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 |
|---|---|---|---|---|---|---|
B0BUP4 | RL18_RICRO | 50S ribosomal protein L18 | spotted fever group | MRSAKLKFEKRRSRIRHKISKTSNRVRLSIFKSGRHIYAQIIDDSKSITIAAASTLDEKRKKSHCNIEHAIKVGEEIAKKAYAAGIKDVVFDRGGYKYHGVVKALADAAREKIKF | 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. | B0BUP4 |
P24076 | BGIA_MOMCH | BGIA | Momordica | SQCQGKRSWPQLVGSTGAAAKAVIERENPRVRAVIVRVGSPVTADFRCDRVRVWVTERGIVARPPAIG | Competitively inhibits Glu S.griseus protease by forming probably a 1:1 complex. BGIA has no inhibitory activity against 2 other acidic amino acid-specific endopeptidases (S.aureus protease V8 and B.subtilis proteinase), chymotrypsin, trypsin, pancreatic elastase, and papain, although subtilisin Carlsberg was strongly ... | P24076 |
A3NUS3 | LFTR_BURP0 | Phenyalanyltransferase | pseudomallei group | MVPWLGPDDPFPSVERALGAASGAPGLLAASADLLPSRLIDAYRRGIFPWYSDGQPVLWWSPDPRMILVPAEFRISATFRKTLKRVLREPRWEIRVDCDFAGVMRACAQAPRRGQRGTWITAEIIDAYSSLHRAGDAHSIETWLDGRRVGGLYGVSFGRMFFGESMYAHASDASKIALAALVAHLREHRVEMIDCQQNTSHLASLGGREIARKTFVAHVRRAVAEPPIPWRFDKRVVAGLLGQAASATAADAFDR | Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine. | A3NUS3 |
G5EC89 | CEH17_CAEEL | Homeobox protein ceh-17 | Caenorhabditis | MMMEYGGYFSSSAVAQQSGDVPTTAPSAVTNSFFYTPQSHNIYHQYATPYLQSGRALTTAHNTSSSSAGNSTSSSSSSSNYRNTTHDSLQAFFNTGLQYQLYQKSQLIGSDTIQRTSSNVLNGLPRSSLVGALCSTGGAPLNPAERRKQRRIRTTFTSGQLKELERSFCETHYPDIYTREEIAMRIDLTEARVQVWFQNRRAKYRKQEKIRRVKDEEEDPLKKEPGQISLEEIIDQI | Probable transcription factor involved in postembryonic differentiation of the ALA neuron, and regulation of genes that contribute to behavioral quiescence, a sleep-like behavior mediated by ALA . Regulates its own expression and also that of homeodomain ceh-14, together forming an autoregulatory loop in the ALA neuron... | G5EC89 |
Q89GR1 | AACP2_BRADU | Aminoacyl carrier protein 2 | Bradyrhizobium | MHNTAINVQNRVLSVVRSVLQQNAISADVHPESRLVDIGLSSMGMVELMLKVEAEFDLILPQFEITPENFRSVKAMERMILNQLGSGSG | Aminoacyl carrier protein. Can be charged with L-glycine via the formation of a thioester bond between the amino acid and the 4'-phosphopantetheinyl prosthetic group, catalyzed by the bll6282 ligase. | Q89GR1 |
Q0G9Q1 | YCF2_DAUCA | Protein Ycf2 | Daucus sect. Daucus | MKGHQFKFWIFELREILREIKNSHYFLDSWTQFNSVGSFIHIFFHQEHFIKLFDPRIWSILLSRNSQGSTSNRYFTIKGVVILFVVAVLIYRINSRNMVERKNLYLIGLLPIPMNSIGPRNDTLEESVGSSNINRLIVSLLYLPKGKKISESCFLNPKESTWVLPITKKCSMPESNWGSRWWRNWIGKKRDSSQLKGSSDQSRDPLDSISNEDSEYHTLINQRKIQQLKERSILWDPSFLQTERTEIESDRFPKSLSGYSSMSRLFTEREKQVINHLLPEEIEEFLGNPTRSVRSFFSDRWSELHLGSNPTERSTRDHKL... | Probable ATPase of unknown function. Its presence in a non-photosynthetic plant (Epifagus virginiana) and experiments in tobacco indicate that it has an essential function which is probably not related to photosynthesis. | Q0G9Q1 |
Q1BU57 | PLSY_BURCA | Lysophosphatidic acid synthase | Burkholderia cepacia complex | MQILLAALVAYLIGSVSFAVVVSSVMGLADPRSYGSKNPGATNVLRSGNKKAAILTLVGDAFKGWIAVWLARHFGLPDVAIAWVAIAVFLGHLYPVFFRFQGGKGVATAAGVLLAVHPVLGLATALTWLIVAFFFRYSSLAALVAAVFAPVFDVFLFGMPGHNPIAWAVLAMSVLLVWRHRGNISKLLAGQESRIGDKKKAAADGGAQDGGKA | Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP. | Q1BU57 |
C0HK28 | CYML1_MELLF | Cyclotide mela-1 | Melicytus | GKYTCGETCFKGKCYTPGCTCSYPICKKD | Probably participates in a plant defense mechanism (Potential). Binds to and induces leakage in phospholipd membranes, particularly ones containing 1-palmitoyl-2-oleophosphatidylethanolamine (POPE) . In vitro, displays cytotoxicity against cultured cells but no hemolytic activity towards fresh erythrocytes . Not active... | C0HK28 |
Q5PJE9 | LSRK_SALPA | Autoinducer-2 kinase | Salmonella | MARLCTHTESGHYLMALDAGTGSVRAVIFDLQGKQIAVDQAEWQHLAVPDVPGSMEFDLAKNWQLACQCIRQALQKAAIPATAIAAVSACSMREGIVIYDSNGEPIWACANVDARAAHEVSELKELHDNTFEEEVYRCSGQTLALSAIPRLLWLAHHRPDIYHRASTVTMISDWMAFMLSGELAVDPSNAGTTGLLDLVTRNWKRSLLQMAGLRSDILSPVKETGTLLGHISQKAAEQCDLQAGTPVIVGGGDVQLGCLGLGVVRPAQTAVLGGTFWQQVVNLPAPVTDPNMNVRINPHVIPGMVQTESISFFTGLTMRW... | Catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. Phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules... | Q5PJE9 |
C1AXZ4 | UREG_RHOOB | Urease accessory protein UreG | Rhodococcus | MPPHFIDGEPHDHHHDRPRRVRVAGEPVRIGIGGPVGSGKTALVAALCRQLREELSLAVLTNDIYTTEDADFLRRHAVLPDERIAAVQTGGCPHTAIRDDITANLDAIDDLIAANPPLDLILVESGGDNLTATFSSGLIDVQIFVVDVAGGDKVPRKGGPGVTFSDLLVINKTDLAPMVGADLAVMRRDAEQVREGRPTALISLTEDPSSGPALAWVREQVRILADVH | Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG. | C1AXZ4 |
Q31XJ7 | SYDP_SHIBS | Protein Syd | Shigella | MDDLTAQALKDFTARYCDAWHEEHKSWPLSEELYGVPSPCIISTTEDAVYWQPQPFTGEQNVNAVERAFDIVIQPTIHTFYTTQFAGDMHAQFGDIKLTLLQTWSEDDFRRVQENLIGHLVTQKRLKLPPTLFIATLEEELEVISVCNLSGEVCKETLGTRKRTHLASNLAEFLNQLKPLL | Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function. | Q31XJ7 |
A0A4P8W796 | PYIF_MAGGR | Pyrichalasin H biosynthesis cluster protein F | Pyricularia | MLPSFIFVYSLLATATATSPDWPEPWPSHWREPGSDLFPNQQVHLAVEEAGTGSGCRISNITSNEMAKGRTIVDFPLYAVGSLEEPKLQPLNSSGGEQWEFDGVSEDGMQSFIFGFYRDPNYAILGTGNLRVSIEFGFEDRTRFSEVYYAQRSVVETCSLGTRGLWVDKEAGWKFSFLVDAAMQEAIITLDSDTVKGRIIITSRAKPLAADGSTWPAENASTVTIPYYYWSQPIPAGTVETNVEIKGKLIKWKGMGGHERFWSSFSWFTCMRSLQAVRAMLGPYVLSYFSFTSNLIPDLTHQSVVLFHDGAVVFRSTLGT... | Diels-Alderase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology (Probable). Pyrichalasin H is indicated as the re... | A0A4P8W796 |
A1RDX6 | FMT_SHESW | Methionyl-tRNA formyltransferase | Shewanella | MKSLNIIFAGTPDFAARHLQALLNSQHNVIGVYTQPDRPAGRGKKLTASPVKELAVANNIPVYQPGSLRKEPAQQALAALNADIMVVVAYGLILPKVVLDTPRLGCINVHGSILPRWRGAAPIQRALWAGDKETGVTVMQMDVGLDTGDMLLKTYLPIEDSDTSASLYEKLAEQGPVALLQALKGLANGTLAAEKQDEALANYAEKLSKEEARLDWNKSAKQLWQEVRAFNPWPVSYFEHQGNTIKVWQAHVSETISTAAPGTIISASKRGIEVATADGVLTLLSMQLPGKKPLNVADILNARGEWFSPNTRLANEAE | 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. | A1RDX6 |
A1U1I8 | PDXB_MARN8 | Erythronate-4-phosphate dehydrogenase | Marinobacter | MLIVADENIPLLDSFFGDIGEIRRVNGRTLTPDQVKDADILLVRSVTRVDRQLLEGTRVRFVGTATIGTDHIDQTWLQEQGIGFAAAPGCNAVSVAEYVLSVLSLYAEKRGIEDWSSLTVGIVGVGNVGGELARMLERLDFTVKLCDPPRQEAEEERAEEFVPLAEALECDVVTLHTPLTRTGDHPTNRMIAGSELAALGQDQLLINAGRGEVIDGEALLARLQQADAPTVVLDVWEHEPRINPDLLDRVWLATPHIAGYSLEGKMQGTEMIYQALCRYLGLPVRKKAGQFLPEPALSKVSFTSSADEDEAVQVALRACY... | Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate. | A1U1I8 |
Q3J2B6 | RF1_CERS4 | Peptide chain release factor 1 | Cereibacter | MVPMDRLLQIVRRFEFLEARLSAGAAPAEIAALSREYAELKPVVVEISAYRTALEDLAEAEAMLSDPEMRALAEDEIPALRARIPGMEQALRLALLPKDAADARPAILEIRPGTGGEEAALFAGDLLRMYQRYAEGQGWRFELLDLAPSELGGIREATARVEGEGAFARLKYESGVHRVQRVPETEAQGRIHTSAATVAVLPEAEEVDLEIPAADIRIDTMRSSGAGGQHVNTTDSAVRITHLPTGIIVTSSEKSQHRNREIAMQVLRARLYDLERQRLADARSADRKAQVGSGDRSERIRTYNFPQGRMTDHRINLTLY... | Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA. | Q3J2B6 |
A6W3C7 | TRMA_MARMS | tmRNA (uracil(341)-C(5))-methyltransferase | Marinomonas | MRPDQIQPEMYEKQLQDKQAELAKLMATLSLPEMEVFASQPTHYRMRAEFRIWHDGDDLYYAMFDSADPRTPIRTDQFLAASRLINELMPKLLDAVRDVPVLRYKLFQVDFLTTTTGEALISLLYHKPIDAEWNAAVQQLNNAFPACHFIGRSRKKKQIITRDFVMETLTVNGQKFHYQQVENSFTQPNAGISEKMLEWALDVTKEASGDLLEMYCGNGNFSIPLARRFDRVVATEISKVSVNSAQLNIAINGMHNVQVVKMASEDVSAALNGDVELPKSLVQAGVSELTPSVVLVDPPRAGLDDATVELIRKIDSILYI... | Dual-specificity methyltransferase that catalyzes the formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, and that of position 341 (m5U341) in tmRNA (transfer-mRNA). | A6W3C7 |
A4WG37 | ILVD_ENT38 | Dihydroxy-acid dehydratase | Enterobacter | MPKYRSATTTHGRNMAGARALWRATGMTDDDFGKPIIAVVNSFTQFVPGHVHLRDLGKLVAEQIEASGGVAKEFNTIAVDDGIAMGHGGMLYSLPSRELIADSVEYMVNAHCADAMVCISNCDKITPGMLMASLRLNIPVIFVSGGPMEAGKTKLSDQIIKLDLVDAMIQGADPKVSDAQSDQVERSACPTCGSCSGMFTANSMNCLTEALGLSQPGNGSLLATHADREQLFLSAGTRIVELTKRYYEQDDASALPRNIANKAAFENAMTLDIAMGGSTNTVLHLLAAAQEAEIDFTMSDIDKLSRKVPQLCKVAPSTPK... | 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 (... | A4WG37 |
Q2NIT9 | RSGA_AYWBP | Small ribosomal subunit biogenesis GTPase RsgA | Candidatus Phytoplasma asteris | MEKALVLRFLAGVYYIKDLETQIILEAKKRGKLKTLVIKTTQKENSSASDFIIKVGDIVLYELSCDTYLIQSILPRKNELKRPNVANIDQVLLVFSLVKPNFQFLLLDKFLLILEQQKLDVVLVFSKIDLLEPENFKTMQQQLSYYQKFQHFYYINSKQKIGIDALKHIFANQITVLAGQTGVGKSTLLKVLIPDAQLKTQEISESLGRGKHTTKNAQLYDFNGGFIVDTPGFSKLDLTTFSPRTLKNFYPDFLEHVCDCFFGESCFHLQEEKCGVKKALENGQILPSRYQNYVIFCEEIKNQPKY | One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimula... | Q2NIT9 |
A1RQ05 | UBIC_SHESW | Probable chorismate pyruvate-lyase | Shewanella | MNVTSLSFPYGESIQWFCADRTDKLPPSPLKEWLLAPGSLTKKLKTCCNQFEVKVLGEGQLAPFKDEYPQQGSVWVREVLLCLDNVPWVFARTLIPLSLLSEREADFLGLGSRPLGELLFSQDNFIPGRIEVASFDTGSRLAHLAASLDQRVEHLLWGRRRYFHHGQDEMIVSEIFLPAAERAICQ | Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway. | A1RQ05 |
Q82DX3 | NUOI1_STRAW | NDH-1 subunit I 1 | Streptomyces | MAEEPKETGPGFQNPVAGFGVTFKAMFKKRLTEQYPEQQKTTAPRFHGRHQLNRHPDGLEKCVGCELCAWACPADAIYVEGADNTDEERYSPGERYGRVYQINYARCILCGLCIEACPTRALTMTNEFELADSSRANLIYTKEQLLAGLDDNMVDSPHAIYPGMDEQDYYRGLVTEAAPGTERQVAVSKGEKPQDEGVEA | 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... | Q82DX3 |
Q8R7W6 | RL5_CALS4 | 50S ribosomal protein L5 | Caldanaerobacter | MSRLREKYEKEVVPALMERFGYKNIMQVPKLEKVVINIGVGEAKENPKALEAAMNDLMMISGQKPVITRAKKSISNFKIRKGMPIGVKVTLRRERMYEFLDKLFNIALPRVRDFKGVSPNSFDGRGNYALGVREQLIFPEIDYDKIDKVRGMDIIIVTTAKTDEEAKALLELLGMPFAK | 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... | Q8R7W6 |
Q85FQ9 | ATPD_CYAM1 | F-type ATPase subunit delta | Cyanidioschyzon | MKQKIVEPYAQALFRLKDDIDLTPLWEMARDSKFMQLLMNPSIPKEKKWQLFQPFDKLVQSWLEVIWKKKRMNLLAEICASYLELRKKKEGIVTVFVTSATPLTDTQTQQLEVQLTRMCQAKHLQCEYQVDAQLLAGLKIQMNGQLIDTSWQTQLKQLMKSLW | This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. | Q85FQ9 |
Q38UQ8 | RS7_LATSS | 30S ribosomal protein S7 | Latilactobacillus | MPRKGYVAKRDVLPDPMYNSKLVSRLINRLMIDGKRGTASTILYDAFDIIKEETGNEPLEVFEEAMNNIMPVLEVKARRIGGSNYQVPIEVRPERRTTLGLRWLVSYARLRGEHTMDQRLAREIMDAANNTGAAVKKREDTHKMADANRAFAHYRW | One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA. | Q38UQ8 |
Q9VHB9 | TRM44_DROME | Probable tRNA (uracil-O(2)-)-methyltransferase | Sophophora | MAAVEEAQFWQAIGILIKNYHALNKKIFEVVITQVTKQQNGRVCESSAEELAMSLKEDPSQRTCTGFTIGFKLLSKKLAENILGTGIVDFENCLYECQFASDSIEGFSVGLLGGEFKLKSKSNTNWLEFVLRPKLLSWSQSKQDEAKVKSLGLVNVEKYNDLYKELKQRHSQRLLEHWKTAQESTDPLKFIYEDLAIAAYLIVLWSQTQSEPTAFADLGCGNGLLVHVLNAEGYKGYGYDIRKRKLWSLYPPDTQRSLIEKAVEPNSFRLDFPGVDWLIGNHSDELSPWLPVLAGRLNINYFLLPCCPFELSGAKFRRRN... | Probable adenosyl-L-methionine (AdoMet)-dependent tRNA (uracil-O(2)-)-methyltransferase. | Q9VHB9 |
B9DV29 | RECX_STRU0 | Regulatory protein RecX | Streptococcus | MKIQKIEKKKRLYLLECDNGDSLYVTEDTIVHFMLSKGMEISPEQLESIKQFAQFSYGKNLALYYISFQVRTQKQVYDYLKKHDLENTIIQKIIEELIKENWINDQKYVESFLRQNMTNGDKGPQLIKQKLMQKGISDKIIEKAISEVDFYPIAEKAALKMISRYQDKLPRKALQDKLTQLLINKGFSYDLVKAVNGNLSIETDQENTLDLLEKEADKQLRKLSKRYEGYALRQKLFQALYRKGYDSDDIQSLLSEIL | Modulates RecA activity. | B9DV29 |
Q4FP16 | LEUD_PELUB | Isopropylmalate isomerase | Candidatus Pelagibacter | MQKFNSLTSIPAYLPIVNIDTDMIIPKQFLKTIKRTGLGKNLFFEMRYDDNGNEIKDFILNQKPHNQSKILIAGKNFGCGSSREHAPWALLDFGITCVISSSYADIFYSNCFKNGILPITLPEEKIKELSEYSKRKEEISIDLNEEKIIFGNSEIKFDIDPFKKKCLLEGLDDIALSLAKKEKIITFEENLKNNKPWIFNDKN | Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. | Q4FP16 |
Q7VZ47 | SELO_BORPE | Protein adenylyltransferase SelO | Bordetella | MKWLRLQDLPTDNSFAALPAEFYTRLQPRPPAAPRLLHANAEAAALIGLDPAEFSTQAFLDVFSGHAPLPGGDTLAAVYSGHQFGVWAGQLGEVRGPAGGWELQLKGAGMTPYSRMGDGRAVLRSSVREYLASEAMHGLGIPTTRSLALVVSDDPVMRETVETAAVVTRMAPSFVRFGSFEHWSARRQPEQLRVLADYVIDRFYPECRVAGAGRLDGEHGEILGLLAAVTRRTALLMADWQAVGFCHGVMNTDNMSILGLTLDYGPYGFMDTFQLGHICNHSDSEGRYAWNRQPSVGLWNLYRLASSLHTLAPDPEALRA... | Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation). | Q7VZ47 |
Q5PQA4 | NB5R2_XENLA | NADH-cytochrome b5 reductase 2 | Xenopus | MLVALAAIGVTVLLFLIKALGSGAKKAPVTLLDPNAKYPLPLIEKQEISHDTKKFRFGLPSAEHVLGLPVGQHIYLSAKVNGSLVVRAYTPVSSDEVKGHVDLVVKVYYKNVNPKFPDGGKMSQHLDSLKIGETIDFRGPNGLLVYKGKGKFAIRPDKKAEPKIKVAKHVGMLAGGTGITPMLQLIRQITQDPNDNTKCYLIFANQTEDDILLRYELETVAKSHPEQFKLWYTLDRPPQGWKYGSGFVTADMIKEHLPPPSEDVLVLMCGPPPMIQFACQDNLTKLGYPEAGRFAY | NADH-cytochrome b5 reductases are involved in desaturation and elongation of fatty acids, cholesterol biosynthesis and drug metabolism. | Q5PQA4 |
Q12MF1 | UPP_SHEDO | UPRTase | Shewanella | MKVVEVKHPLIRHKVGLMREADISTKRFRELATEVGSLLTYEATSDFETEKVTIEGWNGPVEIDQIKGKKVTVVPILRAGLGMMDGVLEHIPSARISVVGIYRDEETLEPVPYFEKIVSNVEERIALVVDPMLATGGSMIATIDLLKSKGCTSIKALVLVAAPEGIAALEKAHPDIELYTASIDKCLNEQGYILPGLGDAGDKIFGTK | Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate. | Q12MF1 |
Q6G4V6 | MIAB_BARHE | tRNA-i(6)A37 methylthiotransferase | Bartonella | MNKANPKNIPPLAPKKVFIKTYGCQMNVYDSQRMTDSLSSKGYVATQTPNDADLILVNTCHIREKAAEKLYSDLGRLRVMRQERTPDKPLMVGVTGCVAQAEGSEILRRAPIVDLVIGPQMYHRLPDLLEQTKQGKKIVATEYAVEDKFAHLPPHNKRAVRKRGVSAFLTVQEGCDKFCTFCVVPYTRGAEISRSVEQITEEARQLIEAGVKEITLLGQNVNGWHGQNVNGKTWRLGDLLYHLAKLDGLKRLRYTTSHPRDMDDSLIAAHRDLDILMPYLHLPVQSGSDRILKAMNRQHKSIHYLQLIEKIRNARPDIAF... | 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. | Q6G4V6 |
B8IN87 | LEXA_METNO | LexA repressor | Methylobacterium | MLTRKQLDLLRFIQQRMRETGVPPSFDEMKDALDLKSKSGIHRLITALEERGFLRRLPNRARAIEVIRIPDAVVPPSGEVVRFTPSVVEGGRTAAPAAKAAPMPSSLGSDDNGRSISIPVMGRIAAGTPISAIQSQSRTVAMSPDFLAGGEHYALEVRGDSMIEAGILDGDLVVIRRQDTANTGDIVVALIDDEEATLKRLRRRGSSIALEAANPAYETRVLGPDRVRIQGRLVSLIRKY | Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair... | B8IN87 |
A9MEG7 | RSXE_SALAR | Rsx electron transport complex subunit E | Salmonella | MSEIKDIVVQGLWKNNSALVQLLGLCPLLAVTSTATNALGLGLATTLVLTLTNLTVSALRRWTPAEIRIPIYVMIIASVVSAVQMLINAYAFGLYQSLGIFIPLIVTNCIVVGRAEAFAAKKGPWLSALDGFSIGMGATGAMFVLGSLREILGNGTLFDGADSLLGSWAKVLRVEIFHTDSPFLLAMLPPGAFIGLGLMLAVKYLIDEKMKKRRAVTAPSAVPAGETGKV | Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Required to maintain the reduced state of SoxR. | A9MEG7 |
A9BCC5 | CH10_PROM4 | Chaperonin-10 | Prochlorococcus | MAAVSLSVSTVKPLGDRVFVKVSESEEKTAGGILLPDTAKEKPQVGEVAQVGPGKRNEDGSRQAPEVGVGDKVLYSKYAGTDIKLGSDEYVLLSEKDILAVVN | Together with the chaperonin GroEL, 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. GroES binds to the apical surface of ... | A9BCC5 |
Q96C11 | FGGY_HUMAN | D-ribulokinase FGGY | Homo | MSGGEQKPERYYVGVDVGTGSVRAALVDQSGVLLAFADQPIKNWEPQFNHHEQSSEDIWAACCVVTKKVVQGIDLNQIRGLGFDATCSLVVLDKQFHPLPVNQEGDSHRNVIMWLDHRAVSQVNRINETKHSVLQYVGGVMSVEMQAPKLLWLKENLREICWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKGWDDSFWKMIGLEDFVADNYSKIGNQVLPPGASLGNGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVIGADVRGHGLICEGQPVTSRLAVICGTSSCHMGISKDPIFVPGVWGPYFSAM... | Catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. Postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, may play a role in regulating D-ribulose 5-phosphate recy... | Q96C11 |
Q5Z1L1 | RS11_NOCFA | 30S ribosomal protein S11 | Nocardia | MPPKSRASGPKKTQKSRRRDKKNVPHGNAHIKSTFNNTIVSITDPNGNVISWASSGHVGFKGSRKSTPFAAQLAAENAARKAQEHGVKKVDVFVKGPGSGRETAIRSLQAAGLEVGTISDVTPQPHNGCRPPKRRRV | Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome. | Q5Z1L1 |
Q5PKV5 | YIDZ_SALPA | HTH-type transcriptional regulator YidZ | Salmonella | MKKSLTSLDLNLLLCLQLLMQERSVTKAAKRMNVTPSAVSKSLAKLRAWFDDPLFVNTPLGLVPTPLMVSMEQSLADWMQMGNQLLDKPHHQTPRGLKFELAAESPLMMIMFNSLSQQIYQRYPQATIKVRNWDYDSLEAITRGEVDIGFTGRESHPRSRELLSLLPLAIDFEVLFSDLPWVWLREDHPALREAWDLDTFLRYPHISICWEQSDTWALDDVLQEMGRKRHIALSLPGFEQSLFMAAQPGHTLIATAPRYCQHYNQLHQLPLVARPLPFDAQQREKLMVPFTLLWHKRNSHNPKIVWLRQAINTLCRRLI | Involved in anaerobic NO protection. | Q5PKV5 |
B2J8Q3 | PETM_NOSP7 | Cytochrome b6-f complex subunit VII | Nostoc | MGGEILNAAILSFGLIFVGWGLGALLLKIQGGEE | Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. | B2J8Q3 |
A6VWM5 | RLMM_MARMS | 23S rRNA 2'-O-ribose methyltransferase RlmM | Marinomonas | MKNVLVYCRQGFEKDCAAELSEVASSKGFYGYAKVVPDAGYIVYNFDQADAGETLIQQLNFNRLIFARQIIAVNDVIELEQGGRVESLLEAARELPLAEEIWIETADTNDAKALSGLIKKLEKPLREGWKRSGVLRNKAVGVRHHVFMLDGEAAYLGVSYAACRSEFPMGIRRLRFPAAGPSRSTLKLEEAFLQFVPEQTLEADLTEGMTAVDLGAAPGGWTYQFVKKGINVIAIDNGPMQKELMSTGLVEHEKADGFKYEPPYTVDWLVCDMVERPIKVAELMAKWLASGWTRRAIFNLKLPMKKRYQEVTLCLQTMEG... | Catalyzes the 2'-O-methylation at nucleotide C2498 in 23S rRNA. | A6VWM5 |
L8EUQ6 | OXYS_STRR1 | 12-dehydrotetracycline 5-monooxygenase/anhydrotetracycline 6-monooxygenase | Streptomyces | MRYDVVIAGAGPTGLMLACELRLAGARTLVLERLAEPVDFSKALGVHARTVELLDMRGLGEGFQAEAPKLRGGNFASLGVPLDFSSFDTRHPYALFVPQVRTEELLTGRALELGAELRRGHAVTALEQDADGVTVSVTGPEGPYEVECAYLVGCDGGGSTVRKLLGIDFPGQDPHMFAVIADARFREELPHGEGMGPMRPYGVMRHDLRAWFAAFPLEPDVYRATVAFFDRPYADRRAPVTEEDVRAALTEVAGSDFGMHDVRWLSRLTDTSRQAERYRDGRVLLAGDACHIHLPAGGQGLNLGFQDAVNLGWKLGATIA... | Involved in the biosynthesis of the antibiotics oxytetracycline and tetracycline. OxyS starts by catalyzing the stereospecific hydroxylation of anhydrotetracycline at C(6) position to yield 5a,11a-dehydrotetracycline (12-dehydrotetracycline). If the released product is captured by OxyR, it is reduced to tetracycline. H... | L8EUQ6 |
Q9GJU3 | APOE_PANTR | Apolipoprotein E | Pan | MKVLWAALLVTFLAGCQAKVEQVVETEPEPELHQQAEWQSGQRWELALGHFWDYLRWVQTLSEQVQEELLSSQVTQELTALMDETMKELKAYKSELEEQLTPVAEETRARLSKELQAAQARLGADMEDVRGRLVQYRGEVQAMLGQSTEELRARLASHLRKLRKRLLRDADDLQKRLAVYQAGAREGAERGVSAIRERLGPLVEQGRVRAATVGSLAGQPLQERAQAWGERLRARMEEMGSRTRDRLDEVKEQVAEVRAKLEEQAQQIRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAMGTSAAPVPSDNH | APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apoliproteins are amp... | Q9GJU3 |
Q9HDX6 | POF15_SCHPO | F-box protein pof15 | Schizosaccharomyces | MSCVTRAPMSVPQTALQPNSYVNFDAQQTSSTLLPVEVIDSVMQYLPAHDVIQSSFASYPLTLIANKIIRARLSFLDEYSLRVFAKDVYTDSPICNLSARRGLYSLQYDGYSVFHLDPNNCSSIFQISFEDDEDLASFERYPGEFLAPHINVRIHVTLSRSSCDRHQADIFSCFQDPIRVRRDWLDSIKPGQPETLWFDQNTQHVIGLIVTRVDAAPGKYDLSVTSVIVQTEYLLSCLEKRVH | Probable substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. | Q9HDX6 |
P81201 | H37_STYLE | Histone H3-7 | Stylonychia | NTGGKAPRKHIAHKQAKKSSAAAATGGVKKPHRFRPGTVALREIRRFQKSTELLIRKLPFQRLVREIASEFKNDLRFQSSAVLALQEASEAYLVGLFEDTNLAAIHAKRVTIMP | 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 v... | P81201 |
P48105 | PSBH_CYAPA | Photosystem II reaction center protein H | Cyanophora | MPQRTALGNILRPLNSEYGKVAPGWGTTPLMAVFMLLFFVFLLIIIQIYNSSLLLENVQVSWTAATA | One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a c... | P48105 |
A7X1J3 | PLSX_STAA1 | Phosphate-acyl-ACP acyltransferase | Staphylococcus | MVKLAIDMMGGDNAPDIVLEAVQKAVEDFKNLEIMLFGDEKKYNLNHERIEFRHCSEKIEMEDEPVRAIKRKKDSSMVKMAEAVKSGEADGCVSAGNTGALMSVGLFIVGRIKGVARPALVVTLPTIDGKGFVFLDVGANADAKPEHLLQYAQLGDIYAQKIRGIDNPKISLLNIGTEPAKGNSLTKKSFELLNQDHSLNFVGNIEAKTLMDGDTDVVVTDGYTGNMVLKNLEGTAKSIGKMLKDTIMSSTKNKLAGAILKKDLAEFAKKMDYSEYGGSVLLGLEGTVVKAHGSSNAKAFYSAIRQAKIAGEQNIVQTMK... | 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. | A7X1J3 |
Q49Y71 | DTD_STAS1 | Gly-tRNA(Ala) deacylase | Staphylococcus | MRIVVQRVKHASVTNDSVDNKINKGYCLLVGVGKSSTEADIATLAKKIVNARLFEDADGKLNLNLQQVEGEILSISQFTLYADVRKGNRPGFTQSMSPDCANELYEQFNDTLRSYGINVLTGEFGTDMLVDIANDGPVTIIYESQDGKII | An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By rec... | Q49Y71 |
Q9CDW0 | MSCL_LACLA | Large-conductance mechanosensitive channel | Lactococcus | MLKEFKNFILRGNVLDLAVGVIIGAAFTALVKSLVDNLINPLIGMFVQSTALAHLSVTVGKTKFTYGAFLNDVINFIITAFVIFILIKFINKLFPKKEETVEEQKNEELETLQEIRDLLKKQ | Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell. | Q9CDW0 |
Q7WP31 | GCST_BORBR | Glycine cleavage system T protein | Bordetella | MSAPLKRTPLAEEHLAAGARMVDFGGWDMPLAYGSQLEEHHAVRQDAGMFDVSHMLNVDVGGADATAFLRRLVANDVARLATPGKALYSCMLNPQGGIIDDLIIYYFAPDQWRVVVNAGTADKDIAWMQRVAAADGFDVAIAPRRDLAMVAVQGPNARAKVWAARPAWQAASEPLAPFSAAAVEAGTLVARTGYTGEDGFEIVLPADAVVQLWRDLLAQGVRPCGLGARDTLRLEAGMNLYGQDMDELVHPDQAGLSWTVALKDEARRFVGRDAIEQFAVPRAFVGLKLQERGVMRAHMPVRCAQGMGELTSGTMSPTLG... | The glycine cleavage system catalyzes the degradation of glycine. | Q7WP31 |
C1CR55 | GUAC_STRZT | Guanosine 5'-monophosphate oxidoreductase | Streptococcus | MLNEFPIFDYEDIQLIPNKCVIKSRAEADTSVTLGNHTFKLPVVPANMQTILDENVAEQLAKGGYFYIMHRFDEAGRIPFIKRMHDQGLIASISVGVKDYEYDFVRQLKTDAPEYITIDIAHGHADSVISMIQHIKKELPDTFVIAGNVGTPEAVRELENAGADATKVGIGPGKVCITKVKTGFGTGGWQLAALRWCAKAARKPIIADGGIRTHGDIAKSIRFGASMIMIGSLFAGHIESPGKTIEVDGEQFKEYYGSASQYQKGAYKNVEGKRILLPAKGHLQDTLTEMEQDLQSAISYAGGRQVADLKHVDYVIVKNS... | 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. | C1CR55 |
B9DV47 | RPOZ_STRU0 | Transcriptase subunit omega | Streptococcus | MMLKPSIDTLLDKVPSKYSLVILQAKRAHELEAGAKATQSFKSVKSTLRALEEIESGNVVIHPDPSAKRAAVRAKIEADRLAKEEEERKIKEQIAKEKEEEGEKI | Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits. | B9DV47 |
Q67QZ8 | ISPH_SYMTH | 4-hydroxy-3-methylbut-2-enyl diphosphate reductase | Symbiobacterium | MEVIKITPRGYCHGVVGAIQLVRRVARDPNVPRPIYVLGQIVHNRHVVEEMEALGVITLDGEDRLSLLEKIDAGTVIFTAHGVSPAVKIRAREKGLYVVDATCPDVTRTHELIAELVSRGYEVIYIGKKGHPEPEGAVGVAPGHVHLVERAEDLEALSFAPGQKLAVTNQTTLSQWDTQALMEQVKARWPQTEIYNEICLATQQRQEAVARMAPEADLVIVVGDRRSNNSNRLVQVAQELAAREAHLVDSVEEIDPAWLKGKRKVAVTSGASTPTHITRAVIEFLEKYNVEVEER | Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis. | Q67QZ8 |
Q03FY3 | FMT_PEDPA | Methionyl-tRNA formyltransferase | Pediococcus | MKSIIFMGTPEFSAPILQSLIDEPNYDVIGVVTQPDRKVGRKHVLTPSPVKKVAVKNDIKVYQPEKLSGSAELTELIALNADLIVTAAFGQFLPMSLINSVKIGAVNVHASLLPKYRGGAPVHYAIMNGDKETGVTIIYMVKKMDAGEMLATAKIPITDQDDVGTMFEKLSLLGRDLLLDTLPQLIEGNVQPVKQDEEQVSFSPNISPEEEEIDINLPARLVDAKVRGLRPFPVAYFMMEGKRTKIWKTKVIDQTTDLKPGQVVSKTKHELLVATGEHGVISIEELQPAGKQKMTITDYLNGVGENLHPGKQIIDNDKSK | 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. | Q03FY3 |
Q98JB6 | HTPG_RHILO | High temperature protein G | Mesorhizobium | MTTDTKATETRAFEADVSRLLHMMVHSVYSDKDVFLRELISNAADACEKLRFEAVSRPELLGDDPKPRISISADPDNKEITVEDNGIGMSRDDMAEALGTIARSGTRAFIERVGSGTEDTQLIGQFGVGFYSAFMVADRVDVISRLAGSEEAWRWSSDGKGSYEIAPAPLEAAPRRGTRVVLHLMDDAVSYTGSYRLEQLAKSQSGHVPVPITLIEKPGAEARDIADGTALWVRPKSEIKPEEYTDFYRSVAGQYDEPAATIHFRAEGRQEYSVLAFVPGSRPFDLFDQDRKGRMKLYVRRVFITDDADLLPRYLRFVRG... | Molecular chaperone. Has ATPase activity. | Q98JB6 |
O13988 | POT1_SCHPO | Protection of telomeres protein 1 | Schizosaccharomyces | MGEDVIDSLQLNELLNAGEYKIGELTFQSIRSSQELQKKNTIVNLFGIVKDFTPSRQSLHGTKDWVTTVYLWDPTCDTSSIGLQIHLFSKQGNDLPVIKQVGQPLLLHQITLRSYRDRTQGLSKDQFRYALWPDFSSNSKDTLCPQPMPRLMKTGDKEEQFALLLNKIWDEQTNKHKNGELLSTSSARQNQTGLSYPSVSFSLLSQITPHQRCSFYAQVIKTWYSDKNFTLYVTDYTENELFFPMSPYTSSSRWRGPFGRFSIRCILWDEHDFYCRNYIKEGDYVVMKNVRTKIDHLGYLECILHGDSAKRYNMSIEKVD... | Single-stranded telomeric DNA-binding protein that is required to protect the 3'-end telomeric overhang. It binds the consensus sequence 5'-GGTTAC-3'. Regulates telomerase and telomere length. | O13988 |
Q5FNS2 | PDXJ_GLUOX | Pyridoxine 5'-phosphate synthase | Gluconobacter | MIRLGVNIDHVATLRNARGGTFPDPVAAAELAIASGADGITAHLREDRRHIRDADMPRLRALSAPLNFEMAATDEMVRIACDLRPHACCLVPEKRQEVTTEGGLDIVGQSEALKPKIARLRDAGIRVSLFIDPEARQIETAAALGAPVVELHTGAYALGGSEELERLRSAAGTVAACGLELHAGHGLTYDNVGAIADLTGLAELNIGHFLIGQAIFDGLGPVVRKMKSLINS | 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. | Q5FNS2 |
B0TC61 | RL22_HELMI | 50S ribosomal protein L22 | Heliomicrobium | MEAKTAQAVAKYVRTSPRKVRQVIDLIRGKSVADAFAILKFTPVKSAADVAKVLKSAVANAEHNYEMNTADLYVQTCFVDQGPSMKRISPRAQGRADVIKKRMSHITVIVAEKPAKPAAAKKDPKAAAAKADANAGTKEG | The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome. | B0TC61 |
A0KJ66 | NUOB_AERHH | NDH-1 subunit B | Aeromonas | MKYTLTRIDPDAPVERYPQEQRQTVEDPLAQEASRGIMIGRLEEVLQDTVNWGRKNSLWPYNFGISCCYVEMCTAFTSPHDVARFGAEVIRASPRQADFMVIAGTPFIKMAPVIQRLYEQLLEPKWVISMGACANSGGMYDIYSVVQGVDKFLPVDVYIPGCPPRPEAFLQALMLLQDSIGKERRPLSWVVGDQGIYRPQMPAEKDRKRGERINVTNLRTPDEI | 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... | A0KJ66 |
Q2SSE2 | RIMP_MYCCT | Ribosome maturation factor RimP | Mycoplasma | MKDFESIKFQINELVNKELEVLNLKVYEINNLKEFENDMIQILVEDALQANKPLDFDILIKANDLVSNKIDQIIKTNQKYLLEISSSGIEKQIRSQEELIKALDQWVYVQLNNEIKKVKEFEGYVTKYNNDTNTFSFLFFIKGQKKTLEVMWNNIKFIRYAVRF | Required for maturation of 30S ribosomal subunits. | Q2SSE2 |
Q4R4H7 | ANXA5_MACFA | Annexin-5 | Macaca | MAQVLRGTVTDFPGFDERADAETLRKAMKGLGTDEESILTLLTSRSNAQRQEISAAFKTLFGRDLLDDLKSELTGKFEKLIVALMKPSRLYDAYELKHALKGAGTDEKVLTEIIASRTPEELRAIKEVYEEEYGSSLEDDVVGDTSGYYQRMLVVLLQANRDPDAGIDEAQVEQDAQALFQAGELKWGTDEEKFITIFGTRSVSHLRKVFDKYMTISGFQIEETIDRETSGNLEQLLLAVVKSIRSIPAYLAETLYYAMKGAGTDDHTLIRVMVSRSEIDLLNIRKEFRKNFATSLYSMIKGDTSGDYKKALLLLCGGED | This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. | Q4R4H7 |
P80356 | AVE3_AVESA | Prolamin | Avena | MKTFLIFALLAMAATMATAQFDPSEQYQPYPEQQQPILQQQQMLLQQQQQMLLQQQPLLQVLQQQLNPCRQFLVQQCSPVAVVPFLRSQILQQSSCQVMRQQCCRQLEQIPEQLRCPAIHSVVQAIIMQQQQFFQPQMQQQFFQPQMQQVTQGIFQPQMQQVTQGIFQPQLQQVTQGIFQPQMQGQIEGMRAFALQALPAMCDVYVPPHCPVATAPLGGF | Seed storage protein. Serves as a source of nitrogen, carbon, and sulfur for the young developing seedling. | P80356 |
Q8MCM1 | MATK_TRISR | Intron maturase | Trifolium | MKEYQVYLERARSRQQDFLYPLIFREYIYGLAYSHNWSRSIFVENGGYDNKYSLLNVKRLITRMYQQNHLIISANDSPKNPFWGYNKNFDSQIISEGFAIVVEIPFFLQLNSSLKEAEIIKSYKNVRSIHSIFPFLEDKFTYLHYVSDIRIPYPIHLEILVQILRYWVKDAPFFHLLRLFLYHFSNWNRFITTKKSISTFSKRNPRLFLFLYNFYVCEYESIFLFLRNKSSHLRLKSFSVFLERIFFYAKREHLVEVFAKDFSYPLPFFKDPNIHYVRYQGKCILASKNVPFLMNKWKHYFIHLWQCFFDVWSQPRTINI... | Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns. | Q8MCM1 |
A6U816 | YQGF_SINMW | Putative pre-16S rRNA nuclease | Sinorhizobium | MAILTIEELAERLPPYQAVAGLDLGTKTIGLSVSDLGRRFATPRDVIRRVKFGIDAQALLFFAEKEKVAAFVIGLPVNMDGSEGPRCQATRAFVRTMGERTDIPSVLWDERLSTVAAERVLIEMDVSRKKRADRIDSAAASFILQGALDRLALLARGASGDRDAP | Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. | A6U816 |
B8D7V3 | CYSN_BUCAT | Sulfate adenylate transferase | Buchnera | MNINMKDNFKKWLDLQQKKTLLKFLTCGSVDDGKSTLIGRLLHDTKQIYDDQLFFLKSDSKRHGTQGNEIDLALVVDGLQSEREQGITIDVAYRYFSTNKRKFIIADTPGHEQYTRNMATGASTCDLSILLVDARKGLSEQTYRHSFISTLLGIKYLIVAINKMDLVNYKQEIFENIKKDFLIFSKKLANDLNIIFIPMSALLGENIVFKTKLMPWYQGVTLLSFLETIKIKNSISSEELRFPVQYINRPNSDFRGYSGILLSGRMHVGQTIKILPENINSRVSRIVTFDKELKKAEIGESITVVLKDEIDINRGDFFVN... | With CysD forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysi... | B8D7V3 |
P61671 | MUTS_THET2 | DNA mismatch repair protein MutS | Thermus | MGNMLKGEGPGPLPPLLQQYVELRDRYPDYLLLFQVGDFYECFGEDAERLARALGLVLTHKTSKDFTTPMAGIPIRAFDAYAERLLKMGFRLAVADQVEPAEEAEGLVRREVTQLLTPGTLTQEALLPREANYLAAIATGDGWGLAFLDVSTGEFKGTLLKSKSALYDELFRHRPAEVLLAPELRENEAFVAEFRKRFPVMLSEAPFEPQGEGPLALRRAQGALLAYARATQGGALSVRPFRLYDPGAFVRLPEASLKALEVFEPLRGQDTLFGVLDETRTAPGRRLLQAWLRHPLLERGPLEARLDRVERFVREGALRE... | This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity. | P61671 |
B3QM27 | RUVB_CHLP8 | Holliday junction ATP-dependent DNA helicase RuvB | Chlorobaculum | MRIEALNTAPDATEVRFEEQIRPQSMSDFAGQKKLTDNLKVFITAARKRGDALDHVLLSGPPGLGKTTLAHIIAAEMGGGIKITSGPLIDKAGNLAGLLTSLKKGDILFIDEIHRLAPAVEEYLYSAMEDYRIDILLDSGPASRAVQLKLEPFTLVGATTRSGLLTSPLRARFGINSRLDYYSPELLQSIIVRAAGILNIGVDEDAAMEIARRSRGTPRIANRLLRRARDFAQVANEASISLAVARRTLESLEIDEGGLDDMDKKILEAIVRKFNGGPVGVASLAVSVGEEQDTIEEVYEPYLIQVGYLARTPRGRVATR... | 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. | B3QM27 |
Q92GU6 | EX7L_RICCN | Exodeoxyribonuclease VII large subunit | spotted fever group | MLDNFIAHQATKEFSVSEISNKIKELLENNFGYIKVKGEISGLKIANSGHAYFNLKENTAILACTCWRPILAKITFPLNDGMEVVISGKLSSYAGNSRYQLSVDNLQPTGLGAMLQILNERKAKLEKEGLFNKIRIPIPFLPDKIGVITSITGAVIKDIIHRIRERFPTRIIIWPVSVQGENSGNEIAEAIEGFNNLEEVNKPRVIIVARGGGSIEDLWSFNDEILVRAAYNSKIPIISAVGHEVDYTLIDLAADKRAPTPTAAAEFAVPVRSILNNTLQSYEKILLNNTSRLIKYHEQNIVNYNKIHRYLSHYINNRQQ... | Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. | Q92GU6 |
P35722 | NEUG_BOVIN | NEUG(55-78) | Bos | MDCCTESACSKPDDDILDIPLDDPGANAAAAKIQASFRGHMARKKIKSGERGRKGPGPGGPGGAGGARGGAGGGPSGD | Acts as a 'third messenger' substrate of protein kinase C-mediated molecular cascades during synaptic development and remodeling. Binds to calmodulin in the absence of calcium. | P35722 |
P16701 | CYST_ECOLI | Sulfate transport system permease protein CysT | Escherichia | MFAVSSRRVLPGFTLSLGTSLLFVCLILLLPLSALVMQLAQMSWAQYWEVITNPQVVAAYKVTLLSAFVASIFNGVFGLLMAWILTRYRFPGRTLLDALMDLPFALPTAVAGLTLASLFSVNGFYGEWLAKFDIKVTYTWLGIAVAMAFTSIPFVVRTVQPVLEELGPEYEEAAETLGATRWQSFCKVVLPELSPALVAGVALSFTRSLGEFGAVIFIAGNIAWKTEVTSLMIFVRLQEFDYPAASAIASVILAASLLLLFSINTLQSRFGRRVVGH | Part of the ABC transporter complex CysAWTP (TC 3.A.1.6.1) involved in sulfate/thiosulfate import. Probably responsible for the translocation of the substrate across the membrane. | P16701 |
A8FQF8 | UBIA_SHESH | 4-HB polyprenyltransferase | Shewanella | MNLRDKLDVYLRLARMDRPIGTLLLLWPCLMALLLAAGGMPDLKVLTIFIFGVVVMRACGCIINDYADRDLDAHVDRTKSRPLASGEVTGREALILFAVMGLFAFGLVLMLNPLVVKLSVVGIILTIIYPFTKRFTNMPQMFLGVVWSWSIPMAYAAQTGEVPAEAWWLFAANWCWTVAYDTMYAMVDREDDLKVGIKSTAILFGKYDRQIIGLFQLAALACFITAGWAADRGLVYGLGIITFVGFSMYQQKLIHERERAPCFKAFLNNNWAGLSLFIALGVDYLI | Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-... | A8FQF8 |
A1BFX2 | SECA_CHLPD | Protein translocase subunit SecA | Chlorobium | MLKIFEKVFGSKHDKDIKRIQPTIQRINEIQASFQSLSDEALREKGSLLRQQVRSRLLPLEQQKKELALKLENPDILPADADNINASLDALGEEYDKVTALALEESLPDVFALVKETCRRLKGHNYQVMGREMIWDMVPYDVQLIGGIVLHSGKITEMATGEGKTLVSTLPVFLNALTGRGVHVVTVNDYLAQRDKEWMNPVFAFHGLTVGVILNTMRPEERKRQYLCDVTYGTNNEFGFDYLRDNMAGTVEEMVQRDFYFAIVDEVDSVLIDEARTPLIISGPVPNADNSKFQEIKPWIEHLVRSQQQLVASCLVEAEK... | Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains acro... | A1BFX2 |
Q57JP7 | MUG_SALCH | Mismatch-specific uracil DNA-glycosylase | Salmonella | MVKDILAPGLRVVFCGINPGLSSANTGFPFAHPANRFWKVIHLAGFTDRQLKPEEAEKLLDFRCGVTKLVDRPTVQATEVKLHGLRSGGRNLIEKIEDYQPAALAVLGKQAFEQGFSQRGIAWGKQKIAIGATMVWVLPNPSGLNRIKTEKLVEAYRELDQALIMRGL | Excises ethenocytosine and uracil, which can arise by alkylation or deamination of cytosine, respectively, from the corresponding mispairs with guanine in ds-DNA. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and the mispaired base. The complementary strand guanin... | Q57JP7 |
P61197 | LIPA_MYCPA | Sulfur insertion protein LipA | Mycobacterium avium complex (MAC) | MTVAPEGRKLLRLEVRNAETPIERKPPWIRVRARMGPEYTELKSLVRREGLHTVCEEAGCPNIFECWEDREATFLIGGDQCTRRCDFCQIDTGKPAELDRDEPRRVADSVRTMGLRYATVTGVARDDLPDGGAWLYAETVRAIKELNPSTGVELLIPDFNGRPDRLAEVFGSRPEVLAHNVETVPRIFKRIRPAFTYRRSLDVLTAAREAGLVTKSNLILGLGETPDEVRTALADLRGAGCDIITITQYLRPSARHHPVERWVKPEEFVEFARHAEELGFSGVLAGPLVRSSYRAGRLYRQTARARA | Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | P61197 |
B2U7U6 | ADE_RALPJ | Adenine aminohydrolase | Ralstonia | MPISSALAERIATSPKAELHIHIEGSLEPELMFALAERNGVKLPYASVEEVRAAYAFDDLQSFLDLYYAGASVLLTEQDFYDMTAAYVARALADNVHHAEIFFDPQTHTARNVPMHVVIHGIVRALDDAEREHGFSSALILCFLRHLSEEDAFDTLEAALPYIQDPANRIIGVGLDSSERGNPPEKFARVFARCKELGLRLVAHAGEEGPAQYVIDALDILKVERIDHGVRAIDDAALVKRLAAERIALTVCPLSNEKLKVYPDLRDHSLKQLLDAGCAVTLHSDDPAYFGGYMNTNWLATFNALDLSAADAHALARNSF... | Catalyzes the hydrolytic deamination of adenine to hypoxanthine. Plays an important role in the purine salvage pathway and in nitrogen catabolism. | B2U7U6 |
A7H6S7 | AROE_ANADF | Shikimate dehydrogenase (NADP(+)) | unclassified Anaeromyxobacter | MITGRTALYGVLGNPVRHSRSPQMQAAAFEHLGLDATYVALPVEPERLPAAVAGAHALGFQGLNVTVPHKRAVVALCEAVDPVAREVGAVNTLRRTERGWEGFNTDAAACLMLLREEGLRPGAPALLAGAGGAARAAAWALVRAGAVLRIAARRQDAAERLAAELGPLAGPGTPAPVAVPWGALEAEADAAEAVVNGTTVGLHPEDAPLPLRVRAGQLVADFVYGDTPLARAARDAGARLVSGERILVRQGALSFALWTGRAAPEALMAAAIAAPGRAT | 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). | A7H6S7 |
B1YK87 | PRSA_EXIS2 | Foldase protein PrsA | Exiguobacterium | MKKKLLSVAAVASVFTLAACGSNDEAVINYKGGEVNKADVQDEAYQKAGAQIAFQQTMNKLLEKEYGKKVTDKEVEAEVKKTKDQFPDKEQFNTTLQTAGIKNEKEFEKVLRTQMLLKEAKSAKSKVTDKEIEDRFNQEKVEVKASHILVEKESEAKAIKKQLDEGGDFAKIAKAKSTDTGSATKGGDLGYFTKGKMVEEFENYAFKDGVEGKISDPIKTQFGYHIIKVTDRKEKKDFTLEKESDRIKKALAEEKSAQVNPNDIYRSLMKKYDVKVENKDFKDAFDLDKQEQQQMQQQMQQQQQ | Plays a major role in protein secretion by helping the post-translocational extracellular folding of several secreted proteins. | B1YK87 |
Q74L09 | RL10_LACJO | 50S ribosomal protein L10 | Lactobacillus | MSKAIIAKKEKLVDDFAAELKEAKAILVIDYLGLTVEEVTNLRKDLRDANVKMKVIKNTYLKRAAEKAGIEGLEDTFVGPTAVVYTADAEDITEPARIVSKYEDDIDALSIKGGMLEGKVASQEEIKKLAAIPGREGLLSMLVSVLQAPVRNFAYAVKAVADSKDE | Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. | Q74L09 |
P52034 | PFKA_DROME | Phosphohexokinase | Sophophora | MNSEINQRFLARGSQKDKGLAVFTSGGDSQGMNAAVRACVRMAIYLGCKVYFIREGYQGMVDGGDCIQEANWASVSSIIHRGGTIIGSARCQDFRERQGRLKAANNLIQRGITNLVVIGGDGSLTGANLFRQEWSSLLDELVKNKTITTEQQEKFNVLHIVGLVGSIDNDFCGTDMTIGTDTALHRIIEAIDAISSTAYSHQRTFIMEVMGRHCGYLALVGGLACEADFIFIPEMPPKVDWPDRLCSQLAQERSAGQRLNIVIVAEGAMDREGHPITAEDVKKVIDERLKHDARITVLGHVQRGGNPSAFDRILACRMGA... | Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. | P52034 |
Q21CL6 | NTPP_RHOPB | Nucleotide pyrophosphatase | Rhodopseudomonas | MTIWLGSQPLVLASQSYARQMLLQNAGIPFEAIPAAIDERGVQQASGLTSPAEIAARLAEEKALAVSQRLPGRLVLGADQTLALGERTFNKPADRAKATAQLRTLSGRRHELHSAIALVRNGKTVFAETSVARMTMRQLTEAEIEAYLNEAGDAATSSVGGYQVEGLGVHLFDGIHGDHFTILGLPLVPLLNYLRQQRLLAF | Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | Q21CL6 |
Q28594 | IFNT4_SHEEP | Trophoblastin | Ovis | MAFVLSLLMALVLVSYGPGGSLGCYLSQRLMLDARENLKLLDRMNRLSPHSCLQDRKDFGLPQEMVEGDQLQKDQAFPVLYEMLQQSFNLFYTEHSSAAWDTTLLDQLCTGLQQQLDHLDTCRDQVMGEKDSELGNMDPIVTVKKYFQGIHDYLQEKGYSDCAWEIVRVEMMRALTVSTTLQKRLTKMGGDLNSP | Paracrine hormone primarily responsible for maternal recognition of pregnancy. Interacts with endometrial receptors, probably type I interferon receptors, and blocks estrogen receptor expression, preventing the estrogen-induced increase in oxytocin receptor expression in the endometrium. This results in the suppression... | Q28594 |
F1B282 | C4H1_PETHY | Cytochrome P450 C4H1 | Petunia | MDLLLLEKTLIGLFFAIIIAIVVSKLRSKKFKLPPGPIPVPVFGNWLQVGDDLNHRNLTEYAKKFGDLFLLRMGQRNLVVVSSPELAKEVLHTQGVEFGSRTRNVVFDIFTGKGQDMVFTVYGEHWRKMRRIMTVPFFTNKVVQQYRGGWEDEVAHVIDDVKKMPESATNGIVLRKRLQLMMYNNMYRIMFDRRFESEDDPLFNKLKALNGERSRLAQSFEYNYGDFIPILRPFLRGYLKICKEVKQRRLQLFKDYFVDERKKLSTTTKSMDNNALKCAIDHILEAEQKGEINEDNVLYIVENINVAAIETTLWSIEWGI... | Component of the floral volatile benzenoid/phenylpropanoid (FVBP) biosynthetic pathway that controls carbon flux to pigments essential for pollination or UV protection, to numerous pytoalexins synthesized by plants when challenged by pathogens, and to lignins. | F1B282 |
Q0AFJ4 | RBFA_NITEC | Ribosome-binding factor A | Nitrosomonas | MPKDFSRTLRVADQVQRELASLIQNEIMDPRIGMITLTGVEVTRDYTYAKVFYTTLGGNENAQLAEEGLKRAAGFLRSQLAGKIRLRIIPKLQFVYDESIERGIKLSRLIDEAVGKT | One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal heli... | Q0AFJ4 |
P17796 | VIRB6_AGRFC | Protein VirB6 | Agrobacterium tumefaciens complex | MNFTIPAPFTAIHTIFDLAFTTSLDTMLGTIQEAVSAPLVACVTLWIIVQGILVMRGEIDTRGGITRVITVTVVVALVVGQANYHDYVVSVFEETIPNFIQQFSGSGLPLQTIPAQLDTMFALTQAAFQRIASEIGPMNDQDILAFQGAQWVFYGTLWSAFGIYDAVGILTKVLLAIGPLILTGYIFDRTRDIAAKWIGQLITYGLLLLLLNLVATIVILTEATALTLMLGVITLAGTTAAKIIGLYELDMFFLTGDALIVALPAIAGNIGGSYWSGATQSANSLYRRFAQVDRR | VirB proteins are suggested to act at the bacterial surface and there play an important role in directing T-DNA transfer to plant cells. | P17796 |
Q8LAS7 | CNBL2_ARATH | SOS3-like calcium-binding protein 1 | Arabidopsis | MSQCVDGIKHLCTSVLGCFDLDLYKQSGGLGDPELLARDTVFSVSEIEALYELFKKISSAVIDDGLINKEEFQLALFKTNKKESLFADRVFDLFDTKHNGILGFEEFARALSVFHPNAPIDDKIHFSFQLYDLKQQGFIERQEVKQMVVATLAESGMNLKDTVIEDIIDKTFEEADTKHDGKIDKEEWRSLVLRHPSLLKNMTLQYLKDITTTFPSFVFHSQVEDT | Acts as a calcium sensor. CBL proteins interact with CIPK serine-threonine protein kinases. Binding of a CBL protein to the regulatory NAF domain of a CIPK protein lead to the activation of the kinase in a calcium-dependent manner. Binds four calcium ions per subunit. Mediates the activation of AKT1 by CIPK proteins (C... | Q8LAS7 |
P52836 | F3ST_FLACH | Flavonol 3-sulfotransferase | Flaveria | MEDIIKTLPQHTCSFLKHRFTLYKYKDAWNHQEFLEGRILSEQKFKAHPNDVFLASYPKSGTTWLKALAFAIITREKFDDSTSPLLTTMPHDCIPLLEKDLEKIQENQRNSLYTPISTHFHYKSLPESARTSNCKIVYIYRNMKDVIVSYYHFLRQIVKLSVEEAPFEEAFDEFCQGISSCGPYWEHIKGYWKASLEKPEIFLFLKYEDMKKDPVPSVKKLADFIGHPFTPKEEEAGVIEDIVKLCSFEKLSSLEVNKSGMHRPEEAHSIENRLYFRKGKDGDWKNYFTDEMTQKIDKLIDEKLGATGLVLK | Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of rhamnetin > isorhamnetin > quercetin > patuletin > kaempferol >ombuin > tamarixetin, but not quercertagetin, gossypetin or myricetin. O-sulfonation of position 3 of flavonol. May play a role in... | P52836 |
B7J444 | RISB_ACIF2 | 6,7-dimethyl-8-ribityllumazine synthase | Acidithiobacillus | MIRHIEGSLQAGEHRFALLVSRFNSFITQQLEQGAIDALRRHGAKEEQLHVVHVPGAYEMPLIAQKLARSGNYDAVLCLGAVIRGGTPHFDYVAAEVSKGVAQVSMDTGVPVIFGVLTTDSIEQAIERAGTKAGNKGFDAAMTALEMVQLLRQI | 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. | B7J444 |
C1D7F0 | PAND_LARHH | Aspartate 1-decarboxylase alpha chain | Laribacter | MQRTLLKSKLHRVHVTQCELHYIGSCAIDEDLLEAADICEYEEIQIWNVNNGERFATYAIRGERGSGMISVNGSAARRAAVGDILIIATFARFDEQERLEHRPRLVHVDEQNRIIELPAGIPVQAAP | Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. | C1D7F0 |
Q9HL17 | FDHD_THEAC | Sulfur carrier protein FdhD | Thermoplasma | MAGEMVEMEVNESAVGSSKTRVISYLRNAGFLEASDSIAVEEPLAIDILGPDGITVRAGVIMRTPVMDRYLVAGFLYSEGLISGISDIEGFEGVDEDGVSHQNHATVKIGKRIGFNVNSRLLNSACGICGRSTIADLLIRHGKIGTDTRIDSETILGLPTAMGRAQALFLKTGGVHAAALFDVQGRLHAVCEDIGRHNAVDKVVGYTLLEGKDTDNSVLMVSGRAGFEIVEKAFLAGFPIVSSVSAPSSLAIQIAEAVGITLVCFVRNNRFNIYSHPERIIP | Required for formate dehydrogenase (FDH) activity. Acts as a sulfur carrier protein that transfers sulfur from IscS to the molybdenum cofactor prior to its insertion into FDH. | Q9HL17 |
Q5P762 | YBEY_AROAE | Endoribonuclease YbeY | Aromatoleum | MSADTETASSRLALTVQRAIGAENRARSPTSALIRRWALAALRGDAEMTVRLVGEAEGRRLNRDYRGKDYATNVLTFVYDESERLAGDLVLCVPVVAREAAEQGKPLEAHFAHLIVHGMLHLQGFDHEAPDEAEEMETLETRVLATLGYPNPYA | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | Q5P762 |
P28375 | 3SPM_DENJA | Platelet aggregation inhibitor | Dendroaspis | RICYNHLGTKPPTTETCQEDSCYKNIWTFDNIIRRGCGCFTPRGDMPGPYCCESDKCNL | Inhibits ADP-induced platelet aggregation and inhibits the binding of purified platelet fibrinogen receptor alpha-IIb/beta-3 (ITGA2B/ITGB3) to immobilized fibrinogen . Has also been described to inhibit cell adhesion to fibrinogen, fibronectin, laminin and collagen . | P28375 |
A6LD04 | GUAA_PARD8 | Glutamine amidotransferase | Parabacteroides | MHEKLIILDFGSQTTQLIGRRVRELNMYCEIVPYNKFPHDATDVKGVILSGSPYSVYDENAFKADLTEIRGKYPVLGICYGAQFLAYTSGGNVEPANSREYGRANLSHIDGEDELLKGIHVGSQIWMSHGDTITVLPDNFKVIASTDDVRAAAYHVEGEQTWGVQFHPEVFHSTDGTKLLDNFLNICGCAKDWTPASFIESTVAELKEQLGDDKVILALSGGVDSSVTAVLLNKAIGKNLTCIFVDHGLLRKNEFENVMRDYEHLGLNVIGVNAKDKFYKELAGVTEPEKKRKIIGKGFIDVFDEEAHKLKDIKWLGQGT... | Catalyzes the synthesis of GMP from XMP. | A6LD04 |
O51718 | APT_BORBU | Adenine phosphoribosyltransferase | Borreliella | MKNKTEYYDQFISKIPNFPKKGVLFYDITSVLLKPEVYSSLINEVYSFYNFKKIDCIAVVESRGYLIGAPLSLKMQLPLVLIRKEGKLPREVFSEEYELEYGFGRIEVHKDDVRTYSNILLIDDILATGGTLKSSAILLERAGGKVKDIFCFIELCAINGRQSLESYEVNSLVRYN | Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. | O51718 |
P85266 | TX35D_CTEON | Neurotoxin Oc F17-11 | Oligoctenus | GKCGEINGSCDECYGGSVTCDCY | Insecticidal neurotoxin that reversibly inhibits the N-methyl-D-aspartate (NMDA)-subtype of ionotropic glutamate receptor (GRIN) and inhibits inactivation of insect sodium channels (Nav). In vivo, is highly toxic to insects. | P85266 |
O73849 | SOMA_RHIMB | Growth hormone | Rhinella | MASGLCSSLGLLLIMCLQSPPGFSAFPQIPLASLLNNAVIRAQYIRQVVADTYRDYEQTFIREDKRYSNKNSYAMFCYSETIPAPTDKDNTHQKSDIDLLRFSLTLIQSWMTPVQSLNKLFTNQVFGNAVYEKLRDLEEGLYALMRELDDGNARNYGLLTFTYDKFDPHPDSDDDGRIKNYGLLSCFKKDMHKVETYLKVMKCRRFVESNCMV | Growth hormone plays an important role in growth control. | O73849 |
Q8FJX7 | NAGB_ECOL6 | Glucosamine-6-phosphate isomerase | Escherichia | MRLIPLTTAEQVGKWAARHIVNRINAFKPTADRPFVLGLPTGGTPMTTYKALVEMHKAGQVSFKHVVTFNMDEYVGLPKEHPESYYSFMHRNFFDHVDIPAENINLLNGNAPDIEAECRQYEEKIRSYGKIHLFMGGVGNDGHIAFNEPASSLASRTRIKTLTHDTRVANSRFFDNDVNQVPKYALTVGVGTLLDAEEVMILVLGSQKALALQAAVEGCVNHMWTISCLQLHPKAIMVCDEPSTMELKVKTLRYFNELEAENIKGL | Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion. | Q8FJX7 |
Q87M06 | PNP_VIBPA | Polynucleotide phosphorylase | Vibrio | MFEKPVVKTFQYGNHTVTLETGVIARQATAAVMVTMDDTAVFVSVVGKKEAVAGQDFFPLTVNYQERTYAAGKIPGGFFKREGRPSEGETLTARLIDRPIRPLFPDAFKNEVQVIATVVSVNPDVQPDIPTMIGTSAALAISGIPFNGPIGAARVGHIDGQLVLNPSQTELNASRLDLVVAGTESAVLMVESEADNLTEEEMLAAVVFGHDQQQVVINAINEFKAEVATPAWDWVAPEENTALKTKIAELAEAKLVEAYQITEKMARYDRIHEIAAEVNEALLAQDPEADTKEIHTIFHDLEKTVVRRSIIAGNPRIDGR... | Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. | Q87M06 |
Q14GD9 | KGUA_FRAT1 | GMP kinase | Francisella | MNNYIFIVSAPSGAGKSSLLKAFLATDIGKDNYAVAISHTTREPRVGEINSREYYFVTVAEFEQLLSQDGFIEYAKVFKNYYGTSKAELDRLLALGKNIILEIDWQGAQQTRAIYGDRAKSIFILPPSLDELRKRLEKRNTDSKETIDYRMEQAQSEISHADEYDYLLVNDDFSQSLEQFCKYFEQNIQS | Essential for recycling GMP and indirectly, cGMP. | Q14GD9 |
P13125 | DN7E_SULAC | Sac7e | Sulfolobus | MAKVRFKYKGEEKEVDTSKIKKVWRVGKMVSFTYDDNGKTGRGAVSEKDAPKELMDMLARAEKKK | Can constrain negative DNA supercoils. May be involved in maintaining the integrity of the genome at high temperature. | P13125 |
Q9KGG3 | MCSB_HALH5 | Protein-arginine kinase | Halalkalibacterium (ex Joshi et al. 2022) | MSLQRFISEAISPWMKKDGPDSDIVLSSRIRLARNLQSFRFPLLATIEESKQLVEHVKHHLAESSYHTNRFELLCMDDMKPNVKRVLVEKHLISPHLAEESKHGAVMLSEDESISIMINEEDHLRIQCLFPGFQLSEALVLASGIDDWIEGKVDYAFDEKRGYLTSCPTNVGTGLRASVMMHLPALVMTQQINRILPAINQLGLVVRGIYGEGSEALGNLFQISNQMTLGKSEEDIVEDLRGVVMQLIQQERAARKRLLESSRLQLEDRVYRSYGILAHSRIIESKEATQKLSDVRLGIDLGLLKGVSGNILNELMILTQ... | 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, ... | Q9KGG3 |
B9LGS9 | NUON_CHLSY | NDH-1 subunit N | Chloroflexus | MFQLTDIPRLLPEILLLVLALLVLGSDILERWGRTPEAQLERVKSSASLTAIGLGMVLVVALLQSGYLYQLPETAPVNFFTNIIRNLQSGGPGGDPIIGVFATDHLTMIARLLIIGAALVTSLLCLDIRPNAHPGEFYALIIFATLGMCLMVGANELLLAYLAIELTSIPLYLLAGYFRNDPRSAEAGLKYFLFGAISSAILLYGMSLAFGAALNAVGGATNFNDLTRFDRIGAFTGSSGGLLTLAMLFIVAGMGYKLAVVPFHGWSPDVYEGSPTPITAFISTASKAAGFILLFRLLTETFPAMAGAPTLNEEAGGWTA... | 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... | B9LGS9 |
C3PFR5 | ATPB_CORA7 | F-ATPase subunit beta | Corynebacterium | MTTALQEQNTQSSATAGRVVRVIGPVVDVEFPRGGLPALYNALTVEVTLEAVAKTVTLEVAQHLGDNLVRAVSMAPTDGLVRGAAVTDTGKPISVPVGDVVKGHVFNALGDCLDQPGLGRDGEQWGIHREPPAFDQLEGKTEILETGIKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMITRIAREFSGTSVFAGVGERTREGTDLFLEMEEMGVLQDTALVFGQMDEPPGVRMRVALSGLTMAEYFRDVQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPTLADEMGVLQERITSTKGKSITSLQAVYVPAD... | Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | C3PFR5 |
Q9ZDE5 | RUVB_RICPR | Holliday junction ATP-dependent DNA helicase RuvB | typhus group | MTNILSPEKSEHDQELPIRPSYLKEFVGQQQIKENLLVFIKAAKSRNEHLDHTLFYGPPGLGKTTLAKIISNEIGGNFKSTAGPAIIKAADLASILTNLEKNDVLFIDEIHRLNTLVEEVLYSAMEDFELDIIIGEGSAARPVKITLPKFTLIGATTRFGLISNPLRDRFGIPMRLNFYNTEELKQVLNRASKLLDIDLTDSGSEEIAKRSRGTPRIALRLLRRIRDFAVVDGKSRIDKEICDFGLKRLTVDSIGLDSNDYRYLKFIADNYHGGPVGIETIAAALSEQRDELEETIEPYLIKIGLVKRTPRGRVITIAAF... | Participates in UV-tolerance of Synechocystis PCC 6803. | Q9ZDE5 |
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