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 |
|---|---|---|---|---|---|---|
Q3SHE4 | ILVC_THIDA | Ketol-acid reductoisomerase type I | Thiobacillus | MKVYYDKDADLSLIKQRKVAIVGYGSQGHAHANNLKDSGVDVTVALRPGSASAKKAENAGLTVKSVPEAVAGADLVMILTPDEFQSRLYRDEIEPNIKQGATLAFAHGFSIHYNQVVPRADLDVIMIAPKAPGHTVRSEFVKGGGIPDLIAIYQDASGKAKETALSYASAIGGGRTGIIETTFKDETETDLFGEQAVLCGGAVELVKAGFDTLVEAGYAPEMAYFECLHELKLIVDLMYEGGIANMNYSISNNAEYGEYVTGVKVINEQSRAAMKECLANIQNGAYAKRFILEGQANYPEMTAWRRNNAAHQIEVVGAKL... | Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobu... | Q3SHE4 |
Q1RMH8 | SNX3_BOVIN | Sorting nexin-3 | Bos | MAETVADTRRLITKPQNLNDAYGPPSNFLEIDVSNPQTVGVGRGRFTTYEIRVKTNLPIFKLKESTVRRRYSDFEWLRSELERESKVVVPPLPGKAFLRQLPFRGDDGIFDDNFIEERKQGLEQFINKVAGHPLAQNERCLHMFLQDEIIDKSYTPSKIRHA | Phosphoinositide-binding protein required for multivesicular body formation. Specifically binds phosphatidylinositol 3-phosphate (PtdIns(P3)). Can also bind phosphatidylinositol 4-phosphate (PtdIns(P4)), phosphatidylinositol 5-phosphate (PtdIns(P5)) and phosphatidylinositol 3,5-biphosphate (PtdIns(3,5)P2). Plays a role... | Q1RMH8 |
Q47IS3 | GMHA_DECAR | Sedoheptulose 7-phosphate isomerase | Dechloromonas | MDLIARVAKNFEDSAQTKLNAVDMMAAPIAAAIETMTNCLINGGKILACGNGGSAGDSQHFAAELIGRFEAERQELAAIALTTDSSILTAIGNDYSFNQIFSKQVRGLGHSGDILLAISTSGNSGNIIEAIKAAHEHDMHVIALTGKGGGQIGEMLRDADIHLCVPADRTARIQETHLLVIHCLCDGIDALLLGVE | Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate. | Q47IS3 |
P08408 | PAPF_ECOLX | Fimbrial adapter PapF | Escherichia | MIRLSLFISLLLTSVAVLADVQINIRGNVYIPPCTINNGQNIVVDFGNINPEHVDNSRGEVTKTISISCPYKSGSLWIKVTGNTMGGGQNNVLATNITHFGIALYQGKGMSTPLILGNGSGNGYGVTAGLDTARSTFTFTSVPFRNGSGILNGGDFQTTASMSMIYN | Adapter that links the PapG adhesin to the distal end of the tip fibrillum. PapF is required for the correct presentation of the adhesin at the distal end of the tip fibrillum. Pili are polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, and ena... | P08408 |
Q17254 | SCXE_BUTOC | Neurotoxin XIV | Buthus | MSSLMISTAMKGKAPYRQVRDGYIAQPHNCAYHCLKISSGCDTLCKENGATSGHCGHKSGHGSACWCKDLPDKVGIIVHGEKCHR | Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin is active only on insects. | Q17254 |
Q57PU4 | BTUD_SALCH | Vitamin B12-transporting ATPase | Salmonella | MSQLMQLKDVAESTRLGPLSGEVSAGEILHLVGPNGAGKSTLLARMAGLTSGEGSIRFGGAPLEAWATATLAQHRAYLAQQQNPPFAMPVWHYLTLHQPDKTRTGQLNEVADMLGLGDKLGRSVNQLSGGEWQRVRLAAVVLQIHPDANPVGQLLLLDEPMNSLDVAQQNALDRVLHHLCQAGIAIVMSSHDLNHTLRHAHKAWLLKRGKLIACGRREEVLTPSYLAQAYGLRFRRLDVEGHPMLISAT | Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Responsible for energy coupling to the transport system. | Q57PU4 |
A9A846 | PSA_METM6 | Proteasome core protein PsmA | Methanococcus | MQQMVPASGYDRAITIFSPEGRLYQVEYAREAVRRGTTAVGIKCNDGVVLAVDRRITSKLIDVSSIEKIFQIDDHIVAATSGLVADARVLIDRARLEAQMNRISYGEAITVEALAKKICDIKQAYTQHGGARPFGLALLITGIDRHSARLFETDPSGALIEYKATAIGSGRPIAMEVLESKYDENMIVSEGMELALYALSKTTEELKPENIDMAIVKDSGKLVEKISVDEIEKIVKAVYKKVEAEEAEAEKNKVEEDIE | Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. | A9A846 |
Q253I4 | GLYA_CHLFF | Serine hydroxymethyltransferase | Chlamydia | MASLLHKFLENASGKKGQDLASTAYLAALDHLLHSFPSIGKSVIDELKSQRSRLKMIASENYSSISVQLAMGNLLTDKYCEGSPFKRFYSCCENVDAIEWECAETAKELFGAESAFVQPHSGADANLLAIMAIITQKIQGPAVKRLGYKTINDLTDKEYAELKAEIGSHVCLGPSLNSGGHLTHGNVRLNVMSKLMRCLPYEVSKKTELFDYAEIARLVRTHKPTVLIAGYSSYSRRLNFSILKQIADDCGAVLWVDMAHFAGLVAGGVFVEEENPIPFADIVTTTTHKTLRGPRGGLMLSTKEYEGMINRACPLMMGGP... | Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent a... | Q253I4 |
Q3JEG4 | AROK_NITOC | Shikimate kinase | Nitrosococcus | MLNFNIFLVGPMGSGKTTIGRYLARITGKNFYDSDREIESRTGVSIPVIFEIEGESGFRQRECKIIAELVQLNNIVLATGGGAVLAAENRRELSQRGIVVYLYAPPKQLYRRTSHDNNRPLLRTGNPLERLKCLLKERDPLYREVADVIIKTGKQPVKAVANEVLRQLRQYKGGAPQRKSFVHVKSNKGA | Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. | Q3JEG4 |
Q3AAN0 | DXS_CARHZ | 1-deoxyxylulose-5-phosphate synthase | Carboxydothermus | MGPILERISLPEDIKKLKPSELMALAQELREYIITVASQNGGHLAPSLGVVELTIALHFVFEAPKDKIIWDVGHQAYAHKILTGRKKQFKTLRTFGGLSGFPKRDESPYDAFGVGHSSTSISAALGMALARDLKGEQYEVVAVIGDGALTGGMAFEALNHAGHLQKKLIVVVNDNEMSIAQNVGALSAYLSRIRTDPKYSRGKDELEALIKKIPHIGPTMVKIGERLKDSFKYLLVPGMLFEELGFTYLGPIDGHNIKEMIEVFSRAKTFAGPVVVHVITKKGKGYHWAEENPDGFHGVGKFYISTGEPVEAPRVSFTEV... | 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). | Q3AAN0 |
Q1QXH6 | PSTB1_CHRSD | Phosphate-transporting ATPase 1 | Chromohalobacter | MTRNENVEENLSVRVRDLNLWYGDHQALKDISIDIFANTVTALIGPSGCGKSTFLRCLNRMNDLINSVSIKGLVEMDGHDVNARGMDEVALRRRVGMVFQKPNPFPKSIYENVAYAPRMHDMVSRKADQDELVERALRDAGLWNEVKDKLHEPGTSLSGGQQQRLCIARAIAVRPDVILMDEPTSALDPISTATIEDLMDKLKKDFTIVTVTHNMQQAARVADYTAFFHLGEMIEYNATKQMFSNPHTKKAEDYITGRYG | Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system. | Q1QXH6 |
B2SPV7 | RLMM_XANOP | 23S rRNA 2'-O-ribose methyltransferase RlmM | Xanthomonas | MSGLLCYCRQGFEPELAAELSARAAFVGIAGYARTQRNDGYVLFVCDEAAQLAAKLQWRELIFARQKLVVIAELKGIDPKDRITPILAALEGQQRFGDLWVEHPDSDAGKPLASLARSFGNALRPALRKAGLLTDKPQPRQPRLHICFLDGDHALLAVADSADSAPWPLGIPRLKLLPEAPSRSALKLDEALLTLLTPEEREALVKPGMRAADLGAAPGGWTWVLTRQHVHVTSVDNGPLRAHVLETGLVEHLRADGFHWKPAQPVDWMVCDMVEQPRRVAERMATWVREGWCRNTIFNLKLPMKKRWDETRLCLELFEQ... | Catalyzes the 2'-O-methylation at nucleotide C2498 in 23S rRNA. | B2SPV7 |
Q9XFM4 | 13S3_FAGES | 13S globulin seed storage protein 3 basic chain | Fagopyrum | MSTKLILSFSLCLMVLSCSAQLLPWQKGQRSRPHHGHQQFQHQCDIQRLTASEPSRRVRSEAGVTEIWDHDTPEFRCAGFVAVRVVIQPGGLLLPSYSNAPYITFVEQGRGVQGVVVPGCPETFQSGSEFEYPRSQRDQRSRQSESGESSRGDQRSRQSESEESSRGDQRSRQSESEEFSRGDQHQKIFRIRDGDVIPSPAGVVQWTHNNGDNDLISITLYDANSFQNQLDENVRNFFLAGQSKQSREDRRSQRQTREEGSDRQSRESQDDEALLEANILSGFEDEILQEIFRNVDQETISKLRGENDQRGFIVQARDLK... | Seed storage protein. | Q9XFM4 |
O15072 | ATS3_HUMAN | Procollagen II amino propeptide-processing enzyme | Homo | MVLLSLWLIAAALVEVRTSADGQAGNEEMVQIDLPIKRYREYELVTPVSTNLEGRYLSHTLSASHKKRSARDVSSNPEQLFFNITAFGKDFHLRLKPNTQLVAPGAVVEWHETSLVPGNITDPINNHQPGSATYRIRRTEPLQTNCAYVGDIVDIPGTSVAISNCDGLAGMIKSDNEEYFIEPLERGKQMEEEKGRIHVVYKRSAVEQAPIDMSKDFHYRESDLEGLDDLGTVYGNIHQQLNETMRRRRHAGENDYNIEVLLGVDDSVVRFHGKEHVQNYLLTLMNIVNEIYHDESLGVHINVVLVRMIMLGYAKSISLI... | Cleaves the propeptides of type II collagen prior to fibril assembly. Does not act on types I and III collagens. | O15072 |
Q2P5E6 | SUCC_XANOM | Succinyl-CoA synthetase subunit beta | Xanthomonas | MNFHEYQSKQLLAEYGIPVPSGKVAATPDEAVDVATSLGKGPWMVKAQIHAGGRGKAGGVKFCKTTDDVKAAAAKMLGTKMSTYQTAGVELPINLVLVTTAGEIVKELYLSILVDRGTKTITYIASSEGGVEIEQVAAETPELIHALNVDFVEGVQGYHGRDFGFKLGLNAKQAGQFASIMVNLYKLFNEKDLALVEINPLAILDDGNLYALDGKFDSDDNAAFRQKQLVAMRDKTQEDETEVTASELDINYVTMDGNIGCMVNGAGLAMATMDVIKLNGGEPANFLDVGGGANKQRVIEAFKLILSSDKVEGIFVNIFG... | 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... | Q2P5E6 |
A7GJT7 | RECR_BACCN | Recombination protein RecR | Bacillus cereus group | MHYPEPISKLIDSFMKLPGIGPKTAVRLAFFVLDMKEDDVLDFAKSLVNAKRNLTYCSVCGHITDRDPCYICDDSHRDQSVVCVVQEPKDVIAMEKMKEYQGVYHVLRGAISPMEGIGPEDINIPQLLKRLQDETVQEVILATNPNIEGEATAMYISRLLKPTGIKVTRIAHGLPVGGDLEYADEVTLSKALEGRREV | May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO. | A7GJT7 |
V5GZ08 | E1132_IXORI | Evasin P1132 | Ixodes | MEVKTFAFLQIAVFIALGAQIFLAGTDALSDEDELFSVEYCGTNCTKQDTGSWTTCSGNCTCYHEDGKKVGLCLSTEYTDFTKFPKPTSEEIANARPLPKREKTLN | Salivary chemokine-binding protein which binds to host chemokines CXCL1, CXCL2, CXCL5 and CXCL8. | V5GZ08 |
Q2YDD1 | CEP43_BOVIN | FGFR1 oncogene partner | Bos | MAATAAAVVAEEDTELRYLLVQTLENSGVLNRIKAELRAAVFLALEEQEKVENKTPLVNESLKKFLNTKDGRLVASLVAEFLQFFNLDFTLAVFQPETSTFQGLEGRENLARDLGIIEAEGTVGGPLLLEVIRRCQQKEKALTSGEGALDLSDVHSPPKSPEGKTGAHTPPSKIPRYKGQGNKKTSGQQPGAKKASNDASHSDTSISSSEPKSRSGLHLLAHETKIGSLLSNNSLDVNAKAGPGPEEDDLEGDSFFDDPIPKPEAAYGWRSEPSKQAGSLASLSDAPPLKSGLSSLAGAPSLKESESKRGNTVLKDLKLV... | Required for anchoring microtubules to the centrosomes. Required for ciliation. | Q2YDD1 |
Q3B6C6 | BCHL_CHLL3 | Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein | Pelodictyon | MSLVLAVYGKGGIGKSTTSANISAALALKGAKVLQIGCDPKHDSTFPITGKLQKTVIEALEEVDFHHEELTAEDVIETGFAGIDGLEAGGPPAGSGCGGYVVGESVTLLQELGLYDKYDVILFDVLGDVVCGGFSAPLNYADYAIIIATNDFDSIFAANRLCMAIQQKSVRYKVKLAGIVANRVDYAKGGGTNMLDQFAEKVGTRLLAKVPYHELIRRSRFAGKTLFAMDDSEEGKEECLQPYLQIAEDLLSEAPMSSVPVPIGDREIFEIVGGWQ | Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and ... | Q3B6C6 |
P42639 | TPM1_PIG | Tropomyosin-1 | Sus | MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKRLEDELVSLQKKLKATEDELDKYSEAPKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSI | Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing c... | P42639 |
Q6HED2 | MTNK_BACHK | Methylthioribose kinase | Bacillus cereus group | MGYYSLTEVTAVQYAKEHGYFEKKANVVCHEIGDGNLNYVFKLDDGVKSIIIKQALPYAKVVGESWPLSIKRATIESKALQIFAKYVPEYVPVVYSHDEELAVTVIEDLSRLTITRKGLIDGEEYPLLSQHIGRFLANVLFYTSDFGLQSEEKRVLEGTFVNPDLCKITEDLVFTDPFGHYDTNDYESELQLAVDELWSDKILKLKVAQYKYKFLTRKEALIHGDLHTGSIFSSPSETKVIDPEFATYGPFGFDIGQFIANLLLNALSREEEQRGVLFFHIEKTWSYFVETFTKLWIGEGVEAYTKEKQWLPIILQNIFT... | Catalyzes the phosphorylation of methylthioribose into methylthioribose-1-phosphate. | Q6HED2 |
B1GZ76 | RPOC_ENDTX | Transcriptase subunit beta' | Endomicrobium | MVKINFQIKKKKSNGPNFIGFDAVRVSVASPDQIKTWSYGEVKKPETINYRTFKPERDGLFCNRIFGPTKDWECHCGKYKYIKYKGTICDRCGVEVTESKVRRERFGHINLAVPVAHLWFLKKPPSRVGILLNMKISDLEKVIYYAKYIVMGDLKDRSGISFFARKGMLMGGEDFNLFKYGINNPIVKEEFKNIFDGIVCEEIKLDSNLTKALKQLKVLVKGQADSAGISTEEAAKKILENVKKGDIYYKVYFKPHSVYYYIDLDPSSHGEIKKILSEKFEKSSTVSITETDKKIRIEFFDIEKDKIYNDLRKDSFALKK... | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | B1GZ76 |
Q45918 | PYRE_COXBU | Orotate phosphoribosyltransferase | Coxiella | MNQATEIAKLLLNIKAVTLNLHEPYRYTSGILSPIYCDNRLIISYPEKRKMIIEAFLQLIEKNHLSFDIVAGTATAGIPHAAWIADRLDLPMIYVRAKAKTHGKQNQIEGRIRKGQRALIVEDLISTGKSALAAGLALREKGVTVTDCIAIFSYQLPQAQQNFSDANINCHALSHFDTLIEMAVDEGYIDEIEKQKALAWNKDPEHWQP | Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). | Q45918 |
Q0KF61 | ARGB_CUPNH | NAG kinase | Cupriavidus | MNADNPGPAATTVAAIAPALKAEILAEALPYIRKFHGKTIVVKYGGNAMTEEKLKHGFARDVILLKLVGMNPVVVHGGGPQIDEALKKVGKVGTFVQGMRVTDEETMEVVEWVLGGEVQQDIVMLINQYGGQAVGLTGKDGGLIRAKRLQMPDRENPGAFIDIGYVGDIEAINPAVVKALQDDAFIPVISPIGFSDDGQAYNINADVVAGKMAEILKAEKLVMMTNIPGVMDKKGNLLTDLSAREIEELFADGTISGGMLPKISSALDAAKSGVHSVHIIDGRIEHSLLLEILTEQAFGTMIRSH | Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. | Q0KF61 |
Q0HTK7 | CLPP_SHESR | Endopeptidase Clp | Shewanella | MHNASDIQSALVPMVIEQTAKGERSFDIYSRLLKERIIFLVGQVEEHMANLIVAQLLFLESESPDKDIFLYINSPGGSVTAGMAIYDTMQFIKPNVSTVCIGQAASMGAFLLAGGEKGKRFCLPNSRVMIHQPLGGFQGQASDIAIHAQEILGIKHKLNLMLAEHTGQPLEVIERDTDRDNFMSATQAVDYGLVDAVMTKRG | Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. | Q0HTK7 |
B2IWK6 | LPXC_NOSP7 | UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase | Nostoc | MQQHTLAAEITQVGVGLHSGVNTQVRILPDETGSGRYFVRVDLPDLPIIPAQVAAVSHTVLSTQLGKGEVYVRTVEHLLAALSGMGVDNARIEIDGSEVPLLDGSASVWVANIAQVGLVSQPVNNQVPLTVTEPIWVYQGDAFVCALPAPETRFSYGIEFDLPAIGNQWYSWSLTTELEKASASFAAEIAPARTFGLLHQIEHLQKTGLIKGGSLDNALVCGPEGWLNPPLRFANEPVRHKILDLVGDLSLLGAFPRAHFLAYKASHNLHIQLAQKILDFGFDFAQSNDFRF | Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis. | B2IWK6 |
A4SGK2 | EFP_CHLPM | Elongation factor P | Chlorobium | MTSISNVSKGAIIRFKGEPHIVESLVHRTPGNLRAFYQANMRNLKSGRNVEYRFSATESVDVIITERKEYQYLYMDGADYVMMDSTTFDQINVSEAAIGSGSRFIKDGITLTIVFSDDGAILSVELPTFVEVEVTETSPASKDDRATSGTKPAIVETGAEVNVPMFVQNGSVIRVDTRSGDYIERVKK | Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase. | A4SGK2 |
Q5FAI2 | DXS_NEIG1 | 1-deoxyxylulose-5-phosphate synthase | Neisseria | MNPSPLLHLIDSPQDLRRLDKKQLPRLAGELRAFLLESVGQTGGHFASNLGAVELTIALHYVYDTPEDKLVWDVGHQSYPHKILTGRKNQMHTMRQYGGLAGFPKRCESEYDAFGVGHSSTSIGAALGMAAADKLLGGDRRSVAIIGDGAMTAGQAFEALNCAGDMDVDLLVVLNDNEMSISPNVGALPKYLASNVVRDMHGLLSTVKAQTGKVLDKIPGAMEFAQKVEHKIKTLAEEAEHAKQSLSLFENFGFRYTGPVDGHNVENLVDVLKDLRSRKGPQLLHVITKKGNGYKLAENDPVKYHAVANLPKEGGAQMPS... | 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). | Q5FAI2 |
Q4V862 | CDK9A_XENLA | Cell division protein kinase 9-A | Xenopus | MAKNYDSVEFPYCDEVSKYERLAKIGQGTFGEVFKAKHRQTGKKVALKKVLMENEKEGFPITALREIKILQLLKHENVVNLIEICRTKVSPTANQYNRCKGTIFLVFDFCEHDLAGLLSNAHVKFTLSEIKKVMQMLLNGLYYIHRNKILHRDMKAANVLITRDGVLKLADFGLARAFSLAKNSQPNKYTNRVVTLWYRPPELLLGERDYGPPIDLWGAGCIMAEMWTRSPIMQGNTEQHQLTLISQLCGSITPEVWPNVDKYELYQKLELPKGQKRKVKDRLKAYVKDPHALDLIDKLLVLDPTQRLDSDDALNNDFFW... | Member of the cyclin-dependent kinase pair (CDK9/cyclin-T) complex, also called positive transcription elongation factor B (P-TEFb), which is proposed to facilitate the transition from abortive to production elongation by phosphorylating the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II) an... | Q4V862 |
Q2JIM0 | RL16_SYNJB | 50S ribosomal protein L16 | unclassified Synechococcus | MLSPKRTKYRKQQRGRMKGKATRGNRINFGEYGLVALEPAWITARQIEASRRAMTRYVRRGGQIWIRIFPDKPVTQRAAETRMGSGKGNPEYWVCVVKPGRILFEMGGVAEPIAREAMRLAAQKLPIKVKFVTKADFEKPEPAQATASEVATSSV | Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs. | Q2JIM0 |
C5B754 | NANE_EDWI9 | ManNAc-6-P epimerase | Edwardsiella | MSVFTTLQQHIQRNGALIVSCQPVPGSPMDSPEIVAAMATAAAQAGAAALRIEGVANLQAVRPHVSLPIIGIIKRDLDESPVRITPFLRDIDDLVQAGADIIAFDGTQRPRPERREALLARIQHHGRLAMADCSSLEDGLYCQRLGCDFIGTTLSGYTHGETPCEPDFALVHALSNAGCRVIAEGRYNTPAQAAQALSQGAWAVTVGSAITRIEHICQWYCQALQAEAHHEYAGH | Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P). | C5B754 |
Q8EB09 | CYSD_SHEON | Sulfate adenylate transferase | Shewanella | MAGRELSHLQQLEAESIQIIREVAAEFDNPVMLYSIGKDSSVMLHLARKAFYPGKIPFPLLHVDTGWKFKEMIAFRDAQAKKFGFELLTHTNPEGVAQGINPFDHGSAKHTDIMKTQGLKQALNQYGFDAAFGGARRDEEKSRAKERVYSFRDRHHRWDPKNQRPELWRTYNGAVNKGESIRVFPLSNWTELDIWQYIYQENIELVPLYFAAERPVVERAGQLIMADDERMKLEEGEAIKYEVVRFRTLGCYPLTAAMHSQADNLEKIIEEMLLTRSSERQGRLIDSDQSASMEQKKRQGYF | With CysN forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysi... | Q8EB09 |
P09905 | HBB_PHYMC | Hemoglobin beta-I/II chain | Physeter | VHLTGEEKSGLTALWAKVNVEEIGGEALGRLLVVYPWTQRFFEHFGDLSTADAVMKNPKVKKHGQKVLASFGEGLKHLDNLKGTFATLSELHCDKLHVDPENFRLLGNVLVVVLARHFGKEFTPELQTAYQKVVAGVANALAHKYH | Involved in oxygen transport from the lung to the various peripheral tissues. | P09905 |
A5V0J4 | ARGB_ROSS1 | NAG kinase | Roseiflexus | MTDPAHHDDRPTLVIKVGGNDLDDATFVAELARVVAAIRPLPVLVHGGGKEIGILQETLGSTPRFVGGLRYTDATALTAAEMVLCGSVSTRLVAALIAAGADALGISGVDRGLIRVVKQEHPAGDLGRVGRPTAVRGEVLRDLLDHGVIPVIAPIALGPDGPYNVNADEAAGAVAAALGVSEAVFVTNVPGVLVKGDVMRYLTRSEIERLIADGTISGGMIPKVRAALTALDAGVHAARITNLEGLLNQGTTIITEREPHE | Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. | A5V0J4 |
A3QBX2 | SYI_SHELP | Isoleucyl-tRNA synthetase | Shewanella | MSDYKSTLNLPETEFPMRGNLAQREPEMLKSWTEKKLYQKIRESRTGAKPFILHDGPPYANGSIHIGHSVNKILKDIIIKSKTLSGFDAPYIPGWDCHGLPIELKVEQKVGKPGQKVSAAEFRQKCREYAAAQVDGQREDFIRLGVLGDWQNPYLTMNFDTEANIVRSLAKVIDNGHLHKGVKPVHWCTDCGSALAEAEVEYEDKTSPAIDVAFVAVDQAAVLAKFGLEQSDAEVATVIWTTTPWTLPANRGLSMAGDIDYDLVEFTKDGSKRAIIVAQELVESCIERYGAELHSVLGTVKGQALELLRFKHPFYDFDVP... | Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrol... | A3QBX2 |
A1US40 | PANB_BARBK | Ketopantoate hydroxymethyltransferase | Bartonella | MSVHKSIKRITASEIQAKKKQEPIVSLTAYQAYSARIADPHCDFLLVGDSVGMIVHGFDTTLPVDVDMMILHGKAVMRGSQRALVVVDMPFGSYEKSPEQAFSNASRILADTGCGAVKLEGGIHMAKTIDFLCKRGIPVMSHIGLTPQAVNHFGGFKTQGRDKSDWEKIEADAAAIEDAGAFAVVVEAVVEPLAVKLTEKLSIPTIGIGASNQCDGQILVMEDMLGYGAWAPKFVRRYGTLEQAMDTAIRNYAEDVKSRAFPSDSEIYKLK | Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. | A1US40 |
P31874 | ILVD_RHOCA | Dihydroxy-acid dehydratase | Rhodobacter | RTTEAFSTGNRYKEVDRDRQAGVIRSAEHAFSKDGGLAVLFGNIAE | 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 (... | P31874 |
Q6BVZ7 | URM1_DEBHA | Ubiquitin-related modifier 1 | Debaryomyces | MGIKVKVEFLGGLDVISNGVREHKCEVPLEEGEATMIDLIKYITATIISDPKDVPVFIEEGTVRPGILVLINDTDWELEGMEDYVVESGDVLTFTSTLHGG | Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by the MOCS3 homolog UBA4. The sulfur is then transferred to tRNA to form 2... | Q6BVZ7 |
Q04664 | CPSE_STRA3 | Galactosyl transferase CpsE | Streptococcus | MIQTVVVYFSASLTLTLITPNFKSNKDLLFVLLIHYIVFYLSDFYRDFWSRGYLEEFKMVLKYSFYYIFISSSLFFIFKNSFTTTRLSFFTFIAMNSILLYLLNSFLKYYRKYSYAKFSRDTKVVLITNKDSLSKMTFRNKYDHNYIAVCILDSSEKDCYDLKHNSLRIINKDALTSELTCLTVDQAFINIPIELFGKYQIQDIINDIEAMGVIVNVNVEALSFDNIGEKRIQTFEGYSVITYSMKFYKYSHLIAKRFLDITGAIIGLLICGIVAIFLVPQIRKDGGPAIFSQNRVGRNGRIFRFYKFRSMRVDAEQIKK... | Galactosyl transferase is essential for the assembly of the group B streptococci (GBS) type III capsular polysaccharide. May be involved in the formation of either or both galactosidic bonds by catalyzing the addition of galactose to an oligosaccharide precursor or to a lipid intermediate. Type III capsular polysacchar... | Q04664 |
Q1QMU2 | PURL_NITHX | Phosphoribosylformylglycinamidine synthase subunit II | Nitrobacter | MNRTDPPITPELVASHGLKPDEYERILKLIGRVPTFTELGIFSAMWNEHCSYKSSRIHLRGLPTKAPWVIQGPGENAGVIDIGDGQAVVFKMESHNHPSYIEPYQGATTGVGGILRDVFTMGARPIACLNALSFGDPSHPKTRHLVGGVVAGVGGYGNSFGVPTVGGQVRFHTRYDGNILVNAMAVGLADADKIFYAAASGVNMPIVYLGSKTGRDGIHGATMASAEFDDDSAEKRPTVQVGDPFAEKLLLEACLEIMETDCVIAIQDMGAAGLTCSAVEMGAKGDLGVDLDLDSVPTREQGMSAYEMMLSESQERMLMV... | Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three su... | Q1QMU2 |
O86847 | LEXA_STRCL | LexA repressor | Streptomyces | MTEAATGPEGADPSRAARSLPGRPPGIRADSSGLTDRQRRVIEVIRDSVQRRGYPPSMREIGQAVGLSSTSSVAHQLMALERKGFLRRDPHRPRAYEVRGSDQPSAQPADTSGKPAASYVPLVGRIAAGGPILAEESVEDVFPLPRQLVGDGELFVLKVVGDSMIEAAICDGDWVTVRRQPVAENGDIVAAMLDGEATVKRFKRENGHVWLLPHNAAYQPIPGDDATILGKVVAVLRRV | Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair... | O86847 |
Q2KXW3 | KYNB_BORA1 | N-formylkynurenine formamidase | Bordetella | MKRLWDISPPISSQSPVFPGDTPYRQQWKWQLSPECPVNVSEITMSPHIGAHADAPLHYANGATAAGCLPLEPFLGPCRVIHALDCGPLILPEHLAHAADDMPERVLVRTAQHAAVHWWTDDFSAYAPQTIEWLASLGVRLIGIDTPSIDPATSKTLDSHHVILRRDIRVLENLVLDTVEPGDYELIALPLALVQADASPVRAVLRELG | Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation. | Q2KXW3 |
P93157 | ANX1_GOSHI | Annexin Gh1 | Gossypium | ATLTVPTTVPSVSEDCEQLRKAFSGWGTNEGLIIDILGHRNAEQRNLIRKTYAETYGEDLLKALDKELSNDFERLVLLWALDPAERDALLANEATKRWTSSNQVLMEIACTRSANQLLHARQAYHARYKKSLEEDVAHHTTGDFHKLLLPLVSSYRYEGEEVNMTLAKTEAKLLHEKISNKAYSDDDVIRVLATRSKAQINATLNHYKNEYGNDINKDLKADPKDEFLALLRSTVKCLVYPEKYFEKVLRLAINRRGTDEGALTRVVCTRAEVDLKVIADEYQRRNSVPLTRAIVKDTHGDYEKLLLVLAGHVEN | Binds to phospholipid vesicles in a calcium-dependent manner in vitro . Prefers phosphatidyl-serine containing membranes. May have a role in the membrane cytoskeleton scaffolding or exocytotic processes . May be involved in oxidative stress response (Probable). | P93157 |
B2TIG8 | RPOB_CLOBB | Transcriptase subunit beta | Clostridium | MVHPVQVGKRTRMSFGKVKDVTEMPNLIEVQLDSYQWFLREGLHEVFEDINPITNFTGNLVLEFVDYKLDMDNIKYSVEECKERDATYAAPLKVSVRLQNNETGEIKEQEVFMGDFPLMTEQGTFIINGAERVIVSQLVRSPGVYYNYSIDKTGKKLYSATVIPNRGAWLEYETDSNDIIYVRIDKTRKLPITILARAMGFGSDQELLDFFGEDERFRASIEKDNTKTREEGLLEIYKRLRPGEPPTVDSAISLIDSLFFDAKRYDLSRVGRYKFNKKLALNLRIANQIAAMDVINPSTGEIMVEKGQKISRLLAEDIQN... | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | B2TIG8 |
P32119 | PRDX2_HUMAN | Thioredoxin-dependent peroxiredoxin 2 | Homo | MASGNARIGKPAPDFKATAVVDGAFKEVKLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDSQFTHLAWINTPRKEGGLGPLNIPLLADVTRRLSEDYGVLKTDEGIAYRGLFIIDGKGVLRQITVNDLPVGRSVDEALRLVQAFQYTDEHGEVCPAGWKPGSDTIKPNVDDSKEYFSKHN | Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling c... | P32119 |
Q8N5A5 | ZGPAT_HUMAN | Zinc finger and G patch domain-containing protein | Homo | MDEESLESALQTYRAQLQQVELALGAGLDSSEQADLRQLQGDLKELIELTEASLVSVRKSSLLAALDEERPGRQEDAEYQAFREAITEAVEAPAAARGSGSETVPKAEAGPESAAGGQEEEEGEDEEELSGTKVSAPYYSSWGTLEYHNAMVVGTEEAEDGSAGVRVLYLYPTHKSLKPCPFFLEGKCRFKENCRFSHGQVVSLDELRPFQDPDLSSLQAGSACLAKHQDGLWHAARITDVDNGYYTVKFDSLLLREAVVEGDGILPPLRTEATESDSDSDGTGDSSYARVVGSDAVDSAQSSALCPSLAVVGSDAVDSG... | Antagonizes the transcription repression by isoform 1 by competing for the binding of the NuRD complex. Does not bind DNA. | Q8N5A5 |
A3D7N0 | YBEY_SHEB5 | Endoribonuclease YbeY | Shewanella | MSLDLALDIQHATTCDWLPTDEQFALWATTAIGNSMDEAELTIRIVDTRESQMLNSTYRGKDKPTNVLSFPFEAPPEIELPLLGDLVICAAVVENEAREQQKTLEAHWAHMVVHGCLHLLGYDHIEDEEAEEMESLETQLIEGLGFTDPYKEQ | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | A3D7N0 |
Q8FYW3 | PURE_BRUSU | 5-(carboxyamino)imidazole ribonucleotide mutase | Brucella | MSVDVAIIMGSQSDWETMRHAAHTLEALGISFDARIVSAHRTPDRLVAFAKGAKAEGFKVIIAGAGGAAHLPGMAAAMTPLPVFGVPVQSKALSGQDSLLSIVQMPAGIPVGTLAIGRAGAVNAALLAAAVLALYDEALAARLDEWRKAQTESVAERPSNEA | Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR). | Q8FYW3 |
A1JJC7 | KHSE_YERE8 | Homoserine kinase | Yersinia | MVKIYAPASIGNVSVGFDVLGAAVSPVDGTLLGDCVSVTASDSFSLRNEGRFVSKLPDDPKENIVYQCWERFCQEMGKEIPVALVLEKNMPIGSGLGSSACSVVAGLMAMNEFCGKPLDKVTLLGMMGELEGRVSGSVHFDNVAPCYLGGMQLILEQPGYISQDVPGFDDWLWVMAYPGIKVSTAEARAILPAQYRRQDCIAHGRNLAGFIHACHTQQPSLAAKMMKDVIAEPYRTQLLPGFAAARQAAQDIGALACGISGSGPTLFAVCNDSETAQRMASWLQNHYLQNDEGFVHICRLDTAGARLLG | Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate. | A1JJC7 |
O95631 | NET1_HUMAN | Epididymis tissue protein Li 131P | Homo | MMRAVWEALAALAAVACLVGAVRGGPGLSMFAGQAAQPDPCSDENGHPRRCIPDFVNAAFGKDVRVSSTCGRPPARYCVVSERGEERLRSCHLCNASDPKKAHPPAFLTDLNNPHNLTCWQSENYLQFPHNVTLTLSLGKKFEVTYVSLQFCSPRPESMAIYKSMDYGRTWVPFQFYSTQCRKMYNRPHRAPITKQNEQEAVCTDSHTDMRPLSGGLIAFSTLDGRPSAHDFDNSPVLQDWVTATDIRVAFSRLHTFGDENEDDSELARDSYFYAVSDLQVGGRCKCNGHAARCVRDRDDSLVCDCRHNTAGPECDRCKP... | Netrins control guidance of CNS commissural axons and peripheral motor axons. Its association with either DCC or some UNC5 receptors will lead to axon attraction or repulsion, respectively. Binding to UNC5C might cause dissociation of UNC5C from polymerized TUBB3 in microtubules and thereby lead to increased microtubul... | O95631 |
Q5WGB8 | RACA_ALKCK | Chromosome-anchoring protein RacA | Alkalihalobacillus | MKTKEMSEAIGVNPTTIQRWTKYFKIDCDVTEQGHFLYTEKHLQLFKKIKRELDEGKRMKDINLNERQGQGEPSVPTKQYEAKLEKMLVQVDALEEKLATKADDVVSYQLLKHRSELDEMMKLVGTLEDRLLFIEKRMMSHHHQEKQVVNEHTPKKIKRGPWRSFMNLFAF | Required for the formation of axial filaments and for anchoring the origin regions at the cell poles in sporulating cells, thus ensuring proper chromosome segregation in the prespore. Binds in a dispersed manner throughout the chromosome but preferentially to sites clustered in the origin portion of the chromosome, cau... | Q5WGB8 |
B4S9K2 | AROE_PROA2 | Shikimate dehydrogenase (NADP(+)) | Prosthecochloris | MCSITSILGLIGRNVNYSYSPFIHNTAAEMLRLPFYYTIFNIADARQIPDALNGMRALGIAGLNVTIPYKQVVTEYVDTLSAEAQAVGAVNTIVNNNGRLSGCNTDIAGVSHPLKPYKERLHQSPAGIFGNGGAALAAVEALRRDYHPSAIRLFVRDPDKGLALAEQVHAKHPEAPIEIFKIDAYDAIRDCHLLINATPIGTKGVQTAGNSALLPQEQKLLHDGQIIFDMVYNPLRTPFVNMAAEAGAVVIPGVEMLIAQAAESFCLWTGETMPVDSIREKILKKLTAQP | Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). | B4S9K2 |
Q0T622 | RUTA_SHIF8 | Pyrimidine monooxygenase RutA | Shigella | MMKIGVFVPIGNNGWLISTHAPQYMPTFELNKAIVQKAEHYHFDFALSMIKLRGFGGKTEFWDHNLESFTLMAGLAAVTSRIQIYATAATLTLPPAIVARMAATIDSISGGRFGVNLVTGWQKPEYEQMGIWPGDDYFSRRYDYLTEYVQVLRDLWGTGKSDFKGDFFTMNDCRVSPQPSIPMKVICAGQSDAGMAFSAQYADFNFCFGKGVNTPTAFAPTAARMKQAAEQTGRDVGSYVLFMVIADETDDATRAKWEHYKAGADEEVLSWLTEQSQKDTRSGTDTNVRQMADPTSAVNINMGTLVGSYASVARMLDEVA... | Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism, adding oxygen atoms in the process to yield ureidoacrylate peracid, that immediately reacts with FMN forming ureidoacrylate and FMN-N(5)-oxide. The FMN-N(5)-oxide reacts spontaneously with NADH to produce F... | Q0T622 |
Q12P74 | YCIB_SHEDO | Inner membrane-spanning protein YciB | Shewanella | MKQLLDFLPLIIFFTVYKLVDIYTATGALIAATAVQIAILYFVYKKVEKMHLVTFAMVTVFGTLTLAFHDDAFIKWKVTIIYSLFAIALAVSQIMNKSIIKAMLGKELKADDNIWARVTWYWALFFIGCGVLNVYVAFSLPLETWVNFKVFGLTALTLLNTVISVFYIYKHAQPEQDDTAN | Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis. | Q12P74 |
P92953 | ATHB4_ARATH | Homeodomain transcription factor ATHB-4 | Arabidopsis | MGERDDGLGLSLSLGNSQQKEPSLRLNLMPLTTSSSSSSFQHMHNQNNNSHPQKIHNISWTHLFQSSGIKRTTAERNSDAGSFLRGFNVNRAQSSVAVVDLEEEAAVVSSPNSAVSSLSGNKRDLAVARGGDENEAERASCSRGGGSGGSDDEDGGNGDGSRKKLRLSKDQALVLEETFKEHSTLNPKQKLALAKQLNLRARQVEVWFQNRRARTKLKQTEVDCEYLKRCCDNLTEENRRLQKEVSELRALKLSPHLYMHMTPPTTLTMCPSCERVSSSAATVTAAPSTTTTPTVVGRPSPQRLTPWTAISLQQKSGR | Probable transcription factor. | P92953 |
A1SRS1 | TATA_PSYIN | Sec-independent protein translocase protein TatA | Psychromonas | MGGIGIWQLAIITVIVILLFGTKKLRGIGGDLGGAIKGFKKAIKEDNDKDSTQVDDKDSTQVDDNAKQPSNKKVEENIKEQSKEKDRA | 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. | A1SRS1 |
Q7WGI7 | SYW_BORBR | Tryptophanyl-tRNA synthetase | Bordetella | MNTRVLTGITTTGTPHLGNYAGAIRPAIQASTQPGVDAFFFLADYHALIKCDDPARVARSRLELAATWLAAGLDPERVTFYRQSDIPEITELCWLLTCVTPKGLMNRAHAYKASVDQNAAKGVEPDDGVTMGLFSYPVLMAADILLFNANQVPVGRDQVQHLEMARDIAQRFNHLYGREFFVLPEVVIAEEVATLPGLDGRKMSKSYNNTIPLFEGGAAGLRNATQRIVTDSRLPGEPKDAEASHLYMLYRAFSTQQESMAFRRQLEEGMGWGDAKQALYERLERDLAPMRERYVELISNPGLIEDILQAGAAKARKLAQ... | Catalyzes the attachment of tryptophan to tRNA(Trp). | Q7WGI7 |
Q9TLZ0 | RRP3_CYACA | Probable 30S ribosomal protein 3, chloroplastic | Cyanidium | MKQYKIKVLWLRNNIAIAVDRLIGDSLFPMTYYYFWPRTDAWEQLKIELDSQPGLFAKDKVVILNQVTRIIDYWQENKKSVFPNLSELQSHFPDLICSGCY | Probably a ribosomal protein or a ribosome-associated protein. | Q9TLZ0 |
Q9CAF9 | IOJAM_ARATH | Protein Iojap-related, mitochondrial | Arabidopsis | MLTTLRSRCSSLLLNQSWKLAPNRIFASSPSFSSSAGISNVSEILTLPEVEKILADVKADNVTVIPTHNHCFWADFTVIATGRSDWHLRNIAQALVYRAKQKQKGAKHVMLPSVQGYNSKWIVIDYGKFVVHALDEKARGYFNLESLWSAESSGTDTSDQDLQNVFVKVRPKNNSKRKPAKVSS | May be a ribosome silencing factor involved in organelle biogenesis and required for germination. | Q9CAF9 |
Q9XYZ1 | O162A_CONPL | Omega-conotoxin-like PuIIA | Conus | MKLTCVVIVAVLFLTACQLITAETYSRGEQKHRALSSTDKNSKLTRTCNTPTQYCTLHRHCCSLYCHKTIHACA | Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels (Cav). | Q9XYZ1 |
P0CY98 | DNAK_CUTAC | Heat shock protein 70 | Cutibacterium | MARSVGIDLGTTNSCVAVLEGGEPTVIPNAEGARTTPSVVAFTNSGETLVGEVAKRQAVTNVDRTVRSVKRHMGEAWTMGVDDKTYKPQQISAFILQKLKRDAEAYLGEPVTNAVITVPAYFSDAQRQATKEAGEIAGLAVDRIVNEPTAAALAYGLDKTDKDQTVLVFDLGGGTFDVSLLDISDGVFEVKATNGDNHLGGDDWDQRIVDWLVTQFKNANGIDLAADKMAKQRLQEAAERAKIELSQASETHINLPYITAGAAGPLHLDEKLTRAEFQRMTSDLLERCRTPFNAVMKDAGLNVSQIDEVILVGGSTRMPA... | Acts as a chaperone. | P0CY98 |
B2J8B8 | RL25_NOSP7 | General stress protein CTC | Nostoc | MTITVESLKRPEGSKPRALRRSGLIPANLYGHKGTESISLTIEAKTVERLLKRVSVNNTLIELNIADAPWRGKALLRELQIHPAKGTPYHLSFFAVAGHGDTTVEVRLRFVGTAVGVKQEGGVLDTVITELQVSCAPENIPDVIEIDVTNLQIGDSLSISDIPFPEGVTPLAELERLVVSVLPPQISADDAGTETETAS | This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance. | B2J8B8 |
Q8ZXR6 | TRUA_PYRAE | tRNA-uridine isomerase I | Pyrobaculum | MPYLYRIAYDGTMFYGFTGHPNSLEPRLRLIFGEILGRGSRTDPGVSAVGNVVMTGRKMALGYVNSKMPKGAWAWGIAEVPEGFNPRRAKLRRYLYVAPHWGEDVDVMREAAKLLTGTHDYSSFIQLRGEKHTPTVTTVYDIDVTLRGDLIFIYFAGRGFRNKMIRKMAWALLAAGRGVLSVDDLADLLKKPRPGAVPSAPAEGLVLLDIVYDVKFEVDFSALRKAYVYFLSKSRHLSAHAAALRAAGEALAMWES | Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | Q8ZXR6 |
P17024 | ZNF20_HUMAN | Zinc finger protein KOX13 | Homo | MMFQDSVAFEDVAVSFTQEEWALLDPSQKNLYRDVMQETFKNLTSVGKTWKVQNIEDEYKNPRRNLSLMREKLCESKESHHCGESFNQIADDMLNRKTLPGITPCESSVCGEVGTGHSSLNTHIRADTGHKSSEYQEYGENPYRNKECKKAFSYLDSFQSHDKACTKEKPYDGKECTETFISHSCIQRHRVMHSGDGPYKCKFCGKAFYFLNLCLIHERIHTGVKPYKCKQCGKAFTRSTTLPVHERTHTGVNADECKECGNAFSFPSEIRRHKRSHTGEKPYECKQCGKVFISFSSIQYHKMTHTGEKPYECKQCGKAF... | May be involved in transcriptional regulation. | P17024 |
Q9X0C8 | HIS5_THEMA | TmHisH | Thermotoga | MRIGIISVGPGNIMNLYRGVKRASENFEDVSIELVESPRNDLYDLLFIPGVGHFGEGMRRLRENDLIDFVRKHVEDERYVVGVCLGMQLLFEESEEAPGVKGLSLIEGNVVKLRSRRLPHMGWNEVIFKDTFPNGYYYFVHTYRAVCEEEHVLGTTEYDGEIFPSAVRKGRILGFQFHPEKSSKIGRKLLEKVIECSLSRR | IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF. | Q9X0C8 |
A5W0D5 | ASTD_PSEP1 | Succinylglutamic semialdehyde dehydrogenase | Pseudomonas | MTTHYIAGNWQAGQGETLQSLNPVTQAVIWQGQGADASQVDTAVQAARQAFPAWAQLSLEARIDVLEKFAAQLKVHAEAMAQCIGEETGKPLWESATEVTSMINKVAISVQSYRERTGEKSGPLADATAVLRHKPHGVVAVFGPYNFPGHLPNGHIVPALLAGNCVVFKPSELTPKVAELTVNCWIAAGLPAGVLNLVQGARETGVALAANPGIDGLFFTGSSRTGNLLHQQFAGRPDKILALEMGGNNPLVVDEVKDLDAAVYTIVQSAFISAGQRCTCARRLLVPQGAWGDALIARLVEVCKTITVGAFDEQPAPFMG... | Catalyzes the NAD-dependent reduction of succinylglutamate semialdehyde into succinylglutamate. | A5W0D5 |
Q8F0Q1 | AMPA_LEPIN | Leucyl aminopeptidase | Leptospira | MKLDKNKIQISIGKNPSKTFYKLQLLLKDHFPENLKTKFSFQTASGIFTGENGQIFTDEVEKIIYLGLGETSKIKIRGVAQHFFQFGEKLKKWEGVGLEIHLPKVLTNSLSADLVVYQIVNSLEQGVYAINVLAKEYKENSKKIGNVSFILQDAAKLKEAEKGLKRGKIVSRYINGVRHIAHLPANHFTPEEFVSRSKEIAKDNGLKITVFDEPQLKKEKMGGILSVCEGSDKKAKMILLEYTPVKPITKKKLAIIGKGLTFDSGGISIKPAQDMHEMKYDMCGAATAIHAIGAIAELGLGVPVIAAIGVAENMPDAAAI... | Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. | Q8F0Q1 |
A4VLM9 | NFUA_PSEU5 | Fe/S biogenesis protein NfuA | Pseudomonas | MSAITITEAAHDYLADLLAKQNTTGIGIRIFITQPGTPYAETCIAYCKPGEEKPDDIALALKSFTAWIDGTSEPFLEDALVDYATDRMGGQLTIKAPNAKVPMVNEDSPMNERINYYLQTEINPGLASHGGQVTLIDVVEEGIAVLQFGGGCQGCGQADVTLKEGIEKTLLARIPELKGVRDVTDHTNRENAYY | Involved in iron-sulfur cluster biogenesis. Binds a 4Fe-4S cluster, can transfer this cluster to apoproteins, and thereby intervenes in the maturation of Fe/S proteins. Could also act as a scaffold/chaperone for damaged Fe/S proteins. | A4VLM9 |
C4LL65 | RS7_CORK4 | 30S ribosomal protein S7 | Corynebacterium | MPRKGPAPARQLPKDPVYGDTIVSQLINKVLVDGKKSTAERIVYGALESCREKTGTDPVLTLKKALDNVKPTLEVRSRRVGGATYQVPVEVRPGRATTLALRWLVMFTRQRRENTMTERLAAEILDASNGLGASVKRREDTHKMAEANRAFAHYRW | One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA. | C4LL65 |
Q9ER64 | OSBL5_MOUSE | Oxysterol-binding protein homolog 1 | Mus | MKEEAFLRRRFSLCPPASTPQKTDPRKVPRNLLLGCENELGPITPGRDMESNGPSQPRDEEPQTPGSATKVPLAEYRLCNGSDKECTSPTTRVSKKDALKAQKENYRQEKKRATKQLFSALTDPSVVIMADSLKIRGTLKSWTKLWCVLKPGVLLIYKTPKVGQWVGTVLLHCCELIERPSKKDGFCFKLFHPLDQSVWAVKGPKGESVGSITQPLPSSYLIFRAASESDGRCWLDALELALRCSSLLRLSTCKQGRDGEQGSSPDASPSSLYGLPTSATIPDQDLFPLNGSALENDAFSDKSERENAEDSDAETQDHSR... | Lipid transporter involved in lipid countertransport between the endoplasmic reticulum and the plasma membrane: specifically exchanges phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the plasma membrane in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphat... | Q9ER64 |
Q6FZD9 | RS5_BARQU | 30S ribosomal protein S5 | Bartonella | MAQKERGERDERDGEFVDRLVHINRVAKVVKGGRRFGFAALVVVGDQKGRVGFGHGKAREVPEAVRKATEAAKRGMIYVPLRSGRTLHHDLEGRHGAGRVLLRSASAGTGIIAGGPMRAIFETLGMQDVVAKSLGSSNPYNMVRATFDALKHQMHPRDIAVQRGIKYSILQARRQHLVDAEG | Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. | Q6FZD9 |
Q8TX99 | IDI2_METKA | Type 2 isopentenyl diphosphate isomerase | Methanopyrus | MRERKWEHVLACIWEDVESEESPLFDCVKIVHRALPELDFDDVDMEIELFGKRLSFPLIIAGMTGGHPKTGEINRKLARVARELEIGIGVGSQRAGVKDPEVRWTFEVVREEYPDGLVLANIGLPQLRENGPDLALEVVDMVDADALAVHVNVLQEAVQLEGEADAAGFVDVLAEVCETVDVPVVLKETGAGVSAEDAKLVRDIVDGIDVGGAGGTNWAVVEAVRSKAHGEIPLGYAFSDWGVPTAASILEVRSVVGNDLAIIGTGGVRTGMDVAKVLALGADCAGMALPVLRKVLAEGVRGCVRFLKSIAREVKIAMLM... | 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). | Q8TX99 |
A8F4R6 | RL22_PSELT | 50S ribosomal protein L22 | Pseudothermotoga | MVSENEKTRRPKRSIQHRQNKDENNIEIKAVAKFLRASPRKVRSVANTIRGKSVSEAFQVLEMSPKKAARLIEKVLRSAVANAENNANLSSDSLYISRCFVDDGPRYKRIWPRGRGRADIIQRRMCHVTVAVKSIEAKS | The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome. | A8F4R6 |
B2U4X2 | CMOB_SHIB3 | tRNA U34 carboxymethyltransferase | Shigella | MIDFGNFYSLIAKNHLSHWLETLPAQIANWQREQQHGLFKQWSNAVEFLPEIKPYRLDLLHSVTAESEEPLSTGQIKRIETLMRNLMPWRKGPFSLYGVNIDTEWRSDWKWDRVLPHLSDLTGRTILDVGCGSGYHMWRMIGAGAHLAVGIDPTQLFLCQFEAVRKLLGNDQRAHLLPLGIEQLPALKAFDTVFSMGVLYHRRSPLEHLWQLKDQLVNEGELVLETLVIDGDENTVLVPGDRYAQMRNVYFIPSALALKNWLKKCGFVDIRVVDVCVTTTEEQRRTEWMVTESLSDFLDPHDPSKTVEGYPAPKRAVLIA... | Catalyzes carboxymethyl transfer from carboxy-S-adenosyl-L-methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form 5-carboxymethoxyuridine (cmo5U) at position 34 in tRNAs. | B2U4X2 |
Q70LM8 | LGRE_BREPA | Linear gramicidin dehydrogenase LgrE | Brevibacillus | MQKTHVSPSRWLLSPKMTAEAEVLLFSFHYAGGHAGIYREWQKKLPVQIGVCPVQLPGRSNRFMEPYYTDLSVMIRELAEALLPHLNRPFAFFGHSMGALVSFELARYLRNQYGIKPRHMFASGRHAPHLPDPGEAIHHLPDAEFLKGLRTLNGTPKELFENEENEEILQMLLPMLRADFTICEQYQYQEEEPLGCGLTAIGGWQDPDITVAHMEAWRKHTSASFQMHMLQGDHFFLHSEQEQLLAIIESTLQSYLVGYRGIG | In the final step of gramicidin biosynthesis, reduces the pentadecapeptide-aldehyde intermediate, that is released from the terminal module of the non-ribosomal peptide synthetase LgrD, to the final product ethanolamine-containing gramicidin. | Q70LM8 |
A5E947 | ATPD_BRASB | F-type ATPase subunit delta | unclassified Bradyrhizobium | MAAEDPPVSGVSGRYATALFELARDEKSVDAVKADLDKFNALLDESADLKRLVRSPVFGADVQLKALNAVLDKAGIAGVAANVLRVLTANRRLFAVADVIRAFNALVAKYKGEATADVTVAEPLSDKNLDALKASLKTVTGKDVALNVKVDPAIIGGLVVKLGSRMIDSSLRTKLNSIKHAMKEAG | 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. | A5E947 |
Q9Y9I0 | MPTA_AERPE | GTP cyclohydrolase IV | Aeropyrum | MDVQDLKPPKPLYLERVGFRGVRRRALLETPEGPVTLDLELDVFVDLDRSKRGVHLSRNIEAVEAVVSERRARSIEGLLRSIAKELLSRHGYAEKATVRARTRYYIDLEAAGVKGREPVDVAVTVSLTRSGGERWRVAVSVKGMTVCPSAQSTIAEAEGISDPSRAPSHSQKVLLKGTVDTGKVMVRIEDLARALLQSFSAPTFTLLKKPQEARLILEAFTRPMFVEDVVREAAWRIAAIPYIPGEALLQVEAVSLESIHPHDLVAMLRSRVSEVRSLASRSV | Converts GTP to 7,8-dihydro-D-neopterin 2',3'-cyclic phosphate, the first intermediate in the biosynthesis of coenzyme methanopterin. | Q9Y9I0 |
B1AIM2 | RL23_UREP2 | 50S ribosomal protein L23 | Ureaplasma | MELTRVILHPYTTEKTYSIRNKSEHETLTFIVDKNANKYQIREAFIAIFGLKPLKIRTTNRRPAKIRTSTARPGYTKAKKIAYVVMPVGVKVAVSKEEVEAANAK | One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome. | B1AIM2 |
A7FJ95 | NUDL_YERP3 | Uncharacterized Nudix hydrolase NudL | Yersinia | MSELITGQYLSEFINRFQLQLPQPDNVLTHSHYFSATNRRAAVLIPIICRPEPTLLLTRRADHLRKHAGQVAFPGGKADPDDQSLISTALREAEEEVAIPASVVHVLGKLAPLNSSSGYHVTPIVGLVPANIPFYGNDEEVAGLFEIPLHEALSLSRYHSLDIHREGINHRVYLSWYENQFIWGLTATIIRHLAQQVSI | Probably mediates the hydrolysis of some nucleoside diphosphate derivatives. | A7FJ95 |
B7LR56 | MURA_ESCF3 | UDP-N-acetylglucosamine enolpyruvyl transferase | Escherichia | MDKFRVQGPTKLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDVDTSMKLLSQLGAKVERNGSVHIDARDVNVFCAPYELVKTMRASIWALGPLVARFGQGQVSLPGGCSIGARPVDLHISGLEQLGATIKLEEGYVKASVEGRLKGAHIVMDKVSVGATVTIMCAATLAEGTTIIENAAREPEIVDTANFLVTLGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTFLVAAAISRGKIICRNAQPDTLDAVLAKLRDAGADIETGDDWISLDMHGKRPKAVNVRTAPHPAFPTDMQAQFTLLNLVAEGT... | Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. | B7LR56 |
A1BGN6 | KAD_CHLPD | Adenylate monophosphate kinase | Chlorobium | MRIILLGAPGAGKGTQASYICKTLNIPQISTGDMLRAAVQAQTPVGIEAKKVMDAGKLVSDEIILALVKERLASQDCINGCLFDGFPRTIAQAESLKNDSILLDYVMEIHVDDKEIIERMSGRRVHLSSGRTYHVRFNPPKKEGLDDLTGEPLVQREDDQEETVKKRLQIYHDQTAPLLQYYHDWSLTGSPDAPRYSSIKGTGSVEEIRQRILDALNS | Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. | A1BGN6 |
Q4R9C4 | G2E3_MACFA | G2/M phase-specific HECT-type E3 ubiquitin transferase | Macaca | MNENKPGDSQNLACVFCRKNDDCPNKYGEKKTKEKWNLTVHYYCLLMSSGIWQRGKEEEGVYGFLIEDIRKEVNRASKLKCCVCKKNGASIGCVAPRCKRSYHFPCGLQRECIFQFTGNFASFCWNHRPVQIITSNNYRESLPCTICLEFIEPIPSYNILRSPCCKNAWFHRDCLQVQAINAGVFFFRCTICSNSDIFQKEMLRMGIHIPEKDASWELEENAYQELLQHHERCDVRRCRCKEGRDYNAPDSKWEIKRCQCCGSSGTHLACSSLRSWEQNWECLECRGIIYNSGEFQKAKKHVLPNSNNVGITDCLLEESS... | E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Essential in early embryonic development to prevent apoptotic death. | Q4R9C4 |
A1S3U9 | ANMK_SHEAM | AnhMurNAc kinase | Shewanella | MSQSLFIGLMSGTSMDGVDAVLVDFDTPSPKLIATHTEAIPEHLFKGLQRLCQPGQDEVNRLGRLDRSVGSLFAKAVNNLLASSGIDKSQVVAIGSHGQTVRHMPNLEVGFTVQIGDPNTIAAETGIDVIADFRRKDIALGGQGAPLVPAFHQQIFAKADKRRVILNIGGIANITWLPGNAEAVLGFDTGPGNTLIDGWIQQVKQQAFDRDGAFAASGKTDNTLLAQLLSHPYFMQPYPKSTGRELFNNAWLEQQLEKFGHLDEADIQSTLLDLTCHSIAADILKLSNSGELFVCGGGALNIELMNRLQALLPGFTLTTT... | Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall ... | A1S3U9 |
P03893 | NU2M_MOUSE | NADH dehydrogenase subunit 2 | Mus | MNPITLAIIYFTIFLGPVITMSSTNLMLMWVGLEFSLLAIIPMLINKKNPRSTEAATKYFVTQATASMIILLAIVLNYKQLGTWMFQQQTNGLILNMTLMALSMKLGLAPFHFWLPEVTQGIPLHMGLILLTWQKIAPLSILIQIYPLLNSTIILMLAITSIFMGAWGGLNQTQMRKIMAYSSIAHMGWMLAILPYNPSLTLLNLMIYIILTAPMFMALMLNNSMTINSISLLWNKTPAMLTMISLMLLSLGGLPPLTGFLPKWIIITELMKNNCLIMATLMAMMALLNLFFYTRLIYSTSLTMFPTNNNSKMMTHQTKT... | Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I. | P03893 |
Q7U363 | TRUA_BORPE | tRNA-uridine isomerase I | Bordetella | MSRIALGLAYDGSAWQGWQTQPHGVTVQDQVEAALASFAGGGGPVATVCAGRTDTGVHAAMQVIHLDTDLQRRDESWVRGVNAFLPPSIVVQWARPVSEAFHARFSARSRTYVYLLWRGRVRPALWAGRAGWAFQPLDVPAMRAAARALLGEHDFSSFRSSQCQARHPVRTLHRLDIDERGAFLVFTLRANAFLHHMVRNLIGALLQVGQGREPVAWMDALLCARDRRLGAPTFMPDGLYLSAIEYPAEFGFDELDGGITLLSPFTGALG | Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | Q7U363 |
P80317 | TCPZ_MOUSE | CCT-zeta-1 | Mus | MAAVKTLNPKAEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEQVKVSKEMDRETLIDVARTSLRTKVHAELADVLTEAVVDSILAIRKKDEPIDLFMVEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVENAYILTCNVSLEYEKTEVNSGFFYKSAEEREKLVKAERKFIEDRVKKIIELKKKVCGDSDKGFVVINQKGIDPFSLDALAKEGIVALRRAKRRN... | Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. The TRiC complex plays a role in the folding of actin and tubulin. | P80317 |
Q13U85 | PROA_PARXL | Glutamyl-gamma-semialdehyde dehydrogenase | Paraburkholderia | MDIDQYMTDLGRRARQASRAMARASTAAKNAALAAVAEAIERDAASLKEANARDVAKAREKGHDAAFIDRLTLSDKALKTMVEGLRQVAALADPIGEISNLKYRPSGIQVGQMRVPLGVIGIIYESRPNVTIDAAALCLKSGNATILRGGSEALECNTALAKLIGEGLEAAGLPQDAVQVVATSDRAAVGKLITMTEYVDVIVPRGGKSLIERLMNEARVPMIKHLDGICHVYVDDRADLTKALTVCDNAKTHRYGTCNTMETLLVARGIAAEVLPPLGKLYRDKQVELRVDAAARAVLADAGVGPLGDATEEDWRTEYL... | Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. | Q13U85 |
A7ZHK9 | SPED_ECO24 | S-adenosylmethionine decarboxylase alpha chain | Escherichia | MKKLKLHGFNNLTKSLSFCIYDICYAKTAEERDGYIAYIDELYNANRLTEILSETCSIIGANILNIARQDYEPQGASVTILVSEEPVDPKLIDKTEHPGPLPETVVAHLDKSHICVHTYPESHPEGGLCTFRADIEVSTCGVISPLKALNYLIHQLESDIVTIDYRVRGFTRDINGMKHFIDHEINSIQNFMSDDMKALYDMVDVNVYQENIFHTKMLLKEFDLKHYMFHTKPEDLTDSERQEITAALWKEMREIYYGRNMPAV | 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. | A7ZHK9 |
Q136S5 | PLSX_RHOPS | Phosphate-acyl-ACP acyltransferase | Rhodopseudomonas | MPQKVRIALDAMGGDFGPSVVIPGAAIALGRHPDAEFLLFGDSALIDKELAAHPALKKVSRVVHTDVAVSMHDKPSQALRRGRKVSSMWLAIEAVKKGEADVAVSAGNTGALMAMARFCLRTLPGIDRPAIAATWPTVRGDSVVLDLGATIGGDAAHLKALAVMGAAMASVLFDLERPTVGLLNIGVEEIKGGEEIREAAELLRAMQSPPFEFIGFVEGDGIGSGAADVIVSEGFSGNIALKAAEGTARQIIQLLRDAMSRTWSAKIGYLFARGAFRALRDKIDPNKSNGGVFLGLNGIVVKSHGGTNADGFAYAVDVSY... | Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA. | Q136S5 |
Q8X8N8 | PYRC_ECO57 | Dihydroorotase | Escherichia | MTAPSQVLKIRRPDDWHLHLRDGDMLKTVVPYTSEIYGRAIVMPNLAPPVTTVEAAVAYRQRILHAVPAGHDFTPLMTCYLTDSLDPNELERGFNEGVFTAAKLYPANATTNSSHGVTSVDAIMPVLERMEKIGMPLLVHGEVTHADIDIFDREARFIESVMEPLRQRLTALKVVFEHITTKDAADYVRDGNERLAATITPQHLMFNRNHMLVGGVRPHLYCLPILKRNIHQQALRELVASGFNRVFLGTDSAPHARHRKESSCGCAGCFNAPTALGSYATVFEEMNALQHFEAFCSVNGPQFYGLPVNDTFIELVREEH... | Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. | Q8X8N8 |
P0C815 | PSMA4_STAA1 | Phenol-soluble modulin alpha 4 peptide | Staphylococcus | MAIVGTIIKIIKAIIDIFAK | Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection. | P0C815 |
P14171 | BLAC_RHOCA | Penicillinase | Rhodobacter | MRFTATVLSRVATGLALGLSMATASLAETPVEALSETVARIEEQLGARVGLSLMETGTGWSWSHREDELFLMNSTVKVPVCGAILARWDAGRLSLSDALPVRKADLVPYAPVTETRVGGNMTLDELCLAAIDMSDNVAANILIGHLGGPEAVTQFFRSVGDPTSRLDRIEPKLNDFASGDERDTTSPAAMSETLRALLLGDVLSPEARGKLAEWMRHGGVTGALLRAEAEDAWLILDKSGSGSHTRNLVAVIQPEGGAPWIATMFISDTDAEFEVRNEALKDLGRAVVAVVRE | Hydrolyzes beta-lactams antibiotics. Rates of hydrolysis relative to benzylpenicillin =100: ampicillin = 27, carbenicillin = 25, cloxacillin = 0, cephaloridine = 4. | P14171 |
Q02V26 | KPTA_PSEAB | Probable RNA 2'-phosphotransferase | Pseudomonas | MDRKTLDDTSKFLSYVLRHQPEAIGLKLDGEGWADIDALIAGAARDGRALDRALLGAVVENNDKKRFALSADGQRIRAVQGHSHAAVAIAYAPAVPPAVLYHGTASRFLDSIRERGLVPGSRHHVHLSARRATALEVGRRYGSPVLLEIDARDMHLAGHLFHQAENGVWLTERVPVRFIREA | Removes the 2'-phosphate from RNA via an intermediate in which the phosphate is ADP-ribosylated by NAD followed by a presumed transesterification to release the RNA and generate ADP-ribose 1''-2''-cyclic phosphate (APPR>P). May function as an ADP-ribosylase. | Q02V26 |
A7ZMA0 | PDXH_ECO24 | Pyridoxal 5'-phosphate synthase | Escherichia | MSDNDELQQIAHLRREYTKGGLRRRDLPADPLTLFERWLSQACEAKLADPTAMVVATVDEHAQPYQRIVLLKHYDEKGMVFYTNLGSRKAHQIENNPRVSLLFPWHTLERQVMVIGKAERLSTLEVMKYFHSRPRDSQIGAWVSKQSSRISARGILESKFLELKQKFQQGEVPLPSFWGGFRISLEQIEFWQGGEHRLHDRFLYQRENDAWKIDRLAP | Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). | A7ZMA0 |
Q5B7X2 | MANA_EMENI | Endo-beta-1,4-mannanase A | Aspergillus subgen. Nidulantes | MKFSQALLSLASLALAAALPHASTPVYTPSTTPSPTPTPSASGSFATTSGIQFVIDGEAGYFPGSNAYWIGFLKNNSDVDLVFDHMASSGLRILRVWGFNDVNTAPTDGSVYFQLHQDGKSTINTGKDGLQRLDYVVHSAEKHGIKLIINFVNYWDDYGGMNAYMRAYGGGDKADWFENEGIQAAYQAYVEAVVKRYINSTAVFAWELANEPRCTGCEPSVLHNWIEKTSAFIKGLDEKHLVCIGDGSDGSYPFQYTEGSDFAAALTIDTIDFGTFHLYPDSWGTNNDWGKLWITSHAAACAAAGKPCLFEEYGVTSNHC... | Endo-1,4-mannanase that catalyzes the random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans and heteromannans. It is a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Active against locust bean gum and gum guar . Also has transglycosylation activity . | Q5B7X2 |
A0NBD9 | OBP66_ANOGA | General odorant-binding protein 66 | Anopheles | MATTIARIGSANWAKVLVLLWLVQLATAGEPNPACKTMPTVDKDNEDKCCDVPEMFPNETLNACMEEYQKSSKPPLQKSCEITTCVLKKQSLIKSDNTVDKDKIKSYIKEMVKGSDEWKTLVEKAVLEECLPLMDKDPSNVLSKLKSSLGDCDPAPALTIACAAAKFYVNCPAKDRTKSPMCDEWRTFLSKCSNSLEDLNAIFMVLENQKTR | Present in the aqueous fluid surrounding olfactory sensory dendrites and are thought to aid in the capture and transport of hydrophobic odorants into and through this fluid. | A0NBD9 |
O51461 | DER_BORBU | GTP-binding protein EngA | Borreliella | MLSYKKVLIVGRPNVGKSALFNRILDTKRSITESTYGVTRDLVEEVCKVDSFKFKLIDTGGFTILKDEISKIVVQKVLSSLEKVDLILLVLDINEILLEDYQIIERLRKYSSKVVLVLNKVDTKDKECLAHEFHNLGFKRYFLVSAAHCRGITKLRDFLKVEVGEVGIESGADIKVGIIGKPNSGKSTLINYLSGNEIAIVSDQPGTTRDFIKTKFTRNGKVFEVVDTAGIRRRARVNEIVEYYSVNRALKVIDMVDIVFLLIDVQEKLTSQDKKIAHYVTKKGKGIVIVFSKWDLVDESKGYFEALKSHVKFFFPILNF... | GTPase that plays an essential role in the late steps of ribosome biogenesis. | O51461 |
B2I6F8 | HRCA_XYLF2 | Heat-inducible transcription repressor HrcA | Xylella | MCASFSPTLDSRSRQLLRTLISCYIQNGEPIGSKTLAQQAGLDISPATIRNILADLEELGLLNSPHTSAGRVPTAHGYRMFVDSLVQMQPPSEDDIRRLRVEMTGGGTQTLLGSASEILSAMTHFVGVVSAPRREQFVFRHIDFVPLDARQIMAILIFADNEVQNRVIEPRRVYEPGELERVSNYLNAHFIGRTLADIRTTVLCELRKAKDEMEQLLAHSLDLASQMLVPNDSEDIVVTGQTRLMALQDLSDMDRLRELFEIFASKREILQLLERTIDAPGVRIFIGEETGMVSMEDISLVTAPYAAHGQVLGVLGVIGP... | Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons. | B2I6F8 |
Q5XI02 | PDILT_RAT | null | Rattus | MELLWTPLLLLAACLSEVLGSPEMDTGINISQPLHILEDHNLMVLTPAGLTQTLNETRFLMVIFHNPTLKQSRKLAKELGKAAEIFGKGKNGLGFGKVDITMETELKQEFDITHAPELKLFYEGNRLEPISCKDVVESTALVVWLRRQISKKALLFNNSNEVADFVKSRPLVIVGFFQDLEEEVAELFYDTIKDFPELTFGAIQIKNSFGRFHVILDSVLVFKKGRVVKRQELINDSTNKDYLNQVIKQQLTGFVIEFNPENKDLIYEMNILNHMLLFISKNSEPYSTIIRHYRQISKEFQNKILFVLVNSDEPKNKRIF... | Probable redox-inactive chaperone involved in spermatogenesis. | Q5XI02 |
Q62780 | DDX46_RAT | Helicase of 117.4 kDa | Rattus | MGRESRHYRKRSASRGRSGSRSRSRSPSDKRSKRGDDRRSRSRDRDRRRERSRSRDKRRSRSRDRKRLRRSRSRERDRSRERRRSRSRDRRRSRSRSRGRRSRSSSPGSKSKKAENRSRSKEKAEGGDSSKEKKKDKDDKEDEKEKDAGNFDQNKLEEEMRKRKERVEKWREEQRKKAMENIGELKKEIEEMKQGKKWSLEDDDDDEDDPAEAEKEGNEMEDEELDPLDAYMEEVKEEVKKFNMRSVKGGAGNEKKSGPTVTKVVTVVTTKKAVVDADKKKGELMENDQDAMEYSSEEEEVDLQTALTGYQTKQRKLLEP... | Plays an essential role in splicing, either prior to, or during A complex formation. | Q62780 |
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