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 |
|---|---|---|---|---|---|---|
P75312 | Y472_MYCPN | DegV domain-containing protein MG326 homolog | Mycoplasma | MKTAIITDSTASIKEGEIQDVYVLPLQVIINGQDTYRDGKDIDYDRVYQLLKEHPQGLNISTSLPRQADLIELIEAIKDKYDRFVFLPLSKGLSGTYDMIVQAVKPLSTPKKEFVVLETSDIAISLKWLVQEVKALTDTNCPTKAIAEVVDQHKQSIFTAVTVKNLVQLRKGGRISGLKKIIATLLRVKPIIFFDKGVNTLSGKAFTFVQALEKIFTFVKSKFGDNFKIKRIGFCNAFTPVKAKEVKALILDFLHTNKITLQREIESSFITSAIIAHTGIDAFSISLLLDKNK | May bind long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism. | P75312 |
B4SZK4 | MOAA_SALNS | Molybdenum cofactor biosynthesis protein A | Salmonella | MASQLTDAFARKFYYLRLSITDVCNFRCTYCLPDGYKPGGVTNNGFLTVDEIRRVTRAFASLGTEKVRLTGGEPSLRRDFTDIIAAVGENDAIRQIAVTTNGYRLARDAANWREAGLTGVNVSVDSLDARQFHAITGQDKFRQVMAGIDAAFDAGFEKVKVNTVLMRDVNHHQLDTFLAWIQPRPIQLRFIELMETGEGSDLFRKHHISGQVLRDELIKRGWIHQLRQRSDGPAQVFCHPDYAGEIGLIMPYEKDFCATCNRLRVSSVGKLHLCLFGDGGVSLRDLLQDDAQQYALEERISDALREKKQTHFLHQSNTGI... | Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate. | B4SZK4 |
Q2NRZ6 | SSRP_SODGM | Small protein B | Sodalis | MTKKKEHKPGSATIAQNKRARHEYFIEQEFEAGLSLQGWEVKSLRAGKANIGDSYVLLKDGEAYLFGATFQPLTVASSHVVCDPMRTRKLLLNKRELDSLFGRVNREGYTVVALSLYWKNAWVKVKIGVAKGKKEYDKRTDIKEREWQLDKSRIMKHASR | 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 resemb... | Q2NRZ6 |
A5DID3 | EFG1P_PICGU | rRNA-processing protein EFG1 | Meyerozyma | MPKSVPSRQGSASADIYNSGSAKIKKKIRDIERLLKKDNVPANIRIDNERALKALKVELANKQQDHKTQKIAKKYHMVRFFERKKALRKLKQARKELQNVSETGERKDIKKARKVVRHCEIDVAYVVLFPKAEKYISLYPNHQPEKNPDTENAKKGLEKTESRRRELRKKVEKLVDDKALPFSIDDLLEGKSVDVKHDFESGHNQEIDAPETKIQEEDDFFE | Involved in rRNA processing. | A5DID3 |
Q8TC84 | FANK1_HUMAN | Fibronectin type 3 and ankyrin repeat domains protein 1 | Homo | MEPQKIMPPSKPHPPVVGKVTHHSIELYWDLEKKAKRQGPQEQWFRFSIEEEDPKMHTYGIIYTGYATKHVVEGLEPRTLYRFRLKVTSPSGECEYSPLVSVSTTREPISSEHLHRAVSVNDEDLLVRILQGGRVKVDVPNKFGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYLRRHGASWQARDLGGCTALHWAADGGHCSVIEWMIKDGCEVDVVDTGSGWTPLMRVSAVSGNQRVASLLIDAGANVNVKDRNGKTPLMVAVLNNHEELVQLLLDKGADASVKNEFGKGVLEMARV... | Through the activation of JUN and AP-1-mediated transcription, may regulate apoptosis. | Q8TC84 |
Q5L708 | RL5_CHLAB | 50S ribosomal protein L5 | Chlamydia | MSRLKKLYTEEIRKTLQEKFGYSNTMQIPVLKKIVISMGLAEAAKDKNLFQAHLDELSMISGQKPLVTKARNSIAGFKLREGQGIGAKVTLRGQRMYDFMDRFCHIVSPRIRDFRGFSSKGDGRGCYSLGLDDQQIFPEVDLDRVKRTQGMNITWVTTAQTDVECTTLLELMGLRFKKAQ | This is 1 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. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement... | Q5L708 |
Q92405 | CATB_ASPFU | Slow catalase | Aspergillus subgen. Fumigati | MRLTFIPSLIGVANAVCPYMTGELNRRDEISDGDAAAATEEFLSQYYLNDNDAFMTSDVGGPIEDQNSLSAGERGPTLLEDFIFRQKIQRFDHERVPERAVHARGAGAHGVFTSYGDFSNITAASFLAKEGKQTPVFVRFSTVAGSRGSSDLARDVHGFATRFYTDEGNFDIVGNNIPVFFIQDAILFPDLIHAVKPRGDNEIPQAATAHDSAWDFFSQQPSTMHTLLWAMSGHGIPRSFRHVDGFGVHTFRFVTDDGASKLVKFHWKSLQGKASMVWEEAQQTSGKNPDFMRQDLHDAIEAGRYPEWELGVQIMDEEDQ... | Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. | Q92405 |
A4W6F5 | APAH_ENT38 | Diadenosine tetraphosphatase | Enterobacter | MSTYLIGDVHGCYDELIALLKQVDFTPGQDTLWLTGDLVARGPGSLDVLRFVKSLGDSVRLVLGNHDLHLLAVFAGISRNKPKDRITPLLEAHDVDELINWLRRQPLLQIDEEKKLVMAHAGITPQWDLQTAKECARDVEAVLASDSYPFFLDAMYGDMPNNWSPELSGVARLRFVTNAFTRMRYCFPNGQLDMYCKDTPENAPSPLKPWFAIPGPVTNEYSVVFGHWASLEGKGTPENIYALDTGCCWGGDMTCLRWEDKAYFIQPSNRQLDLGEGEAAAS | Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. | A4W6F5 |
A9KWX0 | COAD_SHEB9 | Pantetheine-phosphate adenylyltransferase | Shewanella | MHTRAIYPGTFDPITNGHADLIERAAKLFKHVIIGIAANPSKQPRFTLEERVELVNRVTAHLDNVEVVGFSGLLVDFAKEQKASVLVRGLRAVSDFEYEFQLANMNRRLSPDLESVFLTPAEENSFISSTLVKEVALHGGDVSQFVHSEVATALAAKLKLAKP | Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. | A9KWX0 |
A9WWG0 | PURA_BRUSI | IMP--aspartate ligase | Brucella | MANVVVVGSQWGDEGKGKIVDWLSERADVIVRYQGGHNAGHTLVIDGVSYKLSLLPSGLVRGKLSVIGNGVVVDPHHFVAEVEKLRGQGIDVTPDVLRVAENAPLILSIHRELDAMREGSNSGLKIGTTKRGIGPAYEDKVGRRAIRVIDLTEPETLRPKVERLLAHHNSLRRGMGLEEIAVETILTELTSVADQILPYIDQVWRVLDERRKAGARILFEGAQGALLDNDHGTYPFVTSSNTVAGQAAAGSGLGPTAIGYVLGITKAYTTRVGEGPFPTELNDEIGEFLGTKGHEFGVVTGRKRRCGWFDAVIVRQTVRT... | Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. | A9WWG0 |
B8NJG9 | LEPE_ASPFN | Leporins biosynthesis protein E | Aspergillus subgen. Circumdati | MDGSSRPLPQTAQRKRRRPVLACDRCRRRKIRCDRKVPCSHCLRTGYASTCTYLANSNSSFPEEDLPGLDTTDPAMDMATSHPNHGHDRVPTDSGIGHSPPAQVEPIPSEGEMYGDFWDPLFVIHNTISTRKHRDPASTPASLGHVPRHTPAQAPTEVQVLIQRVRQLEQKVFSQQEPESSLAAPHIQQRHPQARRTVCQANLLGKSHWLVGFAQFDTIVHTLNNRLQDNDVEFRALFVKCQRLSRAIQQQYSLRASSLQALDGSLPSQEACDVCVNAYCRTFESVLRILHVPTFRQVYNEMWTGSQPTSRLFLLKLQLV... | Transcription factor involved in regulation of gene cluster 23 that mediates the biosynthesis of leporins . | B8NJG9 |
Q2NTZ1 | LOLA_SODGM | Outer-membrane lipoprotein carrier protein | Sodalis | MKKQLMTSCLFAAVLAAPAFAEDADVLQSRLNQVNSFHASFTQRVTGAEGGAVQEGEGELWIKRPNLFNWHMTTPDESVLVSDGKTLWFYNPFVEQAIANWLKNATGNTPFMLITRNSAADWGQYNVKQQGDSFSLVPKADNGNLKQFTINVTANGTITGFTAVEQDGQRSTYQLKSQKNGPVDDAKFHFTLPKGVTLDDQRQ | Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). | Q2NTZ1 |
A7GRM0 | SYI_BACCN | Isoleucyl-tRNA synthetase | Bacillus cereus group | MEYKNTLLMPKTEFPMRGNLPKREPAIQEKWAEMNIYEKVQERTKGRPLFVLHDGPPYANGDIHMGHALNKVLKDFIVRYKSMTGYCAPYVPGWDTHGLPIEQALTNKGVKRKEMPVAEFRKLCAEYAYEQVNRQREQFKRLGVRADWDHPYITLEPAYEAQQIKVFGEMAKKGYIYKGQKPVYWSPTSESALAEAEIEYKDKKSASIYVAFEVKDGKDVLEGDEKFIIWTTTPWTLPANLGISVHPKLEYSIVKVNDEKYIIASDLFDTVAKTLEWENPEVVRTVKGSELEYTVAKHPFYDRDSLVMLGEHVTTDAGTG... | Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrol... | A7GRM0 |
Q604V6 | FTSW_METCA | Peptidoglycan polymerase | Methylococcus | MSTQAIRGARGLVLKWGAGRFYLDTVLLSVSLGLMLFGFVMVSSASLHLGEKMASDSFYFPKHQLVHILLGLAAGWGAARVRLDTLERHSRSLFWAGIALLVLVLIPGVGKSVNGSVRWINLFGLRVQVSEVFKLVAAIYVAGYISRHLDTVRTSVKGMIFPLSLLAIGAVLLLKEPDFGATAVVMATALGMLFLAGARLWVFVGLLGLVAVAGTVLIYTAEYRLRRVLSFLDPWADPLNSGFQLTQALIAFGRGEWQGVGLGSSVQKLFYLPEAHTDFLFSVIGEELGLWGATTVILLFAIVVWRALAIGRLAERSGNL... | Peptidoglycan polymerase that is essential for cell division. | Q604V6 |
P49919 | CDN1C_MOUSE | p57Kip2 | Mus | MGMSDVYLRSRTAMERLASSDTFPVIARSSACRSLFGPVDHEELGRELRMRLAELNAEDQNRWDFNFQQDVPLRGPGRLQWMEVDSESVPAFYRETVQVGRCRLQLGPRPPPVAVAVIPRSGPPAGEAPDGLEEAPEQPPSAPASAVVAEPTPPATPAPASDLTSDPIPEVTLVATSDPTPDPIPDANPDVATRDGEEQVPEQVSEQGEESGAEPGDELGTEPVSEQGEEQGAEPVEEKDEEPEEEQGAEPVEEQGAEPVEEQNGEPVEEQDENQEQRGQELKDQPLSGIPGRPAPGTAAANANDFFAKRKRTAQENKAS... | Potent tight-binding inhibitor of several G1 cyclin/CDK complexes (cyclin E-CDK2, cyclin D2-CDK4, and cyclin A-CDK2) and, to lesser extent, of the mitotic cyclin B-CDC2. Negative regulator of cell proliferation. May play a role in maintenance of the non-proliferative state throughout life. | P49919 |
Q6R6L8 | FSHR_MESAU | Follitropin receptor | Mesocricetus | MALLLVSLLAFLGSGAGCHHWLCHCSDRVFLCQDSKVTEIPPDLPRNAIELRFVLTKLRVIPQGSFSGFKDLEKIEISQNDVLEVIEADVFSNLPKLHEIRIERANTLLYINPEAFQNLPNLRYLLISNTGIKHLPVVHKIQSLQKVLLDIQDNINLHTIARNSFMGLSFDSLILWLNKNGIQEIHNCAFNGTQLDELNLSDNNNLEELPNDVFRGASGPVILDISRTKVHSLPSHGLENLKKLRARSTYSLKKLPSLDKFVTLVEASLTYPSHCCAFANWRRQISELHPLCNKSVLRQDIDYVTQARDQNTSLIDDDLS... | G protein-coupled receptor for follitropin, the follicle-stimulating hormone. Through cAMP production activates the downstream PI3K-AKT and ERK1/ERK2 signaling pathways. | Q6R6L8 |
Q44777 | MURF_BORBU | UDP-MurNAc-pentapeptide synthetase | Borreliella | MRIKIKDILISSKDVKFVGNIKNIERVVSFYSLDSREIKDDNINDSLYFAYKGNKVDGFSFVKYLIDLGVKCFACSREHESECIKYLNDNEGLVFLLTSNVIKLLQALASFLIEKTSFKRIAITGSNGKTTTKEMLYSILSKKYKTYKTWGNLNSDIGLPLSILRVEGNEEYAVFEVGVSYVGEMDLLSQILKPEIVIITNISYAHMQAFKELQAIAFEKSKIIGKNIEIFVVNEMNDYCVYLEKRAKIANPNVKIVYFDFENLSIKSFSFLDGKFSFDFVYKGFEYSILLLGRHNIFNAIGCINLALFLGMREKEIKEG... | Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein. | Q44777 |
C3K605 | LPXD_PSEFS | UDP-3-O-acylglucosamine N-acyltransferase | Pseudomonas | MTATIKLGELAEFLGATLRGSPEKEITGLATLQEAGPAQLSFLANPQYRKYLVDSQAAAVLLKAADAEGFAGDALVVADPYLAYARVSHLFDPKPKAAAGVHPSAVIADDAQVDPAASIGAFAVVESGARIAAGVTVGAHCFIGARCEIGADGWLAPRVTLYHDVRIGERVVIQSGAVIGGEGFGFANAKGIWNKIAQVGGVLIGDDVEIGVNTAVDRGALADTVIGNGVKLDNQIQIAHNVQIGDHTAMAACVGISGSTKIGKHCMLAGGVGLVGHIDICDNVFITGMTMVTHSITEPGAYSSGTAMQPAAEWRKSAAR... | 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. | C3K605 |
O13220 | IHH_DEVPA | Indian hedgehog protein | Devario | VMNLWPGVRLRVTEGWDEDGHHSEESLHYEGRAVDITTSDRDRNKYAMLARLAVEAAF | Intercellular signal essential for a variety of patterning events during development. | O13220 |
Q12400 | TRM10_YEAST | tRNA(m1G9)-methyltransferase | Saccharomyces | MSNDEINQNEEKVKRTPPLPPVPEGMSKKQWKKMCKRQRWEENKAKYNAERRVKKKRLRHERSAKIQEYIDRGEEVPQELIREPRINVNQTDSGIEIILDCSFDELMNDKEIVSLSNQVTRAYSANRRANHFAEIKVAPFDKRLKQRFETTLKNTNYENWNHFKFLPDDKIMFGDEHISKDKIVYLTADTEEKLEKLEPGMRYIVGGIVDKNRYKELCLKKAQKMGIPTRRLPIDEYINLEGRRVLTTTHVVQLMLKYFDDHNWKNAFESVLPPRKLDAEAKSASSSPAPKDT | S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNAs. | Q12400 |
A2QX24 | ADAC_ASPNC | 2-acetyl-2-decarboxamidoanthrotainin biosynthesis cluster protein C | Aspergillus subgen. Circumdati | MTPPILIIGAGLSGLTVSRILTNASIPNIVFEASTPDRSQGYAISLRDWGYTSLLTALGDLPLRSLTRGVAPDRILGGTGWIDQALRDNHTGNLLVAPDPEAKQCIVRANRNALRTWIADSGDEEVDIRYGHRLRSVQGSMGNVTATFENGAKYQGSLVIAADGVHSSVRSQILPHVSPDIVPVVVYHGELELPRKEFDNLIRPHSGPSNILAGVGDGFNTPITVCNITPTHVHLDWSYSRPSTENKENKDPLYRPHVSAAEAKQIPPALLEEIASRDLARPWSQLLNAEALPTHRVFNWVSRCVSVTREDVNAAQKQGV... | FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the linear tetracyclic TAN-1612 neuropeptide Y receptor antagonist . The decaketide backbone of TAN-1612 is synthesized by the non-reducing polyketide synthase adaA via condensation of one acetyl-CoA starter unit with 9 malonyl-CoA ... | A2QX24 |
Q7FAE1 | MOMAS_ORYSJ | Momilactone A synthase | Oryza sativa | MAAGSSHVSADARKLVGKVAVITGGASGIGACTARLFVKHGARVVVADIQDELGASLVAELGPDASSYVHCDVTNEGDVAAAVDHAVARFGKLDVMFNNAGVSGPPCFRMSECTKEDFERVLAVNLVGPFLGTKHAARVMAPARRGSIISTASLSSSVSGAASHAYTTSKHALVGFTENAAGELGRHGIRVNCVSPAGVATPLARAAMGMDDEAIEAIMANSANLKGAGALKADDIAAAALFLASDDGRYVSGQNLRVDGGLSVVNSSFGFFRD | Involved in momilactone phytoalexins biosynthesis. Catalyzes the last step of momilactone A biosynthesis. | Q7FAE1 |
O13048 | NOD4A_XENLA | Xnr4 | Xenopus | MHLYFYCLILLFVPGGNSLGINSYLKHMSNKPQDHVNRTKTVDSKDLAALPLSSYMLNLYQSFHHSELNHGTEGAPSLPSNHRADIIRSLAAKSFDHGGSRWTLVFDFSSLSQEEEHQLAEVRFDFRAFEGAISAEMEVMVDFLHQSSSCQSISGWCQSYLYVGSLTGTLRSRSSDTWVTFEATDIIHKWFERNEKGKSRYEDREKQLKKLPRAKSAERRYQQQNTEDQQIVMMVYSNISKKERLSGTATLLQDAAHSKYLVVMPGIQTIAHTRRHRRSHIFKEHVMGMKHVPPADSSRTLCRRVDFFVDFKQIGWDSWI... | Cooperation and regulatory loops of multiple nodals are essential for mesendoderm patterning in early embryos. Plays a role in mesoderm formation and may be required for neural development. | O13048 |
Q98M73 | GLPK_RHILO | Glycerokinase | Mesorhizobium | MSGFVLAIDQGTTSTRAILFDGQMKVAGSGQKEFAQHYPASGWVEHDPEEIWASVVTTVKAALKNAGKAASDVAAIGITNQRETVVVWDRATGKPIHNAIVWQDRRTAPLCQKLKKQGLEKKFTRKTGLLLDPYFSGTKIAWILDKVKGGRKRAEKGELLAGTIDSFLIWRLTGGKVHATDATNASRTLVYNIAENAWDDELLAILNIPAKLLPQVKDCADDYGVTERDLFGAEIRILGVAGDQHAATIGQACFEPGMMKSTYGTGCFALLNTGSDLVRSKNRLLTTIAYRLNGKTTYALEGSIFIAGAAVQWLRDGIKV... | Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate. | Q98M73 |
P30079 | CHSY_PINSY | Naringenin-chalcone synthase | Pinus subgen. Pinus | MAAGMMKDLEAFRKAQRADGPATILAIGTATPPNAVDQSSYPDYYFKITNSEHMTELKEKFRRMCDKSAIKKRYMYLTEEILKENPKVCEYMAPSLDARQDMVVVEVPRLGKEAAAKAIKEWGQPKSKITHVIFCTTSGVDMPGADYQLTKLLGLRPSVKRVMMYQQGCFAGGTVLRVAKDLAENNRGARVLVVCSEITAVTFRGPSDTHLDSMVGQALFGDGAAALIVGADPVPEVEKPCFELMWTAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNIEKSLVEAFQQFGISDWNQLFWIAHPGGPAILDQVEA... | The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin. | P30079 |
B8ZYW0 | GLNK1_HALMT | Nitrogen regulatory protein GlnK1 | Haloferax | MSETETGNDGIKLVMAIIRPDKLADVKTALAEVGAPSLTVTNVSGRGSQPAKKGQWRGEEYTVDLHQKVKIECVVADIPAGDVVDAIAEAAHTGEKGDGKIFILPVEGAVQVRTGKEGSPAV | Involved in the regulation of nitrogen metabolism . Regulates the activity of its targets by protein-protein interaction in response to the nitrogen status of the cell . Increases the activity of the glutamine synthetase 3 in the presence of 2-oxoglutarate . May regulate the activity of the ammonia channel Amt1 via dir... | B8ZYW0 |
Q8R2H5 | PHLD_RAT | Glycosyl-phosphatidylinositol-specific phospholipase D | Rattus | MSVGRLWSGLLLLLLFFCSRSSSCGLSTHVEIGHRALQFLQLQDGRINYKELLLEHQDAYQAGTVFPDAFYPSICKQGKFHEVSESTHWTPFLNASIHYIRENYPLPWEKDTEKLVAFLFGVTSHMVADVSWHSLGIEQGFLRTMGAIDFYDSYSEAHSAGDFGGDVLSQFEFNFNYLSRRWYVPIQDLLRIYDNLYGRKVITKNVIVDCTYLQFLEMHGEMLAVSKLYSTYSTKSPFLVEQFQDYFLGGLDDMAFWSTNIYRLTSFMLENGTSDCNLPENPLFISCDGRKNHTLSSSKVQKNDFHRNLTMFISKDIRKN... | This protein hydrolyzes the inositol phosphate linkage in proteins anchored by phosphatidylinositol glycans (GPI-anchor) thus releasing these proteins from the membrane. | Q8R2H5 |
Q5L4T1 | SYT_CHLAB | Threonyl-tRNA synthetase | Chlamydia | MIRVICNNETYELPQGTTAADFASKIKNSHYFAGVVINDQIKDLSTTLNEGDTLRFVTFTDPEGREIFLHTSAHILAQAILRLWPDAIPTIGPVIDQGFYYDFANLSISEDDFLMIENMMGQIAEEKFAVQKKTFNSKHEALEEFARNPFKVELIKELPEGESITAYSQGEFMDLCRGPHLPSTGPVKAFKLLRTSAAYWRGDPQRESLVRIYGVAFPTTKELKEHLHQLKEAKKRDHRVLGMKLDLFSQQECSAGMPFFHPRGMIIWDALIGYWKRLHQLAGYKEIQTPQLMSRSLWEVSGHWSNYRENMYTLKIEDED... | Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr). | Q5L4T1 |
Q318K7 | RPOA_PROM9 | Transcriptase subunit alpha | Prochlorococcus | MQYQIERIDHQIADDRSQTGTFLIGPLERGQATTLGNSLRRVLMGGLEGSAVTAVRIAGINHEYATIPGVREDVLDILLNCKQLSINSSNPELEIGRLVASGPLDVKANDIQFSSQVEIVDGEKPIATIQEGHNLELEIHVERGVGYRPVDRKNQETTAIDLLQIDAVFMPVKRVNFSIDETAVAEGGTGRERLKMEVVTDGSTSPDDAIAEAANQLIELFQPLATVTMVEEIPEEPEPSPEAQIPLEELNLSVRAYNCLKRAQVNSVSDLMGFSYEDLLEIKNFGSKSADEVIEALERIGISIPQSRTSV | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | Q318K7 |
O04547 | CLE26_ARATH | CLE26p | Arabidopsis | MRNNHSLRLQLWFRTLFTVGVVTLLMIDAFVLQNNKEDDKTKEITTAVNMNNSDAKEIQQELEDGSRNDDLSYVASKRKVPRGPDPIHNRFLLLSRFILSLLTNPYPYLHICVLDVSV | Extracellular signal peptide that regulates cell fate. Represses root apical meristem maintenance. Regulates the transition of protophloem cells from proliferation to differentiation, thus impinging on postembryonic growth capacity of the root meristem; this signaling pathway requires CRN and CLV2 . | O04547 |
Q3YX22 | NANR_SHISS | HTH-type transcriptional repressor NanR | Shigella | MGLMNAFDSQTEDSSPAIGRNLRSRPLARKKLSEMVEEELEQMIRRREFGEGEQLPSERELMAFFNVGRPSVREALAALKRKGLVQINNGERARVSRPSADTIIGEFSGMAKDFLSHPGGIAHFEQLRLFFESSLVRYAAEHATDEQIDLLAKALEINSQSLDNNAAFIRSDVDFHRVLAEIPGNPIFMAIHVALLDWLIAARPTVADQALHEHNNVSYQQHIAIVDAIRRHDPDEADRALQSHLNSVSATWHAFGQTTNKKK | Transcriptional repressor that controls expression of the genes required for the catabolism of sialic acids. | Q3YX22 |
P9WJA6 | HIGA1_MYCTO | Antitoxin HigA1 | Mycobacterium tuberculosis complex | MSIDFPLGDDLAGYIAEAIAADPSFKGTLEDAEEARRLVDALIALRKHCQLSQVEVAKRMGVRQPTVSGFEKEPSDPKLSTLQRYARALDARLRLVLEVPTLREVPTWHRLSSYRGSARDHQVRVGADKEILMQTNWARHISVRQVEVA | Antitoxin component of an atypical, type II toxin-antitoxin chaperone (TAC) system. Probably neutralizes the toxic effects of cognate toxin HigB1, which also requires SecB-like chaperone MT2006 (AC Q7D7P7). Autorepresses its operon (higB1-higA1-MT2006). | P9WJA6 |
Q8P855 | HTPG_XANCP | High temperature protein G | Xanthomonas | MTVDTDKQTLGFQTEVKQLLQLMIHSLYSNKEIFLRELVSNAADAADKLRFEALVKPELLEGSGELRIRVDFDKEARTVTIDDNGIGMSREDAVSHLGTIAKSGTADFLKHLSGDQKKDANLIGQFGVGFYSAFIVADQVDVYSRRAGLPASDGVHWSSRGEGEFEVASVDKPERGTRIVLHLKDGEDSFADGWTLRNILKKYSDHIGLPIEMRKEHYGEDADKPAEPEWEVVNRASALWTRPKSEIKDEEYQEFYKHVAHDAGNPLAWSHNKVEGKLDYTSLLFVPGRAPFDLYHRDSAKGLKLYVQRVFIMDQAEQFL... | Molecular chaperone. Has ATPase activity. | Q8P855 |
A7GU98 | GLGA_BACCN | Starch [bacterial glycogen] synthase | Bacillus cereus group | MNILFAVSECVPFIKSGGLADVAGALPKELKKLGVNVRIMLPNYSLIPANLRESFKLHKVIHVPLGWRNQYCGILKGEQDGITYYLIDNEYYFKRDSLYGHYDDGERFSFFSKAILESIPYLDFEVDLIHSHDWHTAMVNFLLHEKYKDNPLYEKIKTVYTIHNLQFQGVFPREVIHDLLELGDEYFNSEQLEFYGNINFMKGGIIAADHITTVSSTYKEEIQYEFFGEKLDGLLRKYNDKLSGIVNGIDTSVYNPRLDSYITATYDVDTLYAKRENKWALQHYFGLPEKENTPIISMVTRLTKQKGLDLVRAVFQEIMQ... | Synthesizes alpha-1,4-glucan chains using ADP-glucose. | A7GU98 |
B1L8W7 | FMT_THESQ | Methionyl-tRNA formyltransferase | unclassified Thermotoga | MRIVFVGTPEFAAEILEHLIKNGFNVVGVVTQPDKPRGRGRKVEPTPVKVVAEKHRVPFIQPESINKKEALEFLRSVGPDVIIVASYGKILGEKVLSLPSLGCYNIHPSLLPKYRGASPIQRVLENGEERTGVTIYKMVRELDAGPIALQREISIDPFETFDQLEKRLIELSKEMSIEFLEKLKVGDIELKEQDHSRATYAPMIKKEDLIVDFSKDAESVKNKIRAYDSRPGARAFLGNDEVKLFGVTAIDSSGDEPGLIHYIDREGAWIGTGKGMVKVKYLQLPGKKKLTFWELRNGRLIEEGMKLEGRYES | Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. | B1L8W7 |
Q9CZG9 | PDZ11_MOUSE | PDZ domain-containing protein 11 | Mus | MDNRIPYDDYPVVFLPAYENPPAWIPPHERVYHPDYNNELTQFLPRIVTLKKPPGAQLGFNIRGGKASQLGIFISKVIPDSDAHRAGLQEGDQVLAVNDVDFQDIEHSKAVEILKTAREISMRVRFFPYNYHRQKERTVH | Mediates docking of ADAM10 to zonula adherens by interacting with PLEKHA7 which is required for PLEKHA7 to interact with the ADAM10-binding protein TSPAN33. | Q9CZG9 |
P40394 | ADH7_HUMAN | Retinol dehydrogenase | Homo | MFAEIQIQDKDRMGTAGKVIKCKAAVLWEQKQPFSIEEIEVAPPKTKEVRIKILATGICRTDDHVIKGTMVSKFPVIVGHEATGIVESIGEGVTTVKPGDKVIPLFLPQCRECNACRNPDGNLCIRSDITGRGVLADGTTRFTCKGKPVHHFMNTSTFTEYTVVDESSVAKIDDAAPPEKVCLIGCGFSTGYGAAVKTGKVKPGSTCVVFGLGGVGLSVIMGCKSAGASRIIGIDLNKDKFEKAMAVGATECISPKDSTKPISEVLSEMTGNNVGYTFEVIGHLETMIDALASCHMNYGTSVVVGVPPSAKMLTYDPMLL... | Catalyzes the NAD-dependent oxidation of all-trans-retinol, alcohol, and omega-hydroxy fatty acids and their derivatives . Oxidizes preferentially all trans-retinol, all-trans-4-hydroxyretinol, 9-cis-retinol, 2-hexenol, and long chain omega-hydroxy fatty acids such as juniperic acid . In vitro can also catalyzes the NA... | P40394 |
A9B2Z8 | GCS2_HERA2 | Gamma-glutamylcysteine synthetase 2 | Herpetosiphon | MEYRDPGHPHFPFTIGIEEEYQIIDPETRELKSYITQILDEGQLILREQMKPEMHQSIVEVGTHVCRTVEEARAEIIRLRGAIGSLAASKGLRIAAAGTHPFSSWQKQDIYPHERYYGVIEEMQEAARRLLIFGMHVHIGMPDNETCIEIMNVARYFLPHLLALSTSSPFWMGRKTGFQSYRSIIFTNFPRTGIPDTFQSYAEFEQYINILLKTHSIDNGKKVWWDARPHPMFGTLEVRICDIATKVDEAIMIAGLVQAIFVKIYSLFRQNQTFRVYSRALINENKWRAARYGMGGKLIDFGRREELSAHDLMAELREFV... | ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity. | A9B2Z8 |
Q34070 | CYB_CYSCR | Ubiquinol-cytochrome-c reductase complex cytochrome b subunit | Cystophora | MTNIRKTHPLMKIINNSFIDLPTPSNISAWWNFGSLLGICLILQILTGLFLAMHYTSDTTTAFSSVTHICRDVNYGWIIRYLHANGASMFFICLYMHVGRGLYYGSYTFTETWNIGIILLFTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGADLVEWIWGGFSVDKATLTRFFAFHFILPFVVSALATVHLLFLHETGSNNPSGITSDSDKIPFHPYYTIKDILGALLLILVLTLLVLFSPDLLGDPDNYTPANPLSTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSILILAIMPLLHTSKQRGMMFRPI... | 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... | Q34070 |
B0UWW2 | YQGF_HISS2 | Putative pre-16S rRNA nuclease | Histophilus | MSITVLAFDFGTKSIGCAVGQSITGTAQALPAFKAQDGIPDWLKIEKCLKDWQPNIVVVGLPLNMDGSEQDLTHLARKFANRLNGRFGVKVELQDERLTTKQARDEIFQRGGYRALKKEKVDSISACLILESWFENGACGE | Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. | B0UWW2 |
Q3SQW4 | DABA2_NITWN | Probable inorganic carbon transporter subunit DabA 2 | Nitrobacter | MVDALNLGRRLRVRSTAYVASELVPFFWPMRNFISRNPLRRLESMPFEQAVRRGAALFHARMFLPRGDYQRWRREGKVRPETLDEEIGRRSQDLPPVPGVDWPRWLHALMQTPHDRDAVVRGVRAKDVHAALRGHPPSAQAVDVAALLPELEQRLHARTLPEAVDALWGTGLADELDDLVIKSYLDFFDEDQSAWRMPGRERGLFSAWSEVTRRNARMVLRRLHVRHILDHVQDAESAVVYVMEEMGIGAEAWPTYFTRVLTRLHGWTGFVRWRASAKHYYWAQQYPADIVDLLAIRLVMGLALLQESARHRGTPMRRDD... | Part of an energy-coupled inorganic carbon pump. | Q3SQW4 |
J3SBP0 | SL9A_CROAD | C-type lectin 9a | Crotalus | MGRFIFVSFGLLVVFLSLSGTGADFDCPSGWSAYDQYCYKPFNEPQNWDDAERFCSEQAKGGHLVSIESDGEADFVAQLAQKIDKPDIYIWIGLRVQGKEQQCSSEWSDGSSIIYVNWNKGESQMCQGLTRWTNFLKWDYTDCQAKKPFVCKFPPEC | Interferes with one step of hemostasis (modulation of platelet aggregation, or coagulation cascade, for example). | J3SBP0 |
P21180 | CO2_MOUSE | Complement C2a fragment | Mus | MAPLLALFYLLQLGPGLAALFCNQNVNITGGNFTLSHGWAPGSLLIYSCPLGRYPSPAWRKCQSNGQWLTPRSSSHHTLRSSRMVKAVCKPVRCLAPSSFENGIYFPRLVSYPVGSNVSFECEQDFTLRGSPVRYCRPNGLWDGETAVCDNGASHCPNPGISVGTARTGLNFDLGDKVRYRCSSSNMVLTGSAERECQSNGVWSGSEPICRQPYSYDFPEDVASALDTSLTNLLGATNPTQNLLTKSLGRKIIIQRSGHLNLYLLLDASQSVTEKDFDIFKKSAELMVERIFSFEVNVSVAIITFASQPKTIMSILSERS... | Component C2 which is part of the classical pathway of the complement system is cleaved by activated factor C1 into two fragments: C2b and C2a. C2a, a serine protease, then combines with complement factor C4b to generate the C3 or C5 convertase. | P21180 |
G4NEB8 | MST7_MAGO7 | MEK MST7 | Pyricularia | MADPFAPRTMKRRNVKGLALTPAAPKPPPTAENAPIHRDSDQHAQLEIGIEFNLDLRPEDLEVIKDLGSGNGGTVSKVRHIPTNTVMARKVIHVEAKREMRKRIVRELQIMHSCNSEYIVTFYGAFLNENNDVIMCMEYADVGSLDRVSRVFGPIRVDVLGKIAEATLGGLTYLYAKHHIMHRDIKPSNILVNSRGSIKLCDFGVSGELINSIADTFVGTSTYMAPERIQGEKYTVKSDVWSFGLSIMELAIGKFPFAASEQLSDAESAPAGILDLLQQIVHEPAPKLPKSDAFPQILEDMIQKCLYKNPDDRPTPEELF... | Mitogen-activated protein kinase kinase; part of the MST11-MST7-PMK1 MAP kinase (MAPK) cascade that is essential for appressorium formation, penetration and invasive growth . The MST11-MST7-PMK1 MAP kinase cascade transduces signals from the cell surface sensors MDB2 and SHO1 that recognize various surface signals such... | G4NEB8 |
Q2J2K9 | MIAB_RHOP2 | tRNA-i(6)A37 methylthiotransferase | Rhodopseudomonas | MAPPRKLHIKSYGCQMNVYDAQRMVDVLAPEGFVETASVDDADLVILNTCHIREKASEKVFSELGRLRLARDEASRDGRRMQIVVAGCVAQAEGDEIVRRQPAVDVVVGPQSYHHLPRLLAQAAQTGRALETEFPIADKFGFLPQPQPEAIRARGISAFVTVQEGCDKFCTFCVVPYTRGAEVSRPVAAILADVERLADHGVRELTLIGQNVNAYHGDGPDGRPWTLGRLLQRLAAVPGIVRLRYSTSHPNDVDDDLIAAHRDLDALMPFVHLPVQSGSDRILAAMNRKHTAADYRRVIDRFRAVRPEIAFSSDFIVGFP... | Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | Q2J2K9 |
Q99383 | HRP1_YEAST | Heterogeneous nuclear ribonucleoprotein 1 | Saccharomyces | MSSDEEDFNDIYGDDKPTTTEEVKKEEEQNKAGSGTSQLDQLAALQALSSSLNKLNNPNSNNSSSNNSNQDTSSSKQDGTANDKEGSNEDTKNEKKQESATSANANANASSAGPSGLPWEQLQQTMSQFQQPSSQSPPQQQVTQTKEERSKADLSKESCKMFIGGLNWDTTEDNLREYFGKYGTVTDLKIMKDPATGRSRGFGFLSFEKPSSVDEVVKTQHILDGKVIDPKRAIPRDEQDKTGKIFVGGIGPDVRPKEFEEFFSQWGTIIDAQLMLDKDTGQSRGFGFVTYDSADAVDRVCQNKFIDFKDRKIEIKRAEP... | RNA-binding protein, which is involved in the polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with the cleavage factor CFIA complex and the cleavage and polyadenylation factor (CPF) complex. May be involved in regulation of poly(A) site selection. Is involved in nonsense-mediated mRNA decay. Seems to... | Q99383 |
W4VRU3 | ICK41_TRILK | Toxin ICK-41 | Trittame | MKPIVYMLLFCAFTVVILGHPNNHGALIPHHDKLPNGESCTRPGYSCSESSQCCTPVDGETFTYGCGRAWMEGSKICYICNRESSMC | Probable neurotoxin with ion channel impairing activity. | W4VRU3 |
P57716 | NICA_MOUSE | Nicastrin | Mus | MATTRGGSGPDPGSRGLLLLSFSVVLAGLCGGNSVERKIYIPLNKTAPCVRLLNATHQIGCQSSISGDTGVIHVVEKEEDLKWVLTDGPNPPYMVLLEGKLFTRDVMEKLKGTTSRIAGLAVTLAKPNSTSSFSPSVQCPNDGFGIYSNSYGPEFAHCKKTLWNELGNGLAYEDFSFPIFLLEDENETKVIKQCYQDHNLGQNGSAPSFPLCAMQLFSHMHAVISTATCMRRSFIQSTFSINPEIVCDPLSDYNVWSMLKPINTSVGLEPDVRVVVAATRLDSRSFFWNVAPGAESAVASFVTQLAAAEALHKAPDVTTL... | Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). The gamma-secretase complex plays a role in Notch and Wnt signaling cascades and regulation of downstream pr... | P57716 |
A5FV66 | PLSX_ACICJ | Phosphate-acyl-ACP acyltransferase | Acidiphilium | MPSPPPTPETATASDRTATPAPGMPILAVDAMGGDSAPGMVIAGLDIAAERHPNARFEVFGDAVQIDELVRLSKRLRNRVSIRPTTEIIPNELKPTAALRLRDASLRRAIDAVANGEAAGVISAGNTGAMLALAKIVLKTMSGIDRPAMAAIGPSARGDVVMLDLGANVVCDARNLVEFAVMGELFARTVLGLPHPTIGLLNVGSEEMKGDETLRRAAEALRESPIGPQFRGFIEGHDIAGGTVDVVVTDGFTGNVALKTGEGALRLVGDLLRRVFSANIASRLAYLLARPGLTRLREWLDPRRYNGAVLLGLNGVVVKS... | 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. | A5FV66 |
A0QJV7 | NUOK_MYCA1 | NDH-1 subunit K | Mycobacterium avium complex (MAC) | MNPINYLYLSALLFTIGAAGVLLRRNAIVMFMCVELMLNAVNLAFVTFARMHGHLDGQMIAFFTMVVAACEVVIGLAIIMTIFRTRKSASVDDANLLKG | 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 a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions ar... | A0QJV7 |
P57252 | NUOA_BUCAI | NUO1 | Buchnera | MLINTEAVNEYLSFFMFIFFSLGLCFFMLCLSWILGGRSSSRYKNTPFESGIVSSGNTNLYFSVKFYLIAMFFVVFDVEALYLYAWSVSIKESGWIGFSEALMFGISLLLGLFYLVRIRALNWSSSVKNNIQLF | NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are t... | P57252 |
Q606C1 | SYV_METCA | Valyl-tRNA synthetase | Methylococcus | MDKVYEPHAIEQRWYQHWEASGFFAPVGEGAPYCIMIPPPNVTGSLHMGHAFQDTVMDVLIRYHRMKGDRTLWQAGTDHAGIATQMVVERQLAGVGQTRHDLGREAFIERVWQWKETSGGTITRQLRRMGASLDWSRERFTLDEGLSRAVREVFVRLYEEGLIYRGKRLVNWDPVLHTAVSDLEVISEEEQGHLWHMRYPLADGSGHLVVATTRPETMLGDTAVAVHPEDERYRHLIGHSVRLPLTGREIPVIGDTYVDPEFGSGCVKITPAHDFNDYAIGVRHALPMISIFDQGAAILPRADIPAKYHGLDRYEARDLV... | Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner. | Q606C1 |
Q1QFS0 | RBL1C_NITHX | Ribulose bisphosphate carboxylase large chain 3 | Nitrobacter | MAVKTYQAGVTQYRQSYWQPDYVPLDTDILACFKITPQPGVDREEAAAAVAAESSCGTWTTVWTDLLTDLDYYKGRAYRLEDVPGDDTCYYAFIAYPIDLFEEGSVVNVFTSLVGNVFGFKAVRALRLEDLRFPIAYVKTCGGPPHGIQVERDRLNKYGRPMLGCTIKPKLGLSAKNYGRACYEALRGGLDFTKDDENINSQPFMRWRDRFDFVMEAVQKAEQETGERKGHYLNVTAPTPEEMYKRAEHAKEIGAPIIMHDYLAGGLCANAGLANWCRDNGILLHIHRAMHAVIDRNPHHGIHFRVLTKILRLSGGDHLH... | RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site. | Q1QFS0 |
A7H4Q6 | RL7_CAMJD | 50S ribosomal protein L7/L12 | Campylobacter | MAISKEDVLEYISNLSVLELSELVKEFEEKFGVSAVPVMVAGGAAAGGAAAAAEEKTEFDIVLTDGGAKKIEVIKIVRALTGLGLKEAKDAVEQTPSTLKEGVAKAEAEEAKKQLEEAGAKVELK | Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation. | A7H4Q6 |
P30278 | CCNB2_MEDSA | CycMs2 | Medicago | NSNEFGNFIAIDDELKLPEDQPEPMTLEHTEPMHSDPLEMEEVEMEDIEGEMILDIDSCDANNSLAVVEYIEDLHAYYRKIEYLGCVSPTYMDEQLDLNERMRAILVDWLIEVHDKFDLMQETLFLTVNLIDRFLAKQNVVRKKLQLVGLVAMLLACKYEEVSVPVVSDLIHIADRAYTRKDILEMEKLMLNTLQYNMSLPTAYVFMRRFLKAAQADKKLELVAFFLVDLSLVEYEMLKFPPSLVAAAAVYTAQCTVSGFKHWNKTCEWHTNYSEDQLLECSMLMVGFHQKAGAGKLTGVHRKYGSAKFSFTAKCEPACF... | Essential for the control of the cell cycle at the G2/M (mitosis) transition. | P30278 |
Q48DB7 | NRDR_PSE14 | Transcriptional repressor NrdR | Pseudomonas | MHCPFCGANDTKVIDSRLVAEGEQVRRRRECLACGERFTTFETAELVLPRLIKQDGSRQPFDEEKLRAGMQRALEKRPVSVERLEAALVHIKHKLRATGEREVKSLVVGELVMAELQKLDEVAYIRFASVYRRFQDLNEFREEIDRLAREPGKE | Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes. | Q48DB7 |
O47669 | COX2_CANAU | Cytochrome c oxidase polypeptide II | Canis | MAYPFQLGLQDATSPIMEELLHFHDHALMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETVWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLNFDSYMIPTQELKPGELRLLEVDNRVVLPMEMTIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMAMRPGLYYGQCSEICGSNHSFMPIVLEMVPLSYFETWSALMV | Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CII... | O47669 |
Q9CN12 | ACCD_PASMU | Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta | Pasteurella | MSWIDRIFNKDTSSTSSRKANVPEGVWTKCTSCEQVLYRDELRRHLEVCPKCGHHMRIDARERLLALLDKDSSQELSAELEPKDILKFKDLKKYKDRISAAQKETGEKDALISMFGTLYGMPIVAAASNFSFMGGSMGSVVGAKFVQAAEKAIAENCPFVCFSASGGARMQEALFSLMQMAKTSAVLAKMREQGVPFISVLTDPTLGGVSASFAMLGDINIAEPKALIGFAGPRVIEQTVREKLPEGFQRSEFLLEKGAIDMIVKRADMRHTLASVLSKLSNKPSPFVEPELVENEEQSKSDNE | 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. | Q9CN12 |
Q57233 | THIM_HAEIN | 4-methyl-5-beta-hydroxyethylthiazole kinase | Haemophilus | MLMQSIYLSKIREQNPLIHNITNIVAANFSANGLLALGASPLMSANVEEMQEVPKISQALVINIGTLIGKDREAMLQAGKTANEVGIPVVLDPVGVGATSYRRETIRELLAEVKFALIRGNAGELAAIAGETWQAKGVDAGQGEVDLKAVAEKVAQRYGCTVLISGAVDIVSDGTQTATVHNGTSLFPKVTASGCLLSAVCAAFLAVSEGNYFSATLEACVAYTIAGECAAQGLTTQVGQFQIRLLDELAALSPETIGQRGRINE | Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ). | Q57233 |
Q2RMH0 | RECR_MOOTA | Recombination protein RecR | Moorella | MYYPEPLNKLITALGRLPGIGPKTAQRLAFHLLKVPASEARDLAAAILEARQKTIYCSICGNFTDRDPCRLCSDPERDHSCICVVEEARDIIALEKTRQYRGLYHVLQGAISPVDGIGPEQLRVKELLARLHDGKVKEVILATNADVEGESTALYLDKLLKTLGVKVTRLAYGLPVGGDLEYADEVTLARAFAGRHELE | 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. | Q2RMH0 |
A4XBH2 | CH602_SALTO | Chaperonin-60 2 | Salinispora | MAKILSFSDDARHQLEHGVNALADAVKVTLGPRGRNVVLDKKFGAPTITNDGVTIAKEIELTDPHENLGAQLVKEVATKTNDVAGDGTTTATVLAQALVREGLRNVAAGANPTGLKRGIDAAATKVSEALLGKAVEVSDKAAIAHVATVSAQDSTIGELIAEAMERVGRDGVITVEEGSTLATELDVTEGLQFDKGFISPNFVTDAEGQESVLEDPYILITTQKISAIEELLPLLEKVLQDSKPLLIIAEDVEGQALSTLVVNALRKTMKVCAVKAPGFGDRRKAMLQDMAILTGAELVAPELGYKLDQVGLEVLGTARR... | Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. | A4XBH2 |
A4YCX6 | RL14_METS5 | 50S ribosomal protein L14 | Metallosphaera | MPEKMQVLGSRKGLTPAVQNYTMVNVSDNSGAKEAMIISVFGYRGALRRVPYANVGDLVMVSVRKGAPDVRKQKFKAVVIRQRMPFRRPDGTWISFDDNAVVIVNPDGTAKGTEIRGPVAREAAERWPKVASLATLIV | Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome. | A4YCX6 |
Q8DBE9 | LPXA_VIBVU | Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase | Vibrio | MIDATAQIHPTAVVEEGAVIGANVKIGPFCYVDSKVEIGEGTELLSHVVVKGPTKIGKENRIFQFASIGEQCQDLKYAGEDTQLVIGDRNTIRESVTMHRGTVQDKGITIVGSDNLFMINAHVAHDCVIGDRCIFANNATLAGHVKVGNQAIVGGMSAIHQFCHIGDHCMLGGGSIVVQDVPPYVMAQGNHCAPFGINVEGLKRRGFEKKEILAIRRAYKTLYRSGLTLEAAKEEIAKETEAFPAVKLFLEFLEKSQRGIIR | Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. | Q8DBE9 |
A7X1T8 | MUTL_STAA1 | DNA mismatch repair protein MutL | Staphylococcus | MGKIKELQTSLANKIAAGEVVERPSSVVKELLENAIDAGATEISIEVEESGVQSIRVVDNGSGIEAEDLGLVFHRHATSKLDQDEDLFHIRTLGFRGEALASISSVAKVTLKTCTDNANGNEIYVENGEILNHKPAKAKKGTDILVESLFYNTPARLKYIKSLYTELGKITDIVNRMAMSHPDIRIALISDGKTMLSTNGSGRTNEVMAEIYGMKVARDLVHISGDTSDYHIEGFVAKPEHSRSNKHYISIFINGRYIKNFMLNKAILEGYHTLLTIGRFPICYINIEMDPILVDVNVHPTKLEVRLSKEEQLYQLIVSK... | This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part ... | A7X1T8 |
Q19468 | MBOA7_CAEEL | Membrane-bound O-acyltransferase domain-containing protein 7 | Caenorhabditis | MENILGLMSKDDWIYTGLLLFSFGASCYVRKIGNNILASGALGFAMSLFIIGPKIVYSLGICSIAISIQLLANKKSTPLYVFLTTFTYLMFVRFAHYILPVNEVASHTNVIQLIITLRIIGITFEENDAWVHKSDENPTKRYLTELPTILEKFAYFYHFCGLFTGPYYTYQMLIDSQNPILKSWDPTLEVKSRFVRLLWSVPVFVITNHYFPLDILRSDAIWEVSFFTRLVYAALIFVVFKTRVYSAWAIAESICVILGIGIYPAASNPKIIMGPTDLNAFDKLKTRENIEMSSDAIVNLDIPKVEFSDGFRDGMKAWNR... | Acyltransferase which mediates the conversion of lysophosphatidylinositol (1-acyl-sn-glycero-3-phosphatidylinositol or LPI) into phosphatidylinositol (1,2-diacyl-sn-glycero-3-phosphoinositol or PI) (LPIAT activity). Prefers sn-2-LPI rather than sn-1-LPI as the acyl acceptor. Lysophospholipid acyltransferases (LPLATs) c... | Q19468 |
Q98BG9 | DNAA_RHILO | Chromosomal replication initiator protein DnaA | Mesorhizobium | MAVSSDAEQKFDRVKTQLKARLGAEVYSSWFGRMKVAEASKGIVRISVPTAFLRSWINGHYLDLISELWKQEDADLLKIEIVVRTATRQGRSHAEPELAPARKMTRQTQTALAAGTVSPGRVERPPVPRPGAAVESEFRHNVLGSPLDPRYTFGSFIEGPSNRVAFAAAKAVAESQSSAVRFNPLFLHATVGLGKTHLLQAIAAESLKQNPKSRVVYLTAEYFMWRFATAIRDNNALTLKEQLRDIDLLIIDDMQFLQGKSIQHEFCHLINMLLDSAKQVVVAADRPPSELESLEPRVRSRLNGGVALEMSAPDFAMRLG... | Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids. | Q98BG9 |
A0LSR8 | ILVD_ACIC1 | Dihydroxy-acid dehydratase | Acidothermus | MRAQPDLKPRSRDVTDGLERAAARGMLRAVGMTDADWEKPQIGVASSWNEITPCNLSLDRLAQAAKEGVHAAGGYPLEFATISVSDGISMGHEGMHFSLISREVIADSVETVFMAERFDGAVLLAGCDKSEPGMLMAAARLDLAAVFLYAGSTLPGKLGDRDINIVDAFEAVGGCLRGLVSREEVDAIERNFCPVEGACAGMFTANTMASAAEALGMSLPGSASPPAPDRRRDGFARASGEAVVNLLRRGITARDIMTREAFENAIAVVMALGGSTNAVLHLLAIAREANVDLAIDDFNRIGDRVPHLADVKPFGRYVMS... | Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (... | A0LSR8 |
Q9V1U4 | RNP1_PYRAB | Rpp29 | Pyrococcus | MRRNGKERKDRTSGGSQRPYQEIVGRTWIFRGSHRGRVTKRNIIWHELIGLKVRVVNSMHPGFVGIEGYVVDETRNMLVIVGDKVWKVPKDVCIFEFETEDGAKIKIPGERLVGRPEMRLKKRWRKW | Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. | Q9V1U4 |
Q4WLC8 | PYR8_ASPFU | Pyripyropene synthesis protein 8 | null | MDLVPSSTLWSIAQELALYLAFTVPTAFVIITTPKSSFLRLAWTPCLLYILYRFSLQVPSLTTSQFLNGVAAGQATVAALQCLNLLLITKLDERELVHAGLCIPSSSLLVRVACAWALLVNFRGIGTVWEVKNVPQHAAYLQKPKQHRLSRRRYVLRESAIIIWQYLLLDLIHMSTKDTPPGDLARLFGPGLEYRYLDATAEQWFGRVSVGIFSWLVPSRVCLNIVSRIYCLVLVVLRISAPESCRPSFGRVRDACTIRGFWGKFWHQSFRWPLTSVGSFVARDVLRLPRPSLLERYTNIFFTFFTSAVLHLACDAILGI... | Acetyltransferase; part of the gene cluster that mediates the biosynthesis of pyripyropene A, a specific human acyl-coenzyme A:cholesterol acyltransferase 2 inhibitor . The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase pyr1 . Nicotinyl-CoA is then a sub... | Q4WLC8 |
P53502 | ACT_FUCDI | Actin | Fucus | MADEDVQALVVDNGSGMCKAGFGDDAPRAVFPSIVGRPKHPGIMVGMDQKDAYVGDEAQSKRGVLTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEVPLNPKANKERMTQIMFETFNVLAMYVNIQAVLSLYASGSTTGCVLDSGDGVSHTVPIYEGYALPHAINRLDLAGRDLTDNLMKVLTERGYSFTTTREREIVRDIREKLTYVALDFDQEMKTAGESSQLEKSYELPDGNVIVIGNERFRCPEVLFQPSFIGMESSGIHDCTFKTIMKCDVDIRKDLYGNIVLSGGTTMFPGIGERMTKELTAL... | Essential component of cell cytoskeleton; plays an important role in cytoplasmic streaming, cell shape determination, cell division, organelle movement and extension growth. | P53502 |
Q08963 | RU2A_YEAST | Looks exceptionally like U2A protein 1 | Saccharomyces | MKFTPSIVIDAPQYYVDHFNGKYNVDKCVILRDLQLETDSESMPSSLKHLTKPTHILDLTNNDLIMIPDLSRRDDIHTLLLGRNNIVEVDGRLLPMNVQNLTLSNNSIRRFEDLQRLRRAPRTLKNLTLIGNQVCHLANYREHVLRLVPHLETLDFQNVTAEERKSAMSFPRQADGDTLGPVNTAIRDNGSRDKTMEIMNLVVSKMTVERRNELKKQLAEATSLEEIARLEKLLSGGV | Involved in pre-mRNA splicing. Associates to U2 snRNA in a MSL1 dependent manner and is required for normal accumulation of U2 snRNA. Required for the spliceosome assembly and the efficient addition of U2 snRNP onto the pre-mRNA. | Q08963 |
P29342 | RL7_STRAT | 50S ribosomal protein L7/L12 | Streptomyces | MALTQDELLAEFEGMTLIQLSEFVKAFEEKFDVTAAAAAPVVVAGGAAGGAAAEAEEEKDEFDVILTGAGDKKIQVIKVVRELTSLGLKEAKDLVDGTPKPVLEKVNKEAADKAAEALKGAGASVEVK | Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation. | P29342 |
B0UUZ6 | RL10_HISS2 | 50S ribosomal protein L10 | Histophilus | MALNLQDKQAIVAEVNEAAKGALSAVIADSRGVTVDKMTELRKAAREAGVSMRVVRNTLLRRAVEGTDFECLTDTFVGPTLIAFSNEHPGAAARLFKDFAKANDKFEIKGAAFEGKIQNVEFLATLPTYEEAIARLMGTMKEAAAGKLARTLAAYRDKLQEAA | Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. | B0UUZ6 |
Q8DZ90 | UVRC_STRA5 | Excinuclease ABC subunit C | Streptococcus | MNELIKHKLELLPDSPGCYLHKDKNGTIIYVGKAKNLKNRVKSYFHGSHNTKTELLVSEIEDFEYIVTTSNTEALLLEINLIQENMPKYNIRLKDDKSYPYIKITNERYPRLMITRQVKKSDGTYFGPYPDSGAATEIKRLLDRLFPFKKCTNPANKVCFYYHLGQCNAHTVCQTNKAYWDSLREDVKQFLNGKDNKIVNGLTEKMKSAAMTMEFERAAEYRDLIEAISLLRTKQRVIHQDMKDRDVFGYFVDKGWMCVQVFFVRNGKLIQRDVNMFPYYNEPEEDFLTYIGQFYQDTKHFLPKEVFIPQDIDAKSVETI... | 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. | Q8DZ90 |
Q5E2K7 | CCA_ALIF1 | Phosphatase | Aliivibrio | MKIYLVGGAVRDSLLNIDVKDKDWVVVGSTPQKMDSLGYQTVGQDFPVFLNPKTKEEYALARTERKSGQGYKGFTCYAEPDVTLEEDLLRRDLTINAIAQADNGELIDPYNGQQDIIDRTLRHVSDAFTEDPLRVLRVARFAARFHHLGFTVAPETMHLMKVLVDSGELSHLTAERVWQEWQKSLSSQHPEIFLSTLKECGALAIVLPELNALFGIPQPEKWHPEIDTGIHTLMVAQQAALLSQDLPTRFAAQVHDLGKGVTPESEWPSHKLHCHTGIKLIKRLCDRVRVPNDYRDLALLVCEHHSNIHRAAELRAQTFI... | Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows phosphatase, 2'-nucleotidase a... | Q5E2K7 |
Q3JZ96 | DLTC_STRA1 | D-alanine--poly(phosphoribitol) ligase subunit 2 | Streptococcus | MDIKSEVLAIIDDLFMEDVSSMMDEDLFDAGVLDSMGTVELIVELESHFNIDIPIAEFGRNDWNTANKIVAGVTELCNA | Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC-carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester bond, proba... | Q3JZ96 |
A2C8D6 | TRHO_PROM3 | tRNA hydroxylation protein O | Prochlorococcus | MNLQDDQTSADLFQVATFYSFTAWPEVTITCLLQDLLSLGDEHQLMGTVLLAEEGVNGTICGSVDGVSALLERLERDLIEGLFELKISWTPEQAFRRFKVRRKAEIVTMGLAGLNPSKTVGTYVDAHEWNDLIDDPDTLLIDTRNDYEIAIGEFKGAINPQTKCFRDFPAWVEQQLRSMVKAKTSARIAMYCTGGIRCEKATSYLIEKGFTNVHHLRGGILRYFEEVSQSESRWQGECFVFDQRVALNHQLSPGVYRLCHACGMPLTPEDQAMNSYRTGVQCRHCVDQFSDTDRIRFAERQRQMEHSSRK | Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs. | A2C8D6 |
Q8ZTA5 | RL7A_PYRAE | Ribosomal protein L8e | Pyrobaculum | MAVTIDPKTFYANPPPGKPFYVRFEVPNDVAEKALEILSIARQTGKIKKGTNETTKAVERGLAKLVLIAEDVDPPEVVAHLPLLCEEKKVPYVYVPSKEKLGKAAGINVSAAAAVVIEPGQAAGELEALVSKINEVRAKHGLNAIPVPAKR | Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, the RNA component of RNase P, box H/ACA, box C/D and box C'/D' sRNAs. | Q8ZTA5 |
Q04L26 | PEPX_STRP2 | X-prolyl-dipeptidyl aminopeptidase | Streptococcus | MRFNQYSYINFPKENVLSELKKCGFDLQNTANHKDSLETFLRRFFFTYQDTNYPLSILAADKKTDLLTFFQSEDELTADIFYTVAFQLLGFSYLVDFEDSDVFRKETGFPIIYGDLIENLYQLLNTRTKKGNTLIDQLVSDGLIPEDNDYHYFNGKSLATFSNQDVIREVVYVESRVDTDQKGLSDLVKVSIIRPRFDGKIPAIMTASPYHQGTNDKASDKALYKMEGELEVKLPHKIELEKPQLNLVQPQGKAELIAEAEEKLTHINSSYTLNDYFLPRGFANLYVSGVGTKDSTGFMTNGDYQQIEAYKNVIDWLNGR... | Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. | Q04L26 |
Q7NA79 | RBSA_PHOLL | Ribose import ATP-binding protein RbsA | Photorhabdus | MQPVLELKGISKSFPGVKALSGAALRVYPGKVMALVGENGAGKSTMMKVLTGIYTRDTGTVHYLGKEVIFSGPRSSQEAGIGIIHQELNLIPQLTIAENIFLGREFVNKFGAIDWRKMYQEADRLLKKLNLSYSSHRLVAELSIGDQQMVEIAKVLSFKSKVIIMDEPTDALTDTETESLFRVIYELKSQRCGIVYISHRLREIFEICDDVTVFRDGQFIGEKSVKELKEETLIEMMVGRKLEDQYPRLNLPRGKKRLEVKQISGPGVTNASFSLYSGEILGISGLMGAGRTELMKIIYGALPKTQGQITLDGTPIVIRN... | Part of the ABC transporter complex RbsABC involved in ribose import. Responsible for energy coupling to the transport system. | Q7NA79 |
Q83GK0 | RUVA_TROWT | Holliday junction ATP-dependent DNA helicase RuvA | Tropheryma | MIASLSGLLEAVRPGSVVVNMHGIGFLVRVPQSFNPEVDAEVKLYTSLQVREDSVSLYGFASVLECTVFEQLITISGVGPRVALAILSVLTPAEVAAAVLEGDDKPLQRVSGVGKKLAGTIVLQLAGKLTSVPLENRKQEQAVDRSAEIVQALIGLGWQRQESAAAVESVLEKDQSLTMPEILRNALRYLAKQE | The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA... | Q83GK0 |
Q03IG4 | RS14Z_STRTD | 30S ribosomal protein S14 type Z | Streptococcus | MAKKSLIAKNKRPAKFSTQAYTRCERCGRPHSVYRKFKLCRVCFRQLAHRGQIPGVTKASW | Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site. | Q03IG4 |
A7FD00 | ARGB_YERP3 | NAG kinase | Yersinia | MMNPLVIKLGGVLLDSEEALERLFTALVTYREKHERPLVIMHGGGCLVDELMKRLALPVVKKNGLRVTPADQIDIITGALAGTANKTLLAWAVKHQINAVGLCLADGNTVTVTLLDAELGHVGKAQPGSAALVQTLLAAGYMPIISSIGITVEGQLMNVNADQAATALAATLGADLILLSDVSGILDGKGQRIAEMTAQKAEQLIAQGIITDGMVVKVNAALDAARSLGRPVDIASWRHSEQLPALFNGVPIGTRISV | Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. | A7FD00 |
P53614 | SAA1_RABIT | Serum amyloid A-1 protein | Oryctolagus | MKLLSGLLLCSLVLGVSSQRWFSFIGEATQGAWDMWRAYSDMREANYINADKYFHARGNYDAAQRGPGGVWAAKVISDAREDLQRLMGHGAEDSMADQAANEWGRSGKDPNHFRPKGLPDKY | Major acute phase protein. | P53614 |
Q9ZWB7 | PCS2_ARATH | Phytochelatin synthase 2 | Arabidopsis | MSMASLYRRSLSPPAIDFASFEGKQIFNEALQKGTMEGFFGLISYFQTQSEPAFCGLASLSMVLNSLSIDPGRKWKGPWRWFDESMLECCEPLEIVKDKGISFGKVVCLAHSSGAKVEAFRTNQSTIDDFRKYVVKCSTSDNCHMISTYHRQVLKQTGTGHFSPIGGYNAERDMALILDVARFKYPPHWVPLKLLWDAMDSIDQSTGRRRGFMLISRPHREPGLLYTLSCKDESWISIAKYLKEDVPRLVSSQHVDTIERILYVVFKSLPANFNQFIKWMAEIRRTEDVNQNLSSEEKSRLKLKQELLKQVQETKLFKHV... | Involved in the synthesis of phytochelatins (PC) and homophytochelatins (hPC), the heavy-metal-binding peptides of plants. | Q9ZWB7 |
A6UNU0 | AROE_METVS | Shikimate dehydrogenase (NADP(+)) | Methanococcus | MIDSKTVLLGLIGHPVEHSFSPIMHNAAINDLKINYVYLGFDISNENLKNVVNSAKTLSILGFNVTIPYKVEIMKYLDKIDDTAKFIGAVNTVKIENGEAVGYNTDGIGAKKSLEEEIGKFNNKNILMIGSGGSSRSISFELAKENEITIINRNIKNAKELSFEISKNLATKEYGEKYLKYGDLSTDISKFDIIINTTPVGMYPDVNSKPVIPLKNAKNDAIIMDIIYNPFEPVFLKEAKKYGLKTLNGLGMLIYQGAVSFEIWTGFKPDTNVMKNSIVNLLKS | 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). | A6UNU0 |
P23309 | RS3_GEOSE | BS3/BS4 | Geobacillus | MGQKVNPIGLRIGIIRDWESRWYAEKDYADLVHEDLKIREYINKRLQDAAVSRVEIERAANRVNVTIHTAKPGMVIGKGGSEVEALRKALTQLTGKREHINIVEIKKPDLDAKLVAENIARQLENRVSFRRAQKQAIQRAMRPGRKGVKTMVVRRLGGAEIARSEHYSEGTVPLHTLRADIDYATAEADTTYGKIGVKVWIYRGEVLPTKKKAEEGGK | Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation. | P23309 |
A7GJ15 | GLMM_CLOBL | Phosphoglucosamine mutase | Clostridium | MGRMFGTDGVRGVANKELTADLAYKLGKAGAFILTEGTHRPKILVGMDTRISGDMLESALVAGILSVGAEAICVGVIPTPAIAYLTRKYNADAGVVISASHNPVEYNGIKFFNKNGYKLSDELEDSIQALIRDDFKDVPVLTGENIGRKIEEDGEAIRDYIDFAKSTIKGDLKGLKVALDCANGASYITSVEAFKELEAEVHVINNKPDGININRNSGSTHPEDLMEYVVKNNCHMGLAFDGDADRCLAIDEKGNLINGDFILAICGKELKKQGRLKKNTIVVTVMSNLGLDIAMKKEEINTIKTKVGDRYVLEEMLKND... | Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. | A7GJ15 |
A4SVW6 | ACPS_POLAQ | 4'-phosphopantetheinyl transferase AcpS | Polynucleobacter | MIIGIGTDILQIERLQAAYDRTNGRLAEKVLGPDEMLVFKHRLARNHKRGIAFLATRFAAKEAFSKAIGLGMHMPMTWRSLQTLNEPSGKPITSYLGALAQFMAEKNWEAHITVSDEQDMAIAHVIVTQK | Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein. | A4SVW6 |
Q6LMM2 | YQGF_PHOPR | Putative pre-16S rRNA nuclease | Photobacterium | MSNSRSVLAFDYGTKSIGVAIGQELTGTANPLAALKAKDGIPNWDDIGKILKEWQPDLVVVGLPLNLEGGELESITPRAKKFANRIHGRFGCVVELHDERLSTVEAKAELFEHGGYRALSKGNIDSQSAVVILESWFERQYG | Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. | Q6LMM2 |
A0A167LUS5 | FUMOA_CORFA | Fumosorinone biosynthesis cluster protein A | Cordyceps | MVATLANLNFPYLILSACLSAILLSRFLPFTRRDRRPTAKGCLPEPRVFQWDVFFGLDIPISQGRALQQNRYLEWLRDLHASMPRTKTFSVNFGGYRWIYSIEPEILKAVYATNFQDFGVEPIRQHPPGFKPFAEKGVSTSDGEDWAFSRSLIKPFFERSVYVSTDRVKPFADKFLTFIPEDGETFDIQPLLQRWFLDMTSEFIFGKSQDSMTHPERAEVIWAMADVLRGTRLRAQTYKILWAFNWDWWFKAIEKVHGFLNPYIRSTLAELAERQQRVKEGLPVGEERTDLLWSMATMLPEEEALRSQVCIIFVPNNDTT... | Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fumosorinone, a 2-pyridone alkaloid that acts as an inhibitor of protein tyrosine phosphatase 1B which is implicated asa negative regulator of insulin receptor signaling and a potential drug target for the treatment of type II dia... | A0A167LUS5 |
Q323W3 | GSIC_SHIBS | Glutathione transport system permease protein GsiC | Shigella | MLNYVIKRLLGLIPTLFIVSVLVFLFVHMLPGDPARLIAGPEADAQVIELVRQQLGLDQPLYHQFWHYISNAVQGDFGLSMVSRRPVADEIASRFMPTLWLTITSMVWAVIFGMAAGIIAAVWRNRWPDRLSMTIAVSGISFPAFALGMLLIQVFSVELGWLPTVGADSWQHYILSSLTLGAAVAAVMARFTRASFVDVLSEDYMRTARAKGVSETWVVLKHGLRNAMIPVVTMMGLQFGFLLGGSIVVEKVFNWPGLGRLLVDSVEMRDYPVIQAEILLFSLEFILINLVVDVLYAAINPAIRYK | Part of the ABC transporter complex GsiABCD involved in glutathione import. Probably responsible for the translocation of the substrate across the membrane. | Q323W3 |
A4WJ22 | SYP_PYRAR | Prolyl-tRNA synthetase | Pyrobaculum | MELIREARPHGREKLRANLIEWFHWLLREAELYDVRYPVKGAYVWRPYGMRLRRHVEELIRRSHDETGHQEVLFPVFIPYEFFGKESQHIRGFEKEVFWVSKGGEEGERLVLRPTSETAIMPMVKLWVHDYKDLPLRLYQIVSVFRAETKMTHPMIRLREISMFKEAHTVHVDREDAERQVREAVEIYKKIFDEMCLAYMINKRPDWDKFAGAEYTIAFDTVLPDGRTLQIGTVHYLGTNFTRVFEVTYLAADGTRRLAHTTSYGISERSIAAMLITHGDDAGTVLPPRLAPIQVVIVPIFYGEEEAASVISYAREVEKA... | 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). | A4WJ22 |
P11560 | MCRB_METTM | Coenzyme-B sulfoethylthiotransferase beta | Methanothermobacter | MAKFEDKVDLYDDRGNLVEEQVPLEALSPLRNPAIKSIVQGIKRTVAVNLEGIENALKTAKVGGPACKIMGRELDLDIVGNAESIAAAAKEMIQVTEDDDTNVELLGGGKRALVQVPSARFDVAAEYSAAPLVTATAFVQAIINEFDVSMYDANMVKAAVLGRYPQSVEYMGANIATMLDIPQKLEGPGYALRNIMVNHVVAATLKNTLQAAALSTILEQTAMFEMGDAVGAFERMHLLGLAYQGMNADNLVFDLVKANGKEGTVGSVIADLVERALEDGVIKVEKELTDYKVYGTDDLAMWNAYAAAGLMAATMVNQGA... | Component of the methyl-coenzyme M reductase (MCR) I that catalyzes the reductive cleavage of methyl-coenzyme M (CoM-S-CH3 or 2-(methylthio)ethanesulfonate) using coenzyme B (CoB or 7-mercaptoheptanoylthreonine phosphate) as reductant which results in the production of methane and the mixed heterodisulfide of CoB and C... | P11560 |
Q0HH96 | LPXH_SHESM | UDP-2,3-diacylglucosamine diphosphatase | Shewanella | MRTLFIGDLHLSADRLDITKAFNRFLDTELDDADALYILGDLFEVWVGDDLAAPFALELARRLKQISQRLPIYFIHGNRDFMLGKQFTDAAGMQMLPEVTCLDLYGVSTVILHGDSLCTLDKAYQRFRKLRSFAFARWLYSCLPKRKRQAIANKIRSNSQSSNQQKSYVIMDVEPSAVDALFAQTHCKQMIHGHTHRPAIHNFTNGCKRIVVGDWYEQGSVLVVSADGVDLKSLPFDAS | Hydrolyzes the pyrophosphate bond of UDP-2,3-diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. | Q0HH96 |
Q8LL17 | SON1_ARATH | Protein SUPPRESSOR OF NIM1 1 | Arabidopsis | MALPWELEEDILSRLPPISLVRFRTVSKHWNSLFNDKTFINNHLSRSRPEFIILTNSKIYSVDIIDHNNIDPTIRLHEIPTYDIHSRGTDLNRTIINTCDEFLFYNYRYWDNMTALWNPWLRQVRWIEYANQEFCVFGLGYDNSRPEKVYKILGHLFCHGKVLRDQKVVIYECASDSLRFIDRPEDDDWPITETAKRSNVSLNGNLYWFGCSNYENDEYYIRIFDFSTEDFKPFCLLPCQMSHSTDELVLAVYKGDRFSLLKQCSVTREIGVWVTKERISNDNGNGGEGVEWLKLMTLSKPNLPKLFGTVSYFIYGKTLY... | Regulates negatively a plant defense signaling pathway which is independent of salicylic acid (SA) and systemic acquired resistance (SAR). Confers sensitivity to P.syringae and P.parasitica. | Q8LL17 |
Q9HSB4 | AROD_HALSA | Type I dehydroquinase | Halobacterium | MEFQDFLLAASTGDLGAAPAAPEHVDLVEFRMDLAADPLAALDDYDGVLPVLATNRADWEGGAAADGGDRIDALAEAARTDCVAAVDIERSALVDDDTADGAEALAAARSTDTTTVVSAHDFDGTPSLSAMADLLGEACSLGDVGKLAVTPQDRGDALDVIRVTHEYSAAGMTVATMGMGDLGRHTRAVTPLYGSKLGYAPVADGETTAPGQYAPAALQALIADLQ | Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. | Q9HSB4 |
Q9SW93 | SCA_LILLO | Lipid transfer protein | Lilium | MARSSAVCFLLLLAFLIGTASAITCGQVDSDLTSCLGYARKGGVIPPGCCAGVRTLNNLAKTTPDRQTACNCLKSLVNPSLGLNAAIVAGIPGKCGVNIPYPIRMQTDCNKVR | Acts as an adhesive agent between the pollen tube wall and the stylar transmitting tract epidermis. Binds a stylar pectin in a pH-dependent manner. Enhances activity of chemocyanin, a diffusible chemotropic factor. | Q9SW93 |
A3MAE3 | ADC_BURM7 | Acetoacetate decarboxylase | pseudomallei group | MKPSQVRSKAFAMPLTSPAFPMGPYRFVNREFLIITYRTDMDRLREIVPEPLEVKEPLVHYEFIRMPDSTGFGDYTESGQVIPVEYKGQPGGYTLAMYLNDHPPIAGGRELWGFPKKLAQPTLQTHIDTLLGTLDYGPVRVATGTMGYKHQELDLEEQAKRLAGANFLLKIIPHVDGSARVCELVRYYLQDIEMKGAWTGPASLQLAPHALAPVADLPVLEIVEARHLLADLTLGLGEVVYDYLAQ | Catalyzes the conversion of acetoacetate to acetone and carbon dioxide. | A3MAE3 |
Q2LPJ8 | CH601_SYNAS | Chaperonin-60 1 | Syntrophus | MAAKEIKYDSVARDKVMKGVDTLANAVKVTLGPRGRNVVIEKAWGGPTITKDGVTVAKEIELEDKFENMGAQMVREVASKTSDMAGDGTTTATILAQAIYREGTKLAAAGMNPMSLKRGIDKSVQLVIDELKKISKDIRDKKEITQVGTISANNDNTIGEIISEAMEKVGKEGVITVEEAKGMETTLEIVEGMQFDRGYVSPYFVTDPEKMEVVMEDPYILLYDKKISVMQDLVPILEQIARSGRPMLIVSEDLEGEALATLVVNNIRGTLKCAAVKAPGFGDRRKAMLEDIAILTGGKVVSEELGIKLDSITLTDLGTC... | Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. | Q2LPJ8 |
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