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 |
|---|---|---|---|---|---|---|
B2S6Q2 | MURB_BRUA1 | UDP-N-acetylmuramate dehydrogenase | Brucella | MMESGEALLKKLDGRLSGLRGRLTPDTGMDKITWFRAGGPAQVLFQPSDEEDLSAFLKAVPEEIPLLVVGIGSNLLVRDGGVPGFVVRLSAKGFGEVEQVCDTQLRAGAAAPDKRVAAAALEAGLAGFHFYHGIPGGIGGALRMNAGANGVETRERVVEVRALDRKGEVHVLSNADMGYAYRHSSASPDLIFTSVLFEGVPGERDDIRRAMDEVQHHRETVQPVREKTGGSTFKNSEGTSAWKEIDKAGCRGLRVGGAQMSEMHCNFMINTGNATGHDLETLGETVRARVFENSGIRLHWEIKRLGLFREGEQIEEFLGK... | Cell wall formation. | B2S6Q2 |
A6VZ30 | SUCC_MARMS | Succinyl-CoA synthetase subunit beta | Marinomonas | MNLHEYQAKQLFAEYGLPVSTGYAVDTPEAAVEAAKKIGGNKWVVKAQVHAGGRGKAGGVKLVDSYEEVAAFTQNWLGKNLVTYQTDANGQPVAKILVESCTDIANELYLGAVVDRSTRRVVFMASTEGGVEIEKVAEETPELIHKAIIDPLVGAQPYQARELAFKLGLNPTQIKQFTKVFLGLSQMFHDYDFALLEINPLVITDEGNLHCLDGKIGIDSNAVYRQKKMQEFHDPSQEDEREAHAAKWELNYVALDGNVGCMVNGAGLAMGTMDIVNLHGGKPANFLDVGGGATKERVAEAFKIILSDSNVKAVLVNIFG... | Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinat... | A6VZ30 |
O32193 | CSSS_BACSU | Sensor histidine kinase CssS | Bacillus | MKNKPLAFQIWVVISGILLAISILLLVLFSNTLRDFFTNETYTTIENEQHVLTEYRLPGSIERRYYSEEATAPTTVRSVQHVLLPENEEASSDKDLSILSSSFIHKVYKLADKQEAKKKRYSADVNGEKVFFVIKKGLSVNGQSAMMLSYALDSYRDDLAYTLFKQLLFIIAVVILLSWIPAIWLAKYLSRPLVSFEKHVKRISEQDWDDPVKVDRKDEIGKLGHTIEEMRQKLVQKDETERTLLQNISHDLKTPVMVIRGYTQSIKDGIFPKGDLENTVDVIECEALKLEKKIKDLLYLTKLDYLAKQKVQHDMFSIVE... | Member of the two-component regulatory system CssS/CssR required to control the cellular response to secretion stress. Required for the transcription of htrA. Could detect misfolded proteins at the membrane-cell wall interface and then activate CssR by phosphorylation. | O32193 |
O26120 | RS17_METTH | 30S ribosomal protein S17 | Methanothermobacter | MVGIDVPEPKSKCSDPNCPFHGDLPLRGQILEGTVVSDKAERTVTVERSFYKFIRKYERYEKRKSKIKAHKPDCIDVRVGDTVKIAECRPLSKTKNFVVVEVKGEE | One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. | O26120 |
Q54BE5 | TPS8_DICDI | Discodiene biosynthesis cluster protein tps8 | Dictyostelium | MDYDIKFTWDKNQFLDQEIRIPKYTLPWDFKSSPFDKDFENQEMEYVKQFFQNYENAVNYVKKNEIGKIAALNFPLGEKDEYMVNSKLLDFLFILDDYIYESRNYEEDYVDNLMDRSSKSHDPFGREIWRLFDEYYRVGVKESVDLLIRDFEYWSRSAIKTNKYKSLNSSLSIEDYFNSRHGDFGMTITASSCTSTLYVENEIRESKNFKKFFKYFELCNLMINDCGSFKMEINEILLTNFVKVRAIQLGSIDLALKYCVGLLNKYIIKVDKYSTKLEQQYPNHSHLKKYIYTLKTFTAGHNKGYGHANRYN | Terpene synthase; part of the gene cluster that mediates the biosynthesis of the trisnorsesquiterpene discodiene which has a function during later stages of multicellular development, during the transition from fingers to Mexican hats . The terpene synthase tps8 converts its substrate farnesyl diphosphate (FDP) into th... | Q54BE5 |
Q3J789 | MURG_NITOC | Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase | Nitrosococcus | MAIRVLIMAGGTGGHIFPALAVADRLRAWGVEVVWMGTRHGLEAELVPKAGYPIEWISIGGLRGKGLTHWLRAPFKLLLALSQALRALRRWQPAVVLGLGGFVSGPGGLGAWLLRRPLLIHEQNAIVGTANRLLAPLAGRVMEAFPGTFPPARKAEWTGNPVRESIEQLSESRARLQARQGCFHLLVLGGSQGARILNETVPQALALLPTKVRPQVWHQCGSRQWEGAVVAYRAAGVEARLVPFIDDMAAAYAWADLVVCRAGALTVAELMAAGIGALLVPFPLAIDDHQRANADYLVVAGAALLLPEKELSPSRLAQEI... | 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). | Q3J789 |
Q31SW8 | RSMC_SHIBS | rRNA (guanine-N(2)-)-methyltransferase RsmC | Shigella | MSAFTPASEVLLRHSDDFEQSRILFAGDLQDDLPARLDTAASRAHTQQFHHWQVLSRQMGDNARFSLVATVDDVADCDTLIYYWPKNKPEAQFQLMNLLSLLPVGTDIFVVGENRSGVRSAEQMLADYAPLNKVDSARRCGLYFGRLEKQPVFDADKFWGEYSVDGLTVKTLPSVFSRDGLDVGSQLLLSTLTPHTKGKVLDVGCGAGVLSVAFARHSPKIRLTLCDVSAPAVEASRATLAANCVEGEVFASNVFSEVKGRFDMIISNPPFHDGMQTSLDAAQTLIRGAVRHLNSGGELRIVANAFLPYPDVLDETFGFH... | Specifically methylates the guanine in position 1207 of 16S rRNA in the 30S particle. | Q31SW8 |
Q8G6B7 | RUVB_BIFLO | Holliday junction ATP-dependent DNA helicase RuvB | Bifidobacterium | MSETTDYGASNTGANEESLRMVSSQPIGNEPVSDEELRPHVLGGFIGQPRLKAQLQLFLDAARKRDVPPDHILLAGPPGLGKTTLAMIVANELEVPIRVTSGPAVQHAGDLASILSSLDVGEVLFIDEIHRLPRAAEELLYIAMEDFRVDVMVGKGPGASSIPLTLPRFTVIGATTREGMLPSPLRARFGFTAHLDFYPHEELEKLIERSANVLGVNLDTGSAHELALRSRGTPRIANRLLRRVRDWAIVHDLIVVRPDDVKEALALYQIDSEGLDRLDIAVLNAIVRNFNGGPVGLNNLAAMVGEESETVETVCEPYLV... | The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. | Q8G6B7 |
Q9BUJ2 | HNRL1_HUMAN | E1B-55 kDa-associated protein 5 | Homo | MDVRRLKVNELREELQRRGLDTRGLKAELAERLQAALEAEEPDDERELDADDEPGRPGHINEEVETEGGSELEGTAQPPPPGLQPHAEPGGYSGPDGHYAMDNITRQNQFYDTQVIKQENESGYERRPLEMEQQQAYRPEMKTEMKQGAPTSFLPPEASQLKPDRQQFQSRKRPYEENRGRGYFEHREDRRGRSPQPPAEEDEDDFDDTLVAIDTYNCDLHFKVARDRSSGYPLTIEGFAYLWSGARASYGVRRGRVCFEMKINEEISVKHLPSTEPDPHVVRIGWSLDSCSTQLGEEPFSYGYGGTGKKSTNSRFENYG... | Acts as a basic transcriptional regulator. Represses basic transcription driven by several virus and cellular promoters. When associated with BRD7, activates transcription of glucocorticoid-responsive promoter in the absence of ligand-stimulation. Also plays a role in mRNA processing and transport. Binds avidly to poly... | Q9BUJ2 |
Q9LA80 | ATPB_GEOTH | F-ATPase subunit beta | Geobacillus thermoleovorans group | MTRGRVIQVMGPVVDVKFENGHLPAIYNALKIQHKARNENEVDIDLTLEVALHLGDDTVRTIAMASTDGLIRGMEVIDTGAPISVPVGEVTLGRVFNVLGEPIDLEGDIPADARRDPIHRPAPKFEELATEVEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELIHNIAQEHGGISVFAGVGERTREGNDLYHEMKDSGVISKTAMVFGQMNEPPGARMRVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTAKGSITSIQAIYVPADDYTDPAPAT... | Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | Q9LA80 |
Q7ZY08 | UBE2T_XENLA | Ubiquitin-protein ligase T | Xenopus | MQRVSRLKRELQLLNKEPPPGVICWQNESNMDDLRAQIIGGSGSPYEGGIFNLEIIVPERYPFEPPKIRFLTPIYHPNIDSAGRICLDILKLPPKGAWRPALNISTVLTSIQLLMSEPNPDDPLMADISSEFKYNRAVFFSNAKKWTEKHALPAPQGSDKESQEKSGSSEGTSHKRKSAEIAEESKKPCREP | Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes monoubiquitination. Involved in DNA repair. | Q7ZY08 |
Q9VN25 | EIF3A_DROME | Eukaryotic translation initiation factor 3 subunit 10 | Sophophora | MARYTQRPENALKRANEFIEVGKPLRALDTLQEVFRNKRWNYAYSETVIEPLMFKYLYLCVELKKSHIAKEGLFQYRNMFQLVNVNSLENVIRGYLKMAEEHTEAAQAQSSAAVAVLELDDLDNIATPESILMSAVCGEDAQDRSDRTILLPWVKFLWESYCQCLELLRVNTHCEALYHDIARMAFQFCLKYNRKSEFRRLCDKLRKHLEDICKSSNQTTGVSINKVETQQLCLDTRLYLLDSAIQMELWQEAYKAIEDIHGLMALSKKTPVPKTMANYYQKLAMVFSKAGNQLFHAAALLKLFQLTRELKKNLTKDDLQ... | RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and... | Q9VN25 |
P05750 | RS3_YEAST | YS3 | Saccharomyces | MVALISKKRKLVADGVFYAELNEFFTRELAEEGYSGVEVRVTPTKTEVIIRATRTQDVLGENGRRINELTLLVQKRFKYAPGTIVLYAERVQDRGLSAVAQAESMKFKLLNGLAIRRAAYGVVRYVMESGAKGCEVVVSGKLRAARAKAMKFADGFLIHSGQPVNDFIDTATRHVLMRQGVLGIKVKIMRDPAKSRTGPKALPDAVTIIEPKEEEPILAPSVKDYRPAEETEAQAEPVEA | Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosom... | P05750 |
Q24MN7 | ATPF_DESHY | F-type ATPase subunit b | Desulfitobacterium | MNPIHFDLTLVVQVLSFLLLVYILRRFAWNPLINMMEERRSQIEANIANAEKERLQAEQIKREYQEEMRKARQEAQEVIAKATKLSEQRAAEILAAAHGEAEKIKQSALADIERERDRAIAQVQAQVADLSVAVAEKIIRKNLDVRGQEDMIEQFIQEVGELPC | Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). | Q24MN7 |
B2U2Q6 | RSMB_SHIB3 | rRNA (cytosine-C(5)-)-methyltransferase RsmB | Shigella | MKKQRNLRSMAAQAVEQVVEQGQSLSNILPPLQQKVSDKDKALLQELCFGVLRTLSQLDWLINKLMARPMTGKQRTVHYLIMVGLYQLLYTRIPPHAALAETVEGAIAIKRPQLKGLINGVLRQFQRQQEELLAKFNASDARYLHPSWLLKRLQKAYPEQWQSIVEANNQRPPMWLRVNRTHHSRDSWLALLDEAGMKGFPHADYPDAVRLETPAPVHALPGFEDGWVTVQDASAQGCMTWLAPQNSEHILDLCAAPGGKTTHILEVAPEAQVVAVDIDEQRLSRVYDNLKRLGMKATVKQGDGRYPSQWCGEQQFDRIL... | Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | B2U2Q6 |
Q8FFC0 | ZIPA_ECOL6 | Cell division protein ZipA | Escherichia | MMQDLRLILIIVGAIAIIALLVHGFWTSRKERSSMFRDRPLKRMKSKRDDDSYDEDVEDDEGVGEVRVHRVNHAPANAQEHEAARPSPQHQYQPPYASAQPRQPVQQPPEAQVPPQHAPRPTQPVQQPVQQPAYQPQPEQPLQQPVSPQVASAPQPVHSAPQPAQQAFQPAEPVAAPQPEPVAEPAPVMDKPKRKEAVIIMNVAAHHGSELNGELLLNSIQQAGFIFGDMNIYHRHLSPDGSGPALFSLANMVKPGTFDPEMKDFTTPGVTIFMQVPSYGDELQNFKLMLQSAQHIADEVGGVVLDDQRRMMTPQKLREY... | Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins. | Q8FFC0 |
O23653 | AK2_ARATH | Aspartate kinase 2 | Arabidopsis | MASLQLYGVKTPGLALSSKRLEFASKGACFSVTLPSSSAVFRDVEHSCRNIGLRVSCEALRVDLLQRKEPETCDSSGTGKELTCVMKFGGSSVESAERMKEVANLILSFPDERPVIVLSAMGKTTNKLLKAGEKAVTCGVTNVESIEELSFIKELHLRTAHELGVETTVIEKHLEGLHQLLKGISMMKELTLRTRDYLVSFGECMSTRLFSAYLNKIGHKARQYDAFEIGFITTDDFTNADILEATYPAVSKTLVGDWSKENAVPVVTGYLGKGWRSCAITTLGRGGSDLTATTIGKALGLREIQVWKDVDGVLTCDPNI... | Involved in the first step of essential amino acids lysine, threonine, methionine and isoleucine synthesis via the aspartate-family pathway. | O23653 |
A4FWB6 | RS3_METM5 | 30S ribosomal protein S3 | Methanococcus | MIERTFVGENVSETLIDEYFKTKLVRAGYSHIDLKKTPIGTRITVFAEKPGFVIGRKGKMVKELTETLAKEYAVKNPQIEVKQVENPDLDPAIVGHKIASSLERGMHFRRTAHSAIRRVMGSGAKGVSIIVSGKLSGERSRTEKFMDGYMKHCGEPAEALVNKSHQLAKLKLGVVGVTVKIMKPDVTLPDEITILSGEIKEVTEYSEASQE | Binds the lower part of the 30S subunit head. | A4FWB6 |
Q85AV3 | CYB_CHIHI | Ubiquinol-cytochrome-c reductase complex cytochrome b subunit | Chimarrogale | MINLRKTHPLMKIINNSFIDLPAPSNITSWWNFGSLLGICLIIQILTGLFLAMHYTSDTMTAFSSVTHICRDVNYGWLIRYLHANGASMFFICLFLHVGRGLYYGSYMFLETWNIGVLLLFAVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGSDLVQWIWGGFSVDKATLTRFFAFHFILPFIIAALAGVHLLFLHETGSNNPIGISSDADKIPFHPYYTIKDILGMLLLILILMTLVLFSPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALIMSILILAIIPLLHTSKQRSLTFRPI... | 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... | Q85AV3 |
P50255 | RBL_PORCA | Ribulose bisphosphate carboxylase large chain | Pyropia | MSQSVESRTRIKSERYESGVIPYAKMGYWDADYVIKETDILALFRITPQPGVDPIEASAAIAGESSTATWTVVWTDLLTACDLYRAKAYRVDPVPNVADQYFAYIAYDIDLFEEGSIANLTASIIGNVFGFKAVKALRLEDMRMPVAYLKTFQGPATGLIVERERMDKFGRPFLGATVKPKLGLSGKNYGRVVYEGLKGGLDFLKDDENINSQPFMRWRERFLYSMEGVNKASASAGEIKGHYLNVTAATMEDMYERAEFSKEVGSIICMIDLVIGYTAIQSMAIWARKHDMILHLHRAGNSTYSRQKNHGMNFRVICKW... | 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 in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. | P50255 |
Q14HY6 | UBIA_FRAT1 | 4-HB polyprenyltransferase | Francisella | MNKQQLKAYFMLMRLHRPIPILLILWPTLTALVLASHGLPDISYLVIFTIGVVVMRTVGCIINDIADVDFDKHVARTNTRPLTSGQLSIKNAIWLCISLTLVAFICVLFLNLYTILLSFVALFLAILYPFCKRFFAIPQLILGLAFNFGIFMAFSTIQNQIPVEAWIFYIATICWTIAYDTIYALADREFDLEIGIKSSAVLFGNKVFRYILLFNFLSLLLLIILGIYCDFNSFFYLGVVICSLFFVRNYFLYKKLGITNCINAFSANHWIGLIIFIIAVIQYI | Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-... | Q14HY6 |
A8YUS2 | EFTU_LACH4 | Elongation factor Tu | Lactobacillus | MAEKEHYVRTKPHVNIGTIGHVDHGKTTLTAAITTVLAEKGLAKAEDYSQIDAAPEEKERGITINTAHVEYETEKRHYAHMDAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVNYIVVFLNKCDLVDDPELIDLVEMEVRDLLTEYDYPGDDIPVVRGSALKALEGDKEAQEQILKLMDTVDEYIPTPERQTDKPFLMPVEDVFTITGRGTVASGRIDRGTVKVGDEVEIVGLVDKVLKSVVTGLEMFHKTLDSGEAGDNVGVLLRGIDRDQVVRGQVLAAPGSIQTHNKFKAQVYVLKKEEGG... | This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. | A8YUS2 |
Q040U0 | RSMG_LACGA | 16S rRNA 7-methylguanosine methyltransferase | Lactobacillus | MNPEIFAEELANHGFKLSNKQKEQFATYYNKLIEFNKKVNLTRITDKNEVYLKHFFDSITPLLEFSDLFKGEKSLCDVGAGAGFPSLPIKILCPDLSITIVDSLGKRLKFLDELINDLSLDKVTLVHSRAEDAGQNKNLREKFDLVTGRAVARMSVLSEYCIPLAKVDGYLVALKGPKAQDELVEAKNAIEVLGGRVEEVKELTLPDTDDERTLIVVKKVKATPKKYPRQAGTPNKKPL | Specifically methylates the N7 position of a guanine in 16S rRNA. | Q040U0 |
A0A3Q7GFB5 | WK72A_SOLLC | WRKY DNA-binding protein 72A | Solanum subgen. Lycopersicon | MHMETVFRKSTHGGVVKQDIKIKASEEGFVEDINDLKVEKERKSIHNEDDNSKSSQQKDLTGDKKDDQLESAKADMEEVMEENQRLKKHLDKIMKDYRNLQMQFHEVAQRDAEKTNTDVKHDEAELVSLSLGRTSSDTKKELSKLILSKKENDEKEEDNLTLALDCKFQSSTKSSPSNLSPENSLGEVKDDEKGTDQTWPPHKVLKTIRNEEDDVTQQNPTKRAKVSVRVRCDTPTMNDGCQWRKYGQKIAKGNPCPRAYYRCTVAPNCPVRKQVQRCIQDMSILITTYEGTHNHPLPHSATSMAFTTSAAASMLLSGSS... | Transcription activator involved in the transcriptional regulation of terpene biosynthesis in glandular trichomes . Binds to the promoter of the linalool synthase TPS5 and promotes TPS5 gene transactivation . In association with WRKY72B, contributes to basal defense against root-knot nematodes (RKNs) and potato aphids,... | A0A3Q7GFB5 |
A4WSL5 | ISPD_CERS5 | MEP cytidylyltransferase | Cereibacter | MTTAAIIVAAGRGTRAGGELPKQWQLLAGQPVVARTLAAFRAAPGVHRTLLVIHPDDRARAEALPDVAEGTVELVEGGASRDASVRNALEALAGRGVKHVLIHDGARPLVAQALITRMIEALDASPGAAPAVPVSDALWRGEGGRVVGTQDRTGLFRAQTPQAFRFEAILAAHRAHPGGAADDVEVARAAGLEVAIVEGCEDNLKVTYPGDFARAERLLTARPAP | Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). | A4WSL5 |
Q92LB0 | RLMH_RHIME | rRNA (pseudouridine-N3-)-methyltransferase RlmH | Sinorhizobium | MRIGLFAVGRLKAGPEKDLAGRYLDRFAKAGPAVGLELARVVETAESRAANAETRKREEAGQLEKALADGSLLVLLDERGKALDSEAFARLLGTLRDSGKRDLMIAIGGADGLDPALHARADAVLNLGKMTWPHQLVRILIAEQLYRAVTILSGHPYHRA | Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA. | Q92LB0 |
P74876 | DPO3X_SALTY | DNA polymerase III subunit gamma | Salmonella | MSYQVLARKWRPQTFADVVGQEHVLTALANGLSLGRIHHAYLFSGTRGVGKTSIARLLAKGLNCETGITATPCGVCDNCREIEQGRFVDLIEIDAASRTKVEDTRDLLDNVQYAPARGRFKVYLIDEVHMLSRHSFNALLKTLEEPPAHVKFLLATTDPQKLPVTILSRCLQFHLKALDVEQIRHQLEHILNEEHIAHEPRALQLLSRAADGSLRDALSLTDQAIASGDGQVSTQAVSAMLGTLDDDQALSLVEAVVDANGERVMSLINEAAARGIEWEALLVEMLSLLHRIAMVQLSPAALGSDMAAIEQRMRELARTV... | Seems to interact with the delta subunit to transfer the beta subunit on the DNA. | P74876 |
Q8S8Y6 | MATK_ATRBE | Intron maturase | Atropa | MEEIQRYLQPDSSQQHNFLYPLIFQEYIYALAHDHGLNINRSILLENPGYNNQFSLLIVKRLITRMYQQNHFLISTNDSNKNTFLGCNKSLYSQMISEGFAFIVEIPFSLRLISSLSSFEGKKILKSHNLRSIHSTFPFLEDNFSHLNYVLDILIPYPVHLEILVQTLRYWVKDASSLHLLRFFLHEYWNLNSLITSKKPGYSFSKKNKRFFFFLYNSYVYECESTFVFLRNQSSHLRPTSFGALLERIYFYGKIERLVEVFAKDLQVTLWLFKDPFMHYVRYQGKSILASKGTFLLINKWKFYLVNFWQCHFSLCFHTG... | Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns. | Q8S8Y6 |
A7Y3G9 | RK20_IPOPU | 50S ribosomal protein L20, chloroplastic | Ipomoea | MTRIKRGYIARRRRTKMHFFASSFRGAHSRLTRTMTQQEKRALVSAHRDRDRQKRDFRRLWITRINAVIRERGVSYSYSKFIHDLYKNQLLLNRKILAQIAISNRKCLDMISNEIV | 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. | A7Y3G9 |
Q8EVI1 | PURA_MALP2 | IMP--aspartate ligase | Malacoplasma | MNENLLMIIGSQFGDEGKGKFVDLLSNQFDYIVRYQGGDNAGHTIVFDNKTFKLRLIPSGIFNPRNRVVIANGVVLNPITLLEEVKYLKSNGVSTDNLYVSDKCHVIFNFHIEMDKMLEELKGSKKIGTTNKGIGPCYTDKVSRVGIRVCDLFDFNVLLAKIQDNLQIKNVLFSRYGKQIFNPYTIAKQYYELGQQIKPFVINTVALLNYAYERNNKILFEGAQGIMLDIDYGTYPYVTSSNVIGLVSSGTGLAINKIKRILGVVKAYSTRVGSGPFVSEIEEENLAHYIREKGHEYGTVTKRPRRIGWLDLFLLKYVVT... | 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. | Q8EVI1 |
Q0WPN0 | DI32L_ARATH | Ribosomal RNA-processing protein 44 homolog B | Arabidopsis | MKSASSEQSVERIENGHKKKRNRPQKQNRRSKQSSVPIEDAHVEESLDGRDSSRSKAKDSTSSSKQQRPNTDELEAMRASNVAFNSMPPMRAESGYPRRSASPLLSSPEVSKQLLSKSCPDPRACEQSPGMNGELFQQIEGSSQRKIFSSHWSLDAVTEALEKGEAFKALFRVNAHNRNEAYCKIDGVPTDILINGNVCQSRAVEGDTVVIKLDPLSLWPKMKGFVTESAAKPEGTNSPPEKDDKKARQKNGIDVVEGFEDGFSKNKSSVIGKGAKNGVTPSSPPSLDSCLGSFCEQKGNCSAVDKLCGILSSFPHKRPT... | Probable inactive 3'-5'-exoribonuclease. Is unable to complement the growth defect of a yeast mutant lacking RRP44 exonuclease . | Q0WPN0 |
Q5JH27 | RFRNP_THEKO | Protein-only RNase P | Thermococcus | MKFVLDTSIFVNPEVRKNFGDNPTEAMKTFLSYAEKLFGKVEFYMPPGIYREVMHFVDSEELRPAIELYIIKKPPNVHELKIPAFVVYELIEDIRRRIDKGLRVAEKAVRESVLDTDNVDNIIQKLRRNYRRALREGIVDSKEDFELILLAMELDATIVSADVGILTWAQKMGIKWVDSSVFREVLEGLVEKLEGKNL | RNA-free RNase P that catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. | Q5JH27 |
Q6CAG4 | MDM10_YARLI | Mitochondrial inheritance component MDM10 | Yarrowia | MLTFMEHILYSFYDASGWHRDNLYALLTHSSQNLIDFRVPEGVAMNVSALSTPNSASSYTLTNLGHIQGSVAYLSTSLSLPRPHSGTLDLHTVVPGYHKLDPINSQDRIYDTIWQGGKPIHRQDSLLFGRLALPTNTLEAMYVRRFNPTTQLLVTCVSGAHLKSGGALTLYWQKDCRQYAHELLYSTNEALLGARGLYNFGVDMSKPHIASRLSVGGEFYYGVLNKSPGMSTALRYVTQSAYTGSPLTMTLTCNPIMGEFSSTYSLRTGPSSSFSTRYDFNMYSYLSNLSMGAEVWKSRDSVFKLSSSLQDKTARVLWGG... | Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM10 is involved in the late assembly steps of th... | Q6CAG4 |
Q03GV0 | GLMM_PEDPA | Phosphoglucosamine mutase | Pediococcus | MKLKYFGTDGVRGIANETLTPELAFQLGRAGGYVLTKHAKDDEQPRVLVSRDTRISGQLLKHALISGLLSVGIEVMDMGIVTTPGVAYLVRKQEADAGVMITASHNPVQDNGIKFFGSDGYKLSDELEAEIEVLLDADKDNLPRPSSTGLGSVTDYPEGGLNYTAFLEQTIPDDLEGLHIAIDAANGATSSYVSQIFADLNTEFDTMATNPDGLNINAGVGSTHPEGLAKFVVEKGADMGVAFDGDGDRCIAVDELGNIVDGDKIMYICGKFLSERGRLKDDTVVTTVMSNLGLYKALEANDMHSVKTQVGDRYVVEEML... | Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. | Q03GV0 |
A6Q4L7 | SURE_NITSB | Nucleoside 5'-monophosphate phosphohydrolase | unclassified Nitratiruptor | MKRILITNDDGFESLGLRALIEALRDIAQLTIVVPANEKSACGHSLTLTKPLRFVEIEDNFYKLEDGTPTDCVYLALSSLYPDGEKPDIIVSGINRGANMGEDITYSGTVAGAMEGAIYDIPSIAISQVCNSNCEETEMEVGYEQAKYVARDLVEKIFQQGWPAGHRRCLNVNVPPTKEFKGYKITRAGYRVYFNQAHLHRNPRGIEYWWLGLHPLDWIPGKERDCDFEAVKEGFVSITPIKADLTAYEEIPKLKSWL | Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates. | A6Q4L7 |
A2RNJ0 | MURC_LACLM | UDP-N-acetylmuramoyl-L-alanine synthetase | Lactococcus cremoris subsp. cremoris | MEKTYHFTGIKGSGMSALALMLHQMGKNVQGSDSTDYFFTQRGLEQAGVPLLPFDEKNIKPEFELIVGNAFRDDNNVEIAFAHKNGFPFKRYHEFLGHFMEDFTSIGVAGAHGKTSTTGMLAHVMSNIVDTSYLIGDGTGRGNAGSEYFVFESDEYERHFMPYHPEYTIMTNIDFDHPDYFEGIEDVTSAFQDYANNIKKGIFAYGEDVNLRKLSAKAPIYYYGFEANDDYRAENLIRSTRGSSFDAYFRGEKIGHFVVPAYGKHNVLNALSVVAVCHNLGLDMTDVADHLLTFRGVKRRFTEKKVGETVIIDDFAHHPT... | Cell wall formation. | A2RNJ0 |
A7Z801 | YIDD_BACVZ | Putative membrane protein insertion efficiency factor | Bacillus amyloliquefaciens group | MKTIMIAFIRGYQKFISPLTPPSCRFYPTCSQYGIEAVKTHGALKGGWLTLKRILKCHPFHPGGVDPVPDKKQKH | Could be involved in insertion of integral membrane proteins into the membrane. | A7Z801 |
Q6LMT6 | SURE_PHOPR | Nucleoside 5'-monophosphate phosphohydrolase | Photobacterium | MRILISNDDGIFAEGINTLATVLSELGEVTIVAPDRNRSGASNSLTLDYPLRIREEGDRRISVDGTPTDCVHFALNEWLDYRPDIVVAGINHGANLGDDVLYSGTVAAATEGHFLGVPAIAISLVGSTHFDTAAQVVKSIVVNLLEKPLPKNKILNINVPDIPFAELKGWKVTRLGARHRAEQMVKDVDPRGKVLYWLGPPGACQDAGPGTDFHAVEQNLVSITPLQVDLTAHDALESVELWMNEVGKK | Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates. | Q6LMT6 |
Q83BF8 | RPPH_COXBU | (Di)nucleoside polyphosphate hydrolase | Coxiella | MEKRSGIGRLYQGSFFNRYSRAGGNPGAPSVRCARVRGDDGVLVFTPFGNDRRGTSSTTMKQWVKMMNDIVIDKRGFRLGVGMVIMNRQGELLWGRRVGNPDAWQFPQGGLLPNETLREALNRELDEEVGLSPHDVIYLRETRQWISYRLPKKFRRPEHRGPVCIGQRQKWFLLQFTGKDDAISLDHCSQPEFDQWRWVDYWYPVDHVVEFKRDVYQKVLTEFAEFIR | 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. | Q83BF8 |
B5XSW5 | GLMM_KLEP3 | Phosphoglucosamine mutase | Klebsiella | MSNRKYFGTDGIRGRVGDAPITPEFVLKLGWAAGKVLARHGSRKIIIGKDTRISGYMLESALEAGLAAAGLSASFTGPMPTPAIAYLTRAFRAEAGIVISASHNPFYDNGIKFFSIEGTKLPDDVEEAIEAEMEKELTCVDSAELGKASRIVDAAGRYIEFCKGTFPNELSLGTLKVVVDCAHGATYHIAPNVFRELGAQVIAMGCEPDGLNINEEVGATDVRALQARVLAEKADLGIAYDGDGDRVIMVDHEGNKVDGDQILYIIAREGLRQGQLRGGAVGTLMSNMGLELALKQLGIPFARAKVGDRYVLEMLQEKGW... | Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. | B5XSW5 |
A7FYV9 | SPEH_CLOB1 | S-adenosylmethionine decarboxylase alpha chain | Clostridium | MKYSGYHLVIDLFGCNFDQLENTEYIIEMLKKLARALDTKIVAKAFHKFHPQGFSGALIISESHITIHTWPEDAYIGIDIFTCSKCFDPRKIVAYLKENLIFKKVEIKEILRGKID | Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine. | A7FYV9 |
P29310 | 1433Z_DROME | Protein Leonardo | Sophophora | MSTVDKEELVQKAKLAEQSERYDDMAQAMKSVTETGVELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTEASARKQQLAREYRERVEKELREICYEVLGLLDKYLIPKASNPESKVFYLKMKGDYYRYLAEVATGDARNTVVDDSQTAYQDAFDISKGKMQPTHPIRLGLALNFSVFYYEILNSPDKACQLAKQAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDTQGDEAEPQEGGDN | Required in Raf-dependent cell proliferation and photoreceptor differentiation during eye development . Acts upstream of Raf and downstream of Ras, and is essential for viability . Acts as a negative regulator of the slo calcium channel via its interaction with slo-binding protein slob . Inhibits yki activity by restri... | P29310 |
A7HKP2 | GCH4_FERNB | null | Fervidobacterium | MLKDVQNERDNRNIYLKRVGVKDLRYPIVVLDRTNVTQNTIATLNMFVDLPKDYRGTHMSRFIEVLNEYHLEINPKRIKEILRSLKKVLNAKRSVIEITFPFFLLKKAPVTGSESYLEYTCSFEAEMNGDHLDFSTTVTAPIHTLCPCSKEISEYGAHNQRAKCSVTFKSKEMVWIEDIIEIIEESASAPIFTLLKRADEKYVTEHAYDNPKFVEDVARDVALRLKKYDKIEWYKVEVESFESIHAHNAYACLTSDEIEKI | Converts GTP to 7,8-dihydroneopterin triphosphate. | A7HKP2 |
A5EX73 | RL1_DICNV | 50S ribosomal protein L1 | Dichelobacter | MAKKTKRALAIREKLEAGKVYTALEALQLLKEMPAAKFVESVDVAINLGVDPRKSDQVVRGAAVLPHGTGKTVRVAVFAQNDNADAAKAAGADIVGMEELADEIKAGRSDFDVVIAEPAAMRVVGQLGQILGPRGLMPNPKVGTVTADIKAAVENAKAGQVRFRADKSGIVHAMIGKIDFDAEKLLENLHALIAEINKLRPTTIKGVYMQKAYISTTMGPGIAVDVASLTNA | Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA. | A5EX73 |
Q31EW3 | IDI2_HYDCU | Type 2 isopentenyl diphosphate isomerase | Hydrogenovibrio | MSDSPITQRKQDHIDWLLQDEKIERQQAGFDQIQLTHRGLPECDYAQVDSGTTFLQHSLSFPLLISSMTGGASNALNTINENLARAAEHCQVAMAVGSQRTMILDRKAEKSFQLRQFAPTVPLIANMGAIQLNYGFGYDEAQRMVEVLEADALYLHLNPLQEVIQPEGDTNFAKLAEKIAHLKNHLSVPIILKEVGCGLSEKDIQLGLDAGIEWFDLAGRGGTSWSRIEAHRTEDSQQAELGKMFQDWGLTTPQALKQARPFQSQAQFIASGGIRNGIDMVKSVIMGAQICGVAAPLLKPAMASTNATIGTIEQLQQEFR... | 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). | Q31EW3 |
P81392 | MYB06_ANTMA | Myb-related protein 306 | Antirrhinum | MGRPPCCDKIGVKKGPWTPEEDIILVSYIQEHGPGNWRAIPSNTGLLRCSKSCRLRWTNYLRPGIKRGDFTEHEEKMIIHLQALLGNRWAAIASYLPHRTDNDIKNYWNTHLKKKLEKLQSPENGKCQDGNSSVDSDKSVSKGQWERRLQTDIHMAKQALCDALSLDKTSSSTDDPKLSTVQTTQPRPFQASTYSSAENIARLLENWKKKSPVNASSTSQAGSSESTTTSFNYPSVCLSTSSPSEGAISTNFISFNSSNSDILEDHDQAKFEAATNGVNFQDESKPILDNQMPLSLLEKWLLDDSAAVAQGQDVDF | Transcription factor. | P81392 |
P9WNK2 | ESXH_MYCTO | Protein TB10.4 | Mycobacterium tuberculosis complex | MSQIMYNYPAMLGHAGDMAGYAGTLQSLGAEIAVEQAALQSAWQGDTGITYQAWQAQWNQAMEDLVRAYHAMSSTHEANTMAMMARDTAEAAKWGG | EsxH, in complex with EsxG, disrupts ESCRT function and impairs host phagosome maturation, thereby promoting intracellular bacterial growth. The complex acts by interacting, via EsxH, with the host hepatocyte growth factor-regulated tyrosine kinase substrate (HGS/HRS), a component of the ESCRT machinery. | P9WNK2 |
P32842 | VATL2_YEAST | Vacuolar proton pump c' subunit | Saccharomyces | MSTQLASNIYAPLYAPFFGFAGCAAAMVLSCLGAAIGTAKSGIGIAGIGTFKPELIMKSLIPVVMSGILAIYGLVVAVLIAGNLSPTEDYTLFNGFMHLSCGLCVGFACLSSGYAIGMVGDVGVRKYMHQPRLFVGIVLILIFSEVLGLYGMIVALILNTRGSE | Proton-conducting pore forming of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons . V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments... | P32842 |
A3QH52 | RLMH_SHELP | rRNA (pseudouridine-N3-)-methyltransferase RlmH | Shewanella | MKLQLVAVGTRMPAWVTTGFEEYQRRFPRDMAFELIEIPAGKRGKNADIARILQKEGEQMLAAIPKGNHIVSLDLPGKNWTTPELATQLNRWQLDGRDVSLLIGGPEGLAPACKQAANQSWCLSALTLPHPLVRVLVAESLYRAWSINNNHPYHRE | Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA. | A3QH52 |
Q6FYH5 | RL19_BARQU | 50S ribosomal protein L19 | Bartonella | MNIIAQLEAEQCAKIEAKRQLPKFQAGDTVRVMVRVTEGTRTRVQAYEGVCIARSGGGLNETFTVRKISYGEGVERVFPVYSPLIEGVELVRRGKVRRAKLYYLRGLRGKAARIAEKRVYRKKDEKVAERVQATAVTVDVAEQAAE | This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site. | Q6FYH5 |
Q03744 | CR1AD_BACTA | Insecticidal delta-endotoxin CryIA(d) | Bacillus cereus group | MEIMNNQNQCVPYNCLNDPTIEILEGERIETGYTPIDISLSLTQFLLSEFVPGAGFVLGLIDLIWGFVGPSQWDAFLVQIEQLINQRIEEFARNQAISRLEGLSNLYQIYAEAFREWEADPTNPALTEEMRIQFNDMNSALTTAIPLFTVQNYQVPLLSVYVQAANLHLSVLRDVSVFGQRWGFDVATINSRYNDLTRLIGTYTDYAVRWYNTGLERVWGPDSRDWVRYNQFRRELTLTVLDIVSLFPNYDSRTYPIRTVSQLTREIYTNPVLENFDGSFRGMAQRIEQNIRQPHLMDLLNSITIYTDVHRGFNYWSGHQ... | Promotes colloidosmotic lysis by binding to the midgut epithelial cells of many lepidopteran larvae. | Q03744 |
F5A6E9 | TPIS_PROCL | Triose-phosphate isomerase | Procambarus | MANQRKFFVGGNWKMNGDRAGIDSIISFMKGPLSADTEVVVGCPQCYLMYTREHLPSNIGVAAQNCYKVAKGAFTGEISPSMIKDCGCEWVILGHSERRNVFNEPDTLISEKVGHALEAGLKVIPCIGEKLEERESNRTEEVVFAQMKALVPNISDWSRVVIAYEPVWAIGTGKTATPEQAQEVHAKLRQWLRDNVNAEVADSTRIIYGGSVTPGNCKELAKTGDIDGFLVGGASLKPDFVQIINARD | It is also responsible for the non-negligible production of methylglyoxal a reactive cytotoxic side-product that modifies and can alter proteins, DNA and lipids. | F5A6E9 |
Q5FGY3 | ATPB_EHRRG | F-ATPase subunit beta | Ehrlichia | MSSLTGKVKGRARKIKGDADIRVNESTENVGLVIRVMTAVVDIKFPSGKVPKILNALESKEIYNGKKLVLEVSQHISDSIVRCIALDSTDGLSRNDEFIDTGAPISVPVGRATLGRVFDVLGNPIDNCGPLTKSDYSIKPIYSEVPKLTDQKVTTEILVTGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIMELIHNIAKAHKGVSVFAGVGERTREGNDLYHEMIESGVINLEEKDKSQAVLVYGQMNEPPGARLRVALSALTMAEYFRDVENQDVLFFVDNIFRFTQSGSEISALLGRIPSAVGYQPTLAAEMGAMQE... | Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | Q5FGY3 |
A9MJT8 | RNPA_SALAR | Protein C5 | Salmonella | MVKLAFPRELRLLTPAHFTFVFQQPQRAGTPQITILGRLNSLGHPRIGLTVAKKNVRRAHERNRIKRLTRESFRQRQHELPAMDFVVVAKKGVADLDNRALSEALEKLWRRHCRLARGS | RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the riboz... | A9MJT8 |
Q8YAM8 | ATPA1_LISMO | F-ATPase subunit alpha 1 | Listeria | MKTIHFDMNKYETHVDLEYLKEHGRVEKISDGVIFCSGLENAALHQAVLIDERHRGVILELNEEFVGIGLIDKTNDILEGMHVGVSGKFIEVDLFEEMAGRIIDTTGKMLYEESEEKPTATSPLFCVTPAIMTIDSVTRPLNTGLAVIDSITPIGRGQRQLILGNRQSGKTQIAVDTIINQHDQNVHCIYVAIGLKAAYIAEVIETLRNHGAMEYSTVVATAASDSLTAQYLTPYAGMALAEALRDQGKDVLIILDDLTKHADAYRAITLLFNRPPGREAYPGDSFYIHSSLLERAVQMNEEHGGGSITAIPMIETLSDD... | Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | Q8YAM8 |
Q8VS06 | XERC_PSEFL | Tyrosine recombinase XerC | Pseudomonas | MERQLDAYCEHLRSERQVSPHTLSAYRRDLEKVLGWCQKQNIGSWAALDIQRLRSLIARLHQQGQSSRSLARLLSAVRGLYHYLNREGLCDHDPATGLAPPKGERRLPKTLDTDRALQLLEGAVEDDFLARRDQAILELFYSSGLRLSELTGLNLDQLDLADGMVQVLGKGSKTRLLPVGRKAREALEQWLPLRALTNPADDAVFVSQQGRRLGPRAIQLRVKAAGERELGQNLHPHMLRHSFASHLLESSQDLRAVQELLGHSDIKTTQIYTHLDFQHLATVYDSAHPRAKRIKGDES | 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 plas... | Q8VS06 |
Q885Z7 | TTCA_PSESM | tRNA 2-thiocytidine biosynthesis protein TtcA | Pseudomonas | MGTLSVNQNKLQKRLRRLAGEAVADFNMIEEGDKVMVCLSGGKDSYTLLDVLMHFQKVAPIRFDIVAVNMDQKQPGFPEHVLPAYLKELGVEYHIVEKDTHSVVKELIPEGKTTCSLCSRLRRGTLYTFADQIGATKMALGHHRDDIIETFFLNMFFNGALKAMPPKLRADDGRNVVIRPLAYCHEKDIQAYSDLKQFPIIPCNLCGSQENLQRQVVKDMLLDWERKTPGRTESIFRALQNVQPSQLADRKLFDFSQLRIDETAASRFVNVVNI | Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system. | Q885Z7 |
Q8X4P8 | FUMA_ECO57 | Oxaloacetate tautomerase | Escherichia | MSNKPFHYQAPFPLKKDDTEYYLLTSEHVSLSEFEGQEILKVAPEALTLLARQAFHDASFMLRPAHQQQVADILRDPEASENDKYVALQFLRNSDIAAKGVLPTCQDTGTAIIVGKKGQRVWTGGGDEAALARGVYNTYIEDNLRYSQNAPLDMYKEVNTGTNLPAQIDLYAVDGDEYKFLCIAKGGGSANKTYLYQETKALLTPGKLKNYLVEKMRTLGTAACPPYHIAFVIGGTSAETNLKTVKLASAKYYDELPTEGNEHGQAFRDVELEKELLIEAQNLGLGAQFGGKYFAHDIRVIRLPRHGASCPVGMGVSCSA... | Catalyzes the reversible hydration of fumarate to (S)-malate. Functions as an aerobic enzyme in the direction of malate formation as part of the citric acid cycle. Accounts for about 80% of the fumarase activity when the bacteria grow aerobically. To a lesser extent, also displays D-tartrate dehydratase activity in vit... | Q8X4P8 |
Q9ZI50 | RL3_AQUPY | 50S ribosomal protein L3 | Aquifex | MPLGLIGEKVGMTRVLLKDGTAIPVTVIKFPVNYVVQVKSVNTKDGYNALQVGAYEAKEKHLTKPLIGHFKKHGVPLLRRLWEFRVDNPEEFKSGQELRVQDVFKPGDLVDVWGISKGRGFAGVMKRWDFAGFPRSHGHRYHRAVGAIGQRTDPGRVWKGKKMPGHYGAKPVRVQGLFVVASLPEENAILVKGSALPGHNKGIVVLLPAVERIAYRKSQKLKQKRLQFIVENLVKEESTEVAES | 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. | Q9ZI50 |
B0BTY3 | MUTL_ACTPJ | DNA mismatch repair protein MutL | Actinobacillus | MNKPLIHILPPQLANQIAAGEVVERPASVVKELVENSLDAGANQIQIDIEKGGAQLIRIRDNGCGIGKQDLALALARHATSKISSLEDLEMILSLGFRGEALASISSVSRLTLTSRPAGQAEAWQAYAQGREMEVEIQPASHPVGTTIEVANLFFNTPARRKFLRTDKTEFTHIDEVVRRIALAKPNIGFTLTHNGKTVRQYRKVQDNSVEQQQRRVAAICGDDFIQNAIHIDWQHGDLHLHGWIGLPNISRPQNDLCYSYVNGRMMRDKTINHAIRQAYEATDMPEGNYPAFVVFLDIDPSQVDVNVHPAKHEVRFHQG... | This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part ... | B0BTY3 |
Q7W2D6 | RL15_BORPA | 50S ribosomal protein L15 | Bordetella | MSDIQLNTLKPAEGSKHAKRRVGRGIGSGLGKTAGRGHKGQKSRSGGFHKVGFEGGQMPLQRRLPKRGFTPLGQHLYAEVRPSELQLMEAEEIDVQALKAAGVVGQSVRYAKVIKSGELSRKVVLRGITATAGARAAIEAAGGSLA | Binds to the 23S rRNA. | Q7W2D6 |
A6UMS8 | KUP3_SINMW | Probable potassium transport system protein kup 3 | Sinorhizobium | MADSLDHAPAQANNLPQFLALTIGSIGVVYGDIGTSPLYAFREALRPFGPGGVGRDEVIGLVSLVLWTLTAIVTIKYVLFLLRADNDGEGGTLSLLALLLKKGTKYPVLMFFAGVLGAALFIGDAMITPALSVLSAVEGLKLVAPALHDYVLPISVVIILLLFAVQSRGTGAVSVFFGPITLVWFLVMAAAGVAHIGDDLAILSAFNPLNAIGFLWNAGLIGFIVLGAIFLTVTGAEALYADLGHFGRHSIQAAWFAVVFPALALNYLGQGALVLSHPDAISNPFFLMFPNWALLPMVILATAGTIIASQSVITGAFSLI... | Transport of potassium into the cell. | A6UMS8 |
P12425 | GLN1A_BACSU | Glutamine synthetase I alpha | Bacillus | MAKYTREDIEKLVKEENVKYIRLQFTDILGTIKNVEIPVSQLGKALDNKVMFDGSSIEGFVRIEESDMYLYPDLNTFVIFPWTAEKGKVARFICDIYNPDGTPFEGDPRNNLKRILKEMEDLGFSDFNLGPEPEFFLFKLDEKGEPTLELNDKGGYFDLAPTDLGENCRRDIVLELEEMGFEIEASHHEVAPGQHEIDFKYAGAVRSCDDIQTFKLVVKTIARKHGLHATFMPKPLFGVNGSGMHCNLSLFKNGVNAFFDENADLQLSETAKHFIAGIVKHATSFTAVTNPTVNSYKRLVPGYEAPCYVAWSAQNRSPLI... | Glutamine synthetase (GS) is an unusual multitasking protein that functions as an enzyme, a transcription coregulator, and a chaperone in ammonium assimilation and in the regulation of genes involved in nitrogen metabolism . It catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia . Feedback-... | P12425 |
Q9RRU8 | LUXS_DEIRA | Autoinducer-2 production protein LuxS | Deinococcus | MPDMANVESFDLDHTKVKAPYVRLAGVKTTPKGDQISKYDLRFLQPNQGAIDPAAIHTLEHLLAGYMRDHLEGVVDVSPMGCRTGMYMAVIGEPDEQGVMKAFEAALKDTAGHDQPIPGVSELECGNYRDHDLAAARQHARDVLDQGLKVQETILLER | Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhom... | Q9RRU8 |
P82878 | RN2CA_LITCL | Ranatuerin-2Ca | Lithobates | GLFLDTLKGAAKDVAGKLLEGLKCKIAGCKP | Antibacterial activity against Gram-positive bacterium S.aureus and Gram-negative bacterium E.coli. Has activity against C.albicans. | P82878 |
Q84FF7 | TOLB_MYXXA | Adventurous gliding motility protein W | Myxococcus | MKALLLSLLLLLPVVALAQAPTIEISGANFRPLPVAVPAPLTQNDGAKALVAPFDSAFSFDLTASGILQVLDRKGFTADAKEGMAAASINFSRWADVGAEALVKVSLAQDGGVLRGELRLFNVGTGREDLKVSKDAPADNASLLAHRLADALYRHFTREPSPFLSRITYVRKAGTNRDVYVADWDGGNARALTKGGINILPALSQDGSQVAFTTYRKNRPDIYVQSPGGEAKAVISGGQMATGAAFSPDGKRIAYSLAEGESAQVYVANADGSGARALTDTPYGLNTSPTWSPDGKRIAFVSNRGGSPQVYIMNADGTGV... | 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. | Q84FF7 |
O81360 | ABA2_PRUAR | PA-ZE | Prunus | MASTLFYNSMNLSAAVFSRTHFPIPINKDFPLEFSPCIHTDYHLRSRTRSGQKKCLTEVRATVASPTEVPSAPASTQPKKLRILVAGGGIGGLVFALAAKKKGFDVVVFEKDLSAVRGEGQYRGPIQIQSNALAALEAIDMDVAEEVMRVGCVTGDRINGLVDGVSGTWYVKFDTFTPAVERGLPVTRVISRIALQQILARAVGEEIIINDSNVVNFEDLGDKVNVILENGQRYEGDMLVGADGIWSKVRKNLFGLNEAVYSGYTCYTGIADFVPADINSVGYRVFLGHKQYFVSSDVGGGKMQWYAFHKESPGGVDSPN... | Converts zeaxanthin into antheraxanthin and subsequently violaxanthin. Involved in the epoxidation of zeaxanthin. | O81360 |
A8IN83 | IHFB_AZOC5 | Integration host factor subunit beta | Azorhizobium | MIKSELVQKIAEANPHLYQRDVENIVNAILDQIVDALAQGDRVELRGFGAFSVKQREARTGRNPRTGKQVDVSSKVVPYFKTGKEMRERLNGAA | This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control. | A8IN83 |
Q7H8L9 | ATPB_IPOOB | F-ATPase subunit beta | Ipomoea | MRINPTTSGSEVSAVEKKNLGRIVKIIGPVLDVAFPPGKMPNIYNALVVQGRDNEQTNVTCEVQQLLGNNRVRAVAMSDTDGLMRGMEVIDTRAPISVPVGGSTLGRIFNVLGQPVDNLGPVDTNTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYLEMKESGVINEENIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSIT... | Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | Q7H8L9 |
Q8ECR2 | PDXB_SHEON | Erythronate-4-phosphate dehydrogenase | Shewanella | MKIVVDENMPYVEPLFGDLGEIIPVNGRTLTPEQVQDADVLLVRSVTRVNAALLEANQKLKFVGSATIGTDHVDLAYLATRGIVFSNAPGCNATAVGEFAFIAMLELAARFNSPLRGKVVGIVGAGNTGSATAKCLEAFGIKVLLNDPIKEAEGDPRDFVSLETLLQEADIISLHVPITRTGEHKTLHLFDEARLMSLKANIWLINCCRGDVIDNQALIKVKQQRDDLKLVLDVWEGEPNPMPELVPFAEFATPHIAGYSLEGKARGTFMLYQKLCELLAIPATKGLSDLLPRFNIKAVELEQLPDEKALLQLARFVYDL... | Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate. | Q8ECR2 |
Q72GY7 | PCKA_THET2 | Phosphoenolpyruvate carboxykinase (ATP) | Thermus | MQRLEALGIHPKKRVFWNTVSPVLVEHTLLRGEGLLAHHGPLVVDTTPYTGRSPKDKFVVREPEVEGEIWWGEVNQPFAPEAFEALYQRVVQYLSERDLYVQDLYAGADRRYRLAVRVVTESPWHALFARNMFILPRRFGNDDEVEAFVPGFTVVHAPYFQADPERDGTRSEVFVGISFQRRLVLIVGTKYAGEIKKSIFTVMNYLMPKRGVFPMHASANVGKEGDVAVFFGLSGTGKTTLSTDPDRPLIGDDEHGWSEDGVFNFEGGCYAKVIRLSPEHEPLIYKASNQFEAILENVVVNPESRRVQWDDDSKTENTRS... | Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA. | Q72GY7 |
Q69GZ5 | SMC_METVO | Chromosome partition protein Smc | Methanococcus | MISISEIHLKNFKSFKNTKLKIPDGFTAILGPNGSGKSNTIDGICFVLGKTSAKSLRAGKFNQLITYHNGKRADYAEVTLFFDNINREIPIDSDKVGICRKVKLNGDNNYYVVWYEVEKQNTKINTESSQKKTSKASKVEKRRRMKKNEVLDLLSKISLIADGPNIILQGDLLRIIDTSPNERRKILDEVSGVAEFDEKSEKAKKELSQAREYIEKIDIRINEVRANLEKLKKEKEDAEKYTVYNKKLKVTKYILTSKKVEFLKMVLDETKDEIEALKETKNCYIQDISNIDSEIIGLKVKINELVNELNEKGSEEVMEL... | Required for chromosome condensation and partitioning. | Q69GZ5 |
A0JY70 | ATP6_ARTS2 | F-ATPase subunit 6 | Arthrobacter | MIALALPAQDSGEFNPPGIEEMHLPAILPWGAADGFSKQMLLVILSVVIIATFFLLAARKQQLVPGKLQFAGEAAYGFVRNSIAKDIIGGKDFMKYVPLLFSLFFFILVNNIYGAIPLIQLPSFSHVGGAYVLAAIVYLTWIAIGVKKNGIKYFKLATVPTGVPVYILPIVIPIEIISNFLVRPVTHSLRLFATMLAGHLIVMIAGSGIEYLVMQENILLKGTSVLVLVGAIAMYMLEALIMALQAYVFTLLTAIYIEGALHADSH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | A0JY70 |
Q0UG91 | MTND_PHANO | Acireductone dioxygenase (Ni(2+)-requiring) | Parastagonospora | MRAYWFDNLEGDQRQPHDSGRAVDPAYLSKLGVLYHHISSQSEVDELAKARDYKNRDEITVSPEKMGDIYEEKVKSFFHEHLHEDEEIRYILDGAGYFDVRSEGDDWVRIWLEKGDLIILPSGIYHRFTTDEQNYTKAMRLFKDEPKWTPLNRGEETDENQFRQEYLKLRQGLAA | Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine... | Q0UG91 |
Q03586 | RPO1C_THEAC | DNA-directed RNA polymerase subunit A'' | Thermoplasma | MASLLWRDTSKNIAAILEKLPADYAVDYDVPNNVEDGYITINKKNFTYHVVISGVRKYSPDVEAIVKKKSGLKSIITIEKVEKIEPLSFMEFRVGGKTLEAMGSFEVAERQVTEIKEKYGENLSEDVQKVLDDARAMGFTLPESVAEEIARRRTEWGEKAYKNILKRIGEEIGNELIDPYEAVGIIAAQSIGEPGTQMTMRTFHFAGVREMNVTLGLPRLIEIVDARRIPSTPSMTIYLRPEYETNDEVVMDVVKRLENTSISDVADIITDIGELTVTVRPDPRKTKDRLIEMEDIMNAISKIKGITVMEDSGQIIIKPQ... | DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Forms part of the jaw domain. | Q03586 |
Q5MJP5 | SCX1_ANUPH | Phaiodotoxin | Anuroctonus | MKTIPLLFLLFIYFECDGKFIRHKDESFYECGQLIGYQQYCVDACQAHGSKEKGYCKGMAPFGLPGGCYCPKLPSNRVKMCFGALESKCA | Sodium channel (Nav) specific neurotoxin. Causes impairment of movement and mild paralysis in crickets at a dose of 0.5 ug per animal. A dose of 0.8 ug per cricket causes clear flaccid paralysis. A dose of 1.0 ug per cricket causes death within 2 hours. | Q5MJP5 |
A4YTQ2 | LFTR_BRASO | Phenyalanyltransferase | unclassified Bradyrhizobium | MNSRDSAASEITPEVLLRAYACGIFPMAESADDPSLFWVEPELRGVIPLDGFRVASRLARTVRSDAFTLTVNQAFKAVMDGCAAPQPGREDTWINRRIRELYGGLHAMGHCHSVECWQDGELVGGLYGVSLGRAFFGESMFHRARDASKVALVHLVARLIAGGFELLDTQYVTEHLKTFGAVEIPRRRYTVLLEKALTGPAANFARLPTDRPLAGAEALAIIAERG | Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine. | A4YTQ2 |
Q9C888 | PLDA4_ARATH | Phospholipase D epsilon | Arabidopsis | MELEEQKKYFHGTLEITIFDATPFSPPFPFNCICTKPKAAYVTIKINKKKVAKTSSEYDRIWNQTFQILCAHPVTDTTITITLKTRCSVLGRFRISAEQILTSNSAVINGFFPLIADNGSTKRNLKLKCLMWFRPAYLEPGWCRALEEASFQGIRNASFPQRSNCRVVLYQDAHHKATFDPRVDDVPFNARNLWEDVYKAIESARHLVYIAGWALNPNLVLVRDNETEIPHAVGVTVGELLKRKSEEGVAVRVMLWNDETSLPMIKNKGVMRTNVERALAYFRNTNVVCRLCPRLHKKLPTAFAHHQKTITLDTRVTNSS... | Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond to generate phosphatidic acids (PA). Promotes growth and plays a role in nitrogen signaling. | Q9C888 |
B5FNT9 | ARNA_SALDC | UDP-glucuronic acid dehydrogenase | Salmonella | MKAVIFAYHDMGCQGVQAVLDAGYEIAAIFTHADNPAENTFFGSVSRLAAELGIPVYAPDNVNHPIWVDRIAEFAPDIIFSFYYRNLLSEEILHLAPAGAFNLHGSLLPAYRGRAPLNWVLVNGESETGVTLHRMVKRADAGEIVASQRVAIAQDDVALTLHHKLCQAARQLLNSILPTMKCGDIPSVPQRESDATYYGRRRPEDGLIDWHKPVSTVHNLVRAVAAPWPGAFSYNGSQKFTIWSSRICPDAQGALPGSVISVSPLRVACADGALEIITGQAGDGITVQGSQLAQTLGLVAGARLNRPPATSGKRRIRVLI... | Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A an... | B5FNT9 |
B1I4Q9 | MINE_DESAP | Cell division topological specificity factor | Candidatus Desulforudis | MDFLARLLGRESPGSKNVAKERLRLVLIHDRADISPQLLQLLKNEIVEVISKYMEIDDKGLEVSLEHVDKQVALVANIPIRKMKRAANI | Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell. | B1I4Q9 |
Q39EE7 | NUOC_BURL3 | NDH-1 subunit C | Burkholderia cepacia complex | MASKIETLKANLEAALGARVVSLTEAIGELTLVVKASDYLEVAKMLRDDPKLRFEQLLDLCGVDYQTFGDGAYDGPRFAAVSHLLSVTNNWRLRLRAFAPDDDLPIVASLVDIWTSANWYEREAFDLYGIVFEGHPDLRRILTDYGFIGHPFRKDFPVSGYVEMRYDPEEKRVVYQPVTIEPREITPRVIREDRYGGLKH | NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are t... | Q39EE7 |
Q1LJV9 | RISB_CUPMC | 6,7-dimethyl-8-ribityllumazine synthase | Cupriavidus | MDHGFYESNLDGEGLRIGIVQARFNEPVCDELREACMAELKKLGVEGEDTLLVTVPGALEVPLALQKMAESGQFDALVALGAVVRGETYHFELVSNESGAGITRVGLDFNVPIANGILTVDTDAQAHARTREKGRDCARAAVEMANLVVALDSLREHGAEDAEDEEDDE | Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. | Q1LJV9 |
A1AXT7 | YIDC_RUTMC | Membrane protein YidC | Candidatus Ruthia | MNNQKNFLIVAIFLSVFLLWDKWGVTHVVGANGNLISQTKIKDASTINNSLTNKNLNASSIIHRNAELDLPNTITKNQAPFTTVVTDLLTLEISHKGGTIQNAWLNDYPIEINSEQKFQLLSNKADEIFQAQSGLLPQGQTPTHHSIFSSKNSHYQMDGNSLVVPFTWKSENGIKVIKRYHFNKNSYVIGIDYQITNTTNNTLNITSYTQLVRNALDQSNMIIPTYTGGARFDDQDVYEKIEFEDFNDQPKTTSKGGWIAMIEHYFFVAAIPDVNQIHTYSSKIINGEYLLTVVNPELVIAPGAIVTLPSSSLYIGPKEQ... | Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning memb... | A1AXT7 |
Q4DC43 | LIPA1_TRYCC | Lipoic acid synthase 1 | Schizotrypanum | MFHRHLCKLCSKTPSAATLASPLGKLQEERGEGVAKDLKKDKQHRQIFLQKFRERLDSDTTGKNTLAGFIDLPEGISPTMAAVGPLKRGEEPLPPWLKMKVAKGVSRLPRFNSIRKSMREKRLATVCEEAKCPNIGECWGGDEEEGTATATIMVMGSHCTRGCRFCSVLTSRTPPPLDPDEPQKVANAVAEMGVDYIVMTMVDRDDLNDGGAAHVVRCVNAIKEKNPLLLLEALVGDFHGDLKLVETVALSPLSVYAHNIECVERITPNVRDRRASYRQSLKVLEHVNSFTKGAMLTKSSIMLGLGEKEEEVRQTLRDLR... | Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | Q4DC43 |
Q6HPW8 | GLMU_BACHK | Glucosamine-1-phosphate N-acetyltransferase | Bacillus cereus group | MSNRFAVILAAGKGTRMKSKLYKVLHPVCGKPMVQHVVDQVSQLGLQKLVTVVGHGAEMVQEQLGNVSEFALQAEQLGTAHAVDQAAGVLANEEGTTLVICGDTPLITAETMEALLQQHKEAGAMATVLTAYIEEPAGYGRIVRNENGHVEKIVEHKDANEKELAIKEINTGTYCFDNKALFASLSKVSNDNVQGEYYLPDVIEILKNEGHIVSAYQTEHFDETLGVNDRVALSQAEIIMKNRINRKNMVNGVTIIDPSNTYISADAIIGSDTVLHPGTIIEGNTVIGSDCEIGPHTVIRDSEIGDRTIIRQSTVHDSKL... | 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 ... | Q6HPW8 |
A1VZ44 | ACKA_CAMJJ | Acetokinase | Campylobacter | MKILVLNSGSSSIKFKFFDNKIVKASGLVEKIGEQNSKVILKNVLNNESFERELTINNHEEGLSIVNELFKESGILADLNALDGCGHRIVHGGRNLSEHCLVDDYVLKEIDRVSIFAPLHNPAHLAGIKTMIKAAPSVANVAIFDTAFHRTMPDFAYMYALPYDFYDKHNIRRYGFHGTSHAFVSSRAASLLEKDKSELNVISAHLGNGASVCAIEKGKSVDTSMGFTPLEGLVMGTRCGDLDPAILPFISHLKGLTIEEIDTLMNKKSGVYGICGYNDFRDIEREIEQGNDKARLALDMFCYRLVKYIGSYFAVLPKTD... | Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction. | A1VZ44 |
Q9UPY3 | DICER_HUMAN | Helicase with RNase motif | Homo | MKSPALQPLSMAGLQLMTPASSPMGPFFGLPWQQEAIHDNIYTPRKYQVELLEAALDHNTIVCLNTGSGKTFIAVLLTKELSYQIRGDFSRNGKRTVFLVNSANQVAQQVSAVRTHSDLKVGEYSNLEVNASWTKERWNQEFTKHQVLIMTCYVALNVLKNGYLSLSDINLLVFDECHLAILDHPYREIMKLCENCPSCPRILGLTASILNGKCDPEELEEKIQKLEKILKSNAETATDLVVLDRYTSQPCEIVVDCGPFTDRSGLYERLLMELEEALNFINDCNISVHSKERDSTLISKQILSDCRAVLVVLGPWCADK... | Double-stranded RNA (dsRNA) endoribonuclease playing a central role in short dsRNA-mediated post-transcriptional gene silencing. Cleaves naturally occurring long dsRNAs and short hairpin pre-microRNAs (miRNA) into fragments of twenty-one to twenty-three nucleotides with 3' overhang of two nucleotides, producing respect... | Q9UPY3 |
Q83CW6 | RLMB_COXBU | 23S rRNA Gm2251 2'-O-methyltransferase | Coxiella | MSKIKSIYGIHAVSGVLDAAPQRIVKLYVQENRDDQRLQSLVEKAKALGVKVILLSRTELNTLSNEKHQGIVADCEEVENLDESALLSLLKKRETPALLLILDGVKDPHNLGACLRSANAFGVRAVIAPKDRAVGVTPVVRKVACGAAEMTPFIRVTNLSRTIDWLQKEGVWIVGTAVEAETLIQEIDLTGDIAIVLGSEGAGLRRLTKERCDFLAQIPLRGSVESLNVSVACGICLYEVQRQREAPAPS | Specifically methylates the ribose of guanosine 2251 in 23S rRNA. | Q83CW6 |
Q2YB83 | PSD_NITMU | Phosphatidylserine decarboxylase beta chain | Nitrosospira | MQTASLSVFPQYLLPKHALTLLAGRIANAEAGNLTTLLIRWFVWRYGVNMNEAINPDIRSYRTFNEFFTRPLLLENRPISDADYVCPADGVISQLGVISGDQIFQAKGHNYSAAALLGGDTRLAEKFYGGNFATLYLSPRDYHRVHMPVDARVSRMIYVPGDLFSVNAKTVRGVPGLFARNERVICIFESEFGPFALVLVGATIVGSVATVWHGVVNPRDSEGARDVQEWRYDSADLVLKKGDEMGRFQLGSTVVMLFPKNEIAFNPAWAPGRTIRFGETMATKADPAK | Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). | Q2YB83 |
Q056X3 | HSLV_BUCCC | ATP-dependent protease subunit HslV | Buchnera | MTTILSVRVQGKVVIGGDGQATFGHTVMKSNVKKVRSIYKNQVIAGFAGGTADAFTLFELFEKKLEKYQGQLQRSAIELAKDWRTDRLLRKLEALLAVADKKNSLIITGTGDVIQPENDIIAIGSGGPYAQAAAYAYALVYNTNLKASNIVKKSLQIASNICIYTNQSFTIKEIKSEK | Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Q056X3 |
Q48FJ9 | COBT_PSE14 | N(1)-alpha-phosphoribosyltransferase | Pseudomonas | MSNSWWLKPAQAIDVPMREAALARQQQLTKPAGSLAQLERLAVQLAGLQGRERPAADKLWIAIFAGDHGVVAEGVSAYPQEVTGQMLHNFVNGGAAISVLARQLSAQLDVVDLGTVAPLDLPGVRHLRIGAGTANFAHGPAMSAEQGLAALQAGRDSVLRAKAVGTELFIGGEMGIGNTTAASAVACSVLECAAPLLVGPGTGLNAEGIEHKTRVIERALALHAEQAGDPLHSLFCLGGFEIAALTGAYLACAQEGIVALVDGFICSVAALVAVRLNPSCRNWLLFGHRGAEPGHRHLLETLQAEPLLDLGLRLGEGSGA... | Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB). | Q48FJ9 |
A9MJS2 | GLMU_SALAR | Glucosamine-1-phosphate N-acetyltransferase | Salmonella | MLNSAMSVVILAAGKGTRMYSDIPKVLHTLAGKAMVQHVIDAANELGASQVHLVYGHGGDLLKQTLKNDNLNWVLQAEQLGTGHAMQQAAPFFGDDENILMLYGDVPLISVETLQRLRDAKPQGGIGLLTVKLDDPSGYGRITRVNGKVTGIVEHKDATDEQRQIKEINTGILIANGADMKRWLSKLTNNNAQGEYYITDIIALAYQEGREIAAVHPARISETEGVNNRLQLSRLERIYQAEQAEKLLLAGVMLRDPARFDLRGNLAHGRDVEIDTNVIIEGNVTLGHRVKIGTGCIIKNSVIGDDCEISPYSVVEDARL... | 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 ... | A9MJS2 |
Q07XR8 | RL13_SHEFN | 50S ribosomal protein L13 | Shewanella | MKTFTATPETVTRDWFVVDAEGKTLGRIATEIATRLRGKHKPEYTPHVDTGDYIIVINAEKVTVTGNKAAGKIYYSHSGFIGGIKQISFEKLQAHKPEMIIEKAVKGMLPKGPLGRAMFRKLKVYAGTEHNHAAQQPQVLDI | This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly. | Q07XR8 |
B2HEF0 | Y4570_MYCMM | Putative S-adenosyl-L-methionine-dependent methyltransferase MMAR_4570 | Mycobacterium | MARTEGDSWDLANSVGATATMVAAARAAATRRSRPIIADPFAEPLVRAVGLDLFTRAASGEVDLDEVAAGLGFARMVDTFAARALFFDKFFADAIAAGLRQVVIVASGLDARPYRLPWPTGMRVYEIDQPEVIEFKTTTLARLGASPTADHHPVGIDLRDDWPSALRAAGFDAARPTAWLAEGVLIGFLPPEAETRLLDNVIELSAVGSRLAADYGTINGSSAESQQLAQQMTEGWRAHGLDMDIAGLTYPGEHTDVAAYLRSHGWETATADHGDVVLAAGLAELTAADRQSPASTIGFVTAVRSTD | Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity. | B2HEF0 |
Q925Y6 | EFTU_RHIME | Elongation factor Tu | Sinorhizobium | MAKSKFERNKPHVNIGTIGHVDHGKTSLTAAITKYFGEFKAYDQIDAAPEEKARGITISTAHVEYETPNRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPAIVVFLNKVDQVDDAELLELVELEVRELLSSYEFPGDDIPIVKGSALAALEDSDKKIGEDAIRELMAAVDAYIPTPERPIDQPFLMPIEDVFSISGRGTVVTGRVERGIVKVGEEIEIVGIRPTTKTTCTGVEMFRKLLDQGQAGDNIGALLRGVDRNGVERGQILCKPGSVKPHRKFKAEAYILTKEEGGRHTPF... | This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. | Q925Y6 |
A5UMK3 | OTC_METS3 | Ornithine carbamoyltransferase | Methanobrevibacter | MSNLLSVCDIKDEVLDILELAKNFKEGKMEEKPLAGKSLAMIFQKSSTRTRVSFDVGMYQLGGQALFLSSSELQMGRGEPIPDTAKVLSRFVDGIMIRAIEHDDVVELAKYSDVPVISGLTNLEHPCQALADMLTIQEHLGKLEGKKLCFVGDGNNVCNSLLLMAPLVGMDMSVACPEGYEPNEDIVNMAKKLAEEHNKEITISSDLKVALDNVDVVYTDVWVSMGDEKEAEQRQKDFAPYQVNSNLMSLANDGAIFMHCLPAIRGQEVSGEVIDGPQSVVFDEAENRLHAQKAVLYHFLK | Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline. | A5UMK3 |
Q68W01 | TATA_RICTY | Sec-independent protein translocase protein TatA | typhus group | MGMSFSHLLIVLLIIFVLFGAGKLPQVMSDLAKGLKAFKEGMKDDGNDNDKNE | Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system. | Q68W01 |
Q6B8Q9 | ATPD_GRATL | F-type ATPase subunit delta | Agarophyton tenuistipitatum | MSSQGFMSKIALPYAEALVESASSASALDQINQDLSLISEILNQSQELKTFFYNPLITTEIKKNVVSSLFTNQVHSLVIRFLLVLIDRRRIALLDVIISKYLELVYQLQSTVIAEVLTPVLLTDVQQSALINKIKDMTNSKTVKLVITIKPMLIAGFIIKIGSKTIDTSLYGRLKHISAYLNAVS | 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. | Q6B8Q9 |
Q9FYL6 | KCR2_ARATH | Beta-ketoacyl reductase 2 | Arabidopsis | MQGACISESQPWYLHFVCFIGFLFLLRVLFIPLLKWFTTRFLLTPKRLKRYGSWAMVTGATEGIGRAFAHELAKHGLNLILVSRNLSKLESVSDDFQQEFPHIKIKIIPFDFSSEGGYGAIEEGIKGLEVGILINNVGITYPRAMFFHEVDQLTWTKILRVNLEATTWVTRSLIGPMLHRRRGAIVNISSGAAVVVPSHPLYAIYAATKAYVDALSRSLHVEYKQFGIDVQCQVPLYVSTRMVSEVAAIDKPSLFVPSPEVYAKAAVAQIGIGSRCSPFWAHSLQWFLVGLVPDNLVDTWRLSIGLRRRSLS | Probable reductase, but unlike KCR1, has no beta-ketoacyl-coenzyme A reductase activity. | Q9FYL6 |
B8HG89 | RECA_PSECP | Recombinase A | Pseudarthrobacter | MAAAPDRAKALEAALAQIDKQFGKGSVMRLGDEVRAPIEVIPTGSIALDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQRAGGIAAFIDAEHALDPDYAAKLGVDTDALLVSQPDTGEQALEIMDMLVGSGSLDIVVIDSVAALVPRAEIEGDMGDSHVGLQARLMSQALRKITGRLSQTKTTAIFINQLREKIGVFFGSPETTTGGKALKFYASVRIDVRRIQTLKEGADSVGNRTKAKIVKNKMAPPFKIAEFDIIYGQGISREGGIIDMGVEHGIIKKSGSWFTYDGDQLGQGMENSRRFLRDNPELAAEL... | Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage. | B8HG89 |
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