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
|
|---|---|---|---|---|---|---|
P34218 | SAS3_YEAST | Something about silencing protein 3 | Saccharomyces | MSLTANDESPKPKKNALLKNLEIDDLIHSQFVRSDTNGHRTTRRLFNSDASISHRIRGSVRSDKGLNKIKKGLISQQSKLASENSSQNIVNRDNKMGAVSFPIIEPNIEVSEELKVRIKYDSIKFFNFERLISKSSVIAPLVNKNITSSGPLIGFQRRVNRLKQTWDLATENMEYPYSSDNTPFRDNDSWQWYVPYGGTIKKMKDFSTKRTLPTWEDKIKFLTFLENSKSATYINGNVSLCNHNETDQENEDRKKRKGKVPRIKNKVWFSQIEYIVLRNYEIKPWYTSPFPEHINQNKMVFICEFCLKYMTSRYTFYRHQLKCLTFKPPGNEIYRDGKLSVWEIDGRENVLYCQNLCLLAKCFINSKTLYYDVEPFIFYILTEREDTENHPYQNAAKFHFVGYFSKEKFNSNDYNLSCILTLPIYQRKGYGQFLMEFSYLLSRKESKFGTPEKPLSDLGLLTYRTFWKIKCAEVLLKLRDSARRRSNNKNEDTFQQVSLNDIAKLTGMIPTDVVFGLEQLQVLYRHKTRSLSSLDDFNYIIKIDSWNRIENIYKTWSSKNYPRVKYDKLLWEPIILGPSFGINGMMNLEPTALADEALTNETMAPVISNNTHIENYNNSRAHNKRRRRRRRSSEHKTSKLHVNNIIEPEVPATDFFEDTVSSLTEYMCDYKNTNNDRLIYQAEKRVLESIHDRKGIPRSKFSTETHWELCFTIKNSETPLGNHAARRNDTGISSLEQDEVENDVDTELYVGENAKEDEDEDEDFTLDDDIEDEQISEENDEEEDTYEEDSDDDEDGKRKGQEQDENDIESHIRKERVRKRRKITLIEDDEE | Catalytic component of the histone acetyltransferase NuA3 complex, that acetylates Lys-14 of histone H3. Recruitment of NuA3 to nucleosomes requires methylated histone H3. In conjunction with the FACT complex, NuA3 may be involved in transcriptional regulation. In vitro, SAS3 acetylates free histones H3 and H4. It is involved in silencing the HMR locus. | P34218 |
P74836 | NSAC_SPHXE | 1,2-dihydroxynaphthalene dioxygenase | Sphingobium | MSSVSELGYLGMSVTDLDAWRAYAAEVAGMEVVDEGESDRIYLRMDLWHHRIALIKGDTDDLAYMGWRLGDPTEFESMVEKLTNAGIAVTVASDAEARERRVLGLAKLTDPGGNPTEIFYGPQVDAHKPFHPGRPMFGKFVTGSEGIGHCILRQDDVEAAAAFYRLLGLRGSVEYQLHLPNGMVAMPYFMHCNERQHSVAFGLGPMEKRINHLMFEYTELDDLGLAHDIVRERQIDVALQLGKHANDLALTFYCANPSGWLWEFGWGARKAPAQQEFYTRDIFGHGNEAQGYGMDVPL | Involved in the naphthalene and naphthalenesulfonate catabolic pathway. Catalyzes the meta-cleavage of 1,2-dihydroxynaphthalene (1,2-DHN) to yield 2-hydroxychromene-2-carboxylic acid. Can also cleave 1,2,5-trihydroxynaphthalene (1,2,5-THN), 1,2,6-trihydroxynaphthalene (1,2,6-THN), 1,2,7-trihydroxynaphthalene (1,2,7-THN), 2,3-dihydroxybiphenyl, 3,4-dihydroxybiphenyl, catechol, 3-methylcatechol and 4-methylcatechol. | P74836 |
O16963 | NH130_CAEEL | Nuclear hormone receptor family member nhr-130 | Caenorhabditis | MQIATSSTSPSIFYTPSISPMEEDMNCQELVVNLYTCQVCALPAHGNHFGAISCRACAAFFRRACTGTKTTYKCKKQNNCDIWENGRYKCKKCRLDRCNEVGMDPGRFQFDRDLISATEKYPNSKNFRRTFGMSRLPETIEHFLGRPHFIIFLERHIYSHSEKNFVDLQHLIAKASKLLELGSEKPLIARNNLEKLALGLNLVRDQPAGSHDVQLVTKLGKDEALTFWETDFLTVAKWLTYFDDFQLLPHNQQILLLKSVWHVWNRLEKLALTATSRRQNVCEQKQLMLTYNSVCNPKTIELDYSWFTKYPKEQLCFFFDEMEDYMLTSALDPLTSLEPTDIELTYMLCQLCFHYAGKRYGGEILEVTEKFQENLADNLHDYYVNELNMPRYCGRLNQMLKINNLIQQDIWEKRAKHELAKVFDIFCIEFSHPEMFEDTG | Orphan nuclear receptor. | O16963 |
A1WFT0 | HIS3_VEREI | Phosphoribosyl-AMP cyclohydrolase | Verminephrobacter | MDWLDDVKWDAQGLVPVIAQEQGTGDVLMLAWMNREALRQTAALGRAVYFSRSRGKLWFKGEDSGHAQTVHEIRLDCDRDVLLLRVTQQGHQPGIACHTGRHSCFFSRLGDGAWQAVDAVLKDPRAIYG | Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP. | A1WFT0 |
C5A6A9 | THIC_THEGJ | Thiamine biosynthesis protein ThiC | Thermococcus | MTQLEAAKRGEITEEMKFIAEREGIDPEKLRRSVAKGYTVIFRNVRHDWVKPVAVGNVVRVKVNANIGTSRDIVNVKAEIEKAKVAVKYGADTIMDLSTGGDLDSIRKAIMHAVDVPIGTVPIYQAAEEMLAKGKAIIEMSEDDMWNAVEKHFKDGVDYTTIHVGVTKEVVEKMKRVKRVVGMVSRGGTFLAAWILHWGEENPFYRDYDYLLELAKEYDVVLSLGDGLRPGGLPDAGDELQIAELYTLGRLVRRAREAGVQTMVEGPGHVPIDQIPAQIKLAKVATDNAPFYVLGPIVTDIFPGYDHITSAIGGAIAALNGADFLCYVTPAEHLGLPTVEHVREGVIAAKIAAHAVNLTRFEADFKKDYLMSLARGKLDWARQFELSQDREKFIEIRKERPTKTEACSMCGDLCAIKLINDMLRKG | Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. | C5A6A9 |
Q47SE7 | GLGB_THEFY | Glycogen branching enzyme | Thermobifida | MTARPAVRQPAGLPCPQPCNRYGYPMTNALLAEIDALVAGTHHNPHALLGAHPGPEGVWVRALRPLARSVHVLLANGSRVELPHLHKGVFAGVVPGAEVPDYRLVVRYDDGTELTVDDPYRHLPTLGELDIHLIQEGRHEELWRVLGAHTKRFPSVLGDTEGTAFTVWAPNARGVRVIGDFNHWDGTGHPMRSLGSCGVWELFIPGVGDGTRYKYQVLGADGVWREKADPVAFATQAPPETASVVFTSRYTWQDDEWLTQRAAADLHRKPMSIYEVHLGSWRPGLSYRELADQLVDYVRELGFTHVEFLPVAEHPFGGSWGYQVTSYYAPTARFGSPDDFRYLVDRLHQAGIGVFLDWVPAHFPKDDWALSRFDGTALYEHPDPRRGIHPDWDTLIFNYGRTEVRNFLVANALFWLEEFHIDGLRVDAVASMLYLDYSRESGQWEPNAYGGRENLDAIDFLRELNATAYRRNPGIAMIAEESTAWPGVTRSTDTGGLGFGFKWNMGWMHDTLSYLQHDPVHRQYHHNEVTFSMVYAYSENYVLPLSHDEVVHGKRSLLYKMPGNEWQRCANLRALLAYMWAHPGKQLLFMGNEIAQGDEWSHDAGVQWWLLRYPHHAGMRRLVADLNRLYRNTRALWSQDTVPEGFTWLDGGDASGNTLSFLRWGDDGSVLACLVNFSGRPHPERRVGLPYAGRWREILNTDAVLYGGSGVSQPGIIEASEETPWQGQPASALVTYPPLGVSWLVFDGT | Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position. | Q47SE7 |
Q3BKD5 | MMS48_MAGGM | Probable magnetosome protein Mms48 | Magnetospirillum | MLLRLIVLLIFMSPVVFATLWFSDNVGSVQVEWLGWHVDSNMPVLLAVILVVFLIFSALSRLSALVADLPSKLGKSRQARGLEKGMSALLAALDAAESGDVGEGRRFAAEAARLLNNPGLAARLDRLLPRPPAQPVAPTRLEAAKGRLFARKPGPPPPPTPVVDKIQPVVVEKLAAAPAGPSREDLEAFSAKIRAGEWGAAQAWIGEAVLAGRLTPLVAARWRSVALEGQALEASPGDPARPLRLAREAMAADQTFLPPALHVIRAEVSEGRKAEAETLLASVWPHVPARVLLDACAPLWRDEDQDACLKRLEALAAIAPHHPDGHLAAGEAAFAVQKWGVARRHIMAALKIAPDALGCRLMAEIEEREPGGSARSAEIWRRREHEASLSPAWVCGACARVVEAWAACCPSCAGVATIEWTRSVKAEEALLPPATTASSMETPRLFRST | Overexpression in wild-type cells increases the number of cells with double magnetosome chains significantly. The 4 genes of this operon collectively influence magnetosome size and number. | Q3BKD5 |
Q5RC94 | NBR1_PONAB | Neighbor of BRCA1 gene 1 protein | Pongo | MEPQVTLNVTFKNEIQSFLVSDPENTTWADIEAMVKVSFDLNTIQIKYLDEENEEVSINSQGEYEEALKMAVKQGNQLQMQVHEGHHVVDEAPPPVVGAKRLAARAGKKPLAHYSSLVRVLGSDMKTPEDSAVQSFPLATCDTDQPQDKPPDWFTSYLETFREQVVKETVEKLEQKLHEKLVLQNPSLGSCPSEVSMPTSEETLFLPENQFSWHIACNNCQRRIVGVRYQCSLCPSYNICEDCEAGPYGHDTNHVLLKLRRPVVGSSEPFCHSKYSTPRLPAALEQVRLPLQPCTPVMPTLSAAFVDENLPDGTHLQPGTKFIKHWRMKNTGNVKWSADTKLKFMWGNLTLASTEKKDVLVPCLKAGHVGVVSVEFIAPALEGTYTSHWRLSHKGQQFGPRVWCSIIVDPFPSEESPDNIEKGMISSSKTDDLTCQQEETFLLAKEERQLGEVTEQTEGTAACIPQKAKNVASERELYIPSVDLLTAQDLLSFELLDINIVQELERVPHNTPVDMTPCMSPLPHDSPLIEKPGLGQIQEENEGAGFKALPDSMVSVKRKAENIASVEEAEEDLSGTQFVCETVIRSLTLDAAPDHNPPCRQKSLQMKFALPEEGPLGNEREEIVHIAEEEAVMEEEEDEEEEDELKDEVQSQSSASSEDYIIILPECFDTSRPLGDSMYSSALSQPGLERGAEGEPGVEAGQEPAEAGERLPGGENQPQEHSISDIFTTSQTLETVPLIPEVVELPPPLPRSSPCVHHHGSPGVDLPVTIPEVSSVPDQIRGEPRGSSGLVNSRQKSYDHSRHHHGSSIAGGLVKGALSVAASAYKALFAGPPVTAQPIVSEDQTAALMAHLFEMGFCDRQLNLQLLKKHNYNILQVVTELLQLNNNDWYSQRY | Acts probably as a receptor for selective autophagosomal degradation of ubiquitinated targets. | Q5RC94 |
A8IQT2 | CCD40_CHLRE | Flagellar-associated protein 172 | Chlamydomonas | MADPMDQPSTSDPVDNQIFGEQGGLRPDHPLLRRAQEALKVQFEANRTRLQEELREKANALKQAKARREALGVELYGFQQNLAKLQLNLETTHQNYQCEDQLNQLKQQLSLEEGDTKGERSRRVCVCVCRVCCRIDTLQDNLKGTQQQLALVSAQLEAQKRETRAALETLAEAEVGGCVRDEALSAIQDGMREQQQQELSLVLEIEGYKKDVVREQLKHESLTAVVRKVEGDAVFVQKQIEGAQERQARLQEILAKLAKSLEHTEAEGEADAVDRAITKVAAEGRAIEEEMLSALSDQTTAEKATSKTAADTQELRKRIRAEELAVVETENELAKLQVDILNTEAHNSRLGETLGLLDEELRDKGRTIEKYELEIKRRNDEIEKKTREIDILNRRRDCRGSAALDTRPLQAPPPPQVKSDLALTTPMYTPPPVPQPSVGMTVTTEKLVSDMEKALTKREIISVKGRATAAKSKSSTPAGSATASSRASPSASVASSTLTRNQLDRATTDLAKSIKDLEAGRYRPVVEDAAAVGEELGRAQDKLGRVVALLEGLRQAAPHLAGELDKVLCHVADVRA | Required for assembly of dynein regulatory complex (DRC) and inner dynein arm complexes, which are responsible for ciliary beat regulation, by acting as a molecular ruler that determines the 96 nanometer (nm) repeat length and arrangements of components in cilia and flagella . Together with CCDC39/FAP59 forms a 96-nm-long complex in flagella. This complex does not act as a physical ruler, but rather act as a negative regulator for radial spokes: the complex lays along specific protofilaments, masking radial spoke binding sites and allowing recruitment of inner dynein arm (IDA) and nexin-dynein regulatory complexes (N-DRC) . | A8IQT2 |
B7GI41 | TATA_ANOFW | Sec-independent protein translocase protein TatA | Anoxybacillus | MLSNIGVPGLILILVIALVIFGPKKLPEIGRAFGETLREFKKSTKGLRDEVLEELDENKK | 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. | B7GI41 |
Q5N3N8 | RL1_SYNP6 | 50S ribosomal protein L1 | Synechococcus | MTRKVSRRLQELQKKVEDRAYEPLAALNLLKETATAKFPESAEAHIRLGIDPKYTDQQLRTTVALPKGTGQTIRVAVIARGEKVAEAKAAGADIAGSEELIEEISKGFLDFDLLIATPDVMPQVAKLGRQLGPRGLMPSPKGGTVTFDLEQAVNEFKAGKLEFRADRTGIVHVLFGKASFSADDLLANLKALQETIDRNRPSGAKGRYWRSVYISATMGPAIEVDINALRDPKLAEA | Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA. | Q5N3N8 |
P13238 | VTU2_DROME | Protein TU-4 | Sophophora | MAFNFGHLLIAGLVALSAVSSETIQLQPTQGILIPAPLAENIRVSRAAYGGYGAAPAAPSYSAPAAPAAQAYSAPAAPAYSAPAAPAYSAPAAPAYSAPAAPAYSAPAAPAYSAPASIPSPPCPKNYLFSCQPSLQPVPCSAPAQSYGSAGAYSQYVPQYAVPFVREL | Major early eggshell protein. | P13238 |
Q83HK9 | RNH_TROW8 | Ribonuclease H | Tropheryma | MTNNEIIAATDGSSLANPGPSGWAWYVDENTWDSGGWDIATNNIAELTAVRELLIATRHTDRPILILSDSKYVINSLTKWVYSWKMRKWRKADGKPVLNQEIIQEIDSLMENRNIRMSWVNAHTGHPLNEAADSLARQAANNFSTRSAHIPGPGWTERSAK | Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. | Q83HK9 |
Q07YI6 | UNG_SHEFN | Uracil-DNA glycosylase | Shewanella | MTSHWQELFEQQQSQEYYQHLQHFIASQRADNKTVYPPDDEVFTAFDLTPLSEVKVVILGQDPYHGPNQAHGLSFSVKKGIKPPPSLANIYKELTNDIEGFVTPEHGNLTSWAEQGVLLLNTVLTVEQGLAHSHAKSGWETFTDNVLLRLDQQPSPIIFVCWGNHAIKKGRLITASHHHVLNGPHPSPLSAYRGFFGCGHFSSINQLLIEQGNLAINWQV | Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | Q07YI6 |
Q64427 | APT_MASNA | Adenine phosphoribosyltransferase | Mastomys | MSEPELQLVARRIRSFPDFPIPGVLFRDISPLLKDPDSFRASIRLLASHLKSLHGGKIDYIAGLDSRGFLFGPSLAQELGVGCVLIRKRGKLPGPTLSASYALEYGKAELEIQKDALEPGQRVVIVDDLLATGGTMCAACELLNQLRAEVVECVSLVELTSLKGRERLGPIPFFSLLQYD | Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. | Q64427 |
B1KEI0 | ASTE_SHEWM | Succinylglutamate desuccinylase | Shewanella | MLQALKESKDFLQLTLAQPQHFDETFTFMLGSHTQVEVWDTGVIVFEPKVARGKDIVLSCAVHGNETAPIELCNGLIKSLLEERLIAEQRVLFLFGNPPAIINGTRFIDENLNRLFNGAHSVGEGLVNPERIRAKKLEFYVDKFFSSSKDNSHKIHYDLHTAIRGSKHEKFAIYPYRPGRKYSGEQIMFLEACGIDTVLFHHEPTTTFSYFSSLNYQADAFTIELGKVLPMGQNDMTRFIALNEMLSRLIGNKSLELPDFNAKTVNLYQVCRAINKGFDDFEFTFANDVENFTSFPKGYILAKEGGENIKVEHEVEAIVFPNAKVPVGQRTVLCLKPASTENIDG | Transforms N(2)-succinylglutamate into succinate and glutamate. | B1KEI0 |
Q7NJY9 | G6PI_GLOVI | Phosphohexose isomerase | Gloeobacter | MTSTFAPTPLTQRAAWQALAAHYEQIREIHLRALFAEDPSRGERFALEAEGFYLDYSKNRLTDETLRLLSVLAEESDLRGRIEAMFSGEKINTTEQRSVLHTALRAPRGATVIEDGENVVPEVHAVLDRMAEFADRVRGGEWRGYTGRRIRTVVNIGIGGSYLGPDMAYDALKHYSDRDLKVRFAANVDGSNFAEVIHDLEPDETLFIVCSKTFTTLETMTNAHSARQWCLAALGDEQAIAKHFVAVSTNAAEVEKFGIDTAHMFGFWDWVGGRYSMDSAIGLSTMIAVGPEHFRAMLAGFHAMDEHFRTAPFERNLPVLMALIGLWYNNFFGAQTLAVLPYDYYLGKLPAYLQQLDMESNGKHVDIDGQPVTYQTGPIIWGQPGTDGQHSFYQLIHQGTKLIPCDFIGFCQTLNPIAPHHDQLMANFFAQTEALAFGKTEAEVRAEGVADWLLPHRVFEGNRPTNTLLAERLTPEVLGKLIALYEHKVFTQGVIWNLDSFDQWGVELGKVLAGRIIPELESAEEPELAHDSSTNALIRRYRRAKRQN | Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate. | Q7NJY9 |
O44665 | NLP28_CAEEL | GMYGGW-amide | Caenorhabditis | MISTSSILILVFLLACFMATSAQWGYGGYGRGYGGYGGYGRGMYGGYGRGMYGGYGRGMYGGWGK | May have antimicrobial activity. | O44665 |
O54909 | RDH16_MOUSE | Cis-retinol androgen dehydrogenase 1 | Mus | MWLYLVALVGLWTLLRFFRVRQVVSHLQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGNRGLWGLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRVSLFGGGYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSARLCSNTQMLWDQTSSEIREIYGEKYLASYLKRLNKLDKRCNKDLSGVTDCMEHALTACHPRTRYSAGWDAKLFYLPLSYLPTFLVDALLYWTSLKPEKAL | Oxidoreductase with a preference for NAD. Oxidizes all-trans-retinol, 9-cis-retinol, 11-cis-retinol and 13-cis-retinol to the corresponding aldehydes. Has higher activity towards CRBP-bound retinol than with free retinol. Oxidizes 3-alpha-hydroxysteroids. Oxidizes androstanediol and androsterone to dihydrotestosterone and androstanedione. Can also catalyze the reverse reaction. | O54909 |
Q12KM1 | RS20_SHEDO | 30S ribosomal protein S20 | Shewanella | MANSKSAKKRALQSEKRRQHNASRRSMLRTYVKKVIAAIKSGDHKAATEAFAAAQPIVDRMATKGLIHKNKAARQKARLNTKIKALAA | Binds directly to 16S ribosomal RNA. | Q12KM1 |
O25536 | DUT_HELPY | dUTP pyrophosphatase | Helicobacter | MKIKIQKIHPNALIPKYQTDGSSGFDLHAVEEVMIKPHSVGLVKIGICLSLEVGYELQVRTRSGLALNHQVMVLNSPGTVDNDYRGEIKVILANLSDKDFKVQVGDRIAQGVVQKTYKAEFIECEQLDETSRGSGGFGSTGVSKA | This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. | O25536 |
Q03QN5 | EFTU_LEVBA | Elongation factor Tu | Levilactobacillus | MAEKEHYERTKPHVNIGTIGHIDHGKTTLTAAITKVLADKGLAKAEDYADIDAAPEERERGITINTAHVEYETEKRHYAHIDAPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVDYIVVFLNKTDLVDDDELVDLVEMEVRELLSEYDYPGDDIPVIRGSALKALEGDEEQEKVILHLMDVVDDYIPTPERENDKPFLMPVEDVFTITGRGTVASGRIDRGTVKVGDEVEVVGLHEDVLKTTVTGLEMFRKTLDLGEAGDNVGALLRGVNREQVVRGQVLAQPGSIQTHEKFKGEVYILSKEEGGRHTPFFSNYRPQFYFHTTDITGVIELPDGVEMVMPGDNVTFTVELIQPAAIEKGTKFTVREGGHTVGAGTVTEIDD | This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. | Q03QN5 |
O13289 | CATA_CANAL | Peroxisomal catalase | Candida | MAPTFTNSNGQPIPEPFATQRVGQHGPLLLQDFNLIDSLAHFDRERIPERVVHAKGSGAYGVFEVTDDITDICAAKFLDTVGKKTRIFTRFSTVGGELGSADTARDPRGFATKFYTEEGNLDLVYNNTPVFFIRDPSKFPHFIHTQKRNPETHLKDANMFWDYLTSNEESIHQVMVLFSDRGTPASYREMNGYSGHTYKWSNKKGEWFYVQVHFISDQGIKTLTNEEAGALAGSNPDYAQEDLFKNIAAGNYPSWTAYIQTMTEAEAKEAEFSVFDLTKVWPHKKYPLRRFGKFTLNENPKNYFAEVEQAAFSPAHTVPYMEPSADPVLQSRLFSYADTHRHRLGTNYTQIPVNCPVTGAVFNPHMRDGAMTVNGNLGSHPNYLASDKPVEFKQFSLQEDQEVWNGAATPFHWKATPADFKQAQELWKVLKRYPNQQEHLAHNIAVHAAGADAAIQDRVFAYFGKVSQDLADAIKKEVLELSPRK | Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Required for hyphal growth. | O13289 |
Q7VPM9 | EPMA_HAEDU | EF-P-lysine lysyltransferase | Haemophilus | MSDASLTKINWQPTASIQTLLKRSKIMAEIRQFFTDRGVLEVETPALSEYSVTDVHLSTFSTEFLSPFAKQAKTLHLITSPEYHMKRLLAAGSSSIFQLCRVFRNEESGKRHNPEFTMLEWYRPHFDMYRLINEVDDLLQQILDCEPIESYSYQFVFQTYVGLDPLSASRAQLVEKARKHGFACEEDENRDTLLQFLFSEIVEANIGQERPTTVYHFPSSQAALAQISSEDHRVAERFEIYYKGLELANGFHELNDAKEQIRRFERDNQLREQMNLPPQPLDMRFLAALKAGIPNCSGVALGVDRLIMLALNANHIQEVMAFGVERA | With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P. | Q7VPM9 |
Q3JBV4 | NADK_NITOC | ATP-dependent NAD kinase | Nitrosococcus | MAKPFKIIGLIGKQKDPRIAESLQQVADFLVAKGLTLMIDQETAALFPSHHWEAVTRHELGQRCDLAIVVGGDGTLLHVARSLADSGIPLLGIKLGRLGFLADVLPEALGTDLAAMLAGHYREEERFLLQAELEQESQSYLIGTALNDITTHIREVVRLIEFETYINGRFLNSQRSDGLVVATPTGSTAYALSAGGPILDVNLNAMVLVSICPHALSNRPLVIDADSLVEIVISEYNTTPGQVSCDGQPGIALKVGDKVKIYKRPGRVRLIHPTAHDHYSILRAKLHWGRKLG | Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP. | Q3JBV4 |
P31069 | KCH_ECOLI | Voltage-gated potassium channel Kch | Escherichia | MSHWATFKQTATNLWVTLRHDILALAVFLNGLLIFKTIYGMSVNLLDIFHIKAFSELDLSLLANAPLFMLGVFLVLNSIGLLFRAKLAWAISIILLLIALIYTLHFYPWLKFSIGFCIFTLVFLLILRKDFSHSSAAAGTIFAFISFTTLLFYSTYGALYLSEGFNPRIESLMTAFYFSIETMSTVGYGDIVPVSESARLFTISVIISGITVFATSMTSIFGPLIRGGFNKLVKGNNHTMHRKDHFIVCGHSILAINTILQLNQRGQNVTVISNLPEDDIKQLEQRLGDNADVIPGDSNDSSVLKKAGIDRCRAILALSDNDADNAFVVLSAKDMSSDVKTVLAVSDSKNLNKIKMVHPDIILSPQLFGSEILARVLNGEEINNDMLVSMLLNSGHGIFSDNDELETKADSKESAQK | K(+)-specific ion channel. May play a role in the defense against osmotic shock. | P31069 |
C5BUP6 | RECF_BEUC1 | DNA replication and repair protein RecF | Beutenbergia | MYVSDLALTDFRSYADLVIGLEPGITAFVGPNGQGKTNLVEAIGYLGTFSSHRVSGDAALVRWGAERAVVRAKVVRRARPTLVELEIVAGRANRARVDRSPVSRVREAAGIARSVIFAPEDLALVKGDPDGRRRFLDDLLVQLSPRLAGVRSEYERVLRQRTALLKSAGPARRRSGDGEPAALRTLDVWDGHLARAGAELVAARVRLVQDLRPHVGATYEQVSAAQSEARISYRASVEEARPDDAPTEVVESVETELTRADLVEARLLEAMARLRTREIERGVSLVGPHRDDLVLTLADMPAKGYASHGESWSYALALRLASYALLRDDGEAGGGGEPVLVLDDVFAELDARRRTRLASIVASAEQVLVTAAVAEDVPEELEGARMDVMGGEVLRVR | The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP. | C5BUP6 |
C5D4R3 | ISPH_GEOSW | 4-hydroxy-3-methylbut-2-enyl diphosphate reductase | unclassified Geobacillus | MEVIKITPRGYCYGVVDAMVIARNVALDPTLPRPIYILGMIVHNKHVTDAFAEEGIITLDGENRLEILEKIDKGTVIFTAHGVSPEVKRRAREKGLVTIDATCPDVTKTHNLIKEKLADGYEIIYIGKKGHPEPEGAVGIDPTRIHLVETMEDVERLTIENDRIMVTNQTTMSQWDVADIMAKVKEKYPHVEMHKEICMATQLRQEAVAEQAKDADVTIVVGDPRSNNSNRLAQVSEEIAGTKAYRVADVTEIDINWIKDAKKVAVTAGASTPTPITKEVIDFLEQFDPNDPNTWKRERKVPLQKILPKVKAKKE | Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis. | C5D4R3 |
Q4WKX3 | FGNE_ASPFU | Fumigermin biosynthesis cluster protein AFUA_1G00970 | Aspergillus subgen. Fumigati | MTVAISNPAAPPVSARAYLSVIGGTCALLCTVGFVVAFGVFQGYYTEHLLRGMSEFDIPWIGSASIFLLYVSAPICGVLVDRFGPKVLLIAGSIGVLVAIFMISLCSQYYQIFLAQAVLLGISMGFVTWPPFAVVSRNLPHHRGLALGVITGGSSVGGIVWSIMIEELLTKRNLGFPWTVRVLGFTMLPLLAFACISITEPPKQSQPQPRPALEATVEGGSASPTPKPEYASLPLLRSTVFISICVGFGLAFLGLFNPFFYISSYAAGHGASAQTSSYMISIMNAATLFGRVIPGIVADRVGHYNVMIFVLLASGITSFCWTEVRSLTGLVIWSIAYGFSSGAILSLQGACAGKIATPQNQGKAIGFLQGSLAVTVLVGSPIGGQLLGHYGYLSLSMFTGATLVMGAVVMGYARLCLNRSPMEAHQFRFLLAPN | MFS-type transporter; part of the gene cluster that mediates the biosynthesis of fumigermin that inhibits germination of spores of the inducing S.rapamycinicus, and thus helps the fungus to defend resources in the shared habitat against a bacterial competitor . May be involved in the secretion of fumigermin (Probable). | Q4WKX3 |
Q7N198 | GCSH_PHOLL | Glycine cleavage system H protein | Photorhabdus | MSNVPAELKYVESHEWVRAEGNDEYTVGITEHAQELLGDMVFVDLPEVGDQINLGDDCAVVESVKAASDIYAPLSGKIIAVNDALNDAPELVNSEPYHEGWLFRIKASDKSELSSLLNAEGYQALLDEEE | The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. | Q7N198 |
Q0BUM8 | RS13_GRABC | 30S ribosomal protein S13 | Granulibacter | MARIAGVNIPTNKRVAISLRYIYGIGPAQAQKICTELSIPDERRVNQLSDDEILRIRELIDREYRVEGDLRREVAMNIKRLMDLGCYRGLRHRRGLPVRGQRTHTNARTRKGKAVAIAGKKKVTR | Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites. | Q0BUM8 |
Q330E6 | NU2M_CHEPA | NADH dehydrogenase subunit 2 | Cheiromeles | MNPLIMSIIMSTIILGTLIVMTSSHWLMIWIGFEMNMLAIIPMLMKHHNPRSTEAATKYFFTQATASMLLMLAVIINLMYSGQWTGMKLFNPTASIIMTLALTMKLGLAPFHFWVPEVAQGIPLSSGLILLTWQKLAPLTVLYMISPAINLYLLLTMSMASIAIGGWGGLNQTQLRKIMAYSSIAHMGWMTAILIYNPTMTLLNLVIYILMTTTMFMLLMINSSTTTLSLSHMWNKMPLITTITLVTLLSLGGLPPLTGFLPKWMIIQELTKNDSIILPTLMAITALLNLFFYMRITYATSLTMFPTTNNMKIKWQFENTKHLNLLTPMIVLSTLTLPLAPMMTILN | 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. | Q330E6 |
Q7VTD5 | EFG_BORPE | Elongation factor G | Bordetella | MARKTPIERYRNIGISAHIDAGKTTTTERILFYTGVNHKLGETHDGSATMDWMEQEQERGITITSAATTAFWRGMAGNYPEHRINIIDTPGHVDFTIEVERSMRVLDGACMVYCAVGGVQPQSETVWRQANKYGVPRLAFVNKMDRTGANFFKVYDQLKTRLRANPVPIVIPIGVEDSFTGVVDLVKMKAIIWDEASQGTKFEYGDIPAELEGTANEWREKLVEAAAESSEELMNKYLETGSLDEDDINVALRQRTIAGEIQPMLCGTAFKNKGVQRMLDAVIDYLPSPADIPPVDGQDDDGNPIKRSADDAEKFSALAFKLMSDPFVGQLTFVRVYSGVLKSGDTVYNPIKGKKERIGRLLQMHANNREEIKEVLAGDIAAVVGLKDVTTGETLCDIDSHILLERMEFPEPVISQAVEPKSKADQEKMGLALSRLAQEDPSFRVRSDEESGQTIISGMGELHLEILVDRMRREFGVEANVGKPQVAYRETIRKNCDEVEGKFVKQSGGRGQYGHVVLKLEPLPPGGGYEFVDAIKGGVVPREYIPAVDKGIQETLPAGILAGYPVVDVKATLFFGSYHDVDSNENAFKMAASMAFKEGMRRASPVLLEPMMAVEVETPEDYAGTVMGDLSSRRGMVQGMDDIVGGGKTIKAEVPLAEMFGYATNLRSLTQGRATYTMEFKHYAEAPKNVADEVIAARGK | Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. | Q7VTD5 |
Q29036 | DAD1_PIG | Defender against cell death 1 | Sus | MSASVLSVISRFLEEYLSSTPQRLKLLDAYLLYILLTGALQFGYCLLVGTFPFNSFLSGFISCVGSFILAVCLRIQINPQNKADFQGISPERAFADFLFASTILHLVVMNFVG | Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. | Q29036 |
Q894P6 | HTPG_CLOTE | High temperature protein G | Clostridium | MAVKQFKAESKRLLDLMINSIYTNKEIFLRELISNASDAIDKRYYRSLTDENISFNKKDFYIRIIPNKEERTLTIIDTGIGMSVEELENNLGTIAKSGSLAFKNKMESKEGIDIIGQFGVGFYSAFMIADKIVVKSHSIDSDEAYKWESKGVEGYEIEKCEKDELGTEIILKIKENTDDENYDEFLEEYNIKNLIKKYSNFIKYPIKMNMKKTKLKEGTKDEYEDYFEDETLNSMVPIWKKNKNEVKTEDYERFYIDKHFGYDKPLKSIRSKVEGVVSYTALLFIPSTTPYDFYTRNFEKGLELYSNGVLIMEKCADLLPDYFSFVQGLVDSEDLSLNISRELLQHDRQLKLIAKNIKEKIKSELLSILKNKREDYIKFYNNFGRQLKYGVYSDFGANKEVLQDLIMFYSSTEKKLVTLDEYVSRMKDDQKYIYYAPGENIDKIEKLPQTEIVRDKGYEILYFADEVDEFAIKMLMNYKEKEFKSVYSKDLGFEAEEKEEQKENDENKEVFEFMKDVLNGKVKEVRASKRLKSHPVCLANASDISIEMEKVLSMMPNNENIKADKILEINTNHNMFNTIKSAFKDDKDKLKMLSSLLYNQALLIEGLPIEDPVQFANDVCKLIK | Molecular chaperone. Has ATPase activity. | Q894P6 |
B4SKG5 | DTD_STRM5 | Gly-tRNA(Ala) deacylase | Stenotrophomonas maltophilia group | MLVLIQRASQAAVHVDDEVVGQIGPGLLALVGMEPGDTEAQLQRMAERLLGYRVFADEAGKMNRSLRDTGGGLLLVSQFTLAADTRSGMRPSFTSAAPPAEAEQGFNRFVEICRENHAPGVETGRFGAHMVVSLVNDGPVTFLLRP | An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality. | B4SKG5 |
Q87YG5 | PLSX_PSESM | Phosphate-acyl-ACP acyltransferase | Pseudomonas | MSAPIIAIDAMGGDFGPRNIVQASLACLTATPSLHLALVGQASLIEELIASHAAVDRSRLRVVNATESIAMDERPSQALRGKSDSSMRVALELVSSGQAQACVSAGNTGALMALSRYVLKTLPGIDRPAMIAAIPTRTGHCQLLDLGANVDCSAEALYQFAVMGSVLAETLGVTKPRVALLNVGTEDIKGNQQVKLAAGLLQAAAGLNYIGYVEGDGVYRGEADVVVCDGFVGNVLLKSSEGLATMIAARIDALFNRNLLSRAVGALALPLLRRLQIDLAPARHNGASLLGLQGVVVKSHGSASVSGFQSAIQRAIVESREDLPQRLKGRLEVMFADGRT | 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. | Q87YG5 |
Q48745 | DDL_LEUME | D-alanylalanine synthetase | Leuconostoc | MTKKRVALIFGGNSSEHDVSKRSAQNFYNAIEATDKYEIIVFAIAQNGFFLDTESSKKILALEDEQPIVDAFMKTVDTSDPLARIHALKSAGDFDIFFPVVHGNLGEDGTLQGLFKLLDKPYVGAPLRGHAVSFDKALTKELLTVNGIRNTKYIVVDPESANNWSWDKIVAELGNIVFVKAANQGSSVGISRVTNAEEYTEALSDSFQYDYKVLIEEAVNGARELEVGVIGNDQPLVSEIGAHTVPNQGSGDGWYDYNNKFVDNSAVHFEIPAQLSPEVTKEVKQMALDAYKVLNLRGEARMDFLLDENNVPYLGEPNTLPGFTNMSLFKRLWDYSDINNAKLVDMLIDYGFEDFAQNKKLSYSFVSLGEEKIGKFN | Cell wall formation. | Q48745 |
A0QND0 | RSMG_MYCA1 | 16S rRNA 7-methylguanosine methyltransferase | Mycobacterium avium complex (MAC) | MKHVGPVEPAAGGPEVPPVAALGAAPESAAALFGPRLATAQRYAEVLGTAGVERGLLGPREVDRIWDRHILNSAAVAGLLGRGDRIIDIGSGAGLPGIPLAIARPDLEVVLLEPLLRRSEFLTEVVDELGLAVEVVRGRAEERPVRNRFGDRDAAVSRAVAALDKLTKWSMPLLRHDGRMLAIKGERAAEEVDRYRRVMTASGAADVRVVTCGANYLRPPATVVSARRAKPPHPKSARTGKAGTR | Specifically methylates the N7 position of guanine in position 518 of 16S rRNA. | A0QND0 |
Q07LR5 | METN_RHOP5 | Methionine import ATP-binding protein MetN | Rhodopseudomonas | MNEIAMNAPWPPHAGATTALASLQPTTGIRIEGVRKVYAARKSSAEVVALDGINLHVPKGSIQGVIGRSGAGKSTLIRLVNGLDKPSEGKVFVNDVEITSLSEPELRQARRSIGMVFQHFNLLSSRTAFGNVALPLEIAGTPKTEIEKRVLPLLDMVGLADKRDRYPAELSGGQKQRVGIARALATEPSVLLSDEATSALDPETTDQILDLLKQINRDLHLTILFITHEMAVVKALADRVAVIEGGRIVEEGSTFDVFATPRHEVTRRFVSSVTGSGAPDWLLAQPHEPPGGKAVLRITFKGSDANQPLLSHIARTLDIDINILSGQVEMIADHPFGTLIVSLTPSPDILRQVIAKLSTNNNLVEQLGYVA | Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system. | Q07LR5 |
O26762 | PDXS_METTH | Pdx1 | Methanothermobacter | MLHGTEVLKKGFAKMTKGGVIMDVVNAEQAAIAEDSGAVAVMALEKVPADIRASGGVARMADPNKVQEIMDAVSIPVMAKVRIGHFVEAQVLEALGVDMIDESEVLTPADERFHIDKKKFTVPFVCGARNLGEALRRIDEGAAMIRTKGEPGTGNIVEAVRHMRIMMSEIREIQNKEEEELWEVSRKIEAPLELVRETAKLGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSDNPEGYARAIVEATAHYDDPEVIAEVSRGLGTAMRGLEISEIPEEGRMQDRGW | Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. | O26762 |
A7MIM2 | LSPA_CROS8 | Signal peptidase II | Cronobacter | MSKPILSTGLRWLWLVVVVLIVDLGSKALILQHFALGETVSLFPSLNLHYARNYGAAFSFLADKGGWQRWFFAGIAIGICVLLVVMMYRAKASQKLNNIAYALIIGGALGNLFDRLWHGFVVDMIDFYVGDWHFATFNLADTAICIGAALVVLEGFLPSKQKATA | This protein specifically catalyzes the removal of signal peptides from prolipoproteins. | A7MIM2 |
Q4R5Q4 | ECSIT_MACFA | Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial | Macaca | MSWVQATLLARGLCRAWGGICRAALPGTSISQVPRQLPRGLHCSAAPHSSEQSLVSSPPEPRQRPTKALVPYEDLFGQAPSGERDKASFLQAVQKFGEHSVRKRGHIDFIYLALRKMREYGVERDLAVYNQLLDIFPKEVFRPRNVIQRIFVHYPRQQECGIAVLEQMESHGVMPNKETEFLLIQIFGRKSYPMLKLLRLKMWFPRFMNINPFPVPRDLSQDPVELATFGLRHMEPDLSARVTIYQVPLPKDSTGAADPPQPHIVGIQSPDQQAALARHNPARPIFVEGPFSLWLRNKCVYYHILRADLLPPEEREVEETPEEWNLYYPMQLDLEYSRSGWDDYEFDINEVEEGPVFAMCMAGAHDQATLAKWIQGLQETNPTLAQIPVVFRLTRATGELHTSSAGLEEPPPPEDHEEDDSRQRQQQGQS | As part of the MCIA complex, involved in the assembly of the mitochondrial complex I. | Q4R5Q4 |
A6KWL3 | LPXD_PHOV8 | UDP-3-O-acylglucosamine N-acyltransferase | Phocaeicola | MEFSAKQIAEYIQGIIVGDENATVHTFAKIEEGVPGAISFLSNPKYTHYIYDTQSTIVLVNKDFVPEQEVKATLIKVDNAYESLAKLLTLYEMSKPKKTGIDPLAYVAPTAKLGKDVYIAPFACVGDGAEIGDNTSLHPHATVGSHAKVGNNCTLYPHATIYHDCLVGNHCTLHAGCVIGADGFGFAPSPEGYEKIPQIGIAIIEDNVEIGANTCVDRATMGATIVHKGVKLDNLIQIAHNVEVGSHTVMASQVGIAGSTKVGEWCMFGGQVGLAGHIKIGDKVGIGAQAGVPGNVKSNEQILGTPAIDAKNFMKSSAVYKKLPEIYTTLNAMQKEIEELKKQLNK | Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. | A6KWL3 |
Q7VRS9 | UPP_BLOFL | UPRTase | Candidatus Blochmannia | MKIIEIRHPLVQHKLGLMRINDISTKRFRELSSELSSLLTYVATDDLEIETVIIKGWNGLVKIARIKGKKITVVPILRAGLGMMDGVLEHVPSARISMIGVYRDEITLEPIPYFHKLVSRINERMAMVLDPMLATGGTVIATVDLLKKAGCHNIKILSLVAAPEGIAALEKKHPDVELYLASIDQKLNKYGYIIPGLGDAGDKIFGTK | Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate. | Q7VRS9 |
Q7U5I2 | CHLL_PARMW | Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein | Parasynechococcus marenigrum | MTTTLTRPTDGEGSVQVHQDPGLNIQEETLVIAVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKHDSTFTLTHKMVPTVIDILEEVDFHSEELRPEDFVFTGFNGVQCVESGGPPAGTGCGGYVTGQTVKLLKEHHLLEDTDVVIFDVLGDVVCGGFAAPLQHANYCLIVTANDFDSIFAMNRIVQAIQAKAKNYKVRLGGVVANRSADTDQIDKFNERTGLRTMAHFKDVDAIRRSRLKKCTIFEMDDEDEAVQAVRSEYLRLAQNMLDKVEPLEATSLKDREIFDLLGFD | 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 binds Mg-ATP. | Q7U5I2 |
A8YXK1 | RS12_LACH4 | 30S ribosomal protein S12 | Lactobacillus | MPTINQLVRKGRHSKVTKSKSPALNYSYNSMKKESVFNPAPQMRGVATRVGTMTPKKPNSALRKYARVRLSNLIEVTAYIPGEGHNLQEHSVVLIRGGRVKDLPGVRYHIIRGALDTAGVDGRKQSRSKYGTKKD | Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit. | A8YXK1 |
Q97X94 | UPPP_SACS2 | Undecaprenyl pyrophosphate phosphatase | Saccharolobus | MNYILIGVILGIVQGISEWIPISSKTQVLIVSSTLLGLSFNVAYSFGLFMEIGTIAAAIFYFRSEISGLLKALVRMSSRREDYLLLKFLVIVTIITGLVGVPLYLFVISLPILGLPMTVLGVVLLIDGIVIYLSRKNYFPRKGLHDLKLRDIIIVGIAQGLAALPGVSRSGMTTSALILLGVKPEEAFKLSFISLIPAALGAISVTVLFSKHEVSQAVHSVSLSGLLISIVVATFVSIFFINALLRFARTNKVVLLVIILGIMAIISGILSDIAKGFY | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). | Q97X94 |
P13704 | HMCS1_CRIGR | 3-hydroxy-3-methylglutaryl coenzyme A synthase | Cricetulus | MPGSLPLNAEACWPKDVGIVALEIYFPSQYVDQAELEKYDGVDAGKYTIGLGQARMGFCTDREDINSLCLTVVQNLMERNSLSYDCIGRLEVGTETIIDKSKSVKSNLMQLFEESGNTDIEGIDTTNACYGGTAAVFNAVNWIESSSWDGRYALVVAGDIAIYATGNARPTGGVGAVALLIGPNAPLIFDRGLRGTHMQHAYDFYKPDMLSEYPIVDGKLSIQCYLSALDRCYSVYRKKIRAQWQKEGNDNDFTLNDFGFMISHSPYCKLVQKSLARMFLNDFLNDQNRDKNSIYSGLEAFGDVKLEDTYFDRDVEKAFMKASSELFNQKTKASLLVSNQNGNMYTSSVYGSLASVLAQYSPQQLAGKRIGVFSYGSGLAATLYSLKVTQDATPGSALDKVTASLCDLKSRLDSRTCVAPDVFAENMKLREDTHHLANYIPQCSIDSLFEGTWYLVRVDEKHRRTYARRPSTNDHNLGDGVGLVHSNTATEHIPSPAKKVPRLPATAAESESAVISNGEH | This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is converted by HMG-CoA reductase (HMGCR) into mevalonate, a precursor for cholesterol synthesis. | P13704 |
C5CKT1 | FABZ_VARPS | Beta-hydroxyacyl-ACP dehydratase | Variovorax | MTTTTLDIHQILKLLPHRYPFLLVDRVLDMEKGKRITALKNVTMNEPFFNGHFPHRPVMPGVLMLEAMAQAAALLSFHSLDIVPDDNTVYYFAAIDGARFKRPVEPGDQLTLEVEIERMKAGISKFKGRALVGSELACEATLMCAMRQIN | Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs. | C5CKT1 |
Q1ACE4 | NU1C_CHAVU | NADH-plastoquinone oxidoreductase subunit 1 | Chara | MSSLVRLKFNAIKLVIDFGISENIAYLISIFLPIVLLLVISVLGVLVTVWLERKISAAVQQRIGPEYAGSLGIMQAIVDGVKLLIKEDIIPAQGDRWLFSIGPVLVVTPVILSYLVVPFGKNIILSDIRLGIFFWIVISSITPLGLLIAGYASNNKYSLLGGLRAAAQSISYEIPLTLCVLSISLLSNTLSTSDIVEQQCKYGILSWNIWRQPVGFITFFIASLAECERLPFDLPEAEEELVAGYQTEYSGIKFGIFYVASYLNLLVSSLFAVVLYLGGWNFPIPTTLIFFISMYKVSLPLDSSNLLLELIIPIIHISITLAKTYLFIFFAILARWTLPRIRIDQLLDLGWKFLLPMAVGNLLLTASFQLTLFEFS | NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. | Q1ACE4 |
Q7N8P5 | PYRH_PHOLL | Uridine monophosphate kinase | Photorhabdus | MATNAKPVYQRILLKLSGEALQGAEGFGIDASVLDRMAQEVKELVELGVEVGVVIGGGNLFRGAGLAEAGMNRVVGDHMGMLATVMNGLAMRDALHRAYVNARLMSAIPLNGVCDNYSWAEAISLLRHGRVVIFSAGTGNPFFTTDSAACLRGIEIEADVVLKATKVDGVYSADPAKDSEAVLFDKLSYQQVLERELKVMDLAAFTLARDHSLPIRVFNMNKPGALRRVVMGENEGTLIFHE | Catalyzes the reversible phosphorylation of UMP to UDP. | Q7N8P5 |
A4IKI6 | RECX_GEOTN | Regulatory protein RecX | Geobacillus | MGTIVDITVTKENAERFWIVIHRDNESALKLTVDQDVLLKFRLKKGMIIDDALLRDIVYADGIKKAYQQALYFLAHRMRSEQEIVEHLRKKGVVDPVIEEVLEKLRAERYVDDEAFAAAYVRTQKNTSTKGPRLIQAELERLGVPASVIEQSLVEYSFNEQVIAARSLYEKAKKQRRAESARAFLERVKQQLMRKGFSHEVIAIVLADGSGHTEEEEREALHVQAEKIRRRYAHHPRPLYEQKMRQALYRKGFSLALIDEWLRRQDDDG | Modulates RecA activity. | A4IKI6 |
Q493P6 | LPXC_BLOPB | UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase | Candidatus Blochmannia | MIKQRTLKRVVQTTGVGLHTGKKVTLTLRPTSANTGIIYRRTDLYPPVDLQVNVKSVGNTVLCTCLINEYGVQIFTVEHLSAAQAGLGIDNIIIELNAPEVPIMDGSASPFVCLLLDAGIEELNSAKKFLRLKQTVRVEDGEKWAELRPFNGFTLDFTIDFNHPAINVDTQHCFFNFSSASFVHNISRARTFGFMRDIKDLQSRGFALGGSFNSAIIIDDYRVLNEDGLRFDDEFVRHKMLDAIGDLFMCGHNLIGSFIAFKSGHTLNNKLLKTVLSCQEAWELATFSNASDLPLVF | 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. | Q493P6 |
A9ULE9 | DJC22_XENTR | DnaJ homolog subfamily C member 22 | Silurana | MGKSLLAAYGLWALGGPLGLYHIYLGRDSHALLWMLTLGGFGMGWMWDFWKIPIHVYKYNRQERKNIEVKEGEPPASPIRFIGQVATGIYFGIVAAIGLSFLSSFHMVVLPLAVALGVHLVATVGEQTSDLKNTLIAAFLTSPIFYGRAVSMIPISLTASITSQKHMRYRLQQEKQEKLSLRLYRIGLVYLAFTGPLAYSALLNTSLTVSYVAGSIGSMLEWLSIFPSISALVERLLLLPYRVWAVFSGGGVFRDHYFKEWEKIYEFVATFQSEKEEMACKVLGVNFKSTMEEINRKYRELVKIWHPDHNRHRLEEAQEHFLEIQAAYETLMRLRKSKTL | May function as a co-chaperone. | A9ULE9 |
B0U6W4 | RPOZ_XYLFM | Transcriptase subunit omega | Xylella | MARITVEDCLEVVNNRFELVMMASKRARQLANGVPPLIENNSEDKPTVLALREIAARKINSKMIDEIEKAERERTEREAMEWAAAEVVADEDISKSDD | Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits. | B0U6W4 |
O13688 | NSE6_SCHPO | Core protein 1 | Schizosaccharomyces | MNASNNISKFPDLDNSSKLIDHILDSDDSEELDELPDISSLVPSARAQSRKQYLKNDSSNSSTYRWNIDLLSSTATIDDSVAKRRKLAVQNLLQYDSTQTFQTGDEIDELIGKSVGSNVLNVLRSNPIYDDDLRYEYCSNSKARVPDWNTLKAECLKDNDLEFNEGIIPTTFGDLLSAKLVPLDIALSICSLQFFRSLGDTTCSEWIANLEKIFYSYKSSSNNLNQIVRFIFETTADMIGIDLAKRQVPIQLERTSASENLKSNLKIKVINFLKCCGTLYRFSDDTVRFEMIQDACRILIDNQVGSFCKWQFSQFMELPISLNPDFLISNIHKVSESPRVWVTILSSLSRSCQKFRKKIAFTLFVGKQSKNDDSDFSSLCQRLDEISASCNNDYTTLLYQIRTFGYAVDEKHFKTNERLECLLEKLRKIDLTISGSTDHLLLSRCEVKDCIHRLFMVLYYLNTNSAPELERIIESDLPNNNKQKDRYFKDKTSNLSMKENKSFSAKKVKKGKKKNKRQAYKR | Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks. May prevent formation of excessive Holliday junctions or assist in their resolution. | O13688 |
Q11HS3 | KAD_CHESB | Adenylate monophosphate kinase | unclassified Chelativorans | MRLILLGPPGAGKGTQAQILVEKLHIPQLSTGDMLRAAVKAETEIGKKAKAVMDAGELVSDAIVNAIVAERIDQPDCANGFILDGYPRTLAQADAVEAMLGERGLKLDAVIELVVDDKALVGRIMKRAEDAQAAGQPVRRDDNPEVFEERLREYYKKTAPLVGYYYAKGLLKGVDGMASIDEVTRQIEGILAKA | 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. | Q11HS3 |
A3NKP8 | BETB_BURP6 | Betaine aldehyde dehydrogenase | pseudomallei group | MSVYGLQRLYIAGAHADATSGKTFDTFDPATGELLARVQQASADDVDRAVASAREGQREWAAMTAMQRSRILRRAVELLRERNNALAELEMRDTGKPIAETRAVDIVTGADVIEYYAGLATAIEGLQVPLRPESFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLSALKLAEIYTEAGVPAGVFNVVQGDGSVGALLSAHPGIAKVSFTGGVETGKKVMSLAGASSLKEVTMELGGKSPLIVFDDADLDRAADIAVTANFFSAGQVCTNGTRVFVQQAVKDAFVERVLARVARIRAGKPSDPDTNFGPLASAAQLDKVLGYIDSGKAEGAKLLAGGARLVNDHFASGQYVAPTVFGDCRDDMRIVREEIFGPVMSILSFETEDEAIARANATDYGLAAGVVTENLSRAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGITTLEHYTRIKSVQVELGRYQPVF | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the irreversible oxidation of betaine aldehyde to the corresponding acid. | A3NKP8 |
Q0ALW2 | METK_MARMM | Methionine adenosyltransferase | Maricaulis | MSRSSYIFTSESVSEGHPDKVCDRISDTIVDLFLGKDPEARVACETLTTTNQIVLAGEVRCAAPIDDAEIEAAAREAVRDIGYEQDGFHWETATLQNFLHEQSVHIAQGVDASGDKDEGAGDQGIMFGYASDETPQLMPAPITYSHQILKRMAELRKSGARPEFEPDAKSQVTMRYENGVPAGVTSVVVSTQHKDGLTQDDIRELVRPVVQDVLPEGWFPPEEEFYVNPTGTFVIGGPDGDAGLTGRKIIVDTYGGAAPHGGGAFSGKDPTKVDRSAAYACRWLAKNVVAAELAKRCTIQVSYAIGVSKPLSLYVDLHGTGRVDEAKLEDALRQLADLSPRGIRTRLQLNKPIYARTAAYGHFGRTPTEDGGFSWERTDLADELRSLL | Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. | Q0ALW2 |
A8HDK4 | 3L21_TROCA | Long neurotoxin 1 | Tropidechis | MKTLLLTLVVVTIVCLDLGNSFSCYKTPHVKSEPCAPGQNLCYTKTWCDAFCFSRGRVIELGCAATCPPAEPKKDISCCSTDNCNPHPAHQSR | Binds with high affinity to muscular (alpha-1/CHRNA1) and neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR) and inhibits acetylcholine from binding to the receptor, thereby impairing neuromuscular and neuronal transmission. | A8HDK4 |
B0BQK6 | RLMN_ACTPJ | tRNA m2A37 methyltransferase | Actinobacillus | MSEQTQTCASEIQATNVAVQHPKSEKINLMNLTRQEMRELFAEMGEKPFRADQLMKWIYHFGEDNFDNMSNINKVLREKLKQIAEIKAPEVSVEQRSSDGTIKWAMQVGDQQIETVYIPEDDRATLCVSSQVGCALACKFCSTAQQGFNRNLTVSEIIGQVWRASKIIGNFGVTGVRPITNVVMMGMGEPLLNLNNVIPAMEIMLDDFAYGLSKRRVTLSTAGVVPALDIMREKIDVALAISLHAPNDELRDEIMPINKKYNIKMLMDSVHKYLEVSNANHGKVTIEYVLLDHVNDGTEHAHQLAEVLKNTPCKINLIPWNPFPEAPYGKSSNSRVDRFQKTLMEYGFTVIVRKTRGDDIDAACGQLAGDVIDRTKRTMEKRKFGKGIAVQNH | Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity. | B0BQK6 |
Q5E249 | DCUP_ALIF1 | Uroporphyrinogen decarboxylase | Aliivibrio | MTELKNDRYLRALLKQPVDYTPVWMMRQAGRYLPEYKATRAEAGDFMSLCKNAELASEVTLQPLRRFPLDAAILFSDILTIPDAMGLGLYFETGEGPKFERPITCKADVDKIGLPDPEGELQYVMNAVRQIRKDLKGEVPLIGFSGSPWTLATYMVEGGSSKAFTKIKKMMYAEPATLHLLLDKLADSVIEYLNAQIKAGAQSVMVFDTWGGVLTPRDYNEFSLRYMHKIVDGLIRENEGRRVPVTLFTKNGGMWLESIAATGCDAVGLDWTINIADAKARIGDKVALQGNMDPSILYAQPERIRQEVGTILEGFGDAGTGHVFNLGHGIHLDVPPENAGVFVDAVHDLSKPYHK | Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. | Q5E249 |
P61755 | CCR5_LOPAT | C-C chemokine receptor type 5 | Lophocebus | MDYQVSSPTYDIDYYTSEPCQKINVKQIAARLLPPLYSLVFIFGFVGNILVVLILINCKRLKSMTDIYLLNLAISDLLFLLTVPFWAHYAAAQWDFGNTMCQLLTGLYFIGFFSGIFFIILLTIDRYLAIVHAVFALKARTVTFGVVTSVITWVVAVFASLPGIIFTRSQREGLHYTCSSHFPYSQYQFWKNFQTLKIVILGLVLPLLVMVICYSGILKTLLRCRNEKKRHRAVRLIFTIMIVYFLFWAPYNIVLLLNTFQEFFGLNNCSSSNRLDQAMQVTETLGMTHCCINPIIYAFVGEKFRNYLLVFFQKHIAKRFCKCCSIFQQEAPERASSVYTRSTGEQEISVGL | Receptor for a number of inflammatory CC-chemokines including CCL3/MIP-1-alpha, CCL4/MIP-1-beta and RANTES and subsequently transduces a signal by increasing the intracellular calcium ion level. May play a role in the control of granulocytic lineage proliferation or differentiation. Participates in T-lymphocyte migration to the infection site by acting as a chemotactic receptor. | P61755 |
Q7N3N2 | PROQ_PHOLL | RNA chaperone ProQ | Photorhabdus | MENQPKLNSSKEIIAFLAERFPLCFVAEGEARPLKIGIFQDIVERIQDEECLSKTQLRSALRLYTSSWRYLYGVKEGAQRVDLDGNSCGELEAEHIEHALQQLTEAKARVQAQRAEQRAKKREAENVAAGEKNERPTAKKPAPRRRANNTEGEKRQPPRPQKRPQQARKPVAKPVQAKPIQAAPIQIVDVSSLKIGQEIKVRVGKSSVDASVLEVAKDGVRVQLPSGLAMIVRAEHLQF | RNA chaperone with significant RNA binding, RNA strand exchange and RNA duplexing activities. May regulate ProP activity through an RNA-based, post-transcriptional mechanism. | Q7N3N2 |
Q8Z8W3 | PANE_SALTI | Ketopantoate reductase | Salmonella | MKITVLGCGALGQLWLSALCKHGHDVQGWLRVPQPYCSVNLIDTDGSFFNESLTANDPDFLAKSELLLVTLKAWQVSDAVRTLASTLPVTSPILLIHNGMGTIEELQSIQQPMLMGAITHAARRDGNIIIHVANGTTHIGPAREQDGDYSYLAEILQGVLPDVAWHNNIRAEMWRKLAVNCVINPLTALWNCPNGELRHHTDEINAICEEVAAVIEREGYHTSADDLCYYVEQVIDSTAENISSMLQDVRAMRHTEIDYITGYLLKRARVHGLAVPENSRLFEMVKRKESEYERSGTGMPRPW | Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid. | Q8Z8W3 |
Q9CNL2 | G6PI_PASMU | Phosphohexose isomerase | Pasteurella | MKNINPTTTNAWKALQQHHKTQSAVTIQQLFAQEKDRFTDYSLSFNNEVLVDFSKNNVTKETLGLLRQLAQECALSEAVDAMFSGAKINKTEDRAVLHTALRNRSNSPVLVDGKDVMPEVNAVLAKMKDFCHRVISGEWKGYTGKAITDVVNIGIGGSDLGPYMVTEALRPYKNHLNLHFVSNVDGTHIAETLKKVNPETTLFLVASKTFTTQETMTNAHSARNWFLATAKDESHVAKHFAALSTNSKAVAEFGIDTNNMFEFWDWVGGRYSLWSAIGLSIALSIGFEHFEALLAGAHEMDKHFRTAPIEQNIPTTLALIGLWNTNFLGAQTEAILPYDQYLHRFAAYFQQGNMESNGKYVDRNGEVIDNYQTGPIIWGEPGTNGQHAFYQLIHQGTTLIPCDFIAPAQTHNPLADHHEKLLSNFFAQTEALAFGKTKEEVEAEFVKAGKSLDEVKEVVPFKVFTGNKPTNSILVQKITPFTLGALIAMYEHKIFVQGVMFNIYSFDQWGVELGKQLANRILPELANRETITTHDSSTNGLINQYKQWR | Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate. | Q9CNL2 |
Q7W4B6 | DDL_BORPA | D-alanylalanine synthetase | Bordetella | MSKQFGKVGVLYGGRSAEREVSLMSGKGVHEALLSAGVDAHLFDTGERSLADLAAAGFERVFIALHGRYGEDGTLQGALELLGIPYTGSGPLASSLSMDKIMTKRVWLQHGLPTPAFEVLGGSTELRLVPDRLGLPLILKPPHEGSTVGITKVAGYSDMKAAYELAARFDAEVLAEQFITGRELTVAVLGSGAAARALPVIEIVAPGGNYDYEHKYFSDDTQYFCPADLPADVAADVAAVAERAYAALGCEGWGRVDFILDRENRPWLLEMNTSPGMTGHSLVPMAARAVGMSYADLCVAILAKAACKVRSPARQD | Cell wall formation. | Q7W4B6 |
Q8NGT1 | OR2K2_HUMAN | Olfactory receptor OR9-17 | Homo | MQGENFTIWSIFFLEGFSQYPGLEVVLFVFSLVMYLTTLLGNSTLILITILDSRLKTPMYLFLGNLSFMDICYTSASVPTLLVNLLSSQKTIIFSGCAVQMYLSLAMGSTECVLLAVMAYDRYVAICNPLRYSIIMNRCVCARMATVSWVTGCLTALLETSFALQIPLCGNLIDHFTCEILAVLKLACTSSLLMNTIMLVVSILLLPIPMLLVCISYIFILSTILRITSAEGRNKAFSTCGAHLTVVILYYGAALSMYLKPSSSNAQKIDKIISLLYGVLTPMLNPIIYSLRNKEVKDAMKKLLGKITLHQTHEHL | Odorant receptor. | Q8NGT1 |
Q3SRA3 | MSCL_NITWN | Large-conductance mechanosensitive channel | Nitrobacter | MWKEFREFAMKGNVVDLAVGVIIGAAFGGIVSSMVADIIMPIVGAVTGGLDFSNYFLPLSESVNASNLSDAKKQGAVLAWGNFLTLTLNFLIVAFVLFMVIKGMNRLKRKDEAASAEPPKPTREEELLTEIRDLLKAKV | Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell. | Q3SRA3 |
Q6FAT7 | PYRG_ACIAD | UTP--ammonia ligase | Acinetobacter | MTHFIFVTGGVVSSLGKGISAASVAALLEARGLKVTMVKMDPYINVDPGTMSPFQHGEVFVTEDGAETDLDLGYYERFLRRAKMTKLNNFTSGRVYQDVLNKERRGDYLGGTVQVIPHITDNIKERVLAAGEGYDVAIVEIGGTVGDIESLPFMESVRQLMVELGHKRTMLMHLTLLPYIRSAAELKTKPTQHSVKELLSIGIQPDILICRTEHDVDADTKRKIALFTNVEARAVVVCKDAKTIYQIPRNFYEQKVDDLICERFGYNDLPQADLSDWDQVCEALFNPEYIVRVAMVGKYVELPDAYKSVNEALLHAGIQNRVKVQIDYVDAETLETQDISILSTADAILVPGGFGERGTEGKMLAIKYAREQGIPFLGICLGMQLAVIEYARNVAGLAEATSTEFNRSTKFPIIGLITEWLDERGELQQRSVESDLGGTMRLGAQKSELVEGTKTRQVYGKAEIVERHRHRYEMNDRFIEPIEKAGMKISGYSTAQHLVETVEIPEHPWFIAVQFHPEFTSSPRDGHPLFASFIDAAKKQHLKTK | Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. | Q6FAT7 |
Q1LT89 | NUOA_BAUCH | NUO1 | Candidatus Baumannia | MTAEISAQYWAFAIFIISAIILCVLILTLSFLLGERKHIKVYSRDLPFESGINPVGNPKLHLSAKFYLIAIFFVLFDIEAFYLYAWSSVIREAGWLGFYEAIIFVSVLLSGLVYLVRIGALKWTPNHS | 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 translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. | Q1LT89 |
P49657 | MNB_DROME | Serine/threonine-protein kinase minibrain | Sophophora | MYRLEDTNSGGVMDKNKQKLSAYGSSGGSVDAAQGSGSGGGRQRHAPLYGRFVDAEDLPATHRDVMHHHSSPSSSSEVRAMQARIPNHFREPASGPLRKLSVDLIKTYKHINEVYYAKKKRRAQQTQGDDDSSNKKERKLYNDGYDDDNHDYIIKNGEKFLDRYEIDSLIGKGSFGQVVKAYDHEEQCHVAIKIIKNKKPFLNQAQIEVKLLEMMNRADAENKYYIVKLKRHFMWRNHLCLVFELLSYNLYDLLRNTNFRGVSLNLTRKFAQQLCTALLFLSTPELNIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYHYIQSRFYRSPEVLLGIQYDLAIDMWSLGCILVEMHTGEPLFSGCNEVDQMNKIVEVLGMPPKYLLDQAHKTRKFFDKIVADGSYVLKKNQNGRKYKPPGSRKLHDILGVETGGPGGRRLDEPGHSVSDYLKFKDLILRMLDFDPKTRVTPYYALQHNFFKRTADEATNTSGAGATANAGAGGSGSSGAGGSSGGGVGGGLGASNSSSGAVSSSSAAAPTAATAAATAAGSSGSGSSVGGGSSAAQQQQAMPLPLPLPLPLPPLAGPGGASDGQCHGLLMHSVAANAMNNFSALSLQSNAHPPPSLANSHHSTNSLGSLNHISPGSTGCHNNNSNSSNNNTRHSRLYGSNMVNMVGHHNSGSSNNHNSISYPHAMECDPPQMPPPPPNGHGRMRVPAIMQLQPNSYAPNSVPYYGNMSSSSVAAAAAAAAAAASHLMMTDSSVISASAAGGGQGGGNPGQNPVTPSAAAFLFPSQPAGTLYGTALGSLSDLPLPMPLPMSVPLQLPPSSSSSVSSGSASVGSGGVGVGVVGQRRHITGPAAQVGISQSVGSGSSGSATGASSSDASSSSPMVGVCVQQNPVVIH | Role in the specific control of proper proliferation of optic lobe neuronal progeny. | P49657 |
A7IC03 | PNP_XANP2 | Polynucleotide phosphorylase | Xanthobacter | MFDIHREELDWGGRTLTLETGKMARQADGSVLATYGDTKVLATVVSAREPKPGQDFFPLTVNYQEKTYAAGRIPGGYFKREGRPSEKETLVSRLIDRPIRPLFPEGYKCDTQVVITVLAHDLENDPDVVAMVAASAALTLSGVPFMGPVGAARVGFIDNEYVLNPTVDEVKESALELVVAGTGDAVLMVESEAKELPEEIMLGAVMFGHRHFQPVIEAIIKLAEKAAKEPRNFQPADVSEVESKVREIAEADLRAAYKIKQKQDRYAAVGAAKSKVKKYYEELALDGTKVPTAQVVSDVLKALEAKIVRWNILDDGIRIDGRDVYTVRPIVSEVGILPRAHGSALFTRGETQALVVATLGTGEDEQFIDSLEGTYKEHFLLHYNFPPFSVGETGRMGSPGRREIGHGKLAWRAIHPMLPAKHEFPYTLRVVSEILESNGSSSMATVCGTSLALMDAGVPLRRPVAGIAMGLILEGEKFAVLSDILGDEDHLGDMDFKVAGTEQGVTSLQMDIKIAGITEEIMKVALTQAKDGRVHILGEMAKALTTARAELGEHAPRIEVMKIAVDKIREVIGSGGKVIREIVEKTGAKINIEDDGTIKIASASGDAIKAAINWIKSIASEPEVGQIYEGTVVKVVDFGAFVNFFGSKDGLVHVSQMANERVAKPSDVVKEGDKVKVKLMGFDERGKTRLSMKVVDQTTGEDLEAKAKAERDAARAAAPAATGDEAGAAE | Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. | A7IC03 |
Q701N9 | MYG_TETNG | Myoglobin | Tetraodon | MGDFDMVLKFWGPVEADYSAHGGMVLTRLFTENPETQQLFPKFVGIAQSELAGNAAVSAHGATVLKKLGELLKAKGNHAAILQPLANSHATKHKIPIKNFKLIAEVIGKVMAEKAGLDTAGQQALRNIMATIIADIDATYKELGFS | Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. | Q701N9 |
Q9RRU5 | KHSE_DEIRA | Homoserine kinase | Deinococcus | MSSPARPFTVRAPASSANLGPGFDSLGLSVPLYTTLRVTPQDKAEVVPLGTELADTPADESNYVYRAMTLAAKRAGRTLPPARVEIETEVPLARGLGSSAAALVAGVVAGNELLGRPLDDETVLDVTAREEGHPDNVAPALFGGIVVATLDKLGTHYVRLDPPAHLGVTVLVPDFELSTSKARAVLPREYSRADTVHALSHAALLAAALAQGRLDLLRHAMQDYVHQVWRAPLVPGLSDILEHAHEYGALGAALSGAGPTVLCFHDQRGSTATLHHYLHDVMTKNGLSGRVMDFPIDAAGTVVEHAK | Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate. | Q9RRU5 |
Q0BHN2 | URED_BURCM | Urease accessory protein UreD | Burkholderia cepacia complex | MSAPDSHASLSRPSVAKSWRGRLELGFERHGARTTLVHRLHDGPLRVQRPLYPEGDAICHAVIVHPPGGVAGGDQLDIGIALGDGTHAVLTTPGATKWYKSNGLDATQRIGITVGAHAKLDWLPQNNLFFDAAHAALDFTVTLGAGASAIGWDATQLGRQAAGETWSAGRIASRSALVDADGRPLWTERALLDAHDPLRGALQGLAGFPVYGTLWAAGAACDAALAEALAARMPFDDTLRAGATCVTPGVVLVRALSTSMEALQRHFADCWLYLRPIVHGVDARPLRLWQT | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | Q0BHN2 |
P34711 | UNC17_CAEEL | Uncoordinated protein 17 | Caenorhabditis | MGFNVPVINRDSEILKADAKKWLEQQDNQKKCVLVIVSIALLLDNMLYMVIVPIIPKYLRDIHNYQVTFEGYHNETSQLANGTYLVREVGGRINFLDEELELGWLFASKALLQIFVNPFSGYIIDRVGYEIPMILGLCTMFFSTAIFALGKSYGVLLFARSLQGFGSAFADTSGLAMIADRFTEENERSAALGIALAFISFGCLVAPPFGSVLYSLAGKPVPFLILSFVCLADAIAVFMVINPHRRGTDSHGEKVQGTPMWRLFMDPFIACCSGALIMANVSLAFLEPTITTWMSEMMPDTPGWLVGVIWLPPFFPHVLGVYVTVKMLRAFPHHTWAIAMVGLAMEGIACFAIPYTTSVMQLVIPLSFVCFGIALIDTSLLPMLGHLVDTRHVSVYGSVYAIADISYSLAYAFGPIIAGWIVTNWGFTALNIIIFATNVTYAPVLFLLRKVHSYDTLGAKGDTAEMTQLNSSAPAGGYNGKPEATTAESYQGWEDQQSYQNQAQIPNHAVSFQDSRPQAEFPAGYDPLNPQW | Involved in acetylcholine transport into synaptic vesicles. | P34711 |
P61242 | YCF2_SOLLC | Protein Ycf2 | Solanum subgen. Lycopersicon | MRGHQFKSWIFELREILREIKNSHHFLDSWTQFNSVGSFIHIFFHQERFLKLFDPRIWSILLSRNSQGSPSNRYFTIKGVILFVVAVLIYRINNRNMVERKNLYLIGLLPIPMNSIGPRNDTLEESVGSSNINRLIVSLLYLPKGKKISESCFLNPKESTWVLPITKKCSMPESNWGSRWWRNWIGKKRDSSCKISNETVAGIEILFKEKDLKYLEFLFVYYMDDPIRKDHDWELFDRLSLRKSRNRINLNSGPLFEILVKHWISYLMSAFREKIPIEVEGFFKQQGAGSTIQSNDIEHVSHLFSRNKWAISLQNCAQFHMWQFRQDLFVSWGKNPPESDFLRNVSRENWIWLDNVWLVNKDRFFSKVQNVSSNIQYDSTRSSFVQVTDSSQLKGSSDQSRDHLDSISNEDSEYHTLINQREIQQRKERSILWDPSFLQTERKEIESGRFPKCLSGYSSMSRLFTEREKQMINHLFPEEIEEFLGNPTRSVRSFFSDRWSELHLGSNPTERSTRDQKLLKKQQDLSFVPSRRSEKKEMVNIFKIITYLQNTVSIHPISSDPGCDMVPKDEPDMDSSNKISFLNKNPFFDLFHLFHDRNRGGYTLHYDFASEERFQEMADLFTLSITEPDLVYHKGFAFSIDSCGLDQKQFLNEARDESKKKSLLVLPPIFYEENESFSRRIRKKWVRISCGNDLEDPKPKIVVFASNNIMEAVTQYRLIRNLIQIQYSTYGYIRNVLNRFFLMNRSDRNFEYGIQRDQIGKDTLNHRTIMKYTINQYLSNLKKSQKKWFEPLILISRTERSMNRDPDAYRYKWSNGSKSFQEHLEQSVSKQKSRFQVVFDRLRINQYSIDWSEVIDKKDLSKSLRFFLSKSLLFLSKLLLFLSNSLPFFCVSFGNIPIHRSEIYIYEELKGPNDQLCNQLLESIGLQIVHLKKLKPFLLDDHDTSQKSKFLINGGTISPFLFNKIPKWMIDSFHTRNNRRKSFDNPDSYFSMIFHDQDNWLNPVKPFHRSSLISSFYKANRLRFLNNPHHFCFYWNTRFPFSVEKARINNSDFTYGQFLNILFIRNKIFSLCVGKKKHAFWGRDTISPIESQVSNIFIPNDFPQSGDETYNLYKSFHFPSRSDPFVRRAIYSIADISGTPLTEGQIVNFERTYCQPLSDMNLSDSEGKNLHQYLNFNSNMGLIHTPCSEKDLSSEKRKKWSLCLKKCVEKGQTYRTFQRDSAFSTLSKWNLFQTYMPWFLTSTGYKYLNLIFLDTFSDLLPILSSSQKFVSIFPDIMHGSGISWRILQKKLCLPQWNLISEISSKCLHNLLLSEEMIHRNNESPLISTHLRSPNAREFLYSILFLLLVAGYLVRTHLLFVSRASSELQTEFERVKSLMTPSSMIELRKLLDRYPTSEPNSFWLKNLFLVALEQLGDSLEEIRGSASGGNMLGPAYGVKSIRSKKKDWNINLIEIIDLIPNPINRITFSRNTRHLSHTSKEIYSLIRKRKNVNGDWIDEKIESWVANSDSIDDEEREFLVQFSTLTTENRIDQILLSLTHSDHLSKNDSGYQMIEQPGAIYLRYLVDIHKKHLMNYEFNPSCLAERRIFLAHYQTITYSQTSCGENSFHFPSHGKPFSLRLALSPSRGILVIGSIGTGRSYLVKYLATNSYVPFITVFLNKFLDNKSKGFLLDEIDIDDSDDIDDSDNLDASDDIDRDLDTELELLTRMNGLTVDMMPEIDRFYITLQFELAKAMSPCIIWIPNIHDLDVNESNDLSLGLLVNHLSRDCERCSTRNILVIASTHIPQKVDPALIAPNKLNTCIKIRRLLIPQQRKHFFTLSYTRGFHLEKKMFHTNGFGSITMGSNARDLVALTNEVLSISITQKKSIIDTNTIRSALHRQTWDLRSQVRSVQDHGILFYQIGRAVAQNVLLSNCPIDPISIYMKKKSCNEGDSYLYKWYFELGTSMKRLTILLYLLSCSAGSVAQDLWSLSVPDEKNGITSYGLVENDSDLVHGLLEVEGALVGSSRTEKDCSQFDNDRVTLLLRPEPRNPLDMMQKGSWSILDQRFLYEKYESEFEEGEGEGALDPQEDLFNHIVWAPRIWRPWGFLFDCIERPNELGFPYWSRSFRGKRIIYDEEDELQENDSGFLQSGTMQYQTRDRSQGLFRISQFIWDPADPLFFLFKDQPPGSVFSHRELFADEEMSKGLLTSQTDPPTSLYKRWFIKNTQEKHFELLINRQRWLRTNSSLSNGSFRSNTLSESYQYLSNLFLSNGTLLDQMPKTLLRKRWLFPDEMKIGFM | Probable ATPase of unknown function. Its presence in a non-photosynthetic plant (Epifagus virginiana) and experiments in tobacco indicate that it has an essential function which is probably not related to photosynthesis. | P61242 |
Q8KCT7 | SYDND_CHLTE | Non-discriminating aspartyl-tRNA synthetase | Chlorobaculum | MSKEPTTADGLQNRFRTHYCGRLNRKSEGELVRIAGWVHRIRDHGGLIFIDLRDHTGICQLVVLPENESQFKLAETLHSESVISAEGKVVLRSDETVNPRLASGAIEVVVSSIQIESNADPLPFPVADDMPTSEELRLKYRFLDLRREKLHENIIFRSKLTAAVRKYLTDLDFIEIQTPILTSSSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLLMVAGFPRYFQIAPCFRDEDARADRSPGEFYQIDIEMSFIEQDDLFVILEGMFKHLVENMSHKRITQFPFPRISYKDVMNRYGSDKPDLRIPLEIQDVTELFVNSGFKVFASNTAEGSCVKAMVLKGMGNESRLFYDKAEKRARELGSAGLAYIQFKEEGPKGPVVKFLSEAEMNALKERLGIVTGDVVFFGAGKWEKTCKIMGGMRNYFADLFPLDKDELSFCWIVDFPMFEYNEEDKKIDFSHNPFSMPQGEMEALESKFPLDILAYQYDIVCNGIELSSGAIRNHRPDIMYKAFEIAGYSKEEVDARFGHMIEAFKHGAPPHGGIAPGLDRLVMILRDEQNIREVIAFPMNQSAQDLMMAAPSEVTAQQLKELCIRIELPEEEK | Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn). | Q8KCT7 |
Q31LW2 | DAPF_SYNE7 | PLP-independent amino acid racemase | Synechococcus | MSLQFAKYHGLGNDFILVDNRESGEPRLTPEQAVQVCDRNFGVGADGVIFALPGSGDSDYVMRIFNSDGSEPEMCGNGIRCLAKFLSELDGGAQSRYRIATGAGLIVPTLTETGLVTVDMGPAYLKPVEIPTTLTGTGDRVVEADLEVGDRPWKVTTVSMGNPHCITFVEDVAAVPLAEIGPLFEHHPVFPQRTNTEFVEVVRPDYLKMRVWERGAGATLACGTGACATLVAAVLTGRSDRQATVELPGGPLQIEWREDGHLFMTGPAVKVFSGSMELAA | Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan. | Q31LW2 |
P60608 | EFC2_HUMAN | Truncated transmembrane protein | Homo | MNSPCDRLQQFIQVLLEESWSFPSFANTLHWPENLLSYIDELVWQGSLQNFHQHEVRFDKPPLRLPLTGFSSLTENWSSRQAVSSRLVATAASPPAGCQAPIAFLGLKFSSLGPARKNPALCFLYDQSNSKCNTSWVKENVGCPWHWCNIHEALIRTEKGSDPMFYVNTSTGGRDGFNGFNLQISDPWDPRWASGVDGGLYEHKTFMYPVAKIRIARTLKTTVTGLSDLASSIQSAEKELTSQLQPAADQAKSSRFSWLTLISEGAQLLQSTGVQNLSHCFLCAALRRPPLVAVPLPTPFNYTINSSTPIPPVPKGQVPLFSDPIRHKFPFCYSTPNASWCNQTRMLTSTPAPPRGYFWCNSTLTKVLNSTGNHTLCLPISLIPGLTLYSQDELSHLLAWTEPRPQNKSKWAIFLPLVLGISLASSLVASGLGKGALTHSIQTSQDLSTHLQLAIEASAESLDSLQRQITTVAQVAAQNRQALDLLMAEKGRTCLFLQEECCYYLNESGVVENSLQTLKKKKSSKRS | Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution. This endogenous envelope protein has lost its original fusogenic properties. | P60608 |
B4ST23 | QUEC_STRM5 | Queuosine biosynthesis protein QueC | Stenotrophomonas maltophilia group | MKKAVVLLSGGMDSAAVIAMAQEQGFAVHALSVRYGQRHTSELDAAARVAKAQGVIAHKTVDVDLRSIGGSALTDDIDVPEAGGAGIPVTYVPARNTIMLSLALGWAEVLGANDIFCGVNAVDYSGYPDCRPEFVAAFQALANLATKSGVEGAGIKVHAPLQFLSKGQIVSEGVRLGVDFGLTVSCYNADANGAACSHCDACRLRAQGFTEAGVADPTLYA | Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). | B4ST23 |
Q640N3 | RHG30_MOUSE | Rho-type GTPase-activating protein 30 | Mus | MKSRQKGKKKGSSKERVFGCDLREHLQHSGQEVPQVLRSCAEFVQEYGVVDGIYRLSGVSSNIQKLRQEFETERKPDLRRDVYLQDIHCVSSLCKAYFRELPDPLLTYRLYDKFAEAVAVQLEPERLVKILEVLQELPIQNYRTLEFLMRHLVHMASFSAQTNMHARNLAIVWAPNLLRSKDIEASGFNGTAAFMEVRVQSIVVEFILTHVDQLFRGDSLSAGVDLESGWKSLPGARASGSSEDLMPTSLPYHLPSILQAGDGPPQIRPYHTIIEIAEHKRKGSLKVRKWRSIFNLGRSGHETKRKLPLRVEDREEKSSKGTLRPAKSMDSLSAAAGASDEPEGLVGSSSSQPSSLMPESLESNSMEGEQEPEAEAPGSANSEPGTPRAGRSAVRALGSSRAERCAGVHISDPYNVNLPLHITSILSVPPNIISNVSLVRLTRGLECPALQPRPSPALGPGPPGSVGPLASDEKSEARSVPGPLDDSSPAAMTPALEDSLSQEVQDSFSFLEDLSSSEPEWVGVEEREVAKAEAAGAAGAAAFSLGEDDPGMGYLEELLRVGPQVEEFSVEPPLDDLSLDDTQYVLAPNCCSLDSAVSTPDVEEDYGEEVFLSAYDDLSPLLGPKPINWEGVGSLEEEAAGCGKQPPTQDEEEQACSETRQEKEAKPRSTSDNREEAEATPETEMEAGKADAEGGEAERSQKVMDSFKEGSREELEAKEENSEGREVESIKETKDVEKIIGEPGKDEEREIGREEGAEKGDDTPVDSDMDPEHVFQEDLVLEESWEVVHKHEAEKGRESETKELRRKSDLKSREDQGHSEDSGSPEEGDDRKEGVFSKEQKSIDVETEVMRGVGDHLEEGALSEGPGVELLRVDSTEEINEQTSEMKQAPLQPSEPEGMEAEGQLNPETCDLYSCPCGSAGGVGMRLASTLVQVRQVRSVPVVPPKPQFAKMPSAMCSKIHVAPASPCPRPGRLDGTPGEKAWGSRASWRNGGSLSFDAAVALARERQRTESQGVLRTQTCTGGGDYSLSSRTPPCSMILAHSSRPLSCLERPPEGTEGSEPRSRLSLPPRELHPVVPLVAPQRQTYAFETQTNHGKDEGV | GTPase-activating protein (GAP) for RAC1 and RHOA, but not for CDC42. | Q640N3 |
A5EKL6 | ERA_BRASB | GTPase Era | unclassified Bradyrhizobium | MTAEQHAGPGAETRCGFVALIGAPNVGKSTLVNALVGSKVTIVSRKVQTTRALIRGIVIEGTSQIILVDTPGIFSPKRRLDRAMVTTAWSGAHDADLVCVLLDAKKGLDDEAQAIIDKAAAVAHQKILVVNKVDLVPREKLLALVAAANEKLPFARTFMISALSGDGVDDLKQALAAMVPPGPFHYPEDQMSDAPMRHLAAEITREKIYSHLHQELPYQSTVETDSWTERKDGSIRIEQTIFVERDSQRKIVLGKGGATIKSIGAQSRKEIAEITGVPVHLFLFVKVRENWGDDPDRYREMGLEFPRE | An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism. | A5EKL6 |
A1STW0 | PLSX_PSYIN | Phosphate-acyl-ACP acyltransferase | Psychromonas | MSKLTIAIDAMGGDVGPHIPILAALKSLQLHPNLHIIIVGNRTQLLPVLKKYQLSEHARLSLIHTDNEISMEVNPVYALRHRSDSSMHIALKLVSQGKVDACVSAGNTGALMLLAKQALKTLPGISRPALISSLPNMHLGHTYMLDLGANLQCDSHTLFNFAVMGSVLCEKVDQINSPRVSILNVGKEKNKGGDVLQHCAELLKQTKHINYAGFVEANELFTCRSNIIVTDGFSGNIALKSCEGMGRVFSEQLDKAINSSLYSKLLGKLLRPILKKQLKHLHPDMYNGASLIGLRGIVVKSHGSANEIAFTCAIEHAIQETQWQIPASISKKLETVLSERDDLSHE | 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. | A1STW0 |
P11006 | MAGA_XENLA | Magainin II | Xenopus | MFKGLFICSLIAVICANALPQPEASADEDMDEREVRGIGKFLHSAGKFGKAFVGEIMKSKRDAEAVGPEAFADEDLDEREVRGIGKFLHSAKKFGKAFVGEIMNSKRDAEAVGPEAFADEDLDEREVRGIGKFLHSAKKFGKAFVGEIMNSKRDAEAVGPEAFADEDLDEREVRGIGKFLHSAKKFGKAFVGEIMNSKRDAEAVGPEAFADEDFDEREVRGIGKFLHSAKKFGKAFVGEIMNSKRDAEAVGPEAFADEDLDEREVRGIGKFLHSAKKFGKAFVGEIMNSKRDAEAVDDRRWVE | Antimicrobial peptides that inhibit the growth of numerous species of bacteria and fungi and induce osmotic lysis of protozoa. Rapidly inactivates channel catfish herpesvirus (ED(50)=48 uM) over a wide temperature range . Magainins are membrane lytic agents. | P11006 |
A4WL88 | RL1_PYRAR | 50S ribosomal protein L1 | Pyrobaculum | MSVLLNRDVLTSKIAEALKAGKPRRFRQSVELIVVLRELDLSKPENRINLLVELPHPPKANKIAAFAHGVFEVNAKNAGVDAIITRDQIESLSGNKRAIRKLAKQYDFFIAPPDLMPLLGRVVGPIFGPRGKMPEVVPPNVDVKSVVERLRRSVRVRIRNEPVIKVRVGAEGQDQKEILANILTVLEEINRKFSLKQYLKEIYVKKTMGPPIKIRAVEVLSR | Protein L1 is also a translational repressor protein, it controls the translation of its operon by binding to its mRNA. | A4WL88 |
Q9JK92 | HSPB8_MOUSE | Small stress protein-like protein HSP22 | Mus | MADGQLPFPCSYPSRLRRDPFRDSPLSSRLLDDGFGMDPFPDDLTAPWPEWALPRLSSAWPGTLRSGMVPRGPPATARFGVPAEGRSPPPFPGEPWKVCVNVHSFKPEELMVKTKDGYVEVSGKHEEKQQEGGIVSKNFTKKIQLPAEVDPATVFASLSPEGLLIIEAPQVPPYSPFGESSFNNELPQDNQEVTCS | Displays temperature-dependent chaperone activity. | Q9JK92 |
C5CGR0 | RS19_KOSOT | 30S ribosomal protein S19 | Kosmotoga | MSRSKKKGPYVHPKLLKKIKEMNEKGEKKPIKTWSRASMVVPEMIGHTIAVYNGMKHIPVYITENMIGHRLGEFSPTRRFGGHADKKSKKGQVK | Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. | C5CGR0 |
Q5KVC4 | HISZ_GEOKA | ATP phosphoribosyltransferase regulatory subunit | Geobacillus thermoleovorans group | MAKKLFMFEKPLGMRDTLPFLYELKKQVRSVMAEEIERWGYEFIETPTLEYYETVGAASAIADHRLFKLLDQQGHTLVLRPDMTAPIARVAASRLYDDGNPLRLAYNANVFRAQQREGGRPAEFEQIGVELIGDGTVTADAEVISLMVALLKRTGLGRFSVAVGHIGYVNALFLEILGNEERASVLRRFLYEKNYVGYREHVKSWPLSSIDQKRLLDLLSLRGGTDVIEQAKTLVTSEKGRRAADELAVLMAVLRTYGVAEAVKLDMALVSHMSYYTGILFEVYAEQVGFPIGNGGRYDDLLAKFSRPAPATGFGLRVDRLIEAIGETDVRDDIECIVFSQERLAEAVELAEAKRAEGKRVVLQHIAGIRDIDAYSQRYRSIVYLLGRSGRDGQ | Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine. | Q5KVC4 |
Q0BCF1 | PDXH_BURCM | Pyridoxal 5'-phosphate synthase | Burkholderia cepacia complex | MTTLADLRINYSRASLDEADVAPDPFAQFDRWFKEALAAKLPEPNTMTLATVGENGRPSARIVLIKGVDERGFVFFTNYESRKGRDLAAHPYAALLFYWIELERQVRIEGRIEKTSTDESDRYFASRPLGSRIGAWASEQSAVIDSRATLEAREKAVAERYGENPPRPPQWGGYRVVPDAIEFWQGRPSRLHDRLLYTRDAAAAPDWTISRLSP | Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). | Q0BCF1 |
A7GW60 | NUOK_CAMC5 | NDH-1 subunit K | Campylobacter | MITLSHYLVVAALMFVLGLIGIMKRNNLIMLFFSSEILLNAANVALAAISKFYNDITGQIFALFIVAVAASEVAVGLGLLILWYKKTGSIELSSMNNMRD | 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 translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. | A7GW60 |
P0A4L1 | THIO1_NOSS1 | Thioredoxin-M | Nostoc | MSAAAQVTDSTFKQEVLDSDVPVLVDFWAPWCGPCRMVAPVVDEIAQQYEGKIKVVKVNTDENPQVASQYGIRSIPTLMIFKGGQKVDMVVGAVPKTTLSQTLEKHL | Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. | P0A4L1 |
Q8DZZ7 | GLMS_STRA5 | L-glutamine--D-fructose-6-phosphate amidotransferase | Streptococcus | MCGIVGVVGNTNATDILIQGLEKLEYRGYDSAGIFVVGDNKSQLVKSVGRIAEIQAKVGDSVSGTTGIGHTRWATHGKPTEGNAHPHTSGSGRFVLVHNGVIENYLQIKETYLTKHNLKGETDTEIAIHLVEHFVEEDNLSVLEAFKKALHIIEGSYAFALIDSQDADTIYVAKNKSPLLIGLGNGYNMVCSDAMAMIRETSEYMEIHDKELVIVKKDSVEVQDYDGNVIERGSYTAELDLSDIGKGTYPFYMLKEIDEQPTVMRKLISTYANESGDMNVDSDIIKSVQEADRLYILAAGTSYHAGFAAKTMIEKLTDTPVELGVSSEWGYNMPLLSKKPMFILLSQSGETADSRQVLVKANEMGIPSLTITNVPGSTLSREATYTMLIHAGPEIAVASTKAYTAQVATLAFLAKAVGEANGKAEAKDFDLVHELSIVAQSIEATLSEKDVISEKVEQLLISTRNAFYIGRGNDYYVTMEAALKLKEISYIQTEGFAAGELKHGTISLIEDNTPVIALISADSTIAAHTRGNIQEVVSRGANALIIVEEGLEREGDDIIVNKVHPFLSAISMVIPTQLIAYYASLQRGLDVDKPRNLAKAVTVE | Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. | Q8DZZ7 |
Q04TV5 | SSRP_LEPBJ | Small protein B | Leptospira | MANKKEEPGHSPLVNKKAKFNFELVSFIEAGIVLSGSEVKSLREKKGNLTDAFAKIKNGEVFLENFSITPYKNGGYVNHPEIRPRKLLLHKKEIEKLERQVKEKGLVLVATKVYFKNNLRVKVEIAVGKPKKIHDKRDDMQKKDAQQEIARALKSSNRYE | Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation. | Q04TV5 |
P07034 | HBA_CHLME | Hemoglobin alpha-A chain | Chloephaga | VLSAADKANVKGVFSKIGGHADDYGAETLERMFIAYPQTKTYFPHFDLHHGSAQIKAHGKKVAAALVEAVNHIDDITGALSKLSDLHAQKLRVDPVNFKFLGHCFLVVVAIHHPAALTPEVHASLDKFMCAVGAVLTAKYR | Involved in oxygen transport from the lung to the various peripheral tissues. | P07034 |
Q2NKR3 | COXM2_BOVIN | COX assembly mitochondrial protein 2 homolog | Bos | MHPDLSPHLHTEECNVLINLLKECHKNHSILKFFGHCNDLDREMRKCLKNEYMEKRNKSRELGNAMRKRLFNPPEESEN | May be involved in cytochrome c oxidase biogenesis. | Q2NKR3 |
B4RCW4 | DAPA_PHEZH | 4-hydroxy-tetrahydrodipicolinate synthase | Phenylobacterium | MIDPMFRGVLPALVTPYRNGQVDEDAFVALVERQIAGGVHGLVPVGTTGESATLTHEEHRRVVELCVKTARGRVPVVAGAGSNSTAEAIELVRHAKTVGADAALVVTPYYNRPSQEGLYAHYRAINDAVQLPILVYNVPTRTSVDISNDVLVRLSKLPNVVGIKDATSDLVRASFQRLHCGEEWVMLSGDDPVALGYMAHGGHGCISVTANVAPEQCADFYNAALSGDWATALQWQDRLVRLHKALFADASPAPTKFALSHLGLCSEETRLPITPASEAARAEVLAAMRDAGLI | Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). | B4RCW4 |
Q89K83 | HPPA_BRADU | Pyrophosphate-energized inorganic pyrophosphatase | Bradyrhizobium | MTALWLIVLCGVLSVVYAIWATSSVLSADAGSPRMQEIAAAVREGAQAYLRRQYTTIGIVGIVIFVLLVYFLGFYVAIGFAIGAILSGAAGFIGMNVSVRANVRTAQAATTSLAGGLELAFKAGAITGMLVAGLALLGVTLYFGFLVYSLKLAPDSRVVVDAMVALGFGASLISIFARLGGGIFTKGADVGGDLVGKVEAGIPEDDPRNPATIADNVGDNVGDCAGMAADLFETYAVTAVATMVLAAIFFAKTPILMSMMTLPLAIGGICIITSIIGTFFVKLGPSQSIMGALYKGLIATGVLSLIGIAVVIYTLIGFGKLDGVDYTGMSLFECGVVGLIVTALIIWITEYYTGTDYRPVKSIAAASVTGHGTNVIQGLAISMEATALPAIVIIAGILVTYSLAGLFGIAIATATMLALAGMIVALDAFGPVTDNAGGIAEMAGLPKEVRKSTDALDAVGNTTKAVTKGYAIGSAGLGALVLFAAYNQDLKFFVADSAHHTYFAGVNPDFSLNNPYVVVGLLFGGLLPYLFGAMGMTAVGRAASAIVEEVRRQFREKPGIMQGTDKPDYGKAVDLLTKAAIKEMIIPSLLPVLSPIVVYFLIYAIAGGGATGKSAAFSAVGAMLLGVIVTGLFVAISMTSGGGAWDNAKKYIEDGHYGGKGSDAHKSAVTGDTVGDPYKDTAGPAVNPMIKITNIVALLLLAILAH | Proton pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for proton movement across the membrane. Generates a proton motive force. | Q89K83 |