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 |
|---|---|---|---|---|---|---|
B6YWA4 | HIS1_THEON | ATP phosphoribosyltransferase | Thermococcus | MRFVLPKGRLFKGSLEILKKAGIELKPPETRELIVRNGRYELLLARAFDVPVYVEHGIDVGIAGSDVVEERGSDVLVPLELPFGKCRLSLAMPKESAVSVEEMDGFRIATKYPNLARKFFERNGVEVEVIKLHGSIELAPKIGVADAIVDIVETGNTLRANGLVEVEKIMDVSALLLVNRISQKTKFDEINELVLKIKEVVRDGF | Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. | B6YWA4 |
P51793 | CLCN4_HUMAN | Chloride transporter ClC-4 | Homo | MVNAGAMSGSGNLMDFLDEPFPDVGTYEDFHTIDWLREKSRDTDRHRKITSKSKESIWEFIKSLLDAWSGWVVMLLIGLLAGTLAGVIDLAVDWMTDLKEGVCLSAFWYSHEQCCWTSNETTFEDRDKCPLWQKWSELLVNQSEGASAYILNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNFFSSLFSKYSKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINPFGNSRLVLFY... | Strongly outwardly rectifying, electrogenic H(+)/Cl(-)exchanger which mediates the exchange of chloride ions against protons . The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons . The presence of conserved gating glutamate res... | P51793 |
B9DSX4 | RS13_STRU0 | 30S ribosomal protein S13 | Streptococcus | MARIAGVDIPNDKRVVISLTYVYGIGLATSKKILAAAGISEDVRVKDLTSDQEDAIRREIDSIKVEGDLRREVNLNIKRLMEIGSYRGIRHRRGLPVRGQNTKNNARTRKGKATAIAGKKK | Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites. | B9DSX4 |
A5FB63 | CHIA_FLAJ1 | Chitinase ChiA | Flavobacterium | MKHYYRLLFLLLFPLLASAQPAHGKKVVGYYAQWSIYARDFNVPKIDGSKLTHLNYSFYGTTYDPAHPENTKLKCLDTYADFEHMEGGIPWDAPVKGNFYDLMKLKQKYPHLKILISVGGWTKGQDLSPIAASPVARAALAADMANFIVTYPFIDGFDIDWEYPLSGGTDGTEIVNGMPVPPQKYSPDDNKNLVLLLKAMRQAMPNKLVTIAAGNNVRNVSKQYLGPNNRAQYGMTEDISTYCDYITYFGYDFGGNWYDKTCYNAPLYASGNPNDPLYGATQSESLDELTNQYLNVIGFPANKLIMGLPFYGKKFDNVAA... | Major extracellular chitinase, which is essential for chitin utilization. | A5FB63 |
Q10XP0 | COBQ_TRIEI | Cobyric acid synthase | Trichodesmium | MKAIMVVGTTSHAGKSLITTAICRILSRRGWKVTPFKGQNMALNSYVTSTGGEMGHAQAVQAWAAGVTPAIEMNPILLKPQGDMTSQVIIKGKASGTVGAVDYYQQYFDIGWNAIQESLETLSQEFNMIVCEGAGSPAEINLKHRDLTNMRVAKHLNASTILVVDIDRGGAFAHIIGTLELLEPEERNLIKGIVINKFRGQRSLLDSGIHWLEKKTNIPVIGVIPWINEAFPAEDSLSILEQRYNKHTTDITIAIIRLPRISNFTDFEPLEAESSVKIKYIHPNDSLGDPDAIIIPGTKTTINDLLVLQKSGMAEAIKSY... | Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. | Q10XP0 |
P07281 | RS19B_YEAST | YS16B | Saccharomyces | MAGVSVRDVAAQDFINAYASFLQRQGKLEVPGYVDIVKTSSGNEMPPQDAEGWFYKRAASVARHIYMRKQVGVGKLNKLYGGAKSRGVRPYKHIDASGSINRKVLQALEKIGIVEISPKGGRRISENGQRDLDRIAAQTLEEDE | Required for proper maturation of the small (40S) ribosomal subunit. Binds to 40s pre-ribosomal particles, probably required after association of NOC4 but before association of ENP1, TSR1 and RIO2 with 20/21S pre-rRNA. | P07281 |
Q0HTS9 | LPXK_SHESR | Lipid A 4'-kinase | Shewanella | MQVLVNKIWYEGHPLRWLLLPFSVLFALITAIRRSLFRLGLKSQTPLPVPVIVVGNITVGGSGKTPTVIYLIELLRQQGFNPGVISRGYGADIQGVKVVTAADSAASVGDEPAMIVARTGVPMVVGAKRVDTAKALLAQFAVDVIICDDGLQHYALGRDIELVVIDGKRGLGNRHLLPAGPLREGAWRLNQVDFVVVNGGPAQANQYEMQLSPSAVLPVNPKAVAVFDPTQPVVAMAGIGHPARFFETLTQQGFQLALSHGFDDHQAYDKEVLCELAASRPLMMTEKDAVKCRDFAQENWWYLAVDAKLSPQFDQQLLSR... | Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA). | Q0HTS9 |
Q8YJ37 | ATPA_BRUME | F-ATPase subunit alpha | Brucella | MDIRAAEISAILKEQIKNFGKEAEVSEVGQVLSVGDGIARVYGLDNVQAGEMVEFPGGIRGMALNLESDNVGVVIFGADRDIKEGDVVKRTGAIVDVPVGPELLGRVVDALGNPIDGKGPIKAKERRRVDVKAPGIIPRKSVHEPMSTGLKAIDALIPVGRGQRELVIGDRQTGKTAIILDTFLNQKPIHDNGPDKDKLYCVYVAVGQKRSTVAQFVKVLEERGALEYSIVVAATASDPAPMQYLAPFAGCAMGEYFRDNGQHALIGYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLNDENGAGS... | Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | Q8YJ37 |
Q2YBA4 | RRF_NITMU | Ribosome-releasing factor | Nitrosospira | MIAEIKKSAEQKMQKSLEALKLDLGKIRTGRAHTGLLDHVTVDYYGNPTAINQVANISLADARTITVAPWEKKMLGAIEKAIRNSDLGLNPTTVGELIRVPMPPLTEERRRDLTKVVKHEGEAARVAMRNIRRDANAHLKDLLKEKKIAEDEERKGQEDIQKLTDRYIADIDKLLQAKEAELMAV | Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another. | Q2YBA4 |
Q5RE69 | NEP_PONAB | Skin fibroblast elastase | Pongo | MGKSESQMDITDINTPKPKKKQRWTPLEISLSVLVLLLTIIAVTMIALYATYDDGICKSSDCIKSAARLIQNMDATAEPCTDFFKYACGGWLKRNVIPETSSRYGNFDILRDELEVVLKDVLQEPKTEDIVAVQKAKTLYRSCINESAIDSRGGEPLLKLLPDVYGWPVATENWEQKYGASWTAEKAIAQLNSKYGKKVLINLFVGTDDKNSVNHVIHIDQPRLGLPSRDYYECTGIYKEACTAYVDFMISVARLIRQEERLPIDENQLALEMNKVMELEKEIANATAKPEDRNDPMLLYKKMTLAQIQNNFSLEINGKP... | Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids. Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond. Catalyzes cleavage of bradykinin, substance P and neurotensin peptides. Able to cleave angi... | Q5RE69 |
Q3K2B0 | AROA_STRA1 | 5-enolpyruvylshikimate-3-phosphate synthase | Streptococcus | MKLLTNANTLKGTIRVPGDKSISHRAIIFGSISQGVTRIVDVLRGEDVLSTIEAFKQMGVLIEDDGEIITIYGKGFAGLTQPNNLLDMGNSGTSMRLIAGVLAGQEFEVTMVGDNSLSKRPMDRIALPLSKMGARISGVTNRDLPPLKLQGTKKLKPIFYHLPVASAQVKSALIFAALQTKGESLIVEKEQTRNHTEDMIRQFGGHLDIKDKEIRLNGGQSLVGQDIRVPGDISSAAFWIVAGLIIPNSHIILENVGINETRTGILDVVSKMGGKIKLSSVDNQVKSATLTVDYSHLQATHISGAMIPRLIDELPIIALL... | Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. | Q3K2B0 |
B9L5I6 | SUCC_NAUPA | Succinyl-CoA synthetase subunit beta | Nautilia | MNIHEYQAKEIFRKYGVPTPRGGVAFTGPEARRVAEELGGNLWVVKAQIHAGGRGKAGGVKLAKSLDEVEKIAEEMLGMTLVTHQTGPEGKVVKKVYIEEGADIKDELYLGMVLDRALEMPVMMASTEGGMEIEEVAEKTPEKIIKVAIDPAIGFQPFHARKLAFGLGLPKDEQREFIKFASALYNVYMDNDAEMIEINPLIKTGDGKFLALDAKMGFDDNALYKHPEIAEMRDLDEEEPTEVEAKKYGLSYIKLDGNVGCMVNGAGLAMATMDIIKHEGGEPANFLDVGGGANPDTVAKGFEIILSDPNVKSIFVNIFG... | Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinat... | B9L5I6 |
Q5HNZ4 | FUR_STAEQ | Ferric uptake regulation protein | Staphylococcus | MNTNDAIKVLKENGLKYTDKRKDMLDIFVKEDKYLNAKHIQQQMDKDYPGISFDTVYRNLHLFKDLGIIESTELDGEMKFRIACTNHHHHHFICENCGETKVIDFCPIEKIKSQLPNVNIHTHKLEVYGICEECQRKAN | Acts as a global negative controlling element, employing Fe(2+) as a cofactor to bind the operator of the repressed genes. | Q5HNZ4 |
B8FP45 | GATC_DESHD | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C | Desulfitobacterium | MKISREEVEHVAFLARLELTEEELVTNTEQLNSILDYAAMLEKLNTDDIKPTAHAVPLHNVLREDQVKPSMAREKVLANAPDAQDGFFKVPRIV | Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated ... | B8FP45 |
Q5HQR7 | AROD_STAEQ | Type I dehydroquinase | Staphylococcus | MTHVDIAATIAPEDKLSKTLLKDIKVNEESIDIIELRIDQWPSFNKALLNEVIKQLKIFHLKILVTYRTSVQGGKGAVNEQEYLNILGELIECPQFDMIDIEWSSAVKIEKYTHLVQRAQQKGLEVVLSHHNFQETPALDELKFIYFKMQKLNPEYLKLAVMPKCQEDVLHLLEAMSLTAKHTTCRIVGISMSSLGKVSRIAQGVFGGTLSYGCIEEPQAPGQIHVSKLKSMVSFYED | 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. | Q5HQR7 |
B1JAU1 | FABA_PSEPW | Trans-2-decenoyl-[acyl-carrier-protein] isomerase | Pseudomonas | MTKQHAFTREDLLRCSRGELFGPGNAQLPAPNMLMVDRITHISEEGGKYGKGELVAELDITPDLWFFACHFEGDPVMPGCLGLDAMWQLVGFFLGWQGLPGRGRALGSGEVKFFGQVLPTAKKVTYNIHIKRVLKGKLNMAIADGSVSVDGREIYTAEALRVGVFTSTDNF | Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active ... | B1JAU1 |
B7NPB4 | LLDD_ECO7I | L-lactate dehydrogenase | Escherichia | MIISAASDYRAAAQRILPPFLFHYMDGGAYSEYTLRRNVEDLSEVALRQRILKNMSDLSLETTLFNEKLSMPVALGPVGLCGMYARRGEVQAAKAADAHGIPFTLSTVSVCPIEEVAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPTPGARYRDAHSGMSGPNAAMRRYLQAVTHPQWAWDVGLNGRPHDLGNISAYLGKPTGLEDYIGWLGNNFDPSISWKDLEWIRDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMIA... | Catalyzes the conversion of L-lactate to pyruvate. Is coupled to the respiratory chain. | B7NPB4 |
A4IYC3 | YBEY_FRATW | Endoribonuclease YbeY | Francisella | MDNLNINFINDDEHPIPSQDLLLKCLQLVADKHHISHAEVNLNIVSNDEIQQINKQFRNKDKPTNIISFKFEKPQGLPDDIANDFLGDIVIAPAVLENEAKEQNKELNDHWQHIFIHGLLHLLGYNHQDDQEAEVMENLEIQLLAQLGIANPYIEQENQNGR | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | A4IYC3 |
Q02I76 | RIMO_PSEAB | Ribosome maturation factor RimO | Pseudomonas | MSTPTPKVGFVSLGCPKALVDSERILTQLRMEGYEVVPTYEDADVVVVNTCGFIDSAKAESLEVIGEAIAENGKVIVTGCMGVEEHTIRDVHPSVLAVTGPQQYEQVVTAVHEVVPPKTEHNPLVDLVPPQGVKLTPRHYAYLKISEGCNHSCSFCIIPSMRGKLVSRPVGDVLSEAERLVKAGVKELLVISQDTSAYGVDLKYKTDFWNGQPVKTRMKELCEALSSMGVWVRLHYVYPYPNVDDVIPLMAAGKLLPYLDIPFQHASPKVLKAMKRPAFEDKTLARIKQWREICPELTIRSTFIVGFPGETEEDFQYLLD... | Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12. | Q02I76 |
B1XHY7 | ATPG_SYNP2 | F-ATPase gamma subunit | unclassified Synechococcus | MPNLKGIRDRIQSVKNTKKITEAMRLVAAAKVRRAQEQVTSTRPFANTLLQVLYSLKSRLRLEEADLPLLKQREVKCVGLLVITGDRGLCGGYNANIIRKAERRAKELAAAGINYKFVLVGRKAVQYFQNRQAPVAKTYAGLEQIPSAAEASDIADELLSLFLSEEVDKIELIYTRFVSLISSQPVVQTLLPLVPEALTNPDDETFNLITRGGKFQVEREKVATEVKELPADMIFEQDPKDILNALLPLYLSNQLLRALQEGAASELAARMTAMNNASDNASDLMKTLTLSYNKARQAAITQELSEVVAGANAL | Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. | B1XHY7 |
Q9S0X4 | TAL_METAM | Transaldolase | Methylomonas | MANLFDQLKEFTTIVADTGDVEAIKSVKPYDATTNPSLLLKASTLPQYAPLIDEAIAYAKSQSGDKAQQIEDAADKLAVLIGQEILKHIPGKISTEVDARLSFDTDAMVQKGRKLIKLYADAGISKDRVLIKLASTWEGIKAGEILEKEGINCNLTLLFSFAQARACAEAGVFLISPFVGRILDWYKAKTGENYTSETDPGVLSVRKIYAYYKEHGYKTVVMGASFRNTGEITALAGCDRLTVSPNLLERAEGYRRYLPRVLVDNGATKQRPALLTEKEFRFDQNEDAMATEKLAEGIRGFVVDQNKLEKALAEKL | Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. | Q9S0X4 |
B7MZ04 | NORR_ECO81 | Anaerobic nitric oxide reductase transcription regulator NorR | Escherichia | MSFSVDVLANIAIELQRGIGHQDRFQRLITTLRQVLECDASALLRYDSRQFIPLAIDGLAKDVLGRRFALEGHPRLEAIARAGDVVRFPADSELPDPYDGLIPGQESLKVHACVGLPLFAGQNLIGALTLDGMQPDQFDVFSNEELRLIAALAAGALSNALLIEQLESQNMLPGDAASFEAVKQTQMIGLSPGMTQLKKEIEIVAASDLNVLISGETGTGKELVAKAIHEASPRAVNPLVYLNCAALPESVAESELFGHVKGAFTGAISNRSGKFEMADNGTLFLDEIGELSLALQAKLLRVLQYGDIQRVGDDRSLRVD... | Required for the expression of anaerobic nitric oxide (NO) reductase, acts as a transcriptional activator for at least the norVW operon. Activation also requires sigma-54. | B7MZ04 |
Q9CR02 | TMA16_MOUSE | Translation machinery-associated protein 16 | Mus | MPKGLKGKMVGREKKVIHPYSRKAAQITRESHKQDKKERLKTEKALRLNLIGDKLQWFHSHLDMKKTRYSKKDACELVERYLDRFSSELEQIELQNSIKDRQGRRHHSREAVIKQTLERERQQYEGYGFEIPDILDSNTLQTFREWDFDLKKLPNIKMRKLCADDAVPKKRKQKNILNIEKDLGELELSGPTGATTDGKLEPASESSDTDEEMTPVPVSPH | Involved in the biogenesis of the 60S ribosomal subunit in the nucleus. | Q9CR02 |
A4TE25 | DDL_MYCGI | D-alanylalanine synthetase | Mycolicibacterium | MNARIRVAVVYGGRSSEHAISCVSAGSILRNLDPDRFEVTAVGITPEGSWVLTEGRPETLAITDGKLPGVTGDSGTALTLTADPARRGQLVSLGEAAGEVLASADVVFPVLHGPYGEDGTIQGLLELAGVPYVGAGVLASAAGMDKEFTKKLLASAGLPVGDHVVLRARDSTLSLQDRERLGLPVFVKPSRGGSSIGVSRVTAWDELPAAIELARRHDPKVIIEAAVPGRELECGVLEFPDGHLEASTLGEIRVEGVRGREDGFYDFETKYLDDGAELDVPAKVDDDVAEAIRALSLRAFTAIDCQGLARVDFFLTDDGP... | Cell wall formation. | A4TE25 |
Q9WYI1 | AROE_THEMA | Shikimate dehydrogenase (NADP(+)) | Thermotoga | MKFCIIGYPVRHSISPRLYNEYFKRAGMNHSYGMEEIPPESFDTEIRRILEEYDGFNATIPHKERVMRYVEPSEDAQRIKAVNCVFRGKGYNTDWVGVVKSLEGVEVKEPVVVVGAGGAARAVIYALLQMGVKDIWVVNRTIERAKALDFPVKIFSLDQLDEVVKKAKSLFNTTSVGMKGEELPVSDDSLKNLSLVYDVIYFDTPLVVKARKLGVKHIIKGNLMFYYQAMENLKIWGIYDEEVFKEVFGEVLK | 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). | Q9WYI1 |
P81060 | PEN3C_PENVA | Penaeidin-3c | Penaeus | MRLVVCLVFLASFALVCQGQVYKGGYTRPIPRPPFVRPVPGGPIGPYNGCPVSCRGISFSQARSCCSRLGRCCHVGKGYSG | Antibacterial activity against M.luteus and E.coli bacteria. Antifungal activity against N.crassa and F.oxysporum. Presents chitin-binding activity. | P81060 |
Q2YY57 | RECU_STAAB | Recombination protein U homolog | Staphylococcus | MNYPNGKPYRKNSAIDGGKKTAAFSNIEYGGRGMSLEKDIEHSNAFYLKSDIAVIHKKPTPVQIVNVNYPKRSKAVINEAYFRTPSTTDYNGVYQGYYIDFEAKETKNKTSFPLNNIHDHQVEHMKNAYQQKGIVFLMIRFKTLDEVYLLPYSKFEIFWKRYKDNIKKSITVDEIRKNGYHIPYQYQPRLDYLKAVDKLILDESEDRV | Endonuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves mobile four-strand junctions by introducing symmetrical nicks in paired strands. Promotes annealing of linear ssDNA with homologous dsDNA. Required for DNA repair, homologous recombination and chromosome segregation. | Q2YY57 |
B9MFY7 | PURA_ACIET | IMP--aspartate ligase | Diaphorobacter | MKASKGRNVVVVGTQWGDEGKGKLVDWLTESAQGVVRFQGGHNAGHTLVINGVKTALHLIPSGIMRPGVKCYIGNGVVLSAGKLFEEIEGLEKAGVEVRSRLRVSEACPLILPFHAALDVAREAAREHGGAEKIGTTGRGIGPAYEDKIARRALRVQDLKYPERFAAKLRELLALHNHVLSTFLGSANFQFGDALKPYITGGQVQFEPVFDEAMRHAEMLKPMMADVSRELNEAHAAGANLLFEGAQGTLLDVDHGTYPYVTSSNCVAGNAAAGSGVGPGHLHYILGITKAYCTRVGGGPFPTELDWETPGTPGYHMSTV... | 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. | B9MFY7 |
A0A3B1EFQ2 | STR9_STRTC | Strobilurin A biosynthesis cluster protein r9 | Strobilurus | MAVDRKIRIAVVGGGPGGVIAALALSKSPNVEIDLYEAATAFGDIGLSLGMPWRPWRILRLLGLQGYLAALLPPDQIPKEDVTVPTIHYRKSDQAVGEDIFTCTSLSGYTRFRRSHFHAALLPHLPSNCKTYTSKRLVSYAEPSNASDPIVITFADGTTAECDVLVGADGIKSPTRASMYNYAADEAEKAGRSAEANDLRSKIRAKFSGVEVYRSVISAEQLRAAAPDHHAFRCPTQFLGKEKVRMPTYPIQSENSQFLNCALYICDYSREGEDYPEPWVTDVEAKDLRSSLPDWEPEAQAAVSCMGEVVSRWAICTLSP... | FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of strobilurin A, an antifungal polyketide that contains a key beta-methoxyacrylate toxophore that targets the complex III of the mitochondrial electron transport chain . Strobilurin biosynthesis begins with construction of benzoyl CoA... | A0A3B1EFQ2 |
A4Y7I2 | PYRD_SHEPC | Dihydroorotate oxidase | Shewanella | MFYKIAQKVMFQMDPERAHNLAIGSLKMTGNSPLNCFYRQTIAPAPVTFMGLTFPNPVGLAAGMDKDGESIDAFHAMGFGHIEVGTVTPRPQPGNDLPRLFRLKPAKGIINRMGFNNKGVDNLVRNLIAKKSDIMVGVNIGKNKDTPVEQGKDDYLICMDKVYPYAAYIAVNISSPNTPGLRSLQYGDLLDELLSAIKTKQLELAEKHKKYVPIALKIAPDLTIEEIENIADALIKNKFDGAIATNTTLTRDGVSGLANANESGGLSGKPLTELSTKVIRQLAACLKGQIPIIGVGGINSAEDALAKFDAGATMVQIYSG... | Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. | A4Y7I2 |
O14236 | NOG2_SCHPO | Nucleolar GTP-binding protein 2 | Schizosaccharomyces | MGTYKKEKSRIGREGANEKKPGNLRVKGENFYRNAKDVARVNMYRGGKAKYNAAGELVRAAEFQSSEVPKARIQPDRRWFNNTRVIAQPTLTQFREAMGQKLNDPYQVLLRRNKLPMSLLQENTEIPKVRVLESEPFENTFGPKSQRKRPKISFDSVAELAKESDEKQNAYEEKIEERILANPDESDDVMLAARDAIFSKGQSKRIWNELYKVIDSSDVLIQVLDARDPVGTRCGTVERYLRNEASHKHMILVLNKVDLVPTSVAAAWVKILAKEYPTIAFHASINNSFGKGSLIQILRQFASLHSDKKQISVGLIGFPN... | GTPase that associates with pre-60S ribosomal subunits in the nucleolus and is required for their nuclear export and maturation. | O14236 |
Q8UIQ2 | LEPA_AGRFC | Ribosomal back-translocase LepA | Agrobacterium tumefaciens complex | MSTNSTRTPLDHIRNFSIVAHIDHGKSTLADRLIQSTGGLAERDMSEQVLDSMDIERERGITIKAQTVRLHYKANNGETYVLNLIDTPGHVDFAYEVSRSLSACEGSLLVVDASQGVEAQTLANVYQAIDNNHELVTVLNKIDLPAAEPERIKEQIEEVIGIDASDAVMISAKTGLGIPDVLEAIVNRLPPPKSDVGENGPLKALLVDSWYDTYLGVMVLVRVIDGVLTKGQQIRMMGSGAKYGVERVGVLTPKMVNVDSLGPGEIGFITASIKEVADTRVGDTITDDKRPTAQALPGFKPAQPVVFCGLFPVDAADFED... | Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-t... | Q8UIQ2 |
P31743 | GSPF_AERHY | General secretion pathway protein F | Aeromonas | MTEGDSARQVRQQLREQGLTPLEVNETTEKAKREANRFVLFRRGASTSELALITRQLATLVGAGLTIEEALRAVAEQCEKAHLRSLVATVRSKVVEGYSLADSLGAFPHVFDQLFRSMVAAGEKSGHLEKVLNRLADYTEQRQHMRTKLLQAMIYPIVLTLVAVGVISILLTAVVPKVVAQFEHMGQQLPATTRFLIGTSELMQHYGLWFLLLLFIGGFVWRWWLTDEKRRRHWHQVVLRLPVIGRVSRGLNTARFARTLSILNASAVPLLEGMKIAGEVLSNDFARTRIGEATERVREGTSLRKALDETKIFPPMMLHM... | Component of the type II secretion system inner membrane complex required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. | P31743 |
Q68X16 | NUOA_RICTY | NUO1 | typhus group | MLQNSELLHEYLPIAIFFGIAVLVSGLIMMLPNLLSTKKYNKDKLEPYECGFAPFSDARSKFDIRFYLVAILFIIFDLEITFLVPWAISLNTIGKIGFFSMMFFLFVLIIGFIYEWTKGALDW | 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... | Q68X16 |
Q8L4H4 | NORK_MEDTR | Symbiosis receptor-like kinase | Medicago | MMELQVIRIFRLVVAFVLCLCIFIRSASSATKGFESIACCADSNYTDPKTTLTYTTDHIWFSDKRSCRQIPEILFSHRSNKNVRKFEIYEGKRCYNLPTVKDQVYLIRGIFPFDSLNSSFYVSIGVTELGELRSSRLEDLEIEGVFRATKDYIDFCLLKEDVNPFISQIELRPLPEEYLHGFGTSVLKLISRNNLGDTNDDIRFPDDQNDRIWKRKETSTPTSALPLSFNVSNVDLKDSVTPPLQVLQTALTHPERLEFVHDGLETDDYEYSVFLHFLELNGTVRAGQRVFDIYLNNEIKKEKFDVLAGGSKNSYTALNI... | Involved in the perception of symbiotic fungi and bacteria. Part of the perception/transduction system leading to nodulation or mycorrhizal infection . Phosphorylates PUB1 . | Q8L4H4 |
O86418 | RBCX_NOSS1 | RuBisCO chaperone RbcX | Nostoc | MNLKQIAKDTAKTLQSYLTYQALMTVLAQLGETNPPLALWLHTFSVGKVQDGEAYVKELFREQPDLALRIMTVREHIAEEVAEFLPEMVRSGIQQANMEQRRQHLERMTHLSLSNPSPESEQQTISDTDWDH | When rbcL-rbcX-rbcS or rbcL-rbcS were overexpressed in E.coli no change in reconstituted RuBisCO activity was observed, which suggests RbcX plays no role in RuBisCO assembly in this system . However in PubMed:8472962 E.coli chaperones groL and groS were also overexpressed, which may compensate for lack of rbcX (Probabl... | O86418 |
C6E7U2 | HEMH_GEOSM | Protoheme ferro-lyase | unclassified Geobacter | MSSKTALLLLQMGGPDSLDAVHPFLMKLFTDRDIIKIGPAFLQPFIARRIVNKRAPKVEEYYRQIGGKSPIRELTEAQGEGLQQLLGEDFRSFVAMRYSRPSTIDALAAIKRAGIERVIALSLYPHYSRATTGSSVNELKRVLNESGAKFEISYIDRFYNHPLYIKALSEKVVQGLAAFPDSKDVEIVFSAHSLPQSFIEEGDPYLDHIQETVRLVMEQVGEGSHTLCFQSKASRVKWLEPSTEATIEQMAKAGKKNLLMVPLSFVSDHIETLYEIDIQYGEEAKALGIERFIRTESLNSSPLFLECLADLVKTAAK | Catalyzes the ferrous insertion into protoporphyrin IX. | C6E7U2 |
A4VUJ6 | RIMM_STRSY | Ribosome maturation factor RimM | Streptococcus | MNYFNVGKIVNTQGLQGEMRVLSVTDFAEERFKKGAKLALFDDKDQFAMEVEIASHRKAKNFDIIKFKGMYHINDIEKYKGFSLKIAEENLTDLEDGEFYYHEIIGLDVYENDILIGQIKEILQPGANDVWVVKRKGKKDLLLPYIPPVVLNIDIPNNRVDVELLEGLDDEN | An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Probably interacts with S19. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosoma... | A4VUJ6 |
P49513 | PSBK_TRICV | Photosystem II reaction center protein K | Trieres | MESLLLARLPEAYVVFSPIVDVLPIIPVFFLLLAFVWQAAIGFR | One of the components of the core complex of photosystem II (PSII). 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 core antenna complex that captures photons, a... | P49513 |
B5CY73 | BAGA_PHOPM | Glycosyl hydrolase 16 family protein A | Phocaeicola | MKRKLFTICLASLQFACAAENLNNKSYEWDIYPVPANAGDGMVWKLHPQSDDFNYIADEKDKGKEFYAKWTDFYHNHWTGPAPTIWQRDHVSVSDGFLKIRASRPEDVPLKKVVSGPNTKELPGTYTGCITSKTRVKYPVYVEAYAKLSNSTMASDVWMLSPDDTQEIDIIEAYGGDRDGGGYGADRLHLSHHIFIRQPFKDYQPKDSGSWYKDDKGTLWRDDFHRVGVFWKDPFTLEYYVDGELVRTISGKDIIDPNNYTGGTGLVKDMDIIINMEDQSWRAVKGLSPTDEELKNVEDHTFLVDWIRVYTLVPEE | Cleaves the beta-1,4-linkages between beta-D-galactose and alpha-L-3,6-anhydro-galactose residues in agarose. Cleaves agarose in a random manner with retention of the anomeric-bond configuration, producing beta-anomers that give rise progressively to alpha-anomers when mutarotation takes place. | B5CY73 |
Q8D370 | PYRD_WIGBR | Dihydroorotate oxidase | Wigglesworthia | MIYKIINFILSKKDHEEKKDLLLKIMKFFNKTPLNFLIKNKFPNNNISCMGLNFKNILGLAAGLDKNGDYIKLFSDIGFGFIELGTVTLKPQHGEKKPRLFCFPNVYGIINRMGFNNNGIENLIENIKNEKNVKSILGINIGKNKDTLIEKAKDDYLICINKAYYYSDYISINISSPNTKDLRKLQFGELFSDLLKSIKEEQNKLNKIYNKYVPILIKISPDINNSEIIQISDCLLSYNIDGVIATNTTVNKDIIMRCCNNCEKGGLSGAPLNENSTRIIKKLSKELKGKIPIIGSGGIISVKSAKEKIKAGASLIQIYS... | Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. | Q8D370 |
A9ISM8 | LPXA_BART1 | Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase | Bartonella | MSGTKIHPTALVEKGAQLGENVRVGPFCHISSEAVIGDECSLTSHVVIMGKTMLGAKSKVFSHAVLGADPQNNKHKGGATILSIGKNCMIREGVTMHRGSDSSTGMTVVGDNCQFFCYAHIAHDCHVGNHVTFANNAMIAGHVTVGDYVIIGGGAAVHQFVRVGHHAFIGGVSALVGDLIPYGTAVGVQAKLAGLNIIGMKRAGLERQDIHALRHAVAMLFDHSKPFKERVNDVASCYSSSRSVADVVRFIKEEGKRFYCTPKFGGDRIK | Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. | A9ISM8 |
B0K754 | GLPK_THEP3 | Glycerokinase | Thermoanaerobacter | MAKYIMAFDQGTTSSRAIIFDRSGKIIASLNQEFKQIYPKAGWVEHDPMEIWGTQIGVAKGVIEKAGINPEDIAAIGITNQRETTVVWDKNTGKPIYNAIVWQCRRTAPICDELKNKGFDKKIREKTGLVVDAYFSGTKIKWILDNVEGAREKAEKGELLFGNIDTWLIWNLTRGKVHVTDYSNASRTMIFNIHELKWDKEILAELNIPEQMLPEVKPSSYVYGYTDKSIFGVEIPIAGDAGDQQAALFGQACFKPGMAKNTYGTGCFMLMNTGEKAVPSNTGLLTTIAWGIDGKVEYALEGSIFIAGAAIQWLRDELRI... | Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate. | B0K754 |
Q59WU8 | KAR5_CANAL | Karyogamy protein 5 | Candida | MNIVLLIYCLAMVVAHDLQLFGDFKFELSDNWRNDCAKKALEPIINQCAEGIETISPFQQKSIAIQLSICEFENAEISYPSECRSQNLDTCILLLEKSPQYWTTFSGYYREIRNICHQVSLPFAKDQILQVYGNITEFYRTLMDEMTNSSKYTENMQNELKAKFDKLIGVIDLILADREKNREDLKSSFNMFKNNFEKSLNNALVVMKHSYEDANSNVKELESHLNYFINDMSQVYILINEKALEVKSQQDRIKEHNADILNQIEEIKKNLDNAYEEASEVQISNNQLVHDIQSSLDYSLFTVSNLNSHLQLSINDFIEK... | Required for nuclear membrane fusion during karyogamy. | Q59WU8 |
A9ADK9 | RL18_BURM1 | 50S ribosomal protein L18 | Burkholderia cepacia complex | MDKTQSRLRRARQTRIKIAELQVARLAVHRTNTHIYAQVFSPCGTKVLASASTLEAEVRAELADKSGKGGNVAAATLIGKRIAEKAKAAGIESVAFDRSGFRYHGRVKALAEAAREAGLKF | 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. | A9ADK9 |
A3DHB8 | Y2143_ACET2 | Nucleoid-associated protein Cthe_2143 | Acetivibrio | MAKGGFPGFGGNINNLVKQAQKMQRDMERVQEELKEKTVEASAGGGAVTVVATGRKDIKEITIKPEVVDPDDVEMLQDLILAAVNEALRKADEMVTAEISKITGGLGGIPGLF | Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | A3DHB8 |
Q12N25 | RNFE_SHEDO | Rnf electron transport complex subunit E | Shewanella | MSQYQEIAKQGLWHNNPGLVQLLGLCPLLAVTATVTNALGLGFATLLVLVGSNMLVSLVRDYVPKEIRIPVFVMIIAALVTSVQLLINAYAYGLYLSLGIFLPLIVTNCVIIGRAEAFASRNNLAHSAFDGLMMGIGFTCVLVVLGAGRELLGQGTLFEGADLLLGDWAKALVMQVWQVDTPFLLALLPPGAFIGMGLLIAGKNVIDARLKARQPKTQAEPVARVRITKVS | Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. | Q12N25 |
Q0AGI1 | ISPF_NITEC | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase | Nitrosomonas | MKKIRIGQGFDIHQLAAGRELVIGGVTIPYEKGLLGHSDADVLLHALCDALLGAAALGDIGKHFSDTDARYKDIDSRKLVCKVHRLLAETGYRVVNIDATIIAQAPKMAPHISGMIANIAQDLAMPAGNINIKAKTAEKLGAVGRGEGIVAEVVCLIANSDEGEAQP | Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a correspond... | Q0AGI1 |
Q9QZH6 | ECSIT_MOUSE | Protein SITPEC | Mus | MSWVQVNLLVRSLSRGWGGLCRPALSGTPFAQVSLQALRGLHCSAATHKDEPWLVPRPPEPQRKPIKVPAMHEDLFKPSGNRERDKASFLNAVRSFGAHNVRKRGHVDFIYLALRKMPEFGVERDLSVYNLLLDVFPKEVFRPRNVIQRIFVHYPRQQECGVAVLEQMERHGVMPSAETEFLLIQIFGRKSYPMLKFLRMKLWFTRFKNINPYPVPRDLPQDPLDLAKLGLRHMEPDLSAKVTVYQMSLPSDSTGMEDPTQPHIVGIQSPDQQAALARHNPSRPVFVEGPFPLWLRNKCVYYHILRADLPPPEEEKVEEI... | As part of the MCIA complex, involved in the assembly of the mitochondrial complex I. | Q9QZH6 |
Q39QM7 | HEM3_GEOMG | Pre-uroporphyrinogen synthase | Geobacter | MAPKQLRIGTRASQLALWQANWVKGELEKRYPGMAVELVKIKTMGDKILDVPLAQVGGKGLFVKEIEEAMLRGEIDIAVHSMKDVPTEFPEGLGLYCITEREDPRDAVISRGVKFADLPQGARIGTSALRRQAQILKVRPDLQMVVIRGNVETRIRKLTDENLDAVILAAAGLNRLGFADQVSEYLPVELSLPAIGQGALGIECRLDDETIKDTIAFFNHPDTAHAVRAERALLWRCEGGCQVPIAAHGQVSGDTLTLTGFVASVDGTRSVKDTISGPVTECEKLGIALAEKLLADGAHEILAEVYQREVAREKEIPV | Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. | Q39QM7 |
Q9JZQ2 | METE_NEIMB | Methionine synthase, vitamin-B12 independent isozyme | Neisseria | MTTLHFSGFPRVGAFRELKFAQEKYWRKEISEQELLAVAKDLREKNWKHQVAANADFVAVGDFTFYDHILDLQVATGAIPARFGFDSQNLSLEQFFQLARGNKDQFAIEMTKWFDTNYHYLVPEFHADTEFKANAKHYVQQLQEAQALGLKAKPTVVGPLTFLWVGKEKGAVEFDRLSLLPKLLPVYVEILTALVEAGAEWIQIDEPALAVDLPKEWVEAYKDVYATLSKVSAKILLSTYFGSVAEHAALLKALPVDGLHIDLVRAPEQLDAFADYDKVLSAGVIDGRNIWRANLNKVLETVEPLQAKLGDRLWISSSCS... | Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation. | Q9JZQ2 |
Q3K107 | KUP_STRA1 | Probable potassium transport system protein kup | Streptococcus | MQHVNHSSFDKASKAGFIIALGIVYGDIGTSPLYTMQSLVENQGGISSVTESFILGSISLIIWTLTLITTIKYVLVALKADNHHEGGIFSLYTLVRKMTPWLIVPAVIGGATLLSDGALTPAVTVTSAVEGLKVVPSLQHIFQNQSNVIFATLFILLLLFAIQRFGTGVIGKLFGPIMFIWFAFLGISGFLNSFAHPEVFKAINPYYGLKLLFSPENHKGIFILGSIFLATTGAEALYSDLGHVGRGNIHVSWPFVKVAIILSYCGQGAWILANKNAGNELNPFFASIPSQFTMHVVILATLAAIIASQALISGSFTLVS... | Transport of potassium into the cell. | Q3K107 |
Q6Q2J0 | AOFA_PIG | Monoamine oxidase type A | Sus | MERQEKANNAGHMVDVVVIGGGISGLSAAKLLNEYGINVLVLEARDRVGGRTYTVRNENVDYVDVGGAYVGPTQNRILRLSKELGLETYKVNVNECLVQYVKGKSYPFRGAFPPVWNPIAYLDYNNLWRTMDDMGKKIPADAPWESPHAEEWDKMTMKDLIDKICWTKTAKRFASLFVNINVTSEPHEVSALWFLWYVKQCGGTTRIFSVTNGGQERKFVGGSGQVSERIMHLLGDRVKLRCPVTYVDQSGDNIIVETLNHELYECQYVISAIPPTLTAKIHFRPELPSERNQLIQRLPMGAIIKCMMYYKEAFWKKKNY... | Catalyzes the oxidative deamination of primary and some secondary amine such as neurotransmitters, with concomitant reduction of oxygen to hydrogen peroxide and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. Preferentially oxidizes se... | Q6Q2J0 |
A5UKU8 | RL10_METS3 | Acidic ribosomal protein P0 homolog | Methanobrevibacter | MAHVAEWKKEEVNELKSLIDKYDVIGIVDLLNIPAKQLQEMRKSLHNKAVIRMSKKNLIDLALEDCNASKNNIVDLSEHMEGQVAVIATEMNPFKLYKILEDSKTSAPAKPGAIATDDIVIPEGDTGFEPGPFLGELQQVGIPAKIDKGKIVVSKETVLVEAGEEVSAAVASTLSRMDINPMEVGIDLRAVYEEEAIYTSEVLAIDEEQTLADVQNAFRNAFNLSVNAAIPTEETISTIITLAYTRAINVGVDAAIMTSETSEPIIGLAQAKMLALASEVSGTEGALDDELAEKLSNVAVAAAPVVEETVEEEEEEEEEE... | Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. | A5UKU8 |
Q93ZS1 | LPAH2_ARATH | Protein LOW PHYTIC ACID 1 homolog 2 | Arabidopsis | MMTEATKVLYIVVREEGDDDDNNGDDSFRYTRPVLQSTLQLMGCKARHAFKISRRVFELIRSEGSCNTSPENGKEPEFAKEVGGSTCVEKLNCLVVAGDVDKNKSKPFEMYKRRTTVVVSREIFVDVVCDALAEYKYVGRDQRADLILACRIRERKESVTVLLCGTSGCGKSTLSALLGSRLGITTVVSTDSIRHMMRSFADEKQNPLLWASTYHAGEYLDPVAVAESKAKRKAKKLKGSRGVNSNAQKTDAGSNSSTTELLSHKQMAIEGYKAQSEMVIDSLDRLITTWEERNESVVVEGVHLSLNFVMGLMKKHPSIV... | May be not required for the accumulation of phytic acid in seeds. Phytic acid is the primary storage form of phosphorus in cereal grains and other plant seeds. | Q93ZS1 |
Q71VZ1 | GSHAB_LISMF | Glutathione synthase | Listeria | MLDSFKEDPKLRKLLFSGHFGLEKENIRVTSDGKLALTPHPAIFGPKEDNPYIKTDFSESQIEMITPVTDSIDSVYEWLENLHNIVSLRSENELLWPSSNPPILPAEEDIPIAEYKTPDSPDRKYREHLAKGYGKKIQLLSGIHYNFSFPEALIDGLYDKISLPEESKQDFKNRLYLKVAKYFMKNRWLLIYLTGASPVYLADFSKTKHDESLPDGSSALRDGISLRNSNAGYKNKEALYVDYNSFDAYISSISNYIEAGKIESMREFYNPIRLKNAHTDQTVESLAEHGVEYLEIRSIDLNPLESNGISKDELAFIHLF... | Synthesizes glutathione from L-glutamate and L-cysteine via gamma-L-glutamyl-L-cysteine. | Q71VZ1 |
Q16AD5 | RS17_ROSDO | 30S ribosomal protein S17 | Roseobacter | MPKRILSGVVTSDANDQTVSVSVERRFTHPVLKKTIRKSKKYRAHDENNTFKKGDAVRIVECAPKSKTKRWEVLQAAEV | One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. | Q16AD5 |
C3K1N5 | QUEA_PSEFS | Queuosine biosynthesis protein QueA | Pseudomonas | MRVADFTFELPDSLIARHPLAERRASRLLTLDGVSGALAHRQFTDLLEHLRPGDLMVFNNTRVIPARLFGQKASGGKLEILVERVLDSHRVLAHVRSSKSPKPGSSILIDGGGEAEMVARHDALFELKFAEEVLPLLERVGHMPLPPYIDRPDEDSDRERYQTVYSQRLGAVAAPTAGLHFDQPLLDAIAAKGVETAYVTLHVGAGTFQPVRVDNIEDHHMHSEWLEVSQDVVDAVEACKARGGRVIAVGTTSVRSLESAARDGVLKPFSGDTDIFIYPGRPFHVVDCLVTNFHLPESTLLMLVSAFAGYPETMAAYQAA... | Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA). | C3K1N5 |
B3Q6W6 | PURA_RHOPT | IMP--aspartate ligase | Rhodopseudomonas | MANVVVVGAQWGDEGKGKIVDWLSEQADIVVRFQGGHNAGHTLVINGQTYKLALLPSGVLRPSKLAVIGNGVVFDPQAFLDEVKKLQGQGVAISPENLRIAENVTLILPLHRELDATRENAAKAGAIGTTQRGIGPAYEDKVGRRAIRLMDLADLDTLPTKIERLLAHHNALRRGLGQPEIDAGQILADLSAMAPHLLPYAESVWRLLDIKRREGKRILFEGAQGALLDVDHGTYPYVTSSNTVAAQAATGTGMGPGAVGYVLGICKAYTTRVGAGPFPTELTNEIGEEIGRRGKEFGVNTGRKRRCGWFDAVLVRQTVR... | 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. | B3Q6W6 |
O78422 | RRP3_GUITH | Probable 30S ribosomal protein 3, chloroplastic | Guillardia | MPKFTLKVLWLDNNVAVAVDQIIGNGTSPLTCYFFWPRNDAWEQVKAELESKPWIEEKERIELLNKTTELINCWQEQSKKYSFKEIQSKFPDFIFAGAN | Probably a ribosomal protein or a ribosome-associated protein. | O78422 |
H6VGI3 | KARG0_SCYPA | Arginine kinase Scy p 2.0101 | Scylla | MADAAVIEKLEEGFKKLEAATDCKSLLKKYLTKSVFDQLKGKKTSLGATLLDVIQSGVENLDSGVGVYAPDAEAYTLFAPLFDPIIEDYHKGFKQTDKHPNKDFGDVNQFVNVDPDGKFVISTRVRCGRSMEGYPFNPCLTEAQYKEMESKVSSTLSNLEGELKGTYYPLTGMTKDVQQKLIDDHFLFKEGDRFLQAANACRYWPTGRGIYHNDNKTFLVWCNEEDHLRIISMQMGGDLGQVYRRLVSAVNEIEKRVPFSHHDRLGFLTFCPTNLGTTVRASVHIKLPKLAANREKLEEVAGKYSLQVRGTRGEHTEAEG... | Catalyzes the reversible transfer of high energy ATP gamma-phosphate group to L-arginine. | H6VGI3 |
A1JP52 | PURR_YERE8 | Purine nucleotide synthesis repressor | Yersinia | MATIKDVAKHAGVSTTTVSHVINKTRFVAENTKAAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAPYFAEVIEAVENSCYSKGYTLILCNSHNNLDKQKAYLAMLAQKRVDGLLVMCSEYPEQLLGMLEDYRNIPMVVMDWGTARGDFTDSIIDNAFEGGYLAGRYLIERGHRDIGAIPGQLSRNTGGGRHQGFLKALEEANITLREEWVVQGDFEPESGYKAMHQILTQKHRPTAVFCGGDIMAMGAICAADELGLRVPQDISVIGYDNVRNARYFSPALTTIHQPKERLGETAFAMLLDRIVSKREDPQTIE... | Is the main repressor of the genes involved in the de novo synthesis of purine nucleotides, regulating purB, purC, purEK, purF, purHD, purL, purMN and guaBA expression. PurR is allosterically activated to bind its cognate DNA by binding the purine corepressors, hypoxanthine or guanine, thereby effecting transcription r... | A1JP52 |
B3E600 | ADE_TRIL1 | Adenine aminohydrolase | Trichlorobacter | MNLTNIPRQALPELLCRMPKAELHIHIEGSLEPELIFALAERNRLQLAYPTIESLRAAYAFTNLQSFLDIYYAGASVLQTEQDFFDMAWAYLLRAKADNVVHAEIFFDPQTHTARGIPFATIINGLDRAIQQGRNELGISAALILCFLRHLTEADAFTVLEEALPFRDKFIGVGLDSGEKGNPPEKFSRVFARCRELGLRLVAHAGEEGTAEYIWHALDLLQAERIDHGVHCLDDPQLVTRLVQQQVPLTVCPLSNVKLRVFPDLAAHNIARLLACGIRATINSDDPAYFGGYLNQNYLETFAALPELGAAEAYQLARNS... | Catalyzes the hydrolytic deamination of adenine to hypoxanthine. Plays an important role in the purine salvage pathway and in nitrogen catabolism. | B3E600 |
E1B7Q7 | TRIPC_BOVIN | Thyroid receptor-interacting protein 12 | Bos | MSNRPNNNPGGSLRRSQRNTAGAQPQDDSIGGRSCSSSSVVIVPQPEDPDRANTSEKQKTGQVPKKDNSRGVKRSASPDYNRTNSPSSAKKPKALQHTESPSETSKPHSKSKKRHLDQEPQLKSAPSPSTSKAHTRKSGAAAGSRSQKRKRTESSCIKSASVSEATGAEERSAKPTKLASKSAASAKAGCSTITDSSSAASTSSSSSAVASASSAVPPGARVKQGKDQNKARRSRSASSPSPRRSSREKEQSKTGGSSKFDWAARFSPKVSLPKTKLSLPGSSKSETSKPGPSGLQAKLASLRKSTKKRSESPPAELPSL... | E3 ubiquitin-protein ligase involved in ubiquitin fusion degradation (UFD) pathway and regulation of DNA repair. Part of the ubiquitin fusion degradation (UFD) pathway, a process that mediates ubiquitination of protein at their N-terminus, regardless of the presence of lysine residues in target proteins. Acts as a key ... | E1B7Q7 |
A8F3S6 | RUVC_PSELT | Holliday junction resolvase RuvC | Pseudothermotoga | MIIFGVDPGFGILGYGVLSVSGNSFQHVSHGTIQTEKQQNIALRLKVLYEELSNVIDNFKPSEIAMEKLFFSRNITTAISVGEARGIVLLLAAQRNIPVFEYTPHEIKKAVTGSGKASKKDVQQMIKILLNLKELPKPDDAADGLAIAWCHCAVRNITRRFS | Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group. | A8F3S6 |
A7MWI6 | RL2_VIBC1 | 50S ribosomal protein L2 | Vibrio | MAIVKCKPTSPGRRHVVKVVNADLHKGKPYAPLLEKNSKNGGRNNNGRITVRHIGGGHKHHYRVVDFKRTKDGIPATVERLEYDPNRSANIALVLYKDGERRYILAPKGVNAGDVIQSGVDAPIKAGNTLPMRNIPVGSTVHNVELKPGKGGQLARSAGAYAQIVARDGAYVTIRLRSGEMRKVLSEGRATIGEVGNSEHMLRELGKAGASRWRGVRPTVRGVVMNPVDHPHGGGEGRTSGGRHPVSPWGMPTKGFKTRKNKRTDKYIVRRRNK | One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. | A7MWI6 |
O32522 | PTHB_ERWAM | Glucitol/sorbitol-specific phosphotransferase enzyme IIB component | Erwinia | MANTIEIRKGESGWGGPLSINVTAGKKIVYITAGTKPAIVDHLVALTGWEAVDGFKQGEPPAEEIGVAVIDCGGTLRCGLYPKRRIPTINIHATGKSGPLAQFITEDIYVSGVRVADIRVANDAEAAPPEVAVADVAVNAGKGTGRDYDTSKKITEQSDGLLAKVGMGMGSAVAILFQSGRETIDTVLKTILPFMAFVSALIGIIMASGLGDFIAHGLTPLANSPVGLVTLALICSFPLLSPFLGPGAVIAQVIGVLVGVQIGQGTIPPHLALPALFAINAQAACDFIPVGLSLANARQETVRVGVPAVLVGRFITGAPT... | The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II complex composed of SrlA, SrlB and SrlE is involved in gl... | O32522 |
Q3AMN6 | RS3_SYNSC | 30S ribosomal protein S3 | unclassified Synechococcus | MGHKINPTGLRLGITQEHRSRWYASSKNYPALLQEDDRIRKFIHKKYGSAGISDVLIARKADQLEVELKTARPGVLVGRQGSGIEELRSGIQKTIGDSSRQVRINVVEVERVDGDAFLLAEYIAQQLEKRVAFRRTIRMAVQRAQRAGVLGLKIQVSGRLNGAEIARTEWTREGRVPLHTLRADIDYATKVASTTYGVLGIKVWVFKGEVLSEQAQPMPVGAAPRRRASRRPQQFEDRSNEG | Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation. | Q3AMN6 |
A4IKW7 | ADDA_GEOTN | ATP-dependent helicase/nuclease AddA | Geobacillus | MNATFRPKPAGSRWTDEQWKAIAAGGRDILVAAAAGSGKTAVLVERIIQKVTAEEGAVDIDRLLVVTFTNAAAAEMKARIGEALERELANRPHSLHLRRQLSLLNRASISTLHSFCLDVIRKYYYLLDLDPSFRIADETEIELLKEDVLEELLEEEYGKADNERFFAVVDAYTGDRSDAELQEMILALYEFSRSHPAPDEWLADLVSMYDVDEQTNVETLPPARYIAQHAAMELAAAKRFIGLALALAEKESGPKPYEKRLREDMDLIADLERRLSGSWDELYHALQSLSFGRLPPCRGDGFDAELIDEAKSLRDQAKKK... | The heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the chi site generating a DNA molecule suitable for the initiation of homologous recombination. The AddA nuclease domain is required for chi fragment generation; this subunit has the h... | A4IKW7 |
Q9A5C1 | SYA_CAUVC | Alanyl-tRNA synthetase | Caulobacter | MPSLNEIRSTFLDYFGKADHAVTPSAPLVPQNDPTLLFVNAGMVPFKNVFTGAETPAHPRAASSQKCVRAGGKHNDLDNVGYTARHHTFFEMLGNFSFGDYFKEQAILHAWTLLTAEFKLPKDKLLVTVYHTDDEAADLWKKIAGLGDDRIIRIPTSDNFWSMGDTGPCGPCSEIFFDHGPHIAGGPPGSPDEDGDRFIEIWNLVFMQFEQLAGGERISLPKPSIDTGMGLERIAAVLQGQHDNYDIDLFKALIAASVELTGVKAEGAQAPSHRVIADHLRSSSFLLADGVSPSNEGRGYVLRRIMRRAMRHAYLLGASE... | Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | Q9A5C1 |
P24504 | NUP3_PENSQ | Endonuclease PA3 | Penicillium | WGALGHATVAYVAQHYVSPEAASWAQGILGSSSSSYLASIASWADEYRLTSAGKWSASLHFIDAEDNPPTNCNVDYERDCGSSGCSISAIANYTQRVSDSSLSSENHAEALRFLVHFIGDMTQPLHDEAYAVGGNKINVTFDGYHDNLHSDWDTYMPQKLIGGHALSDAESWAKTLVQNIESGNYTAQATGWIKGDNISEPITTATRWASDANALVCTVVMPHGAAALQTGDLYPTYYDSVIDTIELQIAKGGYRLANWINEIHGSEIAK | Hydrolyzes only single-stranded DNA and RNA without apparent specificity for bases. | P24504 |
Q9NYW3 | TA2R7_HUMAN | Taste receptor family B member 4 | Homo | MADKVQTTLLFLAVGEFSVGILGNAFIGLVNCMDWVKKRKIASIDLILTSLAISRICLLCVILLDCFILVLYPDVYATGKEMRIIDFFWTLTNHLSIWFATCLSIYYFFKIGNFFHPLFLWMKWRIDRVISWILLGCVVLSVFISLPATENLNADFRFCVKAKRKTNLTWSCRVNKTQHASTKLFLNLATLLPFCVCLMSFFLLILSLRRHIRRMQLSATGCRDPSTEAHVRALKAVISFLLLFIAYYLSFLIATSSYFMPETELAVIFGESIALIYPSSHSFILILGNNKLRHASLKVIWKVMSILKGRKFQQHKQI | Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5. | Q9NYW3 |
Q6G543 | ILVD_BARHE | Dihydroxy-acid dehydratase | Bartonella | MPSYRSRISTHGRNMAGARSLWRATGMKESDFGKPIIAIANSFTQFVPGHVHLKDLGQLVAQQIVASGGIAKEFNTIAIDDGIAMGHDGMLYSLPSREIIADSVEYMINAHCADALVCISNCDKITPGMLMASLRLNIPTIFVSGGPMEAGKIKWKDQDLTVDLVDAMVAAAAENNSEEEVAEMERAACPTCGSCSGMFTANSMNCLTEALGLSLPGNGSMLATHADRQMLFEEAGRQIVTLVKRYYEKGDETVLPRSIASRKAFENAMTVDISMGGSTNTVLHLLAAAQEGEVDFTMTEIDRLSRRVPVLCKVAPAVAN... | 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 (... | Q6G543 |
O04019 | PS6AB_ARATH | Tat-binding protein 1 homolog B | Arabidopsis | MATAMAEDTSFEGDQLASMTTDDIGRASRLLANEIRILKEESQRTNLDLESVKEKIKENQEKIKLNKQLPYLVGNIVEILEMSPEDDAEEDGANIDLDSQRKGKCVVLKTSTRQTIFLPVVGLVDPDTLKPGDLVGVNKDSYLILDTLPSEYDSRVKAMEVDEKPTEDYNDIGGLEKQIQELVEAIVLPMTHKEQFEKLGIRPPKGVLLYGPPGTGKTLMARACAAQTNATFLKLAGPQLVQMFIGDGAKLVRDAFLLAKEKSPCIIFIDEIDAIGTKRFDSEVSGDREVQRTMLELLNQLDGFSSDDRIKVIAATNRAD... | The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex. | O04019 |
A3LVL1 | RCF1_PICST | Respiratory supercomplex factor 1, mitochondrial | Scheffersomyces | MVIRSKEQPVVPLGALATTGAIILAARSMKRGEKLRTQVYFRYRVVFQLITLVALVAGGVMMQQESAEQKKTREDKLREKAKQREKLWIEELERRDALIQERKRRLEESRAELKKMAEEGFKQENDNSKGK | Cytochrome c oxidase subunit which plays a role in assembly of respiratory supercomplexes. | A3LVL1 |
A1WLI3 | IF2_VEREI | Translation initiation factor IF-2 | Verminephrobacter | MSSNTVAEFATELKKSPATLLDQLKAAGVGKAALSDALTESDKQRLLAYLQASHGTTSVDRKKITLVKKSTSEIKQADATGKARTIQVEVRKKRTFVKRDDAQEGAADGAGSAAFAEPEHPAPAAQHDVPEAPAEQAQADAAPAADGAAPALSSEDQELARREEQARHQAELIRRQEAELAAKRAAREAREKREREAEERAAAYAAQEAEKKAAASAVKQVATREQAAEATARNAAQLQARAKAAAESKARSDEEAARAADLDARRRKAEAEAAAIRSMLATPKKAVMVAKKPEPPPKPVPKPAAAAGDAKKGTLHKPAV... | One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex. | A1WLI3 |
Q54VX4 | MCFJ_DICDI | Mitochondrial substrate carrier family protein J | Dictyostelium | MSSSHTIQETKEVHTKTNKRIQWDDLDPKRYYFYNFLLGGSIDLLMFPLDVIRTRLQVQGSQNVIQSFPQYNGTFDGFKKLIRLEGKRALYKGFLTSECGYLCSRAIYFGSYEFVKQGFLKGRSDSDSDLLFVTTISGAISEALASVIWVPFDVATQSVQIQGSLSKPKYKGGSDVFKKIYGERGIKGLYKGFGATIIRNVPYSGIWWGTYEISKSKLTQFNIRQKLGLKERSSHSLAVSAEIDKNNPSHEVENEDPIIHFISGFFAAVFATSITNPLDVAKTRLQTGVFPENEKPNFYTIIKSTIRKEGIRALWKGLVP... | Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. | Q54VX4 |
Q0HDV7 | AROB_SHESM | 3-dehydroquinate synthase | Shewanella | MTQQIQVDLGERSYPIYIGQSLMSDSETLSRYLLKKRILIVTNETVAPLYLKQIQDTMASFGEVSSVILPDGEQFKDLTHLDSIFTALLQRNYARDSVLVALGGGVIGDMTGFAAACYQRGVDFIQIPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPQIVIIDTECLQTLPAREFAAGMAEVIKYGIMWDAEFFQWLENNVQALKSLDTQALVYAISRCCEIKADVVSQDETEQGVRALLNLGHTFGHAIEAEMGYGNWLHGEAVAAGTVLAAQTAKSMGLIDESIVRRIVQLFHAFDLPITAPESMDFDSFIKHMR... | Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). | Q0HDV7 |
Q9R1K5 | FZR1_MOUSE | Cdh1/Hct1 homolog | Mus | MDQDYERRLLRQIIIQNENTVPCVSEMRRTLTPANSPVSSPSKHGDRFIPSRAGANWSVNFHRINENEKSPSQNRKAKDATSDNGKDGLAYSALLKNELLGAGIEKVQDPQTEDRRLQPSTPEHKGLFTYSLSSKRSSPDDGNDVSPYSLSPVSNKSQKLLRSPRKPTRKISKIPFKVLDAPELQDDFYLNLVDWSSLNVLSVGLGTCVYLWSACTSQVTRLCDLSVEGDSVTSVGWSERGNLVAVGTHKGFVQIWDAAAGKKLSMLEGHTARVGALAWNADQLSSGSRDRMILQRDIRTPPLQSERRLQGHRQEVCGLK... | Substrate-specific adapter for the anaphase promoting complex/cyclosome (APC/C) E3 ubiquitin-protein ligase complex. Associates with the APC/C in late mitosis, in replacement of CDC20, and activates the APC/C during anaphase and telophase. The APC/C remains active in degrading substrates to ensure that positive regulat... | Q9R1K5 |
Q1H361 | ISCS_METFK | Cysteine desulfurase IscS | Methylobacillus | MTVRTPIYLDYSATTPIDPRVAEKMIPYLTEHFGNPASRSHAFGWTAEKAVENAREEVARLVNADPREIVWTSGATESNNLAIKGAANFYSPSKGKHIVTVQTEHKAVIDTVRELERLGYEATYLIPEPNGLIDLDKFKAALRPDTVLASVMLVNNEIGVIQDIEAIGNICREQGVIFHVDAAQATGKVHIDLQKLPVDLMSFSAHKTYGPKGIGALYVRRKPRVRIEAQMHGGGHERGMRSGTLATHQIVGMGEAFRIAREEMDSENVRIRQLRDRLLKGLQEIEEVYVNGDLEHRVAHNLNISFNFVEGESLIMAVKD... | Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assemb... | Q1H361 |
B9M7S3 | RECF_GEODF | DNA replication and repair protein RecF | Geotalea | MKLNKIYLQSFRNLQETMLMPAQHFNIFYGNNGQGKTNLLESIFIMATMKSFKTARSSDLVRWGAISSLLKGWVERDGVTREIAVFLDNQGKKIRVDQKAVTRIDDFFGHLNVVVFTPEEVNMVKGLPELRRKYLDRAVFSSDITYLSVYHAYSKILKNRNMLLKRGEKASFDIWTEKLVEQGKNIILSRLAYLDALRDLLKRFYREISGNEEAVDISYRPYHMDLADCRGDVADAFAEALAKTATEEERRGTTLAGPHRDDVEFILNGRPLKQFGSQGQQKSYVLALKMAETEYLQKKFHSQPIFLLDDLSSELDQERK... | The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP. | B9M7S3 |
Q9XA10 | CRGA_STRCO | Cell division protein CrgA | Streptomyces albidoflavus group | MPKSRIRKKADYTPPPSKQATSIKLTSRGWVAPVMLAMFVIGLAWIVVFYVTDGSLPIDSLGNWNIVVGFGFIAAGFGVSTQWK | Involved in cell division. Coordinates growth and cell division. May act as an inhibitor of Z-ring formation. | Q9XA10 |
Q891R5 | SYV_CLOTE | Valyl-tRNA synthetase | Clostridium | MNDNINIAKTYDPKEFEERIYKMWEEGEYFTPKVDKDKKPYTIVMPPPNITGKLHLGHALDNSMQDFLIRVKRMQGYSTLWLPGQDHASIATEVKVENELLKTGLKKKEMGREAFLERVWEWSEEYRGRIRDQLKKLGSSADFTRESFTMDDNLDKAVRAVFVKLYEEGLIYKGNRIVNWCPKCMTALSDAEIEYEENYGNFWHVKYPLVDSEEYLEIATTRPETMLGDTAVAVNPNDERYKHLIGKKLMLPLVNREIPIVADDYVDVEFGTGAVKITPAHDPNDYEVGKRHDLEEIIIMNENGTINELGGKYSGMDRYE... | 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. | Q891R5 |
B4U609 | MURD_HYDS0 | UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase | unclassified Hydrogenobaculum | MAYLVWGKGRSGLAAFNLLKAKGFKAYIGDDKEDKNLWQDVWNEIDTVVLSPGIPPFHPLWKEAIKSSKEVIGETELAYRFYKGKNIIAVTGTDGKSTTVHLIHHFTSFKEGGNFGTPFSEIVLDNDKENVALEASSFQGKTLDTFRPNVGVFLNFSKDHLDWHPSLEDYLLSKQKIFKNQTQEDILILNAQKPVCDTPSLAKKIFFGENGDLKVVGSDVYYKDELLIENISHPSLKGLHNLYNIAVASFVAFSMGISLEEIKKNLETFEALPFRYQYLGNFEGIDICNDSKSTTVNALMSALESTKAPILLIAGGIDKG... | Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). | B4U609 |
Q42850 | PORB_HORVU | NADPH-protochlorophyllide oxidoreductase B | Hordeum | MALQAATSFLPSALSARKEGAAKDSAFFGVRLADGLKLDATSLGLRTKRVNTSSVAIRAQAAAVSAPTATPASPAGKKTVRTGNAIITGASSGLGLATAKALAESGKWHVIMACRDYLKTARAARAAGMPKGSYTIVHLDLASLDSVRQFVKNVRQLDMPIDVVVCNAAVYQPTAKEPSFTADGFEMSVGVNHLGHFLLARELLEDLKASDYPSKRLIIVGSITGNTNTLAGNVPPKANLGDLRGLAAGLNGVGSAAMIDGAEFDGAKAYKDSKVCNMLTMQEFHRRYHEETGVTFASLYPGCIATTGLFREHIPLFRLL... | Phototransformation of protochlorophyllide (Pchlide) to chlorophyllide (Chlide). | Q42850 |
C5CBJ8 | RISB_MICLC | 6,7-dimethyl-8-ribityllumazine synthase | Micrococcus | MSGAGAPTFTPDPAAASGLNVAIVAAQWHTEIMDGLIAGAQAAAADLGLEPVLVRVPGTVELTVAAARLAERFDVVVVLGVVVRGDTPHFDYVCQSVTQGVTEVSVRTGVPVGFGVLTVDTEQQARDRAGLPGSREDKGREALEAAVLTELALRRAGA | 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. | C5CBJ8 |
Q9P6L8 | SRB8_SCHPO | Suppressor of RNA polymerase B srb8 | Schizosaccharomyces | MSNRDSANPPGFNDAVPLAICYIDSSTSSHDEYLTLLQSKVSAPDKNFRDETVDGAPFLAGDAISKGHRYSPPVRSDRASAQGLLQQHLEKSSTLENLKRYSSTLLGRQNDAVIDEPFAPFRPPPRVTLSESRRDRWLQGLSDPMVPLSSLIKTIPHGLWGEDILRMLVKFRVPFTRAIWFIRCAGVNEARSFLRKVQTTDITEWVKNWTDVAAGFLISFISSFLNADIYSFADDYTYLLKLFGRLLAEELVSPKHFLLRIVSFSGDSSLKSFSLHFFALQFFSTSLIQYTHICRKCVITILQSYQQLIVDQPANLLKFS... | Component of the srb8-11 complex. The srb8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The srb8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. ... | Q9P6L8 |
Q9TL12 | PSAI_NEPOL | Photosystem I reaction center subunit VIII | Nephroselmis | MVTSFLPSLFVPLVGLVFPAVAMASLFLYIEKDEIA | May help in the organization of the PsaL subunit. | Q9TL12 |
Q7U7I0 | GLMU_PARMW | Glucosamine-1-phosphate N-acetyltransferase | Parasynechococcus marenigrum | MLAVAVLAAGKGTRMKSALPKVLQPLAGATLVERVLASAANLQPDRRMLIVGHQADRVEEQLAAIGLLEFVLQQPQNGTGHAVQQLLPVLQGFEGELLVLNGDVPLLRAETIESLVNGHRESGADVTLLTARLEDPTGYGRVFVDADGKVSAIVEHRDCSEEQLSNNLTNAGIYCFNWQALAEVLPKLSTDNDQGELYLTDTVAMLPKAMHVEVADPDEVNGINNRKQLAQCEAVLQQRLRDHWMAEGVTFVDPGSCTLSENCCFGRDVVIEPQTHLRGSCRIGDNCRLGPGSLLENAELGSDVSVLHSVVREATVGNGV... | Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted ... | Q7U7I0 |
B0VRV3 | FPG_ACIBS | DNA-(apurinic or apyrimidinic site) lyase MutM | Acinetobacter calcoaceticus/baumannii complex | MPELPEVETTKTSLFPLLNQKVLSVEVRNPSLRWPIPDNVQKLVGQRLIGLNRRSKYILAEFEQDQMLWHLGMSGSFRLCQPNDELRKHDHLIIQFEDQQLRYHDPRRFGCILWLNPETQGKLIDTLGPEPLSTDFHAEYLASKLKNKSVGIKIALMDNHVVVGVGNIYATESLFNVGIHPAQPAGDLTMQQIEKLVVEIKRILKSAIDLGGSTLRDYSNAMGENGYFQQTLLAYGRAREMCVNCETTLENLKLGQRASVFCPQCQPLKKLRKP | Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. ... | B0VRV3 |
B2GJ30 | ACPS_KOCRD | 4'-phosphopantetheinyl transferase AcpS | Kocuria | MIVGTGVDIVDIARFERQLERTPRLRERLFVPHERELAPRSLAARFAVKEAAAKALLAPPGMIWQDCWVSNDEHGAPHLHTTGTVARQQRARGVDTWHVSISHDGGMAVAFVVAEAQEGSRDD | Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein. | B2GJ30 |
Q2GK70 | SYP_ANAPZ | Prolyl-tRNA synthetase | phagocytophilum group | MRLSEFYSPTVKNVSSDVVSASHKYSIRAGIVSQTASGIYTLLPLGLMVLRKVENIIREEINAVGFSEILMPTMQPADLWKESQRYDSYGQELIRIHDRGGREMVLGPTHEEVVTDLVRSSLKSYRDLPVNLYQIQWKFRDELRPRNGILRSREFLMMDAYSFDTDFEKAMKTYDAVFRAYRKAFKRMNLQTIALKADMGAIGGSVSHEFHVLTPTGESTVYYDERALELSEMNDYGIEELKEVYAATDDMHDEKSCGIAPEDLKTARGIEVGHIFYLDDRYSRTMNVKFCNTDGHSGTHVKMGCYGIGISRLIGALIEV... | 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). | Q2GK70 |
A0B8Q8 | PURA_METTP | IMP--aspartate ligase | Methanothrix | MFTIITGAQFGDEGKGKIVDLLAEKYDIIARFQGGDNAGHTVKVGDKTYKLHLVPSGVLFDKRLLIGPGVVLNPKVLWEELQTLWGMGMKVDLGIDPKTSIIMPYHIEMDALREKARTAKIGTTRRGIGYAYIDKIAREEVQMADITDPEMLKRKLEEIAPAKESAIKEMGGDPSVVRDEAQLRAYLEIGRALKNNLTDVSLEINRALDEDKMVLAEGAQGAFLDVIHGTQKFVTSSFTTAGSACANLGVGPVRVDNVVGVVKAYITRVGEGPMPTELKDEIGDRLREAGGEYGTTTGRPRRCGWFDAVLGRKAVYLNGY... | 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. | A0B8Q8 |
P59522 | RSMH_BUCBP | rRNA (cytosine-N(4)-)-methyltransferase RsmH | Buchnera | MKNNFSHTPVLLNETIQNLDIKNDGIYIDATFGYGGHSKEILKHLGKNGKLYSIDQDPYAIKIANKLKNDTRFNIIHGKFSNILKYSNKNKIRGKVNGILLDLGMSSMQINNPNRGFSFISDGPLDMRMNPNTGIPAYMWLKKTNLTTLYHVLKKYGEEPFSKKIAYNIIAYNKKKTITRTLELSKIITNSIPIKKYRKHPARRVFQAIRIYINHEIYELQQALEHVLNILIPGGKLLILSFHSLEDRTVKKFMIKYSKPPFVPPGLAITETQLKSLANKQLKIITKIFPSTIEIRKNPRAHSAILRVAQKNNNE | Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. | P59522 |
Q28ZT4 | CLP1_DROPS | Protein CLP1 homolog | Sophophora | MSDHQNRGQDFSLEADSELRFEIEQKDAKVLVTLVNGFAELFGTELVKKKKYEFGMGAKVAIFTYQGCVLHVTGKMDVCYISKETPMVQYVNCHAALEQFRTEAEEKDRRGPVAMVVGPTDVGKSTLCRILLNYAVRVGRRPLYADLDVGQGAIAISGNVATILIERPASVEEGFPKTAPLVYHFGHKSPSGNSVLYNAVVSKMAEVTLQSLNGNKRTKSSGIIVNTCGWVKGHGYAHLLHAARAYGACAIFVLDQERLYNELLRDVPSSVHVVLLPKSGGVVERSKELRHECRDQRIKEYFYGNARAPFYPFSFEVKFQ... | Required for endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation. | Q28ZT4 |
Q8CSS7 | RNY_STAES | Ribonuclease Y | Staphylococcus | MNLLSLLLILLGIILGVVVGYIVARNLLHQKQVQARQTADDIVSYANKEADNIKKEKLLEAKEENQILKEQAENELRERRGELQRQETRLLQKEENLDRKSDLLDKKDEILEQKESKLEERQQQVDAKESSVQTLIMKHEQELERISGLTQEEAVKEQLQRVEEELSQDIAILVKEKEKEAKEKVDKTAKELLATTVQRLAAEHTTESTVSVVNLPNDEMKGRIIGREGRNIRTLETLTGIDLIIDDTPEAVILSGFDPIRREIARTALVNLVSDGRIHPGRIEDMVEKARKEVDDIIRDAGEQATFEINVHNMHPDLVK... | Endoribonuclease that initiates mRNA decay. | Q8CSS7 |
O59264 | RF1_PYRHO | Translation termination factor aRF1 | Pyrococcus | MSKMTRHDAQLYELKKKIEELKKIRGRGTELISLYIPAGYDLSKVMQQLREEYSTAQNIKSKTTRKNVLGALERAMQHLKLYKQTPENGLALFVGNVSEIEGNTDIRLWAIIPPEPLNVRLYRCDQTFVTEPLEEMLRVKDAYGLITVEKNEATIGLLRGKRIELLDELTSNVPGKTRAGGQSARRYERIREQETHEFMKRIGEHANRAFLPLLEKGELKGIIIGGPGPTKEEFVEGEYLHHELKKKILGVVDISYHGEYGLRELVEKASDILRDHEVIREKKLVNEFLKHVVKDTGLATYGEREVRRALEIGAVDVLLI... | Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA. | O59264 |
Q9DEQ4 | SFRP1_CHICK | Secreted frizzled-related protein 1 | Gallus | MGVGRSEGGRRGAALGVLLALGVALLAVGSASEYDYVSYQSDLGPYPGGRFYTKPHQCVAIPADLRLCHSVGYDKMVLPNLLDHETMAEVKHQASSWVPLLNKNCHMGTQVFLCSLFAPVCLDRPVYPCRWLCEAVRDSCEPVMQFFGFFWPEMLKCDQFPQDYVCIAMTTPNATEVSRPKGTTVCPPCDNEMKSEAIVEHLCASEFALKMTIKEVKKENGDKVIIPRKRKALKLGPIRKKNLKKLVLLLKNGADCPCHQLDNLGHHFLIMGRQVKTQHLLTAIYKWDKKNKEFKKFMKKVKAPDCPTFPSVFK | Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types. | Q9DEQ4 |
Q9HCE6 | ARGAL_HUMAN | GrinchGEF | Homo | MASSNPPPQPAIGDQLVPGVPGPSSEAEDDPGEAFEFDDSDDEEDTSAALGVPSLAPERDTDPPLIHLDSIPVTDPDPAAAPPGTGVPAWVSNGDAADAAFSGARHSSWKRKSSRRIDRFTFPALEEDVIYDDVPCESPDAHQPGAERNLLYEDAHRAGAPRQAEDLGWSSSEFESYSEDSGEEAKPEVEVEPAKHRVSFQPKLSPDLTRLKERYARTKRDILALRVGGRDMQELKHKYDCKMTQLMKAAKSGTKDGLEKTRMAVMRKVSFLHRKDVLGDSEEEDMGLLEVSVSDIKPPAPELGPMPEGLSPQQVVRRHI... | Acts as guanine nucleotide exchange factor (GEF) for RHOA, RHOB and RHOC. | Q9HCE6 |
Q5F5B4 | PRMC_NEIG1 | Protein-glutamine N-methyltransferase PrmC | Neisseria | MFKPHRRQTGRKMTFDEWLGLSKLPKIEARMLLQYVSEYTRVQLLTRGGEEMPDEIRQRADRLAQRRLNGEPVAYILGVREFYGRRFTVNPNVLIPRPETEHLVEAVLARLPENGRVWDLGTGSGAVAVTVALERPDAFVRASDISTPALETARKNAADLGARVEFAHGSWFDTDMPSERQWDIIVSNPPYIENGDKHLSQGDLRFEPQIALTDFSDGLSCIRTLAQGAPDRLAEGGFLLLEHGFDQGAAVRGVLAENGFSGVEILPDLAGLDRVTLGKYMKHLK | Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif. | Q5F5B4 |
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