accession stringlengths 6 10 | name stringlengths 6 11 | Full Name stringlengths 1 147 ⌀ | taxon stringlengths 3 46 ⌀ | sequence stringlengths 16 2.75k | function stringlengths 6 5.51k | AlphaFoldDB stringlengths 6 10 |
|---|---|---|---|---|---|---|
Q54T57 | PONM_DICDI | Ponticulin-like protein M | Dictyostelium | MKFLSTLILLLSVLALVRGEQYNKFTVDLNGVCTNSGSLDTCTNQCGNAGGSFQISQSGGEYQYEQYATKDCDLMASLTSKFACLADEAPVTLGLGNIKITCQDPSNSASSPLTTAVLFVVAFAAAIALLL | Binds F-actin and nucleates actin assembly. | Q54T57 |
A4WWP0 | PNP_CERS5 | Polynucleotide phosphorylase | Cereibacter | MFNVTKKSIEWGGETLTLETGKVARQADGSVIATLGETSVMANVTFAKAAKPGQDFFPLTVHYQERYYAAGKVPGGFFKREARPSEKETLTSRLIDRPIRPLFVDGFKNEVLLIVTVLSHDLVNEPDIVAMIAASAALTISGVPFMGPIGAARVGYANGEYVLNPDVDDMQKLRENPEQRLDLVIAGTKDAVMMVESEAYELSEAEMLGAVKFGHEAMQPVIDMIIDFAEEAAKEPFDFSPPDYAALYAKVKSLGEAQMRAAFAIREKQERVNAIDAARAAIKAQLSDAELADENLGTAFKKLESSILRGDIINGGARID... | Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. | A4WWP0 |
A9JX75 | TOX1_PHANO | Toxin 1 | Parastagonospora | MKLTMVLSVAFATLTFANEGILTFEGLGLARRQTICHTPGGSGCRASISGDQCCCTSCTPEDCSDLCKNGKQAAHEAQKQKKCAKCCNAGGESHELCCSIASAGIDCNPCTAGLRMC | Necrotrophic effector that plays a critical role during fungal penetration, via its interaction with the host Snn1 protein . Snn1 is a member of the wall-associated kinase class of receptors, which are known to drive pathways for biotrophic pathogen resistance . Recognition of Tox1 by Snn1 induces mitogen-activated pro... | A9JX75 |
Q10YP7 | PSTB_TRIEI | Phosphate-transporting ATPase | Trichodesmium | MLEHQTNTYQQNSTPALSAENLSIFYGDFKALKDISMRIPKNKVTAFIGPSGCGKSTLLRCFNRLNDLIDIFRLEGRILYHNQNIYDPDIDPVEIRRHIGMVFQKPNPFPKSIYDNIAYGVRVNGLAKSKEEMDEIVERSLRQAVLWDEVKDKLGQSGFALSGGQQQRLCIARAVAISPDVVLMDEPCASLDPISTVKVEELINELRQKYTIIIVTHNMQQATRIADLTAFFNAKAVESGQRFGYLVEFDKTNNIFQNPREKATQDYVSGRFG | Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system. | Q10YP7 |
B5ZYC6 | EX7L_RHILW | Exodeoxyribonuclease VII large subunit | Rhizobium | MSNVFDSDSPTNLAEYSVSELSGSIKRTVETAFDQVRVRGEISGYRGPHSSGHAYFALKDDRARIDAVIWKGTFSRLKFRPEEGMEVIATGKVTTFPGSSKYQIVIETLEPAGAGALMALIEERKRKLGAEGLFDAARKKRLPFMPRVIGVVTSPTGAVIRDILHRISDRFPVHVLVWPVKVQGEGSGEEVANAIRGFNALEPAGLIPRPDVLIVARGGGSLEDLWSFNDEIVVRAAAESRIPLISAVGHETDWTLIDYAADVRAPTPTGAAEMAVPVKAELEAQAAALAARLQGCMNRQMDQRRQSVRALMRALPSLDQ... | Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. | B5ZYC6 |
Q8GYC7 | PGL1B_ARATH | Ferredoxin-plastoquinone reductase 2 | Arabidopsis | MAFTLTIPRFSAISRKPITCSSSRTQCPAPFTHGRSISLRRRLTLLPLKASTDQSGQVGGEEVDSKILPYCSINKNEKRTIGEMEQEFLQAMQSFYYEGKAIMSNEEFDNLKEELMWEGSSVVMLSSDEQRFLEASMAYVSGNPILSDEEYDKLKMKLKMDGSEIVCEGPRCSLRSKKVYSDLAIDYFKMFLLNVPATVVALGLFFFLDDITGFEITYLLELPEPFSFIFTWFAAVPAIVYLALSLTKLILKDFLILKGPCPNCGTENVSFFGTILSIPNDSNTNNVKCSGCGTEMVYDSGSRLITLPEGGKA | Ferredoxin-plastoquinone reductase involved in cyclic electron flow (CEF) around photosystem I. The homodimer is probably not involved in CEF. | Q8GYC7 |
Q1LLY7 | HBOH_CUPMC | D-(-)-3-hydroxybutyrate oligomer hydrolase | Cupriavidus | MQQRHLSQSAHSHGHGTRRAHRRNTIAIAVATLAVAACGGFGTNGSGGNTGPNVKPAFISGPVGVKSYDGNTDDLLTAGLGKDGLAAAAPAFANPNAPTAVELRRNAIWANYRAIVDVQAAGGYGSLYGPNVDAKGNVTTGQGKVPGTEYIAFTDDGSGRQNVTVMAQVPDGFDVKHPCIISATSSGSRGVYGGIAVGEWGLKHNCAVAYTDKGTGAAPHDLGSDTVPLIDGTRQTRAGAGTQAQFAAQPGASETLAGFNSSTPHRLAFKHAHSQQNPEANWGANTLQAIQFTLWAVNDKFGRTNTDGMRQATFTPANVL... | Participates in the degradation of poly-3-hydroxybutyrate (PHB). It works downstream of poly(3-hydroxybutyrate) depolymerase, hydrolyzing D(-)-3-hydroxybutyrate oligomers of various length (3HB-oligomers) into 3HB-monomers. | Q1LLY7 |
Q94JS0 | UCRI1_ARATH | Ubiquinol-cytochrome c reductase iron-sulfur subunit 1 | Arabidopsis | MLRVAGRRLFSVSQRSSTATSFVVSRDHTLSDGGGDSSSAPRSLPSADLSSYHRSLIRGFSSQVLAQGNEIGFGSEVPATVEAVKTPNSKIVYDDHNHERYPPGDPSKRAFAYFVLSGGRFVYASVLRLLVLKLIVSMSASKDVLALASLEVDLGSIEPGTTVTVKWRGKPVFIRRRTEDDIKLANSVDVGSLRDPQEDSVRVKNPEWLVVVGVCTHLGCIPLPNAGDYGGWFCPCHGSHYDISGRIRKGPAPYNLEVPTYSFLEENKLLIG | Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidor... | Q94JS0 |
P01942 | HBA_MOUSE | Hemopressin | Mus | MVLSGEDKSNIKAAWGKIGGHGAEYGAEALERMFASFPTTKTYFPHFDVSHGSAQVKGHGKKVADALASAAGHLDDLPGALSALSDLHAHKLRVDPVNFKLLSHCLLVTLASHHPADFTPAVHASLDKFLASVSTVLTSKYR | Hemopressin acts as an antagonist peptide of the cannabinoid receptor CNR1. Hemopressin-binding efficiently blocks cannabinoid receptor CNR1 and subsequent signaling. | P01942 |
P32340 | NDI1_YEAST | NADH:ubiquinone reductase (non-electrogenic) | Saccharomyces | MLSKNLYSNKRLLTSTNTLVRFASTRSTGVENSGAGPTSFKTMKVIDPQHSDKPNVLILGSGWGAISFLKHIDTKKYNVSIISPRSYFLFTPLLPSAPVGTVDEKSIIEPIVNFALKKKGNVTYYEAEATSINPDRNTVTIKSLSAVSQLYQPENHLGLHQAEPAEIKYDYLISAVGAEPNTFGIPGVTDYGHFLKEIPNSLEIRRTFAANLEKANLLPKGDPERRRLLSIVVVGGGPTGVEAAGELQDYVHQDLRKFLPALAEEVQIHLVEALPIVLNMFEKKLSSYAQSHLENTSIKVHLRTAVAKVEEKQLLAKTKH... | Catalyzes the oxidation of NADH generated inside the Mitochondrion. | P32340 |
B2IMY9 | SYE_STRPS | Glutamyl-tRNA synthetase | Streptococcus | MSKDIRVRYAPSPTGVVHIGNARTALFNYLYARHHGGTFLIRIEDTDRKRHVEDGERSQLENLRWLGMDWDESPESHENYRQSERLDLYQKYIDQLLAEGKAYKSYVTEEELAAERERQEAAGETPRYINEYLGMSEEEKAAYIAEREAAGIIPTVRLAVNESGIYKWHDMVKGDIEFEGGNIGGDWVIQKKDGYPTYNFAVVIDDHDMQISHVIRGDDHIANTPKQLMVYEALGWEAPEFGHMTLIINSETGKKLSKRDTNTLQFIEDYRKKGYLPEAVFNFIALLGWNPGGEDEIFSREELIKLFDENRLSKSPAAFD... | Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). | B2IMY9 |
Q6CF69 | RLP24_YARLI | Ribosome biogenesis protein RLP24 | Yarrowia | MRVYNCHFCSSPVYPGKGIMFVRNDSKEFRFCRSKCHKNFKMKRNPRKLRWTKAFRKAAGKEMVVDSTLAFSARRDVPVRYNRDLVEKTLEAMEKVEEIRLKRERAFYKNRMRGNKAAQLEEDRKLVEAHPELLREREVELRRMQEAGEDDDDEDMSEMEVSEEEESEEEREKVEIALKSKSKRKMRA | Involved in the biogenesis of the 60S ribosomal subunit. Ensures the docking of YALI0_B00990g/NOG1 to pre-60S particles. Activates and recruits ATPase AFG2 to cytoplasmic pre-60S ribosomal particles. | Q6CF69 |
Q57JA4 | AAEB_SALCH | p-hydroxybenzoic acid efflux pump subunit AaeB | Salmonella | MGIFSIANQHIRFAVKLACAIVLALFIGFHFQLETPRWAVLTAAIVAAGPAFAAGGEPYSGAIRYRGMLRIIGTFIGCIAALIIIISMIRAPLLMILVCCVWAGFCTWISSLVRIENSYAWGLSGYTALIIVITIQTEPLLTPQFALERCSEIVIGIGCAILADLLFSPRSIKQEVDRELDSLLVAQYQLMQLCIKHGDSEEVDNAWGDLVRRTAALEGMRSNLNMESSRWVRANRRLKALNTLSLTLITQSCETYLIQNTRPELITDTFRELFETPVETVQDVHRQLKRMRRVIVWTGERETPVTLYSWVGAATRYLLL... | Forms an efflux pump with AaeA. Could function as a metabolic relief valve, allowing to eliminate certain compounds when they accumulate to high levels in the cell. | Q57JA4 |
Q9S757 | CYSC1_ARATH | O-acetylserine (thiol)-lyase 5 | Arabidopsis | MASVSRRLLRRETIPCFSHTVRKLFSTVGSPSFAQRLRDLPKDFPSTNAKRDASLLIGKTPLVFLNKVTEGCEAYVAAKQEHFQPTCSIKDRPAIAMIADAEKKKLIIPGKTTLIEPTSGNMGISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAELVLTDPAKGMGGTVKKAYDLLDSTPDAFMCQQFANPANTQIHFDTTGPEIWEDTLGNVDIFVMGIGSGGTVSGVGRYLKSKNPNVKIYGVEPAESNILNGGKPGPHAITGNGVGFKPEILDMDVMESVLEVSSEDAIKMARELALKEGLMVGISSGANTVA... | Acts as a major beta-cyanoalanine synthase. The cyanoalanine synthesis reaction is more efficient than the cysteine synthase activity. Probably unable to interact with SAT and to form the decameric Cys synthase complex (CSC) and is therefore not an enzymatically true OASTL protein. Probably involved in the detoxificati... | Q9S757 |
B0TEJ8 | NADK_HELMI | ATP-dependent NAD kinase | Heliomicrobium | MPTVGVVLNDDKPQALEVARRMADWLSQREVPMGIPLTRVAELVHSPSPELRDRLRQLDLIVVLGGDGTLLNTARLAAPHGIPVVGVNLGRLGFLTEVEVSDLFPALERIIAGDYRIEERMMLEARLIRDGLEQPSYFALNDVVVTKGDHPRMIRVEAAVGDEVVWTYSADGLIVSSPTGSTAYSLSAGGPIVSPELHALLLTPISPHALDARPLVIPQDQAVRLTVISSHSHAVVTVDGQPGQPMVCGDSVLVRKASVACRLIRLGERTFFRILREKMQQGR | Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP. | B0TEJ8 |
P08303 | COXZ_PARDE | Cytochrome c oxidase assembly protein CtaG | Paracoccus | MSGGKPRSNTRTVAMLAGVVVLMGALSWAAVPFYSWFCKVTGFAGTTNVAEAASDTVLDEKIRVRFDANADSNLGWTFRPMQREMELKIGENAIAFYEAINNTDEPVTGTASYNVAPDAAGYFFNKIECFCFTEQTLQPGERVEMPVSFFVDADLVNDRDAVIRDITLSYTFHRTDPPAPKQAALDAKTEPTVN | Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I. | P08303 |
P0A0M0 | ETXH_STAAU | SEH | Staphylococcus | MINKIKILFSFLALLLSFTSYAKAEDLHDKSELTDLALANAYGQYNHPFIKENIKSDEISGEKDLIFRNQGDSGNDLRVKFATADLAQKFKNKNVDIYGASFYYKCEKISENISECLYGGTTLNSEKLAQERVIGANVWVDGIQKETELIRTNKKNVTLQELDIKIRKILSDKYKIYYKDSEISKGLIEFDMKTPRDYSFDIYDLKGENDYEIDKIYEDNKTLKSDDISHIDVNLYTKKKV | Staphylococcal enterotoxin that activates the host immune system by binding as unprocessed molecules to major histocompatibility (MHC) complex class II and T-cell receptor (TCR) molecules via their alpha domain, in particular TRAV27 . In turn, this ternary complex activates a large number of T-lymphocytes initiating a ... | P0A0M0 |
A6WNV3 | DAPE_SHEB8 | N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase | Shewanella | MIPADDYPVTELTKALIARPSVTPLDEGCQTLMAERLSAIGFNIEPMVFEDTTNMWARRGNEGPVFCFAGHTDVVPTGDVSRWHTPPFVPTIIDGYLYGRGAADMKGSLAAMVIATERFVAKHPDHNGSIAFLITSDEEGPFINGTTRVIDTLEARNEKITWALVGEPSSTLKLGDVVKNGRRGSLTGNLIVKGIQGHVAYPHLADNPIHKAAPFLAELSQMHWDNGNEFFPPTSFQIANINGGTGASNVIPGALDVMFNFRYSTEVTAEILIERVEALLKAHELGYDISWIFNGLPFLTGDGPLLDATRIAIRQVTGYE... | Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls. | A6WNV3 |
B8EBJ4 | RL24_SHEB2 | 50S ribosomal protein L24 | Shewanella | MAAKIRREDEVIVLAGKDKGKRAKVSQVLPTGKLIVEGINLVKKHQKPNPQLGVAGGIVEKEAPIQASNVAIFNSATGKADRVGFRFEDGKKVRFFKSNSELVK | One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. | B8EBJ4 |
A9JRZ0 | SMUF2_DANRE | SMAD-specific E3 ubiquitin-protein ligase 2 | Danio | MSNQGVRRNGPVKLRLTVLCAKNLVKKDFFRLPDPFAKVVVDGSGQCHSTDTVRNTLDPKWNQHYDLYIGKSDSITISVWNHKKIHKKQGAGFLGCVRLLSNSINRLKDTGYQRLDLNKLGPNDSDTVRGQIVVSLQSRDRIGSGGPVVDCSRLFDNDLPDGWEERRTASGRIQYLNHITRSTQWERPTRPASEYSSPGRPLSCLVDENTPIMTPNGAAGVPADDPRVQERRVRSQRHRNYMSRTHLHTPPDLPEGYEQRTTQQGQVYFLHTQTGVSTWHDPRVPRDLSNVNCEELGPLPPGWEIRNTATGRVYFVDHNN... | E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. | A9JRZ0 |
Q9JYJ8 | PYRG_NEIMB | UTP--ammonia ligase | Neisseria | MTKFIFVTGGVVSSLGKGIAAASIAAILESRGLNVTMLKLDPYINVDPGTMSPFQHGEVFVTDDGAETDLDLGHYERFIDSTMTRRNSFSTGQVYENVIAKERRGDYLGGTVQVIPHITDEIKRRIHEGAAGYDVAIVEIGGTVGDIESLPFLEAIRQMRSQLGRNNTLFAHLSYVPYIAAAGEIKTKPTQHTVKEMLSIGLQPDILICRMDRTMPADERRKIALFCNVEERAIVGSYDVDSIYECPEMLHDQGIDNIITEQLQLNVQQADLTAWKKIVHAIQNPKHTVKIAMVGKYVDLTESYKSLIEALKHAGIHTET... | Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. | Q9JYJ8 |
Q1H1Z8 | CRCB_METFK | Putative fluoride ion transporter CrcB | Methylobacillus | MYQVMLVALGGAIGSAARFTLSGLVLRYSLDWRFPLPTFTVNIIGCLVIGMLAGLASKEGFISPDMRVLLFTGLVGGFTTFSAFGLETLVLLREGLVGIAAAYIVSSIVVGLVLMWLGFELVKMTMQA | Important for reducing fluoride concentration in the cell, thus reducing its toxicity. | Q1H1Z8 |
Q2RLU8 | UVRC_MOOTA | Excinuclease ABC subunit C | Moorella | MDLEEKLARLPDHPGVYIMHDANGAIIYVGKAASLRNRVRSYFRGQHQPRTQAMVSHVADFEYILTDNEVEALILECNLIKQHRPRYNVSLKDDKSYPYIKITTQEDFPRIQITRSVTRDGSRYFGPYTSAGSLKETLKLLRGLFPIRTCRDTPLQPRSRPCLNAHIGRCLAPCAGQVDRETYREAVDNVIMFLEGRHTALVKELKEQMEAAAARLEFEKAARLRDQLRAVQEVCEKQKLAAASGEDADAIAFAREGEAALGLIFFSRGGKVIGRDHFFLTGSEGLSRGEVMAALLKEYYSRGVEIPPEILLHDEPEDAA... | The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. | Q2RLU8 |
P52894 | ALA2_HORVU | Glutamic--pyruvic transaminase 2 | Hordeum | MAATVAVDNLNPKVLKCEYAVRGEIVIHAQRLQEQLKTQPGSLPFDEILYCNIGNPQSLGQQPVTFFREVLALCDHPDLLQREEIKTLFSADSISRAKQILAMIPGRATGAYSHSQGIKGLRDAIASGIASRDGFPANADDIFLTDGASPGVHLMMQLLIRNEKDGILVPIPQYPLYSASIALHGGALVPYYLNESTGWGLETSDVKKQLEDARSRGINVRALVVINPGNPTGQVLAEENQYDIVKFCKNEGLVLLADEVYQENIYVDNKKFHSFKKIVRSLGYGEEDLPLVSYQSVSKGYYGECGKRGGYFEITGFSAP... | Transfer of C3 units between the cytosol of mesophyll and bundle sheath cells to maintain a nitrogen-carbon balance in the C4-dicarboxylic pathway. | P52894 |
A0KSP4 | RAPA_SHESA | ATP-dependent helicase HepA | Shewanella | MPFALGQRWISDTESELGLGTVVQVEGRMVTVLFPATGENRMFSRNEAPLTRVIYNPGDTVESHEGWSLSVEELTEKDGLVVYHGIHSETGEKVSLRETLLNHNIRFNKPQDRLFAGQIDRLDRFGIRYQCQLLRHQLATSDLLGLQGPRVGLIPHQMWIAHEVGRRYAPRVLLADEVGLGKTIEAGLIIHQQLLTGRAERVLIIVPDTLRHQWLVEMLRRFNLRFSVFDEDRCVEAFADHDNPFYTEQLVICSLELLRKKKRLDQALDADWDLLVVDEAHHLEWTEEAPSRAYQVVEALSEVVPGVLLLTATPDQLGHE... | Transcription regulator that activates transcription by stimulating RNA polymerase (RNAP) recycling in case of stress conditions such as supercoiled DNA or high salt concentrations. Probably acts by releasing the RNAP, when it is trapped or immobilized on tightly supercoiled DNA. Does not activate transcription on line... | A0KSP4 |
Q882V6 | MOAA_PSESM | Molybdenum cofactor biosynthesis protein A | Pseudomonas | MSEPVLMDRFARKVDYLRMSVTDRCDFRCVYCMAEEMTFLPRQQILSLEEIHQVAERFVALGTRKIRLTGGEPLVRAGVVGLCEKIAALPGLRELCMTTNGSQLDKLAAPLFKAGVTRLNISLDSLDPQRFRELTRTGDLHKVIAGIDAANAAGFVHTKLNCVVMHGRNDHEINDLLAFAIDRNLDVSFIEEMPLGIISEHSRAESFYSSDQVRERIAERYTLIPSTDSTQGPSRYWRLAQAPGIRIGFISPHSHNFCGTCNRVRLTVEGRLLLCLGNEHSVDLKAVLRATPGQPEKLEKAIIDAMQLKPWSHNFTHDDG... | Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate. | Q882V6 |
B1IIG7 | SYE_CLOBK | Glutamyl-tRNA synthetase | Clostridium | MTNKVRTRFAPSPTGYMHVGNLRTALYAYLIAKHDNGDFILRIEDTDQERLVEGALDVIYNTLKITGLSHDEGPDIGGPVGPYVQSERRNIYIEYAEKLIEKGEAYYCFCSKERLDMLRANSEALKRPFRYDKHCIDLSKEEIDKKIAEGVPYVIRQKNPTTGSTSFHDEIYGDISVDNSELDDMILIKSDGLPTYNFANVVDDHLMGITHVVRGSEYLSSSPKYNRLYEAFGWDVPIYVHCPPIMKDEHHKLSKRNGDASFEDLMAKGYLKEAILNYIALLGWNPGGEKEVFSMEELIEAFNYRNINKAPAVFDTKKLK... | Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). | B1IIG7 |
A6Q4N8 | GUAA_NITSB | Glutamine amidotransferase | unclassified Nitratiruptor | MQEVPIVILDFGSQYTQLIARRLREVGVYCEIYPFFEPIENIRAKKPQGIILSGGPASVYEPDAPRVDKAIYELGIPVLGICYGMQLITVDFGGQVVRALEHEYGKAKLYFDPIHGKVCPLFEGTKDGQIVWMSHGDKVTELPAGFIRIAHTDNSPYAAIANEEKQIYALQFHPEVSHSQEGQKILENFARKICGITSKWDMGHFAKEQIEKIRQRVGEDKVLCALSGGVDSSVVTALLYEAIGDKLIPVFVDNGLLREGEREKVEYVFKNMLKVPLIVVDAKERFLNALQGITDPEQKRKIIGHTFIEVFEEEAKKHTD... | Catalyzes the synthesis of GMP from XMP. | A6Q4N8 |
A0LXV8 | NADK_GRAFK | ATP-dependent NAD kinase | Gramella | MKIGIYGQFYHANAAQYIGQLLELLDQRNIEVLIEEDFLKLIHSNNKIEKDYKHFSAFEELDNSFDLFFCIGGDGTILKSINYIRNLDIPIVGINTGRLGFLATIQKEQIESTLEELLEKKFSLSPRSVLTMQTNPRSYDPVFSHIALNEIAVSRKNTTSMITVDTWLDDQYLTSYWADGLIISTPTGSTGYSLSCGGPVITPDADSLVITPIAPHNLNARPLVIKDHTTIKLKVSGRGKEHLVSMDSRIATLQNDTEIIIKKAPYTINFVELQGDSFLNTLRKKLLWGEDKRN | Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP. | A0LXV8 |
Q9KGJ6 | GLMU_HALH5 | Glucosamine-1-phosphate N-acetyltransferase | Halalkalibacterium (ex Joshi et al. 2022) | MSNRFAVILAAGQGTRMKSKLYKVLHSVCGKPMVQHVVDQVSALGFDEIVTIIGHGADAVKSQLGERVSYALQEEQLGTGHAVLQAESALGGRRGVTIVLCGDTPLLTAETIDHVMSYHEEEQAKATVLTAELADPTGYGRIVRNDKGLVERIVEHKDATSEEKQITEVNTGTYCFDNEALFQALKEVGNNNAQGEYYLPDVIQILQTKGEKVAAYKTAHVEETLGVNDRVALAQAEQVMKRRINEAWMRKGVTFIDPEQTYVSPDATIGQDTVIYPGTMVLGQTTIGEGCVLGPHTELKDSKIGNKTAVKQSVVHNSEV... | Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted ... | Q9KGJ6 |
Q1RH25 | TGT_RICBR | tRNA-guanine transglycosylase | belli group | MSKFSFNINHQYKKARSGIITTAHGNIRTPAFMPVGTRGTVKAMLPESVAETGADILLGNTYHLMLQPSAERIAKLGGLHKFMNWGKPILTDSGGFQVMSLSKLRKITEEGVSFNSHINGDKYLLTPERSTEIQHLLGSTITMAFDECTPYPATFEEAKTSMQLTTRWAHRSREAFVKRDGYAQFGIIQGSTYEELREQSAKDLIELDFEGYAIGGLAVGEGQELMFKVLAPDFLPQNKPRYLMGVGKPADIIGAVSRGVDMFDCVIPTRSGRNGQAFTKYGTVNIRNSKYAEDNDPLEADCLCPACQNYSKAYLHHLVR... | Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks th... | Q1RH25 |
Q9W4C5 | NAAT1_DROME | Sodium-dependent nutrient amino acid transporter 1 | Sophophora | MELKGVQPSNGSSNGSGNGATNAASTEKTDAEKPTAERTNWGNGLEFLMSCISVSVGLGNVWRFPFTAYENGGGAFLIPYIIVLFLIGKPMYYLEMIMGQFTSQGTVKIWSVVPGFVGVGYGQAFGTICIISYYSSLLALTLYYLFVSFQSELPWSYCRDEWTNCVNSRPQEYVDNLLTGVSLANESARNLSGIVANDETEKLQSSSELYFLNVVIKEKLDISDGVGDPDWKLTLALFVAWVVIFLVIMRGVKSSGKAAYFLALFPYVVLFVLLIRAVTLEGARDGILFFLEPQWGELLNPTVWKEAVVQCFFSLAVGSG... | Unusual broad substrate spectrum amino acid:sodium cotransporter that promotes absorption of the D isomers of essential amino acids. Neutral amino acids are the preferred substrates, especially methionine and phenylalanine. | Q9W4C5 |
P62452 | HIS6_PHOPR | ImGP synthase subunit HisF | Photobacterium | MLAKRIVPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRVVDKSWVARVAEVIDIPFCVAGGIKSVEDASRILQFGADKVSINSPALANPALITELADKFGVQCIVVGIDSYFDAETGKYQVYQFTGDESRTKATQWETRDWVLEVQKRGAGEIVLNMMNQDGVRNGYDLKQLNMVREVCHVPLIASGGAGEMVHFADAYQKANVDGALAASVFHKQIINIGELKQYLKEQNVEIRL | IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit. | P62452 |
Q3B3Q8 | G6PI_CHLL3 | Phosphohexose isomerase | Pelodictyon | MDLSRSAAWSALVSHRQEVEQLHMRDMFMSDHDRFKHFSIRWNGLLLDYSKNRINSRTMGLLVELARQANLIEARDGMFAGEKINFTENRAVLHTALRRQPGYTLNVDGLDVPAEVDSVLRQMKAFTDKVVGGEWKGYTGKRITDVVNIGIGGSDLGPCMVTEALRPFADGAIAVHFVSNIDGTHVSEVLKRVDAETTLFVIASKTFTTQETLTNSMTAREWFLSRAIDPAHIALHFAAVSTNRTKVVEFGIDPENMFRFWDWVGGRYSLWSAIGLSIALYLGFEAFQELLRGARAMDEHFQEAPLEENIPVILALLGVW... | Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate. | Q3B3Q8 |
A4WIW5 | SYT_PYRAR | Threonyl-tRNA synthetase | Pyrobaculum | MRVLYIHAERFSWDPRDPALDIRDEPVSGSASNALVVFVSVERGDSPDEGFLKAVAADVVETAKKVGASSIVVYPYAHLSTDLARPYTAREVVGKLYEVVKAQFKGQVLKAPFGYYKAFELKCLGHPLSELSRVFKPEEAKTEKRAEERRDYYVVLTPDGAEYDPAKFNYAGLDDFKALVEKEVFKRELGGGEPKYLDYLRKFGFEWEPMSDVGHMRYAPEATVMMELVEDYAYMVAKSLGIPVFKIRGTNMFKLSEYAIESHARLFGERLYVVESDTDLILRYAACFQQFAMVKDWVISYRHLPFGLLEIADSYRHEQP... | Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr). | A4WIW5 |
Q1BUV6 | MSBA_BURCA | Lipid A export ATP-binding/permease protein MsbA | Burkholderia cepacia complex | METQNTLRKPMDGTGTSPMTVLKRLWPYIRPLIGIVVLAVVTMGVVAATEAGIPALLKPLLDHGFGSHGSDSAKWYVPIAVIGLALVRGVSQYTSNYLLNYVSNRILLQLRLEMFQRMIHTGASFFQRETASTVINAIVFEVNQILSVLTGVMVTLVRDSLTVIFLLGYLFYLNWRLTLIVAVILPGIGWLVSKINRRLRRLNREHQTLTNELSYIVEETVGGYKVVKVHNGEAYEMDRFTTMSKRLRGYAMRMTISGGLAQPLTQFLASIALAVVITIAVVQSSNDQTTVGGFVAFVTSMLLVISPLKHLIDVNQPLQR... | Involved in lipopolysaccharide (LPS) biosynthesis. Translocates lipid A-core from the inner to the outer leaflet of the inner membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation. | Q1BUV6 |
P41271 | NBL1_HUMAN | Zinc finger protein DAN | Homo | MMLRVLVGAVLPAMLLAAPPPINKLALFPDKSAWCEAKNITQIVGHSGCEAKSIQNRACLGQCFSYSVPNTFPQSTESLVHCDSCMPAQSMWEIVTLECPGHEEVPRVDKLVEKILHCSCQACGKEPSHEGLSVYVQGEDGPGSQPGTHPHPHPHPHPGGQTPEPEDPPGAPHTEEEGAED | Possible candidate as a tumor suppressor gene of neuroblastoma. May play an important role in preventing cells from entering the final stage (G1/S) of the transformation process. | P41271 |
O77061 | MRJP2_APIME | Bee-milk protein | Apis | MTRWLFMVACLGIACQGAIVRENSPRNLEKSLNVIHEWKYFDYDFGSEERRQAAIQSGEYDHTKNYPFDVDQWRDKTFVTILRYDGVPSTLNVISGKTGKGGRLLKPYPDWSFAEFKDCSKIVSAFKIAIDKFDRLWVLDSGLVNRTVPVCAPKLHVFDLKTSNHLKQIEIPHDIAVNATTGKGGLVSLAVQAIDLANTLVYMADHKGDALIVYQNADDSFHRLTSNTFDYDPRYAKMTIDGESFTLKNGICGMALSPVTNNLYYSPLASHGLYYVNTAPFMKSQFGENNVQYQGSEDILNTQSLAKAVSKNGVLFVGLV... | May play an important role in honeybee nutrition. It is found in the royal jelly which is the food of the queen honey bee larva. The royal jelly determines the development of the young larvae and is responsible for the high reproductive ability of the honeybee queen. | O77061 |
Q31Y50 | PTYBC_SHIBS | PTS system N-acetylmuramic acid-specific EIIC component | Shigella | MAKEISSELLNTILTRVGGPGNIASCGNCMTRLRLGVHDSSLVDPNIKTLEGVKSVILTSDQVQVVFGPGKAHRAAKAMSELLGEAPVQDAAEIAAQNKRQLKAKQTSGVQQFLAKFATIFTPLIPGFIAAGLLLGIATLIATVMHVPADAQGTLPDALNFMKVFSKGLFTFLVILVGYNAAQAFGGTGVNGAIIAALFLLGYNPAATTGYYAGFHDFFGLPIDPRGNIIGVLIAAWACARIEGMVRRFMPDDLDMLLTSLITLLITATLAYLIIMPLGGWLFEGMSWLFMHLNSNPFGCAVLAGLFLIAVVFGVHQGFI... | The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in N-acetylmuramic acid (MurNAc) transport, yie... | Q31Y50 |
C6DKV2 | OPGH_PECCP | Glucans biosynthesis glucosyltransferase H | Pectobacterium | MNKSTSSLDYIEKLPLPAEQAEVLREKLPQAAWNDQAVLHQALSEGSPSEEHQVNVQSEDDATLQSVQARLEMAWAEGLDNGKQLGTDREGRTALKAMPVITRASMFPDVWRTNPLVRWWESLLGRTVPPRPHYSPEEKISENRWRLVGTIRRYILLVLTLFQTAIATWYMKTILPYQGWALIDPFEMAGQPWTRSLMQLLPYVLQSGILVLFAVLFCWVSAGFWTALMGFLQLLIGRDKYSISSTTVGNEPLNPEHRTALIMPICNEDVERVFAGLRATYESVEATGNLEHFDIYVLSDSNDPDICVAEQKAWMELCRD... | Involved in the biosynthesis of osmoregulated periplasmic glucans (OPGs). | C6DKV2 |
P61316 | LOLA_ECOLI | P20 | Escherichia | MKKIAITCALLSSLVASSVWADAASDLKSRLDKVSSFHASFTQKVTDGSGAAVQEGQGDLWVKRPNLFNWHMTQPDESILVSDGKTLWFYNPFVEQATATWLKDATGNTPFMLIARNQSSDWQQYNIKQNGDDFVLTPKASNGNLKQFTINVGRDGTIHQFSAVEQDDQRSSYQLKSQQNGAVDAAKFTFTPPQGVTVDDQRK | May act as a regulator of the RCS-phosphorelay signal transduction pathway. | P61316 |
P38837 | NSG1_YEAST | INSIG homolog 1 | Saccharomyces | MGKKKSKNQLNTGGVPNGVHNTKKEAALPPLGNKLGSASFTAINTLTKPALFSFYDDDITKNEGNVYDKALLSNASQLEMVPPSATARHERSLYAKIINTIAAFFILFIAGILFPMISECLFDNDQLAKGDIVSFLKHGIEIKNKIVAEPDMVPDWAVFGTEGVIFGSIVPFIDSFVRYQHQPKTRSSVYKNTLGSFIRCANTLLGLIFGIRKLEWSSSLQAAGAWSLLNIVLWLFFDGTLTVFFPGLVIGALSAFTCSQCFSQLSLALYFIDFYFFGFLMFSKLGRYLFN | Stabilizes the HMG-CoA reductase HMG2 by preventing its HRD1-dependent degradation. Binds directly to the sterol-sensing domain (SSD)-containing transmembrane region of HMG2, promoting its folding to protect it from degradation. | P38837 |
Q14CS0 | UBX2B_HUMAN | p97 cofactor p37 | Homo | MAEGGGPEPGEQERRSSGPRPPSARDLQLALAELYEDEVKCKSSKSNRPKATVFKSPRTPPQRFYSSEHEYSGLNIVRPSTGKIVNELFKEAREHGAVPLNEATRASGDDKSKSFTGGGYRLGSSFCKRSEYIYGENQLQDVQILLKLWSNGFSLDDGELRPYNEPTNAQFLESVKRGEIPLELQRLVHGGQVNLDMEDHQDQEYIKPRLRFKAFSGEGQKLGSLTPEIVSTPSSPEEEDKSILNAVVLIDDSVPTTKIQIRLADGSRLIQRFNSTHRILDVRNFIVQSRPEFAALDFILVTSFPNKELTDESLTLLEAD... | Adapter protein required for Golgi and endoplasmic reticulum biogenesis . Involved in Golgi and endoplasmic reticulum maintenance during interphase and in their reassembly at the end of mitosis . The complex formed with VCP has membrane fusion activity; membrane fusion activity requires USO1-GOLGA2 tethering and BET1L ... | Q14CS0 |
Q4JTZ6 | RS18_CORJK | 30S ribosomal protein S18 | Corynebacterium | MKRTNMKKARMEQSRRPKKNPLKAEGIETVDYKNYDLLRKFISERGKIRSRRVTGLTPQQQRQVATAVKNAREMALLPFHSR | Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit. | Q4JTZ6 |
Q9PQI5 | END4_UREPA | Endonuclease IV | Ureaplasma | MDKYNLIIGSHVSLKAKDFFYGSVKEALSYGSNTFMVYTGAPQNTKRQPIKSFKIEEAHNLLKKHNINLDDLIVHAPYIINPCSSKKNVRELAKEFLIQEIQRTESMGITKLVLHPGSRLEQNEDIALEQVYTMLNDIFSTINTNVIVCLETMAGKGSEIGVNIKQLKTIIDNVHSKKNIGVCLDTCHMNDSGLILDYYNFNQYLKEFDAQIGINYIKVLHINDSKNPCGANKDRHENLGYGTIGFANLINIIYHPLLNNIPKILETPWFNVNDELIPLYKHEIKMIRDCKWYDIKNKLLSKK | Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate. | Q9PQI5 |
P04969 | RS11_BACSU | 30S ribosomal protein S11 | Bacillus | MAAARKSNTRKRRVKKNIESGIAHIRSTFNNTIVTITDTHGNAISWSSAGALGFRGSRKSTPFAAQMAAETAAKGSIEHGLKTLEVTVKGPGSGREAAIRALQAAGLEVTAIRDVTPVPHNGCRPPKRRRV | Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome. | P04969 |
C6DIA0 | PAGP_PECCP | Lipid A acylation protein | Pectobacterium | MYLKRTLITLSLITLPIVPFLSYAAESINNTSSTENLAPVTVDSSDPVSDKQGESWWQRSKNNLSTTWNAPQSHDIYIPAITWHNRWTYDKEKTDRYNERPWGAGYGVSRLDKDGDWHGLYIMAFKDSFNKWEPIGGYGYEKRWRPTSDQDFQLGLGFTAGVTMRDNWNYIPIPVLLPLASISYSKLSFQATYIPGTYNNGNVFFAWLRWQI | Transfers a palmitate residue from the sn-1 position of a phospholipid to the N-linked hydroxymyristate on the proximal unit of lipid A or its precursors. | C6DIA0 |
P57776 | EF1D_MOUSE | Elongation factor 1-delta | Mus | MATNFLAHEKIWFDKFKYDDAERRFYEQMNGPVTSGSRQENGASVILRDIARARENIQKSLAGSSGPGASSGPGGDHSELIVRITSLEVENQNLRGVVQDLQQAISKLEARLSSLEKSSPTPRATAPQTQHVSPMRQVEPPTKKGATPAEDDEDKDIDLFGSDEEEEDKEAARLREERLRQYAEKKAKKPTLVAKSSILLDVKPWDDETDMAQLETCVRSIQLDGLVWGASKLVPVGYGIRKLQIQCVVEDDKVGTDLLEEEITKFEEHVQSVDIAAFDKI | Regulates induction of heat-shock-responsive genes through association with heat shock transcription factors and direct DNA-binding at heat shock promoter elements (HSE). | P57776 |
A9LYY9 | PROA_NEIM0 | Glutamyl-gamma-semialdehyde dehydrogenase | Neisseria | MSNTQKQLALAKAAKKSVNTADTEEKNRALLAMADSLEAAAADILAANRQDLEAAAGNIPESMTDRLLLDGKRICAMADGIRAVAALPDPVGEILETSTLPNGLEIVKKRVAMGVIGIIYESRPNVTSDAAALALKSGSAVVLRSGKDAFQSARAIVAALKAGLAQTRIDPDALQLIEDTGREGSYEMMRAKDYLDLLIPRGGAGLIRAVVENAVVPVIETGTGIVHIYIDKDADWDKALRIVYNAKTSRPSVCNSMEVLLVHEDIAADFLPKLERLLVRDRIEAGLPPVRFRLDPQAARHIGGEAAGADDFDTEFLDYI... | Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. | A9LYY9 |
A1A1K1 | RUVC_BIFAA | Holliday junction resolvase RuvC | Bifidobacterium | MIILGVDPGLTRCGVGVIEAGAYRRLSFIHVDVVRSDPKTSQDLRLLAIYNGLVEKIERFAPDAVSIERVFAQENRNTVLGTAQAAGLAMLAAAQRGIPVALHTPTESKLAITGNGKAEKIQMERMVARILGLNTLPKPADAADALAIAICHALRPAGALQGGEREQHLTAAQRQWAQASQKAARRQGVRRGM | Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group. | A1A1K1 |
Q93CX7 | UPP_LATSK | UPRTase | Latilactobacillus | MAKFTVLNHPLIQHKLTIIRNKNTGTKVFREVANEIAELMVYEITRDLAMEDVEVETPMGPAIEKQLSGKKLAVVPILRAGLGMVDGVLELIPAAKVGHIGMYRDEKTLQPHEYFVKLPTDIDQRQLFIVDPMLATGGSAIMAIDALKKRGATSMRLVVLVAAPEGVKAVQEAHPDVDIYAAGLDDGLNEEGYIYPGLGDAGDRLFGTK | Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate. | Q93CX7 |
C1DI51 | PYRE_AZOVD | Orotate phosphoribosyltransferase | Azotobacter | MQAYQREFIRFAIERGVLRFGEFTLKSGRTSPYFFNAGLFDSGLALARLGRFYASALVGSGIAFDVLFGPAYKGIPLAAATAVALAEHHGLDLPWCFNRKEAKDHGEGGSLVGAPLSGRVLIVDDVITAGTAIREVMQIIQGQGARAAGVLIALNRQERGQGALSAIQEVERDFAMPVVSIASLSDVLEYLAEDAQLKRHLSAVEAYRAQYGI | Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). | C1DI51 |
Q9H0B6 | KLC2_HUMAN | Kinesin light chain 2 | Homo | MAMMVFPREEKLSQDEIVLGTKAVIQGLETLRGEHRALLAPLVAPEAGEAEPGSQERCILLRRSLEAIELGLGEAQVILALSSHLGAVESEKQKLRAQVRRLVQENQWLREELAGTQQKLQRSEQAVAQLEEEKQHLLFMSQIRKLDEDASPNEEKGDVPKDTLDDLFPNEDEQSPAPSPGGGDVSGQHGGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKEAAHLLNDALAIREKTLGKDHPAVAATLNNLAVLYGKRGKYKEAEPLCKRALEIREKVLGKFH... | Kinesin is a microtubule-associated force-producing protein that plays a role in organelle transport. The light chain functions in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (Probable). Through binding with PLEKHM2 and ARL8B, recruits kinesin-1 to lysosomes and hence direct lysosom... | Q9H0B6 |
Q0TRK5 | COBT_CLOP1 | N(1)-alpha-phosphoribosyltransferase | Clostridium | MLNEVLKGIEGLDNDMILKAKNRVDSLAKPLGSLGKLEDIAIRLSGITGNMFNNIDKKCVIIMSSDNGVEEEGVASAPQCVTLLQTKNFIKGTTGVATLAKSNGTDLMVFDVGINSDEVVEGVINRKISKGTKNIYKEPAMTYEEAKKSLEIGIEAVKIAKEKGYKILGVGEMGIGNTTTSAAVLKALIGCETSQVVGKGGGINNASFEKKKRIVEEVVKKHNINFDDPIDIISKVGGYDIGAMTGVFLGAAFYRIPVVIDGFISVVAALLANRLNPLVKEFCFTSHKSQEIGYELAIKELGLDPMLDLNMRLGEGSGCP... | Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB). | Q0TRK5 |
B3PW62 | RS12_RHIE6 | 30S ribosomal protein S12 | Rhizobium | MPTVNQLIRKPRQANVKRNKVPALQENPQKRGVCTRVYTTTPKKPNSALRKVAKIRLTNGFEVIGYIPGEGHNLQEHSVVMIRGGRVKDLPGVRYHIIRGVLDTQGVKNRKQRRSKYGAKRPK | Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The com... | B3PW62 |
Q9NII6 | KAX15_MESMA | Neurotoxin TX1 | Mesobuthus | MKISFLLLALVICSIGWSEAQFTDVKCTGSKQCWPVCKQMFGKPNGKCMNGKCRCYS | Potent blocker of both large-conductance calcium-activated potassium channels (KCa1.1/KCNMA1) and voltage-gated potassium channels (Kv1.3/KCNA3) . Has also been shown to moderately inhibit Kv1.2/KCNA2 and weakly inhibit Kv1.1/KCNA1 channels, as well as 5-hydroxytryptamine 3 receptors (HTR3A) . | Q9NII6 |
P53689 | ACT_PHARH | Actin | Phaffia | MDDEVAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNAPAFYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGFALPHAILRLDLAGRDLTGYLVKCLMERGYPFTTTAEREIVRDIKEKLCYVALDFEQEMQTAAQSSQLEKSYELPDGQVITIGNERFRCPEALFQPSFLGLEAAGIHETTYNSIMKCDLDIRKDLYGNVVLSGGTTMYSGIADRMQKEITSL... | Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. | P53689 |
P23212 | MSRA_STAEP | Erythromycin resistance ATP-binding protein MsrA | Staphylococcus | MEQYTIKFNQINHKLTDLRSLNIDHLYAYQFEKIALIGGNGTGKTTLLNMIAQKTKPESGTVETNGEIQYFEQLNMDVENDFNTLDGSLMSELHIPMHTTDSMSGGEKAKYKLANVISNYSPILLLDEPTNHLDKIGKDYLNNILKYYYGTLIIVSHDRALIDQIADTIWDIQEDGTIRVFKGNYTQYQNQYEQEQLEQQRKYEQYISEKQRLSQASKAKRNQAQQMAQASSKQKNKSIAPDRLSASKEKGTVEKAAQKQAKHIEKRMEHLEEVEKPQSYHEFNFPQNKIYDIHNNYPIIAQNLTLVKGSQKLLTQVRFQ... | Confers resistance to 14-membered ring macrolides (like erythromycin) and to B streptogramins, by acting as an ATP-dependent efflux pump. | P23212 |
A7GRN4 | DIVIB_BACCN | Cell division protein DivIB | Bacillus cereus group | MKNSKVIKLQDRVPKLKNQKKRNKPPVNHRLILYISILFLLVLFLIYFRSPLSNIKKISVFGNHYMTDEQVMEKSGITYKTSYFRVTARQAEENLKKQIEIKSVDVKKRFPNKIDIHIEEYVTIGYINKNGKLQPLLENGKTLDILPSGKLPVAAPIFEPFKEEKMKELISELEKLTPTILRSISEIRYTPTTSNESHLTLYMNEGYEVSTTIQDFAKRMEAYPLILKQIEPGRKALIDLEVATYFKYLDDEKKK | Cell division protein that may be involved in stabilizing or promoting the assembly of the division complex. | A7GRN4 |
P33533 | OPRD_RAT | Opioid receptor A | Rattus | MEPVPSARAELQFSLLANVSDTFPSAFPSASANASGSPGARSASSLALAIAITALYSAVCAVGLLGNVLVMFGIVRYTKLKTATNIYIFNLALADALATSTLPFQSAKYLMETWPFGELLCKAVLSIDYYNMFTSIFTLTMMSVDRYIAVCHPVKALDFRTPAKAKLINICIWVLASGVGVPIMVMAVTQPRDGAVVCTLQFPSPSWYWDTVTKICVFLFAFVVPILIITVCYGLMLLRLRSVRLLSGSKEKDRSLRRITRMVLVVVGAFVVCWAPIHIFVIVWTLVDINRRDPLVVAALHLCIALGYANSSLNPVLYAF... | G-protein coupled receptor that functions as receptor for endogenous enkephalins and for a subset of other opioids. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Sig... | P33533 |
Q9UQ88 | CD11A_HUMAN | PITSLRE serine/threonine-protein kinase CDC2L2 | Homo | MGDEKDSWKVKTLDEILQEKKRRKEQEEKAEIKRLKNSDDRDSKRDSLEEGELRDHCMEITIRNSPYRREDSMEDRGEEDDSLAIKPPQQMSRKEKVHHRKDEKRKEKWKHARVKEREHERRKRHREEQDKARREWERQKRREMAREHSRRERDRLEQLERKRERERKMREQQKEQREQKERERRAEERRKEREARREVSAHHRTMREDYSDKVKASHWSRSPPRPPRERFELGDGRKPGEARPAPAQKPAQLKEEKMEERDLLSDLQDISDSERKTSSAESSSAESGSGSEEEEEEEEEEEEEGSTSEESEEEEEEEEE... | Appears to play multiple roles in cell cycle progression, cytokinesis and apoptosis. The p110 isoforms have been suggested to be involved in pre-mRNA splicing, potentially by phosphorylating the splicing protein SFRS7. The p58 isoform may act as a negative regulator of normal cell cycle progression. | Q9UQ88 |
Q2RVU8 | FTSQ_RHORT | Cell division protein FtsQ | Rhodospirillum | MRRVSQPPPRPRHRRRRRRDVLPSLPRASMVFLIAGGVGMAYLAARTPALAGLIGLAPPPALGAPGSSVPPAGARDAGEGWGLGETARVLTRQGLVLRQVTVTGRDLTAGRDILGAIGVPQGGPLLAIDPETVRTRLEALPWVASARVERRLPDQVHVAITEREPMALWQHNGAFAVIDREGRAIAADPGRWRTLPLVVGAGAPGHAAELLNLLTSQPGIAERVKAATLIGERRWTLRLDSIENGLVVRLPEEDPSAALDQLVQIDARDHLLSKNLSVIDMRLPGRLVVRLAEDGPVDPEAEIAGGKPARGAPAGGQKPP... | Essential cell division protein. | Q2RVU8 |
Q215X7 | YQGF_RHOPB | Putative pre-16S rRNA nuclease | Rhodopseudomonas | MPAPILPLIEAAAQWPARGALIGLDLGTKTIGVAVSDPDRRLATGVETIIHTAFKANAARLLLLAGQRNAVGFVLGLPINMDGSEGPRAQSTRAFARNFARLTDLPIGLWDERLSTSAVERELIANDVSRAKRAKVIDEHAAIFILQGALDRLTVLNAAPRTD | Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. | Q215X7 |
Q6L3A7 | RPOB_SACHY | Plastid-encoded RNA polymerase subunit beta | unclassified Saccharum | MLRNGNEGMSTIPGFSQIQFEGFCRFINQGLAEELEKFPTIKDPDHEIAFQLFAKGYQLLEPSIKERNAVYESLTYSSELYVSARLIFGFDVQKQTISIGNIPIMNSLGTFIINGIYRIVINQILLSPGIYYRSELDHKGISICTGTIISDWGGRLELAIDKKERIWARVSRKQKISILVLLSAMGLNLREILDNVSYPEIFLSFLNAKEKKRIESKEKAILEFYQQFACVGGDLVFSESLCEELQKKFFQQKCELGRVGRRNMNRRLNLDIPQNNTFLLPRDVLAATDHLIGMKFGTGILDDDDMNHLKNKRIRSVADL... | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | Q6L3A7 |
B1V8A0 | SH3GH_CAEEL | Uncoordinated protein 57 | Caenorhabditis | MSLSGLRKQFNKANQYLSETMGAAEPTKLDDVFNEMEKNVDTTYNLITDLVAGTNEYLQPNPATRAKMATQVALSKVRGTTKTSPYPQTEGMLADVMQKYGQQLGDNSDLGKSLNDAAETYRQMADIKYQMEDNVKQNFLDPLTHLQNNELKDVNHHRTKLKGRRLDYDCKKRQQRRDDEMIQAEEKLEESKRLAEMSMFNVLSNDVEQISQLRALIEAQLDFHRQTAQCLENLQQQLGHRIKDAAARPREEHVPLSVLANESRTPRSSFRSPAPSDMSHNSTAAAAFKMPPQNGGGITQAPPSYQGPPPGGLPPPLSQQ... | Involved in synaptic vesicle (SV) recycling in neurons probably by regulating clathrin-mediated endocytosis . By controlling SV endocytosis, regulates the rate of excitatory postsynaptic currents (EPSCs) at neuromuscular junctions and thus locomotion . In a similar manner, involved in necrotic neuronal cell death induc... | B1V8A0 |
P83283 | IBB2_AMBCE | TcTI2 | Amburana | SSKWEACCDRCACTKSIPPQCHCADIRLNSCHSACESCACTHSIPAQCRCFDITDFCYKPCSG | Inhibits trypsin, chymotrypsin, plasmin and factor XIIa. Does not inhibit factor Xa, thrombin, human plasma kallikrein, porcine pancreatic kallikrein and human urinary kallikrein. | P83283 |
Q64391 | CP1A2_CAVPO | Hydroperoxy icosatetraenoate dehydratase | Cavia | MPLSWLLPFSAMELLLTATIFYLVLWVVKAFRLQVPKGLKSPPGPWGWPLIGHVLTLGKNPHLALTRLSARYGDVLQIRIGSTPVVVLSGLDTIRQALVRQSDDFKGRPDLYSSTFISDGQSMIFNPDSGPVWAARRRLAQSALQSFSVASDPASVSSCYLEEHVSREAEHLVTKLLDLMAGPGCFEPSSQIVGSVANVIGAMCFGKNFPQTSEEMLQIVNTSKEFTEFASSGNPVDFFPILRYLPNPMLQQFKDFNKRFLQFLQKTVQEHYQDFDKNHVQDIASALFKHSEESPHVNGDLIPRKKIVNLVNDIFGAGFD... | A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cy... | Q64391 |
A5GN62 | AMPA_SYNPW | Leucyl aminopeptidase | unclassified Synechococcus | MKISLSPATPEAWSGSVLALGIPENDPQGLVAAMEQRFSLQLSDWLKQKPFSGKPGDCVSLPLLRSDCTALVLVGLGEASSVDRDRLRLAAAAAARAAQGQGGTLGLLLPWSSDTPEEDAAAAAEAVRLALYSDERFRSKPEPSPKPDQLELLGSLPGGLSHGLEAVHPVCAGVELARELVAAPPNSVTPAELARTASHLAHEHGLELTILERSDCEERGMGSFLSVCQGSDMDPKFIHLTYRPNDAASKRLVLVGKGLTFDSGGYNLKVGAAQIDMMKFDMGGSAAVFGAMRAIAELRPAGVEVHMLVASCENMINGSA... | Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. | A5GN62 |
A3CP56 | SYT_STRSV | Threonyl-tRNA synthetase | Streptococcus | MIKITFPDGAVREFESGVTTFEIAQSISNSLAKKALAGKFNGKLIDTTRAITEDGAIEIVTPDHEDALDILRHSAAHLFAQAARRLFPDIHLGVGPAIQDGFYYDTDNEAGQISNEDLPRIEEEMKKIVKENFPSIREEVTKDEAREIFKNDPYKLELIEEHSEDEGGLTIYRQSEYVDLCRGPHVPSTGRIQIFHLLNVAGAYWRGNSDNAMMQRVYGTAWFDKKDLKKYLQMREEAKERDHRKLGKELDLFMISQEVGQGLPFWLPNGATVRRELERYIVDKELASGYQHVYTPPLASVELYKTSGHWEHYQEDMFPT... | Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr). | A3CP56 |
Q8DBE8 | LPXB_VIBVU | Lipid-A-disaccharide synthase | Vibrio | MSNKPLRIGIVAGELSGDTLGEGFIKAIKAVHPDAEFVGIGGPKMIALGCQSLFDMEELAVMGLVEVLGRLPRLLKVKAELVRYFTENPPDVFVGIDAPDFNLRLELDLKNAGIKTVHYVSPSVWAWRQKRIFKIAKATHLVLAFLPFEKAFYDKFNVPCEFIGHTLADAIPLESDKAPARELLGLEQDKQWLAVLPGSRGSELKMLSQPFIETCKKLQQAFPELGFVVALVNQKRREQFEQAWKEYAPELDFKLVDDTARNVITASDAVMLASGTVALECMLLKRPMVVGYRVNAVTAFLAKRLLKTQYVSLPNILADT... | Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. | Q8DBE8 |
A2RAW3 | CLP1_ASPNC | mRNA cleavage and polyadenylation factor clp1 | Aspergillus subgen. Circumdati | MSLPGLDLTQPSADREFAPAPPSQISLPKGSEWRFEVAFGTTVRVKLLAGTAELFGTELAPSQTYTFSGTKAAIYTWHGCTLESEYVAEETPMVEYANVHFALETLRQEAKATGKDGPRVLILGPEDAGKTSLSKILTAYATKVGRQPLVVNLDPTEGMLSVPGTLTATAFRTMIDVEEGWGSSPMSGPSAVPVKLPLVYFYPMQNPLEADGSVYKAIVSRLALSVTGRMAEDEDARETGIIVDTPGILSQSKAGNVEMINHIVTEFAITTILVIGSERLYSIMMKNFDNKPTASASAAASDERISVVKLSKSGGCVDRD... | Required for endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation. | A2RAW3 |
Q7VJX1 | SSRP_HELHP | Small protein B | Helicobacter | MPIRVIAKNKKAYFDYEILQSLESGIVLQGSEVKSIRAGRVNLKDSFIKIIRGEAFLFNAHISFLQTTYTHFKPNERRERKLLLHKKEIDKLFGSVSKESLSIVPLNIYFNQKNKIKLCIALVRGKKLHDKRESIKKKMLEREARAHMKSYGKKL | Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemb... | Q7VJX1 |
A3GH78 | MPH1_PICST | FANCM-like protein 1 | Scheffersomyces | MPIDSDDNVFDDDDDFIELLQDSSNQTSNVTNEIATDSTNSTNTRLVVPNNRLLEEIPVPKRILLGPTHHKIDYGNLDKYVYPSNFEVRDYQFNIVQRAFYHNLLVALPTGLGKTFIASTVMLNFLRWFPESKMIFVAPTKPLVAQQIKACCSITGIPSSKVAILLDKTRKNRGEIWDEKQVFFTTPQVVENDLASGLVDPKTIALLVIDEAHRAKGNYAYNNIVKFMDRFTNSYRILALTATPASDVDGVQEIIDNLNISKVEVRSEESIDIIKYMKRKRIIRRNIYQSDEIKECIDLLCTAIAPVLKVANGKGILEIT... | ATP-dependent DNA helicase involved in DNA damage repair by homologous recombination and in genome maintenance. Capable of unwinding D-loops. Plays a role in limiting crossover recombinants during mitotic DNA double-strand break (DSB) repair. Component of a FANCM-MHF complex which promotes gene conversion at blocked re... | A3GH78 |
Q6CG56 | DHYS_YARLI | Deoxyhypusine synthase | Yarrowia | MSETPNLATEAVLVHSAPVPEDAVPVSGIDFDKPENKNTRAADLVGAMNGMGFQATSLGQACNIIDEMRTWEGVDKEGNPAKTTIFLGYTSNLISSGLRSTLKYLVKNKMVSAIVSSAGGIEEDLIKCLAETYLGDFALKGSVLRETGMNRIGNLLVPNDNYCKFEEWVVPILDTMLEEQEKQGVSWTPSTVIDRLGKEIDNEDSVLYWAHKNQIPVFCPALTDGSLGDMLFFHTFKASPLQLKIDIVADIRKINSMSMAATRAGMIILGGGLVKHHIANACLMRNGADYAVYINTGQEFDGSDAGARPDEAISWGKIKA... | Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue. | Q6CG56 |
Q6NHR6 | GLGB_CORDI | Glycogen branching enzyme | Corynebacterium | MVSPTQITPVHPDVLHALKICQYHDPHGVYGWHEVDAERAVIRTRHIGAERVETLLSDSTVVELAAVGDDIFEAIVDHDASCDYRLRIHWQGGQVTEQADAYHFLPTLGDLDLHLINEGRHERLWEVLGANPTTITTAMGDVEGTAFAVWAPNASGVAVIGDFCGWNPSQYPMRSLGSTGIWELFIPNIGVGTVYKFAIHTHEGHRLDKADPMAKRAEVAPATGSIIASSSYTWNDDTWMTNRAHTDHDNTAMSVYEVHLGSWSQGQNYEELATNLVDYVKEMGYTHVEFLPVAEHPFGGSWGYQVSGYYAPTSRWGTPD... | Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position. | Q6NHR6 |
P58749 | TM6S1_MOUSE | Transmembrane 6 superfamily member 1 | Mus | MSASAATGVFVLSLSAIPVTYIFNHLAAQHDSWTIVGVAALILLLVALLARVLVRRKPPRDPLFYVYAVFGFTSVVNLIIGLEQDGIIDGFMTHYLREGEPYLNTAYGHMICYWDGSVHYLMYLVMVAAIAWEESYRTIGLYWVGSIIMSIVVFVPGNIVGKYGTRICPAFFLSIPYTCLPVWAGFRIYNQPSENYNYPSKVLQEAQAKALLRRPFDLVLVLCLFLATGFCLFRGLIALDCPAELCRLYTQFQEPYLKDPAAYPKIQMLAYMFYSVPYFVIALYGLVVPGCSWMPDITLVHAGGLAQAQFSHIGASLHAR... | May function as sterol isomerase. | P58749 |
B4I9X1 | EI3G1_DROSE | Eukaryotic translation initiation factor 3 subunit 4-1 | Sophophora | MPGVETIKSSWADEVELDYGGLPPTTETVENGQKYVTEYKYNKDDKKTKVVRTYKISKQVVPKTVAKRRTWTKFGESKNDKPGPNSQTTMVSEEIFMQFLNSKEDEKANDPLLDPTKNIAKCRICNGEHWSVNCPYKGTAMDTNMMEKKASAAAAAAVDAPKSGKYVPPFLKDSQKGALGMRGRDDTAAIRISNLSESMTEADLEELVKKIGPQSKMYLARDKNTGLCKGFAYVHFKQRKDAAAAIEILNGHGYDHLILSVEWSKPQNN | RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and... | B4I9X1 |
Q3K0E8 | PYRR_STRA1 | Uracil phosphoribosyltransferase | Streptococcus | MKRKEIIDDVTMKRAITRITYEIIERNKNLDNIVLAGIKTRGVFLAKRIQERLKQLENLDIPVGELDTKPFRDDMKVEVDTTTMPVDITDKDIILIDDVLYTGRTIRAAIDNLVSLGRPSRVSLAVLIDRGHRELPIRADYVGKNIPTSQFEEILVEVMEHDGYDRVSIIDPS | Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant. | Q3K0E8 |
A3PAT7 | OBG_PROM0 | GTP-binding protein Obg | Prochlorococcus | MQFIDQANIILKAGKGGNGIVSFRREKFVPAGGPSGGNGGRGGSVILMADNNLQTLLDFKFKREIIAEDGCKGGPNKRSGASGQDTILKVPCGTEIRDIKTGIILGDLTKDKQSLTIAIGGRGGHGNAYYLSNQNRAPESFTEGKDGEIWEVQLELKLLAEVGIIGLPNAGKSTLISVVSSARPKIANYPFTTLIPNLGVVRKMDGNGCLFADIPGLISGAADGVGLGHDFLRHIQRTKILVHLIDAIAENPLHDFEIIEQELKKYGKGLLDKERIIVLNKMELVDDDYLQIITKKLEDLSKKKVLVISSSLKKGLSSLL... | An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control. | A3PAT7 |
P01461 | 3SA4_NAJHA | Toxin CM-11 | Naja | LKCNKLIPPFWKTCPKGKNLCYKMYMVSTLTVPVKRGCIDVCPKNSALVKYVCCNTNKCN | Shows cytolytic activity on many different cells by forming pore in lipid membranes. In vivo, increases heart rate or kills the animal by cardiac arrest. In addition, it binds to heparin with high affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a calcium-independent manner, and binds to integrin a... | P01461 |
Q82W26 | HISX_NITEU | Histidinol dehydrogenase | Nitrosomonas | MIKIRRLSSVDDHFQAELDQLLSFEVSVDSEIERTVTQILHQIRTHGDRALLELTRQFDNPDIDRIEEIELPRDEWQSALMSLDKVQREALEQAASRIRAYHEKQLAQSWDYVELDGTRLGQKITALDRVGLYVPGGKAAYPSSVLMNAIPARVAGVRELIMVTPTPKGEKNPLVLAAAAICEVDRVFTIGGAQAVAALAYGTTTVPKVDKIVGPGNAYVAAAKRHVFGTVGIDMLAGPSEILVICDGKTNPDWIAMDLFSQAEHDEQAQSILLCPDKAFLDRVADSISRLIDTLPRRDVIRSSLENRGALIHVRDLEEA... | Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. | Q82W26 |
Q3IZ13 | ATPL_CERS4 | Lipid-binding protein | Cereibacter | MEGDIAEMGKFIGAGLATIGLGGAGIGVGHVAGNFLAGALRNPSAAPGQMANLFVGIAFAEALGIFSFLIALLLMFAV | Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits. | Q3IZ13 |
A4SLX9 | RECR_AERS4 | Recombination protein RecR | Aeromonas | MKFSPLLDEMMKALQVLPGVGPKSAQRMAFTLLERERSGGLRLAQLLNRALTEIGHCSHCRTFTENALCEICANPKREESGLLCVVESPADVAAIEHTGQFSGRYFVLMGHLSPLDGIGPEELGLEILEQRLKAESISELILATNPTIEGDATAWYIADMARAAGVKVSRIAHGVPVGGELELVDGTTLSHSLMGRQPLN | May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO. | A4SLX9 |
D5VGV1 | RUTB_CAUST | Ureidoacrylate amidohydrolase RutB | Caulobacter | MSSPITPLSPGCVMLPARPEPVPVDPKTTAVIVIDMQNAYASPGGYLDLAGFDISGAAKVIHEIKGVLEVARSAGMQVIYFQNGWDDQYVEAGGPGSPNWWKSNALKTMRAKPELQGKLLARGQWDYELVDELKPQPGDIQLHKTRYSGFFNSQLDSVLRARGIRHLVFVGIATNVCVESTLRDGFFLEYFGTVLEDATHQAGPEFVQKAALFNIESFFGWVSTTADFKGTFGQLAPRT | Hydrolyzes ureidoacrylate to form aminoacrylate and carbamate. The carbamate hydrolyzes spontaneously, thereby releasing one of the nitrogen atoms of the pyrimidine ring as ammonia and one of its carbon atoms as CO2. | D5VGV1 |
Q2JL88 | MURC_SYNJB | UDP-N-acetylmuramoyl-L-alanine synthetase | unclassified Synechococcus | MPVPSQPLPLHLDPLDPLLSTYHFVGIGGVGMSALAYILAKQGFRVSGSDIVANGRTRRLEALGVRFFQGHSSEGLVGDPQVVYSSAIRPTNPELAAALGKGLTVWHRADLLAALFNRRSGIGVAGTHGKTTTSSMIGYVLLSAGWDPTLIIGGEVDAWDGNARLGKGEYWVAEVDESDGSLVRLYPKIGVITNIELDHPDHYADLGQVIRAFQQYGQQSQTLVACLDCPNVAAHLRVDVGYSLTGHPQAQYQARQILYTASFTCAEIWEKGSLLGQLRLQVLGSHNLSNALAAVAVGRQLGLEFAVIASALAQFRGAHR... | Cell wall formation. | Q2JL88 |
Q0I3R3 | ACKA_HAES1 | Acetokinase | Histophilus | MSQKLVLILNCGSSSLKFAILDPVSGAEKLSGLAEAFYLPDARIKWKLNGEKGNADLGAGAAHSEALNFIVSTILTEDLKNSIAAIGHRVVHGGEKYTKSVVITDEVIQGIKDAAEFAPLHNPAHLIGIEEAFKAFPHLKDNNVAIFDTAFHQTMPEEAFLYALPYSLYKEHGVRRYGMHGTSHYFVSREAAKRLNIAEDKINVITCHLGNGASVAAIRQGKCIDTSMGFTPLEGLVMGTRSGDLDPAIIFYMHNTLGMSVAQIEETLVKKSGLLGLTEVTSDCRYSEDNYEKESAAKRALDVFCYRLAKYIGSYMAIIG... | Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction. | Q0I3R3 |
P17305 | STP1_BOVIN | Spermatid nuclear transition protein 1 | Bos | MSTSRKLKSQGMRRGKNRTPHKGVKRSGSKRKYRKSSLKSRKRCDDANRNLRSHL | Plays a key role in the replacement of histones to protamine in the elongating spermatids of mammals. In condensing spermatids, loaded onto the nucleosomes, where it promotes the recruitment and processing of protamines, which are responsible for histone eviction. | P17305 |
A7M916 | PETG_CUSGR | Cytochrome b6-f complex subunit V | Cuscuta sect. Oxycarpae | MIEAFLLGIILGLIPITLIGLFVTAYLQYRRGDQLDF | Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetG is required for either the stability or assembly of the cytochrome b6-f complex. | A7M916 |
A7I058 | SYDND_CAMHC | Non-discriminating aspartyl-tRNA synthetase | Campylobacter | MRSNYCTELDSGDIGKIVDVCGWVNSYRDHGGVIFIDLRDRSGLIQLVCDPKHSQEAYTIANSVRDEFVLRAHGKIRARGKDLINPKLKTGEIEVVVENLIVENPSKPLPFVIGDKNVSEETRLKYRFLDLRTNENFNKFFTRSKAAIAARNALDRLGFVEVETPILTRATPEGARDYLVPSRVYNGQFYALPQSPQLFKQLLMCSCFDKYFQIARCFRDEDLRADRQPEFTQIDIEMSFCDQKDVMKVGEAVLKDIFKSCGKDIKTPFRVMQYKDAMENYGSDKPDLRFGMKFIDVADIFEKSSNEIFANIAKDKKKNR... | Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn). | A7I058 |
Q3JD12 | GLGA2_NITOC | Starch [bacterial glycogen] synthase 2 | Nitrosococcus | MYKILFATSEAHPLIKTGGLGDVAGILPIELARLGLEAGIILPAYPACKTHLKNLKEVARLRLPAALEPVRILKGQLLEGPNPVWLVDSPAHFDRPGNPYLNEQGQDWPDNAARFTTFCRAVATLANSPEFDWQPDLIHCNDWQTGLIPPFLAPLRSRPATLFTIHNLAYQGVFSRQQFDALELPSAWWSPAALEFYNQISFIKGGLVFADWLTTVSPTYAKEILTPEFGCGLDGVLRGRSKRLTGILNGADYQRWDPRHDPFIEKRYDQTCWSHKASNKLALQRRYGLPEDDTLPVLGFVGRLVEQKGIDLILGALPKL... | Synthesizes alpha-1,4-glucan chains using ADP-glucose. | Q3JD12 |
Q8FMT9 | CLPS_COREF | ATP-dependent Clp protease adapter protein ClpS | Corynebacterium | MCSSPSAPTAEPDVEMDVHTVSSENLPWLCIVWDDPVNLMSYVTYVFQTVLGYSRKRANELMMQVHTEGKAVVSSGEKDKVEGDVKKLHVAGLWATMQQAG | Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation. | Q8FMT9 |
A5V8U1 | PYRG_RHIWR | UTP--ammonia ligase | Rhizorhabdus | MARFIFITGGVVSSLGKGLMAASLAALLQARGYKVRIRKFDPYLNVDPGTMSPYQHGEVYVTDDGAETDLDLGHYERFTGVPGRQSDNITSGRIYQTIIQKERRGDYLGATVQVIPHVTDAIKEFARADTEGLDFVLCEIGGTVGDIESLPFMEAIRQLRNDLGRGNSIFVHLTLVPYIAAAGELKTKPTQHSVRDLTSLGIQPDVLVCRCDRPLPEGERAKIALFCNVPTEAVIPALDASSIYGVPLQYHEEGLDEAVLSAFGIEAKDEPDLTRWTEIMDRLENPEGEVTIGVVGKYVGLLDAYKSLHEALVHGGIANR... | Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. | A5V8U1 |
A1WX12 | FABZ_HALHL | Beta-hydroxyacyl-ACP dehydratase | Halorhodospira | MSERDAQGATDIEGIMNLLPHRYPLLLIDRVLDFQPHEHLASIKNVTINEPFFVGHFPQKPVMPGVLILESLAQACGMLAFKSVQDTLTDNDVLYLVGIDKARFKRPVQPGDQLRHDVSVRRVTRGIWIFEARGSVDGELAAECEIRCTVRTV | Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs. | A1WX12 |
Q58605 | METK_METJA | Methionine adenosyltransferase | Methanocaldococcus | MRNIIVKKLDVEPIEERPTEIVERKGLGHPDSICDGIAESVSRALCKMYMEKFGTILHHNTDQVELVGGHAYPKFGGGVMVSPIYILLSGRATMEILDKEKNEVIKLPVGTTAVKAAKEYLKKVLRNVDVDKDVIIDCRIGQGSMDLVDVFERQKNEVPLANDTSFGVGYAPLSTTERLVLETERFLNSDELKNEIPAVGEDIKVMGLREGKKITLTIAMAVVDRYVKNIEEYKEVIEKVRKKVEDLAKKIADGYEVEIHINTADDYERESVYLTVTGTSAEMGDDGSVGRGNRVNGLITPFRPMSMEAASGKNPVNHVG... | Catalyzes the formation of S-adenosylmethionine from methionine and ATP. | Q58605 |
Q9Z8I4 | LEPA_CHLPN | Ribosomal back-translocase LepA | Chlamydia | MKEYKIENIRNFSIIAHIDHGKSTIADRLLESTSTVEEREMREQLLDSMDLERERGITIKAHPVTMTYLYEGEVYQLNLIDTPGHVDFSYEVSRSLSACEGALLIVDAAQGVQAQSLANVYLALERDLEIIPVLNKIDLPAADPVRIAQQIEDYIGLDTTNIIACSAKTGQGIPAILKAIIDLVPPPKAPAETELKALVFDSHYDPYVGIMVYVRIISGELKKGDRITFMAAKGSSFEVLGIGAFLPKATFIEGSLRPGQVGFFIANLKKVKDVKIGDTVTKTKHPAKTPLEGFKEINPVVFAGIYPIDSSDFDTLKDAL... | Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-t... | Q9Z8I4 |
A6TF99 | ARNC_KLEP7 | Undecaprenyl-phosphate Ara4FN transferase | Klebsiella | MLTYPPVKKVSVVIPVYNEQDSLPELLRRTDAACATLGRQYEILLIDDGSSDDSARMLTEAAEAEGSHVVAVLLNRNYGQHSAIMAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQDSIFRKTASKMINRLIQRTTGKAMGDYGCMLRAYRRHIIDAMLNCHERSTFIPILANTFARRAVEIPVMHAEREFGDSKYSFMRLINLMYDLVTCLTTTPLRLLSIFGSVIALLGFAFGLLLVVLRLAFGPQWAAEGVFMLFAVLFMFIGAQFVGMGLLGEYIGRIYNDVRARPRYFIQRVVRQPETA... | Catalyzes the transfer of 4-deoxy-4-formamido-L-arabinose from UDP to undecaprenyl phosphate. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. | A6TF99 |
A5GHN9 | MURC_SYNPW | UDP-N-acetylmuramoyl-L-alanine synthetase | unclassified Synechococcus | MRSLVCTLDIQSPVHFIGAGGIGMSALARILLSRGHRVSGSDRRLSPAMESLKTAGMVAFESQAAANFQALDRLDRSSPIVVISSAIPDHNPELVAARERQLEVWHRSDLLAALIDQQPSIAIAGSHGKTTTSTVVTTLLHGAGEDPTAVIGGIVPCYDSNGHAGQGRLLVAEADESDGSLVKFRASLGVITNLELDHTDHYRDLDDLIATLQRFGDGCKRLLANQDDPILSEHFQADAWWSVQRSDNVDFAGLPVALEGDRTIADLYEQGTFVGQITLPMPGLHNLSNTIGALAACRMEGVPLEHLISHLSELKTPGRR... | Cell wall formation. | A5GHN9 |
P26772 | CH10_RAT | Chaperonin 10 | Rattus | MAGQAFRKFLPLFDRVLVERSAAETVTKGGIMLPEKSQGKVLQATVVAVGSGGKGKGGEIQPVSVKVGDKVLLPEYGGTKVVLDDKDYFLFRDGDILGKYVD | Co-chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp60, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matri... | P26772 |
Q8SXL2 | CCHA2_DROME | Neuropeptide CCHamide-2 | Sophophora | MKSTISLLLVVICTVVLAAQQSQAKKGCQAYGHVCYGGHGKRSLSPGSGSGTGVGGGMGEAASGGQEPDYVRPNGLLPMMAPNEQVPLEGDFNDYPARQVLYKIMKSWFNRPRRPASRLGELDYPLANSAELNGVN | Ligand for the CCHamide-2 receptor CCHa2-R . In one study, shown to be an orexigenic peptide which induces appetite and stimulates food intake, leading to the release of insulin-like peptides which stimulate growth . In another study, shown to be a nutrient-sensitive peptide derived from peripheral tissues which contro... | Q8SXL2 |
A5IJR7 | CH10_THEP1 | Chaperonin-10 | Thermotoga | MMKVIPLGERLLIKPIKEEKKTEGGIVLPDSAKEKPMKAEVVAVGKIDDEEKFDIKVGDKVIYSKYAGTEIKIDDEDYIIIDVNDILAKIEE | Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of ... | A5IJR7 |
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