ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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A0A3B9NU19 | MQSTFFWYDLETTGTDPILDRIVQFAGQRTDSDLRPIGSPVNFYIKPSVDTLFHPDATLITGIDPDQIDAEGLSELAGLRKMLACFTEPGTCVVGYNNLNFDDEFVRQSLYRNFFDPYAREWQNGNSRWDLINLLRMTFALRPAGIKWPKREDGKPSFTLVKMAEANGLSHENAHDALSDIEATISLAKLVKTAQPKLFDYHFQMRKKQPVLDLLYPLGKAPVLLIQPFFDSSDRYLAPILPLIAHPSNQNSVICLDLRQDPEAYCALKGDALTDFLLPKRVEGARSKPSVVQRIQINRCPPIAPMNTLPPALAADLSWS... | Cofactor: Binds 2 Mg(2+) ions per monomer.
EC: 3.1.11.1
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Length: 472
Sequence Mass (Da): 53130
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A0A183TKS8 | MKRRHVDLLLGVVHAAVAFYLVYLTNEVQPTAYMDEYFHEKQTHAYLAGRWSEWDSNITTPPGLYLLTAIFLKSREIFLGDNTRQDLNVTHFRYLNALHLGVNAFLVSSILSHLNRLPLPLHLLYLTSIVTLPVLFFTSFLFYTDQVSLAAVLATALAFLYKRRLTAFLLACFACSVRQTNIVWCAFLVGMSIASRLSSIRRKRGSPTEASPFSWFCVLLRSPVRVIQAVIQGIAYDAPLLTLVGGLFMAFVWWNGGVVLGDRSSHEFTFHIPQLLYFLAFCAAQTPLRFFLFLLHLSRSLCKRQRMLPLLLLLLFLTAL... | 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... |
A0A820XLV3 | MTDYELNFSLKTEEMLGRILDPAYRCLVVEMFESINVLLERNPELCFVQPLDVDYLISDAIKLFEQQTKSVDPLKDFYNLPISLVGGSTGYMTQVIINYLFSAQIQKSDVADLNSSASNSICKIS | Pathway: Glycan biosynthesis; glycogen metabolism.
Function: Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I.
Subcellular Location: Cell membrane
Sequence Length: 125
Sequence Mass (Da): 14129
Location Topology: Lipid-anchor
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A0A0N4YM25 | MAAFESNLRGKERIVVFIFGGAAFSKHLSNTINEMVPGVRTTVCDHFLLDDGFCRITENPADLNIADAVLFHNADYNAALVPKPRKSNRPHVLWSLESPSNDRFRPGPNVINWTMTFRRDANIWYPYGHFRKLKSPVDVDFDEIWDMKNDSKTAVWLASNCFAKNSRTAVVDMLMKQGLHIDRFGRCGSRPPGCDGVNRQGDPCVAELVKPYKFYIALENSNCQDYVTEKFYEALISRMAVPIVLKKEIYVNVGAPKDSFIAISDFKTISDAVKYVNEVADDKEKYLAYHKWRTSYEYVNLD | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 302
Sequence Mass (Da): 34488
Location Topology: Single-pass type II membrane protein
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A0A183BAY8 | MPTLLFRFLILKNRYGQIVEVTKRPKSKWRPVALDTVELEKLATRKLRIGAKAAMQLAERLYTQGYISYPRTETNIFPADMDLASLVRVQLDDSRWSGFATRVLERGPNPRNGKSTDKAHPPIHPLKTGSNLQGNEARLYELVTRHFLACLSADAQGAETLVRLCVGKASVPANSSSSSSFSLPPTDLMTSEDGEMFESKGLVILQPNYLEVYPYDRWTEKDMPNFHLGDWILPTNIEVSNLFVFQFER | Function: Introduces a single-strand break via transesterification at a target site in duplex DNA. Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. The scissile phosphodiester is attacked by... |
A0A0N4YWP2 | MEVAKKEGMRLFEGIYVMTGGPHYETPAEVAMLREMGGDAVGMSTCPEVIVAAQCGIKVFGFSVITNMANTDIDDAVVVSHEQILKVATEAGSIKVATFLLAEKTTYKVCPIRVKVASLFHSRKVVDKNPTEV | Pathway: Purine metabolism; purine nucleoside salvage.
EC: 2.4.2.1
Catalytic Activity: 2'-deoxyguanosine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + guanine
Sequence Length: 133
Sequence Mass (Da): 14365
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A0A8T7AEH6 | MNFVALLLGLSVERLLTNLFHLREFRWLDPLFDWLTVKLKDQSRTGAVIGVAFSTFLIVLPVALASAMLSGTLFQVPYFLLAVLVLLFSLGPRDLKKEVDEYCAAAKEGDEVELCRVARELWEGELQHDPEIQVRLVRRAIFIQANNRIFAVVFWFLLLGPTGAWLFRVLDLMRRRLAFEYNRTEHDFCNTALVWAVRSVHGVFAWLPARVLIFTYAMAGSFDGAIAAWRAYLRKNEEESFRATNDLLDRVGDGAAGGLPDDLSATALDYPAVANYVDLAMDLVSRTLWLVWCPAIAIMTLTDLLS | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 306
Sequence Mass (Da): 34577
Location Topology: Multi-pass membrane protein
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A0A814ERD5 | MMSTTMEHDPASEELAAHPSRLPTHPKEMAEERKSEPEGIFSPSVLHPLDPLTANEISLTTKIIQESSYFQKYLRIVTIVLLEPEDKSIILNFQPNTEIHRRVTVFIRDPVKHVTLEMIVDLTKKTIKNVLELTNVQPGLTYDEIIAADSALRSDKNFLAAIAKRNLDVNSIVFYPFTACYRDQSDAASKRRIYRPLSAVSYGNEDNYYAHPIEGLVITVNLDDMTVEIEDHEVVPIPTNTANYNPESISTPNNVPYFPNGVRDDLKPLIITQPDGPSFKVDGYQVTWQKWRFRIGFNVREALVLHCIEYFDKARWRSII... | PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Cofactor: Contains 1 topaquinone per subunit.
EC: 1.4.3.-
Sequence Length: 697
Sequence Mass (Da): 78808
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A0A6A0H1V1 | MDESWECLSPLLHPAVAAGVKEFNFPKMTAVQAACVPNMLSHYEVVAEAVTGSGKTLAFLVPTLQIILQREYPIKKYEVYAMILSPSRELASQIHGVLQVLLKHCKEVSSLLLVGGGAVSEDVAKFESNGGHIIVGTPGRIEDIFNRCESGSTSLKLACRALEILILDEADKLLEVGFTETISTILACLPKQRRTGLFSATQTSDKVKLIRAGLRKPRRIRVMQSPQQ | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 228
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): 24944
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A0A183THC8 | MSESSRDNAKSEPGEPSSSQCPPEGNEVPSSSTSGTTGSFECNICLESAKDAVVSRCGHLFCWPCLHQWFETVRSRPSCPVCKAAISRDSVIPLYGRGGDHKTDPRSKIPPRPPGQRTEPQQGSRVS | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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.
Sequence Length: 127
Sequence Mass (Da): 13703
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A0A0N4Y2X2 | MALAQTIASFLGATLIGQMNTVVALDRFLATVFPIWYFQTTIRYPITVLSVAYGISVVALILNWVLVLTNPVEKYAQISSLCSFVGSTYPGFRDTLMYYRWVCIVIAAVMYIVMAVLIRKRFKITSQLFAPSMSKIQNNKIMRSHVTMALMSGRKIAAATVQNRTQTPFWVWLRNKLLAVQRQPVTPPPGLPTADGKAEYHNPLRFPKTQSARPGSAEAPSLPGGVHHLISENYYYTRDGRREVLPPKPLYKADGQHVEFATYTGDKLSRNREEELITQKEDPELSRLERFDRFAASKGPLVNMRPTPVSMGKHFGMLGK... | 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.
... |
A0A8T7D1D5 | PRGLSQAEQLPEPVFTPSTKAEEGEHDENIDFDSTVRLIGRELAEKVKSVSLQLYREAARFALERGIIIADTKFEFGTDSSGNLVLIDEVLTPDSSRFWPVDEYRTGTSPPSFDKQFVRDYLEGLAWNKQPPAPRLPADVIAQTAEKYKEGQKRLTG | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(... |
A0A8S9DYQ2 | MKIPPLDKAVDVIKQGGIVAYPTESVYALGCDPRKLATIHRLLDIKQRAIEKGFILIAADFEQLQPYLGPVDQTIMKKIMATWPGAVTWLMPVADNVPPSVRGNHEGIAVRVTAHPVAAALCRAADTALISTSANTAGKAPMRCAEDVGTELGSLVDYVLAGDVGDAVKPTEIRDALTDEIIRSA | Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosp... |
A0A7T4VIC1 | QHLFWFFGHPEVYILILPGFGLISHIIMQETGKKETFGSTGMIYAMISIGALGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWMATMYGTKIKFSPQMLWASGFVFLFTMGGLTGIILANSTIDIVLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWFPLFTGLYMNKKWLKIQFITMFVGVNMTFFPQHF | 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... |
A0A140X397 | TTTAFSSVTHICRDVNYGWIIRYLHANGASMFFICLFIHVRRGLYYGSYTFLQSWNIGIILLFTVMPTAFMRYVLPWGQMSFWGATV | Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membra... |
A0A814C3N2 | MQYLFILLNIVYGIGLLLFLNGFLLTRRTILQNSTDISSQQQFKNGSSEFNQIVLLVIDALRYDFIQPQQHTKLNPFYHNQMSHVQQLLIRHPRQARLVKLHADPPTTTLQRLKALTTGTLPTFIDFSYNFFGYEVNEDNILFQSHNNNKWNISFLGDDTWLTLYPTMFHRHHAYPSFNVYDLDTVDNGILEHLDELIKQQKSFIIAHFLGVDHCGHRYSPSHTEMSRKLRQMDMVILNITSQLKSNSLLIVVGDHGMTSSGDHGGDELNEIETAMFVYTNKQNYFTLLEDSSTTIHYSQMDFVPTLSWYLQILVPYSNL... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 373
Sequence Mass (Da): 43304
Location Topology: Multi-pass membrane protein
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A0A7J3HP20 | MNQRTLVNPFIPHNEEEIAEMMQTIGIKSLEELFSDIPREYIITEEPEFEGPLSEKEMINQIFRIASKNLTFPKLQLHIGQGAYLRYVPAAVKEVLRRSEFLTSYTPYQPEASQGILTALFEYQSLMAELLGLEIVNSSMYDWSTALGEACRMTIRLTGKKKILVGRYTFKQRLETLSTYIEPISGVVREIGYTPDGRLNIDELEQNLNDTAALYVEYPNSLGFITQNLDELADIVHRKGAYLITGVEPTVLGIIKSPGELGADIAVGEGQSLGLPLSFGGPSLGIFACRDDPKMLRNMPGRLIGMTEDVQGTRRCFTMV... | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
EC: 1.4.4.2
Catalytic Activity... |
G8YS25 | MKVITVIAQLLAITSWVDATSKQRVYRDLGTSSRVKYFHSRIPIHEANALLDPKVEGNFIGSYEVLKIGKNDHESAYLCYVPSDETTNSSEPETGIHDSYLYVEKEKELIEKGVRELPRSFSNKFCLFSNGLNGGYWTFAYCYGNKVVQFHDDTMRFMKTGKHYAENPDFVFTLGHFKKSKKKNRSKLEEDGIYLSDFTLHDEFSEPLSTNLGFANRQRYLKHTLNDGSICDITGRPRSIDVVYKCIPSSQGEAQIIDVQELKSCKYHMVVGVPSLCNIEEFSPDTFEDMSIDIDCKLIDQETKGESNTKQSDSLTTTHD... | Function: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Le... |
A0A0C5BCM0 | MARATKSRRPERNETRTSENAPNPVWFKPVMFGFMLLGFAWIIVFYLSQGAYPIPLGDNNKFNMLIGFGIIFIGFLMTTRWR | Function: Involved in cell division.
Subcellular Location: Cell membrane
Sequence Length: 82
Sequence Mass (Da): 9549
Location Topology: Multi-pass membrane protein
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A0A182EU79 | DELFIMLKKPEKGPVTVLLGAQWGDEGKGKIVDYLIAKDKVQVVARCQGGNNAGHTVVANGRKYDFHILPSGIIAEKCFNIIGNGTVVNLDSFFEELNHNKITNIPGWEERLLISDRAHLVCSIHMFVDGYSEDRLNINKIGTTKKGIGPTYSNKCFRNGLRVGDLVYDFNGFSLKFRELIKYYQGQYPDLEVDIDLELSKFKKHAEKLNELALVGDTVVALDELRSSGKTVLVEGANGTML | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Function: Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP... |
A0A967TX34 | YYLVLGLRYGKARHGVRERLGIYRQDLRRLLQGHKVIWVHAVSVGETRAAIPLLKALRLSYPDAQLVLSNVTETGRKIASTIKVVDHYIFFP | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP... |
A0A6U2NYI0 | MAVAVGFCTSSSSTQGASATEVIEILSDDDDPTDDAQPEEDDSMQLHASQMDKVKEQKSLSQTKKRDARGIFKMKPFNAFFLSGLKGYKEVKAKYFNFEKGLESKSEARRLALQEADKAWAQVALACQNFHKKRNGSYKFAFEACHDKLLEEKGKDLSKLGSTTQDAFTSSMTNCNNEIIASRLQKLCAAMGAEAELTRLRKKSGQRASLGTNDDSMSKPKRNISQQYRSVTYDRIATTIRQYPSQVDLNCIDYGYGTSHTRAKKRNDPVFRIEDYIAKPTRSSTNGVERPPLIKAGGSCFRRLIRAIIFTEGPSGANFS... | Function: DNA polymerase that functions in several pathways of DNA repair. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination. Has both template... |
E3M354 | MSDVPEDANAGCPGTGSAGAGKASGCAGCPNQGACATGQGPPPDADVPKIQDRFSRIKHKILILSGKGGVGKSTLTSNLARALASDPSKQVAILDVDICGPSQPRMMGVEDEEVHNSADGWTPVGIQPNLTLMSIAFLLGDKNDAVIWRGARKNGMIKQFLKDVDWGEVDYLLIDTPPGTSDEHISLVQFLLQAGTLDGALIVSTPQEVSLLDVRKEVSFCIKTKVPILGVVENMARFVCPNCAHTTLLFPTSTGGAEKMCQDSNLELLAQLPLEPALAKALDNGEDFFETNPDSTLAKSFMDLAEKVKAKLK | Cofactor: Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of NUBP1 and two labile, bridging clusters between subunits of the NUBP1-NUBP2 heterotetramer.
Function: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extram... |
A0A813QEN8 | MFCMAVTLLKVLIRLKNGQYHSTEIRDKYRILDLYKQIANELHLSIEQVKLLTIYRSTADGVQVLLYPSSYGMYFDESRTLDTFSILQNEQLYIDIGELFDESTLSMSPSSTASSTSSIVINESNLSPSVTNLQHYQAKPKPQKPVFDQQQHKTSSSITSPPKSMSKALKSSIGQLIRYSVPADNSCLFSSINFVLHSGKMDLASNKYLRNMVATKIESDEKTYSEAILGRKNSDYCKWIRK | 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... |
A0A814VB14 | MGLPMGNSLSPLLADLVMNDFIVKNRDKNKFPYNMLKRYVDDIILMSELDKDQIKDLVAYLNKIDKNNIQFTSEFENESNLSFLDVLIKVDKENHKFKTTWYPKPTAAKSLLDFRMGLLEEGHPLTWNQIAVHLPELKKQALEQLIRIWEKNKNRTNDTQTWGDEVGLKIVEFSLLRFDHASKRVQLLLKAHEYLPKLKKLNEQVEEKSQITWHEEAGDHCVEGVLSSPFDHSSAHYSMVEESLRRRREQAQHLLAKDEYILNVCAFPRMGCAEFTWPVLKSDPLSSWEQSICFPQEFISPIHPQMKIVKNMVERRKSKF... | Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
EC: 6.3.2.2
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Length: 471
Sequence Mass (Da): 54853
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A0A815JAK5 | MSSSTGANLTQVSINTKTDSHQQDRRVHQQRSLECFEIIWLDAHIDKKTNDNSNTITQLRRVVNNNLKTFDNPDQCSTYISSIQNQKIFLIVSGSFGEIVVPQVHALTQIELIYVFCFDKAKHEKWTNKYKKIVGAFSDIDSICDKLGVDVNSCTNDLMPFSAISSAEEINKQDPSFMWFQLLLDILLNMKHTDGTKQEMIDLCQERYKDNEEQLKYVREFKTYAPDKAIWWYTCNCFLYGMLNNALRTLDIGTLFKLRFFITDLHDQLKQFHSEFIHSTSIKAMTVYRGQGMSLEELKKFTTGGLLSMNYFMSTSTEKM... | Catalytic Activity: L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] + nicotinamide
EC: 2.4.2.31
Subcellular Location: Cytoplasm
Sequence Length: 941
Sequence Mass (Da): 108744
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A0A0S3IS07 | TLYFIFGAWAGMVGTSLSILIRTELGHPGTLIGNDQIFNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSIVETGTGTGWTVYPPLSSTIAHSGASVDLSIFSLHLAGISSILGAVNFITTIINMKSPGMTMDKMPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF | 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... |
A0A0N4YD47 | MERFNVQLSMIVNTCRATINNKDFVGWLERERFDLAFGHMFDICSIGLIHNAKIPSWIWLNSGSVMDYVAYYIGAPLIPSYVPPMMMEAGGEMNFIQRTKSFIGHGLTQFFWKRLIADPETALFRELISPDFPDLLELAAKCPVVMANTNNLYEIPRPTLAKIVNIGGIGMESRNAKPLPKNIDDIVAKGKGTVLFSLGSVTAAYKMPYEWKMAFLEAFRRFPDYQFLWLPQSDILHHPKTKAFISHGGYNSVQEAILTGMPLIAVPLFGDQPKNARLAERHGFGVILHKKEISIDTISSAIREVTENSRYAEKATRMLR... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 405
Sequence Mass (Da): 45960
Location Topology: Single-pass membrane protein
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A8TJU1 | FSSVAHIRRDVNYGWLVRNIHANGASLFFICIYLHIGRGLYYGSYMFKETWNIGVVLLFLVMATAFVGYVLPWGQMSFWGATVITNLLSAVPYLGDSLVQWIWGGFSVDKATLTRFFAFHFLFPFL | Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membra... |
A0A0V0J258 | MSTAISPRIAPRISLSMRDLHCLLMLLACCLGAEATECLKMLCHQTNTSDCHPCVGLNSEQLSRWRRYLDAILSDWRDTSHMPSYYEEIRNQPLCCTLQENGTCHLSLIYEPKVDPTRLYDLKCMDGNDMWTQFRCISGHNTRCCKGNFCNMPTDKEVDAVTRETPQRLHMIVVGAILALVLLLLLIGILLFSRYKRESGHSKAKRNSQNSPSDTCAWISNANGLGSAGDPLITKNTVPSIVAGFGNQRGVYVSGPPSMITSLGSGSATTNLPNPSFHPNPSFTISVPKTSEIITGGGNTTATATNSYAPVSGSAAIMSS... | EC: 2.7.11.30
Subcellular Location: Membrane
Sequence Length: 779
Sequence Mass (Da): 85707
Location Topology: Single-pass type I membrane protein
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A0A846NJ34 | MATETLSPERFRTLDDVDIDDKVVLVRVDINSPINPFTGEIMNDLRIRAVLDTLKELEGSKVVLISHQSRPGMGDFTSLSLHTSVLRSYLGDRVRFVPDIIGPTAIREIRRLESGDILLLDNIRLMAEEMMKAPPEVHANTLLVKTLSKHFNLYVNDAFSCIHRSHASLVGFPSHITSVIGRLMERELRALNRVLGSEKDKLVFMLGGAKPEDRIGVIKNIFESSPKDCSFLLGGVIAKVFLVATGQRLPKSVKKETAAHYEEVEMAKSLLEKYGERLILPVDYAYEMEGERVEEPLENIKNSQMVYDVGLKTIEKYLQI... | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
EC: 2.7.2.3
Subcellular Location: Cytoplasm
Sequence Length: 407
Sequence Mass (Da): 45330
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A0A183BD77 | MRKSEICKLKKVLDPARKSRNKRKSVKSSKKSRVPQYSTLTIGNGLMKKVRTKDSLDALIHSSIKEALELFEEDPKAFEVYHAGFQQQLTQWPDDPLQWIVNYVNEISRGRKIRIADMGCGDARLAMALGEEKKVYSFDLVAVNSRVTACDMAHVSHVLICFSQIPCLYWGSLKQSLVTLQSYDTNNSILQTISFLQNSISEI | Function: Probable methyltransferase required to silence rDNA.
EC: 2.1.1.-
Subcellular Location: Nucleus
Sequence Length: 203
Sequence Mass (Da): 23044
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A0A820CVZ6 | MSNIYIQEPATRGKVILDTTVGDIEIELFSKECPLACRNFLQLCMNGYYDGTIFHRVVPNFIAQGGDPTGTGEGGESATGTAFAAR | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 86
Sequence Mass (Da): 9247
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A0A5S6R1S5 | MRSLWKKFPFSGNDEEEDIISEVTSGSSLSWGTRIKLFALCFCFGIFFSILGSICVYLHNFTMFSVLFSFGSIMSISSTCFLMGPIKQLKKMADPNRWISSLIVVVMIVMTLFAAFYWKKGALCLLCVMLQYIAMTWYSLSYIPYARSTVRKCFEACIP | Function: May be involved in fusion of retrograde transport vesicles derived from an endocytic compartment with the Golgi complex.
Subcellular Location: Membrane
Sequence Length: 159
Sequence Mass (Da): 18163
Location Topology: Multi-pass membrane protein
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A0A5N5UBX5 | MPEESDDDTTPPEPAVRRLDDETGDGSDSDADDAPQTGNTPDSDDTTAGATDSDEPLDPEDDPDTPTADPVETPADDDGDAGDDPNTSPTTMADDPFDGYEVDTTPAVERDSLERDADDDEDGPDETDDIGDRGDASFDDGSPGVSGSVGDSAEVAQPGPVSEPEEFEGAPDDQEMPLADHIEEMVKRLGVVIVVMAAVSGVVFPFATYLINFLWFNYLPGTEEICRQVAQVGATNVDPQTACARVYHPLAVVLARLKVATLAGFVVALPLFVYETYLFMRPGLYPRERRYYLASVPTSLVLAAAGMLFAHHLVIPILFD... | 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: 425
Sequence Mass (Da): 45814
Location Topology: Multi-pass membrane protein... |
A0A183T1P7 | MRTDLVKVNDLQKKRPAQARCLEYVVTHTFVHRQVRAISTWVYSSHFSLALLSFVRGARRLRMALVGRVVVKTLLNSIFPDIQFTMEEEVNNQLPLLDIQVTKLADGKIRTTVYRKATNTMRILHFKNIDKEQETYGEIVQQDFIDHYDNNTYKAIMGLKWASAYCPQANFVVSLDDDFYANPRLLNQLLDRRTALLINQPYQLVGHVYENASPYRTWFSKWYVSLADYPWTHWPPYPAAGAYVTSMQLIRLMALEADHVAYLRFDDVFIGFLALKLNVQPEHDDRFMLSTRTCRIELHKAIACHTVGSPSTVLWLWEHR... | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 329
Sequence Mass (Da): 38507
Location Topology: Single-pass type II membrane protein
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A0A6A0GTX7 | MTVTYSRNVALSQKSFSVFLKLLFRWRGSVYKLVWRDLVVFTLVYAALSLVYNFALQDGGKRLFANVVTGVRENGRIEVSSLIFVLGFYTSHVMQQRHAFYSVIPCTDAFAMAVSAALRGRDSHVLRLRQTLVRYANLACTLTLTNICLPLKKRMPTAKHFIETGFMTEQESEIIQNLDPKAKGFGRTYWVPLVWATNVITRSETYVGDREKTTEISGLNTSRMLDELHKLSRSCNQLMSHDQEIIPLVYTQMVTLAVYLYALGAVIAGQFLDGDHTTEGLNYNYYVPAALLLQIGFYCGWLRVAETLINPLGEDDNDFD... | Function: Forms chloride channels.
Subcellular Location: Cell membrane
Sequence Length: 468
Sequence Mass (Da): 53933
Location Topology: Multi-pass membrane protein
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A0A183AT94 | MFQVLPASCFALGCWQVGRRRWKLDLLAKIDENVKKPPIPLPRDVNTSLDLPEYLPVTVRGQFDHSREVYMGPRALIADLVPDSVLECGNKIMPTPEEKSNSTQEQRRKHVPHLSLPGYFVITPFFLADRPGQSILVNRGWVHMDLLDPATRPMGQVKGTVTISGYNRYPEAALSMGPFSMLVGSPNKKDPHTHPQYFNRQVDDMAQTLGTLPIFIDATYGEFL | Function: Probably involved in the biogenesis of the COX complex.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 224
Sequence Mass (Da): 25244
Location Topology: Multi-pass membrane protein
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A0A814GNI0 | MEPFMTIMVAMDENNGIGLNNILPWCLPGDWNWFLTISTNTIDPKKRNAVIFGRLSYESLLKQDRSPLKHWHTIVISSNSEAIKQQSSETSVTVVPTFERAAQYSYDMFHNADQNIENVYVLGGVQVYDQAVKLKLVKRIYLTRIFATFNCDTYWTTLDLSGFKPVKRNSNEILSTEDGQIKEENGCKYQFQIYEIA | 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: 197
Sequence Mass (Da): 22708
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A0A183T6Z0 | MTKYNEMKVALQKLQTQAEFQNQVSNLTGRCWDLCYTGTPGAKLDDKRANCLKNCVERYIDVSNYTGRLAKISWMVGHNCIVIIPL | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer me... |
A0A846Q3R7 | MGKVVLIVGLPGTGKTTVVLRAVKLAKKEGIKLREVNYGTLMLEKALEKNYVSGRDGIRKLPLESQEELQRRASEEITGLREREDIVIVDTHMIVNTPRGWWPGISVKNLKKVDPEQIILIEAQPSEILKRRRKDASRIRDIEEIDKINKELLYSRDIAASCSVLTGSPVSIVMNKEGKLEEVAERVLNIIRXVVFGVSVLLSLSYIFLNKKFIYTPDYTRKKSIIDQWKREYGEARKKKDSRHVKRLEKKQDQIRKLESQLAMKTMKLFVITTIPFWLVFYLLSQNFSSLGQFLILPLSFP | Catalytic Activity: AMP + ATP = 2 ADP
EC: 2.7.4.3
Subcellular Location: Membrane
Sequence Length: 302
Sequence Mass (Da): 34793
Location Topology: Multi-pass membrane protein
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A0A0K8U1Y4 | MASIKLSNGLQLLSRNSTSRALSSSVVNSWRNYSNSRGDLETTTHTGQVFDKDDYRNVRFVNAKRYVNENWGIKLIDEIPPIEVTDRVVYCDGGDANLGHPKIYINLDKPGPQICGYCGLRFVKKDGHHH | 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.
... |
A0A813UYW1 | MLNGVRSLSYRVSAPAEHQLSQLRIKILNVKLPSSTKLVDVCVILEVDSKYSYRTEIIKKKHRPLSQITSSSTSNATMSTVLNSTSPSISATSNTSSHPTVNVNESFDVLVTNNSKILLKVIAPTRLFGTNDIGQVKFDIKTILNEYQMKRHTFQETSPPSYKTELPLENSSRRTADHLNNSGTSTTASERGSIEILLHGAILNESENTTNNSNETAHIENNTLLNNTRSLSICQQDHPQNSLTTSNRQLLTSLENHSIPTESAVLNSPIRHPQNQSSSADASQPSRRSILLKQPSARDVDTGTASPRRGSGSSSSDAVS... | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.26
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.
Sequence Length: 963
Sequence Mass (Da): 110040
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A0A2P2I1R5 | MSEEEQLSLYRDLARYPVLKDAYIVAEKNNSIVCESQWSTRNLSVLKQVGSMCTQVVTGEASSIPRHTPLLNNVVLIGRSGECSAMLVQSGGAGEKEETLVCYIFLQQPSQPSTIIDLSKTKLHGKVYSDGELGCLVFSPNSSQLAFVAEEHRPKPSSMLDPPSQEDEPSGRGQQFSRLPDWGEQFTGKHRSVVVVVPCKDTGSVPEKQSGRVVLNPPADYAGVGQLQWAEHNTLVGVAYIDASPRLGLIYCRIREAVIFHVSLNDGVFKELTPRGWWVGSPRLSPDNTRLVYLRGSVGGPHVREAQLVTRPWSSEPEIQ... | Catalytic Activity: Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide.
EC: 3.4.19.1
Subcellular Location: Cytoplasm
Sequence Length: 719
Sequence Mass (Da): 78597
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A0A814LLD7 | MRIVLHTSHADTTFLATPDISEILETLLKQEGYADKPRSQANEAYVAQFNKSHLALPPTRNVAIVACMDARIDPAKILGLEEGDAHVIRNAGGMVTFKDADLQDKLKKELHSTADHIAFLSIAKLEDSVRDDVDFLKSSPLLFKDVPVSGWLYDVKTGKLNRIV | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 164
Sequence Mass (Da): 18153
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G8YIW3 | MLARQYLKKNFAAPTRFFSSGKVAFQKTPEIYENGADRPKELISGAPAELTTKRVVRIYQEAKSATQSGQFNSSHWKLNWDVLGKGNRWENDLIGYQSSADYMQGTTMKFDTKEAAIRFAEGQGWDHYVQEPKKKHFRKKEYAMNFYHSSGPLKHIRTK | 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.
... |
A0A158R1A5 | MSWRVEDVYSDRCILLTGSTGFLGKVLVEKMLWALPSVGQIFLLIRPIKGMSPKERLEKVLQDPLFNRLREQRPHVFEKLVPISGDLMEDNLGLNQHDMQKICDQVSIVIHSAATVKFDEELRVAVEMNVVGTMRLIALCHKLKQLIALVHVSTAYANCDRAETEEKVM | 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: 169
Sequence Mass (Da): 19229
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A0A813T0N8 | MTESGDSFQLCFQLDNICTDPERFLSAISTYVNKVHVLNKRVSTAILAKSLSKQDFKFLQSIYPQITANFYIDKRQLLSKNSQLYSDVEEYILYDHLSNNVTFFPVNKEITISFPHETSRRPCSPLIPYCIELTNENNLRLLVSSTSECDNKTMEWFKQILLKKLSTWCQLKDACSSEQTTLKLINITQYQKQYEYLKQKYGKYLIENWQELTDPQKHVHEDIGKIICSVLGIASYLITYWNENACRNEKPTFVDFGCGNGLLTCILNSEGYRGIGIDMRKRRSWKLFDSSSTSYYRELTIDPHNTILFNLLLEQKFSYI... | Function: Adenosyl-L-methionine (AdoMet)-dependent tRNA (uracil-O(2)-)-methyltransferase.
Catalytic Activity: S-adenosyl-L-methionine + uridine(44) in tRNA(Ser) = 2'-O-methyluridine(44) in tRNA(Ser) + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.211
Subcellular Location: Cytoplasm
Sequence Length: 661
Sequence Mass (Da):... |
A0A6L7LW95 | MLVDVFEVLYLSLGLVFLYAGVAKVKDFQELLLAIEHQQFIPEFMTKNVALIVVGIELILALGFIFGVFLSVTLWTSLVMIIGITILSRIFQTGEKQNDCMCFGQDEVLLKSWKSWSRAILMIAGVCVGIVLFYLLPEVDPLSMSLDTLLISLIVLLLLSWVTDIAEVKNHAIDP | Pathway: One-carbon metabolism; methylamine degradation.
Function: May be specifically involved in the processing, transport, and/or maturation of the MADH beta-subunit.
Subcellular Location: Cell membrane
Sequence Length: 175
Sequence Mass (Da): 19551
Location Topology: Multi-pass membrane protein
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A0A6L8F9T6 | MIFILITVFIDMLGIGIIIPILPELIREFVGGSSALAGRWYGVLAATYAVTQFVFAPLLGALSDRVGRRPVILISLFGLGIDYLIMGFAPAIGWLFVGRLIAGVMGANVTTANAYIADVSKPENRARNFGLIGVAFGLGFIFGPAIGGLLGSIDLRLPFFASAGLALLNWLYGFFVLPESLPAEKRDVFRWRKANPVGSLHVLRTYPLVAGLTAAFVFVILAQRGLETVWVLYTGHKFGWDERANGLSLALVGIMSAIVQGGLVQPVIKRIGERRAVLYGLIWAVVAFLGYGLATAGWMLLVVIVVGSISGVAGPAIQSL... | Function: Resistance to tetracycline by an active tetracycline efflux. This is an energy-dependent process that decreases the accumulation of the antibiotic in whole cells. This protein functions as a metal-tetracycline/H(+) antiporter.
Subcellular Location: Membrane
Sequence Length: 397
Sequence Mass (Da): 42217
Locat... |
A0A814QTV7 | MQFVESGKFFVARLIDKAGVDRESHCALNSTCKKYDDNYRLTIDYFDGSLNVSDSKMLVESVGKYFDENGVLCYKRFCADLKKIYDSLRLQTRKQQ | Function: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Enhances the enzymatic activity of SPC and facilitates the interactions between different components of the tr... |
A0A947IP91 | MKSGAIFLVGPMGAGKSTIGRLLADTLRFDFRDVDREIEDRSGVDIPWIFDMEGEEGFRDREESMLAELSDAAQVVISTGGGAVLRGDSRKLMVAKGTVIYLKTSVDEQIRRTARDRKRPLLQT | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
EC: 2.7.1.71
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Length: 124
Sequence Mass (Da): 13762
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A0A8B7NX57 | MLQTTLLKGLRRLCLPRLQPCCHMSYVVLLPEDPVDTAENNALLRTAHGDLPNFEEITGEKCHAGVGKLALDLETGVWEIEEKIRDKPKSVSFDTVLKPLDALDAQLNFGWSTAKVLYIARQDKLPQKTYLGLHERARKARVQKFQSLPIYKACKVISEQEAPSLDSNKRRVLQKFLLESRLNGMDLSPTKADQFLSIINKLDQKKQQYRQKVQVSTSRFAYEITDPNIVQHFPPHLLERMSPSGSDTTRGPWHVTLKSDVYEGFMAHCSKRALRWNTWQAYNMRATRFIDPQLDNSVNIEEIRASRNDLARILGYSNFA... | Cofactor: Binds 1 zinc ion.
EC: 3.4.24.70
Catalytic Activity: Hydrolysis of oligopeptides, with broad specificity. Gly or Ala commonly occur as P1 or P1' residues, but more distant residues are also important, as is shown by the fact that Z-Gly-Pro-Gly-|-Gly-Pro-Ala is cleaved, but not Z-(Gly)(5).
Sequence Length: 728
... |
A0A183BD43 | MEKTDISKRAFGTAEEELSYYAPRGIMMWGETVSEALNMGRLAVRAVGENDVETYRPLTLLIEGPPKAGKTALAVEIAKLSGFPFVKILTSHKMIGYTETAKCAAMKKVCRSVVSVFKSFPHCYASKATVEQVLIFL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo p... |
G8H0K5 | IKLFTKETSMILKSNYLYFLISPVLSMMVMLMLWYNIPMFSNIMTMKMNLLIILCILSMGVYSMMVAGWSSNSLYSLIGSLRSIAQTISYEVSMILIMLCLILLIESFNLNNLSKYQYFQWFSLMNFPIMLIFYVSFLAELNRTPFDLA | Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.2
Subcellular Location: Membrane
Sequence Length: 149
Sequence Mass (Da): 17397
Location Topology: Multi-pass membrane protein
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A0A101E638 | MLTTVLMVMQVVVSIFLIVIVLLQKGKSAGISGVIAGGAETFFGKHKAKTLEGTLERLTVIGATLFIVLSIILTILMAR | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 79
Sequence Mass (Da): 8386
Location Topology: Multi-pass membrane protein
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A0A0B0HE01 | MLQTIFWTIIAIGLLVTVHEFGHFWVARKLGVKVLRFSVGFGSPLWKRTARDGVEYVVAAIPLGGYVKMLDEREGGVDEAELPKAFNRQKLGVRTAIVLAGPLANLIFAIFAYWAIFLSGETGLKPILDEPIPESAAAAAGFRSGDEIVEVGGESANSWERVIYQLVEYAVDGEAAPVSVVGEDGMQRELFLPAESLLVLTESQGAVSQIGLVQKLPHIPAVIGEVVTDSPAEAAGFQPGDRVTGVNGKPIQDWHGWSREIRENPGRGLEVEVERNGRLQLLQLIPGEKGSGDSVIGFAGVSYTDDVDFGRYRSEIHYTP... | EC: 3.4.24.-
Subcellular Location: Membrane
Sequence Length: 449
Sequence Mass (Da): 48241
Location Topology: Multi-pass membrane protein
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A0A1X1T7H5 | MSATSTVNVINGPNLGRLGRREPAVYGNTTHADLVSMIEQEAAGLGLSVSVRQSDSEAELIGWIHAAADAGEPVVLNAGALTHTSIALRDACAELGAPLIEVHMSNVHRREEFRHYSYLSAVATGVIVGLGVQGYLLALRYLASAQRRFSGGVAGSVPPP | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
Function: Catalyzes a trans-dehydration via an enolate intermediate.
EC: 4.2.1.10
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Length: 160
Sequenc... |
A0A099UCT5 | MDRIILGIDIGSTKICAIIAEIKDDGIPHIVGTGMHKAEGVRKGSISNIEQASTAIRNAVNDAKMVSGEQIDKAIISLSGAYVKSIRETAIINAPKNEIGLTEIRRVMQTAIYNADIPDDHTLIHALPYEFRLDGQSYAEDPMGMSASRLEAFVHIVAAKKTALENLKRAVSEAGIEIKNIVLSAYASSIAVLSNEEKELGVACLDMGGQTCDLMIYSGYSMRYCDFLSVGSHNITIDLATALNAHPSIAEEIKAECGKLILSEDDKTKSVKVSMMTGENVEKFVPLEVIHAVIFARVEETLRLLAKSIEKSGLKDKIGA... | Function: Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring.
Subcellular Location: Cell membrane
Sequence Length: 455
Sequence Mass (Da): 49542
Location Topology: Peripheral membrane protein
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A0A6I3DGE2 | MFRSGFVSLVGRPNVGKSTLVNNVVGRKVSIVSDKPQTTRTKIRGVHTTSSSQIVLLDTPGIHRPRTLLGERCNERSVQTLREVDVVCLLVEADSPIGPGDRFIANLVKESRTPAILVVNKVDLADAAAVAKRLSDSSGLADFAAFVPISALTGDGVDLLVAEINARLPEGPEYYPGGVVTDQPEAVLVAELVREKLLAIAREELPHSIMVTAEAFEEEEQESFNRRGRKVEGSEEGSEEGGQDGESSAPEKEEILRFRVTIRVERDSQKGIVIGHKGSVLRDAGTAARVEAEQLLGARVYIENKVKVDPNWQRRGHALD... | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Subcellular Location: Cytoplasm
Sequence Length: 324
Sequence Mass (Da): 35197
Location To... |
A0A3N4CY86 | MTAHAVTRHEIFQTSLISALAQGVYEDEMTLAELLGHGSFGIGTFNGLDGEMIILGGVCYRLRGDGSVSVPELTERTPYAVVTNFVPSLSRSLTGPMTREEFSRAIDAFVPSSNYMYALRVTGRFAWASARTVTKQDRPYRPMIEATDGEEIARHEDFSGTIAGFRTPLYESGISVAGCHAHIVDDDRTWGGHLVDFVLEEGEAELCLGTDFHMRLPLTEEFRTADLSEDMTEEIRRVEHH | Pathway: Polyol metabolism; (R,R)-butane-2,3-diol biosynthesis; (R,R)-butane-2,3-diol from pyruvate: step 2/3.
EC: 4.1.1.5
Catalytic Activity: (2S)-2-acetolactate + H(+) = (R)-acetoin + CO2
Sequence Length: 241
Sequence Mass (Da): 26765
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A0A7K0VAP5 | MADLIEIKGIKAFGYHGVFESENIAGQDFYVDIFMELDLTRASVTDDVNDTVNYAEITDLVVEEITGERVSLIEKLAARIADRITAAYPQIAQVSITVHKPQAPVSAQVKDISVTIKR | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.
Function: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
EC: 4.1.2.25
Catalytic Activity: 7,8-dihydr... |
A0A0K2Y4N6 | MVRTYQQSGVDLDKAQALIQAIAPLASQTYNESVLQGVGGFFGACALPSGYKEPVLISCTDGIGTKLKLAKEAHQLYNLGLDLVAMNVNDLICAFAKPLFFLDYFATSKLEPAQTLALIEGMAFGCKESGCALIGGESAQMPGVYKAGEFDLAGFCVGLAEKSDLAKKDKIKAGDILVGFKSSGLHSNGFSLVREILKSKPKNAPSLATLLTPTRLYTPLLALKDKIHSLAHITGGGLKGNLLRILPAHLSAQIELKALPRMPVFNWLLEHIDFSECLRVFNMGVGMVALAPLESLGALMRAGGFYLGALHTGGQSGAQE... | 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... |
A0A7M7HG44 | MEAGSLDIQHGLEEVNQELQHVEKQIERLLTKQQRLLQRKEQLEVQTSRLHELSLQTGSTDWEKSDYPWSAKLRSLCETVFGIKKYRPLQEKTMNASLSGRDVILLMPTGGGKSLCYQLPALVSKGFTLVVSPLLSLMEDQTMALEEIGVNATVLNSNTPPESVKDVHRQMIDARSELKLLYVTPEKIAKSKRFMACLEKAYKANLLTRIAIDEVHCCSQWGHDFRPDYKILGLLKRQFTDTPILGLTATATMDVLDDVKGILGLQGCQVFRAGFNRPNLFYEVRPKPSKQAEFVEELIKLINGEFKGQSGIIYCFSRKD... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Nucleus
Sequence Length: 636
Sequence Mass (Da): 72290
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A0A7N0U2M5 | MVDAHTARSIVGIIGNVISFGLFVSPCPTFWRIWKNKSVEEFKPDPYLATAMNCLFWVFYGLPFVHPDSTLVATINGIGLVLELFYLTLFYIYGDNKQRKKMSAVLAVEAIIMAAIAAVTLTVFHTHAKRSTFVGAFCVAFGILMYASPLTVMYKVCRDKSVEYMPFWLSFTSFANGIVWVAYALLQFDLNILISNGTGAVLGAIQLLLWTYYREIYPKCCAGDARQTDIEIMAATKVQDQV | Function: Mediates both low-affinity uptake and efflux of sugar across the membrane.
Subcellular Location: Membrane
Sequence Length: 242
Sequence Mass (Da): 27082
Location Topology: Multi-pass membrane protein
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L0AGU6 | MTGYTATVTVRLKHGVLDPEAETTQQALERLGFELEDLRSADRFEIDLEAESAEDARERADEMAERLLANPTIHDYDVEVDER | 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 1/2.
Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent ... |
A0A6J3KZK7 | MVRKMTDRKVLFACLVLITLLHPLVHMVSGEECTTPNNQTGNCLNIKTCNPLQEILQTQGHTATDFLRQSLCRYEGHAPIVCCPNDPNKEKRGILIETVYKYVPLRPPYCGFSNGEHTRVVDGKPAKLGAWPWIAALGFHNPQNPDTEPEWKCGGSLISARHVLTAAHCAIRSDLYVVRIGDLNLKRDDDGAHPIQMGFESKLIHPDYTPNIHNHDIAILRLVEEVPFSKYIHPICLPIEESLRNNDFVGYNPLVAGWGALRYRGPRSDVLMEVQVPVVSNAECKTAYSKFPNAPITDGVICAGYAQGGKDACTGDSGGP... | EC: 3.4.21.-
Subcellular Location: Secreted
Sequence Length: 366
Domain: The clip domain consists of 35-55 residues which are 'knitted' together usually by 3 conserved disulfide bonds forming a clip-like compact structure.
Sequence Mass (Da): 40424
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A0A075P7Z9 | MKEFDLIGRYFSNGGYKRKDVIIGIGDDCAVTKVPENQQLAVTTDTLVGGVHFLSDAPAKSVAYKTVAVNLSDLAAMGAEPAWISLSLSLPEVKEDWLAEFVDGLYELTQYYSVQLIGGDTVKGPMSMTITAQGFIPPGSELTRSGANPGDWVYVTGTLGDAGAGLDILQNTLEVKGEARDVLINRHYFPTPRVAVGTALRRIATSCIDISDGLLSDLNHILTASGCGANIHVDRLPLSRAITSAVDNDTAIEYALSAGDDYELIFTVSEEQKGNLETSLASTNVKATCIGQLSGHSSNLSLFKGEKPYTPKRDKGYEHN... | 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... |
A0A4W2HGF7 | MRRIRWTRRGLLCAGVYIRVLRLRATRAGWGRSGLLGVGCFSCSSVGRASGSTGLNLSWKLCVTIMRLVILDNYDLASEWAAKYICNRIIQFRPGQDRYFTLGLPTGSTPLGCYKKLIEYHKNGDLSFKYVKTFNMDEYVGLPRNHPESYHSYMWNNFFKHIDIDPNNAHILDGNATDLQAECDAFEKKIKEAGGIDLFVGGIGPDGHIAFNEPGSSLVSRTRLKTLAMDTILANAKYFDGDLSKVPTMALTVGVGTVMDAREVMILITGAHKAFALYKAIEEGVNHMWTVSAFQQHPRTIFVCDEDATLELRVKTVKYF... | Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-fructose 6-phosphate: step 1/1.
EC: 3.5.99.6
Catalytic Activity: alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-phosphate + NH4(+)
Sequence Length: 523
Sequence Mass (Da): 57704
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A0A2G6DWP3 | MPEVDYSLYLVTDPAMCAAHGLRHVVHRAVSGGASIVQVRAKNASTAELIAQVQMLRATVGVPVLVNDDVDAAAHAHGVHLGPSDTDPLSARQALGPSALIGLSVSSADQAQAAAQLPAGTVDYLGVGPVWATATKPNAAAPLGPAGLPAIVRAAAGLPCVAIGGIDTARVGQLRGLGLAGICSVSEICTAQDPGERAQALLRAWQGPHTPAGPARPASRTDPA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-met... |
A0A173XP32 | MEFYNSEENNRIRHVVNWIVDITVVIAFAWFIVYAYGTQIPIAGHSMTPLLQSEDVVLMDRLSYDFGKPDRFDVVVFEREDQKMNVKRVIGLPGETVQIKGGQIYINDELIEQPEGAGSISLAGIAENPVKLGEDEYFLLGDNRDSSEDSRFSNVGNVSGKQIQGRVWIRIAPLANLELIRSK | 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: 183
Sequence Mass (Da): 20662
Location Topology: Single-pass type II membrane protein
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E7CCA5 | MSTLAPLRLLREPWNASEGNQSNATAGAGGAWCQGLDIPNELFLTLGLVSLVENLLVVAAILKNRNLHSPMYYFICCLAVSDMLVSVSNLAETLFMLLMEHGVLVIRASIVRHMDNVIDMLICSSVVSSLSFLGVIAVDRYITIFYALRYHSIMTLQRAVVTMASVWLASTVSSTVFITYYRNNAILLCLIGFFLFMLVLMLVLYIHMFALARHHVRNISSQQKQPTIYRTSSLKGAVTLTILLGVFFICWGPFFFHLILIVTCPTNPFCTCFFSYFNLFLILIICNSVIDPLIYAFRSQELRRTLREVVLCSW | Function: Receptor for MSH (alpha, beta and gamma) and ACTH. The activity of this receptor is mediated by G proteins which activate adenylate cyclase.
Subcellular Location: Cell membrane
Sequence Length: 314
Sequence Mass (Da): 35440
Location Topology: Multi-pass membrane protein
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A0A2E4R5A1 | MSWNSAADFFAMGGYGLYVWGSVGVTVAALILELFVLGQRRKSALSRIKRASTTERNDDNEKQT | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 64
Sequence Mass (Da): 7085
Location Topology: Single-pass membrane protein
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A0A0U2UHD1 | MFVTNWIKRWIRRSLFVKILMYTALLSLIPYVLFSIYFLIEVKALTKKMIHETSSNNILQASVSLEERTRRLNEQWGGKTDKASRELLAGELLDIAVYGYKPMAYILDTNGAVIAKARNDLEPEVHIDLLEAHHSTILDHKSGHVTVNAPGEKVHLLYMSLDKAGWFIAYLIPESRLMSIAAGQAEDYADTQVYKLVQRMSFFLFIGMLLILFFSYFFSEFFTTPIRQLTSALIQRAKGFEIDPLHTKRSDEIGELIHTFNYMDSTIQKLITELHSRSNQLEENVQKRTRDLQEANDLLQQTYSKLKRSEKSRSELIVQV... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 552
Sequence Mass (Da): 63425
Location Topology: Multi-pass membrane protein
|
A0A1Y1MPY7 | MTAVTSDVRFRRIITLHSICTSIYTSFIIFILVYTHKIYEIGKRSSLPVIGVLIVGECLKVVFRPFTSETSTKEKQNKPKKFNLSSKLKCALVLCTSIVIYYCLAVLFGAPFLSSHEETFMFALLLTVLTVLPSCLAVGADVTIAILIDLTSFEGDIITETIKQNICVTLVGAWLGAVVIPLDWDRPWQAWPIPCSLGAVIAYMCSNLFNIVGMSSKTLKKKTGRYNL | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 228
Sequence Mass (Da): 25299
Location Topology: Multi-pass membrane protein
|
A4EAH2 | MHNKRVLVAMSGGVDSSVTAYLLKSQGYECVGATMRLTCPAPDPTTGMSKVDRDIADAKAVAERLGIPHHVLDLQQTFDRNVIERFVNAYQEGLTPNPCIICNRHIKFGALLDAALDMGCDYIATGHYAKTSQAADGTWQLHRGEDPKKDQSYFLYSLTQERLAHTIFPLAGLDKERDVRRIAAEQGFTNAQKAESEDICFIPDGDYADYIERRCGHTAAPGDIVWRDGSVVGRHNGALRYTIGQRKGLGVAMAHPVYVTGIDAANNTVHLGEAEDLTAVALTADEWIWSAPDARMEAELDAGGIRVGAKYRYRQKDQAA... | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
EC: 2.8.1.13
Subcellular Lo... |
G9J027 | AYSSIAHMGWMTAILAYNPTMTLLNLTLYILMTTTTFMLFMFSSSTTTLSLSRSWNKMPLITASILVMMLSLGGLPPLTGFLPKWMIIQELTKNDSIIMPTLMAITALLNLYFYMRLAYSTSLTMFPSTNNTKIKWQFEPTKRMPCLAPMIIFSTLALPLAPMLSVLN | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Catalytic Activity: a ubiquinone + 5 ... |
A0A1Y1MYG6 | MRTFLLLLAATFINAENSSTSIAFVERQINLEINETKKLSVTVTNLNNSGVLLSFDVLQEDLVYVYPRKILLEAGNKTYHFTIEGISPGHSDILAITNDSSITIPQEHFSVNVYKKKILDIVSQIIGWIFIISWGSSFYPQLYSNYERKCVIGLNFDYLALNIVGYISFAAFILNLYFNLEIQDEYYERYPRGQIPVKLNDVVYILHGTLAIFVTIGQCCVFERGHQKVSTTAKSLVTLIVSFYITCVALERLKFLKWLDFLYYCSYVKLAITLLKYIPQAYMNYKRKSTSGWSIALVFLDLNGGLFSILQMMLDCYNYD... | Catalytic Activity: H(+)(out) + L-cystine(out) = H(+)(in) + L-cystine(in)
Subcellular Location: Membrane
Sequence Length: 361
Sequence Mass (Da): 41513
Location Topology: Multi-pass membrane protein
|
A0A1S1L9K8 | MSEKLKLVSRVSAINWNRVPDEKDAEVWDRLTGNFWLPEKVPVSNDIPSWNTLTDHEKQLTMRVFTGLTLLDTIQGTVGAVSLIPDAITPHEEAVYTNIAFMESVHAKSYSSIFSTLCSTRDIDDAFRWSEENPNLQRKAEIVMEYYRGDEPLKRKVASTLLESFLFYSGFYLPMYWSSRAKLTNTADMIRLIIRDEAVHGYYIGYKFQRGLERVDEAKRAEIKEYTYDLLYELYENETDYTEDLYDEVGLTEDVKKFLRYNANKALMNLGYEALFPREETDVNPAILSALSPNADENHDFFSGSGSSYVIGKAVNTEDE... | Cofactor: Binds 2 iron ions per subunit.
Pathway: Genetic information processing; DNA replication.
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
EC: 1.17.4.1
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deo... |
A0A1V8U1V3 | MAARFSYPRAVRRLILAVTVPAAAAVAIQDNLYEITPVTGTSMSPTLSPDYNLTGRCDRVLWSKVSPSANLVRGELVTYRSPQRPDRTAVKRVVALEGDTVILDPRRRPGGVDRSSGREEADRTQAESWDQMGPKFEVPFGHVWVEGDNWRSSNDSNNFGPISKSLIIGHAPTIVYPWERMGTKPWEDRRRIGTRVVYGKQGVPPEGFRDMFE | EC: 3.4.21.-
Subcellular Location: Membrane
Sequence Length: 213
Sequence Mass (Da): 23870
Location Topology: Single-pass membrane protein
|
A0A537VVW3 | MPAVGILGLGVSFRRAPVELLERLAFDDADLTKAYLHAQDLDGLDEVVILSTCNRVEAYGNVRSYHSGFIALKRVLVETRGIEHEELTDPLYAHWERDATDHLFSVAAGLDSMVLGETQIQRQVREALRRAETEGAAGPMLDAVFHAAVRAGRRVRQETGLGAAPDAYVAIGTDLADEALGGIAGRRTVVIGAGGMAELAVHHLRGRGVGPVRVLNRSLEHARALAERTHADHGGLDALPDALEDADLIVSATGAAGHVIARGDLVRAAAGRAGRALVVLDLAVPRDVEPSAAGLDGVRVIDILSLRERIGDHSPQTVED... | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
EC: 1.2.1.70
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tR... |
A0A958HWU8 | MMLRNKIVKLAVAVGVLTVTLLFTTCSDSEDNITNGEHEAAHWGYEGEDGPEHWGDLDPDYAACSNGIHQSPIDIDTAAVIHVDLPNVQINYQASTLNVVNNGHTIQAKNSAVNYIEVEGTRFDLLQFHFHASSEHTVLGSAYPMEMHLVHQNAAGALAVIGVLITEGLENPVFNPIWDNLSALTAEDFPLANPLNLDDLLPMDQRTYRYTGSLTTPPCSEIVSWLVMAAPIEMSPAQIQAFEAIHDGNARPVQALNGRYILFDASMN | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 268
Sequence Mass (Da): 29290
|
A0A097RN14 | MSLFTTIMASSMSLLGLGRLTALNTARRILLNPTRSTSTSTWRLSVNKGTDTLLVPENQKLDLSPLSGVPEEHITTRKVHIFVPTKSAMQSGINGTKKWKMDFDTRDRWENPLMGWASSADPLSNMVLTFSSKEDAIAFAEKNGWSYDVSEKKSSKPRVKSYGANFSWDKRTRRSAK | 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.
... |
A0A8T6S0X6 | MPPDTGGPTVHKFGGSCLATPELTVRCARIVTESASAPNGTLIVVSALKGQTNLIREMLDRLLAGGNGIDNFMEEVRARHQYIAQSTIMDRHIRSAVMERVETLATRLERLLYGVIYTEELTPRSRDQALTHGERMSAHLFAGVLADRGTTAIPLEADEAGVITDGVFGSATADIEATSLHLGSTVQQTLERGDVPVLTGFFGSDVDGHTTTFGKNGSDYSAAVAARAIGSPVLTLWKDVSGFMSADPNVVARARLVPLISYEEAAELAYFGLEVLHPRTVEPLRPAGIPIQIRDIHNPDSPGSMISPRAQSNDRDIKSI... | 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: 435
Sequence Mass (Da): 46182
|
A0A1Y1MSD6 | MATVLYLVTIFVCIQIGYALKCYKCNSQTMDGCKKGSENLQETNCSLEHPDFNQFCLLKFVYDEQQNKDNVLSGCEIAAKSTILSTNMTQCQTDGRYRVKECIVCDTELCNYTNTGSSKKTSIFCTAVLFVLYNFLR | Function: Required for homeostatic regulation of sleep under normal conditions and after sleep deprivation. Important regulator of the Sh K(+) channel, acting as a signaling molecule that connects sleep drive to lowered membrane excitability, possibly by enhancing K(+) channel activity and thus reducing neuronal excita... |
Q5BK44 | MGILGPRPLKLARSLRAPRGARLRSLTPDPDSWQASPAKKARVEQDEPATPPSSPLSAEQLVRIQRNKAAALLRLAARNVPAGLGESWKQQLCGEFGKPYFVKLMGFVAEERKHHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGPNQAHGLCFSVQRPVPPPPSLENIFKELSTDIDGFVHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLNGLVFLLWGSYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGCRHFSKANELLQRSGKKPISWKEL | 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... |
A0A2Y9QTU4 | MPAKGRYFLNEGEEGPDQDALYERYRLTSQHGPLLLTFLLVAITACTALIIIEFINWDTSKLKSLLGTAIVVLVVFVALYLLVYVDCLVRRGLRALALLIWACLMTLGYVLLYDSRMKGACAWEQVPFFLFVIFVVYTLLPFSMWGAVAVGVVSTVSHLLVLSILAGVHEMPSDHIELKLLANAIIFLCGNLTGAFHKHQMQDASRDLFTYTVKCIQVRSKLRIEKRQQENLLLSVLPAHISMGMKLAIIERLKEHRDRRYMPDNNFHSLYVKRHQNVSILYADIVGFTRLASDCSPKELVVMLNELFGKFDQIAKANEC... | Cofactor: Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro).
Function: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling.
EC: 4.6.1.1
Catalytic Activity: ATP = 3',5'-cyclic AMP + diphosphate
Subcellular Location: Membrane
Sequence Length: 1016
Sequence ... |
E5V774 | MVIYISNDEMEKCKKIVVVGSTNVDLIARVSHLPEPGETIGDAEYCLSYGGKGANQAIAAARSGGHVSFISCLGDDAYADTLITSFVDSGIDVDYIQKCVRHSTGIAFIFVAENGENCIAVAPGANNLLRGERMDTILPVIKEADALVLQLEIPYESVISLIEYAHTVDTKIILNPAPAKQIPSYILEKVDILILNETEAMLIAGQSLDFSEPIGIARSLLRRVGQVVILTLGEKGSVIVSDEMEKQIPSYVVNTVDTTGAGDTFCGAFVAQWVEGVDLQDCVQFATAAAALSVTRIGAQVSIPYQKEVIEFMRNRIL | Cofactor: Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.
Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step ... |
A0A0S7EDF8 | MYIDNKYYRLSTILYRVKDIVDKAISNNYFWLRAEIGQLKEDRKGHLYLELVEHKDGVVLAKCRANIWQSNAYVIKKTLGENANEILKNGAEIMCYCEVTFSNLYGMSINIHRIDLSYSLGEVERIKQENLRKLVERGYHQKNKELYLPAVLQRIALVSSKGTAGHADFIKQLEENEYNFVYHLDHYDCQVQGDGAVASIQEALSEIESDAYDVIVLIRGGGSALDLDVFNHYELAVTLATSHTPVFTGIGHETDSSLADFVANRYFKTPSAVAAYIVERTALFYTDISRMYDGIMQSYKQCITVEQHKLEVAEKEIRLY... | Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular Location: Cytoplasm
Sequence Length: 493
Sequence Mass (Da): 56690
|
A0A1Y1KVI4 | MKPIRFGVLTVSDTCFSKQNQDLSGPKLQECIRASFPDASIIATRIVPDEKEMIKNALLEWSSQGVMDVILTTGGTGFAQRDVTPEATKAIIDKEAPGLSYAIISKGMAVTELAVLSRAVSGIKNKTLIINLPGSVKGASESFGFIKNVLKHAVAHVREDRETIKCDHKHIRDLSPSKVKIHQSAYRNRNSPYPQIDVDVALAMIFEKLPIASVTECVDISKSLCRILAEDVYAKEPMPPFNASIKDGYAVKTSDGAGVRKVRNVVAAGDVPDSARPLDDDEIVSISTGAPVPQGADAVVQIEDTVLVQASSDGSRELLV... | 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 ... |
A0A6A8MNN8 | MLTQLDNLFAQSKSQNRAILIGYLPAGFPTQRKAKKIIKAMIDGGVDAIEIGYPYSDPVMDGPVIQAASEEAINNGAGVSEVFELLKTSVDFGAPSVVMSYWSPIEKYGVDRFAHEVAKNGGSGIITPDLTYEESNNWKIEAEKNSLNRIYVVAPSSSNDRLAKVTNECSGFIYAASLMGVTGARTSVSVNAKQLVERIRSVSNKPIAVGLGVSTSQQAQEVATYADGVIVGSAFIKIVQEFGAGRNGLKKIKQLAKSLSEGIKSAR | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
EC: 4.2.1.20
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-s... |
A0A6I3D3G1 | MALDATDPPEKPGGTAPHVIVDEIDDPVMCVEDVHHLSKVRRLRNGDLVSATDGRGSWRWCAFENASLSVVGDITVEAAPSPRLTVGFALVKGSKPELVVQKLTELGIDSIIPFIAERSVVRWDDAKTERQGERLVKVAREASMQSRRVWLPTVAPVARLSDLISSEGVVRADRDGRALSSGDTTVLIGPEGGWSPAEADMTSVVGLGHTVLRAETAAIAAATLMVALRDGFVA | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
S... |
J7HKL5 | MESRFKLKVESHQSCCAILERGPVIKISSTKPRTRHYESGLKKMPNSSSSKVPSIKAQHRIAKKRAVRRRRIDLDCGCSIYIHINCAKDGNGFTHMGRHHCASGREFRFYLGGSKSPLFQDVQRGGSTLHAHKDIPHSNPVQPQPEESTKSSQSVPELPSLDGIDSSFWDDIFE | Function: Strong activator of the late viral genes promoters. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. Also suppresses the host basal defense by interacting with and inhib... |
Q14Q27 | MLISEKFIDNYAAALMDLALETKKNDHFLEVSNIIVELFKQEPDYIKLMMNADIPKEERKNILAKPFQKVIDPLILNALFLLIDREAFCYVRRIFKRLRKLINISYDVQYGNIYSTQPLTKKQITTIETKLSKKFGYHIELVNKIDSSLLGGVRIKIKHEIIDGSIAGQLETMRQKAIHNK | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A0A1Y1L6Z0 | MILIHKHEDNLYIFIRDWLIHYNYTTSTYTEFQIHQPTDVREKLSEDRNVAAVSASKDNRLIAVTLCNKQLVIYDEKLNVIANVVCKRAACALTFTDDDDLLIADKTGDVFVYKLDRQPELLLGHLSMLLDVAVSECGRYVITCDRDEKIRVSHYPDSYNIASYCLGHEEFVTHLKMYGDILISAGGDGTVRFWDFVNGRQLNVVNTNDHLPDKAVVAEFRKEMGVENADVTALPIVDLQVYKSEQSAYLGVRLLGSDSVQVYRLQNASDVRLVDVLTVPSLLAFHLGERLLVVTERGFLHYTVAPNKLTKTDVSDACFE... | 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: 363
Sequence... |
A0A7C2ZRS8 | MFRLGLYKVEVIITYRKELRDPESEIIHKDLILKKGYANVKKVTTGKYFSMLVESDTKENAISTVRELCEKLRIYNPIAQEIEVFVRE | 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 1/2.
Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent ... |
A0A6I3CH83 | MKALFVALGAGLGAPARYVVDYYVKRAHSSLIPYETLGINILGSFILGLVIDGNQNVSLLLGTGFAGAFTTWSTLSVEQHSLLKNKRYLAAVTYLIATLVLGVGAAALGIYLTK | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 114
Sequence Mass (Da): 12047
Location Topology: Multi-pass membrane protein
|
V2YEB6 | MSDTMNLFEKAPVPQAVLKNALPAMAAMLMVLIYNLADTFFISQTRSDILVAAVSLATPVFLIFMAVGTVFGIGGTSVISRAFGQGRAEHAKKVCSFCMWGCVAVGIIMSLAFLFFMDQILTLIGASTDTWEPTKTYLTIVALGGPFVLISVCYSNVLRAEGQPNKAMAGQVLGNLLNVILDPIMILAFNWGIAGAAIATVIGNVAGAGYYILYFLQGKSTLSIHIRDFSVKDQIFTGVLAIGIPASLGSLLMSVSQIIVNARMAGYGDMAVAGMGVAMKVTMMTGMVCIGFGQGVQPLLGYCVGAKLWERFKKIMRFSI... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell membrane
Sequence Length: 596
Sequence Mass (Da): 64639
Location Topology: Multi-pass membrane protein
|
A0A6I3HR18 | MTIETIVAELTAANLDVRTDVPLAPLTTYGVGGHGACVVKVTSTDQAISVGSILRRFPDVETLVIGRGSNLLVADSGFNGVVIVMSPSVTDKEVAINGDVVEANGSMLMPVLARRSVGAGRGGLEWCVGIPGTVGGAIRMNAGGHGADMASAVVDATVLSLRTGQTALVDAQRLGFFFRGSALLSHHVLLSVRLLTIAQDAAIGTNVINEVVGWRREHQPGGRNAGSVFVNPGSGDDSSGALIDSSGLRGFTIGAVQVSEKHANFIQAAEGATAADIAAVMAHVQSTVESAHGIRLYSEVCLVGFSSDLMTRFTHPSHTA... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 338
Sequence Mass (Da): 34952
|
A0A673M858 | MMSLKELCAYETPSVAEMQNFMLADRRPTGHVNQVWPNVYIGNEVAARDKSMLYNMGITHIVNAASGPPHVNTGPRFYRDMDIDYYGVEADDSSDFILSVFFYPTARFIRAALSKNGRVFVHCLMGVSRSATLVLAFLMICEDLTLMEAIKAVRQHRDICPNPGFLNQLRHLDMSLVRERKKKLEAYKL | Function: Dual specificity phosphatase able to dephosphorylate phosphotyrosine, phosphoserine and phosphothreonine residues within the same substrate, with a preference for phosphotyrosine as a substrate (By similarity). Involved in the modulation of AMPK and MAPK1/2 signaling pathways.
EC: 3.1.3.16
Catalytic Activity:... |
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