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 |
|---|---|---|---|---|---|---|
Q5NGR3 | SECA_FRATT | Protein translocase subunit SecA | Francisella | MLSLVQKIIGSRNERFIKKVSRIVQKINSLEPEFEKLSDEQLKAKTFEYRERLANGEILDNLLPEAFATVREAGKRTKNMRHYDVQLIGGIVLHQGKVAEMRTGEGKTLVATLPAYLNALTGDGVHVITVNDYLAKRDAELMSDIYEFLGMSVGVIVADLNPQQRKEAYACDITYGTNNEFGFDYLRDNMAYEKEQQVQRSRNYVIIDEVDSILIDEARTPLIISGASDDRSEMYNLFNRLVPYLEKQEKEEVENEQEQRDFYVDEKSKNAYLTEKGYAKIENMLKKEGILEEDDNLYSPHNITKMHYLNACLRAHSLYQ... | Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor drivin... | Q5NGR3 |
P56070 | PPSA_HELPY | Pyruvate, water dikinase | Helicobacter | MRYIKFFKELNNKNVNLVGGKNASIGEMFQELVPIGIKVPDGFAITSEAYWYLLEQGGAKQKIIELLENVDATEIDVLKIRSKQIRELIFGTPFPSDLRDEIFQAYEILSQQYHMKEADVAVRSSATAEDLPDASFAGQQDTYLNIKGKTELIHYIKSCLASLFTDRAISYRASRGFDHLKVALSVGVQKMVRADKGSAGVMFSIDTETGFKDAVFITSAWGLGENVVGGTINPDEFYVFKPTLEQNKRPIIKRQLGNKTQKMVYAPRGSEHPTRNIKTTKKEWQSFSLSDEDVLILAKYAIEIEKHYSKEAKQYRPMDI... | Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate. | P56070 |
P82826 | BR1LB_RANLU | Brevinin-1Lb | Rana | FLPMLAGLAASMVPKFVCLITKKC | Antibacterial activity against Gram-positive bacterium S.aureus and Gram-negative bacterium E.coli. | P82826 |
Q4K9U7 | CLPS_PSEF5 | ATP-dependent Clp protease adapter protein ClpS | Pseudomonas | MHAISQIRLTFNQDRPDLHDDDSAGLAVQEAKPALQAPPMYKVVLFNDDYTPMDFVVEVLEMFFNLNRELATKVMLAVHTEGRAVCGLFTRDIAETKAMQVNQYARESQHPLLCEIEKDG | Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation. | Q4K9U7 |
B2II88 | NDK_BEII9 | Nucleoside-2-P kinase | Beijerinckia | MAIERTFSILKPDVTRRNLTGAVNALIEKAGLRIIAQKRVLITKAQAETFYAVHSARPFFGELVESMISGPVVVQVLEGEDAIKKYREVLGATDPAKADAGTIRKEFALSVGENSAHGSDAPETAAVEIAQWFAGNELVG | Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. | B2II88 |
Q9RUN0 | UVRC_DEIRA | Excinuclease ABC subunit C | Deinococcus | MHFDDLPVLPTTPGVYIFRKGGVPIYIGKANNLRSRVSQHFKAGGKSGKFTKLAESLEFISAANEVEALVLEANLIKQHRPHYNVLLKDDKHYPFLKLTNEAYPMLVVTRRVLKDGANYYGPYPDASAVRRVKHLIDTMFPLRKNSGLPMQKKPRPCLNYHMGRCLGPCIDAAQPDEYRQAVEDVKALLEGRAAPVIARLKEDMKVAAQGQDFEQAARLRDRVQAVEKLFGTEQHAFVSEETDLDFLGAAQAGEFAMVQLFRMRGGRVVGRDKRFLTGADETGLGEIIGAFVADYYTQATHVPPLILLPAEYEDAALWSE... | 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. | Q9RUN0 |
B1XM11 | MNMA_SYNP2 | tRNA-specific 2-thiouridylase MnmA | unclassified Synechococcus | MGKVAVGLSGGVDSSVTAGILHRQGYTVEGVTLWLMKGKGQCCSEGMVDAADICEQLGIPHHIVDSRDLFQKYIVDYVVSGYEVGVTPLPCSQCNRMVKFGPMLQWAKAELGIDQIATGHYARIRYNDQTGRYELLRAVDRHKDQSYFLYDLTQEMLAGTLFPLGEMTKGETRQIAAEMQLSTAKKPESQDLCLIEAHGSMKTFLDKYIEQREGEIVDLDGKVLGHHTGIHHYTIGQRKGLGIAAPEPLYVVKLDNVMNRVVVSTRDRAGQSECTVQRMNWLALPGITSPIRAEVQVRYRSGAVPVTVIPLEGDRLKLVF... | Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. | B1XM11 |
Q1CBG7 | METE_YERPA | Methionine synthase, vitamin-B12 independent isozyme | Yersinia | MTILNHTLGFPRVGLKRELKKAQESYWAGNSTQEELLNVGRELRARHWQQQQQAGVDLVPVGDFAWYDHVLTTSLLLGNVPERHQNADGSIDIDTLFRIGRGRAPTGKPAAAAEMTKWFNTNYHYMVPEFQQGQQFKLGWTQLLDEVDEALALGHKIKPVLLGPITYLWLGKVKGEQFDRLSLLNDILPVYQQVLAELAKRGIEWVQIDEPALVLELPQEWLDAYQPAYQALQGQVKLLLTTYFDSIGHNIDTIRALPVQGLHVDVVTGHDDLAVLNKNLPKEWLLSLGVINGRNVWRADLSSWFERLQPLVNSRPLWLG... | Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation. | Q1CBG7 |
Q8KX40 | NU3C_SYNP2 | NDH-1 subunit 3 | unclassified Synechococcus | MFVLSGYEYFLGFLIVSSLVPILALTASKLLRPKGGGPERKTTYESGMEPIGGAWIQFNIRYYMFALVFVVFDVETVFLYPWAVAFNQLGLLAFVEALIFIAILVIALVYAWRKGALEWS | NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus co... | Q8KX40 |
Q6IRC7 | UBE2F_XENLA | Ubiquitin-conjugating enzyme E2 F | Xenopus | MLTLASKLKRDDGVKGSRTTSTTLDSMRRISVRDRLLVKEVAELEANLPCTCKVNFPDPNKLHYFHLTVSPDESYYQGGRFQFEIEVPDAYNMVPPKVKCLTRIWHPNITETGEICLSLLREHSIDGTGWAPTRTLKDVVWGLNSLFTDLLNFDDPLNIEAAEHHLRDKDEYRNKVEDYIKRYAR | Accepts the ubiquitin-like protein NEDD8 from the uba3-nae1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase rbx2, but not rbx1, suggests that the rbx2-ube2f complex neddylates specific target proteins, such as cul5. | Q6IRC7 |
A9MJM8 | END8_SALAR | Endonuclease VIII | Salmonella | MPEGPEIRRAADHLEAAIKGKLLTDVWFAFAQLKPYESQLTGQMVTRIETRGKALLTHFSNGLTLYSHNQLYGVWRVIDTGEIPHTTRILRVRLQTADKTILLYSASDIEMLTAEQLTTHPFLQRVGPDVLDARLTPEEVKARLLSPRFRNRQFSGLLLDQAFLAGLGNYLRVEILWQSELTGQHKAKDLSEAQLNTLSHALLDIPRLSYATRGQTDENKHHGAQFRFKVFHRDGEACERCGGIIEKTTLSSRPFYWCPHCQK | Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, 5,6-dihydrouracil and 5,6-dihydrothymine. Has AP (apurinic/apyrimidinic) lyase activity and introduce... | A9MJM8 |
Q59596 | KAD_NEIFL | Adenylate monophosphate kinase | Neisseria | FITAAFGIPQISTGDMLRAAIKAGTPLGLEAKKIIDEGGLVRDDIIIGMVKERIAQDDCKNGFLFDGFPRTLAQAEAIVEAGVDLDAVVEIDVPDSVIVDRMSGRRVHLASGRTYHVTYNPPKVEGKDDVTGEDLIQRDDDKEETVKKRLAVYHEQTEVLVDFYSKLEGEHAPK | Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. | Q59596 |
B1HPJ4 | RLMH_LYSSC | rRNA (pseudouridine-N3-)-methyltransferase RlmH | Lysinibacillus | MNITIVSVGKLKEKYLKMGIDEYVKRLGGYAKIDLIEVADEKAPEQLSDAEMEIVKKKEGERILAKISTDTYVIALAINGKMKTSEQMAADLESLMTYGKSKIAFVIGGSLGLHEDVLKRADEQQSFGKMTLPHQLMKLVLVEQVYRSFRIMKGEPYHK | Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA. | B1HPJ4 |
A3MTL3 | RS3_PYRCJ | 30S ribosomal protein S3 | Pyrobaculum | MSTAQRRLPVYKKILEENKKKWMIKEFLEYRLAKYGYIDSEILKTPLGTRIVIYAERPSRIIGRKGAIVKEVSSILANKLGVENPQIDVIDVSKIEAPELFPKVVAYRIANAMARGVRFRRVMFVAVRQLMEAGAKGFEIVVSGKLSTERAKFEKITYGKLYKIGYDAKNRVRRAVVHVLLKPGIYGIEVRITPATLRYSDEYKIKPPTRPEAAAQ | Binds the lower part of the 30S subunit head. | A3MTL3 |
A9R2S1 | AAS_YERPG | Long-chain-fatty-acid--[acyl-carrier-protein] ligase | Yersinia | MAYRLLRALFRGLFRVTIDGVTDQFKHEKLIITPNHVSFLDGALLALFLPIKPVFAVYTSITDTWYMRWLKPYVDFVALDPTNPMAIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDGPEFTHFGRLQGVLKTRWFPKISIHVLPATTIPMPQAPRSRERRVLAGEHLHTIMMAARMATVPRETLFEALLSAQTRYGRFKPCIEDVSFKEDSYQTLLKKTLGVSRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKLTH... | Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactio... | A9R2S1 |
O74347 | COXM1_SCHPO | Cx9C motif-containing protein 1 | Schizosaccharomyces | MHPHLDVNNQKQCADLIRALEECHKSFGKFFGECNTIKYELKACLTKDRNDKARLNRENARMRKKVIEENRKKEEIEERILTDRILQQERKKSHANEGAGDNNN | Required for mitochondrial cytochrome c oxidase (COX) assembly and respiration. | O74347 |
Q65L04 | UXUA1_BACLD | D-mannonate hydro-lyase 1 | Bacillus | MKMVFRWYGEGNDSVTLEQIRQIPGVEGIVWALHHQPPGEEWPLEEILEVKRQCEQHGFHIEVVESVNIHEDIKLGLPTRDLYIEKYKRTIENLAKAGVKVICYNFMPVFDWLRTDLYKKAPDGSTALFYEHAKVHTIDPFALVDQIAKHPEFTMPGWEPERLEHLTRLFEAYQNVTEEDLWSHLHYFLERIIPTAARCGIKMAIHPDDPPWPVFGLPRIMTSGESIGRLLQLVDHPANGVTLCSGSLGANPENDISAMIHAYADRIPFAHIRNVKVYENGDFIETSHRTKDGTVDICGIVKAYHETGFSGYVRPDHGRH... | Catalyzes the dehydration of D-mannonate. | Q65L04 |
Q5T7W0 | ZN618_HUMAN | Zinc finger protein 618 | Homo | MNQPGGAAAPQADGASAAGRKSTASRERLKRSQKSTKVEGPEPVPAEASLSAEQGTMTEVKVKTELPDDYIQEVIWQGEAKEEKKAVSKDGTSDVPAEICVVIGGVRNQQTLDGKAPEGSPHGGSVRSRYSGTWIFDQALRYASGSYECGICGKKYKYYNCFQTHVRAHRDTEATSGEGASQSNNFRYTCDICGKKYKYYSCFQEHRDLHAVDVFSVEGAPENRADPFDQGVVATDEVKEEPPEPFQKIGPKTGNYTCEFCGKQYKYYTPYQEHVALHAPISTAPGWEPPDDPDTGSECSHPEVSPSPRFVAAKTQTNQS... | Regulates UHRF2 function as a specific 5-hydroxymethylcytosine (5hmC) reader by regulating its chromatin localization. | Q5T7W0 |
Q8K9Z3 | LSPA_BUCAP | Signal peptidase II | Buchnera | MKRKYYWIYINIIFFIITVDFYSKKWILNHLNIYEKQKVFFILNLFHVHNFGAAFSILSDQNGWQKYFLLIFSIIIILAIIKIMIKFKKKDKNKILSYSLILAGAIGNLIDRINYGFVIDFIDLHFKSWHFATFNIADFSIFIGMIMIIKKNYYNS | This protein specifically catalyzes the removal of signal peptides from prolipoproteins. | Q8K9Z3 |
Q8XZI7 | ISPT_RALSO | Isoprenyl transferase | Ralstonia | MHISSTLAVPDTADTPHHVAIIMDGNGRWATERHLPRMAGHSRGLDAVRAAVQAADHRGVRYLTLFAFSSENWRRPAEEISFLMKLFMTALRREVSKLNDSGIRLRVVGDLSAFSPRIQLMIREAEAKTATNPGLTVTIAANYGGRWDILQAMRALVADQPDIAPEAITEEALSPYMALAYASEPDLFIRTGGEQRISNFMLWQLAYSELYFTERYWPDFDAAEMDRAFAWYRNRERRFGRTSAQLEPGTAPALSAGA | Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids. | Q8XZI7 |
Q2RQV9 | RS10_RHORT | 30S ribosomal protein S10 | Rhodospirillum | MESQNIRIRLKAFDHRVLDQSTREIVSTAKRTGAQVRGPIPLPTRIEKFTVNRSPHIDKKSREQFEIRTHKRLLDIVDPTPQTVDALMKLDLAAGVDVEIKL | Involved in the binding of tRNA to the ribosomes. | Q2RQV9 |
Q74GY3 | ATPD_GEOSL | F-type ATPase subunit delta | Geobacter | MISNAIARRYAKALVQLGAEEGAVDRFGVELGQFTALLDGNADLASVLKSPAYRIEAKREILRDVLAKLNLSGTVSNFLQVLLDRGRIGFTPQIAHSYAVFADELSGIVRPVLTSAFPLDDAQVEGMKSALAKATGKRVELSAQVDSALIGGVVTKIGDKVFDGSVRTQLNRIQDILQKG | This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. | Q74GY3 |
O75023 | LIRB5_HUMAN | Leukocyte immunoglobulin-like receptor 8 | Homo | MTLTLSVLICLGLSVGPRTCVQAGTLPKPTLWAEPASVIARGKPVTLWCQGPLETEEYRLDKEGLPWARKRQNPLEPGAKAKFHIPSTVYDSAGRYRCYYETPAGWSEPSDPLELVATGFYAEPTLLALPSPVVASGGNVTLQCDTLDGLLTFVLVEEEQKLPRTLYSQKLPKGPSQALFPVGPVTPSCRWRFRCYYYYRKNPQVWSNPSDLLEILVPGVSRKPSLLIPQGSVVARGGSLTLQCRSDVGYDIFVLYKEGEHDLVQGSGQQPQAGLSQANFTLGPVSRSHGGQYRCYGAHNLSPRWSAPSDPLDILIAGLI... | May act as receptor for class I MHC antigens. | O75023 |
A6TXE5 | MNME_ALKMQ | tRNA modification GTPase MnmE | Alkaliphilus | MFLDDTIAAIATAHGEAGIGIVRISGEKALHIIDQVFQSKQGKKLKDISPRRITYGHIIDTERNERIDEVLVSYMKGPHTYTTEDVVEINCHGGMIPVKRILELILRKGARAADAGEFTKRAFLNGRIDLAQAEAVMDLVSAKTDMGFDVALNQLEGSLSKRVKKVKDELLDMLAHIEVSIDFSDEDVDEVTLDLLLKQSMEIEKKIKVLLETADTGKILREGLNTVIVGKPNVGKSSLLNALLKESRAIVTEVPGTTRDAIEEHFNIRGIPLNLIDTAGIRETEDIVEKIGVERSKAFFNKADLIILMLDASRELTPED... | Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34. | A6TXE5 |
Q63P06 | RBSA_BURPS | Ribose import ATP-binding protein RbsA | pseudomallei group | MQRSDPPRPLLEMRGISKTFPAVRALAGVSLTVHPGEVHSLMGENGAGKSTLMKILSGAYQADPGGEILIDGRPISIDGPLAARDAGVAVIYQELCLAPNLSVAENIHVGRELRRGNGRRGTIDRAAMARGCQDVLERLGADFGPNTLVGTLSIAEQQLVEIARAVHTRARILVMDEPTTPLSSRETDNLFRLIRQLRAEGLAIIYISHRMAEIYELSDRVSVLRDGAYVGTLERDALSAERLVGMMVGRDISGFYKKAHAPYDPGNLLLSVRDIADGARVRGCSLDLHAGEVLGIAGLVGAGRTELARLIFGAEPRVRG... | Part of the ABC transporter complex RbsABC involved in ribose import. Responsible for energy coupling to the transport system. | Q63P06 |
Q6YRB0 | RL31_ONYPE | 50S ribosomal protein L31 | Candidatus Phytoplasma asteris | MKANIHPQFETVEVSCATCGKQHPIGTTVTSIKIETCSNCHPFYTGAQTFVVKAGPVDKFNKRYGITQDQKVKTVSSNADNQKETTEELIKNK | Binds the 23S rRNA. | Q6YRB0 |
P49144 | 5HT1B_RABIT | Serotonin receptor 1B | Oryctolagus | MEEPGAQCAPPLAAGSQIAVPQANLSAAHSHNCSAEGYIYQDSIALPWKVLLVLLLALFTLATTLSNAFVVATVYRTRKLHTPANYLIASLAVTDLLVSILVMPISTMYTVTGRWTLGQVVCDLWLSSDITCCTASIMHLCVIALDRYWAITDAVEYSAKRTPKRAAIMIRLVWVFSICISLPPFFWRQAKAEEEVSECLVNTDHVLYTVYSTVGAFYLPTLLLIALYGRIYVEARSRILKQTPNRTGKRLTRAQLITDSPGSTTSVTSINSRAPDVPSESGSPVYVNQVKVRVSDALLEKKKLMAARERKATKTLGIIL... | G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, su... | P49144 |
P94210 | DHLO_AGRVI | Octopine synthase | Agrobacterium | MAKVAILGAGNLALTLAGDLARRLGQTPSIWAPISNRSSFNDVRCLGSLELVGPDYGGDFQPRLEDDLGTAISGAAFIFLTVPTLGQQGILRELAKFNLSNSVLVALPGSATSLACKQTLVPTFAPIAVIESTTSPYACRRVKARVLMLGVKATFEVATTQPLSEEVKGRFEVLFPNPPQWYQHPASIFFSNTNPVAHPAGILAARDSIEQGILPVPKFYRQFVPQAITRVIAIDEERLSIVDALGLESETDFSYSKKWYGGHACNAREFYETYEGYAEIETPKTMNHRYLTEDVKHILVLWVEIAEAIGVQVPEMKSVV... | Reductive condensation of pyruvate and arginine, lysine, histidine, or octopine to form octopine, lysopine, histopine, or octopinic acid, respectively. NADPH is the preferred cofactor, but NADH can also be used. | P94210 |
B7UVR5 | PHNX_PSEA8 | Phosphonoacetaldehyde phosphonohydrolase | Pseudomonas | MNYNQPATLQAAILDWAGTVVDFGSFAPTQIFVEAFAEFGVQVSLEEARGPMGMGKWDHIRTLCDIPAIAERYRAVFGRLPSDDDVTAIYERFMPLQIEKIAEHSAVIPGALQAIAELRGMGLKIGSCSGYPAVVMEKVVALAETNGYVADHVVATDEVPNGRPWPAQALANVIALGIDDVAACVKVDDTWPGILEGRRAGMWTVALTCSGNALGLTYEQYKALPAAELERERTRIEQMFEGSRPHYLIETIAELPAVVRDINARLARGEMPQGN | Involved in phosphonate degradation. | B7UVR5 |
Q6NAR1 | TOLB_RHOPA | Tol-Pal system protein TolB | Rhodopseudomonas | MSFDLNRRQLMISAATAAGALALGPARDAFGQARVQITEGNVAPLPIAIPNFVAGTPSDAEVGTGVSQVITNNLKRSGLFAPIDQAAYLEKITNIDVPPQFKSWASINAQALVTGRMTRQGDGRLKAEFRLWDVATGQQLAGQQYFTSPEYWRRIAHIISDQIYERLTGEKGYFDSRVVFIDESGPADRRVKRLALMDQDGANVRYLTRGSDLVLTPRFSPTNQEITYMEFGQGEPRVYLFNVETGQREIVGNFPGMSFAPRFSPDGQRIIMSLQQGGNSNLFVMDLRSKATTRLTDTPAIDTSPSYAPDGSRICFESDR... | Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. | Q6NAR1 |
B7HIP0 | ILVD_BACC4 | Dihydroxy-acid dehydratase | Bacillus cereus group | MRSDMIKKGFDKAPHRSLLKATGLKDEDFDKPFIAICNSFIEIIPGHKHLNEFGKLVKEAVRAAGMVPFEFNTIGVDDGIAMGHIGMRYSLPSREIIADSVETVVNAHWFDGMICIPNCDKITPGMMMAALRINIPTVFVSGGPMAAGKTSKGEVVDLSSVFEGVGAYQSGKISEEELKDIEDHGCPSCGSCSGMFTANSMNCLCEVLGLALPGNGSILAIDPRREELIKQAAEKLKILIERDIKPRDIVTEEAIDDAFALDMAMGGSTNTVLHTLALAQEAGLDYDMNRIDAVSRRVPHLCKVSPASNWHMEDIDRAGG... | Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (... | B7HIP0 |
C0Q4L6 | CAIT_SALPC | L-carnitine/gamma-butyrobetaine antiporter | Salmonella | MKNEKKKSGIEPKVFFPPLIIVGILCWLTVRDLDAANVVINAVFSYVTNVWGWAFEWYMVVMLFGWFWLVFGPYAKKRLGDEKPEFSTASWIFMMFASCTSAAVLFWGSIEIYYYISTPPFGLEPNSTGAKEIGLAYSLFHWGPLPWATYSFLSVAFAYFFFVRKMDVIRPSSTLVPLVGEKHAKGLFGTIVDNFYLVALIFAMGTSLGLATPLVTECMQWLFGIPHTLQLDAIIITCWIILNAICVACGLQKGVRIASDVRSYLSFLMLGWVFIVSGASFIMNYFTDSVGMLLMHLPRMLFYTDAIGKGGFPQGWTVFY... | Catalyzes the exchange of L-carnitine for gamma-butyrobetaine. | C0Q4L6 |
Q9Z2T1 | KCNK7_MOUSE | Putative potassium channel DP3 | Mus | MGSLKPWARYLLLLMAHLLAMGLGAVVLQALEGPPARHLQAQVQAELASFQAEHRACLPPEALEELLGAVLRAQAHGVSSLGNSSETSNWDLPSALLFTASILTTTGYGHMAPLSSGGKAFCVVYAALGLPASLALVAALRHCLLPVFSRPGDWVAIRWQLAPAQAALLQAAGLGLLVACVFMLLPALVLWGVQGDCSLLEAIYFCFGSLSTIGLGDLLPAHGRGLHPAIYHLGQFALLGYLLLGLLAMLLAVETFSELPQVRAMVKFFGPSGSRTDEDQDGILGQDELALSTVLPDAPVLGPTTPA | Probable potassium channel subunit. No channel activity observed in vitro as protein remains in the endoplasmic reticulum. May need to associate with an as yet unknown partner in order to reach the plasma membrane. | Q9Z2T1 |
Q6A8H3 | METK_CUTAK | Methionine adenosyltransferase | Cutibacterium | MPTRLFTSESVTEGHPDKIADAISDAVLDAMLTEDSHSHAAVETVVTTGQVMVCGEVTTEAYVDIADIARSRILDIGYDSSSKGFDGASCGVSVAIDAQSPDIAQGVTAAYETRHGSTDLIDSQGAGDQGLMFGYACTETPSLMPLPIDMAHALSLQLTKVRKEGALDYLCPDGKTQVTIRYNEDDKPVAVDTVIVSSQHRAGIDLDATMTPDLRRLVIDPVLERYDLDHKDMRVLVNPTGKFVIGGPMGDAGLTGRKIIVDTYGGMARHGGGAFSGKDPSKVDRSGAYAMRWVAKNVVAAGLADRCECQVAYAIGAARP... | Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. | Q6A8H3 |
Q9APC2 | NIFJ_NOSSO | Pyruvate-flavodoxin oxidoreductase | Nostoc | IDGNEAVAQVVYQINEVIAIYPITPSSPMAEWADAWASEGKPNIWGTVPTVVQMQSEGGVAGAVHGALQTGSLTTTFTASQGLLLMIPNMYKIAGELTPTVFHIAARSLAAQALSIFGDHSDVMATRGTGFAMLCAASVQEAHDFALISTRTTLESRIPFLHFFDGFRTSHEINKIELLTTENLQTFIPNELVIAHRSRAFTPDNSFTRGTGQNPDVYFQGEEGTVIYYIACQASLKSMDEFAQMTGRQYQLFEYHGDSTAERVIVLMGSGCETVHETVDYLNTLGEKVGVIKVRLYHPFDSQRFIAALPPTTRSIAVLD... | Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin, which reduces nitrogenase. | Q9APC2 |
Q5BKL9 | CAB45_XENTR | Stromal cell-derived factor 4 | Silurana | MVSKQAFLFSLGSLYLSLLFVFLLMDVYARPANNSALKVEGKEKATDNKDENEIMPPDHLNGVKMEMDGHLNKEFHQEVFLGKEIEEFDEDSEPRRNRRKLAAIFAKVDRNEDKQISANEMQRWIMEKTEEHFQEAVNENKLHFRAVDPDGDGHVSWDEYKIKFLASKGFNEKEVAEKLKNNEDLKIDEETQEVLDNLKDRWFQADNPPADQLLNEEEFLSFLHPEHSQGMLKFMVKEIIRDLDQDGDKKLTLSEFISLPVGTVENQQAQDIDDDWVRDRKKEYEEVIDANHDGIVTMEELEEYMDPMNEYNALNEAKQM... | May regulate calcium-dependent activities in the endoplasmic reticulum lumen or post-ER compartment. | Q5BKL9 |
Q1DD74 | PRMA_MYXXD | Ribosomal protein L11 methyltransferase | Myxococcus | MSQTYLSLTVELPEEASEAVQDLLHESGALGLEVRDREAPLMPGVRGPNPGEAIIIGYFDERDTAESARDEVASSFPEAKLTLDEQPQQDWSNEWKSLIKSVHVGRLWVGPPWDKANAPAGTVQLVIEPKMAFGTGDHPTTSLCLAAVDAYMAEHPGAAVLDVGTGTGVLAIAAKKLGAGRTVATDNDPISVELAQENQAENGTPDIEVSGKELTQVEGTFDLVLANILANTLIELAPLIVAKTKDRLVLAGVLSHQRADVEAAYRNLGLTVLTGATQGEWVRIDLQR | Methylates ribosomal protein L11. | Q1DD74 |
Q98N50 | RL16_RHILO | 50S ribosomal protein L16 | Mesorhizobium | MLQPKRTKFRKQFKGRIHGTAKGGTNLDFGGFGLKALEPNRVTAREIEAARRAITREMKRAGRVWIRIFPDLPVTSKPTEVRMGKGKGAVDYWAARVKPGRIMFEIDGVSEETAREALRLGAAKLSVRTRFVQRIAE | Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs. | Q98N50 |
Q3II62 | SYY1_PSET1 | Tyrosyl-tRNA synthetase 1 | Pseudoalteromonas | MTTQLLEDITHRGLVSQVSDLAQLEQLLATSQVVYCGFDPTAGSLHIGHLVPLLMLKRFNDAGHKAVALIGGATGLIGDPSFKATERSLNSKETVQGWVADLSSQVESVMNPHLSEPIQLKNNADWFSGIEVLDFFRDVGKHFSINNMINRESVKQRLQRPDQGLSFTEFSYTLLQSYDFAKLNSELGCSVQIGGNDQWGNIVSGIDLTRRLNKQTVYGLTLPLITKSDGTKFGKTEGGAIWLDPKKTSPYRFYQFWLNCDDADVYNFLRFYTFLSVKEIEAIEANDITSQQKPQAQGILAEQLTRFVHGEQGLASAQRI... | Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). | Q3II62 |
Q3IX55 | RBL2_CERS4 | Ribulose bisphosphate carboxylase | Cereibacter | MDQSNRYARLDLQEADLIAGGRHVLCAYVMKPKAGYGYLETAAHFAAESSTGTNVEVSTTDDFTRGVDALVYEIDPEKEIMKIAYPVELFDRNIIDGRAMLCSFLTLTIGNNQGMGDVEYAKMHDFYVPPCYLRLFDGPSMNIADMWRVLGRDVRNGGMVVGTIIKPKLGLRPKPFADACHEFWLGGDFIKNDEPQGNQTFAPLKETIRLVADAMKRAQDETGEAKLFSANITADDHYEMVARGEYILETFGENADHVAFLVDGYVTGPAAITTARRQFPRQFLHYHRAGHGAVTSPQSMRGYTAFVLSKMARLQGASGI... | RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site. | Q3IX55 |
Q4G073 | TRDMT_RAT | DNA (cytosine-5)-methyltransferase-like protein 2 | Rattus | MEPLRVLELYSGIGGMHHALRESRVPAHVVAAIDVSTVANEVYKHNFPHTHLLAKTIEGISLEEFDKLSFNMILMSPPCQPFTRIGLQGDMSDRRTNSFLYILDILPRLQKLPKYILLENVKGFEVSSTRGLLIQTMEACGFQYQEFLLSPSSLGIPNSRLRYFLIAKLQSEPLCFQAPGQILMEFPNSGTVQPQEYAVVEEGKLRVRTREPDVCLDSSSTQCSGQDSILFKHETAADIDRKRQQDSDLSVQMLKGFLEDGDTAQYLLPAKSLLRYALLLDIVKPTSRRSMCFTKGYGSYIEGTGSVLQTAEDVQIENIY... | Specifically methylates cytosine 38 in the anticodon loop of tRNA(Asp). | Q4G073 |
K0K750 | BCAS_SACES | Type I terpene cyclase | Saccharothrix | MGRPATPQQTAFHIPFPRAISPDVSAVHPGSMAWLRRHGMLRSDASARRVDGWRLTELAGRFFPDARGEDLRLGADVMGFFFLFDDQFDHPGGLRAEAVAVSKRLLHLTSLPAGPAPEGAGPVVAAWADLWNRSCQGMSSAWRVRAAREWRRYFVGNLEESVAREGMSGESVEDYLRLRAMTIGTTPVYDLCERTQHFEIPDEVLHSHHVQAMRDLATEIVVLCNDVASTIKESARGETLNAVLLLERHHEAERGPAVARVQRMVEARLAAFRRLRDRTSRTCAALDLTAEQCDRVDRYVRTALMSVVRGNYDWQQRSAR... | Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) to yield the bicyclic sesquiterpene (2S,10R)-(-)-(E)-beta-caryophyllene via a probable 1,10-cyclization, which could involve the abstraction of the pyrophosphate from FPP to yield a (E,E)-germacradienyl cation. | K0K750 |
A3N1B4 | LEXA_ACTP2 | LexA repressor | Actinobacillus | MSRKHLTARQQEIFDFVKHHIETTGMPPTRVEIAREIGFKSPNAAEEHLKALARKGYIEMLSGTSRGIRILVDNEETAANDDGLPLIGKVAAGTPIMAIEHVESHYPVNGAMFNPNADYLLKVNGNSMEKIGILDGDLLAVHKTNFARNGQVVVARVDDEVTVKRLEKKGDLIYLHPENDELQPIIVDPRIEYIEIEGIAVGVIRNNAWM | Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair... | A3N1B4 |
A3PFC5 | IF3_PROM0 | Translation initiation factor IF-3 | Prochlorococcus | MPPRPRFDRRAPVRELPNINERIKYPQLRVVDSDGKQLGVIDRLKALEIASQRELDLVLVSEKANPPVCRIMDYGKYKFEQEKKAKEARKKSHQTEVKEVKMRYKIDKHDYDVRIGQATKFLKSGDKVKCTVIFRGREIQHSNLAETLLLRMANDLEEQSEVQQKPKREGRNMIMFLSPRKTPLIKKDDA | IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins. | A3PFC5 |
Q5X3P2 | KGUA_LEGPA | GMP kinase | Legionella | MVSDNSGNLYIVAAPSGGGKTSLVKKLIEMVGEIEVSVSHTTRPMRPGEKEGVDYFFIDEEQFISMVNEGAFIEHAKVFNHWYGTSVAQINKRLQFGIDVVLDIDWQGAEQIRHSYPDAVSVFIIPPSLDTLKERLMNRRQDKDNVISERMTKAQDELGHYPEFDYLIVNDDFEKAAMELQSIVIANRLRIEKQVNKQAKLLSFLLSSQ | Essential for recycling GMP and indirectly, cGMP. | Q5X3P2 |
Q8DFF6 | ISPE_VIBVU | 4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase | Vibrio | MITSPTTWPSPAKLNLFLYINGRTDNGYHELQTLFQFLDHGDQLTITANDSGHITLTPDIVDLPVEQNLIWKAANALQKKTGCTLGANIHLNKILPMGGGIGGGSSNAATALVALNFLWQLGLSDDELADIGLKLGADVPVFVRGHAAFAEGVGEKLTPAQPEEKWYLVVRPDVHIATVDIFTHPQLTRNTPKRSLETLLDSEYGNDCEKIVRMIHPKVDKQLSWLLQYAPSRLTGTGSCVFAEFNSRSEAESILAQLSDNVSAFVAQGRNISPLKETLADYLSAQNRPI | Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. | Q8DFF6 |
A1K8P4 | HEMH_AZOSB | Protoheme ferro-lyase | Azoarcus | MARFWTEAPHRHGSTARTGILLVNLGTPVAPTAAALRPYLQQFLSDPRVVEIPRAVWLPLLNGVILNTRPRKSAAKYASIWTDEGSPLAVHTRRQAELIAARFASRDDVRVDWAMRYGAPAVADKLGALRAAGCTRILVVPMYPQYAASTTASVMDEVARCLQHWRNLPELRFVRSFHDDPGYIGALAASVREHWTRHGQPDRLLMSFHGLPRYTLERGDPYHCECHRTARLLAESLGLAPERVIVSFQSRFGRTRWLEPYTQPTLEALARDGVGRVDVMCPGFVADCLETLEEIAMECRAAFLGAGGREFHYIPCLNER... | Catalyzes the ferrous insertion into protoporphyrin IX. | A1K8P4 |
Q16082 | HSPB2_HUMAN | DMPK-binding protein | Homo | MSGRSVPHAHPATAEYEFANPSRLGEQRFGEGLLPEEILTPTLYHGYYVRPRAAPAGEGSRAGASELRLSEGKFQAFLDVSHFTPDEVTVRTVDNLLEVSARHPQRLDRHGFVSREFCRTYVLPADVDPWRVRAALSHDGILNLEAPRGGRHLDTEVNEVYISLLPAPPDPEEEEEAAIVEP | May regulate the kinase DMPK. | Q16082 |
Q2LVI3 | PYRC_SYNAS | Dihydroorotase | Syntrophus | MKILLKGGRVIDPAQNLDGQMDLLLENGKIAAIAEAVGSVPEDTRLLDLKGMILLPGLVDMHTHLREPGYEYKETIRSGSEAAAVGGFTSIACMPNTLPVNDNRTVTEYILKRAKECDTVHVYPVAAVSRNSEGKILAEFGDLKEAGAIAFSDDGKPVMNSILMRRALEYASSLDRIIISHCEDLNLSAGGLMNEGKISTELGLPGIPTLAEDVMVARDLLLAEFSGAALHIAHVSSAGAVRMIRDAKKRGVRVTAETTPHYFTLTDEAVTNFNTNTKVSPPLRSREDLQAVREGLRDGTLDAIVTDHAPHALTDKEVEF... | Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. | Q2LVI3 |
Q03R52 | MURI_LEVBA | Glutamate racemase | Levilactobacillus | MQNDPIGLMDSGVGGLTVLKEVQRLLPTENTVFLGDQARLPYGPRSVAEVTMFTKQIAQFLRQQAGIKALVIACNTATAAALTTMQQTLPIPVIGVIAPGAQAAVQTTRNHRIGVIATAGTVKSDQYRRDILAAAPNSQIFSVACPEMVTLAEQNDLTTTHARSVVAANLASLMDKKIDTLVMGCTHFPLLRSAIQHAVGSQVTLVDPGLATAEQTAAILKTHGLLNPATTRGTAQFFTTGETAHFDTLASQWLDQQPMPAKHVSIAQLTTPMEVN | Provides the (R)-glutamate required for cell wall biosynthesis. | Q03R52 |
Q1I563 | ALGL_PSEE4 | Poly(beta-D-mannuronate) lyase | Pseudomonas | MTIINRKTAPALLALALFGGAAQAALVPPQGYYEGIEKLKSSDGDFRCEAAPRPYTGSLRFRSKYEGSDKARATLNVASEKAFRASTKDITTLEKGVSKMVGQYMRDGRPAQLDCALTWLGTWARADALMSSDYNHTGKSMRKWALGSMSGSWLRLKFSNSQPLAAHQAEAEQIEKWFARLAQQTVRDWSGLPLEKINNHSYWAAWSVMATAVATDRRDLFDWAVKEYKVGANQVDEQGFLPNELKRRQRALAYHNYALPPLAMIASFAQANGVDLRKENNFALQRLGEGVLAGARDPSQFTAHAGVKQDLHDLKIDSKY... | Catalyzes the depolymerization of alginate by cleaving the beta-1,4 glycosidic bond between two adjacent sugar residues via a beta-elimination mechanism. May serve to degrade mislocalized alginate that is trapped in the periplasmic space. | Q1I563 |
A9M1P7 | GCSP_NEIM0 | Glycine dehydrogenase (aminomethyl-transferring) | Neisseria | MKLSELFNPDEFAARHLSFGDEAALLAAVGEKSMDDFVGNTVPQSIRMPSELDLPEALTEADALAKLKGIASKNMINKSYIGLGYYPTRVPNVILRNVLENPGWYTAYTPYQAEIAQGRLEALLNFQQVCIDLTGFPVAGASLLDEATAAAEAMAMAHRVGKVKSERFFVDARVYPQTLDVMKTRAKYFGFELVVGDFAQADEGEYFGALFQYVGKDGDVQDLQDVIGRLKAKGTIVAVSADIMSLVLLKSPAELGADIALGNTQRFGVPMGFGGPHAAYFAFKDEFKRSAPGRIIGVSKDASGKPALRMALSTREQHIR... | The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein. | A9M1P7 |
A0PKZ7 | MOAA_MYCUA | Molybdenum cofactor biosynthesis protein A | Mycobacterium | MTVTALGVPTVRGRSEGSAVASDAPGDGPLLDRFGRSATDLRVSLTDRCNLRCGYCMPAEGLNWLPGEQLLGPAELARLPRIAVTPLGITSVRFTGGEPLLARHLEEVVAAAAQLRPRPEISLTTNGVGLAKRAAALAEAGLDRVNVSLDTVDRAHFAAVTRRDRLTDVLDGLAGARAAGLTPVKVNAVLDPETGRQDVVELLRFCLEQGYQLRVIEQMPLDAGHQWRRNALLGSDDVLAALQPHFRLRPDPAPRGSAPAELWLVDAGPDTPAGKFGVIASVSHAFCSTCDRTRLTADGQVRSCLFSTEETDLRGLLRAG... | Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate. | A0PKZ7 |
Q8EQQ3 | LYTT_OCEIH | Sensory transduction protein LytT | Oceanobacillus | MKIHIMIAEDERLAREELMYLLQQENDIILCPSAENGDQLLNLYQEYNPNVIFLDIHMPGINGIEVAKKIRNEFEDKDIIIIFTTAYESYGVQAFEIQATDYLLKPFSEERFKIAMNRIRKTLSTKKVRKPKVDKLVVNLDEKMMVIDPNQIGFAAREGRTVKIHFISNEVIETKMNLKELEEKLSGFPFYRPHRSYLVNMDCIKEITPWFNGAYNLVIKDLAESTIPVSRTAAKGLFDALQGVHH | Member of the two-component regulatory system LytS/LytT that probably regulates genes involved in cell wall metabolism. | Q8EQQ3 |
B8FBE8 | DPO4_DESAL | DNA polymerase IV | Desulfatibacillum | MTENLIIHVDMDAFYASVELLDNPELRGQCVIVGGASNRGVVCSASYEARALGVRSAMPIVTARKLCPRGVFLPVRRARYQEISRKVFEIFHQYTPLVEPISLDEAFMDVTSSTRLFGSGEEIAANIRRQIESSLGITASAGIAKNKLVAKIASDLCKPNGLLVVPADQTQEFLDPLPISRLWGVGPASRNKLISLGVKTIRDVRKLTQEMLSANFGRNGEVIYAFARGMDDRPVEPPGAAKSIGREITFDRNVYTLEEAYKWMLFLSERVARRMRKEEATGRTVNIKVKYADFIQVTRSVTLESPTDDPGEIYTHAKKL... | 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' exonuclease (proofreading) activity. May be involved in... | B8FBE8 |
P78697 | DIM1_KLULA | S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase | Kluyveromyces | MGKAVKKKYSGASSGGKEVDAEKHLTTVFKFNTDLGQHILKNPLVAQGIVDKAQIKPSDIVLEIGPGTGNLTVRILEQARKVVAVEFDPRMAAELTKRVHGTPVEKKLEILLGDFMKTELPYFDVCISNTPYQISSPLVFKLINQPKPPRVSILMFQREFAMRLLARPGDSLYCRLSANVQMWANVTHIMKVGKNNFRPPPKVESSVVRIEIKNPRPQVDFNEWDGLLRIVFVRKNRTIAAGFKSTTVLEILEKNYKAFLATQSAVPTTSSGDSLINEVKEKIEQVLSETGLAEKRAGKCDQTDFLKLLYGFHQVGIHFA | Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle. | P78697 |
Q8VDZ4 | ZDHC5_MOUSE | Zinc finger DHHC domain-containing protein 5 | Mus | MPAESGKRFKPSKYVPVSAAAIFLVGATTLFFAFTCPGLSLNVSPAVPIYNAIMFLFVLANFSMATFMDPGIFPRAEEDEDKEDDFRAPLYKTVEIKGIQVRMKWCATCRFYRPPRCSHCSVCDNCVEEFDHHCPWVNNCIGRRNYRYFFLFLLSLTAHIMGVFGFGLLYVLYHIEELSGVRTAVTMAVMCVAGLFFIPVAGLTGFHVVLVARGRTTNEQVTGKFRGGVNPFTNGCCNNVSRVLCSSPAPRYLGRPKKEKTIVIRPPFLRPEVSDGQITVKIMDNGIQGELRRTKSKGSLEITESQSADAEPPPPPKPDL... | Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates such as CTNND2, CD36, STAT3 and S1PR1 thus plays a role in various biological processes including cell adhesion, fatty acid uptake, bacterial sensing or cardiac functions . Plays an important role in the regulation of synapse ... | Q8VDZ4 |
Q61Y48 | LIN53_CAEBR | Probable histone-binding protein lin-53 | Caenorhabditis | MATIEDGTSEDRVANDEYKIWKKNTPFLYDLVMTHALEWPSLSVQWLPEIEKESSDHTVHRLILGTHTSDEQNHLLISKICMPTDEAQFDASRYDTERGEFGGFGAVNGKVEPDIRINHEGEVNRARYMPQKPTIIATKSPSADVYIFDYTKYPSVPKDNTFNPLLKLKGHTKEGYGLSWNPNKEGLILSASDDQTVCHWDINGNAGANGELKAREIFKGHESVVEDVAWHVLHDGVFGSVGDDKKLLIWDLRTNVPGHAIDAHSAEVNCLAFNPYSEFILATGSADKTVALWDLRNLRLKLHSFESHRDEIFQVQWSPH... | Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Required for hcp-3 and his-1 stabilization, localization of hcp-3 to centromeres and for proper chromosome segregat... | Q61Y48 |
Q54IA8 | HEMH_DICDI | Protoheme ferro-lyase | Dictyostelium | MISRKIISTINSKTFYNKSLSYCTVNNNKNTTININNNNEKPKIKTGILMLNLGGPSKLEEVEPFLTRLFTDKEIFKLPFQKYTGTLIAKRRSNAVMKLYEAIGGGSPIRKWTEKQGELLSSMMDKISPETAPHKHYIGFRYSDPLIADTLDQMENDNVERVVAFSQYPQYSCTTTGSSLNNLWKTLEEKQMQSKFKWSVIDRWQDHKGFIDATIHKIKKAYNQFNSKLRELDIDDVDANNNNNNNKPVLVFSAHSLPMSTVEKGDPYPQEVAETVCRVMDGLGIRDEETGKPLEYILAWQSKVGPLPWLSPKTSFVIEQ... | Catalyzes the ferrous insertion into protoporphyrin IX. | Q54IA8 |
A6UPM1 | CBIT_METVS | Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating) | Methanococcus | MIKDSEFYRLDGVPITKEEIRAISVEKLNICPEDIILDIGCGSGGMTVEISKRCKFVYAVDGSKDAIDTTLKNMDKFNVKNCEVYFGDAKDLISNFKVNKAFIGGTQNIESVIEKLNEKNVRNIVINTIVLENSVKVIQILERLNFSIEVISVLISYGKRISSGHMMLSKNPITIITAKK | Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7. | A6UPM1 |
Q2GH51 | RL22_EHRCR | 50S ribosomal protein L22 | Ehrlichia | MSKVLIVAKGMGLKSTPSKLNLVADLIRGKDVSVAMMYLKFCRKKSAGYISKVLKSAVANAQANYNIDLDNLYVKEVLVGKSFSLRRIHARARGKACRVYKHYGNVIIKLFERI | The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome. | Q2GH51 |
P0C248 | COW_CONAA | Contryphan-Am Am918 | Leptoconus | MGKLTILVLVAAALLSTQVMVQGDGDQPADRDAVPRDDNPSGMSGKFMNVLRRAGCPWDPWCG | Inhibits high voltage-activated calcium channels (Cav). | P0C248 |
B9K286 | HUTU_AGRVS | Imidazolonepropionate hydrolase | Agrobacterium | MTNPRHNIRDVRAATGTELSAKSWMTEAPLRMLMNNLDPDVAERPHELVVYGGIGRAARTWEDFDRIVATLKTLTEEETLIVQSGKPVGVFKTHKDAPRVLIANSNLVPHWATWDHFNELDKKGLAMYGQMTAGSWIYIGTQGIVQGTYETFVEAGRQHYNGNLKGKWILTGGLGGMGGAQPLAAVMAGACCLAVECDETRVDFRLRTRYVDAKAHTLDEALALIDQWTKAGEAKSVGLIGNAADIFPELVKRGIRPDIVTDQTSAHDPINGYLPSGWTVAEWRAKQESDPKAVERAARASMKVHVAAMVDFWNMGVPTL... | Catalyzes the conversion of urocanate to 4-imidazolone-5-propionate. | B9K286 |
Q9VZ08 | RME6_DROME | Receptor-mediated endocytosis protein 6 homolog | null | MEPPAAGNLLEIMDLARTLRQEQLFIQQEQAAFAQLTGAFESNAGTITKLAFVCAQQRQILNELLLARTDQDPLLFCRRASAYDSAQFVDAKQLLPYEHALAYEDLFNYLYNTPYLLALSLATADRLSLLSASQLGQIINTIATGLYGNAINTKDVELLLKLLRELIEIQLLTSEQPRRLLRTNSSSFARLYQRLVESLFSARIFLTAALHAPLMGVLSEHEIWLDLDPHKLMQTFTPKEREKRFGREGDEEYQRNVARFHAETLGKLHSHVQEFVKSLQQSWALFPSSLRWLLQTLSQQLRQSLRHEEQEIRQLLTDLV... | Acts both as a GTPase-activating protein (GAP) and a guanine nucleotide exchange factor (GEF), and participates in endocytosis. | Q9VZ08 |
B9EBF6 | ILVD_MACCJ | Dihydroxy-acid dehydratase | Macrococcus | MRSNMIKKGPEQAPARSLLHATGQIKSPEDMNKPFIAICNSYIDIVPGHVHLRELADIAKEAIREAGGIPFEFNTIGVDDGIAMGHIGMRYSLPSREIIADAAETVINAHWFDGVFYIPNCDKITPGMLLAAVRTNVPAIFCSGGPMKAGLSATGKALTLSSMFEAVGAFKEGTLTKEDFLDMEQNACPTCGSCAGMFTANSMNCLMEVLGLALPFNGTALAVSKERRALIRESAFKLMDLVKRDIKPKDIVTKEAIDDAFALDMAMGGSTNTVLHTLALANEAGIDYDLERINEIAEKTPYLSKIAPSSSYSMHDVHTA... | Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (... | B9EBF6 |
Q3K6Q6 | PANB_PSEPF | Ketopantoate hydroxymethyltransferase | Pseudomonas | MPAITLTTLQSLKQKGEKITMLTCYDATFAHACNEAGVEVLLVGDSLGMVLQGHDSTLPVTTAEMAYHVASVKRGNSDALILADLPFMANATLEQTMTNSALLMQAGAHMVKVEGALWLADSIRLLAERGVPVCAHMGLTPQAVNILGGYKVQGRNENQARQMRADAISLEQAGAAMLLLECVPSELAAEITQAVKIPVIGIGAGSDTDGQVLVLHDMLGLSISGRVPKFVKNFMQGQDSIQSALKAYVSEVKATTFPGIEHGFSA | Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. | Q3K6Q6 |
A5UHT0 | RL3_HAEIG | null | Haemophilus | MIGLVGRKVGMTRIFNEDGVSVPVTVIEIEANRVTQVKTLENDGYTAVQVTTGSKKANRVTKPEAGHFVKAGVEAGRGLWEFRTEGEEFTLGQEINVDIFADVKKVDVTGTSKGKGFQGGVKRWNFRTQDATHGNSLSHRVLGSIGQNQTPGRVFKGKKMAGHLGAERVTVQSLEVVRVDAERKLLLVKGSVPGAINGNVIVKPAVKA | One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. | A5UHT0 |
B9J8E2 | ENGB_AGRRK | Probable GTP-binding protein EngB | Agrobacterium tumefaciens complex | MAEQTTKDDKPLFGRPWIFIRGVPAMKFLPPEGPLEVAFAGRSNVGKSSLINALVGHKGLARTSNTPGRTQELNYFVPDGFSGEGGDLPPMALVDMPGYGYAEAPKEQVDAWTKLVFDYLRGRTTLKRVYVLIDSRHGIKKNDEEVLALLDKAAVSYQIVLTKTDKIKEAGLPKLLADTAEKIRKRPAAYPGILSTSSEKGDGLEEVRQAIRLTVGIPF | Necessary for normal cell division and for the maintenance of normal septation. | B9J8E2 |
P41165 | RL23A_TRYBB | L25 | Trypanosoma | MPAKAASAAASKKNSAPKSAVSKKVAKKGAPAAAAKPTKVVKVTKRKAYTRPQFRRPHTYRRPATVKPSSNVSAIKNKWDAFRIIRYPLTTDKAMKKIEENNTLTFIVDSRANKTEIKKAIRKLYQVKTVKVNTLIRPDGLKKAYIRLSASYDALDTANKMGLV | This protein binds to a specific region on the 26S rRNA. | P41165 |
B0G186 | UFM1_DICDI | Ubiquitin-fold modifier 1 | Dictyostelium | MSKVTFKITLTSDPKLPFRVINVTEDTPFTAVLRFACEQFNVPWQTSAIITNDGIGINPAQTSGNIFLKNGSDLRLIPRDRVGGL | Ubiquitin-like modifier which can be covalently attached to substrate proteins as a monomer or a lysine-linked polymer in a post-translational process called ufmylation. Ufmylation on lysine residues of proteins may play a crucial role in a number of cellular processes. | B0G186 |
Q9Z3Q1 | SYRB2_RHIME | Probable transcriptional regulator syrB2 | Sinorhizobium | MADESNTGSIAAAVAPNADVKAPAAKKKRSPRRQKAVAEPRRAVSETPAAKPRRYSEQQRKEKLKLIETQVTEGKVTLKDAIKSAGISEQTYYQWKRTVKPVEQKAEKRLPTGEELADLVRLEEENQRLRKLLAEKLRAENADLRKRLGLD | Seems to affect the transcription of cya3. May be negatively autoregulated. | Q9Z3Q1 |
Q23369 | BST22_CAEEL | Bestrophin homolog 22 | Caenorhabditis | MTISYTLDVSQTNLQSFFSLLLRWRGSVWKAVFGQLAVWTAVFLLISCIYRYMLSPSQQDVFEQLIRYFDNKLDANIPLTFLLGFFVSFVVARWGSILNGIGWIDDASLLFATYIRGADEETRVIRRNLVRYLVLSQALVLRDISMQVRKRFPTMDTLAASGLMTHEEMDILDHIKDPYSRYWTSIQWSLNLVYECQKKGKVDSYYLMNKIVDEIGKFRHGLASLLKYDWVPVPLVYPQVIFLAVRIYFMICLIGRQFIVTGPNPSGIDLWLPITTMVQFLVYMGWMKVAEALLNPLGEDDDDLECNYIIDKNLITGLSI... | Forms chloride channels. | Q23369 |
Q36644 | CYB_CORRA | Ubiquinol-cytochrome-c reductase complex cytochrome b subunit | Corynorhinus | MTNIRKSHPLLKIINDSFIDLPTPSNISSWWNFGSLLGICLVLQISTGLFLAMHYTSDTATAFNSVTHISRDVNYGWVLRYLHANGASMFFICLYLHVGRGLYYGSYLYKETWNVGVILLFATMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTDLVEWIWGGFSVDKATLT | 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 membrane that is... | Q36644 |
Q65Q77 | FTSB_MANSM | Cell division protein FtsB | Basfia | MRLFILILSAILLLFQYDLWFGKNGYLDYKETAEEIAMHKAENTKLSQRNQVVAAEIRDLKDGVEAIQERARLQYELVKPNETFYRIAKENKDNR | Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. | Q65Q77 |
Q1GIU8 | MURB_RUEST | UDP-N-acetylmuramate dehydrogenase | unclassified Ruegeria | MTDLPAVRGRLTPNRDLSDLTWLRVGGPADYLFQPADLEDLQEFLRNLPADMDVFPMGVGSNLIVRDGGLRSVVIRLGRGFNGIEVDGDTVTAGAAALDAHVARKSAEAGVDLTFLRTIPGSIGGAVRMNAGCYGSYVADVFMSAQVVLRDGSLATLSAEDLQFKYRQTELAPGAVLVSATLRGPKGDPDALAARMEDQLRKRDETQPTKERSAGSTFRNPAGFSSTGKADDVMDLKAWKVIDNAGLRGATLGGAQMSEKHSNFMINAGGATAADLEGLGENVRKKVYADSGIWLEWEIMRVGDPKRS | Cell wall formation. | Q1GIU8 |
B5XW50 | HEM1_KLEP3 | Glutamyl-tRNA reductase | Klebsiella | MTLLALGINHKTAPVDLRERVTFSPETLDQALESLLAQPMVQGGVVLSTCNRTELYLSVEEQDNLQEALIRWLCNYHGLNEEDLRKSLYWHQDNDAVSHLMRVASGLDSLVLGEPQILGQVKKAFADSSRGHLNVSELERMFQKSFSVAKRVRTETDIGASAVSVAFAACTLARQIFESLSSVTVLLVGAGETIELVARHLREHHVRKMVIANRTRERAQALADEVGAEVIALSDIDERLKEADIIISSTASPLPIIGKGMVERALKARRNQPMLLVDIAVPRDVEPEVGKLANAYLYSVDDLQNIIQHNLAQRKAAAVQ... | Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). | B5XW50 |
B0CG35 | LEUC_ACAM1 | Isopropylmalate isomerase | Acaryochloris | MSQGTLFDKVWDLHTVDVLPSGQTQLFIGLHLIHEVTSPQAFTMLKDRGLNVLYPQRTVATVDHIVPTENQARPFADTLAEEMMQALEQSCQDHGITFHNIGSGKQGIVHVIAPEQGLTQPGMTIACGDSHTSTHGAFGAISFGIGTSQVRDVLASQTLALAKLKVRKVEVNGTLPAGVYAKDVILHIIRTLGVKGGVGYAYEFAGTTFEQMTMDERMTVCNMSIEGGARCGYVNPDTITFEYLKGREAAPKGADWDQAVAWWQSIRSDADAVYDDVVVFDAQDISPTVTWGITPGQGIGIDEAIPGLDHFTDADQPIAS... | Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. | B0CG35 |
P9WIS0 | BKDB_MYCTO | Branched-chain alpha-ketoacid dehydrogenase E1 component subunit beta | Mycobacterium tuberculosis complex | MTQIADRPARPDETLAVAVSDITQSLTMVQAINRALYDAMAADERVLVFGEDVAVEGGVFRVTEGLADTFGADRCFDTPLAESAIIGIAVGLALRGFVPVPEIQFDGFSYPAFDQVVSHLAKYRTRTRGEVDMPVTVRIPSFGGIGAAEHHSDSTESYWVHTAGLKVVVPSTPGDAYWLLRHAIACPDPVMYLEPKRRYHGRGMVDTSRPEPPIGHAMVRRSGTDVTVVTYGNLVSTALSSADTAEQQHDWSLEVIDLRSLAPLDFDTIAASIQRTGRCVVMHEGPRSLGYGAGLAARIQEEMFYQLEAPVLRACGFDTP... | Component of the branched-chain alpha-ketoacid dehydrogenase (BCKADH) complex, that catalyzes the overall conversion of branched-chain alpha-ketoacids to acyl-CoA and CO(2). | P9WIS0 |
C1B4H9 | AROC_RHOOB | 5-enolpyruvylshikimate-3-phosphate phospholyase | Rhodococcus | MLRWITAGESHGPALVAMLEGMVAGVEVTSEDISTQLARRRLGYGRGARMKFEADKVTIVGGVRHGRTLGGPIAVEVGNTEWPKWETIMSADPVDADLLADQARNAPLTRPRPGHADYSGMLKYGFDDARPVLERASARETAARVAAATFARGFLRQVFGVEVLSHVISIGASDPYAGPEPTASDLAAIDASPVRAFDKAAEESMIAEIEAAKRDGDTLGGIVEVVIHGLPVGLGSFISGADRLDARLASALMGIQAIKGVEVGDGFETARRRGSQAHDEMRPGPDGILRSTNRAGGLEGGMTNGEALRVRAAMKPISTV... | Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a s... | C1B4H9 |
A8G978 | AMPA_SERP5 | Leucyl aminopeptidase | Serratia | MEFSVKSGSPEKQRSACIVVGVFEPRRLSPIAEQLDKISDGYISALLRRGELEGKVGQTLLLHHVPNILSERILLIGCGKERELDERQYKQVIQKTINTLNDTGSMEAVCFLTELHVKGRNTYWKVRQAVETAKETLYTFDQLKSNKVEPRRPLRKMVFNVPTRRELTSGERAIQHGLAVSSGIKAAKDLGNMPPNICNAGYLASQARQLADAFSTNITTRVIGEQQMKELGMNAYLAVGAGSRNESLMSVMEYKGNPNPDAKPIVLVGKGLTFDAGGISIKPAEGMDEMKYDMCGAATVYGVMRVVAELNLPLNVIGVL... | Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. | A8G978 |
Q49A26 | GLYR1_HUMAN | Putative oxidoreductase GLYR1 | Homo | MAAVSLRLGDLVWGKLGRYPPWPGKIVNPPKDLKKPRGKKCFFVKFFGTEDHAWIKVEQLKPYHAHKEEMIKINKGKRFQQAVDAVEEFLRRAKGKDQTSSHNSSDDKNRRNSSEERSRPNSGDEKRKLSLSEGKVKKNMGEGKKRVSSGSSERGSKSPLKRAQEQSPRKRGRPPKDEKDLTIPESSTVKGMMAGPMAAFKWQPTASEPVKDADPHFHHFLLSQTEKPAVCYQAITKKLKICEEETGSTSIQAADSTAVNGSITPTDKKIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAEKCDLFIQEGARLGRTPAEV... | Cytokine-like nuclear factor with chromatin gene reader activity involved in chromatin modification and regulation of gene expression . Acts as a nucleosome-destabilizing factor that is recruited to genes during transcriptional activation . Recognizes and binds histone H3 without a preference for specific epigenetic ma... | Q49A26 |
A0RJZ5 | MOBA_BACAH | Molybdopterin-guanine dinucleotide synthase | Bacillus cereus group | MSKYAGIVLAGGMSSRFGEPKALASWQGGTFIEHILKVMTSTLQEVVVISHSDIKERVEKLVQVPVIEDIPHYKGNGPLAGIVSGMEYIEADWYAIMPCDAPNVSHEWFTILLGQTSNEYDAVVPIINGRKQPLLAAYHNRVKEKIYALLQEEKRSMVQLLSQCNVKYIAGEDVQANADWFINVNTKEEYVQAQKDLSNE | 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. | A0RJZ5 |
Q03W55 | RNZ_LEUMM | tRNase Z | Leuconostoc | MQLEFLGTGSGQPSKFRNVTSIALRLLDERNAVWLFDVGEATQHQILKTTLRPRKVEKIFITHLHGDHIFGLPGFLSSRSFQGADKNEPLTIYGPKGVKEFVQTALRISETRLSYPIEYVDLTEGVIFEDHTFQVVAAPMRHRIETWGFRVIEKDHPGELLVDKLKQGNIPSGPVYGQLKAGKTVTLPDGRIVNGHDFIGKAQKGRIVTFILDTRPNDNVEWLAKNADVLVHESTYGSSEEEAKMAKAHAHSTSANAASVARRAHVNKLVLTHLSARYIGPMVKELIHDVRRNFANTYVARDFDIIDIPFKKDSNESK | Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA. | Q03W55 |
P83476 | TXPR2_THRPR | Protoxin-II | Thrixopelma | YCQKWMWTCDSERKCCEGMVCRLWCKKKLW | Gating-modifier toxin that targets voltage-gated sodium channels with a selective activity on Nav1.7/SCN9A (IC(50)=1-1.5 nM) . It inhibits both activation and inactivation . For inhibition of activation, it is 100-fold more selective for Nav1.7/SCN9A (IC(50)=0.26-3) than for other sodium channels (Nav1.2/SCN2A (IC(50)=... | P83476 |
Q60BA9 | EFTS_METCA | Elongation factor Ts | Methylococcus | MSITAGMVKELRERTGSGMMECKKALTETGGDLEAAVELMRKQGLAKADKKSGRTAAEGRICARVSEDGKAAAIVEVNCETDFVAKGDDFVKFADDVAAVALASSAMTVEELLAGEMRAGATVDQVRREMIAKIGENINVRRFERLSSQDGRIASYLHGTRIGVLVELVGGDAELGKDIAMHIAASKPLCCDEKGVPAEVIAKEKEIFSAQAQASGKPANIVEKMVEGRIGKFLGEITLVGQPFVKDPDQTVGKLLQSKGASVVRFVRFEVGEGIEKEETNFAEEVMAQVRAS | Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. | Q60BA9 |
A5VHM0 | PURA_LIMRD | IMP--aspartate ligase | Limosilactobacillus | MSSVVIVGSQWGDEGKGKMTDYLSQEADVVVRSQGGNNAGHTIAFDGKKFALRLVPSGIFAKDKLAVIGNGVVINPPALLKELHYLQDNGIDISGLRISSRSHITFPYHILLDKCQEEAKGDHKVGTTKNGIGPTYMDKVSRVGIRMCDLLEKDTFKEKLERNLAEKNELFTKLYHVDPISFDDIFESYYEYGQELKQYVTDTAQIVNDALDQDKKVLFEGAQGVMLDVDQGTYPYVTASNPIAGGVCTGVGVGPNKIETVVGICKAYSTRVGAGPFPTELTDEIGDQIRETGHEYGTVTGRPRRVGWFDSVAMRHARRV... | Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. | A5VHM0 |
Q9STQ3 | AGP13_ARATH | Arabinogalactan peptide 13 | Arabidopsis | MEAMKMRLFVAVLVAAMAFSAVQQAAAVEAPAPSPTSDASLAIPAFFASVATLAFGFLF | Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death. | Q9STQ3 |
Q11LD2 | DAPE_CHESB | N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase | unclassified Chelativorans | MTLPTDPAQNLASLIRCRSVTPVEGGALTALEAMLRPLGARVDRPVFSEEGEADVENLYARIGKDGPHLMFAGHTDVVPPGDEDAWTHPPFAAEIAGGEMFGRGAVDMKGGIACFVAALARHLEVSGTPKGSVSFLITGDEEGPSVNGSVKLLEWAAARGERWDAALVGEPTNVETLGDMVKIGRRGSLSGRITLFGRQGHVAYPHLADNPSRGLVALLEALMEPAFDQGTADFPPTNLEITTIDVGNPSVNVIPARATAAFNVRFNDTWSVETLQAEIHNRLDRAAAENRLRPGRTEPVSFELEWRDRPSPVFLTRDDK... | 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. | Q11LD2 |
Q0A4N0 | GLMU_ALKEH | Glucosamine-1-phosphate N-acetyltransferase | Alkalilimnicola | MEQALSIVVLAAGKGTRMRSRYPKLLHPVGGRPMLDHVLRTAFSLEPEAVHVVHGHGAEAVQAAHADWPVRWVVQEPQLGTGHAVEQAIPAIPDDHQVLVLYGDVPLVRPETLQALLAEADGGLGLLSVDFPDPTGYGRVLRDGHGAVTGVVEHKDATAAQRRVTECNTGLLAAPAGRLKAWLQRLDNDNAQAEYYLTDVIAMAVADGVRVAAYPVADPAEVQGVNDRVQLAAAERVWQRRQAEDWMRAGVTILDPDRFDLRGHFAAGEDCRIDVGVVLEGRVELGAGVEIGPHCVLRDVALGDGTRVEAHSVLDGATAG... | 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 ... | Q0A4N0 |
Q54VX7 | BL1S1_DICDI | Biogenesis of lysosome-related organelles complex 1 subunit 1 | Dictyostelium | MLSKLVKDHQTHQNKLKEENEVLKKEAIASMGVVTNGLIDSVNTGVACIFANQKKLETEARLLQANTAKFSKQTNQWIHLIENFNNSLKEIGDVENWSKKIESDMHNISDIIEFLYINSNPIQQQPQQQPQQQQQ | May negatively regulate aerobic respiration through mitochondrial protein lysine-acetylation. | Q54VX7 |
Q5SDL7 | TROPA_IXOSC | Tick receptor for ospA | Ixodes | MVAMEAMAAMEVMVAAMAATADTVASSAASATATEATVAMDTASLSLPLQLSPRSLPQSSLSATAATVATDTVVSSADTEVSDTEDSAATVSATASLSMLPQSSPRSLPQSSLSATAATVDSVTDMADTAMDTKQFISKGNEHFFAASYLCAWADQSAAGS | Serves as a receptor for ospA protein of B.burgdorferi, the Lyme disease agent. Required for spirochetal colonization. Essential for pathogen adherence to the vector. | Q5SDL7 |
B5F7T6 | RS17_SALA4 | 30S ribosomal protein S17 | Salmonella | MTDKIRTLQGRVVSDKMEKSIVVAIERFVKHPIYGKFIKRTTKMHVHDENNECGIGDVVEIRECRPLSKTKSWTLVRVVEKAVL | One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. | B5F7T6 |
Q1KXR8 | RR19_HELAN | 30S ribosomal protein S19, chloroplastic | Helianthus | MTRSLKKNPFVANHLLKKINKLNTKEEKEIIITWSRASTIIPIMVGHTIAIHNGKEHLPIYITDRMVGHKLGEFAPTLNFRGHAKSDNRSRR | Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. | Q1KXR8 |
Q1GZS0 | RL20_METFK | 50S ribosomal protein L20 | Methylobacillus | MPRVKRGVIARARHKKVLNAAKGYRGRRKNVYRIAKQAVMKAGQYAYRDRRQRKRQFRALWIARINAGAREYGLTYSRFINGLKKSAVEVDRKVLADLAVFDKQAFAKFAELAKSGLAAA | Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit. | Q1GZS0 |
Q9HNU8 | COFH_HALSA | FO synthase subunit 2 | Halobacterium | MTDASALDFDVVPSTDQSFENALANARDGRRLTVADGIELITTGTDTDGIDPRRKELVLEAADRRRADVVGDDVTFVANLNNNVTTACNTGCLFCNFKDTAHRFETEHEAAHGGFTKTPAESKATVADAIQRGVSEVTSVSGLHPAFGLNEAHRDALDPDDPDHNYKPPEAYDTDPTTYAAQIAAMSEAGAHVHSITPEEAHHAQRGVSWGYDEVYETLADAGLDTVPGTAAEILVDEVRDVICPGKMTTDEWVAAMEAAADAGLGTTATIMYGHVENAAHRIHHLDVIRALQDRTHNITEFVPLSFIHEQTPLYERGVV... | Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine. | Q9HNU8 |
L0E159 | MALF_MALAU | Malbrancheamide biosynthesis cluster protein F | Malbranchea | MKYTATFALLILAIGIQTQRRSTICRCRQEDACWPTTAEWSSLNQSIDGKLRHLRPVGLPCQQSAYHKEKCDEVLAMTHNSSWRVDHPESLQLVSWESWPEKNQSCQIVREAVDGCAQGRIPLYSAAVESTKQVQQAVSFAKHRNLRLVVRNTGHDMAGRSSAPGSLQILTSGLKGINYTENFVPFITQGSAEPMGPAVTIGAGILTGELYATGSEKGFVVLGGACSTVGIAGGFIQSGGMGILSPSKGLGSDHVLQVEIVTADGSHIIANQYQNEDLFWAVRGGGGGTFGVITSVTLRAFADLPATVTGIQINTPSADA... | FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of malbrancheamide, a dichlorinated fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core . The first step of malbrancheamide biosynthesis involves coupling of L-pr... | L0E159 |
P98025 | COX2_CHOBI | Cytochrome c oxidase polypeptide II | Choristoneura | MATWSNFNLQNSASPLMEQIIFFHDHTLIILIMITILVGYLMISLFFNSYINRFLLEGQMIELIWTILPTITLIFIALPSLRLLYLLDELNNPLITLKSIGHQWYWSYEYSDFQNIQFDSYMIPINEMKNNNFRLLDVDNRIILPMNNQIRILVTATDVIHSWTIPSLGVKVDANPGRLNQTNFFINRPGIFYGQCSEICGANHSFMPIVIESISIKNFINWINNYS | Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CII... | P98025 |
C6DZH8 | UPP_GEOSM | UPRTase | unclassified Geobacter | MSVHEVNHPLVKHKIGLMREAGISTKKFRELTSEIASLLAYEASRDFQIEPRTITGWDGSKVGIQQLKGKKVTVVPILRAGIGMLDGVLDMIPNAKVSVVGLARNEETLEAHTYFERFVGNLDERLALIIDPMLATGGSMAATIEMLKNNGCLQIRVLCLVAAPEGLARITAAYPEIDIYVAAIDERLNEQGYILPGLGDAGDKIFGTK | Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate. | C6DZH8 |
A9XMT5 | CCLOP_ORYSJ | Protein IPD3 homolog | Oryza sativa | MEGRGLSELFRNTSEDMFLKAMMENSMGVAAAAPSMEMMGFRNLSQGFREDSEELFNSWLMNGEIPGFSAMNNRPRQPSRLSSEAAGFPNQQHEIAQEHFPTDNLIPQNLAVHSEFTMNHNQQQLKNAAEKGMQASDLLLAKAWFHSTQPMTRSRSSELRKRYAAMQSNMPPITTETIETANKLRQDLTNASTVNSAPMSNTPSQTPTFVSPSSSSTSPLDNPHIVAQDTITSVVSMLKDTLERKKLSSHANGDTSSGISFGFYDSQHFQQNILGGTDIFPLVTTSQIQDSVMLPKVERPTEQGSGNFVAPANQVWLGTA... | Involved in arbuscular mycorrhizal (AM) symbiosis. Required for fungal infection in roots and arbuscule development during AM symbiosis. | A9XMT5 |
P23192 | MTM2_MORBO | Modification methylase MboII | Moraxella | MLEINKIHQMNCFDFLDQVENKSVQLAVIDPPYNLSKADWDSFDSHNEFLPFTYRWIDKVLDKLDKDGSLYIFNTPFNCAFICQYLVSKGMIFQNWITWDKRDGMGSAKRGFSTGQETILFFSKSKNHTFNYDEVRVPYESTDRIKHASEKGILKNGKRWFPNPNGRLCGEVWHFSSQRHKEKVNGKTVKLTHITPKPRDLIERIIRASSNPNDLVLDCFMGSGTTAIVAKKLGRNFIGCDMNAEYVNQANFVLNQLEIN | A beta subtype methylase that recognizes the double-stranded sequence 5'-GAAGA-3', methylates A-5 on the top strand, and protects the DNA from cleavage by the MboII endonuclease. It is not known if the cytosine of the complementary sequence TCTTC is also methylated by this enzyme. | P23192 |
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