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 |
|---|---|---|---|---|---|---|
Q5FW53 | MBPHL_MOUSE | Myosin-binding protein H-like | Mus | METATTLEIASCSQRQVEAAADPADAKGPRTSHQQEAGSPSLQLLPSIEEHPKIWLPRALKQTYIRKAGETVNLLIPIQGKPKPQTTWTHNGCALDSSRVSVRNGEHDSILFIREAQRTDSGCYQLCVQLGGLQATATINILVIEKPGPPQSIKLVDVWGANATLEWTPPQDTGNTALLGYTVQKADKKSGLWFTVLERYHRTSCVVSNLIVGNSYAFRVFAENQCGLSDTAPVTADLAHIQKAATVYKAKGFAQRDLSEAPKFTQPLADCTTVTGYDTQLFCCVRASPRPKIIWLKNKMDLQGNPKYRALSQLGICSLE... | Myosin-binding protein which plays a role in cardiac function . Seems to regulate conduction in the atria and ventricular conduction systems . | Q5FW53 |
C3P552 | DEOD_BACAA | Purine nucleoside phosphorylase DeoD-type | Bacillus cereus group | MSVHIEAKQGEIAESILLPGDPLRAKYIAETFLEDVTCYNNVRGMLGFTGTYKGKRVSVQGTGMGVPSISIYVNELIQSYGVKNLIRVGTCGAIQKDVKVRDVIIAMTACTDSNMNRLTFPGFDFAPAANFDLLKKAYDAGTEKGLHVRVGNVLTADVFYRESMDMVKKLGDYGVLAVEMETTALYTLAAKYGVNALSVLTVSDHIFTGEETTSEERQTTFNEMIEIALDAAIQQ | Catalyzes the reversible phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. | C3P552 |
Q6BXX5 | RTC1_DEBHA | Restriction of telomere capping protein 1 | Debaryomyces | MPDPNELNANQSSLSRFAFNIYGALNQAQSLEGNSSASPTPSMNPKQHNKSGTSSSNKEKLVYNCEREVSCISQFNHSLNGLVKNYEEDPLHHLIIGGKNYLKLLAMNNDQTKIVHEVDILESSKSIYSSSRTLSSNKLTSVNTIESQHDTIACELATGLISVYKVQNNGKCKLVRKYSDHIRCVNSLDFINQSNVANSSSPYQLISGSQDGTIKLWDLRSASNKPTLTISSNSHSDPVRSCQYSPHSTVRNKLTILSVHDSGALCKYDLRSPNGGYQHNINVPERKWNFHTGPALSLNIHPEKEYVITGGRDQKVCIWN... | May be involved in a process influencing telomere capping. | Q6BXX5 |
E3X5D6 | RU1C_ANODA | U1 small nuclear ribonucleoprotein C | Anopheles | MPKYYCDYCDTYLTHDSPSVRKTHCTGRKHKDNVKFYYQKWMEEQAQHLIDATTAAYKAGKIAQNPFTAGPPKPNISIPPPTMNMPPRPGIIPGMPAGAPPLLMGPNGPLPPPMMGMRPPPMMVPTMGMPPMGLGMRPPVMSAAPPQLNPK | Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. U1-C is directly involved in initial 5' splice-site recognition for both constitutive and regulated alternative splicing. The interaction with the 5' splice-site seem... | E3X5D6 |
Q93743 | GPA6_CAEEL | Guanine nucleotide-binding protein alpha-6 subunit | Caenorhabditis | MGAGATGLRGARLSPEERANSSKSRAIDRALSKDHTDDLNRFKILLLGTAESGKSTIFKQMRVLHLDGYAKEDALEYLSIIHSNCMEALTQLVDACTAFGINHDITVQEDVNRFEDFKRKLRDPEGLVIPVVIGRCMDRVWHSPSLQLCYDTRRFRFALLDSAKYFMDNIVRLTEDNYVPSIQDIVHCRISTTGINELAFNYKKMDFKMVDVGGQRSERRKWIHCFDNVDMILFIVSMSDYDQLDPEDNKYNRMKQSYEIFKTIVHSDLFRHASIVLFLNKYDVFVEKLKTSPLRRSFKNYEGDNSEESAREFIKKLFRR... | Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. | Q93743 |
A9B9W1 | TRPD_PROM4 | Anthranilate phosphoribosyltransferase | Prochlorococcus | MSDFSWPKILDKLLNGNELTSEETNALMNAWLNQELAPVQTGAFLAAFRSKNVSGLELAAMAKVLRDACVFPFPVPDLYLVDTCGTGGDGADTFNISTAVAFLSASLGVKIAKHGNRSASGKVGSADVLEGVGIRLDTPIENVVTALDKTGISFLFAPIWHSSLVNLAPLRKTLGVRTVFNLLGPLVNPFRPSAQVLGVATSELLDPIAQALKYLGLKRAVVVHGAGGLDEASLEGSNQVRFLKDGEISSSEIDITDLGLTPASNNQLKGGDLSKNEAIFMSVLKGNATKPQMEVVALNTALVLWASGLEEDLSQGVEMA... | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). | A9B9W1 |
P46403 | PRL_FELCA | Prolactin | Felis | MDNKGWSLKGSLLFLLLLLSDLLLCKSVASLPICPSGAVNCQVSLRDLFDRAVILSHYIHNLSSEMFNEFDKRYAQGRGFITKAINSCHTSSLPTPEDKEQAQQIHHEDLLNVILRVLRSWNDPLYHLVTEVRGLHEAPDAILSRAIEIEEQNRRLLEGMEKIVHQVHPGVRENEVYSVWSGLPSLQMADEDSRLFAFYNLLHCLRRDSHKIDSYLKLLKCRIVYDSNC | Prolactin acts primarily on the mammary gland by promoting lactation. | P46403 |
A1KJR3 | UREF_MYCBP | Urease accessory protein UreF | Mycobacterium tuberculosis complex | MTSLAVLLTLADSRLPTGAHVHSGGIEEAIAAGLVTGLATLEAFLKRRVRTHGLLTASIAAAVHRGELAVDDADRETDARTPAPAARHASRSQGRGLIRLARRVWPDSGWEELGPRPHLAVVAGRVGALSGLAPEHNALHLVYITMTGSAIAAQRLLALDPAEVTVVTFQLSELCEQIAQEATAGLADLSDPLLDTLAQRHDERVRPLFVS | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | A1KJR3 |
Q67QQ0 | G6PI_SYMTH | Phosphohexose isomerase | Symbiobacterium | MSSSLRFTVSPSLLGPHPHELTYQAEAIRIAHRMLHERTGPGAGFTGWLDLPERYDREEFRRIQEAAARIRGDSDVLVVIGIGGSYLGARATVEALGHAFHNLLPPERRGAPQIFFAGTDLSPRYLTELLDVLEDREVSLNVVSKSGTTTEPAIAFRLLRNWMERRYGKEGARRRIYATTDAARGALKQLADAEGYTRFVIPDDVGGRYSVLTAVGLLPIAAAGIDIDALMAGAAAAAAAYSDPDLERNPCYQYAAARNALYRKGMTTEVLVTYEPALKATAEWWKQLFGESEGKDGKGIFPAAAAFTTDLHSLGQYIQE... | Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate. | Q67QQ0 |
A3MPB4 | QUEA_BURM7 | Queuosine biosynthesis protein QueA | pseudomallei group | MLTLSDFDFDLPPELIAQTALPERSASRLLEVDNTNPSAPPRLIDRRFAELPACVAPGDLLVFNDTKVLKARFFGRKASGGKIEVLIERVTGERTALAQIRASKSPPPGTTLTLADAFDVTVGERVEPFFTLHFPDNCLVLIERHGRLPLPPYIEHAPDAADETRYQTVFAANPGAVAAPTAGLHFDDAVLAALEARGVERATLTLHVGAGTFQPVRVENLAEHRMHSESYELTDALVEKIAATRARGGRVIAVGTTSMRALEAAARDAQAAGRPLAATRAETDIFITPGYRFRVVDRLVTNFHLPKSTLLMLVSAFAGI... | Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA). | A3MPB4 |
Q4QMR0 | TSAC_HAEI8 | tRNA threonylcarbamoyladenosine biosynthesis protein TsaC | Haemophilus | MNREQIAEALRQNQVVAYPTEAVFGLGCNPQSESAVKKLLDLKQRPVEKGLILVAPSLDFFRPFVDFEQINDEQLSHLQGKYERPTTWIVPAKSTTSHFLTGKFDSIAIRLCDHPSVKALCELTGFALTSTSANLTGEPPCRTADEVRLQFGADFPVLDEIVGDARNPSEIRDLRTNQLFRQG | Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate. | Q4QMR0 |
Q971B7 | VATA_SULTO | V-ATPase subunit A | Sulfurisphaera | MVSEGRVVRVNGPLVIADGMREAQMFEVVYVSDLKLVGEITRIEGDRAFIQVYESTDGVKPGDKVYRSGAPLSVELGPGLIGKIYDGLQRPLDSIAKVSNSPFVARGVSIPALDRQTKWHFVPKVKSGDKVGPGDIIGVVQETDLIEHRILIPPNVHGTLKELAREGDYTVEDVVAVVDMNGDEIPVKMYQKWPVRIPRPYKEKLEPVEPLLTGIRVLDTVFPIAKGGTAAIPGPFGSGKTVTLQSLAKWSAAKVVIYVGCGERGNEMTDELRSFPKLKDPWTGKPLLLRTILVANTSNMPVAARESSIYVGVTMAEYFR... | Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal alpha chain is a catalytic subunit. | Q971B7 |
Q47SA3 | LEUC_THEFY | Isopropylmalate isomerase | Thermobifida | MARTMAEKVWEEHVVRRAEGEPDLLYIDLHLIHEVTSPQAFEGLRLANRKLRRPDLTIATEDHNVPTENIFLPIADPVSRTQVETLRKNAAEFGVRLHPMGDIDQGIVHVIGPQLGLTQPGMTIVCGDSHTSTHGAFGALAFGIGTSQVEHVMATQTLPMTPFKTMAVNVEGKLKPGVTAKDIILAVIAQIGTGGGQGHVIEYRGEAIRSLSMEARMTICNMSIEAGARAGMIAPDQTTFDYLKGRPHAPKGELWDQAVEYWKTLPTDEGAVFDKEVFLNADELSPFVTWGTNPGQGVPLDSVVPDPESFTDPVERAAAE... | Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. | Q47SA3 |
Q475R7 | RUVA_CUPPJ | Holliday junction ATP-dependent DNA helicase RuvA | Cupriavidus | MIGRIAGTLIEKNPPHLLVDCHGVGYEIDVPMSTFYNLPATGQPVTLLTQLIVREDAHLLYGFGSAAERNTFRELIKITGIGARMALAVLSGMSVSELAQAITLQEAGRLTRVPGIGKKTAERLMLELKGKLGAELGHAPGAAPVHDSAVDILNALLALGYSEKEAATAIKQVPAGTGVSDGIKLALKALSKA | The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA... | Q475R7 |
A8XDR5 | SHE1_CAEBR | Protein spermless hermaphrodites 1 | Caenorhabditis | MSSHLKNLTENFENLAINPIFNTNWCDMPAEIKVECVGKMELTERLSLRSTAKAERSLVDSQKINIRRCAIHGLPEIRRVTLASKTGKIVFRAFRSANKEFEFLKYIWKIGVFENLYIWLDGKDSKEKLENFNGTIAAKSIDFHFCDEEFIVAILGKVKNGVESITMNADRGISYSVNEILKISHVQNVKYWQIDNYKRMSVLWKVAQVWIDISSKIGTTFQLSTEVYGLFHEFLQHFVDRIVSISQIRVRIRTNHPDRHILLELEFDGFVEFQHSFKFFRLMDMTANTRQKKVAAALLLLQEQESVLLTVCRPYQLEEG... | Sex-determining factor which regulates hermaphrodite development. | A8XDR5 |
P17058 | CRTC_RHOCB | Neurosporene hydratase | Rhodobacter | MIAFIGSVFSPWYRWSGRREPQNHCCINMVTTGTDGRFTMTDRGRSALRQSRDSFQVGPSKLTWTGKELVIDVDEWGALPKLGKLKGRVVLTPRAVTGVEVRLTPDAGHTWRPFAPIADVEVDLAPGHKWTGHGYFDANFGTRALEEDFSFWTWGRFPLKDRTVCFYDATRLDRTKVALAVQINPDGSVCEIDSPPPLVKMKRTPWFVRRETRCDAGAHPAGVYSLLEAPFYSRALMRTQIDGEETVGMHEALDLVRFRQPVLKPMLAVRVPRRAGWKHKD | Involved in the biosynthesis of carotenoids spheroidene and spirilloxanthin. Catalyzes the hydration of neurosporene to the corresponding hydroxylated carotenoids 1-HO-neurosporene and that of lycopene to 1-HO-lycopene. It exhibits negligible activity in converting HO-neurosporene, HO-lycopene, or any other derivative ... | P17058 |
Q465T0 | KUP_METBF | Probable potassium transport system protein kup | Methanosarcina | MFSKSEFREVVKSMGLVFGDIGTSPIYTLTVIFLLTRPTHTHIIGVLSLIIWTLIILVTVEYAWLAMSLGKKGEGGTIVLKEILVPLLKSSRNVAFVTLLAYIGTSFLMGDGVITPAISILSAVEGLRIIPQFENIGQSTIILISAAIAIALFSVQSKGIEKITWVFGPIMVLWFATIGFSGIASIFYTPEVLKAINPYYAIRFLLDNGIIGFFVLSEVILCATGGEALYADMGHLGREPILKAWRFVFLALVLNYLGQGAFLIRNPGSTNFLFEMINQQANILYIPFLLLSVVATIIASQAMISGMFSIVYQGITTRII... | Transport of potassium into the cell. | Q465T0 |
Q5KYR0 | IOLD_GEOKA | 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase | Geobacillus thermoleovorans group | MKTIRLTTAQALVKFLNQQYVEFDGHIQKFVKGIFTIFGHGNVLGLGQALEEDPGELEVYQGRNEQGMAHAAIAFAKQKHRRQIMACTSSVGPGAANMVTAAATASANHIPVLLLPGDTFATRQPDPVLQQIEHWHDLTVSTNDAFRAVSKYWDRISRPEQLMSAMIQAMRVLTDPANTGAVTIALPQDVQGEAYDFPESFFQKRIHRIERRVPAKAAIHEAVELIRRKKKPIIICGGGVRYSEAAEELKQFAEKFHIPYGETQAGKSAVESAHPYNLGGIGVTGNLAANIIAKEADLVIGIGTRYTDFTTGSKQLFQHP... | Involved in the cleavage of the C1-C2 bond of 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione (THcHDO) to yield 5-deoxy-glucuronate (5DG). | Q5KYR0 |
P29230 | VLPC_MESHY | VlpC prolipoprotein | Mesomycoplasma | MKKSIFSKKLLVSFGSLVALASIPLIAISCGQTNTDKSQQPGSGSSTSGDQSGTTTGGHSGSGTSTSGGQSGTTSGSGTTTGEQTETAPKSPESGSQEATPKSPESGSQEATPKSPESGSQEAAPKSSESGSQEAAPKSSESGSQEAAPKSSESGSQKTT | Responsible for the antigenic diversity for host adaptation. | P29230 |
Q15678 | PTN14_HUMAN | Protein-tyrosine phosphatase pez | Homo | MPFGLKLRRTRRYNVLSKNCFVTRIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLDKFANEPLLFFGVMFYVPNVSWLQQEATRYQYYLQVKKDVLEGRLRCTLDQVIRLAGLAVQADFGDYNQFDSQDFLREYVLFPMDLALEEAVLEELTQKVAQEHKAHSGILPAEAELMYINEVERLDGFGQEIFPVKDNHGNCVHLGIFFMGIFVRNRIGRQAVIYRWNDMGNITHNKSTILVELINKEETALFHTDDIENAKYISRLFATRHKFYKQNKICTEQSNSPPPIRR... | Protein tyrosine phosphatase which may play a role in the regulation of lymphangiogenesis, cell-cell adhesion, cell-matrix adhesion, cell migration, cell growth and also regulates TGF-beta gene expression, thereby modulating epithelial-mesenchymal transition. Mediates beta-catenin dephosphorylation at adhesion junction... | Q15678 |
P93738 | ACT9_ARATH | Putative actin-9 | Arabidopsis | MKPIVCDKGHGMVQAGFAGDEAPKVVFPCVVGRPRDGLNPNESYVGEEGHANRDILTLKDPMEHGIVNNWDDMEKIWHYTFYNELRVDPEEHPVLLTEAPYNPKANREKMTQIMFESFDVPAMYVSMQSVLYLYSSGRTTGVVLDLGERVSHTVPVYEGYALPHGILRLDLGGRDLTDYLIEIMTERGYTYTTSAEREIVRDIKEKLCYVALDYEQEMEKTTKGWTIDKTYVLPDGQEITIEAERFMCPEVLFQPSVIGKESSGIHEATRNSILKCPVDTRRDMYGNILMTGGTTMLHGIKERMTKELNALVPSSMKVKV... | Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Essential component of cell cytoskeleton; plays an important role in cytoplasmic streaming, cell shape determination, cell division, organelle movement and extension growth. | P93738 |
A6L9X1 | ISPE_PARD8 | 4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase | Parabacteroides | MICFPNAKINLGLNVVSKRPDGYHNIETIFYPIPVRDALEIVASDRTCFTQTGIPVDAPQEKNLVIKALNALKTRYEIPPLEIHLLKAIPFGAGLGGGSADAAFMLKLVNDFCGLDIHPDELEAIASTIGADCPFFIRNTPVFATGTGNQFEPVDLSLKDYYLCLVKPDVAVSTPEAYSMVTPAAPETSLKEIIRLPVSEWKERMVNDFERSVFPRHPVIERIKDTLYEGGALYAAMSGSGSSVFGLFEKPTHFKEQSLFSDCFLWEGQLS | Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. | A6L9X1 |
P37330 | MASZ_ECOLI | Malate synthase G | Escherichia | MSQTITQSRLRIDANFKRFVDEEVLPGTGLDAAAFWRNFDEIVHDLAPENRQLLAERDRIQAALDEWHRSNPGPVKDKAAYKSFLRELGYLVPQPERVTVETTGIDSEITSQAGPQLVVPAMNARYALNAANARWGSLYDALYGSDIIPQEGAMVSGYDPQRGEQVIAWVRRFLDESLPLENGSYQDVVAFKVVDKQLRIQLKNGKETTLRTPAQFVGYRGDAAAPTCILLKNNGLHIELQIDANGRIGKDDPAHINDVIVEAAISTILDCEDSVAAVDAEDKILLYRNLLGLMQGTLQEKMEKNGRQIVRKLNDDRHYT... | Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA. | P37330 |
Q31UE5 | UBID_SHIBS | Polyprenyl p-hydroxybenzoate decarboxylase | Shigella | MDAMKYNDLRDFLTLLEQQGELKRITLPVDPHLEITEIADRTLRAGGPALLFENPKGYSMPVLCNLFGTPKRVAMGMGQEDVSALREVGKLLAFLKEPEPPKGFRDLFDKLPQFKQVLNMPTKRLRGVPCQQKIVSGDDVDLNRIPIMTCWPEDAAPLITWGLTVTRGPHKERQNLGIYRQQLIGKNKLIMRWLSHRGGALDYQEWCAAHPGERFPVSVALGADPATILGAVTPVPDTLSEYAFAGLLRGTKTEVVKCISNDLEVPASAEIVLEGYIEQGETAPEGPYGDHTGYYNEVDSFPVFTVTHITQREDAIYHST... | Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis. | Q31UE5 |
Q2JU34 | NU4LC_SYNJA | NDH-E | unclassified Synechococcus | MLQLQFFLVVAAILFCIGIYGLIVSRNAIRVLMSIELMLNAVNLNFMAFSNFVDSGLIRGQVFSVFVITVAAAEAAVGLAIVLGIYRNRATIDMESFNLLRW | NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus co... | Q2JU34 |
C1CLR7 | ENGB_STRZP | Probable GTP-binding protein EngB | Streptococcus | MELNIHNAEILLSAANKSHYPQDELPEIALAGRSNVGKSSFINTMLNRKNLARTSGKPGKTQLLNFFNIDDKMRFVDVPGYGYARVSKKEREKWGCMIEEYLTTRENLRAVVSLVDLRHDPSADDVQMYEFLKYYEIPVIIVATKADKIPRGKWNKHESAIKKKLNFDPSDDFILFSSVSKAGMDEAWDAILEKL | Necessary for normal cell division and for the maintenance of normal septation. | C1CLR7 |
Q57GK0 | ULAG_SALCH | L-ascorbate utilization protein G | Salmonella | MSKVQSITRESWILSTFPEWGSWLNEEIEQEQVAPGTFAMWWLGCTGIWLKSEGGTNVCVDFWCGTGKQSHGNPLMKTGHQMQRMAGVKKLQPNLRTTPFVLDPFAIRQIDAVLATHDHNDHIDVNVAAAVMQNCADDVPFIGPQTCVDLWVGWGVPKERCIVVKPGDVVKVKDIEIHALDAFDRTALITLPADQKAAGVLPEGMDVRAVNYLFKTPGGNLYHSGDSHYSNYYAKHGNEHQIDVALGSYGENPRGITDKMTSADILRMAESLNTKVVIPFHHDIWSNFQADPQEIRVLWEMKKDRLKYGFKPFIWQVGGK... | Probably catalyzes the hydrolysis of L-ascorbate-6-P into 3-keto-L-gulonate-6-P. Is essential for L-ascorbate utilization under anaerobic conditions. | Q57GK0 |
A5F623 | TILS_VIBC3 | tRNA(Ile)-lysidine synthetase | Vibrio | MDDLYLHFVQQLARYPFRKILLALSGGVDSQVLLALLARGRDEFGWDVTAVHVHHGLSPNADQWAQHCQRCCREVGMACQIEYVQLDVASGESIEKLAREARYRVLAPHVNAQTLLLLGQHADDQLETFLLALKRGSGPKGLAAMAAYAPFAEGHLLRPLLTVSRQHIEAYAKQHKLTWVIDESNADIRYERNFLRHQVTPVLTERWPSIRQAVQRSAELCAEQEALLQEFLAEALKKAITAEGGLSIAVLAEGSEGMRRQLIRAWFAHHRLPMPSRQHTERIWCEVALASEDANPKLKLNHIEVRRFQHCLYLVPPEKD... | Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. | A5F623 |
A7HWQ3 | RL7_PARL1 | 50S ribosomal protein L7/L12 | Parvibaculum | MTDLAKIVEDLSNLTVLEAAELSKMLEEKWGVSAAAPVAVAAAGAAPAAAAEEQTEFDVILAAAGDKKIEVIKEVRAITGLGLKEAKDLVEGAPKTVKEAASKDEAAKIKAQLEKAGAKVELK | Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation. | A7HWQ3 |
A9JS51 | F166B_XENLA | Protein FAM166B | Xenopus | MAVTFPPKISPTLMTPDPHFIPGYSGFCPQYRYSLGKTYGQLTSHLLTNPDIRRSGHLVLQSNPFPPAPRGHSYNEASQELGGRRRRQRLGDPKLTISMIPGYTGFIPRSQKFFAKTYAETSWDALSDFHNEQQMQESQRQEMLLTSKLQEGRQPQTEHEKQLLTARHRTPLPALSKEPAPFMSLRGFQPQGSPYYMEEENPNKYFISGYTGYVPRSRFLIGNGYPITTNRAMVEFAHMNQKKGVRFSDQQGHNEGDNLHTEQGQIYLEELGLLPRYTGYVPGYKFQFGNTFGRLTQNALGQSTLQKQTVN | Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating. | A9JS51 |
B6YSX7 | RL11_THEON | 50S ribosomal protein L11 | Thermococcus | MPQVVEVLVEGGKASPGPPLGPAIGPLGLNVKQVVDEINKATKDFEGMQVPVKIIVEDPKKKTFRIEVGVPPVSQLIKKELGIPKGSSEAGHSPVGNLTMEQVIRIAKAKMDQMLAADLKAAAKEVIGTALSMGVTVEGKDPREVQKEIDEGVYDEIFANAEE | Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | B6YSX7 |
Q9WZ15 | KHSE_THEMA | Homoserine kinase | Thermotoga | MKVLVPATTTNLGAGFDVFGLALDLFNEVEFSFDTKETTIESTGKYASDLKDHNLFFEVLRFFERKTGYRVPPVRIKQTCNIPVSSGLGSSAAVIVAALHIANEGTGRNLSREDLMKLAVELEGHPDNVVPAFTGGLVVCYQNGSHLDFEKFEIDLSLTFLVPNFPVCTNEMRKILPEKVPFEDAVFNIKNSCQFLAKIAAGKIKEALKYVGDRLHQNYRINGNKKMKEFVEAILSKNPEYWFVSGSGPSVCSNINDFEGIPYLKDVLKLRVNNRGMIVSE | Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate. | Q9WZ15 |
P30083 | VIPR1_RAT | Pituitary adenylate cyclase-activating polypeptide type II receptor | Rattus | MRPPSPPHVRWLCVLAGALACALRPAGSQAASPQHECEYLQLIEIQRQQCLEEAQLENETTGCSKMWDNLTCWPTTPRGQAVVLDCPLIFQLFAPIHGYNISRSCTEEGWSQLEPGPYHIACGLNDRASSLDEQQQTKFYNTVKTGYTIGYSLSLASLLVAMAILSLFRKLHCTRNYIHMHLFMSFILRATAVFIKDMALFNSGEIDHCSEASVGCKAAVVFFQYCVMANFFWLLVEGLYLYTLLAVSFFSERKYFWGYILIGWGVPSVFITIWTVVRIYFEDFGCWDTIINSSLWWIIKAPILLSILVNFVLFICIIRI... | This is a receptor for VIP. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. | P30083 |
D2QZ34 | FTSH_PIRSD | ATP-dependent zinc metalloprotease FtsH | Pirellula | MSSDNGSGRQGGDRGGSTGYNLLMYLGFGAIIATLVALYVLQMFQTSLDYTDLERLVAASQYEKDESKLTAGSPGYIDVKVEARNTLRRMRVSNLRKVELGPTAVRGQIDLVELKPVGTSGDRWEPDSKTLRQNVEFRTNLSDKGSNRDDIETAIRNSNIPFRHADPPGPWEQHSQLIIGMLLAAMLIYIVVRRLSAAGSPMSFGRSRGKLYAQEELGITFNDVAGIDEAVEEVREVVDFLRSPEKYQKLGGRIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSLSGSDFVEMFVGVGAARVRDMFQQAEAKAPCIIFI... | Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins. | D2QZ34 |
B5E9T1 | AROA_CITBB | 5-enolpyruvylshikimate-3-phosphate synthase | Citrifermentans | MQNYTVRPAKSVRGEISVPGDKSISHRSIMFGSIASGVTTVTGFLRGEDALATLEAFRAMGVQIDDDGETVTIQGRGLHGLSEPTDVLDCGNSGTSMRLLTGLLAGQNFFSVLSGDKYLRARPMKRVVGPLAQMGARISGRAGGEKAPLAIQGSKLKGIEYDSPVSSAQVKSAIMLAGLYAGGETVVREPHLSRDHSERMLRAFGAHVETFPGGVKVRGGAELTGRDIVVPGDISSAAFFLVAGLIVPGSDLLIRGVGVNPTRTGIIDVLKGMGGDLELINQRDESGEPVADIRVRHSKLTAMEISGDVVPRAIDEFPAI... | 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. | B5E9T1 |
P47368 | TOP1_MYCGE | Untwisting enzyme | Mycoplasma | MIKNLVVIESPNKVKTLKQYLPSDEFEIVSTVGHIREMVYKNFGFDENTYTPIWEDWTKNKQKNPKQKHLLSKFEIIKSIKAKASDAQNIFLASDPDREGEAISWHVYDLLDQKDKAKCKRITFNEITKKAVVDALKQPRNIDLNWVESQFARQILDRMIGFRLSRLLNSYLQAKSAGRVQSVALRFLEEREKEIAKFVPRFWWTVDVLLNKENNQKVVCANKSIPLVLREINPELSASLKLDFEAAENVSGIDFLNEASATRFANQLTGEYEVYFIDEPKIYYSSPNPVYTTASLQKDAINKLGWSSKKVTMVAQRLYE... | Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked b... | P47368 |
Q82Y49 | UPPP_NITEU | Undecaprenyl pyrophosphate phosphatase | Nitrosomonas | MDWLILLKALLLGIVEGLTEFLPISSTGHLILAGDLLNFNDDKAKVFTVAIQLGAILAVCWEYRERLVNIIRNLGTRQANRFVINLFIAFLPAAILGLLFIKTIKHYLFHPMPVAIALVTGGILILWAERREHRIEAETVDDMSWKQALQVGCAQCLALIPGTSRSGATIIGGLLFGLSRKAAAEFSFFLAIPVMFAATFYDVYKHREFLYIDDLGMFATGSVAAFISALIAIRGFIRYISHHDFTLFAWYRIGFGLIVLLTAYSGLVDWSVD | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | Q82Y49 |
A0A2P1GIW7 | SAT_CATRO | Stemmadenine O-acetyltransferase | Catharanthus | MAPQMQILSEELIQPSSPTPQTLKTHKLSHLDQVLLTCHIPIILFYPNQLDSNLDRAQRSENLKRSLSTVLTQFYPLAGRININSSVDCNDSGVPFLEARVHSQLSEAIKNVAIDELNQYLPFQPYPGGEESGLKKDIPLAVKISCFECGGTAIGVCISHKIADALSLATFLNSWTATCQEETDIVQPNFDLGSHHFPPMESIPAPEFLPDENIVMKRFVFDKEKLEALKAQLASSATEVKNSSRVQIVIAVIWKQFIDVTRAKFDTKNKLVAAQAVNLRSRMNPPFPQSAMGNIATMAYAVAEEDKDFSDLVGPLKTSL... | Component of iboga and aspidosperma monoterpenoid indole alkaloids (MIAs, e.g. tabersonine and catharanthine) biosynthesis pathway from 19E-geissoschizine. Acetyltransferase that catalyzes the formation of O-acetylstemmadenine from stemmadenine. | A0A2P1GIW7 |
Q9X4K2 | AZOR_GEOSE | FMN-dependent NADH-azoreductase | Geobacillus | MTNVLYITAHPHDDTQSYSMAVGKAFIDTYKQVHPDHEVIHLDLYKEYIPEIDVDVFSGWGKLRSGKSFEELSDEEKAKVGRMNELCEQFISADKYVFVTPMWNFSFPPVLKAYIDAVAVAGKTFKYTEQGPVGLLTDKKALHIQARGGFYSEGPAAEMEMGHRYLSVIMQFFGVPSFEGLFVEGHAAVPEKAEEIKANAIARAKDLAHTF | Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. | Q9X4K2 |
A5IQ31 | Y500_STAA9 | Nucleoid-associated protein SaurJH9_0500 | Staphylococcus | MRGGGNMQQMMKQMQKMQKKMAQEQKKLKEERIVGTAGGGMVAVTVTGHKEVVDVEIKEEAVDPDDIEMLQDLVLAATNEAMNKADELTQERLGKHTQGLNIPGM | Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | A5IQ31 |
Q486Z0 | ISCS_COLP3 | Cysteine desulfurase IscS | Colwellia | MKLPIYFDYSATTPVDKRVAEKMMQYMTNDGHFGNPASRSHKFGWQAEEAVDIARNQIAELINADPREIVFTSGATESNNLAIKGAANFYNKKGKHIITCKTEHKAVLDTCRELERQGFEVTYLDPEENGLIDLNKLNDAMRDDTILVSIMQVNNEIGVIQDISEIGEMCRARKIVFHVDAAQSAGKINIDMQALKVDLMSISAHKMYGPKGIGALYVSRKPRIRLEAQTHGGGHERGMRSGTLATHQIVGMGEACRLAKEEMAQDQAHVTAMRDRLWAGLNSMEQVFINGDADKRYPGNLNVSFNFVEGESLIMALKDL... | 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... | Q486Z0 |
A9BAQ7 | ILVD_PROM4 | Dihydroxy-acid dehydratase | Prochlorococcus | MLRSSAITQGIQRSPNRAMLRAVGFNDNDFNKPIIGIANGYSTITPCNVGLNNLALHAEASTKVSGAMPQMFGTITVSDGISMGTEGMKYSLVSREVIADSIETACNAQSMDGVLAIGGCDKNMPGAMIAMARMNIPAIFVYGGTIKPGKLDGCDLTVVSAFEAVGQLTSGKITEDKLIAVEKNCIPGAGSCGGMFTANTMSAAIETLGLSLPYSSTMAAEDKEKIESAERSAKVLVDAIEKNIRPLDLLTKKSFENAIAVVMAVGGSTNAVLHLLAIARSSGVDLCIDDFERIRQKVPVICDLKPSGKYVTVDLHKAGG... | 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 (... | A9BAQ7 |
P49286 | MTR1B_HUMAN | Melatonin receptor type 1B | Homo | MSENGSFANCCEAGGWAVRPGWSGAGSARPSRTPRPPWVAPALSAVLIVTTAVDVVGNLLVILSVLRNRKLRNAGNLFLVSLALADLVVAFYPYPLILVAIFYDGWALGEEHCKASAFVMGLSVIGSVFNITAIAINRYCYICHSMAYHRIYRRWHTPLHICLIWLLTVVALLPNFFVGSLEYDPRIYSCTFIQTASTQYTAAVVVIHFLLPIAVVSFCYLRIWVLVLQARRKAKPESRLCLKPSDLRSFLTMFVVFVIFAICWAPLNCIGLAVAINPQEMAPQIPEGLFVTSYLLAYFNSCLNAIVYGLLNQNFRREYK... | High affinity receptor for melatonin. Likely to mediate the reproductive and circadian actions of melatonin. The activity of this receptor is mediated by pertussis toxin sensitive G proteins that inhibit adenylate cyclase activity. | P49286 |
A8FYV9 | NQRD_SHESH | NQR-1 subunit D | Shewanella | MANAKELKEVLSGPIVSNNPIALQVLGVCSALAVTSKLETALVMTIALTAVCAFSNLFISMLRNHIPSSVRIIVQMTVIASLVIVVDQVLQAYAYDVAKQLSVFVGLIITNCIVMGRAEAYAMKTPPMMSFMDGIGNGIGYGAILLSVGFVRELFGNGSLFGVEILSKISDGGWYQPNGLLLLPPSAFFLIGTLIWIIRTIKPEQVEAKG | NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol. | A8FYV9 |
C1KWK6 | MGSA_LISMC | Methylglyoxal synthase | Listeria | MHIALIAHDEKKDLMVGFATAYKHLLEPHQLYATGTTGLRIIEATGLTVHRFKSGPLGGDQQIGARISENKMDLVIFLRDPLTAQPHEPDVTALIRLCDVYEIPLATNIGTAEILIRGLGAGFLDWRDLRRNDE | Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate. | C1KWK6 |
B5BDQ0 | CRL_SALPK | Sigma factor-binding protein Crl | Salmonella | MTLPSGHPKSRLIKKFTALGPYIREGQCEDNRFFFDCLAVCVNVKPAPEKREFWGWWMELEAQEKRFTYRYQFGLFDKEGNWTVVPINETEVVERLEYTLREFHEKLRDLLISMELALEPSDDFNDEPVKLSA | Binds to the sigma-S subunit of RNA polymerase, activating expression of sigma-S-regulated genes. Stimulates RNA polymerase holoenzyme formation and may bind to several other sigma factors, such as sigma-70 and sigma-32. | B5BDQ0 |
Q3B2C2 | LPXK_CHLL3 | Lipid A 4'-kinase | Pelodictyon | MHERRLNILLRPAALLYGLVAAVRNALFDRGMLKAWKSPIPVVSIGNLTAGGTGKTPLVDWVLKYYLSIGCRPAVVSRGYGRRSKGVQLVSDGRNILLGSTRSGDETAMLAANNPEAVVVVAEQRSEGVQFIMERFRGERPDVIILDDAFQHRQLARDLDIVVINSREPFAAAKMLPEGRLREPKSGIGRADVAVLSKITDESKADAIEAELTGSVALVARTRVVIGELSPFGPKGRSTAPHPDPAGLKALAFAGIASPASFVESLMKKGVHVVEQRFFRDHEPYTLNNFLPLVEEARRKGLTLVTTEKDRYRLEGEPGL... | 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). | Q3B2C2 |
Q9GGE2 | RR14_CHLRE | 30S ribosomal protein S14, chloroplastic | Chlamydomonas | MAKKSMIQRELKRQKLVMKYATKRAALKEQIKQTTFLKEKLSLHRKLQQLPRNSSAVRLHNRCMITGRPKGYFRDFGLSRHVLREMAHQGLLPGVCKSSW | Binds 16S rRNA, required for the assembly of 30S particles. | Q9GGE2 |
P09116 | CASB_RABIT | Beta-casein | Oryctolagus | MKVLILACLVALALAREKEQLSVPTEAVGSVSSSEEITHINKQKLETIKHVEQLLREEKLQDKILPFIQSLFPFAERIPYPTLPQNILNLAQLDMLLPLLQPEIMEDPKAKETIIPKHKLMPFLKSPKTVPFVDSQILNLREMKNQHLLLPQLLPFMHQVFQPFPQTPIPYPQALLSLPQSKFMPIVPQVVPYPQRDMPIQALQLFQELLFPTHQGYPVVQPIAPVNV | Important role in determination of the surface properties of the casein micelles. | P09116 |
Q8FAD1 | SYV_ECOL6 | Valyl-tRNA synthetase | Escherichia | MEKTYNPQDIEQPLYEHWEKQGYFKPNGDESQESFCIMIPPPNVTGSLHMGHAFQQTIMDTMIRYQRMQGKNTLWQVGTDHAGIATQMVVERKIAAEEGKTRHDYGREAFIDKIWEWKAESGGTITRQMRRLGNSVDWERERFTMDEGLSNAVKEVFVRLYKEDLIYRGKRLVNWDPKLRTAISDLEVENRESKGSMWHIRYPLADGAKTADGKDYLVVATTRPETLLGDTGVAVNPEDPRYKDLIGKYVILPLVNRRIPIVGDEHADMEKGTGCVKITPAHDFNDYEVGKRHALPMINILTFDGDIRESAQVFDTKGNE... | 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. | Q8FAD1 |
Q93ZR6 | WSD1_ARATH | Wax synthase | Arabidopsis | MKAEKVMEREIETTPIEPLSPMSHMLSSPNFFIVITFGFKTRCNRSAFVDGINNTLINAPRFSSKMEINYKKKGEPVWIPVKLRVDDHIIVPDLEYSNIQNPDQFVEDYTSNIANIPMDMSKPLWEFHLLNMKTSKAESLAIVKIHHSIGDGMSLMSLLLACSRKISDPDALVSNTTATKKPADSMAWWLFVGFWFMIRVTFTTIVEFSKLMLTVCFLEDTKNPLMGNPSDGFQSWKVVHRIISFEDVKLIKDTMNMKVNDVLLGMTQAGLSRYLSSKYDGSTAEKKKILEKLRVRGAVAINLRPATKIEDLADMMAKGS... | Bifunctional wax ester synthase/diacylglycerol acyltransferase . Involved in cuticular wax biosynthesis . Required to reduce leaf water loss, especially during drought . | Q93ZR6 |
A1R5H8 | PANB_PAEAT | Ketopantoate hydroxymethyltransferase | Paenarthrobacter | MAPSNLPESTTPAEVPAPYGTGPAAAAQAASAAGRKPISRVRIHHLQQAKDNGEHFAMLTAYEQYTAEIFDQAGIEVLLVGDSASNNVYGNETSLPVTVDELLPLTRAVSRSAKRALIVADLPFGSYEVSPGQAVATGVRFLKEGLAHAVKIEGTAYYADTVRAMVQAGIPVMAHIGFTPQSEHSLGGYRVQGRGDDAQRLVDDAVALQDAGAFSVLMEMVPAETAAAVDAALRVPTVGIGAGKTTTGQVLVWQDMAGLRGGKMAKFVKQYADLRTTLSDAAAAYGEDVRSGQFPGPEHSF | Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. | A1R5H8 |
O15254 | ACOX3_HUMAN | Pristanoyl-CoA oxidase | Homo | MASTVEGGDTALLPEFPRGPLDAYRARASFSWKELALFTEGEGMLRFKKTIFSALENDPLFARSPGADLSLEKYRELNFLRCKRIFEYDFLSVEDMFKSPLKVPALIQCLGMYDSSLAAKYLLHSLVFGSAVYSSGSERHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPATEEFIIHSPDFEAAKFWVGNMGKTATHAVVFAKLCVPGDQCHGLHPFIVQIRDPKTLLPMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLLNRMGDVTPEGTYVSPFKDVRQRFGASLGSLSSGRVSIVSLAILNLK... | Oxidizes the CoA-esters of 2-methyl-branched fatty acids. | O15254 |
P51188 | CHLN_PORPU | Light-independent protochlorophyllide reductase subunit N | Porphyra | MSIVQSDALTFECETGNYHTFCPISCVSWLYQKIEDSFFLVIGTKTCGYFLQNAMGVMIFAEPRYAMAELEEGDISAKLNDYGELRRLCLQIKKDRNPSVIFWIGTCTTEIIKMDLEGIAPKLEAEIRVPIVVARANGLDYAFTQGEDTVLAAMAQRCPSHHYIENTNPHVPLVLFGSLPDPVVTQLVMELKKQGIIVSGWLPSKRYTELPVIQEGYYVAGVNPFLSRTATTLMRRRKTKLIGAPFPIGPDGTRAWIEKICSVFSIKPEGLAEREKDIWDSLEDYIALIRGKSVFFMGDNLLEVSLARFLTRCGMTVYEI... | Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. | P51188 |
A8F0E7 | RL9_RICM5 | 50S ribosomal protein L9 | spotted fever group | MEIILIKPVRKLGKIGDILKVADGFGRNYLLPQKLAIRATEPNKELIVKQKHEFEAKDKQIREEVEKINALIKDQKLVFIRQTSDDGKLFGSVTNKEIADKLSENVSYNISHSNIILDKQIKSTGIYTVEIRLHAELNAIVMVIVARSESEAQDYLREQKTETSEDLAESA | Binds to the 23S rRNA. | A8F0E7 |
D1AXT4 | FTSH_STRM9 | ATP-dependent zinc metalloprotease FtsH | Streptobacillus | MEDKNIKDDEILDDQNDNQEDVQNQDEEKEIKPKKPKKKVYISDDENAEEIKKRIESLKNKNNNISFRVKPPIFFFLILILMSTLFYFYGNKTALFQEKREISYTQFVTKVKQGDITEIRESQEKLTGIKKVAGKVEVFETNKLTDRLGQDTYLMEISKEKNVNIVVLGTPVSSIITRAIFSFAPLFMLLFFFYFINKKMMGSSGGVIGNPFNIGKGKGKISERPNVKFSDVAGLTEEKEELKEIVEFLKNPARFEKAGARVPKGVLLLGEPGTGKTLLAKAVAGESEAAFFPISGSEFIELYVGVGASRVRELFKDAKK... | Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins. | D1AXT4 |
A6UTP9 | DPCKG_META3 | Dephospho-coenzyme A kinase | Methanococcus | MYMLNESTKEILKKPFGKVYKELPPINRKVNIIAVGDITTKNLLSKSIIPNLSIIDLKTKRNIPVKINHKFKTVFEVNNPQGCISDEAEETIKYISSLDMVDTALIVKDGEEDLLTMMVIRYFPKDTIVLYGQPDEGVVLLTINQDLKHKINNILSMMDKI | Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA). | A6UTP9 |
A1A1M3 | UPPP_BIFAA | Undecaprenyl pyrophosphate phosphatase | Bifidobacterium | MNFFQAIFLGLVQALTEYLPVSSSAHIRIIGDLMLGSDPGAAFTAIIQIGTELAVILYFRHDIIRILGAWFGSLFGKEGKDFKSRMGAHNRDTQMGWFIIIGTLPILIAGLLFKDAIESTLRNLWITVTVLIIFGILLWVVDARAKQVKTMDEMTWKDALIFGIGQMLALIPGVSRSGGTITFGRAMGYTREAAVRVSFLMAIPAVFGAGILEAVSAVKDVAAGNAGMFPGWGATIAATIVAFVVGYVVIIGFLKFVSTFSYKAFAIYRIALAVVVALLLICGVLHPTEVVAAA | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | A1A1M3 |
A0KX80 | RNFB_SHESA | Rnf electron transport complex subunit B | Shewanella | MSTMLIAVILLTLLALFFGVLLGFAALKFKVEGNPIVDELEAILPQTQCGQCGYPGCRPYAEAIANGDKVNKCPPGGTATMEKLANLMGVEPEPLNAEAQSQVKKVAYIREDECIGCTKCIQACPVDAIIGAGKLMHTVLTADCTGCDLCVEPCPVDCIDMIPVGQNLKNWNWRLNAIPVTLIQETPHEEKRG | Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. | A0KX80 |
A0RXK2 | VATE_CENSY | V-ATPase subunit E | Cenarchaeum | MPPDPRLEAAVDKILDRTGEEILSGLGESRKEAAEALAGSAKTLEREYDRIVEEGRKEADKIHRKIVGSADLEARNKQILLLETAIDRVLEKVLASISAERGPGYPDMIKSLIGEATATLGTTQVVVRAGSRDKDVVQASLGGFPGAELAQEPIECLGGVKVSSKDGSMTLDNTIDARFDRMKPLIRKEIVSKFGIGI | Produces ATP from ADP in the presence of a proton gradient across the membrane. | A0RXK2 |
Q5FFR6 | RL15_EHRRG | 50S ribosomal protein L15 | Ehrlichia | MDVVMKLNNIFSGLPKKKKSKVLGRGIGCGKGKTSGRGHKGQKARSGVSINGFEGGQQSIFTRLPKRGFNSLPKNKYSIINVSLIQRLIDSGKIDNVSAITKEVLYNLGVISSVKQKIKILGDGKLNTTVCIEYDFISKSAKSQVTLLNSLSDSESK | Binds to the 23S rRNA. | Q5FFR6 |
A4G7G3 | RNH_HERAR | Ribonuclease H | Herminiimonas | MEKIDIFTDGACKGNPGRGGWGALLVMGEREKELFGGEPGTTNNRMELKAVIEALNALTRPCEVIVHTDSQYVQKGISEWIHGWKARGWKTAARAPVKNVDLWQALDAAQARHQIEWRWVRGHNGHVGNERADALANRGVETVNSN | Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. | A4G7G3 |
Q4WXX5 | ASF1_ASPFU | Anti-silencing function protein 1 | Aspergillus subgen. Fumigati | MSVVSLLGVKIVNNPAPFLAPYQFEITFECLEQLQKDLEWKLTYVGSATSSEYDQELDSLLVGPIPVGVNKFLFEADAPDLKRIPTSEILGVTVILLTCSYDGREFVRVGYYVNNEYDSEELTQDPPAKPIIERIRRNILAEKPRVTRFAIKWDSEEDAPAEYPPDQPEADLEDDGAAYGAEEAELEAALIRELEEAEREAAKGGDHEMEGAEETAGKDDEEEDLSDAESEDIEDESDDEEDDLDEDEGGDRDEDVEMGDDTESKDTNAASGHHQQQDIMVH | Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. | Q4WXX5 |
A8MFJ0 | EX7S_ALKOO | Exodeoxyribonuclease VII small subunit | Alkaliphilus | MESINFEETLKKLEDVVHKLEVEELSLDDSLKIFEEGIGLYRQCSNELNKIEKKISIIIEENEEFKKVPFPHDEEES | Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. | A8MFJ0 |
Q5PJB8 | SYV_SALPA | Valyl-tRNA synthetase | Salmonella | MEKTYNPQDIEQPLYEHWEKQGYFKPNGDESKESFCIMIPPPNVTGSLHMGHAFQQTIMDTMIRYQRMQGKNTLWQVGTDHAGIATQMVVERKIAAEEGKTRHDYGRDAFIDKIWQWKAESGGTITRQMRRLGNSVDWERERFTMDEGLSNAVKEVFVRLYKEDLIYRGKRLVNWDPKLRTAISDLEVENRESKGSMWHIRYPLADGAKTADGKDYLVVATTRPETVLGDTGVAVNPEDPRYKDLIGKFVILPLVNRRIPIVGDEHADMEKGTGCVKITPAHDFNDYEVGKRHALPMINILTFDGDIRESAEVFDTKGEE... | 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. | Q5PJB8 |
P10651 | H33_SCHPO | Histone H3.3 | Schizosaccharomyces | MARTKQTARKSTGGKAPRKQLASKAARKAAPATGGVKKPHRYRPPTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAIGALQEAVEAYLVSLFEDTNLCAIHGKRVTIQPKDMQLARRLRGERS | 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... | P10651 |
O06291 | HTRA1_MYCTU | High-temperature requirement A protease | Mycobacterium tuberculosis complex | MDTRVDTDNAMPARFSAQIQNEDEVTSDQGNNGGPNGGGRLAPRPVFRPPVDPASRQAFGRPSGVQGSFVAERVRPQKYQDQSDFTPNDQLADPVLQEAFGRPFAGAESLQRHPIDAGALAAEKDGAGPDEPDDPWRDPAAAAALGTPALAAPAPHGALAGSGKLGVRDVLFGGKVSYLALGILVAIALVIGGIGGVIGRKTAEVVDAFTTSKVTLSTTGNAQEPAGRFTKVAAAVADSVVTIESVSDQEGMQGSGVIVDGRGYIVTNNHVISEAANNPSQFKTTVVFNDGKEVPANLVGRDPKTDLAVLKVDNVDNLTV... | Essential protein that may act as a regulatory protease that is conditionally activated upon appropriate environmental triggers. | O06291 |
Q9BR61 | ACBD6_HUMAN | Acyl-CoA-binding domain-containing protein 6 | Homo | MASSFLPAGAITGDSGGELSSGDDSGEVEFPHSPEIEETSCLAELFEKAAAHLQGLIQVASREQLLYLYARYKQVKVGNCNTPKPSFFDFEGKQKWEAWKALGDSSPSQAMQEYIAVVKKLDPGWNPQIPEKKGKEANTGFGGPVISSLYHEETIREEDKNIFDYCRENNIDHITKAIKSKNVDVNVKDEEGRALLHWACDRGHKELVTVLLQHRADINCQDNEGQTALHYASACEFLDIVELLLQSGADPTLRDQDGCLPEEVTGCKTVSLVLQRHTTGKA | Binds long-chain acyl-coenzyme A molecules with a strong preference for unsaturated C18:1-CoA, lower affinity for unsaturated C20:4-CoA, and very weak affinity for saturated C16:0-CoA. Does not bind fatty acids. | Q9BR61 |
A2SQV7 | PELO_METLZ | Protein pelota homolog | Methanocorpusculum | MKAELPEPLKKDGFGEYKLMPESIDDLWHLSHLISPGNTVYAVTLRTVDGPSDKLRSEKLEKRPVRIGVKCEKAEFVPESSRLRVFGVISYGPDMGQHHTLNIEAGYEISVVRQWRQIDLARLERAVSSSVHGVVHIAAIEDGEAELYRVRQYGPERITTLTVGSGKTAELDSRQALFAELLTFLEKVTGSIVIAGPGFVKEDFVKFAKTKAPEIAERMLIADTRRCGYGAVQEAIGNGVLTRVAEDLQLAKEVSFMDEVFLRIGQNGAVAYGKSEVRQAIDYGAAETILVADSFVKDGGIEKMIEGAERLGANVVVLST... | May function in recognizing stalled ribosomes, interact with stem-loop structures in stalled mRNA molecules, and effect endonucleolytic cleavage of the mRNA. May play a role in the release non-functional ribosomes and degradation of damaged mRNAs. Has endoribonuclease activity. | A2SQV7 |
Q2KD88 | MIAB_RHIEC | tRNA-i(6)A37 methylthiotransferase | Rhizobium | MTQDSALLKAPEQTLRDGSNSRKVFIKTYGCQMNVYDSTRMSDALARDGYEPTEDMEEADLVLLNTCHIREKAAEKVYSALGRLREMKKKKAADGREMMIGVAGCVAQAEGEEILRRAPAVDVVIGPQTYHRLPEALRRAKEGQRVVDTEYAIEDKFEHLPVAESRKIRARGVTAFLTVQEGCDKFCTFCVVPYTRGSEVSRPVSQIVEEAEKLVEGGVREITLLGQNVNAWHGAGPRGEAWSLGDLLYRLAEIPGLARLRYTTSHPRDMDDRLIAAHRDLRALMPYLHLPVQSGSDRILKAMNRRHTAAEYLSLIERIR... | 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. | Q2KD88 |
A1RPC2 | PCKA_SHESW | Phosphoenolpyruvate carboxykinase (ATP) | Shewanella | MADGLHRVHYNPSTAQLVEFALLRGEGELTANGALVAKTGARSGRSPGDRFIVKEPSSEADIEWGPVNQAFEPGAFEGLWARVEAYLADKELFVSDLEVGADTEHYQPVRVTTQYAWHQLFARNLFIIPEEFNRKDKPVWQIINAPDFVCDPARDGTNSDAAVILNFAERKVLLAGLKYAGEMKKSMFSVQNFLLPAQGVLPMHCSANVGKDGDTTLFFGLSGTGKTTLSADPKRFLIGDDEHGWAPGGVFNIEGGCYAKCIDLSQKNEPVIWDAIRFGTVLENVVMDEHRVPNYKDSSLTENTRAAYPLEHIAQRKEDN... | Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA. | A1RPC2 |
Q5EA49 | MIS12_BOVIN | Protein MIS12 homolog | Bos | MSVDPMTYEAQFFGFTPQTCMLRIYIAFQDYLFEVMQAVEQVILKKLDGIPDCAISPVEIRKCTEKFLCFMKGRFDNLFGKMEQLFLQLILRIPPNVLLPEDKSQETQSYSEEEFHFLQKEIEQLQEKYKTELCTKQALLAELEEQKIVQAKLKQTLSLFDELENVGRDHGASDFREGLVFLIQNSRKLQNIRENVEKEGKRLKIS | Part of the MIS12 complex, which may be fundamental for kinetochore formation and proper chromosome segregation during mitosis. Essential for proper kinetochore microtubule attachments. | Q5EA49 |
Q47JA7 | RS7_DECAR | 30S ribosomal protein S7 | Dechloromonas | MPRRREVPKRDILPDPKFGNVEVSKFVNAIMQSGKKSVAERIVYGAFDIITTKGGKDPLEVFSAAMSNVKPMVEVKSRRVGGANYQVPVEVRPARRAALAMRWLRESARKRSEKSMGQRLAAEMLEAAENRGGAVKKRDEVHRMAEANKAFAHFRF | 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. | Q47JA7 |
Q86WP2 | GPBP1_HUMAN | Vascular wall-linked protein | Homo | MAQHDFAPAWLNFPTPPSSTKSSLNFEKHSENFAWTENRYDVNRRRHNSSDGFDSAIGRPNGGNFGRKEKNGWRTHGRNGTENINHRGGYHGGSSRSRSSIFHAGKSQGLHENNIPDNETGRKEDKRERKQFEAEDFPSLNPEYEREPNHNKSLAAGVWEYPPNPKSRAPRMLVIKKGNTKDLQLSGFPVVGNLPSQPVKNGTGPSVYKGLVPKPAAPPTKPTQWKSQTKENKVGTSFPHESTFGVGNFNAFKSTAKNFSPSTNSVKECNRSNSSSPVDKLNQQPRLTKLTRMRTDKKSEFLKALKRDRVEEEHEDESRA... | Functions as a GC-rich promoter-specific transactivating transcription factor. | Q86WP2 |
P70325 | TBX4_MOUSE | T-box transcription factor TBX4 | Mus | MLQDKGLSESEEAFRAPGPALGEASNTSTTNAPEPALATPGLSGAALSSPPGQGADVAAAAAAAAEQTIENIKVGLHEKELWKKFHEAGTEMIITKAGRRMFPSYKVKVTGMNPKTKYILLIDIVPADDHRYKFCDNKWMVAGKAEPAMPGRLYVHPDSPATGAHWMRQLVSFQKLKLTNNHLDPFGHIILNSMHKYQPRLHIVKADENNAFGSKNTAFCTHVFPETSFISVTSYQNHKITQLKIENNPFAKGFRGSDDSDLRVARLQSKEYPVISKSIMRQRLVSSQLSAKPDVSPLHSAHQALQHYQYENGAHMQFAA... | Transcriptional regulator that has an essential role in the organogenesis of lungs, pelvis, and hindlimbs. | P70325 |
P53453 | DRD2L_TAKRU | D(2)-like dopamine receptor | Takifugu | MDVFTQYAYNDSIFDNGTWSANETTKDETHPYNYYAMLLTLLIFVIVFGNVLVCMAVSREKALQTTTNYLIVSLAVADLLVATLVMPWVVYLEVVGEWRFSKIHCDIFVTLDVMMCTASILNLCAISIDRYTAVAMPMLYNTRYSSRRRVTVMISVVWVLSFAISCPLLFGLNNTATRDQSLCFIANPAFVVYSSIVSFYVPFIVTLLVYVQIYVVLRKRRKRVNTKPKQRLCQAADPDIPTSLKDKCTHPEDVRLCTMIVKSNGSFPVNKKKVIFIKDGVNEVEGLELDELNYCGGSHKQPPPQQQPRALGDTPATSHQ... | Receptor for dopamine. | P53453 |
O59418 | RL3_PYRHO | 50S ribosomal protein L3 | Pyrococcus | MGKIHRPRKGSLAFSPRKRAKSIVPRIRSWPKETEVRMLGFAGYKAGMTHILMIDDEPGLTNGKEIFMPVTIIETPPLRVFGIRAYRQGYLGLETAGEVIVPDFELDNYTPSKKGKGRKFTFYQFLGRRIATLPKDYTQEEFEQKLGALEDMIKEGEIVEVRALVSTQPWVIKLKKKPEVMEYAIGGTSVEEKFNYIKEKLGKEIRVGEVLKEGELLDVIAVTKGKGTQGPVKRWGIKLRAHKDSKGRRKVGSIGPWHPARVMWTVPMAGQMGFHHRTELNKRLIAIGENGKLVIDGNEIEITPKGGFPHYGIVRGDFMM... | One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. | O59418 |
Q476H8 | COXX_CUPPJ | Heme O synthase | Cupriavidus | MVTATHSHPVGRVRHLARQYAALTKPRVTQLAVFCAIIGMFLATPGMVPWRVLIGGGAGIWLLAGAAFAINCLVEQKIDALMRRTAWRPSATGEITTTQTLIFSAVLGGAGMWLLHVFANDLTMWLTFATFLGYAVVYTILLKPATPQNIVIGGLSGAMPPALGWAAVANDVPAEAWFLVLIIFTWTPPHFWALALYRRADYAKSGLPMLPITHGEKYTLLNILLYTLVMIAATLLPFVYGMSGYIYLASALVLGAWFLKYSWTMYRNYSDQLAQRAFRFSILYLSLLFAALLIDHYFKFVPQI | Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. | Q476H8 |
Q1LQB1 | NTPPA_CUPMC | Nucleotide pyrophosphatase | Cupriavidus | MTSILYLASQSPRRRELLTQLGVTYELLLADAGEDAEALEAVRPGESPDDYVQRVCALKADAALQRRARRGLPDAPILTSDTTVCRGGDILGKPADARDAAAMLASLSGTTHRVLTAVTVATSAGQRHALSISHVTFRPILAPEIERYVASGEPLGKAGAYGIQGRAAEFVERIDGSYSGIMGLPLFETAALLREAGLHF | Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | Q1LQB1 |
Q51769 | MERT_PSEFL | Mercury ion transport protein | Pseudomonas | MSEPQNGRGALFTGGLAAILASACCLGPLVLIALGFSGAWIGNLTVLEPYRPIFIGVALVALFFAWRRIYRPSAACKPGEVCAIPQVPATYKLIFWGVAVLVLVALGFPYVVPFFY | Involved in mercury resistance. Probably transfers a mercuric ion from the periplasmic Hg(2+)-binding protein MerP to the cytoplasmic mercuric reductase MerA. | Q51769 |
Q4USQ0 | LPXD_XANC8 | UDP-3-O-acylglucosamine N-acyltransferase | Xanthomonas | MRLTASEIAAQFGLTVVGDGATEVSGVATLAHAGTGQLSFLANPRYRPQLAETQASVVILRADDAESAQGTALVAKDPYTAFAKIAALFDVAPVRAPGIHASAVIDPTATVSPTAHVGPFVSIGAGSRVGDGCVIGAGSIIGEDCVVDDGCELIARVTLVTRVRLGKRVRVHPGAVLGADGFGLAMDAGHWIKVPQLGGVVIGDDCEIGANTCIDRGALEDTVLEEDVRVDNLVQIAHNCRIGAHSAIAGCTGIAGSAKIGRYCLLGGHVGVVGHLEICDKVVITGKSVVRNSIHEPGEYSSGTPLTDNRTWRKNAARFK... | Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. | Q4USQ0 |
P00823 | ATPA_TOBAC | F-ATPase subunit alpha | Nicotiana | MVTIRADEISNIIRERIEQYNREVKIVNTGTVLQVGDGIARIHGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLLIQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISASEFRLIESAAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYLGDVFYLHSRLLERAAKLSSSLGEGSMTALPIV... | Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | P00823 |
A0RVY6 | RL5_CENSY | 50S ribosomal protein L5 | Cenarchaeum | MAGDMRKITLEKVVLNMGVGQSGNAVEVAKRALGEISGKKPCGRDAHETQRDFGVRKGEPIGAAVTIRGEDAGALARRLFEAKGGQVKGRSFDDFGNFSFGIGEHIDIPGIKYDPGIGILGLDVCMTLSRPGYGIRKRSKHKARVGRSHRITATEAKDFVVREFGVEIV | 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... | A0RVY6 |
A6T656 | MTNA_KLEP7 | S-methyl-5-thioribose-1-phosphate isomerase | Klebsiella | MQTLQTTSLRVSENQLFILDQQALPQETRWLAADNVALLVDHIHTLRVRGAPLIGLSASLLLALLAQRGLNRDALQQALETLRAARPTAVNLMNNLDRMKQALAREDYPQALEAEALRLVEEDKQLCARIAEAGSALVKPGSRLLTHCNTGGLATAGVGTALGVIALAHRQGKVTNVWVDETRPLLQGGRLTAWELGELGVPYQLIADSMAASLMAQGQVDAVWVGADRIAANGDVANKIGTYSLAVLAHYHQIPFYVAAPQTTLDRYCPNGAAIPIEQRAAAEVTGVAGSFGAVQWAPTGAAVYNPAFDVTPAGLISGW... | Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P). | A6T656 |
Q96EK5 | KBP_HUMAN | Kinesin family binding protein | Homo | MANVPWAEVCEKFQAALALSRVELHKNPEKEPYKSKYSARALLEEVKALLGPAPEDEDERPEAEDGPGAGDHALGLPAEVVEPEGPVAQRAVRLAVIEFHLGVNHIDTEELSAGEEHLVKCLRLLRRYRLSHDCISLCIQAQNNLGILWSEREEIETAQAYLESSEALYNQYMKEVGSPPLDPTERFLPEEEKLTEQERSKRFEKVYTHNLYYLAQVYQHLEMFEKAAHYCHSTLKRQLEHNAYHPIEWAINAATLSQFYINKLCFMEARHCLSAANVIFGQTGKISATEDTPEAEGEVPELYHQRKGEIARCWIKYCLT... | Required for organization of axonal microtubules, and axonal outgrowth and maintenance during peripheral and central nervous system development. | Q96EK5 |
B3E421 | DER_TRIL1 | GTP-binding protein EngA | Trichlorobacter | MKSIVAIVGRPNVGKSTLFNRIVGERRAIVDDMPGVTRDRNYAVVERYDKPFILVDTGGFEPVTEDRMLQQMREQSLLAMEEADVILFLMDAKQGLTPADNEVASMLRRVDKPVFYVVNKVDGEKVENEAAEFYALGIDNMHTISAAHNRGIRDLLDEIMALLPDEPLPGEDEVTNIAVVGRPNVGKSSLVNRLLGFERVVANPVAGTTRDSVDTFFTCNKKRYCLIDTAGIRRKGKTSQKLEKYSVVDALKSIERADVALIVLNAEDGITEQDKHIAGYVYEAGRACVFVVNKWDTLEKDNKTIGKFVEQIQYEFKFLA... | GTPase that plays an essential role in the late steps of ribosome biogenesis. | B3E421 |
P21154 | GLNA_METVO | Glutamine synthetase I alpha | Methanococcus | MTSLEMALEYIKINNVKFLRFQFVDIHGEPKNIAYPVKLGTADGEEELMGVLENGLFFDGSSIEGFVEIEDSDMVLKPDLSTLSVLPWRPSEKSVARIICDVYRKNGKPFEGDPRGCLKRVLAEFKEEFKGEYFVGPEPEFFILKNENGKWVPGDDAGYFELEPLDEGNDLRRNIVFALENLGFHVEASHHEVAPGQHEVDFKYDNAVKTADSVITFKTTIKTLAKQSGVLATFMPKPFFGMNGSGMHCNQSIWLDGKPSFYDENNAHQLSDICLSYIGGILEHTKALVSVTNPTVNSYKRLVPGYEAPVNIAWANSNRT... | Probably involved in nitrogen metabolism via ammonium assimilation. Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. | P21154 |
Q9KNR1 | TPIS_VIBCH | Triose-phosphate isomerase | Vibrio | MRRPVVMGNWKLNGSKAMVTDLLNGLNAELEGVEGVDVVVAPPAMYLDLAERLIKEGGNKLILGAQNTDTHNSGAYTGDMSPAMLKDFGASHIIIGHSERRDYHKESDEFVAKKFAFLKENGLTPVFCIGETEAQNEAGETEAVCARQINAVIDAYGVEALNGAIIAYEPIWAIGTGKAATADDAQRIHASIRALIAAKDAAVAEQVIIQYGGSVKPENAASYFAQPDIDGALVGGASLDAKGFAAIAKAAAEAKKA | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | Q9KNR1 |
B9MQG5 | RPOB_CALBD | Transcriptase subunit beta | Caldicellulosiruptor | MALPRPVQYGKVQRMSYGKVKEVLDLPYLLEIQKKSFQWFLDEGLREVLREISPIKDYSETLLLEFVDYYFDGPPKYSEQECKERDATYARPLKVKVRLINKETGEIKEQDIYMGEFPIMTETGTFIINGAERVIVSQLIRSPGCYFASSIDKQGRKIFSGTLIPNRGAWLEFETDASELLSVRLDRTRKVSLTTLLKAFGLYNQQLIFEKFGEDERLKASLEKEANKGELGNPVENALLEVYRRLRPGEPPNVENARNLLYSMFFDPRRYDLAKVGRYKFNKKLSLWKRIFNKRAAQDVVDPKTGEILVKEGELITREI... | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | B9MQG5 |
Q5WVC4 | FETP_LEGPL | Probable Fe(2+)-trafficking protein | Legionella | MSRTVFCCKLKQEAEGLEKQPFPGELGKKVFNEVSKQAWNMWLSHQTMLINEYRLNLIEARAREFLKEEMQKYFFGEGSDKPSGYKEIK | Could be a mediator in iron transactions between iron acquisition and iron-requiring processes, such as synthesis and/or repair of Fe-S clusters in biosynthetic enzymes. | Q5WVC4 |
Q08636 | NTPA_ENTHA | V-type sodium pump catalytic subunit A | Enterococcus | MQIGKIIKVSGPLVMAENMSEASIQDMCLVGDLGVIGEIIEMRQDVASIQVYEETSGIGPGEPVRSTGEALSVELGPGIISQMFDGIQRPLDTFMEVTQSNFLGRGVQLPALDHEKQWWFEATIEEGTEVSAGDIIGYVDETKIIQHKIMVPNGIKGTVQKIESGSFTIDDPICVIETEQGLKELTMMQKWPVRRGRPIKQKLNPDVPMITGQRVIDTFFPVTKGGAAAVPGPFGAGKTVVQHQIAKWSDVDLVVYVGCGERGNEMTDVVNEFPELIDPNTGESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDM... | Involved in ATP-driven sodium extrusion. | Q08636 |
Q1XDR7 | YCF4_NEOYE | Photosystem I assembly protein Ycf4 | Neopyropia | MKKTLSIHSVRKDLILGSRRLSNYWWATIIFIGALGFLLAGLSSYFQVDLLPFTNSTDLVFIPQGIVMTFYGSIGVFLSLFLWLTIIWNIGAGYNEFNKDKGIVKIFRLGFPGKNRKICLQFNIKEIKSIKIDIKEGLNPRREIYLCTKDKRVIPLTRVGQPLLLSEVEEQAAEIARFLDVVLEGA | Seems to be required for the assembly of the photosystem I complex. | Q1XDR7 |
Q493I2 | FMT_BLOPB | Methionyl-tRNA formyltransferase | Candidatus Blochmannia | MVHSKSLRIAFFGTTSFAAWHLHTLAHLSTHQIIAVFTQEIQISTCKSFLSLHKIAKKYNISLFQSRTLSISDIIYIIKKINVDLIVVVSYGLILPQEILNIPRLGCINVHGSLLPRWRGPAPIQRALEYGDSITGITIIQMDLGIDTGDILHIMPCKIFPKDTSCTLSNRLVNIGSAMLSQVLDQFILGTFTLIPQDSTYATYAHKLNKQEARINWNLSAIQLERCIRAFNPWPISFFQIKNDRIRVWDAEVSNQNINNYSSSTSILPGTILAAHPNGIYVVTGSGILILTMLQISGKKITSVRDLLNAYKEWFKPNSV... | 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. | Q493I2 |
Q85DA0 | NU4LM_GALSE | NADH dehydrogenase subunit 4L | Galago | MPSISTNIILAFTTALLGVLIYRSHLMSSLLCLEGMMLSMFILVSLTTLNLHFSLATVTPIILLVFAACEAAVGLALLVMVSNTYGMDYIQNLNLLQC | Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. | Q85DA0 |
Q94UZ9 | CYB_MICGU | Ubiquinol-cytochrome-c reductase complex cytochrome b subunit | Microtus | MTIMRKKHPLIKIINHSFIDLPAPSNISSWWNFGSLLGLCLIIQILTGLFLAMHYTPDTTTAFSSVTHICRDVNNGWLIRYMHANGASMFFICLFLHVGRGMYYGSYNMIETWNMGIILLFAVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFAFHFILPFIITALVLVHLLFLHETGSNNPIGLNSNADKIPFHPYYTIKDLLGAFILLMAFMILTLFFPDILGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALILSILILAIMPLLHTSKQQTLTFRPI... | Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is... | Q94UZ9 |
Q9LYN0 | PR1B1_ARATH | Prenylated Rab acceptor 6 | Arabidopsis | MATPPTLPVTNQQAVQSQPPINTPAFRTFFSRLSTSIRDGLSQRRPWTELIDRSSMARPESLTDALSRIRKNLAYFKVNYVAIVSLVLAFSLFSHPLSLLVLIGLLGGWMFLYLFRPSDQPLVVFGRTFSDRETLLALVLSTIVVVFMTSVGSLLTSALMIGVAIVCVHGAFVVPDDLFLDEQEPANAGLLSFLGGSATSAAAAVSGRV | May be involved in both secretory and endocytic intracellular trafficking in the endosomal/prevacuolar compartments. | Q9LYN0 |
C3MTQ6 | NCPP_SULIM | Nucleoside-triphosphate phosphatase | Sulfolobus | MVTIALGSRNPVKINATKEALDVLKLNWDLIGIEVDNGVDKQPFCDQTYVGARNRALNVIRVTNADIGLGIEGGVCNVYGKFIANAVVYVITKEGLENFAISSSFTLPSSMVSLILQGKELGEASDIIFKTNNSKTKEGAIGLLTNNVINRKMLYVQPIVLALYPIYNTMINNTPF | Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA/RNA precursor pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. | C3MTQ6 |
A8F2Q0 | RECA_RICM5 | Recombinase A | spotted fever group | MSNTDKERAIAAALAQIEKSYGKGSVMKLGQRPHVDIEAVSTGSLGLDIALGIGGIPKGRIIEIFGPESSGKTTLTLHLIAEAQKKGGTCAFIDAEHALDPAYAKKLGVNIDELIISQPDTGEQALEIADTLIRSGGIDMIIIDSVAALVPKSEIEGEMGDAQMASQARLMSQALRKLTASINRTNCITVFINQIRMKIGVMFGSPETTTGGNALKFYASVRIDIRRIGSIKDKEEVIGSQTKVKVVKNKVSPPFKTADFDIMYGSGISKEGEIIDLGVKLDIVEKSGSWFSYKNVRIGQGRENVKQYLKEHPQISNEIE... | Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage. | A8F2Q0 |
O65258 | BAM2_ARATH | Beta-amylase 9 | Arabidopsis | MAIRLNHSVIPVSVKLGAPTRVSARSSLPFSVGDWRGVSTFSGARPLVLAKVKLRAESTEEDRVPIDDDDDSTDQLVDEEIVHFEERDFAGTACVPVYVMLPLGVIDMNSEVVEPEELLDQLRTLKSVNVDGVMVDCWWGIVESHTPQVYNWSGYKKLFQMIRELGLKIQVVMSFHECGGNVGDDVHIQIPEWVREIGQSNPDIYFTDSAGRRNTECLTWGIDKQRVLRGRTALEVYFDYMRSFRVEFDEFFEEKIIPEIEVGLGPCGELRYPSYPAQFGWKYPGIGEFQCYDKYLMNSLKEAAEVRGHSFWGRGPDNTE... | Low beta-amylase activity. Interacts poorly with starch or other alpha-1,4-glucan. | O65258 |
A4T4S9 | RSMG_MYCGI | 16S rRNA 7-methylguanosine methyltransferase | Mycolicibacterium | MKHAEIPPPPDAAAEVFGPALGAARRYAEILAGAGVERGLLGPREVDRIWDRHILNCAVIGELVEAGERVADVGSGAGLPGIPLALARPDVHVVLIEPLLRRSDFLREAIEDVGIECSVVRGRAEDRSVREEVGPTDVVVSRAVASLDKLAKWSSPLLRPGGRMLAIKGERAAEEIEEHRRALAALGVSELKVERCGARFVDPPATVVVGFQATAPEKRPRSGRRQR | Specifically methylates the N7 position of guanine in position 518 of 16S rRNA. | A4T4S9 |
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