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 |
|---|---|---|---|---|---|---|
W6Q9S9 | FGOX3_PENRF | Old yellow enzyme homolog fgaOx3 | Penicillium | MTKLFTPLHVGRMELANRIAMAPMTRYRASDNHVPLPIMKDYYAQRASVPGTLLITEATTISARAGGYANAPGIYNDAQIAAWKEVTDAVHAKGSYIYVQLWAVGRPANPQLLQAEGGYDLVSSSATAVSADAPTPRALSETEIYAWIADYAQAARNAVAAGFDGVEIHAANGYLIDQFTQDICNTRTDAWGGSVQGRARFALEVSRAVVEAVGADRTGIRFSPWSTFQGMRMKDPKPQFEYLAVQTAKLGLAYVHLVESRIAGGADVDATDRLDFFLRAYGKASPVIFAGGYDAESAVRAVDVEYADYDAIVGIGRPFISNPDLPFRVQNGIPFVPYDRATFYVPKDPKGYTDYAFSAEFQKAIEAAA | Chanoclavine-I aldehyde reductase; part of the gene cluster that mediates the biosynthesis of isofumigaclavines, fungal ergot alkaloids . The tryptophan dimethylallyltransferase ifgA catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan . The second step is catalyzed by the methyltransferase ifgB that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of N-methyl-dimethylallyl-L-tryptophan . The catalase ifgD and the FAD-dependent oxidoreductase ifgC then transform N-methyl-dimethylallyl-L-tryptophan to chanoclavine-I which is further oxidized by ifgE in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde . The chanoclavine-I aldehyde reductases ifgG and/or fgaOx3 reduce chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline . The festuclavine dehydrogenases ifgF1 and/or ifgF2 then catalyze the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine . Hydrolysis of festuclavine by a yet undetermined cytochrome P450 monooxygenase (called ifgH) then leads to the formation of isofumigaclavine B which is in turn acetylated by ifgI to isofumigaclavine A . Penicillium roqueforti has interestingly at least two sets of genes for the consumption of chanoclavine-I aldehyde on three different loci, the OYEs ifgG/fgaOx3 and the festuclavine synthase homologs ifgF1/ifgF2 . The reason for the duplication of these genes is unclear, probably to ensure the conversion of chanoclavine-I aldehyde by differential gene expression under various environmental conditions . | W6Q9S9 |
G5E8F4 | FPGT_MOUSE | GDP-L-fucose pyrophosphorylase | Mus | MASLREATLRKLRRFSELRGKPVAAGEFWDVVAITAADEKQELAYKQQLSEKLKKRELPLGVQYHVFPDPAGTKIGNGGSTLCSLECLESLCGDKWNSLKVLLIHSGGYSQRLPNASALGKIFTALPLGEPIYQMLELKLAMYVDFPSNMRPGVLVTCADDIELYSVGDSEYIAFDQPGFTALAHPSSLAVGTTHGVFVLHSDSSLQHGDLEYRQCYQFLHKPTIENMHRFNAVHRQRSFGQQNLSGGDTDCLPLHTEYVYTDSLFYMDHKSAKKLLDFYKSEGPLNCEIDAYGDFLQALGPGATAEYTRNTSHVTKEESQLLDMRQKIFHLLKGTPLNVVVLNNSRFYHIGTLQEYLLHFTSDSALKTELGLQSIAFSVSPSVPERSSGTACVIHSIVDSGCCVAPGSVVEYSRLGPEVSIGENCIISSSVIAKTVVPAYSFLCSLSVKINGHLKYSTMVFGMQDNLKNSVKTLEDIKALQFFGVCFLSCLDIWNLKATEKLFSGNKMNLSLWTACIFPVCSSLSESATASLGMLSAVRNHSPFNLSDFNLLSIQEMLVYKDVQDMLAYREHIFLEISSNKNQSDLEKS | Catalyzes the formation of GDP-L-fucose from GTP and L-fucose-1-phosphate . Functions as a salvage pathway to reutilize L-fucose arising from the turnover of glycoproteins and glycolipids (Probable). | G5E8F4 |
O80933 | SCL9_ARATH | GRAS family protein 13 | Arabidopsis | MITEPSLTGISGMVNRNRLSGLPDQPSSHSFTPVTLYDGFNYNLSSDHINTVVAAPENSVFIREEEEEEDPADDFDFSDAVLGYISQMLNEEDMDDKVCMLQESLDLEAAERSLYEAIGKKYPPSPERNLAFAERNSENLDRVVPGNYTGGDCIGFGNGGIKPLSSGFTLDFRNPQSCSSILSVPQSNGLITIYGDGIDESSKNNRENHQSVWLFRREIEEANRFNPEENELIVNFREENCVSKARKNSSRDEICVEEERSSKLPAVFGEDILRSDVVDKILVHVPGGESMKEFNALRDVLKKGVEKKKASDAQGGKRRARGRGRGRGRGGGGGQNGKKEVVDLRSLLIHCAQAVAADDRRCAGQLLKQIRLHSTPFGDGNQRLAHCFANGLEARLAGTGSQIYKGIVSKPRSAAAVLKAHQLFLACCPFRKLSYFITNKTIRDLVGNSQRVHVIDFGILYGFQWPTLIHRFSMYGSPKVRITGIEFPQPGFRPAQRVEETGQRLAAYAKLFGVPFEYKAIAKKWDAIQLEDLDIDRDEITVVNCLYRAENLHDESVKVESCRDTVLNLIGKINPDLFVFGIVNGAYNAPFFVTRFREALFHFSSIFDMLETIVPREDEERMFLEMEVFGREALNVIACEGWERVERPETYKQWHVRAMRSGLVQVPFDPSIMKTSLHKVHTFYHKDFVIDQDNRWLLQGWKGRTVMALSVWKPESKA | Probable transcription factor involved in plant development. | O80933 |
Q0HYK9 | HEM1_SHESR | Glutamyl-tRNA reductase | Shewanella | MSLVAIGINHKTATVDLREKVAFSPDKIHDAMKSLASRTRSGEAVIVSTCNRTELYCNNGDEADIIEWLEEYHGLDHQDVAPCLYNYHGQAAVKHLMRVASGLDSLILGEPQILGQVKQAFVKAKEAGTVALTIDRLFQNTFSVAKKVRTETEIGAAAVSVAFAAVSMAKHIFSSLSTTKVLLIGAGETIELVAKHLKDNGVASMVVANRTLERAQSMCEEFNATAITLAQIPDFLPKADIVISSTASPLPILGKGMVEKALKQRRHQPMLLVDIAVPRDIEPEVADLDDAFLYTVDDLHSIIEQNKASRKEAAEQAELITEEQSYLFMDWVRSLESVDSIREYRSQSMAIKDELVERALNKLAQGGDTEQVLIELANRLTNRLIHAPTQALTVASRQGDLNTLGQLRTALGLDKN | Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). | Q0HYK9 |
Q8X170 | ABCA_ASPFM | ABC multidrug transporter A | Aspergillus subgen. Fumigati | MNESHEAGKNSSTNVEEREEEVLRLARQFTEQSSYSTAGQTPFAAEAGSALDPNGERFNARAWCKAMLQMHIGDKEAHPLRTLGVAFSNLNVHGFGSDTDYQKSVGNVWLKTLSLARIAFGQKQRKVDILQNLEGLVEAGEMLVVLGPPGSGCSTFLKTIAGETYGFHVDKNSNINFQGIAKQMAHEFRGEAIYTAEVDVHFPKLTVGDTLYFAARARTPRHIPGGVNATQYAGHMRDVIMAMFGISHTKNTIVGNDFIRGVSGGERKRVSIAEACLSNAPLQCWDNSTRGLDSANAIEFCKTLRMQADINGTTACVSLYQAPQAAYDYFDKVLVLYEGREIYFGPTSMAKHYFLQMGFVCPDRQTDADFLTSMTSHLERVVQPGYEDRVPRTPDEFAARWKASPQRAQLMQHIKSYNAKFALDGEYLDKFKQSRRAQQAKAQRVSSPYTLSYVQQVKLCLWRGYQRLKADPSVTISSLFGNTIISLVIASIFYNLKADTSTFFQRGALLFFAVLMNALGCGLEMLTLYAQRGIIEKHSRYALYHPSAEAFSSMIMDLPYKILNAITSNIVLYFMTNLRRAPGAFFFFVFTSFILTLTMSMFFRSMASLSRSLVQVLPFSAVLLLGLSMYTGFAIPTGYMLGWARWIAYINPISYGFESLMINEFHNRDFPCMDYVPSGPGYTDVGLNNRVCSTVRSVPGQAFVNGNAYIESAYSYTASHKWRNIGVIFAYMFLLGAVYLVATDFITEKKPKGEILVFPRGHKALKKGKSDEDLEGGGGRSATVEKIGSDGLAMIERQTAIFQWKDVCFDIKIGKENCRILDHVDGWVKPGILTALMGVSGAGKTTLLDVLATRTTMGIISGEMLVDGQPRDESFQRKTGYAQQQDLHLSTATVREALEFSALLRQSAHVPRQEKIDYVTEVIKLLDMTEYADAVIGVPGEGLNVEQRKRLTIGVELAARPQLLLFLDEPTSGLDSQTSWAILDLLDKLKKNGQAILCTIHQPSAMLFQRFDRLLFLQAGGRTVYFGEIGQNSQILIDYFVRNGAPPCPPDANPAEWMLDVIGAAPGSHTSINWFETWRRSPEYARVQEHLAELKHERRHQTNLFRTTSGQKREDKDSYREFAAPFWAQLYQVQVRVFQQIWRSPTYINSKTALCVLSALFVGFSLFHTPNTIQGLQNQMFGIFMLLTLFGQLIQQIMPHFVAQRALYEVRDRPAKTYSWKAFLIANIVVELPWNSLMSVLMFLCWYYPIGLYRNAEPTDAVHLRGTQMWLMIWTFLLFSSTFAHFMIAAFDAAENAGNLGNLLFLLCLLFCGVLATPDQLPRFWIFMYRVSPFTYLVSGMLSVGISNTNVTCADNEYLRFDPVNGTCGEYMGSYMSNLGGYLADEMATANCSFCPIKETNVFLGRVSSSYSDIWRNFGLMWVFIVFNIFAACSLYWWVRVPRDKKPVAKAE | ABC transporter that seems not to be involved in the efflux of toxic substances, at least not the classical compounds such as itraconazole, amphotericin B, voriconazole, posaconazole, ravuconazole, or echinocandins. | Q8X170 |
Q5L407 | RL7_GEOKA | 50S ribosomal protein L7/L12 | Geobacillus thermoleovorans group | MMTKEQIIEAVKNMTVLELNELVKAIEEEFGVTAAAPVVVAGGAAAGAEAAAEKTEFDVILADAGAQKIKVIKVVREITGLGLKEAKDLVDNTPKPIKEGIAKEEAEEIKAKLEEAGAKVEIK | Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation. | Q5L407 |
P25497 | 3S11_PSEAU | Neurotoxin PA A | Pseudechis | MKTLLLTLVVVTIVCLDLGYTMTCCNQQSSQPKTTTICAGGESSCYKKTWSDHRGSRTERGCGCPHVKPGIKLTCCKTDECNN | Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission. | P25497 |
C0ZA70 | RNPA_BREBN | Protein C5 | Brevibacillus | MHRSHRLKKNEQFQAVFQRGSSAANKQFVLYSAKQEGQAAFRAGISVSKKIGNAVVRNRVKRLIREAVARMESDIPVGLDLVIIARPGVEAMTLEAIEQSLLHVMKRAKVIKQAPVHNGKRDGKRG | RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. | C0ZA70 |
Q6N1S9 | AROE_RHOPA | Shikimate dehydrogenase (NADP(+)) | Rhodopseudomonas | MAATKRAACLIGCPAAHSRSPLIHHYWLRQLGIEGGYSIEAVPPEGFAEFVLHLKTHGYVGANVTIPHKERALQLTEPDERACAVGAANTLYYDGDLLRSTNTDIEGFIGNLDASAPGWDRSAHALVLGAGGSSRAVVFGLLERGVQRIALANRSIERAQALRDLFGERVVPIAWSDIPAALPGAGLLVNTTSLGMKGQPPLQIDLSALPADAVVSDLVYVPLETDLLAAAKARGLRTADGLGMLLHQAVRGFDLWFGARPHVTPELRALVEADLAPK | 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). | Q6N1S9 |
Q9RVD3 | AROA_DEIRA | 5-enolpyruvylshikimate-3-phosphate synthase | Deinococcus | MSDALPATFDVIVHPARELRGELRAQPSKNYTTRYLLAAALAEGETRVVGVATSEDAEAMLRCLRDWGAGVELVGDDAVIRGFGARPQAGVTLNPGNAGAVARFLMGVAALTSGTTFVTDYPDSLGKRPQGDLLEALERLGAWVSSNDGRLPISVSGPVRGGTVEVSAERSSQYASALMFLGPLLPDGLELRLTGDIKSHAPLRQTLDTLSDFGVRATASDDLRRISIPGGQKYRPGRVLVPGDYPGSAAILTAAALLPGEVRLSNLREHDLQGEKEAVNVLREMGADIVREGDTLTVRGGRPLHAVTRDGDSFTDAVQALTAAAAFAEGDTTWENVATLRLKECDRISDTRAELERLGLRARETADSLSVTGSAHLAGGITADGHGDHRMIMLLTLLGLRADAPLRITGAHHIRKSYPQFFAHLEALGARFEYAEATA | Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. | Q9RVD3 |
Q5R6J7 | GPAT4_PONAB | Lysophosphatidic acid acyltransferase zeta | Pongo | MFLLLPFDSLIVNLLGISLTVLFTLLLVFIIVPAIFGVSFGIRKLYMKTLLKIFAWATLRMERGAKEKNHQLYKPYTNGIIAKDPTSLEEEIKEIRRSGSSKALDNTPEFELSDIFYFCRKGMETIMDDEVTKRFSAEELESWNLLSRTNYNFQYISLRLTVLWGLGVLIRYCFLLPLRIALAFTGISLLVVGTTVVGYLPNGRFKEFMSKHVHLMCYRICVRALTAIITYHDRENRPRNGGICVANHTSPIDVIILASDGYYAMVGQVHGGLMGVIQRAMVKACPHVWFERSEVKDRHLVAKRLTEHVQDKSKLPILIFPEGTCINNTSVMMFKKGSFEIGATVYPVAIKYDPQFGDAFWNSSKYGMVTYLLRMMTSWAIVCSVWYLPPMTREADEDAVQFANRVKSAIARQGGLVDLLWDGGLKREKVKDTFKEEQQKLYSKMIVGNHKDRSRS | Converts glycerol-3-phosphate to 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) by incorporating an acyl moiety at the sn-1 position of the glycerol backbone. Active against both saturated and unsaturated long-chain fatty acyl-CoAs. Protects cells against lipotoxicity. | Q5R6J7 |
Q2PFD7 | PSD3_MOUSE | Pleckstrin homology and SEC7 domain-containing protein 3 | Mus | MEGRNAAAEPFVWVNSASAHSQSVAKAKYEFLFGKSEEKTPDSSDHGGSTLLPPTVTNEFPEYGTMEEGGEGLRASLDFDAKSPPCRLPGQQAVHLLAGQDSILNSVTEGPNDAPQCHPQEQSLQPIDSLISALKATEARIASGTFQATKVLDKDANFSVYQVDKELSTASHKPQRAHRTFPVGPGKSPDIPLSAEVPTEENLSLHIQEDLSALLPEEAQAHRSQITNYRRQGPLRVPESACPVSSSSAGSHNPVDRVGALREQRSDLGREHPRGYDRGGSMGRQGRIKHVEFQGVEILWTGEEAESRHPPERTASPVSKEFAKRPSHSSPACGVCSTSTHLTGDVWDETCKAPSERPGTSAGTLSPMPLGESGEDDVFLRESKEHLEENFAIQGDKERILDQEEHLRGDDDILGPGYTEDSTDVYSSQFETILDNTSLYYSAESLETLYSEPDSYFSFEMPLTPMIQQRIKEGGQFLERTSVGGQHDVLSVSADGGIVMGYSAGITNGLHDSANSVYTRGPQEIAFWGSRDRCFAEGKTTGVDAGSEMGSTDILEKETTESLSNGTNSNVEAAKRLAKRLYHLDRFKRSDVAKHLGKNNEFSKLVAEEYLKFFDFTGMTLDQSLRYFLKAFSLVGETQERERVLIHFSNRYFSCNPDTITSKDGVHCLTCAMMLLNTDLHGHVNIGKKMTCQEFITNLQGVNEGGDFSKDLLKALYNSIKNEKLEWAVDDEEKKKSPSEGTDEKANGTHPKTISRIGSTTNPFLDIPHDPNAAVYKSGFLARKIHADMDGKKTPRGKRGWKTFYAVLKGTVLYLQKDEYKPEKSLSDEDLKNAVSVHHALASKATDYEKKPNVFKLKTADWRVLLFQTQSPEEMQGWINKINCVAAVFSAPPFPAAIGSQKKFSRPLLPATTTKLSQEEQLKSHESKLKQITTELAEHRSYPPDKKVKAKDVDEYKLKDHYLEFEKTRYEIYVSVLKEGGKELLTTDGNEPVGLKKSHSSPSLNPDASPVTAKVKRNVSERKDHRPETPGIKQKVT | Guanine nucleotide exchange factor for ARF6. | Q2PFD7 |
Q98K73 | TAM_RHILO | Trans-aconitate 2-methyltransferase | Mesorhizobium | MADWSAAQYLKFEDERTRPARDLVAQVPVDFPRRVVDIGCGPGNSTELLVQRWPDAQVSGFDTSPDMIEKARVRLPNVSFDLADASTWQPAEPVNVIFANAVFQWLPTHPAVFQRLMGFLAPGGALAVQMPDNLLEPSHQMMRDTAAEMPFADKLKGAARGPLPPVSFYYDLMSPLADRLDIWHTAYNHPLADAEAIVEWVKSTGLKPFLDPLDADERKMFLDSYTAKIAKAYPKTADGKVLLRFPRIFIVAKRAG | Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate. | Q98K73 |
Q0HFZ0 | LSPA_SHESM | Signal peptidase II | Shewanella | MPLTWKDSGLRWYWVVVLVFLADQLSKQWVLANFDLFESVKLLPFFNFTYVRNYGAAFSFLSEAGGWQRWLFTLVAVGFSTLLTVWLRKQSASLWKLNLAYTLVIGGALGNLIDRLMHGFVVDFIDFYWGKSHYPAFNIADSAIFIGAVLIIWDSFFNSKSEQDKTEEVK | This protein specifically catalyzes the removal of signal peptides from prolipoproteins. | Q0HFZ0 |
Q92FU8 | RECF_LISIN | DNA replication and repair protein RecF | Listeria | MHLESIVLRNFRNYENLELEFSPSVNVFLGENAQGKTNLLEAVLMLALAKSHRTTNDKDFIMWEKEEAKMEGRVVKRGQTVPLELAITQKGKRAKVNHLEQKKLSQYVGNLNVVIFAPEDLSLVKGAPGVRRRFLNMEIGQMQPIYLHNLSEYQRILQQRNQYLKMLQMKRKVDPMLLDILTEQFADVAINLTKRRADFIQKLEAYAAPIHHQISRGLETLKIEYKASVTLNGDDPEVWKADLLQKMESIKQREIDRGVTLIGPHRDDSLFYINGQNVQDFGSQGQQRTTALSVKLAEIDLIHEETGEYPVLLLDDVLSELDDYRQSHLLGAIEGKVQTFVTTTSTSGIDHNTLRQATTFYVEKGTVKKS | 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. | Q92FU8 |
A0A0H3JT80 | ODH_STAAM | Staphylopine dehydrogenase | Staphylococcus | MSKLLMIGTGPVAIQLANICYLKSDYEIDMVGRASTSEKSKRLYQAYKKEKQFEVKIQNEAHQHLEGKFEINRLYKDVKNVKGEYETVVMACTADAYYDTLQQLSLETLQSVKHVILISPTFGSQMIVEQFMSKFSQDIEVISFSTYLGDTRIVDKEAPNHVLTTGVKKKLYMGSTHSNSTMCQRISALAEQLKIQLEVVESPLHAETRNSSLYVHPPLFMNDFSLKAIFEGTDVPVYVYKLFPEGPITMTLIREMRLMWKEMMAILQAFRVPSVNLLQFMVKENYPVRPETLDEGDIEHFEILPDILQEYLLYVRYTAILIDPFSQPDENGHYFDFSAVPFKQVYKNEQDVVQIPRMPSEDYYRTAMIQHIGKMLGIKTPMIDQFLTRYEASCQAYKDMHQDQQLSSQFNTNLFEGDKALVTKFLEINRTLS | Catalyzes the NADPH-dependent reductive condensation of pyruvate to the intermediate formed by the adjacently encoded enzyme CntL, namely (2S)-2-amino-4-{[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate, leading to the production of staphylopine. This is the last step in the biosynthesis of the metallophore staphylopine, which is involved in the acquisition of nickel, cobalt, zinc, copper, and iron, and thus enables bacterial growth inside the host, where metal access is limited. Therefore, this enzyme probably contributes to staphylococcal virulence. Can use neither NADH nor alpha-ketoglutarate in place of NADPH and pyruvate, respectively. | A0A0H3JT80 |
Q9PMK3 | TRUD_CAMJE | tRNA-uridine isomerase D | Campylobacter | MNLEEENTIFKPLYSLKHSPINAYFSKNSDDFVVRERPLYEFSGKGEHLILHINKKDLTTNEALKILSEASGVKIRDFGYAGLKDKQGSTFQYLSMPKKFESFLSNFSHPKLKILEIFTHENKLRIGHLKGNSFFIRLKKVLPSDALKLEQALMNLDKQGFANYFGYQRFGKFGDNYKEGLEILRGKKMKNVKMKEFLISAFQSELFNRYLSKRVELSHFANDFSEKELIQIYKISKEEAKELKKQEQFFKLLKGEVLGHYPFGKCFLCEDLSAELGRFKARDISAMGLLIGAKAYETGEGLALNLENEIFKDTLEFKAKMQGSRRFMWGYLEELKWRYDEEKAHFCIEFFLQKGSYATVVLEEILHKNLFE | Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs. | Q9PMK3 |
Q606J9 | UBIE_METCA | Demethylmenaquinone methyltransferase | Methylococcus | MSENTTHFGFRTVPEHEKANMVRAVFDSVAGKYDVMNDLMSIGIHRLWKRIAVDLAHVRSGEKVLDLAGGTGDLTALFRKRVGARGFVVLSDINAEMLRRGRDRIIDDGLAESVAYAQIDAEKLPFPHDSFDCISIGFGLRNVTHKDKALNSMYRALKPGGRLIVLEFSEVHNELLRKAYDLYSFKVLPFLGKLVANDAESYRYLAESIRMHPNQEKLKAMMEKAGFERCEYFDLMQGIVAVHRGYKF | Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2). | Q606J9 |
A6Q596 | DAPB_NITSB | 4-hydroxy-tetrahydrodipicolinate reductase | unclassified Nitratiruptor | MLNVGIYGGSGRVGSLLIKNLQHDEVARVSVVHVLKGIELAVPGATVTNDIDTLIQKSDVIIDFTLPEGTESLLERLLEHPKPLVSGTTGLNKHQQNLMQTLAQKTPVLYATNMSLGIALLKRLVAVTSEKLRDFDIEIVEMHHRYKKDAPSGTALTLAEFAAKARGLDLEKVRVSGRDGNIGERSKEEIGVFALRGGDIVGRHTVGFYNDGEYIELNHTATSRDTFAKGAIKAAKWLVSQEPGFYTIDDCLGL | Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. | A6Q596 |
Q6MT06 | DNAK_MYCMS | Heat shock protein 70 | Mycoplasma | MAKEKIIGIDLGTTNSVVSVIEGGQPIILENPEGQRTTPSVVAFKNSDIIVGGAAKRQAVTNPNVVQSIKSKMGTTSKVNLEGKDYSPEQISAEILRYMKNYAEAKLGQKVTKAVITVPAYFNDAQRKATKDAGTIAGLQVERIINEPTAAALAYGLDKQDKEETILVYDLGGGTFDVSILAIGGGSFDVIATSGNNKLGGDNFDEEIIKWLLGKIKAEYNIDLSKEKMALQRLKDEAEKAKINLSSQLEVEINLPFIAMNESGPISFATTLTRSEFNKITKHLVDLTIQPVKDALSAAKKTPSEINEVLLVGGSTRIPAVQELVKSLLNKEPNRSINPDEVVAMGAAVQGGVLAGEVTDILLLDVTPLSLGIETMGGVMTKLIERNTTIPAKRTQIFSTATDNQPAVDINVLQGERAMAADNKSLGQFQLTGIQPAPRGVPQIEVTFEIDANGIVSVSAKDKNTNEEKTITISNSGNLSEAEVERMIKEAQENAANDEVKKKNIELKNKAENYINIIENSLLQAGDKISAEQKEQSQKMVDEIKELVKNENYEALEQKMAELEQAMAQAAEFANKQNESDPNNNSSEQNN | Acts as a chaperone. | Q6MT06 |
A7GJZ2 | MCSB_BACCN | Protein-arginine kinase | Bacillus cereus group | MSLDRIMNEAISPWMKGDGPDSDIVLSTRIRLARNLKNYHFPIMQTAEEANQITELFQQKLVNKTMRDFGSFELLKMNELTPLQRRVLVEKHLISPNLAETEFGACILSESEHISVMLNEEDHVRIQCLFPGLQLSEALQSANKIDNVFEEVVEYAFDEELGYVTSCPTNVGTGLRASVMIHLPALVLTKRINRIIQAIQQLGLVVRGIYGEGSEALGNIFQVSNQMTLGKSEEDIIADLTSVIHQLIQQEKAARELIVKNSSIELEDKVYRSYGILAHSRLIQSAEAATCLSDVRLGIDLGYIKDVSRNILTELMVLTQPGILQQYAGGQLGPEERDYRRAALIRERLRIEENEA | Catalyzes the specific phosphorylation of arginine residues in a large number of proteins. Is part of the bacterial stress response system. Protein arginine phosphorylation has a physiologically important role and is involved in the regulation of many critical cellular processes, such as protein homeostasis, motility, competence, and stringent and stress responses, by regulating gene expression and protein activity. | A7GJZ2 |
Q0D155 | AT329_ASPTN | Isoflavipucine biosynthesis cluster protein ATEG_00329 | Aspergillus subgen. Circumdati | MSPVKQRLLRIAVSHNRHPSLSEEQFHQWATKEHCARAARIHSRHGIEAYGMLFSPETARTTVQNLNRQLGGRWKIDEHDVTVEFYLHSLDELTSVLEDPEFKALQQEEEPYVSGEDIVATLGWVETYVQDGRVVNVDSEGVPTYPGFGVLADFSSEQVNQK | Putative oxygenase; part of the gene cluster that mediates the biosynthesis of isoflavipucine . The PKS part of the PKS-NRPS ATEG_00325 probably assembles a triketide from an acetyl starter and two malonyl-CoA extender units . The poly-beta-keto intermediate would then be fused to the leucine unit by the NRPS part . The resulting amide would be liberated from the PKS-NRPS through reductive release of the linear PKS-NRPS product from the enzyme complex . Further steps in isoflapucine synthesis include a cyclization step, an oxidation step, a hydrolysis step involving a trans-amidation, and an additional oxidation step, leading to flavipucine . Formation of isoflavipucine from flavipucine requires an unusual rearrangement . Alternative rearrangement reactions could build up rubrobramide, representing a branching of flavipucine biosynthesis . The enzymes involved in the post-PKS-NRPS steps have not been identified yet, but the putative oxygenases ATEG_003329 and ATEG_00330 encoded by the cluster could play a role . | Q0D155 |
Q74JN8 | UVRC_LACJO | Excinuclease ABC subunit C | Lactobacillus | MATEHIENKLKLLPDKPGCYLMKDVNGNVIYVGKSKNLKNRVRSYFKSKQVGRRAELVREIRDFDIITVSSDKESFLLEITLIKKYQPYYNVQLKQGTGYPYIEITNERDPQTRLTSIVHKDHGYYFGPYPNVYAAQATLKFIQKVWPLRRCTGHQGRPCLYYHMGQCLGACFKEVPKSTYDAQIRKIKRFLNGDIAQVKQDLTEKMTQASMDLEFERAAEIRDQLKYIEQTVEKQKIISNDHTQRDIFNFYVDKSWISIQIFFLRQAKLLRRETRLFPLTDTNDPQDAFVSFIAQFYGQRNRVLPKEVLVPAGMDNESLSEVLKVPVRTPQRGQKKALLEMAHDNAKLKLDEKFRLLELGNRKTKGAQKEIFDALGLPYGHRIESFDHSHIQGADPVSALVVFTDGEADKHEYRKYKLKGEVEHQNAADEVGNTREVVRRRYSRLLKEHKKMPDLILMDGGQIQVEACLDVLRNELNVNIPVAGMVKDDHHRTNHLIFGDPTKGEELKLIPLDPKSEGFYLMTRIQDEVHRFAITFHRRTHAKNALSSKLDEIKGIGPKSRNKLLRKFGSLKKIKEASVDELREAGLTLPQAQTVKLSL | The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. | Q74JN8 |
G5EEL5 | DBL1_CAEEL | Dpp and BMP-like protein 1 | Caenorhabditis | MNDSVRTTTTISSTKSLVHSFQLSAILHLFLLISFTPMSAAADQHASHATRRGLLRKLGLEHVPVQTGPSIDVPQHMWDIYDDDNDVDWVRHYYPKEIIEDNEGFLLSYNLSLAARNAHNEEVTKATLKLRLRRNNKARRSGNISIYFFEDDINNDRFQIESRSVDNLTEWIDFDVTAAFLRRTNRISFFIDLPEDVEIEETQSSSLSSLPYARAQSAPLIVFSDLSEPSSVRRKRSAQTGNSERKNRKKGRKHHNTEAESNLCRRTDFYVDFDDLNWQDWIMAPKGYDAYQCQGSCPNPMPAQLNATNHAIIQSLLHSLRPDEVPPPCCVPTETSPLSILYMDVDKVIVIREYADMRVESCGCR | Ligand for the serine/threonine-protein kinase receptor type-1 sma-6 which activates a TGF-beta-like signaling pathway . Multifunctional protein that is involved in body size, male ectodermal patterning, innate immunity, lipid metabolism and neural plasticity . Dose-dependent regulator of body size, probably influencing the sizes of some or all cells rather than their number . Plays a role in patterning of male-specific genital sensilla (simple sense organs), known as rays, and mating-associated structures, spicules . Plays a protective role in response to infection by the Gram-negative bacterium S.marcescens, by activating expression of genes involved in innate immunity . Regulator of lipid homeostasis, acting non cell-autonomously in the hypodermis; partly dependent on the Insulin/IGF-1-like signaling (IIS) mediated pathway . Required for aversive olfactory learning of pathogenic bacteria in adults . Involved in gland cell morphology, possibly via activation of a Smad-independent TGF-beta signaling pathway . Required to oppose the autoregulation of expression of Runt-related transcription factor rnt-1. | G5EEL5 |
P77873 | NIFH_HERSE | Nitrogenase reductase | Herbaspirillum | MASLRQIAFYGKGGIGKSTTSQNTLAALAQMGQRILIVGCDPKADSTRLILHAKAQDTILSLAADAGSVEDLELEDVMKIGYQNIRCVESGGPEPGVGCAGRGVITSINFLEEEGAYDDTDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMAMYAANNISKGILKYANSGGVRLGGLICNERKTDKELELATALAAKLNSKLIHFVPRDNIVQHAELRRMTVLEYAPDSKQAGEYRTLANKIHENAGNGTIPTPITMDELEDLLMQHGLMPVVDESMVGKSAEVAA | The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein. | P77873 |
Q6AAI8 | NAGB_CUTAK | Glucosamine-6-phosphate isomerase | Cutibacterium | MEVIICSDEQAVGRIAADRIAKVLGRAKAPVLGVATGSTPLTTYSSLAALAAEGKADFTDLRAFALDEYIGLPADDERSYAATIRHTVTEQLGLDPANVHTPDGMADDLDAACAAYETAIQEADGVDVQILGIGANGHIGFNEPTSSLSSRTRVKTLAERTKADNARFFEEGEKVPSHCVTQGLGTIMDARNVVLLAIGANKADALAGAVEGPVSAMCPASVLQFHPHVLVIADDAAASKLTMAEYFRWTDSQRGDLSGAM | Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion. | Q6AAI8 |
Q0SP20 | YIDD_BORAP | Putative membrane protein insertion efficiency factor | Borreliella | MNIFKIFFILNYTIIFLIKIYQNTFSKLFGQQCIYKPTCSKYSIECLKKYNFLTALVLMTLRTIRCNALFKGGNDFIPKYNPISTSLKEFQKRLIK | Could be involved in insertion of integral membrane proteins into the membrane. | Q0SP20 |
P0AAK0 | HYBA_SHIFL | Hydrogenase-2 operon protein HybA | Shigella | MNRRNFIKAASCGALLTGALPSVSHAAAENRPPIPGSLGMLYDSTLCVGCQACVTKCQDINFPERNPQGEQTWSNNDKLSPYTNNIIQVWTSGTGVNKDQEENGYAYIKKQCMHCVDPNCVSVCPVSALKKDPKTGIVHYDKDVCTGCRYCMVACPYNVPKYDYNNPFGALHKCELCNQKGVERLDKGGLPGCVEVCPAGAVIFGTREELMAEAKKRLALKPGSEYHYPRQTLKSGDTYLHTVPKYYPHLYGEKEGGGTQVLVLTGVPYENLDLPKLDDLSTGARSENIQHTLYKGMMLPLAVLAGLTVLVRRNTKNDHHDGGDDHES | Participates in the periplasmic electron-transferring activity of hydrogenase 2 during its catalytic turnover. | P0AAK0 |
P83142 | AFP2S_MALPA | CW-2 | Malva | SDYSRKRDPPQKYEEE | Possesses antifungal activity against P.infestans but not F.graminearum. | P83142 |
A4QBJ1 | RS17_CORGB | 30S ribosomal protein S17 | Corynebacterium | MSEANVNNQEKSTRKVRTGYVVSDKMQKTIVVEVEDRKQHALYGKILRSAKKVKAHDEEQIAGIGDLVRIEETRPLSKDKNYRLIEIVEKAK | One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. | A4QBJ1 |
A9MFP1 | MIAA_SALAR | Isopentenyl-diphosphate:tRNA isopentenyltransferase | Salmonella | MNDVSKASLPKAIFLMGPTASGKTALAIELRKVLPVELISVDSALIYRGMDIGTAKPSADELKAAPHRLLNIRDPSQAYSAADFRRDALAQMAEITAAGRIPLLVGGTMLYFKALLEGLSPLPSADPEVRSRIEQQAAELGWELLHQQLQEIDPVAAARIHPNDPQRLSRALEVFFISGKTLTELTQTSGDALPYQVHQFAIAPASRELLHQRIELRFHQMLASGFEAEVRALFARGDLHTDLPSIRCVGYRQMWSYIEGEISYDEMVYRGVCATRQLAKRQMTWLRGWEGVRWLDSENPDRARKEVLQVVGAIAD | Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A). | A9MFP1 |
A1AW13 | GATA_RUTMC | Glutamyl-tRNA(Gln) amidotransferase subunit A | Candidatus Ruthia | MHTKTIVELAQGFKDKDFSCVELTQYYLNRIDQSDLNAFITVTDELALAQAQVADDKIASGNANILTGIPYAHKDIFCTKGVKTSAGSRMLDTFVSPYDATVSQKLNQVNLVMLGKTNMDEFAMGSSNENSFYGAVKNPWNYLKIPGGSSGGSAASVAGGLSCFATGTDTGGSIRQPASLCGITGIKPTYGRISRYGMIAYASSLDQAGPMTKTAQDAAIVLNVMAGFDEKDSTSVEQKVPDYTTHLNDSIKGLIIGLPKEFFSSGLDDEVANNIMAAVKEFEAMGAIVKEVSLPNLAYAIPVYYIVAPCECSSNLSRLDGVRYGYRAKNVKNLEDLYLRSRSEGFGEEVKRRIMIGAYALSAGYYDAYYLKAQKVRHLISDDFKKVFEQIDVIMGPVSPTTAFDLGSVKDPVSMYLADIYTLSANLAGLPGMSIPAGFAQNLPVGLQLIGNFWSESRLLNIAHQFQLQTDWHLKTPQEC | Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). | A1AW13 |
Q1CWZ9 | CHEB5_MYXXD | Protein-glutamate methylesterase/protein-glutamine glutaminase 5 | Myxococcus | MTVVSPIRVLVVDDSAFARKVLRQVLSSAEGLEVVGVARDGLDALEKVAELSPDVLTLDLVMPGLDGLGVLRALASSAAAPRVVVVSSAGEESELAVAALQAGAVELVNKPTALATERLYELGGELVAKVRTAAGAVARAPPEPAPSPEATSAPVARAAAKSLVVVGTSTGGPQALTRLLSELPVDFPAPLALALHIPTGYTEAVARRLNAHCALEVFEAVDGLELRPGRVVLARSGQHLKLERHGPVTLARLDRQPLRTAHHPSVDVLFESAARSWGSDVVGLVLTGMGDDGVAGARAIREAGGTVLTESESSCVVYGMPRAVKEAGLATDSAPLEGMLALLRRHVR | Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid. | Q1CWZ9 |
B7VMW3 | HEM6_VIBA3 | Oxygen-dependent coproporphyrinogen-III oxidase | Vibrio | MSAIDKEAVKQFLLSLQDSICQQLEQADGTALFEEDAWQREPGERLGGGGRTRVMTNGAVFEQGGVNFSHVAGKAMPASATAHRPELAGRKFEAMGVSLVIHPKNPYIPTSHANVRFFIAEKEGEDPIWWFGGGFDLTPFYPVDEDCQSWHQTAKDLCAPFGDDVYQEHKEWCDKYFYLPHRDETRGVGGLFFDDLNEWGFEKSFAYMQAVGEGFAAAYLPIVERRKETPYGERERDFQLYRRGRYVEFNLVYDRGTLFGLQSGGRTESILMSMPPLARWEYRYEPQACSPEALLYSDYLKPRVW | Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX. | B7VMW3 |
A2VDZ9 | VAPB_BOVIN | Vesicle-associated membrane protein-associated protein B | Bos | MAKVEQVLSLEPQHELKFRGPFTDVVTTNLKLGNPTDRNVCFKVKTTAPRRYCVRPNSGIIDAGASINVSVMLQPFDYDPNEKSKHKFMVQSMFAPTDTSDMEAVWKEAKPEDLMDSKLRCVFELPAENDKPHDVEINKIIPTTASKTETPTVSKALSSSLDDTEVKKVMEECKRLQSEVQRLREENKQFKEEDGLRMRKTAQSNSPAPASAMAGKEEGLSTRLLALVVLFFIVGVIIGKIAL | Participates in the endoplasmic reticulum unfolded protein response (UPR) by inducing ERN1/IRE1 activity. Involved in cellular calcium homeostasis regulation. | A2VDZ9 |
Q9JIH2 | NUP50_MOUSE | Nucleoporin Nup50 | Mus | MAKRVAEKELTDRNWDEEDEVEEMGTFSVASEEVMKNRAVKKAKRRNVGFESDSGGAFKGFKGLVVPSGGGGFSGFGGSGGKPLEGLTNGNSTDNATPFSNVKTAAEPKAAFGSFAVNGPTTLVDKKISSPKCNNSNQPPSSGPASSTACPGNAYHKQLAGLNCSVRDWIVKHVNTNPLCDLTPIFKDYERYLATIEKQLENGGGSSSESQTDRATAGMEPPSLFGSTKLQQESPFSFHGNKAEDTSEKVEFTAEKKSDAAQGATSASFSFGKKIESSALGSLSSGSLTGFSFSAGSSSLFGKDAAQSKAASSLFSAKASESPAGGGSSECRDGEEEENDEPPKVVVTEVKEEDAFYSKKCKLFYKKDNEFKEKGVGTLHLKPTATQKTQLLVRADTNLGNILLNVLIAPNMPCTRTGKNNVLIVCVPNPPLDEKQPTLPATMLIRVKTSEDADELHKILLEKKDA | Component of the nuclear pore complex that has a direct role in nuclear protein import . Actively displaces NLSs from importin-alpha, and facilitates disassembly of the importin-alpha:beta-cargo complex and importin recycling . Interacts with regulatory proteins of cell cycle progression including CDKN1B . This interaction is required for correct intracellular transport and degradation of CDKN1B . | Q9JIH2 |
O58739 | SYY_PYRHO | Tyrosyl-tRNA synthetase | Pyrococcus | MDIEERINLVLKKPTEEVLTVENLRHLFEIGAPLQHYIGFEISGYIHLGTGLMAGAKIADFQKAGIKTRVFLADWHSWINDKLGGDLEVIQEVALKYFKVGMEKSIEVMGGDPKKVEFVLASEILEKGDYWQTVIDISKNVTLSRVMRSITIMGRQMGEAIDFAKLIYPMMQVADIFYQGVTIAHAGMDQRKAHVIAIEVAQKLRYHPIVHEGEKLKPVAVHHHLLLGLQEPPKWPIESEEEFKEIKAQMKMSKSKPYSAVFIHDSPEEIRQKLRKAFCPAREVRYNPVLDWVEYIIFREEPTEFTVHRPAKFGGDVTYTTFEELKRDFAEGKLHPLDLKNAVAEYLINLLEPIRRYFEKHPEPLELMRSVKITR | 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). | O58739 |
Q8CS66 | ACCD_STAES | Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta | Staphylococcus | MFKDFFNRSKKKKYLTVQDSKQNDVPAGIMTKCPKCKKIMYTKELNENLNVCFNCDHHIALTAYKRIEAISDEGSFIEFDRGMTSANPLDFPGYEEKIEKDQQKTGLNEALVSGTAKLDGIQYGVAVMDARFRMGSMGSVVGEKICRIIDYCTEHRLPFILFSASGGARMQEGIISLMQMGKTSVSLKRHSDAGLLYISYITNPTTGGVSASFASVGDINLSEPKALIGFAGRRVIEQTINEKLPDDFQTAEFLLEHGQLDKVIHRKDMRETLSNILKIHQEVSN | Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA. | Q8CS66 |
Q21389 | LGE1_CAEEL | Glycosyltransferase-like protein LARGE | Caenorhabditis | MQSNYSISYFLLILFTGTSSYFTIWNFVDHTRVGAFPEEDYIRLAYIIGGNFMTRLMFMQHFKSVLKYSDHFFRLHLITDENHRSDIHELMTSWNISNCEWFFHNLTEFEKRVAWIPNSHYSKYYGLSKLLIPEIIGNDIGKIMFMDVDIIFQTNIFDLWKQFRNFNNSQVFGMVENLSDWYLNKDGKKSVWPALGRGFNTGIIMFDLDKLRKNGWASKWRVVANKYLRIHGKTAMSDQDIFNAYIHDYPTEIIQIPCAYNYQLGALTKSKELCPETPLALHFNSQNKTVGKNYAFFDKIRKAFDEMDGSDLKRRRRSFKGNNQKDICHEYLPLDNFRIIPNAIGRMTKPAELCMVTQFSKDRLNHFLESANAWRHPISTAVYGKDKDLLDIAKAVTELNRTDITIHLVFEEPTESWMLDSLYPINFLRNVAIEHANCKYILMTDVDFVVLGDYGTIIDQTGNLKQKEVLVIPALEMTYPQLRLNLSNFLSRKDLVIEHLLNKTIQTFRETIWPSSHVPTNISKWIKSNRTYMVNYEKNYEPYFVIKKEECPFYDQRFGGFGWNKVTHVMQLKMMNYKFLVSPTSFMIHQNHNASKSLKRWRRDPHYQKCLHTLKNKFMKKTASRLGIKLR | Probable glycosyltransferase. | Q21389 |
Q5N1P5 | TIG_SYNP6 | PPIase | Synechococcus | MSIKVTQEKLPASRVGLQIEVSGEQSRQVYERTLTRLSREVRFPGFRPGKVPRPVLIQRLGETALKANAIEDLVQQSLESAIAQESIPAIGNYQLSSDFETLVAAFQPGKSFSFEASVDVQPTATLAQYTGLTVEVAEVPFDANRVDNVLAEQQKQMATLVPVEGRNAAIGDVAVIDFQGILVESGEEIPGGSGTDFQIEVEEDRFIPGFISGIVGMAIEETRTVDATFPETYAQEEVAGKAAQFTITLKELKTRDLPELDDAFAQEASQYETIEELKTALTERFQAEHESEVKASKRDAILTALADQLDVEIPESLLQREISAMINETASRLSGQGMDVRKLFTEEVLERLRENSKDEDEQRLRRTIALGELAKVTETQVDDEAVKARAAELLSNYPRPQEVDRDRLITVVREELLEDKLLEWFEANNSVTFVAPKAAETEVDAASATVETTATETAEEAPEAPKAKKGKKKA | Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase. | Q5N1P5 |
C8V4J7 | DBAC_EMENI | Derivative of benzaldehyde biosynthesis cluster protein C | Aspergillus subgen. Nidulantes | MAQLYDWLVETPANAEDLESRINTRPAHLEHNKPLIEAGTLVWGGPSLAAHPKAAGEDLAIVGSVMCIRAGSEEEVREMIRNDPYAKLGQVSIRMSVK | Part of the gene cluster that mediates the biosynthesis of the antibiotic 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA) and its derivatives . The direct non-reducing polyketide synthase dbaI product is 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA), produced by condensation of one acetyl-CoA starter unit with 4 malonyl-CoA units and one methylation step . The FAD-dependent monooxygenase dbaH is responsible for the synthesis of yellow pigments derived from the oxidation of DHMBA . The roles of dbaB, C, E and F have still to be determined (Probable). | C8V4J7 |
Q8XL16 | CBID_CLOPE | Cobalt-precorrin-6A synthase | Clostridium | MFDMYIESGGKKLRCGYTTGSCAAAAAKAATYMLFNKKDISVIEIDTPKNIKLNLEIQDIQVEKNSISCSIVKDGGDDIDATSGLEIFAKAEEVEEGFELCGGEGVGVVTKEGLFVEKGQPAINPVPREMIKKEVLSVLPKDKGVRITIFVPRGREIAKKTFNPRLGIVNGISILGTTGIVYPMSEEALKESIRIEIRQKAVNNKDLVFVFGNMGERFLRERGYKKDNIVVISNYVGFSIECALAQGIKDLTIVGHIGKLSKIAFGCFNTHSRVSDVRLEVIALELTLMGYDLELVQKVLDQKTSEGAVRLLGEDFPMLYERIGEKVLNRLDIYAYGEANFNILMYYGSKEMKLLYESKNSNLFD | Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A. | Q8XL16 |
Q1IS49 | ATP6_KORVE | F-ATPase subunit 6 | Candidatus Koribacter | MPHQLWFTAFLNQYLAGPVSAMMSVLHVPNPHPRAPISNYVAMEILVFLLLVLFFIATRISLSWDKPGVLQHIAEGMNNFVSNQGEEMIGHGYETYTSYIVTLGVFILSMNLIGLIPGFEAPTAFPSVPLGCALVTWFFYHVHGLRENGVIGYLKHFLGPVWWISPLLFVIEICSHFARIMSLTIRLYANMFAGDMVTLAFFSLVPLGFPVVFMGLHIFVSLIQTYIFITLAAVYLAEATAHGHD | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Q1IS49 |
P43666 | EPTB_SALTY | Phosphoethanolamine transferase EptB | Salmonella | MRYIKSMTQQKLSFLLALYIGLFMNCAVFYRRFGSYAQEFTIWKGLSAVVELGATVLVTFFLLRLLSLFGRRVWRVLATLVVLFSAGASYYMTFLNVVIGYGIIASVMTTDIDLSKEVVGLHFVLWLIAVSVLPLIFIWSNHCRYTLLRQLRTPGQRFRSAAVVVLAGVMVWAPIRLLDIQQKKVERATGIDLPSYGGVVANSYLPSNWLSALGLYAWAQVDESSDNNSLINPARKFTYVAPKDGDDTYVVFIIGETTRWDHMGIFGYERNTTPKLAQEKNLAAFRGYSCDTATKLSLRCMFVREGGADNNPQRTLKEQNVFAVLKQLGFSSDLYAMQSEMWFYSNTMADNISYREQIGAEPRNRGKTVDDMLLIDEMQNSLAQNPEGKHLIILHTKGSHFNYTQRYPRSYAQWKPECIGVDSGCTKAQMINSYDNSVTYVDHFITSVFDQLRDKKAIVFYAADHGESINEREHLHGTPRNMAPPEQFRVPMLVWMSDKYLASPQHAQMFAHLKQQAEIKVPRRHVELYDTIMGCLGYTSPNGGINQNNNWCHIPDVQKVAAK | Catalyzes the addition of a phosphoethanolamine (pEtN) moiety to the outer 3-deoxy-D-manno-octulosonic acid (Kdo) residue of a Kdo(2)-lipid A. Phosphatidylethanolamines with one unsaturated acyl group functions as pEtN donors and the reaction releases diacylglycerol. | P43666 |
A3QIM9 | RSMH_SHELP | rRNA (cytosine-N(4)-)-methyltransferase RsmH | Shewanella | MTQEFAHLSVLLTETVAGLNIKPEGIYIDGTFGRGGHSREVLKQLGPNGRLIAIDRDPQAIAAAEQFADDARFSIVHGGFGQLAQYVDDLGLRGKIDGILFDFGVSSPQLDDAERGFSFLRDGPLDMRMDNSQGETAAEWLARAEIEDMAWVFKTYGEEKNARHIARCIAADRDKTPFLRTKELADLIARVSKSKERNKHPATRVFQAIRIYINSELEQIDQALEGAVTVLAPQGRLSVISFHSLEDRMVKRFIRRHSQGESVPHGLPLTEAEINKTRLLKAVGKAIKPSAEEIDRNARARSSVLRVAERLDY | Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. | A3QIM9 |
A8FH04 | AMPA_BACP2 | Leucyl aminopeptidase | Bacillus | MFFSTNELQHKDTLAIGLFQKSQLSGKAKEMDELLEGRITELLKEGDISSKRNQLSKFFPSPETGIKRIYFVGLGKESDYTFEEAKEGFAHLFRKLHQDKKQAVSVLLDTFIGKDLPAQDAAHTLSESCLLATYELQDFKHKTNEPDRFIEFVYAMTDHDTTEIQASLKVGEVYGQSVNSARTLVNMPPNMLTSSDLASYAAELAYKYEFEIEILDKEQMEELGMGGILAVNRGSTEPPKLIVLKYQGKEEWTDVIGLVGKGITYDTGGYSLKPRASMIGMKTDMGGSASVLGAMEIIGELRPEQNVIAVIASTDNMISADAMKPDDVIVSLSGKTIEVLNTDAEGRLVLADGVTYAKQHGASVLIDVATLTGGVIVALGNETTGVMTNNDELYAQFKEASEECGEMIWQLPITEKDKKRVRNSKMADLNNSPGRDGHAIMAGAFIGEFAENTPWVHLDIAGTATTEKPSCFGPTGATGVMVRSLATFVERFEGKK | Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. | A8FH04 |
Q15QR7 | PYRG_PSEA6 | UTP--ammonia ligase | Pseudoalteromonas | MTNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTMLKLDPYINVDPGTMSPIQHGEVFVTDDGAETDLDLGHYERFIRTRMTKRNNFTTGRVYEEVIKRERRGDYLGATIQVIPHITNEIKRRIIAGAEGVDVAIVEIGGTVGDIESQPFLEAIRQLGTEVGRDHAMYMHLTLVPYIAVSGEVKTKPTQHSVKELRSIGIQPDILVCRSENALPSNERSKIALFTNVADKAVISLKDANSIYKIPAALKAQGMDELVVQRFGLECPEADLTEWEQVLYAESNPVGEVTIGMVGKYVELPDAYKSVNEALKHAGLKNRLTVNIRYVDSQDIESKGEQILHGLDAILVPGGFGERGIEGKIAAAKYAREQKVPYLGICLGMQVAIIEFARNVAGMESANSSEFDPQTPYPVVGLITEWLDADGSTAQRSEASDLGGTMRLGSQLCHLIPGSKVHDLYGSAEIYERHRHRYEVNNNLRDKLEASGLKVTGLSTDKRLVEVIELGDHPWFVAGQFHPEFNSTPRDGHPLFEGFVKAAGEYYKNNN | 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. | Q15QR7 |
B2U826 | PDXH_RALPJ | Pyridoxal 5'-phosphate synthase | Ralstonia | MTSIADIRTDYARASLDIADVDASPLRQFRRWFDEALKAEVAEVNAMTLATVDPHGQPSARIVLLKNLDERGFTFFTNYASHKGEELAANPRAALLFHWIGLERQVRVQGIVEKVSEAESDAYYHSRPLGSRLGAWASEQSSEVPDRATLEAREAEYRQRFGDAPPRPPHWGGYRLLPERLEFWQGRPSRLHDRLEYRKHADGSWTIVRLAP | Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). | B2U826 |
C0ZB50 | PRMA_BREBN | Ribosomal protein L11 methyltransferase | Brevibacillus | MKWSEISIHTTAEATEAVSSLLYELGANGVVIEDPEVLYREWDTPFGEIYQLSPDDFPAEGVFVKAYLPVDSSELLDVVEELKEQLAQLIEYGLDIGKASIAVNDVHEDEWAHAWKKYYKPVHVSDRMTIKPVWEEYVPKHPDEIIIEMDPGMAFGTGTHPTTILCLRALEKYMAKGDQVYDVGTGTAILSIAAIKLGAKDVLAMDLDEVAVRSAQANTELNGVHEHINVRQNNLLDGIEEQVEVVVANILAEVIVRFTDDVFRVLKPGGTFISSGIIAAREADVKAALVASGLEIVETIFIDDWVAIVAKKR | Methylates ribosomal protein L11. | C0ZB50 |
Q3K5Z2 | RS19_PSEPF | 30S ribosomal protein S19 | Pseudomonas | MPRSLKKGPFIDLHLLKKIEVAAEKNDRKPIKTWSRRSMILPQMVGLTIAVHNGRQHVPVLVNEDMVGHKLGEFAGTRNYRGHVADKKAKR | Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. | Q3K5Z2 |
Q1LX49 | DEN11_DANRE | Protein LCHN | Danio | MVEQSDRAPLLDWEEIPPAELAPSVPSPDTGDSLQSGLSSYPTEATLGADITLNTSPTRPSSVAAVHSPHKQHSGPGGDALAEEDEPGDCAFHGLSVRDRRITGWEEKDQIVAVFVVTFDTRSGNMIEWCLPHDVNLEGVEFKSMASGSHRISSDFIYFRKGCYFGLACFANMPVESELERGARMKSVGILSPSYTLLYRYMHFLENQVRHQLQCPGQYSPLEAFYEDKKAVLPSGGNGLVTACPTSALAPIVNRCMHPEMKITHPAGCMSQFIRFFGEQIMVLWKFALLRKRILIFSPPPVGVVCYRVYCCCCLANVSIPGMGVSVPEFRPFFYINVADIPALETELSYVACTTEKIFEEKKELYDVYIDNQNVKTHRESLQPLLRLNSADREKYRKLCEQRQLLLYSQEVDGDCTSNEEDLFILFFMEQNNRIFQTLSEVAVSADPTLTAEHVRAMGLDPQGDRGFLVDLLEIYGIDVMLVIDNPCCP | Probable guanine nucleotide exchange factor (GEF). May promote the exchange of GDP to GTP, converting inactive GDP-bound small GTPases into their active GTP-bound form. | Q1LX49 |
P81765 | POI_MUSDO | Phenoloxidase inhibitor | Musca | AVTDNEIVPQCLANGSKCYSHDVCCTKRCHNYAKKCVT | Potent reversible, competitive inhibitor of tyrosinase (phenol oxidase) in the nanomolar range. | P81765 |
Q3J0R1 | SYA_CERS4 | Alanyl-tRNA synthetase | Cereibacter | MPSLNDIRSTFLDYFRRNGHRVVESSPLVPRNDPTLMFTNSGMVQFKNCFTGLEHRDYTRATTAQKCVRAGGKHNDLDNVGYTARHHTFFEMLGNFSFGDYFKSDAIPFAWELLTKDFDIPKEKLLVTVYHTDDEAAEIWKKVAGLPDERIIRIPTNDNFWMMGPTGPCGPCTEIFFDHGPSIWGGPPGSADEDGDRFIEIWNLVFMQNEQHPDGSMTPLPKQSIDTGMGLERIGALLQGKHDNYDTDLMRSLIEASAHATSTDPDGPGKTHHRVIADHLRSTSFLIADGVMPSNEGRGYVLRRIMRRAMRHAHLLGAQDPVMHRLVPALVRQMGAAYPELTRGQALIEETLKLEETRFRQTLERGLRLLEDELGHLPEGSPLPGEAAFKLYDTYGFPLDLTQDALREKGRKVDVEGFEAAMAEQKAKARASWSGSGETKDAAIWFDLAETHGATEFLGYDTEQAEGQVLALVAAGAETASAGAGQTVQIILNQTPFYAESGGQVGDTGELRTDTGRARITDVKKGQGLFLHFAEVVEGEIRQGQGATLVVDHARRSAIRANHSATHLLHEALRRALGDHVAQRGSLNAPDRLRFDFSHSRALSPEELAAVEAEVNGFIRSNGAVETRIMSPDDARALGAQALFGEKYGDEVRVVSMGTLAGSGKGTDGQTYSLELCGGTHVSRLGDIGLCVILGDSASSAGVRRIEALTGEGALAYLNEQMKRLTDVAAALKAAPAELVDRVKALVEERRQLQNEVAQLRREAAMGGGAASEAKEIGGVKFLAQVVQGVPGKDMPGLIDEMKARVGSGAVLLISDTGGKAALAAGVTPDLTDRLSAVTLVKAAAEALGGRGGGGRPDMAQAGAADASQADAAIRAAEAVMGG | Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | Q3J0R1 |
Q90ZH8 | SX18A_XENLA | SRY (sex determining region Y)-box 18A | Xenopus | MHRSESSYCREETTLCQGVNSTWVPPADTVPEVSLIPSSPPAPDSPAPSPKPGYGFSTCEEKHGDPRIRRPMNAFMVWAKDERKRLAQQNPDLHNAVLSKMLGQSWKNLTSVEKRPFVEEAERLRVQHLQDHPNYKYRPRRKKQAKKLKRMDPSPLLRNEGFTRGQPMVNLSHFRNLHPLGGSGELESYGLPTPEMSPLDVLEPSEPAFFPPHMREDTDPVPFRTYQHGMDFSQEKTMREISLPYSSSPSHMGSFLRTPTPSAFYYKAHGGSPVCTPLGQLSPPPEAPALDAMDHLNQAELWGDFDRNEFDQYLNMSRTQRPGYSFPMSKLGAPRTIPCEENSLISALSDASTAMYYTPCITG | Probable transcription factor. Binds to the consensus DNA sequence 5'-AACAAT-3'. Also binds 5'-CACAAT-3' and 5'-AATAAT-3' with similar affinity. | Q90ZH8 |
Q6LN48 | SYP_PHOPR | Prolyl-tRNA synthetase | Photobacterium | MRTSNYLLSTLKETPNDAEVISHQLMLRAGMIRKLASGLYTWLPTGLRVLRKVENIVRQEIDNAGAVEILMPVVQPFELWEETGRSEKMGPELLRFTDRHSRPFVLSPTAEEVVTSLVRNEISSYKQLPLNLYQIQTKFRDERRPRFGVMRAREFSMMDAYSFDIDKEGLEKSYQAMHDAYCKAFDRMGLEYRPVLADSGAIGGSGSQEFHVLAESGEDLIAFSSDSDYAANIEKAEALAPTAELAAATQEMELVDTPNAKTIAELVEQHGLAIEKTVKTLFVKASDEIDADIVALIIRGDHELNEVKAENLPQVASPLEMAEEAEIRALIGAGPGSLGPVGLELPFIVDRTVAIMSDFGAGANVDGKHYFGINWGRDVELAQVEDLRNVVEGDLSPCGQGTIQLKRGIEVGHIFQLGTNYSKKMNCNVLGPDGKSATLEMGCYGIGVSRIVASAIEQNNDENGIIWPTALAPFQVAIVPMNMAKSEEVKAAAESLYAELTAAGIEVLFDDRKERPGVMFKDIELIGIPHTIVIGNRSLENGEMEYKDRRDGNKVAVPVADVVEMIKQKLA | Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS. | Q6LN48 |
B8ZSC6 | RPOC_MYCLB | Transcriptase subunit beta' | Mycobacterium | MLDVNFFDELRIGLATAEDIRQWSYGEVKKPETINYRTLKPEKDGLFCEKIFGPTRDWECYCGKYKRVRFKGIICERCGVEVTRAKVRRERMGHIELAAPVTHIWYFKGVPSRLGYLLDLAPKDLEKIIYFAAYVITTVDEEMRHNELSTLEAEMMVERKSVEDQRDADLEARAQKLEADLAALEAEGAKADARRKFRDGGEREMRQLRERAQRELDRLEDIWSTFTKLAPKQLIVDENLYRELVDRYGEYFTGAMGAESIQKLMQDFDIEAEAESLREVIRNGKGQKKLRALKRLKVVAAFQQSGNSPMGMVLDAVPVIPPELRPMVQLDGGRFATSDLNDLYRRVINRNNRLKRLIDLGAPDIIVNNEKRMLQESVDALFDNGRRGRPVTGPGNRPLKSLSDLLKGKQGRFRQNLLGKRVDYSGRSVIVVGPQLKLHQCGLPKLMALELFKPFVMKRLVDLNHAQNIKSAKRMVERQRPQVWDVLEEVIAEHPVLLNRAPTLHRLGIQAFEPMLVEGKAIQLHPLVCEAFNADFDGDQMAVHLPLSAEAQAEARILMLSSNNILSPASGRPLAMPRLDMVTGLYYLTTAVDGDTGAYRPAAEDRPESGVYSSPAEAIMAADRGVLSVRAKIKVQLTQVRPPADIEARWFGANGWRPGDPWIADTTLGRVMFNELLPLGYPFVNKQMHKKVQAAIINDLAERYPMIVVAQTVDKLKDAGFYWATRSGVTVSMADVLVPPRKKEILDHYEERADKVEKQFQRGALNHDERNEALVEIWKEATDEVGQALRDHYPVDNPIITIVDSGATGNFTQTRALAGMKGLVTNPKGEFIPRPVKSSFREGLTVLEYFINTHGARKGLADTALRTADSGYLTRRLVDVSQDVIVREHDCQTERGIVVELAVRVPDGSLIRELYIETSAYARTLGANAVDEAGNVIVARGEDLGDPEIDALLAAGITQVKVRSVLTCTTGTGVCATCYGRSMATGKLVDIGEAVGIVAAQSIGEPGTQLTMRTFHQGGVGEDITGGLPRVQELFEARVPRGKAPIADVTGRVRLEDGERFYKITIVPDDGGEEVVYDKLSKRQRLRVFKHADGSERVLSDGDYVEVGQQLMEGSADPHEVLRVQGPREVQIHLVREVQEVYRAQGVSIHDKHIEVIVRQMLRRVTIIDSGSTEFLPGSLIDRAEFESENRRVVAESGEPAAGRPVLMGITKASLATDSWLSAASFQETTRVLTDAAINCRSDKLNGLKENVIIGKLIPAGTGINRYRNIQVQPTEEARASAYTIPSYEDQYYSPDFGQATGAAVPLDDYGYSDYR | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | B8ZSC6 |
Q0SZ21 | METE_SHIF8 | Methionine synthase, vitamin-B12 independent isozyme | Shigella | MTILNHTLGFPRVGLRRELKKAQESYWAGNSTREELLTVGRELRARHWDQQKQAGIDLLPVGDFAWYDHVLTTSLLLGNVPPRHQNKDGSVDIDTLFRIGRGRAPTGEPAAAAEMTKWFNTNYHYMVPEFVKGQQFKLTWTQLLEEVDEALALSHNVKPVLLGPVTYLWLGKVKGEQFDRLSLLNDILPVYQQVLAELAKRGIEWVQIDEPALVLELPQAWLDAYKPAYDALQGQVKLLLTTYFEGVTPNLDTITALPVQGLHVDLVHGKDDVVELHKRLPSDWLLSAGLINGRNVWRADLTEKYAQIKDIVGKRDLWVASSCSLLHSPIDLSVETRLDAEVKSWFAFALQKCHELALLRDALNSGDTAALAEWSAPIQARRHSTRVHNPAVEKRLAAITAQDSQRANVYEVRAEAQRARFKLPAWPTTTIGSFPQTTEIRTLRLDFKKGNLDANNYRTGIAEHIKQAIVEQERLGLDVLVHGEAERNDMVEYFGEHLDGFVFTQNGWVQSYGSRCVKPPIVIGDISRPAPITVEWAKYAQSLTDKPVKGMLTGPVTILCWSFPREDVSRETIAKQIALALRDEVADLEAAGIGIIQIDEPALREGLPLRRSDWDAYLQWGVEAFRINAAVAKDDTQIHTHMCYCEFNDIMDSIAALDADVITIETSRSDMELLESFEEFDYPNEIGPGVYDIHSPNVPSVEWIEALLKKAAKRIPAERLWVNPDCGLKTRGWPETRAALANMVQAAQNLRRG | Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation. | Q0SZ21 |
A1S4C0 | RISB_SHEAM | 6,7-dimethyl-8-ribityllumazine synthase | Shewanella | MHIVEGHIEAKSAKVAIVVSRFNSFVVESLLSGAIDTLKRFGQVSEDNITVVRVPGAFELPLAAKKVAASGKFDGIIALGAVIRGGTPHFDFVAGECNKGLAQVSLEFNTPVSFGVLTTDTIEQAIERSGTKAGNKGGEAALGLLEMVNVLNAIDKEL | 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. | A1S4C0 |
A6MW01 | RK3_RHDSA | 50S ribosomal protein L3, chloroplastic | Rhodomonas | MIPGILGTKLGMTQIFDESGLAIPVTVIKAGPCILTQIKTQESDSYQAIQIGFSEVKESSLNKPLLGHLKKSQAPALKHLKEYRVKSVEGLEVAQKITLDSFEVGKTVSVSGKTIGKGFAGTVRRYSFTRGPMTHGSKNHREPGSIGQGSTPGKVHKGKKMAGRLGGKQSTIKNLEIVHVNTDNNILVVKGAVPGKKGNILSIQQEEI | One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. | A6MW01 |
Q8FU10 | RECR_COREF | Recombination protein RecR | Corynebacterium | MFEGPLQDLIDELSRLPGVGPKSAQRIAFHLLNVDPDDITRLQDALGAVRDGVRFCRICCNISRDEVCRICNDSGRDRGLICVVEEPKDIQVIERTGEFRGRYHVLGGALDPLANVGPRELTISTLLQRIGGVLDDRELADSTPDTPLLDDKPQIHEVILATDPNTEGEATASYLARLLQDFPDLVVSRLASGMPLGGDLEFVDELTLSRALSGRLPL | May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO. | Q8FU10 |
Q9G6G2 | CYB_OCHHY | Ubiquinol-cytochrome-c reductase complex cytochrome b subunit | Ochotona | MTNIRKNHPLMKIVNHSLIDLPTPSNISTWWNFGSLLGLCLVIQIITGLFLAMHYTSDTLTAFSSVTHICRDVNYGWIIRYLHANGASMFFICLFLHVGRGIYYGSYTYSETWNIGILLLFAVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTDLVQWIWGGFSVDKATLTRFFAFHFILPFIIAALVMVHLLFLHETGSNNPTGIISDADKIPFHPYYTVKDALGFLVLTTLLLTLVLFSPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSIAILAIMPLLHTSKQRSMMFRPISQTLFWILVADLLTLTWIGGQPVEHPFIIIGQLASFLYFFLILILMPTCSLIENKLLKW | Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis. | Q9G6G2 |
Q9ZKG4 | GUAA_HELPJ | Glutamine amidotransferase | Helicobacter | MILVLDFGSQYTQLIARRLRESGIYAEIVPFFESVENIQKKAPKGLILSGGPASVYAKDAYKPSEKIFDLNLPILGICYGMQYLVDFFGGVVAYANEQEFGKAILEIVQNSVIFEGVKIKSLVWMSHMDKVIELPKGFTTLAKSPNSPYCAIESDKIFGLQFHPEVIQSEEGGKILENFALLVCGCEKTWGMQHFAQREIVRLKEKIANAKVLCAVSGGVDSTVVATLLHRAIKDNLIAVFVDHGLLRKNEKEKVQAMFKDLQIPLNTIDAKEVFLSKLKGVSEPELKRKIIGETFIEVFEKEAKKHHLKGKIEFLAQGTLYPDVIESVSVKGPSKVIKTHHNVGGLPEWMDFKLIEPLRELFKDEVRLLGKELGVSQDFLMRHPFPGPGLAIRILGEINENKIKRLQEADAIFIEELKKANLYDKVWQAFCVLLNVNSVGVMGDNRTYENAICLRAVNASDGMTASFSFLEHSFLEKVSNRITNEVNGINRVVYDITSKPPGTIEWE | Catalyzes the synthesis of GMP from XMP. | Q9ZKG4 |
P0DJ63 | VKT_OXYMI | Kunitz-type serine protease inhibitor OMI | Oxyuranus | KDFCHLPPKPGPCRAAI | Serine protease inhibitor that inhibits plasma kallikrein (Ki=1.7 nM), and plasmin (Ki=33.0 nM). | P0DJ63 |
Q7WP62 | MODC_BORBR | Molybdenum import ATP-binding protein ModC | Bordetella | MPSDFPPGQAGIHARFRVDYPEFSLDVDLRLPGRGVTALFGQSGSGKTTCLRCMAGLAPVSDGYLDINGEVWLDSAARRAVPTHKRALGYVFQEASLFEHLDVLANLRYGMKRVPPALRRVDLEQATGLLGIGHLLARMPAGLSGGERQRVGIARALLTSPRLLLMDEPLAALDVQRKREILPYLERLHDELDIPVIYVSHSPDEVARLADHLVLLEQGRAVASGPLDALLTRLDLPMAMTDDASVVVTGEAAGFDPGYALLTLQLPGGRARLRFVHQAAPAGQRLRVVVHARDVSLALQQPREGSILNVLAVRVLEMAPAANPAHVMVRLDADGTPLLARITRYSRDRLALAPGMQAWAQIKAVSLLA | Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system. | Q7WP62 |
A5CUT3 | RL1_CLAM3 | 50S ribosomal protein L1 | Clavibacter | MAKSKAYRAAAEKIDPAKAYTASEAVELARETGSSKFDSTVEVALKLGVDPRKADQMVRGTVILPHGTGKTARVIVFATGPAAEAAIAAGADEVGGDELIEKVAGGYTSFDSAVSTPELMGKVGRLGKVLGPRGLMPNPKTGTVTPDVARAVSDIKGGKIEFRVDKHANVHFVVGKASFSPEQLSENVGAALEEIVRLKPSSSKGRYVQKATVSTTFGPGIPVDVNSI | Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA. | A5CUT3 |
Q5ZJ56 | RL7_CHICK | 60S ribosomal protein L7 | Gallus | MADKEAKKVPSVPESLLKRRQAYAAAKAKRLKRLLAQKKFRKAQRKIIYERAKAYHKEYRHMYRQEIRMARMARKAGNYYVPAEPKLAFVIRIRGINGVSPKVRKVLQLLRLRQIFNGTFVKLNKASINMLRIVEPYIAWGYPNLKSVHDLIYKRGYGKINKKRIALTDNSLIRKRLGKLGIICMEDVIHEIYTVGKNFKVVNNFLWPFKLSSPRGGMKKKTIHFVEGGDAGNREDQINRLIRRMN | Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. Binds to G-rich structures in 28S rRNA and in mRNAs. Plays a regulatory role in the translation apparatus; inhibits cell-free translation of mRNAs. | Q5ZJ56 |
A5EKH8 | NUSB_BRASB | Antitermination factor NusB | unclassified Bradyrhizobium | MAESSNKPFRGPVRANDRKANRRGAARLAAVQALYQMDIAGAGINDVLAEFESHWLGSEVEGEQYLPAEAAFFRDIVSGVVRDQTKIDPVLDTALERGWPLQRIEAILRAVLRAGAYELERRKDVPAKVVVSEYVDIAHAFVERDETGMVNAVLEQLARQYRADEMGPK | 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. | A5EKH8 |
O49339 | PTI12_ARATH | PTI1-like tyrosine-protein kinase 2 | Arabidopsis | MRRWICCGDKKGDSDLSNEEVHLKSPWQNSEANQKNQKPQAVVKPEAQKEALPIEVPPLSVDEVKEKTDNFGSKSLIGEGSYGRVYYATLNDGKAVALKKLDVAPEAETNTEFLNQVSMVSRLKHENLIQLVGYCVDENLRVLAYEFATMGSLHDILHGRKGVQGAQPGPTLDWLTRVKIAVEAARGLEYLHEKVQPPVIHRDIRSSNVLLFEDYQAKVADFNLSNQAPDNAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMPRGQQSLVTWATPRLSEDKVKQCVDPKLKGEYPPKSVAKLAAVAALCVQYESEFRPNMSIVVKALQPLLKPPAPAPAPVPES | Probable tyrosine-protein kinase involved in oxidative burst-mediated signaling leading to specific genes expression. | O49339 |
Q12289 | CRC1_YEAST | Mitochondrial carnitine carrier | Saccharomyces | MSSDTSLSESSLLKEESGSLTKSRPPIKSNPVRENIKSFVAGGVGGVCAVFTGHPFDLIKVRCQNGQANSTVHAITNIIKEAKTQVKGTLFTNSVKGFYKGVIPPLLGVTPIFAVSFWGYDVGKKLVTFNNKQGGSNELTMGQMAAAGFISAIPTTLVTAPTERVKVVLQTSSKGSFIQAAKTIVKEGGIASLFKGSLATLARDGPGSALYFASYEISKNYLNSRQPRQDAGKDEPVNILNVCLAGGIAGMSMWLAVFPIDTIKTKLQASSTRQNMLSATKEIYLQRGGIKGFFPGLGPALLRSFPANAATFLGVEMTHSLFKKYGI | Transports carnitine, acetylcarnitine, propionylcarnitine and to a much lower extent medium- and long-chain acylcarnitines. | Q12289 |
Q4WE86 | AGALB_ASPFU | Melibiase B | Aspergillus subgen. Fumigati | MTTFFSLTTAAAVLTLARGSNALVRPGNVGKLPALGWNTWNAFGCDIDATKIMTAANEVVNLGLKDLGYEYINIDDCWSVKSGRDASTQRIIPDPDKFPDGISGVADQIHDLGLKIGIYSSAGLTTCAGYPASLGYEDIDAQTFAEWGIDYLKYDNCGVPSNWTDTYTYCVPDPGSKATNGTCPDNKNPAPAGYDWRTSLTAERYRRMRDALVSVDRTILYSLCEWGQANVNDWGNETGNSWRTTGDITPSWPRIAAIANENSFLMNHVDFWGYPDPDMLEVGNGNLTLAENRAHFALWAAMKSPLIIGTALDSISQDHLAILSNKILLKFHQDPVIGRPAQPYKWGYNPDWTFDPAHPAEYWSGASSVLGGTLVLMLNSEDTTQRRTAVWKEVPELKDVLGRQGKRRIGFRVTDVWTGKDLGCVRDHYSVELESHDVAALVVGRAC | Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides. | Q4WE86 |
P38883 | RIX1_YEAST | Ribosomal export protein 1 | Saccharomyces | MSEEFIAVSTLARNLEIAKGNEFHTILATLRSPVYINEQLLKSELSFLVTKILKLIRSGNDFDLWKGCHTSVVTCAYNPLVLSTHGGQLLAAIYSRLEQKTGFYSSVISSSHGKQLFNTLISSVAIIIDLMKNKPTLSREALVPKLKAIIPTLITLSQYEPELVLPVLQRILKRNTTTFKPFTNKFRTVLINLIISDYASLGTKTQRLVCENFAYLHLLKIQVSDTSDDETQAHHKIYADSNWRTGLMSILSQFKPIIQLCGEILDFEQDNELYKLIKSLPVIDESNNKEEFLPSLKLDFNAPLTLWEIPQRLSLLADMLVAFISLPTPFPIRVPLGGINSLCEVLLGVSNKYLPLKKELRHDNELNGVINTILPQIQFQGIRLWEIMVSKYGKCGLSFFEGILSSIELFIPLKKKSNNEIDFNVVGSLKFEFATVFRLVNMILSHLGHQLNIISVISQLIEVALFLSHDKTLIDSLFKNRKSIMKQQTKTKQSKRSKSAEGAFSDIYTHPELFVCKNSMNWFNEINDFFITALNNWILPSTPHIQILKYSITQSLRLKERFGYIPESFVNLLRCEVLHPGSERVSILPIAISLLKNINDDMFELLCHPKVPVGMVYQLHKPLDLGEDGEVRDDINKKEVETNESSSNANTGLETLKALENLENVTIPEPKHEVPKVVDDTAIFKKRSVEEVIERESTSSHKKVKFVEETTVDNGEELIVKKAVSQTKEEEKPMEDSEDEEQEEFEIPAIELSDDEEEEEEEE | Component of the RIX1 complex required for processing of ITS2 sequences from 35S pre-rRNA and the nucleoplasmic transit of the pre-60S ribosomal subunits . Regulates pre-60S association of the critical remodeling factor MDN1 . | P38883 |
Q3ZBX9 | H2AJ_BOVIN | Histone H2A.J | Bos | MSGRGKQGGKVRAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKKTESQKTKSK | Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. | Q3ZBX9 |
O52594 | ACKA_ACET2 | Acetokinase | Acetivibrio | MNILVINTGSSSLKYQLIDMTNESVLAKGVCDRIGLEHSFLKHTKTGGETVVIEKDLYNHKLAIQEVISALTDEKIGVIKSMSEISAVGHRIVHGGEKFKESAIIDEDVMKAIRDCVELAPLHNPSNIIGIEACKQILPDVPMVAVFDTAFHQTMPRHAYIYALPYEIYEKYKLRKYGFHGTSHKYVAHRAAQMLGKPIESLKLITCHLGNGASICAVKGGKSVDTSMGFTPLQGLCMGTRSGNVDPAVITYLMEKEKMNINDINNFLNKKSGVLGISGVSSDFRDVQDAAEKGDDRAQLALDIFCYGVRKYIGKYIAVLNGVDAVVFTAGIGENNAYIRREVLKDMDFFGIKIDLDKNEVKGKEADISAPDAKVKTLVIPTNEELEIARETLRLVKNL | Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction. | O52594 |
P13783 | FLP_KLULC | Recombinase Flp protein | Kluyveromyces | MSTFAEAAHLTPHQCANEINEILESDTFNINAKEIRNKLASLFSILTMQSLSIRREMKINTYRSYKSAIGKSLSFDKDDKIIKFTVRLRKTESLQKDIESALPSYKVVVSPFKNQEVSLFDRYEETHKYDASMVGLQFTNILSKEKDIWKIVSRIACFFDQSCVTTTKRAEYRLLLLGAVGNCCRYSDLKNLDPRTFEIYNNSFLGPIVRATVTETKSRTERYVNFYPVNGDCDLLISLYDYLRVCSPIEKTVSSNRPTNQTHQFLPESLARTFSRFLTQHVDEPVFKIWNGPKSHFGRHLMATFLSRSEKGKYVSSLGNWAGDREIQSAVARSHYSHGSVTVDDRVFAFISGFYKEAPLGSEIYVLKDPSNKPLSREELLEEEGNSLGSPPLSPPSSPRLVAQSFSAHPSLQLFEQWHGIISDEVLQFIAEYRRKHELRSQRTVVA | Catalyzes the recombination between the large inverted repetitions of the plasmid. | P13783 |
B1KUY7 | PANB_CLOBM | Ketopantoate hydroxymethyltransferase | Clostridium | MRNTVSTFQELKNKGEKITMLTAYDYSMAKLIDSSGINGILVGDSLGMVCLGYENTLSVTMEDMLHHTKAVVRGTSNALVVGDMPFMSYQTSIYDAVYNAGRFIKEAGAHAVKLEGGATVAEEIKAIVKAQIPVMGHIGLTPQSVNMFGGFKVQGKNEKVAKKLIEDAKILEEAGAFAIVLECIPEKLSKIISESISIPTIGIGAGKYCDGQILVYQDMLSMFSDFKPKFVKSFGSIGESIKDGVSQYIKEVKEAKFPEEKHAFKIDDDVINKLY | Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. | B1KUY7 |
Q3B8N7 | T22D4_RAT | Thg-1pit | Rattus | MSGGKKKSSFQITSVTTDYEGPGSPGASDPPAPPAPAGPPPRLPNGEPNPDPGGRGTPRNGSPPPGAPASRFRVVKLPQGLGEPYRRGRWTCVDVYERDLEPPSFGRLLEGIRGASGGTGGRSLDSRLELASLGISTPIPQPGLSQGPTSWLRPPPTSPGPQARSFTGGLGQLAGPGKAKVETPPLSASPPQQRPPGPGTGDSAQTLPSLRVEVESGGLAAGTPPLSRRRDGAVRLRMELVAPEETGKVPPIDSRPNSPALYFDASLVHKSPDPFGAAAAQSLSLARSMLAISGHLDSDDDSGSGSLVGIDNKIEQAMDLVKSHLMFAVREEVEVLKEQIRDLAERNAALEQENGLLRALASPEQLAQLPSSGLPRLGPSAPNGPSI | Transcriptional repressor. | Q3B8N7 |
Q8D304 | PDXJ_WIGBR | Pyridoxine 5'-phosphate synthase | Wigglesworthia | MSKLLLGVNVDHVASLRNVRGGKFPDPVQLAILAEIAGADSITTHLREDNRHINEKDVICIKKSIQSRLNLEISTKKEMINKAINILPYSCCLVPENRQEITTESGIDVIKNKKYLKKVICKLKSLGIKVSLFVDPIKNQILSSSEINADCIEINTGKYSEQDKKENKEEINLIKLCAKYANKLGLEVHAGHGLNYFNVRSIVNIKEIKELNIGHSIISRSLIVGMQNAVKEMKDIIYSEKIKWQ | Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate. | Q8D304 |
Q94JJ7 | H2B3_ORYSJ | Histone H2B.3 | Oryza sativa | MAPKAEKKPAAKKPAEEEPAAEKAEKAPAGKKPKAEKRLPAGKAEKGSGEGRKAGRKKAKKSVETYKIYIFKVLKQVHPDIGISSKAMSIMNSFINDIFEKLAGESAKLARYNKKPTITSREIQTSVRLVLPGELAKHAVSEGTKAVTKFTSA | Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. | Q94JJ7 |
Q3AFE0 | Y272_CARHZ | Nucleotide-binding protein CHY_0272 | Carboxydothermus | MRFLIVTGLSGAGKTQAMRALEDLGYFCVDNLPPVLMPKFAELVAHAENKIEKVALVVDVRGQKFFQDLDWALGELTKLGIKYEILFLEARDEVLLKRFKANRRGHPLGVRGSQILDNIKKERKFLENLRARADKVIDTSDLQPADLRNEILNYYGEEQKRSKISINIVTFGYKYGLPLDADLIMDVRFLPNPFYVKELRPLSGSDKPVYDYVFNYEVTKKFTEKFLDLIEFLMPFYQKEGKSNLVIAIGCTGGRHRSVAIANFLARTLEEKNYEVYLRHRDLEKHREE | Displays ATPase and GTPase activities. | Q3AFE0 |
Q0SHT6 | LSPA_RHOJR | Signal peptidase II | Rhodococcus | MDDERVSQDPTAENETDAEDRNDDDPSGSAPPQPVTHQRRLLLFVIAGVVLATDLLTKILAVANIEPGRPVWLIGDIVSLRLVRNPGAAFSMATGMTWLLTLVAVGVVIGVVRIGRTLRSPWWALGLGLVLGGALGNLVDRFFRAPGVMQGHVVDFVSVGWWPVFNVADSGIVCGAILLVVLTLIGLEPDGTRKGVEK | This protein specifically catalyzes the removal of signal peptides from prolipoproteins. | Q0SHT6 |
F8J2E1 | 3L273_DRYCN | Long neurotoxin 73 | Drysdalia | MKTLLLTLVVVTIVCLDLGDSLICYQAYNTPQTCAPGENLCYTKTWCDYWCHVKGKRIDLGCAATCPTAKPGEDVTCCSRDKCNPHPLQRPR | 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. | F8J2E1 |
Q9SBQ7 | METK3_PETHY | Methionine adenosyltransferase 3 | Petunia | METFLFTSESVNEGHPDKLCDQISDAVLDACLEQDPESKVACETCTKTNLVMVFGEITTKANVDYEKIVRDTCRNIGFISDDVGLDADNCKVLVYIEQQSPDIAQGVHGHLTKQPEEIGAGDQGHMFGYATDETPEFMPLSHVLATKLGARLTEVRKNGTCPWLRPDGKTQVTVEYYNENGAMVPVRVHTVLISTQHDETVTNDEIAHDLKEHVIKPVIPEKYLDEKTIFHLNPSGRFVIGGPHGDAGLTGRKIIIDTYGGWGAHGGGAFSGKDPTKVDRSGAYIVRQAAKSVVANGLARRCIVQVSYAIGVPEPLSVFVDTYGTGMIPDKEILKIVKENFDFRPGMIAINLDLKRGGNGRFLKTAAYGHFGRDDTDFTWEVVKPLKCEKAQD | Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate. | Q9SBQ7 |
O46521 | CY24A_BOVIN | p22-phox | Bos | MGQIEWAMWANEQALASGLILITGGIVATAGQFTQWYLGAYSIAAGVLVCLLEYPRGKRSKGSTMERCGQKYLTRVVKLFGPLTRNYYIRAFLHLGLAVPAGFLLATILGTACLAIASGIYLLAAIRGEQWSPIEPKPKERPQIGGTIKQPPSNPPPRPPAEARKKPSEEAAGVPTGGPQENPMPVNDEVV | Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. Associates with NOX3 to form a functional NADPH oxidase constitutively generating superoxide. | O46521 |
P25490 | TYY1_HUMAN | Yin and yang 1 | Homo | MASGDTLYIATDGSEMPAEIVELHEIEVETIPVETIETTVVGEEEEEDDDDEDGGGGDHGGGGGHGHAGHHHHHHHHHHHPPMIALQPLVTDDPTQVHHHQEVILVQTREEVVGGDDSDGLRAEDGFEDQILIPVPAPAGGDDDYIEQTLVTVAAAGKSGGGGSSSSGGGRVKKGGGKKSGKKSYLSGGAGAAGGGGADPGNKKWEQKQVQIKTLEGEFSVTMWSSDEKKDIDHETVVEEQIIGENSPPDYSEYMTGKKLPPGGIPGIDLSDPKQLAEFARMKPRKIKEDDAPRTIACPHKGCTKMFRDNSAMRKHLHTHGPRVHVCAECGKAFVESSKLKRHQLVHTGEKPFQCTFEGCGKRFSLDFNLRTHVRIHTGDRPYVCPFDGCNKKFAQSTNLKSHILTHAKAKNNQ | Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair; proposed to target the INO80 complex to YY1-responsive elements. | P25490 |
Q41011 | EF1A_PEA | Elongation factor 1-alpha | Pisum | MGKEKVHINIVVIGHVDSGKSTTTVHVIYKLGGIDKRVIERFEKEADEMNKRSFKYAWLLDKLKAERERGITIDIALLKFETTKYYSTVMDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTPKYSKGRYEEIVKEVSSYLKEVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKGPTLLDALDNINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVVKPGMLVTFAPTGLTTEVKSVEMHHEALTEALPGDNVRFNVKNVAVKDLKHGLVASNSKDDPAKDAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAELITKIDRRSGKEIEKEPKFLKNGDAGMVKMIPTKPMVVETFAEYPPLGRFAVRDMRQTVAVGVIKSVEKKDPTGAKVTKAAAKKK | This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. | Q41011 |
A8FYR3 | RF3_SHESH | Peptide chain release factor 3 | Shewanella | MSGNKVEVDKRRTFAIISHPDAGKTTITEKVLLFGNALQKAGTVKGKKSGQHAKSDWMEMEKDRGISITTSVMQFPYNGALVNLLDTPGHEDFSEDTYRTLTAVDSCLMVIDSAKGVEQRTIKLMEVTRLRDTPIVTFMNKLDRDIRDPLELMDEVEKVLNIACAPITWPIGCGKEFKGVYHLLRDEVILYQSGQGHTIQDSTIIKGLDNPELDAAIGTYAAEVREELELVLGASNEFDLELFLAGELTPVYFGTALGNFGVDHILDGIVEWAPKPQARETEVREVQPEDEKFSGFVFKIQANMDPKHRDRVAFMRVCSGRYEQGMKMHHVRLGKDVNVSDALTFMAGDRNRAEVAYPGDIIGLHNHGTMRIGDTFTQGEKLRFTGIPNFAPEMFRRIRLKDPLKQKQLLKGLVQLSEEGAVQVFRPIDTNDLIVGAVGILQFEVVVGRLKSEYKVEAIYEAISVSTARWVYCDDERKLEEFRRKCSTNLALDGGDNLTYIAPTMVNLNLSMERYPDIKFAKTREN | Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP. | A8FYR3 |
B4PST7 | SOTI_DROYA | Male-specific protein scotti | Sophophora | MDTLLEHEAADLYDEQQIDRIGDAVTGDAGDDSDDTLEDGQQLLGVNRQMDILLDAPQEPPMAVFPARGGPNGGPPRLRKKRSFYTMVKPTPPCQSREPEMCRLMASVTRAMRQVREDQRGEYFANYLVENMTSQNYPNGVGLPQHWGQF | Post-meiotically transcribed gene that has a role in late spermiogenesis; required for actin cone progression during spermatid individualization. | B4PST7 |
Q2K6Q4 | ZNUC_RHIEC | Zinc import ATP-binding protein ZnuC | Rhizobium | MLSPANAKNQRLVSLEDVGVLRGGRWLVRGVEFSVSRGEIVTLIGPNGSGKSTSAKAAIGVLKPDEGRVERLSGLKVGYVPQKLSIDWTLPLTVRRLMTLTGPLPERDMQAALEAAGIAHMIGAEVQHLSGGEFQRALMARAIARKPDLLVLDEPVQGVDFSGEIALYHLIKSIRNASGCGILLISHDLHVVMAETDTVICLNGHVCCRGTPEAVSRSPEYVRLFGSRAAQTLAVYSHHHDHTHLPDGRVLHADGSVTDHCHPEDGHHAHDSQEHAHGQDHVHAHEHSHDDHHGHDHAHEHAHSRSGEGRHA | Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. | Q2K6Q4 |
Q9SWG0 | IVD_ARATH | Isovaleryl-CoA dehydrogenase, mitochondrial | Arabidopsis | MQRFFSARSILGYAVKTRRRSFSSRSSSLLFDDTQLQFKESVSKFAQDNIAPHAERIDKTNSFPKDVNLWKLMGEFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVALSYGAHSNLCINQLVRNGTAAQKEKYLPKLISGEHVGALAMSEPNAGSDVVGMKCKAEKVDGGYILNGNKMWCTNGPSAETLVVYAKTDTKAGSKGITAFIIEKGMTGFSTAQKLDKLGMRGSDTCELVFENCFVPEENILDKEGKGVYVLMSGLDLERLVLAAGPLGIMQACLDNVLPYIRQREQFGRPVGEFQFIQGKVADMYTALQSSRSYVYSVARDCDNGKVDPKDCAGTILCAAERATQVALQAIQCLGGNGYINEYATGRLLRDAKLYEIGAGTSEIRRIVIGRELFKEE | Involved in degradation of the branched-chain amino acids, phytol and lysine for the supply of carbon and electrons to the ETF/ETFQO complex during dark-induced sugar starvation. | Q9SWG0 |
C5BQA1 | FABA_TERTT | Trans-2-decenoyl-[acyl-carrier-protein] isomerase | Teredinibacter | MQDFVPNSSYTREELIACGNGELFGPGNAQLPVPNMLMLDRIAHISTTGGEYGKGEIIAELDIHKDLWFFGCHFPGDPVMPGCLGLDAMWQLVGFFLAWKGNPGRGRALGSGEVKFTGQILPTAKQVTYHIHLKRVIERKLIMGIADGRVAVDGKEIYFAKDLRVGLFSNTDTF | Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length. | C5BQA1 |
Q8LWM2 | CYB_URILO | Ubiquinol-cytochrome-c reductase complex cytochrome b subunit | Uria | MAPNLRKSHPLLKLINNSLIDLPTPSNISAWWNFGSLLGICLLTQILTGLLLATHYTADTTLAFSSVAHTCRNVQYGWLIRNLHANGASFFFICIYLHIGRGFYYGSYLNKETWNTGVILLLALMATAFVGYVLPWGQMSFWGATVITNLFSAIPYIGQTLVEWAWGGFSVDNPTLTRFFALHFLLPFMIAGLAFIHLTFLHESGSNNPLGILSNCDKIPFHPYFSLKDILGFIIMFLPLTTLALFSPNLLGDPENFTPANPLVTPPHIKPEWYFLFAYAILRSIPNKLGGVLALAASVLVLFLTPLLHKSKQRAMTFRPLSQLLFWTLVANLLILTWVGSQPVEHPFIIIGQLASLAYFTILLLLFPIVGALENKMLNY | Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis. | Q8LWM2 |
P48089 | IL1A_MACMU | Hematopoietin-1 | Macaca | MAKVPDMFEDLKNCYSENEEDSSSIDHLSLNQKSFYDVSYGPLHEGCMDQSVSLSISEISKTSKLTFKQSMVVVSTNGKVLKKRRLSLSQSITDNNLEAIANDSEEEIIKPRSAPFSFLSNMTYHFIRIIKHEFILNDTLNQTIIRANDQHLTAAAIHNLDEAVKFDMGAYTSSKDDTKVPVILRISKTQLYVSAQDEDQPVLLKEMPEINKTITGSETNFLFFWETHGTKNYFISVAHPNLFIATKHDNWVCLAKGLPSITDFQILENQA | Cytokine constitutively present intracellularly in nearly all resting non-hematopoietic cells that plays an important role in inflammation and bridges the innate and adaptive immune systems. After binding to its receptor IL1R1 together with its accessory protein IL1RAP, forms the high affinity interleukin-1 receptor complex. Signaling involves the recruitment of adapter molecules such as MYD88, IRAK1 or IRAK4. In turn, mediates the activation of NF-kappa-B and the three MAPK pathways p38, p42/p44 and JNK pathways. Within the cell, acts as an alarmin and cell death results in its liberation in the extracellular space after disruption of the cell membrane to induce inflammation and alert the host to injury or damage. In addition to its role as a danger signal, which occurs when the cytokine is passively released by cell necrosis, directly senses DNA damage and acts as signal for genotoxic stress without loss of cell integrity. | P48089 |
Q6LGK4 | GUAC_PHOPR | Guanosine 5'-monophosphate oxidoreductase | Photobacterium | MRIEQDLKLGFKDVLFRPKRSTLKSRSQVELTRDFTFKHSGRQWSGVPIIAANMDSVGSFEMAASLSKHNVMTAIHKHYTVDDWAGFVKNNDAAVLNNAMVSTGTSEADFQKTKDIMALTEDLIFICIDIANGYSEHLVEYVQKVRAEFPTKVISAGNVVTGDMVEELILAGADIVKVGIGPGSVCTTRVKTGVGYPQLSAIIECSDAAHGLGGRIIGDGGCSCAGDVSKAFGGGADFVMLGGMLAGHEESNGEVIEKDGEMFMKFYGMSSQSAMDKHSGGVANYRAAEGKTVLLPFRGPVENTIQDIMGGIRSTCTYVGAAQLKELTKRATFIRVQEQENNVYGKE | Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides. | Q6LGK4 |
A7FD14 | BTUB_YERP3 | Outer membrane cobalamin translocator | Yersinia | MTIKKYTLLTALSVTAFSGWAQGNNTTDNNNEMVVTANRFPQPKSSVLAPVDVVTRADIDRWQSTNINDVLRRLPGINIAQYGGPRQLSSLFIRGTNSSHVLVLVDGVRLNQAGISGSSDLSQIPISLVQRIEYIRGPRSAVYGSDAIGGVVNIITERETLGSTLTAGLGSNGYQNYNGSTQQKLGDDTTITLAGNYDYSKGYDVVAKGNTGMASQPDRDGYLGKMLWLGANHKFNEQFSGFVRGYGFDNRSDYDSYYYPGSPLVDTRSLSSRTYDTGINFSNGGYASQLIGSYSRTQDYNYDPSYGRYDQSATLDDISQYNLQWTNTYQLGLGNVGGGLDWQKQTTEPGTNYLSNGYEQRNTGVYGTVQQFVGPVTLEGAIRGDDNSQFGWHTTWQSSAGWEFVDGYRLIGSYGTAFKAPNLGQIYSSTYGNRDLKPEESTQWEAAITGITGPLDWRLSAYRNDIDQMIATRGVYPNSRYYNVEKATIKGVEWTGSFETGPLSHQVTLEYLDPRNADTHEILARRAKQQVKYQLDWQMADLDWSVTYQYIGQRYDSVFDPITYAASPVKLAGISLWDLAVSYPVTSHLTVRGRIANLFDKDYEMVYGYQTPGREYYFTGSYNF | Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans-periplasmic membrane protein TonB. | A7FD14 |
C1CV60 | SUCC_DEIDV | Succinyl-CoA synthetase subunit beta | Deinococcus | MKLHEYQGKEILRQFGVNVQDGKVARTPDEVRQIAREYGQPVVVKAQVHVGGRGKAGGVKFSPTEDKAFENGEKILGMDIKGLTVNKVLVTKAVDIDAGTEYYVGMIVDRNVQSFTLMASAEGGMEIEEVAAATPEKIIKHRVDPVTGLRPYEAREVAIRAGFKGNLNKIADMMVKMSEAALKRDAVLVEINPLFVGPDGVPLALDTKFEIDDNAMYRHQDLADWRELEAEHPLEIEASKYGFAYVKLDGNVGVLGNGAGIVMTSLDVVNRAGAKPANFLDIGGGAKAEVVYNAVKLVSKDSDVKAIFINIFGGITRADEVAKGVIQALKDGILTKPVRMRIAGTAEDEAKALLAEVNSPLIQMYPTMFEAADEAAKEANAAEAK | Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. | C1CV60 |
Q9Z255 | UBE2A_MOUSE | Ubiquitin-protein ligase A | Mus | MSTPARRRLMRDFKRLQEDPPAGVSGAPSENNIMVWNAVIFGPEGTPFEDGTFKLTIEFTEEYPNKPPTVRFVSKMFHPNVYADGSICLDILQNRWSPTYDVSSILTSIQSLLDEPNPNSPANSQAAQLYQENKREYEKRVSAIVEQSWRDC | Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In association with the E3 enzyme BRE1 (RNF20 and/or RNF40), it plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B at 'Lys-120' to form H2BK120ub1. H2BK120ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. In vitro catalyzes 'Lys-11', as well as 'Lys-48'-linked polyubiquitination. Required for postreplication repair of UV-damaged DNA. | Q9Z255 |
P95619 | CRTC_RUBGE | Neurosporene hydratase | Rubrivivax | MRAAESGADARVRPVDRVEPADAPAGDAGGLRAAVPGDGGSAVRPGDARLDVLVPPGLVDEPAAGALPGGGQRAPGAGRADGGDVRPVGGRDADGAPRFDQPVPPGGYLWWYVDAVSDDGRHGLTFIAFVGSVFSPYYAWAGGPKADRADPENHCALNIALYGDAGKRWTMTERGRRWMRRSRDEFVIGPSRLHWDGESLLVEFDEVGVPIPRRVKGRVRVWPKALCRFVTSLDSGGRHRWGPIAPCSRIEVELDSPRVRWSGHAYLDSNEGDEPIDRPFREWDWSRATMADSSTAVIYDVRQKRDGDRVIAERFLLDGSTESFEAPPRQPLPTTLWRIGRTMRTEPGVPALVEQTLEDTPFYARSMVRSGLLGEVVTSVHETMLLPRVITLPVRLMLPWRMPRRA | Involved in the biosynthesis of carotenoids spheroidene and spirilloxanthin. Catalyzes the hydration of neurosporene to the corresponding hydroxylated carotenoids 1-HO-neurosporene and 1,1'-(HO)2-neurosporene and that of lycopene to 1-HO-lycopene and 1,1'-(HO)2-lycopene. Can also act on demethylspheroidene, spheroidene, 1-HO-3,4-didehydrolycopene and geranylgeraniol. | P95619 |
Q02T64 | RL18_PSEAB | 50S ribosomal protein L18 | Pseudomonas | MSVKKETRLRRARKARLKMRELETVRLCVYRSSQHIYAQVIAADGGKVLASASTLDKDLREGATGNIDAAKKVGQLVAERAKAAGVTQVAFDRSGFKYHGRVKALADAAREGGLEF | This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. | Q02T64 |
Q9PC50 | RSMG_XYLFA | 16S rRNA 7-methylguanosine methyltransferase | Xylella | MNDSSLSPEVTADLEYGLDILELDRVYVVPLLAYLTLLIRWNRTYNLTAIRDPREMVVRHLLDSLAIQRYVTVGRLADLGSGPGLPGIPLAISCPSLQVTLVESNGKKARFLREVVRQLGLSNVGVSEVRAEALDEALTYEHLTARALDTLNGIVTVGGHLLKSEGTLLAMKGAYPHEEIAMLPPHWVVEAVHPLQVPKLTGKRHLVIVRKR | Specifically methylates the N7 position of guanine in position 527 of 16S rRNA. | Q9PC50 |
Q85PP8 | NU2M_GENSE | NADH dehydrogenase subunit 2 | Genetta | MKPPIFFLIMSTVISGTLIVMTSSHWMLTWIGFEMNMLAIIPILMKKFNPRSMEASTKYFLTQATASMLLMMGIIINLLYSGQWTVPNNPNPMASILMTTALAMKLGLAPFHFWVPEVTQGIPLSSGMILLTWQKIAPLSVLYQISPTINPNLLLPMATLSVLIGGWGGLNQTQLRKILAYSSIAHMGWMTAILLYNPTMMILNLTIYIIMTLTTFMLFMLNSTTTTLSLSQTWNKMPLITSLITMLMLSLGGLPPLSGFMPKWMIIQELTKNEMIIMPTFLAITALLNLYFYMRLTYATALTMFPSTNNMKMKWQFESTKKMTFLPPLIITSTMLLPLTPMISILD | 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. | Q85PP8 |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.