeb_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1saec_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1saed_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1safa_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1safb_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1safc_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1safd_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1saga_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1sagb_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1sagc_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1sagd_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1saha_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1sahb_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1sahc_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1sahd_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1saia_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1saib_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1saic_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1said_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1saja_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1sajb_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1sajc_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1sajd_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1saka_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1sakb_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1sakc_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1sakd_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1sala_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1salb_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1salc_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1sald_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d3saka_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d3sakb_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d3sakc_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d3sakd_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1adt_1 1.55.1.1.1 (176-265) Domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
pivsawekgmeaaralmdkyhvdndlkanfkllpdqvealaavcktwlneehrglqltft
snktfvtmmgrflqaylqsfaevtykhhep
>d1ihfa_ 1.56.1.1.1 Integration host factor (IHF) {Escherichia coli}
altkaemseylfdklglskrdakelvelffeeirralengeqvklsgfgnfdlrdknqrp
grnpktgedipitarrvvtfrpgqklksrvenaspk
>d1ihfb_ 1.56.1.1.1 Integration host factor (IHF) {Escherichia coli}
mtkselierlatqqshipaktvedavkemlehmastlaqgerieirgfgsfslhyraprt
grnpktgdkvelegkyvphfkpgkelrdraniyg
>d1hnr__ 1.56.1.1.2 DNA-binding domain of H1 protein, (H-NS) {Escherichia coli}
aqrpakysyvdengetktwtgqgrtpavikkamdeqgkslddflikq
>d1hns__ 1.56.1.1.2 DNA-binding domain of H1 protein, (H-NS) {Escherichia coli}
aqrpakysyvdengetktwtgqgrtpavikkamdeqgkslddflikq
>d1huua_ 1.56.1.1.3 HU protein {Bacillus stearothermophilus}
mnktelinavaetsglskkdatkavdavfdsitealrkgdkvqligfgnfevreraarkg
rnpqtgeemeipaskvpafkpgkalkdavk
>d1b8za_ 1.56.1.1.4 HU protein {Thermotoga maritima}
mnkkelidrvakkagakkkdvklildtiletitealakgekvqivgfgsfevrkaaarkg
vnpqtrkpitiperkvpkfkpgkalkekvk
>d1wtua_ 1.56.1.1.5 Transcription factor 1, TF1 {Phage SPO1 (Bacillus subtilis)}
mnktelikaiaqdteltqvsvskmlasfekittetvakgdkvqltgflnikpvarqarkg
fnpqtqealeiapsvgvsvkpgeslkkaaeglkyedfak
>d1alo_1 1.57.1.1.1 (81-193) Aldehyde oxidoreductase, domain 2 {Desulfovibrio gigas}
qpenlhplqkawvlhggaqcgfcspgfivsakglldtnadpsredvrdwfqkhrnacrct
gykplvdavmdaaavingkkpetdlefkmpadgriwgskyprptavakvtgtl
>d1qj2a1 1.57.1.1.3 (82-161) Carbon monoxide (CO) dehydrogenase iron-sulfur protein, C-domain {Pseudomonas carboxydovorans}
apdgtlsalqegfrmmhglqcgyctpgmimrshrllqenpspteaeirfgiggnlcrctg
yqnivkaiqyaaakingvpf
>d1dj8a_ 1.58.1.1.1 Protein HNS-dependent expression A; HdeA {Escherichia coli}
nkkpvnswtcedflavdesfqptavgfaealnnkdkpedavldvqgiatvtpaivqactq
dkqanfkdkvkgewdkikk
>d1af7_1 1.59.1.1.1 (11-91) Chemotaxis receptor methyltransferase CheR, N-terminal domain {Salmonella typhimurium}
svllqmtqrlalsdahfrricqliyqragivladhkrdmvynrlvrrlralglddfgryl
smleanqnsaewqafinaltt
>d1bqv__ 1.60.1.1.1 Ets-1 transcription factor pointed domain {Mouse (Mus musculus)}
mecadvplltpsskemmsqalkatfsgftkeqqrlgipkdprqwtethvrdwvmwavnef
slkgvdfqkfcmsgaalcalgkecflelapdfvgdilwehleilqkedvk
>d1b0xa_ 1.60.1.2.1 EphA4 receptor tyrosine kinases {Mouse (Mus musculus)}
fsavvsvgdwlqaikmdrykdnftaagyttleavvhmsqddlarigitaithqnkilssv
qamrtqmqqmhg
>d1b4fa_ 1.60.1.2.2 EphB2 receptor {Human (Homo sapiens)}
pdytsfntvdewleaikmgqykesfanagftsfdvvsqmmmedilrvgvtlaghqkkiln
siqvmraqmnqiqs
>d1coka_ 1.60.1.2.4 C-terminal domain of p73 {Human (Homo sapiens)}
yhadpslvsfltglgcpncieyftsqglqsiyhlqnltiedlgalkipeqyrmtiwrglq
dlkqghdy
>d1cuk_2 1.60.2.1.1 (65-142) DNA helicase RuvA subunit, middle domain {Escherichia coli}
nkqertlfkeliktngvgpklalailsgmsaqqfvnavereevgalvklpgigkktaerl
ivemkdrfkglhgdlftp
>d1bvsa2 1.60.2.1.2 (64-134) DNA helicase RuvA subunit, middle domain {Mycobacterium leprae}
daenrdlflallsvsgvgprlamatlavhdaaalrqaladsdvasltrvpgigrrgaeri
vleladkvgpv
>d1coo__ 1.60.3.1.1 C-terminal domain of RNA polymerase alpha subunit {Escherichia coli}
fdpillrpvddleltvrsanclkaeaihyigdlvqrtevellktpnlgkkslteikdvla
srglslgmrlenwppasiade
>d1doqa_ 1.60.3.1.2 C-terminal domain of RNA polymerase alpha subunit {Thermus thermophilus}
eqeeeldlpleelglstrvlhslkeegiesvrallalnlkdlknipgigersleeikeal
ekkgftlke
>d1b22a_ 1.60.4.1.1 DNA repair protein Rad51, N-terminal domain {Human (Homo sapiens)}
eeesfgpqpisrleqcginandvkkleeagfhtveavayapkkelinikgiseakadkil
aeaaklvpmg
>d2ezya_ 1.60.5.1.1 Barrier-to-autointegration factor, BAF {Human (Homo sapiens)}
mttsqkhrdfvaepmgekpvgslagigevlgkkleergfdkayvvlgqflvlkkdedlfr
ewlkdtcganakqsrdcfgclrewcdafl
>d1bpya1 1.60.6.1.1 (10-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
tlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtki
aekideflatgklrklekirqd
>d1tfr_1 1.60.7.1.1 (183-305) T4 RNase H {Bacteriophage T4}
gsaeidcmtkilkgdkkdnvasvkvrsdfwftrvegertpsmktsiveaiandreqakvl
lteseynrykenlvlidfdyipdniasnivnyynsyklpprgkiysyfvkaglskltnsi
nef
>d1bgxt1 1.60.7.1.2 (174-289) 5' to 3' exonuclease domain of DNA polymerase <i>Taq</i> {Thermus aquaticus}
lrpdqwadyraltgdesdnlpgvkgigektarklleewgsleallknldrlkpairekil
ahmddlklswdlakvrtdlplevdfakrrepdrerlraflerlefgsllhefglle
>d1xo1a1 1.60.7.1.3 (186-290) T5 5'-exonuclease {Bacteriophage T5}
vddveqfislkaimgdlgdnirgvegigakrgyniirefgnvldiidqlplpgkqkyiqn
lnaseellfrnlilvdlptycvdaiaavgqdvldkftkdileiae
>d1a77_1 1.60.7.1.4 (209-316) Flap endonuclease-1 {Methanococcus jannaschii}
islddlidiaifmgtdynpggvkgigfkrayelvrsgvakdvlkkeveyydeikrifkep
kvtdnyslslklpdkegiikflvdendfnydrvkkhvdklynliankt
>d1b43a1 1.60.7.1.5 (220-339) Fen-1 nuclease {Pyrococcus furiosus}
ltreklielailvgtdynpggikgiglkkaleivrhskdplakfqkqsdvdlyaikeffl
nppvtdnynlvwrdpdeegilkflcdehdfseervknglerlkkaiksgkqstleswfkr
>d1bmy__ 1.60.8.1.1 MRF-2 DNA-binding domain {Human (Homo sapiens)}
radeqaflvalykymkerktpieripylgfkqinlwtmfqaaqklggyetitarrqwkhi
ydelggnpgstsaatctrrhyerlilpyerfikgeedkplppikprk
>d1d8ba_ 1.60.9.1.1 HRDC domain from RecQ helicase {Baker's yeast (Saccharomyces cerevisiae)}
elnnlrmtyerlrelslnlgnrmvppvgnfmpdsilkkmaailpmndsafatlgtvedky
rrrfkyfkatiadlskkrsse
>d4crxa1 1.60.10.1.1 (20-129) Cre recombinase {Bacteriophage P1}
sdevrknlmdmfrdrqafsehtwkmllsvcrswaawcklnnrkwfpaepedvrdyllylq
arglavktiqqhlgqlnmlhrrsglprpsdsnavslvmrrirkenvdage
>d1a0p_1 1.60.10.1.2 (3-100) Recombinase XerD {Escherichia coli}
qdlarieqfldalwleknlaentlnayrrdlsmmvewlhhrgltlataqsddlqallaer
leggykatssarllsavrrlfqylyrekfreddpsahl
>d1zyma1 1.60.11.1.1 (22-144) Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain {Escherichia coli}
deividrkkisadqvdqeverflsgrakasaqletiktkagetfgeekeaifeghimlle
deeleqeiialikdkhmtadaaaheviegqasaleelddeylkeraadvrdigkrllrni
lgl
>d1ed1a_ 1.61.1.1.2 SIV matrix antigen {Simian immunodeficiency virus}
svlsgkkadelekirlrpggkkkymlkhvvwaaneldrfglaesllenkegcqkilsvla
plvptgsenlkslyntvcviwcihaeekvkhteeakqivqrhlvvetgtaetmp
>d1jvr__ 1.61.1.2.1 HTLV-II matrix protein {Human t-cell leukemia virus type II, TTLV-II}
hmgqihglsptpipkaprglsthhwlnflqaayrlqpgpsdfdfqqlrrflklalktpiw
lnpidysllaslipkgypgrvveiinilvknqvspsapaapvptpicptttpppppppsp
eahvpppyveptttqcf
>d1bax__ 1.61.1.3.1 Mason-pfizer monkey virus matrix protein {Simian mason-pfizer virus, MPMV}
mgqelsqheryveqlkqalktrgvkvkyadllkffdfvkdtcpwfpqegtidikrwrrvg
dcfqdyyntfgpekvpvtafsywnlikelidkke
>d1a6s__ 1.61.1.4.1 GAG polyprotein M-domain {Rous sarcoma virus, RSV}
geavikvissacktycgktspskkeigamlsllqkegllmspsdlyspgswdpitaalsq
ramilgksgelktwglvlgalkaaree
>d1qgta_ 1.62.1.1.1 Hepatitis B viral capsid (hbcag) {Hepatitis B virus, HBV}
mdidpykefgatvellsflpsdffpsvrdlldtasalyrealespehcsphhtalrqail
cwgelmtlatwvgnnledpasrdlvvnyvntnmglkirqllwfhiscltfgretvleylv
sfgvwirtppayrppnapilst
>d1aep__ 1.63.1.1.1 Apolipophorin-III {African locust (Locusta migratoria)}
niaeavqqlnhtivnaahelhetlglptpdealnllteqanafktkiaevttslkqeaek
hqgsvaeqlnafarnlnnsihdaatslnlqdqlnslqsaltnvghqwqdiatktqasaqe
awapvqsalqeaaektkeaaanlqnsiqsavqk
>d1nkl__ 1.64.1.1.1 NK-lysin {Pig (Sus scrofa)}
gyfcescrkiiqkledmvgpqpnedtvtqaasqvcdklkilrglckkimrsflrriswdi
ltgkkpqaicvdikicke
>d1qdma1 1.64.1.2.1 (1s-104s) (Pro)phytepsin {Barley (Hordeum vulgare)}
vvsqecktivsqygqqildlllaetqpkkicsqvglctfdgtrgvsagirsvvddepvks
nglradpmcsacemavvwmqnqlaqnktqdlildyvnqlcnrlp
>d1bo9a_ 1.65.1.1.1 Annexin I {Human (Homo sapiens)}
tfnpssdvaalhkaimvkgvdeatiidiltkrnnaqrqqikaaylqetgkpldetlkkal
tghleevvlallk
>d1axn__ 1.65.1.1.2 Annexin III {Human (Homo sapiens)}
sasiwvghrgtvrdypdfspsvdaeaiqkairgigtdekmlisiltersnaqrqlivkey
qaaygkelkddlkgdlsghfehlmvalvtppavfdakqlkksmkgagtnedalieilttr
tsrqmkdisqayytvykkslgddissetsgdfrkalltladgrrdeslkvdehlakqdaq
ilykagenrwgtdedkfteilclrsfpqlkltfdeyrnisqkdivdsikgelsghfedll
laivncvrntpaflaerlhralkgigtdeftlnrimvsrseidlldirtefkkhygysly
saiksdtsgdyeitllkicggdd
>d1a8a__ 1.65.1.1.6 Annexin V {Rat (Rattus norvegicus)}
alrgtvtdfsgfdgradaevlrkamkglgtdedsilnlltarsnaqrqqiaeefktlfgr
dlvndmkseltgkfeklivalmkpsrlydayelkhalkgagtdekvlteiiasrtpeelr
aikqayeeeygsnleddvvgdtsgyyqrmlvvllqanrdpdtaiddaqveldaqalfqag
elkwgtdeekfitilgtrsvshlrrvfdkymtisgfqieetidretsgnlenlllavvks
irsipaylaetlyyamkgagtddhtlirvivsrseidlfnirkefrknfatslysmikgd
tsgdykkallllcggedd
>d1dm5a_ 1.65.1.1.9 Annexin XII {Hydra vulgaris}
vvqgtvkphasfnsredaetlrkamkgigtdeksithilatrsnaqrqqiktdyttlfgk
hledelkselsgnyeaaalallrkpdeflaeqlhaamkglgtdknalidilctqsnaqih
aikaafkllykedlekeiisetsgnfqrllvsmlqggrkedepvnaahaaedaaaiyqag
egqigtdesrfnavlatrsypqlhqifheyskisnktilqaienefsgdikngllaivks
venrfayfaerlhhamkglgtsdktlirilvsrseidlaniketfqamygkslyefiadd
csgdykdlllqitgh
>d1azsc1 1.66.1.1.1 (86-201) Transducin (alpha subunit), insertion domain {Bovine (Bos taurus)}
gfngdgekatkvqdiknnlkeaietivaamsnlvppvelanpenqfrvdyilsvmnvpdf
dfppefyehakalwedegvracyersneyqlidcaqyfldkidvikqddyvpsdqdllrc
r
>d1cipa1 1.66.1.1.2 (61-181) Transducin (alpha subunit), insertion domain {Rat (Rattus rattus)}
yseeeckqykavvysntiqsiiaiiramgrlkidfgdaaraddarqlfvlagaaeegfmt
aelagvikrlwkdsgvqacfnrsreyqlndsaayylndldriaqpnyiptqqdvlrtrvk
t
>d1ezm_1 1.67.1.1.1 (154-298) Elastase {Pseudomonas aeruginosa}
iyrgqsggmneafsdmageaaefymrgkndfligydikkgsgalrymdqpsrdgrsidna
sqyyngidvhhssgvynrafyllanspgwdtrkafevfvdanryywtatsnynsgacgvi
rsaqnrnysaadvtrafstvgvtcp
>d8tlne1 1.67.1.1.2 (156-316) Thermolysin {Bacillus thermoproteolyticus}
iyqnesgaineaisdifgtlvefyanknpdweigedvytpgisgdslrsmsdpakygdpd
hyskrytgtqdnggvhinsgiinkaaylisqggthygvsvvgigrdklgkifyraltqyl
tptsnfsqlraaavqsatdlygstsqevasvkqafdavgvk
>d1ej5a_ 1.68.1.1.1 Wiscott-Aldrich syndrome protein, WASP, C-terminal domain {Human (Homo sapiens)}
sgfkhvshvgwdpqngfdvnnldpdlrslfsragiseaqltdaetskliydfiedqggle
avrqemrrqggsggsqsseglvgalmhvmqkrsraihssdegedqag
>d1bmfa1 1.69.1.1.1 (380-510) C-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
tramkqvagtmklelaqyrevaafaqfgsdldaatqqllsrgvrltellkqgqyspmaie
eqvaviyagvrgyldklepskitkfenaflshvisqhqallgkirtdgkiseesdaklke
ivtnflagfea
>d1bmfd1 1.69.1.1.1 (358-475) C-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
mdpnivgsehydvargvqkilqdykslqdiiailgmdelseedkltvsrarkiqrflsqp
fqvaevftghlgklvplketikgfqqilageydhlpeqafymvgpieeavakadklae
>d1skyb1 1.69.1.1.3 (372-502) C-terminal domain of alpha and beta subunits of F1 ATP synthase {Bacillus ps3}
ikamkkvagtlrldlaayreleafaqfgsdldkatqanvargartvevlkqdlhqpipve
kqvliiyaltrgflddipvedvrrfekefylwldqngqhllehirttkdlpneddlnqai
eafkktfvvsq
>d1abv__ 1.70.1.1.1 N-terminal domain of the delta subunit of the F1F0-ATP synthase {Escherichia coli}
sefitvarpyakaafdfavehqsverwqdmlafaaevtkneqmaellsgalapetlaesf
iavcgeqldengqnlirvmaengrlnalpdvleqfihlravseat
>d1dvka_ 1.71.1.1.1 Functional domain of the splicing factor Prp18 {Baker's yeast (Saccharomyces cerevisiae)}
mriqeaiaqdktisviidpsqigstegkpllsmkcnlyiheilsrwkasleayhpelfld
tkkalfplllqlrrnqlapdllislatvlyhlqqpkeinlavqsymklsignvawpigvt
svgiharsahskiqggrnaanimidertrlwitsikrlitfeewytsnh
>d1ak4c_ 1.72.1.1.1 HIV-1 capsid protein {Human immunodeficiency virus, type 1, HIV-1}
pivqnlqgqmvhqaisprtlnawvkvveekafspevipmfsalsegatpqdlntmlntvg
ghqaamqmlketineeaaewdrlhpvhagpiapgqmreprgsdiagttstlqeqigwmth
nppipvgeiykrwiilglnkivrmy
>d2eiaa2 1.72.1.1.2 (17-147) EIAV capsid protein p26 {Equine infectious anemia virus, EIAV}
prgyttwvntiqtngllneasqnlfgilsvdctseemnafldvvpgqagqkqilldaidk
iaddwdnrhplpnaplvappqgpipmtarfirglgvprerqmepafdqfrqtyrqwiiea
msegikvmigk
>e1qrj.1b 1.72.1.1.3 (16-130) HTLV-I capsid protein {Human t-cell leukemia virus type i, HTLV-I}
qmkdlqaikqevsqaapgspqfmqtirlavqqfdptakdlqdllqylcsslvaslhhqql
dsliseaetrgitgynplagplrvqannpqqqglrreyqqlwlaafaalpgsakd
>d1d1da2 1.72.1.1.4 (11-150) RSV capsid protein {Rous sarcoma virus, RSV}
wtplepklitrladtvrtkglrspitmaevealmsspllphdvtnlmrvilgpapyalwm
dawgvqlqtviaaatrdprhpangqgrgertnldrlkgladgmvgnpqgqaallrpgelv
aitasalqafrevarlaepa
>d1vin_1 1.73.1.1.2 (181-308) Cyclin A {Bovine (Bos taurus)}
dihtylremevkckpkvgymkkqpditnsmrailvdwlvevgeeyklqnetlhlavnyid
rflssmsvlrgklqlvgtaamllaskfeeiyppevaefvyitddtytkkqvlrmehlvlk
vlafdlaa
>d1vin_2 1.73.1.1.2 (309-432) Cyclin A {Bovine (Bos taurus)}
ptinqfltqyflhqqpanckveslamflgelslidadpylkylpsviaaaafhlalytvt
gqswpeslvqktgytletlkpclldlhqtylrapqhaqqsirekyknskyhgvsllnppe
tlnl
>d1jkw_1 1.73.1.1.3 (11-161) Cyclin H (mcs2) {Human (Homo sapiens)}
wtfsseeqlarlradanrkfrckavangkvlpndpvflepheemtlckyyekrllefcsv
fkpamprsvvgtacmyfkrfylnnsvmeyhpriimltcaflackvdefnvsspqfvgnlr
esplgqekaleqileyellliqqlnfhlivh
>d1jkw_2 1.73.1.1.3 (162-287) Cyclin H (mcs2) {Human (Homo sapiens)}
npyrpfegflidlktrypilenpeilrktaddflnrialtdayllytpsqialtailssa
sragitmesylseslmlkenrtclsqlldimksmrnlvkkyepprseevavlkqkldrch
saelal
>d1bu2a1 1.73.1.1.4 (22-148) Viral cyclin {Herpes virus saimiri}
rvlnnlklrelllpkftslweiqtevtvdnrtilltwmhllcesfeldksvfplsvsild
rylckkqgtkktlqkigaacvligskirtvkpmtvskltylscdcftnlelinqekdile
alkwdte
>d1bu2a2 1.73.1.1.4 (149-250) Viral cyclin {Herpes virus saimiri}
avlatdfliplcnalkipedlwpqlyeaasttickaliqpniallspglicaggllttie
tdntncrpwtcyledlssilnfstntvrtvkdqvseafslyd
>d1vola1 1.73.1.2.1 (113-207) Transcription factor IIB (TFIIB), core domain {Human (Homo sapiens)}
ammnafkeittmadrinlprnkvdrtnnlfrqayeqkslkgrandaiasaclyiacrqeg
vprtfkeicavsriskkeigrcfklilkaletsvd
>d1vola2 1.73.1.2.1 (208-316) Transcription factor IIB (TFIIB), core domain {Human (Homo sapiens)}
littgdfmsrfcsnlclpkqvqmaathiarkaveldlvpgrspisvaaaaiymasqasae
krtqkeigdiagvadvtirqsyrliyprapdlfptdfkfdtpvdklpql
>d1aisb1 1.73.1.2.2 (1108-1205) Transcription factor IIB (TFIIB), core domain {Pyrococcus woesei}
nlafalseldritaqlklprhveeeaarlyreavrkglirgrsiesvmaacvyaacrllk
vprtldeiadiarvdkkeigrsyrfiarnlnltpkklf
>d1aisb2 1.73.1.2.2 (1206-1300) Transcription factor IIB (TFIIB), core domain {Pyrococcus woesei}
vkptdyvnkfadelglsekvrrraieildeaykrgltsgkspaglvaaalyiasllegek
rtqrevaevarvtevtvrnrykelveklkikvpia
>d1guxa_ 1.73.1.3.1 Retinoblastoma tumor suppressor domains {Human (Homo sapiens)}
ntiqqlmmilnsasdqpsenlisyfnnctvnpkesilkrvkdigyifkekfakavgqgcv
eigsqryklgvrlyyrvmesmlkseeerlsiqnfskllndnifhmsllacalevvmatys
rstsqnldsgtdlsfpwilnvlnlkafdfykviesfikaegnltremikhlercehrime
slawlsdsplfdlikqsk
>d1guxb_ 1.73.1.3.1 Retinoblastoma tumor suppressor domains {Human (Homo sapiens)}
tslslfykkvyrlaylrlntlcerllsehpelehiiwtlfqhtlqneyelmrdrhldqim
mcsmygickvknidlkfkiivtaykdlphavqetfkrvlikeeeydsiivfynsvfmqrl
ktnilqyastrpptlspiphi
>d1rss__ 1.74.1.1.2 Ribosomal protein S7 {Thermus thermophilus}
lqpdlvygdvlvtafinkimrdgkknlaarifydackiiqektgqeplkvfkqavenvkp
rmevrsrrvgganyqvpmevsprrqqslalrwlvqaanqrperraavriahelmdaaegk
ggavkkkedvermaeanrayahyrw
>d1bi1_2 1.75.1.1.1 (65-140) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
tptgrtlatavmrkhrlaerlltdiigldinkvhdeaxrwehvmsdeverrlvkvlkdvs
rspfgnpipgldelgv
>d1ddna2 1.75.1.1.1 (65-120) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
tptgrtlatavmrkhrlaerlltdiigldinkvhdeadrwehvmsdeverrlvkvl
>d1b1ba2 1.75.1.1.2 (65-140) Iron-dependent regulator {Mycobacterium tuberculosis}
tekgralaiavmrkhrlaerllvdviglpweevhaeacrwehvmsedverrlvkvlnnpt
tspfgnpipglvelgv
>d1ngr__ 1.76.1.1.1 p75 low affinity neurotrophin receptor {Rat (Rattus norvegicus)}
gnlysslpltkreevekllngdtwrhlagelgyqpehidsftheacpvrallaswgaqds
atldallaalrriqradiveslcse
>d1ddf__ 1.76.1.1.2 Fas {Human (Homo sapiens)}
metvainlsdvdlskyittiagvmtlsqvkgfvrkngvneakideikndnvqdtaeqkvq
llrnwhqlhgkkeaydtlikdlkkanlctlaekiqtiilkditsdsensnfrneiqslvl
ehhhhhh
>d1a1w__ 1.76.1.1.3 FADD (Mort1) {Human (Homo sapiens)}
mdpflvllhsvssslssseltelkylclgrvgkrklervqsgldlfsmlleqndlepght
ellrellaslrrhdllrrvddfe
>d1fada_ 1.76.1.1.4 FADD (Mort1) {Mouse (Mus musculus)}
aappgeaylqvafdivcdnvgrdwkrlarelkvseakmdgieekyprslservreslkvw
knaekknasvaglvkalrtcrlnlvadlveeaqes
>d3crd__ 1.76.1.1.5 Raidd CARD domain {Human (Homo sapiens)}
meardkqvlrslrlelgaevlveglvlqylyqegiltenhiqeinaqttglrktmllldi
lpsrgpkafdtfldslqefpwvreklkkareeamtdlpag
>d1cy5a_ 1.76.1.1.6 Apoptotic protease activating factor 1, APAF-1 {Human (Homo sapiens)}
mdakarncllqhrealekdiktsyimdhmisdgfltiseeekvrneptqqqraamlikmi
lkkdndsyvsfynallhegykdlaallhdgipv
>d3ygsp_ 1.76.1.1.7 Procaspase 9 prodomain {Human (Homo sapiens)}
smdeadrrllrrcrlrlveelqvdqlwdvllsrelfrphmiediqragsgsrrdqarqli
idletrgsqalplfiscledtgqdmlasflrtnrqag
>d1d2za_ 1.76.1.1.8 Pelle death domain {Drosophila melanogaster}
ldntmairllplpvraqlcahldaldvwqqlatavklypdqveqissqkqrgrsasnefl
niwggqynhtvqtlfalfkklklhnamrlikdyvsedlhkyi
>d1d2zb_ 1.76.1.1.9 Tube death domain {Drosophila melanogaster}
lsskysrntelrrvedndiyrlakildenscwrklmsiipkgmdvqacsgagclnfpaei
kkgfkytaqdvfqideaanrlppdqsksqmmidewktsgklnerptvgvllqllvqaelf
saadfvaldflnestparpvdgpgalisle
>d1eyva_ 1.77.1.1.1 Antitermination factor NusB {Mycobacterium tuberculosis}
grhqarkravallfeaevrgisaaevvdtraalaeakpdiarlhpytaavargvsehaah
iddlitahlrgwtldrlpavdrailrvsvwellhaadvpepvvvdeavqlakelstddsp
gfvngvlgqvm
>d1baq__ 1.77.1.1.2 Antitermination factor NusB {Escherichia coli}
mkpaarrrarecavqalyswqlsqndiadveyqflaeqdvkdvdvlyfrellagvatnta
yldglmkpylsrlleelgqvekavlrialyelskrsdvpykvaineaielaksfgaedsh
kfvngvldkaapvirpnkk
>d1b79a_ 1.78.1.1.1 N-terminal domain of DnaB helicase {Escherichia coli}
pphsieaeqsvlgglmldnerwddvaervvaddfytrphrhiftemarlqesgspidlit
laeslerqgqldsvggfaylaelskntpsaanisayadivre
>d1qc7a_ 1.79.1.1.1 FliG C-terminal domain {Thermotoga maritima}
mfvfedilklddrsiqlvlrevdtrdlalalkgasdelkekifknmskraaallkdeley
mgpvrlkdveeaqqkiiniirrleeageiviargggeelim
>d1qh4a1 1.80.1.1.2 (2-102) Creatine kinase, N-terminal domain {Chicken (Gallus gallus), brain-type}
pfsnshnllkmkysvddeypdlsvhnnhmakvltldlykklrdrqtssgftlddviqtgv
dnpghpfimtvgcvagdeesyevfkelfdpviedrhggykp
>d1bg0_1 1.80.1.1.5 (2-95) Arginine kinase {Horseshoe crab (Limulus polyphemus)}
vdqatldkleagfkklqeasdcksllkkhltkdvfdsiknkktgmgatlldviqsgvenl
dsgvgiyapdaesyrtfgplfdpiiddyhggfkl
>d1al01_ 1.81.1.1.1 Scaffolding protein gpD of bacteriophage procapsid {Bacteriophage phi-x174}
eqsvrfqtalasikliqasavldlteddfdfltsnkvwiatdrsrarrcveacvygtldf
vgyprfpapvefiaaviayyvhpvniqtaclimegaefteniingverpvkaaelfaftl
rvragntdvltdaeenvrqklra
>d1lla_1 1.82.1.1.1 (2-109) Hemocyanin, N-terminal domain {Limulus polyphemus}
lhdkqirichlfeqlssatvigdgdkhkhsdrlknvgklqpgaifscfhpdhleearhly
evfweagdfndfieiakeartfvneglfafaaevavlhrddckglyvp
>d1hc2_1 1.82.1.1.2 (5-135) Hemocyanin, N-terminal domain {Spiny lobster (Panulirus interruptus)}
tgnaqkqqdinhlldkiyeptkypdlkdiaenfnplgdtsiyndhgaavetlmkelndhr
lleqrhwyslfntrqrkealmlfavlnqckewycfrsnaayfrermnegefvyalyvsvi
hsklgdgivlp
>d1lla_2 1.83.1.1.1 (110-379) Hemocyanin, middle domain {Limulus polyphemus}
pvqeifpdkfipsaaineafkkahvrpefdespilvdvqdtgnildpeyrlayyredvgi
nahhwhwhlvypstwnpkyfgkkkdrkgelfyymhqqmcarydcerlsngmhrmlpfnnf
deplagyaphlthvasgkyysprpdglklrdlgdieisemvrmrerildsihlgyvised
gshktldelhgtdilgalvessyesvnheyygnlhnwghvtmarihdpdgrfheepgvms
dtstslrdpifynwhrfidnifheykntlk
>d1bt3a_ 1.83.1.2.1 Catechol oxidase {Sweet potato (Ipomoea batatas)}
apiqapeiskcvvppadlppgavvdnccppvasnivdyklpavttmkvrpaahtmdkdai
akfakavelmkalpaddprnfyqqalvhcaycnggydqvnfpdqeiqvhnswlffpfhrw
ylyfyerilgkligdpsfglpfwnwdnpggmvlpdflndstsslydsnrnqshlppvvvd
lgyngadtdvtdqqritdnlalmykqmvtnagtaelflgkayragdapspgagsietsph
ipihrwvgdprntnnedmgnfysagrdiafychhsnvdrmwtiwqqlagkprkrdytdsd
wlnatflfydengqavkvrigdsldnqkmgykyaktplpwl
>d1dbha1 1.84.1.1.1 (198-404) Son of sevenless-1 (sos-1) {Human (Homo sapiens)}
eqtyydlvkafxaeirqyirelnliikvfrepfvsnsklfsandvenifsrivdihelsv
kllghiedtvextdegsphplvgscfedlaeelafdpyesyardilrpgfhdrflsqlsk
pgaalylqsigegfkeavqyvlprlllapvyhclhyfellkqleeksedqedkeclkqai
tallnvqsgxekicskslakrrlsesa
>d1by1a_ 1.84.1.1.2 beta-pix {Human (Homo sapiens)}
mkgfdttainksyynvvlqnileteneyskelqtvlstylrplqtseklssanisylmgn
leeicsfqqmlvqsleectklpeaqqrvggcflnlmpqmktlyltycanhpsavnvlteh
seelgefmetkgasspgilvlttglskpfmrldkyptllkelerhmedyhtdrqdiqksm
aafknlsaqcqevrkrkelelqilteair
>d1boua_ 1.85.1.1.1 LigA subunit of an aromatic-ring-opening dioxygenase LigAB {Pseudomonas paucimobilis}
idvhaylaefddipgtrvftaqrarkgynlnqfamslmkaenrerfkadesayldewnlt
paakaavlardynamideggnvyflsklfstdgksfqfaagsmtgmtqeeyaqmmidggr
spagvrsikggy
>d1mroa1 1.86.1.1.1 (270-549) Alpha chain {Methanobacterium thermoautotrophicum}
rxargenepggvpfgyladicqssrvnyedpvrvsldvvatgamlydqiwlgsymsggvg
ftqyataaytdnilddftyfgkeyvedkyglceapnnmdtvldvatevtfygleqyeeyp
alledqfggsxraavvaaaagcstafatgnaqtglsgwylsmylhkeqhsrlgfyxydlq
dqxgasnvfsirgdeglplelrgpnypnyamnvghqgeyagisqaphaargdafvfnplv
kiafaddnlvfdftnvrgefakgalrefepageralitpa
>d1mrob1 1.86.1.1.2 (189-443) Beta chain {Methanobacterium thermoautotrophicum}
gyalrnimvnhvvaatlkntlqaaalstileqtamfemgdavgafermhllglayqgmna
dnlvfdlvkangkegtvgsviadlveraledgvikvekeltdykvygtddlamwnayaaa
glmaatmvnqgaaraaqgvsstllyyndliefetglpsvdfgkvegtavgfsffshsiyg
gggpgifngnhivtrhskgfaipcvaaamaldagtqmfspeatsglikevfsqvdefrep
lkyvveaaaeiknei
>d1bgf__ 1.87.1.1.1 Transcription factor STAT-4 N-domain {Mouse (Mus musculus)}
ggsqwnqvqqleikfleqvdqfyddnfpmeirhllaqwietqdwevasnnetmatillqn
lliqldeqlgrvskeknlllihnlkrirkvlqgkfhgnpmhvavvisnclreerrilaaa
nmpi
>d1agre_ 1.88.1.1.1 Regulator of G-protein signalling 4, RGS4 {Rat (Rattus norvegicus)}
vsqeevkkwaeslenlinhecglaafkaflkseyseenidfwisceeykkikspsklspk
akkiynefisvqatkevnldsctreetsrnmleptitcfdeaqkkifnlmekdsyrrflk
srfyldlt
>d1a9xa1 1.89.1.1.1 (403-555) Carbamoyl phosphate synthetase, large subunit connection domain {Escherichia coli}
evgatgfdpkvslddpealtkirrelkdagadriwyiadafraglsvdgvfnltnidrwf
lvqieelvrleekvaevgitglnadflrqlkrkgfadarlaklagvreaeirklrdqydl
hpvykrvdtcaaefatdtaymystyeeeceanp
>d1aru__ 1.90.1.1.2 Peroxidase {Arthromyces ramosus}
svtcpggqstsnsqccvwfdvlddlqtnfyqgskcespvrkilrivfhdaigfspaltaa
gqfggggadgsiiahsnielafpanggltdtiealravginhgvsfgdliqfatavgmsn
cpgsprlefltgrsnssqpsppslipgpgntvtaildrmgdagfspdevvdllaahslas
qeglnsaifrspldstpqvfdtqfyietllkgttqpgpslgfaeelspfpgefrmrsdal
lardsrtacrwqsmtssnevmgqryraamakmsvlgfdrnaltdcsdvipsavsnnaapv
ipggltvddievscpsepfpeiatasgplpslapap
>d1ryc__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d7atja_ 1.90.1.1.6 Peroxidase {Horseradish (Armoracia rusticana)}
qltptfydnscpnvsnivrdtivnelrsdpriaasilrlhfhdcfvngcdasilldntts
frtekdafgnansargfpvidrmkaavesacprtvscadlltiaaqqsvtlaggpswrvp
lgrrdslqafldlananlpapfftlpqlkdsfrnvglnrssdlvalsgghtfgknqcrfi
mdrlynfsntglpdptlnttylqtlrglcplngnlsalvdfdlrtptifdnkyyvnleeq
kgliqsdqelfsspnatdtiplvrsfanstqtffnafveamdrmgnitpltgtqgqirln
crvvn
>e1cxp.1a 1.90.1.2.1 Myeloperoxidase {Human (Homo sapiens)}
cpeqdkyrtitgmcnnrrsptlgasnrafvrwlpaeyedgfslpygwtpgvkrngfpval
aravsneivrfptdqltpdqerslmfmqwgqlldhdldftpepa
>e1cxp.1c 1.90.1.2.1 Myeloperoxidase {Human (Homo sapiens)}
vncetscvqqppcfplkippndpriknqadcipffrsxpacpgsnitirnqinaltsfvd
asmvygseeplarnlrnmsnqlgllavnqrfqdngrallpfdnlhddpclltnrsaripc
flagdtrssempeltsmhtlllrehnrlatelkslnprwdgerlyqearkivgamvqiit
yrdylplvlgptamrkylptyrsyndsvdprianvftnafryghtliqpfmfrldnryqp
mepnprvplsrvffaswrvvleggidpilrglmatpaklnrqnqiavdeirerlfeqvmr
igldlpalnmqrsrdhglpgynawrrfcglpqpetvgqlgtvlrnlklarklmeqygtpn
nidiwmggvseplkrkgrvgpllaciigtqfrklrdgdrfwwenegvfsmqqrqalaqis
lpriicdntgittvsknnifmsnsyprdfvncstlpalnlaswrea
>d1cvua1 1.90.1.2.4 (74-583) Prostaglandin H2 synthase {Mouse (Mus musculus)}
fltriklllkptpntvhyilthfkgvwnivnnipflrslimkyvltsrsylidspptynv
hygyksweafsnlsyytralppvaddcptpmgvkgnkelpdskevlekvllrrefipdpq
gsnmmfaffaqhftaqffktdhkrgpgftrglghgvdlnhiygetldrqhklrlfkdgkl
kyqviggevypptvkdtqvemiypphipenlqfavgqevfglvpglmmyatiwlrehqrv
cdilkqehpewgdeqlfqtskliligetikiviedyvqhlsgyhfklkfdpellfnqqfq
yqnriasefntlyhwhpllpdtfniedqeysfkqflynnsillehgltqfvesftrqiag
rvaggrnvpiavqavakasidqsremkyqslneyrkrfslkpytsfeeltgekemaaelk
alysdidvmelypallvekprpdaifgetmvelgapfslkglmgnpicspqywkpstfgg
evgfkiintasiqslicnnvkgcpftsfnvq
>d1aa7a_ 1.91.1.1.1 Influenza virus matrix protein M1 {Influenza virus}
mslltevetyvlsiipsgplkaeiaqrledvfagkntdlevlmewlktrpilspltkgil
gfvftltvpserglqrrrfvqnalngngdpnnmdkavklyrklkreitfhgakeislsys
agalascmgliynrmgavttevafglvcatceqiadsq
>d2abk__ 1.92.1.1.1 Endonuclease III {Escherichia coli}
mnkakrleiltrlrennphpttelnfsspfelliavllsaqatdvsvnkataklypvant
paamlelgvegvktyiktiglynskaeniiktcrilleqhngevpedraalealpgvgrk
tanvvlntafgwptiavdthifrvcnrtqfapgknveqveekllkvvpaefkvdchhwli
lhgrytciarkprcgsciiedlceykekvdi
>d1mun__ 1.92.1.2.1 Catalytic domain of MutY {Escherichia coli}
mqasqfsaqvldwydkygrktlpwqidktpykvwlsevmlqqtqvatvipyferfmarfp
tvtdlanapldevlhlwtglgyyararnlhkaaqqvatlhggkfpetfeevaalpgvgrs
tagailslslgkhfpilngnvkrvlarcyavsgwpgkkevenklwslseqvtpavgverf
nqammdlgamictrskpkcslcplqngciaaannswalypgkkpk
>d1mpga1 1.92.1.3.1 (100-282) 3-Methyladenine DNA glycosylase II (gene alkA or aidA) {Escherichia coli}
aarpglrlpgcvdafeqgvrailgqlvsvamaakltarvaqlygerlddfpeyicfptpq
rlaaadpqalkalgmplkraealihlanaalegtlpmtipgdveqamktlqtfpgigrwt
anyfalrgwqakdvflpddylikqrfpgmtpaqirryaerwkpwrsyallhiwytegwqp
dea
>d1ebma1 1.92.1.3.2 (136-325) 8-oxoguanine glycosylase {Human (Homo sapiens)}
dpieclfsficssnnniaritgmverlcqafgprliqlddvtyhgfpslqalagpeveah
lrklglgyraryvsasaraileeqgglawlqqlressyeeahkalcilpgvgtqvadcic
lmaldkpqavpvdvhmwhiaqrdyswhpttsqakgpspqtnkelgnffrslwgpyagwaq
avlfsadlrq
>d1gln_1 1.93.1.1.1 (306-468) Anticodon-binding (C-terminal) domain of glutamyl-tRNA synthetase (GluRS) {Thermus thermophilus}
dleklrwmngkyirevlsleevaervkpflreaglsweseaylrravelmrprfdtlkef
pekarylftedypvsekaqrkleeglpllkelyprlraqeewteaaleallrgfaaekgv
klgqvaqplraaltgsletpglfeilallgkeralrrlerala
>d1rlr_1 1.94.1.1.1 (10-221) R1 subunit of ribonucleotide reductase, N-terminal domain {Escherichia coli}
rdgsterinldkihrvldwaaeglhnvsisqvelrshiqfydgiktsdihetiikaaadl
isrdapdyqylaarlaifhlrkkaygqfeppalydhvvkmvemgkydnhlledyteeefk
qmdtfidhdrdmtfsyaavkqlegkylvqnrvtgeiyesaqflyilvaaclfsnypretr
lqyvkrfydavstfkislptpimsgvrtptrq
>d1qnf_1 1.95.1.1.2 (205-475) FAD-binding (C-terminal) domain of DNA photolyase {Anacystis nidulans}
pvepgetaaiarlqefcdraiadydpqrnfpaeagtsglspalkfgaigirqawqaasaa
halsrsdearnsirvwqqelawrefyqhalyhfpsladgpyrslwqqfpwenrealftaw
tqaqtgypivdaamrqltetgwmhnrcrmivasfltkdliidwrrgeqffmqhlvdgdla
annggwqwsassgmdpkplrifnpasqakkfdatatyikrwlpelrhvhpkdlisgeitp
ierrgypapivnhnlrqkqfkalynqlkaai
>d2pgd_1 1.96.1.1.1 (177-473) 6-phosphogluconate dehydrogenase (6PGD) {Sheep (Ovis orientalis aries)}
gaghfvkmvhngieygdmqliceayhlmkdvlglghkemakafeewnkteldsflieita
silkfqdadgkhllpkirdsagqkgtgkwtaisaleygvpvtligeavfarclsslkder
iqaskklkgpqnipfegdkksfledirkalyaskiisyaqgfmllrqaatefgwtlnygg
ialmwrggciirsvflgkikdafdrnpglqnlllddffksavencqdswrraistgvqag
ipmpcfttalsfydgyrhamlpanliqaqrdyfgahtyellakpgqfihtnwtghgg
>d1qmga1 1.96.1.2.1 (308-595) Acetohydroxy acid isomeroreductase, ketoacid reductoisomerase (KARI) {Spinach (Spinacia oleracea)}
leqeyksdifgergillgavhgiveclfrrytesgmsedlaykntvecitgvisktistk
gmlalynslseegkkdfqaaysasyypsmdilyecyedvasgseirsvvlagrrfyekeg
lpafpmgkidqtrmwkvgekvrsvrpagdlgplypftagvyvalmmaqieilrkkghsys
eiinesvieavdslnpfmhargvsfmvdncsttarlgsrkwaprfdyilsqqalvavdng
apinqdlisnflsdpvheaigvcaqlrpsvdisvtadadfvrpelrqa
>d2hdha1 1.96.1.3.1 (204-304) Short chain L-3-hydroxyacyl CoA dehydrogenase {Human (Homo sapiens)}
gfivnrllvpylxeairlyergdaskedidtaxklgagypxgpfelldyvgldttkfivd
gwhexdaenplhqpspslnklvaenkfgkktgegfykykaa
>d1dlja1 1.96.1.4.1 (197-294) UDP-glucose dehydrogenase (UDPGDH), middle domain {Streptococcus pyogenes}
aseaeavklfantylalrvayfneldtyaesrklnshmiiqgisyddrigmhynnpsfgy
ggyslpkdtkqllanynnipqtlieaivssnnvrksyi
>d1bg6_1 1.96.1.5.1 (188-359) N-(1-D-carboxylethyl)-L-norvaline dehydrogenase {Arthrobacter strain 1c}
nvlhtsltnvnavmhplptllnaarcesgtpfqyylegitpsvgslaekvdaeriaiaka
fdlnvpsvcewykesygqspatiyeavqgnpayrgiagpinlntryffedvstglvplse
lgravnvptplidavldlisslidtdfrkegrtleklglsgltaagirsave
>d1utg__ 1.97.1.1.1 Uteroglobin {Rabbit (Oryctolagus cuniculus)}
gicprfahvienlllgtpssyetslkefepddtmkdagmqmkkvldslpqttrenimklt
ekivksplcm
>d1ccd__ 1.97.1.1.2 Clara cell 17kDa protein {Rat (Rattus rattus)}
ssdicpgflqvlealllgsesnyeaalkpfnpasdlqnagtqlkrlvdtlpqetrinivk
ltekiltsplceqdlrv
>d1gai__ 1.98.1.1.1 Glucoamylase {Aspergillus awamori, variant x100}
atldswlsneatvartailnnigadgawvsgadsgivvaspstdnpdyfytwtrdsglvi
ktlvdlfrngdtdllstiehyissqaiiqgvsnpsgdlssgglgepkfnvdetaytgswg
rpqrdgpalratamigfgqwlldngytsaateivwplvrndlsyvaqywnqtgydlweev
ngssfftiavqhralvegsafatavgsscswcdsqapqilcylqsfwtgsyilanfdssr
sgkdtntllgsihtfdpeagcddstfqpcspralanhkevvdsfrsiytlndglsdseav
avgrypedsyyngnpwflctlaaaeqlydalyqwdkqgsleitdvsldffkalysgaatg
tyssssstyssivsavktfadgfvsivethaasngslseqfdksdgdelsardltwsyaa
lltannrrnsvvppswgetsassvpgtcaatsasgtyssvtvtswpsivatg
>d1cem__ 1.98.1.2.1 CelA cellulase {Clostridium thermocellum}
agvpfntkypygptsiadnqsevtamlkaewedwkskritsngaggykrvqrdastnydt
vsegmgyglllavcfneqalfddlyryvkshfngnglmhwhidannnvtshdggdgaatd
adedialalifadkqwgssgainygqeartlinnlynhcvehgsyvlkpgdrwggssvtn
psyfapawykvyaqytgdtrwnqvadkcyqiveevkkynngtglvpdwctasgtpasgqs
ydykydatrygwrtavdyswfgdqrakancdmltkffardgakgivdgytiqgskisnnh
nasfigpvaaasmtgydlnfakelyretvavkdseyygyygnslrlltllyitgnfpnpl
sdl
>d1tf4a1 1.98.1.2.2 (1-460) Endo/exocellulase:cellobiose E-4, N-terminal domain {Thermomonospora fusca}
epafnyaealqksmffyeaqrsgklpennrvswrgdsglndgadvgldltggwydagdhv
kfgfpmaftatmlawgaiespegyirsgqmpylkdnlrwvndyfikahpspnvlyvqvgd
gdadhkwwgpaevmpmerpsfkvdpscpgsdvaaetaaamaassivfadddpayaatlvq
hakqlytfadtyrgvysdcvpagafynswsgyqdelvwgaywlykatgddsylakaeyey
dflsteqqtdlrsyrwtiawddksygtyvllaketgkqkyiddanrwldywtvgvngqrv
pyspggmavldtwgalryaantafvalvyakviddpvrkqryhdfavrqinyalgdnprn
ssyvvgfgnnpprnphhrtahgswtdsiaspaenrhvlygalvggpgspndaytddrqdy
vanevatdynagfssalamlveeyggtpladfppteepdg
>d1clc_1 1.98.1.2.3 (135-575) CelD cellulase {Clostridium thermocellum}
amnvyedafktamlgmyllrcgtsvsatyngihyshgpchtndayldyingqhtkkdstk
gwhdagdynkyvvnagitvgsmflawehfkdqlepvaleipeknnsipdfldelkyeidw
iltmqypdgsgrvahkvstrnfggfimpenehderffvpwssaatadfvamtamaarifr
pydpqyaekcinaakvsyeflknnpanvfanqsgfstgeyatvsdaddrlwaaaemwetl
gdeeylrdfenraaqfskkieadfdwdnvanlgmftyllserpgknpalvqsikdsllst
adsivrtsqnhgygrtlgttyywgcngtvvrqtmilqvankispnndyvnaaldaishvf
grnyynrsyvtglginppmnphdrrsgadgiwepwpgylvgggwpgpkdwvdiqdsyqtn
eiainwnaaliyalagfvnyn
>d1fce__ 1.98.1.2.4 Processive endocellulase CelF {Clostridium cellulolyticum}
asspankvyqdrfesmyskikdpangyfseqgipyhsietlmveapdyghvttseamsyy
mwleamhgrfsgdftgfdkswsvteqyliptekdqpntsmsrydankpatyapefqdpsk
ypspldtsqpvgrdpinsqltsaygtsmlygmhwildvdnwygfgaradgtskpsyintf
qrgeqestwetipqpcwdehkfggqygfldlftkdtgtpakqfkytnapdadaravqaty
wadqwakeqgksvstsvgkatkmgdylrysffdkyfrkigqpsqagtgydaahyllswyy
awgggidstwswiigsshnhfgyqnpfaawvlstdanfkpkssngasdwaksldrqlefy
qwlqsaegaiaggatnswngryeavpsgtstfygmgyvenpvyadpgsntwfgmqvwsmq
rvaelyyktgdarakklldkwakwingeikfnadgtfqipstidwegqpdtwnptqgytg
nanlhvkvvnygtdlgcasslantltyyaaksgdetsrqnaqklldamwnnysdskgist
veqrgdyhrfldqevfvpagwtgkmpngdviksgvkfidirskykqdpewqtmvaalqag
qvptqrlhrfwaqsefavangvyailfpd
>d1dl2a_ 1.98.2.1.1 Class I alpha-1;2-mannosidase, catalytic domain {Baker's yeast (Saccharomyces cerevisiae)}
gagemrdriesmfleswrdyskhgwgydvygpiehtshnmprgnqplgwiivdsvdtlml
mynsstlyksefeaeiqrsehwindvldfdidaevnvfettirmlggllsayhlsdvlev
gnktvylnkaidlgdrlalaflstqtgipyssinlhsgqavknhadggasstaefttlqm
efkylayltgnrtywelvervyeplyknndllntydglvpiytfpdtgkfgastirfgsr
gdsfyeyllkqyllthetlyydlyrksmegmkkhllaqskpsslwyigereqglhgqlsp
kmdhlvcfmggllasgsteglsihearrrpffslslerksdwdlakgitdtcyqmykqss
sglapeivvfndgnikqdgwwrssvgdffvkpldrhnlqrpetvesimfmyhlshdhkyr
ewgaeiatsffentcvdcndpklrrftslsdcitlptkksnnmesfwlaetlkylyilfl
defdltkvvfnteahpfpvldeeilksqslttgwsl
>d1qaza_ 1.98.3.1.1 Alginate lyase A1-III {Sphingomonas, sp. A1}
gshpfdqavvkdptasyvdvkarrtflqsgqlddrlkaalpkeydctteatpnpqqgemv
iprrylsgnhgpvnpdyepvvtlyrdfekisatlgnlyvatgkpvyatcllnmldkwaka
dallnydpksqswyqvewsaataafalstmmaepnvdtaqrervvkwlnrvarhqtsfpg
gdtsccnnhsywrgqeatiigviskddelfrwglgryvqamglinedgsfvhemtrheqs
lhyqnyamlpltmiaetasrqgidlyaykengrdihsarkfvfaavknpdlikkyasepq
dtrafkpgrgdlnwieyqrarfgfadelgfmtvpifdprtggsatllaykp
>d1cb8a1 1.98.3.2.1 (26-335) Chondroitinase AC, N-terminal domain {Flavobacterium heparinum}
gtaelimkrvmldlkkplrnmdkvaeknlntlqpdgswkdvpykddamtnwlpnnhllql
etiiqayiekdshyygddkvfdqiskafkywydsdpksrnwwhneiatpqalgemlilmr
ygkkpldealvhkltermkrgepekktganktdialhyfyralltsdeallsfavkelfy
pvqfvhyeeglqydysylqhgpqlqissygavfitgvlklanyvrdtpyalsteklaifs
kyyrdsylkairgsymdfnvegrgvsrpdilnkkaekkrllvakmidlkhteewadaiar
tdstvaagyk
>d5eau_1 1.98.4.1.1 (21-220) 5-Epi-aristolochene synthase, N-terminal domain {Tobacco (Nicotiana tabacum)}
spslwgdqflsfsidnqvaekyakeiealkeqtrnmllatgmkladtlnlidtierlgis
yhfekeiddildqiynqnsncndlctsalqfrllrqhgfnispeifskfqdengkfkesl
asdvlgllnlyeashvrthaddiledalafstihlesaaphlksplreqvthaleqclhk
gvprvetrffissiydkeqs
>d2sqca1 1.98.4.2.1 (8-36,308-630) Squalene-hopene cyclase {Alicyclobacillus acidocaladarius}
apayartldraveyllscqkdegywwgplXispvwdtglavlalraaglpadhdrlvkag
ewlldrqitvpgdwavkrpnlkpggfafqfdnvyypdvcdtavvvwalntlrlpderrrr
damtkgfrwivgmqssnggwgaydvdntsdlpnhipfsdfgevtdppsedvtahvlecfg
sfgyddawkvirraveylkreqkpdgswfgrwgvnylygtgavvsalkavgidtrepyiq
kaldwveqhqnpdggwgedcrsyedpayagkgastpsqtawalmaliaggraeseaarrg
vqylvetqrpdggwdepyytgtgfpgdfylgytmyrhvfptlalgrykqaier
>d2sqca2 1.98.4.2.1 (37-307) Squalene-hopene cyclase {Alicyclobacillus acidocaladarius}
lsnvtmeaeyvllchildrvdrdrmekirryllheqredgtwalypggppdldttieayv
alkyigmsrdeepmqkalrfiqsqggiessrvftrmwlalvgeypwekvpmvppeimflg
krmplniyefgswaratvvalsivmsrqpvfplperarvpelyetdvpprrrgakggggw
ifdaldralhgyqklsvhpfrraaeiraldwllerqagdgswggiqppwfyalialkild
mtqhpafikgweglelygveldyggwmfqas
>d1d8db_ 1.98.4.3.1 Protein farnesyltransferase, beta-subunit {Rat (Rattus norvegicus)}
pvwseplyslrpeharerlqddsvetvtsieqakveekiqevfssykfnhlvprlvlqre
khfhylkrglrqltdayecldasrpwlcywilhslelldepipqivatdvcqflelcqsp
dggfgggpgqyphlaptyaavnalciigteeaynvinrekllqylyslkqpdgsflmhvg
gevdvrsaycaasvasltniitpdlfegtaewiarcqnweggiggvpgmeahggytfcgl
aalvilkkerslnlksllqwvtsrqmrfeggfqgrcnklvdgcysfwqagllpllhralh
aqgdpalsmshwmfhqqalqeyilmccqcpagglldkpgksrdfyhtcyclsglsiaqhf
gsgamlhdvvmgvpenvlqpthpvynigpdkviqatthflqkpvpgf
>d1c3d__ 1.98.4.4.1 C3D, a C3 fragment and ligand for complement receptor 2 {Human (Homo sapiens)}
mldaerlkhlivtpsgageqnmigmtptviavhyldeteqwekfglekrqgalelikkgy
tqqlafrqpssafaafvkrapstwltayvvkvfslavnliaidsqvlcgavkwlilekqk
pdgvfqedapvihqemigglrnnnekdmaltafvlislqeakdiceeqvnslpgsitkag
dfleanymnlqrsytvaiagyalaqmgrlkgpllnkflttakdknrwedpgkqlynveat
syallallqlkdfdfvppvvrwlneqryygggygstqatfmvfqalaqyqkdap
>d1csh__ 1.99.1.1.1 Citrate synthase {Chicken (Gallus gallus)}
stnlkdvlaslipkeqariktfrqqhgntavgqitvdmsyggmrgmkgliyetsvldpde
girfrgfsipecqkllpkagggeeplpeglfwllvtgqiptpeqvswvskewakraalps
hvvtmldnfptnlhpmsqlsaaitalnsesnfarayaeginrtkywefvyedamdliakl
pcvaakiyrnlyragssigaidskldwshnftnmlgytdpqftelmrlyltihsdheggn
vsahtshlvgsalsdpylsfaaamnglagplhglanqevllwlsqlqkdlgadasdeklr
dyiwntlnsgrvvpgyghavlrktdprytcqrefalkhlpsdpmfklvaqlykivpnvll
eqgkaknpwpnvdahsgvllqyygmtemnyytvlfgvsralgvlaqliwsralgfplerp
ksmstagleklsagg
>d1a59__ 1.99.1.1.4 Citrate synthase {Antarctic bacterium, ds2-3r}
eptihkglagvtadvtaiskvnsdtnsllyrgypvqelaakcsfeqvayllwnselpnds
elkafvnfershrkldenvkgaidllstachpmdvartavsvlganharaqdsspeanle
kamsllatfpsvvaydqrrrrgeeliepredldysanflwmtfgeeaapevveafnvsmi
lyaehsfnastftarvitstladlhsavtgaigalkgplhgganeavmhtfeeigirkde
sldeaatrskawmvdalaqkkkvmgfghrvykngdsrvptmksaldamikhydrpemlgl
yngleaameeakqikpnldypagptynlmgfdtemftplfiaaritgwtahimeqvadna
lirplseyngpeqrqvp
>d1phb__ 1.100.1.1.1 Cytochrome P450-CAM {Pseudomonas putida}
nlaplpphvpehlvfdfdmynpsnlsagvqeawavlqesnvpdlvwtrcngghwiatrgq
lireayedyrhfssecpfipreageaydfiptsmdppeqrqfralanqvvgmpvvdklen
riqelacslieslrpqgqcnftedyaepfpirifmllaglpeediphlkyltdqmtrpdg
smtfaeakealydylipiieqrrqkpgtdaisivangqvngrpitsdeakrmcglllvgg
ldtvvnflsfsmeflakspehrqelierperipaaceellrrfslvadgriltsdyefhg
vqlkkgdqillpqmlsglderenacpmhvdfsrqkvshttfghgshlclgqhlarreiiv
tlkewltripdfsiapgaqiqhksgivsgvqalplvwdpattkav
>d1bu7a_ 1.100.1.1.2 Cytochrome P450 bm-3 {Bacillus megaterium}
tikempqpktfgelknlpllntdkpvqalmkiadelgeifkfeapgrvtrylssqrlike
acdesrfdknlsqalkfvrdfagdglftswtheknwkkahnillpsfsqqamkgyhammv
diavqlvqkwerlnadehievpedmtrltldtiglcgfnyrfnsfyrdqphpfitsmvra
ldeamnklqranpddpaydenkrqfqedikvmndlvdkiiadrkasgeqsddllthmlng
kdpetgeplddeniryqiitfliaghettsgllsfalyflvknphvlqkaaeeaarvlvd
pvpsykqvkqlkyvgmvlnealrlwptapafslyakedtvlggeyplekgdelmvlipql
hrdktiwgddveefrperfenpsaipqhafkpfgngqracigqqfalheatlvlgmmlkh
fdfedhtnyeldiketltlkpegfvvkakskkipl
>d1cmna_ 1.100.1.1.3 Cytochrome P450-NOR, nitric reductase {Fungus (Fusarium oxysporum)}
apsfpfsrasgpeppaefaklratnpvsqvklfdgslawlvtkhkdvcfvatseklskvr
trqgfpelsasgkqaakakptfvdmdppehmhqrsmveptftpeavknlqpyiqrtvddl
leqmkqkgcangpvdlvkefalpvpsyiiytllgvpfndleyltqqnairtngsstarea
saanqelldylailveqrlvepkddiisklcteqvkpgnidksdavqiaflllvagnatm
vnmialgvatlaqhpdqlaqlkanpslapqfveelcryhtavalaikrtakedvmigdkl
vranegiiasnqsanrdeevfenpdefnmnrkwppqdplgfgfgdhrciaehlakaeltt
vfstlyqkfpdlkvavplgkinytplnrdvgivdlpvif
>d1fipa_ 1.101.1.1.1 FIS protein {Escherichia coli}
plrdsvkqalknyfaqlngqdvndlyelvlaeveqalldmvmqytrgnqtraalmmginr
gtlrkklkkygmn
>d1ntca_ 1.101.1.1.2 DNA-binding domain of NTRC {Salmonella typhimurium}
mdlpgelfeastpdspshlppdswatllaqwadralrsghqnllseaqpelertllttal
rhtqghkqeaarllgwgaatltaklkelgme
>d1jhga_ 1.102.1.1.1 Trp repressor {Escherichia coli}
saamaeqrhqewlrfvdllknayqndlhlpllnlmltpderealgtrvriieellrgems
qrelknelgagiatitrgsnslkaapvelrqwleevllksd
>d1iiea_ 1.103.1.1.1 MHC class II-associated invariant chain ectoplasmic trimerization domain {Human (Homo sapiens)}
ygnmtedhvmhllqnadplkvypplkgsfpenlrhlkntmetidwkvfeswmhhwllfem
srhsleqkptdappk
>d1b25a1 1.104.1.1.2 (211-619) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
dkeelkklsqeayneilnspgypfwkrqgtmaavewcntnyalptrnfsdgyfefarsid
gytmegmkvqqrgcpycnmpcgnvvldaegqeseldyenvallgsnlgigklnevsvlnr
iademgmdtislgvsiahvmeavergilkegptfgdfkgakqlaldiayrkgelgnlaae
gvkamaeklgthdfamhvkglevsgyncyiypamalaygtsaigahhkeawviaweigta
piegekaekveykisydpikaqkvvelqrlrgglfemltacrlpwvevglsldyypkllk
aitgvtytwddlykaadrvysliraywvrefngkwdrkmdyppkrwfteglksgphkgeh
ldekkydellseyyrirgwdergipkketlkeldldfvipelekvtnle
>d1qi9a_ 1.105.1.1.1 Haloperoxidase {Ascophyllum nodosum}
tcstsddaddptppnerddeafasrvaaakrelegtgtvcqinngetdlaakfhkslphd
dlgqvdadafaaledcilngdlsicedvpvgnsegdpvgrlvnptaafaidisgpafsat
tippvptlpspelaaqlaevywmalardvpfmqygtdditvtaaanlagmegfpnldavs
igsdgtvdplsqlfratfvgvetgpfisqllvnsftidsitvepkqetfapdvnymvdfd
ewlniqnggppagpellddelrfvrnardlarvtftdninteayrgalillgldafnrag
vngpfididrqagfvnfgishyfrligaaelaqrsswyqkwqvhrfarpealggtlhlti
kgelnadfdlsllenaellkrvaainaaqnpnnevtyllpqaiqegspthpsypsghatq
ngafatvlkaligldrggdcypdpvypdddglklidfrgscltfegeinklavnvafgrq
mlgihyrfdgiqglllgetitvrtlhqelmtfaeestfefrlftgeviklfqdgtftidg
fkcpglvytgvencv
>d1vns__ 1.105.1.2.1 Chloroperoxidase {Curvularia inaequalis}
vtpiplpkidepeeyntnyilfwnhvglelnrvthtvggpltgpplsaralgmlhlaihd
ayfsicpptdfttflspdtenaayrlpspngandarqavagaalkmlsslymkpveqpnp
npganisdnayaqlglvldrsvleapggvdresasfmfgedvadvffallndprgasqeg
yhptpgrykfddepthpvvlipvdpnnpngpkmpfrqyhapfygkttkrfatqsehflad
ppglrsnadetaeyddavrvaiamggaqalnstkrspwqtaqglywaydgsnligtpprf
ynqivrriavtykkeedlansevnnadfarlfalvdvactdagifswkekwefefwrpls
gvrddgrpdhgdpfwltlgapatntndipfkppfpaypsghatfggavfqmvrryyngrv
gtwkddepdniaidmmiseelngvnrdlrqpydptapiedqpgivrtrivrhfdsawelm
fenaisriflgvhwrfdaaaardiliptttkdvyavdnngatvfqnvediryttrgtred
eeglfpiggvplgieiadeifnnglkptppeiqp
>d1sig__ 1.106.1.1.1 sigma70 subunit fragment from RNA polymerase {Escherichia coli}
megeidiakriedginqvqcsvaeypeaitylleqynrveaeearlsdlitgfvdpnaee
dlaptathvgselsqedldddededeedgdddsadddnsidpelarekfaelraqyvvtr
dtikakgrshataqeeilklsevfkqfrlvpkqfdylvnsmrvmmdrvrtqerlimklcv
eqckmpkknfitlftgnetsdtwfnaaiamnkpwseklhdvseevhralqklqqieeetg
ltieqvkdinrrmsigeakarrakkemveanlrlvisiakkytnrglqfldliqegnigl
mkavdkfeyrrgykfstyatwwirqaitrsiadq
>d1dg3a1 1.107.1.1.1 (284-583) Interferon-induced guanylate-binding protein 1 (GBP1), C-terminal domain {Human (Homo sapiens)}
ggiqvngprleslvltyvnaissgdlpcmenavlalaqiensaavqkaiahyeqqmgqkv
qlpteslqelldlhrdsereaievfirssfkdvdhlfqkelaaqlekkrddfckqnqeas
sdrcsgllqvifspleeevkagiyskpggyrlfvqklqdlkkkyyeeprkgiqaeeilqt
ylkskesmtdailqtdqtltekekeievervkaesaqasakmlhemqrkneqmmeqkers
yqehlkqltekmendrvqllkeqertlalklqeqeqllkegfqkesrimkneiqdlqtkm
>d1bvp11 1.108.1.1.1 (1-120,255-349) Bluetongue virus coat protein vp7 (BTV-10 vp7), alpha-helical domain {Bluetongue virus}
mdtiaaraltvmracatlqearivleanvmeilgiainryngltlrgvtmrptslaqrne
mffmcldmmlsaaginvgpispdytqhmatigvlatpeipftteaaneiarvtgetstwg
Xktlnqypaltaeifnvysfrdhtwhglrtailnrttlpnmlppifppndrdsiltllll
stladvytvlrpefaihgvnpmpgpltraiaraayv
>d1tx4a_ 1.109.1.1.1 p50 RhoGAP domain {Human (Homo sapiens)}
plpnqqfgvslqhlqeknpeqepipivlretvaylqahalttegifrrsantqvvrevqq
kynmglpvdfdqynalhlpavilktflrelpeplltfdlyphvvgflnidesqrvpatlq
vlqtlpeenyqvlrfltaflvqisahsdqnkmtntnlavvfgpnllwakdaaitlkainp
intftkflldhqgelf
>d1pbwa_ 1.109.1.1.2 p85 alpha subunit RhoGAP domain {Human (Homo sapiens)}
lpdlaeqfappdiapplliklveaiekkglecstlyrtqsssnlaelrqlldcdtpsvdl
emidvhvladafkrylldlpnpvipaavysemislapevqsseeyiqllkklirspsiph
qywltlqyllkhffklsqtssknllnarvlseifspmlfrfsaassdntenlikvieili
stew
>d1wer__ 1.109.1.2.1 p120GAP domain {Human (Homo sapiens)}
mpeeeysefkelilqkelhvvyalshvcgqdrtllasillriflhekleslllctlndre
ismedeattlfrattlastlmeqymkatatqfvhhalkdsilkimeskqscelspsklek
nedvntnlthllnilselvekifmaseilpptlryiygclqksvqhkwptnttmrtrvvs
gfvflrlicpailnprmfniisdspspiaartlilvaksvqnlanlvefgakepymegvn
pfiksnkhrmimfldelgnvpelpdttehsrtdlsrdlaalheicvahsdelrtlsnerg
aqqhvlkkllaitellqqkqnqyt
>d1nf1a_ 1.109.1.2.2 GAP related domain of neurofibromin {Human (Homo sapiens)}
erlvelvtmmgdqgelpiamalanvvpcsqwdelarvlvtlfdsrhllyqllwnmfskev
eladsmqtlfrgnslaskimtfcfkvygatylqklldpllrivitssdwqhvsfevdptr
lepsesleenqrnllqmtekffhaiissssefppqlrsvchclyqvvsqrfpqnsigavg
samflrfinpaivspyeagildkkpppiierglklmskilqsianhvlftkeehmrpfnd
fvksnfdaarrffldiasdcptsdavnhslsfisdgnvlalhrllwnnqekigqylssnr
dhkavgrrpfdkmatllaylgppe
>d1bkds_ 1.110.1.1.1 Son of sevenless-1 (sos-1) {Human (Homo sapiens)}
rlpsadvyrfaepdseeniifeegipiikagtviklierltyhmyadpnfvrtflttyrs
fckpqellsliierfeipeprfrkeyiqpvqlrvlnvcrhwvehhfydferdayllqrme
efigtvrgkamkkwvesitkiiqrkkitfqsspptvewhisrpghietfdlltlhpieia
rqltllesdlyravqpselvgsvwtkedkeinspnllkmirhttnltlwfekcivetenl
eervavvsriieilqvfqelnnfngvlevvsamnsspvyrldhtfeqipsrqkkileeah
elsedhykkylaklrsinppcvpffgiyltnilkteegnpevlkrhgkelinfskrrkva
eitgeiqqyqnqpyclrvesdikrffenlnpmgnsmekeftdylfnksleieprnpkplp
rfpkkysyplkspgvrpsn
>d3bct__ 1.111.1.1.1 beta-Catenin {Mouse (Mus musculus)}
qxvsaivrtxqntndvetarctagtlhnlshhregllaifksggipalvkxlgspvdsvl
fyaittlhnlllhqegakxavrlagglqkxvallnktnvkflaittdclqilaygnqesk
liilasggpqalvnixrtytyekllwttsrvlkvlsvcssnkpaiveaggxqalglhltd
psqrlvqnclwtlrnlsdaatkqegxegllgtlvqllgsddinvvtcaagilsnltcnny
knkxxvcqvggiealvrtvlragdreditepaicalrhltsrhqeaexaqnavrlhyglp
vvvkllhppshwplikatvglirnlalcpanhaplreqgaiprlvqllvrahqdtqrgvr
xeeivegctgalhilardvhnrivirglntiplfvqllyspieniqrvaagvlcelaqdk
eaaeaieaegatapltellhsrnegvatyaaavlfr
>d1qgra_ 1.111.1.1.3 Importin beta {Human (Homo sapiens)}
melitilektvspdrleleaaqkfleraavenlptflvelsrvlanpgnsqvarvaaglq
iknsltskdpdikaqyqqrwlaidanarrevknyvlhtlgtetyrpssasqcvagiacae
ipvnqwpelipqlvanvtnpnstehmkestleaigyicqdidpeqlqdksneiltaiiqg
mrkeepsnnvklaatnallnsleftkanfdkeserhfimqvvceatqcpdtrvrvaalqn
lvkimslyyqymetymgpalfaitieamksdidevalqgiefwsnvcdeemdlaieasea
aeqgrppehtskfyakgalqylvpiltqtltkqdendddddwnpckaagvclmllatcce
ddivphvlpfikehiknpdwryrdaavmafgcilegpepsqlkplviqamptlielmkdp
svvvrdtaawtvgricellpeaaindvylapllqclieglsaeprvasnvcwafsslaea
ayeaadvaddqeepatyclsssfelivqkllettdrpdghqnnlrssayeslmeivknsa
kdcypavqkttlvimerlqqvlqmeshiqstsdriqfndlqsllcatlqnvlrkvqhqda
lqisdvvmasllrmfqstagsggvqedalmavstlvevlggeflkymeafkpflgiglkn
yaeyqvclaavglvgdlcralqsniipfcdevmqlllenlgnenvhrsvkpqilsvfgdi
alaiggefkkylevvlntlqqasqaqvdksdydmvdylnelrescleaytgivqglkgdq
envhpdvmlvqprvefilsfidhiagdedhtdgvvacaagligdlctafgkdvlklvear
pmihelltegrrsktnkaktlarwatkelrklknqa
>d1qbkb_ 1.111.1.1.4 Karyopherin beta2 {Human (Homo sapiens)}
yewkpdeqglqqilqllkesqspdttiqrtvqqkleqlnqypdfnnylifvltklksede
ptrslsglilknnvkahfqnfpngvtdfikseclnnigdsspliratvgilittiaskge
lqnwpdllpklcslldsedyntcegafgalqkicedsaeildsdvldrplnixipkflqf
fkhsspkirshavacvnqfiisrtqalxlhidsftenlfalagdeepevrknvcralvxl
levrmdrllphxhniveyxlqrtqdqdenvaleacefwltlaeqpickdvlvrhlpklip
vlvngxkysdidiillkgdveedetipdseqdirprfhrsrtvaqqhdedgieeeddddd
eiddddtisdwnlrkcsaaaldvlanvyrdellphilpllkellfhhewvvkesgilvlg
aiaegcxqgxipylpeliphliqclsdkkalvrsitcwtlsryahwvvsqppdtylkplx
tellkrildsnkrvqeaacsafatleeeactelvpylayildtlvfafskyqhknllily
daigtladsvghhlnkpeyiqxlxppliqkwnxlkdedkdlfplleclssvatalqsgfl
pycepvyqrcvnlvqktlaqaxlnnaqpdqyeapdkdfxivaldllsglaeglggnieql
varsniltlxyqcxqdkxpevrqssfallgdltkacfqhvkpciadfxpilgtnlnpefi
svcnnatwaigeisiqxgiexqpyipxvlhqlveiinrpntpktllentaitigrlgyvc
pqevapxlqqfirpwctslrnirdneekdsafrgictxisvnpsgviqdfiffcdavasw
inpkddlrdxfckilhgfknqvgdenwrrfsdqfplplkerlaafygv
>d1ee4a_ 1.111.1.1.5 Karyopherin alpha {Baker's yeast (Saccharomyces cerevisiae)}
qelpqmtqqlnsddmqeqlsatvkfrqilsrehrppidvviqagvvprlvefmrenqpem
lqleaawaltniasgtsaqtkvvvdadavplfiqllytgsvevkeqaiwalgnvagdstd
yrdyvlqcnamepilglfnsnkpslirtatwtlsnlcrgkkpqpdwsvvsqalptlakli
ysmdtetlvdacwaisylsdgpqeaiqavidvripkrlvellshestlvqtpalravgni
vtgndlqtqvvinagvlpalrlllsspkenikkeacwtisnitagnteqiqavidanlip
plvkllevaedktkkeacwaisnassgglqrpdiirylvsqgcikplcdlleiadnriie
vtldalenilkmgeadkearglninenadfiekaggmekifncqqnendkiyekaykiie
tyf
>d1b3ua_ 1.111.1.2.1 Constant regulatory domain of protein phosphatase 2a, pr65alpha {Human (Homo sapiens)}
aaadgddslypiavlidelrnedvqlrlnsikklstialalgvertrsellpfltdtiyd
edevllalaeqlgtfttlvggpeyvhcllppleslatveetvvrdkaveslraishehsp
sdleahfvplvkrlaggdwftsrtsacglfsvcyprvssavkaelrqyfrnlcsddtpmv
rraaasklgefakvleldnvkseiipmfsnlasdeqdsvrllaveacvniaqllpqedle
alvmptlrqaaedkswrvrymvadkftelqkavgpeitktdlvpafqnlmkdceaevraa
ashkvkefcenlsadcrenvimsqilpcikelvsdanqhvksalasvimglspilgkdnt
iehllplflaqlkdecpevrlniisnldcvnevigirqlsqsllpaivelaedakwrvrl
aiieympllagqlgveffdeklnslcmawlvdhvyaireaatsnlkklvekfgkewahat
iipkvlamsgdpnylhrmttlfcinvlsevcgqdittkhmlptvlrmagdpvanvrfnva
kslqkigpildnstlqsevkpilekltqdqdvdvkyfaqealtvlsla
>d1b89a_ 1.111.1.3.1 Clathrin heavy chain proximal leg segment {Bovine (Bos taurus)}
rlaeleefingpnnahiqqvgdrcydekmydaakllynnvsnfgrlastlvhlgeyqaav
dgarkanstrtwkevcfacvdgkefrlaqxcglhivvhadeleelinyyqdrgyfeelit
xleaalglerahxgxftelailyskfkpqkxrehlelfwsrvnipkvlraaeqahlwael
vflydkyeeydnaiitxxnhptdawkegqfkdiitkvanvelyyraiqfylefkplllnd
llxvlsprldhtravnyfskvkqlplvkpylrsvqnhnnksvneslnnlfiteedyqalr
tsidaydnfdnislaqrlekheliefrriaaylfkg
>d1lrv__ 1.111.1.4.1 Leucine-rich repeat variant {Azotobacter vinelandii}
tpigdcrvcsfrmsllltgrctpgdacvavesgrqidrffrnnphlavqyladpfwerra
iavryspvealtplirdsdevvrravayrlpreqlsalmfdedrevritvadrlpleqle
qmaadrdylvrayvvqrippgrlfrfmrdedrqvrklvakrlpeeslglmtqdpepevrr
ivasrlrgddllellhdpdwtvrlaavehaslealreldepdpevrlaiagrl
>d1qmma1 1.111.1.5.1 (525-725) Phoshoinositide 3-kinase (PI3K) helical domain {Pig (Sus scrofa)}
aaseetlafqrqlnaligydvtdvsnvhddeleftrrrlvtprmaevagrdpklyamhpw
vtskplpeyllkkitnncvfivihrsttsqtikvsaddtpgtilqsfftkmakkkslmdi
pesqnerdfvlrvcgrdeylvgetpiknfqwvrqclkngeeihlvldtppdpaldevrke
ewplvddctgvtgyheqltihgkdhesvftvslwdcdrkfrvkirgidipvlprtadltv
fveaniqygqqvlcqrrtspkpfteevlwnvwlefsikikdlpkgallnlqiycgkapal
sgktsaempspeskgkaqllyyvnlllidhrfllrhgeyvlhmwqlsgkgedqgsfnadk
ltsatnpdkensmsisilldnychpialpkhrptpdpegdrvraempnqlrkqleaiiat
dplnpltaedkellwhfryeslkdpkaypklfssvkwgqqeivaktyqllakrevwdqsa
ldvgltmqlldcnfsdenvraiavqklesledddvlhyllqlvqavkfepyhdsalarfl
lkrglrnkrighflfwflrseiaqsrhyqqrfavileaylrgcg
>d1ycsb1 1.111.2.1.1 (327-456) 53BP2 {Human (Homo sapiens)}
plallldsslegefdlvqriiyevddpslpndegitalhnavcaghteivkflvqfgvnv
naadsdgwtplhcaascnnvqvckflvesgaavfamtysdmqtaadkceemeegytqcsq
flygvqekmg
>d1awcb_ 1.111.2.1.2 GA bindinig protein (GABP) beta 1 {Mouse (Mus musculus)}
dlgkklleaaragqddevrilmangapfttdwlgtsplhlaaqyghfsttevllragvsr
dartkvdrtplhmaaseghanivevllkhgadvnakdmlkmtalhwatehnhqevvelli
kygadvhtqskfcktafdisidngnedlaeilq
>d1bd8__ 1.111.2.1.3 Cell cycle inhibitor p19ink4D {Human (Homo sapiens)}
ragdrlsgaaargdvqevrrllhrelvhpdalnrfgktalqvmmfgstaialellkqgas
pnvqdtsgtspvhdaartgfldtlkvlvehgadvnvpdgtgalpihlavqeghtavvsfl
aaesdlhrrdargltplelalqrgaqdlvdilqghm
>d1bi7b_ 1.111.2.1.5 Cell cycle inhibitor p16ink4A {Human (Homo sapiens)}
epsadwlataaargrveevralleaganpnapnsygrrpiqvmmmgsarvaellllhgae
pncadpatltrpvhdaaregfldtlvvlhragarldvrdawgrlpvdlaeelghrdvary
lraaa
>d1iknd_ 1.111.2.1.7 I-kappa-B-alpha {Human (Homo sapiens)}
dgdsflhlaiiheekaltmevirqvkgdlaflnfqnnlqqtplhlavitnqpeiaeallg
agcdpelrdfrgntplhlaceqgclasvgvltqscttphlhsilkatnynghtclhlasi
hgylgivellvslgadvnaqepcngrtalhlavdlqnpdlvslllkcgadvnrvtyqgys
pyqltwgrpstriqqqlgqltlenlqmlpesedeesydtes
>d1myo__ 1.111.2.1.8 Myotrophin {Rat (Rattus norvegicus)}
mcdkefmwalkngdldevkdyvakgedvnrtleggrkplhyaadcgqleileflllkgad
inapdkhhitpllsavyeghvscvklllskgadktvkgpdgltaleatdnqaikallq
>d1sw6a_ 1.111.2.1.9 Swi6 ankyrin-repeat fragment {Baker's yeast (Saccharomyces cerevisiae)}
gpiitfthdltsdflssplkimkalpspvvndneqkmkleaflqrllfpeiqemptslnn
dssnrnseggssnqqqqhvsfdsllqevndafpntqlnlnipvdehgntplhwltsianl
elvkhlvkhgsnrlygdnmgesclvkavksvnnydsgtfealldylypcliledsmnrti
lhhiiitsgmtgcsaaakyyldilmgwivkkqnrpiqsgtnekeskpndkngerkdsile
nldlkwiianmlnaqdsngdtclniaarlgnisivdalldygadpfianksglrpvdfga
g
>d1dcqa1 1.111.2.1.10 (369-522) Pyk2-associated protein beta {Mouse (Mus musculus)}
adtaaklhslceavktrdifgllqayadgvdltekiplanghepdetalhlavrsvdrts
lhivdflvqnsgnldkqtgkgstalhyccltdnaeclklllrgkasieianesgetpldi
akrlkhehceelltqalsgrfnshvhveyewrll
>d1pbv__ 1.111.3.1.1 Exchange factor ARNO {Human (Homo sapiens)}
anegsktlqrnrkmamgrkkfnmdpkkgiqflvenellqntpeeiarflykgeglnktai
gdylgereelnlavlhafvdlheftdlnlvqalrqflwsfrlpgeaqkidrmmeafaqry
clcnpgvfqstdtcyvlsfavimlntslhnpnvrdkpglerfvamnrgineggdlpeell
rnlydsirnepfkip
>d1qsaa1 1.111.5.1.1 (1-450) 70 KDa soluble lytic transglycosylase (SLT70), superhelical domain {Escherichia coli}
dsldeqrsryaqikqawdnrqmdvveqmmpglkdyplypyleyrqitddlmnqpavtvtn
fvranptlppartlqsrfvnelarredwrgllafspekpgtteaqcnyyyakwntgqsee
awqgakelwltgksqpnacdklfsvwrasgkqdplaylerirlamkagntglvtvlagqm
padyqtiasaiislannpntvltfarttgatdftrqmaavafasvarqdaenarlmipsl
aqaqqlnedqiqelrdivawrlmgndvtdeqakwrddaimrsqstslierrvrmalgtgd
rrglntwlarlpmeakekdewrywqadlllergreaeakeilhqlmqqrgfypmvaaqri
geeyelkidkapqnvdsaltqgpemarvrelmywnldntarsewanlvkskskteqaqla
ryafnnqwwdlsvqatiagklwdhleerfp
>d1d8da_ 1.111.6.1.1 Protein farnesyltransferase alpha-subunit {Rat (Rattus norvegicus)}
flsldsptyvlyrdraewadidpvpqndgpspvvqiiysekfrdvydyfravlqrderse
rafkltrdaielnaanytvwhfrrvllrslqkdlqeemnyiiaiieeqpknyqvwhhrrv
lvewlkdpsqelefiadilnqdaknyhawqhrqwviqefrlwdnelqyvdqllkedvrnn
svwnqrhfvisnttgysdravlerevqytlemiklvphnesawnylkgilqdrglsrypn
llnqlldlqpshsspyliaflvdiyedmlenqcdnkedilnkalelceilakekdtirke
ywryigrslqskhsresdipasv
>d1dcea1 1.111.6.1.2 (2-240,351-443) Rab geranylgeranyltransferase alpha-subunit, N-terminal domain {Rat (Rattus norvegicus)}
hgrlkvktseeqaeakrlereqklklyqsatqavfqkrqageldesvleltsqilganpd
fatlwncrrevlqhletekspeesaalvkaelgflesclrvnpksygtwhhrcwllsrlp
epnwarelelcarfleadernfhcwdyrrfvaaqaavapaeelaftdslitrnfsnyssw
hyrscllpqlhpqpdsgpqgrlpenvllkelelvqnafftdpndqsawfyhrwllgraeX
lfrcelsvekstvlqselesckelqelepenkwclltiillmraldpllyeketlqyfst
lkavdpmraaylddlrskfllensvlkmeyadv
>d1qjba_ 1.111.7.1.2 zeta isoform {Bovine (Bos taurus)}
mdknelvqkaklaeqaeryddmaacmksvteqgaelsneernllsvayknvvgarrsswr
vvssieqktegaekkqqmareyrekietelrdicndvlsllekflipnasqaeskvfylk
mkgdyyrylaevaagddkkgivdqsqqayqeafeiskkemqpthpirlglalnfsvfyye
ilnspekacslaktafdeaiaeldtlseesykdstlimqllrdnltlwtsdt
>d1a17__ 1.111.8.1.1 Protein phosphatase 5 {Human (Homo sapiens)}
ppadgalkraeelktqandyfkakdyenaikfysqaielnpsnaiyygnrslaylrtecy
gyalgdatraieldkkyikgyyrraasnmalgkfraalrdyetvvkvkphdkdakmkyqe
cnkivkqkaferaiagdehkrsvvdsldiesmtiedeys
>d1elra_ 1.111.8.1.2 Hop {Human (Homo sapiens)}
gkqalkekelgndaykkkdfdtalkhydkakeldptnmtyitnqaavyfekgdynkcrel
cekaievgrenredyrqiakayarignsyfkeekykdaihfynkslaehrtpdvlkkcqq
aekilkeq
>d1elwa_ 1.111.8.1.2 Hop {Human (Homo sapiens)}
eqvnelkekgnkalsvgniddalqcyseaikldphnhvlysnrsaayakkgdyqkayedg
cktvdlkpdwgkgysrkaaaleflnrfeeakrtyeeglkheannpqlkeglqnmear
>d1qqea_ 1.111.8.1.3 Vesicular transport protein sec17 {Yeast (Saccharomyces cerevisiae)}
isdpvellkraekkgvpssgfmklfsgsdsykfeeaadlcvqaatiyrlrkelnlagdsf
lkaadyqkkagnedeagntyveaykcfksggnsvnavdslenaiqifthrgqfrrganfk
felgeilendlhdyakaidcyelagewyaqdqsvalsnkcfikcadlkaldgqyieasdi
ysklikssmgnrlsqwslkdyflkkglcqlaatdavaaartlqegqsedpnfadsresnf
lkslidavnegdseqlsehckefdnfmrldkwkitilnkikesiqqqedd
>d1eyha_ 1.111.9.1.1 Epsin 1 {Rat (Rattus norvegicus)}
hnyseaeikvreatsndpwgpssslmseiadltynvvafseimsmiwkrlndhgknwrhv
ykamtlmeyliktgservsqqckenmyavqtlkdfqyvdrdgkdqgvnvrekakqlvall
rdedrlreerahalktkeklaqta
>d1dvpa1 1.111.9.2.1 (1-145) Hrs {Fruit fly (Drosophila melanogaster)}
mfrssfcknlenatshlrlepdwpsillicdeinqkdvtpknafaaikkkmnspnphssc
ysllvlesivkncgapvheevftkencemfssflestphenvrqkmlelvqtwayafrss
dkyqaikdtmtilkakghtfpelre
>d1elka_ 1.111.9.2.2 Tom1 protein {Human (Homo sapiens)}
sdfllgnpfsspvgqriekatdgslqsedwalnmeicdiineteegpkdalravkkrivg
nknfhevmlaltvletcvkncghrfhvlvasqdfvesvlvrtilpknnpptivhdkvlnl
iqswadafrsspdltgvvtiyedlrrkglefpm
>d1bpoa1 1.111.10.1.1 (331-487) Clathrin heavy-chain linker domain {Rat (Rattus norvegicus)}
eeniipyitnvlqnpdlalrmavrnnlagaeelfarkfnalfaqgnyseaakvaanapkg
ilrtpdtirrfqsvpaqpgqtspllqyfgilldqgqlnkyeslelcrpvlqqgrkqllek
wlkedklecseelgdlvksvdptlalsvylranvpnk
>d1c9ia1 1.111.10.1.1 (331-357) Clathrin heavy-chain linker domain {Rat (Rattus norvegicus)}
eeniipyitnvlqnpdlalrmavrnnl
>d1c9ib1 1.111.10.1.1 (331-358) Clathrin heavy-chain linker domain {Rat (Rattus norvegicus)}
eeniipyitnvlqnpdlalrmavrnnla
>d1c9la1 1.111.10.1.1 (331-359) Clathrin heavy-chain linker domain {Rat (Rattus norvegicus)}
eeniipyitnvlqnpdlalrmavrnnlag
>d1c9lb1 1.111.10.1.1 (331-359) Clathrin heavy-chain linker domain {Rat (Rattus norvegicus)}
eeniipyitnvlqnpdlalrmavrnnlag
>d2occe_ 1.111.11.1.1 Cytochrome c oxidase subunit E {Bovine (Bos taurus)}
hetdeefdarwvtyfnkpdidawelrkgmntlvgydlvpepkiidaalracrrlndfasa
vrilevvkdkagphkeiypyviqelrptlnelgistpeelgldkv
>d1yge_1 1.112.1.1.1 (150-839) Lipoxigenase, C-terminal domain {Soybean (Glycine max), isozyme L1}
vpsetpaplvsyreeelkslrgngtgerkeydriydydvyndlgnpdkseklarpvlggs
stfpyprrgrtgrgptvtdpntekqgevfyvprdenlghlkskdaleigtkslsqivqpa
fesafdlkstpiefhsfqdvhdlyeggiklprdvistiiplpvikelyrtdgqhilkfpq
phvvqvsqsawmtdeefaremiagvnpcvirgleefppksnldpaiygdqsskitadsld
ldgytmdealgsrrlfmldyhdifmpyvrqinqlnsaktyatrtilflredgtlkpvaie
lslphsagdlsaavsqvvlpakegvestiwllakayvivndscyhqlmshwlnthaamep
fviathrhlsvlhpiyklltphyrnnmninalarqslinangiiettflpskysvemssa
vyknwvftdqalpadlikrgvaikdpstphgvrlliedypyaadgleiwaaiktwvqeyv
plyyardddvkndselqhwwkeavekghgdlkdkpwwpklqtledlvevcliiiwiasal
haavnfgqypygglimnrptasrrllpekgtpeyeeminnhekaylrtitsklptlisls
vieilsthasdevylgqrdnphwtsdskalqafqkfgnklkeieeklvrrnndpslqgnr
lgpvqlpytllypsseegltfrgipnsisi
>d1c1ka_ 1.113.1.1.1 gene 59 helicase assembly protein {Bacteriophage T4}
miklrmpaggeryidgksvyklylmikqhmngkydvikynwcmrvsdaayqkrrdkyffq
klsekyklkelalifisnlvanqdawigdisdadalvfyreyigrlkqikfkfeedirni
yyfskkvevsafkeifeynpkvqssyifkllqsniisfetfilldsflniidkhdeqtdn
lvwnnysiklkayrkilnidsqkaknvfietvkscky
>d1a5t_1 1.114.1.1.1 (167-330) delta prime subunit of DNA polymerase III, C-terminal domain {Escherichia coli}
ppeqyavtwlsrevtmsqdallaalrlsagspgaalalfqgdnwqaretlcqalaysvps
gdwysllaalnheqaparlhwlatllmdalkrhhgaaqvtnvdvpglvaelanhlspsrl
qailgdvchireqlmsvtginrellitdlllriehylqpgvvlp
>d2tct_2 1.115.1.1.1 (68-208) Tetracyclin repressor (Tet-repressor, TetR), C-terminal domain {Escherichia coli}
lpaageswqsflrnnamsfrrallryrdgakvhlgtrpdekqydtvetqlrfmtengfsl
rdglyaisavshftlgavleqqehtaaltdrpaapdenlppllrealqimdsddgeqafl
hgleslirgfevqltallqiv
>d1dkfa_ 1.116.1.1.2 Retinoid-X receptor (RXR-alpha) {Mouse (Mus musculus)}
sanedmpvekileaelavepktetyveanmglnpsspndpvtnicqaadkqlftlvewak
riphfselplddqvillragwnelliasashrsiavkdgillatglhvhrnsahsagvga
ifdrvltelvskmrdmqmdktelgclraivlfnpdskglsnpaevealrekvyasleayc
khkypeqpgrfaklllrlpalrsiglkclehlfffkligdtpidtflmemlea
>d1exaa_ 1.116.1.1.4 Retinoic acid receptor gamma (RAR-gamma) {Human (Homo sapiens)}
lspqleelitkvskahqetfpslcqlgkyttnssadhrvqldlglwdkfselatkciiki
vefakrlpgftglsiadqitllkaacldilmlrictrytpeqdtmtfsdgltlnrtqmhn
agfgpltdlvfafagqllplemddtetgllsaiclicgdrmdleepekvdklqeplleal
rlyarrrrpsqpymfprmlmkitdlrgistkgaeraitlkmeipgpmppliremle
>d1a28a_ 1.116.1.1.5 Progesterone receptor {Human (Homo sapiens)}
qlipplinllmsiepdviyaghdntkpdtssslltslnqlgerqllsvvkwskslpgfrn
lhiddqitliqyswmslmvfglgwrsykhvsgqmlyfapdlilneqrmkessfyslcltm
wqipqefvklqvsqeeflcmkvllllntipleglrsqtqfeemrssyirelikaiglrqk
gvvsssqrfyqltklldnlhdlvkqlhlyclntfiqsralsvefpemmseviaaqlpkil
agmvkpllfhk
>d3erda_ 1.116.1.1.6 Estrogen receptor alpha {Human (Homo sapiens)}
slalsltadqmvsalldaeppilyseydptrpfseasmmglltnladrelvhminwakrv
pgfvdltlhdqvhllecawleilmiglvwrsmehpgkllfapnllldrnqgkcvegmvei
fdmllatssrfrmmnlqgeefvclksiillnsgvytflsstlksleekdhihrvldkitd
tlihlmakagltlqqqhqrlaqlllilshirhmsnkgmehlysmkcknvvplydllleml
dahrlh
>d2prga_ 1.116.1.1.7 Peroxisome proliferator activated receptor gamma, PPAR-RXR {Human (Homo sapiens)}
esadlralakhlydsyiksfpltkakarailtgkttdkspfviydmnslmmgedkikfkh
itplqeqskevairifqgcqfrsveavqeiteyaksipgfvnldlndqvtllkygvheii
ytmlaslmnkdgvlisegqgfmtreflkslrkpfgdfmepkfefavkfnalelddsdlai
fiaviilsgdrpgllnvkpiediqdnllqalelqlklnhpessqlfakllqkmtdlrqiv
tehvqllqvikktetdmslhpllqeiykdly
>d1db1a_ 1.116.1.1.9 Vitamin D nuclear receptor {Human (Homo sapiens)}
lrpklseeqqriiailldahhktydptysdfcqfrppvrvndgggsvtlelsqlsmlphl
adlvsysiqkvigfakmipgfrdltsedqivllkssaievimlrsnesftmddmswtcgn
qdykyrvsdvtkaghslelieplikfqvglkklnlheeehvllmaicivspdrpgvqdaa
lieaiqdrlsntlqtyircrhpppgshllyakmiqkladlrslneehskqyrclsfqpec
smkltplvlevfg
>d1ah7__ 1.117.1.1.1 Bacterial phosholipase C {Bacillus cereus}
wsaedkhkegvnshlwivnraidimsrnttlvkqdrvaqlnewrtelengiyaadyenpy
ydnstfashfydpdngktyipfakqaketgakyfklagesyknkdmkqaffylglslhyl
gdvnqpmhaanftnlsypqgfhskyenfvdtikdnykvtdgngywnwkgtnpeewihgaa
vvakqdysgivndntkdwfvkaavsqeyadkwraevtpmtgkrlmdaqrvtagyiqlwfd
tygdr
>d1ca1_1 1.117.1.1.2 (1-249) Alpha-toxin, N-terminal domain {Clostridium perfringens}
wdgkidgtgthamivtqgvsilendlsknepesvrknleilkenmhelqlgstypdydkn
aydlyqdhfwdpdtdnnfskdnswylaysipdtgesqirkfsalaryewqrgnykqatfy
lgeamhyfgdidtpyhpanvtavdsaghvkfetfaeerkeqykintvgcktnedfyadil
knkdfnawskeyargfaktgksiyyshasmshswddwdyaakvtlansqkgtagyiyrfl
hdvsegndp
>d1ak0__ 1.117.1.2.1 P1 nuclease {Penicillium citrinum}
wgalghatvayvaqhyvspeaaswaqgilgsssssylasiaswadeyrltsagkwsaslh
fidaednpptncnvdyerdcgssgcsisaianytqrvsdsslssenhaealrflvhfigd
mtqplhdeayavggnkinvtfdgyhdnlhsdwdtympqkligghalsdaeswaktlvqni
esgnytaqaigwikgdnisepittatrwasdanalvctvvmphgaaalqtgdlyptyyds
vidtielqiakggyrlanwineih
>d1bm0a1 1.118.1.1.1 (5-196) Serum albumin {Human (Homo sapiens)}
sevahrfkdlgeenfkalvliafaqylqqcpfedhvklvnevtefaktcvadesaencdk
slhtlfgdklctvatlretygemadccakqepernecflqhkddnpnlprlvrpevdvmc
tafhdneetflkkylyeiarrhpyfyapellffakrykaafteccqaadkaacllpklde
lrdegkassakq
>d1bm0a2 1.118.1.1.1 (197-388) Serum albumin {Human (Homo sapiens)}
rlkcaslqkfgerafkawavarlsqrfpkaefaevsklvtdltkvhtecchgdllecadd
radlakyicenqdsissklkeccekpllekshciaevendempadlpslaadfveskdvc
knyaeakdvflgmflyeyarrhpdysvvlllrlaktyettlekccaaadphecyakvfde
fkplveepqnli
>d1bm0a3 1.118.1.1.1 (389-582) Serum albumin {Human (Homo sapiens)}
kqncelfeqlgeykfqnallvrytkkvpqvstptlvevsrnlgkvgskcckhpeakrmpc
aedylsvvlnqlcvlhektpvsdrvtkccteslvnrrpcfsalevdetyvpkefnaetft
fhadictlsekerqikkqtalvelvkhkpkatkeqlkavmddfaafvekcckaddketcf
aeegkklvaasqaa
>d1fura_ 1.119.1.1.2 Fumarase {Escherichia coli}
vrsekdsmgaidvpadklwgaqtqrslehfristekmptslihalaltkraaakvnedlg
llseekasairqaadevlagqhddefplaiwqtgsgtqsnmnmnevlanrasellggvrg
merkvhpnddvnksqssndvfptamhvaallalrkqlipqlktltqtlneksrafadivk
igrtnlqdatpltlgqeisgwvamlehnlkhieyslphvaelalggtavgtglnthpeya
rrvadelavitcapfvtapnkfealatcdalvqahgalkglaaslmkiandvrwlasgpr
cgigeisipenepgssimpgkvnptqcealtmlccqvmgndvainmggasgnfelnvfrp
mvihnflqsvrlladgmesfnkhcavgiepnrerinqllneslmlvtalnthigydkaae
iakkahkegltlkaaalalgylseaefdswvrpeqm
>d1auwa_ 1.119.1.1.5 Argininosuccinate lyase/delta-crystallin {Domestic duck (Anas platyrhynchos), delta-crystallin}
tdpimeklnssiaydqrlsevdiqgsmayakalekagiltktelekilsglekiseewsk
gvfvvkqsdedintanerrlkeligdiagklhtgrsrndqvvtdlklfmknslsiisthl
lqliktlveraaieidvilpgythlqkaqpirwsqfllshavaltrdserlgevkkrinv
lplgsgalagnpldidremlrselefasislnsmdaiserdfvveflsfatllmihlskm
aedliiystsefgfltdsdafstgsslmpqkknpdslelirskagrvfgrlasilmvlkg
lpstynkdlqedkeavfdvvdtltavlqvatgvistlqiskenmekaltpemlatdlaly
lvrkgvpfrqahtasgkavhlaetkgitinklsledlksispqfssdvsqvfnfvnsveq
ytalggtakssvttqieqlrelmkkqk
>d1c3ca_ 1.119.1.1.7 Adenylosuccinate lyase {Thermotoga maritima}
veryslspmkdlwteeakyrrwlevelavtrayeelgmipkgvterirnnakidvelfkk
ieektnhdvvafvegigsmigedsrffhygltssdvldtanslalveagkilleslkefc
dvlwevanrykhtptigrthgvhaeptsfglkvlgwysemkrnvqrleraieevsygkis
gavgnyanvppeveekalsylglkpepvstqvvprdrhafylstlaivaagieriaveir
hlqrtevleveepfrkgqrgssamphkknpitcerltglsrmmrayvdpslenialwher
dishssveryvfpdatqtlyymivtatnvvrnmkvneermkknidltkglvfsqrvllkl
iekgltrkeaydivqrnalktwnsekhfleylledeevkklvtkeeleelfdisyylkhv
dhiferfek
>d1b8fa_ 1.119.1.2.1 Histidine ammonia-lyase (HAL) {Pseudomonas putida}
teltlkpgtltlaqlraihaapvrlqldasaapaidasvacveqiiaedrtaygintgfg
llastriashdlenlqrslvlshaagigapldddlvrlimvlkinslsrgfsgirrkvid
alialvnaevyphiplkgsvgasgdlaplahmslvllgegkarykgqwlsatealavagl
epltlaakeglallngtqastayalrglfyaedlyaaaiacgglsveavlgsrspfdari
heargqrgqidtaacfrdllgdssevslshknadkvqdpyslrcqpqvmgacltqlrqaa
evlgieanavsdnplvfaaegdvisggnfhaepvamaadnlalaiaeigslserrislmm
dkhmsqlppflvenggvnsgfmiaqvtaaalasenkalshphsvdslptsanqedhvsma
paagkrlwemaentrgvlaiewlgacqgldlrkglktsaklekarqalrsevahydrdrf
fapdiekavellakgsltgllpagvlpsl
>d1uby__ 1.120.1.1.1 Farnesyl diphosphate synthase {Chicken (Gallus gallus)}
spvvverereefvgffpqivrdltedgighpevgdavarlkevlqynapggkcnrgltvv
aayrelsgpgqkdaeslrcalavgwcielfqaaslvaddimdqsltrrgqlcwykkegvg
ldaindsfllessvyrvlkkycrqrpyyvhllelflqtayqtelgqmldlitapvskvdl
shfseerykaivkyktafysfylpvaaamymvgidskeehenakaillemgeyfqiqddy
ldcfgdpaltgavgtdiqdnkcswlvvqclqrvtpeqrqllednygrkepekvakvkely
eavgmraafqqyeessyrrlqeliekhsnrlpkeiflglaqkiykrqk
>d5eau_2 1.120.1.2.1 (221-548) 5-Epi-aristolochene synthase, C-terminal domain {Tobacco (Nicotiana tabacum)}
knnvllrfakldfnllqmlhkqelaqvsrwwkdldfvttlpyardrvvecyfwalgvyfe
pqysqarvmlvktismisivddtfdaygtvkeleaytdaiqrwdineidrlpdymkisyk
aildlykdyekelssagrshivchaiermkevvrnynvestwfiegytppvseylsnala
tttyyylattsylgmksateqdfewlsknpkileasviicrviddtatyeveksrgqiat
gieccmrdygistkeamakfqnmaetawkdinegllrptpvstefltpilnlarivevty
ihnldgythpekvlkphiinllvdsiki
>d1ps1a_ 1.120.1.3.1 Pentalenene synthase {Streptomyces UC5319}
qdvdfhiplpgrqspdharaeaeqlawprslglirsdaaaerhlrggyadlasrfyphat
gadldlgvdlmswfflfddlfdgprgenpedtkqltdqvaaaldgplpdtappiahgfad
iwrrtcegmtpawcarsarhwrnyfdgyvdeaesrfwnapcdsaaqylamrrhtigvqpt
vdlaeragrfevphrvfdsavmsamlqiavdvnlllndiaslekeeargeqnnmvmilrr
ehgwsksrsvshmqnevrarleqylllesclpkvgeiyqldtaerealeryrtdavrtvi
rgsydwhrssg
>d1oela1 1.121.1.1.1 (2-136,410-525) GroEL {Escherichia coli}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1a6da1 1.121.1.2.1 (17-145,404-519) Thermosome {Thermoplasma acidophilum}
reqgknaqrnnieaakaiadavrttlgpkgmdkmlvdsigdiiisndgatilkemdvehp
takmivevskaqdtavgdgtttavvlsgellkqaetlldqgvhptvisngyrlavneark
iideiaeksXflwgggaveaelamrlakyansvggreqlaieafakaleiiprtlaenag
idpintliklkaddekgrisvgvdldnngvgdmkakgvvdplrvkthalesavevatmil
riddvi
>d1ecma_ 1.122.1.1.1 Chorismate mutase domain of P-protein {Escherichia coli}
npllalrekisaldekllallaerrelavevgkakllshrpvrdidrerdllerlitlgk
ahhldahyitrlfqliiedsvltqqallqqh
>d5csma_ 1.122.1.2.1 Allosteric chorismate mutase {Baker's yeast (Saccharomyces cerevisiae)}
mdftkpetvlnlqnirdelvrmedsiifkfiershfatcpsvyeanhpgleipnfkgsfl
dwalsnleiahsrirrfespdetpffpdkiqksflpsinypqilapyapevnyndkikkv
yiekiipliskrdgddknnfgsvatrdieclqslsrrihfgkfvaeakfqsdiplytkli
kskdvegimknitnsaveekilerltkkaevygvdpterrierrispeylvkiykeivip
itkeveveyllrrlee
>d1pprm1 1.123.1.1.1 (1-156) Peridinin-chlorophyll protein {Dinoflagellate (Amphidinium carterae)}
deigdaakklgdasyafakevdwnngiflqapgklqplealkaidkmivmgaaadpkllk
aaaeahhkaigsisgpngvtsradwdnvnaalgrviasvpenmvmdvydsvskitdpkvp
aymkslvngadaekayegflafkdvvkksqvtsaag
>d1qq8a_ 1.124.1.1.1 Heme oxygenase-1 (HO-1) {Human (Homo sapiens)}
pqdlsealkeatkevhtqaenaefmrnfqkgqvtrdgfklvmaslyhiyvaleeeiernk
espvfapvyfpeelhrkaaleqdlafwygprwqevipytpamqryvkrlhevgrtepell
vahaytrylgdlsggqvlkkiaqkaldlpssgeglafftfpniasatkfkqlyrsrmnsl
emtpavrqrvieeaktafllniqlfeelqellth
>d1poc__ 1.125.1.1.1 Phospholipase A2 {European honeybee (Apis mellifera)}
iiypgtlwcghgnkssgpnelgrfkhtdaccrthdmcpdvmsageskhgltntashtrls
cdcddkfydclknsadtissyfvgkmyfnlidtkcyklehpvtgcgertegrclhytvdk
skpkvyqwfdlrky
>d1poa__ 1.125.1.2.1 Snake phospholipase A2 {Taiwan cobra (Naja naja atra)}
nlyqfknmiqctvpsrswwdfadygcycgrggsgtpvddldrccqvhdncyneaekisgc
wpyfktysyecsqgtltckggnnacaaavcdcdrlaaicfagapyndndyninlkarc
>d1vapa_ 1.125.1.2.5 Snake phospholipase A2 {Eastern cottonmouth snake (Agkistridon piscivorus)}
nlfqfeklikkmtgksgmlwysaygcycgwggqgrpkdatdrccfvhdccygkvtgcnpk
mdiytysvdngnivcggtnpckkqicecdraaaicfrdnlktydsktywkypkknckees
epc
>d1bxm__ 1.126.1.1.1 beta-cryptogein {Phytophthora cryptogea}
rgtctatqqtaayhtlvsilsdasfnqcstdsgysmltakalpttaqyklmcastacntm
ikkivtlnppncdltvptsglvlnvysyangfsnkcssl
>d1b2nb_ 1.127.1.1.1 Methanol dehydrogenase, light chain {Methylophilus w3a1}
ydgqnckepgncwenkpgypekiagskydpkhdpvelnkqeesikamdarnakrian
>d1gg2g_ 1.127.2.1.1 Transducin (heterotrimeric G protein), gamma chain {Bovine (Bos taurus)}
siaqarklveqlkmeanidrikvskaaadlmayceahakedplltpvpasenpf
>d1gotg_ 1.127.2.1.1 Transducin (heterotrimeric G protein), gamma chain {Bovine (Bos taurus)}
ltekdklkmevdqlkkevtlermlvskcceefrdyveersgedplvkgipedknpfke
>d1gp2g_ 1.127.2.1.1 Transducin (heterotrimeric G protein), gamma chain {Bovine (Bos taurus)}
siaqarklveqlkmeanidrikvskaaadlmayceahakedplltpvpasenpf
>d1hfes_ 1.127.3.1.1 Fe-only hydrogenase smaller subunit {Desulfovibrio vulgaris}
vkqikdymldringvygadakfpvrasqdntqvkalyksylekplghkshdllhthwfdk
skgvkelttagklpnprasefegpypye
>d1ef1c_ 1.127.4.1.1 Moesin tail domain {Human (Homo sapiens)}
aeasadlradamakdrseeertteaeknervqkhlkaltselanardeskktandxihae
nxrlgrdkyktlrqirqgntkqridefes
>d2prgc_ 1.127.5.1.1 Nuclear receptor coactivator Src-1 {Human (Homo sapiens)}
qtshklvqlltttaeqqlrhadidtsckdvlsctgtsnsasanssggscpsshsslterh
kilhrllqegspsdit
>d1dp5b_ 1.127.6.1.1 Proteinase A inhibitor IA3 {Baker's yeast (Saccharomyces cerevisiae)}
ntdqqkvseifqsskeklqgdakvvsdafmm
>d1dpjb_ 1.127.6.1.1 Proteinase A inhibitor IA3 {Baker's yeast (Saccharomyces cerevisiae)}
tdqqkvseifqsskeklqgdakvvsdafk
>d1aqe__ 1.128.1.1.1 Cytochrome c3 {Desulfovibrio desulfuricans, different strains}
tfeipesvtmspkqfegytpkkgdvtfnhashmdiacqqchhtvpdtytiescmtegchd
nikerteissvertfhttkdsekscvgchrelkrqgpsdaplacnschvq
>d2cy3__ 1.128.1.1.1 Cytochrome c3 {Desulfovibrio desulfuricans, different strains}
adapgddyvisapegmkakpkgdkpgalqktvpfphtkhatvecvqchhtleadggavkk
cttsgchdslefrdkanakdiklvenafhtqcidchkalkkdkkptgptacgkchttn
>d3cyr__ 1.128.1.1.1 Cytochrome c3 {Desulfovibrio desulfuricans, different strains}
apavpnkpvevkgsqktvmfphaphekvecvtchhlvdgkesyakcgssgchddltakkg
ekslyyvvhakgelkhtsclachskvvaekpelkkdltgcakskchp
>d2ctha_ 1.128.1.1.2 Cytochrome c3 {Desulfovibrio vulgaris}
apkapadglkmeatkqpvvfnhsthksvkcgdchhpvngkedyrkcgtagchdsmdkkdk
sakgyyhvmhdkntkfkscvgchvevagadaakkkdltgckkskche
>d1wad__ 1.128.1.1.3 Cytochrome c3 {Desulfovibrio gigas}
vdvpadgakidfiaggeknltvvfnhsthkdvkcddchhdpgdkqyagcttdgchnildk
adksvnswykvvhdakggakptcischkdkagddkelkkkltgckgsachp
>d1f22a_ 1.128.1.1.4 Cytochrome c7 (cytochrome c551.5) {Desulfuromonas acetoxidans}
advvtyenkkgnvtfdhkahaeklgcdachegtpakiaidkksahkdacktchksnngpt
kcggchik
>d19hca_ 1.128.1.1.5 Nine-haem cytochrome c {Desulfovibrio desulfuricans atcc 27774}
aaleptdsgapsaivmfpvgekpnpkgaamkpvvfnhlihekkiadcetchhtgdpvscs
tchtvegkaegdyitldramhatdiaarakgntptscvschqsetkerrecagchaittp
kddeawcatchditpsmtpsemqkgiagtllpgdnealaaetvlaeatvapvspmlapyk
vvidaladkyepsdfthrrhltslmesikddklaqafhdkpeilcatchhrsplsltppk
cgschtkeidaadpgrpnlmaayhlecmgchkgmavarprdtdcttchkaaa
>d6prcc_ 1.128.1.2.1 Photosynthetic reaction centre (cytochrome subunit) {Rhodopseudomonas viridis}
cfepppatttqtgfrglsmgevlhpatvkakkerdaqyppalaavkaegppvsqvyknvk
vlgnlteaeflrtmtaitewvspqegctychdennlaseakypyvvarrmlemtraintn
wtqhvaqtgvtcytchrgtplppyvryleptlplnnretpthvervetrsgyvvrlakyt
aysalnydpftmflandkrqvrvvpqtalplvgvsrgkerrplsdayatfalmmsisdsl
gtnctfchnaqtfeswgkkstpqraiawwgirmvrdlnmnylaplnaslpasrlgrqgea
pqadcrtchqgvtkplfgasrlkdypelgpik
>d1fgja_ 1.128.1.3.1 Hydroxylamine oxidoreductase, HAO {Nitrosomonas europaea}
distvpdetydalkldrgkatpketyealvkrykdpahgagkgtmgdywepiaisiymdp
ntfykppvspkevaerkdcvechsdetpvwvrawkrsthanldkirnlksddplyykkgk
leevennlrsmgklgeketlkevgcidchvdvnkkdkadhtkdirmptadtcgtchlref
aereserdtmvwpngqwpagrpshaldytaniettvwatmpqrevaegctmchtnqnkcd
nchtrhefsaaesrkpeacatchsgvdhnnweaytmskhgklaemnrdkwnwevrlkdaf
skggqnaptcaachmeyegeythnitrktrwanypfvpgiaenitsdwsearldswvltc
tqchserfarsyldlmdkgtleglakyqeanaivhkmyedgtltgqktnrpnppepekpg
fgiftqlfwskgnnpaslelkvlemgennlakmhvglahvnpggwtytegwgpmnrayve
iqdeytkmqelsalqarvn
>d1bvb__ 1.128.1.3.2 Cytochrome c554 {Nitrosomonas europaea}
adapfegrkkcsschkaqaqswkdtahakameslkpnvkkeakqkakldpakdytqdkdc
vgchvdgfgqkggytiespkpmltgvgceschgpgrnfrgdhrksgqafeksgkktprkd
lakkgqdfhfeercsachlnyegspwkgakapytpftpevdakytfkfdemvkevkamhe
hyklegvfegepkfkfhdefqasakpakkgk
>d1ddca_ 1.128.1.3.3 Dimeric di-heme split-soret cytochrome c {Desulfovibrio desulfuricans, ATCC 27774}
rfdqvggafgwkphkldpkecaqvaydgywykgfgcgfgafysivglmgekygapynqfp
famleankggisdwgtiygalygaaatfslfwgrkevhpmvnelfrwyevtklpifnpgd
aaqgvkgdlpmsasdsvlchisvskwcyenkieatskqrseragrltadaafkaaeiint
kidqgkdfkstfpmqasvsscgechmtkgndanwakgimdctpchsgtaatqnkfvnh
>d1qdba_ 1.128.1.3.4 Cytochrome c nitrite reductase {Sulfurospirillum deleyianum}
giagkekseewakyyprqfdswkktkeydsftdmlakdpalviawsgyafskdynsprgh
yyalqdnvnslrtgapvdaktgplptacwtckspdvprlieedgeleyftgkwakygsqi
vnvigcanchddktaelkvrvphlnrglqaaglktfeesthqdkrtlvcaqchveyyfkk
tewkdakgadktamvvtlpwangvgkdgnagvegmikyydeinfsdwthnisktpmlkaq
hpgfefwksgihgqkgvscadchmpytqegsvkysdhqvkenpldsmdqscmnchreses
klrgivhqkyerkeflnkvafdnigkahletgkaieagasdeelkevrklirhgqfkadm
aiaahgnyfhapeetlrllaagsddaqkarlllvkilakhgvmdyiapdfdtkdkaqkla
kvdiaalaaekmkfkqtleqewkkeakakgranpelykdvdtindgksswnkk
>d1qjda1 1.128.1.3.5 (1-102) Flavocytochrome c3 (respiratory fumarate reductase), N-terminal domain {Shewanella frigidimarina}
adnlaefhvqnqecdschtpdgelsndsltyentqcvschgtlaevaettkhehynahas
hfpgevactschsaheksmvycdschsfdfnmpyakkwlrde
>d1neu__ 2.1.1.1.1 Myelin membrane adhesion molecule P0 {Rat (Rattus norvegicus)}
ivvytdrevygavgsqvtlhcsfwssewvsddisftwryqpeggrdaisifhyakgqpyi
devgtfkeriqwvgdpswkdgsivihnldysdngtftcdvknppdivgktsqvtlyvfe
>d1kacb_ 2.1.1.1.2 Coxsackie virus and adenovirus receptor (Car), domain 1 {Human (Homo sapiens)}
gittpeemiekakgetaylpckftlspedqgpldiewlispadnqkvdqviilysgdkiy
ddyypdlkgrvhftsndlksgdasinvtnlqlsdigtyqckvkkapgvankkihlvvlvk
psga
>d1qfoa_ 2.1.1.1.3 N-terminal domain of sialoadhesin {Mouse (Mus musculus)}
twgvsspknvqglsgscllipcifsypadvpvsngitaiwyydysgkrqvvihsgdpklv
dkrfrgraelmgnmdhkvcnlllkdlkpedsgtynfrfeisdsnrwldvkgttvtvtt
>d1akjd_ 2.1.1.1.4 CD8 {Human (Homo sapiens)}
sqfrvspldrtwnlgetvelkcqvllsnptsgcswlfqprgaaasptfllylsqnkpkaa
egldtqrfsgkrlgdtfvltlsdfrrenegyyfcsalsnsimyfshfvpvflpa
>d1bqhg_ 2.1.1.1.5 CD8 {Mouse (Mus musculus)}
kpqapelrifpkkmdaelgqkvdlvcevlgsvsqgcswlfqnsssklpqptfvvymassh
nkitwdeklnssklfsamrdtnnkyvltlnkfskenegyyfcsvisnsvmyfssvvpvlq
kv
>d1cdy_1 2.1.1.1.6 (1-97) CD4 {Human (Homo sapiens)}
kkvvlgkkgdtveltctasqkksiqfhwknsnqikilgnqgsfltkspsklndradsrrs
lwdqgnfpliiknlkiedsdtyicevedqkeevqllv
>d1wioa2 2.1.1.1.6 (179-291) CD4 {Human (Homo sapiens)}
fqkassivykkegeqvefsfplaftvekltgsgelwwqaerassskswitfdlknkevsv
krvtqdpklqmgkklplhltlpqalpqyagsgnltlaleaktgklhqevnlvv
>d1cid_1 2.1.1.1.7 (1-105) CD4 {Rat (Rattus rattus)}
tsitayksegesaefsfplnlgeeslqgelrwkaekapssqswitfslknqkvsvqksts
npkfqlsetlpltlqipqvslqfagsgnltltldrgilyqevnlv
>d1hnf_1 2.1.1.1.8 (4-104) CD2, first domain {Human (Homo sapiens)}
tnaletwgalgqdinldipsfqmsddiddikwektsdkkkiaqfrkeketfkekdtyklf
kngtlkikhlktddqdiykvsiydtkgknvlekifdlkiqe
>d1cdca_ 2.1.1.1.9 CD2, first domain {Rat (Rattus rattus)}
gtvwgalghginlnipnfqmtddidevrwergstlvaefkrkmkpflksgafeilangdl
kiknltrddsgtynvtvystngtrildkaldlrile
>d1ccza1 2.1.1.1.10 (1-93) CD2-binding domain of CD58, first domain {Human (Homo sapiens)}
fsqqiygvvygnvtfhvpsnvplkevlwkkqkdkvaelensefrafssfknrvyldtvsg
sltiynltssdedeyemespnitdtmkfflyvl
>d1mfa_1 2.1.1.1.34 (1l-111l) Immunoglobulin (variable domains of L and H chains) {Fab SE155-4 (mouse), lambda L chain}
qivvtqesalttspgetvtltcrsstgtvtsgnhanwvqekpdhlftgligdtnnrapgv
parfsgsligdkaaltitgaqpedeaiyfcalwsnnhwifgggtkltvlgq
>d1mfa_2 2.1.1.1.34 (251h-367h) Immunoglobulin (variable domains of L and H chains) {Fab SE155-4 (mouse), lambda L chain}
evqvqqsgtvvarpgasvkmsckasgytftnywmhwikqrpgqglewigaiypgnsatfy
nhkfraktkltavtstttaymelssltsedsavyyctrgghgyygdywgqgasltvs
>d1teth1 2.1.1.1.36 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab TE33 (mouse), kappa L chain}
qiqlvqsgpelktpgetvrisckasgytfttygmswvkqtpgkgfkwmgwintysgvpty
addfkgrfafsletsastaylqinnlknedtatyfcarrswyfdvwgtgttvtvs
>d1a2yb_ 2.1.1.1.43 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
qvqlqesgpglvapsqslsitctvsgfsltgygvnwvrqppgkglewlgmiwgdgntdyn
salksrlsiskdnsksqvflkmnslhtddtaryycarerdyrldywgqgttltvss
>d1a7ol_ 2.1.1.1.43 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
divltqspaslsasvgetvtitcrasgnihnylawyqqkqgkspqllvyytttladgvps
rfsgsgsgtqyslkinslqpddfgsyycqhfwstptfgggtkleik
>d1nfde1 2.1.1.1.95 (2-107) Immunoglobulin (variable domains of L and H chains) {Fab H57 (hamster), lambda(?) L chain}
yeliqpssasvtvgetvkitcsgdqlpknfaywfqqksdknillliymdnkrpsgiperf
sgstsgttatltisgaqpedeaayyclssygdnndlvfgsgtqltvlr
>d1dlfh_ 2.1.1.1.141 Immunoglobulin (variable domains of L and H chains) {Anti-dansyl Fv, (mouse), kappa L chain}
evkleesggglvqpggsmklscatsgftfsdawmdwvrqspekglewvaeirnkannhat
yyaesvkgrftisrddskrrvylqmntlraedtgiyyctgiyyhypwfaywgqgtlvtvs
>d1dlfl_ 2.1.1.1.141 Immunoglobulin (variable domains of L and H chains) {Anti-dansyl Fv, (mouse), kappa L chain}
dvvmtqtplslpvslgnqasiscrssqslvhsngntylhwylqkpgqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyfcsqsthvpftfgsgtkleikr
>d2rhe__ 2.1.1.1.164 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (lambda) dimer RHE (human)}
esvltqppsasgtpgqrvtisctgsatdigsnsviwyqqvpgkapklliyyndllpsgvs
drfsasksgtsaslaisglesedeadyycaawndsldepgfgggtkltvlgqpk
>d1cd0b_ 2.1.1.1.170 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (lambda) dimer JTO (human)}
nfmlnqphsvsespgktvtisctrssgnidsnyvqwyqqrpgsapitviyednqrpsgvp
drfagsidrssnsasltisglktedeadyycqsydarnvvfgggtrltvl
>d1nfda1 2.1.1.1.177 (1-117) T-cell antigen receptor {Mouse (Mus musculus), alpha-chain}
dsvtqteglvtvteglpvklnctyqttyltiaffwyvqylneapqvllksstdnkrtehq
gfhatlhkssssfhlqkssaqlsdsalyycalseggnykyvfgagtrlkviah
>d1tcra1 2.1.1.1.177 (1-117) T-cell antigen receptor {Mouse (Mus musculus), alpha-chain}
qsvtqpdarvtvsegaslqlrckysysatpylfwyvqyprqglqlllkyysgdpvvqgvn
gfeaefsksnssfhlrkasvhwsdsavyfcavsgfasaltfgsgtkvivlpy
>d1ac6a_ 2.1.1.1.178 T-cell antigen receptor {Human (Homo sapiens), alpha-chain}
dsvtqtegqvalseedfltihcnysasgypalfwyvqypgegpqflfrasrdkekgssrg
featynkeatsfhlqkasvqesdsavyycalsggnnkltfgagtkltikp
>d1ao7d_ 2.1.1.1.178 T-cell antigen receptor {Human (Homo sapiens), alpha-chain}
keveqnsgplsvpegaiaslnctysdrgsqsffwyrqysgkspelimsiysngdkedgrf
taqlnkasqyvsllirdsqpsdsatylcavttdswgklqfgagtqvvvtpdiqnp
>d1b88a_ 2.1.1.1.178 T-cell antigen receptor {Human (Homo sapiens), alpha-chain}
mqqvrqspqsltvwegetailncsyensafdyfpwyqqfpgegpallisilsvsnkkedg
rftiffnkrekklslhiadsqpgdsatyfcaasasfgdnskliwglgtslvvnp
>d1bec_1 2.1.1.1.179 (3-117) T-cell antigen receptor {Mouse (Mus musculus), beta-chain}
avtqsprnkvavtggkvtlscqqtnnhnnmywyrqdtghglrlihysygagstekgdipd
gykasrpsqeqfslilelatpsqtsvyfcasgggrgsyaeqffgpgtrltvle
>d1kb5b_ 2.1.1.1.179 T-cell antigen receptor {Mouse (Mus musculus), beta-chain}
vtlleqnprwrlvprgqavnlrcilknsqypwmswyqqdlqkqlqwlftlrspgdkevks
lpgadylatrvtdtelrlqvanmsqgrtlyctcsaapdwgasaetlyfgsgtrltvl
>d1nfdb1 2.1.1.1.179 (1-117) T-cell antigen receptor {Mouse (Mus musculus), beta-chain}
dsgvvqsprhiikekggrsvltcipisghsnvvwyqqtlgkelkfliqhyekverdkgfl
psrfsvqqfddyhsemnmsaleledsamyfcasslrwgdeqyfgpgtrltvle
>d1tvda_ 2.1.1.1.181 T-cell antigen receptor {Human (Homo sapiens), delta-chain}
dkvtqsspdqtvasgsevvllctydtvysnpdlfwyrirpdysfqfvfygddsrsegadf
tqgrfsvkhiltqkafhlvispvrtedsatyycaftlppptdklifgkgtrvtvep
>d1ah1__ 2.1.1.1.182 Immunoreceptor CTLA-4 (CD152), N-terminal fragment {Human (Homo sapiens)}
amhvaqpavvlassrgiasfvceyaspgkatevrvtvlrqadsqvtevcaatymmgnelt
flddsictgtssgnqvnltiqglramdtglyickvelmypppyylgigngtqiyvidpep
cpdsdqepk
>d3frua1 2.1.1.2.1 (179-269) Fc (IgG) receptor, alpha-3 domain and beta subunit {Rat (Rattus norvegicus)}
keppsmrlkarpgnsgssvltcaafsfyppelkfrflrnglasgsgncstgpngdgsfha
wsllevkrgdehhyqcqveheglaqpltvdl
>d1duza1 2.1.1.2.4 (182-275) Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-A2.1}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrdgedqtqdtelvetrpagdgtf
qkwaavvvpsgqeqrytchvqheglpkpltlrwe
>d1duzb1 2.1.1.2.4 Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-A2.1}
miqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskd
wsfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1de4a1 2.1.1.2.13 (182-275) Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), hemochromatosis protein Hfe}
qqvpplvkvthhvtssvttlrcralnyypqnitmkwlkdkqpmdakefepkdvlpngdgt
yqgwitlavppgeeqrytcqvehpgldqpliviw
>d1zaga1 2.1.1.2.19 (184-277) Zinc-alpha-2-glycoprotein, ZAG {Human (Homo sapiens)}
qdppsvvvtshqapgekkklkclaydfypgkidvhwtragevqepelrgdvlhngngtyq
swvvvavppqdtapyschvqhsslaqplvvpwea
>d1b3ja1 2.1.1.2.20 (181-274) MHC I homolog {Human (Homo sapiens) Mic-a}
tvppmvnvtrseasegnitvtcrasgfypwnitlswrqdgvslshdtqqwgdvlpdgngt
yqtwvatricqgeeqrftcymehsgnhsthpvps
>d8faba2 2.1.1.2.24 (106-208) Immunoglobulin (constant domains of L and H chains) {Fab HIL (human), lambda L chain}
lgqpkaapsvtlfppsseelqankatlvclisdfypgavtvawkadsspikagvetttps
kqsnnkyaassylsltpeqwkshrsyscqvthegstvektvap
>d8fabb2 2.1.1.2.24 (122-223) Immunoglobulin (constant domains of L and H chains) {Fab HIL (human), lambda L chain}
astkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkvepks
>d2fbjh2 2.1.1.2.37 (119-220) Immunoglobulin (constant domains of L and H chains) {Fab J539 (mouse), kappa L chain}
esarnptiypltlppalssdpviigclihdyfpsgtmnvtwgksgkdittvnfppalasg
grytmsnqltlpavecpegesvkcsvqhdsnpvqeldvncsg
>e1cl7.1i 2.1.1.2.143 Immunoglobulin (constant domains of L and H chains) {Fab 1696, (mouse), kappa L chain}
smvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsdlytlsssvtvpssprpsetv
tcnvahpasstkvdkkivprdc
>d1dqqa2 2.1.1.2.144 (108-214) Immunoglobulin (constant domains of L and H chains) {Anti-lysozyme Fab HYHEL-63, (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1deeb2 2.1.1.2.149 (622-723) Immunoglobulin (constant domains of L and H chains) {Fab of human IgM RF 2A2}
gsasaptlfplvscensnpsstvavgclaqdflpdsitfswkyknnsdisstrgfpsvlr
ggkyaatsqvllpskdvaqgtnehvvckvqhpngnkekdvpl
>d1dn2a1 2.1.1.2.155 (237-341) Immunoglobulin (constant domains of L and H chains) {Fc (human) IgG1 class}
gpsvflfppkpkdtlmisrtpevtcvvvdvshenpevkfnwyvdgvevhnaktkpreeqy
nstyrvvsvltvlhqdwlngkeykckvsnkalpapiektiskakg
>d1cqka_ 2.1.1.2.158 Immunoglobulin (constant domains of L and H chains) {Fc MAK33 (mouse)}
paapqvytipppleqmakdlvsltcmitdffpeditvewqwngqpaenykntqpimdtdg
syfvysklnvqksnweagntftcsvlheglhnhhtekslsh
>d1tcra2 2.1.1.2.159 (118-213) T-cell antigen receptor {Mouse (Mus musculus), alpha-chain}
iqnpepavyalkdprsqdstlclftdfdsqinvpktmesgtfitdatvldmkamdsksng
aiawsnqtsftcqdifketnatypssdvpc
>d1bd2d2 2.1.1.2.160 (118-203) T-cell antigen receptor {Human (Homo sapiens)}
iqnpdpavyqlrdskssdksvclftdfdsqtnvsqskdsdvyitdktvldmrsmdfksns
avawsnksdfacanafnnsiipedtf
>d1bec_2 2.1.1.2.161 (118-246) T-cell antigen receptor {Mouse (Mus musculus), beta-chain}
dlrqvtppkvslfepskaeiankqkatlvclargffpdhvelswwvngkevhsgvstdpq
aykesnysyclssrlrvsatfwhnprnhfrcqvqfhglseedkwpegspkpvtqnisaea
wgrad
>d1cd1a1 2.1.1.2.163 (186-279) CD1, beta2-microglobulin and alpha-3 domain {Mouse (Mus musculus)}
qekpvawlssvpssahghrqlvchvsgfypkpvwvmwmrgdqeqqgthrgdflpnadetw
ylqatldveageeaglacrvkhsslggqdiilyw
>d1hdma1 2.1.1.2.164 (94-196) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dm}
srgfpiaevftlkplefgkpntlvcfvsnlfppmltvnwhdhsvpvegfgptfvsavdgl
sfqafsylnftpepsdifscivthepdrytaiaywvprnalps
>d1hdmb1 2.1.1.2.164 (88-185) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dm}
trppsvqvakttpfntrepvmlacyvwgfypaevtitwrkngklvmhssahktaqpngdw
tyqtlshlaltpsygdtytcvvehigapepilrdwtpg
>d1iaka1 2.1.1.2.169 (82-181) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA i-ak}
atneapqatvfpkspvllgqpntlicfvdnifppvinitwlrnsksvtdgvyetsffvnr
dysfhklsyltfipsdddiydckvehwgleepvlkhwepe
>d1iakb1 2.1.1.2.169 (93-190) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA i-ak}
rleqpsvvislsrtealnhhntlvcsvtdfypakikvrwfrngqeetvgvsstqlirngd
wtfqvlvmlemtprrgevytchvehpsltspitvewra
>d1vcaa1 2.1.1.3.1 (91-199) Second domain of vascular cell adhesion molecule-1 (VCAM-1) {Human (Homo sapiens)}
fpkdpeihlsgpleagkpitvkcsvadvypfdrleidllkgdhlmksqefledadrksle
tkslevtftpviedigkvlvcraklhidemdsvptvrqavkelqvyisp
>d1iam_1 2.1.1.3.2 (83-185) Second domain of intercellular cell adhesion molecule-1 (ICAM-1) {Human (Homo sapiens)}
ywtpervelaplpswqpvgkqltlrcqveggapraqltvvllrgekelkrepavgepaev
tttvlvrrdhhgaqfscrteldlrpqglelfentsapyqlqtf
>d1zxq_1 2.1.1.3.3 (87-192) Second domain of intercellular cell adhesion molecule-2 (ICAM-2) {Human (Homo sapiens)}
pprqviltlqptlvavgksftiecrvptvepldsltlflfrgnetlhyetfgkaapapqe
atatfnstadredghrnfsclavldlmsrggnifhkhsapkmleiy
>d1cdy_2 2.1.1.3.4 (98-178) CD4 {Human (Homo sapiens)}
fgltansdthllqgqsltltlesppgsspsvqcrsprgkniqggktlsvsqlelqdsgtw
tctvlqnqkkvefkidivvla
>d1wioa4 2.1.1.3.4 (292-363) CD4 {Human (Homo sapiens)}
mratqlqknltcevwgptspklmlslklenkeakvskrekavwvlnpeagmwqcllsdsg
qvllesnikvlp
>d1cid_2 2.1.1.3.5 (106-177) CD4 {Rat (Rattus rattus)}
vmkvtqpdsntltcevmgptspkmrlilkqenqearvsrqekviqvqapeagvwqcllse
geevkmdskiqv
>d1hnf_2 2.1.1.3.6 (105-182) CD2, second domain {Human (Homo sapiens)}
rvskpkiswtcinttltcevmngtdpelnlyqdgkhlklsqrvithkwttslsakfkcta
gnkvskessvepvscpek
>d1ccza2 2.1.1.3.8 (94-171) CD2-binding domain of CD58, second domain {Human (Homo sapiens)}
emvskpmiywecsnatltcevlegtdvelklyqgkehlrslrqktmsyqwtnlrapfkck
avnrvsqesemevvncpe
>d1vcaa2 2.1.1.4.1 (1-90) N-terminal domain of vascular cell adhesion molecule-1 (VCAM-1) {Human (Homo sapiens)}
fkiettpesrylaqigdsvsltcsttgcespffswrtqidsplngkvtnegttstltmnp
vsfgnehsylctatcesrklekgiqveiys
>d1iam_2 2.1.1.4.2 (1-82) N-terminal domain of intracellular adhesion molecule-1, ICAM-1 {Human (Homo sapiens)}
qtsvspskvilprggsvlvtcstscdqpkllgietplpkkelllpgnnrkvyelsnvqed
sqpmcysncpdgqstaktfltv
>d1zxq_2 2.1.1.4.3 (1-86) N-terminal domain of intracellular adhesion molecule-2, ICAM-2 {Human (Homo sapiens)}
kvfevhvrpkklavepkgslevncsttcnqpevggletslnkilldeqaqwkhylvsnis
hdtvlqchftcsgkqesmnsnvsvyq
>d2ncm__ 2.1.1.4.4 Neural cell adhesion molecule (NCAM) {Human (Homo sapiens)}
rvlqvdivpsqgeisvgeskfflcqvagdakdkdiswfspngeklspnqqrisvvwnddd
sstltiynaniddagiykcvvtaedgtqseatvnvkifq
>d3ncma_ 2.1.1.4.4 Neural cell adhesion molecule (NCAM) {Human (Homo sapiens)}
yvmfknaptpqefkegedavivcdvvsslpptiiwkhkgrdvilkkdvrfivlsnnylqi
rgikktdegtyrcegrilargeinfkdiqviv
>d1bqsa1 2.1.1.4.5 (1-90) Mucosal addressin cell adhesion molecule-1 (MADCAM-1) {Human (Homo sapiens)}
vkplqveppepvvavalgasrqltcrlacadrgasvqwrgldtslgavqsdtgrsvltvr
naslsaagtrvcvgscggrtfqhtvqllvy
>d1bqsa2 2.1.1.4.5 (91-209) Mucosal addressin cell adhesion molecule-1 (MADCAM-1) {Human (Homo sapiens)}
afpnqltvspaalvpgdpevactahkvtpvdpnalsfsllvggqelegaqalgpevqeee
eepqgdedvlfrvterwrlpplgtpvppalycqatmrlpglelshrqaipvlhsptspe
>d1tlk__ 2.1.1.4.6 Telokin {Turkey (Meleagris gallopavo)}
vaeekphvkpyftktildmdvvegsaarfdckvegypdpevmwfkddnpvkesrhfqidy
deegncsltisevcgdddakytckavnslgeatctaellvetm
>d1nct__ 2.1.1.4.7 Titin {Human (Homo sapiens), module M5}
skttlaariltkprsmtvyegesarfscdtdgepvptvtwlrkgqvlstsarhqvtttky
kstfeissvqasdegnysvvvensegkqeaeftltiqk
>d1koa_1 2.1.1.4.8 (6265-6361) Twitchin {Nematode (Caenorhabditis elegans)}
qprfivkpygtevgegqsanfycrviassppvvtwhkddrelkqsvkymkryngndyglt
inrvkgddkgeytvraknsygtkeeivflnvtrhsep
>d1wiu__ 2.1.1.4.8 Twitchin {Nematode (Caenorhabditis elegans)}
lkpkiltasrkikikagfthnlevdfigapdptatwtvgdsgaalapellvdakssttsi
ffpsakradsgnyklkvknelgedeaifevivq
>d1tiu__ 2.1.1.4.9 Twitchin {Human (Homo sapiens), Ig repeat 27}
lievekplygvevfvgetahfeielsepdvhgqwklkgqpltaspdceiiedgkkhilil
hncqlgmtgevsfqaanaksaanlkvkel
>d1iray1 2.1.1.4.10 (1-101) Type-1 interleukin-1 receptor {Human (Homo sapiens)}
dkckereekiilvssaneidvrpcplnpnehkgtitwykddsktpvsteqasrihqhkek
lwfvpakvedsghyycvvrnssyclrikisakfvenepnlc
>d1iray2 2.1.1.4.10 (102-204) Type-1 interleukin-1 receptor {Human (Homo sapiens)}
ynaqaifkqklpvagdgglvcpymeffknennelpklqwykdckpllldnihfsgvkdrl
ivmnvaekhrgnytchasytylgkqypitrviefitleenkpt
>d1iray3 2.1.1.4.10 (205-311) Type-1 interleukin-1 receptor {Human (Homo sapiens)}
rpvivspanetmevdlgsqiqlicnvtgqlsdiaywkwngsvideddpvlgedyysvenp
ankrrstlitvlniseiesrfykhpftcfaknthgidaayiqliypv
>d1ev2e1 2.1.1.4.12 (150-250) Fibroblast growth factor receptor, FGFR {Human (Homo sapiens), FGFR2}
nkrapywtntekmekrlhavpaantvkfrcpaggnpmptmrwlkngkefkqehriggykv
rnqhwslimesvvpsdkgnytcvveneygsinhtyhldvve
>d1ev2e2 2.1.1.4.12 (251-360) Fibroblast growth factor receptor, FGFR {Human (Homo sapiens), FGFR2}
rsphrpilqaglpanastvvggdvefvckvysdaqphiqwikhvekngskygpdglpylk
vlkaagvnttdkeievlyirnvtfedageytclagnsigisfhsawltvl
>d1biha1 2.1.1.4.13 (5-98) Hemolin {Moth (Hyalophora cecropia)}
kypvlkdqpaevlfrennptvleciiegndqgvkyswkkdgksynwqehnaalrkdegsl
vflrpqasdeghyqcfaetpagvassrvisfrkt
>d1biha2 2.1.1.4.13 (99-209) Hemolin {Moth (Hyalophora cecropia)}
yliaspakthektpiegrpfqldcvlpnaypkplitwkkrlsgadpnadvtdfdrritag
pdgnlyftivtkedvsdiykyvctaknaavdeevvlveyeikgvtkdnsgy
>d1biha3 2.1.1.4.13 (210-306) Hemolin {Moth (Hyalophora cecropia)}
kgepvpqyvskdmmakagdvtmiycmygsnpmgypnyfkngkdvngnpedritrhnrtsg
krllfkttlpedegvytcevdngvgkpqkhslkltvv
>d1biha4 2.1.1.4.13 (307-395) Hemolin {Moth (Hyalophora cecropia)}
sapkyeqkpekvivvkqgqdvtipckvtglpapnvvwshnakplsggratvtdsglvikg
vkngdkgyygcratnehgdkyfetlvqvn
>d1cs6a1 2.1.1.4.14 (7-103) Axonin-1 {Ckicken (Gallus gallus)}
rsygpvfeeqpahtlfpegsaeekvtltcraranppatyrwkmngtelkmgpdsryrlva
gdlvisnpvkakdagsyqcvatnargtvvsreaslrf
>d1cs6a2 2.1.1.4.14 (104-208) Axonin-1 {Ckicken (Gallus gallus)}
gflqefsaeerdpvkitegwgvmftcsppphypalsyrwllnefpnfipadgrrfvsqtt
gnlyiakteasdlgnyscfatshidfitksvfskfsqlslaaeda
>d1cs6a3 2.1.1.4.14 (209-299) Axonin-1 {Ckicken (Gallus gallus)}
rqyapsikakfpadtyaltgqmvtlecfafgnpvpqikwrkldgsqtskwlssepllhiq
nvdfedegtyeceaenikgrdtyqgriiiha
>d1cs6a4 2.1.1.4.14 (300-388) Axonin-1 {Ckicken (Gallus gallus)}
qpdwldvitdteadigsdlrwscvasgkprpavrwlrdgqplasqnrievsggelrfskl
vledsgmyqcvaenkhgtvyasaeltvqa
>d1fltx_ 2.1.1.4.15 Second domain of the Flt-1 receptor {Human (Homo sapiens)}
grpfvemyseipeiihmtegrelvipcrvtspnitvtlkkfpldtlipdgkriiwdsrkg
fiisnatykeiglltceatvnghlyktnylthrqt
>d1wwwx_ 2.1.1.4.16 NGF binding domain of trkA receptor {Human (Homo sapiens)}
vsfpasvqlhtavemhhwcipfsvdgqpapslrwlfngsvlnetsfifteflepaanetv
rhgclrlnqpthvnngnytllaanpfgqasasimaafmdnp
>d1wwbx_ 2.1.1.4.17 Ligand binding domain of trkB receptor {Human (Homo sapiens)}
vhfaptitflesptsdhhwcipftvkgnpkpalqwfyngailneskyictkihvtnhtey
hgclqldnpthmnngdytliakneygkdekqisahfmgwpgid
>d1wwca_ 2.1.1.4.18 NT3 binding domain of trkC receptor {Human (Homo sapiens)}
tvyypprvvsleepelrlehciefvvrgnppptlhwlhngqplreskiihveyyqegeis
egcllfnkpthynngnytliaknplgtanqtinghflkepfpvde
>d2fcba1 2.1.1.4.20 (6-90) Tc gamma receptor ectodomain (CD32) {Human (Homo sapiens) IIb}
appkavlklepqwinvlqedsvtltcrgthspesdsiqwfhngnlipthtqpsyrfkann
ndsgeytcqtgqtslsdpvhltvls
>d2fcba2 2.1.1.4.20 (91-178) Tc gamma receptor ectodomain (CD32) {Human (Homo sapiens) IIb}
ewlvlqtphlefqegetivlrchswkdkplvkvtffqngkskkfsrsdpnfsipqanhsh
sgdyhctgnigytlysskpvtitvqapa
>d1f2qa1 2.1.1.4.21 (4-85) IgE high affinity receptor alpha subunit {Human (Homo sapiens)}
kpkvslnppwnrifkgenvtltcngnnffevsstkwfhngslseetnsslnivnakfeds
geykcqhqqvnesepvylevfs
>d1f2qa2 2.1.1.4.21 (86-174) IgE high affinity receptor alpha subunit {Human (Homo sapiens)}
dwlllqasaevvmegqplflrchgwrnwdvykviyykdgealkywyenhnisitnatved
sgtyyctgkvwqldyeseplnitvikapr
>d1gof_1 2.1.1.5.1 (538-639) Galactose oxidase, C-terminal domain {Dactylium dendroides}
gnlatrpkitrtstqsvkvggritistdssiskaslirygtathtvntdqrripltltnn
ggnsysfqvpsdsgvalpgywmlfvmnsagvpsvastirvtq
>d1qba_1 2.1.1.5.2 (781-885) Bacterial chitobiase, c-terminal domain {Serratia marcescens}
gethfvdtqalekdwlrfanilgqrelakldkggvayrlpvpgarvaggkleanialpgl
gieystdggkqwqrydakakpavsgevqvrsvspdgkrysraekv
>d1svb_1 2.1.1.5.3 (303-395) Envelope glycoprotein, domain III (C-terminal) {Tick-borne encephalitis virus, TBE}
tytmcdktkftwkraptdsghdtvvmevtfsgtkpcripvravahgspdvnvamlitpnp
tienngggfiemqlppgdniiyvgelshqwfqk
>d1cyg_1 2.1.1.5.5 (492-574) Cyclodextrin glycosyltransferase, domain E {Bacillus stearothermophilus}
estpiighvgpmmgqvghqvtidgegfgtntgtvkfgttaanvvswsnnqivvavpnvsp
gkynitvqsssgqtsaaydnfev
>d1qhoa1 2.1.1.5.6 (496-576) Cyclodextrin glycosyltransferase, domain E {Bacillus stearothermophilus maltogenic alpha-amylase}
asapqigsvapnmgipgnvvtidgkgfgttqgtvtfggvtatvkswtsnrievyvpnmaa
gltdvkvtaggvssnlysyni
>d1pama1 2.1.1.5.7 (497-582) Cyclodextrin glycosyltransferase, domain E {Alkalophilic bacillus, sp. 1011}
ttpiignvgpmmakpgvtitidgrgfgsgkgtvyfgttavtgadivawedtqiqvkipav
pggiydirvanaagaasniydnfevl
>d1ciu_1 2.1.1.5.8 (496-578) Cyclodextrin glycosyltransferase, domain E {Thermoanaerobacterium thermosulfurigenes, EM1}
snsplighvgptmtkagqtitidgrgfgttsgqvlfgstagtivswddtevkvkvpsvtp
gkynislktssgatsntynnini
>d1smaa1 2.1.1.5.9 (1-123) Maltogenic amylase, N-terminal domain {Thermus sp.}
mrkeaihhrstdnfayaydsetlhlrlqtkkndvdhvellfgdpyewhdgawqfqtmpmr
ktgsdglfdywlaevkppyrrlrygfvlraggeklvytekgfyheapsddtayyfcfpfl
hrv
>d1bvza1 2.1.1.5.10 (1-120) Maltogenic amylase, N-terminal domain {Thermoactinomyces vulgaris, TVAII}
mlleaifheakgsyaypisetqlrvrlrakkgdvvrcevlyadryaspeeelahalagka
gsderfdyfeallecstkrvkyvflltgpqgeavyfgetgfsaerskagvfqyayihrse
>d1bf2_1 2.1.1.5.11 (1-162) Isoamylase, N-terminal domain {Pseudomonas amyloderamosa}
ainsmslgasydaqqanitfrvyssqatrivlylysagygvqesatytlspagsgvwavt
vpvssikaagitgavyygyrawgpnwpyasnwgkgsqagfvsdvdangdrfnpnkllldp
yaqevsqdplnpsnqngnvfasgasyrttdsgiyapkgvvlv
>d1lla_3 2.1.1.5.12 (380-628) Hemocyanin, C-terminal domain {Horseshoe crab (Limulus polyphemus), hemolymph}
pydhdvlnfpdiqvqdvtlharvdnvvhtfmreqelelkhginpgnarsikaryyhldhe
pfsyavnvqnnsasdkhatvriflapkydelgneikadelrrtaieldkfktdlhpgknt
vvrhsldssvtlshqptfedllhgvglnehkseycscgwpshllvpkgnikgmeyhlfvm
ltdwdkdkvdgsesvacvdavsycgardhkypdkkpmgfpfdrpihtehisdfltnnmfi
kdikikfhe
>d1clc_2 2.1.1.5.14 (35-134) CelD cellulase, N-terminal domain {Clostridium thermocellum}
ietkvsaakitenyqfdsrirlnsigfipnhskkatiaancstfyvvkedgtivytgtat
smfdndtketvyiadfssvneegtyylavpgvgksvnfki
>d1edqa1 2.1.1.5.15 (24-132) Chitinase A, N-terminal domain {Serratia marcescens}
aapgkptiawgntkfaivevdqaataynnlvkvknaadvsvswnlwngdtgttakvllng
keawsgpstgssgtanfkvnkggryqmqvalcnadgctasdateivvad
>d1f13a1 2.1.1.5.16 (5-190) Transglutaminase factor XIII, N-terminal domain {Human (Homo sapiens), blood}
rtafggrravppnnsnaaeddlptvelqgvvprgvnlqeflnvtsvhlfkerwdtnkvdh
htdkyennklivrrgqsfyvqidfsrpydprrdlfrveyvigrypqenkgtyipvpivse
lqsgkwgakivmredrsvrlsiqsspkcivgkfrmyvavwtpygvlrtsrnpetdtyilf
npwced
>d1eut_1 2.1.1.5.17 (403-505) Sialidase, "linker" domain {Micromonospora viridifaciens}
gicapftipdvalepgqqvtvpvavtnqsgiavpkpslqldaspdwqvqgsveplmpgrq
akgqvtitvpagttpgryrvgatlrtsagnasttftvtvglld
>d1ksr__ 2.1.1.5.18 F-actin cross-linking gelation factor (ABP-120), one repeat (ROD 4) {Slime mold (Dictyostelium discoideum), different domains}
adpeksyaegpgldggecfqpskfkihavdpdgvhrtdggdgfvvtiegpapvdpvmvdn
gdgtydvefepkeagdyvinltldgdnvngfpktvtvkpa
>d1qfha1 2.1.1.5.18 (646-749) F-actin cross-linking gelation factor (ABP-120), one repeat (ROD 4) {Slime mold (Dictyostelium discoideum), different domains}
kpapsaehsyaegeglvkvfdnapaeftifavdtkgvartdggdpfevaingpdglvvda
kvtdnndgtygvvydapvegnynvnvtlrgnpiknmpidvkcie
>d1qfha2 2.1.1.5.18 (750-857) F-actin cross-linking gelation factor (ABP-120), one repeat (ROD 4) {Slime mold (Dictyostelium discoideum), different domains}
gangedssfgsftftvaaknkkgevktyggdkfevsitgpaeeitldaidnqdgtytaay
slvgngrfstgvklngkhiegspfkqvlgnpgkknpevksftttrtan
>d1rhoa_ 2.1.1.5.19 Rho GDP-dissociation inhibitor 1, RhoGDI {Human (Homo sapiens)}
vavsadpnvpnvvvtgltlvcssapgpleldltgdlesfkkqsfvlkegveyrikisfrv
nreivsgxkyiehtyrkgvkidktdyxvgsygpraeeyefltpveeapkgxlargsysik
srftdddktdhlswewnltikkdwk
>d1cf1a1 2.1.1.5.21 (10-182) Arrestin {Bovine (Bos taurus)}
hvifkkisrdksvtiylgkrdyidhvervepvdgvvlvdpelvkgkrvyvsltcafrygq
edidvmglsfrrdlyfsqvqvfppvgasgattrlqeslikklgantypflltfpdylpcs
vmlqpapqdvgkscgvdfeikafathstdveedkipkkssvrllirkvqhapr
>d1cf1a2 2.1.1.5.21 (183-393) Arrestin {Bovine (Bos taurus)}
dmgpqpraeaswqffmsdkplrlavslskeiyyhgepipvtvavtnstektvkkikvlve
qvtnvvlyssdyyiktvaaeeaqekvppnssltktltlvpllannrerrgialdgkikhe
dtnlasstiikegidktvmgilvsyqikvkltvsgllgeltssevatevpfrlmhpqped
pdtakesfqdenfvfeefarqnlkdageyke
>d1a02n1 2.1.1.5.22 (577-678) Transcription factor NFATC, C-terminal domain {Human (Homo sapiens)}
lpmverqdtdsclvyggqqmiltgqnftseskvvftekttdgqqiwemeatvdkdksqpn
mlfveipeyrnkhirtpvkvnfyvingkrkrsqpqhftyhpv
>d1bfs__ 2.1.1.5.24 p50 subunit of NF-kappa B transcription factor, C-terminal domain {Mouse (Mus musculus)}
asnlkivrmdrtagcvtggeeiyllcdkvqkddiqirfyeeeenggvwegfgdfsptdvh
rqfaivfktpkykdvnitkpasvfvqlrrksdletsepkpflyype
>d1bfta_ 2.1.1.5.24 p50 subunit of NF-kappa B transcription factor, C-terminal domain {Mouse (Mus musculus)}
taelkicrvnrnsgsclggdeifllcdkvqkedievyftgpgweargsfsqadvhrqvai
vfrtppyadpslqapvrvsmqlrrpsdrelsepmefqylpd
>d1a9v__ 2.1.1.5.28 Major mite allergen {House-dust mite (Dermatophagoides pteronyssinus), Der p 2}
sqvdvkdcanheikkvlvpgchgsepciihrgkpfqleavfeanqntktakieikasidg
levdvpgidpnachymkcplvkgqqydikytwnvpkiapksenvvvtvkvmgddgvlaca
iathakird
>d1soxa1 2.1.1.5.29 (344-466) Sulfite oxidase, C-terminal domain {Chicken (Gallus gallus)}
elpvqsavtqprpgaavppgeltvkgyawsgggrevvrvdvsldggrtwkvarlmgdkap
pgrawawalweltvpveagteleivckavdssynvqpdsvapiwnlrgvlstawhrvrvs
vqd
>d1cvra1 2.1.1.5.30 (351-432) Gingipain R (RgpB), C-terminal domain {Porphyromonas gingivalis}
ptemqvtapanisasaqtfevacdyngaiatlsddgdmvgtaivkdgkaiiklnesiade
tnltltvvgynkvtvikdvkve
>d2hft_1 2.1.2.1.1 (1-106) Extracellular region of human tissue factor {Human (Homo sapiens)}
sgttntvaaynltwkstnfktilewepkpvnqvytvqistksgdwkskcfyttdtecdlt
deivkdvkqtylarvfsypagnvestgsageplyenspeftpylet
>d2hft_2 2.1.2.1.1 (107-211) Extracellular region of human tissue factor {Human (Homo sapiens)}
nlgqptiqsfeqvgtkvnvtvedertlvrrnntflslrdvfgkdliytlyywksssqekg
efrsgkktaktntneflidvdkgenycfsvqavipsrtvnrkstdspvecmg
>d1fna__ 2.1.2.1.3 Fibronectin, different Fn3 modules {Human (Homo sapiens)}
levvaatptslliswdapavtvryyritygetggnspvqeftvpgskstatisglkpgvd
ytitvyavtgrgdspasskpisinyrtei
>d1fnf_1 2.1.2.1.3 (1142-1235) Fibronectin, different Fn3 modules {Human (Homo sapiens)}
plspptnlhleanpdtgvltvswersttpditgyritttptngqqgnsleevvhadqssc
tfdnlspgleynvsvytvkddkesvpisdtiipa
>d1fnf_2 2.1.2.1.3 (1236-1326) Fibronectin, different Fn3 modules {Human (Homo sapiens)}
vppptdlrftnigpdtmrvtwapppsidltnflvryspvkneedvaelsispsdnavvlt
nllpgteyvvsvssvyeqhestplrgrqktg
>d1fnf_3 2.1.2.1.3 (1327-1415) Fibronectin, different Fn3 modules {Human (Homo sapiens)}
ldsptgidfsditansftvhwiapratitgyrirhhpehfsgrpredrvphsrnsitltn
ltpgteyvvsivalngreesplligqqst
>d1fnha1 2.1.2.1.3 (3-92) Fibronectin, different Fn3 modules {Human (Homo sapiens)}
paptdlkftqvtptslsaqwtppnvqltgyrvrvtpkektgpmkeinlapdsssvvvsgl
mvatkyevsvyalkdtltsrpaqgvvttle
>d1fnha2 2.1.2.1.3 (93-182) Fibronectin, different Fn3 modules {Human (Homo sapiens)}
nvspprrarvtdatettitiswrtktetitgfqvdavpangqtpiqrtikpdvrsytitg
lqpgtdykiylytlndnarsspvvidasta
>d1fnha3 2.1.2.1.3 (183-271) Fibronectin, different Fn3 modules {Human (Homo sapiens)}
idapsnlrflattpnsllvswqppraritgyiikyekpgspprevvprprpgvteatitg
lepgteytiyvialknnqksepligrkkt
>d2fnba_ 2.1.2.1.3 Fibronectin, different Fn3 modules {Human (Homo sapiens)}
mrgsevpqltdlsfvditdssiglrwtplnsstiigyritvvaagegipifedfvdssvg
yytvtglepgidydisvitlinggesapttltqqt
>d1qr4a1 2.1.2.1.5 (1-87) Tenascin, a Fn3 repeat {Human (Homo sapiens)}
dnpkdlevsdptettlslrwrrpvakfdryrltyvspsgkknemeipvdstsfilrglda
gteytislvaekgrhkskpttikgstv
>d1qr4a2 2.1.2.1.5 (88-175) Tenascin, a Fn3 repeat {Human (Homo sapiens)}
vgspkgisfsditensatvswtpprsrvdsyrvsyvpitggtpnvvtvdgsktrtklvkl
vpgvdynvniisvkgfeesepisgilkt
>d1ten__ 2.1.2.1.5 Tenascin, a Fn3 repeat {Human (Homo sapiens)}
rldapsqievkdvtdttalitwfkplaeidgieltygikdvpgdrttidltedenqysig
nlkpdteyevslisrrgdmssnpaketftt
>d1cfb_1 2.1.2.1.6 (610-709) Neuroglian, two amino proximal Fn3 repeats {Drosophila melanogaster}
ivqdvpnapkltgitcqadkaeihweqqgdnrspilhytiqfntsftpaswdaayekvpn
tdssfvvqmspwanytfrviafnkigasppsahsdscttq
>d1cfb_2 2.1.2.1.6 (710-814) Neuroglian, two amino proximal Fn3 repeats {Drosophila melanogaster}
pdvpfknpdnvvgqgtepnnlviswtpmpeiehnapnfhyyvswkrdipaaawennnifd
wrqnniviadqptfvkylikvvaindrgesnvaaeevvgysgedr
>d1qg3a1 2.1.2.1.7 (1126-1217) Integin beta-4 subunit {Human (Homo sapiens)}
dlgapqnpnakaagsrkihfnwlppsgkpmgyrvkywiqgdseseahlldskvpsveltn
lypycdyemkvcaygaqgegpysslvscrthq
>d1qg3a2 2.1.2.1.7 (1218-1320) Integin beta-4 subunit {Human (Homo sapiens)}
evpsepgrlafnvvsstvtqlswaepaetngeitayevcyglvnddnrpigpmkkvlvdn
pknrmllienlresqpyrytvkarngagwgpereaiinlatqp
>d1axib1 2.1.2.1.8 (32-130) Growth hormone receptor {Human (Homo sapiens)}
epkftkcrsperetfschwtdevhhgtknegpiqlfytrrntqewtqewkecpdyvsage
nscyfnssftsiaipycikltsnggtvdekcfsvdeivq
>d1axib2 2.1.2.1.8 (131-236) Growth hormone receptor {Human (Homo sapiens)}
pdppialnwtllnvsltgihadiqvrweaprnadiqkgwmvleyelqykevnetkwkmmd
pilttsvpvyslkvdkeyevrvrskqrnsgnygefsevlyvtlpqm
>d1eerb1 2.1.2.1.9 (8-116) Erythropoietin (EPO) receptor {Human (Homo sapiens)}
dpkfeskaallaargpeellcfterledlvcfweeaasagvgpgqysfsyqledepwklc
rlhqaptargavrfwcslptadtssfvplelrvtaasgapryhrvihin
>d1eerb2 2.1.2.1.9 (117-220) Erythropoietin (EPO) receptor {Human (Homo sapiens)}
evvlldapvglvarladesghvvlrwlpppetpmtshiryevdvsagqgagsvqrveile
grtecvlsnlrgrtrytfavrarmaepsfggfwsewsepvsllt
>d1bp3b1 2.1.2.1.10 (202-300) Prolactin receptor {Human (Homo sapiens)}
lppgkpeifkcrspnketftcwwrpgtdgglptnysltyhregetlmhecpdyitggpns
chfgkqytsmwrtyimmvnatnqmgssfsdelyvdvtyi
>d1bp3b2 2.1.2.1.10 (301-404) Prolactin receptor {Human (Homo sapiens)}
vqpdpplelavevkqpedrkpylwikwspptlidlktgwftllyeirlkpekaaeweihf
agqqtefkilslhpgqkylvqvrckpdhgywsawspatfiqips
>d1iarb1 2.1.2.1.11 (1-96) Interleukin-4 receptor alpha chain {Human (Homo sapiens)}
fkvlqeptcvsdymsistcewkmngptncstelrllyqlvfllseahtcipennggagcv
chllmddvvsadnytldlwagqqllwkgsfkpsehv
>d1iarb2 2.1.2.1.11 (97-197) Interleukin-4 receptor alpha chain {Human (Homo sapiens)}
kprapgnltvhtnvsdtllltwsnpyppdnylynhltyavniwsendpadfriynvtyle
pslriaastlksgisyrarvrawaqaynttwsewspstkwh
>d1c8pa_ 2.1.2.1.12 Common beta-chain in the GM-CSF, IL-3 and IL-5 receptors {Human (Homo sapiens)}
miqmappslnvtkdgdsyslrwetmkmryehidhtfeiqyrkdtatwkdsktetlqnahs
malpalepstrywarvrvrtsrtgyngiwsewsearswdtes
>d1cd9b1 2.1.2.1.13 (1-107) Granulocyte colony-stimulating factor (GC-SF) receptor {Mouse (Mus musculus)}
agyppaspsnlsclmhlttnslvcqwepgpethlptsfilksfrsradcqyqgdtipdcv
akkrqnncsiprknlllyqymaiwvqaenmlgssespklcldpmdvv
>d1cd9b2 2.1.2.1.13 (108-213) Granulocyte colony-stimulating factor (GC-SF) receptor {Mouse (Mus musculus)}
kleppmlqaldigpdvvshqpgclwlswkpwkpseymeqecelryqpqlkganwtlvfhl
psskdqfelcglhqapvytlqmrcirsslpgfwspwspglqlrptm
>d1jrhi_ 2.1.2.1.14 Interferon-gamma receptor alpha chain {Human (Homo sapiens)}
svptptnvtiesynmnpivyweyqimpqvpvftvevknygvknsewidacinishhycni
sdhvgdpsnslwvrvkarvgqkesayakseefavs
>d1bqua1 2.1.2.1.15 (5-99) Cytokyne receptor gp130 cytokine-binding domains {Human (Homo sapiens)}
glppekpknlscivnegkkmrcewdggrethletnftlksewathkfadckakrdtptsc
tvdystvyfvnievwveaenalgkvtsdhinfdpv
>d1bqua2 2.1.2.1.15 (100-214) Cytokyne receptor gp130 cytokine-binding domains {Human (Homo sapiens)}
ykvkpnpphnlsvinseelssilkltwtnpsiksviilkyniqyrtkdastwsqippedt
astrssftvqdlkpfteyvfrircmkedgkgywsdwseeasgityedrpskepsf
>d1nkr_1 2.1.2.1.17 (6-101) Killer cell inhibitory receptor {Human (Homo sapiens), p58-cl42 kir}
rkpsllahpgplvkseetvilqcwsdvmfehfllhregmfndtlrligehhdgvskanfs
isrmtqdlagtyrcygsvthspyqvsapsdpldivi
>d1nkr_2 2.1.2.1.17 (102-200) Killer cell inhibitory receptor {Human (Homo sapiens), p58-cl42 kir}
iglyekpslsaqpgptvlagenvtlscssrssydmyhlsregeaherrlpagpkvngtfq
adfplgpathggtyrcfgsfhdspyewskssdpllvsvt
>d1bpv__ 2.1.2.1.19 Type I titin module {Human (Homo sapiens)}
spidppgkpvplnitrhtvtlkwakpeytggfkitsyivekrdlpngrwlkanfsnilen
eftvsgltedaayefrviaknaagaisppsepsdaitcrddvea
>d1b4ra_ 2.1.3.1.1 Polycystein-1, PKD-1 {Human (Homo sapiens)}
atlvgphgplasgqlaafhiaaplpvtatrwdfgdgsaevdaagpaashryvlpgryhvt
avlalgagsallgtdvqvea
>d1bgla1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgla2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bhga1 2.1.4.1.2 (226-328) beta-Glucuronidase {Human (Homo sapiens)}
tyidditvttsveqdsglvnyqisvkgsnlfklevrlldaenkvvangtgtqgqlkvpgv
slwwpylmherpaylyslevqltaqtslgpvsdfytlpvgirt
>d1f13a2 2.1.5.1.1 (516-627) Coagulation factor XIII, two C-terminal domains {Human (Homo sapiens), blood}
snvdmdfevenavlgkdfklsitfrnnshnrytitaylsanitfytgvpkaefkketfdv
tleplsfkkeavliqageymgqlleqaslhffvtarinetrdvlakqkstvl
>d1f13a3 2.1.5.1.1 (628-728) Coagulation factor XIII, two C-terminal domains {Human (Homo sapiens), blood}
tipeiiikvrgtqvvgsdmtvtveftnplketlrnvwvhldgpgvtrpmkkmfreirpns
tvqweevcrpwvsghrkliasmssdslrhvygeldvqiqrr
>d1ncia_ 2.1.6.1.1 N-cadherin (uvomorulin), domain 1 {Mouse (Mus musculus)}
gsdwvippinlpensrgpfpqelvrirsgrdknlslrysvtgpgadqpptgifiinpisg
qlsvtkpldreliarfhlrahavdingnqvenpidivinvid
>d1edha2 2.1.6.1.2 (102-213) E-CADHERIN DOMAINS 1 AND 2 {Mouse (Mus musculus)}
ndnrpeftqevfegsvaegavpgtsvmkvsatdadddvntynaaiaytivsqdpelphkn
mftvnrdtgvisvltsgldresyptytlvvqaadlqgeglsttakavitvkd
>d2mcm__ 2.1.7.1.1 Macromycin {Streptomyces macromomyceticus}
apgvtvtpatglsngqtvtvsatgltpgtvyhvgqcavvepgvigcdattstdvtadaag
kitaqlkvhssfqavvgadgtpwgtvnckvvscsaglgsdsgegaaqaitfa
>d1noa__ 2.1.7.1.2 Neocarzinostatin {Streptomyces carzinostaticis}
aaptatvtpssglsdgtvvkvagaglqagtaydvgqcawvdtgvlacnpadfssvtadan
gsastsltvrrsfegflfdgtrwgtvdcttaacqvglsdaagngpegvaisfn
>d1acx__ 2.1.7.1.3 Actinoxanthin {Actinomyces globisporus, number 1131}
apafsvspasgasdgqsvsvsvaaagetyyiaqcapvggqdacnpatatsfttdasgaas
fsftvrksyagqtpsgtpvgsvdcatdacnlgagnsglnlghvaltfg
>d1akp__ 2.1.7.1.4 Kedarcidin (apo form) {Actimomycete strain L585-6}
asaavsvspatgladgatvtvsasgfatstsatalqcailadgrgacnvaefhdfslsgg
egttsvvvrrsftgyvmpdgpevgavdcdtapggceivvggntgeygnaaisfg
>d1mfma_ 2.1.8.1.2 Cu,Zn superoxide dismutase, SOD {Human (Homo sapiens)}
atkavavlkgdgpvqgiinfeqkesngpvkvwgsikglteglhgfhvheeedntagctsa
gphfnplsrkhggpkdeerhvgdlgnvtadkdgvadvsiedsvislsgdhsiigrtlvvh
ekaddlgkggneqstktgnagsrlacgvigiaq
>d1yaia_ 2.1.8.1.6 Cu,Zn superoxide dismutase, SOD {Photobacterium leiognathi}
qdltvkmtdlqtgkpvgtielsqnkygvvftpeladltpgmhgfhihqngscassekdgk
vvlggaagghydpehtnkhgfpwtddnhkgdlpalfvsanglatnpvlaprltlkelkgh
aimihaggdnhsdmpkalggggarvacgviq
>d1ej8a_ 2.1.8.1.9 Copper chaperone for superoxide dismutase, C-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
ssavailetfqkytidqkkdtavrglarivqvgenktlfditvngvpeagnyhasihekg
dvskgvestgkvwhkfdepiecfnesdlgknlysgktflsaplptwqligrsfvisksln
hpenepssvkdysflgviar
>d1qtsa1 2.1.9.1.1 (692-824) Alpa-adaptin AP2, N-terminal subdomain {Mouse (Mus musculus)}
gspgirlgssednfarfvcknngvlfenqllqiglksefrqnlgrmfifygnktstqfln
ftptlicaddlqtnlnlqtkpvdptvdggaqvqqvvniecisdfteapvlniqfryggtf
qnvsvklpitlnk
>d1qpxa1 2.1.10.1.1 (1-124) Pilus chaperone PapD, N-domain {Escherichia coli}
avsldrtravfdgseksmtldisndnkqlpylaqawienenqekiitgpviatppvqrld
pgaksmvrlsttpdisklpqdreslfyfnlreipprsekanvvqialctkiklfyrpaai
ktrp
>d1quna1 2.1.10.1.2 (1-121) Periplasmic chaperone FimC {Escherichia coli}
gvalgatrviypagqkqvqlavtnndenstyliqswvenadgvkdgrfivtpplfamkgk
kentlrildatnnqlpqdreslfwmnvkaipsmdkskltentlqlaiisriklyyrpakl
a
>d1mspa_ 2.1.10.2.1 Major sperm protein, alpha isoform (recombinant), ph 4.6 {Pig roundworm (Ascaris suum)}
svppgdintqpsqkivfnapyddkhtyhikitnaggrrigwaikttnmrrlsvdppcgvl
dpkekvlmavscdtfnaatedlnndritiewtntpdgaakqfrrewfqgdgmvrrknlpi
eynl
>d4kbpa1 2.1.11.1.1 (9-120) Purple acid phosphatase, N-terminal domain {Kidney bean (Phaseolus vulgaris)}
rdmpldsdvfrvppgynapqqvhitqgdlvgramiiswvtmdepgssavrywsekngrkr
iakgkmstyrffnyssgfihhttirklkyntkyyyevglrnttrrfsfitpp
>d1dqia_ 2.1.12.1.1 Superoxide reductase (SOR) {Pyrococcus furiosus}
misetirsgdwkgekhvpvieyeregelvkvkvqvgkeiphpnttehhiryielyflpeg
enfvyqvgrveftahgesvngpntsdvytepiayfvlktkkkgklyalsycnihglwene
vtle
>d1dfx_1 2.1.12.1.2 (37-125) Desulfoferrodoxin C-terminal domain {Desulfovibrio desulfuricans}
vegstdgamekhvpviekvdggylikvgsvphpmeekhwiewielladgrsytkflkpgd
apeaffaidaskvtareycnlhghwkaen
>d1e1ba1 2.1.13.1.1 (1-89) Intimin {Escherichia coli, enteropathogenic serotype O127}
tltiddgnieivgtgvkgklptvwlqygqvnlkasggngkytwrsanpaiasvdassgqv
tlkekgtttisvissdnqtatytiatpns
>d1cwva1 2.1.13.1.2 (503-596) Invasin {Yersinia pseudotuberculosis}
ltltaavigdgapangktaitveftvadfegkplagqevvittnngalpnkitektdang
varialtnttdgvtvvtaevegqrqsvdthfvkg
>d1cwva2 2.1.13.1.2 (597-692) Invasin {Yersinia pseudotuberculosis}
tiaadkstlaavptsiiadglmastitlelkdtygdpqaganvafdttlgnmgvitdhnd
gtysapltsttlgvatvtvkvdgaafsvpsvtvnft
>d1cwva3 2.1.13.1.2 (693-795) Invasin {Yersinia pseudotuberculosis}
adpipdagrssftvstpdiladgtmsstlsfvpvdknghfisgmqglsftqngvpvsisp
iteqpdsytatvvgnsvgdvtitpqvdtlilstlqkkislfpv
>d1cwva4 2.1.13.1.2 (796-886) Invasin {Yersinia pseudotuberculosis}
ptltgilvngqnfatdkgfpktifknatfqlqmdndvanntqyewsssftpnvsvndqgq
vtityqtysevavtakskkfpsysvsyrfyp
>d1ddt_1 2.2.1.1.1 (381-535) Diphtheria toxin, C-terminal domain {Corynebacterium diphtheriae}
spghktqpflhdgyavswntvedsiirtgfqgesghdikitaentplpiagvllptipgk
ldvnkskthisvngrkirmrcraidgdvtfcrpkspvyvgngvhanlhvafhrsssekih
sneissdsigvlgyqktvdhtkvnsklslffeiks
>d1exh__ 2.2.2.1.1 Exo-1,4-beta-D-glycanase (cellulase, xylanase) {Cellulomonas fimi}
assgpagcqvlwgvnqwntgftanvtvkntssapvdgwtltfsfpsgqqvtqawsstvtq
sgsavtvrnapwngsipaggtaqfgfngshtgtnaaptafslngtpctvg
>d2xbd__ 2.2.2.1.2 Xylan binding domain {Cellulomonas fimi}
tgcsvtatraeewsdrfnvtysvsgssawtvnlalngsqtiqaswnanvtgsgstrtvtp
ngsgntfgvtvmkngssttpaatcags
>d1nbca_ 2.2.2.2.1 Cellusomal scaffolding protein A, scafoldin {Clostridium thermocellum}
nlkvefynsnpsdttnsinpqfkvtntgssaidlskltlryyytvdgqkdqtfwcdhaai
igsngsyngitsnvkgtfvkmssstnnadtyleisftggtlepgahvqiqgrfakndwsn
ytqsndysfksasqfvewdqvtaylngvlvwgkep
>d1tf4a2 2.2.2.2.2 (461-605) Endo/exocellulase:cellobiose E-4, C-terminal domain {Thermomonospora fusca}
peifveaqintpgttfteikamirnqsgwparmldkgtfrywftldegvdpaditvssay
nqcatpedvhhvsgdlyyveidctgekifpggqsehrrevqfriaggpgwdpsndwsfqg
ignelapapyivlyddgvpvwgtap
>d1aoha_ 2.2.2.2.4 Cohesin domain from scaffolding protein CipA {Clostridium thermocellum}
avrikvdtvnakpgdtvripvrfsgipskgiancdfvysydpnvleiieiepgelivdpn
ptksfdtavypdrkmivflfaedsgtgayaitedgvfativakvksgapnglsvikfvev
ggfanndlveqktqffdggvnvg
>d1qba_2 2.2.2.3.1 (28-200) Bacterial chitobiase, n-terminal domain {Serratia marcescens}
dqqlvdqlsqlklnvkmldnragengvdcaalgadwascnrvlftlsndgqaidgkdwvi
yfhsprqtlrvdndqfkiahltgdlykleptakfsgfpagkaveipvvaeywqlfrndfl
prwyatsgdakpkmlantdtenldqfvapftgdqwkrtkddknilmtpasrfv
>d1amx__ 2.2.3.1.1 Collagen-binding domain of adhesin {Staphylococcus aureus}
tssvfyyktgdmlpedtthvrwflninneksyvskditikdqiqggqqldlstlninvtg
thsnyysgqsaitdfekafpgskitvdntkntidvtipqgygsynsfsinyktkitneqq
kefvnnsqawyqehgkeevngksfnhtvhn
>d1qunb1 2.2.3.2.1 (1-158) Mannose-specific adhesin FimH {Escherichia coli}
facktangtaipigggsanvyvnlapvvnvgqnlvvdlstqifchndypetitdyvtlqr
gsayggvlsnfsgtvkysgssypfpttsetprvvynsrtdkpwpvalyltpvssaggvai
kagsliavlilrqtnnynsddfqfvwniyanndvvvpt
>d1qunb2 2.2.3.2.1 (159-279) Mannose-specific adhesin FimH {Escherichia coli}
ggcdvsardvtvtlpdypgsvpipltvycaksqnlgyylsgttadagnsiftntasfspa
qgvgvqltrngtiipanntvslgavgtsavslgltanyartggqvtagnvqsiigvtfvy
q
>d1pdkb_ 2.2.3.2.2 PapK pilus subunit {Escherichia coli}
lldrpchvsgdslnkhvvfktrasrdfwyppgrsptesfvirlenchatavgkivtltfk
gteeaalpghlkvtgvnagrlgialldtdgssllkpgtshnkgqgekvtgnslelpfgay
vvatpealrtksvvpgdyeatatfeltyr
>d1ayoa_ 2.2.4.1.2 Receptor domain from alpha-2-macroglobulin {Bovine (Bos taurus)}
efpfalevqtlpqtcdgpkahtsfqislsvsyigsrpasnmaivdvkmvsgfiplkptvk
mlersnvsrtevsnnhvliyldkvtnetltltftvlqdipvrdlkpaivkvydyyetdef
avaeysapcs
>d1ycsa_ 2.2.5.1.1 p53 tumor supressor, DNA-binding domain {Human (Homo sapiens)}
vpsqktyqgsygfrlgflhsgtaksvtctyspalnkmfcqlaktcpvqlwvdstpppgtr
vramaiykqsqhmtevvrrcphhercsdsdglappqhlirvegnlrveylddrntfrhsv
vvpyeppevgsdcttihynymcnsscmggmnrrpiltiitledssgnllgrnsfevrvca
cpgrdrrteee
>d1a02n2 2.2.5.1.2 (399-576) Transcription factor NFATC, DNA-binding domain {Human (Homo sapiens)}
wplssqsgsyelrievqpkphhrahyetegsrgavkaptgghpvvqlhgymenkplglqi
figtaderilkphafyqvhritgktvtttsyekivgntkvleiplepknnmratidcagi
lklrnadielrkgetdigrkntrvrlvfrvhipessgrivslqtasnpiecsqrsahe
>d1a3qa2 2.2.5.1.4 (37-226) p50 subunit of NF-kappa B (NFKB), N-terminal domain {Mouse (Mus musculus)}
gpylviveqpkqrgfrfrygcegpshgglpgassekgrktyptvkicnyegpakievdlv
thsdpprahahslvgkqcselgicavsvgpkdmtaqfnnlgvlhvtkknmmgtmiqklqr
qrlrsrpqglteaeqreleqeakelkkvmdlsivrlrfsaflrslplkpvisqpihdsks
pgas
>d1bvoa_ 2.2.5.1.7 Dorsal homologue Gambif1 {African malaria mosquito (Anopheles gambiae)}
pyveiteqphpkalrfryecegrsagsipgvnttaeqktfpsiqvhgyrgravvvvscvt
kegpehkphphnlvgkegckkgvctveinsttmsytfnnlgiqcvkkkdveealrlrqei
rvdpfrtgfghakepgsidlnavrlcfqvflegqqrgrftepltpvvsdiiydkk
>d1xbra_ 2.2.5.1.8 T domain from Brachyury transcription factor {African clawed frog (Xenopus laevis)}
elkvsleerdlwtrfkeltnemivtkngrrmfpvlkvsmsgldpnamytvlldfvaadnh
rwkyvngewvpggkpepqapscvyihpdspnfgahwmkdpvsfskvkltnkmngggqiml
nslhkyeprihivrvggtqrmitshsfpetqfiavtayqneeitalkikhnpfakaflda
kern
>d1bg1a2 2.2.5.1.10 (322-575) STAT3b {Mouse (Mus musculus)}
vverqpcmpmhpdrplviktgvqfttkvrllvkfpelnyqlkikvcidkdsgdvaalrgs
rkfnilgtntkvmnmeesnngslsaefkhltlreqrcgnggrancdaslivteelhlitf
etevyhqglkidlethslpvvvisnicqmpnawasilwynmltnnpknvnfftkppigtw
dqvaevlswqfssttkrglsieqlttlaekllgpgvnysgcqitwakfckenmagkgfsf
wvwldniidlvkky
>d1cmoa_ 2.2.5.1.11 Acute myeloid leukemia 1 protein (AML1), RUNT domain {Human (Homo sapiens)}
vevladhpgelvrtdspnflcsvlpthwrsnktlpiafkvvalgdvpdgtlvtvmagnde
nysaelrnataamknqvarfndlrfvgrsgrgksftltitvftnppqvatyhraikitvd
gpreprr
>d1ci3m1 2.2.6.1.3 (1-169,232-249) Cytochrome f, large domain {Phormidium laminosum}
ypfwaqqnyanpreatgrivcanchlaakpaeievpqavlpdsvfkavvkipydhsvqqv
qadgskgplnvgavlmlpegftiapedripeemkeevgpsylfqpyaddkqnivlvgplp
gdeyeeivfpvlspnpatnksvafgkysihlganrgrgqiyptgeksnnXnvggfgqkdt
eivlqspn
>d1bw8a_ 2.2.7.1.1 Second domain of Mu2 adaptin subunit (ap50) of ap2 adaptor {Rat (Rattus norvegicus)}
igwrregikyrrnelfldvlesvnllmspqgqvlsahvsgrvvmksylsgmpeckfgmnd
kiviekqgkgtadetsksgkqsiaiddctfhqcvrlskfdsersisfippdgefelmryr
ttkdiilpfrviplvrevgrtklevkvviksnfkpsllaqkievriptplntsgvqvicm
kgkakykasenaivwkikrmagmkesqisaeiellptndkkkwarppismnfevpfapsg
lkvrylkvfepklnysdhdvikwvryigrsgiyetrc
>d1qhoa2 2.3.1.1.3 (577-686) Cyclodextrin glycosyltransferase, C-terminal domain {Bacillus stearothermophilus maltogenic alpha-amylase}
lsgtqtsvvftvksapptnlgdkiyltgnipelgnwstdtsgavnnaqgpllapnypdwf
yvfsvpagktiqfkffikradgtiqwengsnhvattptgatgnitvtwqn
>d1pama2 2.3.1.1.4 (583-686) Cyclodextrin glycosyltransferase, C-terminal domain {Alkalophilic bacillus, sp. 1011}
tgdqvtvrfvinnattalgqnvfltgnvselgnwdpnnaigpmynqvvyqyptwyydvsv
pagqtiefkflkkqgstvtwegganrtfttptsgtatvnvnwqp
>d1acz__ 2.3.1.1.6 Glucoamilase, granular starch-binding domain {Aspergillus niger}
cttptavavtfdltatttygeniylvgsisqlgdwetsdgialsadkytssdplwyvtvt
lpagesfeykfiriesddsvewesdpnreytvpqacgtstatvtdtwr
>d1cqya_ 2.3.1.1.7 beta-amylase {Bacillus cereus}
tpvmqtivvknvpttigdtvyitgnraelgswdtkqypiqlyydshsndwrgnvvlpaer
niefkafikskdgtvkswqtiqqswnpvplkttshtssw
>d1vcbc_ 2.3.2.1.1 VHL {Human (Homo sapiens)}
lrsvnsrepsqvifcnrsprvvlpvwlnfdgepqpyptlppgtgrrihsyrghlwlfrda
gthdgllvnqtelfvpslnvdgqpifanitlpvytlkerclqvvrslvkpenyrrldivr
slyedledhpnvqkdlerltqe
>d1etb1_ 2.3.3.1.1 Transthyretin (synonym: prealbumin) {Human (Homo sapiens)}
kcplmvkvldavrgspainvavhvfrkaaddtwepfasgktsesgelhgltteeefvegi
ykveidtksywkalgispfhehaevvftandsgprrytiatllspysysttavvtnpk
>d1dmha_ 2.3.4.1.1 Catechol 1,2-dioxygenase {Acinetobacter calcoaceticus}
vkifntqdvqdflrvasgleqeggnprvkqiihrvlsdlykaiedlnitsdeywagvayl
nqlganqeagllspglgfdhyldmrmdaedaalgienatprtiegplyvagapesvgyar
mddgsdpnghtlilhgtifdadgkplpnakveiwhantkgfyshfdptgeqqafnmrrsi
itdengqyrvrtilpagygcppegptqqllnqlgrhgnrpahihyfvsadghrklttqin
vagdpytyddfayatreglvvdavehtdpeaikandvegpfaemvfdlkltrlvdgvdnq
vvdrprlav
>d3pcca_ 2.3.4.1.2 Protocatechuate-3,4-dioxygenase, alpha chain {Pseudomonas aeruginosa}
piellpetpsqtagpyvhiglaleaagnptrdqeiwnrlakpdapgehilllgqvydgng
hlvrdsflevwqadangeyqdaynlenafnsfgrtattfdagewtlhtvkpgvvnnaagv
pmaphinislfarginihlhtrlyfddeaqanakcpvlnlieqpqrretliakrcevdgk
tayrfdiriqgegetvffdf
>d3pccm_ 2.3.4.1.3 Protocatechuate-3,4-dioxygenase, beta chain {Pseudomonas aeruginosa}
paqdnsrfvirdrnwhpkaltpdyktsiarsprqalvsipqsisettgpnfshlgfgahd
hdlllnfnngglpigeriivagrvvdqygkpvpntlvemwqanaggryrhkndrylapld
pnfggvgrcltdsdgyysfrtikpgpypwrngpndwrpahihfgisgpsiatklitqlyf
egdplipmcpivksianpeavqqliakldmnnanpmdclayrfdivlrgqrkthfe
>d1hoe__ 2.4.1.1.1 alpha-Amylase inhibitor tendamistat {Streptomyces tendae}
dttvsepapscvtlyqswrysqadngcaetvtvkvvyeddteglcyavapgqittvgdgy
igshgharylarcl
>d1aac__ 2.5.1.1.1 Amicyanin {Paracoccus denitrificans}
dkatipsespfaaaevadgaivvdiakmkyetpelhvkvgdtvtwinreamphnvhfvag
vlgeaalkgpmmkkeqaysltfteagtydyhctphpfmrgkvvve
>d1plc__ 2.5.1.1.2 Plastocyanin {Poplar (Populus nigra), variant italica}
idvllgaddgslafvpsefsispgekivfknnagfphnivfdedsipsgvdaskismsee
dllnakgetfevalsnkgeysfycsphqgagmvgkvtvn
>d1kdj__ 2.5.1.1.10 Plastocyanin {Fern (Adiantum capillus-veneris)}
akvevgdevgnfkfypdsitvsageaveftlvgetghnivfdipagapgtvaselkaasm
dendllsedepsfkakvstpgtytfyctphksanmkgtltvk
>d1nin__ 2.5.1.1.11 Plastocyanin {Anabaena variailis}
etytvklgsdkgllvfepakltikpgdtveflnnkvpphnvvfdaalnpaksadlaksls
hkqllmspgqststtfpadapageytfycephrgagmvgkitvag
>d1bxua_ 2.5.1.1.14 Plastocyanin {Cyanobacterium (Synechocystis), pcc 7942}
qtvaikmgadngmlafepstieiqagdtvqwvnnklaphnvvvegqpelshkdlafspge
tfeatfsepgtytyycephrgagmvgkivvq
>d2b3ia_ 2.5.1.1.15 Plastocyanin {Photosynthetic prokaryote (Prochlorothrix hollandica)}
asvqikmgtdkyaplyepkalsisagdtvefvmnkvgphnvifdkvpagesapalsntkl
aiapgsfysvtlgtpgtysfyctphrgagmvgtitve
>d1bqk__ 2.5.1.1.18 Pseudoazurin {Achromobacter cycloclastes}
adfevhmlnkgkdgamvfepaslkvapgdtvtfiptdkghnvetikgmipdgaeafkski
nenykvtftapgvygvkctphygmgmvgvvqvgdapanleavkgaknpkkaqerldaala
algn
>d2cbp__ 2.5.1.1.20 Cucumber basic protein {Cucumber (Cucumis sativus)}
avyvvggsggwtfnteswpkgkrfragdillfnynpsmhnvvvvnqggfstcntpagakv
ytsgrdqiklpkgqsyficnfpghcqsgmkiavnal
>d1nwpa_ 2.5.1.1.25 Azurin {Pseudomonas putida}
aeckvtvdstdqmsfntkdiaidkscktftvelthsgslpknvmghnlviskeadmqpia
tdglsagidkqylkdgdarviahtkvigagekdsvtfdvsklaagekygffcsfpghism
mkgtvtlk
>d1rcy__ 2.5.1.1.27 Rusticyanin {Thiobacillus ferrooxidans}
ttwkeatlpqvkamlekddgkvsgdtvtysgktvhvvaaavlpgfpfpsfevhdkknptl
eipagatvdvtfintnkgfghsfditkkgppyavmpvidpivagtgfspvpkdgkfgytd
ftwhptagtyyyvcqipghaatgmfgkivvk
>d1jer__ 2.5.1.1.28 Stellacyanin {Cucumber (Cucumis sativus)}
mqstvhivgdntgwsvpsspnfysqwaagktfrvgdslqfnfpanahnvhemetkqsfda
cnfvnsdndvertspvierldelgmhyfvctvgthcsngqklsinvvaan
>d1cyx__ 2.5.1.2.1 Quinol oxidase (CYOA) {Escherichia coli}
kpitievvsmdwkwffiypeqgiatvneiafpantpvyfkvtsnsvmhsffiprlgsqiy
amagmqtrlhlianepgtydgicaeicgpghsgmkfkaiatpdraafdqwvakakqspnt
msdmaafeklaapseynqveyfsnvkpdlfadvinkfm
>d2occb1 2.5.1.2.2 (91-227) Cytochrome c oxidase {Bovine (Bos taurus)}
nnpsltvktmghqwywsyeytdyedlsfdsymiptselkpgelrllevdnrvvlpmemti
rmlvssedvlhswavpslglktdaipgrlnqttlmssrpglyygqcseicgsnhsfmpiv
lelvplkyfekwsasml
>d2cuaa_ 2.5.1.2.4 Cytochrome c oxidase {Thermus thermophilus, ba3 type}
agklervdpttvrqegpwadpaqavvqtgpnqytvyvlafafgyqpnpievpqgaeivfk
itspdvihgfhvegtninvevlpgevstvrytfkrpgeyriicnqycglghqnmfgtivv
ke
>d1nif_1 2.5.1.3.1 (8-166) Nitrite reductase, NIR {Achromobacter cycloclastes}
distlprvkvdlvkppfvhahdqvaktgprvveftmtieekklvidregteihamtfngs
vpgplmvvhendyvelrlinpdtntllhnidfhaatgalgggaltqvnpgeettlrfkat
kpgvfvyhcapegmvpwhvtsgmngaimvlprdglkdek
>d1nif_2 2.5.1.3.1 (167-340) Nitrite reductase, NIR {Achromobacter cycloclastes}
gqpltydkiyyvgeqdfyvpkdeagnykkyetpgeayedavkamrtltpthivfngavga
ltgdhaltaavgervlvvhsqanrdtrphligghgdyvwatgkfrnppdldqetwlipgg
tagaafytfrqpgvyayvnhnlieafelgaaghfkvtgewnddlmtsvvkpasm
>d1aoza1 2.5.1.3.4 (1-129) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
sqirhykweveymfwapncnenivmgingqfpgptiranagdsvvveltnklhtegvvih
whgilqrgtpwadgtasisqcainpgetffynftvdnpgtffyhghlgmqrsaglygsli
vdppqgkke
>d1aoza2 2.5.1.3.4 (130-338) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
pfhydgeinlllsdwwhqsihkqevglsskpirwigepqtillngrgqfdcsiaakydsn
lepcklkgsescapyifhvspkktyririasttalaalnfaignhqllvveadgnyvqpf
ytsdidiysgesysvlittdqnpsenywvsvgtrarhpntppgltllnylpnsvsklpts
pppqtpawddfdrsknftyritaamgspk
>d1aoza3 2.5.1.3.4 (339-552) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
ppvkfnrrifllntqnvingyvkwaindvslalpptpylgamkynllhafdqnpppevfp
edydidtpptnektrigngvyqfkigevvdvilqnanmmkenlsethpwhlhghdfwvlg
ygdgkfsaeeesslnlknpplrntvvifpygwtairfvadnpgvwafhchiephlhmgmg
vvfaegvekvgriptkalacggtakslinnpknp
>d1a65a1 2.5.1.3.5 (1-131) Laccase {Inky cap fungus (Coprinus cinereus)}
qivnsvdtmtltnanvspdgftragilvngvhgplirggkndnfelnvvndldnptmlrp
tsihwhglfqrgtnwadgadgvnqcpispghaflykftpaghagtfwyhshfgtqycdgl
rgpmviyddnd
>d1a65a2 2.5.1.3.5 (132-303) Laccase {Inky cap fungus (Coprinus cinereus)}
phaalydeddentiitladwyhipapsiqgaaqpdatlingkgryvggpaaelsivnveq
gkkyrmrlislscdpnwqfsidgheltiievdgeltephtvdrlqiftgqrysfvldanq
pvdnywiraqpnkgrnglagtfangvnsailryagaanadpttsanpnpaql
>d1a65a3 2.5.1.3.5 (304-504) Laccase {Inky cap fungus (Coprinus cinereus)}
neadlhalidpaapgiptpgaadvnlrfqlgfsggrftingtayespsvptllqimsgaq
sandllpagsvyelprnqvvelvvpagvlggphpfhlhghafsvvrsagsstynfvnpvk
rdvvslgvtgdevtirfvtdnpgpwffhchiefhlmnglaivfaedmantvdannppvew
aqlceiyddlppeatsiqtvv
>d1kcw_1 2.5.1.3.6 (1-192) Ceruloplasmin {Human (Homo sapiens)}
kekhyyigiiettwdyasdhgekklisvdtehsniylqngpdrigrlykkalylqytdet
frttiekpvwlgflgpiikaetgdkvyvhlknlasrpytfhshgityykehegaiypdnt
tdfqraddkvypgeqytymllateeqspgegdgncvtriyhshidapkdiasgligplii
ckkdsldkekek
>d1kcw_2 2.5.1.3.6 (193-338) Ceruloplasmin {Human (Homo sapiens)}
hidrefvvmfsvvdenfswyledniktycsepekvdkdnedfqesnrmysvngytfgslp
glsmcaedrvkwylfgmgnevdvhaaffhgqaltnknyridtinlfpatlfdaymvaqnp
gewmlscqnlnhlkaglqaffqvqec
>d1qasa2 2.6.1.1.1 (626-756) PI-specific phospholipase C isozyme D1 (PLC-D1), C-terminal domain {Rat (Rattus norvegicus)}
wrperlrvriisgqqlpkvnknknsivdpkviveihgvgrdtgsrqtavitnngfnprwd
mefefevtvpdlalvrfmvedydssskndfigqstipwnslkqgyrhvhllskngdqhps
atlfvkisiqd
>d1rlw__ 2.6.1.1.2 Domain from cytosolic phospholipase A2 {Human (Homo sapiens)}
sshkftvvvlratkvtkgafgdmldtpdpyvelfisttpdsrkrtrhfnndinpvwnetf
efildpnqenvleitlmdanyvmdetlgtatftvssmkvgekkevpfifnqvtemvlems
levass
>d1d5ra1 2.6.1.1.3 (188-351) Pten tumor suppressor (Phoshphoinositide phosphatase), N-terminal domain {Human (Homo sapiens)}
yrpvallfhkmmfetipmfsggtcnpqfvvcqlkvkiyssnsgptrredkfmyfefpqpl
pvcgdikveffhkqnkmlkkdkmfhfwvntffipgpeevdndkeylvltltkndldkank
dkanryfspnfkvklyftktv
>e1bdy.1a 2.6.1.1.5 Domain from protein kinase C delta {Rat (Rattus norvegicus)}
mapflrisfnsyelgslqaeddasqpfcavkmkealttdrgktlvqkkptmypewkstfd
ahiyegrviqivlmraaedpmsevtvgvsvlaerckknngkaefwldlqpqakvlmcvqy
fle
>d1dqva2 2.6.1.2.1 (425-569) Synaptogamin I {Rat (Rattus norvegicus)}
sekadlgelnfslcylptaglltvtiikasnlkamdltgfsdpyvkaslisegrrlkkrk
tsikkntlnptynealvfdvapesvenvglsiavvdydcighnevigvcrvgpeaadphg
rehwaemlanprkpvehwhqlveek
>d1rsy__ 2.6.1.2.1 Synaptogamin I {Rat (Rattus norvegicus)}
gggildsmvekeepkeeeklgklqysldydfqnnqllvgiiqaaelpaldmggtsdpyvk
vfllpdkkkkfetkvhrktlnpvfneqftfkvpyselggktlvmavydfdrfskhdiige
fkvpmntvdfghvteewrdlqsa
>d1dsya_ 2.6.1.2.2 C2 domain from protein kinase c (alpha) {Rat (Rattus norvegicus)}
tekrgriylkaevtdeklhvtvrdaknlipmdpnglsdpyvklklipdpkneskqktkti
rstlnpqwnesftfklkpsdkdrrlsveiwdwdrttrndfmgslsfgvselmkmpasgwy
kllnqeegeyynvpipe
>d3rpba_ 2.6.1.2.4 C2b-domain of rabphilin {Rat (Rattus norvegicus)}
rgkilvslmystqqgglivgiircvhlaamdangysdpfvklwlkpdmgkkakhktqikk
ktlnpefneeffydikhsdlakksldisvwdydigksndyiggcqlgisakgerlkhwye
clknkdkkierwhqlqnenh
>d1qpxa2 2.6.2.1.1 (125-215) PapD {Escherichia coli}
nevwqdqlilnkvsggyrienptpyyvtviglggsekqaeegefetvmlsprseqtvksa
nyntpylsyindyggrpvlsficngsrcsvk
>d1quna2 2.6.2.1.2 (122-205) FimC {Escherichia coli}
lppdqaaeklrfrrsansltlinptpyyltvtelnagtrvlenalvppmgesavklpsda
gsnityrtindygaltpkmtgvme
>d1who__ 2.6.3.1.1 Pollen allergen PHL P 2 {Timothy grass (Phleum pratense)}
vpkvtftvekgsnekhlavlvkyegdtmaevelrehgsdewvamtkgeggvwtfdseepl
qgpfnfrfltekgmknvfddvvpekytigatyap
>d1dcea2 2.6.4.1.1 (241-350) Rab geranylgeranyltransferase alpha-subunit, insert domain {Rat (Rattus norvegicus)}
phdvlccvhvsreeaclsvcfsrpltvgsrmgtlllmvdeaplsvewrtpdgrnrpshvw
lcdlpaaslndqlpqhtfrviwtgsdsqkecvllkdrpecwcrdsatdeq
>d1czya1 2.7.1.1.1 (350-501) TNF receptor associated factor 2 (TRAF2) {Human (Homo sapiens)}
ydgvfiwkisdfprkrqeavagripaifspafytsrygykmclriylngdgtgrgthlsl
ffvvmkgpndallrwpfnqkvtlmlldqnnrehvidafrpdvtsssfqrpvndmniasgc
plfcpvskmeaknsyvrddaifikaivdltgl
>d2bn2a_ 2.8.1.1.1 Neurophysin II {Bovine (Bos taurus)}
amsdlelrqclpcgpggkgrcfgpsiccgdelgcfvgtaealrcqeenylpspcqsgqkp
cgsggrcaaagiccndescvtepec
>d2bpa1_ 2.9.1.1.1 Bacteriophage capsid proteins {Bacteriophage phiX174}
sniqtgaermphdlshlgflagqigrlitisttpviagdsfemdavgalrlsplrrglai
dstvdiftfyvphrhvygeqwikfmkdgvnatplptvnttgyidhaaflgtinpdtnkip
khlfqgylniynnyfkapwmpdrteanpnelnqddarygfrcchlkniwtaplppetels
rqmttsttsidimglqaayanlhtdqerdyfmqryrdvissfggktsydadnrpllvmrs
nlwasgydvdgtdqtslgqfsgrvqqtykhsvprffvpehgtmftlalvrfpptatkeiq
ylnakgaltytdiagdpvlygnlppreismkdvfrsgdsskkfkiaegqwyryapsyvsp
ayhllegfpfiqeppsgdlqervlirhhdydqcfqsvqllqwnsqvkfnvtvyrnlpttr
dsimts
>d2bpa2_ 2.9.1.1.1 Bacteriophage capsid proteins {Bacteriophage phiX174}
mfqtfisrhnsnffsdklvltsvtpassapvlqtpkatsstlyfdsltvnagnggflhci
qmdtsvnaanqvvsvgadiafdadpkffaclvrfesssvpttlptaydvyplngrhdggy
ytvkdcvtidvlprtpgnnvyvgfmvwsnftatkcrglvslnqvikeiiclqplk
>d1stma_ 2.9.1.2.1 SPMV coat protein {Satellite panicum mosaic virus}
aaatslvydtcyvtlterattsfqrqsfptlkgmgdrafqvvaftiqgvsaaplmynarl
ynpgdtdsvhatgvqlmgtvprtvrltprvgqnnwffgnteeaetilaidglvstkgana
psntvivtgcfrlapselqss
>d1a34a_ 2.9.1.2.2 STMV coat protein {Satellite tobacco mosaic virus}
tgdnsnvvtmiragsypkvnptptwvraipfevsvqsgiafkvpvgslfsanfrtdsfts
vtvmsvrawtqltppvneysfvrlkplfktgdsteefegrasnintrasvgyriptnlrq
ntvaadnvcevrsncrqvalvisccfn
>d2stv__ 2.9.1.2.3 STNV coat protein {Satellite tobacco necrosis virus}
tmravkrminthlehkrfalinsgntnatagtvqnlsngiiqgddinqrsgdqvrivshk
lhvrgtaitvsqtfrfiwfrdnmnrgttptvlevlntanfmsqynpitlqqkrftilkdv
tlncsltgesikdriinlpgqlvnyngatavaasngpgaifmlqigdslvglwdssyeav
ytda
>d1smva_ 2.9.1.2.4 SMV coat potein {Sesbania mosaic virus}
gaitvlhceltaeigvtdsivvsselvmpytvgtwlrgvadnwskyswlsvrytyipscp
sstagsihmgfqydmadtvpvsvnklsnlrgyvsgqvwsgsaglcfinnsrcsdtstais
ttldvselgkkwypyktsadyatavgvdvniatdlvparlvialldgssstavaagriyd
tytiqmieptasalnl
>d1bmv1_ 2.9.1.2.5 BPMV coat protein {Bean pod mottle virus}
sisqqtvwnqmatvrtplnfdsskqsfcqfsvdllgggisvdktgdwitlvqnspisnll
rvaawkkgclmvkvvmsgnaavkrsdwaslvqvfltnsnstehfdacrwtksephsweli
fpievcgpnngfemwssewanqtswhlsflvdnpkqsttfdvllgisqnfeiagntlmpa
fsvpq
>d1bmv2_ 2.9.1.2.5 BPMV coat protein {Bean pod mottle virus}
metnlfklslddvetpkgsmldlkisqskialpkntvggtilrsdllanfltegnfrasv
dlqrthrikgmikmvatvgipentgialacamnssirgrassdiyticsqdcelwnpact
kamtmsfnpnpcsdawsleflkrtgfhcdiicvtgwtatpmqdvqvtidwfissqecvpr
tycvlnpqnpfvlnrwmgkltfpqgtsrsvkrmplsigggagaksailmnmpnavlsmwr
yfvgdlvfevskmtspyikctvsffiafgnladdtinfeafphklvqfgeiqekvvlkfs
qeefltawstqvrpattlladgcpylyamvhdssvstipgdfvigvkltiienmcaygln
pgisgsrllgtipq
>d1a6ca1 2.9.1.2.6 (1-176) TRSV capsid protein {Tobacco ringspot virus}
avtvvpdptccgtlsfkvpkdakkgkhlgtfdirqaimdygglhsqewcakgivnptftv
rmhaprnafaglsiactfddykridlpalgnecppsemfelptkvfmlkdadvhewqfny
geltghglcnwanvatqptlyffvastnqvtmaadwqcivtmhvdmgpvidrfeln
>d1a6ca2 2.9.1.2.6 (177-348) TRSV capsid protein {Tobacco ringspot virus}
ptmtwpiqlgdtfaidryyeakeikldgstsmlsisynfggpvkhskkhaisysravmsr
nlgwsgtisgsvksvsslfctasfvifpweceapptlrqvlwgphqimhgdgqfeiaikt
rlhsaatteegfgrlgilplsgpiapdahvgsyefivhintwrpdsqvhppm
>d1a6ca3 2.9.1.2.6 (349-513) TRSV capsid protein {Tobacco ringspot virus}
fssselynwftltnlkpdantgvvnfdipgyihdfaskdatvtlasnplswlvaatgwhy
gevdlciswsrskqaqaqegsvsittnyrdwgaywqgqariydlrrteaeipiflgsyag
atpsgalgkqnyvrisivnakdivalrvclrpksikfwgrsatlf
>d2tbva_ 2.9.1.2.8 TBSV coat protein {Tomato bushy stunt virus}
ggvtvtshreyltqvnnssgfvvnggivgnslqlnpsngtlfswlpalasnfdqysfnsv
vldyvplcgttevgrvalyfdkdsqdpepadrvelanfgvlketapwaeamlriptdkvk
rycndsatvdqklidlgqlgiatyggagadavgelflarsvtlyfpqptntllsskrldl
tgsladatgpgylvltrtptvlthtfratgtfnlsgglrcltsltlgatgavvindilai
dnvgtasdyflnctvsslpatvtftvsgvaagillvgraranvvnll
>d1cwpa_ 2.9.1.2.9 Cowpea chlorotic mottle virus {Host: cowpea (Vigna unguiculta), (L.)}
kaikawtgysvskwtascaaaeakvtsaitislpnelssernkqlkvgrvllwlgllpsv
sgtvkscvtetqttaaasfqvalavadnskdvvaamypeafkgitleqlaadltiylyss
aaltegdvivhlevehvrptfddsftpvy
>d1auya_ 2.9.1.2.11 TYMV coat protein {Turnip yellow mosaic virus}
spltikqpfqsevlfagtkdaeasltianidsvstlttfyrhasleslwvtihptlqapt
fpttvgvcwvpaqspvtpaqitktyggqifciggaiqtlsplivkcplemmqprvkdsiq
yldspkllisitaqptappastciitvsgtlsmhsplitdtst
>d1qjza_ 2.9.1.2.12 PHMV coat protein {PHMV (Physalis mottle virus)}
kqasipapgsilsqpnteqspaivlpfqfeattfgtaetaaqvslqtadpitkltapyrh
aqiveckailtptdlavsnpltvylawvpanspatptqilrvyggqsfvlggaisaakti
evplnldsvnrmlkdsvtytdtpkllaysraptnpskiptasiqisgrirlskpmlian
>d1f15a_ 2.9.1.2.13 CMV coat protein {Cucumber mosaic virus strain fny}
ercrpgytftsitlkppkidrgsyygkrlllpdsvteydkklvsrlqirvnplpkfdstv
wvtvrkvpassdlsvaaisamfadgaspvlvyqyaasgvqannkllydlsamradigdmr
kyavlvyskddaletdelvlhvdiehqriptsgvlpv
>d2bbva_ 2.9.1.3.1 Black beetle virus (BBV, Nodamura virus) capsid protein {Nodamura virus}
ltrlsqpglaflkcafappdfntdpgkgipdrfegkvvtrkdvlnqsinftanrdtfili
aptpgvaywvadvpagtfpistttfnavnfpgfnsmfgnaaasrsdqvssfryasmnvgi
yptsnlmqfagsitvwkcpvklsnvqfpvattpatsalvhtlvgldgvlavgpdnfsesf
ikgvfsqsvcnepdfefsdilegiqtlppanvtvatsgqpfnlaagaeavsgivgwgnmd
tivirvsaptgavnsailktwacleyrpnpnamlyqfghdsppcdevalqeyrtvarslp
vaviaaqn
>d1dnv__ 2.9.1.3.2 Galleria mellonella densovirus capsid protein {Wax moth (Galleria mellonella), densovirus}
vyiiprpfsnfgkklstytkshkfmifglannvigptgtgttavnrllttclaeipwqkl
plymnqsefdllppgsrvvecnvkvifrtnriafetsstvtkqatlnqisnvqtaiglnk
lgwginraftafqsdqpmiptattapkyepvtgdtgyrgmiadyygadstndtafgnagn
yphhqvssftflqnyycmyqqtnqgtggwpclaehlqqfdsktvnnqclidvtykpkmgl
iksplnykiigqptvkgtisvgdnlvnmrgavvtnppeatqnvaesthnltrnfpadlfn
iysdieksqvlhkgpwghenpqiqpsvhigiqavpalttgallinssplnswtdsmgyid
vmssctvmeaqpthfpfsteantnpgntiyrinltpnsltsafnglygngatlgn
>d1b35a_ 2.9.1.3.3 Cricket paralysis virus (CRPV) {Host: australian black field cricket (Teleogryllus commodus)}
vmgedqqiprneaqhgvhpisidthrisnnwspqamcigekvvsirqlikrfgifgdant
lqadgssfvvapftvtsptktltstrnytqfdyyyylyafwrgsmrikmvaetqdgtgtp
rkktnftwfvrmfnslqdsfnslistsssavtttvlpsgtinmgpstqvidptvegliev
evpyynishitpavtiddgtpsmedylkghsppclltfsprdsisatnhiitasfmralg
ddfsfmyllgvpplvnvara
>d1b35b_ 2.9.1.3.3 Cricket paralysis virus (CRPV) {Host: australian black field cricket (Teleogryllus commodus)}
enshienedkrltseqkeivhfvsegvtpsttalpdivnlstnyldkntredrihsikdf
lsrpiiiatnlwsvsdpvekqlytanfpevlisnamyqdklkgfvglratlvvkvqvnsq
pfqqgrlmlqyipyaqympnrvtlinetlqgrsgcprtdlelsvgtevemripyvsphly
ynlitgqgsfgsiyvvvysqlhdqvsgtgsieytvwahledvdvqyptganiftgneayi
kgtsrydaaqkahaa
>d1b35c_ 2.9.1.3.3 Cricket paralysis virus (CRPV) {Host: australian black field cricket (Teleogryllus commodus)}
skptvqgkigecklrgqgrmanfdgmdmshkmalsstneietneglagtsldvmdlsrvl
sipnywdrftwktsdvintvlwdnyvspfkvkpysatitdrfrcthmgkvanaftywrgs
mvytfkfvktqyhsgrlrisfipyyynttistgtpdvsrtqkivvdlrtstavsftvpyi
gsrpwlycirpesswlskdntdgalmyncvsgivrvevlnqlvaaqnvfseidvicevng
gpdlefagptcpryvpyagdftladtrkieaertqeysnned
>d1vpsa_ 2.9.1.4.1 Murine polyomavirus coat protein vp1 {Murine polyoma virus, strain small-plaque 16}
ggmevldlvtgpdsvteieaflnprmgqpptpeslteggqyygwsrginlatsdtedspg
nntlptwsmaklqlpmlnedltcdtlqmweavsvktevvgsgslldvhgfnkptdtvntk
gistpvegsqyhvfavggepldlqglvtdartkykeegvvtiktitkkdmvnkdqvlnpi
skakldkdgmypveiwhpdpaknentryfgnytggtttppvlqftntlttvlldengvgp
lckgeglylscvdimgwrvtrnydvhhwrglpryfkitlrkrwvk
>d1qqp1_ 2.9.1.4.2 Foot-and-mouth desease virus {Foot-and-mouth disease virus (strain bfs, 1860)}
ttsagesadpvtttvenyggetqiqrrqhtdvsfimdrfvkvtpqnqinildlmqvpsht
lvgallrastyyfsdleiavkhegdltwvpngapekaldnttnptayhkapltrlalpyt
aphrvlatvyngecrysrnavpnlrgdlqvlaqkvartlptsfnygaikatrvtellyrm
kraetycprpllaihptearhkqkivapvk
>d1qqp2_ 2.9.1.4.2 Foot-and-mouth desease virus {Foot-and-mouth disease virus (strain bfs, 1860)}
dkkteettlledrilttrnghttsttqssvgvtygyataedfvsgpntsgletrvvqaer
ffkthlfdwvtsdsfgrchllelptdhkgvygsltdsyaymrngwdvevtavgnqfnggc
llvamvpelcsiqkrelyqltlfphqfinprtnmtahitvpfvgvnrydqykvhkpwtlv
vmvvapltvntegapqikvyaniaptnvhvagefpske
>d1qqp3_ 2.9.1.4.2 Foot-and-mouth desease virus {Foot-and-mouth disease virus (strain bfs, 1860)}
gifpvacsdgygglvttdpktadpvygkvfnpprnqlpgrftnlldvaeacptflrfegg
vpyvttktdsdrvlaqfdmslaakhmsntflaglaqyytqysgtinlhfmftgptdakar
ymvayappgmeppktpeaaahcihaewdtglnskftfsipylsaadytytasdvaettnv
qgwvclfqithgkadgdalvvlasagkdfelrlpvdarae
>d2cas__ 2.9.1.4.3 Parvovirus capsid {Host: canine (Canis familiaris)}
gvgistgtfnnqtefkflengwveitanssrlvhlnmpesenyrrvvvnnmdktavngnm
alddihaqivtpwslvdanawgvwfnpgdwqlivntmselhlvsfeqeifnvvlktvses
atqpptkvynndltaslmvaldsnntmpftpaamrsetlgfypwkptiptpwryyfqwdr
tlipshtgtsgtptniyhgtdpddvqfytiensvpvhllrtgdefatgtfffdckpcrlt
htwqtnralglppflnslpqsegatnfgdigvqqdkrrgvtqmgntnyiteatimrpaev
gysapyysfeastqgpfktpiaagrggaqtdenqaadgnpryafgrqhgqkttttgetpe
rftyiahqdtgrypegdwiqninfnlpvtndnvllptdpiggktginytnifntygplta
lnnvppvypngqiwdkefdtdlkprlhvnapfvcqnncpgqlfvkvapnltneydpdasa
nmsrivtysdfwwkgklvfkaklrashtwnpiqqmsinvdnqfnyvpsniggmkivyeks
qlaprkly
>d1aym1_ 2.9.1.4.9 Rhinovirus coat protein {Human (Homo sapiens), rhinovirus 16}
npveryvdevlnevlvvpninqshpttsnaapvldaaetghtnkiqpedtietryvqssq
tldemsvesflgrsgcihesvldivdnyndqsftkwninlqemaqirrkfemftyarfds
eitmvpsvaakdghighivmqymyvppgapipttrddyawqsgtnasvfwqhgqpfprfs
lpflsiasayymfydgydgdtyksrygtvvtndmgtlcsrivtseqlhkvkvvtriyhka
khtkawcprppravqyshthttnyklssevhndvairprtnlttv
>d1aym2_ 2.9.1.4.9 Rhinovirus coat protein {Human (Homo sapiens), rhinovirus 16}
sdriiqitrgdstitsqdvanavvgygvwphyltpqdataidkptqpdtssnrfytldsk
mwnstskgwwwklpdalkdmgifgenmfyhflgrsgytvhvqcnaskfhqgtllvvmipe
hqlatvnkgnvnagykythpgeagrevgtqvenekqpsddnwlnfdgtllgnllifphqf
inlrsnnsatlivpyvnavpmdsmvrhnnwslviipvcqlqsnnisnivpitvsispmca
efsgaraktvvq
>d1aym3_ 2.9.1.4.9 Rhinovirus coat protein {Human (Homo sapiens), rhinovirus 16}
glpvyvtpgsgqfmttddmqspcalpwyhptkeifipgevknliemcqvdtlipinstqs
nignvsmytvtlspqtklaeeifaikvdiashplattligeiasyfthwtgslrfsfmfc
gtanttlkvllaytppgigkprsrkeamlgthvvwdvglqstvslvvpwisasqyrfttp
dtyssagyitcwyqtnfvvppntpntaemlcfvsgckdfclrmardtdlhkqtgpitq
>d2mev1_ 2.9.1.4.13 Mengo virus {Host: monkey brain; middle size plaque variant}
gvenaekgvtentdatadfvaqpvylpenqtkvaffydrsspigafavksgslesgfapf
snkacpnsviltpgpqfdpaydqlrpqrlteiwgngneetsevfplktkqdysfclfspf
vyykcdlevtlsphtsgahgllvrwcptgtptkpttqvlhevsslsegrtpqvysagpgt
snqisfvvpynsplsvlpavwynghkrfdntgdlgiapnsdfgtlffagtkpdikftvyl
ryknmrvfcprptvffpwptsgdkidmt
>d1dzla_ 2.9.1.4.20 L1 protein {Human papillomavirus type 16}
kvvstdeyvartniyyhagtsrllavghpyfpikkpnnnkilvpkvsglqyrvfrihlpd
pnkfgfpdtsfynpdtqrlvwacvgvevgrgqplgvgisghpllnklddtenasayaana
gvdnrecismdykqtqlcligckppigehwgkgspctqvavqpgdcpplelintviqdgd
mvdtgfgamdfttlqanksevpldictsickypdyikmvsepygdslffylrreqmfvrh
lfnragtvgenvpddlyikgsgstanlassnyfptpsgsmvtsdaqifnkpywlqraqgh
nngicwgnqlfvtvvdttrstnmslcaaistsettykntnfkeylrhgeeydlqfifqlc
kitltadvmtyihsmnstiledwnfglqpppggtledtyrfvtsqaiacqkhtppapked
plkkytfwevnlkekfsadldqfplgrkfllqlgl
>d1amm_1 2.10.1.1.1 (1-85) gamma-Crystallin {Bovine (Bos taurus), isoform II (B)}
gkitfyedrgfqghcyecssdcpnlqpyfsrcnsirvdsgcwmlyerpnyqghqyflrrg
dypdyqqwmgfndsirscrlipqht
>d1amm_2 2.10.1.1.1 (86-174) gamma-Crystallin {Bovine (Bos taurus), isoform II (B)}
gtfrmriyerddfrgqmseitddcpslqdrfhltevhslnvlegswvlyempsyrgrqyl
lrpgeyrryldwgamnakvgslrrvmdfy
>d1a7ha_ 2.10.1.1.3 gamma-Crystallin {Bovine (Bos taurus), isoform S}
mykiqifekgdfngqmhettedcpsimeqfhmrevhsckvlegawifyelpnyrgrqyll
dkkeyrkpvdwgaaspavqsfrrive
>d2bb2_1 2.10.1.1.5 (-2-85) beta-Crystallin {Bovine (Bos taurus)}
lnpkiiifeqenfqghshelngpcpnlketgvekagsvlvqagpwvgyeqanckgeqfvf
ekgeyprwdswtssrrtdslsslrpikvds
>d2bb2_2 2.10.1.1.5 (86-175) beta-Crystallin {Bovine (Bos taurus)}
qehkitlyenpnftgkkmevidddvpsfhahgyqekvssvrvqsgtwvgyqypgyrglqy
llekgdykdsgdfgapqpqvqsvrrirdmqw
>d1bd7a_ 2.10.1.1.6 beta-Crystallin {Rat (Rattus norvegicus), isoform E}
ehkiilyenpnftgkkmeivdddvpsfhahgyqekvssvrvqsgtwvgyqypgyrglqyl
lekgdykdnsdfgaphpqvqsvrrirdmqgnpkiiifeqenfqghshelsgpcpnlketg
mekagsvlvqagpwvgyeqanckgeqfvfekgeyprwdswtssrrtdslsslrpik
>d1npsa_ 2.10.1.2.1 Protein S {Myxococcus xanthus}
anitvfynedfqgkqvdlppgnytraqlaalgienntissvkvppgvkailyqndgfagd
qievvanaeelgplnnnvssirvisvpv
>d1prr_2 2.10.1.2.1 (91-173) Protein S {Myxococcus xanthus}
prarffykeqfdgkevdlppgqytqaelerygidnntissvkpqglavvlfkndnfsgdt
lpvnsdaptlgamnnntssiris
>d1ag4__ 2.10.1.2.2 Spherulin 3a (S3a) {Slime mold (Physarum polycephalum)}
msvckgvsgnpakgevflykhvnfqgdswkvtgnvydfrsvsglndvvssvkvgpntkaf
ifkddrfngnfirleessqvtdlttrnlndaissiivatfesa
>d1wkt__ 2.10.1.3.1 Yeast killer toxin {Williopsis mrakii}
gdgylimckncdpntgscdwkqnwntcvgiganvhwmvtggstdgkqgcatiwegsgcvg
rsttmccpantccnintgfyirsyrrve
>d1bhu__ 2.10.1.4.1 Streptomyces metalloproteinase inhibitor, SMPI {Streptomyces nigrescens}
apscpagslctysgtglsgartvipasdmekagtdgvklpasarsfangthftlrygpar
kvtcvrfpcyqyatvgkvapgaqlrslpspgatvtvgqdlgd
>d1yge_2 2.11.1.1.1 (1-149) Plant lipoxigenase {Soybean (Glycine max), isozyme L1}
mfsaghkikgtvvlmpknelevnpdgsavdnlnaflgrsvslqlisatkadahgkgkvgk
dtflegintslptlgagesafnihfewdgsmgipgafyiknymqvefflksltleaisnq
gtirfvcnswvyntklyksvriffanhty
>d1lox_2 2.11.1.1.3 (2-112) 15-Lipoxygenase {Rabbit (Oryctolagus cuniculus)}
gvyrvcvstgasiyagsknkvelwlvgqhgevelgsclrptrnkeeefkvnvskylgsll
fvrlrkkhflkedawfcnwisvqalgaaedkywfpcyrwvvgdgvqslpvg
>d1bu8a1 2.11.1.2.6 (337-449) Pancreatic lipase, C-terminal domain {Rat (Rattus norvegicus)}
rwrykvsvtlsgakklsgyilvalygnngnskqyeifkgslkpearhvrdidvdinvgei
qkvkflwnnkvinlfrptlgasqitvqsgvdgkeynfcssdtvredvlqslypc
>d1ca1_2 2.11.1.3.1 (250-370) Alpha-toxin, C-terminal domain {Clostridium perfringens}
svgknvkelvayistsgekdagtddymyfgiktkdgktqewemdnpgndfmtgskdtytf
klkdenlkiddiqnmwirkrkytafpdaykpenikviangkvvvdkdinewisgnstyni
k
>d1pgs_1 2.12.1.1.1 (4-140) Peptide:N-glycosidase F, PNGase F {Flavobacterium meningosepticum}
dntvniktfdkvknafgdglsqsaegtftfpadvttvktikmfiknecpnktcdewdrya
nvyvknkttgewyeigrfitpywvgteklprgleidvtdfksllsgntelkiytetwlak
greysvdfdivygtpdy
>d1pgs_2 2.12.1.1.1 (141-314) Peptide:N-glycosidase F, PNGase F {Flavobacterium meningosepticum}
kysavvpviqynkssidgvpygkahtlglkkniqlptntekaylrttisgwghakpydag
srgcaewcfrthtiainnantfqhqlgalgcsanpinnqspgnwtpdragwcpgmavptr
idvlnnsltgstfsyeykfqswtnngtngdafyaissfviaksntpisapvvtn
>d1phm__ 2.12.1.2.1 Peptidylglycine alpha-hydroxylating monooxygenase, PHM {Rat (Rattus norvegicus)}
neclgtigpvtpldasdfaldirmpgvtpkesdtyfcmsmrlpvdeeafvidfkprasmd
tvhhmllfgcnmpsstgsywfcdegtctdkanilyawarnapptrlpkgvgfrvggetgs
kyfvlqvhygdisafrdnhkdcsgvsvhltrvpqpliagmylmmsvdtvippgekvvnad
iscqykmypmhvfayrvhthhlgkvvsgyrvrngqwtligrqnpqlpqafypvehpvdvt
fgdilaarcvftgegrteathiggtssdemcnlyimyymeakyalsfmtctknvapdmfr
tipaeanipi
>d1cjda_ 2.12.2.1.1 Coat protein p3 {Bacteriophage prd1}
lrnqqamaanlqarqivlqqsypviqqvetqtfdpanrsvfdvtpanvgivkgflvkvta
aitnnhateavaltdfgpanlvqrviyydpdnqrhtetsgwhlhfvntakqgapflssmv
tdspikygdvmnvidapatiaagatgeltmyywvplaysetdltgavlanvpqskqrlkl
efannntafaavganpleaiyqgagaadcefeeisytvyqsyldqlpvgqngyilplidl
stlynlensaqagltpnvdfvvqyanlyrylstiavfdnggsfnagtdinylsqrtanfs
dtrkldpktwaaqtrrriatdfpkgvyycdnrdkpiytlqygnvgfvvnpktvnqnarll
mgyeyftsr
>d1ruxa_ 2.12.2.2.2 Adenovirus hexon {Human adenovirus type 5}
mmpqwsymhisgqdaseylspglvqfaratetyfslnnkfrnptvapthdvttdrsqrlt
lrfipvdredtaysykarftlavgdnrvldmastyfdirgvldrgptfkpysgtaynala
pkgapnpcewdeaataleinleeedddnedevdeqaeqqkthvfgqapysginitkegiq
igvegqtpkyadktfqpepqigesqwyeteinhaagrvlkkttpmkpcygsyakptneng
gqgilvkqqngklesqvemqffstteatagngdnltpkvvlysedvdietpdthisympt
ikegnsrelmgqqsmpnrpnyiafrdnfiglmyynstgnmgvlagqasqlnavvdlqdrn
telsyqllldsigdrtryfsmwnqavdsydpdvriienhgtedelpnycfplggvintet
ltkvkpktgqengwekdatefsdkneirvgnnfameinlnanlwrnflysnialylpdkl
kyspsnvkisdnpntydymnkrvvapglvdcyinlgarwsldymdnvnpfnhhrnaglry
rsmllgngryvpfhiqvpqkffaiknllllpgsytyewnfrkdvnmvlqsslgndlrvdg
asikfdsiclyatffpmahntastleamlrndtndqsfndylsaanmlypipanatnvpi
sipsrnwaafrgwaftrlktketpslgsgydpyytysgsipyldgtfylnhtfkkvaitf
dssvswpgndrlltpnefeikrsvdgegynvaqcnmtkdwflvqmlanynigyqgfyipe
sykdrmysffrnfqpmsrqvvddtkykdyqqvgilhqhnnsgfvgylaptmregqaypan
fpypligktavdsitqkkflcdrtlwripfssnfmsmgaltdlgqnllyansahaldmtf
evdpmdeptllyvlfevfdvvrvhrphrgvietvylrtpfsa
>d1df0a2 2.13.1.1.2 (356-514) Calpain large subunit, middle domain (domain III) {Rat (Rattus norvegicus)}
wkltkmdgnwrrgstaggcrnypntfwmnpqylikleeededdedgergctflvgliqkh
rrrqrkmgedmhtigfgiyevpeeltgqtnihlsknfflttrarersdtfinlrevlnrf
klppgeyvlvpstfephkngdfcirvfsekkadyqtvdd
>d1shsa_ 2.14.1.1.1 Small heat shock protein {Methanococcus jannaschii}
tgiqisgkgfmpisiiegdqhikviawlpgvnkediilnavgdtleirakrsplmitese
riiyseipeeeeiyrtiklpatvkeenasakfengvlsvilpkaessikkginie
>d1ejfa_ 2.14.1.2.1 Co-chaperone p23 {Human (Homo sapiens)}
mqpasakwydrrdyvfiefcvedskdvnvnfekskltfsclggsdnfkhlneidlfhcid
pndskhkrtdrsilcclrkgesgqswprltkeraklnwlsvdfnnwkdwe
>d1slua_ 2.15.1.1.1 Ecotin, trypsin inhibitor {Escherichia coli}
iapypqaekgmkrqviqltpqedestlkvelligqtlevdcnlhrlggklenktlegwgy
dyyvfdkvsspvstmmhcpdgkkekkfvtaylgdagmlrynsklpivvytpdnvdvkyrv
wkaeekidnavvr
>d1a44__ 2.16.1.1.2 Phosphatidylethanolamine binding protein, PEBP {Bovine (Bos taurus)}
pvdlskwsgplslqevderpqhplqvkyggaevdelgkvltptqvknrptsitwdgldpg
klytlvltdpdapsrkdpkyrewhhflvvnmkgnnissgtvlsdyvgsgppkgtglhryv
wlvyeqegplkcdepilsnrsgdhrgkfkvasfrkkyelgapvagtcyqaewddyvpkly
eqlsg
>d1qoua_ 2.16.1.1.3 Centroradialis protein Cen {Garden snapdragon (Antirrhinum majus)}
grvigdvvdhftstvkmsviynsnnsikhvynghelfpsavtstprvevhggdmrsfftl
imtdpdvpgpsdpylrehlhwivtdipgttdssfgkevvsyemprpnigihrfvfllfkq
kkrgqamlsppvvcrdgfntrkftqenelglpvaavffncqret
>d1gof_2 2.17.1.1.1 (1-150) Galactose oxidase, N-terminal domain {Dactylium dendroides}
asapigsaisrnnwavtcdsaqsgnecnkaidgnkdtfwhtfygangdpkpphtytidmk
ttqnvnglsmlprqdgnqngwigrhevylssdgtnwgspvasgswfadsttkysnfetrp
aryvrlvaiteangqpwtsiaeinvfqass
>d1eut_2 2.17.1.1.2 (506-647) Sialidase, C-terminal domain {Micromonospora viridifaciens}
qarmsiadvdseetaredgrasnvidgnpstfwhtewsradapgyphrisldlggthtis
glqytrrqnsaneqvadyeiytslngttwdgpvasgrfttslapqravfpardaryirlv
alseqtghkyaavaelevegqr
>d1d7pm_ 2.17.1.2.2 C2 domain of factor VIII {Human (Homo sapiens)}
lnscsmplgmeskaisdaqitassyftnmfatwspskarlhlqgrsnawrpqvnnpkewl
qvdfqktmkvtgvttqgvkslltsmyvkeflisssqdghqwtlffqngkvkvfqgnqdsf
tpvvncldpplltrylrihpqswvhqialrmevlgceaq
>d1ciy_1 2.17.1.3.2 (462-609) delta-Endotoxin, C-terminal domain {Bacillus thuringiensis, CRYIA (A)}
nniipssqitqipltkstnlgsgtsvvkgpgftggdilrrtspgqistlrvnitaplsqr
yrvriryasttnlqfhtsidgrpinqgnfsatmssgsnlqsgsfrtvgfttpfnfsngss
vftlsahvfnsgnevyidriefvpaevt
>d1nuka_ 2.17.1.4.1 Ligand-binding domain of the ephb2 receptor tyrosine kinase {Mouse (Mus musculus)}
eetlmdsttataelgwmvhppsgweevsgydenmntirtyqvcnvfessqnnwlrtkfir
rrgahrihvemkfsvrdcssipsvpgscketfnlyyyeadfdlatktfpnwmenpwvkvd
tiaadesfsqvdlggrvmkintevrsfgpvsrngfylafqdyggcmsliavrvfyr
>d1bgla3 2.17.1.5.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bhga2 2.17.1.5.2 (22-225) beta-Glucuronidase {Human (Homo sapiens)}
glqggmlypqespsreckeldglwsfradfsdnrrrgfeeqwyrrplwesgptvdmpvps
sfndisqdwrlrhfvgwvwyerevilperwtqdlrtrvvlrigsahsyaivwvngvdtle
heggylpfeadisnlvqvgplpsrlritiainntltpttlppgtiqyltdtskypkgyfv
qntyfdffnyaglqrsvllyttpt
>d1cx1a_ 2.17.1.6.1 Cellulose-binding domain {Cellulomonas fimi}
asldsevellphtsfaeslgpwslygtsepvfadgrmcvdlpggqgnpwdaglvyngvpv
gegesyvlsftasatpdmpvrvlvgegggayrtafeqgsapltgepatreyaftsnltfp
pdgdapgqvafhlgkagayefcisqvslttsat
>d1ulo__ 2.17.1.6.1 Cellulose-binding domain {Cellulomonas fimi}
aspigegtfddgpegwvaygtdgpldtstgalcvavpagsaqygvgvvlngvaieegtty
tlrytatastdvtvralvgqngapygtvldtspaltseprqvtetftasatypatpaadd
pegqiafqlggfsadawtlclddvaldsevel
>d1xnaa_ 2.17.1.7.1 N-terminal domain of xrcc1 {Human (Homo sapiens)}
mpeirlrhvvscssqdsthcaenllkadtyrkwraakagektisvvlqlekeeqihsvdi
gndgsafvevlvgssaggageqdyevllvtssfmspsesrsgsnpnrvrmfgpdklvraa
aekrwdrvkivcsqpyskdspfglsfvrfhs
>d1bvp12 2.18.1.1.1 (121-254) Virus coat protein vp7 (BTV-10 vp7), central (top) domain {Bluetongue virus}
parqpygffleteetfqpgrwfmraaqavtavvcgpdmiqvslnagargdvqqifqgrnd
pmmiylvwrrienfamaqgnsqqtqagvtvsvggvdmragriiawdgqaalhvhnptqqn
amvqiqvvfyismd
>d1ahsa_ 2.18.1.1.2 Virus coat protein vp7 (BTV-10 vp7), central (top) domain {African horse sickness virus}
tgpyagavevqqsgryyvpqgrtrggyinsniaevcmdagaagqvnallaprrgdavmiy
fvwrplrifcdpqgaslesapgtfvtvdgvnvaagdvvawntiapvnvgnpgarrsilqf
evlwyt
>d2viua_ 2.18.1.2.1 Hemagglutinin {Influenza A virus, different strains}
statlclghhavpngtlvktitddqievtnatelvqssstgkicnnphrildgidctlid
allgdphcdvfqnetwdlfverskafsncypydvpdyaslrslvassgtlefitegftwt
gviqnggsnackrgpgsgffsrlnwltksgstypvlnvtmpnndnfdklyiwgihhpstn
qeqtslyvqasgrvtvstrrsqqtiipnigsrpwvrglssrisiywtivkpgdvlvinsn
gnliaprgyfkmrtgkssimrsdapidtcisecitpngsipndkpfqnvnkitygacpky
vkqntlklatgmrnvpekqt
>d1flca1 2.18.1.3.1 (218-321) Hemagglutinin domain of haemagglutinin-esterase-fusion glycoprotein HEF1 {Influenza C virus}
hlvascyfiydskevynkrgcdnyfqviydsfgkvvggldnrvspytgnsgdtptmqcdm
lqlkpgrysvrssprfllmpersycfdmkekgpvtavqsiwgkg
>d1aol__ 2.19.1.1.1 F-MuLV receptor-binding domain {Friend murine leukemia virus, F-MuLV}
qvynitwevtngdretvwaisgnhplwtwwpvltpdlcmlalsgpphwgleyqapysspp
gppccsgssgssagcsrdcdepltsltprcntawnrlkldqvthkssegfyvcpgshrpr
eakscggpdsfycaswgcettgrvywkpssswdyitvdnnlttsqavqvckdnkwcnpla
iqftnagkqvtswttghywglrlyvsgrdpgltfgirlryqnlgprvp
>d1qhva_ 2.20.1.1.2 Adenovirus fiber protein head domain (knob domain) {Adenovirus serotype 2}
aitignknddkltlwttpdpspncrihsdndckftlvltkcgsqvlatvaalavsgdlss
mtgtvasvsiflrfdqngvlmensslkkhywnfrngnstnanpytnavgfmpnllaypkt
qsqtaknnivsqvylhgdktkpmiltitlngtsestetsevstysmsftwswesgkytte
tfatnsytfsyiaqe
>d1aly__ 2.21.1.1.1 Extracellular domain of CD40 ligand {Human (Homo sapiens)}
gdqnpqiaahviseasskttsvlqwaekgyytmsnnlvtlengkqltvkrqglyyiyaqv
tfcsnreassqapfiaslclkspgrferillraanthssakpcgqqsihlggvfelqpga
svfvnvtdpsqvshgtgftsfgllkl
>d1c28a_ 2.21.1.1.2 30 kd adipocyte complement-related protein {Mouse (Mus musculus)}
myrsafsvgletrvtvpnvpirftkifynqqnhydgstgkfycnipglyyfsyhitvymk
dvkvslfkkdkavlftydqyqeknvdqasgsvllhlevgdqvwlqvygdgdhnglyadnv
ndstftgfllyhdt
>d1tnra_ 2.21.1.1.3 Tumor necrosis factor (TNF) {Human (Homo sapiens)}
kpaahligdpskqnsllwrantdraflqdgfslsnnsllvptsgiyfvysqvvfsgkays
pkatssplylahevqlfssqypfhvpllssqkmvypglqepwlhsmyhgaafqltqgdql
sthtdgiphlvlspstvffgafal
>d2tnfa_ 2.21.1.1.4 Tumor necrosis factor (TNF) {Mouse (Mus musculus)}
sdkpvahvvanhqveeqlewlsqranallangmdlkdnqlvvpadglylvysqvlfkgqg
cpdyvllthtvsrfaisyqekvnllsavkspcpkdtpegaelkpwyepiylggvfqlekg
dqlsaevnlpkyldfaesgqvyfgvial
>d1dg6a_ 2.21.1.1.5 Apoptosis-2 ligand, apo2l/TRAIL {Human (Homo sapiens)}
qrvaahitgtrgrsntlsspnsknekalgrkinswessrsghsflsnlhlrngelvihek
gfyyiysqtyfrfqeeikentkndkqmvqyiykytsypapillmksarnscwskdaeygl
ysiyqggifelkendrifvsvtnehlidmdheasffgaflvg
>d1sfp__ 2.22.1.1.1 Acidic seminal fluid protein (ASFP) {Bovine (Bos taurus)}
lprntncggilkeesgviatyygpktncvwtiqmppeyhvrvsiqylqlncnkesleiid
glpgspvlgkicegslmdyrssgsimtvkyirepehpasfyevlyfqdpqa
>d1sppa_ 2.22.1.1.2 Major seminal plasma glycoprotein PSP-I {Pig (Sus scrofa)}
ldyhacggrltddygtiftykgpktecvwtlqvdpkykllvsiptlnltcgkeyvevleg
apgskslgkfceglsilnrgssgmtvkykrdsghpaspyeiiflrdsqg
>d1sppb_ 2.22.1.1.3 Major seminal plasma glycoprotein PSP-II {Pig (Sus scrofa)}
aringpdecgrvikdtsgsisntdrqknlctwtilmkpdqkvrmaipylnlacgkeyvev
fdgllsgpsygklcagaaivflstantmtikynrisgnssspfliyfygssp
>d1cb8a2 2.23.1.1.1 (600-700) Chondroitinase AC, C-terminal domain {Flavobacterium heparinum}
pkvlantnqlqavyhqqldmvqaifytagklsvagieietdkpcavlikhingkqviwaa
dplqkektavlsirdlktgktnrvkidfpqqefagatvelk
>d1thw__ 2.24.1.1.3 Thaumatin {Ketemfe (Thaumatococcus daniellii benth)}
atfeivnrcsytvwaaaskgdaaldaggrqlnsgeswtinvepgtkggkiwartdcyfdd
sgsgicktgdcggllrckrfgrppttlaefslnqygkdyidisnikgfnvpmdfspttrg
crgvrcaadivgqcpaklkapgggcndactvfqtseyccttgkcgpteysrffkrlcpda
fsyvldkpttvtcpgssnyrvtfcpta
>d1ygs__ 2.25.1.1.1 Smad4 tumor suppressor C-terminal domain {Human (Homo sapiens)}
apeywcsiayfemdvqvgetfkvpsscpivtvdgyvdpsggdrfclgqlsnvhrteaier
arlhigkgvqleckgegdvwvrclsdhavfvqsyyldreagrapgdavhkiypsayikvf
dlrqchrqmqqqaataqaaaaaqaaavagnipgpgsvggiapaislsaaagigvddlrrl
cilrmsfvkgwgpdyprqsiketpcwieihlhralqlldevlhtm
>d1dmza_ 2.25.1.2.1 Phosphotyrosine binding domain of Rad53 {Baker's yeast (Saccharomyces cerevisiae)}
gngrfltlkplpdsiiqesleiqqgvnpffigrsedcnckiednrlsrvhcfifkkrhav
gksmyespaqglddiwychtgtnvsylnnnrmiqgtkfllqdgdeikiiwdknnkfvigf
kveindttglfneglgmlqeqrvvlkqtaeekdlvkkl
>d1cq3a_ 2.26.1.1.1 Soluble secreted chemokine inhibitor, VCCI {Virus (Cowpox virus)}
sfssssscteeenkhhmgidviikvtkqdqtptndkicqsvtevtesedeseevvkgdpt
tyytvvgggltmdfgftkcpkissiseysdgntvnarlssvspgqgkdspaitreealsm
ikdcemsinikcseeekdsnikthpvlgsnishkkvsyediigstivdtkcvknleisvr
igdmckesselevkdgfkyvdgsasedaaddtslinsakliacv
>d1p35a_ 2.27.1.1.1 Paculovirus p35 {Nuclear polyhedrosis virus (Autographa californica), ACMNPV}
cvifpveidvsqtiirdcqvdkqtrelvyinkimntqltkpvlmmfnisgpirsvtrknn
nlrdrikskvdeqfdqlerdysdqmdgfhdsikyfkdehysvscqngsvlkskfakilks
hdytdkksieayekyclpklvderndyyvavcvlkpgfengsnqvlsfeynpignkvivp
faheindtglyeydvvayvdsvqfdgeqfeefvqslilpssfknsekvlyyneasknksm
iykalefttesswgksekynwkifcngfiydkkskvlyvklhnvtsalnknvilntika
>d1nls__ 2.28.1.1.1 Concanavalin A {Jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>e1bqp.1b 2.28.1.1.3 Lectin {Garden pea (Pisum sativum)}
vtsytlsdvvslkdvvpewvrigfsattgaeyaahevlswsfhsels
>e1bqp.2d 2.28.1.1.3 Lectin {Garden pea (Pisum sativum)}
vtsytlsdvvslkdvvpewvrigfsattgaeyaahevlswsfhsels
>e1rin.1b 2.28.1.1.3 Lectin {Garden pea (Pisum sativum)}
vtsytlsdvvslkdvvpewvrigfsattgaeyaahevlswsfhsels
>e1rin.2d 2.28.1.1.3 Lectin {Garden pea (Pisum sativum)}
vtsytlsdvvslkdvvpewvrigfsattgaeyaahevlswsfhselsgt
>e2ltn.1a 2.28.1.1.3 Lectin {Garden pea (Pisum sativum)}
tettsflitkfspdqqnlifqgdgyttkekltltkavkntvgralysspihiwdretgnv
anfvtsftfvinapnsynvadgftffiapvdtkpqtgggylgvfnsaeydkttqtvavef
dtfynaawdpsnrdrhigidvnsiksvntkswklqngeeanvviafnaatnvltvsltyp
n
>e2ltn.1b 2.28.1.1.3 Lectin {Garden pea (Pisum sativum)}
vtsytlsdvvslkdvvpewvrigfsattgaeyaahevlswsfhselsg
>e2ltn.2d 2.28.1.1.3 Lectin {Garden pea (Pisum sativum)}
vtsytlsdvvslkdvvpewvrigfsattgaeyaahevlswsfhselsg
>d1lemb_ 2.28.1.1.4 Lectin {Common lentil (Lens culinaris)}
vtsytlnevvplkdvvpewvrigfsattgaefaaqevhswsfnsqlg
>d1lesb_ 2.28.1.1.4 Lectin {Common lentil (Lens culinaris)}
vtsytlnevvplkdvvpewvrigfsattgaefaahevhswsfhsqlg
>d1lesd_ 2.28.1.1.4 Lectin {Common lentil (Lens culinaris)}
vtsytlnevvplkdvvpewvrigfsattgaefaahevhswsfhsqlg
>e1len.1b 2.28.1.1.4 Lectin {Common lentil (Lens culinaris)}
vtsytlnevvplkdvvpewvrigfsattgaefaaqevhswsfnsqlg
>e1len.2d 2.28.1.1.4 Lectin {Common lentil (Lens culinaris)}
vtsytlnevvplkdvvpewvrigfsattgaefaaqevhswsfnsqlg
>e2lal.1b 2.28.1.1.4 Lectin {Common lentil (Lens culinaris)}
vtsytlnevvplkdvvpewvrigfsattgaefaaqevhswsfnsqlg
>e2lal.2d 2.28.1.1.4 Lectin {Common lentil (Lens culinaris)}
vtsytlnevvplkdvvpewvrigfsattgaefaaqevhswsfnsqlg
>d1led__ 2.28.1.1.5 Lectin {West-central african legume (Griffonia simplicifolia)}
xntvnftypdfwsyslkngteitflgdatripgalqltktdangnpvrssagqasysepv
flwdstgkaasfytsftfllknygaptadglafflapvdssvkdyggflglfrhetaadp
sknqvvavefdtwinkdwndppyphigidvnsivsvattrwenddaygssiatahityda
rskiltvllsyehgrdyilshvvdlakvlpqkvrigfsagvgydevtyilswhffstldg
tnk
>e1loa.1b 2.28.1.1.8 Lectin {Lathyrus ochrus, isolectin I}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1loa.2d 2.28.1.1.8 Lectin {Lathyrus ochrus, isolectin I}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfhselag
>e1loa.3f 2.28.1.1.8 Lectin {Lathyrus ochrus, isolectin I}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1loa.4h 2.28.1.1.8 Lectin {Lathyrus ochrus, isolectin I}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfhselag
>e1lob.1b 2.28.1.1.8 Lectin {Lathyrus ochrus, isolectin I}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1lob.2d 2.28.1.1.8 Lectin {Lathyrus ochrus, isolectin I}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfhselag
>e1lob.3f 2.28.1.1.8 Lectin {Lathyrus ochrus, isolectin I}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1lob.4h 2.28.1.1.8 Lectin {Lathyrus ochrus, isolectin I}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfhselag
>e1loc.1b 2.28.1.1.8 Lectin {Lathyrus ochrus, isolectin I}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1loc.2d 2.28.1.1.8 Lectin {Lathyrus ochrus, isolectin I}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfhselag
>e1loc.3f 2.28.1.1.8 Lectin {Lathyrus ochrus, isolectin I}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1loc.4h 2.28.1.1.8 Lectin {Lathyrus ochrus, isolectin I}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfhselag
>e1lod.1b 2.28.1.1.8 Lectin {Lathyrus ochrus, isolectin I}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1lod.2d 2.28.1.1.8 Lectin {Lathyrus ochrus, isolectin I}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfhselag
>e1lod.3f 2.28.1.1.8 Lectin {Lathyrus ochrus, isolectin I}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1lod.4h 2.28.1.1.8 Lectin {Lathyrus ochrus, isolectin I}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfhselag
>e1loe.1b 2.28.1.1.8 Lectin {Lathyrus ochrus, isolectin I}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1loe.2d 2.28.1.1.8 Lectin {Lathyrus ochrus, isolectin I}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1lof.1b 2.28.1.1.8 Lectin {Lathyrus ochrus, isolectin I}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1lof.2d 2.28.1.1.8 Lectin {Lathyrus ochrus, isolectin I}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhselagtssn
>e1log.1b 2.28.1.1.8 Lectin {Lathyrus ochrus, isolectin I}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1log.2d 2.28.1.1.8 Lectin {Lathyrus ochrus, isolectin I}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhselagtss
>e1lgb.1b 2.28.1.1.9 Lectin {Lathyrus ochrus, isolectin II}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfnselav
>e1lgc.1b 2.28.1.1.9 Lectin {Lathyrus ochrus, isolectin II}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfnselsvtss
>e1lgc.2d 2.28.1.1.9 Lectin {Lathyrus ochrus, isolectin II}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfnselsv
>e1lgc.3f 2.28.1.1.9 Lectin {Lathyrus ochrus, isolectin II}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfnselsv
>e1qmo.1a 2.28.1.1.12 Lectin {Field bean (Dolichos lab lab), Fril}
aqslsfsftkfdpnqedlifqghatstnnvlqvtkldsagnpvsssagrvlysaplrlwe
dsavltsfdtiinfeistpytsriadglaffiappdsvisyhggflglfpnan
>d1dhkb_ 2.28.1.1.17 Phytohemagglutinin-L, PHA-L, also arcelin {Kidney bean (Phaseolus vulgaris)}
atetsfiidafnktnlilqgdatvssngnlqlsynsydsmsrafysapiqirdsttgnva
sfdtnftmnirthrqansavgldfvlvpvqpeskgdtvtvefdtflsrisidvnnndiks
vpwdvhdydgqnaevritynsstkvfsvslsnpstgksnnvsttvelekevydwvsvgfs
atsgayqwsyethdvlswsfsskf
>d2ayh__ 2.28.1.2.2 Bacillus 1-3,1-4-beta-glucanase {Hybrid protein: residues 1-16 from Bacillus amyloliquefaciens and Bacillus macerans}
qtggsffepfnsynsgtwekadgysnggvfnctwrannvnftndgklklgltssaynkfd
caeyrstniygyglyevsmkpakntgivssfftytgpahgtqwdeidieflgkdttkvqf
nyytngvgghekvislgfdaskgfhtyafdwqpgyikwyvdgvlkhtatanipstpgkim
mnlwngtgvddwlgsynganplyaeydwvkytsn
>d1cpn__ 2.28.1.2.3 Bacillus 1-3,1-4-beta-glucanase {Bacillus macerans}
fdcaeyrstniygyglyevsmkpakntgivssfftytgpahgtqwdeidieflgkdttkv
qfnyytngvgghekvislgfdaskgfhtyafdwqpgyikwyvdgvlkhtatanipstpgk
immnlwngtgvddwlgsynganplyaeydwvkytsngsvfwepksyfnpstwekadgysn
ggvfnctwrannvnftndgklklgltss
>d1slta_ 2.28.1.3.1 S-lectin, different isoforms {Bovine (Bos taurus)}
cglvasnlnlkpgeclrvrgevaadaksfllnlgkddnnlclhfnprfnahgdvntivcn
skdagawgaeqresafpfqpgsvvevcisfnqtdltiklpdgyefkfpnrlnleainyls
aggdfkikcvafe
>d1bkza_ 2.28.1.3.2 S-lectin, different isoforms {Human (Homo sapiens)}
snvphksslpegirpgtvlrirglvppnasrfhvnllcgeeqgsdaalhfnprldtsevv
fnskeqgswgreergpgvpfqrgqpfevliiasddgfkavvgdaqyhhfrhrlplarvrl
vevggdvqldsvrif
>d1hlca_ 2.28.1.3.2 S-lectin, different isoforms {Human (Homo sapiens)}
elevknmdmkpgstlkitgsiadgtdgfvinlgqgtdklnlhfnprfsestivcnsldgs
nwgqeqredhlcfspgsevkftvtfesdkfkvklpdgheltfpnrlghshlsylsvrggf
nmssfklke
>d1lcl__ 2.28.1.3.5 Charcot-Leyden crystal (CLC) protein {Human (Homo sapiens)}
sllpvpyteaaslstgstvtikgrplvcflnepylqvdfhtemkeesdivfhfqvcfgrr
vvmnsreygawkqqvesknmpfqdgqefelsisvlpdkyqvmvngqssytfdhrikpeav
kmvqvwrdisltkfnvsylkr
>d1a3k__ 2.28.1.3.6 Galectin-3 CRD {Human (Homo sapiens)}
livpynlplpggvvprmlitilgtvkpnanrialdfqrgndvafhfnprfnennrrvivc
ntkldnnwgreerqsvfpfesgkpfkiqvlvepdhfkvavndahllqynhrvkklneisk
lgisgdidltsasytmi
>d1c1la_ 2.28.1.3.7 Congerin I {Conger eel (Conger myriaster)}
gglqvknfdftvgkfltvggfinnspqrfsvnvgesmnslslhldhrfnygadqntivmn
stlkgdngweteqrstnftlsagqyfeitlsydinkfyidildgpnlefpnryskeflpf
lslagdarltlvkle
>d1d2sa_ 2.28.1.4.1 Sex hormone-binding globulin {Human (Homo sapiens)}
ppavhlsngpgqepiavmtfdltkitktsssfevrtwdpegvifygdtnpkddwfmlglr
dgrpeiqlhnhwaqltvgagprlddgrwhqvevkmegdsvllevdgeevlrlrqvsghpi
mrialggllfpasnlrlplvpaldgclrrdswldkqaeisasaptslrsc
>d1qu0a_ 2.28.1.4.2 Laminin alpha2 chain {Mouse (Mus musculus)}
sgtyfdgtgfakavggfkvgldllvefefrttrptgvllgissqkmdgmgiemideklmf
hvdngagrftaiydaeipghmcngqwhkvtakkiknrlelvvdgnqvdaqspnsastsad
tndpvfvggfpgglnqfglttnirfrgcirslkltkgtgkplevnfakalelrgvqpvsc
p
>d1saca_ 2.28.1.5.1 Serum amyloid P component (SAP) {Human (Homo sapiens)}
htdlsgkvfvfpresvtdhvnlitplekplqnftlcfraysdlsrayslfsyntqgrdne
llvykervgeyslyigrhkvtskviekfpapvhicvswesssgiaefwingtplvkkglr
qgyfveaqpkivlgqeqdsyggkfdrsqsfvgeigdlymwdsvlppenilsayqgtplpa
nildwqalnyeirgyviikplvwv
>d1a8d_1 2.28.1.6.1 (1-247) Tetanus neurotoxin {Clostridium tetani}
mknldcwvdneedidvilkkstilnldinndiisdisgfnssvitypdaqlvpgingkai
hlvnnessevivhkamdieyndmfnnftvsfwlrvpkvsashleqygtneysiissmkkh
slsigsgwsvslkgnnliwtlkdsagevrqitfrdlpdkfnaylankwvfititndrlss
anlyingvlmgsaeitglgairednnitlkldrcnnnnqyvsidkfrifckalnpkeiek
lytsyls
>d1kit_1 2.28.1.8.1 (25-216) Vibrio cholerae sialidase, N-terminal and insertion domains {Vibrio cholerae}
alfdynatgdtefdspakqgwmqdntnngsgvltnadgmpawlvqgiggraqwtyslstn
qhaqassfgwrmttemkvlsggmitnyyangtqrvlpiisldssgnlvvefegqtgrtvl
atgtaateyhkfelvflpgsnpsasfyfdgklirdniqptaskqnmivwgngssntdgva
ayrdikfeiqgd
>d1kit_2 2.28.1.8.1 (347-543) Vibrio cholerae sialidase, N-terminal and insertion domains {Vibrio cholerae}
dvtdqvkersfqiagwggselyrrntslnsqqdwqsnakirivdgaanqiqvadgsrkyv
vtlsidesgglvanlngvsapiilqsehakvhsfhdyelqysalnhtttlfvdgqqittw
agevsqenniqfgnadaqidgrlhvqkivltqqghnlvefdafylaqqtpevekdleklg
wtkiktgntmslygnas
>d2sli_1 2.28.1.9.1 (81-276) Leech intramolecular trans-sialidase, N-terminal domain {North american leech (Macrobdella decora)}
ipegilmeknnvdiaegqgysldqeagakyvkamtqgtiilsykstsengiqslfsvgns
tagnqdrhfhiyitnsggigielrntdgvfnytldrpasvralykgervfntvalkadaa
nkqcrlfangellatldkdafkfisditgvdnvtlggtkrqgkiaypfggtigdikvysn
alsdeeliqatgvtty
>d6cel__ 2.28.1.10.1 Cellobiohydrolase I (cellulase) {Trichoderma reesei}
sactlqsethppltwqkcssggtctqqtgsvvidanwrwthatnsstncydgntwsstlc
pdnetcaknccldgaayastygvttsgnslsidfvtqsaqknvgarlylmasdttyqeft
llgnefsfdvdvsqlpcglngalyfvsmdadggvskyptntagakygtgycdsqcprdlk
fingqanvegwepssnnantgigghgsccsqmdiweansisealtphpcttvgqeicegd
gcggtysdnryggtcdpdgcdwnpyrlgntsfygpgssftldttkkltvvtqfetsgain
ryyvqngvtfqqpnaelgsysgnelnddyctaeeaefggssfsdkggltqfkkatsggmv
lvmslwddyyanmlwldstyptnetsstpgavrgscstssgvpaqvesqspnakvtfsni
kfgpigstgnpsg
>d1xnb__ 2.28.1.11.1 Xylanase II {Bacillus circulans}
astdywqnwtdgggivnavngsggnysvnwsntgnfvvgkgwttgspfrtinynagvwap
ngngyltlygwtrsplieyyvvdswgtyrptgtykgtvksdggtydiytttrynapsidg
drttftqywsvrqskrptgsnatitftnhvnawkshgmnlgsnwayqvmategyqssgss
nvtvw
>d2nlra_ 2.28.1.11.11 Endo-1,4-beta-glucanase (cellulase) CelB2 catalytic domain {Streptomyces lividans}
dtticepfgtttiqgryvvqnnrwgstapqcvtatdtgfrvtqadgsaptngapksypsv
fngchytncspgtdlpvrldtvsaapssisygfvdgavynasydiwldptartdgvnqte
imiwfnrvgpiqpigspvgtasvggrtwevwsggngsndvlsfvapsaisgwsfdvmdfv
ratvarglaendwyltsvqagfepwqngaglavnsfsstvet
>d1bgla4 2.29.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1oaca1 2.29.2.1.1 (301-724) Copper amine oxidase, domain 3 (catalytic) {Escherichia coli}
pavkpmqiiepegknytitgdmihwrnwdfhlsmnsrvgpmistvtyndngtkrkvmyeg
slggmivpygdpdigwyfkayldsgdygmgtltspiargkdapsnavllnetiadytgvp
meipraiavferyagpeykhqemgqpnvsterrelvvrwistvgnxdyifdwifhengti
gidagatgieavkgvkaktmhdetakddtrygtlidhnivgtthqhiynfrldldvdgen
nslvamdpvvkpntaggprtstmqvnqynigneqdaaqkfdpgtirllsnpnkenrmgnp
vsyqiipyaggthpvakgaqfapdewiyhrlsfmdkqlwvtryhpgerfpegkypnrsth
dtglgqyskdnesldntdavvwmttgtthvaraeewpimptewvhtllkpwnffdetptl
galk
>d1cb8a3 2.29.3.1.1 (336-599) Chondroitinase AC, central domain {Flavobacterium heparinum}
iepyhhqfwngdyvqhlrpaysfnvrmvskrtrrsesgnkenllgrylsdgatniqlrgp
eyynimpvwewdkipgitsrdyltdrpltklwgeqgsndfaggvsdgvygasayaldyds
lqakkawfffdkeivclgaginsnapenitttlnqswlngpvistagktgrgkittfkaq
gqfwllhdaigyyfpeganlslstqsqkgnwfhinnshskdevsgdvfklwinhgarpen
aqyayivlpginkpeeikkyngta
>d1qexa_ 2.30.1.1.1 gp9 {Bacteriophage T4}
mfiqepkklidtgeignastgdilfdggnkinsdfnaiynafgdqrkmavangtgadgqi
ihatgyyqkhsiteyatpvkvgtrhdidtstvgvkviiergelgdcvefinsngsisvtn
pltiqaidsikgvsgnlvvtspyskvtlrcissdnstsvwnysiesmfgqkespaegtwn
istsgsvdiplfhrteynmakllvtcqsvdgrkiktaeinilvdtvnsevisseyavmrv
gneteedeianiafsikenyvtatissstvgmraavkviatqkigvaq
>d1rie__ 2.31.1.1.1 ISP subunit of the mitochondrial cytochrome bc1-complex {Bovine (Bos taurus)}
amskieiklsdipegknmafkwrgkplfvrhrtkkeidqeaavevsqlrdpqhdlervkk
pewviligvcthlgcvpianagdfggyycpchgshydasgrirkgpaplnlevpsyefts
ddmvivg
>d1rfs__ 2.31.1.1.3 ISP subunit from chloroplast cytochrome bf complex {Spinach (Spinacia oleracea)}
tiakdalgndviaaewlkthapgdrtltqglkgdptylvvesdktlatfginavcthlgc
vvpfnaaenkficpchgsqynnqgrvvrgpaplslalahcdvddgkvvfvpwtetdfrtg
eapwwsa
>d1eg9a1 2.31.1.2.1 (1-154) Napthalene 1,2-dioxygenase alpha subunit, N-domain {Pseudomonas putida}
mnynnkilvsesglsqkhlihgdeelfqhelktifarnwlflthdslipapgdyvtakmg
idevivsrqndgsiraflnvcrhrgktlvsveagnakgfvcsyhgwgfgsngelqsvpfe
kdlygeslnkkclglkevarvesfhgfiygcfdq
>d1bia_2 2.32.1.1.1 (271-317) Biotin repressor/biotin holoenzyme synthetase, C-terminal domain {Escherichia coli}
finrpvkliigdkeifgisrgidkqgallleqdgiikpwmggeislr
>d1bib_2 2.32.1.1.1 (271-317) Biotin repressor/biotin holoenzyme synthetase, C-terminal domain {Escherichia coli}
finrpvkliigdkeifgisrgidkqgallleqdgiikpwmggeislr
>d1bi1_3 2.32.1.2.1 (148-225) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
pgtrvidaatsmprkvrivqineifqvetdqftqlldadirvgseveivdrdghitlshn
gkdvellddlahtiriee
>d1ckaa_ 2.32.2.1.1 C-Crk, N-terminal SH3 domain {Mouse (Mus musculus)}
aeyvralfdfngndeedlpfkkgdilrirdkpeeqwwnaedsegkrgmipvpyveky
>d1shfa_ 2.32.2.1.2 Fyn proto-oncogene tyrosine kinase, SH3 domain {Human (Homo sapiens)}
vtlfvalydyearteddlsfhkgekfqilnssegdwwearslttgetgyipsnyvapvd
>d1neb__ 2.32.2.1.3 SH3 domain from nebulin {Human (Homo sapiens)}
tagkiframydymaadadevsfkdgdaiinvqaidegwmygtvqrtgrtgmlpanyveai
>d1bbza_ 2.32.2.1.5 Abl tyrosine kinase, SH3 domain {Human (Homo sapiens)}
nlfvalydfvasgdntlsitkgeklrvlgynhngewceaqtkngqgwvpsnyitpvns
>d1pht__ 2.32.2.1.6 Phosphatidylinositol 3-kinase (p85-alpha subunit, pi3k), SH3 domain {Human (Homo sapiens)}
aegyqyralydykkereedidlhlgdiltvnkgslvalgfsdgqearpeeigwlngynet
tgergdfpgtyveyigrkkispp
>d1pwt__ 2.32.2.1.8 alpha-Spectrin, SH3 domain {Chicken (Gallus gallus)}
mgtgkelvlalydyqeksprevtmkkgdiltllnstnkdwwkvevndrqgfvpaayvkkl
d
>d1tuc__ 2.32.2.1.8 alpha-Spectrin, SH3 domain {Chicken (Gallus gallus)}
mgprevtmkkgdiltllnstnkdwwkvevndrqgfvpaayvkkldsgtgkelvlalydyq
e
>d1tud__ 2.32.2.1.8 alpha-Spectrin, SH3 domain {Chicken (Gallus gallus)}
rqgfvpaayvkkldsgtgkelvlalydyqeksprevtmkkgdiltllnstnkdwwkvevn
>d1awj__ 2.32.2.1.9 IL-2 inducible T-cell (Itc) kinase {Mouse (Mus musculus)}
kkplpptpednrrsfqepeetlvialydyqtndpqelalrcdeeyylldsseihwwrvqd
knghegyapssylveks
>d1qcfa1 2.32.2.1.10 (80-145) Hemapoetic cell kinase Hck {Human (Homo sapiens)}
sgiriivvalydyeaihhedlsfqkgdqmvvleesgewwkarslatrkegyipsnyvarv
dslet
>d1fmk_1 2.32.2.1.11 (82-145) c-src tyrosine kinase {Human (Homo sapiens)}
mvttfvalydyesrtetdlsfkkgerlqivnntegdwwlahslstgqtgyipsnyvapsd
siqa
>d1awx__ 2.32.2.1.13 Bruton's tyrosine kinase {Human (Homo sapiens)}
gsmstselkkvvalydympmnandlqlrkgdeyfileesnlpwwrardkngqegyipsny
vteaeds
>d1gria1 2.32.2.1.14 (1-56) Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {Human (Homo sapiens)}
meaiakydfkataddelsfkrgdilkvlneecdqnwykaelngkdgfipknyiemk
>d1gria2 2.32.2.1.14 (157-217) Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {Human (Homo sapiens)}
qptyvqalfdfdpqedgelgfrrgdfihvmdnsdpnwwkgachgqtgmfprnyvtpvnrn
v
>d1azea_ 2.32.2.1.15 Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {Mouse (Mus musculus)}
meaiakvdfkataddelsfkrgdilkvlneesdqnwykaelngkdgfipknyiemk
>d1sema_ 2.32.2.1.16 Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {Caenorhabditis elegans, SEM-5}
etkfvqalfdfnpqesgelafkrgdvitlinkddpnwwegqlnnrrgifpsnyvcpyn
>d2hsp__ 2.32.2.1.17 Phospholipase C, SH3 domain {Human (Homo sapiens)}
gsptfkcavkalfdykaqredeltfiksaiiqnvekqeggwwrgdyggkkqlwfpsnyve
emvnpegihrd
>d1cska_ 2.32.2.1.19 Src kinase, SH3 domain {Human (Homo sapiens)}
gteciakynfhgtaeqdlpfckgdvltivavtkdpnwykaknkvgregiipanyvqkr
>d1lcka1 2.32.2.1.21 (63-116) p56-lck tyrosine kinase, SH3 domain {Human (Homo sapiens)}
dnlvialhsyepshdgdlgfekgeqlrileqsgewwkaqslttgqegfipfnfv
>d1ycsb2 2.32.2.1.22 (457-519) 53BP2 {Human (Homo sapiens)}
imnkgviyalwdyepqnddelpmkegdcmtiihrededeiewwwarlndkegyvprnllg
lyp
>d1bb9__ 2.32.2.1.23 Amphiphysin 2 {Rat (Rattus norvegicus)}
ttgrldlppgfmfkvqaqhdytatdtdelqlkagdvvlvipfqnpeeqdegwlmgvkesd
wnqhkelekcrgvfpenftervq
>d1aoja_ 2.32.2.1.24 EPS8 SH3 domain {Mouse (Mus musculus)}
kkyakskydfvarnsselsvmkddvleilddrrqwwkvrnasgdsgfvpnnildimrtpe
>d1br1a1 2.32.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br1c1 2.32.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br1e1 2.32.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br1g1 2.32.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br2a1 2.32.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br2b1 2.32.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br2c1 2.32.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br2d1 2.32.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br2e1 2.32.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br2f1 2.32.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br4a1 2.32.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br4c1 2.32.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br4e1 2.32.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br4g1 2.32.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d2mysa1 2.32.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
axssvfvvhpkqsfvxgtiqsxeggxvtvxteggetltvkedqvfs
>d1b7ta1 2.32.3.1.2 (29-76) Myosin S1 fragment, N-terminal domain {Bay scallop (Aequipecten irradians)}
dgkkncwvpdekegfasaeiqsskgdeitvkivadsstrtvkkddiqs
>d1d0xa1 2.32.3.1.3 (34-79) Myosin S1 fragment, N-terminal domain {Dictyostelium discoideum}
yiwynpdpkerdsyecgeivsetsdsftfktvdgqdrqvkkddanq
>d1d0ya1 2.32.3.1.3 (34-79) Myosin S1 fragment, N-terminal domain {Dictyostelium discoideum}
yiwynpdpkerdsyecgeivsetsdsftfktvdgqdrqvkkddanq
>d1d0za1 2.32.3.1.3 (34-79) Myosin S1 fragment, N-terminal domain {Dictyostelium discoideum}
yiwynpdpkerdsyecgeivsetsdsftfktvdgqdrqvkkddanq
>d1d1aa1 2.32.3.1.3 (34-79) Myosin S1 fragment, N-terminal domain {Dictyostelium discoideum}
yiwynpdpkerdsyecgeivsetsdsftfktvdgqdrqvkkddanq
>d1d1ba1 2.32.3.1.3 (34-79) Myosin S1 fragment, N-terminal domain {Dictyostelium discoideum}
yiwynpdpkerdsyecgeivsetsdsftfktvdgqdrqvkkddanq
>d1d1ca1 2.32.3.1.3 (34-79) Myosin S1 fragment, N-terminal domain {Dictyostelium discoideum}
yiwynpdpkerdsyecgeivsetsdsftfktvdgqdrqvkkddanq
>d1lvk_1 2.32.3.1.3 (34-79) Myosin S1 fragment, N-terminal domain {Dictyostelium discoideum}
yiwynpdpkerdsyecgeivsetsdsftfktsdgqdrqvkkddanq
>d1mma_1 2.32.3.1.3 (34-79) Myosin S1 fragment, N-terminal domain {Dictyostelium discoideum}
yiwynpdpkerdsyecgeivsetsdsftfktsdgqdrqvkkddanq
>d1mmd_1 2.32.3.1.3 (34-79) Myosin S1 fragment, N-terminal domain {Dictyostelium discoideum}
yiwynpdpderdsyecgeivsetsdsftfktvdgqdrqvkkddanq
>d1mmg_1 2.32.3.1.3 (34-79) Myosin S1 fragment, N-terminal domain {Dictyostelium discoideum}
yiwynpdpkerdsyecgeivsetsdsftfktsdgqdrqvkkddanq
>d1mmn_1 2.32.3.1.3 (34-79) Myosin S1 fragment, N-terminal domain {Dictyostelium discoideum}
yiwynpdpkerdsyecgeivsetsdsftfktsdgqdrqvkkddanq
>d1mnd_1 2.32.3.1.3 (34-79) Myosin S1 fragment, N-terminal domain {Dictyostelium discoideum}
yiwynpdpderdsyecgeivsetsdsftfktvdgqdrqvkkddanq
>d1mne_1 2.32.3.1.3 (34-79) Myosin S1 fragment, N-terminal domain {Dictyostelium discoideum}
yiwynpdpderdsyecgeivsetsdsftfktvdgqdrqvkkddanq
>d1vom_1 2.32.3.1.3 (34-79) Myosin S1 fragment, N-terminal domain {Dictyostelium discoideum}
yiwynpdpderdsyecgeivsetsdsftfktvdgqdrqvkkddanq
>d1vie__ 2.32.4.1.1 R67 dihydrofolate reductase {Escherichia coli, plasmid PLZ1}
psnatfgmgdrvrkksgaawqgqivgwyctnltpegyaveseahpgsvqiypvaalerin
>d1psf__ 2.32.4.2.1 Photosystem I accessory protein E (PsaE) {Cyanobacterium (Synechococcus sp., strain PCC 7002}
aiergskvkilrkesywygdvgtvasidksgiiypvivrfnkvnyngfsgsagglntnnf
aehelevvg
>d1qp2a_ 2.32.4.2.2 Photosystem I accessory protein E (PsaE) {Cyanobacterium (Nostoc sp., strain pcc8009}
mvqrgskvrilrpesywfqdvgtvasvdqsgikypvivrfekvnysgintnnfaedelve
veapkakpkk
>d1dj7b_ 2.32.4.3.1 Ferredoxin thioredoxin reductase (FTR), alpha (variable) chain {Synechocystis sp.}
mnvgdrvrvtssvvvyhhpehkktafdlqgmegevaavltewqgrpisanlpvlvkfeqr
fkahfrpdevtli
>d2ahjb_ 2.32.4.4.1 Nitrile hydratase beta chain {Rhodococcus sp. r312}
mdgvhdlagvqgfgkvphtvnadigptfhaewehlpyslmfagvaelgafsvdevryvve
rmeprhymmtpyyeryvigvatlmvekgiltqdeleslaggpfplsrpsesegrpapvet
ttfevgqrvrvrdeyvpghirmpaycrgrvgtishrttekwpfpdaighgrndageepty
hvkfaaeelfgsdtdggsvvvdlfegylepa
>d2eifa1 2.32.5.1.1 (1-73) N-terminal domain of eukaryotic initiation translation factor 5a {Methanococcus jannaschii}
viimpgtkqvnvgslkvgqyvmidgvpceivdisvskpgkhggakarvvgigifekvkke
fvaptsskvevpi
>d1bkb_1 2.32.5.1.2 (4-74) N-terminal domain of eukaryotic initiation translation factor 5a {Pyrobaculum aerophilum}
kwvxstkyveagelkegsyvvidgepcrvveieksktgkhgsakarivavgvfdggkrtl
slpvdaqvevp
>d1rl2a1 2.32.5.2.1 (126-195) C-terminal domain of ribosomal protein L2 {Bacillus stearothermophilus}
gnalplenipvgtlvhnielkpgrggqlvraagtsaqvlgkegkyvivrlasgevrxilg
kcratvgevg
>d3vub__ 2.32.6.1.1 CcdB {Escherichia coli}
mqfkvytykresryrlfvdvqsdiidtpgrrmviplasarllsdkvsrelypvvhigdes
wrmmttdmasvpvsvigeevadlshrendiknainlmfwgi
>d1ex4a1 2.32.7.1.1 (223-270) DNA-binding domain of retroviral integrase {Human immunodeficiency virus, HIV-1}
frvyyrdsrnslwkgpakllwkgegavviqdnsdikvvprrkakiird
>d1ex4b1 2.32.7.1.1 (223-270) DNA-binding domain of retroviral integrase {Human immunodeficiency virus, HIV-1}
frvyyrdsrnslwkgpakllwkgegavviqdnsdikvvprrkakiird
>d1ihva_ 2.32.7.1.1 DNA-binding domain of retroviral integrase {Human immunodeficiency virus, HIV-1}
miqnfrvyyrdsrdpvwkgpakllwkgegavviqdnsdikvvprrkakiird
>d1ihvb_ 2.32.7.1.1 DNA-binding domain of retroviral integrase {Human immunodeficiency virus, HIV-1}
miqnfrvyyrdsrdpvwkgpakllwkgegavviqdnsdikvvprrkakiird
>d1ihwa_ 2.32.7.1.1 DNA-binding domain of retroviral integrase {Human immunodeficiency virus, HIV-1}
miqnfrvyyrdsrdpvwkgpakllwkgegavviqdnsdikvvprrkakiird
>d1ihwb_ 2.32.7.1.1 DNA-binding domain of retroviral integrase {Human immunodeficiency virus, HIV-1}
miqnfrvyyrdsrdpvwkgpakllwkgegavviqdnsdikvvprrkakiird
>d1qmca_ 2.32.7.1.1 DNA-binding domain of retroviral integrase {Human immunodeficiency virus, HIV-1}
miqnfrvyyrdsrnplwkgpakllwkgegavviqdnsdikvvprrkakiird
>d1qmcb_ 2.32.7.1.1 DNA-binding domain of retroviral integrase {Human immunodeficiency virus, HIV-1}
miqnfrvyyrdsrnplwkgpakllwkgegavviqdnsdikvvprrkakiird
>d1c0ma1 2.32.7.1.2 (217-269) DNA-binding domain of retroviral integrase {Rous sarcoma virus, RSV}
vltegppvkirietgewekgwnvlvwgrgyaavknrdtdkviwvpsrkvkpdi
>d1aono_ 2.33.1.1.1 Chaperonin-10 (GroES) {Escherichia coli}
mnirplhdrvivkrkevetksaggivltgsaaakstrgevlavgngrilengevkpldvk
vgdivifndgygvksekidneevlimsesdilaivea
>d1lepa_ 2.33.1.1.2 Chaperonin-10 (GroES) {Mycobacterium leprae}
akvkikpledkilvqageaetmtpsglvipenakekpqegtvvavgpgrwdedgakripv
dvsegdiviyskyggteikyngeeylilsardvlavvsk
>d1g31a_ 2.33.1.1.3 GP31 co-chaperonin {Bacteriophage T4}
qqlpiravgeyvilvsepaqagdeevtesgliigkrvqgevpelcvvhsvgpdvpegfce
vgdltslpvgqirnvphpfvalglkqpkeikqkfvtchykaipclyk
>d3btoa1 2.33.1.2.1 (1-174,325-374) Alcohol dehydrogenase {Horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1keva1 2.33.1.2.3 (1-150,315-351) Bacterial secondary alcohol dehydrogenase {Clostridium beijerinckii}
mkgfamlginklgwiekerpvagsydaivrplavspctsdihtvfegalgdrknmilghe
avgevvevgsevkdfkpgdrvivpcttpdwrslevqagfqqhsngmlagwkfsnfkdgvf
geyfhvndadmnlailpkdmplenavmitdXdlsklvthvyhgfdhieealllmkdkpkd
likavvil
>d1qora1 2.33.1.2.5 (2-135,266-327) Quinone oxidoreductase {Escherichia coli}
atriefhkhggpevlqaveftpadpaeneiqvenkaiginfidtyirsglypppslpsgl
gteaagivskvgsgvkhikagdrvvyaqsalgayssvhniiadkaailpaaisfeqaaas
flkgltvyyllrktXlqgyittreelteasnelfsliasgvikvdvaeqqkyplkdaqra
heilesratqgssllip
>d1auua_ 2.33.2.1.1 SacY {Bacillus subtilis}
mkikrilnhnaivvkdqneekillgagiafnkkkndivdpskiektfirkdtpdy
>d1auub_ 2.33.2.1.1 SacY {Bacillus subtilis}
mkikrilnhnaivvkdqneekillgagiafnkkkndivdpskiektfirkdtpdy
>d1kwaa_ 2.34.1.1.2 Cask/Lin-2 {Human (Homo sapiens)}
rsrlvqfqkntdepmgitlkmnelnhcivarimhggmihrqgtlhvgdeireingisvan
qtveqlqkmlremrgsitfkivpsyref
>d1be9a_ 2.34.1.1.3 Synaptic protein PSD-95 {Rat (Rattus norvegicus)}
flgeedipreprrivihrgstglgfniiggedgegifisfilaggpadlsgelrkgdqil
svngvdlrnasheqaaialknagqtvtiiaqykpeeysrfeansrvnssgrivtn
>d1qlca_ 2.34.1.1.3 Synaptic protein PSD-95 {Rat (Rattus norvegicus)}
aekvmeiklikgpkglgfsiaggvgnqhipgdnsiyvtkiieggaahkdgrlqigdkila
vnsvgledvmhedavaalkntydvvylkvakpsna
>d1qaua_ 2.34.1.1.4 Syntrophin {Rat (Rattus norvegicus)}
nvisvrlfkrkvgglgflvkervskppviisdlirggaaeqsgliqagdiilavndrplv
dlsydsalevlrgiasethvvlilrgpegftthlettftgdgtpktirvtqp
>d1qava_ 2.34.1.1.5 Syntrophin {Mouse (Mus musculus)}
gslqrrrvtvrkadagglgisikggrenkmpiliskifkglaadqtealfvgdailsvng
edlssathdeavqalkktgkevvlevkymk
>d3pdza_ 2.34.1.1.7 Phosphatase hPTP1e {Human (Homo sapiens)}
pkpgdifevelakndnslgisvtggvntsvrhggiyvkavipqgaaesdgrihkgdrvla
vngvslegathkqavetlrntgqvvhlllekgqspt
>d1i16__ 2.34.1.2.1 Interleukin 16 {Human (Homo sapiens)}
mpdlnsstdsaasasaasdvsvestaeatvctvtlekmsaglgfsleggkgslhgdkplt
inrifkgaaseqsetvqpgdeilqlggtamqgltrfeawniikalpdgpvtivirrkslq
skettaagds
>d1g3p_1 2.35.1.1.1 (1-65) N-terminal domains of the minor coat protein g3p {Bacteriophage fd}
aetvesclakshtensftnvxkddktldryanyegclwnatgvvvctgdetqcygtwvpi
glaip
>d1g3p_2 2.35.1.1.1 (91-217) N-terminal domains of the minor coat protein g3p {Bacteriophage fd}
enegggsegggsegggsegggtkppeygdtpipgytyinpldgtyppgteqnpanpnpsl
eesqplntfmfqnnrfrnrqgaltvytgtvtqgtdpvktyyqytpvsskamydaywngkf
rdcafhsgfnedifvceyqgqssdlpqppvna
>d1b34a_ 2.36.1.1.1 D1 core SNRNP protein {Human (Homo sapiens)}
klvrflmklshetvtielkngtqvhgtitgvdvsmnthlkavkmtlknrepvqletlsir
gnniryfilpdslpldtllv
>d1b34b_ 2.36.1.1.2 D2 core SNRNP protein {Human (Homo sapiens)}
tgplsvltqsvknntqvlincrnnkkllgrvkafdrhcnmvlenvkemwtevpksgkgkk
kskpvnkdryiskmflrgdsvivvlrnpliagk
>d1d3ba_ 2.36.1.1.3 D3 core SNRNP protein {Human (Homo sapiens)}
gvpikvlheaeghivtcetntgevyrgklieaednmncqmsnitvtyrdgrvaqleqvyi
rgckirflilpd
>d1d3bb_ 2.36.1.1.4 B core SNRNP protein {Human (Homo sapiens)}
skmlqhidyrmrcilqdgrifigtfkafdkhmnlilcdcdefrkikpknskqaereekrv
lglvllrgenlvsmtvegppp
>d1whi__ 2.37.1.1.1 Ribosomal protein L14 {Bacillus stearothermophilus}
miqqesrlkvadnsgarevlvikvlggsgrryanigdvvvatvkdatpggvvkkgqvvka
vvvrtkrgvrrpdgsyirfdenacviirddksprgtrifgpvarelrdkdfmkiislape
vi
>d1sty__ 2.38.1.1.1 Staphylococcal nuclease {Staphylococcus aureus}
klhkepatlikaidgdtvklmykgqpmtfrlllvdtpetkhpkkgvekygpeasaftkkm
venakkievefdkgqrtdkygrglayiyadgkmvnealvrqglakvayvykpnntheqhl
rgkseaqakkeklniws
>d1tiid_ 2.38.2.1.2 Heat-labile toxin {Escherichia coli, type IIB}
gasqffkdncnrttaslvegveltkyisdinnntdgmyvvsstggvwrisrakdypdnvm
taemrkiamaavlsgmrvnmcaspasspnviwaielea
>d3chbd_ 2.38.2.1.3 Cholera toxin {Vibrio cholerae}
tpqnitdlcaeyhntqihtlndkifsyteslagkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktpraiaaisman
>d2bosa_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
adcakgkiefskynedntftvkvsgreywtnrwnlqpllqsaqltgmtvtiisntcssgs
gfaevqfn
>d1qnua_ 2.38.2.1.5 Verotoxin-1/shiga-toxin, B-pentamer {Shigella dysenteriae}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1prtb1 2.38.2.1.6 (90-199) Pertussis toxin S2/S3 subunits, C-terminal domain {Bordetella pertussis}
ttrntgqpatdhyysnvtatrllsstnsrlcavfvrsgqpvigactspydgkywsmysrl
rkmlyliyvagisvrvhvskeeqyydyedatfetyaltgisicnpgsslc
>d1prtd_ 2.38.2.1.7 Pertussis toxin S4 subunit {Bordetella pertussis}
dvpyvlvktnmvvtsvamkpyevtptrmlvcgiaaklgaaasspdahvpfcfgkdlkrpg
sspmevmlravfmqqrplrmflgpkqltfegkpalelirmvecsgkqdcp
>d1prtf_ 2.38.2.1.8 Pertussis toxin S5 subunit {Bordetella pertussis}
lpthlyknftvqelalklkgknqefcltafmsgrslvraclsdaghehdtwfdtmlgfai
sayalksrialtvedspypgtpgdllelqicplngyce
>d1esfa1 2.38.2.2.1 (1-120) Staphylococcal enterotoxin A, SEA {Staphylococcus aureus}
sekseeinekdlrkkselqgtalgnlkqiyyynekaktenkeshdqflqhtilfkgfftd
hswyndllvdfdskdivdkykgkkvdlygayygyqcaggtpnktacmyggvtlhdnnrlt
>d3tss_1 2.38.2.2.3 (5-93) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
nikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkgekvdl
ntkrikksqhtsegtwihfqisgvtntek
>d3seb_1 2.38.2.2.4 (1-121) Staphylococcal enterotoxin B, SEB {Staphylococcus aureus}
esqpdpkpdelhksskftglmenmkvlyddnhvsainvksidqflyfdliysikdtklgn
ydnvrvefknkdladkykdkyvdvfganyyyqcyfskktndinshqtdkrktcmyggvte
h
>d1enfa1 2.38.2.2.6 (2-101) Staphylococcal enterotoxin H, SEH {Staphylococcus aureus}
dlhdkseltdlalanaygqynhpfikeniksdeisgekdlifrnqgdsgndlrvkfatad
laqkfknknvdiygasfyykcekiseniseclyggttlns
>d1an8_1 2.38.2.2.7 (3-95) Streptococcal superantigen Spe-C {Streptococcus pyogenes}
kkdisnvksdllyaytitpydykdcrvnfstthtlnidtqkyrgkdyyissemsyeasqk
fkrddhvdvfglfyilnshtgeyiyggitpaqn
>d1et9a1 2.38.2.2.8 (1-95) Streptococcal superantigen Spe-H {Streptococcus pyogenes}
nsynttnrhnleslykhdsnlieadsiknspdivtshmlkysvkdknlsvffekdwisqe
fkdkevdiyalsaqevcecpgkryeafggitltns
>d1eu3a1 2.38.2.2.9 (2a-96) Streptococcal superantigen Smez-2 {Streptococcus pyogenes}
glevdnnsllrniystivyeysdividfktshnlvtkkldvrdardffinsemdeyaand
fktgdkiavfsvpfdwnylskgkvtaytyggitpyqk
>d1b1za1 2.38.2.2.11 (3-107) Streptococcal pyrogenic exotoxin A1 {Streptococcus pyogenes}
dpdpsqlhrsslvknlqniyflyegdpvthenvksvdqllshdliynvsgpnydklktel
knqematlfkdknvdiygveyyhlcylcenaersaciyggvtnhe
>d1d2ba_ 2.38.3.1.1 TIMP-1 {Human (Homo sapiens)}
ctcvpphpqtafcnsdlvirakfvgtpevnqttlyqryeikmtkmykgfqalgdaadirf
vytpamesvcgyfhrshnrseefliagklqdgllhittcsfvapwnslslaqrrgftkty
tvgcee
>d1br9__ 2.38.3.1.2 TIMP-2 {Human (Homo sapiens)}
cscspvhpqqafcnadvvirakavsekevdsgndiygnpikriqyeikqikmfkgpekdi
efiytapssavcgvsldvggkkeyliagkaegdgkmhitlcdfivpwdtlsttqkkslnh
ryqmgceckitrcpmipcyisspdeclwmdwvtekninghqakffacikrsdgscawyrg
aa
>d1asza1 2.38.4.1.1 (68-204) Aspartyl-tRNA synthetase (AspRS) {Baker's yeast (Saccharomyces cerevisiae)}
edtakdnygklpliqsrdsdrtgqkrvkfvdldeakdsdkevlfrarvhntrqqgatlaf
ltlrqqasliqglvkankegtisknmvkwagslnlesivlvrgivkkvdepiksatvqnl
eihitkiytisetpeal
>d1b8aa1 2.38.4.1.2 (1-103) Aspartyl-tRNA synthetase (AspRS) {Pyrococcus kodakaraensis}
myrthysseiteelngqkvkvagwvwevkdlggikflwirdrdgivqitapkkkvdpelf
klipklrsedvvavegvvnftpkaklgfeilpekivvlnraet
>d1c0aa1 2.38.4.1.3 (1-106) Aspartyl-tRNA synthetase (AspRS) {Escherichia coli}
mrteycgqlrlshvgqqvtlcgwvnrrrdlgslifidmrdregivqvffdpdradalkla
selrnefciqvtgtvrardekninrdmatgeievlassltiinrad
>d1efwa1 2.38.4.1.4 (1-104) Aspartyl-tRNA synthetase (AspRS) {Thermus thermophilus}
mrrthyagslrethvgeevvlegwvnrrrdlgglifldlrdreglvqlvahpaspayata
ervrpewvvrakglvrlrpepnprlatgrvevelsalevlaeak
>d1lyla1 2.38.4.1.6 (14-153) Lysyl-tRNA synthetase (LysRS) {Escherichia coli, gene lysU}
fndelrnrreklaalrqqgvafpndfrrdhtsdqlheefdakdnqeleslnievsvagrm
mtrrimgkasfvtlqdvggriqlyvardslpegvyndqfkkwdlgdiigargtlfktqtg
elsihctelrlltkalrplp
>d1cuk_3 2.38.4.2.1 (1-64) DNA helicase RuvA subunit, N-terminal domain {Escherichia coli}
migrlrgiiiekqpplvlievggvgyevhmpmtcfyelpeagqeaivfthfvvredaqll
ygfn
>d1bvsa3 2.38.4.2.2 (1-63) DNA helicase RuvA subunit, N-terminal domain {Mycobacterium leprae}
mifsvrgevlevaldhavieaagigyrvnatpsalatlnqgsqarlvtamvvredsmtly
gfs
>d3ulla_ 2.38.4.3.1 ssDNA-binding protein {Human (Homo sapiens), mitochondria}
lerslnrvhllgrvgqdpvlrqvegknpvtifslatnemwrsgdsevyqlgdvsqkttwh
risvfrpglrdvayqyvkkgsriylegkidygeymdknnvrrqattiiadniifl
>d1qvca_ 2.38.4.3.2 ssDNA-binding protein {Escherichia coli}
asrgvnkvilvgnlgqdpevrympnggavanitlatseswrdkatgemkeqtewhrvvlf
gklaevaseylrkgsqvyiegqlrtrkwtdqsgqdryttevvvnvggtmqmlggrqggga
paggnigggqpqggwgqpqqpqggn
>d1ewia_ 2.38.4.3.3 Replication protein A 70 KDa subunit (RPA70) fragment {Human (Homo sapiens)}
mvgqlsegaiaaimqkgdtnikpilqvinirpittgnsppryrllmsdglntlssfmlat
qlnplveeeqlssncvcqihrfivntlkdgrrvvilmelevlksaeavgvkign
>d1jmca1 2.38.4.3.3 (183-298) Replication protein A 70 KDa subunit (RPA70) fragment {Human (Homo sapiens)}
kvvpiasltpyqskwticarvtnksqirtwsnsrgegklfslelvdesgeiratafneqv
dkffplievnkvyyfskgtlkiankqftavkndyemtfnnetsvmpceddhhlptv
>d1jmca2 2.38.4.3.3 (299-420) Replication protein A 70 KDa subunit (RPA70) fragment {Human (Homo sapiens)}
qfdftgiddlenkskdslvdiigicksyedatkitvrsnnrevakrniylmdtsgkvvta
tlwgedadkfdgsrqpvlaikgarvsdfggrslsvlssstiianpdipeayklrgwfdae
gq
>d1quqa_ 2.38.4.3.4 Replication protein A 32 KDa subunit (RPA32) fragment {Human (Homo sapiens)}
hivpctisqllsatlvdevfrignveisqvtivgiirhaekaptnivykiddmtaapmdv
rqwvdtddtssentvvppetyvkvaghlrsfqnkkslvafkimpledmneftthilevin
ahmvlsk
>d1quqb_ 2.38.4.3.5 Replication protein A 14 KDa (RPA14) subunit {Human (Homo sapiens)}
dmmdlprsrinagmlaqfidkpvcfvgrlekihptgkmfilsdgegkngtielmepldee
isgivevvgrvtakatilctsyvqfkedshpfdlglyneavkiihdfpqfyplg
>d1otca1 2.38.4.3.6 (37-204) Telomere end binding protein alpha subunit {Oxytricha nova}
eyvelakasltsaqpqhfyavvidatfpyktnqeryicslkivdptlylkqqkgagdasd
yatlvlyakrfedlpiihragdiirvhratlrlyngqrqfnanvfyssswalfstdkrsv
tqeinnqdavsdttpfsfsskhatiekneisilqnlrkwanqyfssys
>d1otca2 2.38.4.3.6 (205-328) Telomere end binding protein alpha subunit {Oxytricha nova}
vissdmytalnkaqaqkgdfdvvakilqvheldeytnelklkdasgqvfytlslklkfph
vrtgevvrirsatydetstqkkvlilshysniitfiqssklakelrakiqddhsvevasl
kknv
>d1otca3 2.38.4.3.6 (329-495) Telomere end binding protein alpha subunit {Oxytricha nova}
slnavvltevdkkhaalpstslqdlfhhadsdkelqaqdtfrtqfyvtkiepsdvkewvk
gydrktkkssslkgasgkgdnifqvqflvkdastqlnnntyrvllytqdglganffnvka
dnlhknadarkkledsaelltkfnsyvdavverrngfylikdtkliy
>d1otcb_ 2.38.4.3.7 Core domain of telomere end binding protein beta subunit {Oxytricha nova}
qqsafkqlytelfnnegdfskvssnlkkplkcyvkesyphflvtdgyffvapyftkeavn
efhakfpnvnivdltdkvivinnwslelrrvnsaevftsyanlearlivhsfkpnlqerl
nptrypvnlfrddefkttiqhfrhtalqaainktvkgdnlvdiskvadaagkkgkvdagi
vkasaskgdefsdfsfkegntatlkiadifvqe
>d1pysb3 2.38.4.4.1 (39-151) Domain B2 of PheRS-beta, PheT {Thermus thermophilus (Thermus aquaticus)}
fpiprgvvfarvleahpipgtrlkrlvldagrtvevvsgaenarkgigvalalpgtelpg
lgqkvgerviqgvrsfgmalsprelgvgeygggllefpedalppgtplseawp
>d1mjc__ 2.38.4.5.1 Major cold shock protein {Escherichia coli}
sgkmtgivkwfnadkgfgfitpddgskdvfvhfsaiqndgyksldegqkvsftiesgakg
paagnvtsl
>d1c9oa_ 2.38.4.5.3 Major cold shock protein {Bacillus caldolyticus}
mqrgkvkwfnnekgygfieveggsdvfvhftaiqgegfktleegqevsfeivqgnrgpqa
anvvkl
>d1sro__ 2.38.4.5.4 S1 RNA-binding domain of polyribonucleotide phosphorylase, PNP {Escherichia coli}
aeievgrvytgkvtrivdfgafvaigggkeglvhisqiadkrvekvtdylqmgqevpvkv
levdrqgrirlsikea
>d1ah9__ 2.38.4.5.5 Translational initiation factor 1, IF1 {Escherichia coli}
akedniemqgtvletlpntmfrvelenghvvtahisgkmrknyiriltgdkvtveltpyd
lskgrivfrsr
>d1d7qa_ 2.38.4.5.6 Translation initiation factor eIF1a {Human (Homo sapiens)}
pknkgkggknrrrgknenesekrelvfkedgqeyaqvikmlgngrleamcfdgvkrlchi
rgklrkkvwintsdiilvglrdyqdnkadvilkynadearslkaygelpehakinetdtf
gpgdddeiqfddigdddediddi
>d1a62__ 2.38.4.5.7 Rho termination factor, N-terminal, RNA-binding domain {Escherichia coli}
nltelkntpvselitlgenxglenlarxrkqdiifailkqhaksgedifgdgvleilqdg
fgflrsadssylagpddiyvspsqirrfnlrtgdtisgkirppkegeryfallkvnevnf
dkpe
>d2eifa2 2.38.4.5.8 (74-132) C-terminal domain of eukaryotic initiation translation factor 5a {Methanococcus jannaschii}
idrrkgqvlaimgdmvqimdlqtyetlelpipegieglepggeveyieavgqykitrvi
>d1bkb_2 2.38.4.5.9 (75-139) C-terminal domain of eukaryotic initiation translation factor 5a {Pyrobaculum aerophilum}
iiekftaqilsvsgdviqlxdxrdyktievpxkyveeeakgrlapgaevevwqildryki
irvkg
>d1rl2a2 2.38.4.5.10 (60-125) N-terminal domain of ribosomal protein L2 {Bacillus stearothermophilus}
qyriidfkrdkdgipgrvatieydpnrsanialinyadgekryiiapknlkvgxeixsgp
dadiki
>d1ckma1 2.38.4.6.1 (239-327) RNA guanylyltransferase (mRNA capping enzyme) {Chlorella virus, PBCV-1}
thhtidfiimsedgtigifdpnlrknvpvgkldgyynkgsivecgfadgtwkyiqgrsdk
nqandrltyektllnieenitidelldlf
>d1a0i_1 2.38.4.6.2 (241-349) ATP-dependent DNA ligase {Bacteriophage T7}
peneadgiiqglvwgtkglanegkvigfevllesgrlvnatnisralmdeftetvkeatl
sqwgffspygigdndactinpydgwacqisymeetpdgslrhpsfvmfr
>d1rip__ 2.38.4.7.1 Ribosomal S17 protein {Bacillus stearothermophilus}
qrkvyvgrvvsdkmdktitvlvetykkhplygkrvkyskkykahdehneakvgdivkime
trplsatkrfrlveivekavr
>d1gvp__ 2.38.4.8.1 Gene V protein {Bacteriophage f1}
mikveikpsqaqfttrsgvsrqgkpyslneqlcyvdlgneypvlvkitldegqpayapgl
ytvhlssfkvgqfgslmidrlrlvpak
>d1pfsa_ 2.38.4.8.2 Gene V protein {Phage pf3 (Pseudomonas)}
mniqitftdsvrqgtsakgnpytfqegflhledkphplqcqffvesvipagsyqvpyrin
vnngrpelafdfkamkra
>d1gpc__ 2.38.4.8.3 Gene 32 protein (GP32) core {Bacteriophage T4}
gfssedkgewklkldnagngqavirflpskndeqapfailvnhgfkkngkwyietcssth
gdydscpvcqyiskndlyntdnkeyslvkrktsywanilvvkdpaapenegkvfkyrfgk
kiwdkinamiavdvemgetpvdvtcpweganfvlkvkqvsgfsnydeskflnqsaipnid
desfqkelfeqmvdlsemtskdkfksfeelntkfgqvm
>d1a1d__ 2.38.4.9.1 RNA polymerase subunit RBP8 {Baker's yeast (Saccharomyces cerevisiae)}
msntlfddifqvsevdpgrynkvcrieaasttqdqckltldinvelfpvaaqdsltvtia
sslnledtpandssatrswrppqagdrsladdydyvmygtaykfeevskdliavyysfgg
llmrlegnyrnlnnlkqenayllirr
>d8prka_ 2.38.5.1.1 Inorganic pyrophosphatase {Baker's yeast (Saccharomyces cerevisiae)}
tyttrqigakntleykvyiekdgkpvsafhdiplyadkennifnmvveiprwtnakleit
keetlnpiiqdtkkgklkfvrncfphhgyihnygafpqtwedpnvshpetkavgdndpid
vleigetiaytgqvkqvkalgimalldegetdwkviaidindplapklndiedvekyfpg
llratnewfriykipdgkpenqfafsgeaknkkyaldiikethdswkqliagkssdskgi
dltnvtlpdtptyskaasdaippaslkadapidksidkwffi
>d1obwa_ 2.38.5.1.3 Inorganic pyrophosphatase {Escherichia coli}
sllnvpagkdlpediyvvieipanadpikyeidkesgalfvdrfmstamfypcnygyinh
tlsldgdpvdvlvptpyplqpgsvtrcrpvgvlkmtdeagedaklvavphsklskeydhi
kdvndlpellkaqiahffehykdlekgkwvkvegwenaeaakaeivasferaknk
>d1b9ma2 2.38.6.1.1 (127-262) C-terminal domain of molybdate-dependent transcriptional regulator ModE {Escherichia coli}
arnqwfgtitardhddvqqhvdvlladgktrlkvaitaqsgarlgldegkevlillkapw
vgitqdeavaqnadnqlpgiishiergaeqcevlxalpdgqtlcatvpvneatslqqgqn
vtayfnadsviiatlc
>d1b3qa2 2.38.7.1.1 (540-671) Histidine kinase CheA, C-terminal domain {Thermotoga maritima}
tlaiicallvkvnnlvyaipianidtilsiskediqrvqdrdvivirgevipvyrlwevl
qiehkeeleemeavivrvgnrkygivvddllgqddivikslgkvfsevkefsgaailgdg
sialiinvsgiv
>d1qovh1 2.39.1.1.2 (36-250) Photosynthetic reaction centre {Rhodobacter sphaeroides}
mregyplenedgtpaanqgpfplpkpktfilphgrgtltvpgpesedrpialartavseg
fphaptgdpmkdgvgpaswvarrdlpeldghghnkikpmkaaagfhvsagknpiglpvrg
cdleiagkvvdiwvdipeqmarflevelkdgstrllpmqmvkvqsnrvhvnalssdlfag
iptiksptevtlleedkicgyvagglmyaapkrks
>d1bfg__ 2.40.1.1.1 Basic FGF (FGF2) {Human (Homo sapiens)}
dpkrlycknggfflrihpdgrvdgvreksdphiklqlqaeergvvsikgvsanrylamke
dgrllasksvtdecffferlesnnyntyrsrkytswyvalkrtgqyklgsktgpgqkail
flpmsa
>d1qqla_ 2.40.1.1.4 Keratinocyte growth factor, FGF7 {Rat (Rattus norvegicus)}
dirvrrlfcrtqwylridkrgkvkgtqemrnsynimeirtvavgivaikgveseyylamn
kegklyakqtpneeclflerleenhyntyiskkhaeknwfvglkkngsckrgprthygqk
ailflplpvss
>d1i1b__ 2.40.1.2.1 Interleukin-1beta {Human (Homo sapiens)}
vrslnctlrdsqqkslvmsgpyelkalhlqgqdmeqqvvfsmsfvqgeesndkipvalgl
keknlylscvlkddkptlqlesvdpknypkkkmekrfvfnkieinnklefesaqfpnwyi
stsqaenmpvflggtkggqditdftmqfvss
>d1ilr1_ 2.40.1.2.3 Interleukin-1 receptor antagonist protein {Human (Homo sapiens)}
skmqafriwdvnqktfylrnnqlvagylqgpnvnleekidvvpiephalflgihggkmcl
scvksgdetrlqleavnitdlsenrkqdkrfafirsdsgpttsfesaacpgwflctamea
dqpvsltnmpdegvmvtkfyfqede
>d2ila__ 2.40.1.2.4 Interleukin-1alpha {Human (Homo sapiens)}
nvkynfmriikyefilndalnqsiiranaqyltaaalhnldeavkfdmgayksskddaki
tvilrisktqlyvtaqdedqpvllkempeipktitgsetnllffwethgtknyftsvahp
nlfiatkqdywvclaggppsitdfqile
>d1abrb1 2.40.2.1.2 (1-140) Plant cytotoxin B-chain (lectin) {Abrus precatorius}
ivekskicssryeptvriggrdgmcvdvydngyhngnriimwkckdrleenqlwtlksdk
tirsngkclttygyapgsyvmiydctsavaeatyweiwdngtiinpksalvlsaesssmg
gtltvqtneylmrqgwrtgn
>d1abrb2 2.40.2.1.2 (141-267) Plant cytotoxin B-chain (lectin) {Abrus precatorius}
ntspfvtsisgysdlcmqaqgsnvwmadcdsnkkeqqwalytdgsirsvqntnncltskd
hkqgstillmgcsngwasqrwvfkndgsiyslyddmvmdvkgsdpslkqiilwpytgkpn
qiwltlf
>d1ce7b2 2.40.2.1.3 (134-255) Plant cytotoxin B-chain (lectin) {European mistletoe (Viscum album)}
taprevtiygfndlcmesgggsvtvetcssgkadkwalygdgsirpeqnqaqcltsggds
vagvnivscsgaasgqrwvftnegailnlknglamdvanpgggriiiypatgkpnqmwlp
vf
>d1xyfa1 2.40.2.1.4 (313-436) Endo-1,4-beta-xylanase C-terminal domain {Streptomyces olivaceoviridis}
gqikgvgsgrcldvpnasttdgtqvqlydchsatnqqwtytdagelrvygdkcldaagtg
ngtkvqiyscwggdnqkwrlnsdgsivgvqsglcldavgggtangtliqlyscsngsnqr
wtrt
>d1dqga_ 2.40.2.2.1 Mannose receptor {Mouse (Mus musculus)}
darqfliynedhkrcvdalsaisvqtatcnpeaesqkfrwvsdsqimsvafklclgvpsk
tdwasvtlyacdskseyqkweckndtlfgikgtelyfnygnrqekniklykgsglwsrwk
vygttddlcsrgye
>d1jlxa1 2.40.3.1.1 (1-153) Agglutinin {Love-lies-bleeding (Amaranthus caudatus)}
aglpvimclksnnhqkylryqsdniqqygllqfsadkildplaqfevepsktydglvhik
srytnkylvrwspnhywitasanepdenksnwactlfkplyveegnmkkvrllhvqlghy
tqnytvggsfvsylfaessqidtgskdvfhvid
>d1jlxa2 2.40.3.1.1 (154-299) Agglutinin {Love-lies-bleeding (Amaranthus caudatus)}
wksifqfpkgyvtfkgnngkylgvitinqlpclqfgydnlndpkvahqmfvtsngticik
snymnkfwrlstddwilvdgndpretneaaalfrsdvhdfnvisllnmqktwfikrftsg
kpgfincmnaatqnvdetaileiiel
>d1wba__ 2.40.4.1.1 Winged bean albumin 1 {Goa bean (Psophocarpus tetragonolobus)}
ddpvydaegnklvnrgkytivsfsdgagidvvatgnenpedplsivkstrnimyatsiss
edktppqprnilenmrlkinfatdphkgdvwsvvdfqpdgqqlklagrypnqvkgaftiq
kgsntprtykllfcpvgspcknigistdpegkkrlvvsyqsdplvvkfhrh
>d1eyla_ 2.40.4.1.3 chymotrypsin inhibitor WCI {Winged bean (Psophocarpus tetragonolobus)}
efdddlvdaegnlvenggtyyllphiwahgggietaktgnepcpltvvrspnevskgepi
rissqflslfiprgslvalgfanppscaaspwwtvvdspqgpavklsqqklpekdilvfk
fekvshsnihvykllycqhdeedvkcdqyigihrdrngnrrlvvteenplelvllkaks
>d1avwb_ 2.40.4.1.4 Soybean trypsin inhibitor {Soybean (Glycine max)}
dfvldnegnplenggtyyilsditafggiraaptgnercpltvvqsrneldkgigtiiss
pyrirfiaeghplslkfdsfavimlcvgiptewsvvedlpegpavkigenkdamdgwfrl
ervsefnnyklvfcpqdkcgdigisidhddgtrrlvvsknkplvvqfqkld
>d1avac_ 2.40.4.1.5 Amylase/subtilisin inhibitor {Barley (Hordeum vulgare), seed}
adpppvhdtdghelradanyyvlsanrahgggltmapghgrhcplfvsqdpngqhdgfpv
ritpygvapsdkiirlstdvrisfrayttclqstewhidselaagrrhvitgpvkdpsps
grenafriekysgaevheyklmscgdwcqdlgvfrdlkggawflgatepyhvvvfkkapp
a
>d1a8d_2 2.40.4.2.1 (248-452) Tetanus neurotoxin {Clostridium tetani}
itflrdfwgnplrydteyylipvassskdvqlknitdymyltnapsytngklniyyrrly
nglkfiikrytpnneidsfvksgdfiklyvsynnnehivgypkdgnafnnldrilrvgyn
apgiplykkmeavklrdlktysvqlklyddknaslglvgthngqigndpnrdiliasnwy
fnhlkdkilgcdwyfvptdegwtnd
>d3btaa2 2.40.4.2.2 (1079-1295) Botulinum neurotoxin serotype A {Clostridium botulinum}
nekeikdlydnqsnsgilkdfwgdylqydkpyymlnlydpnkyvdvnnvgirgymylkgp
rgsvmttniylnsslyrgtkfiikkyasgnkdnivrnndrvyinvvvknkeyrlatnasq
agvekilsaleipdvgnlsqvvvmkskndqgitnkckmnlqdnngndigfigfhqfnnia
klvasnwynrqierssrtlgcswefipvddgwgerpl
>d1hcd__ 2.40.5.1.1 Histidine-rich actin-binding protein (hisactophilin) {Dictyostelium discoideum}
mgnrafkshhghflsaegeavkthhghhdhhthfhvenhggkvalkthcgkylsigdhkq
vylshhlhgdhslfhlehhggkvsikghhhhyisadhhghvstkehhdhdttfeeiii
>d1fnc_1 2.41.1.1.1 (19-154) Ferredoxin reductase (flavodoxin reductase) {Spinach (Spinacia oleracea)}
hskkmeegitvnkfkpktpyvgrcllntkitgddapgetwhmvfshegeipyregqsvgv
ipdgedkngkphklrlysiassalgdfgdaksvslcvkrliytndagetikgvcsnflcd
lkpgaevkltgpvgke
>d1fdr_1 2.41.1.1.4 (2-100) Ferredoxin reductase (flavodoxin reductase) {Escherichia coli}
adwvtgkvtkvqnwtdalfsltvhapvlpftagqftklgleidgervqraysyvnspdnp
dlefylvtvpdgklsprlaalkpgdevqvvseaagffvl
>d1a8p_1 2.41.1.1.5 (2-100) Ferredoxin reductase (flavodoxin reductase) {Azotobacter vinelandii}
snlnvervlsvhhwndtlfsfkttrnpslrfengqfvmiglevdgrplmraysiaspnye
ehleffsikvqngpltsrlqhlkegdelmvsrkptgtlv
>d1qfja1 2.41.1.1.6 (1-97) NAD(P)H:flavin oxidoreductase {Escherichia coli}
ttlsckvtsveaitdtvyrvrivpdaafsfragqylmvvmderdkrpfsmastpdekgfi
elhigaseinlyakavmdrilkdhqivvdiphgeawl
>d2cnd_1 2.41.1.1.7 (11-124) Nitrate reductase core domain {Corn (Zea mays)}
grihcrlvakkelsrdvrlfrfslpspdqvlglpigkhifvcatiegklcmraytptsmv
deighfdllvkvyfknehpkfpngglmtqyldslpvgsyidvkgplghveytgr
>d2pia_1 2.41.1.2.1 (1-103) Phthalate dioxygenase reductase {Pseudomonas cepacia, db01}
ttpqedgflrlkiaskekiardiwsfeltdpqgaplppfeaganltvavpngsrrtyslc
ndsqernryviavkrdsngrggsisfiddtsegdavevslprn
>d1cqxa2 2.41.1.3.1 (151-261) Flavohemoglobin, central domain {Alcaligenes eutrophus}
wkgwrtfvirekrpesdvitsfilepadggpvvnfepgqytsvaidvpalglqqirqysl
sdmpngrtyrisvkregggpqppgyvsnllhdhvnvgdqvklaapygsfhi
>d1amoa1 2.41.1.4.1 (243-518) NADPH-cytochrome p450 reductase {Rat (Rattus norvegicus)}
rqyelvvhedmdvakvytgemgrlksyenqkppfdaknpflaavtanrklnqgterhlmh
leldisdskiryesgdhvavypandsalvnqigeilgadldvimslnnldeesnkkhpfp
cpttyrtaltyylditnpprtnvlyelaqyasepseqehlhkmasssgegkelylswvve
arrhilailqdypslrppidhlcellprlqaryysiassskvhpnsvhicavaveyeaks
grvnkgvatswlrakepagenggralvpmfvrksqf
>d1flma_ 2.41.1.5.1 FMN-binding protein {Desulfovibrio vulgaris, strain Miyazaki F}
mlpgtffevlknegvvaiatqgedgphlvntwnsylkvldgnrivvpvggmhkteanvar
dervlmtlgsrkvagrngpgtgflirgsaafrtdgpefeaiarfkwaraalvitvvsaeq
tl
>d1dnla_ 2.41.1.5.3 Pyridoxine 5'-phoshate oxidase (PNP oxidase) {Escherichia coli}
gglrrrdlpadpltlferwlsqaceakladptaxvvatvdehgqpyqrivllkhydekgx
vfytnlgsrkahqiennprvsllfpwhtlerqvxvigkaerlstlevxkyfhsrprdsqi
gawvskqssrisargileskflelkqkfqqgevplpsfwggfrvsleqiefwqggehrlh
drflyqrendawkidrlap
>d1fuia1 2.41.2.1.1 (356-591) L-fucose isomerase, C-terminal domain {Escherichia coli}
aqvfadvrtywspeaiervtghkldglaehgiihlinsgsaaldgsckqrdsegnptmkp
hweisqqeadaclaatewcpaiheyfrgggyssrflteggvpftmtrvniikglgpvlqi
aegwsvelpkdvhdilnkrtnstwpttwfaprltgkgpftdvysvmanwganhgvltigh
vgadfitlasmlripvcmhnveetkvyrpsawaahgmdiegqdyracqnygplykr
>d1exma1 2.41.3.1.3 (213-312) Elongation factor Tu (EF-Tu), domain 2 {Thermus thermophilus}
pvrdvdkpflmpvedvftitgrgtvatgriergkvkvgdeveivglapetrktvvtgvem
hrktlqegiagdnvgvllrgvsreevergqvlakpgsitp
>d1dar_1 2.41.3.1.5 (283-400) Elongation factor G (EF-G), domain II {Thermus thermophilus}
pldippikgttpegevveihpdpngplaalafkimadpyvgrltfirvysgtltsgsyvy
nttkgrkervarllrmhanhreeveelkagdlgavvglketitgdtlvgedaprvile
>d1exma2 2.42.1.1.3 (313-405) Elongation factor Tu (EF-Tu), C-terminal domain {Thermus thermophilus}
htkfeasvyvlkkeeggrhtgffsgyrpqfyfrttdvtgvvqlppgvemvmpgdnvtftv
elikpvaleeglrfaireggrtvgagvvtkile
>d1d2ea2 2.42.1.1.4 (349-451) Elongation factor Tu (EF-Tu), C-terminal domain {Bovine (Bos taurus), mitochondrial}
hqkveaqvyiltkeeggrhkpfvshfmpvmfsltwdmacriilppgkelampgedlkltl
ilrqpmilekgqrftlrdgnrtigtglvtdtpamteedknikw
>d1fmta1 2.43.1.1.1 (207-314) Methionyl-tRNAfmet formyltransferase, C-terminal domain {Escherichia coli}
lskeearidwslsaaqlercirafnpwpmswleiegqpvkvwkasvidtatnaapgtile
ankqgiqvatgdgilnllslqpagkkamsaqdllnsrrewfvpgnrlv
>d1bnka_ 2.43.1.2.1 3-methyladenine DNA glycosylase (AAG, ANPG, MPG) {Human (Homo sapiens)}
kghltrlgleffdqpavplaraflgqvlvrrlpngtelrgriveteaylgpedeaahsrg
grqtprnrgmfmkpgtlyvyiiygmyfcmnissqgdgacvllraleplegletmrhvrsq
lrkgtasrvlkdrelcsgpsklcqalainksfdqrdlaqdeavwlergplepsepavvaa
arvgvghagewarkplrfyvrgspwvsvvdrvaeqd
>d1arb__ 2.44.1.1.1 Achromobacter protease {Achromobacter lyticus, strain m497-1}
gvsgscnidvvcpegdgrrdiiravgaysksgtlactgslvnntandrkmyfltahhcgm
gtastaasivvywnyqnstcrapntpasgangdgsmsqtqsgstvkatyatsdftlleln
naanpafnlfwagwdrrdqnypgaiaihhpnvaekrisnstsptsfvawgggagtthlnv
qwqpsggvtepgssgspiyspekrvlgqlhggpsscsatgtnrsdqygrvftswtgggaa
asrlsdwldpastgaqfidglds
>d1qq4a_ 2.44.1.1.2 alpha-Lytic protease {Lysobacter enzymogenes, 495}
anivggieysinnaslcsvgfsvtrgatkgfvtaghcgtvnatariggavvgtfaarvfp
gndrawvsltsaqtllprvangssfvtvrgsteaavgaavchsgrttgyqcgtitaknvt
anyaegavrgltqsnacmgrgdsggswitsagqaqgvmsggnvqsngnncgipasqrssl
ferlqpilsqyglslvtg
>d1sgpe_ 2.44.1.1.7 Protease B {Streptomyces griseus, strain k1}
isggdaiysstgrcslgfnvrsgstyyfltaghctdgattwwansarttvlgttsgssfp
nndygivrytnttipkdgtvggqditsaanatvgmavtrrgsttgthsgsvtalnatvny
gggdvvygmirtnvcaepgdsggplysgtraigltsggsgncssggttffqpvtealvay
gvsvy
>d1agja_ 2.44.1.1.8 Epidermolytic (exfoliative) toxin A {Staphylococcus aureus}
evsaeeikkheekwnkyygvnafnlpkelfskvdekdrqkypyntignvfvkgqtsatgv
ligkntvltnrhiakfangdpskvsfrpsintddngntetpygeyevkeilqepfgagvd
lalirlkpdqngvslgdkispakigtsndlkdgdkleligypfdhkvnqmhrseielttl
srglryygftvpgnsgsgifnsngelvgihsskvshldrehqinygvgignyvkriinek
ne
>e1ept.1a 2.44.1.2.2 Trypsin(ogen) {Porcine (Sus scrofa)}
ivggytcaansipyqvslnsgshfcggslinsqwvvsaahcyk
>e1ept.1b 2.44.1.2.2 Trypsin(ogen) {Porcine (Sus scrofa)}
sriqvrlgehnidvlegneqfinaakiithpnfngntldndimliklsspatlnsrvatv
slprscaaagteclisgwgntk
>e1ept.1c 2.44.1.2.2 Trypsin(ogen) {Porcine (Sus scrofa)}
ssgssypsllqclkapvlsnssckssypgqitgnmicvgflqggkdscqgdsggpvvcng
qlqgivswgygcaqknkpgvytkvcnyvnwiqqtiaan
>d1try__ 2.44.1.2.6 Trypsin(ogen) {Mold (Fusarium oxysporum)}
ivggtsasagdfpfivsisrnggpwcggsllnantvltaahcvsgyaqsgfqiragslsr
tsggitsslssvrvhpsysgnnndlailklstsipsggnigyarlaasgsdpvagssatv
agwgatseggsstpvnllkvtvpivsratcraqygtsaitnqmfcagvssggkdscqgds
ggpivdssntligavswgngcarpnysgvyasvgalrsfidtya
>e1ab9.1b 2.44.1.2.7 (alpha,gamma)-chymotrypsin(ogen) {Bovine (Bos taurus)}
ivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgvttsdvvvagefdqgs
ssekiqklkiakvfknskynsltinnditllklstaasfsqtvsavclpsasddfaagtt
cvttgwgltry
>e1ab9.1c 2.44.1.2.7 (alpha,gamma)-chymotrypsin(ogen) {Bovine (Bos taurus)}
ntpdrlqqaslpllsntnckkywgtkikdamicagasgvsscmgdsggplvckkngawtl
vgivswgsstcststpgvyarvtalvnwvqqtlaan
>d2hlca_ 2.44.1.2.10 HL collagenase {Common cattle grub (Hypoderma lineatum)}
iingyeaytglfpyqaglditlqdqrrvwcggslidnkwiltaahcvhdavsvvvylgsa
vqyegeavvnseriishsmfnpdtylndvalikiphveytdniqpirlpsgeelnnkfen
iwatvsgwgqsntdtvilqytynlvidndrcaqeyppgiivesticgdtsdgkspcfgds
ggpfvlsdknlligvvsfvsgagcesgkpvgfsrvtsymdwiqqntgikf
>d1dx5d_ 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1a2c.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1a3b.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1a3e.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1a46.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
dcglrplfekksledkterellesyi
>e1a4w.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
dcglrplfekksledkterellesyi
>e1a5g.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1a61.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1abi.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
sgeadcglrplfekksledkterellesyidgr
>e1abj.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1ad8.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
eadcglrplfekksledkterellesyi
>e1ae8.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1afe.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1aht.1h 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1aht.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
eadcglrplfekksledkterellesyi
>e1ai8.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1aix.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1awf.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1awh.1a 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1awh.2c 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1ay6.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
geadcglrplfekksledkterellesyi
>e1b5g.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
eadcglrplfekksledkterellesyid
>e1b7x.1a 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1ba8.1a 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
sgeadcglrplfekksledkterellesyi
>e1bb0.1a 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1bcu.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1bhx.1a 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
sgeadcglrplfekksledkterellesyi
>e1ca8.1a 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1d4p.1a 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
eadcglrplfekksledkterellesyi
>e1dm4.1a 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyi
>e1dwb.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
eadcglrplfekksledkterellesyid
>e1dwc.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
eadcglrplfekksledkterellesyid
>e1dwd.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
eadcglrplfekksledkterellesyid
>e1dwe.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
eadcglrplfekksledkterellesyi
>e1dx5.1a 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1dx5.2b 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1dx5.3c 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1fpc.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
dcglrplfekksledkterellesyi
>e1fph.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1hah.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1hai.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1hao.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1hap.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1hbt.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1hgt.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1hlt.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1hlt.2j 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1hut.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1hxe.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
dcglrplfekksledkterellesyi
>e1hxf.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
dcglrplfekksledkterellesyi
>e1ihs.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
geadcglrplfekksledkterellesyid
>e1iht.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
geadcglrplfekksledkterellesyid
>e1lhc.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1lhd.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1lhe.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1lhf.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1lhg.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1nrn.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
dcglrplfekksledkterellesyidgr
>e1nro.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
dcglrplfekksledkterellesyidgr
>e1nrp.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
dcglrplfekksledkterellesyidgr
>e1nrq.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
dcglrplfekksledkterelle
>e1nrr.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1nrs.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1ppb.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1qbv.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1qhr.1a 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1qj1.1a 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1qj6.1a 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1qj7.1a 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1qur.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1tbz.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
cglrplfekksledkterellesyi
>e1thp.1a 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1thr.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1ths.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
sgeadcglrplfekksledkterellesyidgr
>e1tmb.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
geadcglrplfekksledkterellesyi
>e1tmt.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1tmu.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
eadcglrplfekksledkterellesyi
>e1tom.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1uma.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1vit.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1vit.2m 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1vr1.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e2hgt.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
sgeadcglrplfekksledkterellesyidgr
>e2hnt.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyid
>e2hpp.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
geadcglrplfekksledkterellesyid
>e2hpq.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
geadcglrplfekksledkterellesyid
>e2thf.1a 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
dcglrplfekksledkterellesyi
>e3hat.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e3htc.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
gsgeadcglrplfekksledkterellesyidgr
>e4htc.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
gsgeadcglrplfekksledkterellesyidg
>e4thn.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e5gds.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e7kme.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
dcglrplfekksledkterellesy
>e8kme.11 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1a0h.1a 2.44.1.2.12 (271-320) Thrombin {Bovine (Bos taurus)}
rtsedhfqpffnektfgageadcglrplfekkqvqdqtekelfesyiegr
>e1a0h.2d 2.44.1.2.12 (271-320) Thrombin {Bovine (Bos taurus)}
rtsedhfqpffnektfgageadcglrplfekkqvqdqtekelfesyiegr
>e1avg.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
ffnektfgageadcglrplfekkqvqdqtekelfesyiegr
>e1bbr.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1bbr.2j 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1bbr.3m 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1bmm.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
geadcglrplfekksledkterellesy
>e1bmn.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
adcglrplfekksledkterellesy
>e1bth.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
geadcglrplfekksledkterellesyidg
>e1bth.2j 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
geadcglrplfekksledkterellesyidg
>e1dit.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
geadcglrplfekksledkterellesyi
>e1etr.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1ets.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1ett.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1hdt.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
sgeadcglrplfekksledkterellesyidgr
>e1hrt.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1mkw.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
eadcglrplfekkqvqdqtekelfesyie
>e1mkx.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
eadcglrplfekkqvqdqtekelfesyie
>e1tbq.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
tsedhfqpffnektfgageadcglrplfekkqvqdqtekelfesyiegr
>e1tbq.2j 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
tsedhfqpffnektfgageadcglrplfekkqvqdqtekelfesyiegr
>e1tbr.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
tsedhfqpffnektfgageadcglrplfekkqvqdqtekelfesyiegr
>e1tbr.2j 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
tsedhfqpffnektfgageadcglrplfekkqvqdqtekelfesyiegr
>e1toc.1a 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
adcglrplfekkqvqdqtekelfesyie
>e1toc.2c 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
adcglrplfekkqvqdqtekelfesyie
>e1toc.3e 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
adcglrplfekkqvqdqtekelfesyie
>e1toc.4g 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
adcglrplfekkqvqdqtekelfesyie
>e1ucy.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1ucy.2j 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1ucy.3m 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1uvs.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
adcglrplfekksledkterellesyi
>e1uvt.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
cglrplfekkqvqdqtekelfesyi
>e1uvu.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
cglrplfekkqvqdqtekelfesy
>e1ycp.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
adcglrplfekkqvqdqtekelfesyieg
>e1ycp.2j 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
adcglrplfekkqvqdqtekelfesyieg
>d1qnja_ 2.44.1.2.15 Elastase {Porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqndgteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1a7s__ 2.44.1.2.18 Heparin binding protein, HBP {Human (Homo sapiens)}
ivggrkarprqfpflasiqnqgrhfcggaliharfvmtaascfpgvstvvlgaydlrrre
rqsrqtfsissmsengydpqqnlndlmllqldreanltssvtilplplqnatveagtrcq
vagwgsqrsggrlsrfprfvnvtvtpedqcrpnnvctgvltrrggicngdggtplvcegl
ahgvasfslgpcgrgpdfftrvalfrdwidgvlnnpgpgpa
>e2pka.1a 2.44.1.2.24 Kallikrein A {Porcine (Sus scrofa)}
iiggreceknshpwqvaiyhyssfqcggvlvnpkwvltaahckndnyevwlgrhnlfene
ntaqffgvtadfphpgfnls
>e2pka.1b 2.44.1.2.24 Kallikrein A {Porcine (Sus scrofa)}
adgkdyshdlmllrlqspakitdavkvlelptqepelgstceasgwgsiepgpddfefpd
eiqcvqltllqntfcadahpdkvtesmlcagylpggkdtcmgdsggplicngmwqgitsw
ghtpcgsankpsiytklifyldwiddtitenp
>d1ejna_ 2.44.1.2.40 Urokinase-type plasminogen activator (LMW U-PA), catalytic domain {Human (Homo sapiens)}
iiggefttienqpwfaaiyrrhrggsvtyvcggslispcwvisathcfidypkkedyivy
lgrsrlnsntqgemkfevenlilhkdysadtlahhndiallkirskegrcaqpsrtiqti
slpsmyndpqfgtsceitgfgkenstdylypeqlkmtvvklishrecqqphyygsevttk
mlcaadpqwktdscqgdsggplvcslqgrmtltgivswgrgcalkdkpgvytrvshflpw
irshtke
>d1svpa_ 2.44.1.3.1 Viral capsid protein {Sindbis virus}
alkleadrlfdvknedgdvighalamegkvmkplhvkgtidhpvlsklkftkssaydmef
aqlpvnmrseaftytsehpegfynwhhgavqysggrftiprgvggrgdagrpimdnsgrv
vaivlggadegtrtalsvvtwnskgktikttpegteewsa
>e1a1r.2d 2.44.1.3.3 NS3 protease {Human hepatitis C virus, Bk strain}
kgsvvivgrivlsgkpaiipk
>e1jxp.1a 2.44.1.3.3 NS3 protease {Human hepatitis C virus, Bk strain}
itaysqqtrgllgciitsltgrdknqvegevqvvstatqsflatcvngvcwtvyhgagsk
tlagpkgpitqmytnvdqdlvgwqappgarsltpctcgssdlylvtrhadvipvrrrgds
rgsllsprpvsylkgssggpllcpsghavgifraavctrgvakavdfvpvesmettm
>d1befa_ 2.44.1.3.4 NS3 protease {Dengue virus serotype 2}
wdvpspppvgkaeledgayrikqkgilgysqigagvykegtfhtmwhvtrgavlmhkgkr
iepswadvkkdlvscgggwklegewkegeevqvlalepgknpravqtkpglfktnagtig
avsldfspgtsgspiidkkgkvvgiygngvvtrsgayvsaiaqteksiednpeiedd
>d1cqqa_ 2.44.1.4.1 3C cysteine protease (picornain 3C) {Human type 2 rhinovirus}
gpeeefgmslikhnscvittengkftglgvydrfvvvpthadpgkeiqvdgittkvidsy
dlynkngikleitvlkldrnekfrdirryipnneddypncnlallanqpeptiinvgdvv
sygnillsgnqtarmlkysyptksgycggvlykigqvlgihvggngrdgfsamllrsyft
>d1hava_ 2.44.1.4.2 3C cysteine protease (picornain 3C) {Human hepatitis A virus}
stleiaglvrknlvqfgvgekngsvrwvmnalgvkddwllvpshaykfekdyemmefyfn
rggtyysisagnvviqsldvgfqdvvlmkvptipkfrditqhfikkgdvpralnrlatlv
ttvngtpmlisegplkmeekatyvhkkndgttvdltvdqawrgkgeglpgmcggalvssn
qsiqnailgihvaggnsilvaklvtqemfqnidkki
>d2hrva_ 2.44.1.4.3 2A cysteine proteinase {Human rhinovirus 2}
gpsdmyvhvgnliyrnlhlfnsemhesilvsyssdliiyrtntvgddyipscdctqatyy
ckhknryfpitvtshdwyeiqeseyypkhiqynlligegpcepgdcggkllckhgvigiv
taggdnhvafidlrhfhca
>d1bco_1 2.45.1.1.1 (481-560) mu transposase, C-terminal domain {Bacteriophage mu}
teeqkrmlllpaeavnvsrkgeftlkvggslkgaknvyynmalmnagvkkvvvrfdpqql
hstvycytldgrficeaecl
>d1bmfa2 2.46.1.1.1 (24-94) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
dleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgndklik
egdivkrtgai
>d1bmfd2 2.46.1.1.1 (9-81) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1skyb2 2.46.1.1.3 (21-95) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bacillus ps3}
sqiqvsdvgtviqvgdgiarahgldnvmsgeavefanavmgmalnleennvgivilgpyt
gikegdevrrtgrim
>d1skye2 2.46.1.1.3 (1-82) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bacillus ps3}
mtrgrviqvmgpvvdvkfenghlpaiynalkiqhkarnenevdidltlevalhlgddtvr
tiamastdglirgmevidtgap
>d1bd0a1 2.46.2.1.1 (2-11,245-382) Alanine racemase {Bacillus stearothermophilus}
ndfhrdtwaeXfslhsrlvhvkklqpgekvsygatytaqteewigtipigyadgwlrrlq
hfhvlvdgqkapivgricmdqcmirlpgplpvgtkvtligrqgdevisiddvarhletin
yevpctisyrvpriffrhkrimevrnaig
>d7odca1 2.46.2.1.2 (2-43,284-418) Eukaryotic ornithine decarboxylase {Mouse (Mus musculus)}
ssftkdefdchildegftakdildqkinevsssddkdafyvaXftlavniiakktvwkeq
pgsddedesneqtfmyyvndgvygsfncilydhahvkallqkrpkpdekyysssiwgptc
dgldrivercnlpemhvgdwmlfenmgaytvaaastfngfqrpniyyvmsrpmwqlmk
>d1dazc_ 2.47.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwkrplvtikiggqlkealldtgaddtvieemslpgrwkpimiggiggfikvrqyd
qiiieiaghkaigtvlvgptpvniigrnlltqigatlnf
>d4fiv__ 2.47.1.1.2 Feline immunodeficiency virus (FIV) protease {Feline (Felis catus), immunodeficiency virus}
vgttttlekrpeilifvngypikflldtgaditilnrrdfqvknsiengrqnmigvgggk
rgtnyinvhleirdenyktqcifgnvcvlednsliqpllgrdnmikfnirlvm
>d1idaa_ 2.47.1.1.3 Human immunodeficiency virus type 2 protease {Rod isolate, HIV-2}
pqfslwkrpvvtayiegqpvevlldtgaddsivagielgnnyspkivggiggfintkeyk
nveievlnkkvratimtgdtpinifgrniltalgmslnl
>d2rspa_ 2.47.1.1.4 Rous sarcoma virus protease {Rous sarcoma virus, strain pr-C}
lamtmehkdrplvrviltntgshpvkqrsvyitalldsgaditiiseedwptdwpvmeaa
npqihgigggipmrksrdmielgvinrdgslerplllfpavamvrgsilgrdclqglglr
ltnl
>d1fmb__ 2.47.1.1.7 EIAV protease {Equine infection anemia virus, EIAV}
vtynlekrpttivlindtplnvlldtgadtsvlttahynrlkyrgrkyqgtgiggvggnv
etfstpvtikkkgrhiktrmlvadipvtilgrdilqdlgaklvl
>d1bxoa_ 2.47.1.2.2 Acid protease {Fungus (Penicillium janthinellum), penicillopepsin}
aasgvatntptandeeyitpvtiggttlnlnfdtgsadlwvfstelpasqqsghsvynps
atgkelsgytwsisygdgssasgnvftdsvtvggvtahgqavqaaqqisaqfqqdtnndg
llglafssintvqpqsqttffdtvksslaqplfavalkhqqpgvydfgfidsskytgslt
ytgvdnsqgfwsfnvdsytagsqsgdgfsgiadtgttllllddsvvsqyysqvsgaqqds
naggyvfdcstnlpdfsvsisgytatvpgslinygpsgdgstclggiqsnsgigfsifgd
iflksqyvvfdsdgpqlgfapqa
>d1zap__ 2.47.1.2.5 Acid protease {Yeast (Candida albicans)}
qavpvtlhneqvtyaaditvgsnnqklnvivdtgssdlwvpdvnidcqvtysdqtadfck
qkgtydpsgssasqdlntpfsigygdgsssqgtlykdtvgfggvsiknqvladvdstsid
qgilgvgyktneaggsydnvpvtlkkqgviaknayslylnspdsatgqiifggvdnakys
gslialpvtsdrelrislgsvevsgktintdnvdvlldsgttitylqqdladqiikafng
kltqdsngnsyevdcnlsgdvvfnfsknakisvpasdfaastqgddgqpydkcqllfdvn
kanilgdnflrsayivydlddneisiaqvkytsasstsalt
>d1dpja_ 2.47.1.2.6 Acid protease {Baker's yeast (Saccharomyces cerevisiae), proteinase A}
gghdvpltnylnaqyytditlgtppqnfkvildtgssnlwvpsnecgslacflhskydhe
asssykangtefaiqygtgslegyisqdtlsigdltipkqdfaeatsepgltfafgkfdg
ilglgydtisvdkvvppfynaiqqdlldekrfafylgdtskdtenggeatfggideskfk
gditwlpvrrkaywevkfegiglgdeyaeleshgaaidtgtslitlpsglaeminaeiga
kkgwtgqytldcntrdnlpdlifnfngynftigpydytlevsgscisaitpmdfpepvgp
laivgdaflrkyysiydlgnnavglakai
>e1b5f.1b 2.47.1.2.7 Plant acid proteinase, phytepsin {Cynara cardunculus}
eelqvdcntlssmpnvsftiggkkfgltpeqyilkvgkgeatqcisgftamdatllgplw
ilgdvfmrpyhtvfdygnllvgfaeaa
>d2psg__ 2.47.1.2.9 Pepsin(ogen) {Pig (Sus scrofa)}
lvkvplvrkkslrqnlikdgklkdflkthkhnpaskyfpeaaaligdeplenyldteyfg
tigigtpaqdftvifdtgssnlwvpsvycsslacsdhnqfnpddsstfeats
>e1avf.1p 2.47.1.2.11 Pepsin(ogen) {Human (Homo sapiens), progastricsin (pepsinogen C)}
avvkvplkkfksiretmkekg
>e1avf.2q 2.47.1.2.11 Pepsin(ogen) {Human (Homo sapiens), progastricsin (pepsinogen C)}
avvkvplkkfksiretmkekgl
>e1htr.1p 2.47.1.2.11 Pepsin(ogen) {Human (Homo sapiens), progastricsin (pepsinogen C)}
avvkvplkkfksiretmkekgllgeflrthkydpawkyrfgdl
>e1lyb.1a 2.47.1.2.14 Cathepsin D {Human (Homo sapiens)}
gpipevlknymdaqyygeigigtppqcftvvfdtgssnlwvpsihcklldiacwihhkyn
sdksstyvkngtsfdihygsgslsgylsqdtvsvpcq
>d1qu2a2 2.48.1.1.2 (201-394) Isoleucyl-tRNA synthetase (IleRS) editing domain {Staphylococcus aureus}
hdkrsasiyvafnvkddkgvvdadakfiiwtttpwtipsnvaitvhpelkygqynvngek
yiiaealsdavaealdwdkasiklekeytgkelewvvaqhpfldreslvingdhvttdag
tgcvhtapghgeddyivgqqyelpvispiddkgvfteeggqfegmfydkankavtdllte
kgallkldfithsy
>d2eng__ 2.49.1.1.1 Endoglucanase V {Humicola insolens}
adgrstrywdcckpscgwakkapvnqpvfscnanfqritdfdaksgcepggvayscadqt
pwavnddfalgfaatsiagsneagwccacyeltftsgpvagkkmvvqststggdlgsnhf
dlnipgggvgifdgctpqfgglpgqryggissrnecdrfpdalkpgcywrfdwfknadnp
sfsfrqvqcpaelvartgcrrnddgnfpav
>d1bw3__ 2.49.1.2.1 Barwin {Barley (Hordeum vulgare)}
eqandvratyhyyrpaqnnwdlgapavsaycatwdaskplswrskygwtafcgpagprgq
aacgkclrvtnpatgaqitarivdqcanggldldwdtvftkidtngigyqqghlnvnyqf
vdcrd
>e1aw8.1a 2.49.2.1.1 Pyruvoyl dependent aspartate decarboxylase, ADC {Escherichia coli}
mirtmlqgklhrvkvthadlhyeg
>e1aw8.1b 2.49.2.1.1 Pyruvoyl dependent aspartate decarboxylase, ADC {Escherichia coli}
caidqdfldaagileneaidiwnvtngkrfstyaiaaergsriisvngaaahcasvgdiv
iiasfvtmpdeeartwrpnvayfegdnemk
>e1aw8.2d 2.49.2.1.1 Pyruvoyl dependent aspartate decarboxylase, ADC {Escherichia coli}
mirtmlqgklhrvkvthadlhyeg
>d1dmr_1 2.49.2.2.2 (626-781) Dimethylsulfoxide reductase (DMSO reductase) {Rhodobacter capsulatus}
erldgpgakyplhiaashpfnrlhsqlngtvlregyavqghepclmhpddaaargiadgd
vvrvhndrgqiltgvkvtdavmkgviqiyeggwydpsdvtepgtldkygdvnvlsadigt
sklaqgncgqtvlaevekytgpavtltgfvapkaae
>d1aa6_1 2.49.2.2.3 (565-715) Formate dehydrogenase H {Escherichia coli}
pidkltdeypmvlstvrevghyscrsmtgncaalaaladepgyaqintedakrlgiedea
lvwvhsrkgkiitraqvsdrpnkgaiymtyqwwigacnelvtenlspitktpeykycavr
vepiadqraaeqyvideynklktrlreaala
>d2napa1 2.49.2.2.5 (601-723) Dissimilatory nitrate reductase (NAP) {Desulfovibrio desulfuricans}
aaeepdaeyplyltsmrvidhwhtatmtgkvpelqkanpiafveineedaartgikhgds
vivetrrdamelparvsdvcrpgliavpffdpkklvnklfldatdpvsrepeykicaarv
rka
>d1qcsa1 2.49.2.3.1 (2-85) N-terminal domain of NSF-N, NSF-Nn {Hamster (Cricetulus griseus)}
agrsxqaarcptdelslsncavvsekdyqsgqhvivrtspnhkyiftlrthpsvvpgsva
fslpqrkwaglsigqeievalysf
>d1cr5a1 2.49.2.3.2 (26-107) N-terminal domain of NSF-N, NSF-Nn {Baker's yeast (Saccharomyces cerevisiae), sec18p}
trhlkvsncpnnsyalanvaavspndfpnniyiiidnlfvfttrhsndippgtigfngnq
rtwggwslnqdvqakafdlfky
>d1cz4a1 2.49.2.3.3 (1-91) N-terminal domain of VAT-N, VAT-Nn {Thermoplasma acidophilum}
mesnngiilrvaeanstdpgmsrvrldessrrlldaeigdvveiekvrktvgrvyrarpe
denkgivridsvmrnncgasigdkvkvrkvr
>d1dfup_ 2.50.1.1.1 Ribosomal protein L25 {Escherichia coli}
mftinaevrkeqgkgasrrlraankfpaiiyggkeaplaieldhdkvmnmqakaefysev
ltivvdgkeikvkaqdvqrhpykpklqhidfvra
>d1gtra1 2.50.1.2.1 (339-547) Gln-tRNA synthetase (GlnRS), C-terminal (anticodon-binding) domain {Escherichia coli}
apramavidpvklvienyqgegemvtmpnhpnkpemgsrqvpfsgeiwidradfreeank
qykrlvlgkevrlrnayvikaervekdaegnittifctydadtlskdpadgrkvkgvihw
vsaahalpveirlydrlfsvpnpgaaddflsvinpeslvikqgfaepslkdavagkafqf
eregyfcldsrhstaekpvfnrtvglrdt
>d1cl3a_ 2.51.1.1.1 Core binding factor beta {Human (Homo sapiens)}
vvpdqrskfeneeffrklsreceikytgfrdrpheerqtrfqnacrdgrseiafvatgtn
lslqffpaswqgeqrqtpsreyvdlereagkvylkapmilngvcviwkgwidlhrldgmg
clefdeeraqqedalaqq
>d1mai__ 2.52.1.1.1 Phospholipase C delta-1 {Rat (Rattus norvegicus)}
glqddpdlqallkgsqllkvkssswrrerfyklqedcktiwqesrkvmrspesqlfsied
iqevrmghrteglekfardipedrcfsivfkdqrntldliapspadaqhwvqglrkiih
>d1btn__ 2.52.1.1.2 beta-spectrin {Mouse (Mus musculus), brain}
megflnrkheweahnkkassrswhnvycvinnqemgfykdaksaasgipyhsevpvslke
aicevaldykkkkhvfklrlsdgneylfqakddeemntwiqaissa
>d1dro__ 2.52.1.1.3 beta-spectrin {Fruit fly (Drosophila melanogaster)}
gsgtgageghegyvtrkhewdsttkkasnrswdkvymaakagrisfykdqkgyksnpelt
frgepsydlqnaaieiasdytkkkhvlrvklangalfllqahddtemsqwvtslkaqsds
ta
>d1dyna_ 2.52.1.1.4 Dynamin {Human (Homo sapiens)}
ilvirkgwltinnigimkggskeywfvltaenlswykddeekekkymlsvdnlklrdvek
gfmsskhifalfnteqrnvykdyrqlelacetqeevdswkasflragvyperv
>d1btka_ 2.52.1.1.5 Bruton's tyrosine kinase {Human (Homo sapiens)}
aavilesiflkrsqqkkktsplnfkkclflltvhklsyyeydfergrrgskkgsidveki
tcvetvvpeknppperqiprrgeessemeqisiierfpypfqvvydegplyvfspteelr
krwihqlknvirynsdlvqkyhpcfwidgqylccsqtaknamgcqilen
>d1pls__ 2.52.1.1.6 Pleckstrin, N-terminal domain {Human (Homo sapiens)}
mepkriregylvkkgsvfntwkpmwvvlledgiefykkksdnspkgmiplkgstltspcq
dfgkrmfvfkitttkqqdhffqaafleerdawvrdinkaikcieglehhhhhh
>d1dbha2 2.52.1.1.8 (418-550) Son of sevenless-1 (sos-1) {Human (Homo sapiens)}
aikkxneiqknidgwegkdigqccnefixegtltrvgakherhiflfdglxiccksnhgq
prlpgasnaeyrlkekffxrkvqindkddtneykhafeiilkdensvifsaksaeeknnw
xaalislqyrstl
>d1bak__ 2.52.1.1.9 G-protein coupled receptor kinase 2 (beta-adrenergic receptor kinase 1) {Human (Homo sapiens)}
gshmgkdcimhgymskmgnpfltqwqrryfylfpnrlewrgegeapqslltmeeiqsvee
tqikerkclllkirggkqfilqcdsdpelvqwkkelrdayreaqqlvqrvpkmknkprs
>d1aqca_ 2.52.1.2.1 X11 {Human (Homo sapiens)}
edlidgiifaanylgstqllsdktpsknvrxxqaqeavsrikxaqklaksrkkapegesq
pxtevdlfiltqrikvlnadtqetxxdhplrtisyiadignivvlxarrriprsnsqenv
eashpsqdgkrqykxichvfesedaqliaqsigqafsvayqeflr
>d1qqga1 2.52.1.2.2 (12-114) Insulin receptor substrate 1, IRS-1 {Human (Homo sapiens)}
dvrkvgylrkpksmhkrffvlraaseaggparleyyenekkwrhkssapkrsiplescfn
inkradsknkhlvalytrdehfaiaadseaeqdswyqallqlh
>d1qqga2 2.52.1.2.2 (159-262) Insulin receptor substrate 1, IRS-1 {Human (Homo sapiens)}
afkevwqvilkpkglgqtknligiyrlcltsktisfvklnseaaavvlqlmnirrcghse
nfffievgrsavtgpgefwmqvddsvvaqnmhetileamramsd
>d1shca_ 2.52.1.2.3 Shc adaptor protein {Human (Homo sapiens)}
gshmgqlggeewtrhgsfvnkptrgwlhpndkvmgpgvsylvrymgcvevlqsmraldfn
trtqvtreaislvceavpgakgatrrrkpcsrplssilgrsnlkfagmpitltvstssln
lmaadckqiianhhmqsisfasggdpdtaeyvayvakdpvnqrachilecpeglaqdvis
tigqafelrfkqylr
>d1ddma_ 2.52.1.2.4 Numb {Fruit fly (Drosophila melanogaster)}
hqwqadeeavrsatcsfsvkylgcvevfesrgmqvceealkvlrqsrrrpvrgllhvsgd
glrvvddetkglivdqtiekvsfcapdrnhergfsyicrdgttrrwmchgflackdsger
lshavgcafavcler
>d1rrpb_ 2.52.1.3.1 Ran-binding domain of nuclear pore complex protein Nup358 {Human (Homo sapiens)}
hfepvvplpdkievktgeedeeeffcnraklfrfdveskewkergignvkilrhktsgki
rllmrreqvlkicanhyispdmkltpnagsdrsfvwhaldyadelpkpeqlairfktpee
aalfkckfeeaqsi
>d1evha_ 2.52.1.4.1 Enabled {Mouse (Mus musculus)}
seqsicqaraavmvyddankkwvpaggstgfsrvhiyhhtgnntfrvvgrkiqdhqvvin
caipkglkynqatqtfhqwrdarqvyglnfgskedanvfasammhalevln
>d1ddwa_ 2.52.1.4.3 Homer {Rat (Rattus norvegicus)}
geqpifstrahvfqidpntkknwvptskhavtvsyfydstrnvyriisldgskaiinsti
tpnxtftktsqkfgqwadsrantvyglgfssehhlskfaekfqefkeaar
>d1ef1a2 2.52.1.5.1 (199-297) Moesin {Human (Homo sapiens)}
exygvnyfsiknkkgselwlgvdalglniyeqndrltpkigfpwseirnisfndkkfvik
pidkkapdfvfyaprlrinkrilalcxgnhelyxrrrkp
>d1ytfc1 2.53.1.1.1 Transcription factor IIA (TFIIA), N-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
enlmlclydkvtrtkarwkcslkdgvvtinrndytfqkaqveaewv
>d1ytfd2 2.53.1.1.1 (55-119) Transcription factor IIA (TFIIA), N-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
ntqskltvkgnldtygfcddvwtfivkncqvtvedshrdasqngsgdsqsvisvdklriv
acnsk
>d1wpoa_ 2.54.1.1.1 Human cytomegalovirus protease {Human cytomegalovirus, hCMV}
qavapvyvggflarydqspdeaelllprdvvehwlhaqgqgqpslsvalplninhddtav
vghvaaxqsvrdglfclgcvtsprfleivrrasekselvsrgpvsplqpdkvveflsgsy
aglslssrrcddveaatslsgsettpfkhvalcsvgrrrgtlavygrdpewvxqrfpdlt
aadrdglraqwqrcgstavdasgdpfrsdsygllgnsvdaxyirerlpklrydkqlvgvt
eresyvka
>d1at3a_ 2.54.1.1.2 HSV-2 protease {Herpes simplex virus type II, HSV-2}
ravpiyvagflalydsgdpgelaldpdtvraalppenplpinvdhrarcevgrvlavvnd
prgpffvgliacvqlervletaasaaiferrgpalsreerllylitnylpsvslstkrrg
devppdrtlfahvalcaigrrlgtivtydtsldaaiapfrhldpatregvrreaaeaela
lagrtwapgvealthtllstavnnmmlrdrwslvaerrrqagiaghtylqa
>d1a49a1 2.55.1.1.1 (116-217) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1pkla1 2.55.1.1.3 (88-186) Pyruvate kinase {Leishmania mexicana}
eirtgqfvggdavmergatcyvttdpafadkgtkdkfyidyqnlskvvrpgnyiyiddgi
lilqvqshedeqtlectvtnshtisdrrgvnlpgcdvdl
>d1a3wa1 2.55.1.1.4 (88-188) Pyruvate kinase {Baker's yeast (Saccharomyces cerevisiae)}
peirtgtttndvdypippnhemifttddkyakacddkimyvdyknitkvisagriiyvdd
gvlsfqvlevvddktlkvkalnagkicshkgvnlpgtdvdl
>d1e0ta1 2.55.1.1.5 (70-167) Pyruvate kinase {Escherichia coli}
peirtmkleggndvslkagqtftfttdksvignsemvavtyegfttdlsvgntvlvddgl
igmevtaiegnkvickvlnngdlgenkgvnlpgvsial
>d1aqb__ 2.56.1.1.2 Retinol binding protein {Pig (Sus scrofa domestica)}
erdcrvssfrvkenfdkarfsgtwyamakkdpeglflqdnivaefsvdenghmsatakgr
vrllnnwdvcadmvgtftdtedpakfkmkywgvasflqkgnddhwiidtdydtyavqysc
rlqnldgtcadsysfvfardphgfspevqkivrqrqeelclarqyriithngycd
>d1obpa_ 2.56.1.1.5 Odorant-binding protein {Bovine (Bos taurus)}
qeeeaeqnlselsgpwrtvyigstnpekiqengpfrtyfrelvfddekgtvdfyfsvkrd
gkwknvhvkatkqddgtyvadyegqnvfkivslsrthlvahninvdkhgqtteltglfvk
lnvededlekfwkltedkgidkknvvnflenedhphpe
>d1bj7__ 2.56.1.1.7 Lipocalin allergen {Bovine (Bos taurus), bos d 2}
idpskipgewriiyaaadnkdkiveggplrnyyrriecindceslsitfylkdqgtclll
tevakrqegyvyvlefygtntlevihvsenmlvtyvenydgeritkmteglakgtsftpe
elekyqqlnsergvpnenienliktdncpp
>d1ew3a_ 2.56.1.1.8 Lipocalin allergen {Horse (Equus caballus), equ c 1}
vairnfdiskisgewysiflasdvkekieengsmrvfvdviraldnsslyaeyqtkvnge
ctefpmvfdkteedgvyslnydgynvfrisefendehiilylvnfdkdrpfqlfefyare
pdvspeikeefvkivqkrgivkeniidltkidrcfqlrg
>d1beba_ 2.56.1.1.9 beta-Lactoglobulin {Bovine (Bos taurus)}
qtmkgldiqkvagtwyslamaasdislldaqsaplrvyveelkptpegdleillqkweng
ecaqkkiiaektkipavfkidalnenkvlvldtdykkyllfcmensaepeqslvcqclvr
tpevddealekfdkalkalpmhirlsfnptqleeqc
>d1epba_ 2.56.1.1.10 Retinoic acid-binding protein {Rat (Rattus norvegicus), albino}
vkdfdiskflgfwyeiafaskmgtpglahkeekmgamvvelkenllaltttyysedhcvl
ekvtategdgpakfqvtrlsgkkevvveatdyltyaiiditslvagavhrtmklysrsld
dngealynfrkitsdhgfsetdlyilkhdltcvkvlqsaa
>d1qqsa_ 2.56.1.1.13 Neutrophil gelatinase-associated lipocalin (NGAL) {Human (Homo sapiens)}
tsdlipapplskvplqqnfqdnqfqgkwyvvglagnailredkdpqkmyatiyeekedas
ynvtsvlfrkkkcdyairtfvpgcqpgeftlgniksypgltsylvrvvstnynqhamvff
kkvsqnreyfkitlygrtkeltselknnfirfskslglpenhivfpvpidqcid
>d1bbpa_ 2.56.1.1.14 Bilin-binding protein {Cabbage butterfly (Pieris brassicae)}
nvyhdgacpevkpvdnfdwsnyhgkwwevakypnsvekygkcgwaeytpegksvkvsnyh
vihgkeyfiegtaypvgdskigkiyhkltyggvtkenvfnvlstdnknyiigyyckyded
kkghqdfvwvlsrskvltgeaktavenyligspvvdsqklvysdfseaackvn
>d1qfta_ 2.56.1.1.15 Histamine binding protein {Brown ear tick (Rhipicephalus appendiculatus)}
nqpdwadeaangahqdawkslkadvenvyymvkatykndpvwgndftcvgvmandvnede
ksiqaeflfmnnadtnmqfatekvtavkmygynrenafryetedgqvftdviaysddncd
viyvpgtdgneegyelwttdydnipanclnkfneyavgretrdvftsacleiaaa
>d1erxa_ 2.56.1.1.18 Nitrophorin 4 {Rhodnius prolixus}
actknaiaqtgfnkdkyfngdvwyvtdyldlepddvpkrycaalaagtasgklkealyhy
dpktqdtfydvselqveslgkytanfkkvdkngnvkvavtagnyytftvmyaddssalih
tclhkgnkdlgdlyavlnrnkdaaagdkvksavsaatlefskfistkenncaydndslks
lltk
>d1hms__ 2.56.1.2.1 Muscle fatty acid binding protein (m-fabp) {Human (Homo sapiens)}
vdaflgtwklvdsknfddymkslgvgfatrqvasmtkpttiiekngdiltlkthstfknt
eisfklgvefdettaddrkvksivtldggklvhlqkwdgqettlvrelidgkliltlthg
tavctrtyeke
>d1ifc__ 2.56.1.2.3 Intestinal fatty acid binding protein {Rat (Rattus rattus)}
afdgtwkvdrnenyekfmekmginvvkrklgahdnlkltitqegnkftvkessnfrnidv
vfelgvdfaysladgteltgtwtmegnklvgkfkrvdngkeliavreisgneliqtytye
gveakrifkke
>d1mdc__ 2.56.1.2.7 Fatty acid-binding protein {Tobacco hornworm (Manduca sexta)}
xsylgkvyslvkqenfdgflksaglsddkiqalvsdkptqkmeangdsysntstggggak
tvsfksgvefddvigagdsvksmytvdgnvvthvvkgdagvatfkkeyngddlvvtitss
nwdgvarryyka
>d1ftpa_ 2.56.1.2.8 Fatty acid-binding protein {Desert locust (Schistocerca gregaria)}
vkefagikykldsqtnfeeymkaigvgaierkaglalspvieleildgdkfkltsktaik
nteftfklgeefdeetldgrkvkstitqdgpnklvheqkgdhptiiirefskeqcvitik
lgdlvatriykaq
>d1cbs__ 2.56.1.2.9 Cellular retinoic-acid-binding protein (CRABP) {Human (Homo sapiens), CRABP-II}
pnfsgnwkiirsenfeellkvlgvnvmlrkiavaaaskpaveikqegdtfyiktsttvrt
teinfkvgeefeeqtvdgrpckslvkwesenkmvceqkllkgegpktswtreltndgeli
ltmtaddvvctrvyvre
>d1opaa_ 2.56.1.2.11 Cellular retinol-binding protein II (CRBP) {Rat (Rattus rattus)}
tkdqngtwemesnenfegymkaldidfatrkiavrltqtkiivqdgdnfktktnstfrny
dldftvgvefdehtkgldgrnvktlvtwegntlvcvqkgekenrgwkqwvegdklylelt
cgdqvcrqvfkkk
>d1lfo__ 2.56.1.2.12 Liver fatty acid binding protein {Rat (Rattus norvegicus)}
mnfsgkyqvqsqenfepfmkamglpedliqkgkdikgvseivhegkkvkltitygskvih
neftlgeexeletmtgekvkavvkmegdnkmvttfkgiksvtefngdtitntmtlgdivy
krvskri
>d1eal__ 2.56.1.2.14 Ileal lipid binding protein {Pig (Sus scrofa)}
aftgkyeieseknydefmkrlalpsdaidkarnlkiisevkqdgqnftwsqqypgghsit
ntftigkecdietiggkkfkatvqmeggkvvvnspnyhhtaeivdgklvevstvggvsye
rvskkla
>d1avgi_ 2.56.1.3.1 Thrombin inhibitor {Triatomine bug (Triatoma pallidipennis)}
aegddcsiekamgdfkpeeffngtwylahgpgvtspavcqkfttsgskgftqiveigynk
fesnvkfqcnqvdnkngeqysfkckssdntefeadftfisvsydnfalvcrsitftsqpk
edrylvfertksdtdpdakeic
>d1swga_ 2.57.1.1.1 Streptavidin {Streptomyces avidinii}
sryvltgrydsapatdgsgtalgwtvawknnyrnahsattwsgqyvggaearintqwllt
sgtteanawkstlvghdtftkvkpsaasgggsaeagitgtwynqlgstfivtagadgalt
gtyesa
>d1swua_ 2.57.1.1.1 Streptavidin {Streptomyces avidinii}
gitgtwynqlgstfivtagadgaltgtfesavgnaesryvltgrydsapatdgsgtalgw
tvawknnyrnahsattwsgqyvggaearintqwlltsgtteanawkstlvghdtftkvkp
>d2cama_ 2.57.1.1.2 Avidin {Chicken (Gallus gallus)}
recsltgewtndlgsnmtigavnsdgeftgtyitavtatsneikesplhgtentinkrtq
ptfgftvnwkfsesttvftgqcfidrngkevlktmwllrssvndigddwkatrvginift
rllt
>d1smpi_ 2.57.2.1.1 Metalloprotease inhibitor {Erwinia chrysanthemi}
sslrlpsaaelsgqwvlsgaeqhcdirlntdvldgttwklagdtaclqkllpeapvgwrp
tpdgltltqadgsavaffsrnrdryehklvdgsvrtlkkk
>d2cpl__ 2.58.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1lopa_ 2.58.1.1.7 Bacterial cyclophilin {Escherichia coli}
mvtfhtnhgdiviktfddkapetvknfldycregfynntifhrvingfmiqgggfepgmk
qkatkepikneannglkntrgtlamartqaphsataqffinvvdndflnfsgeslqgwgy
cvfaevvdgmdevdkikgvatgrsgmhqdvpkedviiesvtvse
>d1jsg__ 2.59.1.1.1 p14-TCL1 {Human (Homo sapiens)}
cptlgeavtdhpdrlwawekfvyldekqhawlpltieikdrlqlrvllrredvvlgrpmt
ptqigpsllpimwqlypdgryrssdssfwrlvyhikidgvedmllellpdd
>d1a1x__ 2.59.1.1.2 MTCP-1 {Human (Homo sapiens)}
agedvgappdhlwvhqegiyrdeyqrtwvavveeetsflrarvqqiqvplgdaarpshll
tsqlplmwqlypeerymdnnsrlwqiqhhlmvrgvqelllkllpdd
>d1c39a_ 2.60.1.1.1 Extracytoplasmic domain of cation-dependent mannose 6-phosphate receptor {Bovine (Bos taurus)}
ektcdlvgekgkesekelallkrltplfqksfestvgqspdmysyvfrvcreagqhssga
glvqiqksngketvvgrfnetqifqgsnwimliykggdeydnhcgreqrravvmiscnrh
tladnfnpvseergkvqdcfylfemdsslacs
>d1hxn__ 2.61.1.1.1 Hemopexin {Rabbit (Oryctolagus cuniculus)}
estrcdpdlvlsamvsdnhgatyvfsgshywrldtnrdgwhswpiahqwpqgpstvdaaf
swedklyliqdtkvyvfltkggytlvngypkrlekelgsppvisleavdaafvcpgssrl
himagrrlwwldlksgaqatwtelpwphekvdgalcmekplgpnscstsgpnlylihgpn
lycyrhvdklnaaknlpqpqrvsrllgcth
>d1qhua1 2.61.1.1.1 (24-215) Hemopexin {Rabbit (Oryctolagus cuniculus)}
ieqcsdgwsfdattlddngtmlffkdefvwkshrgireliserwknfigpvdaafrhght
svylikgdkvwvytseknekvypkslqdefpgipfpldaavechrgecqdegilffqgnr
kwfwdlttgtkkerswpavgnctsalrwlgryycfqgnqflrfnpvsgevppgypldvrd
yflscpgrghrs
>d1gen__ 2.61.1.1.2 Gelatinase A (MMP-2), C-terminal domain {Human (Homo sapiens)}
lgpvtpeickqdivfdgiaqirgeifffkdrfiwrtvtprdkpmgpllvatfwpelpeki
davyeapqeekavffagneywiysastlergypkpltslglppdvqrvdaafnwsknkkt
yifagdkfwrynevkkkmdpgfpkliadawnaipdnldavvdlqggghsyffkgayylkl
enqslksvkfgsiksdwlgc
>d1tl2a_ 2.62.1.1.1 Tachylectin-2 {Japanese horseshoe crab (Tachypleus tridentatus)}
ggesmlrgvyqdkfyqgtypqnkndnwlaratligkggwsnfkflflspggelygvlndk
iykgtppthdndnwmgrakkignggwnqfqflffdpngylyavskdklykasppqsdtdn
wiaratevgsggwsgfkflffhpngylyavhgqqfykalppvsnqdnwlaratkigqggw
dtfkflffssvgtlfgvqggkfyedyppsyaydnwlaraklignggwddfrflff
>d3sil__ 2.63.1.1.1 Salmonella sialidase {Salmonella typhimurium, strain lt2}
eksvvfkaegehftdqkgntivgsgsggttkyfripamcttskgtivvfadarhntasdq
sfidtaaarstdggktwnkkiaiyndrvnsklsrvmdptcivaniqgretilvmvgkwnn
ndktwgayrdkapdtdwdlvlykstddgvtfskvetnihdivtkngtisamlggvgsglq
lndgklvfpvqmvrtknittvlntsfiystdgitwslpsgycegfgsenniiefnaslvn
nirnsglrrsfetkdfgktwtefppmdkkvdnrnhgvqgstitipsgnklvaahssaqnk
nndytrsdislyahnlysgevkliddfypkvgnasgagysclsyrknvdketlyvvyean
gsiefqdlsrhlpviksyn
>d2qwc__ 2.63.1.1.2 Influenza neuraminidase {Influenza virus A, different strains}
rdfnnltkglctinswhiygkdnavrigedsdvlvtrepyvscdpdecrfyalsqgttir
gkhsngtihdrsqyraliswplsspptvynsrvecigwsstschdgktrmsicisgpnnn
asaviwynrrpvteintwarnilrtqesecvchngvcpvvftdgsatgpaetriyyfkeg
kilkweplagtakhieecscygeraeitctckdnwqgsnrpviridpvamthtsqyicsp
vltdnprpndptvgkcndpypgnnnngvkgfsyldgvntwlgrtisiasrsgyemlkvpn
altddkskptqgqtivlntdwsgysgsfmdywaegecyracfyvelirgrpkedkvwwts
nsivsmcssteflgqwdwpdgakieyfl
>d1eur__ 2.63.1.1.4 Micromonospora sialidase, N-terminal domain {Micromonospora viridifaciens}
geplyteqdlavngregfpnyripaltvtpdgdllasydgrptgidapgpnsilqrrstd
ggrtwgeqqvvsagqttapikgfsdpsylvdretgtifnfhvysqrqgfagsrpgtdpad
pnvlhanvatstdggltwshrtitaditpdpgwrsrfaasgegiqlrygphagrliqqyt
iinaagafqavsvysddhgrtwrageavgvgmdenktvelsdgrvllnsrdsarsgyrkv
avstdgghsygpvtidrdlpdptnnasiirafpdapagsarakvllfsnaasqtsrsqgt
irmscddgqtwpvskvfqpgsmsystltalpdgtygllyepgtgiryanfnlawlggica
p
>d2sli_2 2.63.1.1.5 (277-759) Leech intramolecular trans-sialidase, C-terminal domain {North american leech (Macrobdella decora)}
genifyagdvtesnyfripslltlstgtvisaadaryggthdskskiniafakstdggnt
wseptlplkfddyiaknidwprdsvgknvqiqgsasyidpvlledkltkriflfadlmpa
gigssnasvgsgfkevngkkylklrwhkdagraydytirekgviyndatnqptefrvdge
ynlyqhdtnltckqydynfsgnnliesktdvdvnmnifyknsvfkafptnylamrysdde
gaswsdldivssfkpevskflvvgpgigkqistgenagrllvplyskssaelgfmysddh
gdnwtyveadnltggataeaqivempdgslktylrtgsnciaevtsidggetwsdrvplq
gisttsygtqlsvinysqpidgkpaiilsspnatngrkngkiwiglvndtgntgidkysv
ewkysyavdtpqmgysysclaelpdgqvgllyekydswsrnelhlkdilkfekysiselt
gqa
>d1kit_3 2.63.1.1.6 (217-346,544-781) Vibrio cholerae sialidase {Vibrio cholerae}
vifrgpdripsivassvtpgvvtafaekrvgggdpgalsntndiitrtsrdggitwdtel
nlteqinvsdefdfsdprpiydpssntvlvsyarwptdaaqngdrikpwmpngifysvyd
vasgnwqapiXvnpgpghgitltrqqnisgsqngrliypaivldrfflnvmsiysddggs
nwqtgstlpipfrwksssiletlepseadmvelqngdllltarldfnqivngvnysprqq
flskdggitwslleannanvfsnistgtvdasitrfeqsdgshfllftnpqgnpagtngr
qnlglwfsfdegvtwkgpiqlvngasaysdiyqldsenaivivetdnsnmrilrmpitll
kqkltlsqn
>d1crua_ 2.63.2.1.1 Soluble quinoprotein glucose dehydrogenase {Acinetobacter calcoaceticus}
dvpltpsqfakaksenfdkkvilsnlnkphallwgpdnqiwlteratgkilrvnpesgsv
ktvfqvpeivndadgqngllgfafhpdfknnpyiyisgtfknpkstdkelpnqtiirryt
ynkstdtlekpvdllaglpsskdhqsgrlvigpdqkiyytigdqgrnqlaylflpnqaqh
tptqqelngkdyhtymgkvlrlnldgsipkdnpsfngvvshiytlghrnpqglaftpngk
llqseqgpnsddeinlivkggnygwpnvagykddsgyayanysaaanksikdlaqngvkv
aagvpvtkesewtgknfvpplktlytvqdtynyndptcgemtyicwptvapssayvykgg
kkaitgwentllvpslkrgvifrikldptysttyddavpmfksnnryrdviaspdgnvly
vltdtagnvqkddgsvtntlenpgslikft
>d1pooa_ 2.63.3.1.1 Thermostable phytase (3-phytase) {Bacillus amyloliquefaciens}
klsdpyhftvnaaaetepvdtagdaaddpaiwldpknpqnsklittnkksglavyslegk
mlhsyhtgklnnvdirydfplngkkvdiaaasnrsegkntieiyaidgkngtlqsitdpn
rpiasaidevygfslyhsqktgkyyamvtgkegefeqyelnadkngyisgkkvrafkmns
qtegmaaddeygslyiaeedeaiwkfsaepdggsngtvidradgrhltpdiegltiyyaa
dgkgyllassqgnssyaiyerqgqnkyvadfqitdgpetdgtsdtdgidvlgfglgpeyp
fglfvaqdgenidhgqkanqnfkmvpweriadkigfhpqvnkqvdprkmtdrs
>d1gof_3 2.64.1.1.1 (151-537) Galactose oxidase, central domain {Dactylium dendroides}
ytapqpglgrwgptidlpivpaaaaieptsgrvlmwssyrndafggspggitltsswdps
tgivsdrtvtvtkhdmfcpgismdgngqivvtggndakktslydsssdswipgpdmqvar
gyqssatmsdgrvftiggswsggvfekngevyspssktwtslpnakvnpmltadkqglyr
sdnhawlfgwkkgsvfqagpstamnwyytsgsgdvksagkrqsnrgvapdamcgnavmyd
avkgkiltfggspdyqdsdattnahiitlgepgtspntvfasnglyfartfhtsvvlpdg
stfitggqrrgipfedstpvftpeiyvpeqdtfykqnpnsivrvyhsislllpdgrvfng
ggglcgdcttnhfdaqiftpnylynsn
>d2bbkh_ 2.64.2.1.1 Methylamine dehydrogenase, H-chain {Paracoccus denitrificans}
deprileapapdarrvyvndpahfaavtqqfvidgeagrvigmidggflpnpvvaddgsf
iahastvfsriargertdyvevfdpvtllptadielpdaprflvgtypwmtsltpdgktl
lfyqfspapavgvvdlegkafkrmldvpdcyhifptapdtffmhcrdgslakvafgtegt
peithtevfhpedeflinhpaysqkagrlvwptytgkihqidlssgdakflpavealtea
eradgwrpggwqqvayhraldriyllvdqrdewrhktasrfvvvldaktgerlakfemgh
eidsinvsqdekpllyalstgdktlyihdaesgeelrsvnqlghgpqvittadmg
>d1gotb_ 2.64.3.1.1 beta1-subunit of the signal-transducing G protein heterotrimer {Bovine (Bos taurus)}
seldqlrqeaeqlknqirdarkacadatlsqitnnidpvgriqmrtrrtlrghlakiyam
hwgtdsrlllsasqdgkliiwdsyttnkvhaiplrsswvmtcayapsgnyvacggldnic
siynlktregnvrvsrelaghtgylsccrflddnqivtssgdttcalwdietgqqtttft
ghtgdvmslslapdtrlfvsgacdasaklwdvregmcrqtftghesdinaicffpngnaf
atgsddatcrlfdlradqelmtyshdniicgitsvsfsksgrlllagyddfncnvwdalk
adragvlaghdnrvsclgvtddgmavatgswdsflkiwn
>d1a12a_ 2.64.4.1.1 Regulator of chromosome condensation RCC1 {Human (Homo sapiens)}
kkvkvshrshstepglvltlgqgdvgqlglgenvmerkkpalvsipedvvqaeaggmhtv
clsksgqvysfgcndegalgrdtsvegsemvpgkvelqekvvqvsagdshtaaltddgrv
flwgsfrdnngvigllepmkksmvpvqvqldvpvvkvasgndhlvmltadgdlytlgcge
qgqlgrvpelfanrggrqglerllvpkcvmlksrgsrghvrfqdafcgayftfaishegh
vygfglsnyhqlgtpgtescfipqnltsfknstkswvgfsggqhhtvcmdsegkayslgr
aeygrlglgegaeeksiptlisrlpavssvacgasvgyavtkdgrvfawgmgtnyqlgtg
qdedawspvemmgkqlenrvvlsvssggqhtvllvkdkeqs
>d1c9la2 2.64.5.1.1 (3-330) Clathrin heavy-chain terminal domain {Rat (Rattus norvegicus)}
qilpirfqehlqlqnlginpanigfstltmesdkficirekvgeqaqvviidmndpsnpi
rrpisadsaimnpaskvialkagktlqifniemkskmkahtmtddvtfwkwislntvalv
tdnavyhwsmegesqpvkmfdrhsslagcqiinyrtdakqkwllltgisaqqnrvvgamq
lysvdrkvsqpieghaasfaqfkmegnaeestlfcfavrgqaggklhiievgtpptgnqp
fpkkavdvffppeaqndfpvamqisekhdvvflitkygyihlydletgtciymnrisget
ifvtapheatagiigvnrkgqvlsvcve
>d1qfma1 2.64.6.1.1 (1-430) Prolyl oligopeptidase, N-terminal domain {Porcine}
mlsfqypdvyrdetaiqdyhghkvxdpyawledpdseqtkafveaqnkitvpfleqxpir
glykermtelydypkyschfkkgkryfyfyntglqnqrvlyvqdslegearvfldpnils
ddgtvalrgyafsedgeyfayglsasgsdwvtikfmkvdgakelpdvlervkfsxmawth
dgkgmfynaypqqdgksdgtetstnlhqklyyhvlgtdqsedilcaefpdepkwmggael
sddgryvllsiregxdpvnrlwycdlqqesngitgilkwvklidnfegeydyvtnegtvf
tfktnrhspnyrlinidftdpeeskwkvlvpehekdvlewvacvrsnflvlcylhdvknt
lqlhdlatgallkifplevgsvvgysgqkkdteifyqftsflspgiiyhcdltkeelepr
vfrevtvkgi
>d1b2na_ 2.65.1.1.1 Methanol dehydrogenase, heavy chain {Methylophilus methylotrophus, w3a1}
dadldkqvntagawpiatggyysqhnsplaqinksnvknvkaawsfstgvlnghegaplv
igdmmyvhsafpnntyalnlndpgkivwqhkpkqdastkavmccdvvdrglaygagqivk
kqanghllaldaktgkinwevevcdpkvgstltqapfvakdtvlmgcsgaelgvrgavna
fdlktgelkwrafatgsddsvrlakdfnsanphygqfglgtktwegdawkigggtnwgwy
aydpklnlfyygsgnpapwnetmrpgdnkwtmtiwgrdldtgmakwgyqktphdewdfag
vnqmvltdqpvngkmtpllshidrngilytlnrengnlivaekvdpavnvfkkvdlktgt
pvrdpefatrmdhkgtnicpsamgfhnqgvdsydpesrtlyaglnhicmdwepfmlpyra
gqffvgatlamypgpngptkkemgqirafdlttgkakwtkwekfaawggtlytkgglvwy
atldgylkaldnkdgkelwnfkmpsggigspmtysfkgkqyigsmygvggwpgvglvfdl
tdpsaglgavgafrelqnhtqmggglmvfsl
>d1qksa2 2.65.2.1.3 (136-567) C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase {Paracoccus denitrificans}
efgmkemreswkvhvapedrptqqmndwdlenlfsvtlrdagqialidgstyeiktvldt
gyavhisrlsasgrylfvigrdgkvnmidlwmkepttvaeikigsearsietskmegwed
kyaiagaywppqyvimdgetlepkkiqstrgmtydeqeyhpeprvaailashyrpefivn
vketgkillvdytdlnnlktteisaerflhdggldgshryfitaanarnklvvidtkegk
lvaiedtggqtphpgrganfvhptfgpvwatshmgddsvaligtdpeghpdnawkildsf
palgggslfikthpnsqylyvdatlnpeaeisgsvavfdikamtgdgsdpefktlpiaew
agitegqprvvqgefnkdgtevwfsvwngkdqesalvvvddktlelkhvikderlvtptg
kfnvyntmtdty
>d1bli_1 2.66.1.1.1 (394-483) Bacterial alpha-Amylase (BLA) {Bacillus licheniformis}
yaygaqhdyfdhhdivgwtregdssvansglaalitdgpggakrmyvgrqnagetwhdit
gnrsepvvinsagwgefhvnggsvsiyvqr
>d1aqm_1 2.66.1.1.2 (355-448) Bacterial alpha-Amylase (BLA) {Alteromonas haloplanctis}
nwavtnwwdntnnqisfgrgssghmainkedstltatvqtdmasgqycnvlkgelsadak
scsgevitvnsdgtinlnigawdamaihknakln
>d1bag_1 2.66.1.1.3 (348-425) Bacterial alpha-Amylase (BLA) {Bacillus subtilis}
qpeelsnpngnnqifmnqrgshgvvlanagsssvsintatklpdgrydnkagagsfqvnd
gkltgtinarsvavlypd
>d1qhoa3 2.66.1.1.6 (408-495) Cyclodextrin glycosyltransferase {Bacillus stearothermophilus maltogenic alpha-amylase}
gtttqrwinndvyiyerkffndvvlvainrntqssysisglqtalpngsyadylsgllgg
ngisvsngsvasftlapgavsvwqysts
>d1pama3 2.66.1.1.7 (407-496) Cyclodextrin glycosyltransferase {Alkalophilic bacillus, sp. 1011}
gstherwinndviiyerkfgnnvavvainrnmntpasitglvtslprgsyndvlggilng
ntltvgaggaasnftlapggtavwqyttda
>d1smd_1 2.66.1.1.10 (404-496) Animal alpha-amylase {Human (Homo sapiens)}
qpftnwydngsnqvafgrgnrgfivfnnddwtfsltlqtglpagtycdvisgdkingnct
gikiyvsddgkahfsisnsaedpfiaihaeskl
>d1jae_1 2.66.1.1.11 (379-471) Animal alpha-amylase {Yellow mealworm (Tenebrio molitor), larva}
gtqvenwwsnddnqiafsrgsqgfvaftnggdlnqnlntglpagtycdvisgelsggsct
gksvtvgdngsadislgsaeddgvlaihvnakl
>d7taa_1 2.66.1.1.13 (382-476) Fungal alpha-amylase {Aspergillus oryzae, Taka-amylase}
yknwpiykddttiamrkgtdgsqivtilsnkgasgdsytlslsgagytagqqltevigct
tvtvgsdgnvpvpmagglprvlypteklagskics
>d1smaa2 2.66.1.1.14 (506-588) Maltogenic amylase {Thermus sp.}
gdvafltaddevnhlvyaktdgnetvmiiinrsneaaeipmpidargkwlvnlltgerfa
aeaetlcvslppygfvlyavesw
>d1bvza2 2.66.1.1.15 (503-585) Maltogenic amylase {Thermoactinomyces vulgaris, TVAII}
gnvrswhadkqanlyafvrtvqdqhvgvvlnnrgekqtvllqvpesggktwldcltgeev
hgkqgqlkltlrpyqgmilwngr
>d1bf2_2 2.66.1.1.16 (638-750) Isoamylase {Pseudomonas amyloderamosa}
ysgsqltwyqpsgavadsnywnntsnyaiayaingpslgdsnsiyvayngwsssvtftlp
appsgtqwyrvtdtcdwndgastfvapgsetliggagttygqcgqsllllisk
>d1jdc_1 2.66.1.1.17 (358-418) G4-amylase (1,4-alpha-D-glucan maltotetrahydrolase) {Pseudomonas stutzeri}
radsaisfhsgysglvatvsgsqqtlvvalnsdlgnpgqvasgsfseavnasngqvrvwr
s
>d1avaa1 2.66.1.1.18 (347-403) Plant alpha-amylase {Barley (Hordeum vulgare), seeds, AMY2 isozyme}
hnesklqiieadadlylaeidgkvivklgprydvgnlipggfkvaahgndyavweki
>d1uok_1 2.66.1.1.19 (480-558) Oligo-1,6-glucosidase {Bacillus cereus}
gsydlilennpsifayvrtygvekllvianftaeecifelpedisysevellihnydven
gpienitlrpyeamvfklk
>d1pina1 2.67.1.1.1 (6-39) Mitotic rotamase PIN1 {Human (Homo sapiens)}
klppgwekrmsrssgrvyyfnhitnasqwerpsg
>d1e0la_ 2.67.1.1.2 Formin binding protein FBP28 domain {Domestic mouse (Mus musculus)}
gatavsewteyktadgktyyynnrtlestwekpqelk
>d1e0na_ 2.67.1.1.3 Hypothetical protein Yjq8 {Saccharomyces cerevisiae}
pgweiihengrplyynaeqktklhypp
>d1aiw__ 2.67.2.1.1 Cellulose-binding domain of endoglucanase Z {Erwinia chrysanthemi}
mgdcananvypnwvskdwaggqpthneagqsivykgnlytanwytasvpgsdsswtqvgs
cn
>d1ed7a_ 2.67.2.1.2 Chitin-binding domain of chitinase A1 {Bacillus circulans}
awqvntaytagqlvtyngktykclqphtslagwepsnvpalwqlq
>d1dkga1 2.68.1.1.1 (139-197) Head domain of nucleotide exchange factor GrpE {Escherichia coli}
veviaetnvpldpnvhqaiamvesddvapgnvlgimqkgytlngrtiraamvtvakaka
>d2cba__ 2.69.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnn
ghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvh
wntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprg
llpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvd
nwrpaqplknrqikasfk
>d1kopa_ 2.69.1.1.6 Carbonic anhydrase {Neisseria gonorrhoeae}
hthwgytghdspeswgnlseefrlcstgknqspvnitetvsgklpaikvnykpsmvdven
nghtiqvnypeggntltvngrtytlkqfhfhvpsenqikgrtfpmeahfvhldenkqplv
lavlyeagktngrlssiwnvmpmtagkvklnqpfdastllpkrlkyyrfagslttppcte
gvswlvlktydhidqaqaekftravgsennrpvqplnarvvie
>d4bcl__ 2.70.1.1.1 Bacteriochlorophyl A protein {Prosthecochloris aestuarii, strain 2k}
tttahsdyeiileggssswgqvkgrakvnvpaaipllptdcniridakpldaqkgvvrft
tkiesvvdsvkntlnvevdianetkdrriavgegslsvgdfshsfsfegsvvnmyyyrsd
avrrnipnpiymqgrqfhdilmkvpldnndlvdtwegfqqsisggganfgdwirefwfig
pafaaineggqrispivvnssnveggekgpvgvtrwkfshagsgvvdsisrwtelfpveq
lnkpasieggfrsdsqgievkvdgnlpgvsrdaggglrrilnhpliplvhhgmvgkfndf
tvdtqlkivlpkgykiryaapqfrsqnleeyrwsggayarwvehvckggtgqfevlyaq
>d1ospo_ 2.71.1.1.1 Outer surface protein A {Lyme disease spirochete (Borrelia burgdorferi)}
sldeknsvsvdlpgemkvlvskeknkdgkydliatvdklelkgtsdknngsgvlegvkad
kckvkltisddlgqttlevfkedgktlvskkvtskdkssteekfnekgevsekiitradg
trleytgiksdgsgkakevlkgyvlegtltaekttlvvkegtvtlsknisksgevsveln
dtdssaatkktaawnsgtstltitvnskktkdlvftkentitvqqydsngtklegsavei
tkldeiknalk
>d1vmoa_ 2.72.1.1.1 Vitelline membrane outer protein-I (VMO-I) {Hen (Gallus gallus)}
rtreytsvitvpngghwgkwgirqfchsgyangfalkvepsqfgrddtalngirlrcldg
svieslvgkwgtwtsflvcptgylvsfslrseksqgggddtaanniqfrcsdeavlvgdg
lswgrfgpwskrckicglqtkvespqglrddtalnnvrffcck
>d1dlc_2 2.72.2.1.1 (290-499) delta-Endotoxin (insectocide), middle domain {Bacillus thuringiensis tenebrionis, CRYIIIA (BT13)}
lypkevkteltrdvltdpivgvnnlrgygttfsnienyirkphlfdylhriqfhtrfqpg
yygndsfnywsgnyvstrpsigsndiitspfygnkssepvqnlefngekvyravantnla
vwpsavysgvtkvefsqyndqtdeastqtydskrnvgavswdsidqlppettdeplekgy
shqlnyvmcflmqgsrgtipvltwthksvd
>d1ciy_2 2.72.2.1.2 (256-461) delta-Endotoxin (insectocide), middle domain {Bacillus thuringiensis, CRYIA (A)}
pirtvsqltreiytnpvlenfdgsfrgmaqrieqnirqphlmdilnsitiytdvhrgfny
wsghqitaspvgfsgpefafplfgnagnaappvlvsltglgifrtlssplyrriilgsgp
nnqelfvldgtefsfaslttnlpstiyrqrgtvdsldvippqdnsvppragfshrlshvt
mlsqaagavytlraptfswqhrsaef
>e1jot.1a 2.72.3.1.2 Lectin MPA {Osage orange (Maclura pomifera)}
gvtfddgaytgireinfeynsetaigglrvtydlngmpfvaedhksfitgfkpvkislef
pseyivevsgyvgkvegytvirsltfktnkqtygpygvtngtpfslpienglivgfkgsi
gywldyfsiylsl
>d1c3ma_ 2.72.3.1.3 Heltuba lectin {Jerusalem artishoke (Helianthus tuberosus)}
asdiavqagpwggnggkrwlqtahggkitsiiikggtcifsiqfvykdkdnieyhsgkfg
vlgdkaetitfaededitaisgtfgayyhmtvvtsltfqtnkkvygpfgtvasssfslpl
tkgkfagffgnsgdvldsiggvvvp
>d1jpc__ 2.73.1.1.1 Lectin (agglutinin) {Snowdrop (Galanthus nivalis)}
dnilysgetlstgeflnygsfvfimqedcnlvlydvdkpiwatntgglsrscflsmqtdg
nlvvynpsnkpiwasntggqngnyvcilqkdrnvviygtdrwatgtht
>d1bwua_ 2.73.1.1.2 Lectin (agglutinin) {Garlic (Allium sativum)}
rnilrndeglyggqsldvnpyhfimqedcnlvlydhstsvwasntgilgkkgcravlqsd
gnfvvydaegrslwashsvrgngnyvlvlqedgnvviyrsdiwstn
>d1b2pa_ 2.73.1.1.4 Lectin (agglutinin) {Bluebell (Scilla campanulata)}
nniifskqpddnhpqilhatesleilfgthvyrfimqtdcnlvlydnnnpiwatntgglg
ngcravlqpdgvlvvitnenvtvwqspvagkaghyvlvlqpdrnvviygdalwatqtvr
>d1kapp1 2.74.1.1.1 (247-470) Metalloprotease, C-terminal domain {Pseudomonas aeruginosa, alkaline protease}
ganlttrtgdtvygfnsnterdfysatssssklvfsvwdaggndtldfsgfsqnqkinln
ekalsdvgglkgnvsiaagvtvenaiggsgsdlligndvanvlkggagndilygglgadq
lwggagadtfvygdiaessaaapdtlrdfvsgqdkidlsgldafvngglvlqyvdafagk
agqailsydaaskagslaidfsgdahadfainligqatqadivv
>d1air__ 2.75.1.1.1 Pectate lyase {Erwinia chrysanthemi, type C}
atdtggyaataggnvtgavsktatsmqdivniidaarldangkkvkggayplvitytgne
dslinaaaanicgqwskdprgveikeftkgitiigangssanfgiwikkssdvvvqnmri
gylpggakdgdmirvddspnvwvdhnelfaanhecdgtpdndttfesavdikgasntvtv
synyihgvkkvgldgssssdtgrnityhhnyyndvnarlplqrgglvhaynnlytnitgs
glnvrqngqaliennwfekainpvtsrydgknfgtwvlkgnnitkpadfstysitwtadt
kpyvnadswtstgtfptvaynyspvsaqcvkdklpgyagvgknlatltstac
>d1bn8a_ 2.75.1.1.3 Pectate lyase {Bacillus subtilis}
adlghqtlgsndgwgaystgttggskasssnvytvsnrnqlvsalgketnttpkiiyikg
tidmnvddnlkplglndykdpeydldkylkaydpstwgkkepsgtqeeararsqknqkar
vmvdipanttivgsgtnakvvggnfqiksdnviirniefqdaydyfpqwdptdgssgnwn
sqydnitinggthiwidhctfndgsrpdstspkyygrkyqhhdgqtdasnganyitmsyn
yyhdhdkssifgssdsktsddgklkitlhhnryknivqraprvrfgqvhvynnyyegsts
sssypfsyawgigksskiyaqnnvidvpglsaaktisvfsggtalydsgtllngtqinas
aanglsssvgwtpslhgsidasanvksnvinqagagkln
>d1qcxa_ 2.75.1.2.2 Pectin lyase {Aspergillus niger, type B}
agvvgaaegfahgvtgggsaspvyptttdelvsylgdneprviildqtfdftgtegtett
tgcapwgtasqcqvainlhswcdnyqasapkvsvtydkagilpitvnsnksivgqgtkgv
ikgkglrvvsgaknviiqniavtdinpkyvwggdaitvddsdlvwidhvttarigrqhiv
lgtsadnrvtisyslidgrsdysatcnghhywgvyldgsndmvtlkgnyfynlsgrmpkv
qgntllhavnnlfhnfdghafeigtggyvlaegnvfqdvnvvvetpisgqlfsspdantn
qqcasvfgrscqlnafgnsgsmsgsdtsiiskfagktiaaahppgaiaqwtmknagqgk
>d1qq1a_ 2.75.1.3.1 P22 tailspike protein {Salmonella typhimurium phage p22}
ysieadkkfkysvklsdyptlqdaasaavdgllidrdynfyggetvdfggkvltieckak
figdgnliftklgkgsriagvfmestttpwvikpwtddnqwltdaaavvatlkqsktdgy
qptvsdyvkfpgietllppnakgqnitstleirecigvevhrasglmagflfrgchfckm
vdannpsggkdgiitfenlsgdwgkgnyviggrtsygsvssaqflrnnggferdggvigf
tsyraggsgvktwqgtvgsttsrnynlqfrdsvviypvwdgfdlgadtdmnpeldrpgdy
pitqyplhqlplnhlidnllvrgalgvgfgmdgkgmyvsnitvedcagsgayllthesvf
tniaiidtntkdfqanqiyisgacrvnglrligirstdgqsltidapnstvsgitgmvdp
srinvanlaeeglgniransfgydsaaiklrihklsktldsgalyshinggagsgsaytq
ltaisgstpdavslkvnhkdcrgaeipfvpdiasddfikdsscflpywennstslkalvk
kpngelvrltlatl
>d1rmg__ 2.75.1.4.1 Rhamnogalacturonase A {Aspergillus aculeatus}
qlsgsvgpltsastkgatktcnilsygavadnstdvgpaitsawaacksgglvyipsgny
alntwvtltggsataiqldgiiyrtgtasgnmiavtdttdfelfsstskgavqgfgyvyh
aegtygarilrltdvthfsvhdiilvdapafhftmdtcsdgevynmairggneggldgid
vwgsniwvhdvevtnkdecvtvkspannilvesiycnwsggcamgslgadtdvtdivyrn
vytwssnqmymiksnggsgtvsnvllenfighgnaysldidgywssmtavagdgvqlnni
tvknwkgteangatrppirvvcsdtapctdltlediaiwtesgsselylcrsaygsgycl
kdssshtsytttstvtaapsgysattmaadlatafgltasipiptiptsfypgltpysal
ag
>d1bhe__ 2.75.1.4.2 Polygalacturonase {Erwinia carotovora}
sdsrtvsepktpsscttlkadsstatstiqkalnncdqgkavrlsagstsvflsgplslp
sgvsllidkgvtlravnnaksfenapsscgvvdkngkgcdafitavsttnsgiygpgtid
gqggvklqdkkvswwelaadakvkklkqntprliqinksknftlynvslinspnfhvvfs
dgdgftawkttiktpstarntdgidpmssknitiaysniatgddnvaikaykgraetrni
silhndfgtghgmsigsetmgvynvtvddlkmngttnglriksdksaagvvngvrysnvv
mknvakpividtvyekkegsnvpdwsditfkdvtsetkgvvvlngenakkpievtmknvk
ltsdstwqiknvnvkk
>d1czfa_ 2.75.1.4.3 Endo-polygalacturonase II {Fungus (Aspergillus niger)}
dsctfttaaaakagkakcstitlnnievpagttldltgltsgtkvifegtttfqyeewag
plismsgehitvtgasghlincdgarwwdgkgtsgkkkpkffyahgldsssitglniknt
plmafsvqanditftdvtinnadgdtqgghntdafdvgnsvgvniikpwvhnqddclavn
sgeniwftggtcigghglsigsvgdrsnnvvknvtiehstvsnsenavriktisgatgsv
seitysnivmsgisdygvviqqdyedgkptgkptngvtiqdvklesvtgsvdsgateiyl
lcgsgscsdwtwddvkvtggkkstacknfpsvasc
>d1daba_ 2.75.1.5.1 Virulence factor P.69 pertactin {Bordetella pertussis}
dwnnqsivktgerqhgihiqgsdpggvrtasgttikvsgrqaqgillenpaaelqfrngs
vtssgqlsddgirrflgtvtvkagklvadhatlanvgdtwdddgialyvageqaqasiad
stlqgaggvqierganvtvqrsaivdgglhigalqslqpedlppsrvvlrdtnvtavpas
gapaavsvlgaseltldgghitggraagvaamqgavvhlqratirrgdalaggavpggav
pggavpggfgpggfgpvldgwygvdvsgssvelaqsiveapelgaairvgrgarvtvpgg
slsaphgnvietggarrfapqaaplsitlqagahaqgkallyrvlpepvkltltggadaq
gdivatelpsipgtsigpldvalasqarwtgatravdslsidnatwvmtdnsnvgalrla
sdgsvdfqqpaeagrfkvltvntlagsglfrmnvfadlglsdklvvmqdasgqhrlwvrn
sgsepasantlllvqtplgsaatftlankdgkvdigtyryrlaangngqwslvgakapp
>d1dbga_ 2.75.1.6.1 Chondroitinase B {Flavobacterium heparinium}
qvvasnetlyqvvkevkpgglvqiadgtykdvqlivsnsgksglpitikalnpgkvfftg
dakvelrgehlilegiwfkdgnraiqawkshgpglvaiygsynritacvfdcfdeansay
ittsltedgkvpqhcridhcsftdkitfdqvinlnntaraikdgsvggpgmyhrvdhcff
snpqkpgnagggirigyyrndigrclvdsnlfmrqdseaeiitsksqenvyygntylncq
gtmnfrhgdhqvainnfyigndqrfgyggmfvwgsrhviacnyfelsetiksrgnaalyl
npgamasehalafdmliannafinvngyaihfnplderrkeycaanrlkfetphqlmlkg
nlffkdkpyvypffkddyfiagknswtgnvalgvekgipvnisanrsaykpvkikdiqpi
egialdlnaliskgitgkplswdevrpywlkempgtyaltarlsadraakfkavikrnke
h
>d1lxa__ 2.76.1.1.1 UDP N-acetylglucosamine acyltransferase {Escherichia coli, gene lpxA}
midksafvhptaiveegasiganahigpfcivgphveigegtvlkshvvvnghtkigrdn
eiyqfasigevnqdlkyageptrveigdrnriresvtihrgtvqgggltkvgsdnllmin
ahiahdctvgnrcilannatlaghvsvddfaiiggmtavhqfciigahvmvggcsgvaqd
vppyviaqgnhatpfgvnieglkrrgfsreaitairnaykliyrsgktldevkpeiaela
etypevkaftdffarstrglir
>d3tdt__ 2.76.1.2.1 Tetrahydrodipicolinate-N-succinlytransferase, THDP-succinlytransferase, DapD {Mycobacterium bovis}
mqqlqnviesaferraditpanvdtvtreavnqviglldsgalrvaekidgqwvthqwlk
kavllsfrindnkvmdgaetryydkvpmkfadydearfqkegfrvvppatvrqgafiarn
tvlmpsyvnigayvdegtmvdtwatvgscaqigknvhlsggvgiggvleplqanptiied
ncfigarsevvegviveegsvismgvylgqstriydretgeihygrvpagsvvvsgnlps
kdgsyslycavivkkvdaktrgkvginellrtid
>d1xat__ 2.76.1.3.1 Xenobiotic acetyltransferase {Pseudomonas aeruginosa}
nyfespfrgkllseqvsnpnirvgrysyysgyyhghsfddcarylmpdrddvdklvigsf
csigsgaafimagnqghraewastfpfhfmheepafagavngyqpagdtlighevwigte
amfmpgvrvghgaiigsralvtgdvepyaivggnpartirkrfsdgdiqnllemawwdwp
ladieaampllctgdipalyqhwkqrqa
>d1qrea_ 2.76.1.4.1 Carbonic anhydrase {Arhaeon (Methanosarcina thermophila)}
tvdefsnirenpvtpwnpepsapvidptayidpqasvigevtiganvmvspmasirsdeg
mpifvgdrsnvqdgvvlhaletineegepiednivevdgkeyavyignnvslahqsqvhg
paavgddtfigmqafvfkskvgnncvleprsaaigvtipdgryipagmvvtsqaeadklp
evtddyayshtneavvyvnvhlaegykets
>d1dzra_ 2.77.1.1.1 dTDP-4-dehydrorhamnose 3,5-epimerase RmlC {Salmonella typhimurium}
mmiviktaipdvlilepkvfgdergfffesynqqtfeeligrkvtfvqdnhskskknvlr
glhfqrgenaqgklvrcavgevfdvavdirkesptfgqwvgvnlsaenkrqlwipegfah
gfvtlseyaeflykatnyyspssegsilwndeaigiewpfsqlpelsakdaaaplldqal
lte
>d2phla2 2.77.1.2.1 (220-381) Phaseolin {French bean (Phaseolus vulgaris)}
ntignefgnltertdnslnvlissiemeegalfvphyyskaivilvvnegeahvelvgpk
gnketleyesyraelskddvfvipaaypvaikatsnvnftgfginannnnrnllagktdn
vissigraldgkdvlgltfsgsgdevmklinkqsgsyfvdah
>d1dgwa_ 2.77.1.2.2 Canavalin 7S vicilin {Jack bean (Canavalia ensiformis)}
nnpylfrsnkfltlfknqhgslrllqrfnedteklenlrdyrvleycskpntlllphhsd
sdllvlvlegqailvlvnpdgrdtykldqgdaikiqagtpfylinpdnnqnlrilkfait
frrpgtvedfflsstkrlpsylsafsknfleasydspydeieqtllqeeqegvivkmp
>e1dgw.1x 2.77.1.2.2 Canavalin 7S vicilin {Jack bean (Canavalia ensiformis)}
dkpfnlrsrdpiysnnygklyeitpeknsqlrdldillnclqmnegalfvphynsratvi
lvanegraevelvgle
>e1dgw.1y 2.77.1.2.2 Canavalin 7S vicilin {Jack bean (Canavalia ensiformis)}
qlrryaatlsegdiivipssfpvalkaasdlnmvgigvnaennernflaghkenvirqip
rqvsdltfpgsgeeveellenqkesyfvdgqp
>d1pmi__ 2.77.2.1.1 Phosphomannose isomerase {Yeast (Candida albicans)}
sseklfriqcgyqnydwgkigsssavaqfvhnsdpsitidetkpyaelwmgthpsvpska
idlnnqtlrdlvtakpqeylgesiitkfgsskelpflfkvlsiekvlsiqahpdkklgaq
lhaadpknypddnhkpemaiavtdfegfcgfkpldqlaktlatvpelneiigqelvdefi
sgiklpaevgsqddvnnrkllqkvfgklmntdddvikqqtakllertdrepqvfkdidsr
lpeliqrlnkqfpndiglfcgclllnhvglnkgeamflqakdphayisgdiiecmaasdn
vvragftpkfkdvknlvemltysyesvekqkmplqefprskgdavksvlydppiaefsvl
qtifdkskggkqvieglngpsiviatngkgtiqitgddstkqkidtgyvffvapgssiel
tadsanqdqdfttyrafvea
>d1bk0__ 2.77.3.1.1 Isopenicillin N synthase {Emericella nidulans}
svskanvpkidvsplfgddqaakmrvaqqidaasrdtgffyavnhginvqrlsqktkefh
msitpeekwdlairaynkehqdqvragyylsipgkkavesfcylnpnftpdhpriqaktp
thevnvwpdetkhpgfqdfaeqyywdvfglssallkgyalalgkeenffarhfkpddtla
svvlirypyldpypeaaiktaadgtklsfewhedvslitvlyqsnvqnlqvetaagyqdi
eaddtgylincgsymahltnnyykapihrvkwvnaerqslpffvnlgydsvidpfdprep
ngksdreplsygdylqnglvslinkngqt
>d1dcs__ 2.77.3.1.2 Deacetoxycephalosporin C synthase {Streptomyces clavuligerus}
mdttvptfslaelqqglhqdefrrclrdkglfyltdcgltdtelksakdlvidffehgse
aekravtspvptmrrgftglesestaqitntgsysdysmcysmgtadnlfpsgdferiwt
qyfdrqytasravarevlratgtepdggveafldcepllrfryfpqvpehrsaeeqplrm
aphydlsmvtliqqtpcangfvslqaevggaftdlpyrpdavlvfcgaiatlvtggqvka
prhhvaaprrdqiagssrtssvfflrpnadftfsvplarecgfdvsldgetatfqdwigg
nyvnirrtska
>d2cgpa2 2.77.4.1.1 (8-137) Catabolite gene activator protein, N-terminal domain {Escherichia coli}
dptlewflshchihkypskstlihqgekaetlyyivkgsvavlikdeegkemilsylnqg
dfigelglfeegqersawvraktacevaeisykkfrqliqvnpdilmrlsaqmarrlqvt
sekvgnlafl
>d1rgs_1 2.77.4.2.1 (113-242) Regulatory subunit of Protein kinase A {Bovine (Bos taurus)}
rkvipkdyktmaalakaieknvlfshlddnersdifdamfpvsfiagetviqqgdegdnf
yvidqgemdvyvnnewatsvgeggsfgelaliygtpraatvkaktnvklwgidrdsyrri
lmgstlrkrk
>d1rgs_2 2.77.4.2.1 (243-376) Regulatory subunit of Protein kinase A {Bovine (Bos taurus)}
myeeflskvsilesldkwerltvadalepvqfedgqkivvqgepgdeffiilegsaavlq
rrseneefvevgrlgpsdyfgeiallmnrpraatvvargplkcvkldrprfervlgpcsd
ilkrniqqynsfvs
>d2arca_ 2.77.5.1.1 Regulatory protein AraC {Escherichia coli}
dpllpgysfnahlvagltpieangyldffidrplgmkgyilnltirgqgvvknqgrefvc
rpgdillfppgeihhygrhpearewyhqwvyfrpraywhewlnwpsifantgffrpdeah
qphfsdlfgqiinagqgegrysellainlleqlllrrmeai
>d1wapa_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
dfvvikavedgvnvigltrgtdtkfhhsekldkgeviiaqftehtsaikvrgealiqtay
gemksekk
>d1qiua2 2.78.1.1.1 (319-395) Adenovirus fibre shaft {Human adenovirus}
vsikkssglnfdntaiainagkglefdtntsespdinpiktkigsgidynengamitklg
aglsfdnsgaitignkn
>d1bdo__ 2.79.1.1.1 Biotinyl domain of acetyl-CoA carboxylase {Escherichia coli}
eisghivrspmvgtfyrtpspdakafievgqkvnvgdtlciveamkmmnqieadksgtvk
ailvesgqpvefdeplvvie
>d1dd2a_ 2.79.1.1.2 Biotin carboxyl carrier domain of transcarboxylase (TC 1.3S) {Propionibacterium freudenreichii shermanii}
agagkagegeipaplagtvskilvkegdtvkagqtvlvleamkmeteinaptdgkvekvl
vkerdavqggqglikig
>d1htp__ 2.79.1.1.3 Protein H of glycine cleavage system {Pea (Pisum sativum)}
snvldglkyapshewvkhegsvatigitdhaqdhlgevvfvelpepgvsvtkgkgfgave
svkatsdvnspisgevievntgltgkpglinsspyedgwmikikptspdelesllgakey
tkfceeedaah
>d1lac__ 2.79.1.1.4 Ipoyl domain of dihydrolipoamide acetyltransferase {Bacillus stearothermophilus}
afefklpdigegihegeivkwfvkpgdevneddvlcevqndkavveipspvkgkvleilv
pegtvatvgqtlitldapgy
>d1iyu__ 2.79.1.1.5 Ipoyl domain of dihydrolipoamide acetyltransferase {Azotobacter vinelandii}
seiirvpdiggdgeviellvktgdlieveqglvvlesakasmevpspkagvvksvsvklg
dklkegdaiielepaagar
>d1qjoa_ 2.79.1.1.6 Ipoyl domain of dihydrolipoamide acetyltransferase {Escherichia coli}
mvkevnvpdiggdevevtevmvkvgdkvaaeqslitvegdkasmevpapfagvvkelkvn
vgdkvktgslimifevegaa
>d1fyc__ 2.79.1.1.7 Ipoyl domain of dihydrolipoamide acetyltransferase {Human (Homo sapiens)}
gsnmsypphmqvllpalsptmtmgtvqrwekkvgeklsegdllaeietdkatigfevqee
gylakilvpegtrdvplgtplciivekeadisafadyrptevtdlk
>d1ghk__ 2.79.1.1.8 Lipoyl domain of the 2-oxoglutarate dehydrogenase complex {Azotobacter vinelandii}
aidikaptfpesiadgtvatwhkkpgeavkrdelivdietdkvvmevlaeadgviaeivk
negdtvlsgellgkltegg
>d1pmr__ 2.79.1.1.9 Lipoyl domain of the 2-oxoglutarate dehydrogenase complex {Escherichia coli}
ssvdilvpdlpesvadatvatwhkkpgdavvrdevlveietdkvvlevpasadgildavl
edegttvtsrqilgrlregn
>d1dv1a1 2.79.2.1.1 (331-446) Biotin carboxylase subunit of acetyl-CoA carboxylase, C-terminal domain {Escherichia coli}
rghavecrinaedpntflpspgkitrfhapggfgvrweshiyagytvppyydsmigklic
ygenrdvaiarmknalqeliidgiktnvdlqirimndenfqhggtnihylekklgl
>d1gsoa1 2.79.2.1.2 (328-426) Glycinamide ribonucleotide synthetase (GAR-syn). {Escherichia coli}
eraslgvvmaaggypgdyrtgdvihglpleevaggkvfhagtkladdeqvvtnggrvlcv
talghtvaeaqkrayalmtdihwddcfcrkdigwraier
>d1b6ra1 2.79.2.1.3 (277-355) N5-carboxyaminoimidazole ribonucleotide synthetase, AIRC, PurK {Escherichia coli}
nnpsvminligsdvnydwlklplvhlhwydkevrpgrkvghlnltdsdtsrltatleali
pllppeyasgviwaqskfg
>d1hcz_2 2.79.2.2.1 (168-230) Cytochrome f, small domain {Turnip (Brassica rapa)}
ntvynataggiiskilrkekggyeitivdasnerqvidiiprglellvsegesikldqpl
tsn
>d1cfma2 2.79.2.2.2 (169-232) Cytochrome f, small domain {Chlamydomonas reinhardtii}
tiynasaagkivaitalsekkggfevsiekangevvvdkipagpdlivkegqtvqadqpl
tnnp
>d1ci3m2 2.79.2.2.3 (170-231) Cytochrome f, small domain {Phormidium laminosum}
avynasaagvitaiakaddgsaevkirtedgttivdkipagpelivsegeevaagaaltn
np
>d1gpr__ 2.79.3.1.1 Glucose permease IIa domain, IIa-glc {Bacillus subtilis}
eplqneigeevfvspitgeihpitdvpdqvfsgkmmgdgfailpsegivvspvrgkilnv
fptkhaiglqsdggreilihfgidtvslkgegftsfvsegdrvepgqkllevdldavkpn
vpslmtpivftnlaegetvsikasgsvnreqedivkie
>d1msi__ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
aaqasvvanqlipintaltlvmmrsevvtpvgipaediprlvsmqvnravplgttlmpdm
vkgyaa
>d1ops__ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
sqsvvatqlipmntaltpammegkvtnpigipfaemsqlvgkqvntpvakgqtlmpnmvk
tyaa
>d3rdn__ 2.80.1.1.2 Antifreeze protein type III {Antarctic eel pout (Lycodichthys dearborni)}
nkasvvanqlipintaltlimmkaevvtpmgipaeeipnlvgmqvnravplgttlmpdmv
knyedgttspglk
>d1c5ea_ 2.80.2.1.1 Head decoration protein D (gpD, major capsid protein D) {Bacteriophage lambda}
sdpahtatapgglsakapamtplmldtssrklvawdgttdgaavgilavaadqtsttltf
yksgtfryedvlwpeaasdetkkrtafagtaisiv
>d4ubpb_ 2.80.3.1.2 Urease, beta-subunit {Bacillus pasteurii}
nyivpgeyrvaegeieinagrekttirvsntgdrpiqvgshihfvevnkellfdraegig
rrlnipsgtaarfepgeemeveltelggnrevfgisdltngsvdnkelilqrakelgykg
ve
>d1euwa_ 2.80.4.1.1 Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) {Escherichia coli}
mmkkidvkildprvgkefplptyatsgsagldlraclndavelapgdttlvptglaihia
dpslaammlprsglghkhgivlgnlvglidsdyqgqlmisvwnrgqdsftiqpgeriaqm
ifvpvvqaefnlvedf
>d1duta_ 2.80.4.1.2 Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) {Feline immunodeficiency virus, FIV}
miiegdgildkrsedagydllaakeihllpgevkviptgvklmlpkgywgliigkssigs
kgldvlggvidegyrgeigviminvsrksitlmerqkiaqliilpckhevleqgkvv
>d1dun__ 2.80.4.1.3 Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) {Equine infectious anemia virus, EIAV}
mlayqgtqikekrdedagfdlcvpydimipvsdtkiiptdvkiqvppnsfgwvtgkssma
kqgllinggiidegytgeiqvictnigksnikliegqkfaqliilqhhsnsrqpwdenki
>d1tul__ 2.80.5.1.1 ACMNPV telokin-like protein {Baculovirus (Autographa californica), nuclear polyhedrosis virus}
gtpdiivnaqinsedenvldfiiedeyylkkrgvgahiikvasspqlrllyknaystvsc
gnygvlcnlvqngeydlnaimfncaeiklnkgqmlfqtkiwr
>d1at0__ 2.81.1.1.1 Hedgehog {Fruit fly (Drosophila melanogaster)}
cftpestallesgvrkplgelsigdrvlsxtangqavysevilfxdrnleqxqnfvqlht
dggavltvtpahlvsvwqpesqkltfvfadrieeknqvlvrdvetgelrpqrvvkvgsvr
skgvvapltregtivvnsvaascya
>d1dfaa1 2.81.1.2.1 (1-180,416-454) PI-Scei intein {Baker's yeast (Saccharomyces cerevisiae)}
cfakgtnvlmadgsiecienievgnkvmgkdgrpreviklprgretmysvvqksqhrahk
sdssrevpellkftcnathelvvrtprsvrrlsrtikgveyfevitfemgqkkapdgriv
elvkevsksypisegperanelvesyrkasnkayfewtieardlsllgshvrkatyqtya
Xcrgfyfelqelkeddyygitlsddsdhqfllanqvvvhn
>d1am2__ 2.81.1.2.2 GyrA intein {Mycobacterium xenopi}
asitgdalvalpegesvriadivpgarpnsdnaidlkvldrhgnpvladrlfhsgehpvy
avrtveglrvtgtanhpllclvdvagvptllwklideikpgdyaviqrsafsvdcagfar
gkpefapttytvgvpglvrfleahhrdpdakaiadeltdgrfyyakvasvtdagvqpvys
lrvdtadhafitngfvshn
>d1umua_ 2.82.1.1.1 UmuD' {Escherichia coli}
dyveqridlnqlliqhpsatyfvkasgdsxidggisdgdllivdsaitashgdiviaavd
geftvkklqlrptvqlipxnsayspitissedtldvfgvvihvvk
>d1b12a_ 2.82.1.2.1 Type 1 signal peptidase {Escherichia coli}
rsfiyepfqipsgsmmptlligdfilvekfaygikdpiyqktlietghpkrgdivvfkyp
edpkldyikravglpgdkvtydpvskeltiqpgcssgqacenalpvtysnvepsdfvqtf
srrnggeatsgffevpknetkengirlserketlgdvthriltvpiaqdqvgmyyqqpgq
qlatwivppgqyfmmgdnrdnsadsrywgfvpeanlvgrataiwmsfdkqegewptglrl
sriggih
>d3ezma_ 2.83.1.1.1 Cyanovirin-N {Cyanobacterium (Nostoc ellipsosporum)}
lgkfsqtcynsaiqgsvltstcertnggyntssidlnsvienvdgslkwqpsnfietcrn
tqlagsselaaecktraqqfvstkinlddhianidgtlkye
>d1lkta_ 2.84.1.1.1 Head-binding domain of phage p22 tailspike protein {Bacteriophage p22}
anvvvsnprpiftesrsfkavangkiyigqidtdpvnpanqipvyienedgshvqitqpl
iinaagkivyngqlvkivtvqghsmaiydangsqvdyianvlky
>d1dtoa_ 2.85.1.1.2 E2 regulatory, transactivation domain {Human papillomavirus, type 16}
hmetlcqrlnvcqdkilthyendstdlrdhidywkhmrlecaiyykaremgfkhinhqvv
ptlavsknkalqaielqltletiynsqysnekwtlqdvslevyltaptgcikkhgytvev
qfdgdicntmhytnwthiyiceeasvtvvegqvdyyglyyvhegirtyfvqfkddaekys
knkvwevhaggqvilcptsvfs
>d4ubpc1 2.86.1.1.2 (1-131,435-483) alpha-Subunit of urease, composite domain {Bacillus pasteurii}
mkinrqqyaesygptvgdevrladtdlwievekdyttygdevnfgggkvlregmgengty
trtenvldllltnalildytgiykadigvkdgyivgigkggnpdimdgvtpnmivgtate
viaaegkivtaXlvlwepkffgvkadrvikggiiayaqigdpsasiptpqpvmgrrmygt
v
>d1aqt_2 2.87.1.1.1 (2-86) Epsilon subunit of F1F0-ATP synthase N-terminal domain {Escherichia coli}
styhldvvsaeqqmfsglvekiqvtgsegelgiypghaplltaikpgmirivkqhgheef
iylsggilevqpgnvtvladtairg
>d1amk__ 3.1.1.1.7 Triosephosphate isomerase {Leishmania mexicana}
sakpqpiaaanwkcngttasieklvqvfnehtishdvqcvvaptfvhiplvqaklrnpky
visaenaiaksgaftgevsmpilkdigvhwvilghserrtyygetdeivaqkvseackqg
fmviacigetlqqreanqtakvvlsqtsaiaakltkdawnqvvlayepvwaigtgkvatp
eqaqevhlllrkwvsenigtdvaaklrilyggsvnaanaatlyakpdingflvggaslkp
efrdiidatr
>d1rpxa_ 3.1.2.1.1 D-ribulose-5-phosphate 3-epimerase {Potato (Solanum tuberosum)}
srvdkfsksdiivspsilsanfsklgeqvkaieqagcdwihvdvmdgrfvpnitigplvv
dslrpitdlpldvhlmivepdqrvpdfikagadivsvhceqsstihlhrtinqikslgak
agvvlnpgtpltaieyvldavdlvlimsvnpgfggqsfiesqvkkisdlrkicaerglnp
wievdggvgpknaykvieaganalvagsavfgapdyaeaikgiktskrpe
>d1dbta_ 3.1.2.2.1 Orotidine 5'-monophosphate decarboxylase (OMP decarboxylase) {Bacillus subtilis}
mknnlpiialdfasaeetlaflapfqqeplfvkvgmelfyqegpsivkqlkerncelfld
lklhdipttvnkamkrlaslgvdlvnvhaaggkkmmqaalegleegtpagkkrpsliavt
qltstseqimkdelliekslidtvvhyskqaeesgldgvvcsvheakaiyqavspsfltv
tpgirmsedaandqvrvatpaiarekgssaivvgrsitkaedpvkaykavrlewegi
>d1dvja_ 3.1.2.2.3 Orotidine 5'-monophosphate decarboxylase (OMP decarboxylase) {Methanobacterium thermoautotrophicum}
mdvmnrlilamdlmnrddalrvtgevreyidtvkigyplvlsegmdiiaefrkrfgcrii
adfkvadipetnekicratfkagadaiivhgfpgadsvraclnvaeemgrevflltemsh
pgaemfiqgaadeiarmgvdlgvknyvgpstrperlsrlreiigqdsflispgvgaqggd
pgetlrfadaiivgrsiyladnpaaaaagiiesikdllipedpaankarkeaelaaata
>d1dqwa_ 3.1.2.2.4 Orotidine 5'-monophosphate decarboxylase (OMP decarboxylase) {Yeast (Saccharomyces cerevisiae)}
mhkatykeraathpspvaaklfnimhekqtnlcasldvrttkellelvealgpkicllkt
hvdiltdfsmegtvkplkalsakynfllfedrkfadigntvklqysagvyriaewaditn
ahgvvgpgivsglkqaaeevtkeprgllmlaelsckgslstgeytkgtvdiaksdkdfvi
gfiaqrdmggrdegydwlimtpgvglddkgdalgqqyrtvddvvstgsdiiivgrglfak
grdakvegeryrkagweaylrrcgqqd
>d1pii_2 3.1.2.3.1 (255-452) N-(5'phosphoribosyl)antranilate isomerase, PRAI {Escherichia coli}
genkvcgltrgqdakaaydagaiygglifvatsprcvnveqaqevmaaaplqyvgvfrnh
diadvvdkakvlslaavqlhgneeqlyidtlrealpahvaiwkalsvgetlparefqhvd
kyvldngqggsgqrfdwsllngqslgnvllagglgadncveaaqtgcagldfnsavesqp
gikdarllasvfqtlray
>d1nsj__ 3.1.2.3.2 N-(5'phosphoribosyl)antranilate isomerase, PRAI {Thermotoga maritima}
mvrvkicgitnledalfsvesgadavgfvfypkskryispedarrisvelppfvfrvgvf
vneepekildvasyvqlnavqlhgeepielcrkiaerilvikavgvsnerdmeralnyre
fpilldtktpeyggsgktfdwslilpyrdrfrylvlsgglnpenvrsaidvvrpfavdvs
sgveafpgkkdhdsikmfiknakgl
>d1a53__ 3.1.2.3.4 Indole-3-glycerophosphate synthase, IPGS {Sulfolobus solfataricus}
prylkgwlkdvvqlslrrpsfrasrqrpiislnerilefnkrnitaiiaeykrkspsgld
verdpieyskfmeryavglsilteekyfngsyetlrkiassvsipilmkdfivkesqidd
aynlgadtvllivkiltereleslleyarsygmeplieindendldialrigarfigins
rdletleinkenqrklismipsnvvkvaesgiserneieelrklgvnafligsslmrnpe
kikefil
>d2tysa_ 3.1.2.3.5 Trp synthase alpha-subunit {Salmonella typhimurium}
meryenlfaqlndrregafvpfvtlgdpgieqslkiidtlidagadalelgvpfsdplad
gptiqnanlrafaagvtpaqcfemlalirekhptipigllmyanlvfnngidafyarceq
vgvdsvlvadvpveesapfrqaalrhniapificppnadddllrqvasygrgytyllsrs
gvtgaenrgalplhhlieklkeyhaapalqgfgisspeqvsaavragaagaisgsaivki
ieknlaspkqmlaelrsfvsamkaasra
>d2tpsa_ 3.1.3.1.1 Thiamin phosphate synthase {Bacillus subtilis}
hgirmtrisremmkellsvyfimgsnntkadpvtvvqkalkggatlyqfrekggdaltge
arikfaekaqaacreagvpfivnddvelalnlkadgihigqedanakevraaigdmilgv
sahtmsevkqaeedgadyvglgpiyptetkkdtravqgvslieavrrqgisipivgiggi
tidnaapviqagadgvsmisaisqaedpesaarkfreeiqtyktgr
>d2dora_ 3.1.4.1.1 Dihydroorotate dehydrogenase A {Lactococcus lactis}
mlnttfanakfanpfmnasgvhcmtiedleelkasqagayitksstlekregnplpryvd
lelgsinsmglpnlgfdyyldyvlknqkenaqegpiffsiagmsaaeniamlkkiqesdf
sgitelnlscpnvpgkpqlaydfeatekllkevftfftkplgvklppyfdlvhfdimaei
lnqfpltyvnsvnsignglfidpeaesvvikpkdgfggiggayikptalanvrafytrlk
peiqiigtggietgqdafehllcgatmlqigtalhkegpaifdriikeleeimnqkgyqs
iadfhgklksl
>d1oyb__ 3.1.4.1.2 Old yellow enzyme (OYE) {Brewer's yeast (Saccharomyces carlsbergensis)}
sfvkdfkpqalgdtnlfkpikignnellhravippltrmralhpgnipnrdwaveyytqr
aqrpgtmiitegafispqaggydnapgvwseeqmvewtkifnaihekksfvwvqlwvlgw
aafpdnlardglrydsasdnvfmdaeqeakakkannpqhsltkdeikqyikeyvqaakns
iaagadgveihsangyllnqfldphsntrtdeyggsienrarftlevvdalveaighekv
glrlspygvfnsmsggaetgivaqyayvagelekrakagkrlafvhlveprvtnpflteg
egeyeggsndfvysiwkgpviragnfalhpevvreevkdkrtligygrffisnpdlvdrl
ekglplnkydrdtfyqmsahgyidyptyeealklgwdkk
>d1gox__ 3.1.4.1.4 Glycolate oxidase {Spinach (Spinacia oleracea)}
meitnvneyeaiakqklpkmvydyyasgaedqwtlaenrnafsrilfrprilidvtnidm
tttilgfkismpimiaptamqkmahpegeyataraasaagtimtlsswatssveevastg
pgirffqlyvykdrnvvaqlvrraeragfkaialtvdtprlgrreadiknrfvlppfltl
knfegidlgkmdkandsglssyvagqidrslswkdvawlqtitslpilvkgvitaedarl
avqhgaagiivsnhgarqldyvpatimaleevvkaaqgripvfldggvrrgtdvfkalal
gaagvfigrpvvfslaaegeagvkkvlqmmrdefeltmalsgcrslkeisrshiaadwd
>d1djna1 3.1.4.1.6 (1-340) Trimethylamine dehydrogenase, N-terminal domain {Methylophilus methylotrophus w3a1}
ardpkhdilfepiqigpktlrnrfyqvphcigagsdkpgfqsahrsvkaeggwaalntey
csinpesddthrlsariwdegdvrnlkamtdevhkygalagvelwyggahapnmesratp
rgpsqyasefetlsyckemdlsdiaqvqqfyvdaakrsrdagfdivyvygahsylplqfl
npyynkrtdkyggslenrarfwletlekvkhavgsdcaiatrfgvdtvygpgqieaevdg
qkfvemadslvdmwditigdiaewgedagpsrfyqqghtipwvklvkqvskkpvlgvgry
tdpekmieivtkgyadiigcarpsiadpflpqkveqgryd
>d1zfja1 3.1.5.1.2 (2-94,221-492) Inosine monophosphate dehydrogenase (IMPDH) {Streptococcus pyogenes}
snwdtkflkkgytfddvllipaeshvlpnevdlktkladnltlnipiitaaxdtvtgskx
aiaiaragglgvihknxsiteqaeevrkvkrseXgrllvaaavgvtsdtferaealfeag
adaividtahghsagvlrkiaeirahfpnrtliagniataegaralydagvdvvkvgigp
gsicttrvvagvgvpqvtaiydaaavareygktiiadggikysgdivkalaaggnavxlg
sxfagtdeapgeteiyqgrkyktyrgxgsiaaxkkgssdryfqgsvneanklvpegiegr
vaykgaasdivfqxlggirsgxgyvgagdiqelhenaqfvexsgaglieshphdvqitne
apnysv
>d1bd0a2 3.1.6.1.1 (12-244) Alanine racemase {Bacillus stearothermophilus}
vdldaiydnvenlrrllpddthimavvkanayghgdvqvartaleagasrlavafldeal
alrekgieapilvlgasrpadaalaaqqrialtvfrsdwleeasalysgpfpihfhlkmd
tgmgrlgvkdeeetkrivalierhphfvleglythfatadevntdyfsyqytrflhmlew
lpsrpplvhcansaaslrfpdrtfnmvrfgiamyglapspgikpllpyplkea
>d7odca2 3.1.6.1.2 (44-283) Eukaryotic ornithine decarboxylase {Mouse (Mus musculus)}
dlgdilkkhlrwlkalprvtpfyavkcndsraivstlaaigtgfdcaskteiqlvqglgv
paerviyanpckqvsqikyaasngvqmmtfdseielmkvarahpkaklvlriatddskav
crlsvkfgatlktsrlllerakelnidvigvsfhvgsgctdpdtfvqavsdarcvfdmat
evgfsmhlldigggfpgsedtklkfeeitsvinpaldkyfpsdsgvriiaepgryyvasa
>d1ct5a_ 3.1.6.2.1 "Hypothetical" protein ybl036c {Baker's yeast (Saccharomyces cerevisiae)}
tgitydedrktqliaqyesvrevvnaeaknvhvnenaskilllvvsklkpasdiqilydh
gvrefgenyvqeliekakllpddikwhfigglqtnkckdlakvpnlysvetidslkkakk
lnesrakfqpdcnpilcnvqintshedqksglnneaeifevidfflseeckyiklnglxt
igswnvshedskenrdfatlvewkkkidakfgtslklsxgxsadfreairqgtaevrigt
difg
>d1frb__ 3.1.7.1.1 FR-1 (fibroblast growth factor-induced) protein {Mouse (Mus musculus)}
atfvelstkakmpivglgtwksppnqvkeavkaaidagyrhidcayaycnenevgeaiqe
kikekavqredlfivsklwptcfekkllkeafqktltdlkldyldlylihwpqglqpgke
lfpkddqgriltskttfleawegmeelvdqglvkalgvsnfnhfqierllnkpglkhkpv
tnqvechpyltqekliqychskgisvtaysplgspdrpsakpedpslledpkikeiaakh
ektsaqvlirfhiqrnvvvipksvtpsriqeniqvfdfqlsdeematilsfnrnwracll
petvnmeeypydaey
>d1qrqa_ 3.1.7.1.2 Voltage-dependent K+ channel beta subunit {Rat (Rattus norvegicus)}
lqfyrnlgksglrvsclglgtwvtfggqitdemaehlmtlaydnginlfdtaevyaagka
evvlgniikkkgwrrsslvittkifwggkaeterglsrkhiieglkaslerlqleyvdvv
fanrpdpntpmeetvramthvinqgmamywgtsrwssmeimeaysvarqfnlippiceqa
eyhmfqrekvevqlpelfhkigvgamtwsplacgivsgkydsgippysraslkgyqwlkd
kilseegrrqqaklkelqaiaerlgctlpqlaiawclrnegvssvllgasnaeqlmenig
aiqvlpklsssivheidsilgnkpy
>d1bli_2 3.1.8.1.1 (3-393) Bacterial alpha-amylase (BLA) {Bacillus licheniformis}
lngtlmqyfewympndgqhwkrlqndsaylaehgitavwippaykgtsqadvgygaydly
dlgefhqkgtvrtkygtkgelqsaikslhsrdinvygdvvinhkggadatedvtavevdp
adrnrvisgehlikawthfhfpgrgstysdfkwhwyhfdgtdwdesrklnriykfqgkaw
dwevsnefgnydylmyadidydhpdvaaeikrwgtwyanelqldgfrldavkhikfsflr
dwvnhvrektgkemftvaeywsydlgalenylnktnfnhsvfdvplhyqfhaastqgggy
dmrkllngtvvskhplksvtfvdnhdtqpgqslestvqtwfkplayafiltresgypqvf
ygdmygtkgdsqreipalkhkiepilkarkq
>d1bag_2 3.1.8.1.3 (1-347) Bacterial alpha-amylase (BLA) {Bacillus subtilis}
ltapsiksgtilhawnwsfntlkhnmkdihdagytaiqtspinqvkegnqgdksmsnwyw
lyqptsyqignrylgteqefkemcaaaeeygikvivdavinhttfdyaaisnevksipnw
thgntqiknwsdrwdvtqnsllglydwntqntqvqsylkrfleralndgadgfrfdaakh
ielpddgsygsqfwpnitntsaefqygqilqdsasrdaayanymdvtasnyghsirsalk
nrnlgvsnishyasdvsadklvtwveshdtyanddeestwmsdddirlgwaviasrsgst
plffsrpegggngvrfpgksqigdrgsalfedqaitavnrfhnvmag
>d1qhoa4 3.1.8.1.6 (1-407) Cyclodextrin glycosyltransferase {Bacillus stearothermophilus maltogenic alpha-amylase}
sssasvkgdviyqiiidrfydgdttnnnpaksyglydptkskwkmywggdlegvrqklpy
lkqlgvttiwlspvldnldtlagtdntgyhgywtrdfkqieehfgnwttfdtlvndahqn
gikvivdfvpnhstpfkandstfaeggalynngtymgnyfddatkgyfhhngdisnwddr
yeaqwknftdpagfsladlsqengtiaqyltdaavqlvahgadglridavkhfnsgfsks
ladklyqkkdiflvgewygddpgtanhlekvryannsgvnvldfdlntvirnvfgtftqt
mydlnnmvnqtgneykykenlitfidnhdmsrflsvnsnkanlhqalafiltsrgtpsiy
ygteqymaggndpynrgmmpafdttttafkevstlaglrrnnaaiqy
>d1jae_2 3.1.8.1.11 (2-378) Animal alpha-amylase {Yellow mealworm (Tenebrio molitor), larva}
kdanfasgrnsivhlfewkwndiadecerflqpqgfggvqisppneylvadgrpwweryq
pvsyiintrsgdesaftdmtrrcndagvriyvdavinhmtgmngvgtsgssadhdgmnyp
avpygsgdfhspcevnnyqdadnvrncelvglrdlnqgsdyvrgvlidymnhmidlgvag
frvdaakhmspgdlsvifsglknlntdygfadgarpfiyqevidlggeaiskneytgfgc
vlefqfgvslgnafqggnqlknlanwgpewgllegldavvfvdnhdnqrtggsqiltykn
pkpykmaiafmlahpygttrimssfdftdndqgppqdgsgnlispginddntcsngyvce
hrwrqvygmvgfrnave
>d1smaa3 3.1.8.1.14 (124-505) Maltogenic amylase, central domain {Thermus sp.}
dlfqapdwvkdtvwyqifperfangnpaispkgarpwgsedptptsffggdlqgiidhld
yladlgitgiyltpifrapsnhkydtadyfeidphfgdketlktlvkrchekgirvmlda
vfnhcgyefapfqdvlkngaasrykdwfhirefplqteprpnydtfafvphmpklntahp
evkrylldvatywirefdidgwrldvaneidhqfwrefrqavkalkpdvyilgeiwhdam
pwlrgdqfdavmnypladaalrffakedmsasefadrlmhvlhsypkqvneaafnllgsh
dtprlltvcggdvrkvkllflfqltftgspciyygdeigmtggndpecrkcmvwdpekqn
kelyehvkqlialrkqyralrr
>d1bf2_3 3.1.8.1.16 (163-637) Isoamylase, central domain {Pseudomonas amyloderamosa}
pstqstgtkptraqkddviyevhvrgfteqdtsipaqyrgtyygaglkasylaslgvtav
eflpvqetqndandvvpnsdanqnywgymtenyfspdrryaynkaaggptaefqamvqaf
hnagikvymdvvynhtaeggtwtssdpttatiyswrgldnatyyeltsgnqyfydntgig
anfntyntvaqnlivdslaywantmgvdgfrfdlasvlgnsclngaytasapncpnggyn
fdaadsnvainrilreftvrpaaggsgldlfaepwaiggnsyqlggfpqgwsewnglfrd
slrqaqnelgsmtiyvtqdandfsgssnlfqssgrspwnsinfidvhdgmtlkdvyscng
annsqawpygpsdggtstnyswdqgmsagtgaavdqrraartgmafemlsagtplmqggd
eylrtlqcnnnaynldssanwltyswttdqsnfytfaqrliafrkahpalrpssw
>d1jdc_2 3.1.8.1.17 (1-357) G4-amylase (1,4-alpha-D-glucan maltotetrahydrolase) {Pseudomonas stutzeri}
dqagkspnavryhggdeiilqgfhwnvvreapndwynilrqqaatiaadgfsaiwmpvpw
rdfsswsdgsksgggegyfwhdfnkngrygsdaqlrqaasalggagvkvlydvvpnhmnr
gypdkeinlpagqgfwrndcadpgnypndcddgdrfiggdadlntghpqvygmfrdeftn
lrsqygaggfrfdfvrgyapervnswmtdsadnsfcvgqlwkgpseypnwdwrntaswqq
iikdwsdrakcpvfdfalkermqngsiadwkhglngnpdprwrevavtfvdnhdtgyspg
qnggqhhwalqdglirqayayiltspgtpvvywdhmydwgygdfirqliqvrraagv
>d1uok_2 3.1.8.1.19 (1-479) Oligo-1,6, glucosidase {Bacillus cereus}
mekqwwkesvvyqiyprsfmdsngdgigdlrgiiskldylkelgidviwlspvyespndd
ngydisdyckimnefgtmedwdellhemhernmklmmdlvvnhtsdehnwfiesrkskdn
kyrdyyiwrpgkegkepnnwgaafsgsawqydemtdeyylhlfskkqpdlnwdnekvrqd
vyemmkfwlekgidgfrmdvinfiskeeglptveteeegyvsghkhfmngpnihkylhem
neevlshydimtvgempgvtteeaklytgeerkelqmvfqfehmdldsgeggkwdvkpcs
lltlkenltkwqkalehtgwnslywnnhdqprvvsrfgndgmyriesakmlatvlhmmkg
tpyiyqgeeigmtnvrfesideyrdietlnmykekvmergediekvmqsiyikgrdnart
pmqwddqnhagfttgepwitvnpnykeinvkqaiqnkdsifyyykklielrknneivvy
>d1byb__ 3.1.8.2.1 beta-Amylase {Soybean (Glycine max)}
snmllnyvpvyvmlplgvvnvdnvfedpdglkeqllqlraagvdgvmvdvwwgiielkgp
kqydwrayrslfqlvqecgltlqaimsfhqcggnvgdivnipipqwvldigesnhdifyt
nrsgtrnkeyltvgvdnepifhgrtaieiysdymksfrenmsdflesgliidievglgpa
gelrypsypqsqgwefprigefqcydkylkadfkaavaraghpewelpddagkyndvpes
tgffksngtyvtekgkffltwysnkllnhgdqildeankaflgckvklaikvsgihwwyk
venhaaeltagyynlndrdgyrpiarmlsrhhailnftclemrdseqpsdaksgpqelvq
qvlsggwredirvagenalprydataynqiilnakpqgvnnngppklsmfgvtylrlsdd
llqksnfnifkkfvlkmhadqdycanpqkynhaitplkpsapkipievlleatkptlpfp
wlpetdmkvdg
>d1edg__ 3.1.8.3.3 Endoglucanase CelA {Clostridium cellulolyticum}
mydaslipnlqipqknipnndgmnfvkglrlgwnlgntfdafngtnitneldyetswsgi
kttkqmidaikqkgfntvripvswhphvsgsdykisdvwmnrvqevvnycidnkmyviln
thhdvdkvkgyfpssqymasskkyitsvwaqiaarfanydehlifegmneprlvghanew
wpeltnsdvvdsincinqlnqdfvntvratggknasrylmcpgyvaspdgatndyfrmpn
disgnnnkiivsvhaycpwnfaglamadggtnawnindskdqsevtwfmdniynkytsrg
ipviigecgavdknnlktrveymsyyvaqakargilcilwdnnnfsgtgelfgffdrrsc
qfkfpeiidgmvkyafglin
>d1ceo__ 3.1.8.3.5 Endoglucanase CelC {Clostridium thermocellum}
mvsfkaginlggwisqyqvfskehfdtfitekdietiaeagfdhvrlpfdypiiesddnv
geykedglsyidrclewckkynlglvldmhhapgyrfqdfktstlfedpnqqkrfvdiwr
flakryinerehiafellnqvvepdstrwnklmlecikaireidstmwlyiggnnynspd
elknladidddyivynfhfynpfffthqkahwsesamaynrtvkypgqyegieefvknnp
kysfmmelnnlklnkellrkdlkpaiefrekkkcklycgefgviaiadlesrikwhedyi
slleeydiggavwnykkmdfeiynedrkpvsqelvnilar
>d1ecea_ 3.1.8.3.6 Endocellulase E1 {Acidothermus cellulolyticus}
agggywhtsgreildannvpvriaginwfgfetcnyvvhglwsrdyrsmldqikslgynt
irlpysddilkpgtmpnsinfyqmnqdlqgltslqvmdkivayagqiglriildrhrpdc
sgqsalwytssvseatwisdlqalaqrykgnptvvgfdlhnephdpacwgcgdpsidwrl
aaeragnavlsvnpnllifvegvqsyngdsywwggnlqgagqypvvlnvpnrlvysahdy
atsvypqtwfsdptfpnnmpgiwnknwgylfnqniapvwlgefgttlqsttdqtwlktlv
qylrptaqygadsfqwtfwswnpdsgdtggilkddwqtvdtvkdgylapikssifdpv
>d7a3ha_ 3.1.8.3.7 Endoglucanase Cel5a {Bacillus agaradherans}
svveehgqlsisngelvnergeqvqlkgmsshglqwygqfvnyesmkwlrddwginvfra
amytssggyiddpsvkekvkeaveaaidldiyviidwhilsdndpniykeeakdffdems
elygdypnviyeianepngsdvtwgnqikpyaeevipiirnndpnniiivgtgtwsqdvh
haadnqladpnvmyafhfyagthgqnlrdqvdyaldqgaaifvsewgtsaatgdggvfld
eaqvwidfmdernlswanwslthkdessaalmpganptggwteaelspsgtfvrekires
>d1bqca_ 3.1.8.3.9 Beta-mannanase {Thermomonospora fusca}
atglhvkngrlyeangqefiirgvshphnwypqhtqafadikshgantvrvvlsngvrws
kngpsdvanvislckqnrlicmlevhdttgygeqsgastldqavdywielksvlqgeedy
vlinignepygndsatvaawatdtsaaiqrlraagfehtlvvdapnwgqdwtntmrnnad
qvyasdptgntvfsihmygvysqastitsylehfvnaglpliigefghdhsdgnpdedti
maeaerlklgyigwswsgngggveyldmvynfdgdnlspwgerifygpngiastakeavi
fg
>d1cz1a_ 3.1.8.3.10 Exo-beta-(1,3)-glucanase {Candida albicans}
awdydnnvirgvnlggwfvlepymtpslfepfqngndqsgvpvdeyhwtqtlgkeaalri
lqkhwstwiteqdfkqisnlglnfvripigywafqlldndpyvqgqvqylekalgwarkn
nirvwidlhgapgsqngfdnsglrdsynfqngdntqvtlnvlntifkkyggneysdvvig
iellneplgpvlnmdklkqffldgynslrqtgsvtpviihdafqvfgywnnfltvaegqw
nvvvdhhhyqvfsggelsrnindhisvacnwgwdakkeshwnvagewsaaltdcakwlng
vnrgaryegaydnapyigscqplldisqwsdehktdtrryieaqldafeytggwvfwswk
tenapewsfqtltynglfpqpvtdrqfpnqcgfh
>d1aq0a_ 3.1.8.3.12 Plant beta-glucanases {Barley (Hordeum vulgare), 1,3-1,4-beta-glucanase}
igvcygmsannlpaastvvsmfksngiksmrlyapnqaalqavggtginvvvgapndvls
nlaaspaaaaswvksniqaypkvsfryvcvgnevaggatrnlvpamknvhgalvaaglgh
ikvttsvsqailgvfsppsagsftgeaaafmgpvvqflartnaplmaniypylawaynps
amdmgyalfnasgtvvrdgaygyqnlfdttvdafytamgkhggssvklvvsesgwpsggg
taatpanarfynqhlinhvgrgtprhpgaietyifamfnenqkdsgveqnwglfypnmqh
vypinf
>d1bgla5 3.1.8.3.13 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bhga3 3.1.8.3.14 (329-632) beta-Glucuronidase, domain 3 {Human (Homo sapiens)}
vavtksqflingkpfyfhgvnkhedadirgkgfdwpllvkdfnllrwlganafrtshypy
aeevmqmcdrygivvidecpgvglalpqffnnvslhhhmqvmeevvrrdknhpavvmwsv
anepashlesagyylkmviahtksldpsrpvtfvsnsnyaadkgapyvdviclnsyyswy
hdyghleliqlqlatqfenwykkyqkpiiqseygaetiagfhqdpplmfteeyqkslleq
yhlgldqkrrkyvvgeliwnfadfmteqsptrvlgnkkgiftrqrqpksaafllrerywk
iane
>d1taxa_ 3.1.8.3.18 Xylanase A, catalytic core {Thermoascus aurantiacus}
asaqsvdqlikargkvyfgvatdqnrlttgknaaiiqanfgqvtpensmkwdatepsqgn
fnfagadylvnwaqqngklirghtlvwhsqlpswvtsitdkntltnvmknhittlmtryk
gkirawdvvneafnqngslrstvflnvigedyipiafqtaraadpnaklyindynldsat
ypktqaivnrvkqwraagvpidgigsqthlsagqgagvlnalpllasagtpevaiteldv
agasptdyvnvvnaclnvsscvgitvwgvadpdswrasttpllfdgnfnpkpaynaivqn
lq
>d2myr__ 3.1.8.4.1 Myrosinase {White mustard (Sinapis alba)}
eitcqennpftcgntdglnsssfeadfifgvassayqiegtigrglniwdgfthrypdks
gpdhgngdttcdsfsywqkdidvldelnatgyrfsiawsriiprgkrsrgvnqkgidyyh
glidglikkgitpfvtlfhwdlpqtlqdeyegfldpqiiddfkdyadlcfeefgdsvkyw
ltinqlysvptrgygsaldapgrcsptvdpscyagnsstepyivahhqllahakvvdlyr
knythqggkigptmitrwflpyndtdrhsiaatermkqfflgwfmgpltngtypqimidt
vgarlptfspeetnlvkgsydflglnyyftqyaqpspnpvnatnhtammdagakltyina
sghyigplfesdggdgssniyyypkgiysvmdyfknkyynpliyvtengistpgsenrke
smldytridylcshlcflnkvikekdvnvkgylawalgdnyefnngftvrfglsyinwnn
vtdrdlkksgqwyqkfisp
>d1qvba_ 3.1.8.4.7 beta-Glycosidase {Thermosphaera aggregans}
mkfpkdfmigyssspfqfeagipgsedpnsdwwvwvhdpentaaglvsgdfpengpgywn
lnqndhdlaeklgvntirvgvewsrifpkptfnvkvpverdengsivhvdvddkaverld
elankeavnhyvemykdwvergrklilnlyhwplplwlhnpimvrrmgpdrapsgwlnee
svvefakyaayiawkmgelpvmwstmnepnvvyeqgymfvkggfppgylsleaadkarrn
miqaharaydnikrfskkpvgliyafqwfellegpaevfdkfkssklyyftdivskgssi
inveyrrdlanrldwlgvnyysrlvykivddkpiilhgygflctpggispaenpcsdfgw
evypeglylllkelynrygvdlivtengvsdsrdalrpaylvshvysvwkaanegipvkg
ylhwsltdnyewaqgfrqkfglvmvdfktkkrylrpsalvfreiathngipdelqhltli
q
>d1nar__ 3.1.8.5.2 Seed storage protein {Vicia narbonensis, Narbonin}
pkpifreyigvkpnsttlhdfpteiintetlefhyilgfaiesyyesgkgtgtfeeswdv
elfgpekvknlkrrhpevkvvisiggrgvntpfdpaeenvwvsnakeslkliiqkysdds
gnlidgidihyehirsdepfatlmgqlitelkkdddlninvvsiapsennsshyqklyna
kkdyinwvdyqfsnqqkpvstddafveifkslekdyhphkvlpgfstdpldtkhnkitrd
ifiggctrlvqtfslpgvffwnandsvipkrdgdkpfiveltlqqllaa
>d1cnv__ 3.1.8.5.3 Seed storage protein {Jack bean (Canavalia ensiformis), Concanavalin B}
dissteiavywgqredgllrdtcktnnykivfisfldkfgceirkpelelegvcgpsvgn
pcsflesqikecqrmgvkvflalggpkgtysacsadyakdlaeylhtyflserregplgk
valdgihfdiqkpvdelnwdnlleelyqikdvyqstfllsaapgclspdeyldnaiqtrh
fdyifvrfyndrscqystgniqrirnawlswtksvyprdknlflelpasqatapgggyip
psaligqvlpylpdlqtryagialwnrqadketgystniiryl
>d2ebn__ 3.1.8.5.4 Endo-beta-N-acetylglucosaminidase {Flavobacterium meningosepticum, endoglycosidase F1}
ttkaniklfsftevndtnplnnlnftlknsgkplvdmvvlfsaninydaandkvfvsnnp
nvqhlltnrakylkplqdkgikvilsilgnhdrsgianlstarakafaqelkntcdlynl
dgvffddeysayqtpppsgfvtpsnnaaarlayetkqampnklvtvyvysrtssfptavd
gvnagsyvdyaihdyggsydlatnypglaksgmvmssqefnqgryataqalrnivtkgyg
ghmifamdpnrsnftsgqlpalkliakelygdelvysntpyskdw
>d1edqa2 3.1.8.5.6 (133-443,517-563) Chitinase A, central domain {Serratia marcescens}
tdgshlaplkeplleknkpykqnsgkvvgsyfvewgvygrnftvdkipaqnlthllygfi
picggngindslkeiegsfqalqrscqgredfkvsihdpfaalqkaqkgvtawddpykgn
fgqlmalkqahpdlkilpsiggwtlsdpfffmgdkvkrdrfvgsvkeflqtwkffdgvdi
dwefpggkganpnlgspqdgetyvllmkelramldqlsvetgrkyeltsaisagkdkidk
vaynvaqnsmdhiflmsydfygafdlknlghqtalnapawkpdtayttvngvnallaqgv
kpgkivvgtamXdarsvqakgkyvldkqlgglfsweidadngdilnsmnaslgnsagvq
>d1qba_3 3.1.8.6.1 (338-780) Bacterial chitobiase, catalytic domain {Serratia marcescens}
fpyrgifldvarnfhkkdavlrlldqmaayklnkfhfhlsddegwrieipglpeltevgg
qrchdlsettcllpqygqgpdvyggffsrqdyidiikyaqarqievipeidmpaharaav
vsmearykklhaagkeqeanefrlvdptdtsnttsvqffnrqsylnpcldssqrfvdkvi
geiaqmhkeagqpiktwhfggdeaknirlgagytdkakpepgkgiidqgnedkpwaksqv
cqtmikegkvadmehlpsyfgqevsklvkahgidrmqawqdglkdaesskafatsrvgvn
fwdtlywggfdsvndwankgyevvvsnpdyvymdfpyevnpdergyywgtrfsderkvfs
fapdnmpqnaetsvdrdgnhfnaksdkpwpgayglsaqlwsetqrtdpqmeymifprals
vaerswhragweqdyragreykg
>d1ex1a1 3.1.8.7.1 (1-388) Beta-D-glucan exohydrolase, N-terminal domain {Barley (Hordeum vulgare)}
dyvlykdatkpvedrvadllgrmtlaekigqmtqierlvatpdvlrdnfigsllsgggsv
prkgatakewqdmvdgfqkacmstrlgipmiygidavhgqnnvygatifphnvglgatrd
pylvkrigeatalevratgiqyafapciavcrdprwgrcyesysedrrivqsmtelipgl
qgdvpkdftsgmpfvagknkvaacakhfvgdggtvdginenntiinreglmnihmpaykn
amdkgvstvmisysswngvkmhanqdlvtgylkdtlkfkgfvisdwegidrittpagsdy
sysvkasilagldmimvpnkyqqfisiltghvnggvipmsriddavtrilrvkftmglfe
npyadpamaeqlgkqehrdlareaarks
>d1a4ma_ 3.1.9.1.1 Adenosine deaminase (ADA) {Mouse (Mus musculus)}
tpafnkpkvelhvhldgaikpetilyfgkkrgialpadtveelrniigmdkplslpgfla
kfdyympviagcreaikriayefvemkakegvvyvevrysphllanskvdpmpwnqtegd
vtpddvvdlvnqglqegeqafgikvrsilccmrhqpswslevlelckkynqktvvamdla
gdetiegsslfpghveayegavkngihrtvhagevgspevvreavdilktervghgyhti
edealynrllkenmhfevcpwssyltgawdpktthavvrfkndkanyslntddplifkst
ldtdyqmtkkdmgfteeefkrlninaakssflpeeekkellerlyreyq
>d4ubpc2 3.1.9.2.2 (132-434,484-570) alpha-subunit of urease, catalytic domain {Bacillus pasteurii}
ggidthvhfinpdqvdvalangittlfgggtgpaegskattvtpgpwniekmlksteglp
invgilgkghgssiapimeqidagaaglxihedwgatpasidrsltvadeadvqvaihsd
tlneagfledtlraingrvihsfhvegaggghapdimamaghpnvlpsstnptrpftvnt
idehldmlmvchhlkqnipedvafadsrirpetiaaedilhdlgiismmstdalamgrag
emvlrtwqtadkmkkqrgplaeekngsdnfrlkryvskytinpaiaqgiahevgsieegk
fadXgdlihdtnitfmskssiqqgvpaklglkrrigtvkncrnigkkdmkwndvttdidi
npetyevkvdgevltcepvkelpmaqryflf
>d1psca_ 3.1.9.3.1 Phosphotriesterase {Pseudomonas diminuta}
drintvrgpitiseagftlthehicgssagflrawpeffgsrkalaekavrglrraraag
vrtivdvstfdigrdvsllaevsraadvhivaatglwfdpplsmrlrsveeltqfflrei
qygiedtgiragiikvattgkatpfqelvlkaaaraslatgvpvtthtaasqrdgeqqaa
ifeseglspsrvcighsddtddlsyltalaargyligldhiphsaiglednasasallgi
rswqtrallikalidqgymkqilvsndwlfgfssyvtnimdvmdrvnpdgmafiplrvip
flrekgvpqetlagitvtnparflsptlr
>d1bf6a_ 3.1.9.3.2 Phosphotriesterase homology protein {Escherichia coli}
sfdptgytlahehlhidlsgfknnvdcrldqyaficqemndlmtrgvrnviemtnrymgr
naqfmldvmretginvvactgyyqdaffpehvatrsvqelaqemvdeieqgidgtelkag
iiaeigtsegkitpleekvfiaaalahnqtgrpisthtsfstmgleqlallqahgvdlsr
vtvghcdlkdnldnilkmidlgayvqfdtigknsyypdekriamlhalrdrgllnrvmls
mditrrshlkanggygydyllttfipqlrqsgfsqadvdvmlrenpsqffq
>d1nal1_ 3.1.10.1.1 N-acetylneuraminate lyase {Escherichia coli}
nlrgvmaalltpfdqqqaldkaslrrlvqfniqqgidglyvggstgeafvqslsereqvl
eivaeegkgkikliahvgcvttaesqqlaasakrygfdavsavtpfyypfsfeehcdhyr
aiidsadglpmvvynipalsgvkltldqintlvtlpgvgalkqtsgdlyqmeqirrehpd
lvlyngydeifasgllagadggigstynimgwryqgivkalkegdiqtaqklqtecnkvi
dlliktgvfrglktvlhymdvvsvplcrkpfgpvdekyqpelkalaqqlmq
>d1dhpa_ 3.1.10.1.2 Dihydrodipicolinate synthase {Escherichia coli}
mftgsivaivtpmdekgnvcraslkklidyhvasgtsaivsvgttgesatlnhdehadvv
mmtldladgripviagtganataeaisltqrfndsgivgcltvtpyynrpsqeglyqhfk
aiaehtdlpqilynvpsrtgcdllpetvgrlakvkniigikeatgnltrvnqikelvsdd
fvllsgddasaldfmqlgghgvisvtanvaardmaqmcklaaeghfaearvinqrlmplh
nklfvepnpipvkwackelglvatdtlrlpmtpitdsgretvraalkhagll
>d1fbaa_ 3.1.10.1.4 Fructose-1,6-bisphosphate aldolase {Drosophila melanogaster, strain sevelen (wild type, pupea)}
xttyfnypskelqdelreiaqkivapgkgilaadesgptmgkrlqdigventednrrayr
qllfstdpklaenisgvilfhetlyqkaddgtpfaeilkkkgiilgikvdkgvvplfgse
devttqglddlaarcaqykkdgcdfakwrcvlkigkntpsyqsilenanvlaryasicqs
qrivpivepevlpdgdhdldraqkvtetvlaavykalsdhhvylegtllkpnmvtagqsa
kkntpeeialatvqalrrtvpaavtgvtflsggqseeeatvnlsainnvplirpwaltfs
ygralqasvlrawagkkeniaagqnellkrakangdaaqgkyvagsagagsgslfvanha
y
>d1qfea_ 3.1.10.1.7 Type I 3-dehydroquinate dehydratase {Salmonella typhi}
mktvtvknliigegmpkiivslmgrdinsvkaealayreatfdilewrvdhfmdiastqs
vltaarvirdampdipllftfrsakeggeqtittqhyltlnraaidsglvdmidlelftg
dadvkatvdyahahnvyvvmsnhdfhqtpsaeemvsrlrkmqalgadipkiavmpqskhd
vltlltatlemqqhyadrpvitmsmakegvisrlagevfgsaatfgavkqasapgqiavn
dlrsvlmilhna
>d1onra_ 3.1.10.1.8 Transaldolase {Escherichia coli}
tdkltslrqyttvvadtgdiaamklyqpqdattnpslilnaaqipeyrkliddavawakq
qsndraqqivdatdklavnigleilklvpgristevdarlsydteasiakakrliklynd
agisndriliklastwqgiraaeqlekegincnltllfsfaqaracaeagvflispfvgr
ildwykantdkkeyapaedpgvvsvseiyqyykehgyetvvmgasfrnigeilelagcdr
ltiapallkelaesegaierklsytgevkarpariteseflwqhnqdpmavdklaegirk
faidqeklekmigdll
>d1dosa_ 3.1.10.2.1 Fructose-bisphosphate aldolase {Escherichia coli}
skifdfvkpgvitgddvqkvfqvakennfalpavncvgtdsinavletaakvkapvivqf
snggasfiagkgvksdvpqgaailgaisgahhvhqmaehygvpvilhtdhcakkllpwid
glldagekhfaatgkplfsshmidlseeslqenieicskylermskigmtleielgctgg
eedgvdnshmdasalytqpedvdyaytelskisprftiaasfgnvhgvykagnvvltpti
lrdsqeyvskkhnlphnslnfvfhggsgstaqeikdsvsygvvkmnidtdtqwatwegvl
nyykaneaylqgqlgnpkgedqpnkkyydprvwlragqtsmiarlekafqelnaidvl
>d1b4ka_ 3.1.10.3.2 5-aminolevulinate dehydratase, ALAD (porphobilinogen synthase) {Pseudomonas aeruginosa}
ypytrlrrnrrddfsrrlvrenvltvddlilpvfvldgvnqresipsmpgverlsidqll
ieaeewvalgipalalfpvtpvekksldaaeaynpegiaqratralrerfpelgiitdva
ldpftthgqdgildddgyvlndvsidvlvrqalshaeagaqvvapsdmmdgrigaireal
esaghtnvrimaysakyasayygpfrdavgsasnlgkgnkatyqmdpansdealhevaad
laegadmvmvkpgmpyldivrrvkdefraptfvyqvsgeyamhmgaiqngwlaesviles
ltafkragadgiltyfakqaaeqlrr
>d1qr7a_ 3.1.10.4.1 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase (DAHP synthase, AroG) {Escherichia coli}
lrikeikellppvallekfpatenaantvaharkaihkilkgnddrllvvigpcsihdpv
aakeyatrllalreelkdeleivmrvyfekprttvgwkglindphmdnsfqindglriar
kllldindsglpaagefldmitpqyladlmswgaigarttesqvhrelasglscpvgfkn
gtdgtikvaidainaagaphcflsvtkwghsaivntsgngdchiilrggkepnysakhva
evkeglnkaglpaqvmidfshansskqfkkqmdvcadvcqqiaggekaiigvmveshlve
gnqslesgeplaygksitdacigwedtdallrqlanavkarrg
>d1d9ea_ 3.1.10.4.2 3-deoxy-D-manno-octulosonate 8-phosphate synthase (KDO8P synthase) {Escherichia coli}
mkqkvvsigdinvandlpfvlfggmnvlesrdlamricehyvtvtqklgipyvfkasfdk
anrssihsyrgpgleegmkifqelkqtfgvkiitdvhepsqaqpvadvvdviqlpaflar
qtdlveamaktgavinvkkpqfvspgqmgnivdkfkeggnekvilcdrganfgydnlvvd
mlgfsimkkvsgnspvifdvthalqcrdpfgaasggrraqvaelaragmavglaglfiea
hpdpehakcdgpsalplaklepflkqmkaiddlvkgfeeldtsk
>d1onea1 3.1.11.1.1 (142-436) Enolase {Baker's yeast (Saccharomyces cerevisiae)}
spyvlpvpflnvlnggshaggalalqefmiaptgaktfaealrigsevyhnlksltkkry
gasagnvgdeggvapniqtaeealdlivdaikaaghdgkvkigldcasseffkdgkydld
fknpnsdkskwltgpqladlyhslmkrypivsiedpfaeddweawshffktagiqivadd
ltvtnpkriataiekkaadalllkvnqigtlsesikaaqdsfaagwgvmvshrsgetedt
fiadlvvglrtgqiktgaparserlaklnqllrieeelgdnavfagenfhhgdkl
>d1ec7a1 3.1.11.2.2 (138-446) D-glucarate dehydratase {Escherichia coli}
dgqqrsevemlgylffvgnrkatplpyqsqpddscdwyrlrheeamtpdavvrlaeaaye
kygfndfklkggvlageeeaesivalaqrfpqaritldpngawslneaikigkylkgsla
yaedpcgaeqgfsgrevmaefrratglptatnmiatdwrqmghtlslqsvdipladphfw
tmqgsvrvaqmchefgltwgshsnnhfdislamfthvaaaapgkitaidthwiwqegnqr
ltkepfeikgglvqvpekpglgveidmdqvmkahelyqkhglgarddamgmqylipgwtf
dnkrpcmvr
>d1muca1 3.1.11.2.3 (131-372) Muconate-lactonizing enzyme {Pseudomonas putida}
rvrdslevawtlasgdtardiaearhmleirrhrvfklkiganpveqdlkhvvtikrelg
dsasvrvdvnqywdesqairacqvlgdngidlieqpisrinrggqvrlnqrtpapimade
siesvedafslaadgaasifalkiaknggpravlrtaqiaeaagiglyggtmlegsigtl
asahafltlrqltwgtelfgplllteeivneppqyrdfqlhiprtpglgltldeqrlarf
ar
>d2mnr_1 3.1.11.2.4 (133-359) Mandelate racemase {Pseudomonas putida}
pvqaydshsldgvklateravtaaelgfravktkigypaldqdlavvrsirqavgddfgi
mvdynqsldvpaaikrsqalqqegvtwieeptlqhdyeghqriqsklnvpvqmgenwlgp
eemfkalsigacrlampdamkiggvtgwirasalaqqfgipmsshlfqeisahllaatpt
ahwlerldlagsvieptltfeggnavipdlpgvgiiwrekeigkylv
>d1e0ta2 3.1.12.1.5 (1-69,168-344) Pyruvate kinase, N-terminal domain {Escherichia coli}
mkktkivctigpkteseemlakmldagmnvmrlnfshgdyaehgqriqnlrnvmsktgkt
aailldtkgXpalaekdkqdlifgceqgvdfvaasfirkrsdvieirehlkahggenihi
iskienqeglnnfdeileasdgimvargdlgveipveevifaqkmmiekcirarkvvita
tqmldsmiknprptraeagdvanaildgtdavmlsgesakgkypleavsimaticertdr
vmnsrle
>d1dik_1 3.1.12.2.1 (510-874) Pyruvate phosphate dikinase, C-terminal domain {Escherichia coli}
ietqeasvsgsferimvwadkfrtlkvrtnadtpedtlnavklgaegiglcrtehmffea
drimkirkmilsdsveareealnelipfqkgdfkamykalegrpmtvryldpplhefvph
teeeqaelaknmgltlaevkakvdelhefnpmmghrgcrlavtypeiakmqtravmeaai
evkeetgidivpeimiplvgekkelkfvkdvvvevaeqvkkekgsdmqyhigtmieipra
altadaiaeeaeffsfgtndltqmtfgfsrddagkfldsyykakiyesdpfarldqtgvg
qlvemavkkgrqtrpglkcgicgehggdpssvefchkvglnyvscspfrvpiarlaaaqa
alnnk
>d1fiy__ 3.1.12.3.1 Phosphoenolpyruvate carboxylase {Escherichia coli}
qysalrsnvsmlgkvlgetikdalgehilervetirklskssragndanrqellttlqnl
sndellpvarafsqflnlantaeqyhsispkgeaasnpeviartlrklknqpelsedtik
kaveslslelvltahpteitrrtlihkmvevnaclkqldnkdiadyehnqlmrrlrqlia
qswhtdeirklrpspvdeakwgfavvenslwqgvpnylrelneqleenlgyklpvefvpv
rftswmggdrdgnpnvtaditrhvlllsrwkatdlflkdiqvlvselsmveatpellalv
geegaaepyrylmknlrsrlmatqawlearlkgeelpkpeglltqneelweplyacyqsl
qacgmgiiangdlldtlrrvkcfgvplvridirqestrhtealgeltrylgigdyeswse
adkqaflirelnskrpllprnwqpsaetrevldtcqviaeapqgsiaayvismaktpsdv
lavhlllkeagigfampvaplfetlddlnnandvmtqllnidwyrgliqgkqmvmigysd
sakdagvmaaswaqyqaqdaliktcekagieltlfhgrggsigrggapahaallsqppgs
lkgglrvteqgemirfkyglpeitvsslslytgaileanllpppepkeswrrimdelsvi
scdvyrgyvrenkdfvpyfrsatpeqelgklplgsrpakrrptggveslraipwifawtq
nrlmlpawlgagtalqkvvedgkqseleamcrdwpffstrlgmlemvfakadlwlaeyyd
qrlvdkalwplgkelrnlqeedikvvlaiandshlmadlpwiaesiqlrniytdplnvlq
aellhrsrqaekegqepdprveqalmvtiagiaagmrntg
>d1d8ca_ 3.1.13.1.1 Malate synthase G {Escherichia coli}
qtitqsrlridanfkrfvdeevlpgtgldaaafwrnfdeivhdlapenrqllaerdriqa
aldewhrsnpgpvkdkaayksflrelgylvpqpervtvettgidseitsqagpqlvvpax
naryalnaanarwgslydalygsdiipqegaxvsgydpqrgeqviawvrrfldeslplen
gsyqdvvafkvvdkqlriqlkngkettlrtpaqfvgyrgdaaaptcillknnglhielqi
dangrigkddpahindviveaaistildcedsvaavdaedkillyrnllglxqgtlqekx
ekngrqivrklnddrhytaadgseislhgrsllfirnvghlxtipviwdsegneipegil
dgvxtgaialydlkvqknsrtgsvyivkpkxhgpqevafanklftrietxlgxapntlkx
gixdeerrtslnlrsciaqarnrvafintgfldrtgdexhsvxeagpxlrknqxkstpwi
kayernnvlsglfcglrgkaqigkgxwaxpdlxadxysqkgdqlragantawvpsptaat
lhalhyhqtnvqsvqaniaqtefnaefepllddlltipvaenanwsaqeiqqeldnnvqg
ilgyvvrwveqgigcskvpdihnvalxedratlrissqhianwlrhgiltkeqvqaslen
xakvvdqqnagdpayrpxagnfanscafkaasdliflgvkqpngytepllhawrlrekes
>d1bura1 3.1.14.1.2 (148-475) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
fqgpphgiqverdklnkygrpllgctikpklglsaknygravyeclrggldftxddenvn
sqpfmrwrdrflfcaealykaqaetgeikghylnatagtcedmmkravfarelgvpivmh
dyltggftanttlshycrdnglllhihramhavidrqknhgmhfrvlakalrlsggdhih
sgtvvgklegerditlgfvdllrddytekdrsrgiyftqswvstpgvlpvasggihvwhm
palteifgddsvlqfgggtlghpwgnapgavanrvaleacvqarnegrdlaregntiire
atkwspelaaacevwkeikfefpamdtv
>d1qtwa_ 3.1.15.1.1 Endonuclease IV {Escherichia coli}
mkyigahvsaagglanaairaaeidatafalftknqrqwraaplttqtidefkaacekyh
ytsaqilphdsylinlghpvtealeksrdafidemqrceqlglsllnfhpgshlmqisee
dclariaesinialdktqgvtavientagqgsnlgfkfehlaaiidgvedksrvgvcidt
chafaagydlrtpaecektfadfartvgfkylrgmhlndakstfgsrvdrhhslgegnig
hdafrwimqddrfdgipliletinpdiwaeeiawlkaqqtekava
>d1xis__ 3.1.15.2.4 D-xylose isomerase {Streptomyces rubiginosus}
nyqptpedrftfglwtvgwqgrdpfgdatrraldpvesvrrlaelgahgvtfhdddlipf
gssdsereehvkrfrqalddtgmkvpmattnlfthpvfkdggftandrdvrryalrktir
nidlavelgaetyvawggregaesggakdvrdaldrmkeafdllgeyvtsqgydirfaie
pkpneprgdillptvghalafierlerpelygvnpevgheqmaglnfphgiaqalwagkl
fhidlngqngikydqdlrfgagdlraafwlvdllesagysgprhfdfkpprtedfdgvwa
saagcmrnylilkeraaafradpevqealrasrldelarptaadglqallddrsafeefd
vdaaaargmaferldqlamdhllgarg
>d1a0ca_ 3.1.15.2.8 D-xylose isomerase {Clostridium thermosulfurogenes, also known as Thermoanaerobacter thermosulfurigenes}
nkyfenvskikyegpksnnpysfkfynpeevidgktmeehlrfsiaywhtftadgtdqfg
katmqrpwnhytdpmdiakarveaafeffdkinapyfcfhdrdiapegdtlretnknldt
ivamikdylktsktkvlwgtanlfsnprfvhgastscnadvfaysaaqvkkaleitkelg
genyvfwggregyetllntdmefeldnfarflhmavdyakeigfegqfliepkpkeptkh
qydfdvanvlaflrkydldkyfkvnieanhatlafhdfqhelryaringvlgsidantgd
mllgwdtdqfptdirmttlamyevikmggfdkgglnfdakvrrasfepedlflghiagmd
afakgfkvayklvkdrvfdkfieeryasykdgigadivsgkadfrslekyalersqivnk
sgrqellesilnqylfa
>d1luca_ 3.1.16.1.1 Bacterial luciferase (alkanal monooxygenase) {Vibrio harveyi}
mkfgnflltyqppelsqtevmkrlvnlgkasegcgfdtvwllehhftefgllgnpyvaaa
hllgatetlnvgtaaivlptahpvrqaedvnlldqmskgrfrfgicrglydkdfrvfgtd
mdnsralmdcwydlmkegfnegyiaadnehikfpkiqlnpsaytqggapvyvvaesastt
ewaaerglpmilswiinthekkaqldlynevatehgydvtkidhclsyitsvdhdsnrak
dicrnflghwydsyvnatkifddsdqtkgydfnkgqwrdfvlkghkdtnrridysyeinp
vgtpeeciaiiqqdidatgidniccgfeangseeeiiasmklfqsdvmpylkekq
>d1nfp__ 3.1.16.2.1 Non-fluorescent flavoprotein (luxF, FP390) {Photobacterium leiognathi}
mtkwnygvfflnfyhvgqqepsltmsnaletlriidedtsiydvvafsehhidksyndet
klapfvslgkqihvlatspetvvkaakygmpllfkwddsqqkriellnhyqaaaakfnvd
ianvrhrlmlfvnvndnptqakaelsiyledylsytqaetsideiinsnaagnfdtclhh
vaemaqglnnkvdflfcfesmkdqenkkslminfdkrvinyrkehnln
>d1qpoa1 3.1.17.1.2 (117-285) Quinolinic acid phosphoribosyltransferase, C-terminal domain {Mycobacterium tuberculosis}
iatataawvdavrgtkakirdtrktlpglralqkyavrtgggvnhrlglgdaalikdnhv
aaagsvvdalravrnaapdlpcevevdsleqldavlpekpelilldnfavwqtqtavqrr
dsraptvmlessgglslqtaatyaetgvdylavgalthsvrvldigldm
>d1qasa3 3.1.18.1.1 (299-625) Phospholipase C isozyme D1 (PLC-D1) {Rat (Rattus norvegicus)}
dqplshylvssshntylledqltgpssteayiralckgcrcleldcwdgpnqepiiyhgy
tftskilfcdvlrairdyafkaspypvilslenhcsleqqrvmarhlrailgpilldqpl
dgvttslpspeqlkgkillkgkklggllpaggengseatdvsdeveaaemedeavrsqvq
hkpkedklklvpelsdmiiycksvhfggfsspgtsgqafyemasfsesralrllqesgng
fvrhnvsclsriypagwrtdssnyspvemwnggcqivalnfqtpgpemdvylgcfqdngg
cgyvlkpaflrdpnttfnsraltqgpw
>d2ptd__ 3.1.18.2.1 Phosphatidylinositol-specific phospholipase C {Bacillus cereus}
assvnelenwskwmqpipdsiplarisipgthdsgtfklqnpikqvwgmtqeydfryqmd
hgarifdirgrltddntivlhhgplylyvtlhefineakqflkdnpsetiimslkkeyed
mkgaedsfsstfekkyfvdpiflktegniklgdargkivllkrysgsnepggynnfywpd
netftttvnqnanvtvqekykvsydekvksikdtmdetmnnsedlnhlyinftslssggt
awnspyyyasyinpeianyikqknparvgwviqdyinekwspllyqeviranksli
>d2plc__ 3.1.18.2.2 Phosphatidylinositol-specific phospholipase C {Listeria monocytogenes}
vttkqwmsalpdttnlaalsipgthdtmsyngditwtltkplaqtqtmslyqqleagiry
idirakdnlniyhgpiflnaslsgvletitqflkknpketiimrlkdeqnsndsfdyriq
pliniykdyfyttprtdtsnkiptlkdvrgkilllsenhtkkplvinsrkfgmqfgapnq
viqddyngpsvktkfkeivqtayqaskadnklflnhisatsltftprqyaaalnnkveqf
vlnltsekvrglgilimdfpekqtikniiknnkf
>d7reqa1 3.1.19.1.1 (4-560) Methylmalonyl-CoA mutase, alpha and beta subunits {Propionibacterium freudenreichii, shermani}
lprfdsvdlgnapvpadaarrfeelaakagtgeawetaeqipvgtlfnedvykdmdwldt
yagippfvhgpyatmyafrpwtirqyagfstakesnafyrrnlaagqkglsvafdlpthr
gydsdnprvagdvgmagvaidsiydmrelfagipldqmsvsmtmngavlpilalyvvtae
eqgvkpeqlagtiqndilkefmvrntyiyppqpsmriiseifaytsanmpkwnsisisgy
hmqeagatadiemaytladgvdyiragesvglnvdqfaprlsffwgigmnffmevaklra
armlwaklvhqfgpknpksmslrthsqtsgwsltaqdvynnvvrtcieamaatqghtqsl
htnsldeaialptdfsariarntqlflqqesgttrvidpwsgsayveeltwdlarkawgh
iqevekvggmakaiekgipkmrieeaaartqaridsgrqpligvnkyrleheppldvlkv
dnstvlaeqkaklvklraerdpekvkaaldkitwaagnpddkdpdrnllklcidagrama
tvgemsdalekvfgryt
>d1ccwb_ 3.1.19.2.1 Glutamate mutase, large subunit {Clostridium cochlearium}
melknkkwtdeefhkqreevlqqwptgkevdlqeavdylkkipaeknfaeklvlakkkgi
tmaqpragvalldehiellrylqdeggadflpstidaytrqnrydecengikesekagrs
llngfpgvnfgvkgcrkvleavnlplqarhgtpdsrllaeiihaggwtsnegggisynvp
yaknvtiekslldwqycdrlvgfyeeqgvhinrepfgpltgtlvppsmsnavgitealla
aeqgvknitvgygecgnmiqdiaalrcleeqtneylkaygyndvfvttvfhqwmggfpqd
eskafgvivtattiaalagatkvivktpheaigiptkeanaagikatkmalnmlegqrmp
mskeletemavikaetkcildkmfelgkgdlaigtvkafetgvmdipfgpskynagkmmp
vrdnlgcvrylefgnvpfteeiknynrerlqerakfegrdvsfqmviddifavgkgrlig
rpe
>d1dioa_ 3.1.19.3.1 Diol dehydratase, alpha subunit {Klebsiella oxytoca}
mrskrfealakrpvnqdgfvkewieegfiamespndpkpsikivngavteldgkpvsdfd
lidhfiaryginlnraeevmamdsvklanmlcdpnvkrseivplttamtpakivevvshm
nvvemmmamqkmrarrtpsqqahvtnvkdnpvqiaadaaegawrgfdeqettvavaryap
fnaiallvgsqvgrpgvltqcsleeatelklgmlghtcyaetisvygtepvftdgddtpw
skgflassyasrglkmrftsgsgsevqmgyaegksmlylearciyitkaagvqglqngsv
scigvpsavpsgiravlaenlicssldlecassndqtfthsdmrrtarllmqflpgtdfi
ssgysavpnydnmfagsnedaedfddynviqrdlkvdgglrpvreedviairnkaaralq
avfagmglppitdeeveaatyahgskdmpernivedikfaqeiinknrnglevvkalaqg
gftdvaqdmlniqkakltgdylhtsaiivgdgqvlsavndvndyagpatgyrlqgerwee
iknipgaldpn
>d1pud__ 3.1.20.1.1 tRNA-guanine transglycosylase {Zymomonas mobilis}
rprfsfsiaaregkartgtiemkrgvirtpafmpvgtaatvkalkpetvratgadiilgn
tyhlmlrpgaeriaklgglhsfmgwdrpiltdsggyqvmslssltkqseegvtfkshldg
srhmlspersieiqhllgsdivmafdectpypatpsraassmersmrwakrsrdafdsrk
eqaenaalfgiqqgsvfenlrqqsadalaeigfdgyavgglavgegqdemfrvldfsvpm
lpddkphylmgvgkpddivgavergidmfdcvlptrsgrngqaftwdgpinirnarfsed
lkpldsechcavcqkwsrayihhlirageilgamlmtehniafyqqlmqkirdsisegrf
sqfaqdfraryf
>d1ad1a_ 3.1.21.1.2 Dihydropteroate synthetase {Staphylococcus aureus}
tktkimgilnvtpdsfsdggkfnnvesavtrvkammdegadiidvggvstrpghemitve
eelnrvlpvveaivgfdvkisvdtfrsevaeaclklgvdiindqwaglydhrmfqvvaky
daeivlmhngngnrdepvveemltsllaqahqakiagipsnkiwldpgigfaktrneeae
vmarldelvateypvllatsrkrftkemmgydttpverdevtaattaygimkgvravrvh
nvelnaklakgidflkenenarhn
>d1uroa_ 3.1.22.1.1 Uroporphyrinogen decarboxylase, UROD {Human (Homo sapiens)}
gfpelkndtflraawgeetdytpvwcmrqagrylpefretraaqdffstcrspeaccelt
lqplrrfpldaaiifsdilvvpqalgmevtmvpgkgpsfpeplreeqdlerlrdpevvas
elgyvfqaitltrqrlagrvpligfagapwtlmtymvegggsstmaqakrwlyqrpqash
qllriltdalvpylvgqvvagaqalqlfeshaghlgpqlfnkfalpyirdvakqvkarlr
eaglapvpmiifakdghfaleelaqagyevvgldwtvapkkarecvgktvtlqgnldpca
lyaseeeigqlvkqmlddfgphryianlghglypdmdpehvgafvdavhkhsrllrq
>d1b5ta_ 3.1.23.1.1 Methylenetetrahydrofolate reductase {Escherichia coli}
gqinvsfeffpprtsemeqtlwnsidrlsslkpkfvsvtygansgerdrthsiikgikdr
tgleaaphltcidatpdelrtiardywnngirhivalrgdlppgsgkpemyasdlvtllk
evadfdisvaaypevhpeaksaqadllnlkrkvdaganraitqfffdvesylrfrdrcvs
agidveiipgilpvsnfkqakkfadmtnvripawmaqmfdgldddaetrklvganiamdm
vkilsregvkdfhfytlnraemsyaichtlgvrpa
>d1pyma_ 3.1.24.1.1 Phosphoenolpyruvate mutase {Blue mussel (Mytilus edulis)}
vkkttqlkqxlnskdlefixeahnglsarivqeagfkgiwgsglsvsaqlgvrdsneasw
tqvvevlefxsdasdvpilldadtgygnfnnarrlvrkledrgvagacledklfpktnsl
hdgraqpladieefalkikackdsqtdpdfcivarveafiagwgldealkraeayrnaga
dailxhskkadpsdieafxkawnnqgpvvivptkyyktptdhfrdxgvsxviwanhnlra
svsaiqqttkqiyddqslvnvedkivsvkeifrlqrddelvqaedkylpkn
>d1dqua_ 3.1.24.2.1 Isocitrate lyase {Aspergillus nidulans}
syieeedqrywdevaavknwwkdsrwrytkrpftaeqivakrgnlkieypsnvqakklwg
ilernfknkeasftygcldptmvtqmakyldtvyvsgwqssstasstdepspdladypmn
tvpnkvnhlwmaqlfhdrkqreermttpkdqrhkvanvdylrpiiadadtghggltavmk
ltklfvergaagihiedqapgtkkcghmagkvlvpisehinrlvairaqadimgtdllai
artdseaatlitstidhrdhpfiigstnpdiqplndlmvmaeqagkngaelqaiedewla
kaglklfndavvdainnsplpnkkaaiekyltqskgksnlearaiakeiagtdiyfdwea
prtregyyryqggtqcainravayapfadliwmesklpdykqakefadgvhavwpeqkla
ynlspsfnwkkamprdeqetyikrlgalgyawqfitlaglhttalisdtfakayakqgmr
aygelvqepemangvdvvthqkwsganyvdnmlkmitgg
>d3btoa2 3.2.1.1.1 (175-324) Alcohol dehydrogenase {Horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1keva2 3.2.1.1.3 (151-314) Bacterial secondary alcohol dehydrogenase {Clostridium beijerinckii}
mmttgfhgaeladiqmgssvvvigigavglmgiagaklrgagriigvgsrpicveaakfy
gatdilnyknghivdqvmkltngkgvdrvimagggsetlsqavsmvkpggiisninyhgs
gdalliprvewgcgmahktikgglcpggrlraemlrdmvvynrv
>d1qora2 3.2.1.1.5 (136-265) Quinone oxidoreductase {Escherichia coli}
yeikpdeqflfhaaaggvgliacqwakalgakligtvgtaqkaqsalkagawqvinyree
dlverlkeitggkkvrvvydsvgrdtwersldclqrrglmvsfgnssgavtgvnlgilnq
kgslyvtrps
>d1ek6a_ 3.2.1.2.1 Uridine diphosphogalactose-4-epimerase (UDP-galactose 4-epimerase) {Escherichia coli}
maekvlvtggagyigshtvlelleagylpvvidnfhnafrgggslpeslrrvqeltgrsv
efeemdildqgalqrlfkkysfmavihfaglkavgesvqkpldyyrvnltgtiqlleimk
ahgvknlvfsssatvygnpqylpldeahptggctnpygkskffieemirdlcqadktwna
vllryfnptgahasgcigedpqgipnnlmpyvsqvaigrrealnvfgndydtedgtgvrd
yihvvdlakghiaalrklkeqcgcriynlgtgtgysvlqmvqamekasgkkipykvvarr
egdvaacyanpslaqeelgwtaalgldrmcedlwrwqkqnpsgfgt
>d1bxka_ 3.2.1.2.2 dTDP-glucose 4,6-dehydratase {Escherichia coli}
mrkilitggagfigsalvryiinetsdavvvvdkltyagnlmslapvaqserfafekvdi
cdraelarvftehqpdcvmhlaaeshvdrsidgpaafietnivgtytlleaaraywnalt
edkksafrfhhistdevygdlhstddfftettpyapsspysaskassdhlvrawlrtygl
ptlitncsnnygpyhfpekliplmilnalagkslpvygngqqirdwlyvedharalycva
ttgkvgetynigghnerknldvveticelleelapnkphgvahyrdlitfvadrpghdlr
yaidaskiarelgcvpqetfesgmrktvqwylaneswwkqvqdgsyqgerlg
>d1bsva_ 3.2.1.2.3 GDP-4-keto-6-deoxy-d-mannose epimerase/reductase (GDP-fucose synthetase) {Escherichia coli}
kqrvfiaghrgmvgsairrqleqrgdvelvlrtrdelnlldsravhdffaseridqvyla
aakvggivanntypadfiyqnmmiesniihaahqndvnkllflgssciypklakqpmaes
ellqgtleptnepyaiakiagiklcesynrqygrdyrsvmptnlygphdnfhpsnshvip
allrrfheataqnapdvvvwgsgtpmreflhvddmaaasihvmelahevwlentqpmlsh
invgtgvdctirelaqtiakvvgykgrvvfdaskpdgtprklldvtrlhqlgwyheisle
aglastyqwflenqdrf
>d1db3a_ 3.2.1.2.4 GDP-mannose 4,6-dehydratase {Escherichia coli}
skvalitgvtgqdgsylaefllekgyevhgikrrassfntervdhiyqdphtcnpkfhlh
ygdlsdtsnltrilrevqpdevynlgamshvavsfespeytadvdamgtlrlleairflg
lekktrfyqastselyglvqeipqkettpfyprspyavaklyaywitvnyresygmyacn
gilfnhesprrgetfvtrkitraianiaqglesclylgnmdslrdwghakdyvkmqwmml
qqeqpedfviatgvqysvrqfvemaaaqlgiklrfegtgveekgivvsvtghdapgvkpg
dviiavdpryfrpaevetllgdptkaheklgwkpeitlremvsemvandleaakkhs
>d1qrra_ 3.2.1.2.5 Sulfolipid biosynthesis protein SQD1 {Thale cress (Arabidopsis thaliana)}
krvmviggdgycgwatalhlskknyevcivdnlvrrlfdhqlglesltpiasihdrisrw
kaltgksielyvgdicdfeflaesfksfepdsvvhfgeqrsapysmidrsravytqhnnv
igtlnvlfaikefgeechlvklgtmgeygtpnidieegyitithngrtdtlpypkqassf
yhlskvhdshniaftckawgiratdlnqgvvygvktdetemheelrnrldydavfgtaln
rfcvqaavghpltvygkggqtrgyldirdtvqcveiaianpakagefrvfnqfteqfsvn
elaslvtkagsklgldvkkmtvpnprveaeehyynakhtklmelglephylsdslldsll
nfavqfkdrvdtkqimpsvswkkigvktks
>d1cyda_ 3.2.1.2.6 Carbonyl reductase {Mouse (Mus musculus)}
lnfsglralvtgagkgigrdtvkalhasgakvvavtrtnsdlvslakecpgiepvcvdlg
dwdatekalggigpvdllvnnaalvimqpflevtkeafdrsfsvnlrsvfqvsqmvardm
inrgvpgsivnvssmvahvtfpnlitysstkgamtmltkamamelgphkirvnsvnptvv
ltdmgkkvsadpefarklkerhplrkfaevedvvnsilfllsdrsastsgggilvdagyl
as
>d1oaa__ 3.2.1.2.7 Sepiapterin reductase {Mouse (Mus musculus)}
adglgcavcvltgasrgfgralapqlarllspgsvmlvsarsesmlrqlkeelgaqqpdl
kvvlaaadlgteagvqrllsavrelprpeglqrlllinnaatlgdvskgflnvndlaevn
nywalnltsmlcltsgtlnafqdspglsktvvnisslcalqpykgwglycagkaardmly
qvlaaeepsvrvlsyapgpldndmqqlaretskdpelrsklqklksdgalvdcgtsaqkl
lgllqkdtfqsgahvdfyd
>d1hdr__ 3.2.1.2.9 Dihydropteridin reductase {Human (Homo sapiens)}
earrvlvyggrgalgsrcvqafrarnwwvasvdvveneeasasiivkmtdsfteqadqvt
aevgkllgeekvdailcvaggwaggnakskslfkncdlmwkqsiwtstisshlatkhlke
gglltlagakaaldgtpgmigygmakgavhqlcqslagknsgmppgaaaiavlpvtldtp
mnrksmpeadfsswtpleflvetfhdwitgknrpssgsliqvvttegrteltpayf
>d1fds__ 3.2.1.2.10 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylahskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevfgdv
>d1hdca_ 3.2.1.2.12 3-alpha,20-beta-hydroxysteroid dehydrogenase {Streptomyces hydrogenans}
ndlsgktviitggarglgaeaarqavaagarvvladvldeegaatarelgdaaryqhldv
tieedwqrvvayareefgsvdglvnnagistgmfletesverfrkvveinltgvfigmkt
vipamkdagggsivnissaaglmglaltssygaskwgvrglsklaavelgtdrirvnsvh
pgmtytpmtaetgirqgegnypntpmgrvgepgeiagavvkllsdtssyvtgaelavdgg
wttgptvkyvmgq
>d1bdb__ 3.2.1.2.13 Cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase {Pseudomonas lb400}
mklkgeavlitggasglgralvdrfvaegakvavldksaerlaeletdhgdnvlgivgdv
rsledqkqaasrcvarfgkidtlipnagiwdystalvdlpeesldaafdevfhinvkgyi
havkaclpalvasrgnviftisnagfypngggplytaakhaivglvrelafelapyvrvn
gvgsgginsdlrgpsslgmgskaistvpladmlksvlpigrmpeveeytgayvffatrgd
aapatgallnydgglgvrgffsgaggndlleqlnih
>d1b16a_ 3.2.1.2.14 Drosophila alcohol dehydrogenase {Fruit fly (Drosophila lebanonensis)}
mdltnknvifvaalggigldtsrelvkrnlknfvildrvenptalaelkainpkvnitfh
tydvtvpvaeskkllkkifdqlktvdilingagilddhqiertiainftglvntttaild
fwdkrkggpggiianicsvtgfnaihqvpvysaskaavvsftnslaklapitgvtaysin
pgitrtplvhtfnswldveprvaelllshptqtseqcgqnfvkaieankngaiwkldlgt
leaiewtkhwdshi
>d1eno__ 3.2.1.2.15 Enoyl-ACP reductase {Oil seed rape (Brassica napus)}
lpidlrgkrafiagiaddngygwavakslaaagaeilvgtwvpalnifetslrrgkfdqs
rvlpdgslmeikkvypldavfdnpedvpedvkankryagssnwtvqeaaecvrqdfgsid
ilvhslangpevskplletsrkgylaaisassysfvsllshflpimnpggasisltyias
eriipgygggmssakaalesdtrvlafeagrkqnirvntisagplgsraakaigfidtmi
eysynnapiqktltadevgnaaaflvsplasaitgatiyvdnglnsmgvaldspvfk
>d1eny__ 3.2.1.2.16 Enoyl-ACP reductase {Mycobacterium tuberculosis, TB, gene InhA}
aglldgkrilvsgiitdssiafhiarvaqeqgaqlvltgfdrlrliqritdrlpakapll
eldvqneehlaslagrvteaigagnkldgvvhsigfmpqtgmginpffdapyadvskgih
isaysyasmakallpimnpggsivgmdfdpsrampaynwmtvaksalesvnrfvareagk
ygvrsnlvaagpirtlamsaivggalgeeagaqiqlleegwdqrapigwnmkdatpvakt
vcallsdwlpattgdiiyadggahtqll
>d1qg6a_ 3.2.1.2.17 Enoyl-ACP reductase {Escherichia coli}
gflsgkrilvtgvasklsiaygiaqamhregaelaftyqndklkgrveefaaqlgsdivl
qcdvaedasidtmfaelgkvwpkfdgfvhsigfapgdqldgdyvnavtregfkiahdiss
ysfvamakacrsmlnpgsalltlsylgaeraipnynvmglakasleanvrymanamgpeg
vrvnaisagpirtlaasgikdfrkmlahceavtpirrtvtiedvgnsaaflcsdlsagis
gevvhvdggfsiaamne
>d2ae2a_ 3.2.1.2.19 Tropinone reductase {Jimsonweed (Datura stramonium), II}
agrwnlegctalvtggsrgigygiveelaslgasvytcsrnqkelndcltqwrskgfkve
asvcdlssrserqelmntvanhfhgklnilvnnagiviykeakdytvedyslimsinfea
ayhlsvlahpflkasergnvvfissvsgalavpyeavygatkgamdqltrclafewakdn
irvngvgpgviatslvemtiqdpeqkenlnklidrcalrrmgepkelaamvaflcfpaas
yvtgqiiyvdgglmancgf
>d1cf2o1 3.2.1.3.6 (1-138,304-336) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Methanothermus fervidus}
mkavaingygtvgkrvadaiaqqddmkvigvsktrpdfearmalkkgydlyvaipervkl
fekagievagtvddmldeadividctpegigaknlkmykekgikaifqggekhediglsf
nslsnyeesygkdytrvvXivpenvdavrailemeedkyksinktnkamnil
>d1dssg1 3.2.1.3.10 (1-148,313-334) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Lobster (Palinurus versicolor)}
skigingfgrigrlvlraalemgaqvvavndpfialeymvymfkydsthgmfkgevkaed
galvvdgkkitvfnemkpenipwskagaeyivestgvfttiekasahfkggakkviisap
sadapmfvcgvnlekyskdmkvvsnasXnefgysqrvidlikhmqkvdsa
>d1brma1 3.2.1.3.12 (1-133,355-367) Aspartate beta-semialdehyde dehydrogenase {Escherichia coli}
mknvgfigwrgmvgsvlmqrmveerdfdairpvffstsqlgqaapsfggttgtlqdafdl
ealkaldiivtcqggdytneiypklresgwqgywidaasslrmkddaiiildpvnqdvit
dglnngirtfvggXaaeplrrmlrqla
>d1ebfa1 3.2.1.3.13 (2-150,341-359) Homoserine dehydrogenase {Baker's yeast (Saccharomyces cerevisiae)}
stkvvnvavigagvvgsafldqllamkstitynlvllaeaersliskdfsplnvgsdwka
alaasttktlplddliahlktspkpvilvdntssayiagfytkfvengisiatpnkkafs
sdlatwkalfsnkptngfvyheatvgaglXaavtaagvlgdvikiaqrl
>d2dap_1 3.2.1.3.14 (1-118,269-320) Diaminopimelic acid dehydrogenase (DAPDH) {Corynebacterium glutamicum}
mtnirvaivgygnlgrsvekliakqpdmdlvgifsrratldtktpvfdvadvdkhaddvd
vlflcmgsatdipeqapkfaqfactvdtydnhrdiprhrqvmneaataagnvalvstgXr
npdftassqiafgraahrmkqqgqsgaftvlevapyllspenlddliardv
>d1dih_1 3.2.1.3.15 (2-130,241-273) Dihydrodipicolinate reductase {Escherichia coli}
hdanirvaiagaggrmgrqliqaalalegvqlgaaleregssllgsdagelagagktgvt
vqssldavkddfdvfidftrpegtlnhlafcrqhgkgmvigttgfdeagkqairdaaadi
aivfaanfsXmtfangavrsalwlsgkesglfdmrdvldlnnl
>d1ofga1 3.2.1.3.16 (1-160,323-381) Glucose-fructose oxidoreductase, N-terminal domain {Zymomonas mobilis}
atlpagasqvpttpagrpmpyairpmpedrrfgyaivglgkyalnqilpgfagcqhsrie
alvsgnaekakivaaeygvdprkiydysnfdkiakdpkidavyiilpnslhaefairafk
agkhvmcekpmatsvadcqrmidaakaankklmigyrchyXnqfsaqldhlaeavinnkp
vrspgeegmqdvrliqaiyeaartgrpvntdwgyvrqggy
>d1dpga1 3.2.1.3.17 (1-181,413-426) Glucose 6-phosphate dehydrogenase, N-terminal domain {Leuconostoc mesenteroides}
vseiktlvtffggtgdlakrklypsvfnlykkgylqkhfaivgtarqalnddefkqlvrd
cikdftddqaqaeafiehfsyrahdvtdaasyavlkeaieeaadkfdidgnrifymsvap
rffgtiakylkseglladtgynrlmiekpfgtsydtaaelqndlenafddnqlfridhyl
gXepyermihdtmngd
>d1qkia1 3.2.1.3.18 (12-199,435-449) Glucose 6-phosphate dehydrogenase, N-terminal domain {Human (Homo sapiens)}
hqsdthifiimgasgdlakkkiyptiwwlfrdgllpentfivgyarsrltvadirkqsep
ffkatpeeklkledffarnsyvagqyddaasyqrlnshmnalhlgsqanrlfylalpptv
yeavtknihescmsqigwnriivekpfgrdlqssdrlsnhisslfredqiyriXdayerl
ildvfcgsq
>d2naca1 3.2.1.4.1 (148-335) Formate dehydrogenase {Pseudomonas sp. 101}
isvaehvvmmilslvrnylpshewarkggwniadcvshaydleamhvgtvaagriglavl
rrlapfdvhlhytdrhrlpesvekelnltwhatredmypvcdvvtlncplhpetehmind
etlklfkrgayivntargklcdrdavaralesgrlagyagdvwfpqpapkdhpwrtmpyn
gmtphisg
>d1qp8a1 3.2.1.4.2 (83-263) Putative formate dehydrogenase {Pyrobaculum aerophilum}
adavaefalalllapykriiqygekxkrgdygrdveipliqgekvavlglgeigtrvgki
laalgaqvrgfsrtpkegpwrftnsleealrearaavcalplnkhtrglvkyqhlalxae
davfvnvgraevldrdgvlrilkerpqfifasdvwwgrndfakdaeffslpnvvatpwva
g
>d1dxy_1 3.2.1.4.3 (101-330) D-2-hydroxyisocaproate dehydrogenase {Lactobacillus casei}
spaaiaefaltdtlyllrnmgkvqaqlqagdyekagtfigkelgqqtvgvmgtghigqva
iklfkgfgakviaydpypmkgdhpdfdyvsledlfkqsdvidlhvpgieqnthiineaaf
nlmkpgaivintarpnlidtqamlsnlksgklagvgidtyeyetedllnlakhgsfkdpl
wdellgmpnvvlsphiayytetavhnmvyfslqhlvdfltkgetstevtg
>d1gdha1 3.2.1.4.4 (101-291) D-glycerate dehydrogenase {Hyphomicrobium methylovorum}
vtvataeiamllllgsarragegekmirtrswpgweplelvgekldnktlgiygfgsigq
alakraqgfdmdidyfdthrasssdeasyqatfhdsldsllsvsqffslnapstpetryf
fnkatikslpqgaivvntargdlvdnelvvaaleagrlayagfdvfagepninegyydlp
ntflfphigsa
>d1psda1 3.2.1.4.5 (108-295) Phosphoglycerate dehydrogenase {Escherichia coli}
ntrsvaelvigelllllrgvpeanakahrgvwnklaagsfeargkklgiigyghigtqlg
ilaeslgmyvyfydienklplgnatqvqhlsdllnmsdvvslhvpenpstknmmgakeis
lmkpgsllinasrgtvvdipalcdalaskhlagaaidvfptepatnsdpftsplcefdnv
lltphigg
>d1pjca1 3.2.1.4.7 (136-303) L-alanine dehydrogenase {Phormidium lapideum}
agrlsvqfgarflerqqggrgvllggvpgvkpgkvvilgggvvgteaakmavglgaqvqi
fdinverlsyletlfgsrvellysnsaeietavaeadlligavlvpgrrapilvpaslve
qmrtgsvivdvavdqggcvetlhptshtqptyevfgvvhygvpnmpga
>d1b3ra1 3.2.1.4.9 (190-352) S-adenosylhomocystein hydrolase {Rat (Rattus norvegicus)}
nlygcreslidgikratdvmiagkvavvagygdvgkgcaqalrgfgarviiteidpinal
qaamegyevttmdeackegnifvtttgcvdiilgrhfeqmkddaivcnighfdveidvkw
lnenavekvnikpqvdryllknghriillaegrlvnlgcamgh
>d2cmd_1 3.2.1.5.4 (1-145) Malate dehydrogenase {Escherichia coli}
mkvavlgaaggigqalalllktqlpsgselslydiapvtpgvavdlshiptavkikgfsg
edatpalegadvvlisagvrrkpgmdrsdlfnvnagivknlvqqvaktcpkacigiitnp
vnttvaiaaevlkkagvydknklfg
>d2hlpa1 3.2.1.5.6 (22-162) Malate dehydrogenase {Haloarcula marismortui}
tkvsvvgaagtvgaaagynialrdiadevvfvdipdkeddtvgqaadtnhgiaydsntrv
rqggyedtagsdvvvitagiprqpgqtridlagdnapimediqssldehnddyislttsn
pvdllnrhlyeagdrsreqvig
>d1b8pa1 3.2.1.5.7 (3-158) Malate dehydrogenase {Aquaspirillum arcticum}
ktpmrvavtgaagqicysllfriangdmlgkdqpvilqlleipnekaqkalqgvmmeidd
cafpllagmtahadpmtafkdadvallvgarprgpgmerkdlleanaqiftvqgkaidav
asrnikvlvvgnpantnayiamksapslpaknftam
>d1hyha1 3.2.1.5.8 (21-166) L-2-hydroxyisocapronate dehydrogenase, L-HICDH {Lactobacillus confusus}
arkigiiglgnvgaavahgliaqgvaddyvfidaneakvkadqidfqdamanleahgniv
indwaaladadvvistlgniklqqdnptgdrfaelkftssmvqsvgtnlkesgfhgvlvv
isnpvdvitalfqhvtgfpahkvigt
>d1ceqa1 3.2.1.5.12 (19-163) Lactate dehydrogenase {Malarial parasite (Plasmodium falciparum)}
pkakivlvgsgmiggvmatlivqknlgdvvlfdivknmphgkaldtshtnvmaysnckvs
gsntyddlagsdvvivtagftkapgksdkewnrddllplnnkimieigghikkncpnafi
ivvtnpvdvmvqllhqhsgvpknkiigl
>d1ldna1 3.2.1.5.13 (15-162) Lactate dehydrogenase {Bacillus stearothermophilus}
mknnggarvvvigagfvgasyvfalmnqgiadeivlidaneskaigdamdfnhgkvfapk
pvdiwhgdyddcrdadlvvicaganqkpgetrldlvdkniaifrsivesvmasgfqglfl
vatnpvdiltyatwkfsglphervigsg
>d1llda1 3.2.1.5.15 (7-149) Lactate dehydrogenase {Bifidobacterium longum, strain am101-2}
ptklavigagavgstlafaaaqrgiareivlediakerveaevldmqhgssfyptvsidg
sddpeicrdadmvvitagprqkpgqsrlelvgatvnilkaimpnlvkvapnaiymlitnp
vdiathvaqkltglpenqifgsg
>d1qmga2 3.2.1.6.1 (82-307) Acetohydroxy acid isomeroreductase, ketoacid reductoisomerase (KARI) {Spinach (Spinacia oleracea)}
sattfdfdssvfkkekvtlsghdeyivrggrnlfpllpdafkgikqigvigwgsqapaqa
qnlkdslteaksdvvvkiglrkgsnsfaearaagfseengtlgdmwetisgsdlvlllis
dsaqadnyekvfshmkpnsilglshgfllghlqslgqdfpknisviavcpkgmgpsvrrl
yvqgkevngaginssfavhqdvdgratdvalgwsialgspftfatt
>d2pgd_2 3.2.1.6.2 (1-176) 6-phosphogluconate dehydrogenase {Sheep (Ovis orientalis aries)}
aqadialiglavmgqnlilnmndhgfvvcafnrtvskvddflaneakgtkvlgahsleem
vsklkkprriillvkagqavdnfieklvplldigdiiidggnseyrdtmrrcrdlkdkgi
lfvgsgvsggedgarygpslmpggnkeawphikaifqgiaakvgtgepccdwvgdd
>d2hdha2 3.2.1.6.4 (12-203) Short chain L-3-hydroxyacyl CoA dehydrogenase {Human (Homo sapiens)}
kiivkhvtviggglxgagiaqvaaatghtvvlvdqtedilakskkgieeslrkvakkkfa
enpkagdefvaktlstiatstdaasvvhstdlvveaivenlkvknelfkrldkraaehti
fasntsslqitsianattrqdrfaglhffnpvpvxklveviktpxtsqktfeslvdfska
lgkhpvsckdtp
>d1dlja2 3.2.1.6.6 (1-196) UDP-glucose dehydrogenase (UDPGDH) {Streptococcus pyogenes}
mkiavagsgyvglslgvllslqnevtivdilpskvdkinnglspiqdeyieyylkskqls
ikatldskaaykeaelviiatptnynsrinyfdtqhvetvikevlsvnshatliikstip
igfitemrqkfqtdriifspeflreskalydnlypsriivsceendspkvkadaekfall
lksaakknnvpvlimg
>d1bg6_2 3.2.1.6.7 (4-187) N-(1-D-carboxylethyl)-L-norvaline dehydrogenase {Arthrobacter strain 1c}
sktyavlglgngghafaaylalkgqsvlawdidaqrikeiqdrgaiiaegpglagtahpd
lltsdiglavkdadvilivvpaihhasiaaniasyisegqliilnpgatggalefrkilr
engapevtigetssmlftcrserpgqvtvnaikgamdfaclpaakagwaleqigsvlpqy
vave
>d1bgva1 3.2.1.7.1 (195-449) Glutamate dehydrogenase {Clostridium symbiosum}
karsfggslvrpeatgygsvyyveavmkhendtlvgktvalagfgnvawgaakklaelga
kavtlsgpdgyiydpegitteekinymlemrasgrnkvqdyadkfgvqffpgekpwgqkv
diimpcatqndvdleqakkivannvkyyievanmpttnealrflmqqpnmvvapskavna
ggvlvsgfemsqnserlswtaeevdsklhqvmtdihdgsaaaaeryglgynlvaganivg
fqkiadammaqgiaw
>d1gtma1 3.2.1.7.2 (181-419) Glutamate dehydrogenase {Pyrococcus furiosus}
ggslgrieatargasytireaakvlgwdtlkgktiaiqgygnagyylakimsedfgmkvv
avsdskggiynpdglnadevlkwknehgsvkdfpgatnitneellelevdvlapaaieev
itkknadnikakivaevangpvtpeadeilfekgilqipdflcnaggvtvsyfewvqnit
gyywtieevrerldkkmtkafydvyniakeknihmrdaayvvavqrvyqamldrgwvkh
>d1bw9a1 3.2.1.7.7 (149-350) Phenylalanine dehydrogenase {Rhodococcus M4}
safttavgvfeamkatvahrglgsldgltvlvqglgavggslaslaaeagaqllvadtdt
ervahavalghtavaledvlstpcdvfapcamggvittevartldcsvvagaannviade
aasdilhargilyapdfvanaggaihlvgrevlgwsesvvheravaigdtlnqvfeisdn
dgvtpdeaartlagrrareast
>d1a4ia1 3.2.1.7.8 (127-296) Tetrahydrofolate dehydrogenase/cyclohydrolase {Human (Homo sapiens)}
ltsinagrlargdlndcfipctpkgcleliketgvpiagrhavvvgrskivgapmhdlll
wnnatvttchsktahldeevnkgdilvvatgqpemvkgewikpgaividcginyvpddkk
pngrkvvgdvaydeakerasfitpvpggvgpmtvamlmqstvesakrfle
>d1do8a1 3.2.1.7.10 (280-573) Mitochondrial NAD(P)-dependenent malic enzyme {Human (Homo sapiens)}
iqgtaavalagllaaqkviskpisehkilflgageaalgianlivxsxvenglseqeaqk
kiwxfdkygllvkgrkakidsyqepfthsapesipdtfedavnilkpstiigvagagrlf
tpdviraxasinerpvifalsnptaqaectaeeaytltegrclfasgspfgpvkltdgrv
ftpgqgnnvyifpgvalavilcntrhisdsvfleaakaltsqltdeelaqgrlypplani
qevsiniaikvteylyankxafrypepedkakyvkertwrseydsllpdvyewp
>d2scua1 3.2.1.8.1 (1-121) Succinyl-CoA synthetase, alpha-chain, N-terminal (CoA-binding) domain {Escherichia coli}
silidkntkvicqgftgsqgtfhseqaiaygtkmvggvtpgkggtthlglpvfntvreav
aatgatasviyvpapfckdsileaidagikliititegiptldmltvkvkldeagvrmig
p
>d1djna2 3.3.1.1.2 (490-645) Trimethylamine dehydrogenase, C-terminal domain {Methylophilus methylotrophus w3a1}
rwntdgtnclthdpipgadaslpdqltpeqvmdgkkkigkrvvilnadtyfmapslaekl
ataghevtivsgvhlanymhftleypnmmrrlhelhveelgdhfcsriepgrmeiyniwg
dgskrtyrgpgvsprdantshrwiefdslvlvtgrh
>d1cjca1 3.3.1.1.3 (107-331) Adrenodoxin reductase of mitochondrial p450 systems {Bovine (Bos taurus)}
hqaldipgeelpgvfsarafvgwynglpenrelapdlscdtavilgqgnvaldvarillt
ppdhlektditeaalgalrqsrvktvwivgrrgplqvaftikelremiqlpgtrpmldpa
dflglqdrikeaarprkrlmelllrtatekpgveeaarrasasrawglrffrspqqvlps
pdgrraagirlavtrlegigeatravptgdvedlpcglvlssigy
>d1b4va1 3.3.1.2.2 (9-318,451-506) Cholesterol oxidase {Streptomyces}
gyvpavvigtgygaavsalrlgeagvqtlmlemgqlwnqpgpdgnifcgmlnpdkrsswf
knrteaplgsflwldvvnrnidpyagvldrvnydqmsvyvgrgvgggslvnggmavepkr
syfeeilprvdssemydryfpransmlrvnhidtkwfedtewykfarvsreqagkaglgt
vfvpnvydfgymqreaagevpksalateviygnnhgkqsldktylaaalgtgkvtiqtlh
qvktirqtkdggyaltveqkdtdgkllatkeiscrylflgagslgstellvrardtgtlp
nlnsevgagwXgcvlgkatddygrvagyknlyvtdgslipgsvgvnpfvtitalaernve
riikqdv
>d1pbe_1 3.3.1.2.3 (1-173,276-391) p-Hydroxybenzoate hydroxylase (PHBH) {Pseudomonas fluorescens}
mktqvaiigagpsglllgqllhkagidnvilerqtpdyvlgriragvleqgmvdllreag
vdrrmardglvhegveiafagqrrridlkrlsggktvtvygqtevtrdlmeareacgatt
vyqaaevrlhdlqgerpyvtferdgerlrldcdyiagcdgfhgisrqsipaerXmqhgrl
flagdaahivpptgakglnlaasdvstlyrlllkayregrgellerysaiclrriwkaer
fswwmtsvlhrfpdtdafsqriqqteleyylgseaglatiaenyvglpye
>d1b3ma1 3.3.1.2.5 (1-217,322-385) Sarcosine oxidase {Bacillus sp.}
sthfdvivvgagsmgmaagyqlakqgvktllvdafdpphtngshhgdtriirhaygegre
yvplalrsqelwyelekethhkiftktgvlvfgpkgesafvaetmeaakehsltvdlleg
deinkrwpgitvpenynaifepnsgvlfsencirayrelaeargakvlthtrvedfdisp
dsvkietangsytadklivsmgawnskllsklnldipXdehfiidlhpehsnvviaagfs
ghgfkfssgvgevlsqlaltgktehdisifsinrpalkeslq
>d1foha1 3.3.1.2.6 (1-240) Phenol hydroxylase {Soil-living yeast (Trichosporon cutaneum)}
tkysesycdvlivgagpaglmaarvlseyvrqkpdlkvriidkrstkvyngqadglqcrt
leslknlgladkilseandmstialynpdenghirrtdripdtlpgisryhqvvlhqgri
erhildsiaeisdtrikverplipekmeidsskaedpeaypvtmtlrymsdhestplqfg
hktenslfhsnlqtqeeedanyrlpegkeageietvhckyvigcdgghswvrrtlgfemi
>d1foha2 3.3.1.2.6 (342-461) Phenol hydroxylase {Soil-living yeast (Trichosporon cutaneum)}
vtekfskdervfiagdachthspkagqgmntsmmdtynlgwklglvltgrakrdilktye
eerhafaqalidfdhqfsrlfsgrpakdvademgvsmdvfkeafvkgnefasgtainyde
>d1gpea1 3.3.1.2.8 (1-328,525-587) Glucose oxidase {Penicillium amagasakiense}
ylpaqqidvqssllsdpskvagktydyiiagggltgltvaakltenpkikvlviekgfye
sndgaiiedpnaygqifgttvdqnyltvplinnrtnnikagkglggstlingdswtrpdk
vqidswekvfgmegwnwdnmfeymkkaeaartptaaqlaaghsfnatchgtngtvqsgar
dngqpwspimkalmntvsalgvpvqqdflcghprgvsmimnnldenqvrvdaarawllpn
yqrsnleiltgqmvgkvlfkqtasgpqavgvnfgtnkavnfdvfakhevllaagsaispl
ileysgiglksvldqanvtqlldlpvgiXcsmmsrelggvvdatakvygtqglrvidgsi
pptqvsshvmtifygmalkvadailddyaksa
>d1b37a1 3.3.1.2.9 (5-293,406-463) Polyamine oxidase {Maize (Zea mays)}
prvivvgagmsgisaakrlseagitdllileatdhiggrmhktnfaginvelganwvegv
nggkmnpiwpivnstlklrnfrsdfdylaqnvykedggvydedyvqkrieladsveemge
klsatlhasgrddmsilamqrlnehqpngpatpvdmvvdyykfdyefaepprvtslqntv
platfsdfgddvyfvadqrgyeavvyylagqylktddksgkivdprlqlnkvvreikysp
ggvtvktednsvysadyvmvsaslgvlqsdliqfkpklptwkvraiyqfXwpvgvnryey
dqlrapvgrvyftgehtsehyngyvhgaylsgidsaeilincaqkkmc
>d1gnd_1 3.3.1.3.1 (1-291,389-430) Guanine nucleotide dissosiation inhibitor, GDI {Bovine (Bos taurus)}
mdeeydvivlgtgltecilsgimsvngkkvlhmdrnpyyggesssitpleelykrfqlle
gppetmgrgrdwnvdlipkflmangqlvkmllytevtryldfkvvegsfvykggkiykvp
stetealasnlmgmfekrrfrkflvfvanfdendpktfegvdpqntsmrdvyrkfdlgqd
vidftghalalyrtddyldqpcletinriklyseslarygkspylyplyglgelpqgfar
lsaiyggtymlnkpvddiimengkvvgvksegevarckqlicdpsyvpdrvXpiddgses
qvfcscsydatthfettcndikdiykrmagsafd
>d1chua2 3.3.1.4.1 (2-237,354-422) L-aspartate oxidase {Escherichia coli}
ntlpehscdvliigsgaaglslalrladqhqvivlskgpvtegstfyaqggiaavfdetd
sidshvedtliagagicdrhavefvasnarscvqwlidqgvlfdthiqpngeesyhltre
gghshrrilhaadatgrevettlvskalnhpnirvlertnavdlivsdkiglpgtrrvvg
awvwnrnketvetchakavvlatggaskvyqyttnpdissgdgiamawragcrvanXcgg
vmvddhgrtdveglyaigevsytglhganrmasnslleclvygwsaaeditrrmpyahdi
stlppw
>d1qlaa2 3.3.1.4.3 (1-250,372-457) Fumarate reductase flavoprotein subunit {Wolinella succinogenes}
mkvqycdslviggglaglraavatqqkglstivlslipvkrshsaaaqggmqaslgnskm
sdgdnedlhfmdtvkgsdwgcdqkvarmfvntapkairelaawgvpwtrihkgdrmaiin
aqkttiteedfrhglihsrdfggtkkwrtcytadatghtmlfavaneclklgvsiqdrke
aialihqdgkcygavvrdlvtgdiiayvakgtliatggygriyknttnavvcegtgtaia
letgiaqlgnXmggirtdyrgeaklkglfsageaacwdmhgfnrlggnsvseavvagmiv
geyfaehcantqvdletktlekfvkgqeaymkslves
>d1qjda2 3.3.1.4.4 (103-359,506-568) Flavocytochrome c3 (respiratory fumarate reductase) {Shewanella frigidimarina}
ptiaelakdkserqaalasaphdtvdvvvvgsggagfsaaisatdsgakviliekepvig
gnaklaaggmnaawtdqqkakkitdspelmfedtmkggqnindpalvkvlsshskdsvdw
mtamgadltdvgmmggasvnrahrptggagvgahvvqvlydnavkrnidlrmntrgievl
kddkgtvkgilvkgmykgyywvkadavilatggfaknnervakldpslkgfistnqpgav
gdgldvaenaggalkdmXtmggvmidtkaevmnakkqvipglygagevtggvhganrlgg
naisdiitfgrlageeaakys
>d3grs_1 3.3.1.5.1 (18-165,291-363) Glutathione reductase {Human (Homo sapiens)}
vasydylvigggsgglasarraaelgaraavveshklggtcvnvgcvpkkvmwntavhse
fmhdhadygfpscegkfnwrvikekrdayvsrlnaiyqnnltkshieiirghaaftsdpk
ptievsgkkytaphiliatggmpstpheXrvpntkdlslnklgiqtddkghiivdefqnt
nvkgiyavgdvcgkalltpvaiaagrklahrlfeykedskld
>d3grs_2 3.3.1.5.1 (166-290) Glutathione reductase {Human (Homo sapiens)}
sqipgaslgitsdgffqleelpgrsvivgagyiavemagilsalgsktslmirhdkvlrs
fdsmistncteelenagvevlkfsqvkevkktlsglevsmvtavpgrlpvmtmipdvdcl
lwaig
>d1gesa2 3.3.1.5.2 (147-262) Glutathione reductase {Escherichia coli}
dipgveygidsdgffalpalpervavvgagyigvelggvinglgakthlfemfdaplpsf
dpmisetlvevmnaegpqlhtnaipkavvkntdgsltleledgrsetvdcliwaig
>d1feca2 3.3.1.5.3 (170-286) Trypanothione reductase {Crithidia fasciculata}
gddlcitsneafyldeapkralcvgggyisiefagifnaykarggqvdlayrgdmilrgf
dselrkqlteqlranginvrthenpakvtknadgtrhvvfesgaeadydvvmlaigr
>d1trb_1 3.3.1.5.5 (1-118,245-316) Thioredoxin reductase {Escherichia coli}
gttkhskllilgsgpagytaavyaaranlqpvlitgmekggqlttttevenwpgdpndlt
gpllmermhehatkfeteiifdhinkvdlqnrpfrlngdngeytcdaliiatgasaryXh
spntaifegqlelengyikvqsgihgnatqtsipgvfaagdvmdhiyrqaitsagtgcma
aldaeryldgl
>d1trb_2 3.3.1.5.5 (119-244) Thioredoxin reductase {Escherichia coli}
lglpseeafkgrgvsacatsdgffyrnqkvavigggntaveealylsniasevhlihrrd
gfraekilikrlmdkvengniilhtnrtleevtgdqmgvtgvrlrdtqnsdniesldvag
lfvaig
>d1vdc_2 3.3.1.5.6 (118-243) Thioredoxin reductase {Mouse-ear cress (Arabidopsis thaliana)}
rlsfvgsgevlggfwnrgisacavcdgaapifrnkplavigggdsameeanfltkygskv
yiihrrdafraskimqqralsnpkidviwnssvveaygdgerdvlgglkvknvvtgdvsd
lkvsglffai
>d1nhp_1 3.3.1.5.7 (1-119,243-321) NADH peroxidase {Streptococcus enterococcus faecalis}
mkvivlgsshggyeaveellnlhpdaeiqwyekgdfisflsagmqlylegkvkdvnsvry
mtgekmesrgvnvfsnteitaiqpkehqvtvkdlvsgeervenydkliispgavpfeldX
gvrpntawlkgtlelhpngliktdeymrtsepdvfavgdatlikynpadtevnialatna
rkqgrfavknleepvkpfp
>d1nhp_2 3.3.1.5.7 (120-242) NADH peroxidase {Streptococcus enterococcus faecalis}
ipgkdldniylmrgrqwaiklkqktvdpevnnvvvigsgyigieaaeafakagkkvtvid
ildrplgvyldkeftdvlteemeannitiatgetveryegdgrvqkvvtdknaydadlvv
vav
>d1lvl_2 3.3.1.5.8 (151-265) Dihydrolipoamide dehydrogenase {Pseudomonas putida}
mlplggpvisstealapkalpqhlvvvgggyiglelgiayrklgaqvsvvearerilpty
dseltapvaeslkklgialhlghsvegyengcllandgkggqlrleadrvlvavg
>d3lada1 3.3.1.5.8 (1-158,278-348) Dihydrolipoamide dehydrogenase {Pseudomonas putida}
sqkfdvivigagpggyvaaiksaqlglktaliekykgkegktalggtclnvgcipskall
dssykfheahesfklhgistgevaidvptmiarkdqivrnltggvaslikangvtlfegh
gkllagkkvevtaadgssqvldtenvilasgskpveipXrrpvttdllaadsgvtlderg
fiyvddycatsvpgvyaigdvvrgamlahkaseegvvvaeriaghkaqmn
>d3lada2 3.3.1.5.8 (159-277) Dihydrolipoamide dehydrogenase {Pseudomonas putida}
papvdqdvivdstgaldfqnvpgklgvigagviglelgsvwarlgaevtvleamdkflpa
vdeqvakeaqkiltkqglkillgarvtgtevknkqvtvkfvdaegeksqafdklivavg
>d1ebda2 3.3.1.5.9 (155-271) Dihydrolipoamide dehydrogenase {Bacillus stearothermophilus}
pnfkfsnrildstgalnlgevpkslvvigggyigielgtayanfgtkvtilegageilsg
fekqmaaiikkrlkkkgvevvtnalakgaeeredgvtvtyeangetktidadyvlvt
>d1ojt_2 3.3.1.5.10 (276-400) Dihydrolipoamide dehydrogenase {Neisseria meningitidis}
vtklpfipedpriidssgalalkevpgklliigggiiglemgtvystlgsrldvvemmdg
lmqgadrdlvkvwqkqneyrfdnimvntktvavepkedgvyvtfeganapkepqrydavl
vaagr
>d1fcda1 3.3.1.5.11 (1-114,256-327) Flavocytochrome c sulfide dehydrogenase, FCSD, flavin-binding subunit {Purple phototrophic bacterium (Chromatium vinosum)}
agrkvvvvgggtggataakyikladpsievtliepntdyytcylsneviggdrklesikh
gydglrahgiqvvhdsatgidpdkklvktaggaefgydrcvvapgieliydkieXqragk
iaqiagltndagwcpvdiktfessihkgihvigdasianpmpksgysansqgkvaaaavv
vllkgee
>d1fcda2 3.3.1.5.11 (115-255) Flavocytochrome c sulfide dehydrogenase, FCSD, flavin-binding subunit {Purple phototrophic bacterium (Chromatium vinosum)}
gyseeaaaklphawkageqtailrkqledmadggtvviappaapfrcppgpyerasqvay
ylkahkpmskviildssqtfskqsqfskgwerlygfgtenamiewhpgpdsavvkvdgge
mmvetafgdefkadvinlipp
>d1djna3 3.4.1.1.2 (341-489,646-729) Trimethylamine dehydrogenase, middle domain {Methylophilus methylotrophus w3a1}
dirvcigcnvcisrweiggppmictqnatageeyrrgwhpekfrqtknkdsvlivgagps
gseaarvlmesgytvhltdtaekigghlnqvaalpglgewsyhrdyretqitkllkknke
sqlalgqkpmtaddvlqygadkviiatgaXsectlwnelkaresewaendikgiyligda
eaprliadatftghrvareieeanpqiaipykretiawgtphmpggnfkieykv
>d1cjca2 3.4.1.1.3 (6-106,332-460) Adrenodoxin reductase of mitochondrial p450 systems {Bovine (Bos taurus)}
tpqicvvgsgpagfytaqhllkhhsrahvdiyekqlvpfglvrfgvapdhpevknvintf
tqtarsdrcafygnvevgrdvtvqelqdayhavvlsygaedXksrpidpsvpfdpklgvv
pnmegrvvdvpglycsgwvkrgptgvitttmtdsfltgqillqdlkaghlpsgprpgsaf
ikalldsrgvwpvsfsdwekldaeevsrgqasgkpreklldpqemlrllgh
>d1an9a1 3.4.1.2.1 (1-194,288-340) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernll
>d1tml__ 3.5.1.1.1 Cellulase E2 {Thermomonospora fusca, strain yx}
ndspfyvnpnmssaewvrnnpndprtpvirdriasvpqgtwfahhnpgqitgqvdalmsa
aqaagkipilvvynapgrdcgnhssggapshsayrswidefaaglknrpayiivepdlis
lmsscmqhvqqevletmayagkalkagssqariyfdaghsawhspaqmaswlqqadisns
ahgiatntsnyrwtadevayakavlsaignpslravidtsrngngpagnewcdpsgraig
tpsttntgdpmidaflwiklpgeadgciagagqfvpqaayemaiaa
>d2bvwa_ 3.5.1.1.3 Cellobiohydrolase II (Cel6a) {Humicola insolens}
ngnpfegvqlwannyyrsevhtlaipqitdpalraaasavaevpsfqwldrnvtvdtllv
qtlseireanqaganpqyaaqivvydlpdrdcaaaasngewaianngvnnykayinrire
ilisfsdvrtilviepdslanmvtnmnvpkcsgaastyreltiyalkqldlphvamymda
ghagwlgwpaniqpaaelfakiyedagkpravrglatnvanynawsvsspppytspnpny
dekhyieafrplleargfpaqfivdqgrsgkqptgqkewghwcnaigtgfgmrptantgh
qyvdafvwvkpggecdgtsdttaarydyhcgledalkpapeagqwfneyfiqllrnanpp
f
>d1cm5a_ 3.6.1.1.1 Pyruvate formate-lyase, PFL {Escherichia coli}
selneklatawegftkgdwqnevnvrdfiqknytpyegdesflagateatttlwdkvmeg
vklenrthapvdfdtavastitshdagyinkqlekivglqteaplkralipfggikmieg
sckaynreldpmikkifteyrkthnqgvfdvytpdilrcrksgvltglpdaygrgriigd
yrrvalygidylmkdklaqftslqadlengvnleqtirlreeiaeqhralgqmkemaaky
gydisgpatnaqeaiqwtyfgylaavksqngaamsfgrtstfldvyierdlkagkiteqe
aqemvdhlvmklrmvrflrtpeydelfsgdpiwatesiggmgldgrtlvtknsfrflntl
ytmgpspepnmtilwseklplnfkkfaakvsidtsslqyenddlmrpdfnnddyaiaaav
spmivgkqmqffgaranlaktmlyainggvdeklkmqvgpksepikgdvlnydevmermd
hfmdwlakqyitalniihymhdkysyeaslmalhdrdvirtmacgiaglsvaadslsaik
yakvkpirdedglaidfeiegeypqfgnndprvddlavdlverfmkkiqklhtyrdaipt
qsvltitsnvvygkktgntpdgrragapfgpganpmhgrdqkgavasltsvaklpfayak
dgisytfsivpnalgkddevrktnlaglmdgyfhheasieggqhlnvnvmnremlldame
npekypqltirvsgyavrfnsltkeqqqdvitrtftqsm
>d1rlr_2 3.6.1.2.1 (222-748) R1 subunit of ribonucleotide reductase, C-terminal domain {Escherichia coli}
fsscvliecgdsldsinatssaivkyvsqragiginagriralgspirggeafhtgcipf
ykhfqtavkscsqggvrggaatlfypmwhlevesllvlknnrgvegnrvrhmdygvqink
lmytrllkgeditlfspsdvpglydaffadqeeferlytkyekddsirkqrvkavelfsl
mmqerastgriyiqnvdhcnthspfdpaiapvrqsnlcleialptkplndvndengeial
ctlsafnlgainnldeldelailavraldalldyqdypipaakrgamgrrtlgigvinfa
yylakhgkrysdgsannlthktfeaiqyyllkasnelakeqgacpwfnettyakgilpid
tykkdldtianeplhydwealresikthglrnstlsalmpsetssqisnatngiepprgy
vsikaskdgilrqvvpdyehlhdayellwempgndgylqlvgimqkfidqsisantnydp
srfpsgkvpmqqllkdlltaykfgvktlyyqntrddiddlsnfql
>d1b8ba_ 3.6.1.3.1 Class III anaerobic ribonucleotide triphosphate reductase NRDD subunit {Bacteriophage T4}
srvfptqrdlmagivskhiaknmvpsfimkahesgiihvhdidyspalpftncclvdlkg
mlengfklgnaqietpksigvataimaqitaqvashqyggttfanvdkvlspyvkrtyak
hiedaekwqiadalnyaqsktekdvydafqayeyevntlfssngqtpfvtltfgtgtdwt
ermiqkailknrikglgrdgitpifpklvmfveegvnlykddpnydikqlalecaskrmy
pdiisaknnkaitgssvpvspmgcrsflsvwkdstgneildgrnnlgvvtlnlprialds
yigtqfneqkfvelfnermdlcfealmcrisslkgvkatvapilyqegafgvrlkpdddi
ielfkngrssvslgyigihelnilvgrdigreiltkmnahlkqwtertgfafslystpae
nlcyrfckldtekygsvkdvtdkgwytnsfhvsveenitpfekisreapyhfiatgghis
yvelpdmknnlkgleavwdyaaqhldyfgvnmpvdkcftcgsthemtptengfvcsicge
tdpkkmntirrtcaylgnpnerg
>d1dik_2 3.7.1.1.1 (377-505) Pyruvate phosphate dikinase, central domain {Escherichia coli}
lhptfnpaalkagevigsalpaspgaaagkvyftadeakaahekgervilvrletspedi
egmhaaegiltvrggmtshaavvargmgtccvsgcgeikineeaktfelgghtfaegdyi
sldgstgki
>d1zyma2 3.7.1.2.1 (3-21,145-249) N-terminal domain of enzyme I of the PEP:sugar phosphotransferase system {Escherichia coli}
sgilaspgiafgkalllkeXkiidlsaiqdevilvaadltpsetaqlnlkkvlgfitdag
grtshtsimarslelpaivgtgsvtsqvknddylildavnnqvyvnptnevidkmravqe
qvase
>d1aco_1 3.7.2.1.2 (529-754) Aconitase, C-terminal domain {Bovine (Bos taurus)}
vdvsptsqrlqllepfdkwdgkdledlqilikvkgkcttdhisaagpwlkfrghldnisn
nlligainsenrkansvrnavtqefgpvpdtaryykqhgirwvvigdenygegssrehsa
leprflggraiitksfarihetnlkkqgllpltfadpadynkihpvdkltiqglkdfapg
kpltciikhpngtqetillnhtfnetqiewfragsalnrmkelqqk
>d1a9xb1 3.7.3.1.1 (1502-1652) Carbamoyl phosphate synthetase, small subunit N-terminal domain {Escherichia coli}
iksallvledgtqfhgraigatgsavgevvfntsmtgyqeiltdpsysrqivtltyphig
nvgtndadeessqvhaqglvirdlpliasnfrntedlssylkrhnivaiadidtrkltrl
lrekgaqngciiagdnpdaalalekarafpg
>d1de4c2 3.7.4.1.1 (190-382) Transferrin receptor ectodomain, apical domain {Human (Homo sapiens)}
iqvkdsaqnsviivdkngrlvylvenpggyvayskaatvtgklvhanfgtkkdfedlytp
vngsivivragkitfaekvanaeslnaigvliymdqtkfpivnaelsffghahlgtgdpy
tpgfpsfnhtqfppsrssglpnipvqtisraaaeklfgnmegdcpsdwktdstcrmvtse
sknvkltvsnvlk
>d1kid__ 3.7.5.1.1 GroEL {Escherichia coli}
glvprgsegmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavaka
gkplliiaedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtvise
eigmelekatledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydre
klqervaklaggv
>d1ass__ 3.7.5.2.1 Thermosome {Thermoplasma acidophilum}
msgividkekvhskmpdvvknakialidsaleikkteieakvqisdpskiqdflnqetnt
fkqmvekikksganvvlcqkgiddvaqhylakegiyavrrvkksdmeklakatgakivtd
lddltpsvlgeaetveerkigddrmtfvmgck
>d1ay7b_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdcltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegcditiils
>d1a4ya_ 3.9.1.1.1 Ribonuclease inhibitor {Pig (Sus scrofa)}
sldiqsldiqceelsdarwaellpllqqcqvvrlddcgltearckdissalrvnpalael
nlrsnelgdvgvhcvlqglqtpsckiqklslqnccltgagcgvlsstlrtlptlqelhls
dnllgdaglqllceglldpqcrleklqleycslsaasceplasvlrakpdfkeltvsnnd
ineagvrvlcqglkdspcqlealklescgvtsdncrdlcgivaskaslrelalgsnklgd
vgmaelcpgllhpssrlrtlwiwecgitakgcgdlcrvlrakeslkelslagnelgdega
rllcetllepgcqleslwvkscsftaaccshfssvlaqnrfllelqisnnrledagvrel
cqglgqpgsvlrvlwladcdvsdsscsslaatllanhslreldlsnnclgdagilqlves
vrqpgclleqlvlydiywseemedrlqalekdkpslrvis
>d1yrga_ 3.9.1.2.1 Rna1p {Fission yeast (Schizosaccharomyces pombe)}
arfsiegkslkldaittedeksvfavlleddsvkeivlsgntigteaarwlseniaskkd
leiaefsdiftgrvkdeipealrlllqallkcpklhtvrlsdnafgptaqeplidflskh
tplehlylhnnglgpqagakiaralqelavnkkaknapplrsiicgrnrlengsmkewak
tfqshrllhtvkmvqngirpegiehllleglaycqelkvldlqdntfthlgssalaialk
swpnlrelglndcllsargaaavvdafskleniglqtlrlqyneieldavrtlktvidek
mpdllflelngnrfseeddvvdeirevfstrgrgeldelddme
>d1d0ba_ 3.9.2.1.1 Internalin B LRR domain {Listeria monocytogenes}
etitvstpikqifpddafaetikdnlkkksvtdavtqnelnsidqiiannsdiksvqgiq
ylpnvtklflngnkltdikpltnlknlgwlfldenkikdlsslkdlkklkslslehngis
dinglvhlpqleslylgnnkitditvlsrltkldtlslednqisdivplagltklqnlyl
sknhisdlralaglknldvlelfsqec
>d1dcea3 3.9.2.2.1 (444-567) Rab geranylgeranyltransferase alpha-subunit, N-terminal domain {Rat (Rattus norvegicus)}
rvlhlahkdltvlchleqlllvthldlshnrlralppalaalrclevlqasdnalenvdg
vanlprlqelllcnnrlqqsaaiqplvscprlvllnlqgnslcqeegiqerlaemlpsvs
silt
>d1a9na_ 3.9.2.3.1 Splicesomal U2A' protein {Human (Homo sapiens)}
vkltaelieqaaqytnavrdreldlrgykipvienlgatldqfdaidfsdneirkldgfp
llrrlktllvnnnricrigegldqalpdlteliltnnslvelgdldplaslksltylcil
rnpvtnkkhyrlyviykvpqvrvldfqkvklkerqeaekmfk
>d1igra1 3.9.2.4.1 (1-149) L1 and L2 domains of the type 1 insulin-like growth factor receptor {Human (Homo sapiens)}
eicgpgidirndyqqlkrlenctviegylhilliskaedyrsyrfpkltviteylllfrv
agleslgdlfpnltvirgwklfynyalvifemtnlkdiglynlrnitrgairieknadlc
ylstvdwslildavsnnyivgnkppkecg
>d1igra2 3.9.2.4.1 (300-478) L1 and L2 domains of the type 1 insulin-like growth factor receptor {Human (Homo sapiens)}
kvceeekktktidsvtsaqmlqgctifkgnllinirrgnniaselenfmglievvtgyvk
irhshalvslsflknlrlilgeeqlegnysfyvldnqnlqqlwdwdhrnltikagkmyfa
fnpklcvseiyrmeevtgtkgrqskgdintrnngerascesdvddddkeqkliseedln
>d1aua_2 3.10.1.1.1 (97-299) C-terminal domain of phosphatidylinositol transfer protein sec14p {Baker's yeast (Saccharomyces cerevisiae)}
ydekpliakfypqyyhktdkdgrpvyfeelgavnlhemnkvtseermlknlvweyesvvq
yrlpacsraaghlvetsctimdlkgisissaysvmsyvreasyisqnyypermgkfyiin
apfgfstafrlfkpfldpvtvskifilgssyqkellkqipaenlpvkfggksevdeskgg
lylsdigpwrdpkyigpegeape
>d1auz__ 3.10.2.1.1 SpoIIaa {Bacillus subtilis}
slgidmnvkesvlcirltgeldhhtaetlkqkvtqslekddirhivlnledlsfmdssgl
gvilgrykqikqiggemvvcaispavkrlfdmsglfkiirfeqseqqalltlgvas
>d1tyfa_ 3.11.1.1.1 Clp protease, ClpP subunit {Escherichia coli}
srgersfdiysrllkervifltgqvedhmanlivaqmlfleaenpekdiylyinspggvi
tagmsiydtmqfikpdvsticmgqaasmgaflltagakgkrfclpnsrvmihqplggyqg
qatdieihareilkvkgrmnelmalhtgqsleqierdterdrflsapeaveyglvdsilt
hrn
>d1nzya_ 3.11.1.2.1 4-Chlorobenzoyl-CoA dehalogenase {Pseudomonas strain CBS-3}
myeaighrvedgvaeitiklprhrnalsvkamqevtdalnraeeddsvgavmitgaedaf
cagfylreipldkgvagvrdhfriaalwwhqmihkiirvkrpvlaaingvaaggglgisl
asdmaicadsakfvcawhtigigndtatsyslarivgmrramelmltnrtlypeeakdwg
lvsrvypkdefrevawkvarelaaapthlqvmakerfhagwmqpveectefeiqnviasv
thphfmpcltrfldghradrpqvelpagv
>d2duba_ 3.11.1.2.2 Enoyl-CoA hydratase (crotonase) {Rat (Rattus norvegicus)}
nfqyiitekkgknssvgliqlnrpkalnalcnglieelnqaletfeedpavgaivltgge
kafaagadikemqnrtfqdcysgkflshwdhitrikkpviaavngyalgggcelammcdi
iyagekaqfgqpeillgtipgaggtqrltravgkslamemvltgdrisaqdakqaglvsk
ifpvetlveeaiqcaekiannskiivamakesvnaafemtltegnklekklfystfatdd
rregmsafvekrkanfkdh
>d1dcia_ 3.11.1.2.3 Dienoyl-CoA isomerase {Rat (Rattus norvegicus)}
ayesiqvtsaqkhvlhvqlnrpekrnamnrafwrelvecfqkiskdsdcravvvsgagkm
ftsgidlmdmasdilqppgddvariawylrdlisryqktftviekcpkpviaaihggcig
ggvdlisacdiryctqdaffqvkevdvglaadvgtlqrlpkvignrslvneltftarkmm
adealdsglvsrvfpdkdvmlnaafalaadisskspvavqgskinliysrdhsvdesldy
matwnmsmlqtqdiiksvqaamekkdsksitfskl
>d1ef8a_ 3.11.1.2.4 Methylmalonyl CoA decarboxylase {Escherichia coli}
msyqyvnvvtinkvaviefnygrklnalskvfiddlmqalsdlnrpeirciilrapsgsk
vfsaghdihelpsggrdplsyddplrqitrmiqkfpkpiismvegsvwggafemimssdl
iiaaststfsmtpvnlgvpynlvgihnltrdagfhivkeliftaspitaqralavgilnh
vveveeledftlqmahhisekaplaiavikeelrvlgeahtmnsdeferiqgmrravyds
edyqegmnaflekrkpnfvgh
>d1cdza_ 3.12.1.1.1 BRCT domain from DNA-repair protein XRCC1 {Human (Homo sapiens)}
elpdffqgkhfflygefpgderrkliryvtafngeledymsdrvqfvitaqewdpsfeea
lmdnpslafvrprwiyscnekqkllphqlygvvpqa
>d1rvv1_ 3.13.1.1.1 beta-subunit of the lumazine synthase/riboflavin synthase complex {Bacillus subtilis}
mniiqgnlvgtglkigivvgrfndfitskllsgaedallrhgvdtndidvawvpgafeip
faakkmaetkkydaiitlgtvirgatthydyvcneaakgiaqaanttgvpvifgivtten
ieqaieragtkagnkgvdcavsaiemanlnrsfe
>d1di0a_ 3.13.1.1.2 beta-subunit of the lumazine synthase/riboflavin synthase complex {Brucella abortus}
tsfkiafiqarwhadivdearksfvaelaaktggsveveifdvpgayeiplhaktlartg
ryaaivgaafvidggiydhdfvatavingmmqvqletevpvlsvvltphhfheskehhdf
fhahfkvkgveaahaalqivsersriaa
>d1cp3a_ 3.14.1.1.1 Apopain (cpp32) {Human (Homo sapiens)}
nsykmdypemglciiinnknfhkstgmtsrsgtdvdaanlretfrnlkyevrnkndltre
eivelmrdvskedhskrssfvcvllshgeegiifgtngpvdlkkitnffrgdrcrsltgk
pklfiiqacrgteldcgietdsgvdddmachkipvdadflyaystapgyyswrnskdgsw
fiqslcamlkqyadklefmhiltrvnrkvatefesfsfdatfhakkqipcivsmltkely
fyh
>e1ibc.1a 3.14.1.1.2 Interleukin-1beta converting enzyme (a cysteine protease) {Human (Homo sapiens)}
gnvklcsleeaqriwkqksaeiypimdkssrtrlaliicneefdsiprrtgaevditgmt
mllqnlgysvdvkknltasdmtteleafahrpehktsdstflvfmshgiregicgkkhse
qvpdilqlnaifnmlntkncpslkdkpkviiiqacrgdspgvvwfkd
>e1ibc.1b 3.14.1.1.2 Interleukin-1beta converting enzyme (a cysteine protease) {Human (Homo sapiens)}
aikkahiekdfiafcsstpdnvswrhptmgsvfigrliehmqeyacscdveeifrkvrfs
feqpagraqmpttervtltrcfylfpgh
>d1cvra2 3.14.1.2.1 (1-350) Gingipain R (RgpB), N-terminal domain {Porphyromonas gingivalis}
ytpveekengrmivivakkyegdikdfvdwknqrglrtevkvaediaspvtanaiqqfvk
qeyekegndltyvllvgdhkdipakitpgiksdqvygqivgndhynevfigrfscesked
lktqidrtihyernittedkwlgqalciasaeggpsadngesdiqhenvianlltqygyt
kiikcydpgvtpkniidafnggislvnytghgsetawgtshfgtthvkqltnsnqlpfif
dvacvngdflfsmpcfaealmraqkdgkptgtvaiiastidqywappmrgqdemneilce
khpnnikrtfggvtmngmfamvekykkdgenmldtwtvfgdpsllvrtlv
>d3euga_ 3.15.1.1.3 Uracil-DNA glycosylase {Escherichia coli}
ltwhdvlaeekqqphflntlqtvaserqsgvtiyppqkdvfnafrftelgdvkvvilgqd
pyhgpgqahglafsvrpgiaippsllnmykelentipgftrpnhgyleswarqgvlllnt
vltvragqahshaslgwetftdkvislinqhregvvfllwgshaqkkgaiidkqrhhvlk
aphpsplsahrgffgcnhfvlanqwleqhgetpidwmpvlpaese
>d1muga_ 3.15.1.2.1 G:T/U mismatch-specific DNA glycosylase {Escherichia coli}
mvedilapglrvvfcginpglssagtgfpfahpanrfwkviyqagftdrqlkpqeaqhll
dyrcgvtklvdrptvqanevskqelhaggrkliekiedyqpqalailgkqayeqgfsqrg
aqwgkqtltigstqiwvlpnpsglsrvsleklveayreldqalvv
>d1mla_1 3.16.1.1.1 (3-127,198-307) Catalytic domain of malonyl-CoA ACP transacylase {Escherichia coli}
qfafvfpgqgsqtvgmladmaasypiveetfaeasaalgydlwaltqqgpaeelnktwqt
qpalltasvalyrvwqqqggkapammaghslgeysalvcagvidfadavrlvemrgkfmq
eavpeXvpshcalmkpaadklavelakitfnaptvpvvnnvdvkcetngdairdalvrql
ynpvqwtksveymaaqgvehlyevgpgkvltgltkrivdtltasalnepsamaaal
>d1cf9a1 3.17.1.1.1 (598-753) Catalase, C-terminal domain {Escherichia coli, HPII}
vkgrvvaillndevrsadllailkalkakgvhakllysrmgevtaddgtvlpiaatfaga
psltvdavivpcgniadiadngdanyylmeaykhlkpialagdarkfkatikiadqgeeg
iveadsadgsfmdelltlmaahrvwsripkidkipa
>d3chy__ 3.17.2.1.1 CheY protein {Escherichia coli}
adkelkflvvddfstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmp
nmdglellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleekln
kifeklgm
>d1tmy__ 3.17.2.1.3 CheY protein {Thermotoga maritima}
gkrvlivddaafmrmmlkdiitkagyevageatngreavekykelkpdivtmditmpemn
gidaikeimkidpnakiivcsamgqqamvieaikagakdfivkpfqpsrvvealnkvs
>d1a04a2 3.17.2.1.4 (5-142) Nitrate/nitrite response regulator (NARL), receiver domain {Escherichia coli}
epatilliddhpmlrtgvkqlismapditvvgeasngeqgielaesldpdlilldlnmpg
mngletldklrekslsgrivvfsvsnheedvvtalkrgadgyllkdmepedllkalhqaa
agemvlsealtpvlaasl
>d1ntr__ 3.17.2.1.5 NTRC receiver domain {Salmonella typhimurium}
mqrgivwvvdddssirwvleralagagltcttfengnevlaalasktpdvllsdirmpgm
dglallkqikqrhpmlpviimtahsdldaavsayqqgafdylpkpfdideavalverais
hyqe
>d1dbwa_ 3.17.2.1.6 Transcriptional regulatory protein FixJ, receiver domain {Rhizobium meliloti}
mqdytvhivddeepvrkslafmltmngfavkmhqsaeaflafapdvrngvlvtdlrmpdm
sgvellrnlgdlkinipsivitghgdvpmaveamkagavdfiekpfedtviieaierase
hlv
>d1dz3a_ 3.17.2.1.7 Sporulation response regulator Spo0A {Bacillus stearothermophilus}
sikvciaddnrelvslldeyissqpdmevigtayngqdclqmleekrpdillldiimphl
dglavleriragfehqpnvimltafgqedvtkkavelgasyfilkpfdmenlahhirqvy
gkt
>d1srra_ 3.17.2.1.8 Sporulation response regulator Spo0F {Bacillus subtilis}
nekilivddqsgirillnevfnkegyqtfqaanglqaldivtkerpdlvlldmkipgmdg
ieilkrmkvidenirviimtaygeldmiqeskelgalthfakpfdideirdavkkylpl
>d1a2oa1 3.17.2.1.9 (1-140) Methylesterase CheB, N-terminal domain {Salmonella typhimurium}
mskirvlsvddsalmrqimteiinshsdmemvatapdplvardlikkfnpdvltldvemp
rmdgldfleklmrlrpmpvvmvssltgkgsevtlralelgaidfvtkpqlgiregmlays
emiaekvrtaarariaahkp
>d1b00a_ 3.17.2.1.10 PhoB receiver domain {Escherichia coli}
arrilvvedeapiremvcfvleqngfqpveaedydsavnqlnepwpdlilldwmlpggsg
iqfikhlkresmtrdipvvmltargeeedrvrgletgaddyitkpfspkelvarikavmr
ri
>d1dcfa_ 3.17.2.2.1 Receiver domain of the ethylene receptor {Thale cress (Arabidopsis thaliana)}
hmsnftglkvlvmdengvsrmvtkgllvhlgcevttvssneeclrvvshehkvvfmdvcm
pgvenyqialrihekftkqrhqrpllvalsgntdkstkekcmsfgldgvllkpvsldnir
dvlsdlleprvlye
>d1qo0d_ 3.17.2.3.1 Negative regulator of the amidase operon AmiR {Pseudomonas aeruginosa}
sansllgslrelqvlvlnppgevsdalvlqlirigcsvrqcwpppeafdvpvdvvftsif
qnrhhdeiaallaagtprttlvalveyespavlsqiielechgvitqpldahrvlpvlvs
arriseemaklkqkteqlqdriagqarinqakvllmqrhgwdereahqhlsreamkrrep
ilkiaqell
>d2scua2 3.17.3.1.1 (122-286) Succinyl-CoA synthetase, alpha-chain, C-terminal domain {Escherichia coli}
ncpgvitpgeckigiqpghihkpgkvgivsrsgtltyeavkqttdygfgqstcvgiggdp
ipgsnfidilemfekdpqteaivmigeiggsaeeeaaayikehvtkpvvgyiagvtapkg
krmgxagaiiaggkgtadekfaaleaagvktvrsladigealktv
>d2scub1 3.17.3.1.2 (245-385) Succinyl-CoA synthetase, beta-chain, C-terminal domain {Escherichia coli}
aaqwelnyvaldgnigcmvngaglamgtmdivklhggepanfldvgggatkervteafki
ilsddkvkavlvnifggivrcdliadgiigavaevgvnvpvvvrlegnnaelgakklads
glniiaakgltdaaqqvvaav
>d1akr__ 3.17.4.1.2 Flavodoxin {Desulfovibrio vulgaris}
pkalivygsttgnteytaetiareladagyevdsrdaasveagglfegfdlvllgcstwa
ddsielqddfiplfdsleetgaqgrkvacfgcgdssyeyfcgavdaieeklknlgaeivq
dglridgdpraarddivgwahdvrgai
>d1rcf__ 3.17.4.1.3 Flavodoxin {Anabaena PCC 7119 and 7120}
skkiglfygtqtgktesvaeiirdefgndvvtlhdvsqaevtdlndyqyliigcptwnig
elqsdweglyselddvdfngklvayfgtgdqigyadnfqdaigileekisqrggktvgyw
stdgydfndskalrngkfvglaldednqsdltddrikswvaqlksefgl
>d5nul__ 3.17.4.1.6 Flavodoxin {Clostridium beijerinckii}
mkivywsgtgntekmaeliakgiiesgkdvntinvsdvnidellnedililgcsamtdev
leesefepfieeistkisgkkvalfgsygwgdgkwmrdfeermngygcvvvetplivqne
pdeaeqdciefgkkiani
>d1bvyf_ 3.17.4.1.7 FMN-binding domain of the cytochrome P450bm-3 {Bacillus megaterium}
ntpllvlygsnmgtaegtardladiamskgfapqvatldshagnlpregavlivtasyng
hppdnakqfvdwldqasadevkgvrysvfgcgdknwattyqkvpafidetlaakgaenia
drgeadasddfegtyeewrehmwsdvaayfnl
>d1b1ca_ 3.17.4.2.2 NADPH-cytochrome p450 reductase, N-terminal domain {Human (Homo sapiens)}
ssfvekmkktgrniivfygsqtgtaeefanrlskdahrygmrgmsadpeeydladlsslp
eidnalvvfcmatygegdptdnaqdfydwlqetdvdlsgvkfavfglgnktyehfnamgk
yvdkrleqlgaqrifelglgdddgnleedfitwreqfwpavcehfg
>d1d4aa_ 3.17.4.3.3 NAD(P)H:quinone reductase {Human (Homo sapiens)}
vgrralivlahsertsfnyamkeaaaaalkkkgwevvesdlyamnfnpiisrkditgklk
dpanfqypaesvlaykeghlspdivaeqkkleaadlvifqfplqwfgvpailkgwfervf
igefaytyaamydkgpfrskkavlsittggsgsmyslqgihgdmnvilwpiqsgilhfcg
fqvlepqltysightpadariqilegwkkrleniwdetplyfapsslfdlnfqagflmkk
evqdeeknkkfglsvghhlgksiptdnqikark
>d1bmta2 3.17.5.1.1 (741-896) Methionine synthase, C-terminal domain {Escherichia coli}
eqgktngkmviatvkgdvhdigknivgvvlqcnnyeivdlgvmvpaekilrtakevnadl
iglsglitpsldemvnvakemerqgftiplliggattskahtavkieqnysgptvyvqna
srtvgvvaallsdtqrddfvartrkeyetvriqhgr
>d1ccwa_ 3.17.5.1.3 Glutamate mutase, small subunit {Clostridium cochlearium}
mekktivlgvigsdchavgnkildhaftnagfnvvnigvlspqelfikaaietkadailv
sslygqgeidckglrqkcdeaglegillyvggnivvgkqhwpdvekrfkdmgydrvyapg
tppevgiadlkkdlnie
>d7reqa2 3.17.5.1.4 (561-728) Methylmalonyl-CoA mutase C-terminal domains of alpha and beta subunits {Propionibacterium freudenreichii, shermani}
aqirtisgvyskevkntpeveearelveefeqaegrrprillakmgqdghdrgqkviata
yadlgfdvdvgplfqtpeetarqaveadvhvvgvsslagghltlvpalrkeldklgrpdi
litvggvipeqdfdelrkdgaveiytpgtvipesaislvkklraslda
>d7reqb2 3.17.5.1.4 (476-638) Methylmalonyl-CoA mutase C-terminal domains of alpha and beta subunits {Propionibacterium freudenreichii, shermani}
tkpfpaaparkglawhrdsevfeqlmdrstsvserpkvflaclgtrrdfggregfsspvw
hiagidtpqveggttaeiveafkksgaqvadlcssakvyaqqglevakalkaagakalyl
sgafkefgddaaeaeklidgrlfmgmdvvdtlsstldilgvak
>d1c4ka1 3.17.6.1.1 (1-107) Ornithine decarboxylase N-terminal "wing" domain {Lactobacillus sp. strain 30a}
ssslkiastqearqyfdtdrvvvdavgsdftdvgaviamdyetdvidaadatkfgipvfa
vtkdaqaisadelkkifhiidlenkfdatvnareietavnnyedsil
>d1qcza_ 3.17.7.1.1 N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) mutase PurE {Escherichia coli}
parvaivxgsksdwatxqfaaeifeilnvphhvevvsahrtpdklfsfaesaeengyqvi
iagaggaahlpgxiaaktlvpvlgvpvqsaalsgvdslysivqxprgipvgtlaigkaga
anaallaaqilathdkelhqrlndwrkaqtdevlenpdprgaa
>d1cex__ 3.17.8.1.1 Cutinase {Fungus (Fusarium solani), subsp. Pisi}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1bs9__ 3.17.8.1.2 Acetylxylan esterase {Penicillium purpurogenum}
scpaihvfgarettaspgygssstvvngvlsaypgstaeainypacggqsscggasysss
vaqgiaavasavnsfnsqcpstkivlvgysqggeimdvalcgggdpnqgytntavqlsss
avnmvkaaifmgdpmfraglsyevgtcaaggfdqrpagfscpsaakiksycdasdpyccn
gsnaathqgygseygsqalafvksklg
>d1esc__ 3.17.9.1.1 Esterase {Streptomyces scabies}
dpvptvffgdsytanfgiapvtnqdsergwcfqakenypavatrsladkgitldvqadvs
cggalihhfwekqelpfgagelppqqdalkqdtqltvgslggntlgfnrilkqcsdelrk
psllpgdpvdgdepaakcgeffgtgdgkqwlddqfervgaeleelldrigyfapdakrvl
vgyprlvpedttkcltaapgqtqlpfadipqdalpvldqiqkrlndamkkaaadggadfv
dlyagtgantacdgadrgigglledsqlellgtkipwyahpndkgrdiqakqvadkieei
ln
>d1flca2 3.17.9.2.1 (1-217,322-427) Esterase domain of haemagglutinin-esterase-fusion glycoprotein HEF1 {Influenza C virus}
ekikiclqkqvnssfslhngfggnlyateekrmfelvkpkagasvlnqstwigfgdsrtd
ksnsafprsadvsaktadkfrflsggslmlsmfgppgkvdylyqgcgkhkvfyegvnwsp
haaincyrknwtdiklnfqkniyelasqshcmslvnaldktiplqvtagtagncnnsflk
npalytqevkpsenkcgkenlafftlptqfgtyecklXresdyavdqaclstpgcmliqk
qkpyigeaddhhgdqemrellsgldyearcisqsgwvnetspftekyllppkfgrcplaa
keesipkipdglliptsgtdttvt
>d1es9a_ 3.17.9.3.1 Platelet-activating factor acetylhydrolase {Bovine (Bos taurus)}
enpaskptpvqdvqgdgkwmslhhrfvadskdkepevvfigdslvqlmhqceiwrelfsp
lhalnfgiggdstqhvlwrlengelehirpkivvvwvgtnnhghtaeqvtggikaivqlv
nerqpqarvvvlgllprgqhpnplreknrrvnelvraalaghprahfldadpgfvhsdgt
ishhdmydylhlsrlgytpvcralhslllrll
>d1deoa_ 3.17.9.4.1 Rhamnogalacturonan acetylesterase {Fungus (Aspergillus aculeatus)}
ttvylagdstmakngggsgtngwgeylasylsatvvndavagrsarsytregrfeniadv
vtagdyvivefghndggslstdngrtdcsgtgaevcysvydgvnetiltfpaylenaakl
ftakgakvilssqtpnnpwetgtfvnsptrfveyaelaaevagveyvdhwsyvdsiyetl
gnatvnsyfpidhthtspagaevvaeaflkavvctgtslksvltttsfegtcl
>d1ex1a2 3.17.10.1.1 (389-602) Beta-D-glucan exohydrolase, C-terminal domain {Barley (Hordeum vulgare)}
lvllkngktstdapllplpkkapkilvagshadnlgyqcggwtiewqgdtgrttvgttil
eavkaavdpstvvvfaenpdaefvksggfsyaivavgehpytetkgdnlnltipepglst
vqavcggvrcatvlisgrpvvvqpllaasdalvaawlpgsegqgvtdalfgdfgftgrlp
rtwfksvdqlpmnvgdahydplfrlgyglttnat
>d2naca2 3.17.11.1.1 (1-147,336-374) Formate dehydrogenase {Pseudomonas sp. 101}
akvlcvlyddpvdgypktyarddlpkidhypggqtlptpkaidftpgqllgsvsgelglr
kylesnghtlvvtsdkdgpdsvferelvdadvvisqpfwpayltperiakaknlklalta
gigsdhvdlqsaidrnvtvaevtycnsXttltaqaryaagtreilecffegrpirdeyli
vqggala
>d1qp8a2 3.17.11.1.2 (2-82,264-302) Putative formate dehydrogenase {Pyrobaculum aerophilum}
elyvnfelppeaeeelrkyfkivrggdlgnveaalvsritaeelakxprlkfiqvvtagl
dhlpwesipphvtvagnagsnXgygnervwrqxvxeavrnlityatggrprniakredyi
g
>d1dxy_2 3.17.11.1.3 (1-100) D-2-hydroxyisocaproate dehydrogenase {Lactobacillus casei}
mkiiaygarvdeiqyfkqwakdtgntleyhtefldentvewakgfdginslqttpyaagv
fekmhaygikfltirnvgtdnidmtamkqygirlsnvpay
>d1gdha2 3.17.11.1.4 (2-100,292-321) D-glycerate dehydrogenase {Hyphomicrobium methylovorum}
kkkilitwplpeaamararesydviahgddpkitidemietaksvdallitlnekcrkev
idripenikcistysigfdhidldackargikvgnaphgXatqaredmahqandlidalf
ggadmsyala
>d1psda2 3.17.11.1.5 (7-107,296-326) Phosphoglycerate dehydrogenase {Escherichia coli}
ekdkikfllvegvhqkaleslraagytniefhkgalddeqlkesirdahfiglrsrthlt
edvinaaeklvaigcfcigtnqvdldaaakrgipvfnapfsXstqeaqeniglevagkli
kysdngstlsavn
>d2dlda2 3.17.11.1.6 (1-103,301-337) D-lactate dehydrogenase {Lactobacillus helveticus}
mtkvfayairkdeepflnewkeahkdidvdytdklltpetaklakgadgvvvyqqldyta
dtlqaladagvtkmslrnvgvdnidmdkakelgfqitnvpvysXytthavrnmvvkafnn
nlklingekpdspvalnknkf
>d1pjca2 3.17.11.2.1 (1-135,304-361) L-alanine dehydrogenase {Phormidium lapideum}
meigvpkeiknqefrvglspssvrtlveaghtvfietqagigagfadqdyvqagaqvvps
akdawsremvvkvkeplpaeydlmqkdqllftylhlaaarelteqlmrvgltaiayetve
lpnrslplltpmsiiXvpwtatqalnnstlpyvvklanqglkaletddalakglnvqahr
lvhpavqqvfpdla
>d1b3ra2 3.17.11.3.2 (4-189,353-431) S-adenosylhomocystein hydrolase {Rat (Rattus norvegicus)}
lpykvadiglaawgrkaldiaenempglmrmremysaskplkgariagclhmtvetavli
etlvalgaevrwsscnifstqdhaaaaiakagipvfawkgetdeeylwcieqtlhfkdgp
lnmilddggdltnlihtkhpqllsgirgiseetttgvhnlykmmangilkvpainvndsv
tkskfdXpsfvmsnsftnqvmaqielwthpdkypvgvhflpkkldeavaeahlgklnvkl
tkltekqaqylgmpingpfkpdhyry
>d2dhqa_ 3.17.12.1.1 Type II 3-dehydroquinate dehydratase {Mycobacterium tuberculosis}
livnvingpnlgrlgrrepavyggtthdelvaliereaaelglkavvrqsdseaqlldwi
hqaadaaepvilnagglthtsvalrdacaelsaplievhisnvhareefrrhsylspiat
gvivglgiqgyllalrylaeh
>d1a9xa2 3.18.1.1.1 (936-1073) Carbamoyl phosphate synthetase, large subunit allosteric, C-terminal domain {Escherichia coli}
nstmkkhgrallsvregdkervvdlaakllkqgfeldathgtaivlgeaginprlvnkvh
egrphiqdrikngeytyiinttsgrraiedsrvirrsalqykvhydttlnggfatamaln
adatekvisvqemhaqik
>d1b93a_ 3.18.1.2.1 Methylglyoxal synthase, MgsA {Escherichia coli}
melttrtlparkhialvahdhckqmlmswverhqplleqhvlyatgttgnlisratgmnv
namlsgpmggdqqvgalisegkidvliffwdplnavphdpdvkallrlatvwnipvatnv
atadfiiqsphfndavdilipdyqryla
>d1fnc_2 3.19.1.1.1 (155-314) Ferredoxin reductase (flavodoxin reductase) {Spinach (Spinacia oleracea)}
mlmpkdpnatiimlgtgtgiapfrsflwkmffekhddykfnglawlflgvptsssllyke
efekmkekapdnfrldfavsreqtnekgekmyiqtrmaqyavelwemlkkdntyvymcgl
kgmekgiddimvslaaaegidwieykrqlkkaeqwnvevy
>d1fdr_2 3.19.1.1.4 (101-248) Ferredoxin reductase (flavodoxin reductase) {Escherichia coli}
devphcetlwmlatgtaigpylsilrlgkdldrfknlvlvhaaryaadlsylplmqelek
ryegklriqtvvsretaagsltgripaliesgelestiglpmnketshvmlcgnpqmvrd
tqqllketrqmtkhlrrrpghmtaehyw
>d1a8p_2 3.19.1.1.5 (101-258) Ferredoxin reductase (flavodoxin reductase) {Azotobacter vinelandii}
tsdllpgkhlymlstgtglapfmsliqdpevyerfekvvlihgvrqvnelayqqfitehl
pqseyfgeavkekliyyptvtresfhnqgrltdlmrsgklfediglppinpqddramicg
spsmldescevldgfglkisprmgepgdylierafvek
>d1qfja2 3.19.1.1.6 (98-232) NAD(P)H:flavin oxidoreductase {Escherichia coli}
rddeerpmiliaggtgfsyarsilltalarnpnrditiywggreeqhlydlcelealslk
hpglqvvpvveqpeagwrgrtgtvltavlqdhgtlaehdiyiagrfemakiardlfcser
naredrlfgdafafi
>d2cnd_2 3.19.1.1.7 (125-270) Nitrate reductase {Corn (Zea mays)}
gsfvingkqrnarrlamicggsgitpmyqiiqavlrdqpedhtemhlvyanrteddillr
deldrwaaeypdrlkvwyvidqvkrpeegwkysvgfvteavlrehvpeggddtlalacgp
ppmiqfaispnlekmkydmansfvvf
>d2pia_2 3.19.1.2.1 (104-223) Phthalate dioxygenase reductase {Pseudomonas cepacia, db01}
efpldkraksfilvaggigitpmlsmarqlraeglrsfrlyyltrdpegtaffdeltsde
wrsdvkihhdhgdptkafdfwsvfekskpaqhvyccgpqalmdtvrdmtghwpsgtvhfe
>d1amoa3 3.19.1.3.1 (519-678) NADPH-cytochrome p450 reductase {Rat (Rattus norvegicus)}
rlpfksttpvimvgpgtgiapfmgfiqerawlreqgkevgetllyygcrrsdedylyree
larfhkdgaltqlnvafsreqahkvyvqhllkrdrehlwkliheggahiyvcgdarnmak
dvqntfydivaefgpmehtqavdyvkklmtkgrysldvws
>d1cqxa3 3.19.1.4.1 (262-403) Flavohemoglobin, C-terminal domain {Alcaligenes eutrophus}
dvdaktpivlisggvgltpmvsmlkvalqapprqvvfvhgarnsavhamrdrlreaakty
enldlfvfydqplpedvqgrdydypglvdvkqieksillpdadyyicgpipfmrmqhdal
knlgihearihyevfgpdlfae
>d2ts1__ 3.20.1.1.1 Tyrosyl-tRNA synthetase (TyrRS) {Bacillus stearothermophilus, nca 1503}
mdllaelqwrglvnqttdedglrkllneervtlycgfdptadslhighlatiltmrrfqq
aghrpialvggatgligdpsgkksertlnaketveawsarikeqlgrfldfeadgnpaki
knnydwigpldvitflrdvgkhfsvnymmakesvqsrietgisftefsymmlqaydflrl
yetegcrlqiggsdqwgnitaglelirktkgearafgltiplvtkadgtkfgktesgtiw
ldkektspyefyqfwintddrdvirylkyftflskeeiealeqelreapekraaqktlae
evtklvhgeealrqairis
>d1d2ra_ 3.20.1.1.2 Tryptophanyl-tRNA synthetase (TrpRS) {Bacillus stearothermophilus}
mktifsgiqpsgvitignyigalrqfvelqheyncyfcivdqhaitvwqdphelrqnirr
laalylavgidptqatlfiqsevpahaqaawmlqcivyigelermtqfkeksagaaaaaa
glltypplmaadillyntdivpvgedqkqhieltrdlaerfnkrygelftipearipkvg
arimslvdptkkmsksdpnpkayitllddaktiekkiksavtdsegtirydkeakpgisn
llniystlsgqsieelerqyegkgygvfkadlaqvvietlrpiqeryhhwmeseeldrvl
degaekanrvasemvrkmeqamglgr
>d1gtra2 3.20.1.1.3 (8-338) Glutaminyl-tRNA synthetase (GlnRS) {Escherichia coli}
tnfirqiidedlasgkhttvhtrfppepngylhighaksiclnfgiaqdykgqcnlrfdd
tnpvkedieyvesikndvewlgfhwsgnvryssdyfdqlhayaielinkglayvdeltpe
qireyrgtltqpgknspyrdrsveenlalfekmraggfeegkaclrakidmaspfivmrd
pvlyrikfaehhqtgnkwciypmydfthcisdalegithslctlefqdnrrlydwvldni
tipvhprqyefsrlnleytvmskrklnllvtdkhvegwddprmptisglrrrgytaasir
efckrigvtkqdntiemaslesciredlnen
>d1gln_2 3.20.1.1.4 (1-305) Glutamyl-tRNA synthetase (GluRS) {Thermus thermophilus}
mvvtriapsptgdphvgtayialfnyawarrnggrfivriedtdraryvpgaeerilaal
kwlglsydegpdvaaptgpyrqserlplyqkyaeellkrgwayrafetpeeleqirkekg
gydgrarnippeeaeerarrgephvirlkvprpgttevkdelrgvvvydnqeipdvvllk
sdgyptyhlanvvddhlmgvtdviraeewlvstpihvllyrafgweaprfyhmpllrnpd
ktkiskrkshtsldwykaegflpealrnylclmgfsmpdgreiftleefiqaftwervsl
ggpvf
>d1a8h_2 3.20.1.1.5 (1-348) Methionyl-tRNA synthetase (MetR) {Thermus thermophilus}
mekvfyvttpiyyvnaephlghayttvvadflarwhrldgyrtffltgtdehgetvyraa
qaagedpkafvdrvsgrfkrawdllgiayddfirtteerhkkvvqlvlkkvyeagdiyyg
eyeglycvscerfytekelveglcpihgrpverrkegnyffrmekyrpwlqeyiqenpdl
irpegyrnevlamlaepigdlsisrpksrvpwgiplpwdenhvtyvwfdallnyvsaldy
pegeayrtfwphawhligkdilkphavfwptmlkaagipmyrhlnvggfllgpdgrkmsk
tlgnvvdpfallekygrdalryyllreipygqdtpvseealrtryead
>d1qqta2 3.20.1.1.6 (3-140,176-388) Methionyl-tRNA synthetase (MetR) {Escherichia coli}
vakkilvtcalpyangsihlghmlehiqadvwvryqrmrghevnficaddahgtpimlka
qqlgitpeqmigemsqehqtdfagfnisydnyhsthseenrqlseliysrlkengfiknr
tisqlydpekgmflpdrfXvvsgatpvmrdsehfffdlpsfsemlqawtrsgalqeqvan
kmqewfesglqqwdisrdapyfgfeipnapgkyfyvwldapigymgsfknlcdkrgdsvs
fdeywkkdstaelyhfigkdivyfhslfwpamlegsnfrkpsnlfvhgyvtvngakmsks
rgtfikastwlnhfdadslryyytaklssriddidlnledfvqrvnadivnk
>d1qu2a3 3.20.1.1.8 (1-200,395-644) Isoleucyl-tRNA synthetase (IleRS) {Staphylococcus aureus}
mdyektllmpktdfpmrgglpnkepqiqekwdaedqyhkaleknkgnetfilhdgppyan
gnlhmghalnkilkdfivryktmqgfyapyvpgwdthglpieqaltkkgvdrkkmstaef
rekckefaleqielqkkdfrrlgvrgdfndpyitlkpeyeaaqirifgemadkgliykgk
kpvywspssesslaeaeieyXphdwrtkkpvifratpqwfasiskvrqdildaientnfk
vnwgktriynmvrdrgewvisrqrvwgvplpvfyaengeiimtketvnhvadlfaehgsn
iwfereakdllpegfthpgspngtftketdimdvwfdsgsshrgvletrpelsfpadmyl
egsdqyrgwfnssittsvatrgvspykfllshgfvmdgegkkmskslgnvivpdqvvkqk
gadiarlwvsstdyladvrisdeilkqtsdd
>d1bs2a2 3.20.1.1.9 (136-483) Arginyl-tRNA synthetase (ArgRS) {Baker's yeast (Saccharomyces cerevisiae)}
scklvenkkviiefsspniakpfhaghlrstiiggflanlyeklgwevirmnylgdwgkq
fgllavgferygneealvkdpihhlfdvyvrinkdieeegdsipleqstngkareyfkrm
edgdeealkiwkrfrefsiekyidtyarlnikydvysgesqvskesmlkaidlfkekglt
hedkgavlidltkfnkklgkaivqksdgttlyltrdvgaamdryekyhfdkmiyviasqq
dlhaaqffeilkqmgfewakdlqhvnfgmvqgmstrkgtvvfldnileetkekmhevmkk
nenkyaqiehpeevadlvgisavmiqdmqgkrinnyefkwermlsfeg
>d1coza_ 3.20.1.2.1 CTP:glycerol-3-phosphate cytidylyltransferase {Bacillus subtilis}
mkkvitygtfdllhwghikllerakqlgdylvvaistdefnlqkqkkayhsyehrklile
tiryvdevipeknweqkkqdiidhnidvfvmgddwegkfdflkdqcevvylprtegistt
kikeei
>d1b6ta_ 3.20.1.3.1 Phosphopantetheine adenylyltransferase {Escherichia coli}
kraiypgtfdpitnghidivtratqmfdhvilaiaaspskkpmftleervalaqqatahl
gnvevvgfsdlmanfarnqhatvlirglravadfeyemqlahmnrhlmpelesvflmpsk
ewsfissslvkevarhqgdvthflpenvhqalmakla
>d1gpma1 3.20.2.1.1 (208-404) GMP synthetase, central domain {Escherichia coli}
wtpakiiddavarireqvgddkvilglsggvdssvtamllhraigknltcvfvdngllrl
neaeqvldmfgdhfglnivhvpaedrflsalagendpeakrkiigrvfvevfdeealkle
dvkwlaqgtiypdviesaasatgkahvikshhnvgglpkemkmglveplkelfkdevrki
glelglpydmlyrhpfp
>d2nsya_ 3.20.2.1.2 NH3-dependent NAD+-synthetase {Bacillus subtilis}
smqekimrelhvkpsidpkqeiedrvnflkqyvkktgakgfvlgisggqdstlagrlaql
avesireeggdaqfiavrlphgtqqdeddaqlalkfikpdkswkfdikstvsafsdqyqq
etgdqltdfnkgnvkartrmiaqyaiggqegllvlgtdhaaeavtgfftkygdggadllp
ltgltkrqgrtllkelgaperlylkeptadlldekpqqsdetelgisydeiddylegkev
sakvsealekrysmtehkrqvpasmfddwwk
>d1ct9a1 3.20.2.1.3 (193-516) Asparagine synthetase B, C-terminal domain {Escherichia coli}
rdwfdydavkdnvtdknelrqaledsvkshlmsdvpygvllsggldssiisaitkkyaar
rvedqerseawwpqlhsfavglpgspdlkaaqevanhlgtvhheihftvqegldairdvi
yhietydvttirastpmylmsrkikamgikmvlsgegsdevfggylyfhkapnakelhee
tvrkllalhmydcarankamsawgvearvpfldkkfldvamrinpqdkmcgngkmekhil
recfeaylpasvawrqkeqfsdgvgyswidtlkevaaqqvsdqqletarfrfpyntptsk
eaylyreifeelfplpsaaecvpg
>d1sur__ 3.20.2.2.1 Phosphoadenylyl sulphate (PAPS) reductase {Escherichia coli}
skldlnalnelpkvdrilalaetnaelekldaegrvawaldnlpgeyvlsssfgiqaavs
lhlvnqirpdipviltdtgylfpetyrfideltdklklnlkvyratesaawqearygklw
eqgvegiekyndinkvepmnralkelnaqtwfaglrreqsgsranlpvlaiqrgvfkvlp
iidwdnrtiyqylqkhglkyhplwdegylsvgdth
>d1dlja3 3.20.3.1.1 (295-402) UDP-glucose dehydrogenase (UDPGDH), C-terminal (UDP-binding) domain {Streptococcus pyogenes}
akqiinvlkeqespvkvvgvyrlimksnsdnfresaikdvidilkskdikiiiyepmlnk
lesedqsvlvndlenfkkqaniivtnrydnelqdvknkvysrdifgrd
>d1brwa2 3.21.1.1.2 (71-330) Pyrimidine nucleoside phosphorylase {Bacillus stearothermophilus}
lssirgvkvdkhstggvgdtttlvlgplvasvgvpvakmsgrglghtggtidklesvpgf
hveiskdefirlvnengiaiigqtgdltpadkklyalrdvtatvnsipliassimskkia
agadaivldvktgagafmkkldearrlarvmvdigkrvgrrtmavisdmsqplgyavgna
levkeaietlkgngphdltelcltlgshmvylaekapsldearrlleeairsgaaiaafk
tflaaqggdasvvddldklp
>d1dnpa2 3.22.1.1.1 (1-200) N-terminal domain of DNA photolyase {Escherichia coli}
tthlvwfrqdlrlhdnlalaaacrnssarvlalyiatprqwathnmsprqaelinaqlng
lqialaekgipllfrevddfvasveivkqvcaensvthlfynyqyevnerardveveral
rnvvcegfddsvilppgavmtgnhemykvftpfknawlkrlregmpecvaapkvrssgsi
epspsitlnyprqsfdtahf
>d1qnf_2 3.22.1.1.2 (1-204) N-terminal domain of DNA photolyase {Anacystis nidulans}
maapilfwhrrdlrlsdniglaaaraqsaqliglfcldpqilqsadmaparvaylqgclq
elqqryqqagsrllllqgdpqhlipqlaqqlqaeavywnqdiepygrdrdgqvaaalkta
giravqlwdqllhspdqilsgsgnpysvygpfwknwqaqpkptpvatptelvdlspeqlt
aiaplllselptlkqlgfdwdggf
>d2uaga1 3.23.1.1.1 (1-93) N-terminal domain of MurD (UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase) {Escherichia coli}
adyqgknvviiglgltglscvdfflargvtprvmdtrmtppgldklpeaverhtgslnde
wlmaadlivaspgialahpslsaaadagieivg
>d1efva1 3.24.1.1.1 (20-207) Electron transfer flavoprotein, ETFP {Human (Homo sapiens)}
qstlviaehandslapitlntitaatrlggevsclvagtkcdkvaqdlckvagiakvlva
qhdvykgllpeeltplilatqkqfnythicagasafgknllprvaaklevapisdiiaik
spdtfvrtiyagnalctvkcdekvkvfsvrgtsfdaaatsggsassekasstspveisew
ldqkltks
>d1efvb1 3.24.1.1.1 Electron transfer flavoprotein, ETFP {Human (Homo sapiens)}
lrvlvavkrvidyavkirvkpdrtgvvtdgvkhsmnpfceiaveeavrlkekklvkevia
vscgpaqcqetirtalamgadrgihvevppaeaerlgplqvarvlaklaekekvdlvllg
kqaidddcnqtgqmtagfldwpqgtfasqvtlegdklkvereidggletlrlklpavvta
dlrlnepryatlpnimkakkkkievikpgdlgvdltsklsvisvedppqrtagvkvette
dlvaklkeigri
>d1mjha_ 3.24.1.2.1 "Hypothetical" protein MJ0577 {Methanococcus jannaschii}
vmykkilyptdfsetaeialkhvkafktlkaeevillhvidereikkrdifslllgvagl
nksveefenelknklteeaknkmenikkeledvgfkvkdiivvgipheeivkiaedegvd
iiimgshgktnlkeillgsvtenvikksnkpvlvvkrkns
>d1ek1a1 3.25.1.1.1 (4-225) Epoxide hydrolase, N-terminal domain {Mouse (Mus musculus)}
rvaafdldgvlalpsiagafrrseealalprdfllgayqtefpegpteqlmkgkitfsqw
vplmdesyrksskacganlpenfsisqifsqamaarsinrpmlqaaialkkkgfttcivt
nnwlddgdkrdslaqmmcelsqhfdfliescqvgmikpepqiynflldtlkakpnevvfl
ddfgsnlkpardmgmvtilvhntasalrelekvtgtqfpeap
>d1dv1a2 3.26.1.1.1 (1-114) Biotin carboxylase (BC) subunit of acetyl-CoA carboxylase {Escherichia coli}
mldkivianrgeialrilrackelgiktvavhssadrdlkhvlladetvcigpapsvksy
lnipaiisaaeitgavaihpgygflsenanfaeqversgfifigpkaetirlmg
>d1gsoa2 3.26.1.1.2 (-2-103) Glycinamide ribonucleotide synthetase (GAR-syn). {Escherichia coli}
efmkvlvignggrehalawkaaqsplvetvfvapgnagtalepalqnvaigvtdipalld
faqnekidltivgpeaplvkgvvdtfraaglkifgptagaaqleg
>d1b6ra2 3.26.1.1.3 (1-78) N5-carboxyaminoimidazole ribonucleotide synthetase, AIRC, PurK {Escherichia coli}
mkqvcvlgngqlgrmlrqageplgiavwpvgldaepaavpfqqsvitaeierwpetaltr
qlarhpafvnrdvfpiia
>d1a9xa3 3.26.1.1.4 (1-127) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
mpkrtdiksililgagpivigqacefdysgaqackalreegyrvinvnsnpatimtdpem
adatyiepihwevvrkiiekerpdavlptmggqtalncalelerqgvleefgvtmigata
daidkae
>d1a9xa4 3.26.1.1.4 (556-676) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
stdrekimvlgggpnrigqgiefdyccvhaslalredgyetimvncnpetvstdydtsdr
lyfepvtledvleivriekpkgvivqyggqtplklaraleaagvpvigtspdaidraedr
e
>d1iow_1 3.26.1.2.1 (1-96) D-Ala-D-Ala ligase {Escherichia coli, gene ddlB}
mtdkiavllggtsaerevslnsgaavlaglreggidaypvdpkevdvtqlksmgfqkvfi
alhgrggedgtlqgmlelmglpytgsgvmasalsmd
>d1ehia1 3.26.1.2.2 (3-134) D-alanine:D-lactate ligase {Leuconostoc mesenteroides Ddl2}
kkrvalifggnssehdvskrsaqnfynaieatgkyeiivfaiaqngffldtesskkilal
edeqpivdafmktvdasdplarihalksagdfdiffpvvhgnlgedgtlqglfklldkpy
vgaplrghavsf
>d1gsa_1 3.26.1.3.1 (1-122) Prokaryotic glutathione synthetase, N-terminal domain {Escherichia coli}
miklgivmdpianinikkdssfamlleaqrrgyelhymemgdlylingearahtrtlnvk
qnyeewfsfvgeqdlpladldvilmrkdppfdtefiyatyileraeekgtlivnkpqslr
dc
>d2hgsa1 3.26.1.4.1 (202-303) Eukaryotic glutathione synthetase {Human (Homo sapiens)}
pnalvlliaqekernifdqraienellarnihvirrtfedisekgsldqdrrlfvdgqei
avvyfrdgymprqyslqnwearlllershaakcpdiatqlag
>d1auva1 3.26.1.5.1 (112-213) Synapsin Ia domain {Bovine (Bos taurus)}
aarvllvidephtdwakyfkgkkihgeidikveqaefsdlnlvahanggfsvdxevlrng
vkvvrslkpdfvlirqhafsxarngdyrslviglqyagipsi
>d1dhs__ 3.27.1.1.1 Deoxyhypusine synthase, DHS {Human (Homo sapiens)}
apagalaavlkhsstlppestqvrgydfnrgvnyralleafgttgfqatnfgravqqvna
miekklepltsctiflgytsnlissgiretirylvqhnmvdvlvttaggveedlikclap
tylgefslrgkelrenginrignllvpnenyckfedwlmpildqmvmeqntegvkwtpsk
miarlgkeinnpesvyywaqknhipvfspaltdgslgdmiffhsyknpglvldivedlrl
intqaifakctgmiilgggvvkhhiananlmrngadyavyintaqefdgsdsgarpdeav
swgkirvdaqpvkvyadaslvfpllvaetfaqkmdafmhekned
>d1efva2 3.27.1.2.1 (208-331) C-terminal domain of the electron transfer flavoprotein alpha subunit {Human (Homo sapiens)}
drpeltgakvvvsggrglksgenfkllydladqlhaavgasraavdagfvpndmqvgqtg
kivapelyiavgisgaiqhlagmkdsktivainkdpeapifqvadygivadlfkvvpemt
eilk
>d1poxa1 3.27.1.3.1 (183-365) Pyruvate oxidase {Lactobacillus plantarum}
yasannyqtpllpepdvqavtrltqtllaaerpliyygigarkagkeleqlsktlkiplm
stypakgivadrypaylgsanrvaqkpanealaqadvvlfvgnnypfaevskafkntryf
lqididpaklgkrhktdiavladaqktlaailaqvserestpwwqanlanvknwraylas
led
>d1pvda1 3.27.1.3.3 (182-360) Pyruvate decarboxylase {Baker's yeast (Saccharomyces cerevisiae)}
qtpidmslkpndaesekevidtilalvkdaknpviladaccsrhdvkaetkklidltqfp
afvtpmgkgsiseqhpryggvyvgtlskpevkeavesadlilsvgallsdktknivefhs
dhmkirnatfpgvqmkfvlqklltniadaakgykpvavpartpanaavp
>d1zpda1 3.27.1.3.4 (188-362) Pyruvate decarboxylase {Zymomonas mobilis}
easdeaslnaavdetlkfianrdkvavlvgsklraagaeeaavkftdalggavatmaaak
sffpeenalyigtswgevsypgvektmkeadavialapvfndysttgwtdipdpkklvla
eprsvvvngirfpsvhlkdyltrlaqkvskktgsldffkslnagelkkaapadps
>d1bfd_1 3.27.1.3.5 (182-341) Benzoylformate decarboxylase {Pseudomonas putida}
svrlndqdldilvkalnsasnpaivlgpdvdaananadcvmlaerlkapvwvapsaprcp
fptrhpcfrglmpagiaaisqlleghdvvlvigapvfryhqydpgqylkpgtrlisvtcd
pleaarapmgdaivadigamasalanlveessrqlptaap
>d1d4oa_ 3.27.1.4.1 Transhydrogenase domain III {Bovine (Bos taurus)}
gthteinldnaidmireansiiitpgyglcaakaqypiadlvkmlseqgkkvrfgihpva
grmpgqlnvllaeagvpydivlemdeinhdfpdtdlvlvigandtvnsaaqedpnsiiag
mpvlevwkskqvivmkrslgvgyaavdnpifykpntamllgdakktcdalqakvres
>d1fsz_1 3.28.1.1.1 (23-231) Cell-division protein FtsZ {Methanococcus jannaschii}
spedkelleylqqtkakitvvgcggagnntitrlkmegiegaktvaintdaqqlirtkad
kkiligkkltrglgaggnpkigeeaakesaeeikaaiqdsdmvfitcglgggtgtgsapv
vaeiskkigaltvavvtlpfvmegkvrmknameglerlkqhtdtlvvipneklfeivpnm
plklafkvadevlinavkglvelitkdgl
>d1tuba1 3.28.1.1.2 (1-245) Tubulin alpha-subunit {Bovine (Bos taurus)}
mrecisihvgqagvqignacwelyclehgiqpdgqmpsdktigggddsfntffsetgagk
hvpravfvdleptvidevrtgtyrqlfhpeqlitgkedaannyarghytigkeiidlvld
rirkladqctglqgfsvfhsfgggtgsgftsllmerlsvdygkksklefsiypapqvsta
vvepynsiltthttlehsdcafmvdneaiydicrrnldierptytnlnrligqivssita
slrfd
>d1nbaa_ 3.29.1.1.1 N-carbamoylsarcosine amidohydrolase {Arthrobacter}
tfndiearlaavleeafeagtsiynergfkrrigygnrpavihidlanawtqpghpfscp
gmetiipnvqrineaarakgvpvfyttnvyrnrdassgtndmglwyskiptetlpadsyw
aqiddriapadgevvieknrasafpgtnlelfltsnridtlivtgataagcvrhtvedai
akgfrpiipretigdrvpgvvqwnlydidnkfgdvestdsvvqyldalpqfedtvpktls
dpqpeveapadpv
>d1yaca_ 3.29.1.2.1 YcaC {Escherichia coli}
tkpyvrldkndaavllvdhqagllslvrdiepdkfknnvlalgdlakyfnlptilttsae
tgpngplvpelkaqfpdapyiarpgninawdnedfvkavkatgkkqliiagvvtevcvaf
palsaieegfdvfvvtdasgtfneitrhsawdrmsqagaqlmtwfgvacelhrdwrndia
glatlfsnhipdyrnlmtsydtlt
>d1deaa_ 3.30.1.1.1 Glucosamine 6-phosphate deaminase {Escherichia coli}
mrliplttaeqvgkwaarhivnrinafkptadrpfvlglptggtpmttykalvemhkagq
vsfkhvvtfnmdeyvglpkehpesyysfmhrnffdhvdipaeninllngnapdidaecrq
yeekirsygkihlfmggvgndghiafnepasslasrtriktlthdtrvansrffdndvnq
vpkyaltvgvgtlldaeevmilvlgsqkalalqaavegcvnhmwtisclqlhpkaimvcd
epstmelkvktlryfneleaenikgl
>d1pvda3 3.31.1.1.2 (361-556) Pyruvate decarboxylase {Baker's yeast (Saccharomyces cerevisiae)}
astplkqewmwnqlgnflqegdvviaetgtsafginqttfpnntygisqvlwgsigfttg
atlgaafaaeeidpkkrvilfigdgslqltvqeistmirwglkpylfvlnndgytiekli
hgpkaqyneiqgwdhlsllptfgakdyethrvattgewdkltqdksfndnskirmieiml
pvfdapqnlvkqaklt
>d1zpda2 3.31.1.1.3 (2-187) Pyruvate decarboxylase {Zymomonas mobilis}
sytvgtylaerlvqiglkhhfavagdynlvlldnlllnknmeqvyccnelncgfsaegya
rakgaaaavvtysvgalsafdaiggayaenlpvilisgapnnndhaaghvlhhalgktdy
hyqlemaknitaaaeaiytpeeapakidhviktalrekkpvyleiacniasmpcaapgpa
salfnd
>d1zpda3 3.31.1.1.3 (363-566) Pyruvate decarboxylase {Zymomonas mobilis}
aplvnaeiarqvealltpnttviaetgdswfnaqrmklpngarveyemqwghigwsvpaa
fgyavgaperrnilmvgdgsfqltaqevaqmvrlklpviiflinnygytievmihdgpyn
niknwdyaglmevfngnggydsgaakglkaktggelaeaikvalantdgptliecfigre
dcteelvkwgkrvaaansrkpvnk
>d1poxa2 3.31.1.1.4 (9-182) Pyruvate oxidase {Lactobacillus plantarum}
tnilagaavikvleawgvdhlygipggsinsimdalsaerdrihyiqvrheevgamaaaa
dakltgkigvcfgsagpggthlmnglydaredhvpvlaligqfgttgmnmdtfqemnenp
iyadvadynvtavnaatlphvideairrayahqgvavvqipvdlpwqqisaedw
>d1poxa3 3.31.1.1.4 (366-593) Pyruvate oxidase {Lactobacillus plantarum}
kqegplqayqvlravnkiaepdaiysidvgdinlnanrhlkltpsnrhitsnlfatmgvg
ipgaiaaklnyperqvfnlagdggasmtmqdlvtqvqyhlpvinvvftncqygfikdeqe
dtnqndfigvefndidfskiadgvhmqafrvnkieqlpdvfeqakaiaqhepvlidavit
gdrplpaeklrldsamssaadieafkqryeaqdlqplstylkqfgldd
>d1bfd_2 3.31.1.1.5 (2-181) Benzoylformate decarboxylase {Pseudomonas putida}
asvhgttyellrrqgidtvfgnpgsnelpflkdfpedfryilalqeacvvgiadgyaqas
rkpafinlhsaagtgnamgalsnawnshsplivtagqqtramigvealltnvdaanlprp
lvkwsyepasaaevphamsraihmasmapqgpvylsvpyddwdkdadpqshhlfdrhvss
>d1bfd_3 3.31.1.1.5 (342-524) Benzoylformate decarboxylase {Pseudomonas putida}
epakvdqdagrlhpetvfdtlndmapenaiylneststtaqmwqrlnmrnpgsyyfcaag
glgfalpaaigvqlaeperqviavigdgsanysisalwtaaqyniptifvimnngtygal
rwfagvleaenvpgldvpgidfralakgygvqalkadnleqlkgslqealsakgpvliev
stv
>d1trka1 3.31.1.2.1 (3-337) Transketolase, TK {Baker's yeast (Saccharomyces cerevisiae)}
qftdidklavstirilavdtvskansghpgaplgmapaahvlwsqmrmnptnpdwinrdr
fvlsnghavallysmlhltgydlsiedlkqfrqlgsrtpghpefelpgvevttgplgqgi
snavgmamaqanlaatynkpgftlsdnytyvflgdgclqegisseasslaghlklgnlia
iyddnkitidgatsisfdedvakryeaygwevlyvengnedlagiakaiaqaklskdkpt
likmtttigygslhagshsvhgaplkaddvkqlkskfgfnpdksfvvpqevydhyqktil
kpgveannkwnklfseyqkkfpelgaelarrlsgq
>d1trka2 3.31.1.2.1 (338-534) Transketolase, TK {Baker's yeast (Saccharomyces cerevisiae)}
lpanwesklptytakdsavatrklsetvledvynqlpeliggsadltpsnltrwkealdf
qppssgsgnysgryirygirehamgaimngisafganykpyggtflnfvsyaagavrlsa
lsghpviwvathdsigvgedgpthqpietlahfrslpniqvwrpadgnevsaayknsles
khtpsiialsrqnlpql
>d1qs0a1 3.31.1.3.2 2-oxoisovalerate dehydrogenase, E1B {Pseudomonas putida}
neyaplrlhvpeptgrpgcqtdfsylrlndagqarkppvdvdaadtadlsyslvrvldeq
gdaqgpwaedidpqilrqgxraxlktrifdsrxvvaqrqkkxsfyxqslgeeaigsgqal
alnrtdxcfptyrqqsilxardvslvexicqllsnerdplkgrqlpixysvreagfftis
gnlatqfvqavgwaxasaikgdtkiasawigdgataesdfhtaltfahvyrapvilnvvn
nqwaistfqaiaggesttfagrgvgcgiaslrvdgndfvavyaasrwaaerarrglgpsl
iewvtyragphstsddpskyrpaddwshfplgdpiarlkqhlikighwseeehqattaef
eaaviaaqkeaeqygtlanghipsaasxfedvykexpdhlrrqrqel
>d1qs0b1 3.31.1.3.2 (2-205) 2-oxoisovalerate dehydrogenase, E1B {Pseudomonas putida}
atttxtxiqalrsaxdvxlerddnvvvygqdvgyfggvfrcteglqtkygksrvfdapis
esgivgtavgxgayglrpvveiqfadyfypasdqivsexarlryrsagefiapltlrxpc
gggiyggqthsqspeaxftqvcglrtvxpsnpydakglliasiecddpviflepkrlyng
pfdghhdrpvtpwskhphsavpdg
>d1b0pa1 3.31.1.4.1 (2-258) Pyruvate-ferredoxin oxidoreductase, PFOR, domains I and VI {Desulfovibrio africanus}
gkkmmttdgntatahvayamsevaaiypitpsstmgeeaddwaaqgrknifgqtltirem
qseagaagavhgalaagaltttftasqglllmipnmykisgellpgvfhvtaraiaahal
sifgdhqdiyaarqtgfamlasssvqeahdmalvahlaaiesnvpfmhffdgfrtsheiq
kievldyadmaslvnqkalaefraksmnpehphvrgtaqnpdiyfqgreaanpyylkvpg
ivaeymqkvasltgrsy
>d1b0pa2 3.31.1.4.1 (786-1232) Pyruvate-ferredoxin oxidoreductase, PFOR, domains I and VI {Desulfovibrio africanus}
vksevlprdslkgsqfqeplmefsgacsgcgetpyvrvitqlfgermfianatgcssiwg
asapsmpyktnrlgqgpawgnslfedaaeygfgmnmsmfarrthladlaakalesdasgd
vkealqgwlagkndpikskeygdklkkllagqkdgllgqiaamsdlytkksvwifggdgw
aydigyggldhvlasgedvnvfvmdtevysntggqsskatptgavakfaaagkrtgkkdl
armvmtygyvyvatvsmgyskqqflkvlkeaesfpgpslviayatcinqglrkgmgksqd
vmntavksgywplfrydprlaaqgknpfqldskapdgsveeflmaqnrfavldrsfpeda
krlraqvaheldvrfkelehmaatnifesfapaggkadgsvdfgegaefctrddtpmmar
pdsgeacdqnragtseqqgdlskrtkk
>d1gky__ 3.32.1.1.1 Guanylate kinase {Baker's yeast (Saccharomyces cerevisiae)}
xsrpivisgpsgtgkstllkklfaeypdsfgfsvssttrtpragevngkdynfvsvdefk
smiknnefiewaqfsgnyygstvasvkqvsksgktcildidmqgvksvkaipelnarflf
iappsvedlkkrlegrgteteesinkrlsaaqaelayaetgahdkvivnddldkaykelk
dfifaek
>d1deka_ 3.32.1.1.3 Deoxynucleoside monophosphate kinase {Bacteriophage T4}
mkliflsgvkrsgkdttadfimsnysavkyqlagpikdalayawgvfaantdypxltrke
fegidydretnlnltklevitimeqafcylngkspikgvfvfddegkesvnfvafnkitd
vinniedqwsvrrlmqalgtdlivnnfdrmywvklfaldyldkfnsgydyyivpdtrqdh
emdaaramgatvihvvrpgqksndthiteaglpirdgdlvitndgsleelfskikntlkv
l
>d1ckea_ 3.32.1.1.4 CMP kinase {Escherichia coli}
aiapvitidgpsgagkgtlckamaealqwhlldsgaiyrvlalaalhhhvdvasedalvp
lashldvrfvstngnlevilegedvsgeirtqevanaasqvaafprvreallrrqrafre
lpgliadgrdmgtvvfpdapvkifldasseerahrrmlqlqvkgfsvnferllaeikerd
drdrnravaplvpaadalvldsttlsieqviekalqyarqklala
>d1qf9a_ 3.32.1.1.5 UMP/CMP kinase {Dictyostelium discodeum}
mekskpnvvfvlggpgsgkgtqcanivrdfgwvhlsagdllrqeqqsgskdgemiatmik
ngeivpsivtvkllknaidanqgknflvdgfprneennnsweenmkdfvdtkfvlffdcp
eevmtqrllkrgessgrsddniesikkrfntfnvqtklvidhynkfdkvkiipanrdvne
vyndvenlfksmgf
>d1qhia_ 3.32.1.1.6 Thymidine kinase {Herpes simplex virus, type 1, HSV1}
mptllrvyidgphgmgkttttqllvalgsrddivyvpepmtywrvlgasetianiyttqh
rldqgeisagdaavvmtsaqitmgmpyavtdavlaphiggeagsshapppaltlifdrhp
iaallcypaarylmgsmtpqavlafvalipptlpgtnivlgalpedrhidrlakrqrpge
rldlamlaairrvygllantvrylqcggswredwgqlsgtavppqgaepqsnagprphig
dtlftlfrapellapngdlynvfawaldvlakrlrsmhvfildydqspagcrdallqlts
gmvqthvttpgsipticdlartfaremgea
>d1nksa_ 3.32.1.1.8 Adenylate kinase {Sulfolobus acidocaldarius}
mkigivtgipgvgkstvlakvkeildnqginnkiinygdfmlatalklgyakdrdemrkl
svekqkklqidaakgiaeearaggegylfidthavirtpsgylpglpsyviteinpsvif
lleadpkiilsrqkrdttrnrndysdesviletinfaryaatasavlagstvkvivnveg
dpsiaaneiirsmk
>d1zin_1 3.32.1.1.14 (1-125,161-217) Adenylate kinase {Bacillus stearothermophilus}
mnlvlmglpgagkgtqaekivaaygiphistgdmfraamkegtplglqakqymdrgdlvp
devtigivrerlskddcqngflldgfprtvaqaealetmladigrkldyvihidvrqdvl
merltXaddneatvanrlevnmkqmkplvdfyeqkgylrningeqdmekvfadirellgg
lar
>d1tmka_ 3.32.1.1.15 Thymidylate kinase {Baker's yeast (Saccharomyces cerevisiae)}
grgkliliegldrtgkttqcnilykklqpnckllkfperstrigglineyltddsfqlsd
qaihllfsanrweivdkikkdllegknivmdryvysgvaysaakgtngmdldwclqpdvg
llkpdltlflstqdvdnnaeksgfgderyetvkfqekvkqtfmklldkeirkgdesitiv
dvtnkgiqevealiwqivepvlsthidhdkfsff
>d4tmka_ 3.32.1.1.16 Thymidylate kinase {Escherichia coli}
rskyivieglegagkttarnvvvetleqlgirdmvftrepggtqlaeklrsllldiksvg
devitdkaevlmfyaarvqlvetvikpalangtwvigdrhdlstqayqgggrgidqhmla
tlrdavlgdfrpdltlyldvtpevglkrarargeldrieqesfdffnrtrarylelaaqd
ksihtidatqpleavmdairttvthwvkel
>d1shka_ 3.32.1.2.1 Shikimate kinase {Erwinia chrysanthemi}
mtepifmvgargcgkttvgrelaralgyefvdtdifmqhtsgmtvadvvaaegwpgfrrr
esealqavatpnrvvatgggmvlleqnrqfmrahgtvvylfapaeelalrlqaspqahqr
ptltgrpiaeemeavlrerealyqdvahyvvdatqppaaivcelmqtmrlpaa
>d1qhxa_ 3.32.1.3.1 Chloramphenicol phosphotransferase {Streptomyces venezuelae}
mttrmiilnggssagksgivrclqsvlpepwlafgvdslieamplkmqsaeggiefdadg
gvsigpefralegawaegvvamaragariiiddvflggaaaqerwrsfvgdldvlwvgvr
cdgavaegretargdrvagmaakqayvvhegveydvevdtthkesiecawaiaahvvp
>d1d6ja_ 3.32.1.4.1 Adenosine-5'phosphosulfate kinase (APS kinase) {Penicillium chrysogenum}
hasaltrsertelrnqrgltiwltglsasgkstlavelehqlvrdrrvhayrldgdnirf
glnkdlgfseadrnenirriaevaklfadsnsiaitsfispyrkdrdtarqlhevatpge
etglpfvevyvdvpvevaeqrdpkglykkaregvikeftgisapyeapanpevhvknyel
pvqdavkqiidyldtkgylpakk
>d1aqua_ 3.32.1.5.1 Estrogen sulfotransferase {Mouse (Mus musculus)}
eyyevfgefrgvlmdkrftkywedvemflarpddlviatypksgttwisevvymiykegd
vekckedaifnripylecrnedlingikqlkekesprivkthlppkllpasfweknckmi
ylcrnakdvavsyyyfllmitsypnpksfsefvekfmqgqvpygswydhvkawwekskns
rvlfmfyedmkedirrevvklieflerkpsaelvdriiqhtsfqemknnpstnytmmpee
mmnqkvspfmrkgiigdwknhfpealrerfdehykqqmkdctvkfrme
>d1nsta_ 3.32.1.5.3 Heparan sulfate N-deacetylase/N-sulfotransferase domain {Human (Homo sapiens)}
dplwqdpcedkrhkdiwskektcdrfpklliigpqktgttalylflgmhpdlssnypsse
tfeeiqffnghnyhkgidwymeffpipsnttsdfyfeksanyfdsevaprraaallpkak
vltilinpadrayswyqhqrahddpvalkytfhevitagsdassklralqnrclvpgwya
thierwlsayhanqilvldgkllrtepakvmdmvqkflgvtntidyhktlafdpkkgfwc
qlleggktkclgkskgrkypemdldsraflkdyyrdhnielskllykmgqtlptwlredl
q
>d1a7j__ 3.32.1.6.1 Phosphoribulokinase {Rhodobacter sphaeroides}
skkhpiisvtgssgagtstvkhtfdqifrregvkavsiegdafhrfnradmkaeldrrya
agdatfshfsyeanelkelervfreygetgqgrtrtyvhddaeaartgvapgnftdwrdf
dsdshllfyeglhgavvnsevniagladlkigvvpvinlewiqkihrdratrgytteavt
dvilrrmhayvhcivpqfsqtdinfqrvpvvdtsnpfiarwiptadesvvvirfrnprgi
dfpyltsmihgswmsransivvpgnkldlamqliltplidrvvreskv
>d1bif_1 3.32.1.7.1 (37-249) 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, kinase domain {Rat (Rattus norvegicus)}
cptlivmvglpargktyiskkltrylnfigvptrefnvgqyrrdmvktyksfefflpdne
eglkirkqcalaalndvrkflseegghvavfdatnttrerramifnfgeqngyktffves
icvdpeviaanivqvklgspdyvnrdsdeatedfmrriecyensyesldeeqdrdlsyik
imdvgqsyvvnrvadhiqsrivyylmnihvtpr
>d1ctqa_ 3.32.1.8.1 cH-p21 Ras protein {Human (Homo sapiens)}
mteyklvvvgaggvgksaltiqliqnhfvdeydptiedsyrkqvvidgetclldildtag
qeeysamrdqymrtgegflcvfainntksfedihqyreqikrvkdsddvpmvlvgnkcdl
aartvesrqaqdlarsygipyietsaktrqgvedafytlvreirqh
>d1mh1__ 3.32.1.8.2 Rac1 {Human (Homo sapiens)}
gspqaikcvvvgdgavgktcllisyttnafpgeyiptvfdnysanvmvdgkpvnlglwdt
agqedydrlrplsypqtdvslicfslvspasfenvrakwypevrhhcpntpiilvgtkld
lrddkdtieklkekkltpitypqglamakeigavkylecsaltqrglktvfdeairavlc
ppp
>d3raba_ 3.32.1.8.5 Rab3a {Rat (Rattus norvegicus)}
nfdymfkiliignssvgktsflfryaddsftpafvstvgidfkvktiyrndkriklqiwd
tagqeryrtittayyrgamgfilmyditneesfnavqdwstqiktyswdnaqvllvgnkc
dmedervvssergrqladhlgfeffeasakdninvkqtferlvdvicek
>d1byua_ 3.32.1.8.6 Ran {Dog (Canis familiaris)}
epqvqfklvlvgdggtgkttfvkrhltgefekkyvptlgvevhplvfhtnrgpikfnvwd
tagqekfgglrdgyyiqaqcaiimfdvtsrvtyknvpnwhrdlvrvcenipivlcgnkvd
ikdrkvkaksivfhrkknlqyydisaksnynfekpflwlarkligdpnlefvampalapp
evvmdpalaaqyehdlevaqtt
>d1e0sa_ 3.32.1.8.11 ADP-ribosylation factor {Human (Homo sapiens), ARF6}
gkvlskifgnkemrilmlgldaagkttilyklklgqsvttiptvgfnvetvtyknvkfnv
wdvggqdkirplwrhyytgtqglifvvdcadrdridearqelhriindremrdaiilifa
nkqdlpdamkpheiqeklgltrirdrnwyvqpscatsgdglyegltwltsnyk
>d1ek0a_ 3.32.1.8.13 Ypt51 {Yeast (Saccharomyces cerevisiae)}
vtsiklvllgeaavgkssivlrfvsndfaenkeptigaafltqrvtinehtvkfeiwdta
gqerfaslapxyyrnaqaalvvydvtkpqsfikarhwvkelheqaskdiiialvgnkidx
lqeggerkvareegeklaeekgllffetsaktgenvndvflgigekiplk
>d1cipa2 3.32.1.8.15 (32-60,182-347) Transducin (alpha subunit) {Rat (Rattus rattus)}
revkllllgagesgkstivkqmkiiheagXtgivethftfkdlhfkmfdvggqrserkkw
ihcfegvtaiifcvalsdydlvlaedeemnrmhesmklfdsicnnkwftdtsiilflnkk
dlfeekikksplticypeyagsntyeeaaayiqcqfedlnkrkdtkeiythftcatdtkn
vqfvfdavtdviiknn
>d1exma3 3.32.1.8.18 (3-212) Elongation factor Tu (EF-Tu), N-terminal (G) domain {Thermus thermophilus}
gefirtkphvnvgtighvdhgkttltaaltfvtaaenpnvevkdygdidkapeerargit
intahveyetakrhyshvdcpghadyiknmitgaaqmdgailvvsaadgpmpqtrehill
arqvgvpyivvfmnkvdmvddpelldlvemevrdllnqyefpgdevpvirgsallaleqm
hrnpktrrgenewvdkiwelldaideyipt
>d1dar_2 3.32.1.8.20 (1-282) Elongation factor G (EF-G), N-terminal (G) domain {Thermus thermophilus}
mavkveydlkrlrnigiaahidagktttterilyytgrihkigevhegaatmdfmeqere
rgititaavttcfwkdhriniidtpghvdftieversmrvldgaivvfdssqgvepqset
vwrqaekykvpriafankmdktgadlwlvirtmqerlgarpvvmqlpigredtfsgiidv
lrmkaytygndlgtdireipipeeyldqareyheklvevaadfdenimlkylegeeptee
elvaairkgtidlkitpvflgsalknkgvqllldavvdylps
>d1egaa1 3.32.1.8.21 (4-182) GTPase Era, N-terminal domain {Escherichia coli}
dksycgfiaivgrpnvgkstllnkllgqkisitsrkaqttrhrivgihtegayqaiyvdt
pglhmeekrainrlmnkaasssigdvelvifvvegtrwtpddemvlnklregkapvilav
nkvdnvqekadllphlqflasqmnfldivpisaetglnvdtiaaivrkhlpeathhfpe
>d1dg3a2 3.32.1.8.22 (6-283) Interferon-induced guanylate-binding protein 1 (GBP1), N-terminal domain {Human (Homo sapiens)}
hmtgpmclientngrlmanpealkilsaitqpmvvvaivglyrtgksylmnklagkkkgf
slgstvqshtkgiwmwcvphpkkpghilvlldteglgdvekgdnqndswifalavllsst
fvynsigtinqqamdqlyyvtelthrirsksspdenenevedsadfvsffpdfvwtlrdf
sldleadgqpltpdeyltyslklkkgtsqkdetfnlprlcirkffpkkkcfvfdrpvhrr
klaqleklqdeeldpefvqqvadfcsyifsnsktktls
>d1b7ta2 3.32.1.9.2 (5-28) Myosin S1, motor domain {Bay scallop (Aequipecten irradians)}
fsdpdfqylavdrkklmkeqtaaf
>d1lvk_2 3.32.1.9.3 (2-33,80-759) Myosin S1, motor domain {Slime mold (Dictyostelium discoideum)}
npihdrtsdyhkylkvkqgdsdlfkltvsdkrXrnpikfdgvedmselsylnepavfhnl
rvrynqdliytysglflvavnpfkripiytqemvdifkgrrrnevaphifaisdvayrsm
lddrqnqsllitgesgagktentkkviqylasvagrnqangsgvleqqilqanpileafg
nakttrnnnssrfgkfieiqfnnagfisgasiqsylleksrvvfqstsernyhifyqlla
gataeekkalhlagpesfnylnqsgcvdikgvsdedefkitrqamdivgfsqeeqmsifk
iiagilhlgnikfekgagegavlkdktalnaastvfgvnpsvlekalmeprilagrdlva
qhlnvekssssrdalvkalygrlflwlvkkinnvlcserkayfigvldisgfeifkvnsf
eqlcinytneklqqffnhhmfkveqekylkekinwtfidfgldsqatidlidgrqppgil
alldeqsvfpnatdntlitklhshfskknakyeeprfsktefgvthyagqvmyeiqdwle
knkdplqqdlelcfkdssdnvvtklfndpniasrakkganfltvaaqykeqlaslmatle
ttnphfvrciipnnkqlpakledkvvldqlrcngvlegiritrkgfpnriiyadfvkryy
dlapnvprdaedsqkatdavlkhlnidpeqfrfgitkiffragqlarieeare
>d1bg2__ 3.32.1.9.4 Kinesin {Human (Homo sapiens)}
dlaecnikvmcrfrplnesevnrgdkyiakfqgedtvviaskpyafdrvfqsstsqeqvy
ndcakkivkdvlegyngtifaygqtssgkthtmegklhdpegmgiiprivqdifnyiysm
denlefhikvsyfeiyldkirdlldvsktnlsvhedknrvpyvkgcterfvcspdevmdt
idegksnrhvavtnmnehssrshsiflinvkqentqteqklsgklylvdlagsekvsktg
aegavldeakninkslsalgnvisalaegstyvpyrdskmtrilqdslggncrttivicc
spssynesetkstllfgqrakti
>d1byi__ 3.32.1.10.1 Dethiobiotin synthetase {Escherichia coli}
skryfvtgtdtevgktvascallqaakaagyrtagykpvasgsektpeglrnsdalalqr
nsslqldyatvnpytfaeptsphiisaqegrpieslvmsaglraleqqadwvlvegaggw
ftplsdtftfadwvtqeqlpvilvvgvklgcinhamltaqviqhagltlagwvandvtpp
gkrhaeymttltrmipapllgeipwlaenpenaatgkyinlall
>d1qf5a_ 3.32.1.10.2 Adenylosuccinate synthetase, PurA {Escherichia coli}
gnnvvvlgtqwgdegkgkivdllterakyvvryqgghnaghtlvingektvlhlipsgil
renvtsiigngvvlspaalmkemkeledrgipvrerlllseacplildyhvaldnareka
rgakaigttgrgigpayedkvarrglrvgdlfdketfaeklkevmeyhnfqlvnyykaea
vdyqkvlddtmavadiltsmvvdvsdlldqarqrgdfvmfegaqgtlldidhgtypyvts
snttaggvatgsglgpryvdyvlgilkaystrvgagpfptelfdetgeflckqgnefgat
tgrrrrtgwldtvavrravqlnslsgfcltkldvldglkevklcvayrmpdgrevtttpl
aaddwkgvepiyetmpgwsestfgvkdrsglpqaalnyikrieeltgvpidiistgpdrt
etmilrdpfda
>d1cp2a_ 3.32.1.10.6 Nitrogenase iron protein {Clostridium pasteurianum}
mrqvaiygkggigkstttqnltsglhamgktimvvgcdpkadstrlllgglaqksvldtl
reegedveldsilkegyggircvesggpepgvgcagrgiitsinmleqlgaytddldyvf
ydvlgdvvcggfampiregkaqeiyivasgemmalyaanniskgiqkyaksggvrlggii
cnsrkvaneyelldafakelgsqlihfvprspmvtkaeinkqtvieydptceqaeeyrel
arkvdanelfvipkpmtqerleeilmqyg
>d1ffh_2 3.32.1.10.7 (89-295) GTPase domain of the signal sequence recognition protein Ffh {Thermus aquaticus}
earlpvlkdrnlwflvglqgsgktttaaklalyykgkgrrpllvaadtqrpaareqlrll
gekvgvpvlevmdgespesirrrveekarleardlilvdtagrlqideplmgelarlkev
lgpdevllvldamtgqealsvarafdekvgvtglvltkldgdarggaalsarhvtgkpiy
fagvsekpeglepfyperlagrilgmg
>d2reb_1 3.32.1.11.1 (3-268) RecA protein, ATPase-domain {Escherichia coli}
denkqkalaaalgqiekqfgkgsimrlgedrsmdvetistgslsldialgagglpmgriv
eiygpessgkttltlqviaaaqregktcafidaehaldpiyarklgvdidnllcsqpdtg
eqaleicdalarsgavdvivvdsvaaltpkaeiegeigdshmglaarmmsqamrklagnl
kqsntllifinqirmkigvmfgnpetttggnalkfyasvrldirrigavkegenvvgset
rvkvvknkiaapfkqaefqilygegi
>d1cr1a_ 3.32.1.11.2 Gene 4 protein (g4p, DNA primase), helicase domain {Bacteriophage T7}
mrerirehlsseesvgllfsgctgindktlgarggevimvtsgsgmgkstfvrqqalqwg
tamgkkvglamleesveetaedliglhnrvrlrqsdslkreiiengkfdqwfdelfgndt
fhlydsfaeaetdrllaklaymrsglgcdviildhisivvsasgesderkmidnlmtklk
gfakstgvvlvvichlknpdkgkaheegrpvsitdlrgsgalrqlsdtiialernqqgdm
pnlvlvrilkcrftgdtgiagymeynketgwlepssy
>d1bmfa3 3.32.1.11.3 (95-379) Central domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
vdvpvgeellgrvvdalgnaidgkgpigskarrrvglkapgiiprisvrepmqtgikavd
slvpigrgqreliigdrqtgktsiaidtiinqkrfndgtdekkklyciyvaigqkrstva
qlvkrltdadamkytivvsatasdaaplqylapysgcsmgeyfrdngkhaliiyddlskq
avayrqmslllrrppgreaypgdvfylhsrlleraakmndafgggsltalpvietqagdv
sayiptnvisitdgqifletelfykgirpainvglsvsrvgsaaq
>d1bmfd3 3.32.1.11.3 (82-357) Central domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
iripvgpetlgrimnvigepidergpiktkqfaaihaeapefvemsveqeilvtgikvvd
llapyakggkiglfggagvgktvlimelinnvakahggysvfagvgertregndlyhemi
esgvinlkdatskvalvygqmneppgararvaltgltvaeyfrdqegqdvllfidnifrf
tqagsevsallgripsavgyqptlatdmgtmqeritttkkgsitsvqaiyvpaddltdpa
pattfahldattvlsraiaelgiypavdpldstsri
>d1cbua_ 3.32.1.11.6 Adenosylcobinamide kinase/adenosylcobinamide phosphate guanylyltransferase CobU {Salmonella typhimurium}
milvtggarsgksrhaealigdapqvlyiatsqilddemaariqhhkdgrpahwrtaecw
rhldtlitadlapddaillecittmvtnllfalggendpeqwdyaameraiddeiqilia
acqrcpakvvlvtnevgmgivpenrlarhfrdiagrvnqrlaaaadevwlvvsgigvkik
>d1b0ua_ 3.32.1.12.1 ATP-binding subunit of the histidine permease {Salmonella typhimurium}
nklhvidlhkrygghevlkgvslqaragdvisiigssgsgkstflrcinflekpsegaii
vngqninlvrdkdgqlkvadknqlrllrtrltmvfqhfnlwshmtvlenvmeapiqvlgl
skhdareralkylakvgideraqgkypvhlsggqqqrvsiaralamepdvllfdeptsal
dpelvgevlrimqqlaeegktmvvvthemgfarhvsshviflhqgkieeegdpeqvfgnp
qsprlqqflkgslkkleh
>d1qhla_ 3.32.1.12.2 Cell division protein MukB {Escherichia coli}
rgkfrsltlinwngffartfdldelvttlsggngagksttmaafvtalipdltllhfrnt
teagatsgsrdkglhgklkagvcysmldtinsrhqrvvvgvrlqqvagrdrkvdikpfai
qglpmsvqptqlvtetlnerqarvlplnelkdkleamegvqfkqfnsitdyhslmfdlgi
iarrlrsasdrskfyrlieaslyggissaitrslrdyllpen
>d1pjr_1 3.32.1.13.1 (1-318) DEXX box DNA helicase {Bacillus stearothermophilus, PcrA}
mnflseqllahlnkeqqeavrttegpllimagagsgktrvlthriaylmaekhvapwnil
aitftnkaaremrervqsllggaaedvwistfhsmcvrilrrdidriginrnfsildptd
qlsvmktilkeknidpkkfeprtilgtisaaknellppeqfakrastyyekvvsdvyqey
qqrllrnhsldfddlimttiqlfdrvpdvlhyyqykfqyihideyqdtnraqytlvkkla
erfqnicavgdadqsiyrwrgadiqnilsferdypnakvilleqnyrstkrilqaanevi
ehnvnrkpkriwtenpeg
>d1pjr_2 3.32.1.13.1 (319-651) DEXX box DNA helicase {Bacillus stearothermophilus, PcrA}
kpilyyeamneadeaqfvagrireavergerryrdfavlyrtnaqsrvmeemllkanipy
qivgglkfydrkeikdilaylrvianpdddlsllriinvpkrgigastidklvryaadhe
lslfealgelemiglgakaagalaafrsqleqwtqlqeyvsvtelveevldksgyremlk
aertieaqsrlenldeflsvtkhfenvsddksliafltdlalisdldeldgteqaaegda
vmlmtlhaakglefpvvfligmeegifphnrsledddemeeerrlayvgitraeeelvlt
saqmrtlfgniqmdppsrflneipahlletasr
>d1qdea_ 3.32.1.13.3 Initiation factor 4a N-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
iqtnydkvvykfddmeldenllrgvfgygfeepsaiqqraimpiieghdvlaqaqsgtgk
tgtfsiaalqridtsvkapqalmlaptrelalqiqkvvmalafhmdikvhaciggtsfve
daeglrdaqivvgtpgrvfdniqrrrfrtdkikmfildeademlssgfkeqiyqiftllp
pttqvvllsatmpndvlevttkfmrnpvrilv
>d1d2ma1 3.32.1.13.4 (2-409) Nucleotide excision repair enzyme UvrB {Thermus thermophilus}
tfryrgpspkgdqpkaiaglvealrdgerfvtllgatgtgktvtmakviealgrpalvla
pnkilaaqlaaefrelfpenaveyfisyydyyqpeayvpgkdlyiekdasinpeierlrh
sttrslltrrdvivvasvsaiyglgdpreyrarnlvvergkpyprevllerllelgyqrn
didlspgrfrakgevleifpayetepirvelfgdeverisqvhpvtgerlrelpgfvlfp
athylspegleeilkeiekelwervryfeergevlyaqrlkertlydlemlrvmgtcpgv
enyaryftgkapgeppytlldyfpedflvfldeshvtvpqlqgmyrgdyarkktlvdygf
rlpsaldnrplrfeeflervsqvvfvsatpgpfelahsgrvveqiirp
>d1d2ma2 3.32.1.13.4 (410-583) Nucleotide excision repair enzyme UvrB {Thermus thermophilus}
tglldplvrvkptenqildlmegireraargertlvtvltvrmaeeltsflvehgirary
lhheldafkrqalirdlrlghydclvginllregldipevslvaildadkegflrsersl
iqtigraarnargevwlyadrvseamqraieetnrrralqeaynlehgitpetv
>d1a5t_2 3.32.1.13.6 (1-166) delta prime subunit of DNA polymerase III, N-terminal domain {Escherichia coli}
mrwypwlrpdfeklvasyqagrghhalliqalpgmgddaliyalsryllcqqpqghkscg
hcrgcqlmqagthpdyytlapekgkntlgvdavrevteklneharlggakvvwvtdaall
tdaaanallktleeppaetwfflatreperllatlrsrcrlhylap
>d1d2na_ 3.32.1.13.7 Hexamerization domain of N-ethylmalemide-sensitive fusion (NSF) protein {Chinese hamster (Cricetulus griseus)}
edyasyimngiikwgdpvtrvlddgellvqqtknsdrtplvsvllegpphsgktalaaki
aeesnfpfikicspdkmigfsetakcqamkkifddayksqlscvvvddierlldyvpigp
rfsnlvlqallvllkkappqgrklliigttsrkdvlqememlnafsttihvpniatgeql
lealellgnfkdkerttiaqqvkgkkvwigikkllmliemslqmdpeyrvrkflallree
gaspld
>d1dooe_ 3.32.1.13.8 HslU {Bacteria (Escherichia coli)}
semtpreivseldkhiigqdnakrsvaialrnrwrrmqlneelrhevtpknilmigptgv
gkteiarrlaklanapfikveatkftevgyvgkevdsiirdltdaavkmvrvqaieknry
raeelaeerildvlippaknnwgqteqqqepsaarqafrkklregqlddkeieidlaaap
mgveimappgmeemtsqlqsmfqnlggqkqkarklkikdamkllieeeaaklvnpeelkq
daidaveqhgivfideidkickrgessgpdvsregvqrdllplvegctvstkhgmvktdh
ilfiasgafqiakpsdlipelqgrlpirvelqalttsdferiltepnasitvqykalmat
egvnieftdsgikriaeaawqvnestenigarrlhtvlerlmeeisydasdlsgqnitid
adyvskhldalvadedlsrfil
>d1a1va1 3.32.1.14.1 (190-325) HCV helicase domain {Hepatitis C virus, HCV}
ppavpqsfqvahlhaptgsgkstkvpaayaaqgykvlvlnpsvaatlgfgaymskahgvd
pnirtgvrtittgspitystygkfladggxsggaydiiicdechstdatsilgigtvldq
aetagarlvvlatatp
>d1a1va2 3.32.1.14.1 (326-624) HCV helicase domain {Hepatitis C virus, HCV}
pgsvtvphpnieevalsttgeipfygkaiplevikggrhlifchskkkcdelaaklvalg
inavayyrgldvsviptsgdvvvvatdalmtgftgdfdsvidcntxvtqtvdfsldptft
ietttlpqdavsrtqrrgrtgrgkpgiyrfvapgerpsgmfdssvlcecydagxawyelt
paettvrlraymntpglpvcqdhlefwegvftglthidahflsqtkqsgenfpylvayqa
tvcaraqapppswdqmwkclirlkptlhgptpllyrlgavqnevtlthpitkyimtcms
>d1ble__ 3.33.1.1.1 Fructose permease, subunit IIb {Bacillus subtilis}
mnivlariddrfihgqiltrwikvhaadriivvsddiaqdemrktlilsvapsnvkasav
svskmakafhspryegvtamllfenpsdivslieagvpiktvnvggmrfenhrrqitksv
svteqdikafetlsdkgvklelrqlpsdasedfvqilrnvt
>d1d0va_ 3.34.1.1.1 Nicotinate mononucleotide:5,6-dimethylbenzimidazole phosphoribosyltransferase (CobT) {Salmonella typhimurium}
lhallrdipapdaeamartqqhidgllkppgslgrletlavqlagmpglngtpqvgekav
lvmcadhgvwdegvavspkivtaiqaanmtrgttgvcvlaaqagakvhvidvgidaepip
gvvnmrvargcgniavgpamsrlqaealllevsryacdlaqrgvtlfgvgelgmanttpa
aamvsvftgsdakevvgiganlppsridnkvdvvrraiainqpnprdgidvlskvggfdl
vgmtgvmlgaarcglpvlldgflsysaalaacqiapavrpylipshfsaekgarialahl
smepylhmamrlgegsgaalampiveaacamfhnmgelaasnivlp
>d1chd__ 3.35.1.1.1 Methylesterase CheB, C-terminal domain {Salmonella typhimurium}
llssekliaigastggteairhvlqplplsspaviitqhmppgftrsfaerlnklcqisv
keaedgervlpghayiapgdkhmelarsganyqikihdgppvnrhrpsvdvlfhsvakha
grnavgviltgmgndgaagmlamyqagawtiaqneascvvfgmpreainmggvsevvdls
qvsqqmlakisagqairi
>d1gci__ 3.36.1.1.5 Subtilisin BL {Bacillus lentus}
aqsvpwgisrvqapaahnrgltgsgvkvavldtgisthpdlnirggasfvpgepstqdgn
ghgthvagtiaalnnsigvlgvapsaelyavkvlgasgsgsvssiaqglewagnngmhva
nlslgspspsatleqavnsatsrgvlvvaasgnsgagsisyparyanamavgatdqnnnr
asfsqygagldivapgvnvqstypgstyaslngtsmatphvagaaalvkqknpswsnvqi
rnhlkntatslgstnlygsglvnaeaatr
>d1d3va_ 3.37.1.1.1 Arginase {Rat (Rattus norvegicus)}
kpieiigapfskgqprggvekgpaalrkaglveklketeynvrdhgdlafvdvpndspfq
ivknprsvgkaneqlaavvaetqkngtisvvlggdhsmaigsisgharvhpdlcviwvda
htdintplttssgnlhgqpvafllkelkgkfpdvpgfswvtpcisakdivyiglrdvdpg
ehyiiktlgikyfsmtevdklgigkvmeetfsyllgrkkrpihlsfdvdgldpvftpatg
tpvvgglsyreglyiteeiyktgllsgldimevnptlgktpeevtrtvntavaltlscfg
tkregnhk
>d1c3pa_ 3.37.1.2.1 HDAC homologue {Aquifex aeolicus}
kkvkligtldygkyrypknhplkiprvslllrfkdamnlidekeliksrpatkeelllfh
tedyintlmeaercqcvpkgarekyniggyenpvsyamftgsslatgstvqaieeflkgn
vafnpaggmhhafksrangfcyinnpavgieylrkkgfkrilyidldahhcdgvqeafyd
tdqvfvlslhqspeyafpfekgfleeigegkgkgynlniplpkglndneflfalekslei
vkevfepevyllqlgtdplledylskfnlsnvaflkafnivrevfgegvylggggyhpya
larawtliwcelsgrevpeklnnkakellksidfeefddevdrsymletlkdpwrggevr
kevkdtlekaka
>d3cla__ 3.38.1.1.1 Chloramphenicol acetyltransferase {Escherichia coli}
mnytkfdvknwvrrehfefyrhrlpcgfsltskidittlkkslddsaykfypvmiyliaq
avnqfdelrmaikddelivwdsvdpqftvfhqetetfsalscpyssdidqfmvnylsvme
ryksdtklfpqgvtpenhlnisalpwvnfdsfnlnvanftdyfapiitmakyqqegdrll
lplsvqvhhavcdgfhvarfinrlqelcnsklk
>d1eaf__ 3.38.1.1.3 Dihydrolipoamide acetyltransferase {Azotobacter vinelandii}
ippippvdfakygeieevpmtrlmqigatnlhrswlnvphvtqfesaditeleafrvaqk
avakkagvkltvlplllkacayllkelpdfnsslapsgqalirkkyvhigfavdtpdgll
vpvirnvdqksllqlaaeaaelaekarskklgadamqgacftisslghiggtaftpivna
pevailgvskasmqpvwdgkafqprlmlplslsydhrvingaaaarftkrlgdlladira
ill
>d1e2o__ 3.38.1.1.5 Dihydrolipoamide succinyltransferase {Escherichia coli}
arsekrvpmtrlrkrvaerlleaknstamlttfnevnmkpimdlrkqygeafekrhgirl
gfmsfyvkavvealkrypevnasidgddvvyhnyfdvsmavstprglvtpvlrdvdtlgm
adiekkikelavkgrdgkltvedltggnftitnggvfgslmstpiinppqsailgmhaik
drpmavngqveilpmmylalsydhrlidgresvgflvtikelledptrllldv
>d1d1qa_ 3.39.1.1.3 Tyrosine phosphatase {Yeast (Saccharomyces cerevisiae)}
iekpkisvafialgnfcrspmaeaifkhevekanlenrfnkidsfgtsnyhvgespdhrt
vsickqhgvkinhkgkqiktkhfdeydyiigmdesninnlkkiqpegskakvclfgdwnt
ndgtvqtiiedpwygdiqdfeynfkqityfskqflkkel
>d1iiba_ 3.39.2.1.1 Enzyme IIB-cellobiose {Escherichia coli}
kkhiylfssagmstsllvskmraqaekyevpviieafpetlagekgqnadvvllgpqiay
mlpeiqrllpnkpvevidsllygkvdglgvlkaavaaikkaaa
>d1vhra_ 3.40.1.1.1 VH1-related dual-specificity phosphatase, VHR {Human (Homo sapiens)}
svqdlndllsdgsgcyslpsqpcnevtpriyvgnasvaqdipklqklgithvlnaaegrs
fmhvntnanfykdsgitylgikandtqefnlsayferaadfidqalaqkngrvlvhcreg
ysrsptlviaylmmrqkmdvksalsivrqnreigpndgflaqlcqlndrlakegklkp
>d1mkp__ 3.40.1.1.2 Mapk phosphotase Pyst1 (mkp3) {Human (Homo sapiens)}
asfpveilpflylgcakdstnldvleefgikyilnvtpnlpnlfenagefkykqipisdh
wsqnlsqffpeaisfideargkncgvlvhslagisrsvtvtvaylmqklnlsmndaydiv
kmkksnispnfnfmgqlldfertl
>d1pty__ 3.40.1.2.1 Tyrosine phosphatase {Human (Homo sapiens), 1B}
emekefeqidksgswaaiyqdirheasdfpcrvaklpknknrnryrdvspfdhsriklhq
edndyinaslikmeeaqrsyiltqgplpntcghfwemvweqksrgvvmlnrvmekgslkc
aqywpqkeekemifedtnlkltlisediksyytvrqlelenlttqetreilhfhyttwpd
fgvpespasflnflfkvresgslspehgpvvvhssagigrsgtfcladtclllmdkrkdp
ssvdikkvllemrkfrmgliqtadqlrfsylaviegakfimgdssvqdqwkelshedl
>d1ypta_ 3.40.1.2.6 Tyrosine phosphatase {Yersinia enterocolitica}
pearaelssrlttlrntlapatndprylqacggeklnrfrdiqcrrqtavradlnanyiq
vgntrtiacqyplqsqleshfrmlaenrtpvlavlassseianqrfgmpdyfrqsgtygs
itveskmtqqvglgdgimadmytltireagqktisvpvvhvgnwpdqtavssevtkalas
lvdqtaetkrnmyeskgssavaddsklrpvihcragvgrtaqligamcmndsrnsqlsve
dmvsqmrvqrngimvqkdeqldvliklaegqgrpllns
>d1d5ra2 3.40.1.3.1 (14-187) Phoshphoinositide phosphatase Pten (Pten tumor suppressor), N-terminal domain {Human (Homo sapiens)}
rryqedgfdldltyiypniiamgfpaerlegvyrnniddvvrfldskhknhykiynlcae
rhydtakfncrvaqypfedhnppqlelikpfcedldqwlseddnhvaaihckagkgrtgv
micayllhrgkflkaqealdfygevrtrdkkgvtipsqrryvyyysyllknhld
>d1qb0a_ 3.41.1.1.2 CDC25b {Human (Homo sapiens)}
dhreligdyskafllqtvdgkhqdlkyispetmvalltgkfsnivdkfvivdcrypyeye
gghiktavnlplerdaesfllkspiapcsldkrvilifhcefssergprmcrfirerdra
vndypslyypemyilkggykeffpqhpnfcepqdyrpmnheafkdelktfrlktrswa
>d1rhs_1 3.41.1.2.1 (1-149) Rhodanese {Bovine (Bos taurus)}
vhqvlyralvstkwlaesvragkvgpglrvldaswyspgtrearkeylerhvpgasffdi
eecrdkaspyevmlpseagfadyvgslgisndthvvvydgddlgsfyaprvwwmfrvfgh
rtvsvlnggfrnwlkeghpvtsepsrpep
>d1rhs_2 3.41.1.2.1 (150-293) Rhodanese {Bovine (Bos taurus)}
aifkatlnrsllktyeqvlenleskrfqlvdsraqgrylgtqpepdavgldsghirgsvn
mpfmnfltedgfekspeelramfeakkvdltkpliatxrkgvtachialaaylcgkpdva
iydgswfewfhrappetwvsqgkg
>d1e0ca1 3.41.1.2.2 (1-135) Sulfurtransferase {Azotobacter vinelandii}
mddfaslplviepadlqarlsapelilvdltsaaryaeghipgarfvdpkrtqlgqppap
glqppreqleslfgelghrpeavyvvyddegggwagrfiwlldvigqqryhylnggltaw
laedrplsrelpapa
>d1e0ca2 3.41.1.2.2 (136-271) Sulfurtransferase {Azotobacter vinelandii}
ggpvalslhdeptasrdyllgrlgaadlaiwdarspqeyrgekvlaakgghipgavnfew
taamdpsralrirtdiagrleelgitpdkeivthxqthhrsgltyliakalgyprvkgya
gswgewgnhpdtpvel
>d2trxa_ 3.42.1.1.1 Thioredoxin {Escherichia coli}
sdkiihltddsfdtdvlkadgailvdfwaewcgpckmiapildeiadeyqgkltvaklni
dqnpgtapkygirgiptlllfkngevaatkvgalskgqlkefldanla
>d1thx__ 3.42.1.1.2 Thioredoxin {Anabaena}
skgvititdaefesevlkaeqpvlvyfwaswcgpcqlmsplinlaantysdrlkvvklei
dpnpttvkkykvegvpalrlvkgeqildstegviskdkllsfldthln
>d1dbya_ 3.42.1.1.3 Thioredoxin {Chlamydomonas reinhardtii}
meagavnddtfknvvlessvpvlvdfwapwcgpcriiapvvdeiageykdklkcvklntd
espnvaseygirsiptimvfkggkkcetiigavpkativqtvekyln
>d1tof__ 3.42.1.1.3 Thioredoxin {Chlamydomonas reinhardtii}
ggsvividskaawdaqlakgkeehkpivvdftatwcgpckmiaplfetlsndyagkvifl
kvdvdavaavaeaagitamptfhvykdgvkaddlvgasqdklkalvakhaaa
>d1quwa_ 3.42.1.1.4 Thioredoxin {Bacillus acidocaldarius}
atmtltdanfqqaiqgdkpvlvdfwaawcgpcrmmapvleefaeahadkvtvaklnvden
pettsqfgimsiptlilfkggrpvkqligyqpkeqleaqladvlq
>d1erv__ 3.42.1.1.5 Thioredoxin {Human (Homo sapiens)}
mvkqiesktafqealdaagdklvvvdfsatwcgpckmikpffhslsekysnviflevdvd
dcqdvasecevksmptfqffkkgqkvgefsgankekleatinelv
>d1aba__ 3.42.1.1.7 Glutaredoxin {Bacteriophage T4}
mfkvygydsnihkcgpcdnakrlltvkkqpfefinimpekgvfddekiaelltklgrdtq
igltmpqvfapdgshiggfdqlreyfk
>d1egr__ 3.42.1.1.7 Glutaredoxin {Bacteriophage T4}
mqtvifgrsgcpycvrakdlaeklsnerddfqyqyvdiraegitkedlqqkagkpvetvp
qifvdqqhiggytdfaawvkenlda
>d3grx__ 3.42.1.1.8 Glutaredoxin {Escherichia coli}
anveiytketcpyshrakallsskgvsfqelpidgnaakreemikrsgrttvpqifidaq
higgyddlyaldarggldpllk
>d1kte__ 3.42.1.1.9 Thioltransferase {Pig (Sus scrofa)}
aqafvnskiqpgkvvvfikptcpfcrktqellsqlpfkegllefvditatsdtneiqdyl
qqltgartvprvfigkeciggctdlesmhkrgelltrlqqvgavk
>d1bjx__ 3.42.1.2.1 Protein disulfide isomerase {Human (Homo sapiens)}
aattlpdgaaaeslvessevavigffkdvesdsakqflqaaeaiddipfgitsnsdvfsk
yqldkdgvvlfkkfdegrnnfegevtkenlldfikhnqlplviefteqta
>d1mek__ 3.42.1.2.1 Protein disulfide isomerase {Human (Homo sapiens)}
dapeeedhvlvlrksnfaealaahkyllvefyapwcghckalapeyakaagklkaegsei
rlakvdateesdlaqqygvrgyptikffrngdtaspkeytagreaddivnwlkkrtgpaa
>d1a8l_1 3.42.1.2.2 (1-119) Protein disulfide isomerase {Pyrococcus furiosus}
mglisdadkkvikeeffskmvnpvklivfvrkdhcqycdqlkqlvqelseltdklsyeiv
dfdtpegkelakryridrapattitqdgkdfgvryfglpaghefaafledivdvsreet
>d1a8l_2 3.42.1.2.2 (120-226) Protein disulfide isomerase {Pyrococcus furiosus}
nlmdetkqairnidqdvrilvfvtptcpycplavrmahkfaientkagkgkilgdmveai
eypewadqynvmavpkiviqvngedrvefegaypekmflekllsals
>d1a8y_1 3.42.1.3.1 (3-126) Calsequestrin {Rabbit (Oryctolagus cuniculus)}
gldfpeydgvdrvinvnaknyknvfkkyevlallyheppeddkasqrqfemeelilelaa
qvledkgvgfglvdsekdaavakklglteedsiyvfkedevieydgefsadtlveflldv
ledp
>d1a8y_2 3.42.1.3.1 (127-228) Calsequestrin {Rabbit (Oryctolagus cuniculus)}
veliegerelqafeniedeikligyfknkdsehykafkeaaeefhpyipffatfdskvak
kltlklneidfyeafmeepvtipdkpnseeeivnfveehrrs
>d1a8y_3 3.42.1.3.1 (229-347) Calsequestrin {Rabbit (Oryctolagus cuniculus)}
tlrklkpesmyetweddmdgihivafaeeadpdgyefleilksvaqdntdnpdlsiiwid
pddfpllvpywektfdidlsapqigvvnvtdadsvwmemddeedlpsaeeledwledvl
>d1fvka2 3.42.1.4.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
aqyedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsek
>d1bed_2 3.42.1.4.2 (1-62,127-181) Disulphide-bond formation facilitator (DSBA) {Vibrio cholerae}
aqfkegehyqvlktpassspvvseffsfycphcntfepiiaqlkqqlpegakfqknhvsf
mgXfavdsmvrrfdkqfqdsgltgvpavvvnnrylvqgqsvksldeyfdlvnylltlk
>d1glqa2 3.42.1.5.3 (1-78) Glutathione S-transferase {Mouse (Mus musculus), class pi}
ppytivyfpvrgrceamrmlladqgqswkeevvtidtwmqgllkptclygqlpkfedgdl
tlyqsnailrhlgrslgl
>d2gsta2 3.42.1.5.5 (1-84) Glutathione S-transferase {Rat (Rattus norvegicus), class mu}
pmilgywnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d1gsea2 3.42.1.5.7 (2-80) Glutathione S-transferase {Human (Homo sapiens), class alpha}
aekpklhyfnargkmestrwllaaagvefeekfiksaedldklrndgylmfqqvpmveid
gmklvqtrailnyiaskyn
>d1ljra2 3.42.1.5.9 (1-79) Glutathione S-transferase {Human (Homo sapiens), class theta}
mglelfldlvsqpsravyifakkngiplelrtvdlvkgqhkskeflqinslgklptlkdg
dfiltessailiylsckyq
>d1pd212 3.42.1.5.10 (1-75) Glutathione S-transferase {Rat (Rattus norvegicus), class sigma}
mpnykllyfnmrgraeiiryifayldikyedhrieqadwpkikptlpfgkipvleveglt
lhqslaiaryltknt
>d2gsq_2 3.42.1.5.11 (1-75) Glutathione S-transferase {Squid (Ommastrephes sloani pacificus), class sigma}
pkytlhyfplmgraelcrfvlaahgeeftdrvvemadwpnlkatmysnampvldidgtkm
sqsmciarhlarefg
>d1duga2 3.42.1.5.12 (1-80) Glutathione S-transferase {Schistosoma japonicum}
spilgywkikglvqptrllleyleekyeehlyerdegdkwrnkkfelglefpnlpyyidg
dvkltqsmaiiryiadkhnm
>d1gnwa2 3.42.1.5.14 (2-85) Glutathione S-transferase {Mouse-ear cress (Arabidopsis thaliana)}
gikvfghpasiatrrvlialheknldfelvhvelkdgehkkepflsrnpfgqvpafedgd
lklfesraitqyiahryenqgtnl
>d1axda2 3.42.1.5.15 (1-80) Glutathione S-transferase {Maize (Zea mays), type I}
apmklygavmswnltrcataleeagsdyeivpinfataehkspehlvrnpfgqvpalqdg
dlylfesraickyaarknkp
>d1aw9_2 3.42.1.5.16 (2-82) Glutathione S-transferase {Maize (Zea mays), type III}
aplklygmplspnvvrvatvlnekgldfeivpvdlttgahkqpdflalnpfgqipalvdg
devlfesrainryiaskyase
>d1a0fa2 3.42.1.5.17 (1-80) Glutathione S-transferase {Escherichia coli}
mklfykpgacslashitlresgkdftlvsvdlmkkrlengddyfavnpkgqvpalllddg
tlltegvaimqyladsvpdr
>d1pmt_2 3.42.1.5.18 (1-80) Glutathione S-transferase {Proteus mirabilis}
mklyytpgscslsphivlretgldfsieridlrtkktesgkdflainpkgqvpvlqldng
diltegvaivqyladlkpdr
>d1f2ea2 3.42.1.5.19 (1-80) Glutathione S-transferase {Sphingomonas paucimobilis}
mklfispgacslaphialretgadfeavkvdlavrkteagedfltvnpsgkvpaltldsg
etltenpaillyiadqnpas
>d2trcp_ 3.42.1.6.1 Phosducin {Rat (Rattus norvegicus)}
egqathtgpkgvindwrkfklesedgdsippskkeilrqmsspqsrddkdskerxsrkxs
iqeyelihqdkedegclrkyrrqcxqdxhqklsfgprygfvyeletgeqfletiekeqkv
ttivvniyedgvrgcdalnssleclaaeypxvkfckirasntgagdrfssdvlptllvyk
ggelisnfisvaeqfaedffaadvesflneygllper
>d1qgva_ 3.42.1.7.1 spliceosomal protein U5-15Kd {Human (Homo sapiens)}
symlphlhngwqvdqailseedrvvvirfghdwdptcmkmdevlysiaekvknfaviylv
ditevpdfnkmyelydpctvmfffrnkhimidlgtgnnnkinwamedkqemvdiietvyr
garkgrglvvspkdyst
>d1gp1a_ 3.42.1.8.1 Glutathione peroxidase {Bovine (Bos taurus)}
rtvyafsarplaggepfnlsslrgkvllienvaslxgttvrdytqmndlqrrlgprglvv
lgfpcnqfghqenakneeilnclkyvrpgggfepnfmlfekcevngekahplfaflrevl
ptpsddatalmtdpkfitwspvcrndvswnfekflvgpdgvpvrrysrrfltidiepdie
tllsq
>d1qk8a_ 3.42.1.8.2 Tryparedoxin I {Crithidia fasciculata}
gldkylpgieklrrgdgevevkslagklvffyfsaswcppcrgftpqliefydkfheskn
fevvfctwdeeedgfagyfakmpwlavpfaqseavqklskhfnvesiptligvdadsgdv
vttraratlvkdpegeqfpwkda
>d1qq2a_ 3.42.1.8.3 Thioredoxin peroxidase 2 (2-cys peroxiredoxin) {Norvey rat (Rattus norvegicus)}
sgnakighpapsfkatavmpdgqfkdislsdykgkyvvfffypldftfvcpteiiafsdr
aeefkklncqvigasvdshfshlawintpkkqgglgpmniplvsdpkrtiaqdygvlkad
egisfrglfiiddkgilrqitindlpvgrsvdeilrlvqafqftdkhgevcpa
>d1prxa_ 3.42.1.8.4 HorF6 peroxidase {Human (Homo sapiens)}
lllgdvapnfeanttvgrirfhdflgdswgilfshprdftpvxttelgraaklapefakr
nvklialsidsvedhlawskdinaynseepteklpfpiiddrnrelaillgmldpaekde
kgmpvtarvvfvfgpdkklklsilypattgrnfdeilrvvislqltaekrvatpvdwkdg
dsvmvlptipeeeakklfpkgvftkelpsgkkylrytpqp
>d1foha3 3.42.1.8.5 (462-662) Phenol hydroxylase, C-terminal domain {Soil-living yeast (Trichosporon cutaneum)}
nlvtdkksskqelakncvvgtrfksqpvvrhseglwmhfgdrlvtdgrfriivfagkatd
atqmsrikkfsayldsensvislytpkvsdrnsridvitihschrddiemhdfpapalhp
kwqydfiyadcdswhhphpksyqawgvdetkgavvvvrpdgytslvtdlegtaeidryfs
gilvepkeksgaqteadwtks
>d1trka3 3.43.1.1.1 (535-680) Transketolase {Baker's yeast (Saccharomyces cerevisiae)}
egssiesaskggyvlqdvanpdiilvatgsevslsveaaktlaaknikarvvslpdfftf
dkqpleyrlsvlpdnvpimsvevlattcwgkyahqsfgidrfgasgkapevfkffgftpe
gvaeraqktiafykgdklisplkkaf
>d1qs0b2 3.43.1.2.2 (206-339) 2-oxoisovalerate dehydrogenase E1b {Pseudomonas putida}
yytvpldkaaitrpgndvsvltygttvyvaqvaaeesgvdaevidlrslwpldldtives
vkktgrcvvvheatrtcgfgaelvslvqehcfhhleapiervtgwdtpyphaqewayfpg
psrvgaalkkvxev
>d1b0pa3 3.43.1.3.1 (259-415) Pyruvate-ferredoxin oxidoreductase, PFOR, domain II {Desulfovibrio africanus}
klfdyvgapdaervivsmgsscetieevinhlaakgekiglikvrlyrpfvseaffaalp
asakvitvldrtkepgapgdplyldvcsafvergeampkilagryglgskefspamvksv
ydnmsgakknhftvgieddvtgtslpvdnafadttpk
>d1a49a3 3.44.1.1.2 (396-530) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1pkla3 3.44.1.1.3 (358-498) Pyruvate kinase, C-terminal domain {Leishmania mexicana}
neyvffnsikklqhipmsadeavcssavnsvyetkakamvvlsntgrsarlvakyrpncp
ivcvttrlqtcrqlnitqgvesvffdadklghdegkehrvaagvefakskgyvqtgdycv
vihadhkvkgyanqtrillve
>d1a3wa3 3.44.1.1.4 (367-500) Pyruvate kinase, C-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
dmrnctpkptsttetvaasavaavfeqkakaiivlstsgttprlvskyrpncpiilvtrc
praarfshlyrgvfpfvfekepvsdwtddvearinfgiekakefgilkkgdtyvsiqgfk
agaghsntlqvstv
>d1e0ta3 3.44.1.1.5 (354-470) Pyruvate kinase, C-terminal domain {Escherichia coli}
iteavcrgavetaekldaplivvatqggksaravrkyfpdatilalttnektahqlvlsk
gvvpqlvkeitstddfyrlgkelalqsglahkgdvvvmvsgalvpsgttntasvhvl
>d1lam_1 3.45.1.1.1 (1-159) Leucine aminopeptidase, N-terminal domain {Bovine (Bos taurus)}
tkglvlgiyskekeedepqftsagenfnklvsgklreilnisgpplkagktrtfyglhed
fpsvvvvglgkktagideqenwhegkeniraavaagcrqiqdleipsvevdpcgdaqaaa
egavlglyeyddlkqkrkvvvsaklhgsedqeawqrgvl
>d1kmma1 3.46.1.1.1 (326-424) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Escherichia coli}
dpvvdiylvasgadtqsaamalaerlrdelpgvklmtnhgggnfkkqfaradkwgarvav
vlgesevangtavvkdlrsgeqtavaqdsvaahlrtllg
>d1adja1 3.46.1.1.2 (326-421) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Thermus thermophilus}
ekgpdlyliplteeavaeafylaealrprlraeyalaprkpakgleealkrgaafagflg
edelragevtlkrlatgeqvrlsreevpgyllqalg
>d1atia1 3.46.1.1.3 (395-505) Glycyl-tRNA synthetase (GlyRS), C-terminal domain {Thermus thermophilus}
qlapikvaviplvknrpeiteyakrlkarllalglgrvlyedtgnigkayrrhdevgtpf
avtvdydtigqskdgttrlkdtvtvrdrdtmeqirlhvdelegflrerlrw
>d1qf6a1 3.46.1.1.4 (533-642) Threonyl-tRNA synthetase (ThrRS), C-terminal domain {Escherichia coli}
fptwlapvqvvimnitdsqseyvneltqklsnagirvkadlrnekigfkirehtlrrvpy
mlvcgdkevesgkvavrtrrgkdlgsmdvnevieklqqeirsrslkqlee
>d1diob_ 3.46.2.1.1 Diol dehydratase, beta subunit {Klebsiella oxytoca}
gfltevgearqgtqqdeviiavgpafglaqtvnivgiphksilreviagieeegikarvi
rcfkssdvafvavegnrlsgsgisigiqskgttvihqqglpplsnlelfpqaplltlety
rqigknaaryakrespqpvptlndqmarpkyqaksailhiketkyvvtgknpqelrval
>d1b78a_ 3.46.3.1.1 XTP pyrophosphatase {Methanococcus jannaschii}
kiyfatgnpnkikeaniilkdlkdveieqikisypeiqgtleevaefgakwvynilkkpv
ivedsgffvealngfpgtyskfvqetignegilkllegkdnrnayfktvigycdengvrl
fkgivkgrvseeirskgygfaydsifipeeeertfaemtteeksqishrkkafeefkkfl
ldri
>d1ex2a_ 3.46.3.2.1 Maf protein {Bacillus subtilis}
mtkplilasqsprrkelldllqlpysiivseveeklnrnfspeenvqwlakqkakavadl
hphaivigadtmvcldgeclgkpqdqeeaasmlrrlsgrshsvitavsiqaenhsetfyd
ktevafwslseeeiwtyietkepmdkagaygiqgrgalfvkkidgdyysvmglpisktmr
alrhf
>d1ckqa_ 3.47.1.1.1 Restriction endonuclease EcoRI {Escherichia coli}
sqgvigifgdyakahdlavgevsklvkkalsneypqlsfryrdsikkteinealkkidpd
lggtlfvsnssikpdggivevkddygewrvvlvaeakhqgkdiinirngllvgkrgdqdl
maagnaiershkniseianfmlseshfpyvlflegsnfltenisitrpdgrvvnleynsg
ilnrldrltaanygmpinsnlcinkfvnhkdksimlqaasiytqgdgrewdskimfeimf
disttslrvlgrdlfeqltsk
>d1eona_ 3.47.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgrk
>d1bam__ 3.47.1.3.1 Restriction endonuclease BamHI {Bacillus amyloliquefaciens}
mevekefitdeakellskdkliqqaynevktsicspiwpatsktftinntekncngvvpi
kelcytlledtynwyrekpldilklekkkggpidvykefienselkrvgmefetgnissa
hrsmnklllglkhgeidlaiilmpikqlayyltdrvtnfeelepyfeltegqpfifigfn
aeaynsnvplipkgsdgmskrsikkwkdkvenk
>d1dmua_ 3.47.1.4.1 Restriction endonuclease BglI {Bacillus subtilis (synonym: Bacillus globigii)}
mynlhrekifmsynqnkqylednpeiqekielyglnllnevisdneeeiradyneanflh
pfwmnyppldrgkmpkgdqipwievgekavgskltrlvsqreditvreiglptgpderyl
ltsptiysltngftdsimmfvdiksvgprdsdydlvlspnqvsgngdwaqleggiqnnqq
tiqgprssqiflptipplyilsdgtiapvvhlfikpiyamrsltkgdtgqslykiklasv
pnglglfcnpgyafdsaykflfrpgkddrtksllqkrvrvdlrvldkigprvmtidmdk
>d1dfma_ 3.47.1.5.1 Restriction endonuclease BglII {Bacillus subtilis (synonym: Bacillus globigii)}
kiditdynhadeilnpqlwkeieetllkxplhvkasdqaskvgslifdpvgtnqyikdel
vpkhwknnipipkrfdflgtdidfgkrdtlvevqfsnypfllnntvrselfhksnxdide
egxkvaiiitkghxfpasnsslyyeqaqnqlnslaeynvfdvpirlvgliedfetdidiv
sttyadkrysrtitkrdtvkgkvidtntpntrrrkrgtivty
>d3pvia_ 3.47.1.6.1 Restriction endonuclease PvuII {Proteus vulgaris}
shpdlnkllelwphiqeyqdlalkhgindifqgnggkllqvllitgltvlpgregndavd
nagqeyelksinidltkgfsthhhmnpviiakyrqvpwifaiyrgiaieaiyrlepkdle
fyydkwerkwysdghkdinnpkipvkyvmehgtkiy
>d1cfr__ 3.47.1.7.1 Restriction endonuclease Cfr10I {Citrobacter freundii}
mdiisksgegnkytinsaiafvayashidinttefskvlsglrdfindeairlggkisdg
sfnkcngdwyewligiraiefflesetnfivvkmpnatsfdvmsiyksclsefiydlrsk
lslnnvnlitsnpdfsiidirgrreelksmlkdisfsnislstiseidnlyknfidyael
ehiksflsvkttfrpdrrlqlahegslmkalythlqtrtwtinptgiryyaaatsignad
viglktvathsitdvkslpqsavdeifkinsvldvdsclshil
>d1d02a_ 3.47.1.8.1 Restriction endonuclease MunI {Eubacteria (Mycoplasma unidentified)}
lsgrlnwqalaglkasgaeqnlynvfnavfegtkyvlyekpkhlknlyaqvvlpddvike
ifnplidlsttqwgvspafaientethkilfgeikrqdgwvegkdpsagrgnahersckl
ftpgllkayrtiggindeeilpfwvvfegditrdpkrvreitfwydhyqdnyfmwrpnes
geklvqhfneklkkyld
>d2foka4 3.47.1.9.1 (387-579) Restriction endonuclease FokI, C-terminal (catalytic) domain {Flavobacterium okeanokoites}
kseleekkselrhklkyvpheyielieiarnstqdrilemkvmeffmkvygyrgkhlggs
rkpdgaiytvgspidygvivdtkaysggynlpigqademqryveenqtrnkhinpnewwk
vypssvtefkflfvsghfkgnykaqltrlnhitncngavlsveelliggemikagtltle
evrrkfnngeinf
>d1avqa_ 3.47.1.10.1 lambda exonuclease {Bacteriophage lambda}
shmtpdiilqrtgidvraveqgddawhklrlgvitasevhnviakprsgkkwpdmkmsyf
htllaevctgvapevnakalawgkqyendartlfeftsgvnvtespiiyrdesmrtacsp
dglcsdgnglelkcpftsrdfmkfrlggfeaiksaymaqvqysmwvtrknawyfanydpr
mkreglhyvvierdekymasfdeivpefiekmdealaeigfvfgeqwr
>d1azo__ 3.47.1.11.1 DNA mismatch repair protein MutH from {Escherichia coli}
prpllsppeteeqllaqaqqlsgytlgelaalvglvtpenlkrdkgwigvlleiwlgasa
gskpeqdfaalgvelktipvdslgrplettfvcvapltgnsgvtwetshvrhklkrvlwi
pvegeasiplaqrrvgspllwspneeedrqlredweelxdxivlgqveritarhgeylqi
rpkaanakalteaigargeriltlprgfylkknftsallarhfliq
>d1vsra_ 3.47.1.12.1 Very short patch repair (VSR) endonuclease {Escherichia coli}
aiekrlaslltgqglafrvqdaslpgrpdfvvdeyrcvifthgcfwhhhhcylfkvpatr
tefwlekigknverdrrdisrlqelgwrvlivwecalrgrekltdealterleewicgeg
asaqidtqgihlla
>d1f1za2 3.47.1.13.1 (8-168) TnsA endonuclease, N-terminal domain {Escherichia coli}
fsevqiarrikegrgqghgkdyipwltvqevpssgrshriyshktgrvhhllsdlelavf
lslewessvldireqfpllpsdtrqiaidsgikhpvirgvdqvmstdflvdckdgpfeqf
aiqvkpaaalqdertleklelerrywqqkqipwfiftdkei
>d1a79a1 3.47.2.1.1 (83-179) tRNA splicing endonuclease, C-terminal domain {Methanococcus jannaschii}
erlclkylvykdlrtrgyivktglkygadfrlyerganidkehsvylvkvfpedssflls
eltgfvrvahsvrkklliaivdadgdivyynmtyvkp
>d1dzfa1 3.47.3.1.1 (5-143) Eukaryotic RPB5 N-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
nernisrlwrafrtvkemvkdrgyfitqeevelpledfkakycdsmgrpqrkmmsfqanp
teesiskfpdmgslwvefcdepsvgvktmktfvihiqeknfqtgifvyqnnitpsamklv
psippatietfneaalvvn
>d2rsla_ 3.48.1.1.1 gamma,delta resolvase, large fragment {Escherichia coli}
mrlfgyarvstsqqsldiqvralkdagvkanriftdkasgsssdrkgldllrmkveegdv
ilvkkldrlgrdtadmiqlikefdaqgvsirfiddgistdgemgkmvvtilsavaqaerq
ri
>d1tfr_2 3.48.1.2.1 (12-180) T4 RNase H {Bacteriophage T4}
kegiclidfsqialstalvnfpdkekinlsmvrhlilnsikfnvkkaktlgytkivlcid
naksgywrrdfayyykknrgkareestwdwegyfesshkvidelkaympyivmdidkyea
ddhiavlvkkfsleghkiliissdgdftqlhkypnvkqwspmhkkwvki
>d1bgxt2 3.48.1.2.2 (1-173) 5' to 3' exonuclease domain of DNA polymerase <i>Taq</i> {Thermus aquaticus}
mrgmlplfepkgrvllvdghhlayrtfhalkglttsrgepvqavygfaksllkalkedgd
avivvfdakapsfrheayggykagraptpedfprqlalikelvdllglarlevpgyeadd
vlaslakkaekegyevriltadkdlyqllsdrihvlhpegylitpawlwekyg
>d1xo1a2 3.48.1.2.3 (19-185) T5 5'-exonuclease {Bacteriophage T5}
rrnlmivdgtnlgfrfkhnnskkpfassyvstiqslaksysarttivlgdkgksvfrleh
lpeykgnrdekyaqrteeekaldeqffeylkdafelckttfptftirgveaddmaayivk
lighlydhvwlistdgdwdtlltdkvsrfsfttrreyhlrdmyehhn
>d1a77_2 3.48.1.2.4 (2-208) Flap endonuclease-1 {Methanococcus jannaschii}
gvqfgdfipkniisfedlkgkkvaidgmnalyqfltsirlrdgsplrnrkgeitsayngv
fyktihllenditpiwvfdgeppklkektrkvrremkekaelkmkeaikkedfeeaakya
krvsyltpkmvenckyllslmgipyveapsegeaqasymakkgdvwavvsqdydallyga
prvvrnltttkempelielnevledlr
>d1ekja_ 3.48.2.1.1 beta-carbonic anhydrase {Pea (Pisum sativum)}
easeriktgflhfkkekydknpalygelakgqsppfmvfacsdsrvcpshvldfqpgeaf
vvrnvanlvppydqakyagtgaaieyavlhlkvsnivvighsacggikgllsfpfdgtys
tdfieewvkiglpakakvkaqhgdapfaelcthcekeavnaslgnlltypfvreglvnkt
lalkggyydfvkgsfelwglefglsstfsv
>d1ddza1 3.48.2.1.2 (84-325) beta-carbonic anhydrase {Red alga (Porphyridium purpureum)}
vmsdlekkfieleaklvaqpagqampgksnifanneawrqemlkqdpeffnrlangqspe
ylwigcadsrvpanqlldlpagevfvhrnianqcihsdisflsvlqyavqylkvkhilvc
ghygcggakaalgdsrlglidnwlrhirdvrrmnakyldkckdgdeelnrlielnvleqv
hnvcatsivqdawdagqeltvqgvvygvgdgklrdlgvvvnssddiskfyrtksdsgalk
ag
>d1pdo__ 3.49.1.1.1 IIA domain of mannose transporter, IIA-Man {Escherichia coli}
tiaivigthgwaaeqllktaemllgeqenvgwidfvpgenaetliekynaqlakldttkg
vlflvdtwggspfnaasrivvdkehyeviagvnipmlvetlmardddpsfdelvalavet
gregvkalk
>d1bupa1 3.50.1.1.1 (4-188) Heat shock protein 70kDa, ATPase fragment {Bovine (Bos taurus)}
gpavgidlgstyscvgvfqhgkveiiandqgnrttpsyvaftdterligdaaknqvamnp
tntvfdakrligrrfddavvqsdmkhwpfmvvndagrpkvqveykgetksfypeevssmv
ltkmkeiaeaylgktvtnavvtvpayfndsqrqatkdagtiaglnvlriineptaaaiay
gldkk
>d1bupa2 3.50.1.1.1 (189-381) Heat shock protein 70kDa, ATPase fragment {Bovine (Bos taurus)}
vgaernvlifdlgggtfdvsiltiedgifevkstagdthlggedfdnrmvnhfiaefkrk
hkkdisenkravrrlrtacerakrtlssstqasieidslyegidfytsitrarfeelnad
lfrgtldpvekalrdakldksqihdivlvggstripkiqkllqdffngkelnksinpdea
vaygaavqaails
>d1yaga1 3.50.1.1.7 (4-146) Actin {Baker's yeast (Saccharomyces cerevisiae)}
evaalvidngsgmckagfagddapravfpsivgrprhqgimvgmgqkdsyvgdeaqskrg
iltlrypiehgivtnwddmekiwhhtfynelrvapeehpvllteapmnpksnrekmtqim
fetfnvpafyvsiqavlslyssg
>d1yaga2 3.50.1.1.7 (147-375) Actin {Baker's yeast (Saccharomyces cerevisiae)}
rttgivldsgdgvthvvpiyagfslphailridlagrdltdylmkilsergysfsttaer
eivrdikeklcyvaldfeqemqtaaqsssieksyelpdgqvitignerfrapealfhpsv
lglesagidqttynsimkcdvdvrkelygnivmsggttmfpgiaermqkeitalapssmk
vkiiapperkysvwiggsilaslttfqqmwiskqeydesgpsivhhkcf
>d1czan1 3.50.1.2.2 (16-222) Mammalian type I hexokinase {Human (Homo sapiens)}
ddqvkkidkylyamrlsdetlidimtrfrkemknglsrdfnptatvkmlptfvrsipdgs
ekgdfialdlggssfrilrvqvnheknqnvhmesevydtpenivhgsgsqlfdhvaeclg
dfmekrkikdkklpvgftfsfpcqqskideailitwtkrfkasgvegadvvkllnkaikk
rgdydanivavvndtvgtmmtcgyddq
>d1czan2 3.50.1.2.2 (223-465) Mammalian type I hexokinase {Human (Homo sapiens)}
hcevgliigtgtnacymeelrhidlvegdegrmcintewgafgddgsledirtefdraid
ayslnpgkqlfekmvsgmylgelvrlilvkmakegllfegritpelltrgkfntsdvsai
eknkeglhnakeiltrlgvepsdddcvsvqhvctivsfrsanlvaatlgailnrlrdnkg
tprlrttvgvdgslykthpqysrrfhktlrrlvpdsdvrfllsesgsgkgaamvtavayr
lae
>d1bu6o1 3.50.1.3.1 (3-253) Glycerol kinase {Escherichia coli}
kkyivaldqgttssravvmdhdaniisvsqrefeqiypkpgwvehdpmeiwatqsstlve
vltkadissdqiaaigitnqrettivweketgkpiynaivwqcrrtaeicehlkrdgled
yirsntglvidpyfsgtkvkwildhvegsrerarrgellfgtvdtwliwkmtqgrvhvtd
ytnasrtmlfnihtldwddkmlevldipremlpevrrssevygqtniggkggtripisgi
agdqqaalfgq
>d1bu6o2 3.50.1.3.1 (254-499) Glycerol kinase {Escherichia coli}
lcvkegmakntygtgcfmlmntgekavksengllttiacgptgevnyalegavfmagasi
qwlrdemklindaydseyfatkvqntngvyvvpaftglgapywdpyargaifgltrgvna
nhiiratlesiayqtrdvleamqadsgirlhalrvdggavannflmqfqsdilgtrverp
evrevtalgaaylaglavgfwqnldelqekavierefrpgietternyryagwkkavkra
maweeh
>d1chma1 3.50.2.1.1 (2-156) Creatinase, N-terminal domain {Pseudomonas putida}
qmpktlrirngdkvrstfsaqeyanrqarlrahlaaenidaaiftsyhninyysdflycs
fgrpyalvvteddvisisanidggqpwrrtvgtdnivytdwqrdnyfaaiqqalpkarri
giehdhlnlqnrdklaarypdaelvdvaaacmrmr
>d2rn2__ 3.50.3.1.1 RNase H {Escherichia coli}
mlkqveiftdgsclgnpgpggygailryrgrektfsagytrttnnrmelmaaivalealk
ehcevilstdsqyvrqgitqwihnwkkrgwktadkkpvknvdlwqrldaalgqhqikwew
vkghaghpenercdelaraaamnptledtgyqvev
>d1vrta1 3.50.3.1.4 (430-539) HIV RNase H (Domain of reverse transcriptase) {Human immunodeficiency virus, type 1}
ekepivgaetfyvdgaanretklgkagyvtnrgrqkvvtltdttnqktelqaiylalqds
glevnivtdsqyalgiiqaqpdqseselvnqiieqlikkekvylawvpah
>d1cxqa_ 3.50.3.2.1 ASV integrase, catalytic domain {Avian sarcoma virus, Rous sarcoma virus, Schmidt-Ruppin strain B}
grglgplqiwqtdftleprmaprswlavtvdtassaivvtqhgrvtsvaaqhhwataiav
lgrpkaiktdngscftskstrewlarwgiahttgipgnsqgqamveranrllkdkirvla
egdgfmkriptskqgellakamyalnh
>d1b9da_ 3.50.3.2.2 HIV-1 integrase, catalytic domain {Human immunodeficiency virus, type 1}
spgiwqldcthlegkvilvavhvasgyieaevipaetgqetayfllklagrwpvktvhtd
ngsnftsttvkaacwwagikqefgipynpqsqgviesmnkelkkiigqvrdqaehlktav
qmavfihnkkrkggiggysagerivdiiatdiqt
>d1bco_2 3.50.3.3.1 (258-480) mu transposase, core domain {Bacteriophage mu}
ehldamqwingdgylhnvfvrwfngdvirpktwfwqdvktrkilgwrcdvsenidsirls
fmdvvtrygipedfhitidntrgaankwltggapnryrfkvkeddpkglfllmgakmhwt
svvagkgwgqakpverafgvggleeyvdkhpalagaytgpnpqakpdnygdravdaelfl
ktlaegvamfnartgretemcggklsfddvfereyartivrkp
>d1b7ea_ 3.50.3.4.1 Transposase inhibitor (Tn5 transposase) {Escherichia coli}
saeairkagamqtvklaqefpellaiedttslsyrhqvaeelgklgsiqdksrgwwvhsv
llleattfrtvgllhqewwmrpddpadadekesgkwlaaaatsrlrmgsmmsnviavcdr
eadihaylqdklahnerfvvrskhprkdvesglylydhlknqpelggyqisipqkgvvdk
rgkrknrparkaslslrsgritlkqgnitlnavlaeeinppkgetplkwllltsepvesl
aqalrvidiythrwrieefhkawktgagaerqrmeepdnlermvsilsfvavrllqlres
ftlpqalraqgllkeaehvesqsaetvltpdecqllgyldkgkrkrkekgslqwaymaia
rlggfmdskrtgiaswgalwegwealqskldgflaakdlmaq
>d1kfsa1 3.50.3.5.1 (324-518) Exonuclease domain of DNA polymerase {Escherichia coli}
misydnyvtildeetlkawiaklekapvfafdtetdsldnisanlvglsfaiepgvaayi
pvahdyldapdqisreralellkplledekalkvgqnlkydrgilanygielrgiafdtm
lesyilnsvagrhdmdslaerwlkhktitfeeiagkgknqltfnqialeeagryaaedad
vtlqlhlkmwpdlqk
>d1qtma1 3.50.3.5.2 (293-450) Exonuclease domain of DNA polymerase {Thermus aquaticus}
aleeapwpppegafvgfvlsrkepmwadllalaaarggrvhrapepykalrdlkeargll
akdlsvlalreglglppgddpmllaylldpsnttpegvarryggewteeageraalserl
fanlwgrlegeerllwlyreverplsavlahmeatgvr
>d1xwl_1 3.50.3.5.3 (297-492) Exonuclease domain of DNA polymerase {Bacillus stearothermophilus, newly identified strain as yet unnamed}
akmaftladrvteemladkaalvvevveenyhdapivgiavvnehgrfflrpetaladpq
fvawlgdetkkksmfdskraavalkwkgielcgvsfdlllaaylldpaqgvddvaaaakm
kqyeavrpdeavygkgakravpdepvlaehlvrkaaaiwelerpfldelrrneqdrllve
leqplssilaemefag
>d1t7pa1 3.50.3.6.1 (1-210) T7-like DNA polymerase {Bacteriophage T7}
mivsdieanallesvtkfhcgviydystaeyvsyrpsdfgayldaleaevargglivfhn
ghkydvpaltklaklqlnrefhlprencidtlvlsrlihsnlkdtdmgllrsgklpgale
awgyrlgemkgeykddfkrmleeqgeeyvdgmewwnfneemmdynvqdvvvtkallekll
sdkhyfppeidftdvgyttfwses
>d1noya_ 3.50.3.6.2 T4-like DNA polymerase {Bacteriophage T4}
defyisietvgnniveryidengkertreveylptmfrhckeeskykdiygkncapqkfp
smkdardwmkrmediglealgmndfklayisdtygseivydrkfvrvancdievtgdkfp
dpmkaeyeidaithydsiddrfyvfdllnsmygsvskwdaklaakldceggdevpqeild
rviympfdnerdmlmeyinlweqkrpaiftgwniegfdvpyimnrvkmilgersmkrfsp
igrvkskllqnmygskeiysidgvsildyldlykkfaftnlpsfslesvaqhetkkgklp
ydgpinklretnhqryisyniidvesvqaidkirgfidlvlsmsyyakmpfsgvmspikt
wdaiifnslkge
>d1tgoa1 3.50.3.6.4 (1-347) T4-like DNA polymerase {Thermococcus gorgonarius}
mildtdyitedgkpvirifkkengefkidydrnfepyiyallkddsaiedvkkitaerhg
ttvrvvraekvkkkflgrpievwklyfthpqdvpairdkikehpavvdiyeydipfakry
lidkglipmegdeelkmlafdietlyhegeefaegpilmisyadeegarvitwknidlpy
vdvvstekemikrflkvvkekdpdvlityngdnfdfaylkkrseklgvkfilgregsepk
iqrmgdrfavevkgrihfdlypvirrtinlptytleavyeaifgqpkekvyaeeiaqawe
tgeglervarysmedakvtyelgkeffpmeaqlsrlvgqslwdvsrs
>d1hjra_ 3.50.3.7.1 RuvC resolvase {Escherichia coli}
aiilgidpgsrvtgygvirqvgrqlsylgsgcirtkvddlpsrlkliyagvteiitqfqp
dyfaieqvfmaknadsalklgqargvaivaavnqelpvfeyaarqvkqtvvgigsaeksq
vqhmvrtllklpanpqadaadalaiaithchvsqnamq
>d1dt9a1 3.50.4.1.1 (143-276) Middle domain of eukaryotic peptide chain release factor subunit 1, ERF1 {Human (Homo sapiens)}
dskfgfividgsgalfgtlqgntrevlhkftvdlpkkhgrggqsalrfarlrmekrhnyv
rkvaetavqlfisgdkvnvaglvlagsadfktelsqsdmfdqrlqskvlklvdisyggen
gfnqaielstevls
>d1sfe_2 3.50.5.1.1 (12-92) Ada DNA repair protein {Escherichia coli}
lavryaladcelgrclvaesergicaillgdddatliselqqmfpaadnapadlmfqqhv
reviaslnqrdtpltlpldir
>d1qnta2 3.50.5.1.2 (6-91) O6-alkylguanine-DNA alkyltransferase {Human (Homo sapiens)}
emkrttldsplgklelsgceqglheikllgkgtsaadavevpapaavlggpeplmqctaw
lnayfhqpeaieefpvpalhhpvfqq
>d1mgta2 3.50.5.1.3 (1-88) O6-alkylguanine-DNA alkyltransferase {Pyrococcus kodakaraensis}
mlsvekfrvgervvwigvifsgrvqgiafafdrgtlmkrihdlaehlgkrgvsisldvqp
sdypekvfkvligeldnasflrelsfeg
>d1cfza_ 3.51.1.1.1 Hydrogenase maturating endopeptidase HybD {Escherichia coli}
mrilvlgvgnilltdeaigvrivealeqryilpdyveildggtagmellgdmanrdhlii
adaivskknapgtmmilrdeevpalftnkisphqlgladvlsalrftgefpkkltlvgvi
peslephigltptveamiepaleqvlaalresgveaiprsds
>d1b8oa_ 3.51.2.1.2 Purine nucleoside phosphorylase, PNP {Bovine (Bos taurus)}
ngytyedyqdtakwllshteqrpqvavicgsglgglvnkltqaqtfdyseipnfpestvp
ghagrlvfgilngracvmmqgrfhmyegypfwkvtfpvrvfrllgvetlvvtnaagglnp
nfevgdimlirdhinlpgfsgenplrgpneerfgvrfpamsdaydrdmrqkahstwkqmg
eqrelqegtyvmlggpnfetvaecrllrnlgadavgmstvpevivarhcglrvfgfslit
nkvimdyesqgkanheevleagkqaaqkleqfvsllmasi
>d1ecpa_ 3.51.2.1.3 Purine nucleoside phosphorylase, PNP {Escherichia coli}
atphinaemgdfadvvlmpgdplrakyiaetfledarevnnvrgmlgftgtykgrkisvm
ghgmgipscsiytkelitdfgvkkiirvgscgavlphvklrdvvigmgactdskvnrirf
kdhdfaaiadfdmvrnavdaakalgidarvgnlfsadlfyspdgemfdvmekygilgvem
eaagiygvaaefgakaltictvsdhirtheqttaaerqttfndmikialesvllgdk
>d1cb0a_ 3.51.2.1.5 5'-deoxy-5'-methylthioadenosine phosphorylase {Human (Homo sapiens)}
avkigiiggtglddpeilegrtekyvdtpfgkpsdalilgkiknvdcvllarhgrqhtim
pskvnyqaniwalkeegcthvivttacgslreeiqpgdiviidqfidrttmrpqsfydgs
hscargvchipmaepfcpktrevlietakklglrchskgtmvtiegprfssraesfmfrt
wgadvinmttvpevvlakeagicyasiamatdydcwkeheeavsvdrvlktlkenankak
slllttipqigstewsetlhnlknmaqfsvllp
>d2pth__ 3.51.3.1.1 Peptidyl-tRNA hydrolase {Escherichia coli}
tiklivglanpgaeyaatrhnagawfvdllaerlraplreeakffgytsrvtlggedvrl
lvpttfmnlsgkavaamasffrinpdeilvahdeldlppgvakfklggghgghnglkdii
sklgnnpnfhrlrigighpgdknkvvgfvlgkppvseqklideaideaarctemwftdgl
tkatnrlhafkaq
>d1a2za_ 3.51.4.1.1 Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase) {Thermococcus litoralis}
mkkvlitgfepfggdsknpteqiakyfdrkqignamvygrvlpvsvkratielkryleei
kpeivinlglaptysnitveriavniidaripdndgyqpidekieedaplaymatlpvra
itktlrdngipatisysagtylcnyvmfktlhfskiegyplkagfihvpytpdqvvnkff
llgkntpsmcleaeikaielavkvsldylekdrddikipl
>d2ctc__ 3.51.5.1.1 Carboxypeptidase A {Bovine (Bos taurus)}
arstntfnyatyhtldeiydfmdllvaehpqlvsklqigrsyegrpiyvlkfstggsnrp
aiwidlgihsrewitqatgvwfakkftedygqdpsftaildsmdifleivtnpdgfafth
sqnrlwrktrsvtssslcvgvdanrnwdagfgkagassspcsetyhgkyansevevksiv
dfvkdhgnfkaflsihsysqlllypygyttqsipdktelnqvaksavealkslygtsyky
gsiittiyqasggsidwsynqgikysftfelrdtgrygfllpasqiiptaqetwlgvlti
mehtlnn
>d1lam_2 3.51.5.3.1 (160-484) Leucine aminopeptidase, C-terminal domain {Bovine (Bos taurus)}
fasgqnlarrlmetpanemtptkfaeiveenlksasiktdvfirpkswieeqemgsflsv
akgseeppvfleihykgspnasepplvfvgkgitfdsggisikaaanmdlmradmggaat
icsaivsaakldlpinivglaplcenmpsgkankpgdvvrarngktiqvdntdaegrlil
adalcyahtfnpkviinaatltgamdialgsgatgvftnsswlwnklfeasietgdrvwr
mplfehytrqvidcqladvnnigkyrsagactaaaflkefvthpkwahldiagvmtnkde
vpylrkgmagrptrtlieflfrfsq
>d1amp__ 3.51.5.4.1 Aminopeptidase {Aeromonas proteolytica}
mppitqqatvtawlpqvdasqitgtisslesftnrfytttsgaqasdwiasewqalsasl
pnasvkqvshsgynqksvvmtitgseapdewivigghldstigshtneqsvapgadddas
giaavtevirvlsennfqpkrsiafmayaaeevglrgsqdlanqyksegknvvsalqldm
tnykgsaqdvvfitdytdsnftqyltqlmdeylpsltygfdtcgyacsdhaswhnagypa
ampfeskfndynprihttqdtlansdptgshakkftqlglayaiemgsatg
>d1qq9a_ 3.51.5.4.2 Aminopeptidase {Streptomyces griseus}
apdiplanvkahltqlstiaannggnrahgrpgykasvdyvkakldaagytttlqqftsg
gatgynlianwpggdpnkvlmagahldsvssgagindngsgsaavletalavsragyqpd
khlrfawwgaeelgligskfyvnnlpsadrsklagylnfdmigspnpgyfvydddpviek
tfknyfaglnvpteietegdgrsdhapfknvgvpvgglftgagytksaaqaqkwggtagq
afdrcyhsscdslsnindtaldrnsdaaahaiwtlss
>d1cg2a1 3.51.5.4.3 (26-213,327-414) Carboxypeptidase G2, catalytic domain {Pseudomonas strain rs-16}
qkrdnvlfqaatdeqpaviktleklvnietgtgdaegiaaagnfleaelknlgftvtrsk
saglvvgdnivgkikgrggknlllmshmdtvylkgilakapfrvegdkaygpgiaddkgg
navilhtlkllkeygvrdygtitvlfntdeekgsfgsrdliqeeakladyvlsfeptsag
deklslgtXfnageggkklvdkavayykeaggtlgveertgggtdaayaalsgkpviesl
glpgfgyhsdkaeyvdisaiprrlymaarlimdlgag
>d1de4c3 3.51.5.5.1 (122-189,383-608) Transferrin receptor ectodomain, protease-like domain {Human (Homo sapiens)}
lywddlkrklsekldstdftstikllnensyvpreagsqkdenlalyvenqfrefklskv
wrdqhfvkXeikilnifgvikgfvepdhyvvvgaqrdawgpgaaksgvgtalllklaqmf
sdmvlkdgfqpsrsiifaswsagdfgsvgatewlegylsslhlkaftyinldkavlgtsn
fkvsaspllytliektmqnvkhpvtgqflyqdsnwaskvekltldnaafpflaysgipav
sfcfcedtdypylgttmdtykelieripelnkvaraaaevagqfviklthdveln
>d1boub_ 3.51.6.1.1 LigB subunit of an aromatic-ring-opening dioxygenase LigAB {Pseudomonas paucimobilis}
arvttgitsshipalgaaiqtgtsdndywgpvfkgyqpirdwikqpgnmpdvvilvyndh
asafdmniiptfaigcaetfkpadegwgprpvpdvkghpdlawhiaqslildefdmtimn
qmdvdhgctvplsmifgepeewpckvipfpvnvvtypppsgkrcfalgdsiraavesfpe
dlnvhvwgtggmshqlqgpraglinkefdlnfidklisdpeelskmphiqylresgsegv
elvmwlimrgalpekvrdlytfyhipasntalgamilqpeetagtpleprkvmsghsl
>d1di6a_ 3.52.1.1.1 Molybdenumm cofactor biosynthesis protein MogA {Escherichia coli}
atlriglvsisdrassgvyqdkgipaleewltsalttpfeletrlipdeqaiieqtlcel
vdemschlvlttggtgparrdvtpdatlavadrempgfgeqmrqislhfvptailsrqvg
virkqalilnlpgqpksiketlegvkdaegnvvvhgifasvpyciqllegpyvetapevv
aafrpksarr
>d1bgva2 3.53.1.1.1 (1-194) Glutamate dehydrogenase {Clostridium symbiosum}
skyvdrviaevekkyadepefvqtveevlsslgpvvdahpeyeevallermvipervief
rvpweddngkvhvntgyrvqfngaigpykgglrfapsvnlsimkflgfeqafkdslttlp
mggakggsdfdpngksdrevmrfcqafmtelyrhigpdidvpagdlgvgareigymygqy
rkivggfyngvltg
>d1gtma2 3.53.1.1.2 (3-180) Glutamate dehydrogenase {Pyrococcus furiosus}
adpyeivikqleraaqymeiseealeflkrpqrivevtipvemddgsvkvftgfrvqhnw
argptkggirwhpeetlstvkalaawmtwktavmdlpygggkggiivdpkklsdrekerl
argyiraiydvispyedipapdvytnpqimawmmdeyetisrrktpafgiitgkplsi
>d1leha2 3.53.1.1.6 (1-134) Leucine dehydrogenase {Bacillus sphaericus}
meifkymekydyeqlvfcqdeasglkaviaihdttlgpalggarmwtynaeeeaiedalr
largmtyknaaaglnlgggktviigdpfadknedmfralgrfiqglngryitaedvgttv
ddmdlihqetdyvt
>d1bw9a2 3.53.1.1.7 (1-148) Phenylalanine dehydrogenase {Rhodococcus M4}
sidsalnwdgemtvtrfdsmtgahfvirldstqlgpaaggtraaqysnladaltdagkla
gamtlkmavsnlpmgggksvialpaprhsidpstwarilrihaenidklsgnywtgpdvn
tnsadmdtlndttefvfgrslerggags
>d1a4ia2 3.53.1.2.1 (2-126) Tetrahydrofolate dehydrogenase/cyclohydrolase {Human (Homo sapiens)}
apaeilngkeisaqirarlknqvtqlkeqvpgftprlailqvgnrddsnlyinvklkaae
eigikathiklprtttesevmkyitslnedstvhgflvqlpldsensinteevinaiape
kdvdg
>d1b0aa2 3.53.1.2.2 (2-122) Tetrahydrofolate dehydrogenase/cyclohydrolase {Escherichia coli}
aakiidgktiaqqvrsevaqkvqariaaglrapglavvlvgsnpasqiyvaskrkaceev
gfvsrsydlpettseaellelidtlnadntidgilvqlplpagidnvkvlerihpdkdvd
g
>d1do8a2 3.53.1.3.1 (21-279) Mitochondrial NAD(P)-dependenent malic enzyme {Human (Homo sapiens)}
ikekgkplxlnprtnkgxaftlqerqxlglqgllppkietqdiqalrfhrnlkkxtsple
kyiyixgiqerneklfyrilqddieslxpivytptvglacsqyghifrrpkglfisisdr
ghvrsivdnwpenhvkavvvtdgerilglgdlgvygxgipvgklclytacagirpdrclp
vcidvgtdniallkdpfyxglyqkrdrtqqyddlidefxkaitdrygrntliqfedfgnh
nafrflrkyrekyctfndd
>d2uaga2 3.54.1.1.1 (298-437) C-terminal domain of MurD (UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase) {Escherichia coli}
glphrfevvlehngvrwindskatnvgsteaalnglhvdgtlhlllggdgksadfsplar
ylngdnvrlycfgrdgaqlaalrpevaeqtetmeqamrllaprvqpgdmvllspacasld
qfknfeqrgnefarlakelg
>d1fgs_1 3.54.1.2.1 (297-425) Folylpolyglutamate synthetase, C-terminal domain {Lactobacillus casei}
wparlekisdtplividgahnpdginglitalkqlfsqpitviagiladkdyaamadrlt
aafstvylvpvpgtpralpeagyealhegrlkdswqealaaslndvpdqpivitgslyla
savrqtllg
>d1qhfa_ 3.55.1.1.1 Phosphoglycerate mutase {Baker's yeast (Saccharomyces cerevisiae)}
pklvlvrhgqsewneknlftgwvdvklsakgqqeaaragellkekkvypdvlytsklsra
iqtanialekadrlwipvnrswrlnerhygdlqgkdkaetlkkfgeekfntyrrsfdvpp
ppidasspfsqkgderykyvdpnvlpeteslalvidrllpywqdviakdllsgktvmiaa
hgnslrglvkhlegisdadiaklniptgiplvfeldenlkpskpsyyldpeaaaagaaav
>d2hpaa_ 3.55.1.2.2 Acid phosphatase {Human (Homo sapiens)}
kelkfvtlvfrhgdrspidtfptdpikesswpqgfgqltqlgmeqhyelgeyirkryrkf
lnesykheqvyirstdvdrtlmsamtnlaalfppegvsiwnpillwqpipvhtvplsedq
llylpfrncprfqelesetlkseefqkrlhpykdfiatlgklsglhgqdlfgiwskvydp
lycesvhnftlpswatedtmtklrelselsllslygihkqkeksrlqggvlvneilnhmk
ratqipsykklimysahdttvsglqmaldvyngllppyaschltelyfekgeyfvemyyr
netqhepyplmlpgcspscplerfaelvgpvipqdwstecmt
>d1ihp__ 3.55.1.3.1 Phytase (myo-inositol-hexakisphosphate-3-phosphohydrolase) {Aspergillus ficuum}
scdtvdqgyqcfsetshlwgqyapffslanesvispevpagcrvtfaqvlsrhgaryptd
skgkkysalieeiqqnattfdgkyaflktynyslgaddltpfgeqelvnsgikfyqryes
ltrnivpfirssgssrviasgkkfiegfqstklkdpraqpgqsspkidvviseasssnnt
ldpgtctvfedseladtveanftatfvpsirqrlendlsgvtltdtevtylmdmcsfdti
ststvdtklspfcdlfthdewinydylqslkkyyghgagnplgptqgvgyaneliarlth
spvhddtssnhtldsspatfplnstlyadfshdngiisilfalglyngtkplstttveni
tqtdgfssawtvpfasrlyvemmqcqaeqeplvrvlvndrvvplhgcpvdalgrctrdsf
vrglsfarsggdwaecfa
>d1bif_2 3.55.1.4.1 (250-468) 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, phosphatase domain {Rat (Rattus norvegicus)}
siylcrhgeselnlkgriggdpglsprgrefskhlaqfisdqnikdlkvftsqmkrtiqt
aealsvpyeqfkvlneidagvceemtyeeiqdhyplefalrdqdkyryrypkgesyedlv
qrlepvimelerqenvlvichqavmrcllayfldkaaeelpylkcplhtvlkltpvaygc
kvesiflnvaavnthrdrpqnvdisrpseealvtvpahq
>d1nula_ 3.56.1.1.1 Xantine-guanine PRTase (XPRTase) {Escherichia coli}
ekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvciss
ydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrplv
ddyvvdipqdtwieqpwdmgvvfvppisgr
>d1hgxa_ 3.56.1.1.2 Hypoxantine-guanine-xanthine PRTase {Tritrichomonas foetus}
mddlervlynqddiqkrirelaaeltefyedknpvmicvltgavffytdllkhldfqlep
dyiicssysgtkstgnltiskdlktniegrhvlvvediidtgltmyqllnnlqmrkpasl
kvctlcdkdigkkaydvpidycgfvvenryiigygfdfhnkyrnlpvigilke
>d1qk3a_ 3.56.1.1.3 Hypoxantine-guanine-xanthine PRTase {Toxoplasma gondii}
maskpiedygkgkgriepmyipdntfynaddflvpphckpyidkillpgglvkdrvekla
ydihrtyfgeelhiicilkgsrgffnllidylatiqkysgressvppffehyvrlksyqn
dnstgqltvlsddlsifrdkhvlivedivdtgftltefgerlkavgpksmriatlvekrt
drsnslkgdfvgfsiedvwivgccydfnemfrdfdhvavlsdaarkkf
>d1ecfa1 3.56.1.1.5 (250-492) Glutamine PRPP amidotransferase, C-terminal domain {Escherichia coli}
npclfeyvyfarpdsfidkisvysarvnmgtklgekiarewedldidvvipipetscdia
leiarilgkpyrqgfvknryvgrtfimpgqqlrrksvrrklnanraefrdknvllvddsi
vrgttseqiiemareagakkvylasaapeirfpnvygidmpsateliahgrevdeirqii
gadglifqdlndlidavraenpdiqqfecsvfngvyvtkdvdqgyldfldtlrnddakav
qrq
>d1tc1a_ 3.56.1.1.8 Hypoxanthine PRTase {Trypanosoma cruzi}
yefaekilfteeeirtrikevakriaddykgkglrpyvnplvlisvlkgsfmftadlcra
lcdfnvpvrmeficvssygegltssgqvrmlldtrhsieghhvlivedivdtaltlnyly
hmyftrrpaslktvvlldkregrrvpfsadyvvanipnafvigygldyddtyrelrdivv
lrpe
>d1qb7a_ 3.56.1.1.9 Adenine PRTase {Leishmania donovani}
pfkevspnsfllddshalsqllkksyrwyspvfsprnvprfadvssitespetlkairdf
lvqryramspapthilgfdargflfgpmiaveleipfvlmrkadknagllirsepyekey
keaapevmtirygsigkgsrvvliddvlatggtalsglqlveasdavvvemvsilsipfl
kaaekihstansrykdikfisllsddalteencgdsknytgprvlscgdvlaehph
>d1oroa_ 3.56.1.1.11 Orotate PRTase {Escherichia coli}
mkpyqrqfiefalskqvlkfgeftlksgrkspyffnaglfntgrdlallgrfyaealvds
giefdllfgpaykgipiatttavalaehhdldlpycfnrkeakdhgeggnlvgsalqgrv
mlvddvitagtairesmeiiqangatlagvlisldrqergrgeisaiqeverdynckvis
iitlkdliayleekpemaehlaavkayreefgv
>d1a3c__ 3.56.1.1.12 Uracil PRTase {Bacillus subtilis}
qkavildeqairraltriahemiernkgmnncilvgiktrgiylakrlaerieqiegnpv
tvgeiditlyrddlskktsndeplvkgadipvditdqkvilvddvlytgrtvragmdalv
dvgrpssiqlavlvdrghrelpiradyigkniptsksekvmvqldevdqndlvaiyen
>d1bd3a_ 3.56.1.1.13 Uracil PRTase {Toxoplasma gondii}
qeesilqdiitrfpnvvlmkqtaqlrammtiirdketpkeefvfyadrlirllieealne
lpfqkkevttpldvsyhgvsfyskicgvsivragesmesglravcrgvrigkiliqrdet
taepkliyeklpadirerwvmlldpmcatagsvckaievllrlgvkeeriifvnilaapq
giervfkeypkvrmvtaavdiclnsryyivpgigdfgdryfgtm
>d1dkra1 3.56.1.2.1 (8-166) Phosphoribosylpyrophosphate synthetase {Bacillus subtilis}
nlkifslnsnpelakeiadivgvqlgkcsvtrfsdgevqinieesirgcdcyiiqstsdp
vnehimellimvdalkrasaktinivipyygyarqdrkarsrepitaklfanlletagat
rvialdlhapqiqgffdipidhlmgvpilgeyfegknle
>d1dkra2 3.56.1.2.1 (167-316) Phosphoribosylpyrophosphate synthetase {Bacillus subtilis}
divivspdhggvtrarkladrlkapiaiidkrrprpnvaevmnivgniegktailiddii
dtagtitlaanalvengakevyaccthpvlsgpaverinnstikelvvtnsiklpeekki
erfkqlsvgpllaeaiirvheqqsvsylfs
>d1lfaa_ 3.57.1.1.1 Integrin CD11a/CD18 (Leukocyte function associated antigen-1, LFA-1) {Human (Homo sapiens)}
gnvdlvflfdgsmslqpdefqkildfmkdvmkklsntsyqfaavqfstsyktefdfsdyv
krkdpdallkhvkhmllltntfgainyvatevfreelgarpdatkvliiitdgeatdsgn
idaakdiiryiigigkhfqtkesqetlhkfaskpasefvkildtfeklkdlftelqkkiy
vie
>d1atza_ 3.57.1.1.2 von Willebrand factor A3 domain {Human (Homo sapiens)}
qpldvillldgsssfpasyfdemksfakafiskanigprltqvsvlqygsittidvpwnv
vpekahllslvdvmqreggpsqigdalgfavryltsemhgarpgaskavvilvtdvsvds
vdaaadaarsnrvtvfpigigdrydaaqlrilagpagdsnvvklqriedlptmvtlgnsf
lhkl
>d1auq__ 3.57.1.1.3 von Willebrand factor A1 domain {Human (Homo sapiens)}
disepplhdfycsrlldlvflldgssrlseaefevlkafvvdmmerlrisqkwvrvavve
yhdgshayiglkdrkrpselrriasqvkyagsqvastsevlkytlfqifskidrpeasri
alllmasqepqrmsrnfvryvqglkkkkvivipvgigphanlkqirliekqapenkafvl
ssvdeleqqrdeivsylcdlapeapppt
>d1ido__ 3.57.1.1.4 Integrin CR3 (CD11b/CD18, Mac-1), alpha subunit {Human (Homo sapiens)}
dsdiaflidgsgsiiphdfrrmkefvstvmeqlkksktlfslmqyseefrihftfkefqn
npnprslvkpitqllgrthtatgirkvvrelfnitngarknafkilvvitdgekfgdplg
yedvipeadregviryvigvgdafrseksrqelntiaskpprdhvfqvnnfealktiqnq
lrek
>d1qc5a_ 3.57.1.1.5 Integrin alpha1-beta1 {Human (Homo sapiens)}
stqldivivldgsnsiypwdsvtaflndllermdigpkqtqvgivqygenvthefnlnky
ssteevlvaakkivqrggrqtmtalgtdtarkeafteargarrgvkkvmvivtdgeshdn
hrlkkviqdcedeniqrfsiailgsynrgnlstekfveeiksiaseptekhffnvsdeia
lvtivktlgeri
>d1poia_ 3.58.1.1.1 Glutaconate-CoA transferase alpha {Acidaminococcus fermentans}
skvmtlkdaiakyvhsgdhialggfttdrkpyaavfeilrqgitdltglggaaggdwdml
igngrvkayincytansgvtnvsrrfrkwfeagkltmedysqdviymmwhaaalglpflp
vtlmqgsgltdewgiskevrktldkvpddkfkyidnpfkpgekvvavpvpqvdvaiihaq
qaspdgtvriwggkfqdvdiaeaakytivtceeiisdeeirrdptkndipgmcvdavvla
pygahpsqcyglydydnpflkvydkvsktqedfdafckewvfdlkdhdeylnklgatrli
nlkvvpglgyhidmtke
>d1poib_ 3.58.1.1.2 Glutaconate-CoA transferase beta {Acidaminococcus fermentans}
dytnytnkemqavtiakqikngqvvtvgtglpligasvakrvyapdchiivesglmdcsp
vevprsvgdlrfmahcgciwpnvrfvgfeineylhkanrliafiggaqidpygnvnstsi
gdyhhpktrftgsggangiatysntiimmqhekrrfmnkidyvtspgwidgpggrerlgl
pgdvgpqlvvtdkgilkfdektkrmylaayyptsspedvlentgfdldvskaveleapdp
aviklireeidpgqafiqvp
>d1b0pa4 3.59.1.1.1 (416-668) Pyruvate-ferredoxin oxidoreductase, PFOR, domain III {Desulfovibrio africanus}
gtiqcqfwglgadgtvgankqaikiigdntdlfaqgyfsydskksggitishlrfgekpi
qstylvnradyvachnpayvgiydilegikdggtfvlnspwssledmdkhlpsgikrtia
nkklkfynidavkiatdvglggrinmimqtaffklagvlpfekavdllkksihkaygkkg
ekivkmntdavdqavtslqefkypdswkdapaetkaepmtneffknvvkpiltqqgdklp
vsafeadgrfplg
>d2gar__ 3.60.1.1.1 Glycinamide ribonucleotide transformylase, GART {Escherichia coli, k12 strain tx635, with plasmid pjs167}
mnivvlisgngsnlqaiidacktnkikgtvravfsnkadafglerarqagiathtliasa
fdsreaydraliheidmyapdvvvlagfmrilspafvshyagrllnihpsllpkypglht
hrqalengdeehgtsvhfvtdeldggpvilqakvpvfagdsedditarvqtqehaiyplv
iswfadgrlkmhenaawl