ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A8T6SBL1 | CIVDMPVELGISEVLKMKAFEAGGLTDYEEKAKVAAKAMETQNAIYVHLKGPDEFGHDGDAIGKMKNIEEIDQRFFKTLVENIDTSKVAIVVSADHSTPCINKGHSDDPVPVLVSAEFIKGDSSVRMTEKEAEKGKIGLIAGADVVSTALELIKSQK | Pathway: Carbohydrate degradation.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Length: 157
Sequence Mass (Da): 16932
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A0A1B6GAB3 | MGFFLGSRLSFIIIVAIAGFVAYDINKHGSFRGSKTGVFLRDCGALRYGELAWTRFRSYSQQAYRWSQKHVPGYMSFMRESLTVYLIIIRDVVTSLATHLWASISQIWHYFEDKKPVIAKWVDQYFPGLSDRVNSWLSQSWSFLLQCAKFVIQWLKDNIFVGSLSAENLQRLSWEAFNTTQTFARKTLSWINGKMAPVIVGSST | Function: Critical mediator, in cooperation with CASP4, of endoplasmic reticulum-stress induced apoptosis. Required or the activation of CASP4 following endoplasmic reticulum stress.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 204
Sequence Mass (Da): 23507
Location Topology: Multi-pass membran... |
R7TV57 | MSGIGKLLRGCLEFNALKKPKLLEQFKAVKEHPAPKAVTFSCMDNRIIITKLLQCDVGDMYLVRNAGNLVPHCETLSYDAVSTEPGALELGCVMNEIPNVLVCGHSDCKAMNALYGMRDQTQIKEGTPLTLWLKKHGHSSVKRYNELLNSPDGIGPLEFKIPGKTLRAYIDPDKKLSEVDKLSQVNVLQQVENACSYDMLKDKLQSGQVNVTALWFNIQTADFFMFSKEKERFLEVNESTIDHLVSDAGGH | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 251
Sequence Mass (Da): 27988
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R7UTF9 | SDAILFHGRHINGRNVPLERDPRQKWVFYEEDPPSHTWRNKKDSFRNWFNITATYSHTSDIPLIQRRLRCREKPEERAARMVNKVNYATGKDGRALWVVDECVTPSQRERYVEELRKHMIVDVFGACGKPLCNSSSSCLEELINSTYKFILIFEKALCHEYLSADLSSILSANVIPVVLGLYDYSNMLLEGSFVEARRFESPQMLAQYLEYIDQNDKVYNKYIRRKYSMECVPLESQTFPCQLCHYLHLNVKTQKEISDVKRYWSE | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 266
Sequence Mass (Da): 31353
Location Topology: Single-pass type II membrane protein
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R7TFU0 | FPRVTLCDFKVRQLGNIHRHTVQCVLPINFFNEKVYMVIWFWLAIVSIINVINLITWIARTLFRLDQLQYIRRHLRYMDKMDRPEDKKISRRFVYEYLRCDGVLVLKLVAMNTSDIVASELTAELWDYFKSNPPTFYKKKNDFVDV | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 146
Sequence Mass (Da): 17641
Location Topology: Multi-pass membrane protein
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K3Z2P3 | MAARCYTAATVVFSSRAGAPDLSLSLPAAAAAAVPSARPGPRGAWTYGGGYSHRPATGRAMGSAPSSSSFPSPQTPPGQAQEKANTSLTEEEWKKRLTKEQYYVTRQKGTERAFTGEYWNTKTPGIYHCVCCDTPLFESSTKFDSGTGWPSYYKPIGDNVKSKLDMSIIFMPRTEVLCAACDAHLGHVFDDGPPPTGKRYCINSASLKLKPQ | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the reduction of methionine sulfoxide (MetSO) to methionine in proteins. Plays a protective role against oxidative stress by restoring activity to proteins that have been inactivated by methionine oxidation. MSRB family specifically reduces the MetSO R-enantio... |
A0A2E4WXX0 | MARLRDIDLSKALFVLPNLFTMSSIACGFYAILKASSNEPTSRDFLTACLAIVFAAIFDTMDGRVARLTKTQSDFGVQLDSLADLVSFGVAPGVLVYRWALQDHGVLGFLFAFVFVAAGAARLARFNVLVARGQEATSDFVGLSIPLGALAVISLVGFCVRAEIDPASFHRLVTLYVVVVSFLMVSNLRMRSFKDFRVRGSALLGIAILSLIPAILAFFLREPYGVLLALSWLYIFYNSIRAVWRRVWTAAPELVAETEEVSAEI | Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + CMP + H(+)
EC: 2.7.8.8
Subcellular Location: Membrane
Sequence Length: 265
Sequence Mass (Da): 29045
Location Topology: Multi-pass membrane protein
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K3Z4V9 | MASSSAVPSSAVAVAAAVLLLAAVGAEAETRKYQFNVQMASVTRLCGTKSIVTVNGQYPGPTLFAREGDHMEVTVVNRSPYNVSLHWHGVRQLLSGWADGPAYITQCPIQPGGSYVYRYQIVGQRGTLWWHAHISWLRSTLYGPIVILPPAGVPYPFPKPDEEVPLMFGEWWRNDTEAVIAQALQTGGGPNISDAYTINGLPGPLYNCSAQDTFRLKVKPGKTYMLRLINAALNDELFFSVANHTLTVVDVDALYVKPFAVDTLVIAPGQTSNVLLAAKPAFPGARYYMEARPYTNTQGTFDNTTVAGILEYEDPSSSSS... | Cofactor: Binds 4 Cu cations per monomer.
Function: Lignin degradation and detoxification of lignin-derived products.
EC: 1.10.3.2
Catalytic Activity: 4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O
Subcellular Location: Secreted
Sequence Length: 585
Sequence Mass (Da): 63047
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K3ZQD2 | MLRAAAAAAAVFPARFAAAPAVAAAEDLRSPLLRVLGTLRGGRGSVLLGRRARFCSNSSASDSEAAAAEAEAKAEDATVAEGEADGKASSAIVPTNPKIEDCLSVVALPLPHRPLFPGFYMPVYVKDQKLLQALIENRKRSASYAGAFLVKDEEGTDPNIVTGSDSEKSIDDLKGKDLLKRLHEVGTLAQITSIQGDQVVLLGHRRLRITEMVEEDPLTVKVDHLKENPYNKDDDVIKATSFEVISTLREVLRASSLWKDHVQTYTQHIGDFNYPRLADFGAAISGANKLLCQEVLEELDVYKRLKLTLELVKKEMEISK... | Function: ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participat... |
A0A5E7V9C3 | MSRAPDTWILTADCPSVLGTVDAVTRFLFEQGCYVTEHHSFDDRLSGRFFIRVEFRQPDGFDEQSFRAGLEERGQAFGMIFELTAPNYRPKVVIMVSKADHCLNDLLYRQRIGQLSMDVAAVVSNHPDLKPLADWHQIPYYHFPLDPNDKPSQERQVWQVIEESGAELVILARYMQVLSPELCRKLDGKAINIHHSLLPGFKGAKPYHQAYNKGVKLVGATAHYINNDLDEGPIIAQGVEAVDHSHYPEDLIAKGRDIEGLTLARAVGYHIERRVFLNANRTVVL | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; formate from 10-formyl-5,6,7,8-tetrahydrofolate: step 1/1.
Function: Catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to formate and tetrahydrofolate (FH4).
EC: 3.5.1.10
Catalytic Activity: (6S)-10-formyltetrahydrofolate + H2O = (6S)-5,... |
A0A3R7YI94 | MVAGVMFLAWRVQMNGSSTTLYTWSIYENEFAHLPSFVSKAMSYAHVHTLYLWKLLWPQYLCYDYGWNTIHAVTSIYDVRNLASSVAYMAVVGAVGTSASHRRTSPLFVLLVLGICPFVPASHVMFPVGTILAERLLYLPSVGFCLVVGYATERVLLAATPASKPKLVALLGLVLAVATSRTIRRNLDWHDEHTLFQSALSVAPTSVKVLTNLGQDILPKDARTAVLYLERAVALMPSYSLGHLNLAAGYAALKKPLQAMHHLVQSIELVQEPKAYTSLGQHFVEFWESHVGAGQNQLAYTILAFFLNVFVLHDRAMMNA... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.109
Subcellular Location: Endoplasmic reticulum
Sequence Length: 410
Sequence Mass (Da): 45563
Location Topology: Multi-pass membrane protein
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A0A290U6Q0 | HKDIGTLYLIFGAWAGMVGTSLSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTIEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFG | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
R7TUU5 | MDALSFRVKAIERLSKNSQLAYAQAEHIHKEVLKPGGHWTPEECAARQRVAMVVPYRNREDHLRIFVSYMHRFMQAQYLEYQIFVVEQASPDVFNRAALMNIGFLEALKLHDFDCFIFHDVDLLPLDTRQPYTCFQAPTHLGAYMSKFSYQMPYDGFFGGAVALSTENIKQMNGFSNLFYGWGGEDDDTLNRVLWRNLTVHRHAQDIGKSYMIKHEKDEGNPTNPNRGIGHEMKPDQYNRNGINSIKYIKQSTDLNVLYTRVLVSIGEN | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Membrane
Sequence Length: 269
Sequence Mass (Da): 31133
Location Topology: Single-pass type II membrane protein
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A0A7R9BQF3 | MPFYAVVRGYNPGIYYSWAECEPQVSGFSGADYRKFPALECAEAYCRDPEAFWRLGLPIRRRSRRPYRRYPFPGAHLQPAIPLRILVQARLAEDDDFHFTEDGFAICYTDGSCMGRLRNAGVGVWFGNDHVANICEPLPIPGTNNKAELLAVLYAIHAARESGLDMLEVRTDSRYAIYSLTEWLPKWKSNNWLTTENTDVQNQGEIRAIDEVRNYMEVRFEWTPGHAGNSGNSAADSLAKRGAARALTVYRQ | Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Length: 252
Sequence Mass (Da): 28607
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A0A7R9BM08 | MVNKVAIAIIAAVIQIVVALVITLPVLYTDCNQLKKCKRSNAEIEQKMVSKVATALIAAFVLVVVALTITLPILYTDCSLLKKCKRSNAEILKTILDEVPLIDGHNDFPMLLRTAIQNKLSKVDLNKSLKDDPAFNKFVYNHVDIPRLRQGQVGAQFWATFIGCSRQYNDSLHEALEQIDVTKRMIEAYPEHFEFVTNAEGITKAHKRGKIASLIGVEGGHMIEESLAVLRMFYQLGVRYLTLTHNCDTPWARYHEISAPGSGRVKGLTRFGHKVIQEMNRLGMMVDLSHTDAQTMRDAMTVSDAPVIFSHSSVYSVCNH... | Catalytic Activity: an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid
EC: 3.4.13.19
Subcellular Location: Membrane
Sequence Length: 511
Sequence Mass (Da): 57016
Location Topology: Lipid-anchor
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K3ZHQ5 | MAASAKPFCSTTQQPPTPIANRLPSPSQPPALSSRAAPRFAHGLSAAAGVRASPSARRLRALARPIRASSQHQQQQQLPRRRPEYVPSRIDDPNYVRIFDTTLRDGEQSPGATMTSAEKLVVARQLARLGVDIIEAGFPASSPDDLDAVRSIAIEVGNTPVGEEGHVPVICGLSRCNRKDIDAAWEAVRHARRPRIHTFIATSEIHMQHKLRKTPEQVVAIAREMVAYARSLGCPDVEFSPEDAGRSNREFLYHILEEVIKAGATTLNIPDTVGYTLPYEFGNLIADIKANTPGIENAIISTHCQNDLGLATANTLAGAR... | Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
EC: 2.3.3.13
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Length: 635
Sequence Mass (Da): 68331
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R7TWQ8 | MGHVEGKGLGKNQQGRAEIIEASKQKGRRGLGSQVKGFEAKDVDWDASKDEVTVDETVSWIETCSDPVPSIEEMRTWMLEGPNKKTIDDETEFCNPDILRDILSCKSVFDHLEGEEMRKARTRSNPYELIKGVFFQNRAAMKMANMDAVLDFCFTEPRTVEGRSLVQPNELLYFADVCAGPGGFSEYVLWRKAPGETKGFGFTLKGNNDFKLEDFYSTHSEFFEPHYGKGGMHGDGDVYNPENLMEFQEFVLNSTDQKGVHFVMADGGFSVDGQENIQEVLSKRLYLCQFLAAMMILRPGGHFVCKLFDVFTPFSVGLTY... | Function: S-adenosyl-L-methionine-dependent methyltransferase that mediates RNA cap1 2'-O-ribose methylation to the 5'-cap structure of RNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped mRNA to produce m(7)GpppNmp (cap1).
Catalytic Activity: a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucl... |
Q7ZZM8 | MRLKLRNIFLVYFVVSSVGLMYALLQIGQPCDCSQHLRSGSNAHGRSRHSFVPKGPRDLSEDDQLPVIYVVTPTYARPHQLAELTRLSQTLLLVPSLHWILVEDSAERSKAVADLLAQSGLHYTHLNVQTPPVMKLKDSDPNWLKPRGVEQRNEALRWLQLNRSPKDSGVVYFADDDNTYSIRIFQEMRYTQKVSVWLVGLVGGLRYEGPLVEKGRVVGFHTAWKPHRPFPIDMAGFAVSLSLLLSHPGARFDPNAERGFLESSLLGQLVSVGELEPRADNCTKVWVWHTRTEKPKLKQEEVLEKQGRGSDLNVQV | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: 3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP
EC: 2.4.1.135
Subcellular ... |
A0A1I8JJP9 | MLTDAFFSGLAASPRRLSLLLAGAGAAAAAAYLLSVAYRRRRGGGRSIRGAGGAARRRALRLSVTSAEPLLHLLEQTCRDEPSELPVVCQFGDTKCRLVMKNRRRVLEKLQSLMRGGPDALEVITDFDHTLSKFSENGRRVPSSHGIMESYPDLSAEDHKYFRELYTKYYAIEICPDMSDEEKLPHMIEWWTRSHDRMVLAGFQKSVLAQTVDVSGVALRDGWHQFFDRLEELGIPCLIFSAGIGDIIQEILVHFDIRGKLIRVVSNFMLYNEKGVLRGFSEPLIHTFNKRFSAFASSEASANDLVGATDRRHVLLMGDT... | Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
EC: 3.1.3.5
Subcellular Location: Cytoplasm
Sequence Length: 382
Sequence Mass (Da): 42338
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A0A150IID0 | MAKLAPSILSADFSRLGDEILEAENAGADLIHIDVMDGHFVPNITIGPLVVEAVSKITELPIDVHLMIENPSDYVEMFFKSLDKNDRDVSLDYISFHIEASYHPHRLLNKIRELKVKSGIALNPSTPVNTITHLLDSTDLLILMTVNPGFGGQSFIETMIPKIKEAKKLVKGHDIEILVDGGVTEKNIKRIKDAGADILVAGSAVFNKNDSIKNNIIRLKALV | Cofactor: Binds 1 divalent metal cation per subunit.
Pathway: Carbohydrate degradation.
Function: Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.
EC: 5.1.3.1
Catalytic Activity: D-ribulose 5-phosphate = D-xylulose 5-phosphate
Sequence Length: 223
Sequence Mass (Da): 24513
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A0A2E7ZS57 | MEHRSIAVLHGGPSSEHDISVISAREVLNSLRGGGYTALSVWVDRQGLWHFAGAQAPSGSSVADPLCLPEALARLRDEDVLCAFLGFHGTYGEDGRVQAALELAGVPYTGSKVTASALAMDKPLARRILASAGVRVPAGRDLVSSDVLGNEAHVAQELVTEFGLPLVLKVSAGGSSLGVEIPNTLAEVQGALSRLAADTQILLCEQFIIGKELTAGVLSRIDGQLEALPAVEIAPKGEGFFDYEAKYDPSLTDEICPARISEHVENKCRHIGVLAHRALGCRGISRTDLILDEQDQLWVLETNTLPGLTPASLLPKSAAA... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
EC: 6.3.2.4
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Length: 339
Sequence Mass (Da): 35... |
A0A2E7ZQK6 | MDDNKRRNIKIFVSMTLIGAVLDLATKAWAEGALTQLPGQSMMIFEPWCEFALSYNQGTAFSAIFDLGEMVRLILGIASLLVVGLLGWSVTRPEVVQIEVWCYGMLAGGAIGNGYDRVFREAPSGGTGVVDFVKLNYPWGGSWPTFNVADSLLVVGVALLIIRWWTHPPTDDANVRAERS | Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, ... |
A0A0C4EEL9 | MINDESASHQTSHPSIISFCHYFLLSFPSVISYCHLLLSSPSVSISWHYFLASSLLSLYTFTRPKMRFSLAVTAAFVARALAAPLTLLETEYSFPRRLVARQTVGTEANEFKNGPCRDIVLLFARGSTQDGNMGQQPGPDLANAMKAKFGADRVAAQGMSYAAILAGNLAEGGATSMESSDFADLIKDVAVKCPDARIVVSGYSQGAALVHRAMRSCSVNVKTHVAAAVTFGDTQNKQDGGRIPGFDASKTLIICNDGDMVCDGTLMVMGPHMQYQSRVPEAVNFISTLVA | Function: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants. Degrades cutin, a macromolecule that forms the structure of the plant cuticle.
Catalytic Activity: cutin + H2O = cutin monomers.
EC: 3.1.1.74
Subcellular Location: Secreted
Sequence Length: 291
Sequence Mass (Da): 3123... |
A0A6J1MEB9 | MDWSSGKHPLPPNANNKRLTDNNNQSMIVDLTYSLLRRSPRSHQPDAAHPLASLNNQTDDTMEVPEPAPAPAPAPVPVPVPAPAPAPAPPPPAPAGPIIFPPPLANGQKQSQDINLPADITESDEDGKHHAYECPICLENVSGRQPATTKCGHVFCYGCILSVLRVNHKCPICSVHLATRRAIKRIYI | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Nucleus
Sequence Length: 1... |
A0A0U3H9B8 | MDVEVLVPLNISGVWYPVYTNNPLTTGSIGIGLVVEPRIMVRGKRSNKAEVEFNGKIIEFPNLAILKRLGELKISVQSQVPLGFGYGLSGSISLAYSYLAYELGLTSLKEALYTAHESEVVNKNGLGDVIAEYIGGGIVYRKVPGAPGIGKAEKINVSWSEQVCSKPEMALPTTVLLKKNENALTYIEEFLKNPDLTKFFEVSRKFTEELGFVSNIPNSFRKKGLIIKHGDCNKEWIQHTPATNGVLIH | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
Function: Phosphorylates (R)-pantoate to form (R)-4-phosphopantoate in the CoA biosynthesis pathway.
EC: 2.7.1.169
Catalytic Activity: (R)-pantoate + ATP = (R)-4-phosphopantoate + ADP + H(+)
Sequence Length: 249
Sequence Mass (Da): 27413
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A0A0R3SE94 | MNEVSPRPMKLKKFLWRNSNKDESNGRTILVNSIPSLSQEARVNNGKFGNNEIISSHYKWWNFLPINLFEQFHVVANFFFLLISILYFFGETPINPVTTIAPLVTVIGISMAKDAIDDIKRHRVDNTFNRIQFMVLTHDSKDNTSSFVQRNSQDIHCGDIVICYDNSSLPCDMLILASSNLNGKVFITTDNLDGESSIKTTNALAFTQNLFTPTVKKIENDQLYNIDLGLERSTIICQNPCEDLKAFEGSLNLPHESIPLALNSVVYRGARLCHTTFMLGVAVYTGKDTKLSLNSKPGFRKFSSSAGRFNTILLCFMGAM... | Catalytic Activity: ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.
EC: 7.6.2.1
Subcellular Location: Membrane
Sequence Length: 916
Sequence Mass (Da): 103194
Location Topology: Multi-pass membrane protein
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Q6DEA4 | MARAFLGAVACTLILAASAMYSPSDDVIELTPSNFNKEVIQSDSLWLVEFYAPWCGHCQRLTPDWKKAATALKGVVKVGAVNADQHQSLGGQYGVRGFPTIKVFGANKNKPDDYQGGRTADAIVDAALNSLRSFVKDRLGGRSGGSDSGRQSHSGGSGGSKKDVIELTDDTFDKNVLNSDDVWLVEFFAPWCGHCKSLEPEWAAAATEVKEKTNGKVKLAAVDATVSQVLASRYGIRGFPTIKIFQKGEEPVDYDGGRNRADIVARALDLFSENAPPPEINEILNGDIVKKTCDEHQLCIVAVLPHILDTGAAGRNSYLE... | Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
EC: 5.3.4.1
Subcellular Location: Endoplasmic reticulum lumen
Sequence Length: 442
Sequence Mass (Da): 47784
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A0A7R9GCG9 | MFPTPRLLTSASFLRRLFRFPFNTQPELDESKLNPCQRALLEERCLLVTERDAVTGSATKRDCHLWQNGSCPLHRAFSVFLFNGKGEMLVQQRAMTKITFPGFYSNTCCSHPLDTQEELQEKDFIGVRRAAVRRCEYELGIQLDPQDLTVVTRVLYKAPSTDVWGEHEIDYVLFARKDVKLLLNPNEVQDFKWIPRENFQEFLAKCASRGIPLTPWFQIVAAKFLQHWWQNLDNLKAVQDLENIHKVISVSGTEVEDLDVRLQILKNQEYRHWWQNLDNLKAVQDLENIHKVISVSGTEVEDMDVRLQILKNQEYPSLGK... | Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1.
Function: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
EC: ... |
A0A6V8NF18 | MRIVNPSVTKELLKQYRVTLRKRLGQNLLVDPNILDKIIEVAQIREDDCILEIGPGLGALTQELVRRARRVVAVEYDRKLCQILKEIFASTQNLLVINADLLSLDLASLAQEHTLTKVVSNLPYNIASTAALRIMEECSNIAEMTVMVQKEVAERMAASPGSAAYGSYTLKLRYFAQVFPLFQVPRTVFLPPPGVDSTMVKIGRDTYWQKVYPVRDFLFRIIELGFGQRRKKLVNCLYSGSALRLSKEDVVQALNSAGIDISARAEELSLEKFVQLGQALWPLLHQSSTRFNNKSPD | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) +... |
A0A9D4J8M0 | MSLEWSPWFYTPCDVTCGTGSRSKLRSCSTTRDEDCSGNAYDTESCNLQECSSLGKIAPGDH | Function: In the vertebrate host, binds to highly sulfated heparan sulfate proteoglycans (HSPGs) on the surface of host hepatocytes and is required for sporozoite invasion of the host hepatocytes.
Subcellular Location: Cell membrane
Sequence Length: 62
Sequence Mass (Da): 6785
Location Topology: Lipid-anchor
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R7VCD1 | MAREEFKRIVPNVTFGSDPVKAKVAGGTLVTLHVRHRGDIMKENYQNMRYTFPGRSFFENSIQFFADADPNLHVVVCCVDIEWCRSNLTDLPATFYFSESKNAIVDLAIMSMGEHAIMTTGTFGWWGAWLANGETVYYSNWPRHGSQMVQIRYVRQDFFMPHWIVLWWRSKSDKNNCSLTSRDQETKPLRPDEANKEITPNKKQPPLHATEKPPKNTTKVYVTGNVYGFRRTGNRLFVFAAIMAVTWRYSMTSVLSPEFELQKYFNIDYRARPGVGISNWAGGRM | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 285
Sequence Mass (Da): 32906
Location Topology: Single-pass type II membrane protein
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O48949 | MNRWNLLALTLGLLLVAAPFTKHQFAHASDEYEDDEEDDAPAAPKDDDVDVTVVTVKNWDETVKKSKFALVEFYAPWCGHCKTLKPEYAKAATALKAAAPDALIAKVDATQEESLAQKFGVQGYPTLKWFVDGELASDYNGPRDADGIVGWVKKKTGPPAVTVEDADKLKSLEADAEVVVVGYFKALEGEIYDTFKSYAAKTEDVVFVQTTSADVAKAAGLDAVDTVSVVKNFAGEDRATAVLATDIDTDSLTAFVKSEKMPPTIEFNQKNSDKIFNSGINKQLILWTTADDLKADAEIMTVFREASKKFKGQLVFVTVN... | Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
EC: 5.3.4.1
Subcellular Location: Endoplasmic reticulum lumen
Sequence Length: 532
Sequence Mass (Da): 58237
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A0A251UJP0 | MDEEKEKKVVFVWDMDETLILLKSLITGTYTKAFNGSKDVEKGIEIGKTWENQILRICDDYFFYEQIEGCNKPFVDSTREYDDGLDLTDYDFANDAFVGAAFDDDANKKKLAYRHRIIAHKYKKGLRSLFGEKMIKSWDNLYEVTDDFTDKWLSSAKACVAQCAGDSGAENINVIVTSGSLIPSLVKCLLFRLDDLISYDNVYSSWEVGKYQCFSLIKERFDGPNVQFCAIGDGWEECEAAENMQWPFVQIDPVPVSTSHRFPGLNLETLGHYIGVVYGGDSDDEDE | Cofactor: Binds 1 Mg(2+) ion per subunit.
EC: 3.1.3.48
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Length: 287
Sequence Mass (Da): 32646
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R7UND8 | MATIQDFYRDRDVFLTGASGFLGKQILEKLLRSCNVRHVYVLVRPKRGRSSEERKDILLKSEIFTPLKMTDQSFSTRVVLIAGDMTSPGMGLQEGDAELLRREVSVVLHAAASVNFTEKIRDAVTVNVLALKEMIKFCKSLPHLQAFVHISTAYVHCYDPFTPECIVKPKESPQVVLDLVKNETDQRLEELTPKLIHPWPNTYTYTKCLAEWMLQEEADDLPCCIFRPSIIGASAEEPYRGWVDNFNAATGILAGIGIGVCNPVYGDASNKADVVPVDLCANAVIA | Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
EC: 1.2.1.84
Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+)
Sequence Length: 286
Sequence Mass (Da): 31833
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A0A660WVH0 | MEKAGNGILEHVKDSHYYDIFGYHLKLPEIPPVKVLGITFDFSITRMVVLLWIAALIISLCFFFSFRKRKLIPSKLGILLEYVILYIRDNIAYPILGRKLGDKYFPLISTLFLFILVCNLLGLVPLLGSPTSNLSVTSGLAIIVFVIIVLEGIKQHGLLGYFKSFIPGGIPAWLIPVMLPLEVLGLFIRIIVLAVRLFANMVSGHINIVVLFFLIIFLKTYLISPFSFGIALFVSLLEILVAFIQAYIFTMLSAIFISMSVKSH | Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 264
Sequence Mass (Da): 29628
Location Topology: Multi-pass membrane protein
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A0A1U8PD78 | MATAASSSSFTMLHLASLISIFALTNARIPGVYTGGSWETAHATFYGGSDASGTMGGACGYGNLYSQGYGVNTAALSTALFNNGLSCGACYEIKCANDPRWCHPGSPSIFITATNFCPPNFALPSDNGGWCNPPRPHFDLAMPMFLKIAEYRAGIVPVSFRRVPCRKQGGIRFTINGFRYFNLVLITNVAGAGDIVKVSIKGTNTGWTSMSRNWGQNWQSNVVLVGQALSFRVKGSDKRTSTSWNVAPTNWQFGQTFTGKNFRY | Function: Causes loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found.
Subcellular Location: Secreted
Sequence Length: 264
Sequence Mass (Da): 28498
Location Topology: Peripheral membrane protein
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A0A8S2LHK9 | MLRIFRYRCIILRYIILWLFLMTMTKLTITFYDDLQQQSIDSTSLALPSDDSELNKNKKQDSFNLTMNESQYVNATAINRTVIEYYREYVQKTNQEQFMHNKHLFSLRTTRYILLVQVHTRVIYLKKFIEMLKDVQAINQTLLIFSHDFIDIDINLLVTNIDFVPVIGNYKGFQIDSTVLYNLL | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 184
Sequence Mass (Da): 21971
Location Topology: Single-pass type II membrane protein
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A0A1T3A290 | MKSSKFSLLAFLMSCLFAGWGLVYVGRIKWAIRVAALMYIGVVLMGVSGLAATPVGLYVFIAFIITLKLATAIASAVLARRYDGPPGLPRKRFHVLYVGVLIVITLLLFEVFRAPLLGFKNYFIPSGSMAPTLSVGDYIISDLRPGAPKVGDIVVYRWDGTEAVKRVAGIGGDTLAIVNGELIRNGENLGLFHAPAERVKKDYSLTLAPLRVEPGHVYLLGDNRDVSNDSRFMGQVADEDVVGKVTGIWFSGDLGRIGTTFP | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 262
Sequence Mass (Da): 28351
Location Topology: Multi-pass membrane protein
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A0A650D3A1 | NVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGPSVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISLYQIPLFVWALLITAILLLLSL | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A251U3H4 | MGDNVLNTPPFYTTKDAETGSLSRRLFRSYDVMHVALRLVCLSASLASVVVMITAKEKSTMSLYGFDIPVYSKWSFSDSFDYLVGVSAAAGVHSLLQLLMTSRMLLRKSSIISSKKHAWLLFASDQVFAYAMMSCGSAASGVTNLNRTGIKHSSLPNFCKPLHSFCDRVAVSIAFAFFGCFLLAMSSVLDVVWLSAY | Function: Regulates membrane-cell wall junctions and localized cell wall deposition. Required for establishment of the Casparian strip membrane domain (CSD) and the subsequent formation of Casparian strips, a cell wall modification of the root endodermis that determines an apoplastic barrier between the intraorganismal... |
A0A496SUN3 | MRLVFMGTPDFAVPSLRKLLEDGHQIVGVVTRPDRPRGRGKHLVPSPVKKEAMTKGLRVLTVEDLKDLDFVRSLRQMSPELIVVVAFRILPPQVLTIPPRGVINLHASLLPKYRGAAPINWAIINGEKQTGLTTFFIDDRVDTGDIILQRAVPIGQEETAGELHDRLMSLGAELLSETVSLVESGDFPRRPQPREGASKAPKLKKEDARIDWSKPAEQIRNLIRGTNPRPGAFTHRKGSVLKIHRASALTAPQKGAPGEILRADPKDGIWIATGQGALFLSQLQPQDRRPMSSAEFVRGYGVRKGELWA | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
EC: 2.1.2.9
Catalytic Acti... |
A0A7Y5TRA6 | MTGVSPLIGPVLLLGAAGQLGQALAPRLARLGAVVPLTRADVDLERLDDVRALVRRVRPGLVVNAAAYTGVDDAEGHEARCRLVNEMVPAVLAEETARLRVPLVHFSTNYVFDGLQPMPYTEDAPPSPLSVYGATKADGERAVAAANPRHLIVRAAAVYGGSGRTFMRRILELAREREELRVVDDQYVSPTPAWVLAHATVAAIDHLLAEHPAAQGLLHLTTTGAASWHAFALRILELDPDRAAHRVRSVVAVDTAGYPTPARRPANGVLDTGKAERELGIRLPGWEEALRRTWAGEGACR | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Length: 301
Sequence Mass (Da): 32352
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F5L506 | MTPTERAYTLTLTVQEGQEGRLAAFLREQHHFSRRLLNKLKREGTVQVNGQTAFFHTQLKTGDKVAVCFPVEKPNPELKPQPMVLDIIHEDQDVLVVNKPAGLTVHPTMTEQEGTLANGVIHHWQKRGTCASFHPVSRLDKHTSGLILIAKHSFVHQQLDVSRQHHGLTRRYYAWVHGVVEKDNGEIVAPIGLEEGSIIKRRVRADGQPARTRFRVIRRYADYTWLELTLDTGRTHQIRIHCQHMGHPLLGDDLYGGSRHLIQRQALHACALAFVHPRHKKVCSFSAPLPEDLKRLAAG | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 299
Sequence Mass (Da): 33923
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R7TRE3 | MRRTGKRNGSSAEQSSTKKESKETATKEIPSQFFHLFGFHLSDFSSWGSFQRLLHRPTDPSSLGVLRILYGLLMVMDIPQERGMSHADYKWGDEDECRFPLFDFLSPLPIAWMYVVYLIMWMGALGIMLGLMFRVSCLMFACSYWYVFLLDKTVWNNHSYLYGLCSLLLLFSDANRYWSLDGLWHRHKRNAHVPLWNYTLFRSQFFLVYFIAGLKKLDADWVTGYSMQKLSEHWVFDPFTWLLSNDLVDLWVVHRGGLAIDLFIGYILFFDKTRIIGIIFGGSFHLMNSQIFSIGMFPWMMLATMPIFCHVDWPRRLFSA... | Function: Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide.
Catalytic Activity: 2,3-epoxyphylloquinone + 4-carboxy-L-glutamyl-[protein] + H(+) +... |
R7UHU5 | MVGKPTPLQLFWCAQTFLAGSSTVYLLLKRSHWVKLALPSGDLSPGFFRFRKRLGMIKSEGSMPRRKYCGGTDTLNGYFNDLFTWATTPKQTNSDFAPTLLALFLFVGHLGRRLYESWGISVFSRRQLLGPIEFIRVYAFYIGAGLTIIAEAPPLTGVASCASLDGLGLRHLLILPIFYFSSRLHHDTHIALAKLRRNKAGHIVTTDHKMPKGGWFDVMSSPHYFAELLVYTSIGLILGTSNVTYWWMVTYVFTNQFYLAYNTHKYYEGKFENYPKERNMFIPYLL | Pathway: Protein modification; protein glycosylation.
Function: Plays a key role in early steps of protein N-linked glycosylation by being required for the conversion of polyprenol into dolichol. Dolichols are required for the synthesis of dolichol-linked monosaccharides and the oligosaccharide precursor used for N-gly... |
A0A0H6DCH8 | MKKPLIVQKFGGTSVGSIERMQTVAEHIIKAKNDGNQVVVVVSAMAGETNRLVGLAQQVDSVPNARELDVLLSAGEQVSMALVAMTLHKMGYAARSLTGAQANIVTDNQHNDATIKHIDTRTITELLEQDFIVIVAGFQGINENGDITTLGRGGSDTSAVALAGALNADECQIFTDVDGIYTCDPRIVPSARKLDVIDFPSMEEMARKGAKVLHLPCVQYAWKHAVPLRVLSTFEVNQGSLIKGSAATHAVCGIALQRDMALIRVESESFPSIIKQCQMLGIEVCTTIDEPTHSAFVIKRDAYAKLQLVGADKIRGSEPV... | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
EC: 2.7.2.4
Catalytic Activity: ATP + L-aspartate = 4-phospho-L-aspartate + ADP
Sequence Length: 395
Sequence Mass (Da): 42470
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A0A2E4WXX9 | MNQDPNQLTFLEHLDELRSRLIRSLACVLVTGIGAFVFKEELFELYKRPLLPLLEKNPNLLVVLSPIEPFLVYIKISAVTGIFIGLPFLLRELWAFLVPALSRDEKRASLPFLLAGTLCFMGGVLFCYFLVLPAALTVLHGLLPPAVHASYSMALFFNFITAMLLAFGLAFDLPVLMVLLAKLGILHPAWLARYRQYVVVGLFVLAAMVTPPDPFTQVAMALPLWLLFEIGLVISRLVIVASPVPPPTVAAPKVEENHESH | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes.
Subcellular Location: Cell membrane
Sequence Length: 261
Sequence Mass (Da): 28956
Location Topology: Multi-pass membrane protein... |
R7UM91 | MTAATMTHSSDGKSEPLKSSCESSCSTRRFVLLGVGLVVSSLLLAWTRTSPAAKASTPAPPNRWGIPSNKNNEFMTILYWSNTPGEEKRELEWSRQRQPQAVSCQQNQIKCMFSSDQSLAPESDALLIHVSKTEHYPNTRPTKQKWIFYEGSSPPRKKGEYPAAFYHHDDHFNVISTYSPRQSQIPASMIPWAKCKQSSTLTEKPIDFSLDKSRKVAWLANRCETGSAREDYITELSKHIHVDIIGKCNSMHCPRINARYRSVCVRSDPYLCSLCNYLHKTKDVVNRTLNIEQYWNRESLCNDADAFYSF | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 310
Sequence Mass (Da): 35329
Location Topology: Single-pass type II membrane protein
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R7VLR0 | MGKVWLLVFGIFLLNSGFILCDDDPADAEEDELDLNEIAEENDVLILTDANFQNAIADNEIILVEFYAPWCGHCKSLAPEFEKAAGILKENDPKVTLAKVDATVEKDLASEYGVSGFPTLIFFKNGAKTAYDGPRSSDGIVSYMKERADPSWKPPPDLVLHLTKANFSEFVDTAELILVEFYAPWCGHCKQLAPVLEKAAQGLQAFDPVIPIYKVDCPKESDLAREYEIKSYPTLKVFRRGKVFDYTGTERTAHAIVSYMENERRPPSTEVTSLSAVKKFMKTDDVTVFAFFKANDAAFETYENAANELRSDYDLGHTFD... | Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
EC: 5.3.4.1
Subcellular Location: Endoplasmic reticulum lumen
Sequence Length: 617
Sequence Mass (Da): 69588
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R7UUS8 | MLKKNSSVEDQANAVEQQRNRGSKVVYGQPIQLRHQFTGKYIHFSKKEMAELATKTMRVELQAYNAKQAQFRIMPRYKVRSEGDVVCIGDQVVLESFKSHGQYISVSEDVFPEDSVYAFRHEINFSVVHSTFTVYRQACAYDAQKEYLTPNGCVRFFHKEIDAYICAEGQFNDSVMQDVHLRVRGIDYSIPKTVFPSTSAITYWQIEAKNSMFPGGFLQWETPVRFQHMITQLYLTVKKDGKYTLTLTDDRNDTGTVFKLYPVVKKNEPIPKGSYCRIKHVITGYWMQALQGVSFILRRKTDLHQHNAIPEEVPRETLVQ... | Function: Receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 957
Domain: The receptor contains a calcium channel in its C-terminal extremity. Its large N-terminal cytoplasmic region has t... |
A0A674EJ90 | MSGKVCSNNSVMQARRTVEQLRVEASMERIKISTAAAQLVQYCQEHSRSDPLLTGISASSNPFKDKKTCVLL | Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Subcellular Location: Cell membrane
Sequ... |
R7TYG3 | MSLSSSNFPTICIILVGCHLSGLNGESPFTTIASKAELYSLPALTFGYADLEPFFDEATLHAHYDGHHETYRKKMNSALSEWRESDPLDSFSTEPILEILKNLNKVPENFRNAIKNSGGGFVNHALYWACMSPNPTREIRQPTGALLQDIENEFGSFVKFSLKFTDRAVSLFGSGYVWLSRNPSSGALIITTTVNQDSPISDGLHPILVIDVWEHSYYLKHQFRRHVYVADWWKVVDWENVEELDKWWREVGSYARDEL | Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
EC: 1.15.1.1
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Length: 259
Sequence Mass (Da): 29539
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A0A6V8Q2L6 | MANNSSRTSSWAEYLVVIAIAVALAFFIRTFIAQPFLVDKESMHPTLLEGNYIIINKFIYYFSRPQKGDIVVFYSPQEQAHLIKRVIGSEGDKIEILQDGQVVLNGRLLEEPYASYASYGVDAESGAITLGPGEYFVMGDNRGNSLDSRWFGPIKESSIKGRAFVLLWPFSRFRFLQ | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 177
Sequence Mass (Da): 20002
Location Topology: Single-pass type II membrane protein
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A0A378YXB0 | MASTLNPNLLLAIPLAPLVGSVIAGLFGKQVGRAGAHTVTILGVLVAFVLSVMTFIDVMNGASFNATVYEWARIGDLKLEIGFLVDTLTVTMMCVVTSVSLMVHIYTIGYMAEDPGYQRFFSYISLFTFSMLMLVMSNNFLQLFFGWEAVGLVSYLLIGFWYTRPTAIYANMKAFLVNRVGDFGFLLGIGLLLAFTGTLNYGEVFAKANEVAALSFPGTDWRLITVACICLFIGAMGKSAQFPLHVWLPDSMEGPTPISALIHAATMVTAGIFMVSRMSPLFELSDTALSFITIIGAITALFMGFLGMIQNDIKRVVAYS... | Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Subcellular Location: Membrane
Sequence Length: 683
Sequence Mass (Da): 74578
Location Topology: Multi-pass membrane protein
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A0A165RK72 | MKNSYSIKYYISFCFLILFLGSCSTSKSTSYSTKGNYKSNVTASYYHKKFNGKRTASGEKFHNSGMTAAHKSLPFNTKVKVTNTKNKKSVKVRINDRGPFTKGREIDLSRKAFMKIADHKGEGLLQVDIKVIK | Function: Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 133
Sequence Mass (Da): 15019
Location Topology: Lipid-anchor
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M1Q730 | MNLKDIWKQQLNFFNSKLYSYKTIKAIPSEWVEKTIILDPEVSRFSGRYSYDLSPYAREIIDNLHPSNPYKIISVMKGAQSGITQGVIVPGMAWIISEHPDNFLFTASDKEIAKLTITTRFDNIMQSSGLKHLIRPNTSRSKGQRSGDTDFSKEFAGGSAIIEGTNNAGKFRFFSVKTVFMDDFDNAPRADKKEGSIRKLVEGRQTSYGNLAKTFYVSTPTITQTSNVYEMYLQGDQRKWHWPCPECNEFVPSDWRIKKADGSFAGIVYELDSENRLIEESVFFKCPCCGHNISNNEKHDLNNKGKWIATAIPKDKYYRS... | Function: The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome from the concetamer to initiate and to end the packaging reaction. The terminase lies at a unique vertex of the procapsid and is composed... |
A0A5C2P0F2 | MKRLPQELHGRVLVTGAGVSGLGITALLKSLDVDVVVVDSGPDSLEKIQVKTGAEVCLDVDIQLQDFSCVITSPGWSPDTPLLVQAKDLGIEVLGDVELAYRLDRAEVCGKPRQWLVVTGTNGKTTTTAMLEAMIKRAGFKAQAVGNIGVPVAEALNAPERIDVFVAELSSFQLHWSEQLVPDVGILLNLADDHIDWHGSFDSYAAAKAKVLQAPIAIAGVDNEHVAQILSTTKTQKLVEFTAAEPRAGQLGIRNKMIVDCAFADSLEIVSAEGIEPAGPAGVYDALAAAAAARAMGVCADTIAAALADFHVAGHRGQIV... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-... |
A0A8S1C1C9 | MDRGISRYCERRFKDKKCLKLHHLKPNLNKFIITFDGKTEIHVKVLTATSEIMVNAIELNLKSVEFTPEGGVATPATVTLCVEEETAILSFAAPIEPCLGKLFFSFSGELNENLKGFYRSKYTSCENSKHTSAAVTFLCPTSARRMFPCFDEPSIKATFSISVLSDAPTILSNMPVASEEVRGDERLLKFERTPVMSTYLVAVVVGEFDFVEDTTRDGVKVRVYTPVGKKEQGKFALQVATEVMPYYTDYFEVKYPLPKIDLIAIADFAAGAMENWGLVTYRELCLLVDPDNTTTDRKQKIALTVGHELAHQWFGNLVTM... | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.11.-
Subcellular Location: Cell membrane
Sequence Length: 877
Sequence Mass (Da): 99537
Location Topology: Lipid-anchor
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A0A1I8J2I7 | MDPTSESLRVRRLRCPTVPCLLCLCPALLLLEQQILLGALALLCCALQLTQARALILASTGLGSVKDLRWALQLYRRLPLNAFSRLWGRCHQLPLPLFARSPAYRLYSKLCNCNLDEADFNDLREFRNLSEFFRRSLKPEVRPICPAARIVSPADGTVLHFGRVASGHVEQVKGVTYTLQGFLGPDPLGDNGSSECSTSPMERKLQDSEYHDHLKQNPENELYHCVIYLSPGDYHRFHSSVDWTVHKRRHFPGHLLSVAPRIAGMIRGLFCINERAVYMGSWRHGFFSYTAVGATNVGSISVFKDEELRTNRGGAGFQDR... | PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme... |
A0A150IMQ5 | MKELYDILFETKSIQIDTNNPFTFASGIKSPIYCDTRRLISYPKERKMILSGFLEKTSKLKIDCVIGVATGGVSWGAWLSDWLDVPFGYVRSSNKDYGKKQSIEGDIDVSKNILVIEDVVSTGGSIGRAINLLKQSSASSLNAFSIFSYQFSESLEMFQKLNVPFESLLTLEGLLEHSSDKIGDNKSEIQLWKKNHGSGEGND | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
EC: 2.4.2.10
Catalytic Activity: diphosphate + orotidi... |
A0A7R9BW88 | MFSGNVSYGKIFGIAVTAFVIIQQVSTSPTRYHRFKKGPTAPVNINPDEYSKEYWNKLAKNELDKSMKINAKLNVARAKNVIMFLGDGMSIPTTTAARILKGQLTKIDSTGEEASLVFEDFPHIALSKTYNVDFQVPDSAGTGTAYLTGVKANSGTVGVTAAVPRYDCNASNIEENQVDSFLQWAIDDGRNAGLVTTTRITHATPAAAYAHCANRDWECVGFEPWEGPETELPDHCKDIATQLVNGKTGKGLKVIFGGGRHAFDGTIKPTENDPKGSCVRNVKESLIEEWQELHKDEKAHYIEKKTELEKLDAKNVDRVL... | Cofactor: Binds 1 Mg(2+) ion.
EC: 3.1.3.1
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Length: 721
Sequence Mass (Da): 79031
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R7TTD3 | MMVNRRDDYSRRGRDRYDRRRRPSGDQFKGSLSEGLRNQDHSSSDEEITLDDDDDDEDEDAIIERRRKEREALLKKLGAETEDSMDVPSEAPGHSSPSSHSSSPRSEVADELEKSGFDFMESINTKRGTMQPDKDSKPFKNGLDMFADEIDTHQFNSPGTVQRGSSAFENPALTDNWDDAEGYYRVRVGEVLDKRYSVMGFTGQGVFSNVVRAQDTARGKQEAAIKIIRNNEMMHKTGLKELDYLKKLNDVDPDDKFHCLRLYRHFFHKNHLCLVFESLSMNLREVLKKYGRDVGLHIKAVRSYTQQLLLALKLMKKCNI... | Function: Has a role in pre-mRNA splicing. Phosphorylates SF2/ASF.
EC: 2.7.11.1
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Length: 516
Sequence Mass (Da): 59465
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R7V6P1 | MTSVAVHIRRGDFITRNLQRNGFAVASLGYLIRAMERFKKKDPNVFFVVASDDIKWARNHLTGIDVKFSVGLSAAEDFALLANCDHIIISSGSFGWWAAWLNGGMTIYYKGFPRKGSRLWSHTDIDQYYYPQWIGME | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 137
Sequence Mass (Da): 15672
Location Topology: Single-pass type II membrane protein
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A0A452DLS0 | MAFPGWWERFDIYRKVPKDLTQPTYTGAIISVCCCLFILFLFLSELTGFITTEIVNELYVDDPDKDSGGKIDVSLNISLPNLHCELVGLDIQDEMGRHEVGHIDNSMKIPLNNGVGCRFEGQFSINKVPGNFHVSTHSATAQPQNPDMTHVIHKLSFGDTLQVHNVHGAFNALGGADRLTSNPLASHDYILKIVPTVYEDKSGKQRYSYQYTVANKEYVAYSHTGRIIPAIWFRYDLSPITVKYTERRQPLYRFITTICAIIGGTFTVAGILDSCIFTASEAWKKIQLGKMH | Function: Plays a role in transport between endoplasmic reticulum and Golgi.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 292
Sequence Mass (Da): 32827
Location Topology: Multi-pass membrane protein
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A0A7R9BJM0 | MGGLGQESAGIVTSDGSEAELKLHKGHGLVSSIFSEDLLYKLQGNLGIGHTRYSTVGGHQDNSNVQPFVVHTQEGPVAVAHNGELVNAKSLRKLVYSKGVGLARNLGIGHTRYSTVGGHQDNSNVQPFVVHTQEGPVAVAHNGELVNAKSLRKLVYSKGVGLASLSDSELITQLICLQPESSENNWPDRIKTLMHMSPISYSLVIMHNDAIYAVRDPYGNRPLSIGRILKNGSVSRSSSFLFKMHENPDSAPATNGNATPLSPDTEETEAWVVASESCAFRAVGAEFVREVAPGEMVEVSKYGLKSTFPLGDATPNPSSL... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2.
EC: 2.4.2.14
Catalytic Activity: 5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ri... |
A0A7R9BX21 | MLSEASVVNEKPVGVAPVKPKFHQPKLEKNVAMDYIPDEAKRKLHDAATDDDGGPPEKAAKLSRKERKKLFAGQNKNRPRPTSFARDKKPCPSIKCVTVDDEWVDCRYTGCAFLHDVKKYMDMKPSDIDDRCHVFYERGFCPSGLACRYGQCHIRETDGKNLINKDLQGKYKTEKNGIPEHLINSLRKRKHDFSKCEEVLKLYQENKDSFVDSARDADVKRVPWKSKPLYLAPLTTVGNLPFRRICKEFGADITCGEMALAKSLLNGRPDEWVLTKRHPTEDFFGVQICGSTANVLTKCVQVLVENLELDFIDLNMGCPI... | Catalytic Activity: 5,6-dihydrouridine(47) in tRNA + NAD(+) = H(+) + NADH + uridine(47) in tRNA
EC: 1.3.1.-
Subcellular Location: Nucleus
Sequence Length: 813
Sequence Mass (Da): 91959
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A0A1S3TGC7 | MVKVEKEKEKEDSYNSVELHLGVDASHSAPPEINHVITEAQRRELHHQVFIFNHLAYKLPPPHHRVQFPSNMSEYSFLGFDQGSRMVPEPHRCRRTDGKKWRCSKSVVPGQKYCERHMHRGRNRSRKPVETSQVNSSLAPKPCSKSPTKSASETLFEISNPNLIMAMQPSDTPSSIPSRSLSIDNCSSMNRSFMVFSSTFAASPGSGLASASAPKAAATLGNVASVAPDDKSYLKMCKKDNQSKSCVSNKGNRSDGKGSIVGDSNNISTGISFSPTSVLQVFGNNPSHLIDKTNIESAPDRCRRTDGKKWQCKSAVLPGQ... | Function: Transcription activator.
Subcellular Location: Nucleus
Sequence Length: 420
Domain: The QLQ domain and WRC domain may be involved in protein-protein interaction and DNA-binding, respectively.
Sequence Mass (Da): 45661
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A0A809XV57 | MKVLPLLVVAMGVVAWEATAQDAQCVRERAAMVEAIRAYARSAAGVLGQQGLSEKVLEAMAQTKRHLFIPEQSCSIAYADRPIPIGLGQTISQPYIVALMTQLAEVAPDHVVLEVGTGSGYQAAILAQLARKVCSIEIIPQLAETAAKTLRDLAYDNVSVRLGDGYDGWPECGPFDAVVVTAALGEPPPPLIEQLKVGGRLVMPVGPGYGTQQLTVVEKIAPGKTTTRGVVFVRFVPFTRSQN | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-m... |
A0A8J1LF58 | MRLVFFFGFSVCIVLGSVFVYYQPDHDAAMPFGCISGRNEKTYNCFSDITDKYEIGQLLCAKEFCEICLAREIQTDRLFICKKFLKKDGRKVRRAAKNEILILKMVNHPNILQLIDTFETKKEFYIIQELATGGDVFDWILEQGYYSEKDASNVIRQVLEAVSYLHSLHIVHRNLKLENLVYYNQKNHSKVVLRDFYLSCFESAEITEPCGTPEYLAPEVVSRHRYGRPVDCWAVGVVMYILLSGNPPFYDENEEENSENHNRKIFRKILAGEYEFDSPYWDVISAPAKDLVSRLMEIDQEQRITAQDALSHTWISGNAA... | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
... |
A0A2E7ZT56 | MIEAIRDAVSMMTGRITQQSIDEVLQLTDMTHVVGQVVKLIGRAPSMKGLCPFHNENTPSFTINTDQKVYYCHGCRAGGNAVQFVMETQSLSFKEAIEYMAQLVGFELRYEQFSESDQRRYQQERSRRGRLLECNEAANAWFIKNFHNPRLGREAKIYANRGRELSLSTLESFEVGFAPDSFDALNRYLQNQGFDADLIVQAGLSRPGRNGGLIDRFRNRLMYPIRNRLGDLVGFGGRALSADDNAKYLNSPDTWIGEPNQSRALYKKGDVVFGLDHVKRNIRRQPKGQRRVMLVEGNLDVMMLHQEGFDHAVCASGTKV... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
EC: 2.7.7.101
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Length: 645
Domain: Contains an N-termi... |
A0A8S2IRD2 | MRVSSVGKGLRQIPSPRSHFCEHISNDDEQSYTCRQRIYVTCPHCQRSLCLHHINEHQIIIRSLLDSLVNRVNEYRYELTVTLSIPSTSQTVVNNCLDELKDVIIPYVQRTCCQNDVKQEDVNRVQVFIDKMFTIIQHIHFYWENHKKEKRSRSTDKMWIIIFAAIVIFIFFVLLYLLRPVYRPECLLTLRDVHVVITGGSSGIGKELARQLLNEHQARVTILARNQQRLDECRQDLALGNNERLLCLSVDVGQSYADIEKAIQQACQYHGNRPVSILINNAGIFYARTFEETTTDDFEKMVRINYLGVVFCTKACLASM... | Pathway: Lipid metabolism; sphingolipid metabolism.
EC: 1.1.1.102
Catalytic Activity: NADP(+) + sphinganine = 3-oxosphinganine + H(+) + NADPH
Sequence Length: 486
Sequence Mass (Da): 55097
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Q6INU9 | MAFKELTSRAVLLYDEWIKDADPRVEDWPLMSSPILQTIIIGAYIYFVTSLGPKIMENRKPFALKEIMACYNLFMVLFSVYMCYEFLMSGWATGYSFRCDIVDYSRSPQALRMAWTCWLFYFSKFIELLDTVFFVLRKKNSQITFLHVYHHSIMPWTWWFGVKFAAGGLGTFHALVNCVVHVIMYSYYGLSALGPAYQKYLWWKKYMTSIQLTQFLMVTFHIGQFFFMENCPYQYPVFLYVIWSYGFVFLILFLNFWFHAYIKGQRLPKFIQNGDCKNNNQENAHCKNKNHKNGLLKSKNN | Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fa... |
A0A833E355 | MGIYVLHTSDTHLGYRQYGIVERENDVYDVFGEIIDIALREHVDLVVHSGDFFDSIRPPPQAILIAIRHLRRLREKGIPFITILGDHDTPKRRVLPPLVLLEELGYVRLVGVGEQRLAYTVKTRSGEVFVAGISNKRKTSSSVLKLMLKKLSNPPSSIPSILLLHQCIRGMCIDYELELGDIPIGYTYYALGHVHTYKEFEIGDGVAVYPGSPEVMRVDEFRAQSERYIVLTELGKGVAYRQKIRLQRVRPQYELVIDDIESMELKVKQFIADIVSRGRASKKPFVYVRVVGGEYNRSKILNVLERFLRRVVLDYRVYIE... | Cofactor: Binds 2 manganese ions per subunit.
Function: Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Mre11 binds to DSB ends and has both double-stra... |
A0A251UKY7 | MLYIIGLGLGDEKDITLRGLEAVKKSQKIYIESYTSLLSFGISEDGISTLEKLYGKALIVADREMVEEKVDDMLLEAREFDVAFLVVGDPFGATTHSDLVVRAKKMDVEVKVIYNASVMNAVGVCGLQLYRYGETVSLPFFTETWRPDSFYEKIQKNRGLGLHTLCLLDIRVKEPSLESLCRGKKQYEPPSFMTIGVAIDQLLEVEQLRGESAYNEDTLCVGFARLGSENQMVVAGSMKQLRTVDFGPPLHCLTIVGKTHPVEEEMLDFYRS | Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Function: S-adenosyl-L-methionine-dependent methyltransferase that catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester. The four successive ... |
A0A7R9BHF6 | MRNWILTHVLRLYFRMAGTHSRNTPSWTNTRLNDRNSPTPLISLPDDSEPPSIVLRSFWNNLKYEWNSKRSKFATGDEVHILGRKYRIPEDETVMRRDFASRIWLTYRRDMPCPLPHSNLRSDCGWGCMIRSGQMILAQTILTHLLGRDWRPGVMCEVHRSIISLFSDHFFLSPPTFGLHRLVSLGLRKGKQAGDWFGPTCIVHILKEAVETSVVPGLRIYVAQDCTVYLDDVDMLCRPRDRNDDTDVTEATEFLQESQCVLSARQASDFVMVTKSGPFEGIQAEELNEEPECDQNDPRRNDDWSTSLLLFVPLRLGTEK... | Function: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins.
Catalytic Activity: [protein]-C-terminal L-amino acid-glycyl-phosphatidylethanolamide + H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-glycero-3-phosphoeth... |
A0A2N7S184 | MPAANEERSQITTHILDTGTGRPASGVKAMLEAKSASGWQEIGSGSTDADGRIKNLGPVQVEAGHYRISFETGAYFGKQGTETFFPAVTIDFFVNDVAEHYHVPLLISPFAYSTYRGS | Function: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
EC: 3.5.2.17
Catalytic Activity: 5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+)
Sequence Length: 118
Sequence Mass (Da): 12729
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A0A5C2NVC1 | MHIVIIGAGAVGGYFGALLHETGTDVTFVARNESLHALRNRGLRIHTPEGLRDVPVQSVSSLSEIESADIVLLATKTLSAPELPESLPRGAVLVTTQNSVEMPQIAIDTFGPAAVIPGVVRSFLIKRGPAEVEFAGGIRSFTFGSVDPATQETVNELQKALAKAGIEPIVHPAVMEDIWAKAMFVTCFGALGALVDKPLGEIRTLYRADLRNLMQEVEEAGRALGIDLPSDIVETTLASLDRQSAQATSSMQRDLLDDLPSELDAQVGGVVRMAELGGREARMHRLILDVLLHR | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
EC: 1.1.1.169
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Length: 294
Sequen... |
R7TC67 | MVGPALDIAFEEAERDYGIKFIKVISLYPDDCNSVFTTGAIADMYYTQNISVLIGPGCSGDIIVCGKLATYFNLPQVTGVGDLVLGKINYPTLTRLSYSLEKQSDFVTAMLNYFEWNHVAIVYDYHDALMAVQGEALTSALREDSEFARPYSISFDTTKNPDLRSFLLEVVPHARVIFFLSSGDDLRRFMLEAESLGMTHGDYAFVTIELFPSEAWGDFSWERGDADDDRAKSAYEALLFVTLTTPSGPKWHNFVDDVKNRSASDYNYTYTGDVNYFVGAFYDGVKYLTLALNQTLEDGEDPYDGLRVAQKRWNTTFQGI... | Catalytic Activity: GTP = 3',5'-cyclic GMP + diphosphate
EC: 4.6.1.2
Subcellular Location: Membrane
Sequence Length: 993
Sequence Mass (Da): 111364
Location Topology: Single-pass type I membrane protein
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A0A1U8NR16 | MGIAGYSYSWFLLSFFALIPTLRAHIAEYDEYWKARELEAIENLNKAYHPNPEEVVRHYNDHFSRTMLEYNSTRRALKGKKKGPCEITNPVDSCWRCDPNWVKNRKRLADCAPGFARGTTGGKDGKFYVVTDPSDDSANPKPGTLRHAVTQLRPLWITFKKSMIIKLEQELIVTSDKTIDARGANVHICYGAGITVQFARNIIIHGLHIHHIKPTTGGIIRDAENHLGLRTASDGDGISLFGATNIWLDHLSLYDSSDGLIDVIQGSTAITISNCHFTDHNEVLLFGASDTYAADEKMQITVALNRFGKGLVDRMPRCRL... | Cofactor: Binds 1 Ca(2+) ion. Required for its activity.
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 2/5.
EC: 4.2.2.2
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at th... |
A0A5E6MUI0 | MYSMTTLTPRRTAILTFIRDRIAQQGQPPSLAEIAEAFGFASRSVARKHVLALTEAGFIEVNPNQARGIRLLNQPARPEWLDVPVLGRVAAGLPIGADAEVHSRLQLDPSTFAKTPDYLLRVQGDSMIEDGILDGDLVGVRRSAEALNGQIVVARLDGEVTIKRFERSGDSVRLLPRNPAYQPIVVGPDQDLAIEGVFCGLVRQG | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually ... |
R7T9M8 | MESICVSAPGKLILHGEHAVVYGKVALAASLNLRSFLKLTFTSDDSIEVFLPDIDIHASWKIKELQSLFSSPHFNGDVQSPQEANSDCLQLIRHFLSLSEDTHDTKPLALVAFVYLLGHITQKLSGMKVELRSSLPTGAGLGSSAAFSTCLAAGLLVASGSIKDSRLGWEEKELDLINKWAFQGEKVIHGRPSGIDNSVSTFGGALCFQGGKITPLEKVPKLDMMLVNTKVPRSTKILVAGLRERYEKYPDIYRPVIDSVEAISVKCEETLSHLNDVPNDPAMIQTLRDLIGLNHHHLNFLGVGHKSLDEVCSICTEHGL... | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 1/3.
Catalytic Activity: (R)-mevalonate + ATP = (R)-5-phosphomevalonate + ADP + H(+)
EC: 2.7.1.36
Subcellular Location: Cytoplasm
Sequence Length: 383
Sequence Mass (Da): 4145... |
K3ZU90 | MAKPSVGVSEVGVSAAPAQSACPCPGTLFPYPPPRGAGIAAAVRRKCLQVELGAGTGLLGGAWGVESMRASSPTHAKAAAALAAGVDDERAAWMVRHPSALGKFEQIVAASEGKRIVMFLDYDGTLSPIVDDPDAAFMSETMRMAVRSVAKHFPTAIVSGRCRDKVFEFVKLAELYYAGSHGMDIKGPAKASSRHAKAKAKGVLFQPASEFLPMIEEVHERLAETTRCIPGAKVENNKFCVSVHFRCVDEKMWGEVSEAVKGVLREYPKLRLTLGRMVLEVRPTIKWDKGKALEFLLESLGFADCTNVLPVYIGDDRTDE... | Pathway: Glycan biosynthesis; trehalose biosynthesis.
Function: Removes the phosphate from trehalose 6-phosphate to produce free trehalose.
EC: 3.1.3.12
Catalytic Activity: alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate
Sequence Length: 380
Sequence Mass (Da): 41459
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A0A7R9BUL3 | MRFTFLVILRIILLAAFGDASEDEERLVRDLFRGYNKLIRPVENMTQRVEVSFGLAFVQLINVVWNDYQLRWDEADYGGIGVLRLPPDKVWKPDIVLFNNADGNYEVRYKSNVLIFPNGEILWVPPAIYQSSCKIDVTYFPFDEQTCLMKFGSWTFNGDQVSLKLYNDKPYVDLSDYWKSGTWDIIEVPAYLNVYNSSIPTETDITFSITIRRKTLFYTVNLILPTALISFLCVLVFYLPAEAGEKVTLGISILLSLVVFLLLVSKILPPTSLVLPLIAKYLLFTGPRTHKMPTWIRVVFLKYLPLMLFMRRPKKTRLRW... | Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular Location: Cell membrane
Sequence Length: 390
Sequence Mass (Da): 44435
Location Topology: Multi-pass membran... |
H9A9I5 | MSHWYLMSLQYSGSLIMNMTLFVYELAMLMIILITSIIMYLMLTLFTNKFINRNLLHGNTIELIWTIIPILILFKLAIPSLKLLYMMDELLDPLTYTVKVIGHQWYWSYEYPEFNNFSFDSYMINNNEELNLFRLLDVDNRMVLPIFNPTRILITSSDVIHSWAIPSLGIKVDATPGRINQSNVVLLRYGLFFGQCSEICGANHSFMPIVIESTNSKFFHLWTHFMTK | Cofactor: Binds a copper A center.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreducta... |
K3YMY6 | MSTAFSDFGPLTERRRVEKQRQQRRRVMVAAGGASVVLILIVMGGAAVAYNASVQDDDASSSSTSSPSSPSGGGSGSSLLSVSKSVKMMCAQTDYRDACEKSLSKAVNASASSPKDIVRAAVAVIGDAVGKAFDRSALATGDDPRVKAAVADCKEIYQNAKDDLARTLRGIDAGGLDEVTRRGYELRVWLSAVIAHMETCIDGFPEGGLKKNMTSAMESGKELTSNALAIIEKASSFLAALHMTGAASHRRLFSIREEEHVEKQPKVNYSGTFHGERDDSPAPASRRLFSFTEEEDMEKQPKVNYSGTFHGERGDSPAPE... | Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
EC: 3.1.1.11
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Length: 669
Sequence Mass (Da): 73048
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A0A656AB32 | MQAAERAKKDLDLAQANASDQLKEAKRTATELIEQANKRKAQIIDEAREEAQAERQKILTQAEAEIEAERNRARDELRKQVATLAIAGAEKILERSIDKDTHKDILDNITAKL | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria.
Subcellular Location: Membrane
Sequence Length: 113
Sequence Mass (Da): 12732
Location Topology: Single-pass membrane p... |
A0A1B6FNA2 | CQTEVESGGPAGRVDKPVQTDGSVEQVSRHDRAVQTGDLQEEEEVHPRPLEECVAIYKEKGSAGSLCDAEVRALVRASYIPTYQIEKAVGDPERGVGIRRQIVGQSGDFTDALTQLPYRNYDYSKVLGACCENVIGYVPMPVGVAGPLLLDGRLVHVPLATTEGCLVASTNRGTRALLQCGVSSRVVADGMTRGPVVRFPSMTRASEAMLWMQTPENFQTMKDSFDSTSRYARLTKLHVRIAGRLLFIRFVATTGDAMGMNMLSKGTEMSLKTVQQHFSDMEVLSLSGNFCSDKKPAAVNWIEGRGKSVVCEAVVPGHIV... | Pathway: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3.
Catalytic Activity: (R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH
EC: 1.1.1.34
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 495
Sequence... |
A0A150ILN2 | MISDRVKIAFIGAGAIGSLFGGLLSKGGEDVLLIGRQPHIDAISKNGLFISGVEEFNVKIDSSSNPFDAIGSDLMIITTKAYDTRDALKDIVPILERDTIVMSLQNGAGNIEEISKFVEKQNILGSVTSMGAFIESPGKIQYRGKGKTFIGPYSEKNNCAKEVVKIFKKAGITAEYTNDIESEIWSKVIINSAINPLASIFDGENGILLDKNLLEIVREVTIEGKMILDNDGITIPDDIFEKTLEVIKNTSKNINSTLLDLRKGNKTEIDYITGKIVETGERLGIPAPFNKALLNILKFKENKLIQKS | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
EC: 1.1.1.169
Catalytic Activity: (R)-pantoate + NAD(+) = 2-dehydropantoate + H(+) + NADH
Sequence Length: 308
Sequence Mass (Da): 33668
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A0A7R9GJK8 | MKAHLLSLRRVRLRSTLLAVWSLIATLTSFWGIFGSRDENASSSSTCLPCHGITRESSVNTSMRLKGFQKSDPLETEPSFSCYSSKSSHPRKNQGKLPTIYVITPTYERPAQLADLTRMAQTLAHVAELFWVLVQDSREREPLVHDFLRYTNINYTYITGS | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: 3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP
EC: 2.4.1.135
Subcellular ... |
A0A2E7ZV60 | MHRVVFMGSPEFAVPALRRLCELSVQVVGVVSQPDRPAGRGRKMTPPAVAVHARSLGLDLFQPHKVRDGQLRQWLLERNPDLAVVAAYGRVLPAAVLDAPRLGCVNLHASLLPRWRGASPIQRAIAARDEQTGVCLMSMDEGLDTGDVYARRHINIAHDDTASSLSARLSALSAELLGYCLEDLLQSRLQAHAQSSEGVTYAPLLSKSEGAVPWHQSAEMVHAHVRAMTPWPGAWSTLITSNERWKFFAEELRTDPRSGVAGQVLAIEPGRVLIAADSGSVWFTELQRPGKRKMAASDALRGGHVGVGECFQ | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
EC: 2.1.2.9
Catalytic Acti... |
A0A2D5PY95 | MKPIETLKNELSEIADLKGAVNVLYWDMETYMPKGGTAARAKQVAMLEAIVHERFIGEDVSNPLGELVNLDSGEIINGLDEETSRLVNEIWRDYHRAVALPKEFVEELSHTSSMAHPNWVEAREKNDFNLFAPHLEKLIALKHREIGYLDTQDTPYDTLLDEFEPGFTTANINVLFGELKTALVPMIKKIQESGVNTKQEILHQYYDADKQWEFSEMILKDIGYDFHCGRQDKAVHPFTIEFHPTDVRVTTRINEHNLLDCLTGSIHEGGHALYEQGLDQKWYGTPFCQAISYGIHESQSRLWENLVGLSKPFWEYYFPK... | Cofactor: Binds 1 zinc ion per subunit.
Function: Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues.
EC: 3.4.17.19
Catalytic Activity: Release of a C-terminal amino acid with broad specificity, except for -Pro.
Sequence Le... |
A0A251TNH7 | MGTLNHLQMVGFNSHVELGSIEGKPIMEPQDEGHSGSVSTKRNMFPVKAVVEFWGKKYIWSTVITSIKIAFLSDKINLLIPFGPLAILVDYFTGHHGWVFFLSLLGIIPLAERLGWATEQLAFYTGPTVGGLLNATFGNATELIISMYAMKHGMLRVVQQSLLGSILSNMLLVLGCAFFCGGIVHPNKQQVFNKSNAVMSSGLLLMAVMGLLFPAVLHFTHTELHFGKSELALSRFSSCIMLVAYCGYIFFQLTSQRNNSYTPIMEETNPDDGGSDDEESPDISKYESVIWLSILTLVISVLSEYLVNTIEGASVAMNIP... | Function: Vacuolar cation/proton exchanger (CAX). Translocates Ca(2+) and other metal ions into vacuoles using the proton gradient formed by H(+)-ATPase and H(+)-pyrophosphatase.
Subcellular Location: Membrane
Sequence Length: 443
Sequence Mass (Da): 48480
Location Topology: Multi-pass membrane protein
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A0A482WQH4 | MRRFTTVLKYFRRGINTSRRVESDECHHRTGGVIGINLPFDIHNETRFTVLTTIFLITGLGLMPFVVHRQLKKQNSVSDDK | Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Membrane
Sequence Length: 81
Sequence Mass (Da): 9417
Location Topology: Single-pass membrane protein
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A0A7C7CBA6 | MKQSLLITALLGILGTLPMTAQATPAEDVQTYRDFFMKRFPGVPLEEFANGVYSIDQVSRDSWEAIEEFPPYEPSIEDGEAMWNKAFANGKSYSSCFPDGPAIMGKYPHWDDGKGMVMTLPLAVNNCRTANGEKPLKYAKGSINKLLSYIGYESRGQVTNVGIPNAAALAAYEDGKQFYFARRGQLNMSCSHCHMQQSGRHLRTDVLSPALGHTTGFPVYRSKWGGQGTLHRRYKGCNKQVRAKPFKPQGEEYRNLEYFMTHMNNGIAINSPSARK | Cofactor: Binds 1 heme group per subunit.
Function: C-type monoheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosu... |
A0A7R9BIG2 | MELLALLFTIVLVSGLSVSLVDPKHYLLRYKIPIHTQVDIDPARYLCHRCNLLRQREDVKHCHECGKCVDGFDHHCYALNHCIGARNYWIMMLLFNNGLLLTTALLIAAVAFIYGVLARSRIMIPQFAQSKTDLASDKLICFGSPCLALIPLIVVIVYVIPTVLVLFSFGALVGAHWSLVAENSTTWQHFKERKSTPEKGKSLIMRQEIES | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 211
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 23822
Location Topology: Multi-pass membrane protein
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A0A1I8HF76 | MYIILQYLGACLFIFITFFFVIIPMLPNAWQYRTKMSVYYMLLLIYGFITTVLALATPRQLSNYKYPMATLAFTRWLYGLRYRVNNLARLRQLQGSYVLVSNHQSSIDLMGVGLLWPYQCTIVAKKSLMFAGWFGLAAWLCGCVFVSRGRQSAQAEMRRLAARMARQDDTVRVWIFPEGTRVSGADLGDFKKGAFHLAVQAQVPVVPIVFSNYSSFYSKRSGLFQQGEVEATVLEPLPTAGLTEADVADLTKRVRDAMSAEYSRLSAASDCKAD | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
EC: 2.3.1.51
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Sequence Length: 274
Domain: The HXXXXD motif is essential for acyltran... |
A0A496STV3 | MAVIPVEKLEESGANPYEIVIAAAKRAKMLGELKGEPETNESDEKEEKPAIQALKELAEGKIKCVYLAEKRK | Function: Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 72
Sequence Mass (Da): 7955
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A0A966AC01 | MARKSLRQRYPHQFLDGGIVVWKPRGPSSRRVVDIVQRRLSLRGLGHCGTLDPLASGIMVLTGGMGSKFQQWLTVHDKVYEATVWFGVGSESGDAEGPLSFSAESISLPTQSDIEAILPQFIGEQMQVPPTHSAVRVDGQRAYKKARAGDMTPLKARPVRIEKLRILEWDGARCRIEVSCGPGTYIRSLAHDLGEALGVPATLMALRRTSCGVHSTEDAFRVDRVTREHWWTLERLVSHLPAMAVSTDVALKMGQGQSVEVTEAEGSEVKVIEDAAGDEDAAGDEDAAGDRVIYSNGKVQGIAVLNDNLLKPRRWLSRGQ... | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
EC: 5.4.99.25
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Length: 326
Sequence Mass (Da): 35706
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A0A0C4DL69 | MMAHQPPLKAAILIVSTTAAQDPTQTDDGLEEKEVEILAQGVKEGENIREVGSDISKGTVILAAGEQISAVGGELGSLAAVGVGEVKVYRRPTVALLSTGDEVVEHDRPGDLRLGEVRDTNRLTLISAARQHGYEVVDLGIASDKQGALEEKLRLALSRADVVITTGGVSMGELDLLKPTIERSLGGTIHFGRVAMKPGKPTTFATVPVKDESLGVRTPRVVFSLPGNPASALVTFHLFVLPSLHRLSGVQPAGLPKVTVTLSHEFPLDKARPEYHRAIVTVDRDGCLVASSTGGQRSSKVGSLRGANGLVCLPKGSESL... | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released.
Catalytic Activity: ATP + H(+) + molybdopterin ... |
A0A8J8BQ00 | MKRVRYALAFLTRIPVKGGTLEETAEASYVFPLIGLCVGCASFAFSWCAHRVFPYTLAGVFTLGFLMVLTGLHHTDGLLDMGDALLVTGTREKKIDVMHDHFIGIGGFFLAFFVLLTTVFCIVEFMALNSLFVGLIGSEVSAKFSMNCIAFFGTPSHEGMGSRVIQATDRKLFLKSCLISGIVLSVFLEVGALLFVSTLVFAYLLAVGAERNLGGIGGDFIGAAHDTTRMMSMILLIVVMR | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-riba... |
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Heavily deduplicated version of Trembl (November 2023) with dense Natural Language protein descriptions.
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