ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A0S8ASD6 | MIDWFTVSAQIINFLILVFLLKRFLYGPIIRAMDKREEAIAGRLNEAGQKREQAQKEIERYIEKNEDLDSQRADMLAAAKEAAEQQKKELIDMARKEIDDIKARWREAVSQEKEAFLGNLRNRMAHELYALARKVCSDLADMSLEEHMTAMFLKKMSALEQEELDTIKTKLKDSGEGITVSTSFALPEQKLEAISQTVRRITGLDVPPKFVQSKDILCGIELRAHGYTLGWNLDAYLTSLEKEFGKVIGS | 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: 250
Sequence Mass (Da): 28544
Location Topology: Single-pass membrane protein
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A0A2E6H0G4 | MTKFILLDIEGTTSSISFVHEKLFPYSFERMEEFIKKNKEVPEVQKILSELSAEQGCGLSLSAAAELFQTWIKEDKKHGLLKQIQGLIWKGGFESGELKGHVYPEVPQNLKSWKEAGIKLGIYSSGSVEAQKLLFKYSEAGDLTSLLSSHFDTKIGHKREVESYENIVLELGVPAEQVLFLSDITEELDAAKKAGMKVTQLFRDEVPGNPAHPYVKNFDELEV | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into t... |
A0A336MA29 | MIRRFFATFFEYQGNSFEIWPGNTSTTVGTNLFNKSSTLESLSWLYTCAPCFPVNADKISIIQVPSVFYETLVAKSSKAKNRIKLASLYLGTGQLEHNLVTAIHDNLKSNKNLTVDILLDFTRGTRGDINSKTKVLPLLNESENCVLSLYHTPVLRGLTKRLAPPRWNELLGLQHMKIYLFDDTVILSGANLSNDYFTNRQDRYIMIEDKRVADFYSNFLSKVQEFSLKVDKNGNESLHEKWKLSPYESSHKEFSVAAKKLITDYFNDTWEEQNRINYNGQSADTWIFPTIEMGQIGIHHDSHIVKRILASALPQSSLKM... | Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Function: Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-... |
A0A2D4K408 | GINTESEEQKPKRLHPQKSMDDGNLQKCFPKLPVQQASAVYAGKASGCNSTGMKGPNALPLSFKEATLAKKFALKTRSQITKRKRMSLIKEKKAAQTLSAILFAFIITWTPYNIIVLVNTFCNCIPKTFWNLGYWLCYINSTVNPMCYALCNKNFRTTFKMLLLCQCDKRKRRRQQYQQRSSVIFHKRIPRETS | Function: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover.
Subcellular Location: Cell membrane
Sequence Le... |
A0A7X2YY14 | MSRSNDSERNVVDDPRMLSANNNNSVSSTDSVNNPIITNSTNSPGLPDASSIKDTGKDWPLAAAFQFLSRFPVPVEVNFTPGVLRRSAKYYPLVGFAIGAALGLAAVGIAWVLPPMPAAVLILALWIWLTGGLHLDGWMDAADALLSYRSRERMLEIMKDSRVGAMGVIACVLLLLLKMSLLYTLIGYGYAQVGAALLTAAIWSRWFMTYAMQAWPTARQGEGLAGNFRGLKTGSIAVSTAAALLLSAAGLTAITSLEQGNDPGSLMLLYCVAPCISWLAGTLAASRISKRLGGLTGDVYGALNEGIEAAVLLAAVICLG | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-riba... |
A0A0S8AGK9 | MIKRYPIKRRMRKKFGQHFLFDKNILKKILACSNVTADDMVVEIGPGLGSLTNIIAQRAKKVIAIEFDKKLIDRLKDNVASSPNVEIIRADALKFPYESITGHFKVVANIPYYITTPLLFKLLEYKETIPTMTLLMQKEVAKRVVASPGSSDYGVLSISAQVYTKPVLKFQVSRKAFSPPPDVDSAVVHFEVSPVPRFDIQDVLLFTDIVRTAFSQRRKTIINSLRKFEGIGDALEAAGIHAKLRPENLSIEDFARLSNIMI | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) +... |
A0A2E5JI66 | MRAFYLNNLANAQVGQKLSIEGEGFNHIKVVRLKPSEEILLLTGQGDNYLARLEVLGKKSAIVEVLRYEHKPQLNALTLAIGLVKKDAFDLCLKMAVELGATTIIPLETRYSQRYELNYERANRLLIQALEQSNSAWLPKLLPVTAIESLSQEIVDNCEKYSNLIIMGMANSTLPAKLPELGTSVMGFIGPEGGFSEDEEKLLAKLPNASTIHLPTPILRAPTALAALGGVIFTKQRVLD | 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... |
A0A0S7BYJ5 | MNPAIPEIEIDRSSGFCSGVERAIKIAEDKLLQEEPIYCLGNLVHNEEELERLSSLGMRFIRHDEINGEMKTVFIRAHGEPPETYSILRNNNASVIDATCPVVLRLQHKVKESSRQFRETGSGLVIIYGKPGHPEITGLLGQTEGNAILISKLEETGSIDYNQPLHLYAQTTAGEEEYASLCRRISENSLQLTGRNDLVTVHNTICRQMSQRAPRMRAFAQKHDVIIFVTGSESSNGRYLSGVAREVNPETHVVGSPSDVENWFAGARSIGITGATSTPLWLMDEVAGRIKAIVENNL | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of is... |
A0A2K2HD23 | MLPRSTIPGRRRSPDSASVVTARPVLPPRCCNSGGHSSRLLLPVVPVAEEPLVLDGAAVERLRLWRARPGEILTFVDPRQTAWRGRLERDGARWRVVPFQPLKRNPAGPLRIDLFQALPQRERFELVLEKATELGAGRLVPYQSERSISLAERDARQKKSHRWPELVLRAARQCRRSELPELYTCCGWNEALDMGSRADLRLMLYEGGCSQQMGEALAVSRAESLALLIGPEGGFSDAEVAEAVRRGFQPVSLGPRLLRTETAAIAAIAVAQACLGDFR | 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... |
A0A3M1KRC8 | MVLPAEVLIIGVVALLVFGPKKLPEIGSSLGKSIKGLKEELENTSSEPEKPDN | 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: 53
Sequenc... |
F4KVN0 | MFFKKQCSLFLLLNVLLCATLTQAQDNTPTVGPAQGALIIVGGGKVGPDIWARFIELAGGEGANIVVIPTANEDASIATGVSVEKDLLQRLGVDNVTILHTRDRKQADDPGFVASLRNATGIWFTGGRHWRLADSYLNTLAHREFKALLTRGGVIAGTSAGATIQGSFMVRGDTKGNALMIGDHVEGLDFIHNVTIDQHLLTRNRQFDLVEVIRQRPELLGIGIDESTAIVVQKDTFEVIGNSFVAIYDAKNFSADASKTTGEAASSGPFYFLGKGQRFDLKERRVLRR | Function: Exopeptidase that catalyzes the hydrolytic cleavage of multi-L-arginyl-poly-L-aspartic acid (cyanophycin; a water-insoluble reserve polymer) into aspartate-arginine dipeptides.
EC: 3.4.15.6
Catalytic Activity: [L-4-(L-arginin-2-N-yl)aspartate](n) + H2O = [L-4-(L-arginin-2-N-yl)aspartate](n-1) + L-4-(L-arginin... |
B3MPF8 | MSTTIFMYAICLAVLSNLLSVSAIRCHDCNSHEDEDCATLVVNTPRAQRDEQFLKECNGKDGLVPFCRKTVIKFEVNNNRRIVRNCGWIPEKVQNACFTADNEGYKQTICTCNGDGCNGASTLLGARQVGYSLIGTVVSLTLATVLRN | 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... |
A0A133XW22 | MAGMFITFEGIDGCGKTTQIKRLAHTLRSSGLSLVELREPGGTTISERIRELLLDVRNHDMSDECELLLYEASRAQLTQQVILPALQDGSIVLCDRFFDSTTAYQAGGRGLDEQLVSRANALGCCGVIPTRTLVFDLDPEEAYARATQTTPDRLEAAGLAFQKRVQQRFMGLAQQESDRVKLIDASGTILQVEARVKRELADIFVELADE | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 210
Sequence Mass (Da): 23179
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A0A1F9XY16 | MRGVFITGTDTGIGKTALAACLLRKYGARKDLLYWKPIQTGIPDDDDTRTVRRLSGLPDGNFLDFGIRLKKPLSPHHAAAFEKKTLKPGFLFERLRRLKLKDPVFVVEGAGGLLVPLNGRAMMADFIRRTGLPVVLAARSDLGTINHTLLTLEAARARRIPVAGVVMIGPLNPGNKASIEKYGGTKVLEEIPWLESRTLRAFSVYAERRFDSRGFLGRLF | Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.... |
A0A2H0WRC6 | MLNPKTIRQLSKILGSDRLKKNVSLASYTTFGIGGPAQLFYEAKTNKEITKAIKTVRKLKIPCFILGGGSNTLIADSGFPGLVTKIESQKIKVKNNTISAEAGVPLSKLVKVAQKYSLSGLECCVGIPGTVGGAVVGNAGAKDQWISQSIKSITILNKNGKIISFKKDYCRFGYRNSFFKKDPSKIILKTIFKLKKENPKIIKEKTRQFLEAKSNQPKEKSAGSIFKNPANDSAGRLIDATGLRGKKVGNAQISPQHANFIINLNKAKAGDVLALIKLAQNSVKEKFGVKLELEIKLIGF | 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: 300
Sequence Mass (Da): 32595
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A0A2G9M3K8 | MLLKNGKVHSVEKGGFIAADLRIKDGLIAEIKPNLLPEQYETVVDCAGKHVIPGLIDAHVHFREPGATHKEDFLSGSKAAAAGGVTTILDMPNNNPPTVFEEQLKEKRELAMKSIVNYGFYLLGCVENKDNLRQKNIAGIKVYLGSSTGNYLTDDLGVFAEILQNSRRPVVVHAENEQLIRHFNHLHGNSQLHHKMRDALCAVTSLAEAITISSYLDRPLHIAHCSTKAEMEFLQKNKTTKVTCEVCPHHLFLTEAFFIQKKNLGKMNPPLRYVEDQEALWTGIRDGVVDMIATDHAPHTKEEKNREFQQAPCGVPGVQT... | Cofactor: Binds 1 FMN per subunit.
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway.
Function: Catalyzes the conversion of dihydroorotate to orotate.
EC: 1.3.-.-
Subcellular Location: Cytoplasm
Catalytic Activity: (S)-dihydroorotate + A = AH2 + orotate
Sequence Length: 740
Sequence Mass (Da): 81919
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A0A3P7KRJ5 | RRFTYYTVFSIPRSIRAWHAHRTINNRFDHAAYGLQPKHDVFGAHTTQNDELPIRLASGTIVVKPNIEKFTENDVYFTDGSRAENIDYVVLSTGYDITFPIVESGKMIKVNNNQVELYKYMFPIDQPHNTFAVIGLIQPLGSIMPIAEMQARVFFAALSGEATLPSVSEMKRDIMVKREKMRKQYVDSHRHTIQVDYIPFMDELATIIGCRPRFFPLILQDTPLAMATTFGPCAPYIY | Catalytic Activity: (2E)-geranial + H(+) + NADPH + O2 = (1E)-2,6-dimethylhepta-1,5-dien-1-yl formate + H2O + NADP(+)
EC: 1.14.13.8
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 238
Sequence Mass (Da): 27302
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A0A3G8M1J7 | MPTAPQTPQFVDFPIDGLPSKETFTHHDADAPDAQIIAHMANAFFGALPNASLPATGAVTQQSGAPALAGALPAVTPSLTDIPAPSIVTTIAPHAPARAPFGPMDFPPTTIPSVVPTPNVPAPSAPQTLHSSTRPLGLADIPQPGASLGGATSSVPGEMDYSAPTRRLAQEFSLVETDAVARPANNYYFLPTAPAPGPTEPLRYETRAPSTGAGYGHPDPFSPQQTSGAMRGDELVSRHSQGGATQGAYPLHPGEFAQGGDASNYAHSAPHLPGAGGREIPGAVHALYGDGVYAAPRQGRQPEKTVATRHLFDPYRVKRD... | Function: Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine.
EC: 2.8.1.7
Catalytic Activity: [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine
Sequence Length: 716
Sequence Mass (Da): 76143
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A0A8K0HER9 | MSLKNGKVSIDFLIGTVGKWKETYQWIPVFGAFTAIATAILTGANILPTPISSPVESGALTLIKASLMACTIYVPGATFACNSFVNVLFSDVIVLATAAIWLALATYLELPVLTQQSIQGALLGTILVTEGFSYVPLWNKNKNYNFNGGGLLWIFLEWTIAPLLACFCAFLPFSALKVSLLLHENAEKRILMFIPSDCGVSARLLCLFVMYQIVPNITTVYRWETTVAVAAAALLDSFEYDRQTLLRHALAEEYDDQVEEFFIFPQLLASCIFVLLQSAGEVAAVVSPYGAIHDIFSHKTKYSGNGKYMESVHVTWWFRA... | Function: Sodium-phosphate symporter.
Subcellular Location: Membrane
Sequence Length: 569
Sequence Mass (Da): 62043
Location Topology: Multi-pass membrane protein
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A0A3P7IQQ3 | MDSSLIYGVSYFSGGLPLLLGIFSIKSTSPWAGPYLKEEYKDLDNLETLTRQMEKDVAMYGFLNLIFFPLIFLYQILYSFFTLSELIKRRPDALGMRRYSNYGRYRVRHFNELTHELNARLNRSHVYANAYLNQFYSTLTEVFAKNIAFVAGAIAGVLAILSAWDEDVLQIEHVLTVISVCGVIMVICHGLISDENLVWQPEVLLAHVTSELHYVPVEWKGQAHTEQVRREFEQFFQLKWMFLLQELSSPILTPFILLFWVRPNCRELVRFFYDNT | Function: Phospholipid scramblase involved in autophagy. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by di... |
A0A343LFJ8 | MNFMLTLIINTLLASXXXXXXXXXXXXXXXXXXXXPYECGFDPMGSARLPFSMKFFLVAITFLLFDLEIALLLPLPWASQTDKLTNMLFMSLFLISLLIISLAYEWMQKGLEWSE | 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 of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NA... |
A0A511AE62 | MARFGIEEEFQLLDEDTLVPVPLGSAARAVLPSGAGEVKKEFLTSQVEFSTSPVGTLAAAREELTAFRRELASFARDHGAVAIGSGTPFGVGPEASVVESERYDTVADWLGHIVDSHHVDALHLHVEVPDEEDRVRALNAVRPWMPTLLAVSGNSPFADGHDTGHDSWRTVIMRRLPLSGCPPQFRDMHHYRTEVDRLIAQHVIPDVGSVCWAARLSAQYPTVELRLFDAQLSTDDALLVAALGRALVETAVGADDPVRTGDDIQASLWSAARHGMEATLVHPSNGELVAARDAVGLLVETIAPALKASGDLAFVEDALA... | Function: ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity.
EC: 6.3.2.2
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Length: 363
Sequence Mass (Da): 39044
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A0A9D9EV86 | MDRREINIVYTEFGSLNELPDDDRELALKAIEATRNSYAPYSRFNVGAAVRLDDGTVVTGANQENIAYPSGLCAERTAMFYAASEYPDIPMKTIAIAASSGGKLCPEPATPCGACRQVMAEYQSRGGHHISIILVGEEKIWKFSSVDDILPLIFDSLGK | Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
EC: 3.5.4.5
Catalytic Activity: 2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+)
Sequence Length: 159
Sequence Mass (Da): 17338
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B3ML97 | MACDETNCDGQISHTFVIFGASGDLSRKKIYPTLWLLYRDDLLAKPIKFCGYARSKLTVENIEGNCRQYMKVQPNEETKYEEFWALNDYVIGSYDNSSGFELLNRQLTLMENKNRANRIFYLALPPSVFEDVTVNIKQNCMSASGWNRVIIEKPFGRDAASSQALSDHLAKLFHEKQIYRIDHYLGKEMVQNLMTIRFGNKILNTTWNRDNIASVLITFKEPFGTQGRGGYFDAFGIIRDVMQNHLLQILSLVAMEKPVSCLPDDIRDEKVKVLKCIKTLTLDDMVLGQYVGNPDGTTDDARNGYLDDPTVKNGSITPTY... | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
Function: Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis.
EC: 1.1.... |
A0A1V0DGS4 | MTIAKRFRWEAAHRLPWHEGPCRNLHGHSYRMTVELTGEPDERGMLLDFQDLKRILKPLVEAWDHAVLVAADDAELLALLAQTDWKRAVLPADTTSENLSAYVAAHLCTEGRAVLQARRVHTVRVRIEETETCYAEVVQAVPPPEAPTPAREARAIVSAVS | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.1.2.50
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphate
Sequence Length: 161
Sequence Mass (Da): 18037
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A0A094I2U7 | PTSSTNFVELKTSLDPSSPRDLQTFERKLLKFWLQSFLLGVPKIIVGFRSANGQLRRLEELETAKIPGIVKKRGGWDGNVAVNFGAGVLSFLKETVVSEGVWRIRRREKSGVVECWKVEEVGHGEILSEEFINWRIKLALGPEGEVNGESEAPSEEQEGGEA | Function: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA (By similarity). The NAD-cap is present at the 5'-end of some RNAs and snoRNAs. In contrast to the canonica... |
A0A6H5IW07 | MLIDNNSFNTATAARMQTMANEPQVVEHFFGVYLLYCKNPKYKGRTYIGYTVDPRRRINQHNAGQKFGGAWRTSNRGPWEMVLIIHGFPNSTSALRVIYLIYQLITTYTLAFYFLFVVLFIVRHHQFEWAWQHPQLSRRLKHVGKKRARQKTFDYLLEVCSAMLNCGPWNKLPLTVRWLDDEFGQKYSTHLTSPLHMPITYGKVTSRKKKTTTTTTTSNDKAKEAVLAVLGTRDDGSSRDCIKPDCGLVAHLVCLAKLFCKESGDILPVEGSCPICATDALWGDLIRKKIGCNLHIDADVDESGSSSSSEEDDDYQSDD | Function: Catalytic subunit of a heterodimeric structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
EC: 3.1.-.-
Subcell... |
A0A831SP07 | MFNPLDILRDPENLQPVLLSLQTAVAALICHLILGVALGYALSRKKLPLRVLLDGLVTLPLIFPPVATGFILLMILGRYGIVGKHLAAQGMDIVFSPAGVYIAAVISGLPLIVKPVQSAIENSAESLKEASFVLGKSELDTFVCIILPTIRRVIIAGLMLSVGRSFGEVGITLMLGGNISNRTETISLAIYNSVFEGNTEKALVLSGLLAVFSLLVFYGMNKLNGNRTTLQ | 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 membrane
Sequence Length: 231
Sequence Mass (Da): 24672
Location Topology: Multi-pass membrane protein
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A0A4Q4UQU9 | MGVEDESLVPVVNLLAPSLVIKRQSSPFGAAPIYKHPDIINLYCVWRDFHTTTTKYLQNSTRQWVDFMAAGVMDQVSAVPLLCQTDPAGRKYEDTASDSLTVGFIDRGLDHSQIYSPTFCWQLREEMWKTVLPALIEGHWNEFKGFNRAFCTDADSNLGKGCLRLLMEALARDKNAIAAAGTVFAQLEPGFGWSSWDLHQRFQYTFSQFVRRRAEGHIGKVTCLPGCVTMIAVRKEMAGAIQKTWHVRPIHFPALIIVPLHHSSPPPQRVTSTNASSSQQGTDRRVTYSMLSQGHNLSTFFVPKAVSEAVAPQPLERYLS... | Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Subcellular Location: Cell membrane
Sequence Length: 843
Sequence Mass (Da): 95638
Location Topology: Multi-pass membrane protein
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A0A4W4EI36 | MPRTHTQQSKMADSKVKQELLDATTTSLKINSSEITTLIRQALEAKKFAYCPYSKFRVGAALLTHDGTVFTGCNVENACYNLGICAERTAISKAVSEGFRDFKAIAIASDLREQFISPCGGCRQFMREFGASWDVYLSKPDGSYMEMTVEELLPESFGPEDLKMKREHSIPKDVEPATK | Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
EC: 3.5.4.5
Catalytic Activity: 2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+)
Sequence Length: 179
Sequence Mass (Da): 19948
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D3EP72 | MKNQLPIFAKIWEQEINWKPTEKHLDQWEELYQEIILINNQVNLTRIVKPEEFWEKHLWDSIAGVVGLPFFQYSRKMKVIDIGTGGGFPGLPINIVFPIWDFTLLDSRRKKIEVVNFLLKILELENSWALTGRAEKIAHDSRFRGKYDIALIRAVGESSTCSEYILPFLNIGGIGVLYRGNWSIQEEQLLKVALKRLGGKLILVKESKTPLTKSVRHFVYVQKTHLTPKCFPRDIGVPKSNPL | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 243
Sequence Mass (Da): 28082
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E0S5V2 | MENIVIIGSGPAAYNAALYTMRGNPLLFEGGYIGNNGPGGQLTTTTSVDNYPGFPGGIEGPELTQLMKEHAVSRGLRVVKETVSDVRKEDEWFVVSSEKGEKKARIVIVATGASARRLFVPGTGDDEFWQKGVSSCAVCDGFIYVNKVTCVIGGGDAAMEEGLYLSNIAKKVYIIHRRNEFRARSDMIEKARNTENIEIMTPYVLERAEGTNKIKEIVVRNTETGETKTIPMDGVFFGIGHDPNTSFLKSVNVDLDSNGYIVVKDDACTSVPGLFAAGDVCDRKYRQAVTAAASGAICGIKAMEFLDKNK | Cofactor: Binds 1 FAD per subunit.
EC: 1.8.1.9
Catalytic Activity: [thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + H(+) + NADPH
Sequence Length: 310
Sequence Mass (Da): 33571
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A0A0J1FL26 | MLWVALLVGVQVLLLGTVIILENKDPGKTVTWLFILSLLPILGFLLYILFSQKQRNKLFRNKAQRTNRLKQRINEYDPIPKNEYSTFSPDNNLDLKLANLLMYSGYARLKMHNKVDVLVNGREKFAALLQSLENAAHHIHLSYYIFKDDEIGADVLKILSHKVSEGVEVRVLLDGVGSLFLAGNFMTTMRQAGIQAQWYFPLRFPFLTPRLNLRYHRKIVIIDGYVGYMGGLNIGDEYLSRDPKLGFWRDTHLKLFGESVHTLQSIFLNDWNTVTHQEIRGENYFPKVEIPDILPIQIGASGPDSNWASILQGFFVAITM... | Function: Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.
Catalytic Activity: 2 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a cardiolipin + glycerol
EC: 2.7.8.-
Subcellular Location: Cell membra... |
A0A1V0DB92 | MTYLTFLLVFLIPPIVLLAVTQPRPLAGVGGWRGRWSIPLVCVIAMLYTTPWDNYLVYRQVWWYGADRVLATIGYVPVEEYLFFLLQPIMTGLLLYQFLARSPHVERLGPARGTAMAGTVFYVVLTAVGCWLLLAGGDQGLYMGLILAWAGPPLAGLWYYGAPIYHAHRRSFAGAVTLATFYLWVADRTAINLGIWDISDRFSFDIDPLGLPVEEATFFLVTNLLVVQGTLLFLFGHLLPSRTSRLPS | Pathway: Carotenoid biosynthesis.
Subcellular Location: Membrane
Sequence Length: 248
Sequence Mass (Da): 27734
Location Topology: Multi-pass membrane protein
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A0A425XNK0 | MQKVSNRLVPGYRLGLSITFVGLLLIVVIPFCSLLVQGLDVGFKKFWLQATNDRVLASYAVSLKGALLAALINALLGLILAWVLTFYQFPGRQLLDYLLDLPFALPTAVAGIALAYLFSNKGWLGRLAAPMHVQISYTFSGIVIAMVFVTIPFVVREVQPVLEQLDSTYQEAALTLGARPWTVFRKIIFPEILPALISGFGLAFARSIGEYGSIIFIAGNQPFKTEITPLMIMFQLEAHSYTGATVIALVMLVFSFCFIFAIHALQRHVQRQKG | Function: Part of the ABC transporter complex (TC 3.A.1.6.1) involved in sulfate/thiosulfate import.
Subcellular Location: Membrane
Sequence Length: 274
Sequence Mass (Da): 30260
Location Topology: Multi-pass membrane protein
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A0A257HQH2 | MTDPLWTSTAAALAVSGKAQGQWAVNGISIDSRAVEPGDLFVALKAERDGHSFVRSALAAGAGAALVVDPTCADAGAPLLVVPDTLLALENLGTQARRRNVIATRVAITGSVGKTTVKEMTATALAATAKTHRSVKSYNNHWGVPLTLARMPGDARFGVFEIGMNHGGEISRLSPQVRPHIAAITMVAPVHIEHFADETGIADAKAEIFLGLDAGGTALIPGENRHAARLAARARDRDGISILTFGMQPGFDSHVVGIDEIDHGRRVTADIMGQQLSWIIQEPGAHWVHNGLCALTLAVLAGGDGQAAAAALSQFGAIDG... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Catalytic Activity: ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-d... |
A0A3A1Y5N8 | MTELNKHSFLVELGTEELPPSDLKNISAGFTDALVLALHKANVAYDEIESFATPRRIAVYIKGLNSVANSQLVEKRGPAKAACFNEDGSLSKAAQGWLKANNLEFSQVSFLETDKGAWLYYSFEQPGASSEEILPQAVAEALAGIPISKGMRWGNHDFTFIRPVHTFTMLLDDKVLEGTAFGVKSDRKIYGHRFLGTKEFTLNHADEYQSRLLAEGSVVASFAERRKMIVNNVKKLASQYNGYVNLEDDLVDEITSLVEYPNVLIANFEKEFLKVPKEALIHTMEGDQRYFPLFADNKFTQLLPHFIFVSNVTPKDPSLI... | Catalytic Activity: ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly)
EC: 6.1.1.14
Subcellular Location: Cytoplasm
Sequence Length: 697
Sequence Mass (Da): 78384
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A0A1V3P5K9 | MDERALADLFVAPISACIADSDMFSAPLFSEEEAYIRKAIPARRREFSAGRAAARKALAKAGADVGPIVAELDRSPRWPDSFCGSITHCEGFCSAVVARSVDADGVGFDAEEAKPLGSDLYHLVCRPNDLEHFHPLPRIDGVDWPKLAFSAKESFYKCYYPSTRSFLGFRDVSVIFSVTAENSKEGTFLIILENKVKPMPRPSTDFVGRWFVHGERVYTGVTLPRA | Pathway: Siderophore biosynthesis; enterobactin biosynthesis.
Function: Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provi... |
A0A317CJE3 | MSRLFRSGMVISIMTLMSRVLGLVRDAVYANYFVMGSAMDAFLVAFRIPNLMRRLSAEGAFSLAFIPVLTEYKEKKSKEELKDLIDHVAGLMGLILFIVSLIAVIASPLLMMVFAPGFEAKPDAEPELAAYLLKITAPYMLFISLAAFFSSILNAFGNFAVPAFTPVLLNVVMISAAIWWAPAFEEPVEALAWGVFIGGIVQAGFQLPFLQRLGLVPHFSLKKGHEGVKRIMKLMGPALLGSSAAQLNITINTMIASTLTAGSISWLYFSDRFVEFPLALIGVAIGTVILPKLSGDHANAEGKAFSGTLDWAMRLSLLVS... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane.
Subcellular Location: Cell inner membrane
Sequence Length: 518
Sequence Mass (Da): 55849
Location... |
A0A4W4EVC8 | MGKQQFRETDVAKKISHICFGVKSAEQMRQQAHLQVVSKSLYSQDSSHTPLAYGVLDHRMGTSEKDRPCESCGKNLADCLGHYGYLDLELPCFHIGYFKAIIGILQMICKTCSSIMLSKEERQGFLDHLRRPGLPYLHKRGLKKKISDKCRKRSVCLHCNAFNGPVKKCGLLKIVHEKYKTTKKVVDPVVSDFLQSFDLAIEHNKEMEALLSRAQENLNPLVVLNLFRRIPSEDIPLLLMNPEAGKPADLILTRLLVPPLCIRPSVVSDLKSGTNEDDLTMKLTEIIFLNDVIKKHRMSGAKTQMIIEDWDFLQLQCALY... | Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 488
Sequence Mass (Da): 55521
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A0A4W4FHK2 | MSSSACACCCFRKAIAKSGIQHLTAQSSASMPNKCEANQEIPQKVDWTENAQFGQHVWFETSLSGDFCYVGEIYCFAKLLQKSLPRYKCAACKIAVHTVCMEQLEKVKYFIAVFTDLGFSLQINFRCKPSFRDPGMRNVREASTVRHHWVHRRRQDGKCRQCGKGFQQKFSFHSKDIVAISCSWCKQAYHNKVTCFMLQQIEETCSLGAHAAVIVPPTWIIRVRRQQASLKSSKRRKKASLKSKGSKKGPEDGKWKSFIVKPIPSPLMKPLLVFVNPKSGGNQGAKIIRSLMWYLNPRQVFDLTQGGPKEGLEMYCKVPN... | Pathway: Lipid metabolism; glycerolipid metabolism.
EC: 2.7.1.107
Catalytic Activity: 1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+)
Sequence Length: 932
Sequence Mass (Da): 104572
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A0A8E6B1W4 | MLTLQLPDGSTRQVNPGTRPREIAEGIGKRLAQAAIAAKVNGAIVDLEREIEASDQPITFQLLTDKDRESLDVLRHSCAHVMARAVMRLFPGTQLAFGPTIENGFYYDIDSPTPITEADFPKIEAEMKAIVKQAEPFERFERSIPEGRGLVADLKQRLKVEHIDEELKKYPSISFYRQGEFIDLCRGPHIPHAGKIGAFKLLSIAGAYWKNDASRKQLQRLYGTAFFTQKELDAYLLQIEEAKKRDHRLLGKQLKLFTISQQAGQGLILWMPKGATVRHLLETFIREELVKRGYSPVYTPHIGNLNLYRTSGHFPYYADA... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr)
EC: 6.1.1.3
Subcellular Location: Cytoplasm
Sequence Length: 752
Sequence Mass (Da): 85454
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A0A4W4E6B3 | MITLHILSGMSARHFLFLCVLCALYVSLCSGACAEVDSDTQAVAGQNFKLGCISCKMRGEVEASATVDWYFRAKGETDFAHIYSYDDESPTIIDERFKERVNWTGSRKTNDLQDASIYLLNVTFNDSGVYRCFFSRTLSYQYYEYQTTVSKLVHLTVVAKATRGVASIVSEVMMYVSIIGLQLWLLVEMVYCYRKIAAAGDEALRASAAEYLAIASESKDNCTGVQVAE | Function: Modulates channel gating kinetics. Causes unique persistent sodium currents. Inactivates the sodium channel opening more slowly than the subunit beta-1. Its association with NFASC may target the sodium channels to the nodes of Ranvier of developing axons and retain these channels at the nodes in mature myelin... |
F6G4B5 | MFSFWKKRKAEPQPAAEPAPPAAAPEAVQAPVPAPVASPTPAPAPAPVAVPDTPAAPAALDMQADDIETVPTPPVMEQARKGWMSRLRSGLSKTSKNLTTLFVGVKVDEALFEELETALLMADAGVDATEYLLDELRRRVKAQRIETAESVKTALRDLLVELLHPLEKTMVLGRDQPMVIMIAGVNGAGKTTSIGKLCKHFQTYGQSVLLAAGDTFRAAAREQLVIWGQRNNVTVVAQESGDPAAVIFDAVNAARARGIDIVMADTAGRLPTQMHLMEELKKVRRVIGKAMVTAPHETLLVIDANTGQNALAQVKAFDDA... | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC). Interaction with SRP-RNC leads to the transfer of the RNC complex to the Sec translocase for ... |
A0A1F9XV41 | MTSHGVADSIREKLDIVDVVQDYIPSLRRTGRNYKAVCPFHNEKTPSFTVSQDKQMFYCFGCNEGGDMFTFVMKIEGLTFVETLKKLSHKAGIPWAETEYHQLSAKEKERLDLKKVLTAAAEFYKKLLFSSNGEKVRLYLGGRKINKATVEHFGLGFAPGEPSLTAELERQKFSKELIVTAGLAGVRDNGSVTDYFRNRVMFPIRNSTGDVIAFGGRALDDGQQPKYLNSPETPLFSKRRTLYGIHEALPQIRKEGRILILEGYMDVIAAHQHGVTFAVAPLGTALSAEHAAFIKRYSKDTILMFDADEAGINASVRASD... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
EC: 2.7.7.101
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Length: 588
Domain: Contains an N-termi... |
A0A1F3SMZ0 | MTTKSKTKFQSQHKSDMLHPLYSYKKNKLFYSGINLSDLPTSLPTPFYLYSLSAVTNNVAAFQQAFANAGIHDLLICYALKANPNPHILSHVSQLAAGADIVSKGELSEAMKANIPSERIVFSGVGKTKEEILEALNAGQNGIRAFNVESIEELDLIASCAQECNKIAQVAFRLNPSIKAPTHHLISTGNKSHKFGLLPKDILETLPHFKTKSLYRKHLKLVGLSVHIGSQLLTFRASKNAFRALASLALTVSDFLGRPLEFLDVGGGLGIAYHHHTMTLSPFHAYAQSVKSGVAAYLDRYPCQIVCEPGRSLVGNAGVF... | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1.
Function: Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.
EC: 4.1.1.20
Catalytic Activity: H(+) + meso-2,6-diaminoheptanedioate = CO2 + L-lysine
Sequence Le... |
A0A238U6X3 | MMNFIKTKIPDLMIIEPKVFGDQRGYFFESFNVKQFEEHIFKVDFVQDNESRSSKGVLRGLHFQKPPYEQAKLVRCVKGSVLDVAVDIRRGSPTFGAYEAVELSEDNKRQLFVQEDLLMALLFCPKVQYFLIKLIIGMLLNLIVV | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
EC: 5.1.3.13
Catalytic Activity: dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose
Sequence... |
A0A8K0GXM5 | MKVIGKELFKVLRERRDTNFESFISEKVTAISGDVSLENLGVQDVQLREALWKHIDIVINFAATTRFDERYDAALDTNTLGVLHVLGFAQRCVKLEMLVHVSTAYVCGEREGLIKEDTVFHMGKTLKATSILDFKEEQKLVAEKLKELRDQNASEDTITTTMRDLGLKKAKLYGWSNVYVFTKAMGETCLVDSKEKFPSIIIRPTVITSTYKEPFAGWIEGLRTLDTLVVGYAKGKVKCFLGDTMSILDLIPGDMVIDLMIVAMVAHANDHQSFKTIIYHIGSSLRNPINISNIRKFSFQYFTRKPLKNNKGEPIKNIGK... | 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: 662
Sequence Mass (Da): 75625
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A0A1F8L2J0 | MALPSRPPPPASGVVLAGGRARRFGRDKLAEPIGGGPLLHRPIAVLAALCSEVIVAIAPGSAAPALPESGELLWVVRDPIPDGGPLAGLVAGLREAREPLVLVVGGDMPDLRPALLEGLLRRADETGAGAVALAEREVVRSLPAVVRSSALPVAERRLGSADRSLVGCFRSLGLVVIPEMEWRAWDAAGDSLRDVDSPEDLPAPER | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytopl... |
A0A336MN17 | MLQAYRSIAVFICSNVKHRDRRRHIRTTWGRVLRPKPIFILGLSTDNEVDNEMALEEAHLYQDVIIENFHESYQNLTLKTLFALKHFLRLTPNETYFLKIDDDVFLNTYQLDHIMEKYQTTPGIIGHLESQRYAHRDKESKWFTPRWMLSKEALPNFINGPAYLISGSLVKKIYEKALETPLITLEDVFLTGLVSNELLNIPLYNNIGFEDYYSIDSIFNRDCFYRSVFTIHRMTLMEQIYELWDKLKENHEPCWDI | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 257
Sequence Mass (Da): 30622
Location Topology: Single-pass type II membrane protein
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A0A0P9A948 | MSWRYASPSRLETSEQTTGRQLQRVLHYSMAPSRALPGLRRAECAIHDVDCDEVYPGIYIGDAAAAKNKTYLRLMGITHVLNAAEGCRYGQVDTGHSYYRDMPSIRYMGFPMIDAPTTDISRYFYVASKFIDSAISSGGKILVHCLVGMSRSATCVLAYLMICRKMSAVDAIRTVRMRRDIRPNDGFLQQLADLDMELKRKNLYPY | Function: Dual specificity phosphatase able to dephosphorylate phosphotyrosine, phosphoserine and phosphothreonine residues, with a preference for phosphotyrosine as a substrate.
EC: 3.1.3.16
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Length: 206
Sequence Mass (Da): 2... |
A0A3P7IXC6 | MGLIRFFKENTITVRSDRLLDKERIYHLDLYNSFSTYSTTLGNLLLLMGSDEHSSRQRELIVDLLPPTSVRSEPHSLPRSVHQILSDDEFNEEQRKAVFSALLCKDYTLIEGFPGSGKTTTIVALLRCLLEMKCSVLLTANTHSALDNVLAKLRKHVEPEKLLRLGKFSSGCSAVSDLTLESKIRSGEGDKYILARNILKNTVCSTLHLKAFTPRVFC | Function: Key enzyme involved in DNA replication and DNA repair. Involved in Okazaki fragments processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA... |
A0A3P7LJ71 | MFLLFNENQPDIVKSGDVVRLFHADQQTFLTLDSVPKTCPPQDVVFLRMTNRPSAADATSSRALWEVQVVQKDAYRGGAAKWREYYRFKHLATDMYLTVIPATSPVKPASNGRRASLMHMKXXXXLDSVPKTCPPQDVVFLRMTNRPSAADATSSRALWEVQENAYFRTKAELLAPPSLYADGPESTEECATSMYFLVPVKSDFPEADKRLLFCLDPGTMPKVGQLYIAKCILINKDVPTKSYVRLQHEATNTWVHATNASEKQNLYYSSKNEKGWVRVICENSRVDKETFALLPVSPNEVRDLDFANDACRALRNFIRH... | Function: Receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 375
Domain: The receptor contains a calcium channel in its C-terminal extremity. Its large N-terminal cytoplasmic region has t... |
A0A3P7KYQ9 | MIVVKSYKIELLKQVGKGGEVKLKVEYRLTQLLKPLPEKITQRENQYVVYHGNAHYAAPYAVEQEKTIVKLGSGKTLSVTQVSPTTQENERVVYGPYKNQPAFNKKHIKIHYENNAPFVVATVVERTIEISHWGNIAVEEYIELVHKGAELKGPFSRIDHQLDRRGRRQPALLHFTVSCSSFM | Pathway: Protein modification; protein glycosylation.
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus m... |
A0A3P7L1C9 | MFVGEDKEKVTKIVRGSMQELAEVYDPILSDDPRIVMQNGKILQDGSTAAIYHRLNL | Pathway: Lipid metabolism.
EC: 2.7.7.41
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 57
Sequence Mass (Da): 6434
Location Topology: Peripheral membrane protein
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A0A3P7LEN6 | MSDARLPCEVRASFTRLMLHLHVVRGSPLSAIRHARLWADIPEEVVVQSYKTTSVEGYSDGGRARVGDQFANDVLNTVESYLDSLRDRHPSGPVLKEDAASVCTNKLTHEMVTLAKALAQFGYYTFDNLLTLTENLLNIKNAPVLARTVSHGMTMIHRVTQSMIGGRSMTLDGPSKSTEKSSIEDTVKTKESRQLLVKTKLIVAEILQVRYLYCLGARLR | Function: Receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 220
Domain: The receptor contains a calcium channel in its C-terminal extremity. Its large N-terminal cytoplasmic region has t... |
Q919T0 | SGLPVGGNEMKAKLANVVRKMMTNSQDTELSFTITGDNTKWNENQNPRVFLAMITYITRNQPEWFRNVLSIAPIMFSNKMARLGKGYMFESKSMKLRTQIPAEMLATIDLKYFNESTRQKIEKIRPLLIEGTASLSPGMMMGMFNMLSTVLGVSILNLGQKRYTKTTYWWDGLQSSDDFAL | Function: RNA-dependent RNA polymerase which is responsible for replication and transcription of virus RNA segments. The transcription of viral mRNAs occurs by a unique mechanism called cap-snatching. 5' methylated caps of cellular mRNAs are cleaved after 10-13 nucleotides by PA. In turn, these short capped RNAs are us... |
A0A5K7YMI5 | MILYLIGYRCTGKTTVGRALARRLGWPFTDTDQMIAATAGNSIARIVDRHGWPYFRQKERQALASVSEMDHQVVATGGGIVLDDRNVAIMKTSGRVTWLKAGRKTIEMRMLADDATAGNRPSLTGQGLMEEIESVLSERRPLYEKAADLALATDHEKIETLCDRIVAEFKISELRD | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
EC: 2.7.1.71
S... |
A0A924S0V5 | MRTLPPLRRRLALATLVVVGAASLAACGFHRRVAQSLSYERIALSGFGDRSTMADEIRRALPSSAHIAPSVLESQVVIEAIEDTQKTTVEASTAFGQVRELELHVKLRYRVLDPNGLELLPLADLERFRDMTFDEKDALAKDTELKALYRDMQSDMAYQLVRVLSAVGNPTGPAAHVQAARAASAALAPASAASAVSAVEWAASQAAGR | Function: Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 209
Sequence Mass (D... |
A0A7S1CU31 | MALRSAVCAALVDRKDFIEPFIGSGIEEYVCEMQKPSTWGGEPELSMASIVLLCKIVVFEPVIEAKVISLSKTSEYCLVEDAKDDDLESIHVLFSGGMHYDALITMP | 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... |
A0A069CXX4 | MGIINQVREKQPLVLNLANTVTQQRVADVISYVGGSPLMTTASNELAELMQIASALVINIGTLNDELLPLYIEAGKLANQLNKPVILDPVAVTLPYRGEIVTALLKEIKVNIIRGNAAEIAWFANQTVAGKGIDALDNQINEAIVLDAAQKTGAIIVQSGPTDLIADGQQVIKITAHSDLFKINVGTGDMLSALIGTFSAVSADYFAAAVEATELFANSGVKAAQIVEQKPANFINALLDCLYEAN | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-methylthiazole: step 1/1.
Function: Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
EC: 2.7.1.50
Catalytic Activity: 5-(2-hydroxyethyl)-4-m... |
A0A8J6NBD5 | MFDFLKNVTYQIISPIASARSRYETFKDLLKNDQKAHELLATLEEVYYQNKKVDINYATRLYSQLSQAVSTMVACLGKMSPGESTNLRAYYRKIDFFCRFALAPPEIDTSPPFILPITKIYPDDSLTGGKGFNFCILKNTLGLPGPHGFIISTSAYNYFIKESGLRHTIDEILAEIDIHSTESLHNSSKQIIDLIGNTALPDSLKKELNQAFKELRNQCSTDITLAVRSSAVGEDSKISFAGQYLSILDADGGNLLESYKQVTASKFSPRALYYRISNGLHDYSTAMAVLVLEMVDASVSGVITTKDSFDKGDDVVCIHS... | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
EC: 2.7.9.2
Catalytic Activity: ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate + phosphoenolpyruvate
Sequence Length: 823
Sequence Mass (Da): 91150
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A0A1F9XRM6 | MPKFIDYYSILGVPKSASEAEIKSAYRKLAMKHHPDRNPGNRESENKFKEINEANEVLSDPKKRQTYDQLGDDWRQGRNFTTPPGGGPRGGGFESRPRGGGGQGFEQFGDFSDFFRSIFGGMGGASYGRSGGEDDFESFTRGVGQSTPGDMESELHLSLSDVIRGGQQRLTFSYKSICPECGGKGRQKARACAPCKGTGHSLETREIRVNLPKVLRDGTRIRLTGQGRRSPSGRNGDLYLSIYITPHTDFKIEGDDLETRIHVMPWDAALGAEISIPAPDGPVKIKLPAGSGAGRRLRIAGKGLPKKDGSRGDLYAILTI... | Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyz... |
A0A3P7LBI4 | MLVIGKLAPRWNVPIIAHMSGDDALSDRSVFPTLGSVALTSASEMARATLAFLQLNNWDELNDHYPWEATNVDKQEVKAAFENVIIITAHGYDKKFFDEFQTKFSQATGMLSSHYATLNYMSLYDALFLYGLALRDAYEEIGGYDVHHNGSFIWSKMTNRQFIGATGQVLMNNKAIRVPSYATYHTTNGTLRIVVELEAKHAERSLCEKNSDQCSEXXXXNFKRSLARQRECSVVINITFPKSELKLLKELKLTENENLNKFYGICFNQQNEFIVLWVYCNRGSLEDILFNEELKLGRNFQVAFAKDVVKNCLVDSNWTV... | Catalytic Activity: GTP = 3',5'-cyclic GMP + diphosphate
Subcellular Location: Membrane
Sequence Length: 648
Sequence Mass (Da): 73240
Location Topology: Single-pass type I membrane protein
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D8LMP5 | MLPQTMINDCESNDPNSLDNNNQDAGAAATATDNAVNAAHPRTKRKNPEKVDDKARCPICQDLLPEENRGIVKCGHVFCLKCVLQWVKKQQNSCPTCRAKVCHIKKTLSLAEALEKNANRKPLTKAQLKRTKRKSTIGKPFPKPDITTEKIRVHKKVSREQIRQNAMAPHPQAPGGFLHAQEQAEAAAEAAQAVPDAQPDQVEAIVDQQVAIAVFSSSPPPPPATPQVPSPLPPSSPRSLATDLEDRRVAIEADRRALLESTSAFRGHRSVGGGSYVGGAGGARSIGDSGGGVGDRVGEASLDVRVENNSGGGGGGGGGA... | 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: 8... |
A0A1G4AYZ1 | MELFSLLALLSIAVTHCSAAFDPTSKNNVVVYYGQGPNQRDLIYQCQQPEIDVIVLSFVYLFPAQANGYPGTNFGNRCGGQVYPGPGFNGVNDPSENELQSNCPTLNAQIPVCQQQYGKKILLSLGGGVTSYQLTGKNEGELLATYLWHMFGPKDPNWTGPRPFDYNGQAVEVDGFDMDIEHPSTDNSQGYIALVTLLRSFYATASKQYYLTGAPQCIVPDANMAAMISAAKFDMIFVQFYNTPSCSAATWVSSNPSYTPGQTYQQAGFTFDAWVQWLSNTPSRDAKVFITLPASPDAANAGNYITPQQANNLISAYYCR... | Catalytic Activity: Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
EC: 3.2.1.14
Subcellular Location: Secreted
Sequence Length: 533
Sequence Mass (Da): 54841
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A0A418JJ38 | MERDKNNHLSHTLNIKWNRDIILAIILGVLGSSVALAMFFLSGYMITESALGAPLFALMGLIVTVKLFGFMRAVTRYYERLFSHRATFTMLRDVRVYFYQALIPIVPNVFRQFKTSDLLGRMVSQIEALQNIYLRVYYPPIVMSLTGGLTICVLLYFSVWHALTLLIVMSLSLWLIPWLSAKRATVIKKDIDDTYQKLMHRYFDYILGYDELMRFNQNQSYEGRLLRTEEALSNAEYQEQMFHIVYQYVLNIISMIAIWGSVCLIIIQVNAGTFDPVYATSIVLMLLTLFEQHVMMSQVAYYKSETDEATHQLNDVMSVA... | Function: May be involved in multidrug export. Transmembrane domains (TMD) form a pore in the cell membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Subcellular Location: Membrane
Sequence Length: 553
Sequence Mass (Da): 63155
Location Topology: Multi-pass membrane protein
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A0A6N8U8T8 | MERAILHCDLNNFYCSVELVKHPRLKGKPVVVAGDITKRHGIILAKSYEAKAYGITTGDALYEAYEKCPDLIAVDAHFEDYLYYSQRVKAIYERYSDQIESYGIDECWIDVTGSLSYFGCDANILADRIRKQVFEELGLTISVGVSWNKVFAKLGSDYQKPYATTVISKDNYQQLVWRLPAQDLLFVGRSSAEKLYRQGIYTIGDIARNEASLMKQLLGKAGEMLWAFARGMDVSKVALSDYMREIKSVGNSITTVRDIYTEEEAKLVFYVLCESVAERLKRQGLEGRTICIYLRSWDLHSFTRQVTLDDPTDICEEIME... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
A0A8E8PWL1 | IISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGTQLSYSPAILWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLMMNPAWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVNSTNGSSISLL | 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... |
A0A3N9TCD7 | MLNPILTGLYNLLILIVSPIYLTVLIRKMSSLPNAQHRWLEYIGLGKIESESTRPIWIHAVSVGESMGIIPLIREIKKSHPAKCIIVTTTTSTGAQIIMSQLKDDVTHYFMPFDIPWCVRRFVTKINPETFIIMETELWPNTLSIVNSLSIPITVINARMSEKSCKSYQKLGSFFRRVLNKIDHIVCQNTSDRERFERLGMDTSKLSVSGSLKFDIKIDDAAIEKGVNIRSEFGDRPIWIAASTHQGEDEQLLTVHQQILKQLPNALLILVPRHPERFDSVFKLCTESFDTVRRTGKLPVKSSSQVYLADTMGELIALFA... | 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... |
A0A834KET6 | MILGWYSVLLATLLAFLIYIAFFWKINWIRDLRCENKIKYRKMEKLPPVYPNGWFALLESSQLKVGQVKHVSALGENFAVFRTEKGIVNILDAYCPHLGANMGEGGRVKGECLECPFHKWLFYGNDGRCIDIPYANKVPNVAKTKAWRSCEVNKIIFVWYHAESAKPDWQPHPHEKISNGTWRFQGRNEFIVNCHIQDIAENGADLAHLSAVHGPALFLSEDVMRFVRHRWSNAGWTPHSSESNDDSSKTPTEKNIPEEETMWEDDLTKKTSTTKTTINGDSKNMLNGRTTMTTTATATIANGQQNSYNGEKHRASMTLR... | Pathway: Hormone biosynthesis.
EC: 1.14.19.21
Catalytic Activity: cholesterol + H(+) + NADH + O2 = 7-dehydrocholesterol + 2 H2O + NAD(+)
Sequence Length: 450
Sequence Mass (Da): 51750
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D7FRS5 | MKYAWLALCLVCGCWAAQGSRGKGAAGTELIITEQPVVAIWAHPSNSSLPDCGGDCDFVKAAYVNWLANAGARSLPIRYDATPEELRPILDQVNGLLLPGGHPLLPEGVRWALKYAKELNDDGDFFPVWGTCLGWEWMAQTFAGDYPVVTDDFDAENFTQPLGLLADAGESRMLSGVPTSLLEKAKVKPLATNAHHKGVSPGDLVESGLDTMFRVMAINADRQGVRTYVSVAEAIDYPMYGLQWHPEKSQFDWGLDPDGTPHYVINHSKDAVELSQVLATFFASETRRNGHSFTSISDWEPGMFHNRDVTASGPINGQMY... | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + (n-1) H2O = (6S)-5,6,7,8-tetrahydrofolate + (n-1) L-glutamate
EC: 3.4.19.9
Subcellular Location: Secreted
Sequence Length: 379
Sequence Mass (Da): 41626
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A0A1F8R7G5 | MRVALSFGLFQAFMTLVGWLAGRTVIGFISPYDHWLAFLLLAFVGGRMVWESFRDKDPGGKRTDITRWGLLLALSVATSLDALAVGLSFAFLKVNISLASLIIGLVALAVTGIGFALGKKLGAVVGKRAEVVGGAILIVIGLRILLENIL | Function: Probably functions as a manganese efflux pump.
Subcellular Location: Cell membrane
Sequence Length: 150
Sequence Mass (Da): 15956
Location Topology: Multi-pass membrane protein
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O03495 | LALAASVLILFLTPLLHTSKQRTMTFRPLSQLLFWTLVANLLILTWVGSQPVEHPFIIIGQIASLTYFTILLVLFPLTSVLEN | 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... |
A0A8K0GZU0 | MQVCHKCARWTCNKRCRSKGMVSINREDKINFIKDELSKESLDNILLTLETHPCGVEMEGASVCRFTNICVFCGSSPGKDKEFLKAVHTLDRMLAEKKVHLVFEGGSLGLMEVVSLAAHIGGSNVLGLLNVNKFFNGLLSFLDHAVEQNFISYSAQQILISASTADELIDKLQRFIHVPDPVMAQLDWLERTVAELRTRTGRWNEELLRDLFEQHSAQEILKLEWPCVPRQDKVLWMGNALGVVESAEHVFRDYHVIGAITFRSKWGIDWDCFNNYDIYILINFSLDPKRGINDIIRVVHVFESAVEEYDKLLQLKQNFD... | Function: Cytokinin-activating enzyme working in the direct activation pathway. Phosphoribohydrolase that converts inactive cytokinin nucleotides to the biologically active free-base forms.
EC: 3.2.2.n1
Catalytic Activity: 9-ribosyl-trans-zeatin 5'-phosphate + H2O = D-ribose 5-phosphate + trans-zeatin
Sequence Length: ... |
A0A141QD47 | IFGSWAGMIGTSLSLLIRAELGNPGSLIGNDQIYNVIVTAHAFIMIFFMVMPIVIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLSLLLMSSMVESGAGTGWTVYPPLSANIAHGGSSVDLAIFSLHLAGISSILGAVNFISTIINMRSIGITFDRMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNL | 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... |
A0A2D4JXZ0 | VEDTAVVEKTKEEIIAKLQGRYGCCRFLRDGYRTPKEDPSRLYYEPAELKLFENIECEWPLFWTYLIIDGLFSGNAEQVQEYREALEGVLVKGTNGLRLVPELYCVPLEEVEEEYSHPHTVERLPVGKLPLMWAQSLYILGCLMAEVSFDPALALSCLELSVGGKGHRQPPPREA | 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: 175
Sequence Mass (Da): 19933
Location Topology: Lipid-anchor
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A0A7W5LHD0 | MKAVASLAFSIASATSLCVGGASVASHMVAQPNRAALRVEEEPDLWTAEPRPVDLSKQRYQRLPPLLSSYAEDQLRNQLRTAKTVTSRPSTDEARTLVDSTTRHTEWCTARYRSYNAKTDTYLSFSGEERPCISSPSDEAVSPFAASRPSDDHVAWCSTRYASYRLEDDTYQPYSGSRTKCISRIARPAPEQVTASGY | Function: Has immunoglobulin-binding and hemagglutination properties, and can bind to mannose. Essential for virulence. May be involved in LPS biosynthesis or polysaccharide transport.
Subcellular Location: Cell membrane
Sequence Length: 198
Sequence Mass (Da): 21937
Location Topology: Single-pass membrane protein
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A0A399JEX5 | MGSGKSSVGRELSRALNLPFVDLDEELVSRHGPIPALFAARGEAAFRELESAALAAVLAGPAVVLATGGGAVLAEANRAALAEHTVIRLTISPETAARRLAGDATRPLLAGDHPEEAWARIARERAPHYQAVASHTVAADADGPQTVARTVLTAMRTEPEEHSS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
EC: 2.7.1.71
S... |
A0A4Q4UZI5 | MDWAFANGLLNWSGQGEEIQAKAIHPSLDYDALQSRHFQLLKASESVETIIDAAMVHSFDKSGTYSFVVEGPIPLAVAPSTKLSGPPAYVKSNAVSMHVEAREASFQGRRSIEGRTNLDFAGCNGTKHEVITAALSNCNKLALAAAADARDPTSARFVEYFKSNSSATRREVVERLEAAAAECSTTDSGPSRLFCYDYYEACETDDGPLVAYTLWTFDTMVMCPLFYERPPLPTGCHRQCHATTVIHETTHCGGVYSPMTNDFAYGYEEIMALKPDWALLNADTYSLYANGHKAQDNKLEAAAVDI | Cofactor: Binds 1 zinc ion per subunit.
Function: Secreted metalloproteinase that allows assimilation of proteinaceous substrates. Shows high activities on basic nuclear substrates such as histone and protamine.
EC: 3.4.24.39
Catalytic Activity: Preferential cleavage of bonds with hydrophobic residues in P1'. Also 3-As... |
D7FVJ5 | MSGNEAPRSKSIEEQTRADSRRRRQERKKAQLGALKTGVWDRCLYRVPGKGRYCAQHRSKHSASFCGTHMGETAEKGKRVPCPVDPNHTVFEQQLSSHVKICNLALQQARMVAQPYYSEGINSGPPLLPGEEEEEKNKEKEEEDRGDVAVVAAVAAAAALDDAFVVDLLSRVEAAHRDLVGEIPTEVLDPPEVQALHRGLVGPAGGDNGHGENGPSVLHVEMGAGKGTLGQSIATAFPGSDVTMVERSSVRRKAENRLEGVSTRARIDIRDLNMGGLPSLTAEGDDRPVVAVAKHLCGVATDLALRAMLTLPPRPESRDA... | 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: 614
Sequence Mass (D... |
G9CI92 | FGYLGLVFATFAIVRIRCVVWAHHMLTVGMDLKSTVFFIPAPMIIGVPTVIKVFSWLFMLSCNNVFKTDHILWRAVAYQLLLLTGGVPGILSPASI | 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... |
A0A2D4L073 | KKLYPNMAMKLKVSPSSVPSLSISPETLSLTPSVDIQAFAILPDSSLAPLFVIEATSPVSAKIDVNSTRIFGNLKLGRLKFSLKHSDVGIFSVQLLESLINVLTASILIPQMNARLAEGFPLPLLDHLELSNPVLQAHQDFLVFASDVRYG | Function: The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope.
Subcellular Location: Secrete... |
A0A4R6U7G9 | MQHSAKPQSHRVIFHIDLNSFFASVEMLLRPELKKHPVAVARTSSQRLGIVVTSNYLARQQGVKTTMPVWKAKQHCRDLVIVPPHFDEYRAYSRRFFSLLRTYTDAVEPASIDEAYLDVSDWRGDYVALAKTIQDELLDKVGLPCSIGIAPNKFLAKMASDLKKPLGISVLRKRDWPRLFYDKPIEVIHGIGEKMGEKLRQAGYDNVQQLAEANPAKMAELFGPKSIRLIDKAQGVDDRMVDPERAEKRKSVGVSSTFDADLRTLSSCERELKKLAAKLSERLSDKQLAGFSLTVQIKYASFETTSKTTSFLSPLSSETD... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
A0A336MZ97 | MLNQVAVEALYSATYVENYLDAVENLPDEIQRYITRIREIDVKHRSYLRDVDIFYEQWANCPTNELESTNATKRNRAMTRIQQSLIAAQELGDEKLQIVQQLTDLIETKTRQLDQNFKNLDYASGHNSSRDTREDTPPQEEAIDPDEPTYCLCDQISFGEMILCDNDLCPIEWFHFSCVGLATKPKGKWYCPNCRGDRPNVMKPKAQFLKELERYNKEKEEKT | Function: Component of an histone acetyltransferase complex.
Subcellular Location: Nucleus
Sequence Length: 223
Domain: The PHD-type zinc finger mediates the binding to H3K4me3.
Sequence Mass (Da): 26069
|
E6SKT9 | MDRWVLHCDLDAFFAAVEQLDRPELRGRPVIVGGDPASRGVVATCSYEARAFGVRSAMPLAQARRLCPHAVFLPVRRERYEAVSRQVMAILARESPVLEPVSIDEAYLEVRGDGVAAARRLREAVRREVGLAMTVGVGPNRLVAKMACQRAKPDGLLAVAPAEVEAWLAPQPVEALPGLGPVTAARLRQAGIATLGQLAAADPVVLHRLLKGRAAELQARARGWDPRPVGLVAPARSLSEERTFPQDRRAQDVLPVLAELCEELGGRLRRQGYEATQITLKVRYADFTTVTRSRTLPRPACADGELFAAARELLARHVPP... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
B4RHL5 | MQRSMGRVRREWRDQLSRYGAALALVAASTAVAEALYRLTATTRLSMVFLAGVLLAAFLLGSGPAYFAAAVAFLVYNFYLVEPRFTIELTTPEELLTLLVFLAVAMLTGNLTGRVRDEAARAEARARATTALFDATREFSASSDEGLIRQRLAEHLAATAGGEGFVRDAGRLQMAPAGLRREDIPGGLPGAAEPAGGWTLRRLEVEGQALGTAGWRAPPDRRLSRDEHDLLELMCDAGAAAIARARLAAGKAEAEARARTEDLRNALLSSISHDLRTPLAAILASATSLREFGDSFDPGVRRDLAATIQEETERLDAVVA... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 485
Sequence Mass (Da): 52173
Location Topology: Multi-pass membrane protein
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A0A559M4K4 | MIPSDWRFWSPSGALFPGGPYTWHIIDWDQRRWISVTGSEEALPDDEDAINILSKHIDHLDLDVFEIKVSDDGELLSTSSNLKDDATWAIHYPRYNVSSTPSMEKDTLTRSLLEEVDRLGPEVDLVRYADESGISKLVVFKYAMIEQHLRRMWKELHIIKSLPQHPFIVPLDRIVLDDTEPRILGFTTPYVPGGTFADNQTRPFRFKWLQQLTSVVDDLNLKFNITHQDISPRNLLVDPVTENIQLFDFDRAAKIGSQGEDRRRNDVDGVIFTIYEILTLDDHFRTIPFDQQDVKNVEEIETWDVKAPVEAGTGGVEAFR... | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N... |
A0A3P7LP80 | MIALALFGDQPKNSKVIEKLGISVTLKKSEINEERVTVAIWEVLENKRYSSTVKRLSEMARKQPVSPKEVLMKWTECLADFKTLDNLRQLE | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 91
Sequence Mass (Da): 10492
Location Topology: Single-pass membrane protein
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A0A3P7IHU4 | MLWRTLCADSVKYTYPVAACDYFDKIILIWRTQSQSVNRRLFGSVTVKSDFEDYSAILQTALELVSAVSFDPKCEVRKLIPKDALFSQKCYEVSYYEDELVVVFIPVQLDLCNNKKTAHIPFPYKLSCQVLSEFRQVEIVCLRLILSVPTCVADTDCRWLLNTVFPALHKWLQFIDPHKTVRKTNNLLDLEEYSHRYKRIKEEYGRKLVESWTEKTDPKKFVYEDCGIAAYLLELWRKRGRFPRKFADLGCGNGLLVHLLNKEGVSGIGIDIRKRKIWSEQFSESSLIEQVVDPSQKETSIPSDVDYLIGNHTDELTPWM... | 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: 527
Sequence Mass (Da):... |
A0A4V1XD99 | MVSLVWGASLARSAVDLNGAQVVAPVIEDDPSPITDNNAGVAATGAPVENPKKWEELLDASLDIVPACAVTGKELQEKLALSASGSGGKGSGGEVAILLEGMRKFFNAEDNYDENFLFAYYRQTVASVYIGGGLGKPTIGSAMETLAARLQTGGSIPGRTVAQLCNGGRQPERVFGVFIDITGDLAGVQKTAWDWSQGNCAADRELVSAGVLPSIKHIQVVAGDSYAFLAFKYGINGADFTKYNLKKDLCSTFMPGDYVCYSAGDPYTEPKPNPPKAGPDGTCTTHLIANRDSCAALAKKYGLTISQIKRFNKGKTWAWT... | Catalytic Activity: Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
EC: 3.2.1.14
Subcellular Location: Secreted
Sequence Length: 746
Sequence Mass (Da): 80656
|
A0A0R3L5Q6 | MKAWRYVGKLLSMRDGEADQFSQAVDNATAVLRQALQQEHDRAEALATELANARRAMEQIPAAVDGRPGVSLPAWANSYALVKPAQTAVQPDVARENGKSAIKPGEPARVEHKPRGGYGCQHFRTYDPASGTYMGYDGRRHSCP | Function: Has immunoglobulin-binding and hemagglutination properties, and can bind to mannose. Essential for virulence. May be involved in LPS biosynthesis or polysaccharide transport.
Subcellular Location: Cell membrane
Sequence Length: 144
Sequence Mass (Da): 15736
Location Topology: Single-pass membrane protein
|
D3ENP3 | MIKTRKNYLRTFLNIIFISSLVLTGCSEISSKFNSSDSKREINSTQQMHQIDVNNYTPRLDSTAVVEMSINDSSIIIEINGREAPITAGNFIDLVERGFYNGLVFHRVIKDPTPFVAQGGDPDGTGMGGFVDPKTKQRRYIPLEIKLENDEKPIYNQSLGIQGSASPKSVVLKHKRGSVAMARSAMPDSASSQFYVALSDLDFLNGDYAVFGTVIEGMKIVDNIKEGDRISSMHVISGLENFKK | 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: 244
Sequence Mass (Da): 26992
|
A0A8K0MPP3 | MKEGGMDAIKLEGGSPARINAVKAIVEAGIVVVGHVGLTPEPINSVGGFIPQGKNAASAIKLVETALALHEAGCFVVILECVLPHMAVATTSALRIPTIGIELGLFAMVKCKSYLRKNTIDCLKTLIPLPL | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
EC: 2.1.2.11
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Length: 131
Sequence Mass (Da): 1... |
A0A8K0GY66 | MAKPRYSRLPSRKTSSSTLVLTLLVMFTFALIILLALGILSVPSSSGDFAKANDLTSIARNSVDRCTKDECEYLIELAKPKMQKSTVVDSETGKSKDSRFVLCISSLFIFELWNILARGRDKIIRNIEKKLADFTFLPVENGEGLQVLHYEVGQKYEPHYDYFLDDFNTVNGGQRMATVLMYLSDVEEGGETVFPAAKGILALFLGGMSCLNVAKGTFCQT | Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 221
Sequence Mass (Da): 24548
Location Topology: Single-pass type II membrane protein
|
A0A3P7IK59 | MCLLLREENIMGEYFDHILDLLVQLKNGHVNGIRVRMGRVHQLLNTSCIEHIDFATSDDVEFDIDVLEETDGNNQILSRLSLRDGIEDDTTVEEDVRVLKDDDLYEIIKKEDMEKPRQLAFALAAMWSRRHPDTPLDGSSIRERMERLYRRVCQLRLWWLVRYCAGRLRKVMNSLAPAITNMLVRGKQVTIGVRGVHEEVIRRPISPGELTNLLFACCPQDEPQVAVMQQELIIACSDLVRISEFSAISIYLHFPTQMGHSPTAFDGVLTIRLSWLADAITLLLNYVRTTGSLSRSGGKLVTPATPTTTGIPEVKVNDEN... | 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: 345
Sequence Mass (Da): 38955
Location Topology: Lipid-anchor
|
A0A2T0ZW87 | MTGLTDQNEITSVVSTHVLETPDFPSEGVLFRDFTPLFCDGSAFARVVDLIAEQVTAKGGVDLVAGIEARGFLLCAAIGYKLGAGVVPIRKAGKLPAPTVTESYALEYAEATIEIGPHAVNKGDRVLLVDDVLATGGTMVAAATLMRKLGAEVVDSWVLLEIEALGGAKAMQAADLTFNTAMTV | Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1.
Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
EC: 2.4... |
G8PBX7 | MKHYIKLFSTILLLGLILAGCMSNDNQSKDKMGTIKTGIARSTVFALVSSAENSTTDYTKQYSYIEDIGDGRGYTGGIIGFTSGTGDMLAVVKKYTHLRPRNNILAKYLLALKKVNGSASHKGLGKNFIVAWKKAADDSRFIKAQDAILNEQYMQPALKYSKKDHLGQLGQYIYYDALVVHGPGTPKEKNTFQGIRHQALKYAKSPSEGGSQHAYLLAFLRARKPIMREEQAHHDLSRLNTQRQFIEDKNYSLKLPLKWKMYGDTYSLTKKQAADFLQKTQ | Function: Aids in the defense against invading fungal pathogens by degrading their cell wall chitosan.
Catalytic Activity: Endohydrolysis of beta-(1->4)-linkages between D-glucosamine residues in a partly acetylated chitosan.
EC: 3.2.1.132
Subcellular Location: Secreted
Sequence Length: 281
Sequence Mass (Da): 31612
|
A0A2P1J271 | FIFGAWAGMVGTSLSILIRAELGHPGALIGNDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWMLPPSLSLLLTSSLVENGAGTGWTVYPPLSANISHAGASVDLAIFSLHLAGISSILGAVNFITTIINMRSNGITFDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTD | 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... |
A0A336M7X6 | MESNKLKSIKEFYNGKIILVTGGTGFLGKTLIEKLLWSCDGVEKIILLLRSKKGKSVEDRIASLKREVAFQRIHEKKPSVLDKIIGIEADLSAGSLKFESENGDFVSNELRNVNLIFHCAASVRFDDPLKKAILINVCATKALLDFAKTLQHLEVFMHVSTAYSNCDRFEIDEKLYPASVDWRYAIKISEQFDEEILDALFYKFSNNMANTYVFTKKIAEHMVDDYKNALPIVIYRPSIVTSAEVEPLPGFIDNFNGPLGLLVATSMGVNRTSWQSHKAAINATPVDMCIKGIIIAAMRCPESWKETKDIQIYNAASIKT... | 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: 982
Sequence Mass (Da): 112626
|
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