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 |
|---|---|---|---|---|---|---|
B7N0S9 | RSMB_ECO81 | rRNA (cytosine-C(5)-)-methyltransferase RsmB | Escherichia | MKKQRNLRSMAAQAIEQVVEQGQSLSNILPPLQQKVSDKDKALLQELCFGVLRTLSQLEWLINKLMARPMTGKQRTVHYLIMVGLYQLLYTRIPPHAALAETVEGAVAIKRPQLKGLINGVLRQFQRQQDELLAEFNASDARYLHPSWLLKRLQKAYPEQWQSIVEANNQRPPMWLRVNRTHHSRDSWLALLDEAGMKGFPHADYPDAVQLETPAPVHALPGFEEGWVTVQDASAQGCMTWLAPQNGEHILDLCAAPGGKTTHILEVAPEAQVLAVDIDEQRLSRVYDNLKRLGMKATVKQGDGRYPSQWCGEQQFDRILLDAPCSATGVIRRHPDIKWLRRDRDIPELAQLQSEILDAIWSHLKSGGTLVYATCSVLPEENSLQIKAFLQRTADAELCETGTPEQPGKQNLPGAEEGDGFFYAKLIKK | Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | B7N0S9 |
Q0T3C3 | COBS_SHIF8 | Cobalamin-5'-phosphate synthase | Shigella | MSKLFWAMLSFITRLPVPRRWSQGLDFEHYSRGIITFPLIGLLLGAISGLVFMVLQAWCGAPLAALFSVLVLALMTGEFHLDGLADTCDGVFSARSRDRMLEIMRDSRLGTHGGLALIFVVLAKILVLSELALRGEPILASLAAACAVSRGTAALLMYRHRYAREEGLGNVFIGKIDGRQTCVTLGLAAIFAAVLLLGMHGVAAMVVTMVAIFILGQLLKRTLDGQTGDTLGAAIELGELVFLLALL | Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate. | Q0T3C3 |
Q9D8E6 | RL4_MOUSE | 60S ribosomal protein L4 | Mus | MACARPLISVYSEKGESSGKNVTLPAVFKAPIRPDIVNFVHTNLRKNNRQPYAVSELAGHQTSAESWGTGRAVARIPRVRGGGTHRSGQGAFGNMCRGGRMFAPTKTWRRWHRRVNTTQKRYAICSALAASALPALVMSKGHRIEEVPELPLVVEDKVEGYKKTKEAVQLLKKLKAWNDIKKVYASQRMRAGKGKMRNRRRIQRRGPCIIYNEDNGIIKAFRNIPGITLLNVSKLNILKLAPGGHVGRFCIWTESAFRKLDELYGTWRKAASLKSNYNLPMHKMMNTDLSRILKSPEIQRALRAPRKKIHRRVLKKNPLKNLRIMLKLNPYAKTMRRNTILRQARNHKLRVKKLEAAATALATKSEKVVPEKGTADKKPAVGKKGKKVDAKKQKPAGKKVVAKKPAEKKPTTEEKKPAA | Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. | Q9D8E6 |
A5CY18 | SECA_VESOH | Protein translocase subunit SecA | Candidatus Vesicomyosocius | MSIINNILSKIVGSRNDRLIKVLYKTVNQITELESNMQALSDEQLKSKTQEFKDRLNKKETLNSILIEAFAVIREASIRVLDLRHHDVQLIGGIVLNNGNIAEMGTGEGKTLVATLPAYLNALNGKGVHIVTVNDYLAFRDAQWMGKVFNFLSMSVGIITSNMSYENKQVAYLCDIVYATNNELGFDYLRDNMAFTSEQKVQRMLNFAIVDEVDSILIDEARTPLIISGPTDDYAQIYQAINHMIPHFTKQIESGAGKEIVIEVAGDYTVDEKHKQVFLTDNGHGKAERLLIDAGALLEGVSLYDASNILLMQHINSALRAHILFQKNVDYIIQNDEVVIVDEFTGRTMLGRRWSEGLHQAIEAKERVSIKKENQTLASITFQNYFRLYRTLSGMTGTADTEAVEFQDIYGLETVVVPPNKPSTRVDKSDLIYLTTQEKFKAIALEVANCQKTGQPVLVGTSSIENSELISTLLEKNNIKHEVLNAKQHEREAIIIANAGSIGAVTIATNMAGRGTDIVLGGKLLEQATNKQKIDWQNRHDDVIKAGGLHIVGTERNESRRVDNQLRGRSARQGDVGSTRFYLSLEDNLMRIFASEKMSSTMQKLGMKKGESIEHKMVNRAIENAQRKVEGMNYDARKHLLEYDDVANDQRKVIYQLRDDLMSVNDVQDRFISIREKVIKQLFSDYISAELMEEDWNVEGFYNALKSDYSVDLPLQQWLNKGVDIDELQSRIIQGMSTICDYKEETVGTKPMREFEKAVMLKTIDHYWKEHLATMDYLRQSVNLRGYAQKNPMQEYKRESFAMFTSLLDTINIEIVKSLSNVTINENTDILDVEQQNNDDAQATHSNPNEQTKQASITNNIQTQTDQQNTYQRKEKKVGRNEPCPCGSGKKYKKCHG | 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 as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane. | A5CY18 |
Q089Q6 | EFTU2_SHEFN | Elongation factor Tu 2 | Shewanella | MAKAKFERIKPHVNVGTIGHVDHGKTTLTAAISAVLSKTYGGEVKNFAQIDNAPEERERGITINTSHIEYDTPIRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLSRQVGVPFIIVFMNKCDMVDDEELLELVEMEVRELLSEYDFPGDDLPVIQGSALKALEGQPEWEAKILELAEALDTYIPEPARDIDKPFLLPIEDVFSISGRGTVVTGRVERGIVRVSDEVEIVGVRPTTKTTCTGVEMFRKLLDEGRAGENCGVLLRGTKRDDVERGQVLAKPGSINPHTTFESEVYVLSKEEGGRHTPFFKGYRPQFFFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIYPIAMDDGLRFAIREGGRTVGAGVVAKIIA | This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. | Q089Q6 |
P96723 | YWQK_BACSU | Immunity protein YwqK | Bacillus | MENEYDMKSIKEKGVDFEDLWFSSVSDEILDNPEDENGQPFTGLAYELYPNGQIIYFTKYKNGLAHGLTCEFYENGNKKSEKEYRYGQLHGISIIWFENGRKKSEQQYEHSILISEKNWDEEGNLLNKYEIDTDSPHFEILESRRETHINLGRE | Immunity component of one of 6 LXG toxin-immunity modules in this strain. They promote kin selection, mediate competition in biofilms, and drive spatial segregation of different strains, indicating that LXG toxins may help avoid warfare between strains in biofilms. Mediates intercellular competition during biofilm formation; disruption of the operon disadvantages the bacteria, but overexpression of the cognate immunity protein restores growth in competition with wild-type. In situ neutralizes the toxic effect of cognate toxin YqcG . Probably neutralizes the ability to inhibit growth of cognate toxin YwqJ. Probably does not have immunity protein activity on other LXG toxins (Probable). | P96723 |
Q9XI91 | IF5A1_ARATH | Eukaryotic translation initiation factor 5A-1 | Arabidopsis | MSDEEHHFESSDAGASKTYPQQAGTIRKNGYIVIKNRPCKVVEVSTSKTGKHGHAKCHFVAIDIFTSKKLEDIVPSSHNCDVPHVNRTDYQLIDISEDGYVSLLTDNGSTKDDLKLPNDDTLLQQIKSGFDDGKDLVVSVMSAMGEEQINALKDIGPK | The precise role of eIF-5A in protein biosynthesis is not known but it may function as a bimodular protein capable of binding to both RNA and proteins. Involved in xylogenesis. | Q9XI91 |
Q1GIC1 | ISPG_RUEST | 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase | unclassified Ruegeria | MSMNHIRPWRNIERRKSRQIHVGNVPVGGDAPIAVQTMTNTLTTDIKGTIAQVQAAADAGADIVRVSVPDEASARALKEIVRESPVPIVADIHFHYKRGIEAAEAGAACLRINPGNIGDEKRVAEVIKAARDHNCSIRIGVNAGSLEKHLLEKYGEPCPDAMVESGLDHIKILQDHDFHEFKISVKASDVFMSAAAYQMLADATDAPIHLGITEAGGLMSGTIKSAIGLGQLLWMGIGDTLRVSLSADPVEEVKVGFEILKSLGLRHRGVNIISCPSCARQGFDVIKTVETLEERLEHIKTPMSLSIIGCVVNGPGEALMTDVGFTGGGAGSGMVYLAGKASHKMSNDQMIDHIVEEVEKKAAALDAQAAEDMKAAE | Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. | Q1GIC1 |
Q68W81 | RL2_RICTY | 50S ribosomal protein L2 | typhus group | MALKNFNPITPSLRELVQVDKTNLWKGRPLKSLTKGMSKTGGRNQQGRITSWHRGGGHKKLYRVIDFKRKKIDIFAVVERIEYDPNRTAFIALIKYDDGEYSYILAPQKLSIGDRVISSQAADIKIGNCLPLKSIPIGTTLHNVEMKVGKGGQIARSAGTSVELVGKDSGYAQIKLRSGEFRLVPLDCKATIGSISNPDQKNINLGKAGRNRWLGWRPHVRGVAMNPIDHPHGGGEGKTSGGRHPVTPWGFSTKGKKTRKNKRTSKFIVKKRK | One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. | Q68W81 |
Q74IP1 | ACP_LACJO | Acyl carrier protein | Lactobacillus | MTEEEIFNKIADMISERFSIDRDKITKDLNFQNDLDADSIDFVELVMDLEDTFGAEIPDDDAEKLQTVGEAVEYIKSHQN | Carrier of the growing fatty acid chain in fatty acid biosynthesis. | Q74IP1 |
B4R8N0 | RS14_PHEZH | 30S ribosomal protein S14 | Phenylobacterium | MAKKSAVNRNERVKKLVKQYAAKREALKAIANDESLPLEERFEARLKLAELPRNSAAVRIRNRCEVTGRPRAYYRKLKMSRVSLRELGSHGLIPGLVKSSW | Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site. | B4R8N0 |
Q9DC37 | MFSD1_MOUSE | Major facilitator superfamily domain-containing protein 1 | Mus | MEDEDGEDRALLGGRREADSAVHGAPRALSALCDPSRLAHRLVVLSLMCFLGFGSYFCYDNPAALQTQVKRDMQVNTTKFMLLYAWYSWPNVVLCFLGGFLIDRIFGIRWGTVIFSCFVCIGQVIFALGGIFNAFWLMELGRFVFGIGGESLAVAQNTYAVSWFKGKELNLVFGLQLSMARIGSTVNMNLMGWLYGKIEALLGSAGHMTLGVTLMIGCITCIFSLICALALAYLDRRAEKILHKEQGKTGEVIKLRDIKDFSLPLILVFVICVCYYVAVFPFIGLGKVFFMEKFRFSSQSASAINSIVYIISAPMSPLFGLLVDKTGKNIIWVLYAVAATLVSHMMLAFTFWNPWIAMCLLGFSYSLLACALWPMVAFIVPEHQLGTAYGFMQSIQNLGLAVIAILAGMILDSKGYLLLEVFFIACVSLSLLAVVCLYLVNRAQGGNLNYSAKQRERMKLSHPE | Lysosomal transporter which is essential for liver homeostasis . Required to maintain stability and lysosomal localization of GLMP . | Q9DC37 |
E4UYA3 | MEP1_ARTGP | Fungalysin MEP1 | Nannizzia | MHGLLLAAGLLSLPLRVLAHPQPSTSLTSQGVDLNAYRMADRSSYMSSDEMKLEQPSISSLSGGNYVETATEVVKRMMPGVTFRMVDDHYVGESGISHVYFRQTMHGMDIDNSDFNVNIGKDGKVLSFGNSFYTNPTPDKAPVEKRDFSDPMKALHGARKALNLPINADKATIKSMNEHEVMFMGTSGALSDPQGKLCYMAKEDGTLALTWRVETDMGDNWLLSYVDAKDTDKVHNVVDYVSHATYQVYPWPVPDPTEGKRAVLQNPWNLKASPFTWISDGKNNYSTTRGNNAIAQANFDGGSDYLNNYRPNNKNLKFEYPYAPNMSPPKSYIDASVTQLFYSANMVHDLYYMLGFTEKAGNFQVNNRNQGGKGGDFVILNAQDGSGTNNANFATPPDGQPGRMRVYIWTKAKPARDSSFEAGTVIHEYTHGLSNRLCGGPANSACLNGMESGGMGEGWGDFFATAIRLKPNDNRNANYVHGEWVNNSPRGNRMFPYSTSLQTNPLVYTSCNKYNEVHAIGTVWCSILYEVLWNLIDKHGKNDGPTPVFENGVPKDGKYLAMKLVLDGMAIQPCKPTFVQARNAILDADMNLTKGANKCELWKAFAKRGLGTGAKYDPKNRTGSKAVPKECQ | Secreted metalloproteinase that allows assimilation of proteinaceous substrates and probably acts as a virulence factor. | E4UYA3 |
P0CV25 | RLR78_PLAVT | Secreted RxLR effector protein 78 | Plasmopara | MMKTVMMMLAILATAKAEPQLAAASSRVILLLDFKKAYDSVAREFLFLVLLRFEFSPMFVRMLRKLHDGTTARFLVNGELSEPQEVVSGIRQGCSLAPLLFILAAEVLALSIQ | Secreted effector that dos not suppress the host cell death induced by cell death-inducing proteins. | P0CV25 |
P63903 | DCD_NEIMA | Deoxycytidine triphosphate deaminase | Neisseria | MSIKSDKWIRRMSEEFGMIDPFEPNQIKEADGKRIISYGTSSYGYDIRCANEFKIFTNINSTIVDPKNFDPKNFVTVEDDCCIIPPNSFALARTVEYFRIPRNVLTVCLGKSTYARCGIIVNVTPFEPEWEGYVTLEFSNTTPLPAKIYAGEGVAQVLFFESDEICETSYKDRNGKYMGQTGVTLPKA | Catalyzes the deamination of dCTP to dUTP. | P63903 |
A4XLF1 | TRMD_CALS8 | tRNA [GM37] methyltransferase | Caldicellulosiruptor | MVFKVLTLFPEVILQATNFSILKRAQEKGLIKIEAINIRDYTKDKHKRTDDYPYGGGFGMVMTAQPIVDAYESIKSSKPHRVIYLTPQGKKYTQDIAKEFSKEEELVIICGHYEGIDQRVIDLIVTDEISIGDYVLSGGEYAALVLIDSISRLVEGVIEKKSVEEESFSECLLEYPHYTRPYEFRGLKVPEVLLSGNHEKIKKWRRYQSLLKTIKSRPDLINAANLTKEDIEFLIKYCESQKIVL | Specifically methylates guanosine-37 in various tRNAs. | A4XLF1 |
O82598 | TIP13_ARATH | Tonoplast intrinsic protein 1-3 | Arabidopsis | MPINRIAIGTPGEASRPDAIRAAFAEFFSMVIFVFAGQGSGMAYGKLTGDGPATPAGLVAASLSHAFALFVAVSVGANVSGGHVNPAVTFGAFIGGNITLLRAILYWIAQLLGAVVACLLLKVSTGGMETAAFSLSYGVTPWNAVVFEIVMTFGLVYTVYATAVDPKKGDIGIIAPLAIGLIVGANILVGGAFDGASMNPAVSFGPAVVSWIWTNHWVYWVGPFIGAAIAAIVYDTIFIGSNGHEPLPSNDF | Potential aquaporin, which may facilitate the transport of water and small neutral solutes across cell membranes. | O82598 |
Q6G0J2 | LLDD_BARQU | L-lactate dehydrogenase | Bartonella | MIISSTFDYRKAAKRRLPPFLFHYIDGGAYAEETMRRNYADLQALALRQRILRQVGEVDLSIKLFDQRLNLPIVLAPVGLTGMYARRGEVKAARAAVAKGIPFTLSSVSVCSLAEVHAEVGSGFWFQLYVLKDRGFMRDVLERSWLAGVRTLVFTVDMPVPGARYRDAHSGMSGPYAGLRRILQAVVHPHWAWNVGIMGRPHDLGNVSTYLQKKITLEDYVGWLGANFDPSIGWSDLQWIRDFWKGKMILKGILDPQDAREAVQFGADGIVVSNHGGRQLDGVLSTARALPAIAEVVTGDLTILADSGVRSGLDVVRMIAQGADAVMIGRAFIYALAAAGEKGVMHLLDLFANEMRVAMTLTGVRAVKEITHESLASTDALNQ | Catalyzes the conversion of L-lactate to pyruvate. Is coupled to the respiratory chain. | Q6G0J2 |
Q7SZK7 | OFD1_DANRE | Oral-facial-digital syndrome 1 protein homolog | Danio | MSASKEESLSPDEMRQKLYQTFKSRGLLDTLKTQLRNQLIQELQAPVRRGESASRRSADHTDSVLVSACNSVVVDHLRSAGYEYTLSVFQPECGLSKDKVLSSRDVLQIMKISPHMPLYKSLVSNIQSGQSGFLKSLLMELTDHSVYRDCSDNSTQTTSIAAHKESLVEKMQLIDEEYEVLRHRGDRWASVEAKLAEYRKEIQEQAQIELNAKLQHFMDVEIAKVKQEEKERSRKEILELRRDMEKTYELKSEALISREKNAIERLQKHQEIEEKDIYAQRQAVLREIESVRSREMELRQRMEAFDKSCALHEEKVKTMEDLLRRRELSVKTMEDSFEQKLKSELLKYQLELKEENMKRPEKLTENEERIRAEAARLQKEAAVVDAKTEDYERKSSEVKQLLMELESSRSQASLLKQQKELLREQLENMRDYPELKKHTLELQTRISLLKQQLEEKQQHNQRLTQELSAPSHEHLMLQAELRRLEAEHKLEKEELETQKNVLHTQLQHEVQQCALLKTQLMECEERTKWMNTHTEELKLQLQQTQQGPALRGPKSRTVAPEHDSDMVISALSRIRELEQEAERLEEAYRSHQQRALSAEDPTLHRGSQNYSRATAAQQHRVISRSPIFAGRPIEEEHEEFSRTPSPAERLASPPARRLSSTPQSASRSKRRADEEHDEHSLNPECVKGSSNTDRPALMFPERLISPIPAEELSSSISPNSPVMKSTTRHTQSPAKLQEILLSSSSQESSPQPEKITLHDLTEPIQMVSADQPCLLKDCEPELQQDHPDVQISSSSSSSSSSQREEEQQRETHTLQQQPHEEQTQEQRDDAGGHVTSAASPTGGAEEANPLQRYMQMLMQDKQQEQSPNKESSGSHEENLQSESHEHSAGVISHDEADDDFW | Component of the centrioles controlling mother and daughter centrioles length. Involved in the biogenesis of the cilium, a centriole-associated function. The cilium is a cell surface projection found in many vertebrate cells required to transduce signals important for development and tissue homeostasis. Plays an important role in development by regulating Wnt signaling and the specification of the left-right axis. | Q7SZK7 |
A6WUU4 | KDSB_BRUA4 | CMP-2-keto-3-deoxyoctulosonic acid synthase | Brucella | MLQTLKTLTLIPARMASTRLPNKPLADICGKPMIVHVADRAAAAKLGRTVVATDSEEIFAIVTAHGHEAIMTREDHESGSDRIYEALMKVDPAGEFDAVVNVQGDLPTIDPDIIRRALLPLEDGPADIATLGVEIEEESEKTNPSVVKIVGSPLAGNSRLRALYFTRATAPYGEGPLYHHIGLYAYRRSALERFVKLGPSPLEKREKLEQLRALEAGMRIDVELVRTVPLGVDTQADLDRARILVAQGI | Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. | A6WUU4 |
A1JLC3 | MNTH_YERE8 | Divalent metal cation transporter MntH | Yersinia | MLNSRVVDTPPRTSRRIKLSLMGPAFIAAIGYIDPGNFATNIQAGASFGYTLLWVVVWANFMAMLIQLLSAKLGIATGKNLAEHIRDRFPRPAVWAYWVQAEIIAMATDLAEFIGAAIGFKLLLGVTLLEGAVLTGIATFLILMLQKRGQKPLELVIGGLLLFVAAAYIVELVFSRPEIAALGRGMLIPDLPNRDAVFLAAGVLGATIMPHVIYLHSSLTQTAGENSKADRYASTKLDVAIAMTIAGFVNLAMMATAAAAFHFNGYGSIAEIEQAYLTLQPLLGNAAATIFGLSLVAAGLSSTVVGTLAGQVVMQGFVRFYIPIWVRRTVTMLPSFIVILMGMDATRILVMSQVLLSFGIALALVPLLAFTGNKELMGDMVNSKLIQILGKLIVLVVIGLNAYLLVSLI | H(+)-stimulated, divalent metal cation uptake system. | A1JLC3 |
B0BUQ3 | RL16_RICRO | 50S ribosomal protein L16 | spotted fever group | MLAPKKQKFRKAHKGRVASTAKAGTTLAFGSFGLKSIDGWRVTARQIEAGRKAATRCMKRQGRLWIRIFPDVPVSQKPAEVRMGKGKGSPEFFAVRVSPGRIMFEIEGVEENVALRALELASAKLPVRTRIVRRYE | Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs. | B0BUQ3 |
Q6MDC8 | UVRC_PARUW | Excinuclease ABC subunit C | Candidatus Protochlamydia | MSYDPKKIDLFPTLPGVYLMKNEEGEVLYVGKAKNLRQRVKQYFVPGRDGRLMIPYLVAKINYIETIVVTSEKEALLLENNLIKQHKPRYNALLKDDKSYIALKISQNDAWATVRLVRYKGTPEPDGLYFGPYTSAQAARQTLDLLNRLFPLRQCSDQEFARRTRPCLLYQMKRCVGPCTQKCTKGEYQQHLDRTIKFLRGQNKDVLKDLYEEMRLLSEQLEFEKANHLLRTIRYIEKTIESQYVDRPLGHDADAIGLFRYGEHVVVVLMIFRGGKLVGSRHFEFDNIIEEDHELLTSFLLQHYEGATEIPSEILLPSKISDEHPVEEILSARREQKVNLQIPQRGEKKALIEIAQKNAEALFKTQKDEATLREKTLLEMQELLFLTNYPTRIECFDNSNIAGSEPVSSMVAFTDGLKDSKRYRTYRLKIGSKPDDYAAMYEVLTRRYKRAKEENDMPDLVVVDGGKGQLNIAIKVFEELNITGVDLLGLAKEAGRHDKGMTAEQVFTCYQKEPILLKANSPILFLLQKIRDEAHRVAISFHRKRRSKKTLKSALDDIPGIGPAKRKTLLTHFGSLKKIELAADAELREVKGISAANIEAIRTFFQGRKE | 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. | Q6MDC8 |
P28880 | O16A_CONST | SNX-157 | Pionoconus | MKLTCVMIVAVLLLTACQLITAEDSRGTQKHRTLRSTARRSKSESTTRCRSSGSPCGVTSICCGRCYRGKCT | Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels (Cav). In vivo, this toxin is a potent paralytic toxic in lower vertebrate species, but it is much less effective in mammals. | P28880 |
Q74CB0 | DXS2_GEOSL | 1-deoxyxylulose-5-phosphate synthase 2 | Geobacter | MSRILDRVDSPSDLKGLTTAELGILAEEIRQEIITVCSRNGGHLAPSLGVVELTLALHRVFTSPEDKIVWDVGHQAYAHKLVTGRRDRFATLRTLGGISGFLKRAESPHDVFDAGHASTSISAALGLAAARDLAGRNNKVVAVIGDGSMTGGIAYEGLNHAGHLNRDLVVVLNDNEMSIAENVGALSNFLSRTVTSEFVHTLKKDVETFLGGLDRIGRNVLKVAKRAEESLKGLFTPGMLFEAFGFEYIGPIDGHDIGRLTETFEKVKRFDDAVLIHVLTKKGKGFAPAEAKPSLFHGVGPFDPVSGEIVKGKGGATSYTGVFGQALTRIADEDERVVAITAAMPDGTGLGSFSARHPGRFFDVGIAEQHGVTFAAGLAAEGYRPVFAIYSSFLQRAYDQLFHDVCLMNLPVTFAIDRSGVVGSDGPTHHGLFDLSYLRTLPNMVVMAPKDENELQHMLKTAIDHNGPAAVRYPRGNGLGVPLDQSLAPIPLGTSEVLRAGSGTCVVLAVGAMVGPALEAANTLEGEGIDLTVVNVRFVKPLDRELILSYVGRAGTLVTIEENVLQGGFGSAVLELLADEGVGGVAVHRFGYPDRYVEQGEQHELRSRYGLDAEGIAGRIRTLSAR | Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP). | Q74CB0 |
Q88AH6 | FPG_PSESM | DNA-(apurinic or apyrimidinic site) lyase MutM | Pseudomonas | MPELPEVETTRRGIAPHLEGQRVSRVIVRDGRLRWPVPEDLDIRLSGQRIVQVSRRAKYLLIQAEVGTLISHLGMSGNLRLVEAGLAALKHEHVDIELESGLALRYTDPRRFGAMLWSHDPHNHELLIRLGPEPLTDLFDGERLYERSRGKSIAVKPFIMDNAVVVGVGNIYATEALFAAGIDPRREARGISRARYLKLAIEIKRILAYAIERGGTTLRDFIGGDGKPGYFQQELFAYGRGGQPCKVCGTTLREIKLGQRASVYCPKCQR | 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 purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. | Q88AH6 |
P94679 | TSAM1_COMTE | Toluenesulfonate methyl-monooxygenase oxygenase component TsaM1 | Comamonas | MFIRNCWYVAAWDTEIPAEGLFHRTLLNEPVLLYRDTQGRVVALENRCCHRSAPLHIGRQEGDCVRCLYHGLKFNPSGACVEIPGQEQIPPKTCIKSYPVVERNRLVWIWMGDPARANPDDIVDYFWHDSPEWRMKPGYIHYQANYKLIVDNLLDFTHLAWVHPTTLGTDSAASLKPVIERDTTGTGKLTITRWYLNDDMSNLHKGVAKFEGKADRWQIYQWSPPALLRMDTGSAPTGTGAPEGRRVPEAVQFRHTSIQTPETETTSHYWFCQARNFDLDDEALTEKIYQGVVVAFEEDRTMIEAHEKILSQVPDRPMVPIAADAGLNQGRWLLDRLLKAENGGTAP | Involved in the toluene-4-sulfonate degradation pathway. Does not discriminate between the sulfonate and the carboxyl substituents and can also be involved in the p-toluenecarboxylate degradation pathway. Can use toluene-4-sulfonate, p-toluate, m-toluate and 4-ethylbenzoate as substrates, but not p-xylene, toluene and p-cresol. Catalyzes also the demethylation of 4-methoxybenzoate to 4-hydroxybenzoate. | P94679 |
A8GIF8 | XNI_SERP5 | Flap endonuclease Xni | Serratia | MMIHLLIVDALNLIRRIHAVQGSPCVNACQHALQQLIQHSRPTHAVAVFDEDDRSESWRHQILPDYKAGRSPMPDNLQQEMPQLRQAFESLGVACWHSPGNEADDLAATLTAKVAGGGHQVTIVSTDKGYCQLLAPSVQIRDYFQKRWLDMPFVQQEFGVSPQQLSDYWGLAGISSSKIPGVAGIGPKTAVLLLQQAGSLDGLYQDLEQVPEKWRGKLEQHREMAYVSKRVATLRTDLALTGNLQQLRLPV | Has flap endonuclease activity. During DNA replication, flap endonucleases cleave the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. | A8GIF8 |
P52020 | ERG1_RAT | Squalene epoxidase | Rattus | MWTFLGIATFTYFYKKCGDVTLANKELLLCVLVFLSLGLVLSYRCRHRNGGLLGRHQSGSQFAAFSDILSALPLIGFFWAKSPPESEKKEQLESKRRRKEVNLSETTLTGAATSVSTSSVTDPEVIIIGSGVLGSALATVLSRDGRTVTVIERDLKEPDRILGECLQPGGYRVLRELGLGDTVESLNAHHIHGYVIHDCESRSEVQIPYPVSENNQVQSGVAFHHGKFIMSLRKAAMAEPNVKFIEGVVLRLLEEDDAVIGVQYKDKETGDTKELHAPLTVVADGLFSKFRKNLISNKVSVSSHFVGFIMKDAPQFKANFAELVLVDPSPVLIYQISPSETRVLVDIRGELPRNLREYMTEQIYPQIPDHLKESFLEACQNARLRTMPASFLPPSSVNKRGVLLLGDAYNLRHPLTGGGMTVALKDIKIWRQLLKDIPDLYDDAAIFQAKKSFFWSRKRSHSFVVNVLAQALYELFSATDDSLRQLRKACFLYFKLGGECLTGPVGLLSILSPDPLLLIRHFFSVAVYATYFCFKSEPWATKPRALFSSGAILYKACSIIFPLIYSEMKYLVH | Catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, and is considered to be a rate-limiting enzyme in steroid biosynthesis. | P52020 |
Q72TF8 | LGT_LEPIC | Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase | Leptospira | MIDRIPVPFLNPLFKFLFNREWDGPSTFSILMMIGFLTASYLLPKELKRRKLEPEHSDWLLLLGILGTLVGAKIFFVFEIWDQIFVETPGFDGKYIYPLTHWYGFPGRMSLWDNLFSGSGLVFYGGFLFGILFITLYMKYFQLDIASYLDAAVPSMAIGYAIGRLGCWVSGDGCYGFATNVEIPLLVFNYHGAHPSGVPVWNTPLIESIISFLFFFYFQFWARNQNFKKFSIGAQYLVLHGFARLLVEFLRVNKAVFPLMDPPAFVNIPNAEQNPEFLTQYYWHGFSQSQLVSIIIILVGAFFILKWKLWKKENTSNI | Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins. | Q72TF8 |
Q21IQ9 | CHEB1_SACD2 | Protein-glutamate methylesterase/protein-glutamine glutaminase 1 | Saccharophagus | MAYKVLVVDDSQFFQVRLKQIINEHPDLEVVGIAANGQEAIDLEESLRPDIISMDYEMPHLDGISAVRSILSKRPIPIVMFSSMTYEGATITLEALDAGAVDFIPKNFAEVSRDSVVLKKRLHEKLLLFAQKAKPSVAARSTTQPSGVRPSALGANLSSSRSPRPASSAPSAPKKRIKGLVKLVAIGASTGGPVAVSEIITRLPANFPVPVIVAQHMPENFTKAFSERLNRQSAVEVREAQDGDLLKSGVVYVAPGGNQLMVDKTGRSIRILDGDARLTYKPSVDVLFASAASAMGDKVLAIVLTGMGADGCDGAKLLKQKGATIWGQDKDSCVVYGMPAAVAKAGLTDEVLPLDQVWQRLVSDV | Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid. | Q21IQ9 |
A7IMW3 | IDI2_XANP2 | Type 2 isopentenyl diphosphate isomerase | Xanthobacter | MDESGAGRRKEDHIDIVLAGGRVASRLDAGFDRVRFVHCALPELDLDAIDLSTRFLGRPLKAPFLISAMTGGPARAESINAHLAEAAQALGIALGVGSQRIAIEDGSAGGLGADLRRRAPDIALFANLGAAQLLAARGLDAARRAVEMIGADVLVIHLNPLQEAIQQGGDRDWRGVFDRIGSLCVSLSAPVVVKEVGFGLSGAVARRLADCGVAALDVAGAGGTNWALVEGERGTGRSRAVATAFADWGIPTAQAVVEVRAACPDLPLIASGGVRHGVDAAKAIRLGADLVGQAAGTLKAAITSTEAVVEHFSQMTDQLRIACFATGAADLDALRRVPLATMD | Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP). | A7IMW3 |
Q8ZLE2 | ACPT_SALTY | 4'-phosphopantetheinyl transferase AcpT | Salmonella | MYQVVLGKVSTLSAGQLPDALIAQAPQGVRRASWLAGRVLLSRALSPLPEMVYGEQGKPAFSAGAPLWFNLSHSGDTIALLLSDEGEVGCDIEVIRPRDNWRSLANAVFSLGEHAEMEAERPEQQLAAFWRIWTRKEAIVKQRGGSAWQIVSVDSTLPSALSVSQCQLDTLSLAVCTPTPFTLTPQTITKAL | May be involved in an alternative pathway for phosphopantetheinyl transfer and holo-ACP synthesis. The native apo-protein substrate is unknown. | Q8ZLE2 |
Q0I6N5 | MNME_SYNS3 | tRNA modification GTPase MnmE | unclassified Synechococcus | MSGIGPDQALSIAAIATAVAPGQGGIAVIRLSGPSAVRAVAAITVIPGQQVWESHRVLYGHVVAAGGVERLDEVLVLVMLAPRSFTGEDVVEIHCHGGVIAVQQVLARVLEQPGVRRALPGEFSQRAVLNGRLDLTRAEAIGDLVGARSQRAAQLAMAGLDGGIQKKMVVLRERLLDQLSELEARVDFEEDLPPLNGEALLQELQAVRLELLTLVADGERGSVVRHGLRVALVGRPNVGKSSLLNLLSRRERAIVTDLPGTTRDLLESEIVLDGVPITLLDTAGIRATSNAVEKLGIARSRDALASADLVLLLFDLAQGWSDDDQALFALIPEGVPCLRVGNKADLPLKAEPVAETVAASVADVRLSAVTGDGEQALVQAVLERCGALGEQPLLLALNQRQSDLAVTAAEALARSEQVAADGLPWDFWTIDLRQAIRSLGEITGEQLTESVLDRIFSRFCIGK | 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. | Q0I6N5 |
Q5HQL0 | MNHA1_STAEQ | Mnh complex subunit A1 | Staphylococcus | MSLLHIAVLLPLIFALIIPFLYRFVKRIHLGWFVLPVPIVLFIYFISLISMTMSGNNVMKNLNWMPHIGMNFNLYVDGLGLLFSLLITGIGSLVVLYSIGYLSKSEQLGNFYCYLLLFMGAMLGVVLSDNFIILYLFWELTSFSSFLLISFWREKKASIYGAQKSLIITVLGGLSMLGGIILLSLATDTFSIQAMISKASDIQNSPFFILVMILFMIGAFTKSAQVPFYIWLPDAMEAPTPVSAYLHSATMVKAGLYLIARITPIFAISEGWVWTITLVGLITLFWASLNATKQHDLKGILAFSTVSQLGMIMSMLGIGAVSYHYQGANSQLYVAGFVAAIFHLINHATFKGALFMITGGIDHSTGTRDVKKLGGLLTIMPISFTLTVITTLSMAGVPPFNGFLSKEKFLESMINVTHLNLMSLNTLGILLPIIAIIGSIFTFVYSIKFILHIFFGSYKPEALPKQAHESSILMLISPIILTSLVIVFGLFPSILTQSIIEPASVAVSQTSNITAEFHLFHGITPAFLSTIGIYIIGILLLISFSYWVRLLQAHPYQLTLNHWYDTSGQRIPGYSENITNSYVTGFSRNNLVIILGILIALTFVTVISVPFSIDFKNVSHLRVFEGATVLFLLIASTFIIFAKSRLFSIIMLSAVGYAISVLFIFFKAPDLALTQFVVESISTALFLLCFYHLPNLNRYNEKPTFKLTNAVISIGVGLSVIILGLIGYGNRHFDSITKFYQEHVFDLAHGKNMVNVILVDFRGMDTLFESSVLGIAGLGVYTMIKLRLKQKNQSSEVNDHE | Mnh complex is a Na(+)/H(+) antiporter involved in Na(+) excretion. | Q5HQL0 |
A1WRC4 | SYM_VEREI | Methionyl-tRNA synthetase | Verminephrobacter | MPSTRKLFVTTALPYANGPFHLGHLMEYIQADIWVRFQRMQGHEVNFVGADDTHGAPIMIAAEKAGKTPQQFVADIAAGRKPYLDGFHLSFDNWHSTDAPENHELARQIYRDLRDRADGSLIERRSIEQFFDPGKSMFLPDRYIVGECPRCHAKEQYGDNCEQCGSVYAPAELIDPVSALSGAKPELRSSEHFFFKLSDPRCVEFLQRWTQDGKLQPEVANKVREWFGLRSNPDGSCSEGLDDWDISRDAPYFGIEIPDAPGKYFYVWLDAPVGYLAALKNLLEKRGQNYDAYMADPALEQYHFIGKDIVTFHTLFWPAMLHLSGRKTPDNVFVHGFLTINGEKMSKSRGTGLDPLKYLSLGMNAEWLRYYLATKLSARNEDMDLGTEDFMVRVNSDLIGKYVNIASRAAGFLTKRFAGRLTSDFGAAGLALLADLHGARDTIAQWYQAREFGKATREIMLLADKVNAYVDRNKPWELAKDAANGQALHQVCSVLINAFATLTRYLSPVLPALARAAQDFVGQDMQRWDAGGAVQAIAPYQHLMQRVTPEQLAALFQPPAAAQIAAAGAQEPGGLALAPGIGIDDFDRVDLRVALIVDCAAVAGSTKLLRLTLDIGEGRQRQVFSGIASACQPADLIGKHTVMVANLAPRRLKFGVSEGMVLAASHGDEKANPGIYLLAPGPGAKPGMRVR | Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | A1WRC4 |
Q3JVC1 | PLSY_BURP1 | Lysophosphatidic acid synthase | pseudomallei group | MQILLATVAAYLIGSVSFAVVVSAAMGLADPRSYGSKNPGATNVLRSGNKKAAILTLVGDAFKGWLAVWLVKRFGIGGEIGVALAAIAVFLGHLYPVFFRFQGGKGVATAAGVLLAVHPVLGLATALTWLIVAFFFRYSSLAALVAAVFAPIFDVFLFGTHDNPVAWAVLAMSVLLIWRHRSNISKLLAGEESRIGQKKKTGA | Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP. | Q3JVC1 |
Q4WQ14 | PRM1_ASPFU | Plasma membrane fusion protein prm1 | Aspergillus subgen. Fumigati | MLFSRSGRSIFPLLPPYAAHAPNPNQGHIIALPPDGLTPYLGLRARLSQVWINRWTILLLLVLVRVLLAASGLQADMSTAKREALSACTSVESMGSSMASMPHYLSQGVNELTATGVEKAVSGLKSMLMLTITGVEELVLFIIKVLYQTYLCLFTLAVRGSVHVAVGVIKEAADFLNSTVKEVGDDIGKAVSTFESAFNKFLDGVNTVASAFGASVPTLDLNSSISTLENLQLPSSIDQGLDKLNSSLPTFDEVNNFTQTVLRTPFEEVKKLVNESLGTYTFDRSLLPVPAKEQLTFCEGSNGIDSFFDSVTDLVMKARKIFIAILIVAATLACVPMAWQEIRRWRSMKERSQLVRKEAHDPMDVVYIVSRPYTAAAGIKAASRFSNSRRQILVRWAIAYATTPAALFVLCLGVAGLLSCLCQYLLLQAVEKTVPELSTQVGAFADKVVDSLQNASAEWANDANGVIGHMSQDLNENVFGWVNTSTTALNDTLNTFVDKTTGVLNDTFGGTLLYEPLMDVFGCLIGLKVQGIQKGLTWVHDHAHIDFPLLPNDTFSRGAAASISSNSSNPSDSFLADAGDQTSNKITEVVIRVVNKVEDGIRTETIISGVIILIWVFIALIGIVRALTLFWVRDRNRGEGGGARVNHHLSDAGGFIDVPLTAVSNTNTDARSMPPPAPAPRYEASTSTVVASRAVPVSSTHHEDEKLGFAGERQYGSALKVDGAADLRGSSYVEYDMEKR | Involved in cell fusion during mating by stabilizing the plasma membrane fusion event. | Q4WQ14 |
A4QLL4 | PSAJ_LOBMA | PSI-J | Lobularia | MRDLKTYLSVAPVLSTLWFGSLAGLLIEINRLFPDALTFPFFSF | May help in the organization of the PsaE and PsaF subunits. | A4QLL4 |
Q8EH98 | RPPH_SHEON | (Di)nucleoside polyphosphate hydrolase | Shewanella | MIDSDGFRANVGIIICNRYGQVMWARRFGQHSWQFPQGGVDDGESAEEAMYRELYEEVGLRPEHVTVLTSTRSWLRYRLPKRLVRQDSKPVCIGQKQKWFLLQLKSQDSAINLSSSGHPEFDDWRWVSYWYPVRQVVSFKRDVYRKVMKEFAVTALSFQTQEIPKKRVRQKTTG | Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage. | Q8EH98 |
Q01Q48 | MURG_SOLUE | Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase | Candidatus Solibacter | MTHQQTLPTTAASFLMAGGGTGGHVIPALAVARELRSRGHKVFFVGTQHGMEARLVPPEGFEFKTIEIGGLNQVSWNQKFATLSRLPITTLKCGRSVRDASAVFSMGGYVAGPPVMAALVRRVPVVVMEPNAFPGFTNRVIARLVSRALVSFPETAAFFPKGRTEVTGLPVREEFFRIPPKARGDVLQILITGGSQGSRTLNHAARQSWPLFRNSGYPVRITHQTGTGSFQEIRDAFAQSGLEGEVVPFIADMPAAFAAADLIVCRSGAGTVSELAAAGKPSILVPFPFAADDHQTRNAQSLERAGAARLVRDAEMTGEKFFEVVTSVTGELSRMGTAARQFAKPGAAKRAADILEEVARP | Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II). | Q01Q48 |
Q081G4 | CLPS_SHEFN | ATP-dependent Clp protease adapter protein ClpS | Shewanella | MAKLGNVEHIEEKVESELQPPHMYKVVLNNDDYTPMDFVVEVLQRFFEKNEQQAVDIMLAIHNQGKGLCGVFPFGIAETKVFQVNQFARENQHPLLCTLEKV | Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation. | Q081G4 |
Q6A7V7 | BIOB_CUTAK | Biotin synthase | Cutibacterium | MTERGLRGESITREEALEILRSSDDELMSIIAAAGKVRRHFFDNRVRLNYLVNLKSGLCPEDCSYCSQRLGSRAEIMKYSWADPQKVHDAVEAGIAGGARRVCMVASGHGPSRRDVERVNGMVRSLKADHPDVEVCVCLGFVDDEKAASIKEAGADAYNHNANTARSHYGKICSTHSYEDRMDTVEVLKRNGLSPCSGVIAGMGETDEEFVDVIFDLRKHGVDSVPVNFLLPFEGTPLAGGAQHITPQWCLKRLAMVRFAHPDSEVRAAAGREQHIRTMQPLALEVVNSIFLGDYLTSEGAAGAADLQMIEDGGFIPEGADGQPMVHTDVNSHHSANLPVNAVPIRHRGIGTEVPANA | Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism. | Q6A7V7 |
Q493X5 | UPPP_BLOPB | Undecaprenyl pyrophosphate phosphatase | Candidatus Blochmannia | MSMIYITLNIIAYVIDVRSLILDVRRLVFSLILGIVEGLTEFLPISSTGHMILVENILNCMDDSVIAFTVIIQLGAILSITKIFWSQLYGMSMICIKKIFFKQHDDHNHLCIRHIFLGTFPGIMLGMIFYEKIGLIFELTYIMYGLIIGGIFLLVGELCASKEPRVSRINNITYLQAFLIGCFQCLAFWPGFSRAGATIGGGLVVGLDRRISSEFSFFLAVPIIFGSAVLTLYHYRSCIGLMDVLLLIAGSATAFFIALFTVRYFLKIVKNVSLIPFAIYRFLLAGGIYWGLMT | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | Q493X5 |
P0CAW7 | SECA_CAUVC | Protein translocase subunit SecA | Caulobacter | MLGFAKKLFGSSNERKVKTLATRVAKINAYEAEYAALSDEALKGKTAEFKARLEKGETLDDILNEAFAVVREASKRVLGMRHFDVQMVGGMVLHFSGISEMRTGEGKTLVATLPTYLNALEGKGVHVITVNDYLARRDADWMGQVYNFLGLSYGVIVNGLSQGERQRAYRSDITYGTNNEFGFDYLRDNLVYSVDEMVQRGHNFAIVDEVDSILIDEARTPLIISGPTEDRSSFYKTIDVLVKELILDKSMFDHDEKQKQVILTEDGQEKIEEILMSGGHLAEDSAGLYDAANVSVVHHVNQALRANILYTRDKDYIVKGGEVVLIDEFTGRMMTGRRLSEGLHQAIEAKEGADIQPENQTLASVTIQNYFRLYKKLSGMTGTASTEAQEFDDIYKMSVSEIPTNRTIQRIDDDDEVYRTEREKNEAILKQIADCHVRGQPILVGTVSIEKSEELSKLLSTFSFEKDGKKVKGIPHQVLNARFHEQEAVIVADAGVPGAVTIATNMAGRGTDIQLGGSIDMRLFNWRQQQRGMGLEITVEDEAEERARLETEIADKKAQALAAGGLFVLGTERHESRRIDNQLRGRTGRQGDPGRSKFFLSCEDDLLRIFAGERLDAIMRTFGVQEGEAITHKWLNNAIATAQKRVEQRNYEIRKNLLKYDDVVNDQRKAVFEQRQEFMESSDLSDIIHEMRRDVIDDLVLRHLPPKAYAEQWDVEGLTERVKSILGLDLPIAEWAAEEGIADEEMKERITKAADEYAAQREVIITPEQMRSVEKSFLLQMIDLQWREHLMHLDHLRNVIGLRGYGQRDPLNEYKTEAFSLFEKLLGDLRTNTTRWLMTVEIAYAEPEVPHTPLDNLVEVHLDPLTGENAAFAGGIPEGLSTAQREALPVSALPEGWDRTNRNAPCPCGSGKKFKQCHGSLVR | 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 driving the stepwise translocation of polypeptide chains across the membrane. | P0CAW7 |
A9M4L8 | MUTS_NEIM0 | DNA mismatch repair protein MutS | Neisseria | MSKSAVSPMMQQYLGIKAQHTDKLVFYRMGDFYEMFFDDAVEAAKLLDITLTTRGQMDGVPIKMAGVPFHAAEQYLARLVKLGKSVAICEQVGEVGAGKGPVERKVVRIVTPGTLTDSALLEDKETNRIVAVSPDKKYIGLAWASLQSGEFKTKLTTVDKLDDELARLQAAEILLPDSKNTPQLQTASGVTRLNAWQFAADAGEKLLTEYFGCQDLRGFGLDGKEHAVAIGAAGALLNYIRLTQNLMPQHLDGLSLETDSQYIGMDAATRRNLEITQTLSGKKSPTLMSTLDLCATHMGSRLLALWLHHPLRNRAHIRARQEAVAALESQYKPLQCRLKNIADIERIAARIAVGNARPRDLAALRDSLFALSEIDLSANGSSLLETLKAVFPETLPVAETLKAAVMPEPAVWLKDGNVINHGFHPELDELRRIQNHGDEFLLDLEAKERERTGLSTLKVEFNRVHGFYIELSKTQAEQAPADYQRRQTLKNAERFITPELKAFEDKVMTAQEQALALEKQLFDGVLKNLQTALPQLQKAAKAAAALDVLSTFSALAKERNFVRPEFADYPVIHIENGRHPVVEQQVRHFTANHTNLDHKHRLMLLTGPNMGGKSTYMRQVALIVLLAHTGCFVPADAATIGPIDQIFTRIGASDDLASNRSTFMVEMSETAYILHHATEQSLVLMDEVGRGTSTFDGLALAHAVAEHLLQKNKSFSLFATHYFELTKLPEAHATAVNMHLSALEQGQDIVFLHHIEPGPASKSYGIAVAKLAGLPVRALKSAQKHLNELEDQAAANRPQLDIFSTMPSEKGDEPNVDSFVDKAEEKHFEGILAAALEKLDPDSLTPREALSELYRLKDLCKSVS | This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity. | A9M4L8 |
A7HP87 | CAS2_PARL1 | CRISPR-associated endoribonuclease Cas2 | Parvibaculum | MWVIAMFDLPTDTPKARKAYARFRKDLLEDGFTMMQYSVYSRHCASIENAEVHVKRMGAVVPAQGEVRFLTITDNQFGRIKVYVGKKRQPTTQSPSQLQLF | CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease. Involved in the integration of spacer DNA into the CRISPR cassette. | A7HP87 |
A4JPG9 | HCP_BURVG | Prismane protein | Burkholderia cepacia complex | MFCYQCEQTDRTGARPGCATAKGNCGKDETTADLQDLLIHAVKGIAQYGALARTMGVRDREADRFVLYAMFTTLTNVNFHAARFVALLREAAQTRDRVKAACDAQARATGAALPALQGPAAWQPADDLPGLLKQAAAVGIDAGLDTVGADIVGLRALVLYGLKGVCAYAHHARVLGYERDDIYEGIEAALAFLATDPTDVNALLEQALDLGRLNLTVMELLDSANTGRFGAQQPSAVRVSPVAGKAILVSGHDLGDLHALLEQTAGTGINVYTHGEMLPAHAYPALNAFPHLVGNYGGAWQDQQSDFAHFPGPILMTSNCIIEPLPQYRQRIFTTGPVGWPGVRHLEHHDFSTLIRAAQALPGFPATAPEETITVGFGRHAVLGVADKVIDAVKAGQIRHFFLIGGCDGAAPGRNYYTEFAEQAPDDTVVMTLGCNKYRFNRHAFGDIGGIPRLLDVGQCNDSYSAIRIATALADAFECGVNDLPLSLVISWFEQKAAAVLLTLLALGIRNIRLGPTLPAFITPGVLNVLVDQFGIQPIGDASADLAAALSRQAA | Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O. | A4JPG9 |
C7MWX8 | MSHC_SACVD | Mycothiol ligase | Saccharomonospora | MQTWSSVAVPRVPGTSRPLRLYDTATGQIRPTAPGRVAKMYVCGITPYDATHLGHAATYLAFDLVHRLWLDAGHEVHYVQNVTDIDDPLLERAERDSEDWVVLGLRETALFREDMEALRVLPPRDFVGAVESIPEVVEMIEKLLASGAAYRVDDPEYPDVYFDRSFTGRFGYESNYDDETMRAIFPERGGDPDRPGKRDPLDALLWRVERPGEPAWDSSLGRGRPGWHIECSAIALKHLGIGFDVQGGGSDLVFPHHEFSAAHAEAMTGEHPFARHYVHAGMIGLDGEKMSKSKGNLVFVSRLRADDVDPSAIRLALFAGHYRDDREWTDELLKQANSRLARWREAVSLPSGPDAEATVDRLRDHLADDLDTPKALAAVDAWVDEALRHRSGTVGSESAPALVRAAVDSLLGVVL | Catalyzes the ATP-dependent condensation of GlcN-Ins and L-cysteine to form L-Cys-GlcN-Ins. | C7MWX8 |
P44399 | FUCK_HAEIN | L-fuculose kinase | Haemophilus | MAIALIFDCGATNLRTIAINEKGQILASHHLANNTKQGIESSDYHIWDIEEIWQKLTSCATQTLNQLMQQGIDLKDIVGISVTTFGVDGAPFDENDQQLYPIISWKCPRTIPVMENLSNQLDIKSLYQRNGIGQYSFNTLFKLHWLKTHKPDVFQKMAKFVFISSMLTQRLTGQFTTDHTMAGTSMMTNLTSGNWDPSILASLGLSNNHFPPMRYAGEKVGKLRTPLAQKWGLNPVPVISCGHDTQFAVFGSGAGLNQPVLSSGTWEILMARTQHAEPRFEFVSQGLTTEFDAQSNCFNPAVQWVGSGVIEWLGKLLFSDVYGSDHYYTTMIKEGEKAFNAGKRAVNFEGIFSQLGQGNISGLSMFATRGEIYVSALQHMANKLKNGLSVLHQVSQFQAKSLICVGGGSKNVLWNQIRANTLNLPIDVVDISESTVLGAAMFTFAGVGIYENVNAAQQAMQPTRKRIYPN | Catalyzes the phosphorylation of L-fuculose. | P44399 |
Q6D6A4 | TRHO_PECAS | tRNA hydroxylation protein O | Pectobacterium | MPVLHNRVSNEELKARMLAETEPRTTVSFYKYFTIDDPKAFRDRLYIQLEQYKVFGRIYIAAEGINAQISVPNNQFDAFKTGLFSAHPALDQIRLNIALEDDGKSFWVLRMKVRERIVADGIDDPTFNPANVGQYLKADRVNAMADDPDTVFVDMRNHYEYEVGHFQNALEVPSDTFREQLPMAVDMLDDIRDKNIVMYCTGGIRCEKASAYMLHHGFKNVYHVEGGIIEYARQAKAQGLPLKFIGKNFVFDERMGERISDDVIAHCHQCGASCDSHTNCRNEGCHLLFIQCPSCAAKYEGCCSTQCQDEMKLPLEEQRAIRSGRENGMKIFNKSKGLLQSTLHIPAPAAKDNAE | Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs. | Q6D6A4 |
Q15R07 | ISPH_PSEA6 | 4-hydroxy-3-methylbut-2-enyl diphosphate reductase | Pseudoalteromonas | MQIHLANPRGFCAGVDRAITIVERALEIFSPPIYVRHEVVHNKFVVDGLKERGAVFVDELVEVPDDSIVIFSAHGVSQAVRNEASSRGLKVFDATCPLVTKVHMEVMRASSKGTECVLIGHQGHPEVEGTMGQYDNQDGGIYLVESVDDVARLEVKNPSALYYCSQTTLSVDDTADVIDALRAKFPAIEGPRKDDICYATQNRQDSVRELSADCDILLVVGAQNSSNSNRLRELAEKIGAKAHLIADANCIQKEWLANAKHIGVTAGASAPEVLVQGVVDRLKEWGASSATERPGRLENIEFAVPKELRVKQVS | Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis. | Q15R07 |
Q9UGP5 | DPOLL_HUMAN | DNA polymerase kappa | Homo | MDPRGILKAFPKRQKIHADASSKVLAKIPRREEGEEAEEWLSSLRAHVVRTGIGRARAELFEKQIVQHGGQLCPAQGPGVTHIVVDEGMDYERALRLLRLPQLPPGAQLVKSAWLSLCLQERRLVDVAGFSIFIPSRYLDHPQPSKAEQDASIPPGTHEALLQTALSPPPPPTRPVSPPQKAKEAPNTQAQPISDDEASDGEETQVSAADLEALISGHYPTSLEGDCEPSPAPAVLDKWVCAQPSSQKATNHNLHITEKLEVLAKAYSVQGDKWRALGYAKAINALKSFHKPVTSYQEACSIPGIGKRMAEKIIEILESGHLRKLDHISESVPVLELFSNIWGAGTKTAQMWYQQGFRSLEDIRSQASLTTQQAIGLKHYSDFLERMPREEATEIEQTVQKAAQAFNSGLLCVACGSYRRGKATCGDVDVLITHPDGRSHRGIFSRLLDSLRQEGFLTDDLVSQEENGQQQKYLGVCRLPGPGRRHRRLDIIVVPYSEFACALLYFTGSAHFNRSMRALAKTKGMSLSEHALSTAVVRNTHGCKVGPGRVLPTPTEKDVFRLLGLPYREPAERDW | DNA polymerase that functions in several pathways of DNA repair . Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA . Also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination . Has both template-dependent and template-independent (terminal transferase) DNA polymerase activities . Has also a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity . | Q9UGP5 |
Q99JY0 | ECHB_MOUSE | Beta-ketothiolase | Mus | MTTILTSTFRNLSTTSKWALRSSIRPLSCSSQLHSAPAVQTKSKKTLAKPNMKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRKMMLDLNKAKTLGQRLSLLSKFRLNFLSPELPAVAEFSTNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSDIVPFKVPGKDTVTKDNGIRPSSLEQMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAQNYMGRKTKVGSPPLEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGGQYALVAACAAGGQGHAMIVEAYPK | Mitochondrial trifunctional enzyme catalyzes the last three of the four reactions of the mitochondrial beta-oxidation pathway. The mitochondrial beta-oxidation pathway is the major energy-producing process in tissues and is performed through four consecutive reactions breaking down fatty acids into acetyl-CoA. Among the enzymes involved in this pathway, the trifunctional enzyme exhibits specificity for long-chain fatty acids. Mitochondrial trifunctional enzyme is a heterotetrameric complex composed of two proteins, the trifunctional enzyme subunit alpha/HADHA carries the 2,3-enoyl-CoA hydratase and the 3-hydroxyacyl-CoA dehydrogenase activities, while the trifunctional enzyme subunit beta/HADHB described here bears the 3-ketoacyl-CoA thiolase activity. | Q99JY0 |
Q83GG2 | ISPT2_TROWT | Isoprenyl transferase 2 | Tropheryma | MGGKMLRSVSELIYKVYARYLLGQINLNNLPGHVALIVDGNRRWARKEKRDRISDGHRAGAGKAVDFLHWCDELDINIVTLYLLSNDNLKNRNRQELNDLVQVICDLIAQVSKRWKVNHVGSCENLPELLGNSLEGVKSSTKTNRYSERSMTVNLAIGYSGRAEITEAVRKIVNTYPIGDLPEKITEEVISANLYTGGLSDPDLIIRTSGEQRLSDFMPWQSTHSEFYFLEALGPDLRKVDFLRAIRDFSIRRRSFGA | Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids. | Q83GG2 |
B1NWH0 | PSAJ_MANES | PSI-J | Manihot | MRDLKTYLSVAPVISTLWFGSLAGLLIEINRFFPDALTFPFFSF | May help in the organization of the PsaE and PsaF subunits. | B1NWH0 |
Q112X4 | THIG_TRIEI | Thiazole synthase | Trichodesmium | MQTVEKLTTETLEKPLIIAGKKFTSRLMTGTGKYPTIETMQQSIEASKCEIITVAVRRVQTQAPGHKGLAEAIDWQKVWMLPNTAGCQTAEDAVRVARLGREMAKLLGQEDNNFVKLEVIPDSKYLLPDPIGTLQAAEQLIKEGFAVLPYINADPLLAKRLEEAGCSTVMPLGSPIGSGQGIQNAANISIIIDNSTVPVVIDAGIGTPSEATQAMEMGADALLINSAIALAKNPPIMAKAMGMATESGRLAYLAGRIPKKSYATPSSPVTGKINTTTSE | Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S. | Q112X4 |
Q5LBD7 | HIS6_BACFN | ImGP synthase subunit HisF | Bacteroides | MLAKRIIPCLDIKDGQTVKGTNFVNLRQAGDPVELGRAYSEQGADELVFLDITASHEGRKTFAELVRRIAANISIPFTVGGGINELSDVDRLLNAGADKISINSSAIRNPQLIDDIAKHFGSQVCVLAVDARQTGNGWKCYLNGGRIETDKELRTWTKEAQERGAGEVLFTSMNHDGVKTGYANEALAELASQLSIPVIASGGAGRMEHFRDAFTLGKADAALAASVFHFGEIKIPELKSYLCGQGITVR | 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. | Q5LBD7 |
Q0KBK5 | TIG_CUPNH | PPIase | Cupriavidus | MSNVIENLGKLDRKVTLAIPKAEVEKEKQERLVRLSKTVKMSGFRPGKVPMKMVEKQYGQQVEFEVRFDKAARKFFDITKEQDVKVAGQPKFEIKNEGVGEDEVAFDATFEVYPEVTIGDLSAAEVTRTGTEITDAEVDKTIDILRKQRVHYHARGEAGEHGDGGADVAAQNGDRVTLDFVGKIDGEEFAGGKAEDFPFVLGEGRMLPEFEQAALGLKVGESKTFPLAFPEDYHGKEVAGKTAEFTVTLKKIEWAHLPEVNDAFAKSLGIADGSVEKMRADIRENLEREVKRRTHSMLKDQVMEALLKASELEVPKALIEQDQERLVEMARRDLEQRGMPNAKDMPIPAEMFAQQAERRVKLGLILAEIVKANGLEAKADQIKAEIEDFAKSYEDPKEVMRWYYGDQQRLAEMEAYVLENNVVNFVCGKAKVTDKKVSFEELTAEGNQQQA | Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase. | Q0KBK5 |
A1SF35 | ACPS_NOCSJ | 4'-phosphopantetheinyl transferase AcpS | Nocardioides | MIVGVGIDVVDVARFGVSLSRTPGLTDRLFTPEEAERPLASLAARFAAKEALAKALGAPEGMHWHDAEIRSEESGRPVFEIRGSVLRRANDLGVGSVHVSLSHDAGIASAVVVLES | Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein. | A1SF35 |
Q3KFL8 | MINC_PSEPF | Probable septum site-determining protein MinC | Pseudomonas | MSQTEPKDQDPVFQLKGSMLAITVLELSRNDLDSLDRQLAAKVAQAPNFFSNAPLVLALDKLPPSEGAVDLPGLMRVCRQHGLRTLAIRASRIEDIAAAIAIDIPVLPPSGARERPLESAEPVAPKKPEKPPEPTVKPTRVITTPVRGGQQIYAQGGDLVVVSSVSPGAELLADGNIHVYGPMRGRALAGVKGDTKARIFCQQLSAELISIAGHYKVSEDLRRDPMWGSGVQVSLSGDVLNIIRL | Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization. | Q3KFL8 |
Q6X632 | GPR75_MOUSE | Probable G-protein coupled receptor 75 | Mus | MNTSAPLQNVPNATLLNMPPLHGGNSTSLQEGLRDFIHTATLVTCTFLLAIIFCLGSYGNFIVFLSFFDPSFRKFRTNFDFMILNLSFCDLFICGVTAPMFTFVLFFSSASSIPDSFCFTFHLTSSGFVIMSLKMVAVIALHRLRMVMGKQPNCTASFSCILLLTLLLWATSFTLATLATLRTNKSHLCLPMSSLMDGEGKAILSLYVVDFTFCVAVVSVSYIMIAQTLRKNAQVKKCPPVITVDASRPQPFMGASVKGNGDPIQCTMPALYRNQNYNKLQHSQTHGYTKNINQMPIPSASRLQLVSAINFSTAKDSKAVVTCVVIVLSVLVCCLPLGISLVQMVLSDNGSFILYQFELFGFTLIFFKSGLNPFIYSRNSAGLRRKVLWCLRYTGLGFLCCKQKTRLRAMGKGNLEINRNKSSHHETNSAYMLSPKPQRKFVDQACGPSHSKESAASPKVSAGHQPCGQSSSTPINTRIEPYYSIYNSSPSQQESGPANLPPVNSFGFASSYIAMHYYTTNDLMQEYDSTSAKQIPIPSV | G protein-coupled receptor that is activated by the chemokine CCL5/RANTES. Probably coupled to heterotrimeric Gq proteins, it stimulates inositol trisphosphate production and calcium mobilization upon activation. Together with CCL5/RANTES, may play a role in neuron survival through activation of a downstream signaling pathway involving the PI3, Akt and MAP kinases. CCL5/RANTES may also regulate insulin secretion by pancreatic islet cells through activation of this receptor. | Q6X632 |
A1ALM1 | KUP_PELPD | Probable potassium transport system protein kup | Pelobacter | MKHGETDSYWGGIIKSMGLVFGDIGTSPIYTLTVIIALTKPTQDNILGIISLIVWTLIILVHLEYAVLAMSLSRKGEGGEIVLREILVRMIKPGRQMAFVTFLTYLGVALLMGDGVITPAISILSAVEGTLLIPGLGGLSQNTLILIAGTIALFLFVFQYKGTDKVARAFGPIMVLWFAALALSGAISVSSHPGILAAISPHHAISFLMHNGLPGFFVLSEVILCATGGEALYADMGHLGRKPVKRAWYFVFVALVINYLGQGAFIITHPDAKNILFGMLQYQAPLFYIPFLILTILATIIASQALISGVFSIVYQGINTRMLPLLKVDYTSNQLKSQIYIGSVNWLLLCLVILIMLVFRKSANLAAAYGFAVTGTMVITGIMMTMIFSRTTKKWKVPLALFVTLVDVVFLVSNCNKLPHGGYWSLILASVPLAVILIWTRGQRGLYLALRPLDLETYLLSYEQIYKKGRIAGTGLFFVKEWNIIPPYLVHCTIRSNIVYERNVLISIVRTDEPFGVESVLECGIGTGLDGFMIKAGYMEIFDIELLLKQNGIQEKVIFYGIEDIATTNPIWRVFSVIKKLTPNFVQFNKVPAAKLQGVITRVEM | Transport of potassium into the cell. | A1ALM1 |
B2HIH1 | LEU3_MYCMM | Beta-IPM dehydrogenase | Mycobacterium | MKLAIVAGDGIGPEVVAQAVKVLDVVQPGVEKTNYDLGARRFHATGEILPDSVIAELREHDAILLGAIGDPSVPSGVLERGLLLRLRFELDHHINLRPGRLYPGVKSPLALEPGNPEIDFVVVREGTEGPYTGNGGAIRVGTANEVATEVSVNTAFGVRRVVRDAFERAMRRRKHLTLVHKNNVLTFAGSLWWRTVQEIGEEYPDVELAYQHVDAATIHMVTDPGRFDVIVTDNLFGDIITDLAAAVCGGIGLAASGNIDATRTNPSMFEPVHGSAPDIAGQGIADPTAAIMSVSLLLAHLGLDDAASRVDRAVEGYLATRGNERLATAAVGERIAAAL | Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. | B2HIH1 |
Q31YR1 | CBPA_SHIBS | Curved DNA-binding protein | Shigella | MELKDYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPDAEARFKEVAEAWEVLSDEQRRAEYDQMWQHRNDPQFNRQFHHGDGQSFNAEDFDDIFSSIFGQHARQSRQRPAARGHDIEIEVAVFLEETLTEHKRTISYNLPVYNAFGMIEQEIPKTLNVKIPAGVGNGQRIRLKGQGTPGENGGPNGDLWLVIHIAPHPLFDIVGQDLEIVVPVSPWEAALGAKVTVPTLKESILLTIPPGSQAGQRLRVKGKGLVSKKQTGDLYAVLKIVMPPKPDENTAALWQQLADAQSSFDPRKDWGKA | DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM. | Q31YR1 |
A9VQ50 | TPIS_BACMK | Triose-phosphate isomerase | Bacillus cereus group | MRKPIIAGNWKMNKTLAEAVSFVEEVKGQIPAASAVDAVVCSPALFLERLVAKAEGTDLQVGAQNMHFEKNGAFTGEISPVALSDLKVGYVVLGHSERREMFAETDESVNKKTLAAFEHGLTPIVCCGETLEERESGKTFDLVAGQVTKALAGLTEEQVKVTVIAYEPIWAIGTGKSSSSADANEVCAHIRKVVAEAVSPEAAEAVRIQYGGSVKPENIKEYMAQSDIDGALVGGASLEPASFLGLLGAVK | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | A9VQ50 |
Q49XF7 | RBSD_STAS1 | D-ribose pyranase | Staphylococcus | MYKTGILNSDISKLLSDLGHTDEIMIADCGLPIPNGVKKIDLALDFGKPSFLDVFHIVKSHMAIEKMTLASEMKTENESLYNVLKEEEIKFTTESHELLKQHSKHVKAIIRTGEAKPYANVILASDVLF | Catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose. | Q49XF7 |
Q5JDB6 | TRUD_THEKO | tRNA-uridine isomerase D | Thermococcus | MDYREFFSQFKHLSEKPGIGGKIKIYPEDFIVIEEPIPSIFEGRKYAIFLLKKRNWETMAAVKEIAKRAGINYREIGFAGTKDRHAVTYQYISVPAEARERVEQVSIRDIELRFVSYGRFIKLGHLLGNRFRIIVRDVSEDAFDRTKEIVRELREKGGFPNYFGYQRFGERRVVNHIIGKLLLQGDFEGAARLFLGAHDGSMEGDEARKNFWETGDVERALEEFPGFLRYERTLLHRYKDTGNWKRAFLSLPLPIMRIFIHAYQSYLFNLYLSRRIEEGLPLNEPLVGDIVVQVKGGIPYRDRTYRVTETNLEFVREKVRKNQAMVSGPLFGFAMRRAKGLPGELEKEILEEEGLSLETFRRLPKPMAEPGGRRELLLRPMGMAYGYIQEEGMCFRFFLPKGTYATSVLREIMKDH | Could be responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs. | Q5JDB6 |
Q8KBZ7 | HPRK_CHLTE | HPr(Ser) kinase/phosphorylase | Chlorobaculum | MNFDQKGLKKRSITVAYFFEHIQKRFDIKFRRLNELDEQKCRIHERDLHRPGLAIAGFTKLFTYKRVQILGNTETRYLNHLSDEERKTAFANFVSFRMPCIILTSNNKLDQELVDMATGAGIPVFITRCSSTKTIYYITDFLDEEFSLYQQYHGSMIDVYGVGVLLTGKSGLGKSEVALDLIERGHGLVADDVVVVKRKGETKTLVASRNNIIDHFMEIRGLGVVDVRQNFGIRAIRDRKEVQVVVELLEWSKESEYERLGLDQKMVKLLGVDLPLVQLPIFPGKNITAIIEVVALNFLLKHYAGYVPAEALTERIRNVINKERAKAPAPSTSFEEYNDEND | Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr). | Q8KBZ7 |
A9BMV7 | NDK_DELAS | Nucleoside-2-P kinase | Delftia | MAIERTLSIIKPDAVAKNVIGQIYARFEGAGLKVIAAKMVHLSRGEAEQFYGVHKERPFFKDLVDFMVSGPVMIQALEGENAILKNRELMGATDPKKAEKGTIRADFADSIDANAVHGSDAAETAAVEVAFFFPGMNVYSR | 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. | A9BMV7 |
A6LF29 | ISPF_PARD8 | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase | Parabacteroides | MKIRVGFGYDVHALVPDRELWLGGIKIEHTLGLLGHSDADVLIHAICDALLGAANMRDIGYHFPDTAGEYKNIDSKILLRDTMRLLREAGYELGNIDATVAAERPKLNPHIPLMKKTLAEVMNVDEEDISIKATTTEKLGFTGRQEGISAYATVLIQRMGS | Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). | A6LF29 |
B4UDT1 | RPOC_ANASK | Transcriptase subunit beta' | unclassified Anaeromyxobacter | MKDIFNFFEKPKDPLSFSAIRISLASPDKIRQWSHGEVKKPETINYRTFKPERDGLFCAKIFGPVKDYECNCGKYKRMKHRGVVCEKCGVEVIQSKVRRERLGHITLATPVAHIWFLKSLPSRIGNLLDITLKDLEKVLYCESYIVIDPKETTFQRGELLSEDRYQKALDEFGDDAFSAGMGGEAVLGLLRGVGPASKEHGEGIPGLANELRAEMKEATSDAKRKKIAKRLKVVEAFVASGNKPEWMMLEVIPVIPPDLRPLVPLDGGRFATSDLNDLYRRVINRNNRLKRLQELNAPDIIIRNEKRMLQEAVDALFDNGRRGKTITGPNKRPLKSLSDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPELKLHQCGLPKIMALELFKPFIYNKLEEKGYVTTIKSAKKMVEKERPEVWDILDEVIREHPVLLNRAPTLHRLGIQAFEPVLIEGKAIQLHPLVCTAFNADFDGDQMAVHVPLSIEAQMEARVLMMSTNNILSPAHGKPIIVPSQDIVLGIYYMTRERAFARGEGKVFASPEEVRAAYDQGEVDLQAKVWVRMDGKRVETTVGRVLLYDIVPRRLSFESINKVMDKKQLQGLIDLTYRLCGEKETVLLADRVRSMGYGNATRAGISIALDNMVIPRKKVDLLERATREVDDIQAQYTEGLITIGERYNKVIDIWAQVTEEVAQEMMGEIGTETAVGTGKDGKREERRQPSFNPIYIMADSGARGSAQQIRQLAGMRGLMAKPSGEIIETPITANFREGLNVLQYFISTHGARKGLADTALKTANSGYLTRRLVDVAQDAIITEYDCGAMDGITLGALVEGGEIIEPMGERILGRVALDDMLDPFSGNVLVKANEEIDEGKVKLIENAGIDKVKIRSVLTCQARRGICVECYGRDLARGRKVNIGEAVGVIAAQSIGEPGTQLTMRTFHIGGAASRRAEQSTIENRNAGLIKFNNVSVAKKRDGTLIVMNRNGEIIVTDDQGRERERYGVVYGAKLLVREGQKVEANQLLAEWDPYSMPIITEVAGRVKYGDLVDGVTISEQVDEITGLARKAVIASKDPDARPRISIKDEEGRTKKLANSDADARYMLPEGANLVVNDGDEVDAGDVIAKMPRETTKTKDITGGLPRVAELFEARKPKEHAVISEIDGVVAFGKDTKGKRKVVITPEVDSKLRPDLAKEYLIGKGKHISVHTGDRVRAGEALMDGAANPHDILRVLGEKELARWLVDEVQEVYRLQGVKINDKHIETIVRQMLRRVRIVDVGDTEFLADEQVEKFAFEEENERVLKAGGRAAQGEPLLLGITKASLSTESFISASSFQETTKVLTEAAISGKVDYLRGLKENVIMGRLVPAGTGLGAYKHLDIEVETPVDAVEEAEEALAVGAEE | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | B4UDT1 |
Q8DPV9 | AGGDS_STRR6 | Alpha-galactosylglucosyldiacylglycerol synthase | Streptococcus | MRKFPLFSSSLSFLLLILFKENDIIVVMEKKKLRINMLSSSEKVAGQGVSGAYRELVRLLHRAAKDQLIVTENLPIEADVTHFHTIDFPYYLSTFQKKRSGRKIGYVHFLPATLEGSLKIPFFLKGIVKRYVFSFYNRMEHLVVVNPMFIEDLVAAGIPREKVTYIPNFVNKEKWHPLPQEEVVRLRTDLGLSDNQFIVVGAGQVQKRKGIDDFIRLAEELPQITFIWAGGFSFGGMTDGYEHYKTIMENPPKNLIFPGIVSPERMRELYALADLFLLPSYNELFPMTILEAASCEAPIMLRDLDLYKVILEGNYRATAGREEMKEAILEYQANPAVLKDLKEKAKNISREYSEEHLLQIWLDFYEKQAALGRK | Galactosyltransferase involved in the biosynthesis of the bilayer-forming membrane lipid alpha-galactosyl-glucosyldiacylglycerol which is involved in maintaining constant nonbilayer/bilayer conditions (curvature packing stress). Also involved in the beta-lactam resistance. Catalyzes the transfer of a galactosyl residue from UDP-Gal to alpha-glucosyl-DAG (1,2-diacyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol) acceptor to form the corresponding galactosyl-glycosyl-DAG product (3-O-alpha-(D-galactopyranosyl-alpha-(1->2)-D-glucopyranosyl)-1,2-diacyl-sn-glycerol). It can only use UDP-Gal as sugar donor and alpha-glucosyl-DAG is the preferred sugar acceptor. | Q8DPV9 |
A3N3Q5 | SLMA_ACTP2 | Nucleoid occlusion factor SlmA | Actinobacillus | MIQPTVKMPKKSVKERQQQVLEVLIGLLNSEDGMQRVTTERLAKAVGVSEGALYRYFPSKTKMFEALIERIEQTLTGYINASKRKENTTASTVKAILYTVIEFARKNPGVTRILTGHALMFEDDQLKARVAKFFDGLEFQFANILQMSKLREGKTFEDERALAGYLVNFCEGQFLRLVRSNFSYNQHQHFEKQWALIKPLFE | Required for nucleoid occlusion (NO) phenomenon, which prevents Z-ring formation and cell division over the nucleoid. Acts as a DNA-associated cell division inhibitor that binds simultaneously chromosomal DNA and FtsZ, and disrupts the assembly of FtsZ polymers. SlmA-DNA-binding sequences (SBS) are dispersed on non-Ter regions of the chromosome, preventing FtsZ polymerization at these regions. | A3N3Q5 |
Q8KAJ0 | RL15_CHLTE | 50S ribosomal protein L15 | Chlorobaculum | MDLSSLRPAKGAVKARKRVGRGPGSGNGTTAGKGNKGQQSRSGYQRPVIEGGQMPIYRRLPKFGFTPPNQKAVACVNVAQIQMWIEKGLVGEEISVLDLKHLCNASNQEYFKVLGNGELTSTVTITAHFFSKSAEEKIAKAGGKIVKAYRTLEEAAKVNGLPFEEALLTPKAKVVKVKKEKKSVKS | Binds to the 23S rRNA. | Q8KAJ0 |
P57962 | DAPF_PASMU | PLP-independent amino acid racemase | Pasteurella | MQFSKMHGLGNDFVVVDAITQNLYFSPETIKRLADRHRGIGFDQMLIVEPPYDPDLDFHYRIFNADGSEVSQCGNGARCFARFVTLKGLTDKKDIAVSTQTGKMILSIKDDGMIRINMGEPIWEPAKIPFTANKFEKNYILRTSIQTVLCGAVSMGNPHCVVQVDDIQTANVEQLGPLLENHERFPERVNAGFMQVIHRGHIKLRVYERGAGETQACGSGACAAVAVGVMQGLLDSKVQVDLPGGSLIIEWEGVGKPLFMTGDATHVYDGVIRL | Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan. | P57962 |
B0U083 | RLMN_FRAP2 | tRNA m2A37 methyltransferase | Francisella | MQQDKINLLGLNQKAIEDFFISIGEKKFHARQVFKWIHKKGVIDFDSMTDLGKNLRNKLKENAEIVIPKVVFNKASKDGTHKWLIDVGGSAVETVFIPEEGRGTLCVSSQVGCTLNCSFCSTGKQGFNRNLSSAEVISQLWIAARTLSKNNGEHDFSVTNIVMMGMGEPLMNFENVVPAMDIMMDDLAYGLSRRKVTLSTSGVVPRIYDLLEQSGVSLAVSLHAPTDSLRNEIVPINKKYNIDELLEACKLYAEKGPHKHITFEYTLMEEVNDNLSDAEQLIELLRSREVPAKINLIPFNPYPGTPYRKPSNNRIHRFKEFLQHNGFVTTVRKTRGDDIDAACGQLAGDVMDKTKRKERYLKKLGDKNAI | Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity. | B0U083 |
Q8EER0 | CRCB_SHEON | Putative fluoride ion transporter CrcB | Shewanella | MNNLLLVALGGSIGAVFRYLISIFMIQVFGSSFPFGTLLVNVLGSFLMGVIYALGQMSHISPEFKALIGVGLLGALTTFSTFSNETLLLMQEGDWLKAALNVVLNLSLCLFMVYLGQQLVFSRI | Important for reducing fluoride concentration in the cell, thus reducing its toxicity. | Q8EER0 |
Q47B65 | PANC_DECAR | Pantoate-activating enzyme | Dechloromonas | MQIHSSIADLRSALKNRGRVVFVPTMGNLHAGHISLMTQARAHGDTVVASIFVNRLQFGPNEDFDKYPRTFQADCDKLAAAGVDVLFAPTEADLYPEPQEYTVEPPAIQNILDGEFRPGHFRGVATVVLKLFNCVQPQAAMFGKKDYQQLMVIRNMTRQLALPIDIIGGETVRAEDGLALSSRNGYLSAAERTEAPRLYRLLNEIRAAIRAGETDTVKLENEAIAALTAAGWKNDYVAVRQQSDLSMPKGVNAPLVALAASRLGSTRLIDNIEI | Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. | Q47B65 |
Q1BLY7 | DXS_BURCA | 1-deoxyxylulose-5-phosphate synthase | Burkholderia cepacia complex | MYDLLKTIDDPADLRRLDRRQLQPLADELRAFVLDSVSKTGGHLSSNLGTVELTIALHYVFNTPNDRIVWDVGHQTYPHKILTGRRDQMHSLRQYDGISGFPRRSESEYDTFGTAHSSTSISAALGMAIGSQLNGDDRFSIAVIGDGAMTAGMAFEAMNNAGVSEDAKLLVILNDNDMSISPPVGALNRHLARLMSGRFYAAARAGVERVLSVAPPVLELARKLEEHAKGMVVPATLFEEFGFNYIGPIDGHDLDSLIPTLQNIRELRGPQFLHVVTKKGQGYKLAEADPVLYHGPGKFNPAEGIKPSTTPAKKTYTQVFGEWLCDEAERDTRVVGITPAMREGSGMVEFEKRFKDRYYDVGIAEQHAVTFAGGLATEGLKPVVAIYSTFLQRAYDQLIHDVALQNLPVVFAIDRAGLVGADGATHAGAYDLAFMRCIPNMTIMAASDENECRQMLHTALQQPNPTAVRYPRGAGTGVATVKEFTEIPLGKGEVRRRTSQPEGKRVAILAFGTMVAPSLAAAEELDATVANMRFVKPVDAALVRELAETHDYLVTVEEGCVMGGAGSACVEALMESGVIRPVLQLGLPDQFVDHGDHAKLLAQCGLDGAGIAKSIRERFLSPAADVAGHAKRVA | Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP). | Q1BLY7 |
Q2RM68 | RL9_MOOTA | 50S ribosomal protein L9 | Moorella | MKVILTADVAKLGNRGTLVEVSEGYARNYLLPRGLAVEATAGRLKELDLEKKRREKKENQELENARRQAARLDGAVVKITTRAGETGKLFGSVTNKEIAEAIKNTFQISLDRRKIDLKEPIKALGSYEVTLKLHPTVQAHLRVQVVAEGS | Binds to the 23S rRNA. | Q2RM68 |
Q03523 | MURE_BACSU | UDP-N-acetylmuramyl-tripeptide synthetase | Bacillus | MKLTKLLTYLTTEPSVNDSQDPEITSIEMDSREVKKGSLFVCVKGYTVDGHDFAQKAVENGAAAIVAEREVDVNVPVIIVRQSLRALSVLSDAFYGQPTKKLQLIGITGTNGKTSTTHMVDEILKKAGKRTGLIGTMYMKIGDETLPVKNTTPESVTLQKTFKKMNDKHVDTAIMEVSSHALSLGRVHGCDYDIAVFTNLTQDHLDYHKTMDEYRHAKSLLFSQLGGAFNHEHPKRAVLNADDEASAYFEKVTAAHISTYGIKNDADVMAKNISITAQGTSFDLVTNKGTKHITMSLVGQFNVYNVLAAVATCIAAGIPFEIITEAVEELHGVRGRFELVNQQQEFPVIVDYAHTPDSLENVLETCRDMTEGKLFVVVGCGGDRDKTKRPKMAKIAVELADEPIFTSDNPRSEDPRAILRDMEAGVENAYYHSIANREQAIFFAIANAKKGDVVLIAGKGHETYQQIGNETFDFDDAEVAARAIVELNKNKTNS | Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. | Q03523 |
A1E9I7 | ATPF_HORVU | ATPase subunit I | Hordeum | MKNVTHSFVFLAHWPSAGSFGLNTDILATNLINLTVVVGVLIFFGKGVLKDLLDNRKQRILSTIRNSEELRRGTIEQLEKARIRLQKVELEADEYRMNGYSEIEREKANLINATSISLEQLEKSKNETLYFEKQRAMNQVRQRVFQQAVQGALGTLNSCLNTELHFRTIRANIGILGSLEWKR | Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). | A1E9I7 |
C1L2I5 | XERC_LISMC | Tyrosine recombinase XerC | Listeria | MIQEGKLEQQFFDYLHSERNYSVNTSTAYENDLLDFRRFLNEQAITTYQQVTFLDVRIYLTELKQKSFSRTTVARKISSLRSFYTFLLRENVINENPFTYVSHAKNQLRLPKFFYSEEMEALFQVVYEDNETLTLRDRVLLEVLYGTGIRVSECAGILLPDLDTSYQAILIRGKGNKERYVPFGVYAEDAITDYLPERANLMSRYKKSHDALLVNHYGDPLTTRGIRYCLSKIISKASLTRKIHPHMLRHTFATDLLNNGADMRTVQELLGHASLSSTQIYTHVTKEHLKSTYMKHHPRA | Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC-XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | C1L2I5 |
O74832 | PT127_SCHPO | mRNA degradation protein pet127, mitochondrial | Schizosaccharomyces | MLIYKKKNFGRRSVYNLKKCLHKGFQINSCNIKAADNVLHSKASAFEKVNVVDKESIGNLQHHLDTVLPKKKFQFLRDPKTNDYKWDEYLSKILPVDKFNFGLLSKFRPPSEDEQLQKVANSIGAEFVGSTSSLTGLMSQLHFFISKWKFPNFSDLSKGFYISPNERNFTRLCRSASSVHISYQNGLYCIDKDKSLTKEPSVNIILMNVGKSLETFFTVDKDQFLLYKKPPSSNGVLKPLKDVFQYGRCSSLLVRSQLDCYDKKIPESGVFDLKTRAVFGVRMNQTQPELFKSYKLTHYYGNRISFEREYFDLIRSAFMKYSLQARLGYMQGVFVAYHNTSDIFGFQYIPLVAMDRAIHGSSEIGEAEFNLNLQLLEKILQYATSIFPKRSFRVMLSTTEDVPNPPLKVYLEVADDKENRGFDLLDGQKNLEAKTVSPSNFCALEVCALQFVNGVHKSVVKHLDEKETWSIKYHFRKPRDQDNLLRNYIRLRDDIKRRESKISNPPESLLHDYYACSEQYYKRN | Required for the degradation of mRNA in mitochondria. | O74832 |
P53849 | GIS2_YEAST | Zinc finger protein GIS2 | Saccharomyces | MSQKACYVCGKIGHLAEDCDSERLCYNCNKPGHVQTDCTMPRTVEFKQCYNCGETGHVRSECTVQRCFNCNQTGHISRECPEPKKTSRFSKVSCYKCGGPNHMAKDCMKEDGISGLKCYTCGQAGHMSRDCQNDRLCYNCNETGHISKDCPKA | May act in the sexual differentiation pathway. | P53849 |
P55555 | Y4LO_SINFN | Serine/threonine-protein acetyltransferase NGR_a02610 | Sinorhizobium | MQLSRRAEIGNPSSRNLSPRINEKVELLGQALEHARRAGMSSSLMEYGRQVARHLSANVQPDEKILSLDIRNLPLLAASYNRRYPDLDLRHMDSPARFFDALNDRSSDGAWRAVVRLADGEQHHVAADVRTRAGAAPTIIVMEGANFYTFVASYFKLRGDSFRQLGTQAKWAFIEVGAQKSAADCVMFGVQFALAAYRELPTFDAWHDNLHHHGTIAHEGDYSSDYMPRRHAGICANKPFSWGEVPPSDLLQALSLQQCN | Serine/threonine-protein acetyltransferase translocated into infected cells, which mediates acetylation of serine and threonine residues of host target proteins. | P55555 |
A0KRQ2 | CCME_SHESA | Heme chaperone CcmE | Shewanella | MNPRRKKRLTLAVALIGGVAAIASLLLYALNSNLNLFYTPSEIVHGKTDTGVKPEAGQRIRVGGMVTVGSMVRDPNSLHVQFAVHDSLGGEILVTYDDLLPDLFREGQGIVAQGVLGEDGKLAATEVLAKHDENYMPPEVAEAMGQKHEKLDYSQQKSAAQ | Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH. | A0KRQ2 |
Q81JA6 | RNM5_BACCR | Ribosomal RNA terminal maturase M5 | Bacillus cereus group | MEASMKIKEIIVVEGKDDTVAIKRAVDADTIETNGSAIGDHVIEQVKLAQQKRGVIIFTDPDYPGERIRKIISDKVPGCKHAFLPKEEALAKRKKGVGIEHASNESIRRALENIHEEMEAYTGEISWSDLVDAGLVGGEMAKSRRERMGKLLKIGYTNAKQLHKRLQMFQVSKESFAEAYKQVIQEEKK | Required for correct processing of both the 5' and 3' ends of 5S rRNA precursor. Cleaves both sides of a double-stranded region yielding mature 5S rRNA in one step. | Q81JA6 |
A1B012 | RL1_PARDP | 50S ribosomal protein L1 | Paracoccus | MAKLSKKQVSARAAFAGKSNLAVEEAVKLVKENASAKFDETVEIAMNLGVDPRHADQMVRGVVTLPNGTGKDVRVAVFARGPKADEAKAAGAEIVGAEDLMETIQSGKIEFDRCIATPDMMPLVGRLGKILGPRNLMPNPKVGTVTMDVKAAVEAAKGGEVQFKAEKAGVVHAGVGKASFEIEKLAENIRAFVDAVNRAKPSGAKGTYVKKVSISSTMGPGVSLDLGSTAAAQ | Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA. | A1B012 |
Q64TM7 | DNLJ_BACFR | Polydeoxyribonucleotide synthase [NAD(+)] | Bacteroides | MTVKEKIEQLRLQLHQHNYNYYVLNAPEISDKEFDDLMRELQDLEQEHPEYKDENSPTMRVGSDINKNFTQVAHKYPMLSLSNTYSENEVTDFYDRVRKALNEDFEICCEMKYDGTSISLTYENGKLIRAVTRGDGEKGDDVTDNVKTIRSIPLVLHGDNYPEVFEIRGEILMPWEVFEALNREKEAREEPLFANPRNAASGTLKLQNSAIVASRKLDAYLYYLLGDNLPTDGHYENLQEAAKWGFKISPLMRKCQTLQEVFDFINYWDVERKNLNVATDGIVLKVNSLKQQRNLGFTAKSPRWAIAYKFQAERALTRLNMVTYQVGRTGAVTPVANLDPVQLSGTVVKRASLHNADIIEGLDLHIGDMVYVEKGGEIIPKITGVDTSVRFMIGEKVKFITHCPECGSKLIRYEGEAAHYCPNETACPPQIKGKIEHFISRKAMNIDGLGPETVDMFYRLGLIHDTADLYRLTTDDIRGLDRMGDKSAENIIKGIMQSKEVPFERVIFALGIRFVGETVAKKIAKSFKDIEELENADLETLINIDEIGEKIARSILNYFANESNRKLVDRLKTAGLQLYRPEEDLSGHTDKLAGQSIVISGVFTHHSRDEYKDLIEKHGGKNVGSISSKTSFILAGDNMGPAKLEKASKLGIKIMNEEEFLKLIS | DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. | Q64TM7 |
C6HEL8 | LCL2_AJECH | Long chronological lifespan protein 2 | Histoplasma | MVHIFTGILLGLLLLATGTQAQFQFFEQMFGGGQQQQHDSREQNVPSDSDWYQRTYDNARCSNYLCPGTLACVAVPHHCPCQHPAVEDKFELGDGSAICVSKGGFKFGEAARKVELARKGLL | Probable component of the endoplasmic reticulum-associated degradation (ERAD) pathway. | C6HEL8 |
Q722T9 | AZOR1_LISMF | FMN-dependent NADH-azoreductase 1 | Listeria | MTNVLFIKANGLPAERSVSVALYEIFLTEYKKSHPDDNVTELDLFEADLPYYDVTMMSGLHKEAAGETLSPEEKRLADIANSYLDQFLAADKIVMAFPLWNFSIPAQFLTYLFYLNQAGKTFKYTANGPVGLVADKKIALLNARGGIYSDGPMQSFEMSLSYVKNVLAHFGISEPEMVIVEGHNAKPDQAKDIISAGAKEAVELAKIF | Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. | Q722T9 |
Q95730 | CYB_ARTGW | Ubiquinol-cytochrome-c reductase complex cytochrome b subunit | Artibeus | MTNIRKTHPLLKIINSSFVDLPAPSSLSSWWNFGSLLGVCLGVQILTGLFLAMHYTSDTATAFNSVNHICRDVNYGWLLRYLHANGASMFFICLYLHVGRGLYYGSYTYSETWNIGILLLFAVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTDLVQWIWGGFSVDKATLTRFFAFHFLLPFIVTALVMVHLLFLHETGSNNPTGIPSDPDMIPFHPYYTIKDILGFLVMLTALATLVLFSPDLLGDPDNYIPANPLTTPPHIKPEWYFFFAYAILRSIPNKLGGVLALVVSILILAIVPILHMSKQRSMMFRPLSQCLFWLLVAVLFTLTWIGGQPVEHPYIIIGQTASALYFLIILFLMPMTSMVENYLLKW | 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 then used for ATP synthesis. | Q95730 |
Q9HDB9 | GAK5_HUMAN | HERV-K_3q12.3 provirus ancestral Gag polyprotein | Homo | MGQTKSKTKSKYASYLSFIKILLKRGGVRVSTKNLIKLFQIIEQFCPWFPEQGTLDLKDWKRIGEELKQAGRKGNIIPLTVWNDWAIIKAALEPFQTKEDSVSVSDAPGSCVIDCNEKTGRKSQKETESLHCEYVTEPVMAQSTQNVDYNQLQGVIYPETLKLEGKGPELVGPSESKPRGPSPLPAGQVPVTLQPQTQVKENKTQPPVAYQYWPPAELQYLPPPESQYGYPGMPPALQGRAPYPQPPTVRLNPTASRSGQGGTLHAVIDEARKQGDLEAWRFLVILQLVQAGEETQVGAPARAETRCEPFTMKMLKDIKEGVKQYGSNSPYIRTLLDSIAHGNRLTPYDWESLAKSSLSSSQYLQFKTWWIDGVQEQVRKNQATKPTVNIDADQLLGTGPNWSTINQQSVMQNEAIEQVRAICLRAWGKIQDPGTAFPINSIRQGSKEPYPDFVARLQDAAQKSITDDNARKVIVELMAYENANPECQSAIKPLKGKVPAGVDVITEYVKACDGIGGAMHKAMLMAQAMRGLTLGGQVRTFGKKCYNCGQIGHLKRSCPVLNKQNIINQAITAKNKKPSGLCPKCGKGKHWANQCHSKFDKDGQPLSGNRKRGQPQAPQQTGAFPVQLFVPQGFQGQQPLQKIPPLQGVSQLQQSNSCPAPQQAAPQ | The products of the Gag polyproteins of infectious retroviruses perform highly complex orchestrated tasks during the assembly, budding, maturation, and infection stages of the viral replication cycle. During viral assembly, the proteins form membrane associations and self-associations that ultimately result in budding of an immature virion from the infected cell. Gag precursors also function during viral assembly to selectively bind and package two plus strands of genomic RNA. Endogenous Gag proteins may have kept, lost or modified their original function during evolution. | Q9HDB9 |
P37528 | PDXT_BACSU | Pyridoxal 5'-phosphate synthase glutaminase subunit | Bacillus | MLTIGVLGLQGAVREHIHAIEACGAAGLVVKRPEQLNEVDGLILPGGESTTMRRLIDTYQFMEPLREFAAQGKPMFGTCAGLIILAKEIAGSDNPHLGLLNVVVERNSFGRQVDSFEADLTIKGLDEPFTGVFIRAPHILEAGENVEVLSEHNGRIVAAKQGQFLGCSFHPELTEDHRVTQLFVEMVEEYKQKALV | Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS. | P37528 |
Q8R4P9 | MRP7_MOUSE | Multidrug resistance-associated protein 7 | Mus | MEGLLAQLCGTDAARPLPLWEGDTTGHCFTQLVLSALPHALLAVLSACHLGTPRTTNHSPALNPGWRLRLAASFLLSIFPLLDLLPVVLPPGSRPGPLWLEVLAGCVTAVAWFTHSLALWALVHSPHGRSRGPLALALAAFLPTPALVLTLLWHCQRGTFLPPLLPGPLGRVCLLILQLAAVLAYGLGWAAPGGPQEPWTHDPFLSSESQETEVAEDGESWLSRFSYAWLAPLLARGVRGELQQPRDTCRLPRRLHPAFLARVFQAHWKEGAQLWRALYRAFGCCYLALGLLKMVGTMLGFSGPLLLSLLVGFLEEGQEPLSHGLLYVLGLAGGTVISAVLQNQYGYEVRKVTLQARVAVLSTLYRKALKLGPSRPPTGEVLNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGMAFLAGLVLALLLVPVNKVIATRIMASNQEMLRHKDARVKLMTELLSGIRVIKFFRWEQALGDRVKACRTKELGRLRVIKYLDAACVYLWAALPVVICITIFITYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLESKVSLDRIQRFLDLPSYSPEAYYSPDPPAEPSTALELHEALFSWDPIGASQKTFISHLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSELSKGFGLATQEPWIQCATIRDNILFGKTFDAQLYREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEILPLVQAVPTAWAEKEQVATSGQSPSVCDLERTTEEELEVEQSTCGCLVQEESKSEGAVALHVYRAYWRAMGSGLAAAILVSLLLMQATRNGADWWLAHWLSQLKAGRNGSREDPASCSPGSTALFSPRLLLFSPGNLYTPLLSTPLHKAASNGTADVHFYLIVYATIAGVNSLCTLLRAVLFAAGALQAAASLHHRLLHRLLMAPVTFYDSTPSGRVLNRFSSDVACVDDSLPFLLNILLANSVGLLGLLAVLGSGLPWLLLLLPPLSFVYYSVQGYYRASFRELRRLGSLTWSPLYSHLADTLAGLPVLRAAGATYRFEEENQRLLELNQRCQFASYATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGLANPGLVGLVLSYALSLTGLLSGLVSSFTQTEAMMVSVERLEEYSCDVPQEPHSQPLQSPHQQRISWLTQGSVEFQDVVLVYRPGLPNALDGVTFRVEPGEKLGIVGRTGSGKSSLFLVLFRLLEPNAGRVLLDNVDTSQLELAELRSQLAVIPQEPFLFSGTIRENLDPQGLHEDRALWQALEQCHLSEVAVAMGGLDGELGERGQNLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPSALRNQPHSLFQQLLQSSQQGAHSGPSGC | ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds, and xenobiotics from cells. Lipophilic anion transporter that mediates ATP-dependent transport of glucuronide conjugates such as estradiol-17-beta-o-glucuronide and GSH conjugates such as leukotriene C4 (LTC4). Does not transport glycocholic acid, taurocholic acid, MTX, folic acid, cAMP, or cGMP. | Q8R4P9 |
A1B673 | ILVD_PARDP | Dihydroxy-acid dehydratase | Paracoccus | MPAYRSRTTTHGRNMAGARGLWRATGVKNSDFGKPIIAIVNSFTQFVPGHVHLKDLGQMVAREVEAAGGIAKEFNTIAVDDGIAMGHDGMLYSLPSRELIADSVEYMVNAHCADAMVCISNCDKITPGMLMAAMRLNIPAIFVSGGPMEAGKVTLGDGRKVSLDLVDAMVAAADDKISDADLAAIEEAACPTCGSCSGMFTANSMNCLSEALGLSLPGNGSTLATHAFRKNLFLEAGRRIVEVTRRHYEQDDASVLPRAIASKAAFLNAMSLDIAMGGSTNTVLHLLAIAQEGGVDFTMDDIDALSRKVPCLCKVAPNTANVHMEDVHRAGGIMAILGELDRAGLIDRDCPTVHAPTIGAAIDQWDIARSNDPQARELFLAAPGGVPTQVAFSQATLWPDLDLDREHGVIRSAKAPFSKDGGLAVLKGNVALDGCIVKTAGVDESILVFSGRAKVYESQDAAVSGILTGKVEAGDVVVIRYEGPKGGPGMQEMLYPTSYLKSKGLGKACALITDGRFSGGTSGLSIGHVSPEAAAGGTIGLVRDGDRIEIDIPNRSIRLAVPEDELAARRAEQDAKGWKPAQPRQRQVSAALKVYAQFAASADKGAVRILPE | 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 (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively. | A1B673 |
P80972 | COX5A_THUOB | Cytochrome c oxidase polypeptide Va-1 | Thunnus | SHGKVETDEEFDARWVTYFS | 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, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. | P80972 |
Q9UU82 | AREH2_SCHPO | Sterol-ester synthase 2 | Schizosaccharomyces | MIAATPAKSKPSDVNLEQTFKGVSETSKIDLRRSRAAYRPLELSPTPSIFARNYQRNAVDFTGFFVLFWVAVSIMIFMSFLENFELTGRPVVGTIFKYFQSNLLDLAKADLAMSSMFLLAFPFQKIFALGYLRWYGLGVYLYSILILLFLSHCVLRCCLSNWSWTHRAMFILHSMVILMKLHSYNVVNGWYSYCYHSLNKLQSKKTDLDDDERSSVEFYEHCLNHHGNTYPENLTIPNALDFLFMPSLCYQLYYPRTAHVRIHYLIECALGTFGCIFLLVIISDHFMVPVLAKAIRTIIEAPEDASATYFAIRLGHTVAFLMFPFMLSFLLVFWVIFEGVCNFSAEITRFADRNFYDDWWNCWTWDQFARTWNKPVHYFLLRHVYVPLNSFMSKSLSTFFTFFVSSVLHELVMGCITLKIRGYGLFFQMTQIPYIIIQRQKFVRRHRLLGNIAFWFSIIIGIALIAALYILF | Sterol O-acyltransferase that catalyzes the formation of stery esters. | Q9UU82 |
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