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 |
|---|---|---|---|---|---|---|
Q2RVE4 | GLMM_RHORT | Phosphoglucosamine mutase | Rhodospirillum | MAKRTLFGTDGVRGTANREPMTADTALRIGMAAGHLLRNGDHRHTVVIGKDTRLSGYMLEPALAAGFISVGMDVVLLGPLPTPAVAMLTRSLRADLGVMITASHNPFQDNGIKLFGPDGYKLSDDQEATIEALLDNGLEGHRAGPTALGKARRLDDCNGRYVEFVKSTFPRGRRLEGLRIVVDCAHGAAYRVAPKVLWELGATIVPIGVTPDGTNINKDCGSLHSRVMCETVVREGADLGVALDGDADRVVLCDEKGALVDGDQLLALIGRNWKRAGTLQGGGVVATVMSNLGLERFLKDEGLALARTPVGDRYVVEHMR... | Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. | Q2RVE4 |
O01578 | MPC2_CAEEL | Probable mitochondrial pyruvate carrier 2 | Caenorhabditis | MGPHRLLYQALCKAGDKFVYPVLPAFAKPAWNHAAGPKTVFFWAPTIKWTLIGAGLADLARPADKLSLYQNSALFATGAIWTRYCLVITPINYYLSSVNFFVMCTGLAQLCRIAHYRYQNPDWETKEIMETHN | May mediate the uptake of pyruvate into mitochondria. | O01578 |
P31698 | GSPC1_DICCH | Pectic enzymes secretion protein OutC | Dickeya | MNISKLPPLSPSVIRRILFYLLMLLFCQQLAMIFWRVGLPDNSPVASVQITPAQARQQPVTLNDFTLFGVSPEKNRSGALDASQMSNLPPSTLNLSLTGVMVGDDTARSIAIISKDNEQFSRGVNEEVPGYNAKIVSIRPDKVVLQYQGRYEVLGLYNQEENSADGVSGAQLNEQLQQRASTTMSDYVSFSPVMNDNKLHGYRLNPGPKSDSFYRVGLQDNDMAVALNGLDLRDEEQAKKAMERMADVHNFTLTVERDGQRQDIYMEFGGDE | Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins. Required for the translocation of the multiple pectic enzymes. | P31698 |
Q725Q9 | FMT_DESVH | Methionyl-tRNA formyltransferase | Desulfovibrio | MAESAPLKIVFMGTPDFAAASLRHLLAWDGCDVVGVYTQPDRPCGRGQQCRPSAVKMLALEHGLDVRQPVSFRDEADVQALRDFGADILVVAAYGLILPQSVLDAAPMGAVNVHGSLLPRYRGAAPIQRAVMNGDAVTGITIMQVVKQLDAGPMLLQKALGIGCDETSGQLHDQLAELGGRLLVETLARLRAGTIMPIPQDDALATYAAKLTKADGLVDWNRTAVEVHAQVRGVTPWPAAYFTLRREGQKDVRVTIEPGTIGPLLEQPAVPGTIVGLVDGAIAFACADRTYLVRTIRPADKKPMTGEAFWCGYLSRCEGE... | Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. | Q725Q9 |
Q8U4L8 | RISB_PYRFU | 6,7-dimethyl-8-ribityllumazine synthase | Pyrococcus | MKVRTFEGDYRGEGLRIAVVVSRFNDLLTEELLKGALDCFKRHGVEEVHIFRVPGSFEIPITVKKIAKRGYDAILALGVLIKGETRHFELVASQVSRGIAQVSLEEGIPVIFGIVPAEDEIQAISRSGIKSNRGFEYALTTIEMANLFRKLGENNER | 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. | Q8U4L8 |
Q6MGL5 | MNME_BDEBA | tRNA modification GTPase MnmE | Bdellovibrio | MGPMIRGDRDKDTICAISTPHGVGGISVIRVSGPQTLNIVSKICQFLPAHPESHKVYFGNLKNSQTGDEIDEVLATYFKEGRSFTGEEVIEISCHGSPLICQTILNQLVNLGARPADRGEFTFRAFMNGKLDLVQAESVLSLIESQSQQAAKLALRQLKGTLSHKLEEIEDDMTWILAHAEASIDFSTEGIEVIEENVIQVRLKKIEAGLKELVATFKVGRLLKDGFRIVLTGLPNVGKSSLLNLFLEDERAIVTDIPGTTRDVIHGDTTFEGVKFTFVDTAGLRDEATDLVERIGIQKSYEAQNESDVVFFVYDIEKGL... | Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34. | Q6MGL5 |
B1VMC3 | PURA_STRGG | IMP--aspartate ligase | Streptomyces | MPALVLLGAQWGDEGKGKATDLLGGSVDYVVRYQGGNNAGHTVVVGDQKYALHLLPSGILSPGCTPVIGNGVVVDPAVLLSELSGLNERGVDTSKLLISGNAHLITPYNVTLDKVTERFLGKRKIGTTGRGIGPTYADKINRVGIRVQDLYDESILEQKVEAALEQKNQLLAKVFNRRAIEAGKVVEDMLQYAEQIKPFVADTTLILNDAIDEGKVVLFEGGQGTLLDVDHGTYPFVTSSNPTAGGACTGAGVGPTKISRVIGILKAYTTRVGAGPFPTELHDEDGEALRRIGGERGVTTGRDRRCGWFDAPIARYATRV... | 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. | B1VMC3 |
Q6P8X9 | FLTOP_MOUSE | Cilia- and flagella-associated protein 126 | Mus | MATNYSANQYEKAYLPTYLQNWSPARPTKEKIAAHEGYTQIIANDRGHLLPSVPRSKASPWGSFMGTWQMPLKIPPAKVTLTARTTTAADNLTKWIHKNPDLLNACNGLRPEISGKPFDPDSQTKQKKSVTKTVQQAPNPTIIPSSPVIQGDNPDEPQSSHPSAGHTPGPQTPVNSPNNPPPSPCKSTK | Acts as a regulator of cilium basal body docking and positioning in mono- and multiciliated cells. Regulates basal body docking and cilia formation in multiciliated lung cells. Regulates kinocilium positioning and stereocilia bundle morphogenesis in the inner ear. | Q6P8X9 |
Q8EC56 | MLTF_SHEON | Murein lyase F | Shewanella | MTRFLFAIILGLLLTACQQETVEETEFVPHKLTELRVGTLYGPQIYMTSGQGNSGFDYDMAVLFAEYLDVPLKMVPYTNLAELYDALKKNEIDIIAAGMTETPARREHFRLGPPLYRVNQVLVYREGMPAPKDISDLKGKITVIADSSFVETLTQLQKRHPTLVWDQVTDKDNEELLTMIANKEIDYTIADSSSVQINRRYLPVLRSGLVLEEKLNVVWLLPPTHSDGLMSQLLAFWHQEKLAGTLDHLNEKYFGHVKRFDYIDTRAFLRAIETVLPRYRQHFETHAGDLDWRKLAATSYQESHWNPNARSPTGVRGMMM... | Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space wit... | Q8EC56 |
Q9HNI8 | PHNC_HALSA | Phosphonates import ATP-binding protein PhnC | Halobacterium | MSNITVTNLHKSYGDVDALEDVSFEILDGEFVVILGESGAGKSTLLRCLNGLTEPTTGSVKIDGEPVNGPRDDVGMIFQQHNIIEEMTAYTNALSGSLNRTSLVRSLFQWNDREEKLDALRALDTVGLLDDAEQRAGRMSGGQQQRVGISRALVQDPNLLLADEPVASLDPASAESVMGYIKDAADQHDLTTLASLHQVNLAREFGQRFIGMKDGRVIFDGYRDDLTFDVIDDIYGNIQTDAIRTGDDANADVAPTTSSDGGTDAAGGPDQQPASDPHLS | Part of the ABC transporter complex PhnCDE involved in phosphonates import. Responsible for energy coupling to the transport system. | Q9HNI8 |
Q72TM7 | KDPA_LEPIC | Potassium-translocating ATPase A chain | Leptospira | MVTEWIQLLIFLFALLIFSPLFGLGLYKVYLYKTSGFEKFLYKICGIDPNRNMDWKEYALSLLVFNFFGFLLLFLILFFQNYLPLNPENFPGLVWDLAFNTAVSFTTNTNWQAYSGESTLSFFSQMAGLTTQNFLSATTGLCVLLALSRGISVNYNVFALGNFWKDMIRGTLYVLLPLSFIFALFLVGFGVVQTFSESVSAITLEGNTQIIPLGPVASQVAIKQLGTNGGGYFGVNASHPFENPSPISNFLQMFSILILPGACVFLYGRITGSIRHAWAIFSVMFTILCVGILIVWTFESSWNPISGTLGFWEGKEIRFG... | Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the periplasmic potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel. | Q72TM7 |
Q9H6S1 | AZI2_HUMAN | TILP | Homo | MDALVEDDICILNHEKAHKRDTVTPVSIYSGDESVASHFALVTAYEDIKKRLKDSEKENSLLKKRIRFLEEKLIARFEEETSSVGREQVNKAYHAYREVCIDRDNLKSKLDKMNKDNSESLKVLNEQLQSKEVELLQLRTEVETQQVMRNLNPPSSNWEVEKLSCDLKIHGLEQELELMRKECSDLKIELQKAKQTDPYQEDNLKSRDLQKLSISSDNMQHAYWELKREMSNLHLVTQVQAELLRKLKTSTAIKKACAPVGCSEDLGRDSTKLHLMNFTATYTRHPPLLPNGKALCHTTSSPLPGDVKVLSEKAILQSWT... | Adapter protein which binds TBK1 and IKBKE playing a role in antiviral innate immunity . Activates serine/threonine-protein kinase TBK1 and facilitates its oligomerization . Enhances the phosphorylation of NF-kappa-B p65 subunit RELA by TBK1 . Promotes TBK1-induced as well as TNF-alpha or PMA-induced activation of NF-k... | Q9H6S1 |
A7MR02 | RLMM_CROS8 | 23S rRNA 2'-O-ribose methyltransferase RlmM | Cronobacter | MNKVILYCRQGFEKECAAEITDKAAQQGVFGFARVKENSAYVIFECYQPDDADKLARELPFSSLIFARQMFVAGELLQDLPPEDRVTPVVGMLQGVVEKGGELRVEVADTNESKELMKFCRKFTVPLRTALRDAKILANFETPKRPVVHVFFIAPGCCYTGYSYTNNNSPFYMGIPRLKFPADAPSRSTLKLEEAFHVFIPADEWDERLANGMYAVDLGACPGGWTYQLVKRNMWVASVDNGPMAQSLMDTGQVTWLREDGFKYRPTRTNITWMVCDMVEKPAKVAALMAQWLVNGWCRETIFNLKLPMKKRYEEVSQNI... | Catalyzes the 2'-O-methylation at nucleotide C2498 in 23S rRNA. | A7MR02 |
Q64ZV9 | RNC_BACFR | Ribonuclease III | Bacteroides | MLRNKIDKIRLLFRKDRESYSCFYRILGFYPRNIRLYEQALLHKSTAVRSEKGRPLNNERLEFLGDAILDAIVGDIVYQHFEGKREGFLTNTRSKIVQRETLNKLAVEIGLDKLIKYSTRSSSHNSYMYGNAFEAFIGAIYLDRGYECCKQFMERRIIEPYIDLDKLSRKEVNFKSKLIEWSQKNKMEVSFELIEQSLDKENNPVFQTEVRIEGILGGSGTGYSKKESQQNAAQMTLKKIKGDPEFMASVQEAKTQNNVPAEDTTPESEMSLTAENQQIDEIISTEEISV | Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism. | Q64ZV9 |
Q4USF9 | RECO_XANC8 | Recombination protein O | Xanthomonas | MLIEHERGFVLHARAWRETSLLVEVLTEQHGRVGLLARGVHGPRKQALRAALQPLQLIQFTAVQRGELAQLRQAEAIDTAPRLLGEAMLAGFYISELLLRLAPRHAPVPELFDCYAQARAHLASGAALAWGLRQFERDVLDGLGFGFDLQHDSDGQPIDPAARYRLDPQDGARRVLSERLAQDRRETVTGAALLALGEDRVPATEDMPGLRRSMRGVLLHHLSGRGLKSWEMLEELARRGA | Involved in DNA repair and RecF pathway recombination. | Q4USF9 |
C4K0Z4 | UVRB_RICPU | Excinuclease ABC subunit B | spotted fever group | MNNFSIISEYKPAGDQPKAIDEIIAGLSSKKRSQMLLGITGSGKTFTMANIIERTNRPTLIMAHNKTLAAQIYSEMKSLFPKNAVEYFVSYYDYYQPEAYIARTDTFIEKDSSINEQIDLMRHAATRSLLERRDVIVVSSVSCIYGLGSPDLYYQMMVNLEPGQSYLRDQLLNDLINLQYERNDIGFERGCFRVKGDNIDIFPSHYSDKAWRLSFFGNELEYIHEFDPLTGEKLAKLDKAMVFGNSHFVMPQETVNNAISGIEEELQKRLEFLKSQDKPLETQRLNQRTQYDLEMLTETGSCKGVENYSRFFTGRHAGEP... | The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP bindi... | C4K0Z4 |
A1WL86 | ENO_VEREI | 2-phosphoglycerate dehydratase | Verminephrobacter | MSAIVDIVGREVLDSRGNPTVECDVLLESGVMGRAAVPSGASTGSREAIEMRDGDPRRYQGKGVLKAVEHVNTEISEAVLGLDASEQAFLDKTLIDLDGTENKSRLGANAMLAVSMAVARAAAEESGLPLYRYLGGMGSVQLPVPMMNVINGGAHANNSLDLQEFMIIPVGAPNFREALRWGAEVFHALKKIIHDLGMSTAVGDEGGFAPSVENHEAAIRLILQAITAAGYSAGEQIALGLDCAASEFYQDGLYVLHGEGGLKLSAPQWIDMLAAWVDKYPIISIEDGMHEGDQDGWKQLSERLRDKVQLVGDDLFVTNT... | Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. | A1WL86 |
Q3B7M6 | NEDD1_BOVIN | Neural precursor cell expressed developmentally down-regulated protein 1 | Bos | MQENLRFASSGDDVKIWDASSMTLVDKFNPHTAPHAISSVCWSSNNNFLVTASSSGDKIVVSSCKCKPVPLLELGEGQKQTCVSLNSTSMYLVSGGLNNTVNIWDLKSKRVHRSLKDHKDEVTCVTYNWNDCYIASGSLSGEIILHSVTTNLSSTPFGHGSNQSIRHLKYSLFKKSLLGSVSDNGIVTLWDVNSQSPYHNFDSTHKAPASGICFSPVNELLFVTVGLDKRIILYDTSSKKLVKTLVADAPLTAVDFMPDGATLAIGSSRGKIYQYDLRMLKSPIKTISAHKTSVQCIAFQYSTVLSKSGLNKGCSNKPTA... | Required for mitosis progression. Promotes the nucleation of microtubules from the spindle. | Q3B7M6 |
Q9SRL4 | ENAS2_ARATH | Endo-beta-N-acetyglucosaminidase 85B | Arabidopsis | MPKSNDDDVAQSEAVPLLDLVKPSLPISFPIKALQDLKSRSYFDSFHFQFNRSTVPFRRNSDCLPNRPRVLVCHDMKGGYVDDKWVQGCENEAGFAIWHWYLMDIFVYFSHSLVTIPPPCWTNTAHRHGVKVLGTFITEWDEGKATCKEMLATKESAQMYAERLAELATALGFDGWLINIENDIDEEQIPNMKEFVSHLKKVLHLSTPGALVIWYDSVTVRGNLQWQDQLTELNKPFFDLCDGIFMNYTWKESYPNLSAEVAGDRKFDVYMGIDVFGRGSFGGGQWTVNAALDLLKRNNVSAAIFAPGWVYETAQPPNFH... | Endoglycosidase that releases N-glycans from glycoproteins by cleaving the beta-1,4-glycosidic bond in the N,N'-diacetylchitobiose core. Involved in the production of high-mannose type N-glycans during plant development and fruit maturation. | Q9SRL4 |
Q9Z1K8 | YLAT1_MOUSE | y(+)L-type amino acid transporter 1 | Mus | MVNSTKYEVAAQHEADDGSALGDGASPVAEQVKLKKEISLLNGVCLIVGNMIGSGIFVSPKGVLMYSASFGLSLVIWAVGGIFSVFGALCYAELGTTIKKSGASYAYILEAFGGFLAFIRLWTSLLIIEPTSQAVIAITFANYMVQPLFPSCGAPYAAGRLLAAACICLLTFINCAYVKWGTLVQDIFTYAKVLALIAVIIAGIVRLGQGATANFENSFEGSSFAMGDIALALYSALFSYSGWDTLNYVTEEIRNPERNLPLSIGISMPIVTIIYLLTNVAYYSVLDIKEILASDAVAVTFADQIFGVFNWIIPVAVAFS... | Involved in the sodium-independent uptake of dibasic amino acids and sodium-dependent uptake of some neutral amino acids. Requires coexpression with SLC3A2/4F2hc to mediate the uptake of arginine, leucine and glutamine. Plays a role in nitric oxide synthesis via transport of L-arginine, and is involved in the transport... | Q9Z1K8 |
Q2GHT4 | LOLD_EHRCR | Lipoprotein-releasing system ATP-binding protein LolD | Ehrlichia | MSTVFALANIYKSFGRNKEVPVIVNATLQIKKGEIVALIGKSGSGKSTLLHIAGLLDTPSSGSILLNNIECTDKTSDKDKTYLRRHFLGFIYQFHHLLQEFSVLENVMLPQIITGKSKSIAKKNAMEILERVRLQDKLSMPISQLSGGERQRVAIARSLINCPLIVLADEPTGSLDNNTALEVFSLLQEYAKEKNIAILLATHNYSLAQKACRIVKIDSGILRSYSIDESGFNKI | Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner. | Q2GHT4 |
P25806 | TPR_PORGI | Thiol protease | Porphyromonas | MEKKLVPQSISKERLQKLEAQATLTPQQEEAKARKIEREKARLKELNIPTESKESKDCSPAGMINPYALTEVILERPLDWSNPRTTDIVERVLGSSMQDLSKGDSVLRAGRDQNAEVKIVDSVLTKTQRGQDGLERILESFNDYDMPPEEKEEAAPKAKKAAQKLDIDDLREQALSSTTITKEISKIILPTKNLRDDNNTVHQYREVGFQSNGAHNLWDTVVQGIAGDCYMLAALSAIAWVWPALLNMDVDIMSNQDEWRLYRYFIGRSKQTYARPSGSGTSTNEILQEGYYKVPIFARSRYWFNGEYWPALFEQAYANW... | Thiol protease. Probably an important virulence factor. | P25806 |
Q8TWY8 | GLMM_METKA | Probable phosphoglucosamine mutase | Methanopyrus | MGKYFGTSGIRGRVGEFLTPELALRAGRALGEYLGGGTVAVGRDTRVHCDALRAAVISGLTAQGCDVVDIGVVCTPTLGCYVATEGLDAGVMITASHNPPEYNGIKFWDSDGMAFSPEQEREIEQIMDGDLEYPNWDEYGEVVDDETALNVHVERILDEVSVDGDGLRIVVDCANGPSAFVTPVVLREMGCEVISLNAHPDGHFPGREPEPKPENLKDLMRTVRATDADLGIAHDGDADRVVFVTEEGKFAGYDEVLALVCRRILEEKGPGKVAVNVDASMVIDEVVREMGGEVVRTKVGDVHVAAAIREEGCVFGGEPN... | Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. | Q8TWY8 |
Q92SI3 | TRMB_RHIME | tRNA(m7G46)-methyltransferase | Sinorhizobium | MTETRGARATEAFFGRRKGKPLRERQAAHLEHLLPLLKLDLEEPAPADLTALFPEPVERIRLEIGFGGGEHLIHRAAEDPATGFIGVEPFVNSMAKLLGQIEAKAIRNIRLYDDDATQVLDWLPAASVDQIDLLYPDPWPKRKHWKRRFVSQINLDRFARILKPGGLFCFASDIDSYINWTLIHCREHAAFEWTAERAADWLTPFAGWPSTRYEAKARREGRSSAYLAFRRA | Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. | Q92SI3 |
B2HGR0 | SEPF_MYCMM | Cell division protein SepF | Mycobacterium | MSTLHKVKAYFGMAPMEDYDDEYYDDRGPSRGYSRPRFEDDYGRYEGRDFEDPRRDPRADMRADLRGEPADYPPPGGYRGGYPDEARFQPREFDRADMARPRFGSWLRNPTRGSLAMDPRRMAMMFEEGHPLSKITTLRPKDYSEARTIGERFRDGTPVIMDLVSMDNADAKRLVDFAAGLAFALRGSFDKVATKVFLLSPADVDVTPEERRRIAETGFYAYQ | Cell division protein that is part of the divisome complex and is recruited early to the Z-ring. Probably stimulates Z-ring formation, perhaps through the cross-linking of FtsZ protofilaments. Its function overlaps with FtsA. | B2HGR0 |
Q7VFT5 | NUON_HELHP | NDH-1 subunit N | Helicobacter | MPESMSFSLNQLNLQLLIPMCISLFGGIILLGVGVFNKTKSRDLYITISMLFVVLNLGFLFLEGNPIRQFGFFNLLLVDGISLLTQIIMLLATFVLLLFFMNQNNLPETQGAEFYALLLFSIAGFAFMASSQNLILILLGLETASLCLYALIALHNQKSAFEASIKYFIMGALATTFYAFGAMLLYAATGSVDIISIATFLHQQSYQPSILVFAGFVFLLCALGFKVTLVPFHSWGPDVYEGSNALLAAFIAIVPKIVTFAVIIRIFSVFIDSHSAFVEYTLYVIVVLTMTIPNLIALTQKDVKRMLAYSSISHSGFVLA... | 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... | Q7VFT5 |
A4XR60 | HEM1_PSEMY | Glutamyl-tRNA reductase | Pseudomonas | MAFIALGINHKTASVEVRERVAFTPEQLVEALQQLCRLTPSREAAILSTCNRSELYLEQDQLSSDEVLKWLADYHRLSLDELRACAYVHSEQDAVRHMMRVACGLDSMVLGEPQILGQLKSAYAVAREAGTVGPLLGRLFQATFSTAKTVRTDTAIGENPVSVAFAAVSLAKQIFADLHRSQALLIGAGETISLVARHLHDQGIKRIVVANRTLERASQLAEQFGAHAVLLSDIPDELAHSDIVISSTASQLPILGKGAVESALKKRKHKPIFMVDIAVPRDIEPQVGELDDVYLYTVDDLHEVIEENLKSRQGAAQAAE... | Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). | A4XR60 |
Q5F359 | TPPC5_CHICK | Trafficking protein particle complex subunit 5 | Gallus | MESRFTRGKSPLLERPLGRPRGEVSLSAFALLFCELVQYCQRRVYSVAELQSKLAQLGHQVGLRLLDPLVSRERGGRRETKVLSVLLFVKGPVWRALFGKEADKLEQANDDDKTYYVIEREPLVNTFISVPRENSTLNCAAFTAGLVEAVLGASGFPAKVTAHWHKGTTLMIKFEEGVIARDKSLEGR | May play a role in vesicular transport from endoplasmic reticulum to Golgi. | Q5F359 |
P85095 | BR2R_PELRI | Brevinin-2R | Pelophylax | KLKNFAKGVAQSLLNKASCKLSGQC | Cytotoxic to cancer cells, acts via the activation of the lysosomal-mitochondrial death pathway and autophagy-like cell death. Does not show significant hemolytic activity. | P85095 |
B7JQU1 | Y2714_BACC0 | Putative metal-dependent hydrolase BCAH820_2714 | Bacillus cereus group | MNDLRYPIGQFTYKRPITEEMIDTWIQEIEDLPNELTKAIKDLDQKQLDTPYRVGGWTVRQVVHHVVDSHMNSYIRFKLALTEKNPTIKPYKEEKWAELPDSKLPVDVSLVMLESLHKRWVNLLYSLELEDLEKTFNHPDTGETKLAAAIGLYAWHGRHHTAHITSLRKRLNW | Possible metal-dependent hydrolase. | B7JQU1 |
Q8TW15 | RS8_METKA | 30S ribosomal protein S8 | Methanopyrus | MTLMDPLADAMATIKNNEMVGNKECVIEPASKLIGRVLKVMQEYGYIGSFEFIDDGRSGKFLVKLVGRINDCGVIKPRHPVKKDEWEYWEQRYLPARDFGLLIVTTPEGVMSHYEAKERGIGGRLLAYVY | One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit. | Q8TW15 |
Q92MF8 | GLO2_RHIME | Glyoxalase II | Sinorhizobium | MAALELDLFLCRTDNYGVLLHDRLSGATASIDAPEERPILDALERRGWQLTHILTTHHHGDHVAANASLKERFGLTIIGPKNEASKIPGIDRTVGHGDRFDFAGHPVDVIETPGHTSGHVCYHLPEDKLLFAADTLFALGCGRLFEGTADTMWQSLSRLMALPDDTAIYFGHEYTLANAHFAITVDPENSALKERAAEIEETRSDGGFTAPTTMGLEKRTNPFLRAGDPKIRALLGMEKASDAAVFAEIRKRKDNF | Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid. | Q92MF8 |
Q6N509 | OADC_RHOPA | Oxaloacetate decarboxylase | Rhodopseudomonas | MAWRDRRGALRAILTGSACVRPASVYDAISIRIADDLGFPFGMFGGSVASLAILGDPDIALITLTELAEQVRRMSRAAALPVVVDADHGYGNALNVRRTVEELEAAGAAGLTIEDTLLPQAYGEAKPQLVSREEGLGKIKAALDARRDPNLVIIGRTGACSITSLDDAIERALAYQAAGVDALFFTGVKTRAQLEAISAATTLPIALGSPPAELGDFDHLAERRVRIAVQGHAPIAAATEAVFKTLSAIKDGAAPKALTGLASAELMDKVTRADVVAERGEHFLGVKR | Catalyzes the decarboxylation of oxaloacetate into pyruvate. Seems to play a role in maintaining cellular concentrations of bicarbonate and pyruvate. | Q6N509 |
B1GYT4 | ISPD_ENDTX | MEP cytidylyltransferase | Endomicrobium | MKNAAIIAAAGSGKRFGSRVSKQFLNLSGKPVFLWSVEAFASIKSFKQIIVVVPSDMVEFLSLKYKTGFVCATGGNERFDSVKNGLALVGDDIDFIAVHDASRPLISKKDILLVLEKAAKTKVAVAVEKAKDTVKLVSADGYILKTLDRTILRNAQTPQIFKTELLKRAYSRKMSAGTTDDSQLVENLKIKVSAVETKFLNFKITTKQDFELAEKILKS | Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). | B1GYT4 |
P01027 | CO3_MOUSE | Complement C3c alpha' chain fragment 2 | Mus | MGPASGSQLLVLLLLLASSPLALGIPMYSIITPNVLRLESEETIVLEAHDAQGDIPVTVTVQDFLKRQVLTSEKTVLTGASGHLRSVSIKIPASKEFNSDKEGHKYVTVVANFGETVVEKAVMVSFQSGYLFIQTDKTIYTPGSTVLYRIFTVDNNLLPVGKTVVILIETPDGIPVKRDILSSNNQHGILPLSWNIPELVNMGQWKIRAFYEHAPKQIFSAEFEVKEYVLPSFEVRVEPTETFYYIDDPNGLEVSIIAKFLYGKNVDGTAFVIFGVQDGDKKISLAHSLTRVVIEDGVGDAVLTRKVLMEGVRPSNADAL... | Adipogenic hormone that stimulates triglyceride (TG) synthesis and glucose transport in adipocytes, regulating fat storage and playing a role in postprandial TG clearance. Appears to stimulate TG synthesis via activation of the PLC, MAPK and AKT signaling pathways. Ligand for C5AR2. Promotes the phosphorylation, ARRB2-... | P01027 |
Q5FQK0 | MTNA_GLUOX | S-methyl-5-thioribose-1-phosphate isomerase | Gluconobacter | MKINGISYRSLWRPSDDASSIRIFDQTRFPWNVEILELRDVGAVADAITSMQVRGAPLIGAVAAYGLVFALQDDASDEALEKAAAFLVATRPTAINLRWAIERMVARLKAVRPTERVAAGYVEADAICDEDVQVNEAIGRHGLELIREIWERKGKQGQVNLLTHCNAGWIATVDWGTALAPIYMAHDEGIPVHVWVDETRPRNQGSLLTAWELGSHGVPHTVIADNAGGHYMQTGRVDMVIVGTDRVTAQGDVANKIGTYLKALAAHDNNVPFWVALPSSTIDWRVRDGVKDIPIEERSADEVLFMTGLDSNGEAGRVRI... | Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P). | Q5FQK0 |
Q5VP70 | PIN3A_ORYSJ | OsPIN3t | Oryza sativa | MISGHDFYTVMAAVVPLYVAMFLAYGSVRWWGIFTPDQCSGINRFVAIFAVPLLSFHFISTNDPYAMNLRFLAADTLQKLLVLAGLAAWSRLPSRTGAPRLDWSITLFSLSTLPNTLVMGIPLLIAMYGPYSGSLMVQIVVLQCIIWYTLMLFLFEFRAARMLIADQFPDTAASIVSLHVDPDVVSLEGGHAETEAEVAADGRLHVTVRRSSVSRRSLLVTPRPSNLTGAEIYSLSSSRNPTPRGSNFNHADFFAMVGGGPPPPTPAAVRGSSFGASELYSLQSSRGPTPRQSNFDEHSARPPKPPATTTGALNHDAKEL... | Acts as a component of the auxin efflux carrier. Involved in the polar auxin transport which may regulate crown root development and response to water stress. | Q5VP70 |
A1WK93 | RS4_VEREI | 30S ribosomal protein S4 | Verminephrobacter | MARYLGPKAKLSRREGTDLFLKSARRSIADKSKFDSKPGQHGRTSGARTSDYGLQLREKQKVKRMYGVLEKQFRRYFEAAESRKGNTGANLLFLLESRLDNVVYRMGFGSTRAEARQLVSHKAITVNGQSVNIPSYLVKTGDLVAVREKSKKQGRIAEALQLATQVGMPAWVEVNTEKAEGLFKKAPDRDEFGADINESLIVELYSR | With S5 and S12 plays an important role in translational accuracy. | A1WK93 |
B0S902 | RSMG_LEPBA | 16S rRNA 7-methylguanosine methyltransferase | Leptospira | MPEKTIQEEIQTIIPELFPILEPEFDWELVKNFYDFLKRDNEKGGFFSKNDSEKILERHILESLIFVWKLKTTGYVSRETNVADVGTGPGLPGFLFAVLKKAPQVFLVDSQKRKLALLEAEITTGSLSKVKKRVEFIYARTEEISSNFDVVTSRAMVPYPYLAEVTTRMVKQKGILCPFLAQPYQDLEKETEVLSNNGFVLKKEILIPELEFVGKRHIKILQKNSLPKKGYPRDWKEIVKETKSKNG | Specifically methylates the N7 position of a guanine in 16S rRNA. | B0S902 |
A8HDK0 | 3S11_NOTSC | Short neurotoxin 1 | Notechis | MKTLLLTLVVVTIVFLDLGYTMTCCNQQSSQPKTTTTCAESSCYKKTWRDHRGTITERGCGCPNVKPGVQINCCKTDECNN | Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission. | A8HDK0 |
O22149 | PME17_ARATH | Pectin methylesterase 17 | Arabidopsis | MMAFRAYIINFVILCILVASTVSGYNQKDVKAWCSQTPNPKPCEYFLTHNSNNEPIKSESEFLKISMKLVLDRAILAKTHAFTLGPKCRDTREKAAWEDCIKLYDLTVSKINETMDPNVKCSKLDAQTWLSTALTNLDTCRAGFLELGVTDIVLPLMSNNVSNLLCNTLAINKVPFNYTPPEKDGFPSWVKPGDRKLLQSSTPKDNAVVAKDGSGNFKTIKEAIDAASGSGRFVIYVKQGVYSENLEIRKKNVMLRGDGIGKTIITGSKSVGGGTTTFNSATVAAVGDGFIARGITFRNTAGASNEQAVALRSGSDLSVF... | Acts in the modification of cell walls via demethylesterification of cell wall pectin. | O22149 |
Q2H9L1 | DOT1_CHAGB | null | Chaetomium | MSIFNQKSKFKVKTEVRKVKQAVEPTPESKKRYVGNGSASASTNGTPRASPTPSSLQVKRPRPRPGAGAASPATGPSLSSSTSASPLDLTRKRRAPAGSSSSRSPATASPAPRALSDSEPGSDDDDDDDWRDRLDPSKRRKRAHTEDPDRRLRHPRLWAGQGDEDKPGIVHAVQVASLADKCQPVMKLARDEVGVRLRYPGAKYTERYELVWGKDKIDGALDIMKVVKFVASTYLTDAEAKPFLDHNLGINRRLEKSKNTNDGEGFKAALAEYNNQLLALQTEGAIARNIDAMRGVPRELVEFILDQVYDRTVAPKVDLL... | Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free h... | Q2H9L1 |
Q9SWS1 | ACFR2_ARATH | Protein b561A.tha4 | Arabidopsis | MAVPVLGGFPIFMVVRVLGFIIAALVLTWTVHYRGGLALSSDNKDHIFNVHPVMMVIGLILFNGEAMLAYKSVQGTKNLKKLVHLTLQLTAFILSLIGVWAALKFHIDKGIENFYSLHSWLGLACLFLFAFQWAAGFVTYWYPGGSRNSRASLMPWHVFLGISIYALALVTATTGILEKVTFLQVNQVITRYSTEAMLVNTMGVLILILGGFVILGVVTPVSGKDQVLTQ | Two-heme-containing cytochrome . Catalyzes ascorbate-dependent transmembrane ferric-chelate reduction (Probable). | Q9SWS1 |
P87323 | MCS4_SCHPO | Mitotic catastrophe suppressor 4 | Schizosaccharomyces | MRIWFKKVPDGITSSVILSEDHLVDDLKDAIARKFPIRISQYYDAPELSIRVVAPPNASSELQSRELSPNESILFVMETYYPHGQDFNDALLVASPDTSVALRYRSSQLSSSTFESTPPVFSEYPPNIIPTPANETVPRIKQPSIALDSLESPVSAPSRHQSTYSYKGGPLNYNLRNASRTRSHQTLPSSNVNKTGVLLLPRSSRQQTLASRPSLPDLTSADKSQPSDEAESITRKNSIGMSTRSDESTAEKLAKAEVATPTNSRSISHSSLYTKQSGTAGVLPAVNADIDAANRMNPDISSQFPIADNKDPLNADTQAH... | Response regulator that coordinately controls the stress activated wak1-wis1-sty1 MAP kinase pathway and fission yeast cell cycle. | P87323 |
P0DMN9 | APOC2_OTOGA | Proapolipoprotein C-II | Otolemur | MGTRFLLALFLVLLVLGFEVQGAQLPQQDEPSSPTLLTQMQESLSSYWDSAKEAARGLYEKTYLPTVDEKLRDMYSKSTAAVSTYAGIFTDQLLTLLKGD | Component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. Plays an important role in lipoprotein metabolism as an activator of lipoprotein lipase. Both proapolipoprotein C-II and apolipoprotein C-II can activate lipoprotein lipase. | P0DMN9 |
Q9US00 | AMT2_SCHPO | Ammonium transporter 2 | Schizosaccharomyces | MSSVNSIPTATSTVYISVLPATATPSGGSGGNVLHEDLNKFYDYGNTSWILACTPLCLIMVPGVAFFYSGLARRKNTLALIMLSMLGLCVSFFQWYFWGYSLAFSQTGTSGYIGNLRHFAFIRTLADYSPGSNNIPELVFANFQGMFAAITVALFTGAAAERGRIGPMLIITFVWLTVVYCPIACWIWNPNGWAFKFGVYDFAGGGPVEVGSGFAALAYTVCLGRRSKFVEEQFRPHSVLNVVLGTSLLWFGWLGFNGGSAYGSNLRAAMAITNTNLAGAVAGLVWVIYDYIFRTRKWSTIGFCSGVVAGLVAATPCAGF... | Transporter for ammonium to use as a nitrogen source. | Q9US00 |
Q96I25 | SPF45_HUMAN | RNA-binding motif protein 17 | Homo | MSLYDDLGVETSDSKTEGWSKNFKLLQSQLQVKKAALTQAKSQRTKQSTVLAPVIDLKRGGSSDDRQIVDTPPHVAAGLKDPVPSGFSAGEVLIPLADEYDPMFPNDYEKVVKRQREERQRQRELERQKEIEEREKRRKDRHEASGFARRPDPDSDEDEDYERERRKRSMGGAAIAPPTSLVEKDKELPRDFPYEEDSRPRSQSSKAAIPPPVYEEQDRPRSPTGPSNSFLANMGGTVAHKIMQKYGFREGQGLGKHEQGLSTALSVEKTSKRGGKIIVGDATEKDASKKSDSNPLTEILKCPTKVVLLRNMVGAGEVDE... | Splice factor that binds to the single-stranded 3'AG at the exon/intron border and promotes its utilization in the second catalytic step. Involved in the regulation of alternative splicing and the utilization of cryptic splice sites. Promotes the utilization of a cryptic splice site created by the beta-110 mutation in ... | Q96I25 |
Q5H7N5 | CECP3_ASCSU | Cecropin-P3 | Ascaris | MFLIYLLVQTAESSWLSKTAKKLENSAKKRISEGIAIAIKGGSRRRRSVGEEDAIPSHIEVNKFFLRKPAKEHI | Has antibacterial activity against several Gram-positive and Gram-negative bacteria. Is weakly active against yeasts. Acts by a nonpore mechanism. | Q5H7N5 |
Q6YR34 | SYI_ONYPE | Isoleucyl-tRNA synthetase | Candidatus Phytoplasma asteris | MTTNYKTTLLMPKTDFPMKGNLGKNEINIQKHWQKLDLYQKKLQQNQDNNPFILHDGPPYANGNIHMGHALNKILKDFIVRFRSMQGFYTPLIPGWDTHGLPIEAAVLKKTSKNAFTRKPLLDKCQEFALENVNNQKHQFQRLGILGDWQNPYLTLDKTFVSDQVRIFGQMVDKGLIFKALKPIHWSPTLESALAEAELEYHNHQSPSVYVAFSMKKLDIFDNVALVIWTTTPWTLPANVAIAVHPEKEYQLIEVLQKRYLVGTKNIPFLQKVFAWNKENIKVVATFEGKTLEHLTYQNHLVSKFGKIILSQHVLDGEGT... | 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... | Q6YR34 |
C5D9Y5 | RSMG_GEOSW | 16S rRNA 7-methylguanosine methyltransferase | unclassified Geobacillus | MDTAQFHTMLEEKGISLSSQALAQFERYYELLMEWNEKMNLTAITDKPSVYLKHFFDSLSPAFYYDFSQSLSICDVGAGAGFPSVPLKICFPHLKLSIVDSLQKRITFLEHLAAELGLTDVAFYHDRAETFGRKKEFRESFDIVTARAVARMSVLSELCLPLVKVNGTFIAMKAASAQEELEQGKKAIDVLGGEISAIERFMLPIEQSERTIIFIQKVRNTPNKYPRKPGMPNKQPIQ | Specifically methylates the N7 position of guanine in position 535 of 16S rRNA. | C5D9Y5 |
Q2P4B6 | FABZ_XANOM | Beta-hydroxyacyl-ACP dehydratase | Xanthomonas | MSHPAYELPIDVNQIQALIPHRYPFLLIDRVIELDLEAKRIVGQKNVSINEPFFQGHFPTRPVMPGVLIIEALAQAGGVMTQLGLGRDALSKLFYMVKVDNARFNKQVVPGDVLILEVQMKRLIRNMGCYYGEAKVNGEIVASAEIMCAAARE | Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs. | Q2P4B6 |
Q47AF6 | CRCB_DECAR | Putative fluoride ion transporter CrcB | Dechloromonas | MSALHQLSALNFLVIGLGAAFGAWTRWLLGLSLNPLFVALPLGTLAANVIGGYLVGVAVGIFHINTHFSLAWKLFAITGFLGGLTTFSTFSAEVVERLLAGQPAWAIGLASVHLAGSLTATYLGLLTVGATRIWA | Important for reducing fluoride concentration in the cell, thus reducing its toxicity. | Q47AF6 |
Q6G3K8 | NUSB_BARHE | Antitermination factor NusB | Bartonella | MVDVEGKYSPRLANKRGAARLAAVQALYQMDIVGSGVMETAAEYEAYRLGKDIDGDQYLDADFQWFLAIITGVVKDQKQLDPMLNQQLSAEWSLSRLDSILRAILRAGLWELINRQDVPIAVVMSEYVDIAKAFFEGDEPKLVNAILDSMAKKIRLLK | Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons. | Q6G3K8 |
Q56TT9 | SCIT_HOTJU | Bj-alpha-IT | Hottentotta | MNYLVVICFALLLMTGVESGRDAYIADNLNCAYTCGSNSYCNTECTKNGAVSGYCQWLGKYGNACWCINLPDKVPIRIPGACRGR | 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 against insects (para/tipE). | Q56TT9 |
P54574 | FUR_BACSU | Ferric uptake regulation protein | Bacillus | MENRIDRIKKQLHSSSYKLTPQREATVRVLLENEEDHLSAEDVYLLVKEKSPEIGLATVYRTLELLTELKVVDKINFGDGVSRYDLRKEGAAHFHHHLVCMECGAVDEIEEDLLEDVEEIIERDWKFKIKDHRLTFHGICHRCNGKETE | Iron uptake repressor. Acts on the transcription of ferri-siderophore uptake genes. | P54574 |
B3QQ80 | LFTR_CHLP8 | Phenyalanyltransferase | Chlorobaculum | MIKVEDILRAYRHGFFPMADSREGTVSWCQPYQRAVVPLDTFRPSRSLRRVIDEGQFTIKTNTAFEKVIRACALPRAVEKETWISEEIIEVFLKLHRLGLAHSVESWQNGELAGGLYGLSMGGAFFGESMFFFERDASKVAFAWLVGYLRKKGFSLLDAQIMNPHLESLGAIEIPHEEYMLRLEHALAKKIFFI | 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. | B3QQ80 |
B0UWR3 | DNAJ_HISS2 | Chaperone protein DnaJ | Histophilus | MAKRDYYEILGVQKGADDKEIKRAYKRLAMKYHPDRTKGDKESEEKFKEINEAYEVLADKEKRAMYDQYGHAAFEQGGGAGGFGGFSGADFGDIFGDMFGDIFGGGRSRQRVVRGEDLRYDIEISLEEAVKSCKKDIQINTLVHCGTCHGSGAEAGSKIESCPTCHGAGRVRRQQSFFVTEQTCPHCHGTGKKIEKPCHTCHGEGRVHKTQNLTVTIPMGVDTGNQLRLAGKGAAGENGAPAGDLYVVIHVKKHHIFERDGNNLYCEVPISFTMAALGGEVEIPTLDGRLKVKIPAETQTGKLLRLRGKGITSRGYAGDL... | Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bou... | B0UWR3 |
Q1GK35 | RL23_RUEST | 50S ribosomal protein L23 | unclassified Ruegeria | MSAKAEHYDVIRKPIITEKSTMASENGAVVFEVAIDSNKPQIKEAVEALFGVKVKAVNTTVTKGKVKRFRGQLGKRKDVKKAYVTLEEGNTIDVSTGL | 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. | Q1GK35 |
P05522 | GUN1_PERAE | Endo-1,4-beta-glucanase 1 | Persea | MDCSSPLSLFHLLLVCTVMVKCCSASDLHYSDALEKSILFFEGQRSGKLPTNQRLTWRGDSGLSDGSSYHVDLVGGYYDAGDNLKFGLPMAFTTTMLAWGIIEFGCLMPEQVENARAALRWSTDYLLKASTATSNSLYVQVGEPNADHRCWERPEDMDTPRNVYKVSTQNPGSDVAAETAAALAAASIVFGDSDSSYSTKLLHTAVKVFEFADQYRGSYSDSLGSVVCPFYCSYSGYNDELLWGASWLHRASQNASYMTYIQSNGHTLGADDDDYSFSWDDKRVGTKVLLSKGFLQDRIEELQLYKVHTDNYICSLIPGT... | Involved in ripening fruit process. | P05522 |
P0C6A7 | VM27B_VIPBB | Disintegrin VB7B | Vipera | ELLQNSGNPCCDPVTCKPREGEHCISGPCCRNCKFKRAGTVCLDAKGDWMNNYCTGISSDCPRN | Poor inhibitor of platelet aggregation. The disintegrin inhibits the adhesion of cells expressing the RGD-dependent integrin alpha-5/beta-1 (ITGA5/ITGB1) to immobilized fibronectin. Inhibition on alpha-IIb/beta-3 (ITGA2B/ITGB3) is low. | P0C6A7 |
A7GAL0 | THIE_CLOBL | Thiamine-phosphate pyrophosphorylase | Clostridium | MEINYELYLITDRRFLKGRQLKKVVEDAILGGVTIVQVREKDVSTREFYNVAKEVKEVTDYYKVPIIINDRLDIAQAIDASGVHLGQKDMHLNIAREILGKDKIIGISVGNVKEALEAQNNGADYLGIGTIFPTGSKKDVDAIIGIDGLSKIKDSISIPSVAIGGINKTNFKDVLKTGIEGISVISAILDEDDIKLAANNLLINK | Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). | A7GAL0 |
B4U300 | Y1013_STREM | UPF0122 protein Sez_1013 | Streptococcus | MKIMEIEKTNRMNALFEFYAALLTDKQMNYIELYYADDYSLAEIAEEFGVSRQAVYDNIKRTEKILEAYEMKLHMYSDYIVRSEIFDDILAKYPSDHYLRDKISILTSIDNRD | Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein. | B4U300 |
B8DU64 | SYY_BIFA0 | Tyrosyl-tRNA synthetase | Bifidobacterium | MAHVIDFKEAGFDSVLDELEWRGLISQSTDRDRLAHTLNGEPVHYYCGFDPTAPSLHIGNLVQLIIMRHLQEAGHHPIALVGGATGLIGDPRQSGERILNPKDIVEQWCERLRIQIGGILEQEGSNPVTFVSNYDWTATMNVLDFLRDIGKNFRVGTMISKDIVARRLNSEEGISFTEFSYQVLQGNDYLYLYDHYDCVLELGGSDQWGNLTSGLDLIHKVRGVNVNVMASPIITDANGKKFGKSEGNAVWLDPNMLSVYKFYQFWLNRPDVEMASLLKAFTFLPKAEIERLVEATDTNPGAREAQRVLAWEVTSLVHGD... | Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). | B8DU64 |
Q24SS5 | PRMA_DESHY | Ribosomal protein L11 methyltransferase | Desulfitobacterium | MNWREIAVTVSSAGEEAVADLFYQLGCPGVSVEDPELLQSYVESGNWDYHDFGEIALTGTSVVKGYICEDHELQPKLRQLDEGLKELLQRFPEWVLQVKGLTVQEEDWATSWKAYFKPVRIGRHFLIKPSWEEVTPLPEDIILELDPGMAFGTGTHATTSLCLETLEETVKPDMRIFDLGTGSGILAIAAAKLGAQVEAIDLDSVAVKVAQENVELNQVADRISVRQGDLGTVLQGQADLVVANIIADVILMLIPDLKRIMKEDGEFLASGIIGHRSSDVEAGLGEHGLEVLEKKEDSGWVLLRARWQRASL | Methylates ribosomal protein L11. | Q24SS5 |
Q4UQF1 | ATPD_XANC8 | F-type ATPase subunit delta | Xanthomonas | MSQALTLARPYARAAFAIAREGGKFAPWSDALAFSAQVAGDPRVAALLLNPALHQDQAVTLLAPPAAEADYQRFLGLLADAQRLALLPEIAGLYEQLRAEAEHVVKATVTSATDMSPAELATITAALKKRFGREVDVTTAVDASLIGGAVIDTGEMVIDGSLKGKLARLQNSLAH | 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. | Q4UQF1 |
Q820D8 | RPOA_TROW8 | Transcriptase subunit alpha | Tropheryma | MLIAHRPTLIEKKVSDIRSRFIIEPLEPGFGYTLGNSLRRTLLSSIPGAAVTSINIQGVMHEFSTIPGVKEDVTEIVLNVKRLVISSEIDEPFTVRLYKTGEGEVLAKDIEVPTGIEIGNGDLVIATLAKDAVFDMQLTIERGRGYVSAEQNRNDGMSLAGHIPVDSIYSPVHKVTYRVEATRAGERTDFDRLIIDVETKPSILPRDAVASAGKTLCELFGLARELNSQAEGVEFGVDSMIPESDEDLRIPIEDLGLSVRSYNCLKREGVNYVSELLGFSEQELLDIRNFGQKSADEVQEKLAELGHSLKGSVPGFDGSY... | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | Q820D8 |
Q479W5 | RBL2_DECAR | Ribulose bisphosphate carboxylase | Dechloromonas | MDQSNRYADLSLTEAELIAGGQHILCAYKMKPKAGHRYLEAAAHFAAESSTGTNVEVCTTDEFTKGVDALVYHIDEASEDMRIAYPLDLFDRNMTDGRMMMASFLTLTIGNNQGMGDIEHAKMVDFYVPRRGIELFDGPSKDISDLWRMLGRPVKDGGYIAGTIIKPKLGLRPEPFARAAYEFWLGGDFIKNDEPQGNQVFAPLKKVIPLVYDSMKRAMDETGEAKLFSMNITADDHFEMCARADFALEAFGPDADKLAFLVDGYVGGPGMITTARRQYPNQYLHYHRAGHGAVTSPSSKRGYTAYVLAKMSRLQGASGI... | RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site. | Q479W5 |
Q9H0M0 | WWP1_HUMAN | WW domain-containing protein 1 | Homo | MATASPRSDTSNNHSGRLQLQVTVSSAKLKRKKNWFGTAIYTEVVVDGEITKTAKSSSSSNPKWDEQLTVNVTPQTTLEFQVWSHRTLKADALLGKATIDLKQALLIHNRKLERVKEQLKLSLENKNGIAQTGELTVVLDGLVIEQENITNCSSSPTIEIQENGDALHENGEPSARTTARLAVEGTNGIDNHVPTSTLVQNSCCSYVVNGDNTPSSPSQVAARPKNTPAPKPLASEPADDTVNGESSSFAPTDNASVTGTPVVSEENALSPNCTSTTVEDPPVQEILTSSENNECIPSTSAELESEARSILEPDTSNSRS... | 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. Ubiquitinates ERBB4 isoforms JM-A CYT-1 and JM-B CYT-1, KLF2, KLF5 and TP63 and promotes their proteasomal degradation. Ubiquitinates R... | Q9H0M0 |
Q6AH11 | RL10_LEIXX | 50S ribosomal protein L10 | Leifsonia | MANKEATVAELENLFDSSTAVLLTEYRGLTVAQLKTLRTSISEHATYAVVKNTLTKIAANKKGISSFDEELVGPSAIAFVHGDPVAVAKSLRDFAKANPLLVVKSGYFDGNPLTAEEVGKLADLESREVLLAKLAGAFKASLFGAAYLFNAPLSQAVRTVDALREKQESAAE | Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. | Q6AH11 |
P37550 | ISPE_BACSU | 4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase | Bacillus | MRILEKAPAKINLSLDVTRKRPDGYHEVEMIMTTIDLADRIELTELAEDEVRVSSHNRFVPDDQRNLAYQAAKLIKDRYNVKKGVSIMITKVIPVAAGLAGGSSDAAATLRGLNRLWNLNLSAETLAELGAEIGSDVSFCVYGGTALATGRGEKIKHISTPPHCWVILAKPTIGVSTAEVYRALKLDGIEHPDVQGMIEAIEEKSFQKMCSRLGNVLESVTLDMHPEVAMIKNQMKRFGADAVLMSGSGPTVFGLVQYESKVQRIYNGLRGFCDQVYAVRMIGEQNALD | Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. | P37550 |
P51196 | FABH_PORPU | 3-oxoacyl-[acyl-carrier-protein] synthase III | Porphyra | MGVHILSTGSSVPNFSVENQQFEDIIETSDHWISTRTGIKKRHLAPSSTSLTKLAAEAANDALSKASINAEDIDLIILATSTPDDLFGSASQLQAEIGATSSTAFDITAACSGFIIALVTASQFIQAGSYNKVLVVGADTMSRWIDWSDRSSCILFGDGAGAVLIGESSINSILGFKLCTDGRLNSHLQLMNSPSDSQQFGLTTVPKGRYDSIRMNGKEVYKFAVFQVPIVIKNCLNDVNISIDEVDWFILHQANIRILEAIATRLSIPLSKMITNLENYGNTSAASIPLALDEAIKEKKIQPGQVVVLAGFGAGLTWGA... | Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-A... | P51196 |
Q1CV87 | UREH_HELPH | Urease accessory protein UreH | Helicobacter | MNTYAQESKLRLKTKIGADGRCVIEDNFFTPPFKLMAPFYPKDDLAEIMLLAVSPGLMKGDAQDVQLNIGPNCKLRITSQSFEKIHNTEDGFASRDMHIVVGENAFLDFAPFPLIPFENAHFKGNTTISLRSSSQLLYSEIIVAGRVACNELFQFNRLHTKISILQDEKPIYYDNTILDPKTTDMMNMCMFDGYTHYLNLVLVNCPIELSGVRGLIEESEGVDGAVSEIASSHLCVKALAKGSEPLLHLREKIARLITQTITPKI | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | Q1CV87 |
Q486Y6 | HSCA_COLP3 | Chaperone protein HscA homolog | Colwellia | MALLQIAEPGQSTVPHEHRLAAGIDLGTTNSLIASVQSGNASTLSDDQGRDILPSIVSYQAGNVLVGQTAQALSIEDAQNTITSAKRLIGRSLKDIQSKYPSLPYEFCGDENHPEIMTRQGAVNPVQVSAEILKSLNLRAQAALGGELTGVVITVPAHFDDAQRQSTKDAAKLAGVSVLRLLNEPTAAAVAYGLDSGQEGVIAVYDLGGGTFDISILRLNKGVFEVLATGGDSALGGDDFDVVLVDYLVEQAGLVRPLSPSLERQLMQQACFAKEQLTTKEEVDITISLDSDSDWKTSLTKAQLNKLISSLVNKTLRACR... | Chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | Q486Y6 |
B4SRB0 | RECA_STRM5 | Recombinase A | Stenotrophomonas maltophilia group | MDENKKRALAAALGQIEKQFGKGSVMRMGDRVVEPVEAIPTGSLMLDIALGIGGLPKGRVVEIYGPESSGKTTLTLQAIAECQKLGGTAAFIDAEHALDPIYAAKLGVNVDDLLLSQPDTGEQALEIADMLVRSGSVDILVVDSVAALTPKAEIEGEMGDQLPGLQARLMSQALRKLTGNIKRSNTLVVFINQLRMKIGVMMPGQSPEVTTGGNALKFYASVRLDIRRIGAIKKGDEIIGNQTKIKVVKNKLAPPFKQVITEILYGEGISREGELIDMGVDAKLVEKAGAWYSYGEERIGQGKDNARGYLRDNPTVAAKL... | 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. | B4SRB0 |
Q2YDN8 | VRK3_BOVIN | Vaccinia-related kinase 3 | Bos | MICPDCGKGIEATFKFCPYCGKPLPAEKHEGSQSFVKPFTSSSQGSRRKTNTSSETSSKKVKWCSYAASPSLPLPSEGKSSGSEDTLSTSGKPKGHLSRSPTPRSSPQTTRQSPQTLKRSRMTASLEALPVGTVLTDKSGQHWKLRCLQTRDDQGILYEAESDSTTGSESSPQKQRFSLKLDAKDGRLFNEQNFFQRAAKPLQVNKWKKLYSIPQLAIPTCIGFGVHQDKYRFLVFPTLGRSLQSILDDFPKHVMSVRSVFQMACRLLDALEFLHENEYVHGNVTAENIFVNPENLCQVTLAGYGFTFRYSPGGRHVAYT... | Inactive kinase that suppresses ERK activity by promoting phosphatase activity of DUSP3 which specifically dephosphorylates and inactivates ERK in the nucleus. | Q2YDN8 |
A6BLY7 | K1C28_MOUSE | Type I inner root sheath-specific keratin-K25irs4 | Mus | MSLRFSGGSRHVGIQSGSLRPPSGGAGFAGSSVAGGSVAGSGFSWALGGTLGSAPGGSHATGALGNVSGVCFIGSEGGLLSGNEKVTMQNLNNRLASYLDNVKALEEANSELERKIKTWHEKYGPGSCRGLDRDYSKYHLTIEDLKSKIISSTAANANIILQIDNARLAADDFRLKYENELTLHQNVEADINGLRRVLDELTLCRTDQELQYESLSEEMTYLKKNHEEEMKVLQCAAGGNVNVEMNAAPGVDLTVLLNNMRAEYEALAEQNRRDAEAWFQEKSATLQQQISNDLGAATSARTELTELKRSLQTLEIELQS... | Essential for the proper assembly of types I and II keratin protein complexes and the formation of keratin intermediate filaments in the inner root sheath (irs). | A6BLY7 |
O14879 | IFIT3_HUMAN | Retinoic acid-induced gene G protein | Homo | MSEVTKNSLEKILPQLKCHFTWNLFKEDSVSRDLEDRVCNQIEFLNTEFKATMYNLLAYIKHLDGNNEAALECLRQAEELIQQEHADQAEIRSLVTWGNYAWVYYHLGRLSDAQIYVDKVKQTCKKFSNPYSIEYSELDCEEGWTQLKCGRNERAKVCFEKALEEKPNNPEFSSGLAIAMYHLDNHPEKQFSTDVLKQAIELSPDNQYVKVLLGLKLQKMNKEAEGEQFVEEALEKSPCQTDVLRSAAKFYRRKGDLDKAIELFQRVLESTPNNGYLYHQIGCCYKAKVRQMQNTGESEASGNKEMIEALKQYAMDYSNK... | IFN-induced antiviral protein which acts as an inhibitor of cellular as well as viral processes, cell migration, proliferation, signaling, and viral replication. Enhances MAVS-mediated host antiviral responses by serving as an adapter bridging TBK1 to MAVS which leads to the activation of TBK1 and phosphorylation of IR... | O14879 |
Q9UZ57 | IORA_PYRAB | Indolepyruvate ferredoxin oxidoreductase subunit alpha | Pyrococcus | MVKVTDIVLWDKPGERVLLLGNQAIVRGALEGNIGVYAAYPGTPSSEITDTMAAVASRAGVYMEYSTNEKVAFETALSASWAGLRAMTAMKHVGLNVAMDSFMTVSYMGVNGGLVVVVADDPSMWSSQNEQDTRAIAKFANIPVLEPSSVQEAKDMVKYAFEISEKYGQMVILRTTTRSSHMRGDVVLGELPQEIKEGKRKFGDFKKNPERYVDIPAFQRPKHKWLLETIEKFREEFNNSPFNWIEGPEDAKVGIIAPGLSYAYVKEALAWLGVDNVKVLKLGTPFPVPYGLLEKFFQGLERVLIVEELEPVVEEQVKVW... | Catalyzes the ferredoxin-dependent oxidative decarboxylation of arylpyruvates. | Q9UZ57 |
A3PGM0 | RS17_CERS1 | 30S ribosomal protein S17 | Cereibacter | MPKRILQGTVTSDKNEQTVTVLVERRFKHPLLKKTVRLSKKYRAHDPENQFKVGDIVRIEECAPISKTKRWKVVTDAVVA | One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. | A3PGM0 |
Q8KL44 | GPMA_RHIEC | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase | Rhizobium | MSTLVIVRHGQSEGNARGEFTGTSDVPLTQEGWSESRRAGSLLANLGISFDIAFSSALLRTVDTCRAILNETNGDLLEPIRRTELNERDYGQLTGINKNVARERWGQDVVQVWRRSYSTPPPGGESIRDISARVLPFLISEVFPPLLRGKSVLVVAHGNTIRSLKQGIERLTIQDTLAIESPTAAPTVYRIASDLSIIEKTNVLVGTVC | Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. | Q8KL44 |
Q8DZL1 | KUP_STRA5 | Probable potassium transport system protein kup | Streptococcus | MQHVNHSSFDKASKAGFIIALGIVYGDIGTSPLYTMQSLVENQGGISSVTESFILGSISLIIWTLTLITTIKYVLVALKADNHHEGGIFSLYTLVRKMTPWLIVPAVIGGATLLSDGALTPAVTVTSAVEGLKVVPSLQHIFQNQSNVIFATLFILLLLFAIQRFGTGVIGKLFGPIMFIWFAFLGISGLLNSFAHPEVFKAINPYYGLKLLFSPENHKGIFILGSIFLATTGAEALYSDLGHVGRGNIHVSWPFVKVAIILSYCGQGAWILANKNAGNELNPFFASIPSQFTMHVVILATLAAIIASQALISGSFTLVS... | Transport of potassium into the cell. | Q8DZL1 |
Q9RPW3 | MCH_METTO | Methenyl-H4MPT cyclohydrolase | Methylococcus | SLSHGEGKNAFYALGSGPARALATKVKDGNEEPVEELYKELGYRDHSNETAIVMEVDKVPPVEVIEKIAKACKVDASGVHVILTPTSSLAGGMQVVGRVLEVALHKAHSLHFPLGNIIDGTGTAPVPPPHPNFVKA | Catalyzes the hydrolysis of methenyl-H(4)MPT(+) to 5-formyl-H(4)MPT. | Q9RPW3 |
O80739 | POT12_ARATH | Putative potassium transporter 12 | Arabidopsis | MEEIEEGSSNNSIRRVGTGSSDRRWVDGSEVDSETPLFSEIRDRDYSFGNLRRRLMKKPKRADSLDVEAMEIAGSHGHNLKDLSLLTTLGIAFQTLGVVYGDMGTSPLYVFSDVFSKVPIRSEVDVLGALSLVIYTIAVIPLAKYVFVVLKANDNGEGGTFALYSLICRYAKVNKLPNQQPADEQISSFRLKLPTPELERALGIKEALETKGYLKTLLLLLVLMGTSMIIGDGILTPAMSVMSAMSGLQGEVKGFGTNALVMSSIVILVALFSIQRFGTGKVGFLFAPVLALWFFSLGAIGIYNLLKYDFTVIRALNPFY... | Putative potassium transporter. | O80739 |
Q2TAK8 | PWP3A_HUMAN | Protein expandere | Homo | MADAKYVLCRWEKRLWPAKVLARTATSTKNKRRKEYFLAVQILSLEEKIKVKSTEVEILEKSQIEAIASSLASQNEVPAAPLEELAYRRSLRVALDVLSEGSIWSQESSAGTGRADRSLRGKPMEHVSSPCDSNSSSLPRGDVLGSSRPHRRRPCVQQSLSSSFTCEKDPECKVDHKKGLRKSENPRGPLVLPAGGGAQDESGSRIHHKNWTLASKRGGNSAQKASLCLNGSSLSEDDTERDMGSKGGSWAAPSLPSGVREDDPCANAEGHDPGLPLGSLTAPPAPEPSACSEPGECPAKKRPRLDGSQRPPAVQLEPMA... | Involved in the DNA damage response pathway by contributing to the maintenance of chromatin architecture. Recruited to the vicinity of DNA breaks by TP53BP1 and plays an accessory role to facilitate damage-induced chromatin changes and promoting chromatin relaxation. Required for efficient DNA repair and cell survival ... | Q2TAK8 |
Q97L52 | ENO_CLOAB | 2-phosphoglycerate dehydratase | Clostridium | MKSYVEIVDVMARQILDSRANPTVEVEVVLEDGTVGRASVPSGASTGQFEAVELRDNDKAQYLGKSVLNAVDNVNETIATELIGMNVFDQTLIDQTMLEIDGTENKSKLGANAMLGVSLAVARAAAEYLGISLYQYLGGVNAKVLPVPMMNIVNGGKHADNNVDFQEFMIMPAGAPSFSEALRSCAEVYHTLKSLLQSKGLETAVGDEGGFAPNLNSNEEAIQIILEAVTKAGYEPGKDMFIAMDPASTEFYENGKYNLKGEGKVYTSEEMVEVYANLVEKYPIISLEDGMAEEDWDGWKLLTDRIGDKVQLVGDDLFVT... | Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. | Q97L52 |
P42851 | IMDH_PYRFU | Inosine-5'-monophosphate dehydrogenase | Pyrococcus | MGKFVEKLENAIRGYTFDDVLLIPQPTEVEPKDVDVSTQITPNVKLNIPILSAAMDTVTEWEMAVAMAREGGLGVIHRNMSIEEQVEQVKRVKRAERFIVEDVITIAPDETIDYALFLMEKHGIDGLPVVEEDRVVGIITKKDIAAREGRTVKELMTREVITVPESVDVEEALKIMMENRIDRLPVVNEDGKLVGLITMSDLVARKKYKNAVRNEKGELLVAAAVSPFDLRRAIELDRAGVDVIVVDTAHAHNLKAIKAMKEMRQKVSADFIVGNIANPKAVDDLTFADAVKVGIGPGSICTTRIVAGVGVPQITAIAMV... | Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. | P42851 |
O14832 | PAHX_HUMAN | Phytanoyl-CoA alpha-hydroxylase | Homo | MEQLRAAARLQIVLGHLGRPSAGAVVAHPTSGTISSASFHPQQFQYTLDNNVLTLEQRKFYEENGFLVIKNLVPDADIQRFRNEFEKICRKEVKPLGLTVMRDVTISKSEYAPSEKMITKVQDFQEDKELFRYCTLPEILKYVECFTGPNIMAMHTMLINKPPDSGKKTSRHPLHQDLHYFPFRPSDLIVCAWTAMEHISRNNGCLVVLPGTHKGSLKPHDYPKWEGGVNKMFHGIQDYEENKARVHLVMEKGDTVFFHPLLIHGSGQNKTQGFRKAISCHFASADCHYIDVKGTSQENIEKEVVGIAHKFFGAENSVNL... | Catalyzes the 2-hydroxylation of not only racemic phytanoyl-CoA and the isomers of 3-methylhexadecanoyl-CoA, but also a variety of other mono-branched 3-methylacyl-CoA esters (with a chain length of at least seven carbon atoms) and straight-chain acyl-CoA esters (with a chain length longer than four carbon atoms) . Doe... | O14832 |
Q96AA3 | RFT1_HUMAN | Protein RFT1 homolog | Homo | MGSQEVLGHAARLASSGLLLQVLFRLITFVLNAFILRFLSKEIVGVVNVRLTLLYSTTLFLAREAFRRACLSGGTQRDWSQTLNLLWLTVPLGVFWSLFLGWIWLQLLEVPDPNVVPHYATGVVLFGLSAVVELLGEPFWVLAQAHMFVKLKVIAESLSVILKSVLTAFLVLWLPHWGLYIFSLAQLFYTTVLVLCYVIYFTKLLGSPESTKLQTLPVSRITDLLPNITRNGAFINWKEAKLTWSFFKQSFLKQILTEGERYVMTFLNVLNFGDQGVYDIVNNLGSLVARLIFQPIEESFYIFFAKVLERGKDATLQKQE... | May be involved in N-linked oligosaccharide assembly. May participate in the translocation of oligosaccharide from the cytoplasmic side to the lumenal side of the endoplasmic reticulum membrane. | Q96AA3 |
A1W1N6 | AROC_CAMJJ | 5-enolpyruvylshikimate-3-phosphate phospholyase | Campylobacter | MNTFGTRLKFTSFGESHGVAVGCIIDGMPAGVKFDEEFLQNELDKRKGGSKFATPRKESDKAQVLSGVFEGYTTGHPIAIVVFNENAHSKDYDNLKDLFRPAHADFTYFYKYGIRDHRGGGRSSARESVARVAGGAVAAMLLCEFGICVQSGVFGIGTFVSNLKEEEFDFEFAKKSEIFCLDPKLESDFKNEILNARNSKDSVGAAVFTKVSGMLVGLGEVLYDKLDSKLAHALMGVNAVKAVEIGEGINASKMRGSCNNDALKDGKFLSNHSGGILGGISNGENLILKTYFKPTPSIFAKQESIDKFGNNLEFELKGRH... | Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a s... | A1W1N6 |
A9M352 | RSMA_NEIM0 | S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase | Neisseria | MKEHKARKRFGQNFLQDTRIISDIVNAVRPQADDVVIEIGPGLAAITEPLAKKLNRLHVVEIDRDIVCRLKTLPFADKLVIHEGDVLQFDFNGIAGKKKIVGNLPYNISTPLLFKLAEVADDVVDMHFMLQKEVVDRMVAAPKSNDYGRLGVMLQYFFDMELLIDVPPESFDPAPKVDSAVVRMIPVKHRIGKADDFEHFAKLVKLAFHQRRKTIRNNLKELAGDDDLQAVDINPQDRAEHIAPEKYVALSNYLAGKAV | Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits. | A9M352 |
A3MKS8 | RNH2_BURM7 | Ribonuclease HII | pseudomallei group | MATTRKPRGGAGGATQPALDFDAPGEIVCGVDEAGRGPLAGPVVAAAVVLDPARPIVGLDDSKALSAKKRERLFDEIVAYALAYSVASASVEEIDSLNILHATMLAMKRAVEGLSVLPTLAKIDGNRCPMLAIRSEAIVGGDALVPSISAASILAKVTRDRMLVELHQQFPMYGFDAHAGYGTPQHLAALREHGPCEHHRRSFAPVREAFDLIR | Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. | A3MKS8 |
Q2JRC6 | AROE_SYNJA | Shikimate dehydrogenase (NADP(+)) | unclassified Synechococcus | MDRRISGSTQLLGLIGDPVAHSLSPAMHNAALAAMGEDYCYVPFPVAAERLAVAVAGLAAIGVRGFNVTIPHKQAILPLLSQVEARAAAVGAVNTVYALPEGGWGGTNTDIDGFVQPLLGLEKGIPTLILGSGGAARAAIQGCLELGLGPVRVAGRSPEKLRALQQTWPQVETLSWAELDRHLAETRLLVNTTPVGMHKPGSLAELSPLSWEQLRLLPAGATVYDLVYVPDPTPLLRMAAELGHTPIGGLEMLIHQGAKALSLWLGGKLVPVEVMRQAARQQLAQIGDPNS | 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). | Q2JRC6 |
Q8UG81 | BPT_AGRFC | Aspartate/glutamate leucyltransferase | Agrobacterium tumefaciens complex | MNTQATPSPQFYLTAPATCPYLPNQMERKVFTHLVGPRAPEMNDLLTQGGFRRSQNIAYRPACETCRACVSVRILTEQFQPTKSMRRVLAANSDVVATVHAAEPSTEQFALFRRYLDHRHQSGGMSDMSALDYAIMVEDTHVNTRIIEYRVREPGSGIDSSKRGELLAVALSDVMSDGLSMVYSFFNPELEKRSLGTFMIIDHITRTRALGLPHVYLGYWVDGSEKMGYKTRYHPQEHLTPRGWEIYSPKEE | Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate. | Q8UG81 |
P83546 | CHY2_PAGMA | Chrysophsin-2 | Pagrus | FFGWLIRGAIHAGKAIHGLIHRRRH | Has antibacterial activity against Gram-positive bacteria B.subtilis ATCC 6633, L.garvieae ATCC 49156 and S.iniae F-8502, and Gram-negative bacteria E.coli WT-2, V.anguillarum ATCC 19264, V.penaeicida KHA, V.harveyi ATCC 14126, V.vulnificus ATCC 33148 and A.salmonicida NCMB 1102. Has hemolytic activity against human re... | P83546 |
Q8U004 | RS3_PYRFU | Small ribosomal subunit protein uS3 | Pyrococcus | MAIERYFIREAVREMLIDEFLEKELRRAGYGGLDIKKTPLGTKVIIFAANPGYVIGRGGRRIRELTRILEKQFGLENPQIEVEEIKNPYLNAKVQAVRLAQALERGIHFRRAAYAALRAIMNNGARGVEIRLSGKLTGERAKSIRFYQGYLAKVGNPAETLVSKGYAQALLKLGVIGVKVAIMPPGARLPDEIEIIEKPVEEEVVSNEAE | Binds the lower part of the 30S subunit head. | Q8U004 |
B7MIE5 | CBPM_ECO45 | Chaperone modulatory protein CbpM | Escherichia | MANVTVTFTITEFCLHTGISEEELNEIVGLGVVEPSEIQETTWVFDDHAAIVVQRAVRLRHELALDWPGIAVALTLMDDIAHLKQENRLLRQRLSRFVAHP | Interacts with CbpA and inhibits both the DnaJ-like co-chaperone activity and the DNA binding activity of CbpA. Together with CbpA, modulates the activity of the DnaK chaperone system. Does not inhibit the co-chaperone activity of DnaJ. | B7MIE5 |
Q48GW4 | FADA_PSE14 | Fatty acid oxidation complex subunit beta | Pseudomonas | MSLNPRDVVIVDFGRTPMGRSKGGMHRNTRAEDMSAHLISKLLERNNKVDPAEVEDVIWGCVNQTLEQGWNIARMASLLTQIPHTSAAQTVSRLCGSSMSALHTAAQAIMTNNGDVFVIGGVEHMGHVSMMHGVDPNPHMSLHAAKASGMMGLTAEMLGKMHGITREQQDAFGLRSHQLAHKATLEGKFKDEIIPMQGYDENGFLKVFDYDETIRPDTTLESLAALKPAFNPKGGTVTAGTSSQITDGASCMIVMSAQRAQDLGIQPLAVIRSMAVAGVDPAIMGYGPVPATQKALKRAGLTIADIDFIELNEAFAAQAL... | Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. | Q48GW4 |
P21920 | COBK_SINSX | Precorrin-6X reductase | Sinorhizobium | MAGSLFDTSAMEKPRILILGGTTEARELARRLAEDVRYDTAISLAGRTADPRPQPVKTRIGGFGGADGLAHFVHDENIALLVDATHPFAARISHNAADAAQRTGVALIALRRPEWVPLPGDRWTAVDSVVEAVSALGDRRRRVFLAIGRQEAFHFEVAPQHSYVIRSVDPVTPPLNLPDQEAILATGPFAEADEAALLRSRQIDVIVAKNSGGSATYGKIAAARRLGIEVIMVERRKPADVPTVGSCDEALNRIAHWLAPA | Catalyzes the reduction of the macrocycle of precorrin-6X into precorrin-6Y. | P21920 |
A3CL11 | METE_STRSV | Methionine synthase, vitamin-B12 independent isozyme | Streptococcus | MSTTIIGFPRLGEFRELKFTTEKYFRHEISAEELLAAAKELRAKHWNIVKEKGISEIPSNDFSHYDNVLDAAFLFNVVPSSVQGLELTDLERYFALARGYQGEKGDVRALPMKKWFNTNYHYIVPKFEKETQVKLAGHKIFDEFAEAKELGLVTRPVVVGPFTLLQVSDFEDGVAPADFVDALVVAYQEVFAKLAELGAERIQLDEPSLVKDLSAEEKALFLDLYKKLLADKKGLEVLVQTYFGDVRDIYADLVQLPVDAIGLDFVEGKKTLELVKGGFPADKTLYAGIVNGKNIWRNNYEKSLAVLEQIPAENIVLTSS... | Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation. | A3CL11 |
C1D5S5 | BIOC_LARHH | Biotin synthesis protein BioC | Laribacter | MTEAFYTDKSRVRASFDRAAATYDRAAVLQREVCDRMATRLDLIRHAPARVLDAGSGTGYGAGLLRARYPEAQVTELDLAPSMLRASRDKQLPQGRLRRLFARAPALVCADLEQLPLASGSLDMVWSSLALQWLNTPDAVLAEFHRVLRVDGLLMFATLGPDTLKELRQAFAGIDGATHVNQFIDMHDMGDALVRAGFATPVMDVERIVLTYDEVKAVMRDLKAIGAHNATAGRGRGLMGRQAWQRIEAAYDRLRQDGRLPATYEVVYGHAWRPAARPRRKLDDGRDIIEFHPHAPA | Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway. | C1D5S5 |
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