ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A7C5RY21 | MNIFFNLFKIVFLLFLLFTLPEIVFCQLQSEAIILDGLHKFSAGDKIEWAKTEFDDSKWGKIKVPESWQSQKVKSDKGMGWYRIHLNITDRFKNIEPAILLGRIGDIDEVYFNGKKIGGLGIIGNRYVEASKIQRLYKIPENLIKYNSENIICIRVMNTYLNGGLFDENIAFGDYKILLIEKMKREKFTLAIEYSLFTFFLMFFIGCLFFYLKGLREREYLFFWLFVTLYGIIFTLNSVSFYNTGLKNNLVQQIISSISILLPAILLMVLKNVFKEKLTKFIKSLLLIFVLLSLTIFFFPYYEIRQIVYAIWKLCFAIIA... | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and tr... |
A0A8J1TSB5 | MKGDARANDGVKINVIVAMMDHNNGIGINNQLPWPKIRTDYEYYTGLTQRVTKPGNVCINMKGRLTFESSGEQERMNPLRHNVVISSTLKECPKGVGFIAPSFDAAIEYASEYANAESIWVMGGYSVYKRALQSPLCHRVHLTRIFHKAEADAFFPIDCLEPSIYKKIDLPEVPSDLIKENGVEYQFEVYERR | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH
Sequence Length: 193
Sequence Mass (Da): 21906
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A0A8J1XSN3 | MLMLLLLVFCGVISETVWAVHILLIPYTQGTNSRLMNMEKLADILIQDGHSVSLMINNRYDEENRPISKDVKIYKFKIPDDAWLVTDDAVVAKAHNTSFIEMASLVKHLTISYCEALLKSGILHELKKIKFDLVLVDYVEECARLSIDYLDIATVTYSNEGGLVNTYFGHLNHPAPWSFVTPFVVGFPDDMRFSERVQSTLINSVIQYVYYTMLLDMDTLRIKYKVNASLSTMNTLSRKTSLHFSNNHFVLDYPRPVMPNHVNIGGMYFQPPNPLSGHIDNIVKNASPGGVIIVSFGSIFNPTHGTLEYVTEQMASAFAG... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 527
Sequence Mass (Da): 60103
Location Topology: Single-pass membrane protein
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A0A7C8JEY0 | MSALLRPTVLASRRLALPAASRTLASKATKSKKTPAHPPSAPPTPAKGGPPAVAAEPPTDATTSAYSPSHTVIPEEHIPADVIPAGAVSGAPLDLQSRTVRIYKPTKNAMQSSNHRGGLWRMDWDVMAKGHRWENPLMGWQSSADYLQGTHLKFRTKEDAIYFAEKQGYNYSVQEPKERVIVSKAYASNFAWSEKKLKKIHTK | 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.
... |
A0A1L5YAY6 | MSVPSWLYHRILQHGGNIPFHQYVDWVLHDQDYGAYGAGSLQIGLKGDFVTSPSLGSSFAYLLALQMEQWLNSFGEEPLSLIETGPGEGHLALQLAQILYNNAPNFRNRLEIILIEPNKGMSQRQKNYLAKSPLPLRWSSLEQLSRNPVKGIILAHEVIDAFAVERLTYYKNDWYRQRVALIPDRMNKKEGKLMLIRGERWDYCIPNAEGLGLHKKNTFPMKSGWCTELHTETLQWLNSCKKSLSQGYLLVIDYFIEASHYYSARYSQGTIMTYKDQIARIDPLQDPGKLDITCHICLETLLSAAAKGGWSFIGQALQGE... | Function: Arginine methyltransferase involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I).
Catalytic Activity: L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine
EC: 2.1.1.320
Subce... |
A0A0R3TM44 | MIHGNFDLKQINNCVEKTYQKIQCKQDSLNNQLASSSKYLDDALKKLCALKASLNAIELGSQPRQENKTLREYLKALKKSLSSMMKGFESQMKGEVNCPLKDSLLRYTHLFHHLLFGDSANLIAVFGRIIFHPGYLKLGTYNSSFDTLASCKRPGSYIFRISSSKSGFWSVAYVSSNLEILQAMSYDWLIIFSINYGHQQGLYLYPRGQDSIDDFSDLCKQIAPSIQNPSGETCRKCFKNSANTRMEPCGHSCCRACYKEILSTSGPPGQPTEDNGGYRHAGEVSSDNDNEAFKAAQANKGETKEFINAVEKITNIGGCE... | Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conju... |
A0A0N4WIG3 | MTVSYNLDISSVSAFSFLRLLFRWRGSIWKSMSTELFIWLCGYYIVFFVYRNLLTIDNQRQFEKVAMYCESKLSYIPLTFMLGFFVTIVVDRWRNIFVNMGWIENLALTVATLLRGDSKEAVLYRRSIIRYAVLCQVLVFRDVSMRVRRRFPNMESIVVAGFLHENELRDLENIKMVYNKYWAPFNWALTICTRAYKEGCIENIPAMVAIQNEVKLFRTSLAQLCHFDWVPIPIAYPQVLFFAYSLYFCTQISRTTIELLSSGKMPLNAELKALSQVVFLAVRVYFVICTVSRQFILSADAKNRSALFRVAKPEEHVKMV... | Function: Forms chloride channels.
Subcellular Location: Cell membrane
Sequence Length: 436
Sequence Mass (Da): 50194
Location Topology: Multi-pass membrane protein
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A0A8D0S0V7 | MQFLLSNARWSGWPDASTELAGGAVAPGPTLNVAITLSLVERLVSPGRTCAEASFRYPRPLPAPLCLLCPGSSSPATVPHPLKMYACARFVSTPALIRRTSPLLSRSLSAVVLKRPEALTDESHSSLAAPRLLTTSLIPSRSFQTSAISRDIDTAAKFIGAGAATVGVAGSGAGIGTVFGSLIIGYARNPSLKQQLFSYAILGFALSEAMGLFCLMVAFLILFAM | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramemb... |
A0A1V3WP35 | MKTSYRTAVHDGIRDALSNDPHVVLMGEDVGRYGGTYAASKGLLEEFGPDRVRDTPLSELGFVGIGIGAALNGLRPIVEVMTVNFSLLALDQIVNTAAALRHMSGGQFSVPIVVRMATGAGRQLAAQHSHSLEPWYAHIPGIKVVAPATIEDAYGMLAPRWPTPTR | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
EC: 1.2.4.1
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltran... |
A0A7C4WGW4 | MDVLDDLYTYAVNSLATSVYTVVRRRCANIGLDDVLAIVEEPARRDYGDLSLPLYRLSRMCGFSLNELEIALNELQLNELFSRFQVVNGYLNAFLDEVNYARLLAEVVRNKGGRYGYVENEKKLNVIVEFVSANPVHPLHIGSGRNAVLGDFLSRVFEVRGHRVQRRYYINDLGRQVAVLVYGYIKLGRPKIPDNVKPDEWLGFIYAVTNTVIDIIELKKEILNAGMDRDVIMAKQSELDELMAILSELRSRDEAVVDRLLDSIAEDADPGKSVEELMARYERGDPDVKEVFRYVVNMVLTGINLTLNRLGITFDKWDWE... | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
EC: 6.1.1.19
Subcellular Location: Cytoplasm
Sequence Length: 647
Sequence Mass (Da): 73997
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A0A0N4WN39 | MSLGKLSIDKVDVKGKRVLIRVDFNVPQKDGKITNNQRIVAALPSIKYCLDNGAKAVVLMSHLGRPDGKKNPKFTLAPVADELKKVLGKDVKFLNDCVGPEVEAACADPAPGSVILLENLRFYIEEEGKCTNEKGEKIKAKDEDVEKFRASLTKLGDIYVNDAFGTAHRAHSSMVGVKLDTRACGFLMKNELVYFGKALSDPSRPFLAILGGAKVADKIQLIKNMLDKVNEMIIGGGMAFTFLKVDKNVEIGNSLFDEEGAKIVKDLLAKAKEKNVQIHLPVDFVIGDKFAEDATAKTVTMEEGIPAGHMGLDVGPKSEE... | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
EC: 2.7.2.3
Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Length: 821
Sequence Mass (Da): 88131
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A0A894JJ27 | NWLVPMMIGSPDMAFPRMNNMSFWLLPPSLMLLLLSSTIEMGCGTGWTVYPPLASNLSHNGAAVDMAIFSLHLAGASSILGAVNFISTIFNMRSNNFSMSTLPLFVWSILITTVLLLLALPVLAGAITMLLTDRNFNTSFFDPVGGGDPILFQHLF | 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... |
A0A8J1TQP1 | MSEDYNNKVLKFLFRYIMGDLPALTDWLKTKPWVLAVPSWILRAIGAPIFLNNPISGLLILIGMFIANPWVAICGITGLISAIATAFLLGQDHGAISNGGCTFHGMLVGIVVSASIDKPDWYPWTVFPVVFLAMLSVYVNSGLGGIFSSWNIPAFNLPFCLVAFVFLAALPPNNPNFPPRIKAAPNETFAQASIDWGQIFLAIPCSCAQIYGSNQAIVGVLILLGLLIGSPILFLHAILGPFMSVFTALCVAAPPEQIYTGEWSYNAMLAATSLGGFFWVLSIQTHILALSAAIFSTIVYGAMFNTFSNNNIGGLVLAFP... | Catalytic Activity: urea(in) = urea(out)
Subcellular Location: Cell membrane
Sequence Length: 372
Sequence Mass (Da): 40309
Location Topology: Multi-pass membrane protein
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A0A099J2F9 | MSTLSLVTLAQTASPRRVRLTLVAVVVVVFAMSVATLLVSRNAEFISAWWPAAGVSVIAVLLARRNRVGMALAIWAAASGARLAVGQPLAPALAYGFANALEAWLIARILEGSDAPHSLDDVRSVGRFVIAVAIGALTMAGLAALIIGVQGGDAPGTFALVAPSHASAILVIAPFLMVARVRVPARLRTELIVQSGLLAIVLALVFLPGQSSQWKFLTLPVLIWAALRFGSWPATGQMLALALTATAIVDLRQAGAVGEPGPGSIAQEYAVLQSYFVVYAASLLVIAAGRTERLRLADEMLMRDRLLRGGIVGSQIGLLL... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 690
Sequence Mass (Da): 72347
Location Topology: Multi-pass membrane protein
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A0A8J1XRE3 | MDQGFVEAIGASLIREYLSRKGFKQTLAMLDNESPRSEQSISNRPTLMKELHLEKLMKRNKEEGQPFRTMIEVMTKHFLEQVNERHSRTSSAALENNKTKPVSPKKEYHGDIIVDDDVEGETLLGDGKSGLMDQQIPDRPMSSRSNRSRGMSGPITSSLDPRDKRLRSAKKKHVGPGTLHGPMKDVLRSEDSASPSPVNTPERQHSAGATRKEPNHLSIDLKPLTAALEEEPQRKPSASRRRTSNSEIPVDPPETSVVSKPQEKPKNITPSEFRGDKKTSFEDSLKKLKENRTKRRDKEKVEIVTPQSEATQGVMPRPST... | Function: Hydrolase that can remove 'Lys-48'-linked conjugated ubiquitin from proteins.
EC: 3.4.19.12
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting... |
S5X650 | TLYFIFGIWAGMVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTTHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSITLLISSSIVENGIGTGWTIYPPLSSNIAHSASSVDLAIFSLHLAGISSILGAINFITTIINMRLNNLSFDQMPLFVWAVGITAFLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF | 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... |
A0A0R3TIJ8 | VDWIVQFDPPDDPKDYIHRVGRTARAGKSGSALLILRPHELGFLDVLRSSRVTPVEYEVASNKVADVQSALEKLISTNYLLASSAHEAFKGIVRSYNSSKLACFNVNELDLSALAKTCGLTVIPKVDLGVEPSKKLDAKRMKRKAFGAAAASSFQTKKRKIYQKIN | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 166
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 18277
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A0A8J1T4H3 | MANVPNQSTLAFFEVLGIFLGLSGCLLLKVTHVQNGPYMDEIFHIGQVTKYCKGLFEEWDPKITTLPGLYLLSSSLMQSLSWFFGYRVADLCTVFWLRGINVILATGNFCLLFALLRKLHGGNKGLSSTWYLLNTATLATFPVLYFCTFLYYTDTGSTFFTLAMYLMHLHGNSKMAAGVGIAAILFRQTNIIWVIFVAGLTVEKVINDYIQPEKKEITQEDIQNPKYIGIILLRIKNDLQNNRTGITQLIMNLIKAVWMYIIVGLGFTTFVIINNGIVVGDRNNHEACLHFPQIFYFCCVVVGFSIPHFLNAQTILGFLK... | Catalytic Activity: a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodoli... |
A0A1L5YCJ0 | MELTYRPRRLRRTSALRQMVRQFHLSPLDFIYPLFIHEGAESEPIEAMPGINRWNLDGLMKHVGVVWELGIRCIVLFPKIKDDLKSEDGIECCNEGGLIPRTIKHIKQEYPEMMIMTDVALDPYSSDGHDGIVNQAGLVLNDETVSILCRQAIVQARAGADLIGPSDMMDGRVGAIRKALDQEGFQDVGIISYTAKYSSAYYGPFREALDSAPRIGSTKKIPKDKSTYQMDPGNAREAITEAHLDQQEGADILMVKPGLAYLDIISQLRKQVNLPIAAYNVSGEYSMVKAAAQRGWIDEKSVVLETLLCFKRAGADLILT... | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
Function: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensat... |
A0A2Z4WX88 | GTLYFIFGIWSGLMGTSMSLIIRMELSHPGMLIGNDQIYNSIVTAHAFLMIFFMVMPMMMGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLLFLLISSFTDYGAGTGWTIYPPLSSNISHLGSSVDLAIFSLHLAGISSTLGAINFISSIINMRPKGMELEQMSLFSWSVFITAFLLLLALPVLAGAITMLLSDRNFNTSFFDPAGGGDPILYQHLFW | 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... |
A0A0N4VVY7 | MRFKEEEMVTGEERVISVMDLSQMTSIRKEDVISTLQHLNLYKYYRGQYVIVITDELKNAYRRMCEKITVRIDPSKLRWQPKDWSRRKL | Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
EC: 2.3.1.48
Subcellular Location: Nucleus
Sequence Length: 89
Sequence Mass (Da): 10872
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A0A349CJ13 | MIKPGPLEIGLVLVIILIVFGVGKLPQVGAALGKSINAFKKGTKGEDEEEQAAQAKTKKKAKKKKATNKKASQATEGASEGETKPAAEETPAKQA | 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. TatA could form the protein-conducting channel of the Tat system.
Subcellular Location: Cell membrane
Sequence Length: 95
Sequenc... |
A0A1L5YCY6 | MRLAKTRAALAINSLVCSIISLNNLMDLRLALVSAPILLALGWAGFNIGRAAVGQLQLMIKRSRR | Function: Manganese-binding polypeptide with L-arginine metabolizing enzyme activity. Component of the core of photosystem II.
Subcellular Location: Cellular thylakoid membrane
Sequence Length: 65
Sequence Mass (Da): 7046
Location Topology: Single-pass membrane protein
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A0A7C4WIF1 | MVKCSSIRRLSGGKTVKVDLEVFDEEIKEIVISGDFFLYPEEYIHTIESELRGRKISEVTKILNTFKDRVEVVGASIEEFAEAISDAYNSCVSG | Pathway: Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2.
EC: 6.3.1.20
Catalytic Activity: (R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + AMP + diphosphate + H(+)
Sequence Length: 94
Sequence M... |
A0A4X1U4N8 | MGLFDRGVQMLLTTVGAFAAFSLMTIAVGTDYWLYSRGVCKTKSVSENETSKKNEEVMTHSGLWRTCCLEGNFKGLCKQIDHFPEDADYEADTAEYFLRAVRASSIFPILSVILLFMGGLCIAASEFYKTRHNIILSAGIFFVSAGLSNIIGIIVYISANAGDPSKSDSKKNSYSYGWSFYFGALSFIIAEMVGVLAVHMFIDRHKQLRATARATDYLQASAITRIPSYRYRYQRRSRSSSRSTEPSHSRDASPVGIKGFNPLPSTEISMYTLSRDPLKAATTPTATYNSDRDNSFLQVHNCIQKENKDSLHSNTANRRT... | Function: Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization. Does not show subunit-specific AMPA receptor ... |
T1FNW6 | MKNIEPGSHCTISVVEDPLHEGEYFFEGTEKLLEIWFSPSSPSSASGSVQGGRASLRDINRSEWELLLKNVNCEILSSRHSTTMDAYLLSESSMFVSKDRIILKTCGKTTLLEAVKPLLGLAKEQCGFDNIVDVFYSHKNYLRPDLQPETYRHFDQEVAMLDTLFEDGAAYVLGKLNKDCWYIYTLDRFNITEPDQTLEIMMMDVNQDVMNMFTQSYGLTASQLTEKTGILDILPGAIIDDWLFEPCGYSMNALLPNGRYFTIHITPEDEFSYVSFETNVPRDSYNDLITKVTDIFQPNKFIVTLMANEASPAYKLCLKM... | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Pathway: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
EC: 4.1.1.50
Catalytic Activity: H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine
Seq... |
T1G001 | MKRQGNRDVVGYGHNGQAVYEDRPEFPAPAIRFKENSKEVLALREKEKGDWKNLTLQDKKALYRASFCQTYAEMDAPTGNWKQVMAIVLAGMTLTLWINYFIKKFVVNDLPHTITREWQEKQLENMIKQRIGHIDGLSSKWDYENNRWK | 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.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 149
Sequence Mass (Da): 17565
Location Topolog... |
A0A220DNB1 | SQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAITQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLL | 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... |
A0A0F5LWT9 | MNACAGSPLGALVLVVGPSGVGKDTLISGARTALEADKRFVFVRRVVTRRADIELEDHDSMDHQQFAALEAAGRFALSWDAHGLRYGLPLSVDTDIALGRVVVANVSRHVIAEARAKYPACAVVMICAEISLRAERLTRRGRESRDQITARLARESAPVPAGIDPIIIDNSGSLAIGVTAFVMALRKIADE | Pathway: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route II): step 3/3.
Function: Catalyzes the phosphorylation of ribose 1,5-bisphosphate to 5-phospho-D-ribosyl alpha-1-diphosphate (PRPP).
EC: 2.7.4.23
Cat... |
A0A1S3AV32 | MDFSHIFLFFLFFFPTLITAQSCSVSKCINDDFAIRFPFRIPDQQPARCGYPGFNLACNKAGVTTVNLSASEYFLVRGIDYATQQIQLYDSDDCLPRRFLQGLNKLNFSNSPFIPLFSQNITFLSCPPQFTMSHFPIIGCLSNSTNSILATSSTSFVKSMSTSCTIMTTLPVPVSNPDETNQFSTNLNGDLVLTWYSPACGICETEGRLCGYKSNSGQGIACFDKYTSEENNGLRVLRIICVVILLPTLMCVIGLGCFICMAKWSYSLTDGRGNQVQHRQQVNPAGSDLEAPSRLSGLNESTIESYQKVILGESRRLPGP... | 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: Membrane
Sequence Length: ... |
T1EF37 | MATCAVLGGGISGLATAYYLNKFGGNLVKKIILIEGTNRFGGWMRSVKYEKDLLFEQGPRSIRGVGRAGFNTLEMVEDLELDDEVLPIPRSHVAAKNRFIYVNKQLCKLPSSLKAVLTTQPPFSKPLCLYGLMEPFRKKGELDDETVDSFFSRRFGPEVAKYAANSMCRGIFAGDSLKLSMRSCFPLFHEFESKYGSIVKAALMRPRTKRRENSELINKFVSENWSMWSLKNGLEDLPRKLLATLQKEDKVKVMSGSKVNTLQFDDVKVKLVTSANGEIMTVDHVFSALPSFDISLLLLPTYANISSLLNDIRFASVGVV... | Cofactor: Binds 1 FAD per subunit.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
Function: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
EC: 1.3.3.4
Subcellular Location: Mitochondrion i... |
L1JHI4 | MESDTRRDILPANILPHLDLVANFRLHGDIPNTLETIHQDIDIGTPRLIEKSGKIIHHVTVTYTPGNLEMYRLQEKQQRSRKMFAAYLVSNCGRPRDAFIARLMSALGDDRLHSYGRCMNNRKFPEEKEHGSNSLSLLKMYKFTIAIENYLSHDYVSERFYQPLLAGSVPVYLGAPNIEEFAPGVNSFIDIRNFPSPEALASYLISLADNHTAYDSFFTWKLDGPSPEFLRMMNMSMTRGNVISFLVVVLRVLTAFFYPQVDLNRLHTSMCKKLVALTRREMKCGA | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 286
Sequence Mass (Da): 32712
Location Topology: Single-pass type II membrane protein
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A0A183P353 | MPFKLNTLNALSWCEFVKLANKSPDPSIRDIFAKHLMQIPGCTGPKITSIMEKYPTPCILMDAYDKQPTMSGKSNMLAQLKPADSNRCIGTALSQSIAFAFNTL | Function: Interacts with EME1 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of st... |
A0A8J7YIY1 | MVYQLGADEAGRGPVIGPMVLCALLGDTEKLVSIGVRDSKQLSEERRNAIFRSLGSISSWRISVVWPEEIDMAVAHSSLNRLELLHFASLIRHFDSEVAFVDAPDVDCKRFSAEMCRITGRKVVAEHRADIRYPAVSAASIVAKVTRDRIISEIAEELGEDIGSGYPGDSATIDFISSYVRKNGVLPPYCRRSWETSKRIISFIRIKNLNEFG | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Subce... |
M5C4C8 | MATDFCPVYAPFFSALGCTSAIVFTCIGASYGTAKSGVGISAMSVIRPDLMMKCVVPVIMAGIIAIYGLVVSVLISGEMQPRMALFTGFIQLGAGLSVGLAGLAAGFAIGIVGDAGVRGTAQQPRLFVGMILILIFAEVLGLYGLIVALIMNTSGKVDDINKLCPLPSV | Function: Proton-conducting pore forming of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular com... |
Q5U3T2 | MAPVPPGIRFLASFNRDQWYKAFTFALTFLLYTSFHLSRKPISIVKSELHKNCSHAVEAPTEISSSSQQPGHHPEFDCSWKPFDRNNYKQLLGAMDYSFLFAYAIGMFLSGIIGERLPIRLYLTVGMLTSGLFTCLFGLGYIYDIHSLGFYIFVQVANGLVQTTGWPSVVTCIGNWFGKGRRGLIMGLWNSHTSVGNILGSLIAGYYVSSNWGLSFIVPGVIIAAMGVICFFFLIEHPNDLKTASTQSSAPSSQKFHKSCNGVNGHKDLYLQYKPGAKAQSWDTELLLGQESIGVCVPVQQVVVVKSEAEPSAISFMGAL... | Catalytic Activity: D-glucose 6-phosphate(in) + phosphate(out) = D-glucose 6-phosphate(out) + phosphate(in)
Subcellular Location: Membrane
Sequence Length: 529
Sequence Mass (Da): 57507
Location Topology: Multi-pass membrane protein
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F1Q7U1 | MEETANTDVLFIELRQKLQSGLLFIRSDVIGGGADVKIESKPDSILNVQTPDSSFQVTLTPGVSLVETQKQKSPANSEQGSHYRLRLKVEQPTESPCSVIGQLRVDESYSVLCQSCGSRVLQHRSFGRVLPLPNGNWNALVDDWCCHPDPFANRKLLPRAGDCLLGDTFILLLRDDGCDESLTRAAAEKRVLVSCRRCSTALGEEITAEVLKLYITEISVKPSEDGECDLTQLSLEPKSESVRQRFLEQTLASRLVELSAAQSIFRFSIQSPDGKAEILLWLLNTDTLVASFPAPAARADGFISVGDSHPRMHQSCQAVA... | Function: E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome.
EC: 2.3.2.26
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine... |
A0A183P4E3 | MSGFSSSADVLLDPAAFPLLICPMDILISSIVRGVTFVERRVGAASMSGGSSGKVGAGTNANLALAKSEKIKTMKPVRDREYTVHFAADTHSLMKWNFKPSQKALRIVPGETALAFYTAENPTDKPIVGIATYSVVPFEASKYFHKIQTSHFSTSSTKSYCQQIIFGMKAAGTKSCFCFEEQRLNPHEKVSVHYRFTRKVFYIYEINQSPCI | Function: Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 212
Sequence Mass (Da): 23425
Location Topology: Single-pass membrane protein
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A0A7J9TCD6 | MSKLVGAVAIAGGGIAGIQSAIDLASSGLKVYLIESSTTIGGKMAQLDKTFPTLDCSMCTLSPKLAEVARHPNIELMTYSEITGITGEPGDFTVTVKKKATYVDYDKCTACELCVSKCPVKVPDEYNEGQNNRKAIYLAFPQAVPRVFTIDANHCLYLTKGKCGNCQKACENDAINFEDTDKEVDINVGSVILNTGFEPYDASNLEQYRIDHPNVVSSLEFERQLSSSGPFEGHVTLADGSHPKNIAWIQCIGSRSPEIGRNTCSSVCCMYATKEAMVAMEHDLDLKTTIFNIDVRAFGKGFEEFYQKAKNEKGIRFINS... | Pathway: Cofactor metabolism; coenzyme M-coenzyme B heterodisulfide reduction; coenzyme B and coenzyme M from coenzyme M-coenzyme B heterodisulfide: step 1/1.
Function: Part of a complex that catalyzes the reversible reduction of CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme M) and H-S-CoB (coenzyme B).
EC: 1.8.... |
T1FRK7 | MASSRQDEEVQSTNDDAVNSKFSAVKLGYWQDPYIQFFSKFSSAIDRKPPELNRGYYARVKGVEYLLKQFLKKTDLKCQVVNLGAGSDTRFWLLSDQNLVPLKWVELDFEPVVNKKIRIIKSKKSLMCKLQANNHDGSSDSIPDVQIKPTEIHSNIYHIVSCDLRDVCQFKSCIDRCSIDCTIPTAFICECVFIYMDPHSSSCLVRTISEMFSDIFFINYEQVNMNDRFGEVMLSNLQNRGCALLGVQHCLNFQTQFDRFLKCGWNGIDGGDMLQIYHGLPQDDVQRIEKIEFLDDIEMLTQLFTHYCIVWAYKHSTKNT... | Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
EC: 2.1.1.233
Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl es... |
A0A2K3N9T6 | MEDYGYSDNDDDYHFSDQEDSELELLQNDLHNFQFSSSKAPIAQVITKESLIAAQKEELQRVMDMLSIRQQDARTLLIYHRWDVDHLFEVYVEKGKEFMFAQAGVSVDEYHDSDSPVSAVVMCEICIDDVPSDEATRMDCGHCFCNSCWTQHFLVKVNEGQSKRIRCMAHKCNSICDETVVITLLGRRHPDMAEKYERFLLESYIDDNKKVKWCPSTPHCGNAIRAEGDDLCEVECSCGEQFCFNCLSEAHSPCSCLMWELWQHEHQDEVESDNWIIIHTKPCPKCHKPVEKNGGCNWVGCICGQPFCWLCGGATGLQHT... | Pathway: Protein modification; protein ubiquitination.
Function: Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates.
EC: 2.3.2.31
Catalytic Activity: [E2 ubiquitin-conjugating enzyme]-S-ubiquit... |
A0A1S3CJV7 | MAAAALDPSSLQFTSTWAVAAVCFFFISLSLFLEHLIHLLSNWLKRKRKAALFEAVEKLKSVLMLLGFMSLTLTVTQQPVSKICIPNSVAYTMLPCQREIQITASKNLEMEKFQSNQSFSWLTEKVESSSSNDDSSSSSSSSSSSSDYCSAKGKASLMSQGGMNQLNNFIFVLAVMQILYSVLTMALGRAKMRRWKAWEEETNTLDYQVANDPNRFRLTRQTTFGRRHISSCATPSFLLWTKCFFRQFFRSVAKVDYLTLRHGFISTHVPGNTSFNFQKYIERSLHDDFKVVVGISPFMWLIVVIFILVDVHGWNAYLWV... | Function: May be involved in modulation of pathogen defense and leaf cell death.
Subcellular Location: Membrane
Sequence Length: 585
Domain: The C-terminus contains a calmodulin-binding domain, which binds calmodulin in a calcium-dependent fashion.
Sequence Mass (Da): 66494
Location Topology: Multi-pass membrane protei... |
A0A0B8NEB3 | MTVFTTMASPVGELLLVGEIQDGETILTAVSMAGGKSVLVEADWVADAEAFANVVPQLAAYFAGNHTGFDLRFGEGGTEFQRRVWRALDEIPYGRTTTYGEIARRIGAPRAAVRAVGSAIGANPLLIVRPCHRVIGVDGSLTGYAGGVERKQRLLELERVAWAPPPLCHRCGPDGSPSRTGRPWPGSSTSMGTH | Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irrever... |
U3JB19 | MRRPSLKNKTPISIIKNLDAFPKVPESYVATSAFGGTVTLTVFILMALLTISEFFVYQDTWMKYEYEVDRDFTSKLKIKIDITVAMKCERLGADVLDIAGAVVASKEIKYDSVSFDPSAQKKQWYQILQQIQNRLREEHSLQDVLFKSALKGYFSDPAPRVDPTPESQNACRIHGKIYVNKVAGNFHITLGKPIETHKGHAHYASFIKDEVYNFSHRIDHLSFGNDVPGHINPLDGMEKTTLEQNTLFQYFITVVPTKLHTSNVSVDMHQFSVTERERVVSNEKGNQGVSGIFFKYKLSPLMVRVSEEHMPLAAFLVRLC... | Function: Plays a role in transport between endoplasmic reticulum and Golgi.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 365
Sequence Mass (Da): 41460
Location Topology: Multi-pass membrane protein
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L1IYU7 | MAAVVRGVSAGMARAIRRGGDAPVYSIAVEQHRKYVDAIAQRVRSVIHVPARDDLPDCCFIEDTAVAVGKKILLTRPGARSRREETKDVELTIKSEISRFKSAYSVVSMAEESNEDVTLDGGDVLFTGRHCFVGISSRTNEAGFEFLRKHFASEFAEGAKSIHAIQVKDDLHLKSLATFAGNDQIAFDDSVGGDHFVQEVERLIGATHGYSMHRMSVHEATNVLRVGDALLVSKGCELLPEMQKLAEMAGVKRQDIVGVENSEFAKADGAITCRSLILPHLF | Function: Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation.
EC: 3.5.3.18
Catalytic Activity: H2O + N(omega),N(omega)-dimethyl-L-arginine = dimethylamine + L-citrulline
Sequence Length: 2... |
A0A352PP53 | MMRLADLGEFGIIERISRLLPATPKDVVVGIGDDVAVLDTSGPNYLLATCDIQVENVHFLRHGISPQQLGRKVVAINVSDIAAMGGRPRWALVSLGLPSDLSVTFIDELYHGLNAQAQVSGLSIVGGNLSQIKGPLVIDLFLLGECDKECFLRRDGARTGDAVLVTGDLGDSRAGMELLMHPELQVPEEVRTQVLAAHLTPHPQLAEGQLLAASRRVHAMLDVSDGILSDLGHICESSGVGASLDLAKIPISSACRQVAEAAAASPEEWALTGGEDYQLLFTADPTEVEAIQALVSQQTGAAVTVVGRIVAAPGMITVIE... | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.
Function: Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
EC: 2.7.4.16
Catalytic Activity: ATP + thi... |
A0A0N0RFS0 | MEALGLNLNFWIAQVVNFVVILVLLRMFLYRPILNMLDQRREKIRESLQAAEKARAEVVASQKAYEEELAKARREAQEIIERAREAAERQRAEILAEARQEAEQLKKRAQEEIAYERQQMLAQLRDEVAQLSLSIAQKVIGAALDESKQRELVEKFIAEAGDLK | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 164
Sequence Mass (Da): 18933
Location Topology: Single-pass membrane protein
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A0A069AKH2 | MLTYKESGVDIDEGNRAVDLIKGKIKGTYDGNVVGDLGNFSGLYSLKDFVGMKEPVLLASTDGVGTKLKIAQMMDKHDTVGIDLVAMCVNDLICQGAKPLFFLDYIALGKLVPEHIEKIVGGIADGCKMSGCALIGGETAEMPGMYGEDDYDLAGFSVGIADKEKIVSGNNVKSGDVLVGISSSGVHSNGFSFIRKIFLETYNYKMEQYVEELGMTVGEALLTPTKIYVKLALDVLAKHDIKAIAHITGGGLIENITRVIPKGLGLDINKKSWEKPPIFKMIEGFNAVDERELHKSFNMGIGLVLIVDKENADDVVNFIN... | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2.
Catalytic Activity: 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + p... |
L1JSZ3 | MAEEESAASRKFVRKVIPSDNSCLFNSIAYCMAPVDNIHQTSSALELRELISAVILSDPEEYCEAVLSKSNQEYSHWIQQSSSWGGAIECSILAGHFQVEICAIDCQTLRLYRFGEGRGLSRRMYLMYDGIHYDAISELEGRKEVTLFRAEELAIALVKTFRDKRQFTDTSNFSLRCLVCGQGIQGSDGAQKHAAETGHGNFAEN | Function: Hydrolase that can remove conjugated ubiquitin from proteins and may therefore play an important regulatory role at the level of protein turnover by preventing degradation.
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of u... |
A0A1S3C4S4 | MEPKCSNLWCVLVFASLMATLSSGSLSAKYYASTCPKLLSIVRSEVVKAVDKEYRMGASLLRLHFHDCFVNGCDASVLLDDTSNFTGEKTAIPNKDSLRGFEVIDSIKTLVEAACPSVVSCADILSLAARDSVVALGGPSWVVGLGRRDSTTASFDNANNDLPSPFLDLPDLISAFSNKGFDTKELVALSGSHTIGQARCSMFRVRAHNETTTIDPDFAASLRTNCPFSGDDQNLSPLDLKTQSLFDNAYFKNLVQNKGLLHSDQALFTNSSADSHVSSYISDPKAFFSDFAAAMVKMSNLSPLTGSDGQIRSDCRKIN | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/... |
A0A914B411 | MDMKSSSSIDLPDIFSPDDSVSSHGRPGGRVFGGAGRSHPSSVKSAGPLRNLSLQTFFRLMALTVVCTTTFALYYINSGVIRNTTPTATTDRGDIARQVLKNPAATNKPTDRIAPPLNHPSGVQNTSTAKLTSGVQNISPVNIPSGVQNISPAKLPSGVQNISPVNIPSGVQNISPAKLPSGVQNISPVNIPSGVQNISPAKLPSGVQNISPVNIPSGVQNISPAKLPSGVQNISPVNIPSGVQNISPAKLPSGVQNISPVNIPSGVQNISPAKLPSGVQNISPVNIPSGVQNISPAKLPSGAPYISPAKIPSGVQNISP... | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Membrane
Sequence Length: 747
Sequence Mass (Da): 80720
Location Topology: Single-pass type II membrane protein
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Q7ZZ56 | MAAIIKEFVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKDHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDKWLSENDNHVAAIHCKAGKGRTGVMICAYLLHRGKFKKAQEALDFYDEVRTRDKKGVTIPSQRRYVYYYSYLLRNKLEYKPVALLFHKMVFETVPMFSGGTCNPQFVVYQLKVKIHTSNPAHTRREEKYMFFEFPQPLPVCGDIKVEFFHKQNKMMKKEKMFHFWVNTFFIPGSEESTEKVENGGLVKDLDGIQTAERGENDKDYLILTLS... | Function: Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-diphosphate, phos... |
A0A6A6LJU1 | MRQFHHQRKKEPLLTSLGRCTISCILVLLTQFALSLVPRFFSASSLLIQLALSVVVLLLVVGFGKWCRRLLGVFASAPAFVFCNIFFVWAVYFVIVRQAIPFFIDAVFNGEVAMLFIGSSSLLKRVRYCKICKAYVKRFDHHCPAFGNCIGQNNHVLFMVLLLGFLSTEASYVMCSFQYWSGWKFGYQYIAIHSSPSTMAGGVYGMAYILYVL | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 213
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 24123
Location Topology: Multi-pass membrane protein
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H1XU80 | MLRTLLAYVFAVLHTLFCSLAAIVFGLFNPYSKIVDKIIRLWARGLLKAAGVKVVVHGQEKLRKDQPYIFMSNHQGAFDILAGVVAIPVTMRFIAKKELFRIPIFAHSMRTVGMIPIDRGNSAEARKSLEEAARTLQNGVSVLIFPEGTRTRDGNIKPFKKGGFVLALKSGLPIMPMVFTGSLNIMRKNSLKLHKGTIHVYFLDEVDTSQYSFEQRNELLKEVRKRIVDFYETVRLE | 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: 237
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence Mass (Da):... |
T1F274 | MLFLIGLGLGNADDITVKGLKLLQQSSKIYLENYTSILSIGKNELEKVYGRELILADREMVEQNADVILDEAEREDVSFLVVGDPFGATTHSDLLLRAKERNIKTQIVHNASICNAVGCCGLQLYKFGETVSIVFWEIDWQPESFYDKILANKERGLHTLCLLDIKIKEKSVENIIKNRNIYEPERFMTVNVAIEQILEISKRRNCQVITPQTKGVGLARIGADNQLIKYGSLEELKIFNFGPKLHSLVIIGDLHPLEHDLLCNFSS | 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 ... |
F2Z4T6 | MAAPLGLHLEFGGGAELLFDGVKNHHVTLPDQSNPWDMKQLLAWIRGNMLKERPELFMQGDTVRPGILVLINDADWELMGELDYQLQDKDNVVFISTLHGG | PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-adenylated (-COAMP) via the hesA/moeB/thiF part of MOCS3, then thiocarboxylated (-COSH) via the rhodanese domain of MOCS3.
Pathway: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.
Function: Acts as a sulfur carrier require... |
A0A0R4IUS5 | MSTTVTQRKRRTSTTCSRRGNSKRNRAQMSQTVMETIDVLENDRTNSEDVVDLTCEGSEPAVVDLTNNDSIVVVEDGVQRRVGPCTESYVLSSDEEEESSLRLSPGLLSSLRDSSRARSTPGAISCPVCMDVYSEIMDSGRLMVSTKCGHLFCSQCIRDSLSRAHSCPTCRKKLTHKQYHPIYI | 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... |
A0A6G7QLK7 | MIFFMVMPVMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGVGTGWTVYPPLAGNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMKPPATSQYQTPLFVWSILITAILLLLSLPVLAAGITML | 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... |
D8J4X7 | MKTEDLVQAAREAHAHAHVPYSEYRVGAAIETVDGTVFTGCNIENANYSNSLHAEEVAVSQAIATGHREFSRLAVSSDRRDGVTPCGMCRQTLAEFCEEAFPIVCDRGDDWTEYTLGELLPDTITQHHLE | Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
EC: 3.5.4.5
Catalytic Activity: cytidine + H(+) + H2O = NH4(+) + uridine
Sequence Length: 130
Sequence Mass (Da): 14354
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Q6PFK7 | MVSRRSLTIDTEKATKTTYVLGTTLTVNLIRCAPPQSKSFSIRCTPNVHYKITPPITDKNALPYPLGPNTILLITMDTVSETAFDSKLSVRYYGEKTETLGDAILHLTAVEISLDVDADRDGVVEKNNPNKASWKWGPNGHGAILLVNCDSESINNKKPDNENSDIGKVSDLKDMSKMVLRTNGPSQLPEGYKLSMHISQSTSESVRVFRPRTNTKTENLWKYQLLKLFLKDFLMVVGTDTLTQEVPYLGGSSELEFHVEGLRFPDKDFDGLVTINLSLLEPCGKGFPETPIFTDKVVFRVSPWIMTPNTLKPVEVYVCS... | Catalytic Activity: H2O + L-arginyl-[protein] = L-citrullyl-[protein] + NH4(+)
EC: 3.5.3.15
Subcellular Location: Cytoplasm
Sequence Length: 647
Sequence Mass (Da): 72890
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A0A183IL52 | XXXXXXXXERNIINFLEALHRAFSVFSFNNHDELLLQQRARSKLTFPGLWTNTCCSHPLHCPAELENTPFAIGVRRAAIRKMSQELGANDINIDSLCFMKRILYRAKWDETHGEHELDYILILRQELALQPNSDEIERIRYVSKEQLRSMLGNQQEYRFSPWFTLIAEHFLFRWWEHLEHIDRFLDYSIDDFD | 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: ... |
A0A1U9KMN6 | MHILGLTGDMGAGKTYVANLFRRRGWPVFDADATVHRLQGPGGEAVAPIKALWPEAVPGDAIDRTALRHIVIGHPDRLKALEAIVHPLVRQERQRFLRRMQARGKRWCVLDIPLLFETDAYRACDRILVVTAAESTRLRRIMRRRGMSEEQARNLLARQIGDAKRRRLADVIIRTDLSRAATFRQLRRLQHDLEAMR | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
EC: 2.7.1.24
Subcellular Location: Cytoplasm
Sequence Le... |
L1ISN7 | MCHSFFSTELPYVSHCLLCTAAWQKKYFNPFSQGLSKKPETSVSPPPAHAPPVESLKGKDLYQALEQLPSDWRDFLADETDKEYFKDLNDFYVDEVSKGATVYPPTRDIFGAFCLCPLDQVSVIIVGQDPYHGPGQAHGLAFSVRQGVAPPPSLQNIFKELESDPAVSFQRPRHGCLEGWAKQGVLLLNTCLTVRAGQALSHQAKGWEKFTDAVISKLDKQCDGLVFLLWGQPAAKKCSSVDESKHMVLKAPHPSPLSARRGFFGCKHFSLCNEYLSAQSKKEINWQT | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
EC: 3.2.2.27
Subcellular L... |
A0A183J610 | MVSAYDKGELPPLTAEQRKEQQVAINKLQEIVKEIRKEHPDFGKLQFKTRHGPVPHPGPFPENPLWKYLDGQIWQKRPMAIGCGKPFKSLQCRAIISNNCNSILLKFMEFKAFVAISLFNNTYVVLFQETCLHPTDDKNILSLESFVCYHLVVVIWTSRILFIPAHTMLSHAKSMYPISNALAAAGHEVVFLEFQYERNGSFRQETEVPAGVANALGPDRGRRTVLPLWDDHCEGKQRSCXXXXXXXXXXXXXXXXXFDTSKTWIGSHEAKGTMWSRSLYPLYRVAVSRKPSSSFEERTINFWTLILFDLTMKITYRLMP... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 599
Sequence Mass (Da): 68736
Location Topology: Single-pass membrane protein
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F1QH81 | MRNMAREILAFILCTSGWVLISSTLPTDYWKVSSIDGTVITTATFWSNLWKTCVTDSTGVSNCKDFPSMLALDGYIQVCRGLMITAVCLGFFGSIFALIGMKCTKIGGPDKFKARVVCFAGFNFACTGLCSLTAYSLYAHRITSEFFDPMFVAQKYELGAALFIGWAGSTLCLLGGALFTLSMADGSSKKSSPNRRVASLMSGAMPQSQTSHTRRTLPEYSSTPQHFDKNAYV | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Subcellular Location: Cell junction
Sequence Length: 233
Sequence Mass (Da): 25382
Location Topology: Multi-pass membrane protein
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A0A818Y3X1 | MSNGAITMTKRLGSDVSGFEYDKRTGKGYFMNATGYDQQGQGGSWAKMYILDCNTQVIDSAKRGDKTYKALVYEAGNKLVWPDMHSGYIEMLNLANNVIDSVHIGVTLDEMDVSPDNNSLFIACRLGGSDIIKYDINTLGTTKFKAGSWPCVVRTDSSLNKVFVLNHFQSTISVINPNTNTVTATINLPLAEGRADAIAVMCYDKFLQKIFVSFPEFGNIVKINAVTNVVESTTPIPGFTFNPDGGGSNFNMSRSIKAPTGTTLSCKNWITEAAMRMLMNNLDADVAERPEDLIVYGGSGKAARNWECYDKIIETLKVLN... | Pathway: Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 2/3.
EC: 4.2.1.49
Catalytic Activity: 4-imidazolone-5-propanoate = H2O + trans-urocanate
Sequence Length: 500
Sequence Mass (Da): 54204
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A0A948AM70 | MRLALFGGSFDPFHNGHLAVVRELGDRGLCEQVLISPARISPGKPAPLAAGHHREVMAVLGAAEHAYVSVLDLELRRPGPSYTVETLAELSRGRPGDEWLLIVGADAWRDFRTWHDPDRILELARIVVFPRPGIDPDPASSTPRVTLLEDFLVPVTSTAIRRRIAAGESVTHLLPGRVLDYIRLHGLYGCPCAADDGG | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide... |
L1JMB6 | MSASQPLPFDPTSGSLSQKKPFDVDVSKLQDPSKVQEGCNPVVLLACGSFSPPTVLHTRIFETARDYFRETAETNKLQVVGGFISPVHPSYGKKGLAAPEHRVEMVKRALETSDWIACDEWEVKQNEWTRTRLSLDRMYQELNKDRGGQEVKVMLLCGADILESMVTPGKWRERSEERRGMILSRGIVCIKRSGSDPERLIQENDLLYERTRPFNSLIVCQAREWVENNVSSTAVRRAIKRNMSVKYFVADPVLDYIKDKRLFLD | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1.
EC: 2.7.7.1
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Length: 265
Sequence Mass (Da): 30270
|
Q503F4 | MSWGALYAQLGGVNKHSTSLGKIWLSVLFIFRICILVIAAETVWGDEQSDFTCNTQQPGCKNVCYDHFFPVSHIRFWCLQLIFVSTPALLVAMHVAYRKRNMKKKSILAKRGGNGKGDDLESLKNRRLPITGPLWWTYTSSLFFRLLFEAGFMYALYYVYDGFQMARLVKCEQWPCPNKVDCFISRPTEKTVFTIFMVGSSAICIVLNVAELAYLIVKALLRCSARAKGRRSFVHQEKMSTEKAHLQNEKNARLLSSASDSSSNKTV | Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Subcellular Location: Cell junction
Sequence Length: 267
Sequence Mass (Da): 30323
Location Topology: Multi-pass membrane prot... |
A0A945CCT2 | MSDFLDYVEIQILSGNGGNGLASFRREKFIPFGGPDGGNGGNGGDIVFVGSNNLNSLRDFRNKRVFKAQNGTNGGSNKRNGKNGSNKVIRVPLGTEILELNTNKKIADIVTEDLEVVLLEGGKGGLGNTFFKSSTNRAPTKYKDGKKGEKLRLALNLKTISDVSLIGYPNVGKSSIIRKITNSKASVGNYQFTTITPNIGVLEAKNKDFLIADIPGLIKGSHSGKGLGHQFLKHIERSDCLIEVLDTSCLNIEELQEQHDTLLFELKEYNIKIISRIKLIVLNKVDACKFRDELSKFKPLKNCSTILASSLDGFGMEDLK... | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis ... |
A0A2H1JJG8 | MTAVSAATATTDLYPTRSGETTEVLPRTGPIVFGSPEDGPLEAADLKHFEDTGYLTIDQLITSEELTLFTDELQRLSRDPEVKADERTVVEAESDEVRSIFDIHRTNEIFRKIANDPRLVDRARQILGTDVYIHQSRINYKPGFVGKEFSWHSDFETWHAEDGMPTPRAVSLSLSLTDNYSFNGPLMIMPGSHKRYISCVGGTPEDNYRKSLIMQGAGTPDRQTLSDFADEYGIDVLEGAAGGAIMFDSNCMHASNGNVTPFSRSNIFIVYNSVENTCVEPFAAPKPRPEFVGSTDFTPAGR | Function: Involved in the biosynthesis of 5-hydroxyectoine, called compatible solute, which helps organisms to survive extreme osmotic stress by acting as a highly soluble organic osmolyte. Catalyzes the 2-oxoglutarate-dependent selective hydroxylation of L-ectoine to yield (4S,5S)-5-hydroxyectoine.
EC: 1.14.11.55
Cata... |
A0A379LNX0 | MSLLTPHLSDMLLPLWLSIKLASITTLCLLLFATPMAYWLAKPSSSTLIARVKIMLMGVIAMPLVLPPTVLGFYLLLLLSPNFALGQWLMAHNIGALAFTFEGLVLGSIIYSLPFYVQPVYAQFLRIPKSVSDMALLLEPSRLRRFTAVSLPQAKTGIILGSLISFAHTIGEFGVVLMIGGSIAGETKVISIAIYEQVEALNYEMAHTMSLLLVVLGIVLVGLIASINRQVNEGFASRPKSKSMK | Function: Part of the binding-protein-dependent transport system for molybdenum; probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell inner membrane
Sequence Length: 245
Sequence Mass (Da): 26647
Location Topology: Multi-pass membrane protein
|
Q5TYP2 | MVASQCVLGFLLLVAVFSARPQARSFDQRMIMEGPHLLDNNFRGYWDQLQSPVKVESLRAPLASNLVSSVQSKQEMLSPVSSKVDWRFPLVREEPAQLDVNFQLRQPQTPNTVAVQCLENGVHVEVKQDFFGTGHLLEPSSFSLGGCGVLNVDTAAGVLIFQSALQDCGSQLVMTDDELVYVFTIDYKPAVLPNIPVVRSNSASVNIECHYSRKHNVSSSALLPAWTPYAATAVAEDVLVFSLKLMTDDWMYERPTNVFFLGDIFNIEASVSQYNHVPLRVFVDSCVATATPDVNAAPLYSFIENHGCFTDAKYTGSASK... | PTM: Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.
Function: Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polys... |
L1I7G2 | PERPYQAREDIQKISVVHWGQRKLFVAEMSFLSAHYTPSITTVVYAGAAPGTHLVELMLKFQKLSWVLVDPEPFHHKLRDFYSSSVTLIQDRFTDAFAAQFAGRNDVLFISDIRTADHNRDNKEENERKIAQDMQNQKRWFRIMNPVAALLKFRLPWDNRMTTYPMGKIQYPVWGRVSTTETQLIVLQNAPDTVYDNKRYESKMFYHNTIAR | Function: Displays methyltransferase, positive regulation of the poly(A) polymerase and transcription elongation activities. Involved in the modification of both mRNA ends and in intermediate and late gene positive transcription elongation. At the mRNAs 5' end, methylates the ribose 2' OH group of the first transcribed... |
Q8JHW1 | MGDWNLLGSILEEVHIHSTIVGKIWLTILFIFRMLVLGVAAEDVWDDEQSEFVCNTEQPGCKNVCYDQAFPISLIRYWVLQIIFVSSPSLVYMGHALYRLRALEKERHKKKVQLKVELEESEALEEHKRIEKELRKLEEQKKVRKAPLRGSLLRTYVFHILTRSVVEVGFIVGQYMLYGIGLTPLYKCERDPCPNSVDCFVSRPTEKNIFMIFMLVISGVSLFLNLLEIFHLGVKKIKQTIYGSMYSDDDSICRSKKNSMVQQVCFLTNSSPQKQLHLTHTSLAMAPDGQMVPLPIYMQTAGHVVSNINPNGSVQPLRQD... | Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Subcellular Location: Cell junction
Sequence Length: 466
Sequence Mass (Da): 52612
Location Topology: Multi-pass membrane prot... |
A0A947RVD1 | MSIRPVHVAGGGLAGCEAALQLARFGIPVVLHEMRPARETPAHQGEALAQIVCSNSLKSVDPTAASGLFKAELASAGCRLLAVARACAVPAGAALAVDKELFSSRIEALLAGDPLIEIVRDEVTAPDVAGDAFWIIATGPLTSADLRLRLEALTGGAGLYFFDAIAPTVTLDSLDLDALFRAARYGKGEADYLNAPLTRPEYEAFHAALTGAARAGVRDFDRSHLFAGCQPIEEIADSGLETMAFGPLRPVGLADPRTGKRPHAVVQLRQENRAGTLYGLVGFQTRLKRAEQRRVFRMIPGLGRAEFVRYGQLHRNFYLD... | Function: Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH + uridine(54) in tRNA = (6S)-5,6,7,8-tetrahydrofolate + 5-methyluridine(54) in tRNA + NAD(+)
EC: 2.1.1.74
Subcellular Location: Cyt... |
A0A6P4ZRX1 | MPEGPLCNLLALCECPGTMWEGSRLRLPCGVRVRFLYDPQGWCALGIISFIWAYNTVFIPSLVIMPMYHDNRLPLATPVFYFLMSSLTVVCLYLSVTTNPGTVPLDIQPSAVEAADWTVCKVCQIRRPPRSHHCRRCQQCVRKMDHHCPWINNCVGEENHWLFMQLLYYTLILVSLSIALAALHLYYSPPCSYCNPGIFPFSYTRPLLWFTCGQGVFFFPAAIGLVFGQTFNIILDRTTLENLADPYFRSGVPSPRAIHEAFSDICGTKNVFCWLWPLRRRRAITAQAGYSYYRHM | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 296
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 33914
Location Topology: Multi-pass membrane protein
|
T1FN31 | MIKCHFLIYSILITSFHLLSVNQDDVLTSDFQSCLTTSTIPDLTDPDNSNNNNCKMICTKLHEKQLVTLINSIIPPLCNKLYKGQAGKIAVIGGSKEYTGAPYFAAISALKMGADLVHVFCTNDSSPIIKSYSPELIVHPMIDSPNVMERIKPWLDKMHAVVVGPGLGTNREILKNVKEIVSYVRAKNLPLIMDADALWIVVEDSEVLRDYKKAVLTPNLVEFSRLYKSLTNTTLNDADAHEPVESVKKLSNLLGNVTIVRKGYQDIITDGVQVVISEVSQSNPRRCGGQGDVLAGLIGTFSHWAYSSTYDDPLLKQLGP... | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
A0A1S6H945 | MAVNHVAIILDGNRRYAKKHNLPLYRGHEFGAKNVEKLFGWAEELSIKELTLYSFSMQNFNRTKEEFNYLMKVFEIFCKKAVAKLKKNPKVQFHFIGRLNLFTRKIQILARELERKSRNNKLLKVNFAFGYGGREEIVDAVKKIVKKGLKNIDEKVISDNLYLKSEPEVIIRTGGDQRTSNFLPWQSIYSEWFFLDKTWPEFNKADLKRIVDDFTRRERRFGV | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with geranylgeranyl diphosphate (GGPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30E,34E,38E)-undecaprenyl diphosphate (tritrans,heptacis-UPP). It is probably the precursor of glycosyl carrier lipids... |
A0A161I258 | MASPKHSHHRASAAPPASSNSNSKHMSNSKQHARATKQRPLSLRRAMLHSFVCFLVGLLTGFAPSDWTDAASRAAVHANAAATAQVFRALHAMNNTAAAGALGHLLTLQHYQSYQQQGKQQQQQPPLDLVVVVTTTTTSTGLSERERRSAGLTRTAHALRLVSPPVVWLVVESAREAGPTARLLRRTGVVYRHLTYGENFTSEAWEEERHHQRNQALAHIEQHRLRGVVLFAGLADVYDVRLLEHLRRIRTVGAWPVATVWEQEKRVAVEGPVCTTAGTGTATAAWFSVSASEEAASTSPSPPVMTDDSVHGFAFASDLL... | Function: Involved in the synthesis of glucuronoxylan hemicellulose in secondary cell walls.
EC: 2.4.-.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 377
Sequence Mass (Da): 41629
Location Topology: Single-pass type II membrane protein
|
Q60I71 | MANSARERNKLWIYIIVLNILPRISSGQIAFSVSEEASPGTTVGNIVKELNLNLQELEHRGFQIVGPNKRYFDVNMKTGILQVKDKLDREEICGQSLKCALELEAIVNSPLNMYRFEVNVLDVNDNSPTFPSSRLQLNVSEAAFIGERYALPNAFDADVGINSVKSYKLSANEHFSLDAQSGGEQSVSAELVLQKALDREKQPVIRLTLTAVDGGKPPRSGTVHIIVNVIDVNDNIPVFTKSLYKARILENAPVEFSVITVNARDADAGLNGEIEYSFIKHGIDKNIESFAINKETGEITVMGKLDHESNNAIEIRVQAR... | Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Subcellular Location: Cell membrane
Sequence Length: 939
Sequence Mass (Da): 102075
Location Topology: Single-pass type I membrane protein
|
T1G978 | MSVADFKPSNVSNGIKRRNLTDGIIEIGSFYKVRKADGRLHTAEVIEVRNDEQKDGQVEYYVHFVGCNRRLDSWITLDKFDSFTKVQDVYKDVNASMNAAKISEMEEEKNSDRKMTRNQKRKYEEMNHIPTSYSDMDPTTAALEKEHEAITKVKYIDRVQMGKYEMDAWYFSPYPEEYGKQTKIWVCEFCLKYMKLEKTFRYHLTECVVRYPPGKEIYRKMSLSLFEVDGKEAKLYCQNLCLLAKLFLDHKTLYFDVEPFMFYILTEVDRHGAHVVGYFSKEKDSPDGNNLACIMILPPFQRKGYGKFLIAFSYELSKLE... | Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
EC: 2.3.1.48
Subcellular Location: Nucleus
Sequence Length: 435
Sequence Mass (Da): 50936
|
A0A0M8KC05 | MNEQTVLTQLEAVIRQRKAERPEGSYTTTLFDGGLDRILKKIGEEAGEIIIASKNANPDEIIYETADFLYHLLVMLAYHDIPWRDVENELQRRFGNRPH | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
EC: 3.6.1.31
Subcellular Location: Cytoplasm
Sequence Length: 99
Sequence M... |
V5IN23 | MAHQLPSTLDLGNDVSLDVSTAPTTPGSNLSFSPVLQAADEQPGIPAMKPQSTSRSLSSTLFDTTARTPPVRNICCVGAGYVGGPTAAVIAFNNPHIRVTVVDKDEKRIRRWNSVHPPIYEPGLNHILRIARDGSKECTIETRSLSTTNTTSSNTPDVSDASTPASECGSQCGDNVSKPIPARQPNLFFTADVAKSISEADIVLIAVNTPTKSRGAGAGSATDMTAFEAVTNVVAQHARPGAIIVEKSTVPCRTAQFVQDTLALHRPGIHFEVLSNPEFLAAGTAIKDLLNADRILIGSSATPSGQRAAAALASVYSAWI... | Pathway: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1.
EC: 1.1.1.22
Catalytic Activity: H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate
Sequence Length: 682
Sequence Mass (Da): 73204
|
A0A327KDN5 | MRNVPQIIGLATAAFALALDQVTKQIALSNLAPGVAVPIAPFFTVRLGFNEGVSFGMFAGWFSGRPLILAAIMMGIIVLLAVWLWRTPRRPQAVALGAILGGALSNVFDRLRIGAVVDYLDFHAWDHHWPAFNFADAAIVCGVAILVLGDVMGRPNDREGQRELR | 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-, ... |
Q1PYN7 | MKILGIDPGTLIAGYGVIEKSGAEIKAVAYGSIKTGKNQNFPERLKTIYTGVTELITIYKPDHMAVEEVFFGKNFKAAIKIGEGRGIIFLCAAMANIPIAEYAARVVKKAVAGNGNAHKGKVQEMVKAILGLPEIPQPEDASDALAIAICHGHRL | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous... |
Q504A1 | MVSHSLVLPMIGFTTLWGLVGIVAPFLVPKGPNRGVIITSLVLTAVCCYLFWLVAILAQANPLFGPQLKNETIWYLRYYWE | Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some c... |
L1K448 | MSDSQDAAKSKEGSKDEQSSWQDNCHGVSALAIKRLIKFAHCKDKTLLIYGGLKTMLVADCSTGSLMELEQSHTERVTSVTVGKDKEVMVSGGNDKRLVVWQLPEMKVASKTVTDKKVVSVVLDEERRRVVFAEIAGEVFQKPIDDLDSKAEHLLGHISSLTDMRISPSGSRLLTSDRDEKVRISNFPHAFEIEAFCLGHTELVTCIETFTLAEEELLLSGGADGSVRLWSVKDGSLLDTYMIDPAGEEEEGEDGQQADSQPLAEEPKTWDRFAAGTAQATAAVSGRMRRRTNSPAVVALAYCPRLSLAACIIENQREVL... | Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Function: Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit.
Subcellular Location: Nucleus
Sequence Length: 447
Sequence... |
H1XT72 | MFTHLKICGITRLEEAQKIAELGVSFLGFNFYERSPRFVTTGRAREIIRQLPAWVNTVGILVRPTLRECLQILKHTEIKFLQIYDPLDFTDFNRLPAPVIAAFRLKDGVEFSYQRRGEQYVLLDAFHSGVYGGTGRTLNWLQLPAEVPRERLFLAGGINPDNILKALTAVNPAVIDVASGAERAPGVKDLEKVRAMQMTVLSFNLAKIDRAKQNGNN | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Length: 217
Sequence Mass (Da): 24413
|
A0A6P4ZMB0 | MSSTSPTVTELTPLACLDPQNKGVRIALIVLNQPQSLDVLAVLWTKAAVLKAVTDGGVNRLYDATRNNPESWIPDLITGDFDSASSENLQYYKDKGSEVICTPDQDHTDFTKCLQLVVQRMQERNIQVDYIVSVGAFGGRMDQVMANINTLYEARSLTSIPVILLDEVSMAFLLSPGKTLLHVQTGGEGEWCGLVPVGGTCPHVTTTGLKWNLNDQALKFGELISTSNTFDQSAAGLVTVETNDPLLWTMGVNVQRS | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine: step 1/1.
EC: 2.7.6.2
Catalytic Activity: ATP + thiamine = AMP + H(+) + thiamine diphosphate
Sequence Length: 257
Sequence Mass (Da): 27961
|
L1JH97 | LQFHIHTPSEHTIDGEHYDMEIHFVHKTDDPKAKSKVRPKGASATRLTGRQIMVMLLPIDFADISQTVMIGSLTHRGADAFSFVPNFKNYLTYSGSFTTPPCSEGVQWVLLRNPIYVYSKDLQVIRSLEGANARPAQPLNGRHV | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 144
Sequence Mass (Da): 16175
|
L1JJF8 | MLRVLYLCFYNLFGLCGWAMILFQVVSILLEGRVTNLWKELEGTVKLVQGAAVLEIMHSLLGLVRSPVSRTFVQVTSRLLTVWASMDPLYTYPYTPFPKGKGCNYSIDVVECSEEWNYYIGAMTLIAWSFAEIIRYSFYGINTVSPKSVPFVLVWFRYSGFIILYPVGVAGEMLCAYMTLPLLQKGMCPRFEGFLQTCPSYSVTLLYVFLANYVSCEDKACSAVEDGVWGLPWLYTTMLGERKKRLYPKPAPKLQGVVFPVSKNGERSTTNAAKEIFAMAMESTDAKMADKVKKEKNWRFGYTKHILNNLVVSAKSQKHQ... | Pathway: Lipid metabolism; fatty acid biosynthesis.
EC: 4.2.1.134
Subcellular Location: Membrane
Sequence Length: 332
Sequence Mass (Da): 37679
Location Topology: Multi-pass membrane protein
|
L1JFY6 | MSLEDNKKEEKVLNGIKHPRERFVALTRELGKNLKLEKALSEKGVRTVELPCIAFEAGIDSDSLPSALKEDWEYVVVTSPEAASVFLDAWRLASQPSLQVACVGTGTKQALQEGGIEPVFMPSKATGKTLADELPGPQGNGRVLYPASAKARTEVQGGLTARGFTVTRLNTYDTVSATWSEQELQMAASAAVVALASPSAVKTWAERLGTKQYAACIGETSASACKELGFEHVFWPESPGIPGWAQAVHDALEEMESAEMSRSK | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O... |
L1J5G3 | MAEAARSERTGGDDGGDEGERMAACTREKKVEALEEEDETAEQKGMSEHGALTIEDPSAGKGSIKKRLGRQWHKYCQTLPRHYKGGLMSSDEVDAKRAGQNVERRRPEKGDHHKDSHRRAGLPEHQRCSFWIEQKKRLCSRPRMERSSFCIGHQVAQGADGKEDSSEARECEFCRTRILPDRYESHLKRCNVRTREDAMRSCPYYKQDINSGSQGRPLPSSQPVMSDAEDPVGFVGRVNENYEIHVRAIEEQDSSLISNMEDKGLLNHVTDSTFIEFGAGKAMLSLSLVQCDEAVNLLLVEKDSGHMKGKADRILRLRSR... | Function: tRNA methylase which 2'-O-methylates cytidine(4) in tRNA(Pro) and tRNA(Gly)(GCC), and adenosine(4) in tRNA(His).
EC: 2.1.1.225
Catalytic Activity: adenosine(4) in tRNA(His) + S-adenosyl-L-methionine = 2'-O-methyladenosine(4) in tRNA(His) + H(+) + S-adenosyl-L-homocysteine
Sequence Length: 475
Sequence Mass (D... |
A0A174BXQ4 | MTKQKQSLIISFLIGFAILAGLDQWTKGLAVQSLKGQKPFVIWNGVFEFYYSENRGAAFGMMQEKQLFFFLIAVLVLGAVAYLIWKMPPEGRYRPLAVCLMMISAGAVGNMIDRVSQGYVVDFLYFKLINFPIFNVADCYVTVGAACLVFLIMFYYKDEDMACFSFKKH | 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-, ... |
F6P1M3 | MADHRVAPVVGFLLFLVAPVWSGCPSACRCSFAMLQCLESDGITSIPALAAQESENVTEIYIESQPNLENITDVDLANYRELKNLTITDCGLVYISENAFQHNFKLQYVNLASNALTHISWRVFQSVTLLSLILRDNLLTCSCDIYWLQQWHRKRLNEIDSQQNCIYNGSQIPLDSFEMDNCSVPEVMIDPPTVTTQEGGNLTFTCRVTGVPTPTIHWRTEQLRSSWTLEQGIWGSTLEVVLHMRNVSSADNLHNLTCEAENRAGMGDAVVQLDIEFPVRIIYLKNPESQHHWCFPFAVDSNPPASIKWLYNNMPLTETR... | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
EC: 2.7.10.1
Subcellular Location: Cell membrane
Sequence Length: 797
Sequence Mass (Da): 90265
Location Topology: Single-pass type I membrane protein
|
L1JUK2 | KLEPAVQNYEWGVRGGGQSSLVARMANAQVAEEKPFAELWMGTHPKAPSVVLEDGWSGMVLGEFLRLNEVFMGSKAGMFGGDLPYLFKCLSVAKALSIQAHPDKTLAKLLHARDKPNYPDDNHKPELACAVTEFEGLCGFRKLDEIVENVGAVPELKELIGQDTVKLMESSLDKDAQSRAEALKQAFNMVMSSPEDRVKHQASKMVDRLKSSQKLRDVEELVLRINEQFPLDVGLFNIFFLNHVKLRPGQALFLGPNLPHAYLSGDCMEIMATSDNVVRAGFTPKFKDVATLCSMLDYERSGPAEIMEGEAREGMRVYAP... | Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 1/2.
EC: 5.3.1.8
Catalytic Activity: D-mannose 6-phosphate = D-fructose 6-phosphate
Sequence Length: 325
Sequence Mass (Da): 36013
|
R9KZH4 | MKRNLLSIIILALLVVNIVLSAIMMVTVSSASRKTAALVADISAIIGLEIDGLPASDVGAAPVTMADTAVYNITAEMTIPLKNDEDGTGHYAVGNVSLSLNKTHDDYKTYNEETLATSEGIIKDIIYGVLGEHTLEEARNNTEQIKAEILGKIQEKFGSEVIYDVSFNFLYS | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell membrane
Sequence Length: 172
Sequence Mass (Da): 18553
Location Topology: Single-pass membrane protein
|
A0A7C4JPD3 | MQLRCPRGTRDLWGDELATARFVVSKMRSVFERFGFQEVQTPIFEHLELFLVKSGSEIIKQIYDFEDKSGRKLALRPELTAPAIRFFIQHLKRNPPPVRLFYFGECFRYEEPQAWRWREFTQAGCEIIGSPNPQADAEVISLTCEIMREVGMNDWKLRIGDVGILRNVLASVGVKEEKQDPILRAVDSGNRNRILEELRKAGVPEEEYERLLKIFSLRGDFRVFQKLSEFDIDESMLERSKELLRILREAGEKFEIDLGIARGLDYYTGTVFEVYVGDVQVAGGGRYDTLVERLGGPKTPATGVGFGVDRISSLLLKDSK... | Catalytic Activity: ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His)
EC: 6.1.1.21
Subcellular Location: Cytoplasm
Sequence Length: 419
Sequence Mass (Da): 47731
|
A0A133Q8B0 | MQKVSQYIIAFIAAIIFVFILNVFIIQGAVVKQQNMAPVLQKNDRVIVNKVKVTFNILQHGDVVMFRQHGDLKFSRIVGMAGESVEVKQGQLYRDDRQIKAPYAKNIKTDFQLRNLPHSEGDIIPPDKYLVLSDDSRLNKQSQSYQLIDKKDIIGDVNLTYYPFHHFRYNYER | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Cell membrane
Sequence Length: 173
Sequence Mass (Da): 20132
Location Topology: Single-pass type II membrane protein
|
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