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 |
|---|---|---|---|---|---|---|
B2JF36 | RSGA_PARP8 | Small ribosomal subunit biogenesis GTPase RsgA | Paraburkholderia | MSGRSPKALRAATANDRAQDRVRGLVIAAHGRHYIVAPEDGSAILQCFPRGKRSEIAVGDQVLYEPTSADQGVIVEIGERRNLLYRSDQYKSKLFAANLDQLLIVLATEPHFSEDLLGRALVAAEENELKPLIVLNKIDVEAALPLARKRLQLYRGLGYTVLEVSIKGQPDAARATLEAHLNGHSTLLLGQSGMGKSTLVNLLIPDAEVATREISTALNSGRHTTTFTRLYPLPGSEGALIDSPGFQEFGLHHLTEGKLERAFPEFRPLLAECRFYNCHHLHEPGCAILEAVADGRIAKERHALYAQLVHEASQIVR | One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimula... | B2JF36 |
P40923 | YOX1_SCHPO | MBF complex negative regulatory component yox1 | Schizosaccharomyces | MSLSDSPSKSGNTGKDLISNNEAKNHEDEETHQKKRRRRTTDAEATLLEQYFLKTPKPSLIERQELSKKLKSSMTPRELQIWFQNKRQSLRRSNCLSRNRLEGTGENSLLRRKSTLTLCETSTGQAELFFQSWPLHSQSVVGEMIHHEQDDYNKENKQQKVVDTTKDISRGSNGNEDSAAHQELEECARSLVELQQQCNDH | Negative regulatory component of the MBF transcription factor complex involved in cell-cycle G1/S phase-specific gene expression and more particularly DNA replication checkpoint-dependent gene expression. | P40923 |
A9MDR7 | FLGH_BRUC2 | Basal body L-ring protein | Brucella | MNKAILAVAMVLLLAGCATKPEEIGRAPDLSPVAAHLGMQNNPQFNGYPARPGKASYSLWDQRSTNFFKDPRAATPGDVLTVIISINDRANLDNKTDRERVSKGIYGGGGSFATSSITGAAAGGDMDASINTHSDSKSKGKGTIERSEDIRLQIAAIVTDTLPNGNLIIRGSQEVRVNNELRVLNVAGVVRPRDISGNNTISYDKIAEARISYGGRGRLSEIQQPPYGQQILDQFSPF | Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. | A9MDR7 |
A5V649 | LIPB_RHIWR | Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase | Rhizorhabdus | MTVDDDIEWRVTPGLSPYAETVAEMEARAAAIRAGEARELIWLLEHPPLYTAGTSAEADELLLPDRFPVFRSGRGGRYTYHGPGQRVGYVLLDLDRRGRDVRCFVAAIENWVIATLGDFGIAGRSEPGRVGIWTGHGPDEAKIGAIGVRVRRWVSFHGFSLNVDPDLSHFSGIVPCGLGEFAVTSMARLGIPAEMAAVDAALRRHFPAMLAGLRCSTRSDKDS | Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | A5V649 |
A2C0W8 | SYP_PROM1 | Prolyl-tRNA synthetase | Prochlorococcus | MRVSRLMLNTLRDVPSEADIISHQLLVRGGYIKRITGGIYAYMPLLWKVLKKITSIVEEELSTKGCLQTLLPQLQPSEIWERSGRWKSYTQGEGIMFSLKDRQGKELGLGPTHEEVITQIISQTIHSYKQLPINIFQIQTKFRDEIRPRFGLMRSREFIMKDAYSFHANENDLQSTYSDMRNAYQNIFTKCGLDFVCVDADSGAIGGAASQEFMVTAESGEDLILISSDGKYGANQEKAVSIIEEGNLLEPNKPSIIKTPNQKTIDELCNYNDFHPSQIVKVLAYLATCDDNKKYPVLVSIRGDQEINDIKLSNKISQEL... | Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two addit... | A2C0W8 |
A5IBI8 | NADD_LEGPC | Nicotinate mononucleotide adenylyltransferase | Legionella | MHSIAIFGGTFDPVHNGHIKTSLAIQANFGFDSYYFLPCKSPAIKPPSFASSEQRVEMLKLALKPYPDFKIDTRELDRDTPSYMVYTLQSFRQEYTDSSLTLIIGYDGLLTLPQWYQWEKIISLANLLVINREEFFQQPVPKSVQTLLNQYRNDDKNILLNHHAGSICLYNAGHYDISSTKIREQLKQHKDVKNNLPDLVYDYIKKQGLYQ | Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). | A5IBI8 |
A7MX36 | BIOB_VIBC1 | Biotin synthase | Vibrio | MEVRHNWTHAEVRDLMEKPFMDLLFEAQLVHRQYQQTNYVQVSTLLSIKTGACPEDCKYCPQSARYTTDIEKERLMEVERVLDAAQKAKNAGSTRFCMGAAWKNPKERDMPHLTDMIKGVKGMGLETCMTLGMLTPDQAKQLATAGLDYYNHNLDTSPEFYGNIITTRTYQDRLDTLSHVRDAGMKICSGGIIGMGESANDRAGLLVELANLPVHPESVPINMLVKVKGTPLEEVDDVEPFDFIRLIAIARIMMPQSAVRLSAGRENMNEQMQALCFMAGANSVFYGCKLLTTPNPSEDKDMMLFNKLGINSQEVSQKPD... | Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism. | A7MX36 |
P22838 | DPO3B_PROMI | DNA polymerase III subunit beta | Proteus | MKFIIEREQLLKPLQQVSGPLGGRPTLPILGNLLLKVTENTLSLTGTDLEMEMMARVSLSQSHEIGATTVPARKFFDIWRGLPEGAEISVELDGDRLLVRSGRSRFSLSTLPASDFPNLDDWQSEVEFTLPQATLKRLIESTQFSMAHQDVRYYLNGMLFETENTELRTVATDGHRLAVCAMDIGQSLPGHSVIVPRKGVIELMRLLDGSGESLLQLQIGSNNLRAHVGDFIFTSKLVDGRFPDYRRVLPKNPTKTVIAGCDILKQAFSRAAILSNEKFRGVRINLTNGQLKITANNPEQEEAEEIVDVQYQGEEMEIGF... | Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalyti... | P22838 |
Q1XDL4 | YCF42_NEOYE | Thioredoxin peroxidase | Neopyropia | MISGPNCLRVGQLAPDFSATAVYDQEFKTLKLSDLKNKYIVLFFYPLDFTFVCPTEITAFSDKYNAFSELNTEVLGVSVDSEYSHLAWLQTDRESGGLGDLSYPLVSDLKKEISAAYNVLNSDGVALRGLFIIDPKGIIQYSTINNLEFGRSVEETLRVLQAIQYVQSHPDEVCPANWKPGDKTMNPDPIKSKNYFAAA | Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. | Q1XDL4 |
P63344 | FTSH_SALTI | ATP-dependent zinc metalloprotease FtsH | Salmonella | MAKNLILWLVIAVVLMSVFQSFGPSESNGRKVDYSTFLQEVNQDQVREARINGREINVTKKDSNRYTTYIPINDPKLLDNLLTKNVKVVGEPPEEPSLLASIFISWFPMLLLIGVWIFFMRQMQGGGGKGAMSFGKSKARMLTEDQIKTTFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVG... | 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. | P63344 |
A6LDS8 | MIAA2_PARD8 | Isopentenyl-diphosphate:tRNA isopentenyltransferase 2 | Parabacteroides | MNSLVILLGPTGVGKTELSLQVAERFGSPIISSDSRQLYKDLPIGTAAPTPEQMARVKHYMVGTLSLTDYYSASNFEEDVVSLLSELHKTIPTVVMTGGSMMYIDAVCKGIDDIPTVTPEIRDALYMQFETEGLAPILAELKEADPVHYEEVDRNNYKRVIHAVEICRMTGKPYSSFRTNIKKERPFRIIKVGLNRDRDELCDRINQRVDQMMSEGLLEEARRAYPFRHLNSLNTVGYKELFNYFSGEWTLDLAVEKIKRNSRVYARKQMTWFKRDPEITWFHPDETEAIFTHLSQQII | Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A). | A6LDS8 |
Q6G928 | AROK_STAAS | Shikimate kinase | Staphylococcus | MNHDKSPIILIGFMGTGKSTIGKYVADEQNLSFIDIDSYIEEKYKLTIPEIFSKHGEQYFRNLEFTCLQECINTADIIATGGGIIESEEAFNFLKNQKNIIWLDCNIDIIYSRINDDPHRPNANNKTIKQLNDLYCSRNLRYNEIAFKKFDSHLLSISEIYYELLNLIKASDQY | Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. | Q6G928 |
P43129 | FRE_PHOLU | NAD(P)H:flavin oxidoreductase | Photorhabdus | MTTLSCKVTSVEAITDTVYRVRLLPDSPFLFRAGQYLMVVMDERDKRPFSMASTPSEKEFIELHIGASELNLYAMAVMDRILDQKVINIDIPHGKAWFRKSSANPLLLIAGGTGFSYTRSILLTALEEQPKRHISMYWGGRESQHLYDLAELRLLTERYPNLKVIPVVEQSDNGWCGRTGTVLKAVLEDFGSLANYDIYIAGRFEMAKIARERFCSERDASADSMYGDAFEFI | Involved in bioluminescence. It is a good supplier of reduced flavin mononucleotide (FMNH2) to the bioluminescence reaction. Preferably uses riboflavin as an electron acceptor when NADPH is used as an electron donor. | P43129 |
B0RZU7 | RL16_FINM2 | 50S ribosomal protein L16 | Finegoldia | MLMPKRVKYRRVHRGRMKGKALKGNTLTYGDYGIQALGSCWLTANQIEAARRAMTRYIKRGGNIWIKVFPDKPVSKKPIGIRMGSGKGAPEYWVAVIKPGRVLFEMAGVPEDVAREAMRLAQHKLPIKTKFIAREEFGEKDGEADEN | Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs. | B0RZU7 |
A6V8R6 | RND_PSEA7 | Ribonuclease D | Pseudomonas | MFVTAPEIQWIRDDASLAQQCREWRTQPYLALDTEFMRVDTFYPAAGLVQVGDGRREWLIDPLLVRDWGPFAELLEDPRVVKVLHACSEDLEVFLRLTGSLPVPLFDTQLAAAYLGMAHSMGYSKLVKEVLDIDLPKDETRSDWLQRPLTEMQMRYAADDVQHLAQVYLALDARLSEEKRAWLLEDGAELVANLCRESDPREAYREVKLGWRLRPQQLAVLRELCAWREEQARLRNRPRNHVLRERTLWPLARLLPKNKTDLAAIEDMHPRTVRQDGDFLIELIAEAARLPQSEWPEALPEPLPPEVTPLLKSLRAIGQR... | Exonuclease involved in the 3' processing of various precursor tRNAs. Initiates hydrolysis at the 3'-terminus of an RNA molecule and releases 5'-mononucleotides. | A6V8R6 |
Q8D234 | RL7_WIGBR | 50S ribosomal protein L7/L12 | Wigglesworthia | MSINKQQILDAVSEMSVLEISELVSMMEKKFGVSSINNNNINVNKVDESVEEKSEFDVLLLEIGKNKISVIKSVRSALSLGLKESKDLIESELPITLKTGLNKKDAESLKKEIETSGARIELK | Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation. | Q8D234 |
A0A0P0X004 | HMA9_ORYSJ | Protein HEAVY METAL ATPASE 5 | Oryza sativa | MAHLQLSAVAGGGRPAAAGGGGDEMEDVRLLDSYDEEMGGGAAAAAAGEEEEAHVRVTGMTCSACTSAVEGAVSARRGVRRVAVSLLQNRAHVVFDPALLKVEDIIEAIEDAGFDAEIIPDTAISQPKAQKTLSAQFRIGGMTCANCVNSVEGILKRLSGVKGAVVALATSLGEVEYDPSVINKDEIVEAIEDAGFEAAFLQSSEQDKILLGLTGLHTERDVNVLHDILKKMIGLRQFDVNATVSEVEIIFDPEAVGLRSIVDAIETGSNGRLKAHVQNPYARGASNDAHEAAKMLHLLRSSLFLSIPVFFIRMVCPHIP... | Metal efflux transporter that may play a role in detoxification of heavy metals, such as zinc, copper, lead and cadmium, especially in the shoots. | A0A0P0X004 |
Q9JXF1 | BICOA_NEIMB | Pantothenic acid kinase | Neisseria | MTVLKLSHWRVLAELADGLPQHVSQLARMADMKPQQLNGFWQQMPAHIRGLLRQHDGYWRLVRPLAVFDAEGLRELGERSGFQTALKHECASSNDEILELARIAPDKAHKTICVTHLQSKGRGRQGRKWSHRLGECLMFSFGWVFDRPQYELGSLSPVAAVACRRALSRLGLDVQIKWPNDLVVGRDKLGGILIETVRTGGKTVAVVGIGINFVLPKEVENAASVQSLFQTASRRGNADAAVLLETLLVELDAVLLQYARDGFAPFVAEYQAANRDHGKAVLLLRDGETVFEGTVKGVDGQGVLHLETAEGKQTVVSGEI... | Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. | Q9JXF1 |
B8E690 | DAPF_SHEB2 | PLP-independent amino acid racemase | Shewanella | MIQFTKMHGLGNDFMVVDGVTQNVFFSPEQIRRLADRNFGIGFDQLLLVEPPYDPDLDFHYRIFNADGTEVEQCGNGARCFARFVRNKGLTNKSKIRVSTSSGKMTLRLERDGTVTVNMGVPILEPSQIPFKAKKPEKTYLLQTPMQTFLCGAASMGNPHCVLDVEDVASASVAEIGAMLTKHERFPRGVNVGFMQVVDSGHIKLRVYERGAAETLACGTGACAAVVVGQVQGKLGQQVRVDLPGGTLTINWEGEGKPLWMTGPAQHVYDGQIQL | Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan. | B8E690 |
P57979 | UVRA_PASMU | Excinuclease ABC subunit A | Pasteurella | MDKIEVRGARTHNLKNINLTIPRDKLIVITGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLSPAISIEQKSTSHNPRSTVGTVTEIHDYLRLLFARVGEPRCPNHDVPLAAQTISQMVDKVLSLPEESKMMLLAPVVKERKGEHVKLLEQIAAQGYIRARIDGEICDLSDAPKLELHKKHTIEVVVDRFKVRSDLATRLAESFETALELSGGTAVVASMDEPETEELVFSANFACPHCGYSVPELEPRLFSFNNPAGACPTCDGLGVQQYFDEKRVVQNPSISLASGAVKGWDRRNFYYYQM... | The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate. | P57979 |
B2JHD4 | RPPH_PARP8 | (Di)nucleoside polyphosphate hydrolase | Paraburkholderia | MLDREGFRPNVGIILLNAHNEVFWGKRLREHSWQFPQGGIKYGETPVQAMYRELHEETGLLPEHVKVIGRTRDWLRYEVPDKFIKREVRGHYRGQKQIWFLLRMVGRDCDICLRATDHPEFDAWRWNEYWVPLDCVIEFKRDVYQLALTELSRFLRRPQPRTERPGGHHHGQRYPRMASSVNAPPGASMASSMTVTTVTTAIAVESTLRATIESDCSSTEDPAVQAPGLRD | Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage. | B2JHD4 |
Q31MN3 | KATG_SYNE7 | Peroxidase/catalase | Synechococcus | MTATQGKCPVMHGGATTVNISTAEWWPKALNLDILSQHDRKTNPMGPDFNYQEEVKKLDVAALKQDLQALMTDSQDWWPADWGHYGGLMIRLTWHAAGTYRIADGRGGAGTGNQRFAPLNSWPDNTNLDKARRLLWPIKQKYGNKLSWADLIAYAGTIAYESMGLKTFGFAFGREDIWHPEKDIYWGPEKEWVPPSTNPNSRYTGDRELENPLAAVTMGLIYVNPEGVDGNPDPLKTAHDVRVTFARMAMNDEETVALTAGGHTVGKCHGNGNAALLGPEPEGADVEDQGLGWINKTQSGIGRNAVTSGLEGAWTPHPTQ... | Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. | Q31MN3 |
Q58DR6 | EMP3_BOVIN | Epithelial membrane protein 3 | Bos | MSLLLLVVSALHILILILLFVATLDKSWWTLPGKESLNLWYDCTWNSDNKTWACSNVSENGWLKAVQVLMVLSLILCCLSFILFMFQLYTMRRGGLFYATGFCQLCTSVAVFTGALIYAIHAEEILADRPSGGSFGYCFALAWVAFPLALASGIIYIHLRKRE | Probably involved in cell proliferation and cell-cell interactions. | Q58DR6 |
Q9P291 | ARMX1_HUMAN | ARM protein lost in epithelial cancers on chromosome X 1 | Homo | MGRTREAGCVAAGVVIGAGACYCVYRLAWGRDENEKIWDEDEESTDTSEIGVETVKGAKTNAGAGSGAKLQGDSEVKPEVSLGLEDCPGVKEKAHSGSHSGGGLEAKAKALFNTLKEQASAKAGKGARVGTISGNRTLAPSLPCPGGRGGGCHPTRSGSRAGGRASGKSKGKARSKSTRAPATTWPVRRGKFNFPYKIDDILSAPDLQKVLNILERTNDPFIQEVALVTLGNNAAYSFNQNAIRELGGVPIIAKLIKTKDPIIREKTYNALNNLSVNAENQGKIKTYISQVCDDTMVCRLDSAVQMAGLRLLTNMTVTNH... | Regulates mitochondrial transport during axon regeneration. Increases the proportion of motile mitochondria by recruiting stationary mitochondria into the motile pool. Enhances mitochondria movement and neurite growth in both adult axons and embryonic neurons. Promotes neuronal survival and axon regeneration after nerv... | Q9P291 |
Q1QXW0 | RMF_CHRSD | Ribosome modulation factor | Chromohalobacter | MKRQKRDRFQRAYVHGYKAGMTGRSRDDCPSQDINLREYWMSGWREGRGDQWAGMTGISGIHKNPMVLS | During stationary phase, converts 70S ribosomes to an inactive dimeric form (100S ribosomes). | Q1QXW0 |
Q870I4 | MTL32_CANGA | MTL3alpha2 protein | Nakaseomyces/Candida clade | MSKKSRISITHLLNPIQEENLKEKLQEINNQLISLCSSLPKRQSLPGPSSDILRFLSRNNLDPQEIGLIKTTYRLSTLLSKLREHEIVFNVVTKDHLLKKGVPNHYAASYRGHRFTRENVQILETWYRNHIDNPYLDHNSQQYLAQKTNLSKIQIKNWVANRRRKQKSIYISLFDIHNIESGEYAYIEKVCYIIIIICHLFLVFSLSCLT | Mating type proteins are sequence specific DNA-binding proteins that act as master switches in yeast differentiation by controlling gene expression in a cell type-specific fashion. | Q870I4 |
Q474Y3 | PANC_CUPPJ | Pantoate-activating enzyme | Cupriavidus | MKVISSIQELRDQLRGQNRVAFVPTMGNLHEGHLSLMRLARQHGDPVVASIFVNRLQFGPNEDFDKYPRTLQDDIEKLQSEGVYVLFAPTERDMYPEPQEYRVDPPHDLGDILEGEFRPGFFKGVCTVVMKLFTAAQPRVAVFGKKDYQQLMIVRRMVHQFALPIEIVPAETVRAEDGLALSSRNRYLTEAERAEAPMLYRTLHDVRDTVLGSDRAATRLATVEADACATLAQRGWKPDYVSIRKRSNLQAPTPEEFAAGEPLVVLTAAKLGATRLIDNLEI | Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. | Q474Y3 |
Q5JDG6 | CUTA_THEKO | Divalent-cation tolerance protein CutA | Thermococcus | MEAIIVYTTFPDWESARKVTRELLERKLIVCANLREHEAMYWWEGKIEEGKEVGAIYKTEVSKWKELRETIKELHPYDVPMIARIDLDKLNREYSEWMARVLFG | Involved in resistance toward heavy metals. | Q5JDG6 |
P0DMY4 | BDSA_ANEVI | Blood depressing substance 10 | Anemonia | MNKALFLCLVVLCAAVVFAAEDLQKAKHAPFKRGAQVCFCPGKVDRGDLWILRGDCPGGYGYTSNCYTWPNICCYPQSFSGR | Blocks Kv3 voltage-gated potassium channels. Reduces blood pressure. | P0DMY4 |
A9BWI1 | KAD_DELAS | Adenylate monophosphate kinase | Delftia | MKLILLGAPGAGKGTQAAFICQKYGIPQISTGDMLRAAVKAGTPLGQQAKAVMDAGQLVSDDLIINLVKERIAQADCANGFLFDGFPRTIPQADAMKAAGVKLDYVLEIDVPFDAIIERMSGRRSHPASGRTYHVKFNPPKVEGQDDVTGEPLVQREDDKEETVKKRLDVYSSQTRPLVDYYRAWAEKEAAAAPKYRAISGLGSVEDITQRALAALAE | Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. | A9BWI1 |
B7N145 | BIOH_ECO81 | Carboxylesterase BioH | Escherichia | MNNIWWHTKGQGNVHLVLLHGWGLNAGVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSLADMAEVVLRQAPDKAIWLGWSLGGLVASQIALTHPERVQALVTVASSPCFSARDEWPGIKPDVLAGFQQQLSDDFQRTVERFLALQTMGTETARQDARALKKTVLALPMPEVDVLNGGLEILKTVDLRQPLQNVPMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAPFISHPDEFCHLLVALKQRV | The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters. | B7N145 |
E1WAC4 | SICP_SALTS | Chaperone protein SicP | Salmonella | MGLPLTFDDNNQCLLLLDSDIFTSIEAKDDIWLLNGMIIPLSPVCGDSIWRQIMVINGELAANNEGTLAYIDAAETLLLIHAITDLTNTYHIISQLESFVNQQEALKNILQEYAKV | Molecular chaperone required for SptP stabilization and secretion. | E1WAC4 |
Q8TV03 | RL7A_METKA | Ribosomal protein L8e | Methanopyrus | MSKPMYVKFEVPEELAEKAYEALEIARDTGRIRKGTNETTKAVEREEAVLVLIAEDVDPEEVVAHLPELCDEKGIPYVYVPSKDELGAAAGIDVAAASACIIDPGDAKDLVDEIIEKVEELRE | Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, the RNA component of RNase P, box H/ACA, box C/D and box C'/D' sRNAs. | Q8TV03 |
Q6K7E6 | ERF1_ORYSJ | Ethylene-responsive element-binding factor 1 | Oryza sativa | MCGGAIIHHLKGHPEGSRRATEGLLWPEKKKPRWGGGGRRHFGGFVEEDDEDFEADFEEFEVDSGDSDLELGEEDDDDVVEIKPAAFKRALSRDNLSTITTAGFDGPAAKSAKRKRKNQFRGIRQRPWGKWAAEIRDPRKGVRVWLGTFNSAEEAARAYDAEARRIRGKKAKVNFPEAPTTAQKRRAGSTTAKAPKSSVEQKPTVKPAFNNLANANAFVYPSANFTSNKPFVQPDNMPFVPAMNSAAPIEDPIINSDQGSNSFGCSDFGWENDTKTPDITSIAPISTIAEVDESAFIKSSTNPMVPPVMENSAVDLPDLE... | Probable transcriptional activator that may be involved in defense signaling pathway. Binds in vitro to the DNA sequence 5'-AGCCGCC-3' of the GCC-box element found in pathogenesis-related (PR) gene promoters. The transcriptional activation is enhanced in vitro by the presence of MPK12/BWMK1. | Q6K7E6 |
Q2VB19 | PUM1_CHICK | Pumilio homolog 1 | Gallus | MSVACVLKRKAVLWQDSFSPHLKQHAQDTANPNMPVVLTSGTGSQAQPQPAANQALAAGTHSSPVPGSIGVAGRSQDDAMVDYFFQRQHGEQLGGGGSGGGGYNNSKHRWPTGDNIHAEHQVRSMDELNHDFQALALEGRAMGEQLLPGKKFWESDDSSKDGPKGIFLGDQWRDSAWGTSDHSVSQPIMVQRRPGQGFHVNSEVNSVLSPRSESGGLGVSMVEYVLSSSPGDSCLRKGGFGPRDAENDENDKGDKKNKGTFDGDKLGDLKEEGDVMDKTNGLPVQNGIDTDVKDFSRTPGNCQNSASEVDLLGPNQNGSE... | Sequence-specific RNA-binding protein that acts as a post-transcriptional repressor by binding the 3'-UTR of mRNA targets. Binds to an RNA consensus sequence, the Pumilio Response Element (PRE), 5'-UGUANAUA-3', that is related to the Nanos Response Element (NRE). Mediates post-transcriptional repression of transcripts ... | Q2VB19 |
P62942 | FKB1A_HUMAN | Rotamase | Homo | MGVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFDVELLKLE | Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruits SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate th... | P62942 |
Q04208 | LPT_SERMA | thr operon attenuator | Serratia | MRNISLTTTIITTTDTTGNGAG | This protein is involved in control of the biosynthesis of threonine. | Q04208 |
A0A1U8QYW8 | ALNF_EMENI | Asperlin biosynthesis cluster protein F | Aspergillus subgen. Nidulantes | MADYVIQNLTSNLQAMQYAYSSREEMPVWATKLLTPIFMAVAVLTTLPPPGPLRVIVGLTAFTSLWLHVLTHWVSGPAFFMDAIFMISITVRWLLMFVAGTPEIDYHQTTQSGTTITHKGTKDSSTLRQGLTKLRWSVELWSCWRGQGWNFVDQHLPRGAERTQSRWEFLVSNAGRVLLNQYISDLVRKYAFCALWPAQVDAHVDFSSLPLLNRHGLVALQLIRDSLMLDSEYRKASILFVGLHLSTPDRWPSLFGNMRDLYTVRNFWGRVWHQIFRQIFTRCGDIVANALNAQKGTLLYKYSRLYVGFLVSGVQHYACA... | Acetyltransferase; part of the gene cluster that mediates the biosynthesis of asperlin, a polyketide showing anti-inflammatory, antitumor and antibiotic activities . The first step of the asperlin biosynthesis is the production of the intermediate 2,4,6-octatrienoic acid by the highly redusing polyketide synthase alnA ... | A0A1U8QYW8 |
Q03QY7 | ATPG_LEVBA | F-ATPase gamma subunit | Levilactobacillus | MAESIHDVQRRINSTKATRQITSAMHMVSTAKLNKIQKQAVGYQDYVSKVKAVVMHLSQSHLLDNSSSSLQSNRPVKKTAYLVITSDRGMVGSYNSSVLRDTNAFIKERTPNPDDYMVLAVGGTGADFYKHRGVNVAYEYRGVSDVPEFNEVREIVKTVTTMFNNEVFDELFVCYNHFVNRISSRFRAEKMLPVDKETMSTDAAKDTQAAPLTAEYDTEPSEEEVLQVVLPQYAESLVYGAILDAKTAEHASSTNAMQSATDNADDLIATLQLHYNRARQAAITTEITEITGGQEALNN | 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. | Q03QY7 |
Q8LBM2 | TIF5A_ARATH | Jasmonate ZIM domain-containing protein 8 | Arabidopsis | MKLQQNCDLELRLFPTSYDSDSSDTTSVVESTSSGNPQPNEESQRITIFYNGKMCFSSDVTHLQARSIISIASREMKTKSSSNGSDPPNKSTSFHHNQLPNPKASMKKSLQSFLQKRKIRIQATSPYHSRR | Repressor of jasmonate responses. Unable to associate strongly with COI1 in the presence of jasmonoyl-isoleucine (JA-Ile) and is therefore more resistant to JA-mediated-degradation than other TIFY/JAZ proteins. Repress gene expression through direct recruitment of the corepressor TOPLESS to cognate transcription factor... | Q8LBM2 |
Q2YYM5 | ECFA2_STAAB | Energy-coupling factor transporter ATP-binding protein EcfA2 | Staphylococcus | MTIRFDNVSYTYQKGTPYQHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQFPESQLFEDTVEREMIFGPKNFKMNLDEAKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVVDEPTAGLDPQSKRQVMRLLKSLQTDENKAIILISHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKEKLADWHIALPEIVQLQYDFEQKHQTKLKDIALTEEAFVSLYKEWQHEK | ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. | Q2YYM5 |
Q9I596 | NCASE_PSEAE | N-acylsphingosine amidohydrolase | Pseudomonas | MSRSAFTALLLSCVLLALSMPARADDLPYRFGLGKADITGEAAEVGMMGYSSLEQKTAGIHMRQWARAFVIEEAASGRRLVYVNTDLGMIFQAVHLKVLARLKAKYPGVYDENNVMLAATHTHSGPGGFSHYAMYNLSVLGFQEKTFNAIVDGIVRSIERAQARLQPGRLFYGSGELRNANRNRSLLSHLKNPDIVGYEDGIDPQMSVLSFVDANGELAGAISWFPVHSTSMTNANHLISPDNKGYASYHWEHDVSRKSGFVAAFAQTNAGNLSPNLNLKPGSGPFDNEFDNTREIGLRQFAKAYEIAGQAQEEVLGELD... | Catalyzes the cleavage of the N-acyl linkage of the ceramides (Cers) to yield sphingosine (Sph) and free fatty acid at an optimal pH of 8-9. Also catalyzes the synthesis of Cers from Sph and fatty acid. | Q9I596 |
P57666 | ORN_STRCO | Oligoribonuclease | Streptomyces albidoflavus group | MNDRMVWIDCEMTGLSLSDDALIEVAALVTDSELNILGEGVDIVIRPPERALETMPEVVREMHTASGLLAELDGGTTLADAEAQVLAYVREHVKEPGKAPLCGNSVGTDRGFLLRDMATLEGYLHYRIVDVSSIKELARRWYPRAYFNSPEKNGNHRALADIRESIAELRYYREAVFVPQPGPDSDTARAIAAKHVVSAG | 3'-to-5' exoribonuclease specific for small oligoribonucleotides. | P57666 |
Q9PQK9 | DBH_UREPA | DNA-binding protein HU | Ureaplasma | MNAKIKAKTRSQMIDELSKMLNIEKKQTKAFMDTYEAFLILELSRAKEVRLGNIGKFKVSVRAERKGINPKTGETVIIPEKTIPKFTFTKGIKEIINAGISIDNERVSIDDNDFDDDDEFVEEYIVSENN | Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions. | Q9PQK9 |
B7V3X6 | METXS_PSEA8 | Homoserine transsuccinylase | Pseudomonas | MPTVFPDDSVGLVSPQTLHFNEPLELTSGKSLAEYDLVIETYGELNATQSNAVLICHALSGHHHAAGYHSVDERKPGWWDSCIGPGKPIDTRKFFVVALNNLGGCNGSSGPASINPATGKVYGADFPMVTVEDWVHSQARLADRLGIRQWAAVVGGSLGGMQALQWTISYPERVRHCLCIASAPKLSAQNIAFNEVARQATLSDPEFLGGYFQEQGVIPKRGLKLARMVGHITYLSDDAMGAKFGRVLKTEKLNYDLHSVEFQVESYLRYQGEEFSTRFDANTYLLMTKALDYFDPAAAHGDDLVRTLEGVEADFCLMSF... | Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine. | B7V3X6 |
A1BDZ0 | QUEF_CHLPD | PreQ(0) reductase | Chlorobium | MKKEILEVFDNTFPGRDYTIEIVNPEFTSVCPITALPDFGTIIIRYIPDKSCVELKSLKYYFLEFRNAGIFYENITNTILDDLTSVLQPREMTVITQWKARGGITETVSVTWPQKQ | Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1). | A1BDZ0 |
P50383 | TRPB1_SACS2 | Tryptophan synthase beta chain 1 | Saccharolobus | MVKEDEILPKYWYNIIPDLPKPLPPPRDPQGAYFSRIDLLRSILPKEVLRQQFTIERYIKIPEEVRDRYLSIGRPTPLFRAKRLEEYLKTPARIYFKYEGATPTGSHKINTAIPQAYFAKEEGIEHVVTETGAGQWGTAVALAASMYNMKSTIFMVKVSYEQKPMRRSIMQLYGANVYASPTNLTEYGRKILETNPQHPGSLGIAMSEAIEYALKNEFRYLVGSVLDVVLLHQSVIGQETITQLDLLGEDADILIGCVGGGSNFGGFTYPFIGNKKGKRYIAVSSAEIPKFSKGEYKYDFPDSAGLLPLVKMITLGKDYV... | The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. | P50383 |
A9B689 | ARAA_HERA2 | L-arabinose isomerase | Herpetosiphon | MLDLKQYEVWFITGSQHLYGPETLEQVAKHSQIIAAGLDQSSTIPVRVVFKPVLKTPDEIYNLVLEANAAKNCIGLVAWMHTFSPAKMWIAGLRSLQKPLAHLHTQFNSEIPWSEIDMDFMNLNQAAHGDREFGFIVSRMRLERKVIVGHWQDSEVHDRIAAWTRAAAAWHDAQGARFARFGDNMREVAVTEGDKVNAQMRLGYSVSGYGVGDLVRFVNEVSDADIDSTLQEYAEQYELAAGLQAGGEQHHSLREAARIELGLRYFLEHGNFKGFTTTFEDLHGLVQLPGLGPQRLMDRGYGFAGEGDWKTAALVRAMKV... | Catalyzes the conversion of L-arabinose to L-ribulose. | A9B689 |
B6JFC5 | COAD_AFIC5 | Pantetheine-phosphate adenylyltransferase | Afipia | MAHVALYPGSFDPVTNGHVDVVRQACTLVDRLIVAIGVHPGKAPLFSVDERRAMIVEVFSPLAATTGCAIECVTFDNLTVAAAEKSGATILIRGLRDGTDLDYEMQIAGMNQTLVPSVQTIFIPASPTVRPITATLVRQIASMGGDVSAFVPKAVAARLKAKFSQ | Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. | B6JFC5 |
B1YKA0 | FPG_EXIS2 | DNA-(apurinic or apyrimidinic site) lyase MutM | Exiguobacterium | MPELPEVETVRRSLERTVSGKTISSVKVFHPKMIRGMEVAPFVDALKQERIERVERRGKFLLFTFDRFYLVSHLRMEGKYFPYPQAIEKDKHTHVIFRFTDGSELHYNDVRKFGTMELREKETAMSVPPLAQLEREPFDPTFTAEVLAENLIRKKRSPIKTSLLDQSIFLGLGNIYVDETLFAARVHPLTKAGALTLDDISRIHAAGVDVLAKAVESGGSTIRSYVSPTGKGEFQLQLAVYGQTGAPCPRCGTAIEKIKVGGRGTHFCPTCQQVAL | 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. ... | B1YKA0 |
A0A1B4XBH9 | SDNS_SORAA | Sordarin/hypoxysordarin biosynthesis cluster protein S | Sordaria | MTEQAQREAELKRRKVRKGTHSCWECRRRKIRCQFGAGNDTVCLPCQARGSTCRSQEYVDKDARPSQQPDRRMAQRLGRLEELMARLVDRILPEAGGQLANRSTTQSNRGSRSPSPDSAQNEGLAFHQTLDVLEASLGPNTPAGLLLGLRDAAQPASMLTPESDHSPAPSKLTPSRNSKTSRSLYALFPPQEALPVLMKANAGPYYLTSLFSSFRDLIEGKVETANSVTVIPPAVSHPTVLARRLLQICICMQQLNPGYDTSPLQIKGTIPEYMNNVVTTVTNLVTSIDEIVSTGEGLESLVLLGLWHANAGNLRKAWLT... | Transcription factor; part of the gene cluster that mediates the biosynthesis of sordarin and hypoxysordarin, glycoside antibiotics with a unique tetracyclic diterpene aglycone structure . First, the geranylgeranyl diphosphate synthase sdnC constructs GGDP from farnesyl diphosphate and isopentenyl diphosphate . The dit... | A0A1B4XBH9 |
C3P4F6 | QUEC_BACAA | Queuosine biosynthesis protein QueC | Bacillus cereus group | MKKEKAVVVFSGGQDSTTCLFWAIEQFAEVEAVTFNYNQRHKLEIDCAVEIAKELGIKHTVLDMSLLNQLAPNALTRTDMEITHEEGELPSTFVDGRNLLFLSFAAVLAKQVGARHIVTGVCETDFSGYPDCRDVFVKSLNVTLNLSMDYPFVIHTPLMWIDKAETWKLSDELGAFEFVREKTLTCYNGIIGDGCGECPACQLRKAGLDTYLQEREGASN | Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). | C3P4F6 |
A5IFJ6 | ATP6_LEGPC | F-ATPase subunit 6 | Legionella | MGEEGFLAHFAFSIGGLPITQSVLTTWFIMISLFIMAWSTTYKCSLLQPSTYQLLWEGVLSTMYDAIKEVLPDHVELIFPFVATLWIFILVSNLIGVIPGFYSPTADLSVTASLAMMTFLSVHWFGIRAEGWREYLKHYIKPTPFLLPFHLISEISRTLALAVRLFGNIMSLQLTALIVLMIAGFLVPIPILILHIIEAIIQAYIFGMLALIYIAGGIQAHELKSQGESL | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | A5IFJ6 |
A2BQ25 | CHLB_PROMS | Light-independent protochlorophyllide reductase subunit B | Prochlorococcus | MELTLWTYEGPPHVGAMRIASSMKDIHYVLHAPQGDTYADLLFTMIERRGQRPPVTYTTFQARDLGGDTAELVKKNIKEAVERFKPKTLLVGESCTAELIQDQPGALAKGMGFDMPIVNLELPAYSKKENWGASETFYQLTRTLLKEKVSSSEKISPLRWKELGRRPKVNILGPSLLGFRCRDDVIEIQRILSEQGIDTNVVAPLGASPDDIERLIDAEINICLYPEIAEASCEWLKRNFGMEYTNTIPIGIKNTIEFINEVHKKLDLPLTNKEELENKSKLPWYSKSVDSNYLTGKRVFIFGDGTHAIAAAKIAKEELG... | 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. | A2BQ25 |
Q44840 | PTGA_BORBU | Glucose-specific phosphotransferase enzyme IIA component | Borreliella | MGFLDFFKKTATLDLIAPISGKVMSIDKVPDEAFAEKIVGDGIAILPTSNELLAPCDGKIGKIFKTNHAFSLETKEGVEIFVHFGINTLNLNGKGFTRVAEEGINVKQGEVIIRLDLEYLKEHSESVITPVVIANSDEVSSIEYSFGRLENDSEYILSSSTVLTEEIRHKISQTKPVIAGKDLVLRVKK | 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 PtsG and Crr is involved in glucose t... | Q44840 |
Q1GCH8 | UBIG_RUEST | 3-demethylubiquinone 3-O-methyltransferase | unclassified Ruegeria | MQAQQSTVDPSEIAKFEAMAAEWWDPNGKFKPLHMLNPCRLDYITSQIAGEFDRDLKTDAPFAGLRILDIGCGGGLLSEPMARLGAEVVGADAAEGNLPVARIHAEQSGLEIDYRHTTAEAMAEAGEQFDVVLNMEVVEHVADPLSYLTATQQLLKSGGLQICSTINRNPKSYAMAIFGAEVVMRWLPRGTHEWSKFITPDELFALLEQAGLNPVDRKGFVFNPILWKWSISDRDLSVNYVTASTKS | O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. | Q1GCH8 |
Q6QJE2 | SULP2_CHLRE | Sulfate permease 2, chloroplastic | Chlamydomonas | MASTTLLQPALGLPSRVGPRSPLSLPKIPRVCTHTSAPSTSKYCDSSSVIESTLGRQTSVAGRPWLAPRPAPQQSRGDLLVSKSGAAGGMGAHGGGLGEPVDNWIKKLLVGVAAAYIGLVVLVPFLNVFVQAFAKGIIPFLEHCADPDFLHALKMTLMLAFVTVPLNTVFGTVAAINLTRNEFPGKVFLMSLLDLPFSISPVVTGLMLTLLYGRTGWFAALLRETGINVVFAFTGMALATMFVTLPFVVRELIPILENMDLSQEEAARTLGANDWQVFWNVTLPNIRWGLLYGVILCNARAMGEFGAVSVISGNIIGRTQ... | Part of the ABC-type chloroplast envelope-localized sulfate transporter. | Q6QJE2 |
B0B7P6 | EX7L_CHLT2 | Exodeoxyribonuclease VII large subunit | Chlamydia | MSITSPPIEVSVLTDSIKNLLEKNFLRVVVKGELSNVSLQTSGHLYFAIKDSKAVLNGAFFHFRSKYFDRKPKDGDYVILHGKLTVYAPRGQYQIVAYALTFSGEGNLLQQFEERKQRLAAEGYFDPKRKKPLPSGARVIGVITSPTGAVIQDILRVLSRRCHQFQVILYPVTVQGATAAQEISQAIQFFNQNSMRVHALIIARGGGSIEDLWAFNEEELVKSIVASSIPIISAVGHETDFTLCDFASDVRAPTPSAAAEIVCKSSDQYRQELQNLRRYVSSHARQFIAAKKNLLTHWQRHLASVDFYHTAQQTLDYTRA... | Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. | B0B7P6 |
Q8KC17 | TRPD_CHLTE | Anthranilate phosphoribosyltransferase | Chlorobaculum | MRQQEILQKLLEGHDLSRQEMETCMNSIMENRFTDAGTGAILALLQKKGATPAEVIGACASIVSKSTPVTLDQQAVDTCGTGGDHTGTFNISTAAAFIACGAGIPIAKHGNRSITSKCGSADVLEALGYQVDLPPCATEELFRETGFAFLFAPLYHPSMKAVAAIRKELGIKTIFNMLGPIINPAGVRRQLIGVFDPSVMDIYAEVLLLNGCEHAMLVHGSTGNSMGLDEPSVCGPTSMIELHQGQIIRHTVEPEDFGLGRWDIGELAGGDSHVNAQIIREILDGSAPQAKIDAALFASAITCYVSGKASCIDEGMSLSK... | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). | Q8KC17 |
B0S6J3 | SRGP2_DANRE | SLIT-ROBO Rho GTPase-activating protein 2 | Danio | MTSPAKFRKDKEIIAEYETQVKEIRAQLVEQLKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTRYTKDPQFKKEQNILSPVNCWNLLLAQVKRESRDHATLSDLYLNNIIPRFAQISEDSGRLFKKSKEVGLQLQEDLMKVLNELYTVMKTYHMYNMDSINAESKLKEAEKQEEKQMSRSVRHEEKQTPRSPDSLTNIKIEDKHVRRSSVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNSCVFKYYIHDLSDLIDCCDLGYHASLNRALRTYLSAEFNVETSKHGGLETIENAAENLE... | Postsynaptic RAC1 GTPase activating protein (GAP) that plays a key role in neuronal morphogenesis and migration mainly during development of the cerebral cortex. Regulates excitatory and inhibitory synapse maturation and density in cortical pyramidal neurons. Mechanistically, acts by binding and deforming membranes, th... | B0S6J3 |
B7IDZ1 | ENGB_THEAB | Probable GTP-binding protein EngB | Thermosipho | MKIKSVELVKTIYKSNDKYPESLNGEFVFVGRSNVGKSTLLNILTGRNIAKTSKKPGKTASINFYKINNSFYFVDLPGYGYAKVSVEERARWRKIIENYFSKRAWNIKLVFVLIDGRHELQKNDEILLEWLKELELDFAIVMTKMDKLKNSERAKMIRYYKDLYGENYTIIPYSAITREGIDKIYELIEIFGGV | Necessary for normal cell division and for the maintenance of normal septation. | B7IDZ1 |
B2RYG1 | FA32A_RAT | Ovarian tumor associated gene 12 | Rattus | MEAYEQVQKGPLKLKGVAELGVTKRKKKKKDKDKAKMLEAMGTSKKNEEEKRRCLDKRTPAQAAFEKMQEKRQMERILKKASKTHKQRVEDFNRHLDTLTEHYDIPKVSWTK | May induce G2 arrest and apoptosis. May also increase cell sensitivity to apoptotic stimuli. | B2RYG1 |
A0A072TH68 | KI104_MEDTR | Kunitz type trypsin inhibitor 104 | Medicago | MSTRSLTIFILAHVWLLMATTSIAQFVIDTSGEPVEDDEEYFIRPAITGNGGGSTLVTGNGPCPLHVGLDNTEGTLGVAVKFTPFAPQHDDDDVRLNRDLRVTFLTSTSCGQSTDWRLGEKDATSGRRLIVTGRDNGAGSQGNFFRIVQTQTGGTYNIQWCPTEACPSCKVQCGTVGVIRENGKNLLALDGDALPVVFQKE | Protease inhibitor involved in the control of mycorrhiza establishment and arbuscule development during root colonization by arbuscular mycorrhizal (AM) fungi (e.g. Rhizophagus irregularis). | A0A072TH68 |
Q91169 | PIT1_ONCKE | Growth hormone factor 1 | Oncorhynchus | MSCQAFSADSFTTLAGDSLPLLMHHASAADCLPSSASTHTHNMVSAVPSGLSLLQSSKRSHMHLSTSTLGNGPPGLHYPVTPCHYSNQQTTYGMMAAQEMLSASISQTRILQTCSVPHPNMVNGANTLQGSLAPCLYKFPEHGLGGGSCSLSHSFPPLPPAVLSEEPPLGGTKDLRLRSRPPDDPPDMDSPQIRELEKFANNFKLRRIKLGYTQTNVGEALAAVHGSEFSQTTICRFENLQLSFKNACTLKAILAKWLDEAEQAGALFNEKMGMNERKRKRRTTISLGAKEALERSFREKIKPSSQEIVRMAEGLHLEKE... | Transcription factor that activates growth hormone and prolactin genes. Specifically binds to the consensus sequence 5'-TAAAT-3'. | Q91169 |
Q7VPP6 | ATP6_HAEDU | F-ATPase subunit 6 | Haemophilus | MAVNTAEYIGHHLSFLSSGDGFWAVHLDTLFFSLVAGVLFLVVFSRVAKNATTGVPGKLQCLVEMVVEWVDGLVKDNFHGPRHMIAPLALTIFCWVFIMNAIDLVPVDFLPQLANMFGIHYLRAVPTADISATLGMSICVFGLILFYTVKSKGFNGLAKEYTLHPFNHWAFIPVNFILETVTLLAKPISLAFRLFGNMYAGELIFILIAVMYMADNFALQALGIPLHLVWAIFHILVITLQAFIFMMLTIVYLSIAYNKADH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Q7VPP6 |
Q0I239 | GLPB_HAES1 | Anaerobic glycerol-3-phosphate dehydrogenase subunit B | Histophilus | MKFDVVIIGGGLAGLTCGIMLQQKGKCCAIINNGQSAMNFSSGSMDLLSQLPNGEKINSFEQGYDSLEEQLPNHPYCLFGKQHVLQKAKQFEQLIEKINLNVTGSYKQNHFRVTPLGGLHRTWLSADCIPTMDLHDEHFGYQKITVLGIEGYHDFQPHLLAENLIQHPQFTHCSITTALLHLPELDQLRLTSREFRSVNISQLLEHRLAFRELVQEIKQASGDGEAIFLPACFGLDNQDFFNKLTLETGLNLYELPTLPPSLVGLRQHKKLKTYFEKLGGFILNGDKALRAVIEDQQVKQIYTQLHQEHGIFAEHFVLAS... | Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses fumarate or nitrate as electron acceptor. | Q0I239 |
Q6AP72 | RS10_DESPS | 30S ribosomal protein S10 | Desulfotalea | MMIPTEKIRIRLKAYDHKLLDQSTSEIVETARRTGSAVVGPIPLPTSINKFCVLRSPHVNKKSREQFEMRTHRRLLDILEPTQQTIDLLMKLELSAGVDVEIKLP | Involved in the binding of tRNA to the ribosomes. | Q6AP72 |
Q8BHM9 | TM11F_MOUSE | Airway trypsin-like protease 4 | Mus | MMYAPVEFSQTAYPRIEYQRRQQQFWDPIRLALFTLAIVAIVGITIGIVTHFVVEDDKSFYYLASFQVTSIKYRENYGIRSSREFIERSHQIERMMSRIFRRSSGVGRFIKSHVIKISPDEQGVNILIVLMFRYPSTDSAERIKKRIERTFYQSLKIKQLPLTISMPSFSLTPIDSKKMRNLLNSRCGIRMSSSNIPLPASSSTERIVQGRETAMEGEWPWQASLQLIGAGHQCGATLISNTWLLTAAHCFWKNRDPTKWIVTFGTTITPPLVKRSVGKIIIHEEYHRDTNENDIALAQLTTRVEFSNVVQRVCLPDSSM... | Probable serine protease. | Q8BHM9 |
A3CYP1 | COAD_SHEB5 | Pantetheine-phosphate adenylyltransferase | Shewanella | MHTRAIYPGTFDPITNGHADLIERAAKLFKHVVIGIAANPSKQPRFTLEERVELVNRVTAHLDNVEVVGFSGLLVDFAKEQKASVLVRGLRAVSDFEYEFQLANMNRRLSPDLESVFLTPAEENSFISSTLVKEVALHGGDVNQFVHSEVATALAAKLKLAKP | Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. | A3CYP1 |
Q8CPP4 | FOLD_STAES | Methenyltetrahydrofolate cyclohydrolase | Staphylococcus | MVAKILDGKQIAKEYRQRLKNQVNDLKEYGFTPKLSVILVGNDGASQSYVKSKKKAAEKIGMISEIIHLDESTSEEVVLSELNRLNNDDTVSGILVQVPLPKQVSEQKVLEAINPEKDVDGFHPINIGKLYIDEQTFVPCTPLGIMEILKHADINLEGKNAVVIGRSHIVGQPVSKLLLQANATVTILHSRTKNMNAHLKQADVIVSAVGQPGLVTKENVKKGAVIIDVGNTPDENGKLKGDVAYDEVKEIASAITPVPGGVGPLTITMVLNNTLLAEKLRRGLTK | Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate. | Q8CPP4 |
P82451 | ABCC9_RABIT | Sulfonylurea receptor 2 | Oryctolagus | MSLSFCGNNISSYNIYDGVLQNPCFVDALNLVPHVFLLFITFPILFIGWGSQSSKVQIHHNTWLHFPGHNLRWILTFALLFVHVCEIAEGIVSDSRRESRHLHLFMPAVMGFVATTTSIVYYHNIETSNFPKLLLALFLYWVMAFITKTIKLVKYWQSGWGVSDLRFCITGIMVILNGLLMAVEINVIRIRRYVFFMNPQKVKPPEDLQDLGVRFLQPFVNLLSKATYWWMNTLIISAHKKPIDLKAIGKLPIAMRAVTNYVCLKDAYEEQKKKAADHPNRTPSIWLAMYRAFGRPILLSSTFRYLADLLGFAGPLCISG... | Subunit of ATP-sensitive potassium channels (KATP). Can form cardiac and smooth muscle-type KATP channels with KCNJ11. KCNJ11 forms the channel pore while ABCC9 is required for activation and regulation. | P82451 |
Q3L6T9 | NU4LM_MARAM | NADH dehydrogenase subunit 4L | Martes | MSMVYINIFLAFILSFMGLLIYRSHLMSSLLCLEGMMLSLFIMMTVTILTNHLTLASMTPIILLVFAACEAALGLSLLVMISNTYGTDYVQNLNLLQC | 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. | Q3L6T9 |
A9WL37 | BIOB_RENSM | Biotin synthase | Renibacterium | MLSGVELSRDEALVLLRSDPANYLSLLAAAARLRSAYFGNSVKLNYLVNLKSGLCPEDCTYCSQRLGSAAQILKYSWLKSEDAIDQAEQGLAGGASRVCFVASGRGPSDRDVDRVAGLVGDFKTRNPQAEVCACLGILKEGQAERLKSCGVDAYNHNLNTSEEKYSEICTTHEFSDRTNTVKAAKAAGLSPCSGLIVGMGESDEELIDALFALRELGSESVPVNFLMPFEGTPLADTWLLTPVKCLQILCVARFVAPRSELRIAGSREMHLRSLQPLALHVANSIFLGDYLTSEGQSAAEDLAMIEDGGFVILDPRASAP... | Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism. | A9WL37 |
B4SZJ8 | BIOF_SALNS | 8-amino-7-ketopelargonate synthase | Salmonella | MSWQQRVDDALTARRATDTLRRRYVVSQGAGRWLVANGRQYLNFSSNDYLGLSQHPQIIRAWQQAATRFGVGSGGSGHISGYSVAHQALEVELAQWLEYPRALLFISGFAANQAVITALMKKNDRIVADRLSHASLLEAANLSPAQLRRFIHNDTQHLSRLLQSPCVGQQLVVTEGVYSMDGDSAPLAEIQHIARRHHAWLLVDDAHGIGVTGDEGRGTCWQRGVKPELLVVTFGKGFGVSGAAVLCSESVADYLLQFARHLVYSTSMPPAQAQALSASLAVIRSDEGRERREKLAALVQRFRAGVNASRFTLLNAHSAI... | Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide. | B4SZJ8 |
Q5SCY7 | TI214_HUPLU | Translocon at the inner envelope membrane of chloroplasts 214 | Huperzia | MLSVLWVLISWINISGPIPNISGSLTLFGLYYGFLAALPIGLSQILTIRAFLLGGNTGGTLAVSGSIMGQLITNLSIYYWPIYVMLLKPHAITLLVLPYMLFYWYRTKDLLYDQPPNPVESLNDAQVRQIFLDSFILSLLNPVILPSPVFARSLNLFIFRYSNKISFVISSSFGWLGGYILFINLIKLLMVRIERDSSVNYPLIKSIINQIFSIIILALRLLYLGRAPVPLFTKKIHDGFESDENQIVKSLWLNKPWPTVLFDYRKWNRPFRYIQNGPNGDSPVKKQVSQYFFDTCSSDGRQRISFTSLPSSSTFQKDLK... | Involved in protein precursor import into chloroplasts. May be part of an intermediate translocation complex acting as a protein-conducting channel at the inner envelope. | Q5SCY7 |
B8CRF7 | CLPP_SHEPW | Endopeptidase Clp | Shewanella | MHKAPESVLNALVPMVVEQTAKGERSYDIYSRLLKERVIFLVGQVEEHMANLIVAQLLFLESESPDKDIYLYINSPGGSVTAGMAIYDTMQFIKPNVSTVCIGQAASMGAFLLAGGAEGKRHCLPNSRVMIHQPLGGFQGQASDIAIHAQEILGIKNKLNTMLAEHTGQPIEVIERDTDRDNFMSADEAAEYGLVDSVLAKRG | Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. | B8CRF7 |
O93631 | RS7_METBU | 30S ribosomal protein S7 | Methanococcoides | MYKLFGKWDLTEVEVADAGIKRYVNLDPVIVPHTSGKHARQQFNKSDITIVERLVNNVMRNAQNTGKKQIALRIVDEAFDIVNSKTKKNPVQVLVEAVSNAGPREEVVRLKYGGISVPKAVDTAPQRRVDHALRNISIGSNQTAFKSKRSAAECLASELIAASNRDAKCFSINRKDGKERVAKAAR | 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. | O93631 |
A8IFY6 | AROE_AZOC5 | Shikimate dehydrogenase (NADP(+)) | Azorhizobium | MKRVAIFGHPVIHSRSPLVHGYWLKQHGIAGDYVRHDVAPDEAEAFFARFAEQGYAGGNVTIPHKEVAFNALAEADPVARALGVANTLWLEDGRLFGANTDAPGFLSNLDVTAPGWDANPRVALVLGAGGASRAVLYGFLQRGFDKVLLANRTLARAEALAAHFGPRVVPIGWDGVSASLKEAQVVANTTSLGMKGQPPLDLDLSVLADDAVVADVVYVPLETPLLKAAKARGLRTVDGLGMLLHQAVPGFARWFGVTPQVDAGLRDLIVADLAAKGQLGA | 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). | A8IFY6 |
P0DUJ7 | SSEK3_SALTS | Salmonella secreted effector K3 | Salmonella | MFSRVRGFLSCQNYSHTATPAITLPSSGSANFAGVEYPLLPLDQHTPLLFQWFERNPSRFGENQIPIINTQQNPYLNNIINAAIIEKERTIGVLVDGNFSAGQKKALAKLEKQYENIKVIYNSDLDYSMYDKKLSDIYLENIAKIEAQPANVRDEYLLGEIKKSLNEVLKNNPEESLVSSHDKRLGHVRFDFYRNLFLLKGSNAFLEAGKHGCHHLQPGGGCIYLDADMLLTGKLGTLYLPDGIAVHVSRKGNSMSLENGIIAVNRSEHPALKKGLEIMHSKPYGDPYIDGVCGGLRHYFNCSIRHNYEEFCNFIEFKHE... | Protein-arginine N-acetylglucosaminyltransferase effector that disrupts TNF signaling in infected cells, including NF-kappa-B signaling and apoptosis . Acts by catalyzing the transfer of a single N-acetylglucosamine (GlcNAc) to a conserved arginine residue in the death domain of host proteins such as TRADD, TNFRSF1A/TN... | P0DUJ7 |
P08238 | HS90B_HUMAN | Heat shock 84 kDa | Homo | MPEEVHHGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELKIDIIPNPQERTLTLVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVRADHGEPIGRGTKVILHLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYLEKEREKEISDDEAEEEKGEKEEEDKDDEEKPKIEDVGSDEEDDSGKDKKKKTKKIKEKYIDQEELNKTKPIWTRNPDDITQEEYGEFYKSLTNDWEDHLAVKH... | (Microbial infection) Binding to N.meningitidis NadA stimulates monocytes . Seems to interfere with N.meningitidis NadA-mediated invasion of human cells (Probable). | P08238 |
Q5E963 | ARP5L_BOVIN | Arp2/3 complex 16 kDa subunit 2 | Bos | MARNTLSSRFRRVDIDEFDENKFVDEQEEAAAAAGEPGPDPSEVDGLLRQGDMLRAFHAALRNSPVNTKNQAVKERAQGVVLKVLTNFKSSEIEQAVQSLDRNGIDLLMKYIYKGFEKPTENSSAVLLQWHEKALAVGGLGSIIRVLTARKTV | May function as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. | Q5E963 |
B8FA41 | TRPD_DESAL | Anthranilate phosphoribosyltransferase | Desulfatibacillum | MFSELLKKIVSGQDLAEDETTTMMDAIMSGEVEVPAIAAFMAALATKGETFTELAGAARSMRRKATRIQVSSNTVVDTCGTGGDGASTFNISTTSAFVVAGCGVTVAKHGNRSVSSKCGSADVLEALGVKLDTHPEVVEQGIEEIGIGFLFAPMYHSAMRFAMPARQAVGIRSIFNMLGPLTNPAGANCQLLGVYDPKLTEMFAEALKLLGARKAYVVHGHDGLDEISICAPTRVSELAEGMVRTFDILPEQLNIEACDISELAGGDAEENAGITKSILEGTPGPKQDVVVVNAGAALVAAGVAEDFKDGMAKAKEAIQS... | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). | B8FA41 |
Q7MUR5 | RISB_PORGI | 6,7-dimethyl-8-ribityllumazine synthase | Porphyromonas | MATAYHNLSDYDYESVPCGKDLRIGIAVAEWNHNITEPLMKGAIDTLLEHGVSADNIIVQHVPGTFELTYASAYLAEQHEVDAVIAIGCVVRGDTPHFDYICQGVTQGITQLNIDGFVPVIFGVLTTETMLQAEERAGGKHGNKGTEAAVTALKMAGLERI | 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. | Q7MUR5 |
Q1QQP6 | TSAD_NITHX | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Nitrobacter | MLVLGIETTCDETAAAVVERHADGSALILSNIVRSQTGEHAPYGGVVPEIAARAHVDMLDGIIASAMKQSGVGFPRLSGVAAAAGPGLIGGVIVGLTTAKAIALVHRTPLIAVNHLEAHALTPRLTSALEFPYCLFLASGGHTQIVAVLGVGNYVRLGTTVDDAMGEAFDKVAKMLGLPYPGGPQVERAAADGDAKRFNFPRPMLGRPDANFSLSGLKTAVRNEAGRIDPLRPRDINDLCAGFQAAVLEATADRLGVGLELFRERFGTPRALVAAGGVAANQAIRGALEGVAARAQTMLIIPPPALCTDNGAMIAWAGAE... | Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct ca... | Q1QQP6 |
P50253 | COX2_DROSI | Cytochrome c oxidase polypeptide II | Sophophora | MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNNYVNRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELTTDGFRLLDVDNRVILPMNSQIRILVTAADVIHSWTVPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNHFIKWISSNNS | Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CII... | P50253 |
Q6AFZ2 | SYV_LEIXX | Valyl-tRNA synthetase | Leifsonia | MPEKPALEGLEGKWGSRWQEDGTYLFDRAAAIAAGRDAVYSIDTPPPTASGSLHIGHVFSYTHTDVVARFQRMLGKRVFYPMGWDDNGLPTERRVQNYYGVRCDPTLPYEPGLTPPFEGGDNKSSKAADQKPISRRNFIELCERLTVEDEKQFEALWRSLGLSVDWSQTYRTIGEESLRTSQLAFLRNVKRGEAYQALAPTLWDITFRTAVAQAELEDRDQPSAYHRVAFHGEAGPVFIETTRPELLPACVALVAHPDDERYQPLLGTTVRTPVFGVEVPVVAHHLAQPDKGSGIAMICTFGDITDVTWWRELDLPNRAI... | 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. | Q6AFZ2 |
Q7VQN8 | RS18_BLOFL | 30S ribosomal protein S18 | Candidatus Blochmannia | MSILPRYIRHRKFCRFTADKCIYVDYKDLSKIQHSIIENAKIIPSRITGTRSKYQRQLARAIKIARFLSLLPYIDQNR | Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit. | Q7VQN8 |
Q57YZ9 | SIR4_TRYB2 | SIR2-related protein 2 | Trypanosoma | MADRLAIFIKQCGLQRCVILTGAGCSTESGVPDYRGPNGLYRRPNFVPLTRQVFLSGSEHRKRYWARSMFGYNTVSGASCNDTHMGLYELYRAGVVNRLLTQNVDGLHHLAAHGGTGSKTVEAYAKYTSSNSGVLELHGNIHQVCCMQCGDVSPRRRLQQRLCEANYQLCRDYEAEFSEVRPDGDYEVPDRVVQAMQLVCCEHCGGLLKPHVVLFGENVPKECVREAYTAVRAASCLICLGTSLQVFSALRFVLAARESGVPIAIVTAGRTRADGLEELKVDTNSTAATMRGVVKQLLGFELGGTK | NAD-dependent protein deacylase. Catalyzes the NAD-dependent hydrolysis of acyl groups from lysine residues. | Q57YZ9 |
Q5M865 | PAGR1_RAT | PTIP-associated protein 1 | Rattus | MSLALGHGTIAGSTAAPLSEEGEVTSGLQALAVEDTGGPSVSASKAEEEGKGSQEEAGREASRAEEALEASSAVSDERAEGESEDWCVPCSDEEVELPANGQSWMPPPSEIQRLYELLATQGTLELQAEILPRRPPTPEAQSEEERSDEEPEAKEEEEEKPHMPTEFDFDDEPVTPKDSLIDRRRTPGSSARSQKREARLDKVLSDMKRHKKLEEQILRTGRDLFSLDSEGPSPASPPLRSSGNSLFPRQRKY | Its association with the histone methyltransferase MLL2/MLL3 complex is suggesting a role in epigenetic transcriptional activation. However, in association with PAXIP1/PTIP is proposed to function at least in part independently of the MLL2/MLL3 complex. Proposed to be recruited by PAXIP1 to sites of DNA damage where th... | Q5M865 |
A0LI59 | RLMH_SYNFM | rRNA (pseudouridine-N3-)-methyltransferase RlmH | Syntrophobacter | MQIHLVFVGKTVFPDVETGIERYVSRLNHYLPTRIHYVKAEKIPPRGMESAVLEKECERILKLIGGKSNQLIVWDRTGKHLDSLEFARVLERLSNGGTGAVWMIIGGPLGISRELRDRANLVLALSEMTFPHDLARLIVAEQLYRAFTIIRGEPYHK | Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA. | A0LI59 |
Q58497 | DCDA_METJA | Diaminopimelate decarboxylase | Methanocaldococcus | MKIMFLGNDTVEIKDGRFFIDGYDAIELAEKFGTPLYVMSEEQIKINYNRYIEAFKRWEEETGKEFIVAYAYKANANLAITRLLAKLGCGADVVSGGELYIAKLSNVPSKKIVFNGNCKTKEEIIMGIEANIRAFNVDSISELILINETAKELGETANVAFRINPNVNPKTHPKISTGLKKNKFGLDVESGIAMKAIKMALEMEYVNVVGVHCHIGSQLTDISPFIEETRKVMDFVVELKEEGIEIEDVNLGGGLGIPYYKDKQIPTQKDLADAIINTMLKYKDKVEMPNLILEPGRSLVATAGYLLGKVHHIKETPVTK... | Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine. | Q58497 |
Q05095 | CDX1_RAT | Caudal-type homeobox protein 1 | Rattus | KTRTKDKYRVVYTDHQRLELEKEFHYSRYITIRRKSELAANLGLTERQVKIWFQNRRAKERKVNKKKQQQQQQQQQQPMPPTQLPLPLDGTPTPSGHPGSLCPTNAGLLGTPSPVPVKEEFLP | Plays a role in transcriptional regulation. Involved in activated KRAS-mediated transcriptional activation of PRKD1 in colorectal cancer (CRC) cells. Binds to the PRKD1 promoter in colorectal cancer (CRC) cells. Could play a role in the terminal differentiation of the intestine. Binds preferentially to methylated DNA. | Q05095 |
D4GYE4 | PTFA_HALVD | Fructose-specific phosphotransferase enzyme IIA component | Haloferax | MDVTDISTITPLELISLEEPPATKEGAIEFLLDLAVDAGRVDDRDAALDALLEREGEATTGVGFGIGIPHAKTDAVSKPTVAFARSAEGIDFDAMDDKPAKLLFMILVPAAGGEDHLQILSALSRSLMHEDVREKLLEAESKQTVQDVLAEVVE | 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 PtfABC PTS system is involved in fructose transport. | D4GYE4 |
B1KQY9 | GRPE_SHEWM | HSP-70 cofactor | Shewanella | MSNDSSKAKQNQVDEAVEGEILTESEVETGNDEASLMDELTQANFRVEELEQALAEANAKIEEQKDSVTRAAASEANIRRRAAQDVEKAHKFALEKFANELLPVIDNMERALQGTNAEAEETKAIYEGVELTLKSFVSTVDKFGLKEVNPHGESFNPEHHQAIGMQPSPEFPANTVMMVMQKGYILNDRLLRPAMVMVSQGGSGVDTQA | Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-b... | B1KQY9 |
Q89AN1 | GRPE1_BUCBP | HSP-70 cofactor 1 | Buchnera | MNIDNDLLSKNKEAKVVSENSTVEINDVTNSDSKNTDNDFQTEELNNFEKIFLNLNSDLLNQQLLVKNNLKLYKIRAEKEINRAYKFSLKSFISSLFPVIDSMEYALNLFKKDDKILCLIFNELDNVSQSLMNLLVKFGVTSIKDINIAFNPDIHQAITTQVSKDIKNNYVISIMQKGYLLYDRLLRPAMVIVSKNDI | Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-b... | Q89AN1 |
C5C2D6 | MNMA_BEUC1 | tRNA-specific 2-thiouridylase MnmA | Beutenbergia | MRVLAALSGGVDSAVAAARAVDAGHDVVGVHMALSRTRAQHRTGSRGCCSIEDASDARRAADVLGIPFYVWDLSEEFTDTVVADFLSEYAAGRTPNPCVRCNEHIKFSALLDRGLALGFDAVATGHYARIERGAAGVPELHRAADAAKDQSYVLAVMGPERLARSLFPLGEVPTKDAVRAEAAARGLSVSAKPDSYDICFVADGDTQGFLRSHLGSQPGPVLDTDGREVGAHDGAYAFTVGQRKGLRLPRPAADGRPRYVVDVRTASNTVVVGPAELLSVRDVLGERPVWLAEEPHEWTDATVQVRAHGAALPARIRTVT... | Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. | C5C2D6 |
P16044 | IBPI_TACTR | BPI-type | Tachypleus | TERGFLDCTSPPVTGPCRAGFKRYNYNTRTKQCEPFKYGGCKGNGNRYKSEQDCLDACSGF | Inhibitor of trypsin and chymotrypsin. | P16044 |
A9BHP7 | AROA_PETMO | 5-enolpyruvylshikimate-3-phosphate synthase | Petrotoga | MKIEVTPTENINAEITLPGDKSISHRALIIGSLAEGETKIHNFLSSEDTLSTLNILNSIGASIKQISEDEVIVEGKGKDNFIEPSNVLNAKNSGTTMRLMMGVLSAQNFYSVITGDDSLRERPMKRVIDPLSKMGGRFFARKNGEFAPITILGTKDISPLVYKTPVASAQVKSAILLAALYAKGETQVIEPAKSRDHTERMLKYFGADIAQKDTTVVIRGLTKNLEGREFFVPGDLSSASFFIVAALITKNSTLLIKNVGINPTRTGILSVLKMMGADIKIINEKTLNNEPVGDLLVKSSSLKGVEIKGEMIPLIIDEIP... | 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. | A9BHP7 |
Q8PN23 | OBG_XANAC | GTP-binding protein Obg | Xanthomonas | MKLVDEAEILVTAGNGGNGCVGFRREKFIPLGGPDGGDGGAGGSVWIVADENVNTLVDFRHERTFKAQRGENGMGRQAYGKGGEDRIIVVPVGTVVINVQTDEVIGDLTQHGDRLLVAKGGKGGLGNMHFKSSVNRAPRQATTGEEGEERLLKLELKLLADVGLLGFPNAGKSTLIRAVSAATPKVADYPFTTLYPNLGVVSVEAYRSFVIADVPGLIEGAADGAGLGTQFLRHLQRTRLLLHLVDISPALGVYGEGGVDGVSPADQVRTIERELERHDPELLKKPRWLVLNKADLMFEDEARAAAETIVAELGWTAPWY... | An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control. | Q8PN23 |
Q0C643 | HIS6_HYPNA | ImGP synthase subunit HisF | Hyphomonas | MLKTRIIPCLDVKDGRTVKGVNFVDLKDAGDPVALARAYDAAGADELCFLDITASHEGRGTLLETVSRTAEACFMPLTVGGGVRSVEDMVALLRAGADKVAINSAAVADPALVSACAAKAGRQCVVVAIDARAVGDSWEIFTHGGRKATGINAVEFAREAAKRGAGEILLTSMDRDGTKSGYDIPLLKAVSSAVTIPVIASGGAGSVEDFAPAVLEGGASAVLAASIFHFGEASLAEARAALAKAGAPVRTV | IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit. | Q0C643 |
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