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 |
|---|---|---|---|---|---|---|
Q6D1I1 | FRSA_PECAS | Esterase FrsA | Pectobacterium | MAQANLSETLFKPSFKHRETSTLVRRTRHDQETQGLHSTLEGEKTSSWYRMINRLMWIWRGVNPWEIEDVLSRIAASQADRSNEQLLDTVIGYRGGNWIYEWAKQGADWQQRATESGDDAQTGQFWLNAANLYSIAAYPHIKGDELAEQAQTLANRAYEEAAKYLPYELKELTFPIAGGGTLTGFLHMPSQGKAPFPTVLMCGSLETLQSDYHRLFQDYFAPAGMAMLTIDVPSVGFSSRWKLTQDSSFLHQQVLRALPDVPWVDHCRVTAFGFRFGANIAVRLAYLESQRLRGVACLGPVVHHLLSDPNRQQQVPDMFM... | Catalyzes the hydrolysis of esters. | Q6D1I1 |
P02256 | H1_PARAN | Histone H1, gonadal | Parechinus | PGSPQKRAASPRKSPRKSPKKSPRKASASPRRKAKRARASTHPPVLEMVQAAITAMKERKGSSAAKIKSYMAANYRVDMNVLAPHVRRALRNGVASGALKQVTGTGASGRFRVGAVAKPKKAKKTSAAAKAKKAKAAAAKKARKAKAAAKRKAALAKKKAAAAKRKAAAKAKKAKKPKKKAAKKAKKPAKKSPKKAKKPAKKSPKKKKAKRSPKKAKKAAGKRKPAAKKARRSPRKAGKRRSPKKARK | Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures. | P02256 |
Q0A598 | FPG_ALKEH | DNA-(apurinic or apyrimidinic site) lyase MutM | Alkalilimnicola | MPELPEVETTRRGLAPLLEGRRVTGMTVRQARLRWPVPAGLPDAITGQTIRAVDRRAKYLLFRTPAGTLILHLGMSGSLRVIPGQQAGACAVPPGRHDHVDLRLADGSCLRYTDPRRFGSLHWCTGEPEAHWLLHRLGPEPFDTAFDGDRLHRLSRGRRTSVKAFIMDSGIVVGVGNIYASESLFRAGIHPGRPAGRVGLARYRRLAGAVREVLAEAIAAGGTTLRDFTASDGRPGYFAQTLNVYGRAGAPCPRCGRSIRQRRIAQRSTWYCPGCQR | 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. ... | Q0A598 |
P80104 | LHB1_HALHL | EHA-beta-1 | Halorhodospira | ADNMSLTGLSDEEAKEFHSIFMQSFLIFTAVAVVAHFLAWAWRPWIPGAEGYG | Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers. | P80104 |
Q8CUK0 | LUXS_OCEIH | Autoinducer-2 production protein LuxS | Oceanobacillus | MTKKMNVESFNLDHTKVKAPYVRLVGVTEGANGDKVHKYDIRIKQPNKAHMEMPGLHSLEHLMAENIRNHSDAVLDIGPMGCQTGFYLSLINHDDYDDVLTMIEKTLEDVLQATEVPACNEVQCGWAANHSLLGAQEIAKEMLNEKASWSEVF | Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhom... | Q8CUK0 |
Q5F878 | SUCC_NEIG1 | Succinyl-CoA synthetase subunit beta | Neisseria | MNLHEYQAKELLASYGLPVQGGILAHNGEEAAAAYDKLGGKFAVVKAQVHAGGRGKAGGVKVVKSREKAKEVAESLIGTNLVTYQTDANGQPVNSVLVCEDMYPVQTELYLGAVVDRSTRRVTFMASTEGGVEIEKVAAETPEKIFKVTVDPLVGLQPCQAREVAFQLGLKDKQINEFAKLMTGAYKAFVENDFALFEVNPLAVRENGALACVDGKIGIDSNALYRLPKIAELRDKSQENERELKASEFDLNYVALEGKIGCMVNGAGLAMATMDIIKLKGGQPANFLDVGGGATKDRVVEAFKLILEDKSVKGVLINIF... | Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinat... | Q5F878 |
A6MN03 | TI214_ILLOL | Translocon at the inner envelope membrane of chloroplasts 214 | Illicium | MILKSFLLGNLLSLCMKIINSVVVVGLYYGFLTTFSIGPSYLFLLRARVMEEGTEKEVSATTGFITGQFMMFISIYYAPLHLALGRPHTITVLVLPYLLFHFFWNNHKHFFDYGSTTRNSMRNLSIQCVFLNNLSFQLFNHFILPSSTLARLVNIYMFRCNNKMLFVTSSFVGWLIGHILFMKWVGLVLFWIRQNHSIRSNVLIRSNKYLVSELRNSMARIFSILLFITCVYYLGRIPSPIVTKKLKETSETEEGEETEEEGDVKIETTSETKGTEQEQKGSTEEGPSLCSEEKEDPDKIDETEEIRVNGKEKTKDELDF... | 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. | A6MN03 |
A8AL94 | SYP_CITK8 | Prolyl-tRNA synthetase | Citrobacter | MRTSQYLLSTLKETPADAEVISHQLMLRAGMIRKLASGLYTWLPTGLRVLKKVENIVREEMNNAGAIEVSMPVVQPADLWQESGRWEQYGPELLRFVDRGERPFVLGPTHEEVITDLIRNELSSYKQLPLNFFQIQTKFRDEVRPRFGVMRSREFLMKDAYSFHTSQESLQETYDAMYAAYSKIFSRMGLDFRAVQADTGSIGGNASHEFQVLAQSGEDDVIFSDSSDYAANIEFAEAVAPKAPRAAASQEMTLVDTPNAKTIAELVEQFNLPIEKTVKTLLVKAVEGSSYPLVALLVRGDHELNEVKAEKLPQVASPLT... | 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... | A8AL94 |
Q8N108 | MIER1_HUMAN | Mesoderm induction early response protein 1 | Homo | MAEPSVESSSPGGSATSDDHEFDPSADMLVHDFDDERTLEEEEMMEGETNFSSEIEDLAREGDMPIHELLSLYGYGSTVRLPEEDEEEEEEEEEGEDDEDADNDDNSGCSGENKEENIKDSSGQEDETQSSNDDPSQSVASQDAQEIIRPRRCKYFDTNSEVEEESEEDEDYIPSEDWKKEIMVGSMFQAEIPVGICRYKENEKVYENDDQLLWDPEYLPEDKVIIFLKDASRRTGDEKGVEAIPEGSHIKDNEQALYELVKCNFDTEEALRRLRFNVKAAREELSVWTEEECRNFEQGLKAYGKDFHLIQANKVRTRSV... | Transcriptional repressor regulating the expression of a number of genes including SP1 target genes. Probably functions through recruitment of HDAC1 a histone deacetylase involved in chromatin silencing. | Q8N108 |
B3QP85 | ISPD_CHLP8 | MEP cytidylyltransferase | Chlorobaculum | MKTVAIIAASGVGKRMKLDGGMSKQMIEIGGHTVIWHTMKAFQDAESVDAVYIATKSDSIEPFKQLARENGFTKIHSIIEGGKERQDSIRNCMDLIEEEIESSGVMPDAILVHDGARPFIQPEEIDEIARISAEHGACVPATKPKDTIKYIGRTPEVFGETLDRSRLLQVQTPQGFTPAKLIEAHRKAASDGVYATDDAALVERYFPEQEIHVYEMGYHNIKITTPEDVPVGEAILAGLKARKSEN | Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). | B3QP85 |
Q11Z44 | RUVA_CYTH3 | Holliday junction ATP-dependent DNA helicase RuvA | Cytophaga | MIAYIEGKLAHKDPTFVVVDVQGIGYHIRVSLHTFSQLKDLERVKIHTFLHIKEDAHTLFGFADLMEKEMFLHLTSISGIGPGTALVVLSSMNPIELKEAIAREDVKTIQSVKGIGLKTAQRVILELKDKMKKDALLAGSDSKQNFSVSHNSIRSEALTALITLGFTKTVAEKNLDLILKGNSNSFTLEDLIKQALKMS | 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... | Q11Z44 |
C0R3W7 | DNAK_WOLWR | Heat shock protein 70 | unclassified Wolbachia | MGRAIGIDLGTTNSCVAIMQGKDTKVIENKEGARTTPSIVALTSSGERLIGAPAKRQATTNASNTFFATKRLIGRQYSDPEMKNLSVPYKVFAAKSGDAWVKTTDNKEYSPSQIGAFILQNMKEAAEAYLGEEVKDAVITVPAYFNDSQRQATKDAGKIAGLNVLRIVNEPTAAALAYGLDKKHGHTIVVYDLGGGTFDVSILEIGDGVFEVKATNGDTHLGGEDFDNGVVSYLLDEFKKSNGIDLKNDPMAMQRIKEAAEKAKIELSSAMETEINLPFITADASGPKHLNMKLTRAKLESLVNDLIERTMAPCKKALED... | Acts as a chaperone. | C0R3W7 |
Q5E9T7 | JADE1_BOVIN | PHD finger protein 17 | Bos | MKRGRLPSSSEDSDDNGSLSTTWSQNSRSQHRRSSCSRPEDRKPSEVFRTDLITAMKLHDSYQLNPDEYYVLADPWRQEWEKGVQVPVSPGTIPQPVARVVSEEKSLMFIRPKKYIVSSGSEPPELGYVDIRTLADSVCRYDLNDMDAAWLELTNEEFKEMGMPELDEYTMERVLEEFEQRCYDNMNHAIETEEGLGIEYDEYVVCDVCQSPDGEDGNEMVFCDKCNICVHQACYGILKVPEGSWLCRTCALGVQPKCLLCPKKGGAMKPTRSGTKWVHVSCALWIPEVSIGSPEKMEPITKVSHIPSSRWALVCSLCNE... | Scaffold subunit of some HBO1 complexes, which have a histone H4 acetyltransferase activity. Plays a key role in HBO1 complex by directing KAT7/HBO1 specificity towards histone H4 acetylation (H4K5ac, H4K8ac and H4K12ac), regulating DNA replication initiation, regulating DNA replication initiation. May also promote ace... | Q5E9T7 |
A4SFG0 | SSRP_CHLPM | Small protein B | Chlorobium | MAKKQQTKTYTQAIQNRKARFEFEILDTVVAGIELLGSEVKSVRLGKASLNESFAIIHHGEVWLENMQITPYEFNHLDSLEPKRSRKLLLHKAEIAKLQSQISEKGLALIPLKAFFNPKGVLKLELAVAKGKKLFDKRETIKNRDNERQLQQIKKQY | Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemb... | A4SFG0 |
O31097 | PHYC_BACIU | Phytate 3-phosphatase | Bacillus | MNHSKTLLLTAAAGLMLTCGAVSSQAKHKLSDPYHFTVNAAAETEPVDTAGDAADDPAIWLDPKTPQNSKLITTNKKSGLVVYSLDGKMLHSYNTGKLNNVDIRYDFPLNGKKVDIAAASNRSEGKNTIEIYAIDGKNGTLQSMTDPDHPIATAINEVYGFTLYHSQKTGKYYAMVTGKEGEFEQYELKADKNGYISGKKVRAFKMNSQTEGMAADDEYGRLYIAEEDEAIWKFSAEPDGGSNGTVIDRADGRHLTRDIEGLTIYYAADGKGYLMASSQGNSSYAIYDRQGKNKYVADFRITDGPETDGTSDTDGIDVLG... | Catalyzes the hydrolysis of inorganic orthophosphate from phytate. Only phytate, ADP, and ATP were hydrolyzed (100, 75, and 50% of the relative activity, respectively). | O31097 |
Q83SR1 | RS20_SHIFL | 30S ribosomal protein S20 | Shigella | MANIKSAKKRAIQSEKARKIIASRRSMMRPFIKKGDAAIEAGDKAAAQKAFNEMQPIVDRQAAKGLIHKNKAARHKANLTAQINKLA | Binds directly to 16S ribosomal RNA. | Q83SR1 |
O29315 | Y947_ARCFU | Putative toxin AF_0947 | Archaeoglobus | MRRRRYLEKLEWVEREINFATEHAMSDEVRKRAVLYSIMTAVEVVMDIVAMLVKDLGKQVEDDYTNISKLLEECVIEESEAELLRRYNGLRNAIAHHYNHLDLSKVERALTQLDELYEVAVKLVKTADKLAG | Probable toxic component of a putative type VII toxin-antitoxin (TA) system, probably an RNase. Probably neutralized by cognate antitoxin AF_0948. Neutralization may be due to AMPylation by AF_0948. | O29315 |
A5WC71 | TIG_PSYWF | PPIase | Psychrobacter | MAKDLQVTTSKVNDNQTQLTVKVPVEQIQNKVEGRIRNVAKTAKIDGFRKGKVPVSHIRAQYGAGIQQEVINDVIRDTVFEAIKAEDVRAVGMPNIDDVKLEDEFLVYQATVEIFPEIKVEGMSDIEVERHTATITDEDVDTMIENLRKQRQEFAEKEGAADEGDQVTFDFEGSIDGEKFEGGSAEDFKLVLGSGQMIPGFEDGIKGLAAGEEKTIDVTFPEDYQAENLAGKEAQFKINVKKVEEAKLPEINDEFLELFGVKEGGVEQLKTDVRKNMTREIKNAARNQVKQAAFDALLEKNEFDVPSAMVDQEVDRQRNL... | Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase. | A5WC71 |
C3L9P9 | HIS5_BACAC | ImGP synthase subunit HisH | Bacillus cereus group | MIAIIDYGMGNIRSVEQALKYIGAAYIVTSDKEEIFRSDGVILPGVGAFPKAMDILEEKDLVRMLQEIGRSRKPLLGICLGMQLLFEKSEELQDCNGLSLLPGVIRKLKVPYKIPHMGWNELKKEGEIALWNGVEDGSFVYYVHSYYADCPNEIVYGISDYGVKVPGFVAKGNIYGAQFHPEKSGDIGMQMLKNFKGVVETWKSSQLSI | IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF. | C3L9P9 |
P18816 | LACR_LACLL | Lactose phosphotransferase system repressor | Lactococcus | MNKKRRLEKILDMLKIDGTITIKEIIDELDISDMTARRDLDALEADGLLTRTHGGAQLLSSKKPLEKTHIEKKSLNTKEKIDIAKKACSLIKDGDTIFIGPGTTLVQLALELKGRKGYKIRVITNSLPVFLILNDSETIDLLLLGGEYREITGAFVGSMASTNLKAMRFAKAFVRANAVTHNSIATYSDKEGVIQQLALNNAVEKFLLVDSTKFDRYDFFNFYNLDQLDTIITDNQISPQHLEEFSQYTTILKAD | Repressor of the lactose catabolism operon. Galactose-6-phosphate is the inducer. | P18816 |
Q9BTE6 | AASD1_HUMAN | Alanyl-tRNA synthetase domain-containing protein 1 | Homo | MAFWCQRDSYAREFTTTVVSCCPAELQTEGSNGKKEVLSGFQVVLEDTVLFPEGGGQPDDRGTINDISVLRVTRRGEQADHFTQTPLDPGSQVLVRVDWERRFDHMQQHSGQHLITAVADHLFKLKTTSWELGRFRSAIELDTPSMTAEQVAAIEQSVNEKIRDRLPVNVRELSLDDPEVEQVSGRGLPDDHAGPIRVVNIEGVDSNMCCGTHVSNLSDLQVIKILGTEKGKKNRTNLIFLSGNRVLKWMERSHGTEKALTALLKCGAEDHVEAVKKLQNSTKILQKNNLNLLRDLAVHIAHSLRNSPDWGGVVILHRKE... | Functions in trans to edit the amino acid moiety from incorrectly charged tRNA(Ala). | Q9BTE6 |
F8GAQ8 | BAMB_FRAST | Outer membrane protein assembly factor BamB | Francisella | MKKLFLVIVPLLLSLLATSCSTSNVPPPTPLAEKPPKEAKVKVKWSRKTGNGNGGLPIYNVSPTYANNTVFVPNQNGVAYGLSITDGKIVWKHDTGTILSSQPNTIANAVIFGSVKGVLTAVDQKDGKILWRTDAPSSIFSQPTIYSNHLYTHTHDGSVTSFDATNGSKVWNVTNNIPEITLPSDSSPIILNDTVMVGSAFGTVLGFTLESGDRTINLPVAIAHGSSPADKMVDITANPMLYGNYLIFAAFQGAIVALDKDTGKMLWAKKASIINNMAINNGVIFTAQANSELKAYDIQTGDTVWTQSTLEWRKITAPIY... | Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. | F8GAQ8 |
C9ZFL1 | MSHD_STRSW | Mycothiol synthase | Streptomyces | MTSDDTAQPSGARRIETRPDLTAAQKDAVLALLDEAAQVDGQQAVSEQGRLQLRGGPREGVRHLLLSVGEDLVGYAQLEDNDPVEAPAAELVVHPSHRGHGHGRALGSALLAESGKRLRVWAHGGHSAARHLAQVLGLTLFRELRQMRRSLTDFDPAEPVLPEGVTVRAFVPGEDDAAWLAANAEAFAHHPEQGSLTQRDLDDRKGEPWFDPAGFFLAFRGEELVGFHWTKAHAAEQLGEVYVVGVRPGAQGGGLGKALTTIGLRHLAAQGLPTAMLYVDADNKAAVTVYERLGFVTYETDLMYRSET | Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol. | C9ZFL1 |
A8GX86 | MUTS_RICB8 | DNA mismatch repair protein MutS | belli group | MNFQEFKHKYGYDAATKMMQQYLDIKFAHLDCLLLFRMGDFYEMFYEDAVLASGVLGIALTKRGKNGDEEVPMCGVPYHALENYLTKLIEENYKVAICDQLETPEEAKNRGGYKAVVNRNVTRIITPGTVIEENLITTAEPNYLASLVVPKNKDTAALCYADLSTSTIFVVNVPELEILNELARLKPREILLSEHLRSSDLASNISKQLNFRITYQVDSFFAVNKCEKIILDFYKMKDIKGVGEISNSQICAIGSILEYLTLTQKENIPNLPKPKIIDFHSYMTIDFSTRRNLEIVTNSCGGNKGSLLSTLNHTVTKQGG... | This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity. | A8GX86 |
Q2P6V6 | RECR_XANOM | Recombination protein RecR | Xanthomonas | MSSLLEQLIEAFRVLPGVGQKSAQRMAYHVLEREREGGRRLATTLANAVEKVGHCVQCRDFTESEICTICASSSRDRQQLCVVESPADRLAIEHATGYRGLYFVLQGRLSPLDGIGPRELGLDRLGERLAAGEVTEMIIATNATVEGEATAHYLAQLARQHAVRPSRLAQGMPLGGELEYVDRGTLSHAFGTRSEVL | May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO. | Q2P6V6 |
Q0RRF4 | GCS21_FRAAA | Gamma-glutamylcysteine synthetase 2-1 | Frankia | MQIPFSSSTSSSLGIEWELQLVDQQSRELRGEATLILDELRAKVGEREAAKAKHELFESTVEVITGVCGSVGEATADLAGTVSLLRDLAERRGVGLMCSGTHPTSDYAGQRITDDNRYSRLVSQMQWLARRLLIFGVHVHVGVRSPDKAMPIMNALMVYIPHFLALSASSPFWLGGDTGLASSRSQVFASLPTAGLPYPLEDWPRFESFMETLIAAGTIETIREVWWDIRPHPNFGTVELRICDGLPTLLEVGAVAALAQCLVDRMNTQIDRGYRLPTPQRWLVQENKWRAARYGLDAQILIDDRGGVRSVRDDLVDLVE... | ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity. | Q0RRF4 |
A5EWF5 | CLPP_DICNV | Endopeptidase Clp | Dichelobacter | MDIMNNLPIPMVVEQTGRGERAFDIYSRLLKERVVFLVGEVNDASANLVVAQLLFLEAENPDQDIHFYINSPGGSVTAGMSIYDTMQFIKPDVSTMVLGQAASMGAVLLAAGAAGKRYALPNSRVMIHQPLGGFRGQASDIDIHAREILFIRERLNQILAKHSGQDLETISRDTERDNFMSAERAQEYGLVDAILTHRESVSA | 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. | A5EWF5 |
A4QJD3 | PETL_AETCO | Cytochrome b6-f complex subunit VI | Aethionema | MPTLTSYFGFLLAALTITSALFIGLSKIRLI | Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetL is important for photoautotrophic growth as well as for electron transfer efficiency and stability of the cytochrome b6-f complex... | A4QJD3 |
C5CUL9 | SURE_VARPS | Nucleoside 5'-monophosphate phosphohydrolase | Variovorax | MKILISNDDGFQAPGIVALHDALKDIADVEVVAPEHNNSAKSNALTLAAPLYVHKAHNGFRYVTGTPADCVHIALKGLLGYRPDLVVSGINNGANMGDDTIYSGTVGAAMEAYLFGIPAIAFSQIEKGWAHVDAAAQVARRLVQQIERERMLDGGAFLLNVNVPNRPLQELKPIQVCRLGRRHSAEKVITQESPRGETMYWIAGAGGAKDSGEGTDFHATAAGHIALTPLQIDLTDHANLGQWRETVARLGN | Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates. | C5CUL9 |
A3Q3A2 | NUCS_MYCSJ | Endonuclease NucS | unclassified Mycobacterium | MRLVIAQCTVDYVGRLTAHLPSARRLLLIKSDGSVSVHADDRAYKPLNWMSPPCRLSEESGDPHPVWVVENKTGEQLRITVEEIEHDSSHDLGVDPGLVKDGVEAHLQKLLAEHVELLGAGYTLVRREYMTAIGPVDLLCRDETGRSVAVEIKRRGEIDGVEQLTRYLELLNRDTLLAPVSGVFAAQQIKPQARTLANDRGIRCLILDYDQMRGMDSDEYRLF | Cleaves both 3' and 5' ssDNA extremities of branched DNA structures. | A3Q3A2 |
C4PWA1 | PPZP_STRAQ | Dihydro-PCA prenyltransferase | Streptomyces | MSESAELTELYSAIEETTRVVGAPCRRDTVRPILTAYEDVIAQSVISFRVQTGTSDAGDLDCRFTLLPKDMDPYATALSNGLTAKTDHPVGSLLEEVHRQFPVDCYGIDFGAVGGFKKAWSFFRPDSLQSASDLAALPSMPSGVSENLGLFDRYGMTDTVSVVGFDYAKRSVNLYFTGASPESFEPRGIQAILRECGLPEPSDELLRFGEEAFAIYVTLSWDSQKIERVTYSVNTPDPMALPVRIDTRIEQLVKDAPLGSAGHRYVYGVTATPKGEYHKIQKYFQWQSRVEKMLTADAG | Involved in the biosynthesis of prenylated phenazines. Catalyzes the transfer of a dimethylallyl moiety to C-9 of 5,10-dihydrophenazine 1-carboxylate (dihydro-PCA). Specific for both dimethylallyl diphosphate and dihydro-PCA. | C4PWA1 |
B5YZ82 | KEFF_ECO5E | Quinone oxidoreductase KefF | Escherichia | MILIIYAHPYPHHSHANKRMFEQARTLEGVEIRSLYQLYPDFNIDIAAEQEALSRADLIVWQHPMQWYSIPPLLKLWIDKVFSHGWAYGHGGTALHGKHLLWAVTTGGGESHFEIGAHPGFDVLSQPLQATAIYCGLNWLPPFAMHCTFICDDETLEGQARHYKQRLLEWQEAHHG | Regulatory subunit of a potassium efflux system that confers protection against electrophiles. Required for full activity of KefC. Shows redox enzymatic activity, but this enzymatic activity is not required for activation of KefC. | B5YZ82 |
B4JSI3 | RRF2M_DROGR | Elongation factor G 2, mitochondrial | Hawaiian Drosophila | MLQYCLLRRYRFLLRQHAQVIKRCYSGDIRNIGILAHIDAGKTTTTERMLFYAGKTRSLGEVHRGNTVTDYLAQERERGITICSSAVTFNWNGKRINLLDTPGHIDFTMEVEQSLYAVDGVIVVLDGTAGVEAQTVTVWTQADKHKLPRLVFVNKMDRPDANFEKCIVDLTEKLDAKPICTQYPTKSADGQLGIFDVITMEQMTWQQNDLGRNYSKVKLESSTELQEKRNELIDQLSGLDDELADVVISTESFDKVSNELIGQALRRATCQQKVVPVLLGSAYKNIGIQPLMDAVNAYLPMPEERNQMYDCFGNDFAGKV... | Mitochondrial GTPase that mediates the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. Not involved in the GTP-dependent ribosomal translocation step during translation elongation. | B4JSI3 |
A8FJX5 | MNTP_CAMJ8 | Putative manganese efflux pump MntP | Campylobacter | MDFYSLIFLSCALGMDAFAVSLCKGFSVKKLHLKHYLIVGIYFGGFQALMPTIGYFIGITFASFIASIDHWIAFILLSLIGLKMIKESLENENCDSNANQFGFKTMLALAIATSIDALAVGVSFAFLNVNLLLAIFLIGIITFILCIIALKIGNKFGIYLKNKAELLGGLVLIILGVKILIEHLFFD | Probably functions as a manganese efflux pump. | A8FJX5 |
Q929X9 | MURE_LISIN | UDP-N-acetylmuramyl-tripeptide synthetase | Listeria | MKLKELMQAIPVYTGEASAAIEVNQIAQDSRKVQPGTLFICIDGEIVDGHQFADRAVQLGAVAIIAEKQLDVSVPVLYVRDSKRAMAMLADYFYGSPTQALKLVGITGTNGKTTVSHLVEQIVRENGEQTGLIGTMYRKIGDEILETKNTTPDSLTLQETFRDMLLSGVSTAVMEVSSHALVQGRVYGSDYDVAVFMNLSQDHLDYHHTMEEYAYAKSLLFAQLGNSYNLSNPKIAVLNADDKESVRMQTATAAHIITFGIKEPADFSASNIQITSHGSTFDLKTPVGDFALKIKMIGNFSVYNVLAAIATSFALRIPVI... | Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. | Q929X9 |
P53214 | MTL1_YEAST | MID two-like protein 1 | Saccharomyces | MASCNPTRKKSSASSLSMWRTILMALTTLPLSVLSQELVPANSTTSSTAPSITSLSAVESFTSSTDATSSASLSTPSIASVSFTSFPQSSSLLTLSSTLSSELSSSSMQVSSSSTSSSSSEVTSSSSSSSISPSSSSSTIISSSSSLPTFTVASTSSTVASSTLSTSSSLVISTSSSTFTFSSESSSSLISSSISTSVSTSSVYVPSSSTSSPPSSSSELTSSSYSSSSSSSTLFSYSSSFSSSSSSSSSSSSSSSSSSSSSSSYFTLSTSSSSSIYSSSSYPSFSSSSSSNPTSSITSTSASSSITPASEYSNLAKTIT... | Involved in cell integrity signaling during vegetative growth at elevated temperature. Acts positively on the PKC1-MAPK pathway. Cell membrane sensor of oxidative stress in the cell integrity pathway upstream of PKC1. Required to transmit the oxidative signal to SLT2 and to restore the correct actin organization follow... | P53214 |
Q8IMQ6 | GR97A_DROME | Putative gustatory receptor 97a | Sophophora | MRFLRRQTRRLRSIWQRSLPVRFRRGKLHTQLVTICLYATVFLNILYGVYLGRFSFRRKKFVFSKGLTIYSLFVATFFALFYIWNIYNEISTGQINLRDTIGIYCYMNVCVCLFNYVTQWEKTLQIIRFQNSVPLFKVLDSLDISAMIVWRAFIYGLLKIVFCPLITYITLILYHRRSISESQWTSVTTTKTMLPLIVSNQINNCFFGGLVLANLIFAAVNRKLHGIVKEANMLQSPVQMNLHKPYYRMRRFCELADLLDELARKYGFTASRSKNYLRFTDWSMVLSMLMNLLGITMGCYNQYLAIADHYINEEPFDLFL... | Probable gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates. | Q8IMQ6 |
A7UI11 | LAP1_TRIEQ | Leucyl aminopeptidase 1 | Trichophyton | MKLLSVLALSATATSVLGASIPVDTRAQKFLIELAPGETRWVTEEEKWELKQKGQDFFDITDEEVGFTAAVAQPAIAYPTSIRHADAVNAMIATLSKENMQRDLTKLSSFHNRYYKSDYGKQSATWLQQQVQAVINSSGASRYGAKVVSVRHNFVQHSIVATIPGRSPEIVVVGAHQDSINQRSPMTGRAPGADDNGSGSVTILEALRGVLQDQTIVQGKAANTIEFHWYAGEEAGLLGSQAIFANYKQTGKKVKGMLNQDMTGYIKGMVDRGLKVSFGIITDNVSTSLTSFIRMVITKYCSIPTIDTRCGYACSDHASA... | Extracellular aminopeptidase which contributes to pathogenicity. | A7UI11 |
Q606H9 | RS18_METCA | 30S ribosomal protein S18 | Methylococcus | MVRQFKRRRYCRFTAEDVKEIDYKDLDTLREYVSETGKIVPSRITGTSAKYQRQLATAIKRARFLALLPFCDAHEQ | 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. | Q606H9 |
B3N1G9 | RS3A_DROAN | 40S ribosomal protein S3a | Sophophora | MAVGKNKGLSKGGKKGGKKKVVDPFSRKDWYDVKAPNMFQTRQIGKTLVNRTQGQRIASDYLKGRVFEVSLADLQKDIDPERSFRKFRLIAEDVQDRNVLCNFHGMDLTTDKYRSMVKKWQTLIEAIVEAKTIDGYLLRVFCIGFTAKDQQSQRKTCYAQQSQVRKIRARMTDIINNEVSGADLKQLVNKLALDSIAKDIEKSCQRIYPLHDVYIRKVKVLKKPRFDVSKLLELHGDGGGKSSDAVVSTEGAVIDRPEGYEPPVQEAV | Essential for oogenesis; required for late follicle cell development. | B3N1G9 |
Q820H8 | LEPA_NITEU | Ribosomal back-translocase LepA | Nitrosomonas | MIQHIRNFSIIAHIDHGKSTLADRIIQFCGGLSDREMEDQVLDSMDLERERGITIKAQTAALHYQAKDGKNYLLNLIDTPGHVDFSYEVSRSLSACEGALLVVDASQGVEAQTVANCYTAIEQGVEVIPVLNKIDLPAADPDRVIAEVEDIIGIEAKGALRISAKTGEGVDQVLEMIVAQIPPPEGDVDAPLKALIIDSWFDSYVGVVMLVRVVDGVLRPGNKILLMSSKANYLCEEVGVFQPKAVSHKSLSAGEVGFIISGIKDLKSAKVGDTVTLADRPAGEPLAGFKEIKPQVFAGLYPVESNQYDALRAALEKLQL... | Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-t... | Q820H8 |
Q891G4 | CH60_CLOTE | Chaperonin-60 | Clostridium | MEMAKSIMFGEDARRSMQKGVDILADTVKVTMGPKGRNVVLDKKFGAPLITNDGVTIAREIELEDAYENMGAQLVKEVATKTNDVAGDGTTTATLLAQAIIREGLKNVTGGANPMLVRRGIQMAVEEAVKGIKEISKPVEGKEDIARVAAISADDKEIGKLIADAMEKVGNEGVITVEESNTMGTELDVVEGMQFDRGYVSPYMVTDTEKMEASLDDAYILITDKKITNIQEILPVLEQIVQQGKRLLIISEDIEGEALATLVVNKLRGTFTCVAVKAPGFGDRRKEMLEDIATLTGGQVISEEIGRDLKDVTVDMLGRA... | Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. | Q891G4 |
Q96T68 | SETB2_HUMAN | SET domain bifurcated 2 | Homo | MGEKNGDAKTFWMELEDDGKVDFIFEQVQNVLQSLKQKIKDGSATNKEYIQAMILVNEATIINSSTSIKGASQKEVNAQSSDPMPVTQKEQENKSNAFPSTSCENSFPEDCTFLTTENKEILSLEDKVVDFREKDSSSNLSYQSHDCSGACLMKMPLNLKGENPLQLPIKCHFQRRHAKTNSHSSALHVSYKTPCGRSLRNVEEVFRYLLETECNFLFTDNFSFNTYVQLARNYPKQKEVVSDVDISNGVESVPISFCNEIDSRKLPQFKYRKTVWPRAYNLTNFSSMFTDSCDCSEGCIDITKCACLQLTARNAKTSPL... | Histone methyltransferase involved in left-right axis specification in early development and mitosis. Specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). H3K9me3 is a specific tag for epigenetic transcriptional repression that recruits HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Contributes to... | Q96T68 |
Q9CQI3 | GMFB_MOUSE | Glia maturation factor beta | Mus | MSESLVVCDVAEDLVEKLRKFRFRKETHNAAIIMKIDKDERLVVLDEELEGVSPDELKDELPERQPRFIVYSYKYQHDDGRVSYPLCFIFSSPVGCKPEQQMMYAGSKNKLVQTAELTKVFEIRNTEDLTEEWLREKLGFFH | This protein causes differentiation of brain cells, stimulation of neural regeneration, and inhibition of proliferation of tumor cells. | Q9CQI3 |
Q7VGC7 | RS5_HELHP | 30S ribosomal protein S5 | Helicobacter | MEINREEFSEVVVNIGRVTKVVKGGRRFRFNALVVVGNKNGLVGFGLGKAKEVPDAIKKAIDDAFKNIIKVNIKGTTIAHDIEHKYNASRILLKPASEGTGVIAGGSTRPVIELAGIKDILTKSLGSNNPYNVVRATIDALARIKA | Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. | Q7VGC7 |
A4WBI4 | MGRB_ENT38 | PhoP/PhoQ regulator MgrB | Enterobacter | MKKIRWVILIIVLIACVILWTQTINVMCDQDVQFFSGICAINQFIPW | PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing. MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. Represses PhoP/PhoQ signaling, possibly by binding to the periplasmic domain of PhoQ, altering its activity and that of downstream effector PhoP. | A4WBI4 |
Q1IJZ0 | HLDE_KORVE | D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase | Candidatus Koribacter | MSTNVADLLHTIKNNWCDRSILVVGDVMLDQYIWGDVGRISPEAPVPIVRATHRTEQPGGAANVALNIARLGARATIVGFTGTDDNERALKDYLSSNRVEADFVSCEGFPTITKLRILSGRQQMLRLDNERAESRPSTAYQKLIERALHHLPQSDALILSDYAKGVLLPEVCQTLIQAAAQRKIPVLVDPKNVDFSRYRGATTISPNLGELALAARVDLENLNDLLYAAQQMVRNLGLSFLTATLGEKGIALVTRDKTTISAAVARQVFDVSGAGDAVIATLSLSLASGLDPELGVHLANLAGAIVVSKVGTAPVEQYEL... | Catalyzes the ADP transfer from ATP to D-glycero-beta-D-manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose. | Q1IJZ0 |
Q21253 | GELS1_CAEEL | Gelsolin-like protein 1 | Caenorhabditis | MGGTSLDPALAEIGKKNGLLVWRINKFVLEPVPEVDHGVFYIGDAYIALYQKYDGCWDVHFWLGKNASTDEIGVAAIKTVEIDDSLGGIPTQHREIQNYESPLFLSYFPDGIRYVSGGYESGYRHVDDQFKNWKPHLFHCKGKRNVRCTEVECEVNSLNLGDVFILDLGKDLYVWMPPESGRLERIKGMARAKNIADHERMGIPKVHILDDVEWDNDSTFWSYFGGVSSVRKVSKGKDDDDNYWKRLTEQITLWKVSDASGAAKVSMVSQGENIRKEQLDPKDAFILDAINGGIFVWIGHECTLEERSKALIWGQNYLKQ... | Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping) . Binds actin but does not nucleate actin polymerization, albeit slows down elongation by blocking the barbed ends . By promoting actin depolymerizati... | Q21253 |
A4QGM5 | ORN_CORGB | Oligoribonuclease | Corynebacterium | MSESENNTTPAVAARDDRLVWVDLEMTGLDLKRHVIVEVAALVTDANLNVLGEGVDLVVHATEEELAQMDDFVTNMHESSGLTEQIRESAVTLKEAEDAVLALIEKHCDPAHPAPLAGNSIATDRAFIREQMPRLDEALHYRMVDVSSVKELARRWYPRVYYKQPEKGLAHRALADIVESIRELDYYRRSFFVAEPGPTSEQCADDAQAAVDRFAPYFD | 3'-to-5' exoribonuclease specific for small oligoribonucleotides. | A4QGM5 |
B7GVX2 | AROE_ACIB3 | Shikimate dehydrogenase (NADP(+)) | Acinetobacter calcoaceticus/baumannii complex | MTKQFAVIGNPIEQSRSPELHHAFAEKTGVDLNYQKRLAPLDGFESSMRSFFAEGGSGMNVTVPFKEQAFALCDVLTERAQIAKAVNTLWMENGKLHGDNTDGQGLVAAIQALEWNLENTTILILGAGGATRGVIYPLVQAGAQKIVIANRTLARAEQLVDDLKTAVPQAQLQAISLNDLEGDFDIMINATSTSLSGDALQLPEKLQFKYAYEMAYGKPSSFIDQAKQRNVPYAEGFGMLVGQAIEAFYIWNGVRPQLKDFL | 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). | B7GVX2 |
Q7VGC8 | RL18_HELHP | 50S ribosomal protein L18 | Helicobacter | MTDKVLKRKQLLKVKRKLRTRGKIFGRADKPRVSVFKSNKYFYAQAINDELGVTLASVDGKKLGLGNNKENAKQIANEFATSLKKAKITEVVFDRNGYLYHGVVAAFADTLRENGIKL | This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. | Q7VGC8 |
Q6G7S2 | HLD_STAAS | Delta-toxin | Staphylococcus | MAQDIISTISDLVKWIIDTVNKFTKK | Lyses erythrocytes and many other mammalian cells. | Q6G7S2 |
P29638 | CYB_BAEIN | Ubiquinol-cytochrome-c reductase complex cytochrome b subunit | Baeolophus | FGSLLGICLLTQIITGLLLAMHYTADTSLAFTSVAHTCRNVQFGWLIRNLHANGASFFFICIYFHIGRGIYYGSYLNKETWNIGVILLLTLMATAFVGYVLPWGQMSFWGATVITNLFSAIPYIGQTLVEWAWGGFSVDNPTLTRFFALHFLLPFVIAGLTLVHLTFLHETGSNNPLGIPSDCDKIPFHPYYSTKDILGFALMFILLVSLALFSPNSLGDPENFTPANPLSTPPHIKPEWYFLFAYAILRSIPNKLGGVLALAASVLVLFLLPLLHTSKQRSMTFRPLSQILFWALVANLLILTWVGS | 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... | P29638 |
Q97W59 | IF2B_SACS2 | eIF-2-beta | Saccharolobus | MSSEKEYVEMLDRLYSKLPEKGRKEGTQSLPNMIILNIGNTTIIRNFAEYCDRIRREDKICMKYLLKELAAPGNVDDKGELVIQGKFSSQVINTLMERFLKAYVECSTCKSLDTILKKEKKSWYIVCLACGAQTPVKPL | eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. | Q97W59 |
P15838 | LEGA2_PEA | Legumin A2 basic chain | Pisum | MATKLLALSLSFCFLLLGGCFALREQPEQNECQLERLNALEPDNRIESEGGLIETWNPNNKQFRCAGVALSRATLQHNALRRPYYSNAPQEIFIQQGNGYFGMVFPGCPETFEEPQESEQGEGRRYRDRHQKVNRFREGDIIAVPTGIVFWMYNDQDTPVIAVSLTDIRSSNNQLDQMPRRFYLAGNHEQEFLRYQHQQGGKQEQENEGNNIFSGFKRDFLEDAFNVNRHIVDRLQGRNEDEEKGAIVKVKGGLSIISPPEKQARHQRGSRQEEDEDEDEERQPRHQRGSRQEEEEDEDEERQPRHQRRRGEEEEEDKKE... | This protein found in the seeds of many leguminous and non-leguminous plants is the source of sulfur-containing amino acids in seed meals. | P15838 |
D4GU70 | AGL11_HALVD | Low-salt glycan biosynthesis nucleotidyltransferase Agl11 | Haloferax | MKGVLLSGGTGSRLRPITHTGPKQLVPVANKPVLEYAVEDLKEAGITEIGVILGHKGREEIQNLLGDGSDYGVEITYIVQGNPLGLAHAAGCAKDFVGDDDFVMYLGDNILKEGVVDLVESFESGDFGAGIALQEVENPQQFGIADVDDQGNVTQLIEKPDEPPTNLALIGMYVFSPAVFDAIEQLEPSWRGELEITDAIQSLLEDGYAIDSHVVEGWWKDTGKPEDILEANQLVLEDKSLKKRGTVSDDATVDGRIELAESATIEDGAVVRGPVSIADGAVIKSGTYVGPYTSVGPNSTLEGVHIENSVVIGESSINTS... | Nucleotidyltransferase involved in N-glycan biosynthetic pathway that takes place under low-salt conditions (1.75 M instead of 3.4 M). Participates in the formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and rhamnose. Involved in the addition ... | D4GU70 |
Q8AAN7 | XPT_BACTN | Xanthine phosphoribosyltransferase | Bacteroides | MQLLKKRILQDGKCYEGGILKVDGFINHQMDPVLMKSIGVEFVRRFAATNVNKIMTIEASGIAPAIMTGYLMDLPVVFAKKKSPKTIQNALSTTVHSFTKDRDYEVVISADFLTPNDNVLFVDDFLAYGNAALGILDLIEQSGAKLVGMGFIIEKAFQNGRKILEEKGVRVESLAIIEDLSNCCIKIKDQ | Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis. | Q8AAN7 |
Q8NB50 | ZFP62_HUMAN | Zinc finger protein 62 homolog | Homo | MSHLKTSTEDEEPTEEYENVGNAASKWPKVEDPMPESKVGDTCVWDSKVENQQKKPVENRMKEDKSSIREAISKAKSTANIKTEQEGEASEKSLHLSPQHITHQTMPIGQRGSEQGKRVENINGTSYPSLQQKTNAVKKLHKCDECGKSFKYNSRLVQHKIMHTGEKRYECDDCGGTFRSSSSLRVHKRIHTGEKPYKCEECGKAYMSYSSLINHKSTHSGEKNCKCDECGKSFNYSSVLDQHKRIHTGEKPYECGECGKAFRNSSGLRVHKRIHTGEKPYECDICGKTFSNSSGLRVHKRIHTGEKPYECDECGKAFIT... | May play a role in differentiating skeletal muscle. | Q8NB50 |
Q9I8Q3 | CFC1_CHICK | Cripto-related factor 1 | Gallus | MFWRKHVRILFTVTLIWQAIHLGKGREKEHEKDVKNFNDTAQKQSPKNSVTIIDAFSDMNQSYQSRKQQNSREFVPFTGITESKNLNRNCCQNGGTCILGAFCACPKHFSGRHCELRKCGSIIHGDWVMKGCWLCRCLYGTLKCLSQNTQDGCELRREEEIIRLYSNGLRLQQTMSALICLLTFLLELCCWQL | May play a role in mesoderm and/or neural patterning during gastrulation. | Q9I8Q3 |
Q9QWN8 | SPTN2_RAT | Spectrin-like protein GTRAP41 | Rattus | MSSTLSPTDFDSLEIQGQYSDINNRWDLPDSDWDNDSSSARLFERSRIKALADEREAVQKKTFTKWVNSHLARVTCRVGDLYSDLRDGRNLLRLLEVLSGETLPKPTKGRMRIHCLENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLVWTIILRFQIQDISVETEDNKEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLLDFESLKKCNAHYNLQNAFNLAEKELGLTKLLDPEDVNVDQPDEKSIITYVATYYHYFSKMKALAVEGKRIGKVLDHAMEAEHLVEKYESLASELLQW... | Probably plays an important role in neuronal membrane skeleton. | Q9QWN8 |
Q99J83 | ATG5_MOUSE | APG5-like | Mus | MTDDKDVLRDVWFGRIPTCFTLYQDEITEREAEPYYLLLPRVSYLTLVTDKVKKHFQKVMRQEDVSEIWFEYEGTPLKWHYPIGLLFDLLASSSALPWNITVHFKSFPEKDLLHCPSKDAVEAHFMSCMKEADALKHKSQVINEMQKKDHKQLWMGLQNDRFDQFWAINRKLMEYPPEENGFRYIPFRIYQTTTERPFIQKLFRPVAADGQLHTLGDLLREVCPSAVAPEDGEKRSQVMIHGIEPMLETPLQWLSEHLSYPDNFLHISIVPQPTD | (Microbial infection) May act as a proviral factor. In association with ATG12, negatively regulates the innate antiviral immune response by impairing the type I IFN production pathway upon vesicular stomatitis virus (VSV) infection. | Q99J83 |
P13111 | MERR_SERMA | Mercuric resistance operon regulatory protein | Serratia | MEKNLENLTIGVFAKAAGVNVETIRFYQRKGLLPEPDKPYGSIRRYGEADVTRVRFVKSAQRLGFSLDEIAELLRLDDGTHCEEASSLAEHKLQDVREKMTDLARMETVLSELVFACHARQGNVSCPLIASLQGEKEPRGADAV | Mediates the mercuric-dependent induction of mercury resistance operon. In the absence of mercury MerR represses transcription by binding tightly to the mer operator region; when mercury is present the dimeric complex binds a single ion and becomes a potent transcriptional activator, while remaining bound to the mer si... | P13111 |
Q55190 | NHAS3_SYNY3 | Sodium/proton antiporter NhaS3 | unclassified Synechocystis | MFMNPLLPPLWPMIATAVETETEIAPLVLAGVLLSLVVIYFASKLGGEVCLRLNLPPVLGELVGGVLVGVSALKLLLFPEGGLAPEDSLVIQLLMGSADLSPEAAQSVFSAQSEVISVISELGVIILLFEIGLESNLKELIRVGPQAAIVAVVGVVTPFSLGTIGLMTIFGVAAIPAIFAGAALTATSIGITAKVLAEINRLSSNEGQIIIGAAVLDDILGIIVLAVVGSLVKTGEIQISNIIYLILSATGFVVGSILIGRLLSPFYVSLVNRMKTRGQLLLVSICVAFVLSYIAQIVQLEAILGSFAAGLILAETEKRE... | Na(+)/H(+) antiporter that transports sodium from the cytoplasm into the thylakoid lumen in exchange for protons. Contributes to sodium homeostasis and tolerance. Has also Li(+)/H(+) antiport activity under K(+)-free conditions, but not under K(+)-rich conditions. | Q55190 |
Q43292 | RL372_ARATH | 60S ribosomal protein L37-2 | Arabidopsis | MTKGTGSFGKRRNKSHTLCVRCGRRSFHIQKSRCSACAYPAARKRTYNWSVKAIRRKTTGTGRMRYLRNVPRRFKTGFREGTEAKPRNKGVASSA | Binds to the 23S rRNA. | Q43292 |
Q0TA77 | RPOC_ECOL5 | Transcriptase subunit beta' | Escherichia | MKDLLKFLKAQTKTEEFDAIKIALASPDMIRSWSFGEVKKPETINYRTFKPERDGLFCARIFGPVKDYECLCGKYKRLKHRGVICEKCGVEVTQTKVRRERMGHIELASPTAHIWFLKSLPSRIGLLLDMPLRDIERVLYFESYVVIEGGMTNLERQQILTEEQYLDALEEFGDEFDAKMGAEAIQALLKSMDLEQECEQLREELNETNSETKRKKLTKRIKLLEAFVQSGNKPEWMILTVLPVLPPDLRPLVPLDGGRFATSDLNDLYRRVINRNNRLKRLLDLAAPDIIVRNEKRMLQEAVDALLDNGRRGRAITGSN... | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | Q0TA77 |
Q9DCM2 | GSTK1_MOUSE | Glutathione S-transferase subunit 13 | Mus | MGPAPRILELFYDVLSPYSWLGFEVLCRYQHLWNIKLQLRPTLIAGIMKDSGNQPPAMVPRKGQYIFKEIPLLKQFFQVPLNIPKDFFGETVKKGSINAMRFLTTVSMEQPEMLEKVSREIWMRVWSRDEDITEYQSILAAAVKAGMSTAQAQHFLEKISTQQVKNKLIENTDAACKYGAFGLPTTVAHVDGKTYMLFGSDRLELLAYLLGEKWMGPVPPTANARL | Glutathione S-transferase that catalyzes the conjugation of glutathione to exogenous and endogenous compounds. | Q9DCM2 |
Q7MIV9 | AQPZ_VIBVY | Aquaporin Z | Vibrio | MNKYLAELFGTFWLVLGGCGSAVLAAAFPDVGIGLLGVSLAFGLTVLTMAFAIGHISGCHLNPAVTIGLWAGGRFEAKEIVPYILAQVIGGVIAGGVLYTIASGQMGFDATSSGFASNGYGEHSPGGYSLTSALVTEIVMAMMFLLVILGATDQRAPQGFAPIAIGLCLTLIHLISIPVTNTSVNPARSTGVALYVGDWATAQLWLFWVAPILGALLGAVAYKLISGSNKD | Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity. | Q7MIV9 |
P59176 | GPMI_SHIFL | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase | Shigella | MSVSKKPMVLVILDGYGYREEQQDNAIFSAKTPVMDALWANRPHTLIDASGLEVGLPDRQMGNSEVGHVNLGAGRIVYQDLTRLDVEIKDRAFFANPVLAGAVHKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPRSAESSLKKFEEKFAALGKGRVASIIGRYYAMDRDNRWDRVEKAYDLLTLAQGEFQADTAVAGLQAAYARDENDEFVKATVIRAEGQPDAAMEDGDALIFMNFRADRAREITRAFVNADFDGFARKKVVNVDFVMLTEYAADIKTAVAYPPASLVNTFGEW... | Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. | P59176 |
A7H0A8 | PURA_CAMC5 | IMP--aspartate ligase | Campylobacter | MRKADLVVGVQWGDEGKGKIVDMLGLNYDMICRSQGGHNAGHTIWVDGVRYAMHLIPSGILHKNIVNVIGNGVVVSPDVLIDEMAQFDHLEGRFYISDRAHLNLTHHGLIDQAKERLKGDKAIGTTGKGIGPTYADKISRSGHRVGELLEPERLCEALMSDFEMNKSLFNALGVKIPKRDELLEELKRYKEALAPYITNTTRLVWKALDDGKKVLLEGAQGTLLDIDHGTYPYVTSSNTISAGACTGLGLNPKEMGEVIGVIKAYTTRVGFGPFPTEDKGSDGDKMCEVGKEFGTTTGRRRRCGWFDAVSVKYASRLDAV... | Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. | A7H0A8 |
Q17YA2 | AMIE_HELAH | Acylamide amidohydrolase | Helicobacter | MRHGDISSSPDTVGVAVVNYKMPRLHTKEQVLENCRNIAKVIGGVKQGLPGLDLIIFPEYSTHGIMYDKQEMFDTAVSIPGEETAILAEACKKNKVWGVFSLTGEKHEQAKKNPYNTLILVNDKGEIVQKYRKILPWCPIECWYPGDKTYVVDGPKGLKVSLIICDDGNYPEIWRDCAMRGAELIVRCQGYMYPAKEQQIAIVKAMAWANQCYVAVANATGFDGVYSYFGHSSIIGFDGHTLGECGEEENGIQYAQLSVQQIRDARKYDQSQNQLFKLLHRGYSGVFASGDGDKGVAECPFEFYKTWVNDPKKAQENVEK... | Also exhibits in vitro acyl transferase activity, transferring the acyl moiety of short-chain amides to hydroxylamine to form hydroxamates. | Q17YA2 |
B9J8M0 | UREE_AGRRK | Urease accessory protein UreE | Agrobacterium tumefaciens complex | MQRVTSYLPAGTPSSNPIDRVELPHDLRHLRRKLLHLENGEMVMLDLKEPVLFANGDLLVREDGELIEIVAAPEKLFEIKPRNRLHLIELAWHLGNRHLSAQIEEERILILRDHVIRAMLEGLGATVTEVSEPFQPARGAYHAHGGHSHGHDHGHSHGHDHHDHSHD | Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly. | B9J8M0 |
B4NFY1 | EI3G2_DROWI | Eukaryotic translation initiation factor 3 subunit 4-2 | Sophophora | MKPIKTSWADEVEADYVDGLPPAKEYIEGEYKYVTEYKYNEDGKKIKVVRTFKIKKQVVSKAVAKRRNWVKFGESSSDKPGPNSQTTMAAEEIFMLFMGSKEFEQTNELQIDPGKNIAKCRICNGEHWSVNCPYKGTAMDSKTMMENKATAAAAAVGDPKSGKYVPPFLKEGGASGKPWARERDDSSAVRISNLSESMTEVDLEELVKKIGPHTKMYLAREKNTGLCKGFAYVHFKFRQDAAAAIEILNGHGYDHLILCVEWSKPQNQ | RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and... | B4NFY1 |
A6VBU6 | LSPA_PSEA7 | Signal peptidase II | Pseudomonas | MPEVDRFGRLPWLWITVLVFVLDQVSKAFFQAELSMYQQVVVIPDLFSWTLAYNTGAAFSFLADSSGWQRWLFALIAIVVSAILVVWLKRLKKGETWLAVALALVLGGALGNLYDRMVLGHVVDFILVHWQNRWYFPAFNLADSAITVGAVMLALDMFRSKKSGEAAHG | This protein specifically catalyzes the removal of signal peptides from prolipoproteins. | A6VBU6 |
P32778 | VSP24_BORHE | Variable major outer membrane lipoprotein 24 | Borrelia | MRKRISAIIMTLFMVFMSCNNGGPELKSDEVAKSDGTVLDLAKVSKKIKEASAFAASVKEVETLVKSVDELAKAIGKKIKNDGGLDTEAGQNGSLIAGVHSVVSAVKIKVGALETTSGISNELKTKITEVKSKAEAFLNKLKDGHTELGKKDASDDDTKKAIKKDNSDKTKGASELEALNTAVDALLKAAEGEVEAAIKELTAPVKAEKPSQNN | The Vlp and Vsp proteins are antigenically distinct proteins, only one vlp or vsp gene is transcriptionally active at any one time. Switching between these genes is a mechanism of host immune response evasion. | P32778 |
Q65JH5 | PNP_BACLD | Polynucleotide phosphorylase | Bacillus | MGQEKHVFSIDWAGRKLTVETGQLAKQANGAVMVRYGDTAVLSTATASKEPKTVDFFPLTVNYEERLYAVGKIPGGFIKREGRPSEKAILASRLIDRPIRPLFADGFRNEVQVVSIVMSVDQDCSSEMAAMFGSSLALCVSDIPFEGPIAGVTVGRVDNKFIINPTLEQLEKSDIHLVVAGTKDAINMVEAGADEVPEEIMLEAIMFGHEEIKRLIAFQEEIVAAVGKEKSEITLYEIDSDLKEKVRGMAESNLLKAIQVHEKHAREDAISEVKNEVLAKFEEEEHDEETLKQVKDILSQLVKNEVRRLITEEKVRPDGR... | Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. | Q65JH5 |
D0B707 | PCS_BRUME | CDP-diglyceride-choline O-phosphatidyltransferase | Brucella | MGGQKEMADSVKTKLTGKLKAKKVTAPQAKAFSVHLLTASGSFLAFLSVVAASDGRYTAMWWWLGLALFVDGIDGPIARKLEVKYVLPNWSGELLDSIIDYVTYVLIPAFALYQSGFMGTNLSFISGAIIVVSSAIYYADTGMKTKENFFKGFPVVWNMVVFTLFIVRPGEWVAFGTVVASAILSFLPINFLHPVRVVRLRPLNLTIFLLWCAFGVIALYYMLDAPLWVRIGISVTGLYIYFIGAIMQLFPSLGREAALAKARKLVEKQQKSGEAP | Condenses choline with CDP-diglyceride to produce phosphatidylcholine and CMP. | D0B707 |
P43674 | YCAL_ECOLI | Metalloprotease YcaL | Escherichia | MKNTKLLLAIATSAALLTGCQNTHGIDTNMAISSGLNAYKAATLSDADAKAIANQGCAEMDSGNQVASKSSKYGKRLAKIAKALGNNINGTPVNYKVYMTSDVNAWAMANGCVRVYSGLMDMMNDNEIEGVLGHELGHVALGHSLAEMKASYAIVAARDAISATSGVASQLSRSQLGDIAEGAINAKYSRDKESEADDFSFDLLKKRGISTQGLVGSFETLASLDGGRTQSMFDSHPPSTERAQHIRDRIASGK | Involved in the degradation of the LPS-assembly protein LptD. Degrades LptD that have engaged the Bam complex but are stalled at an early step in the outer membrane protein assembly process. | P43674 |
Q7NQG7 | RL6_CHRVO | 50S ribosomal protein L6 | Chromobacterium | MSRVAKNPVAIPAGVEVKFGAADVTVKGALGSLSTALCNDVEVKLDNGQLTFAAKNDSKFARAMSGTLRALLNNMVNGVSKGFEKKLQLVGVGYRAQAQGDTLNLSLGFSHPVAHKMPAGIKVETPTQTEILVKGADKQLVGQVAAEIRAYRSPEPYKGKGVRYADEVVVLKETKKK | This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. | Q7NQG7 |
Q6AD41 | CH10_LEIXX | Chaperonin-10 | Leifsonia | MSVSIKPLEDRIVIKQVEAEQTTASGLVIPDTAKEKPQEGVVEAVGPGRIDDNGNRVPLDVAVGDKVIYSKYGGTEVKFGGQDYLVLSARDVLAVVVR | Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of ... | Q6AD41 |
Q827Q6 | PYRD_STRAW | Dihydroorotate oxidase | Streptomyces | MYKLFFRLVFKRMDPEQAHYLAFRWIRLAARIPVLRTFVAAALAPRFKELRTEAFGLRMHGPFGLAAGFDKNAVAVDGMSMLGFDHVEIGTVTGEPQPGNPKKRLFRLVPDRALINRMGFNNEGSAAVAARLAAREAVFRTVVGVNIGKTKVVPEEEAADDYVKSTERLARHADYLVVNVSSPNTPGLRNLQATEALRPLLSAVREAADRTVTERRVPLLVKIAPDLADDDIDAVADLAVELGLDGIIATNTTIAREGLGLKSEPTLVKETGGLSGAPLKARSLEVLSRLYARVGDRITLVGVGGIENAEDAWQRILAGA... | Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. | Q827Q6 |
C1A3F2 | SUCC_RHOE4 | Succinyl-CoA synthetase subunit beta | Rhodococcus erythropolis group | MDLFEYQAKELFAKHGVPTSAGRVTDTVAGAREIAEEIGKPVMVKAQVKVGGRGKAGGVKYSPDVDAAVANAEAILGLDIKGHVVKKLLVAEASDIAEEYYISFLLDRTNRTYLAMCSVEGGVEIEVTAEENPDALAKIPVDAVKGVDLAFARSIAEAGKLPAEVLDAAAVTIQKLWEVFINEDALLVEVNPLVRTPDDQILALDGKVTLDENAAFRQPGHEAFEDRDATDPLELKAKENDLNYVKLDGEVGIIGNGAGLVMSTLDVVAYAGENHGGVKPANFLDIGGGASAAVMAAGLDVILNDAQVKSVFVNVFGGIT... | Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinat... | C1A3F2 |
Q7U3T6 | RL11_PARMW | 50S ribosomal protein L11 | Parasynechococcus marenigrum | MAKKVTAVIKLALQAGKANPAPPVGPALGQHGVNIMMFCKEYNARTQDKAGFVIPVEISVYEDRSFTFITKTPPASVLITKAAKIEKGSGESAKGNVGSINRAQLEEIAKTKLPDLNCTSVESAMRIIEGTARNMGVSISD | Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | Q7U3T6 |
P9WMR3 | DNAB_MYCTU | Mtu dnaB intein | Mycobacterium tuberculosis complex | MAVVDDLAPGMDSSPPSEDYGRQPPQDLAAEQSVLGGMLLSKDAIADVLERLRPGDFYRPAHQNVYDAILDLYGRGEPADAVTVAAELDRRGLLRRIGGAPYLHTLISTVPTAANAGYYASIVAEKALLRRLVEAGTRVVQYGYAGAEGADVAEVVDRAQAEIYDVADRRLSEDFVALEDLLQPTMDEIDAIASSGGLARGVATGFTELDEVTNGLHPGQMVIVAARPGVGKSTLGLDFMRSCSIRHRMASVIFSLEMSKSEIVMRLLSAEAKIKLSDMRSGRMSDDDWTRLARRMSEISEAPLFIDDSPNLTMMEIRAK... | The intein is an endonuclease. | P9WMR3 |
A9MHM3 | EX7L_SALAR | Exodeoxyribonuclease VII large subunit | Salmonella | MLSSQTSSIFTVSRLNQTVRLLLEQEMGQVWISGEISNFTQPASGHWYFTLKDDTAQVRCAMFRNSNRRVTFRPQHGQQVLVRANITLYEPRGDYQIIVESMQPAGEGLLQQKYEQLKAKLQAEGLFDQQYKHPLPSPAYCVGVITSKTGAALHDILHVLKRRDPSLPVIIYPAAVQGEDAPGQIVRAITLANARKECDVLIVGRGGGSLEDLWSFNDERVARAIFASTIPVVSAVGHETDVTIADFVADLRAPTPSAAAEVVSRNQQELLRQMQTACQRLEMAMDYYLANRQRRFSQLYHRLQQQHPQLRLARQQTTLE... | Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. | A9MHM3 |
Q8DY84 | YIDC2_STRA5 | Membrane protein YidC 2 | Streptococcus | MKKTLKRILFSSLSLSMLLLLTGCVSVDKAGKPYGVIWNTLGVPMANLITYFAQHQGLGFGVAIIIVTVIVRVVILPLGLYQSWKASYQAEKMAYFKPLFEPINERLRNAKTQEEKLAAQTELMTAQRENGLSMFGGIGCLPLLIQMPFFSAIFFAARYTPGVSSATFLGLNLGQKSLTLTVIIAILYFVQSWLSMQGVPDEQRQQMKTMMYLMPIMMVFMSISLPASVALYWFIGGIFSIIQQLVTTYVLKPKLRRKVEEEYTKNPPKAYKANNARKDVTNSTKATESNQAIITSKKTNRNAGKQKRRG | Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. | Q8DY84 |
C9RGE3 | ARFB_METVM | Formamide hydrolase | Methanocaldococcus | MVEIRLSSGKILNKKVHKIGVIALGSFLENHGAVLPIDTDIKIASYIALNASILTGAKFLGVVIPSTEYEYVKHGIHNKVDEILDYLRFMINWGKKIGVEEIIIVNCHGGNVLIEEHLKNLEKELDVSIEMINITFTHASTEEVSVGEVIGISDVKRLEEHTNFEKYPEVGMVGLKEARRNNPIIDQEAKEVETSGVKVDRELGRSILKNAIEKVVKKIEEKIAKK | Catalyzes the hydrolysis of the formamide of 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-monophosphate (FAPy) to form 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (APy). | C9RGE3 |
O51641 | TRMD_BORBU | tRNA [GM37] methyltransferase | Borreliella | MKFTVLSLFPAIIKPFFENSIMKKAINKGIVSFELVDVRDFSKDKHKRCDDLPYGGGAGMVLKAEPISFALEHVESAKKTTIFLSPSGIKYSQELAYSLSKREEIVIICGRYEGIDQRIIDLYVDFEISIGDYVLSSGEIAALVLIDSVYRLLDGVINPNSLLEESFGVKNGLLEYPHYTRPYDFKGIKVPEVLLSGHHANIKNWRLVKAREKTKKNRYDLYLKYLEIIGEDNGFDKKN | Specifically methylates guanosine-37 in various tRNAs. | O51641 |
Q9TLW8 | TRPA1_CYACA | Tryptophan synthase alpha chain | Cyanidium | MKNSIKNIFESERGLLLLPFVSLGTPNTQINKQAIIAMDKNGANIIELGIPYSDPVADGPVIQDAYNKAIKNGVNIRKAFKILMNLKGKIKSPIIVFIYYNQLLNYGINKFLEKLIQLEVQGIIVPDLPYDESQILKKKCTINNIALISLIALTSSFSRIKKIARNAEGFLYLISKTGVTGGTGKLMNKLKIIIKTIQKLTSKPVVVGFGINSRRQIKQLIEWNSNGIVIGSPCVQILLQSSKEVCVIKLSGLIKQIKESTSSTSN | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. | Q9TLW8 |
Q7UB34 | ILVC_SHIFL | Ketol-acid reductoisomerase type II | Shigella | MANYFNTLNLRQQLAQLGKCRFMGRDEFADGASYLQGKKVVIVGCGAQGLNQGLNMRDSGLDISYALRKEAIAEKRASWRKATENGFKVGTYEELIPQADLVVNLTPDKQHSDVVRTVQPLMKDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHPENDPKGEGMAIAKAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLVEEGTDPAYAEKLIQFGWETITEALKQGGITLMMDRLSNPAKLRAYALSEQLKEIMAPLFQKHMDDIISGEFSSGMMADW... | Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobu... | Q7UB34 |
B2I7H7 | HEMH_XYLF2 | Protoheme ferro-lyase | Xylella | MNHTSDTALLIVNLGTPEAPTAAAVRRYLGEFLSDRRVVSIPPLFWKPLLHMVILPIRGPRSASKYAKVWLQEGSPLSVYTRRIAEGLTQHLPDWRVAWAMRYGAPALTKALDALQAQQVRRIVILPLYPQYSTTTTASVQDVVEAWCKRTPQVQVECIQDYAEDPAWVAAVAASIRRHWQAHGRSEKLMFSFHGLPQRVANNGDPYPQRCQVSASLIAAALNLNESEWVLGYQSRFGAERWLQPYAEPTLWALAESGIRRFDLVCPGFSVDCLETLEEVALGFSETLAARGATMRYIPCLNDDPAHVQALAGLAQRALP | Catalyzes the ferrous insertion into protoporphyrin IX. | B2I7H7 |
Q0HVC0 | ASTE_SHESR | Succinylglutamate desuccinylase | Shewanella | MLQALLDSKDFLALTLANPETLGDEFSFALGEHTRVEVWDTGVIVFEPAQAQGKDVILSCGVHGNETAPIELCNTLIKQLLQQKIIAKQRTLFLIGNPLAINNGTRIIDENMNRLFSGEHSNPPGLVNPERVRAKKLEAYVDRFFKGAAAGRQRIHYDLHTAMRASKHEKFAIYPYRPGRAYSAEQIMFLAASGVDTVLFHHEPTTTFSYFSSEQYGADAFTIELGKVYPMGQNDMTRFIAAQEMFMRLITDKPLALEPFSADKVNLYQVCRVINKHFDDFEFTFATDVENFRSFPKGFVLAREGGQEIKVEQEFEAIVF... | Transforms N(2)-succinylglutamate into succinate and glutamate. | Q0HVC0 |
O87939 | TDIS_THAAR | Sensor protein TdiS | Thauera | MSGNAIASTETEMEADHGNDPATGYEVIFRNTPLAICHLRNRAFVRCNTRFEELFGYARGELDNKSVRLLYPTDESFRTIGENYGHFFERHDTFKDERPIIRKDGSVIWCIVTGSLLDSSNPRLGSIWVVQDISEHKRTEDDLKASVEKLEILVHQRTLELHKHVNKLEQEVATRKLAEEVANEHREKYEKLFHMLPIGISITDNEGRILEANRQFTELVGTPEKPPITWQQLPQRFFLSDGTKVARKRLPWRIHDVQKDSIKNIEIGMREEESRKQRWLSVSSSLLELKGQKMVVAAFTDITYRKRIEELERLRHAELT... | Member of the two-component regulatory system TdiR/TdiS, which probably regulates transcription of toluene catabolic genes (bss operon). May activate TdiR by phosphorylation. | O87939 |
Q8NZ24 | MUTS_STRP8 | DNA mismatch repair protein MutS | Streptococcus | MAKTNISPGMQQYLDIKKDYPDAFLLFRMGDFYELFYEDAVKAAQLLEIGLTSRNKNAENPIPMAGVPHHSAQQYIDVLIELGYKVAVAEQMEDPKQAVGVVKREVVQVITPGTVVDSAKPDSANNFLVAVDFDGCRYGLAYMDVSTGEFCVTDLADFTSVRSEIQNLKAKEVLLGFDLSEEEQTILVKQMNLLLSYEETVYEDKSLIDGQLTTVELTAAGKLLQYVHKTQMRELSHLQALVHYEIKDYLQMSYATKSSLDLVENARTNKKHGSLYWLLDETKTAMGMRLLRSWIDRPLVSKEAILERQEIIQVFLNAFI... | This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity. | Q8NZ24 |
Q9M376 | VA727_ARATH | Vesicle-associated membrane protein 727 | Arabidopsis | MSQKGLIYSFVAKGTVVLAEHTPYSGNFSTIAVQCLQKLPTNSSKYTYSCDGHTFNFLVDNGFVFLVVADESTGRSVPFVFLERVKEDFKKRYEASIKNDERHPLADEDEDDDLFGDRFSVAYNLDREFGPILKEHMQYCMSHPEEMSKLSKLKAQITEVKGIMMDNIEKVLDRGEKIELLVDKTENLQFQADSFQRQGRQLRRKMWLQSLQMKLMVAGAVFSFILIVWVVACGGFKCSS | Involved in the targeting and/or fusion of transport vesicles to their target membrane. | Q9M376 |
P0CY07 | HMAL1_YEAST | Alpha-1 activator | Saccharomyces | MFTSKPAFKIKNKASKSYRNTAVSKKLKEKRLAEHVRPSCFNIIRPLKKDIQIPVPSSRFLNKIQIHRIASGSQNTQFRQFNKTSIKSSKKYLNSFMAFRAYYSQFGSGVKQNVLSSLLAEEWHADKMQHGIWDYFAQQYNFINPGFGFVEWLTNNYAEVRGDGYWEDVFVHLAL | 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. Silenced copy of ALPHA1 at HML. | P0CY07 |
B1KNU0 | RRF_SHEWM | Ribosome-releasing factor | Shewanella | MLNEIKKDAQDRMDKCVEATKTQMAKVRTGRAHPSLLDSIKVPYYGSLTPLKQVGNVSIEDSRTLAISVFDSTMIPAVEKAIMSSDLGLNPMSAGATIRVPLPALTEERRKDLIKVVRAEAENGRIAVRNVRRDANSDVKALEKEKECTEDDVHRSEDEVQKFTDAHIKLIDEILAAKEAELMEV | Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another. | B1KNU0 |
Q7VBM9 | SYW_PROMA | Tryptophanyl-tRNA synthetase | Prochlorococcus | MTKKRVLSGVQPTGAIHIGNWLGAIRNWVSLQNEYDTYVCVVDLHAITVPHDPQQLKENTLRTAALYVACGMDPKKCSIFVQSHISAHSELCWLLNCVTPLNWMERMIQFKEKAIKQGDNVSIGLLDYPVLMAADILLYDADLVPVGEDQKQHLELARDIAQQRVNSRFNKESKSILKIPKPLIMKEGGKIMSLIDGNMKMSKSDPNENSRIALLDSPEIIKKKIKRAKTDSFLGLEFDNNQRPEANNLLGIYSMVSNQNREAVQKEFSNIGWGKFKPILTDAIIESLNPIQQKYYSLIKDKTELNNILNKGYIKANTIS... | Catalyzes the attachment of tryptophan to tRNA(Trp). | Q7VBM9 |
O13750 | SUCA_SCHPO | Succinyl-CoA synthetase subunit alpha | Schizosaccharomyces | MFKTQTTLLTSLRRFSSSSQLKNSKSLYEQTIPNLMINSDTKVIFQGFTGKQGTFHAQHAMDYGTKVVGGTNPKKAGTTHLGKPVFGTIEEAMKETKADASAVFVPPPLAAGAIEEAIAAEVPLIVAITEGIPQHDMLRVSDILKTQSKSRLVGPNCPGIIRPGQCKIGIMPSHIHKPGCIGIVSRSGTLTYEAVNQTTQTDLGQSLVIGIGGDPFPGTNFIDALKLFLDDPNTQGIILIGEIGGSAEEDAAEFIRAANASRSTPKPVVSFIAGATAPKGRRMGHAGAIVAGGKGTAAAKFEALEAAGVRISRSPATLGS... | Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nu... | O13750 |
B2LML9 | PSBB_GUIAB | Protein CP-47 | Guizotia | MGLPWYRVHTVVLNDPGRLLSVHIMHTALVAGWAGSMALYELAVFDPSDPVLDPMWRQGMFVIPFMTRLGITNSWGGWSITGGTTTNPGIWSYEGVAGAHIMFSGLCFLAAIWHWVYWDLEIFCDERTGKPSLDLPKIFGIHLFLAGVACFGFGAFHVTGLYGPGIWVSDPYGLTGKVQSVNPSWGVEGFDPFVPGGIASHHIAAGTLGILAGLFHLSVRPPQRLYKGLRMGNIETVLSSSIAAVFFAAFVVAGTMWYGSATTPIELFGPTRYQWDQGYFQQEIYRRVSAGLAENQSLSEVWSKIPEKLAFYDYIGNNPA... | One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient sub... | B2LML9 |
Q6GMK0 | MGT4B_DANRE | UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IVb | Danio | MRLRNGTFLTVLLFGLCGLISLSWYTAFSNSKGNVVDIYQREFLALRDRLHSAEQENLKRSKELNLVLDEIKRAIAEKQALRDINRTWSSLSDETKLKLWNVTSSKNVLQLPSIFHHLPHLLAKESSLQPAVHIGQGRTGVSIVLGVPSVKREVHSYLTDTLSSLMTELSPAEKEDCVIVVFIAETDQQYANSVADNLKRLFPGEIQSGLLEIISPSVHFYPDFSHLKESFGDPKERVRWRTKQNLDYCFLMMYAQTKGNYYVQLEDDIVARPNYFTTMKNFALQQPSEEWMILEFSQLGFIGKMFKSLDLPLIVEFMLM... | Glycosyltransferase that catalyze the transfer of GlcNAc from UDP-GlcNAc to the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans through a beta1-4 linkage and participates in the production of tri- and tetra-antennary N-linked sugar chains. Prefers complex-type N-glycans over hybrid-types. Has low... | Q6GMK0 |
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