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 |
|---|---|---|---|---|---|---|
Q1JHN8 | ATPD_STRPD | F-type ATPase subunit delta | Streptococcus | MTKKEQALIEQYAKSLVEVASEHHSLDALQADVLAILETFVTTNLDQSLSSLAVPHAEKIKLLTLLKGSNSVYMNNFLNLILQNEREAYLYQMLQTVLNEIAIVSNQYDVTVTSSLPLTEEQKSRVRAVVAKKFAVTAGRLIEKVDPSLIGGFIISVNNKVIDTSIRRQLQAFKMNLK | This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. | Q1JHN8 |
A4SP04 | RLMN_AERS4 | tRNA m2A37 methyltransferase | Aeromonas | MMSEIKTNLLDLDRDAMRAFFVELGEKPFRADQIMKWIYHFGCDDFDQMNNVNKVLRERLKAIAEIRAPEVSREQRSSDGTIKWALQVGGQEVETVYIPEEDRATLCVSSQVGCALACKFCSTAQQGFNRNLKVSEIIGQVWRAAKIVGGKRPITNVVMMGMGEPLLNLANVIPAMRLMMDDFGYGISKRRVTISTSGVVPALDILGDQIDVALAISLHAPNDKLRSEIMPINDKYNIEDFLAGVRRYLAKSNANGGRVTVEYVLLDHINDDMQHAHELAKVLKDTPSKINLIPFNPFPGNPYGKPSNSRIDRFSKVLMEYGFTVIVRKTRGDDIDAACGQLVGEVIDRTKRTMKNRMQQDGISVKMV | Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity. | A4SP04 |
E5AE43 | RTA1_LEPMJ | Phomenoic acid biosynthesis cluster protein RTA1 | Leptosphaeria maculans species complex | MNAYAYTACLGIYGSTPNNEQLVLGSPDQLQRNKPRFRLIVLPHAPAASPFYPPWRSFAPDWEGQGARPMDHFKVGNLRFQLETHRIDEHSTFGKLFGHAPSPSQSCVSFQKKSDRAEPLLLARCSAASWSCIHPPTVLYFVAYQLEYPFAARFSATKISPIQDKMVATSDVPIVGSLYVYAPNKGAPIFFTIAFAISTILHSWQCHRYKAWKLIWLQPACAALFTLGYALREYGAYNYLYDGTEKAPLALFILSQICIYLGPPLLELANYHILGRVFHYVPYAAPFNPGRVTAFFGGLMAIVEGLSGSGVSLTANAKAKESTKKTGHNLLLVALALQVCVIFIFVYLSVLFHRRCIKAKVPAQSKAVKSTLMTLYLSMALIFIRCVFRLVEMATSSTSVDITSMERLMKLSPVLRNEAYFYAFEASLMLINSFLWNVQHPGPHLPGDTHIYLAQDGTEVEGEGDGSEDRPLLLNMANTLMFGLLYRDDKDHTHSQPQELYENPNGNGHKKFRLGNGGRAT | Lipid-translocating exporter-like protein; part of the gene cluster that mediates the biosynthesis of phomenoic acid, a long chain aliphatic carboxylic acid that does not appear to be essential for pathogenicity but may play a role in allowing to outcompete other fungi in the environmental niche via its antifungal properties. | E5AE43 |
P0CU75 | CLAC_PASFU | Cladofulvin biosynthesis cluster protein C | Fulvia | MAVVNGNYIPGRLDGRVAVVTGSGRGIGAAIAVHLGRLGANIVVNYANSALDAQKVVDQIKGAGSEAIAIKADIRDVSQIMRLFDEAVAHFGHVDIAVSNSGVVSFGHLKDVTEEEFDRVFSLNTRGQFFVAREAYRHLSEGGRIIMTSSNTSKDFSVPRHSLYSGSKGAVDSFVRIFSKDCGDKKITVNGVAPGGTVTDMFHDVSHHYIPDGEKYTAEQRQQMAAFASPLHRNGFPEDIANVVGFLASKEGEWINGKVINLDGGAA | Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bianthraquinone cladofulvin, a conidial pigment not required for virulence but that plays a role in fitness and resistance to environmental stresses including UV light and low-temperature stress . The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) claG. The atrochrysone carboxyl ACP thioesterase claF then breaks the thioester bond and releases the atrochrysone carboxylic acid from claG . This compound is decarboxylated by claH to yield emodin, which is further converted to chrysophanol hydroquinone by the reductase claC and the dehydratase claB . The cytochrome monooxygenase P450 claM then catalyzes the dimerization of nataloe-emodin to cladofulvin . | P0CU75 |
Q87KE2 | TSAC_VIBPA | tRNA threonylcarbamoyladenosine biosynthesis protein TsaC | Vibrio | MDNFEQVLNALQQGEVIAYPTEGVFGVGCDPDNPDAIQKLLDLKQRPVEKGLILIAASYEQLLPYIDESQLTPEQLATVHATWPGPYTWIMPASDKVSNWVSGQFDSIAVRVTDHPLVQKMCNAFGKPLTSTSANLSGLPPCMTTEEVEQQLGDKLVAILRGETSGRDKPSEIRDAKTSQILRQG | Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate. | Q87KE2 |
Q8FQ20 | ATPB_COREF | F-ATPase subunit beta | Corynebacterium | MTTALTEQNAQQAATAGRVVRVIGAVVDVEFPRGELPALYNALTAEVTLESVAKTVVLEVAQHLGDNLIRTIAMAPTDGMVRGATVTDTGKPISVPVGDVVKGHVFNALGDCLDVPGLGRDGEQWGIHREPPSFDQLEGKTEILETGIKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMITRIAREFSGTSVFAGVGERTREGTDLFLEMEEMGVLQDTALVFGQMDEPPGVRMRVALSGLTMAEYFRDVQNQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPTLADEMGVLQERITSTKGRSITSLQAVYVPADDYTDPAPATTFAHLDATTELDRSIASKGIYPAVNPLTSTSRILEPSIVGERHYEVSQRVIGILQKNKELQDIIAILGMDELSEEDKITVARARRLERFLGQNFFVAEKFTGLPGSYVPLADTIDAFERICNGDFDHYPEQAFNGLGGLDDVEAAYKKLTGK | Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | Q8FQ20 |
P44643 | RLMD_HAEIN | 23S rRNA(m5U1939)-methyltransferase | Haemophilus | MVLLYTPKQKTKNVQTITADILDLDYQGLGVAKINGKTWFIENALPHEKVECRILEDKRQYGHAIVKKWRVKSPERLEPKCAHFMRCGGCQGQHIPIEMQRKAKESALFKRLSKLQSEPISFQPMICGDAWAYRRRVRLSLWFNPSTKQIEMGFRQKNTNDLIPVQSCEVAEPAINYLLPKLTALLEKFSAPKQLGHIELVAADNGVAMLLRYTKNLAEIDRTLLLKFAEQEKLMLFLQSDKGIEQIYGDAPYYQFSDGIKLHFDIRDFIQVNSALNEPMVNTALDWLELSQQDCVLDLFCGMGNFTLPLAKRVKSAVGIEGVFEMVQKAAQNAERNQIKNIEFFQADLDQSFVEQPWANQSFNKILLDPPRSGAAFALNALCELKAEKILYVSCNPATLVRDAEILCNFGYKIEKSAVIDMFPHTGHLESITLFTTK | Catalyzes the formation of 5-methyl-uridine at position 1939 (m5U1939) in 23S rRNA. | P44643 |
B8MLU5 | LIPA_TALSN | Lipoic acid synthase | Talaromyces sect. Talaromyces | MAASSTRLRCLYASSAPAWKKSPSQSIISLSRHYATTSSTTPSLNPDESSSSSSSTIPKRRKTTTFRDKLNAGPSFADFVTGGNGNNASLDPEEAYALEKVMIPGPAGRKKEHTRLPSWLKTPIPDSTNYKRIKKDLRGLDLHTVCEEARCPNISDCWGGSDKSAATATIMLMGDTCTRGCRFCSVKTLRTPGPLDPHEPENTAEALSRWGLGDDLPDGGAHHFAETVIKIKQKAPGILVECLTGDFAGDLDMVSLVAKSGLDVYAHNVETVEALTPHVRDRRATFKQSLRVLEAAKRAKPSLITKTSMMLGFGETEDQLWDALRQLRASNVDVVTFGQYMRPTKRHMAVHEYVTPDKFELWRQRALEMGFLYVASGPLVRSSYKAGEAFIENVLKKRRGVGNTPGAEVASAKDVPVDVLGK | Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | B8MLU5 |
Q12FJ6 | COBS_POLSJ | Cobalamin-5'-phosphate synthase | unclassified Polaromonas | MNPISQFVREYLLAVQFFTRIPVVGRLADWVGYSPELLRASAGHFPGVGILVGVMAALVYGLIQALLPNTPFTPLVAAVLSTAATVLLTGGFHEDGLADVADGLGGSQDRERALEIMKDSRVGAFGAMALMLALLGKTALLAMLGSVDVSPAELGDDASFSSWYIGAALLTGHVVSRGLPLLLIWLLPHVGNTASSKSKPLADQISQGSLLVAFIWSFVVLALAGLALDAISLIVACSFSLLALLWMGALFKRRLQGFTGDCLGATQQVCEIAFYLGLAVSL | Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate. | Q12FJ6 |
P70617 | NINJ1_RAT | Secreted ninjurin-1 | Rattus | MDPGTEEYELNGDLRPGSPGSPDASPPRWGLRNRPINVNHYANKKSAAESMLDIALLMANASQLKAVVEQGNEFAFFVPLVVLISISLVLQIGVGVLLIFLVKYDLNNPAKHAKLDFLNNLATGLVFIIVVVNIFITAFGVQKPVMDVAPRQ | Secreted form generated by cleavage, which has chemotactic activity. Acts as an anti-inflammatory mediator by promoting monocyte recruitment, thereby ameliorating atherosclerosis. | P70617 |
Q0ADI8 | RS18_NITEC | 30S ribosomal protein S18 | Nitrosomonas | MANRPLFKRKKFCRFTAEGIKKIDYKDVDLLKDFISENGRIIPARITGTRSYYQRQLNLAIERARFLALLPYTDQH | 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. | Q0ADI8 |
A1KS00 | RNPA_NEIMF | Protein C5 | Neisseria | MDYRFGRQYRLLKTDDFSSVFAFRNRRSRDLLQVSRSNGNGLDHPRIGLVVGKKTAKRANERNYMKRVIRDWFRLNKNRLPPQDFVVRVHRKFDRSTAKQARAELAQLMFGNPATGCRKQA | RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. | A1KS00 |
Q31KZ4 | PSBZ_SYNE7 | Photosystem II reaction center protein Z | Synechococcus | MVILFQLALLLLVVMSFVLIVGVPVLYATNGDRVQSNRLILVGGLAWTALVVLVGVLNYFVV | Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna. | Q31KZ4 |
Q91ZP9 | NECA2_MOUSE | Neuronal calcium-binding protein 2 | Mus | MCERAARLCRAGAHRLLREPPPQGRALGGLLRWVGARMGEPRAPLVPDIPSADPGPGPAASRGGTAVILDIFRRADKNDDGKLSLEEFQLFFADGVLNEKELEGLFHTIDSDNTNHVDTKELCDYFVEHMGDYEDVLASLETLNHSVLKAMGYTKKVYEGGSNVDQFVTRFLLKETANQIQSLLSSVESAVEAIEEQTSQIRQDHCKPSHAVNESRYGGPTPPYIPNHKLVAPEPMKSLPVATGEPKEDGLEGQISRLAELIGRLESKTLSFDLQQRLSDEEGTNMHLQLVRQEMAVCPEQLSEFLDSLRQYLRSTAEERNCFHVAAVRMADGLTFVIYEFWETEEEWKRHLQSPVCKAFRHVKVDTLSQPEALSQISVPAAWCTSGRD | May act as a signaling scaffold protein that senses intracellular calcium. Can modulate ligand-induced internalization of ADORA2A and coupling efficiency of mGluR5/GRM5; for both receptors may regulate signaling activity such as promoting MAPK1/3 (ERK1/2) activation. | Q91ZP9 |
Q54JH6 | CMT1_DICDI | DNA (cytosine-5)-methyltransferase | Dictyostelium | MEQLRVLEFYSGIGGMHYGLQESGVDFQVIQSFDINTNANLNYKYTFNEDSSQKSIESYSVEELEGFKANAWLMSPPCQPFTRLGLQKDDQDNRTNSFFHLLDVLTKIKDPPTYILIENVFGFAKKGSSNTRDHLLDTLIKMNYSFQEFHLSPQQFGLANQRLRYFCIAKRNGKLNFKKEQDKHNEKVDENKLNNNSNNNNEQNKYDNLKILDHIPGYDFHTTLEECDEISNYFDKDLTDDELYEKYKVPHNLLLSKGMLFDIKQKDSKTSNCVTKSYGKFIEGTGSIIQMDNNFKADINDNKSLIPLKLRYFSPKEITRLHGFPEEFKFSPKLTTIQCYRLIGNSLNVKIVSELLKVLVSPNEEEEQQEQQKEKEGKK | Involved in epigenetic gene silencing. Methylates specific cytosine residues in the retrotransposons DIRS-1 and Skipper. | Q54JH6 |
C3PL50 | GLMM_CORA7 | Phosphoglucosamine mutase | Corynebacterium | MTRLFGTDGVRGLANKKLTPILALRLGQAAAEVLTSDRESYERRPLAIIGRDPRVSGEMLDAAIASGLASRGVDVVRVGVLPTPAIAFLTDDFGADLGVMISASHNPMPDNGIKFFSAGGKKLPDEVEDRIQAAMDNLTEDGPTATKIGRIISEAPDGRERYLKHLAEVVTTDLSGIKVVVDTANGAASKVAPQAYEAAGAEVVAIHNKPNAFNINEDCGSTHIEKTQEAVVEHGADLGLAHDGDADRCLAVDAEGNVVDGDQIMAILAVGMKEENDLRFNTLVATVMSNLGLKLAMQEQGIDIKETAVGDRYVLEELNRGDFSLGGEQSGHVVLPDDCTTGDGTLTGLSIMARMAKSGKSLKELASVMTVLPQVLINVPVSDKAVILNAPEVKEAIAAAEAELGETGRVLLRPSGTEELFRVMVEAAEKEQARKVAGKLAAVVAAV | Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. | C3PL50 |
P81655 | RK1_RABIT | Corticostatin-related peptide RK-1 | Oryctolagus | MPCSCKKYCDPWEVIDGSCGLFNSKYICCREK | Has antimicrobial activity against E.coli and activates ion channel activity. | P81655 |
P54685 | CDK7_DICDI | MO15 homolog | Dictyostelium | MDKYNIEALIGEGTYGVVSRATVKATGQIVAIKKIRKILIQNQTDDGINFSAIREIKILQELKHDNVVNLLDIFAHKSNVYLVFELMQWDLQEVIEDKSIILKPADIKSYMKMLLQGIEACHRNWVLHRDLKPNNLLMSINGDLKLADFGLARQYGSPNKVFSPQAVTIFYRAPELLFGAKSYGPSVDIWSIGCIFAELMLRTPYLPGTGEIDQLRKICSALGTPNESNWPGVTCLPNYIKFTDHPATPFKQLFTAASDEAIDLISKMLLFNPSNRISAADALNHPYFTSGVKHTNPADLPVPFAKKASLLQQRQVLAQVQQQLLQKQQQQQQQQQQQIQSQPEPIQVDNVEQTQQAQQV | Catalytic part of CAK which activates cyclin-associated CDK1/CDK2/CDK4 by threonine phosphorylation, thereby allowing MPF activation. | P54685 |
P23321 | PSBO1_ARATH | OEC 33 kDa subunit | Arabidopsis | MAASLQSTATFLQSAKIATAPSRGSSHLRSTQAVGKSFGLETSSARLTCSFQSDFKDFTGKCSDAVKIAGFALATSALVVSGASAEGAPKRLTYDEIQSKTYMEVKGTGTANQCPTIDGGSETFSFKPGKYAGKKFCFEPTSFTVKADSVSKNAPPEFQNTKLMTRLTYTLDEIEGPFEVASDGSVNFKEEDGIDYAAVTVQLPGGERVPFLFTVKQLDASGKPDSFTGKFLVPSYRGSSFLDPKGRGGSTGYDNAVALPAGGRGDEEELVKENVKNTAASVGEITLKVTKSKPETGEVIGVFESLQPSDTDLGAKVPKDVKIQGVWYGQLE | Stabilizes the manganese cluster which is the primary site of water splitting. | P23321 |
Q971T0 | IF5A_SULTO | eIF-5A | Sulfurisphaera | MSIQYTTVGDLKVGNYVVIDGEPCRVVEISKAKTGKHGSAKANIVAIGLFTGQKRTLMAPVDQQVEVPIIEKHIGQILADKGDTITIMDMENYETFDIEKPTDADIVDKIRPGAEVEYWEIMGRKKIVRVK | Functions by promoting the formation of the first peptide bond. | Q971T0 |
A5II94 | TATA_LEGPC | Sec-independent protein translocase protein TatA | Legionella | MGLSGISPLSLLLILAIIVALFGTSKLKTIGSDLGEAIKNFRKAMNSEETNDTQKDDHKPL | Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system. | A5II94 |
A5JZQ2 | RU1C_PLAVS | U1 small nuclear ribonucleoprotein C | Plasmodium (Plasmodium) | MPKYYCEYCDIYLTHSSPVGRRQHIQGRKHISAKIEYFQNLLREEGITPQNFLGFLGNRAFNNMLGNPMMNNMMPGNFPMHMKHGGMKHHSHYSRHSHRHHMSHGRYNRERHGHHSYSSKYHSHPMHMNSNSIGNPSGFSNGKYSGSFFSSPNAMHGNGKMFNNTIRDLVSNVNIDSDPVKDSQNGERVGDNAIDKVSSGMHDQGDRGDLGDHADHADHAGPVSATDGTANGNDQVSVDA | Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. U1-C is directly involved in initial 5' splice-site recognition for both constitutive and regulated alternative splicing. The interaction with the 5' splice-site seems to precede base-pairing between the pre-mRNA and the U1 snRNA. Stimulates commitment or early (E) complex formation by stabilizing the base pairing of the 5' end of the U1 snRNA and the 5' splice-site region. | A5JZQ2 |
Q4WQU0 | SED4_ASPFU | Sedolisin-D | Aspergillus subgen. Fumigati | MLSSTLYAGWLLSLAAPALCVVQEKLSAVPSGWTLIEDASESDTITLSIALARQNLDQLESKLTTLATPGNPEYGKWLDQSDIESLFPTASDDAVLQWLKAAGITQVSRQGSLVNFATTVGTANKLFDTKFSYYRNGASQKLRTTQYSIPDHLTESIDLIAPTVFFGKEQNSALSSHAVKLPALPRRAATNSSCANLITPDCLVEMYNLGDYKPDASSGSRVGFGSFLNESANYADLAAYEQLFNIPPQNFSVELINRGVNDQNWATASLGEANLDVELIVAVSHPLPVVEFITGGSPPFVPNADEPTAADNQNEPYLQYYEYLLSKPNSHLPQVISNSYGDDEQTVPEYYARRVCNLIGLMGLRGITVLESSGDTGIGSACMSNDGTNKPQFTPTFPGTCPFITAVGGTQSYAPEVAWDGSSGGFSNYFSRPWYQSFAVDNYLNNHITKDTKKYYSQYTNFKGRGFPDVSAHSLTPYYEVVLTGKHYKSGGTSAASPVFAGIVGLLNDARLRAGKSTLGFLNPLLYSILAEGFTDITAGSSIGCNGINPQTGKPVPGGGIIPYAHWNATAGWDPVTGLGVPDFMKLKELVLSL | Secreted tripeptidyl-peptidase which degrades proteins at acidic pHs and is involved in virulence. | Q4WQU0 |
Q4V7H8 | BORE2_XENLA | Dasra-A | Xenopus | MPPKRNRNRLGTRGEGSGDSGVGMFERNDAVQEHKKEKIRLFMQDFVQQGKDRLAELKKDLESLSTTADKALEVELLKMPLAIRHMKVQDYLSLMGGDKSAVAAAAVKLDCSVDELSEPKLVRKNSKKVKVTTNVEYQDDVRTKVMTTSTKNRTVQKVPKSKSMLSLTGKNGKKTTALTRSVSATPLDKASKKLLVTNSSSKPAQRSSRTAMTPLTRSARSDTMFTFGDGAFLDEGVPFVKIPLADGKTVFSAGDDLDSLNVELLRGDTVQHIHNLVGQLTSLCAKASIQHHGNTL | Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Contributes to CPC function by facilitating loading of the CPC onto chromosomes. | Q4V7H8 |
O28359 | RL22_ARCFU | 50S ribosomal protein L22 | Archaeoglobus | MPMARVNYAYKPEDETKAAKAMGYEMPISFKHAVEICRAIRGKKIEEARKLLEDVVEMKRAIPFKRHKKKVAHRRGLEKWYAGRYPQKAAKYVLKVLRNLEANAEYKGLDVENLVIVHAQAQKGRVIERYMPRAFGRATPRFQQLTTVELVAEVR | The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome. | O28359 |
P84908 | DAIP_STRMB | Dispase autolysis-inducing protein | Streptomyces | MKRMGWAVTAAVTTIVLAQSSLAAQAADSTSGWRAPSCTKVTGDGAVTFTTDDGATLAPTTGTLQSVSYTHGLVALDTPNTLLATHNDELQRSTDAGCTWTKVATLGSGSTWLTAATGGRAFAWEKNGGYLARVDGRTVTKLSSPSADIVGVGTDKARRDHVRLAGSDGQLYDSTDAGATWKPLGKLAFGPGASVYTVSFDPADLDHAVAGGMTTGGAVTTDGGATWTAATGLSATAGGKSNLFAASVSPADRNVVYALGIDLVEAAPNSGAEGRHLYRSTDGGRTYTRIVDDTPDTELTNSTLLAPSPVDPNVLYFEYGTYFQAYGTDLYRYDARTGKVGKTHNAHDGISAIAFNPARPSVMYLGLEEVQIHH | Induces autolysis of dispase and thermolysin. | P84908 |
P0DC94 | PCP_STRP3 | Pyroglutamyl-peptidase I | Streptococcus | MKILVTGFDPFGGEAINPALEAIKKLPATIHGAEIKCIEVPTVFQKSADVLQQHIESFQPDAVLCIGQAGGRTGLTPERVAINQDDARIPDNEGNQPIDTPIRVDGKAAYFSTLPIKAMVAAIHQAGLPASVSNTAGTFVCNHLMYQALYLVDKYCPNAKAGFMHIPFMMEQVVDKPNTAAMNLDDITRGIEAAIFAIVDFKDRSDLKRVGGATH | Removes 5-oxoproline from various penultimate amino acid residues except L-proline. | P0DC94 |
A9IK70 | HFQ_BORPD | RNA-binding protein Hfq | Bordetella | MSNKGQTLQDPFLNTLRKEHVPVSIYLVNGIKLQGQIESFDQYVVLLRNTVTQMVYKHAISTVVPARAVNFQVDVPAE | RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs. | A9IK70 |
Q82DN0 | RL18_STRAW | 50S ribosomal protein L18 | Streptomyces | MAYGVKIAKGDAYKRAAIKRRHIRIRKHISGTAERPRLVVTRSNRHIVAQVIDDVKGHTLASASTLDTTIRGGESDKSAQAKSVGALVAERAKAAGVEAVVFDRGGNQYAGRIAALADAAREAGLKF | 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. | Q82DN0 |
A6TGG8 | GPPA_KLEP7 | pppGpp-5'-phosphohydrolase | Klebsiella | MSSTSLYAAIDLGSNSFHMLVVREVAGSIQTLSRIKRKVRLAAGLNSDNTLSAEAMERGWQCLRLFAERLQDIPPTQIRVVATATLRLAVNAGEFLAKAQEILGTPVQVISGEEEARLIYQGVAHTTGGADQRLVVDIGGASTELVTGTGAQTTSLFSLSMGCVTWLERYFADRSLTKENFDLAEAAAREVLLPVADVLRYHGWKVCVGASGTVQALQEIMMAQGMDERITLAKLQQLKQRAIQCGRLEELEIEGLTLERALVFPSGLAILIAIFSELNIQCMTLAGGALREGLVYGMLHLSVEQDIRSRTLRNIQRRFMIDTEQAQRVGGLASHLLSQLDGSWELDPLSRDLLLSACALHEIGLSVDFKRAPQHAAYLVNNLDLPGFTPAQKKLIATLLLNQTNAIDLSSLHQQNAVPPRVAEHLCRLLRLAILFASRRRDDLLPAIQLTAQDEQLTLILPGNWLDEHPLGREMVDQECQWQSYVHWILRVASGDTLK | Catalyzes the conversion of pppGpp to ppGpp. Guanosine pentaphosphate (pppGpp) is a cytoplasmic signaling molecule which together with ppGpp controls the 'stringent response', an adaptive process that allows bacteria to respond to amino acid starvation, resulting in the coordinated regulation of numerous cellular activities. | A6TGG8 |
B8D9V0 | EFG_BUCA5 | Elongation factor G | Buchnera | MSRTTPISRYRNIGISAHIDAGKTTTTERILFYTGINHKIGEVHDGAATMDWMEQEQERGITITSAATTTFWSGMAKQFKPHRINIIDTPGHVDFTIEVERSMRVLDGAVMVYCAVGGVQPQSETVWRQANKYNVPRIAFVNKMDRMGANFLKVVKQIKIRLGANPVPLQLAIGAEDTFVGVVDLIKMKAVHWKDSDQGVTFVYNDIPPEMIELSKKWNQNLIESAVESNEDLLEKYLNGDRLSESEIKSALRKRALNNEIVLITCGSAFKNKGVQALLDAIIEFLPAPNDIQDIKGILNDVEQTPAIRNSDDKAPFSALAFKIASDPFVGNLTFFRVYSGVVKSGDTVFNSAKSQRERFGRIVQMHANKREEIKEVYAGDIAAAIGLKDVTTGDTLCDLNDPIILERMEFPEPVISISVEPKTKVDQEKMGLALGRLAKEDPSFRVRTDQESNQTIISGMGELHLEIIIDRMKREFSVDANVGKPQVAYRETILNKVEDIEGKHIKQSGGRGQYGHVVIELFPLQPGGEGYLFVNDIKGGVIPSEYISAIDKGIQEQLKCGPLAGYPVVDIGVRLYFGSYHDVDSSELAFKLAASAAFKKGFKQAKPILLEPIMKVEVETPDDYMGDVIGDLNRRRGIIEGMKDLSISKIINACVPLSEMFGYATDLRSQTQGRASYSMEFLKYIEAPFNISKDIIERREK | Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. | B8D9V0 |
A1USC1 | EFTU1_BARBK | Elongation factor Tu 1 | Bartonella | MAKSKFERTKLHVNIGTIGHVDHGKTSLTAAITKYFGEFKAYDQIDAAPEERARGITISTAHVEYETDQRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPAIVVFLNKVDQVDDAELLELVELEVRELLSKYDFPGDDIPIVKGSALAALEDSDKSIGEDAVRLLMSEVDRYIPTPERPVDQSFLMPIEDVFSISGRGTVVTGRVERGVVKVGEEIEIVGIRPTSKTTVTGVEMFRKLLDQGQAGDNIGALLRGIDREGIERGQVLAKPGSVTPHTKFKAEAYILTKDEGGRHTPFFTNYRPQFYFRTTDVTGIVTLPEGTEMVMPGDNVAMDVSLIVPIAMEEKLRFAIREGGRTVGAGIVSKIIE | This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. | A1USC1 |
Q8KQF5 | COP_STAEP | Protein cop | Staphylococcus | MTFNKIFKYLISLLFLSILFHTIIHKNNLVFSKTMHKKVAFFSFSIFFVWIRHLKRYNSMLEKATFFVLQTSYTNELKGLYIAGNSYPYYQDKKKLVFNSFQKPFKNHQSTKIPRE | Putative control of replication message. | Q8KQF5 |
Q45374 | KDTA_BORPT | Monofunctional Kdo transferase | Bordetella | MGRGVYTLALRGLAPLIWLWMWRRARRAGGQWELFAPARFGRAGARAPAPLAAPVWVHAVSLGETRAAQPLVQALLERGLPVLLTHTTATGRAEGERLFGAAIGRGQLQQAWLPYDFPGATRRFLARHAPRCGLLMEREVWPNLLAAARAQGVPMALVSARFSASSLRQAGWLGQALREALAGLDRVLAQTDEDGARLCQAGANAYTVTGSLKFDVALPEAQLRVGHAWAGATGRPVIALASTREGEDAMFIEAIGALQAHRAATPRPLILLIPRHPQRFDEAAAQLQAAGLAYARRSAGSGEPGPHIDVLLGDTLGEMPFYYAAADVAIVGGSFARLGGQNLIEACAAGTPVIVGPHTFNFKDAARDAIAAGAALRAPDARTALDWALQLLAEPARRQAMSEAARAWTAAHAGATRRTLDALEDWLG | Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of a single 3-deoxy-D-manno-octulosonate (Kdo) residue from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A. | Q45374 |
P43834 | SYV_HAEIN | Valyl-tRNA synthetase | Haemophilus | MTQKFEMADRFNPSAVEQALYQRWEESGYFKPSENENAPSYCIAIPPPNVTGSLHMGHAFQQTLMDTLIRFNRMEGHNTLWQTGTDHAGIATQMVVERKIAAEEGKTRHDYGREAFINKIWDWKAYSGGTISQQMRRLGNSIDWERERFTMDDGLSNAVKEVFVRLHEEGLIYRGKRLVNWDPKLHTAISDLEVENKESKGSLWHFRYPLANDAKTADGKDYLVVATTRPETMLGDTAVAVHPEDERYQSLIGKTVVLPLANREIPIIADEYVDREFGTGVVKITPAHDFNDYEVGKRHNLPMVNVLTLNANIRDEAEIIGTDGKPLAGYEATIPADYRGLERFAARKKIVADFEALGLLDEIKPHDLKVPYGDRGGVPIEPMLTDQWYVSVKPLADVAIKAVEDGEIQFVPKQYENLYFSWMRDIQDWCISRQLWWGHRIPAWYDAEGNVYVARNEEEVRSKYNLDSAVELKQDEDVLDTWFSSGLWTFSTLGWPEQTKELKMFHPTDVLITGFDIIFFWVARMIMFTMHFVKDENGKPQVPFKTVYVTGLIRDEQGQKMSKSKGNVLDPIDMIDGISLEDLLEKRTGNMMQPQLAEKIAKATRKEFAEGIAAHGTDALRFTLAALASNGRDINWDMKRLEGYRNFCNKLWNASRFVLTNEKLDLSQGEIEFSLADRWIQSEFNRTVETFRSSLSQYRFDLCANAIYEFTWNQFCDWYLELTKPVFANGNAAQIRAASQTLVHVLEKLLRLAHPLIPFITEEIWQKVKGFVGITADSIMLQPFPQVEESGFDPEAEAEIEWLKEVIVAVRNIRAESNIAPSKGLDLLFRNLSAENAKILEKQTALLKAMAKLDNVQVLATNETAPLAVAKLVGNAELLVPMAGFINKEAELARLTKEIEKYQNEVKRIENKLSNEAFVAKAPEAVIAKEREKQAEYQSGLEKIQEQYKAIEAL | 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. | P43834 |
Q7K284 | CLP1_DROME | Crowded by cid | Sophophora | MSEDQGKDYTLESDSELRFEIEQKDAKVLVSLVSGFAELFGTELVKKKQYEFGVGAKVAIFTYQGCVLHVSGKMDVCYISKETPMVQYVNCHAALEQFRMEAEEKDRYGPVAMVVGPMDVGKSTLCRILLNYAVRVGRRPLYADLDVGQGSIAISGSVATILIERPANVEEGFAKTAPLVYHFGHKSPSGNSVLYNAVVSKMAEVTLQSLNSNKRTKSSGIIINTCGWVKGSGYAHLLHAAKAYGACAIFVLDQERLYNELLRDVPKGVHVVLLPKSGGVVERSKELRHEARDQRIKEYFYGNTRAPFYPFSFEVKFQDLRLYKIGAPPLPDSCMPIGMKAEDNKTKVVAVTPTPALIHHVLALSFAESVEDDVIGTNVAGFCCVTEVDMERQAVMLLSPQPRPLPPNALLLWSELQFMDNHT | Required for endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation. | Q7K284 |
A5IIX7 | TDXH_THEP1 | Thioredoxin-dependent peroxiredoxin | Thermotoga | MEGRIPLIGEEFPRLEVKTTHGKKILPDDFRGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFKKLNTELIGLSIDQVFSHIKWIEWIKEKLGVEIEFPVIADDLGEVSRRLGLIHPSKGTNTVRAVFIVDPNGIIRAIVYYPQEVGRNIDEILRAVRALQTSDEKGVAIPANWPSNELINDSVIVPPASSVEEARERLESKDFECYDWWFCYKKV | 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. | A5IIX7 |
P62642 | CHEB2_LEPIC | Putative protein-glutamate methylesterase/protein-glutamine glutaminase | Leptospira | MNYEAIVIGVSAGGINAMKTILPTLPTQFGIPIVIVQHIGARSDGEWFRILEKLCNIKIKEAEEKEEIKSGMVYVAPPNYHLLIEKDKTFSFSIGERVNFSRPSIDVLFETASEVYEDKLIGVILTGANSDGAQGLKKIKENGGLAVVQDPLTAEIALMPRSAIEATSVDYVLSLEKIAELFIRLDQNNLEQR | May be involved in chemotaxis. | P62642 |
Q5LGW6 | RECF_BACFN | DNA replication and repair protein RecF | Bacteroides | MILKRISILNYKNLEQVELNFSAKLNCFFGQNGMGKTNLLDAVYFLSFCKSAGNPIDSQNIRHEQDFFVIQGFYEAMDGTPEEIYCGMKRRSKKQFKRNKKEYSRLSDHIGFIPLVMVSPADSELIAGGSDERRRFMDVVISQYDKEYLDALIRYNKALVQRNTLLKSEQPIEEELFLVWEEMMAQAGEVVFRKREAFISEFIPIFQSFYSYISQDKEQVGLTYESHARKASLLEVLKESRVRDKIMGYSLRGIHKDELNMLLGDFPIKREGSQGQNKTYLVALKLAQFDFLKRTGSTVPLLLLDDIFDKLDASRVEQIVKLVAGDNFGQIFITDTNREHLDRILYKVGSDYKMFRVESGAINEMEEKER | The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP. | Q5LGW6 |
B2J3K1 | CYF_NOSP7 | Cytochrome f | Nostoc | MRNVFRTARLTRSARAIVKTLLIAIATVTFYFTSDLALPQSAAAYPFWAQQTYPETPREPTGRIVCANCHLAAKVTEVEVPQSVLPDTVFKAIVKIPYDLSAQQVGADGSKVGLNVGAVLMLPEGFKIAPEDRISEELKEEIGDTAFQPYSEDKENVVIVGPLPGEQYQEIIFPVLSPNPATDKNIHFGKYSVHVGGNRGRGQVYPTGEKSNNSVYNASATGTITKIAKEEDADGNVKYLVNIQPESGDVVVDTVPLGPDLIVSEGQAVKTGDALTNNPNVGGFGQIDAEIVLQDSSRVKWMIAFVALVMLAQVMLVLKKKQVEKVQAAEMNF | 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. | B2J3K1 |
P94966 | BIOB_METSK | Biotin synthase | unclassified Methylobacillus | MRDSVIDIRGLDRVQRARVQAKEEAPKRWSVDDIVALFELPFSDLMHRAQSVHRENFDPNGVQVSTLLSIKTGGCSEDCGYCPQAARYHTDVEKQDLHAAGRGTRSRVLPRRMRQPFCMAAWQPKQRDLEPVLAMIREVKAMGLETCATLGMLKDGQAEQLKEAGLDYYNHNLDTAPEYYGEVITTRTYQDRLDTLDRVREQDINVCCGGIIGMGESRVQRAGLLAQLANMERPPESVPDQLLTQVEGTPMYGMDELDPFEFVRTIAAARITMPQSFVRLSVGRQSMHEGIQALCFLAGANSIFYGEKLLTTGNPEAEADRKLFDKLGIHPL | Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism. | P94966 |
Q8K9E5 | METK_BUCAP | Methionine adenosyltransferase | Buchnera | MTEYLFTSESVSEGHPDKIADQISDALLDEIIKQDLKARVACETYVKTGMVLIGGEITTTAWVDVEEITRNTINNIGYINSETGFDANSCAVLSTIGKQSPDITQGVDRCNPLEQGAGDQGIIFGYATNETEVLMPAPITYAHLLVKKQSELRKKNILHWLRPDAKSQVTFKYKNGRIIGIDTVVFSTQHKESITQDVLKEAVMEEIIKPVLPNKWLTKNTKFFINPTGRFVIGGPMGDCGLTGRKIIVDTYGGMSRHGGGAFSGKDPSKVDRSAAYAARYVAKNIVAAGLADRCEIQLSYAIGIAEPTSIMIETFRTGKISNKSLINLVRNIFDLRPYGLIEMLDLLRPIYLNTAVYGHFGREEFPWEKLDKVDELLQ | Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. | Q8K9E5 |
A4VYR8 | RPOA_STRS2 | Transcriptase subunit alpha | Streptococcus | MIEFEKPTITKIDENKDYGRFVIEPLERGYGTTLGNSLRRVLLASLPGAAVTSIKIDGVLHEFDTVPGVREDVMQIILNIKGIAVKSYVEDEKKIELDVVGPAEVTAGDILTDSDIEIVNPDHYLFTIADGATFKAVLTVNSGRGYVPAEDNKKDDAPVGTLAVDSIYTPVKKVNYQVEPARVGSNDGFDKLTLEINTNGTIIPEDALGLSARILMEHLGLFTDLTEVAKSAEVMKEAEVASDDRMLDRTIEELDLSVRSYNCLKRAGINTVFDLTEKTEPEMMKVRNLGRKSLEEVKVKLADLGLGLKKDK | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | A4VYR8 |
P61885 | RS10_PYRFU | 30S ribosomal protein S10 | Pyrococcus | MQKARIKIASTNVRSLDEVANQIKQIAERTGVRMSGPIPLPTKRIRITTRKSPDGEGSATFDRWELRVHKRLIDIEADERAMRQIMRIRVPEDVTIEIELIS | Involved in the binding of tRNA to the ribosomes. | P61885 |
Q9GLW7 | PRDX5_CHLAE | Thioredoxin-dependent peroxiredoxin 5 | Chlorocebus | MGLAGVCVLRRSAGYILGGAARQSVAATAAARRRSEGGWASGGVRSFSRAAAAMAPIKVGDAIPAVEVFEGEPGNKVNLAELFKGKKGVLFGVPGAFTPGCSKTHLPGFVEQAEALKAKGVQVLACLSVNDAFVTGEWGRAHKAEGKVRLLADPTGAFGKETDLLLDDSLVSIFGNRRLKRFSMVVQDGIVKALNVEPDGTGLTCSLAPSIISQL | 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 and as sensor of hydrogen peroxide-mediated signaling events. | Q9GLW7 |
B2V910 | TSAD_SULSY | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | unclassified Sulfurihydrogenibium | MVVLGIETSCDDTSIAVYDSEKGIPSNVVTSQLIHAQFGGVYPEIAAREHTKNFLPVLDKALRDASITLSDIDAIATTFMPGLIVSLVAGVSGAKTLSFSLKKPLIPVHHIEAHIFANFITKEIEYPFLALVVSGGHTELILVKEFEDYIYLGGTLDDAVGEVYDKVARALGLGFPGGPLIDKLAKEGKEAIKFPRPLLNDEENKYNFSFSGLKSAVIREINKGIYKKEDITKSFQNAVVDVLVKKTVLACKEFGINRVVVAGGVSANSQLREEFLNIKDLEVHFPPMHLCTDNGAMVAYTGYKRFKEKGISVSLDFEAKARCRIDKFPQLLRSFHA | 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 catalytic role in this reaction. | B2V910 |
Q8FK37 | CUSS_ECOL6 | Sensor histidine kinase CusS | Escherichia | MVSKPFQRPFSLATRLTFFISLATIAAFFAFAWIMIHSVKVHFAEQDINDLKEISATLERVLNHPDETQARRLMTLEDIVSGYSNVLISLADSHGKTVYHSPGAPDIREFTRDAIPDKDAQGGEVYLLSGPTMMMPGHGHGHMEHSNWRMINLPVGPLVDGKPIYTLYIALSIDFHLHYINDLMNKLIMTASVISILIVFIVLLAVHKGHAPIRSVSRQIQNITSKDLDVRLDPQTVPIELEQLVLSFNHMIERIEDVFTRQSNFSADIAHEIRTPITNLITQTEIALSQSRSQKELEDVLYSNLEELTRMAKMVSDMLFLAQADNNQLIPEKKMLNLADEVGKVFDFFEALAEDRGVELRFVGDECQVAGDPLMLRRALSNLLSNALRYTPTGETIVVRCQTVDHLVQVTVENPGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSDVRGTRFVIILPA | Member of the two-component regulatory system CusS/CusR involved in response to copper and silver. Acts as a copper/silver ion sensor. Activates CusR by phosphorylation. | Q8FK37 |
A4XHE0 | SYE1_CALS8 | Glutamyl-tRNA synthetase 1 | Caldicellulosiruptor | MEVRTRFAPSPTGHLHIGGARTALFNYLFAKRYGGKFILRIEDTDLERSSIESEKVIIESLRWLGIEWDEGVEVGGPYGPYRSTERVDIYKKYVDVLFEKGYAYYCYCTEEELEAQRQELLSKGQMPRYLGKCRNLTEDQKRRFEQEGRKPTVRFKVPEGVKIVVHDLVRGDVEFLSDDIGDFVIVKSDGIPTYNFAVVIDDHLMKISHVIRGEEHLSNTPRQILIYNALGFELPQFAHVSLILGKDRTKMSKRHGSTWVEQYRDQGYLKEGLINFLALLGWSPPEDREIFDMEYLIENFSLERVSKNPAIFDIDKLNYINSQHIKLKSLDELTQMCIPYFVEAGYIKEDEAKSKFEWLKKIVKSVYEGLDYLSQIKDRVDIFFNNEVKIEEDEAKEVLKWDHVKDLINVFENKIRQMNELTPEAIKLLFKEIQKETGYKGKNLFMPIRVALTGKTHGPELVEIIEIVGKENILKRLEFFKTWYN | Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). | A4XHE0 |
Q97IQ4 | CRCB1_CLOAB | Putative fluoride ion transporter CrcB 1 | Clostridium | MKKYILIGLGGAIGAILRCFIRNTKIPVYKGEFPISTLMINLSGAFILAVILITANEIWSFNEEIRLGIATGFVGAYTTFSTMCKETIILMNKNLYFLAFCYVTVSVVFGLLFAYFGALSARKILSRLLKVRKEDEKAS | Important for reducing fluoride concentration in the cell, thus reducing its toxicity. | Q97IQ4 |
O31456 | YBFP_BACSU | Uncharacterized HTH-type transcriptional regulator YbfP | Bacillus | MYYEKAVQKTINWIESHLHEQISNEDIVNVSSFSKFHFHRIFQKEVGMSVASYIRLRRLANAAAALLYTDHRIIDIALYYQFESQEAFTRTFKKMYHMPPGAYRTFMKRFTSKKEESYMEKKMKGWVLSGSHPFQFEMGIDRENVHQGKASGYLKSTMVQDIGEFATMMQQFKADRYLGKRLRLSSFIKTKGVQHFASLWMRVDSAADDVLQFDNMSNRPITGTTNWNHYAIVLDVPENSAVISFGVQLSGPGQVWMDHVVFEEVDESVPSTNLEMPGELLDEPVNLSFEEELQK | Probable transcriptional regulator. | O31456 |
A1U776 | ZNUC_MARN8 | Zinc import ATP-binding protein ZnuC | Marinobacter | MTDPLVRLEQITVAFDDRPVVDRVNLTVSRGDIVTIIGPNGAGKTTLIKTVLGIQRATSGQLSVAPGLVIGYVPQHLTLEPTLPLSVRRFMLLSGRTLADCTAALERTGVAHLLDASVHHLSGGEKQRLLLARALARKPDLLVLDEPAQGVDINGQATLYDLIRQLRDELHCGIIMISHDLHLVMAATDRVICLNQHVCCSGYPEDISQDPAFVETFGHQVAESLAVYHHHHNHRHNLHGDVVSSADAHEGCSHDHH | Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. | A1U776 |
Q473U3 | NUOA_CUPPJ | NUO1 | Cupriavidus | MTLEAYFPVLIFIIFGVVLGIALMSIGRILGPNKPDPAKLSPYECGFEAFEDARMKFDVRYYLIAILFILFDLETAFLFPWGVALREIGWPGFIAMGVFLLEFIVGFVYIWKKGALDWE | NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. | Q473U3 |
P43218 | GIPR_MESAU | Glucose-dependent insulinotropic polypeptide receptor | Mesocricetus | MPLRPRLLLLCLWGLLLQQAETDSEGQTTGELYQRWERYARECEETLTAADPPSGMVCNGSFDMYVCWDYTAANTTAQASCPWYLPWYRHVAAGYVFRQCGSDGQWGPWRDHTQCENPEKNGAFQDQRLILERLQVVYTVGYSLSLGTLLLALLILSLFRRLHCTRNYIHMNVFLSFMLRAVAILTRDRLLPTLGPYPGDRTLTLRNQALAACRTAQIVTQYCVGANYTWLLVEGVYLHHLLVIVGGSEKGHFRCYLLLGWGAPALFVIPWVIVRYLLENTQCWERNEVKAIWWIIRTPILITILINFFIFIRILGILVSKLRTRQMRCPDYRLRLARSTLTLVPLLGVHEVVFAPVTEEQAEGTLRFAKLAFEIFLSSFQGFLVSVLYCFINKEVQSEIRRSWRHRVLHLSLRDERPCPHAELGPQALPSRSAPREVPITGSTLPSGPLHGPGEEVLESYC | This is a receptor for GIP. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. | P43218 |
A6V4E2 | NUOH_PSEA7 | NDH-1 subunit H | Pseudomonas | MSWLTPALVTIILTVVKAIVVLLAVVICGALLSWVERRLLGLWQDRYGPNRVGPFGAFQLGADMIKMFFKEDWTPPFADKMIFTLAPVIAMGALLVAFAIVPITPTWGVADLNIGILFFFAMAGLTVYAVLFAGWSSNNKFALLGSLRASAQTISYEVFLALSLMGIVAQVGSFNMRDIVQYQIDNVWFIIPQFFGFCTFIIAGVAVTHRHPFDQPEAEQELADGYHIEYAGMKWGMFFVGEYIGIVLVSALLATLFFGGWHGPFLDTLPWLSFFYFAAKTGFFIMLFILIRASLPRPRYDQVMAFSWKVCLPLTLINLLVTGALVLAAAQ | NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. | A6V4E2 |
B2VHX9 | LPXB_ERWT9 | Lipid-A-disaccharide synthase | Erwinia | MPKHPLTIALVAGETSGDILGAGLIRALKEKHPDARFVGVAGPLMQSEGCEAWYEMEELAVMGIVEVLGRLRRLLHIRRDLTRRFTALKPDVFVGIDAPDFNITLEGRLKQQGIRTIHYVSPSVWAWRQKRVFKIGRATDLVLAFLPFEKAFYDRFNVPCRFIGHTMADAMPIVPDKQAARRELGIAPQALCLALLPGSRSAEVEMLSADFLKTAMLLREKYPQLEIVVPLVNPRRRAQFEAIKAEVAADLPMHLLDGKGREAMLASDAALLASGTAALECMLAKCPMVVGYRMKPFTFWLAKRLVKTDYVSLPNLLAGRELVPELLQDECQPQRLAAALEPLLAQGETRDTLLATFAELHHQIRWNADEQAAAAVLELCR | Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. | B2VHX9 |
Q3K076 | TRHO_STRA1 | tRNA hydroxylation protein O | Streptococcus | MSEKIRVLLYYKYVSIENAEEYAAKHLEFCKSIGLKGRILIADEGINGTVSGDYETTQKYMDWVHSDERFADLWFKIDEENQQAFRKMFVRYKKEIVHLGLEDNNFDSDINPLETTGEYLNPKQFKEALLDEDTVVLDTRNDYEYDLGHFRGAIRPDIRNFRELPQWVRDNKDKFMEKRVVVYCTGGVRCEKFSGWMVREGFKDVGQLHGGIATYGKDPEVQGELWDGAMYVFDDRISVPINHVNPTVISKDYFDGTPCERYVNCANPFCNKQIFASEENEAKYVRGCSPECRAHERNRYVQENGLSRQEWAERLEAIGESLPQVANV | Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs. | Q3K076 |
Q723T1 | IOLA_LISMF | Methylmalonate-semialdehyde dehydrogenase | Listeria | MADVRKLKNYINGEWVESRADKYEDVINPATGEVLCQVPISTRAELDQAAVIAEQAFEKWSQVAVPRRARVLFSFQQLLIQHKEKLARLITLENGKNLSEARGEVQRGIENVEFAAGAPTLMMGDSLASIATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPMAIALGNSFILKPSERTPLLMEKLVELFSEAGLPKGVFNVVYGAHDVVNGILENEIIKAVSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVLNDADLEDTVTNVISAAFGSAGERCMACAVVTVEEGIADEFLAALRTAAQNVKIGNGLDDGVFLGPVIREENQKRTIAYIEKGLEEGAKLTVDGRETGLSEGHFVGPTILEDVTTDMTIWKDEIFAPVLSVIRVKNLQEAVRVANQSEFANGACIFTNNAKAIRYFREKIDAGMLGVNLGVPAPMAFFPFSGWKSSFYGTLHANGKDSVDFYTHKKVVTARYSLKGYEE | Catalyzes the oxidation of malonate semialdehyde (MSA) and methylmalonate semialdehyde (MMSA) into acetyl-CoA and propanoyl-CoA, respectively. | Q723T1 |
Q1JJC0 | RECF_STRPC | DNA replication and repair protein RecF | Streptococcus | MWIKELELKHYRNYDHLLASFSSGLNVFIGNNAQGKTNFLEAIYFLSLTRSHRTRADKELIHFDHSTVSLTGKIQRISGTVDLEINLSDKGRVTKINALKQAKLSDYIGTMMVVLFAPEDLQLVKGAPSLRRKFIDIDLGQIKPVYLSELSHYNHVLKQRNSYLKSAQQIDAAFLAVLDEQLASYGARVMEHRIDFINALEKEANTHHQAISNGLESLSLSYQSSVVFDKKTNIYQQFLYQLEKNHQKDFFRKNTSVGPHRDELAFYINGMNANFASQGQHRSLILSLKMAEVSLMKALTGDNPILLLDDVMSELDNTRQTKLLETVIKENVQTFITTTSLDHLSQLPEGIRIFHVTKGTVQIDSDIH | The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP. | Q1JJC0 |
B5XV26 | CYSH_KLEP3 | PAdoPS reductase | Klebsiella | MSVLDLNALNALPKVERILALAETNAKLEKLSAEERVAWALENLPGEYALSSSFGIQAAVSLHLVNQLRPDIPVILTDTGYLFPETYQFIDELTDKLKLNLKVYRAQESAAWQEARYGKLWEQGVEGIEKYNEINKVEPMNRALKELNTQTWFAGLRREQSGSRATLPVLAIQRGVFKVLPIIDWDNRTVYQYLQKHGLKYHPLWDQGYLSVGDTHTTRKWEPGMAEEETRFFGLKRECGLHEG | Catalyzes the formation of sulfite from phosphoadenosine 5'-phosphosulfate (PAPS) using thioredoxin as an electron donor. | B5XV26 |
A7ZXG5 | ALLB_ECOHS | Allantoin-utilizing enzyme | Escherichia | MSFDLIIKNGTVILENEARVVDIAVKGGKIAAIGQDLGDAKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPLNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNIDRLHELDEVGVVGFKCFVATCGDRGIDNDFRDVNDWQFFKGAQKLGELGQPVLVHCENALICDALGEEAKSEGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHICHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLQQKGRIAPGKDAEFVFIQPNSSYVLTNDDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVAPKGQFILKHQQ | Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. | A7ZXG5 |
A1URK5 | PURA_BARBK | IMP--aspartate ligase | Bartonella | MANVVVVGTQWGDEGKGKIVDWLSEQADVVVRYQGGHNAGHTLVINGISYKLSLLPSGVVRGKLSVIGNGVVVDPHHFVSELKKLRDQGVEITPKVLRVAENASLILSVHRDLDAARENGISGLTIGTTKRGIGPAYEDKVGRRSIRMIDLAETNTLMAKIERLLRHHNALRRGMGIAEIDPKTLYDELMQVADEILPFMDCTWRLLDERHRMGQRILFEGAQGASLDNDFGTYPYVTSSNTVSGQAFIGSGMGPGSVHYVLGIAKAYTTRVGEGPFPTEQVNDVGEFLGMRGNEFGVVTGRKRRCGWFDAVLVRQMVKICSVRGIALTKLDVLDGLDEIKICIGYEIDGRKIDYLPSCIEEQARVKPIYETLEGWKEATACTLNWEELPVQAIKYVRRIEELIGVPIALLSTSPEREDTIFIIDPFAD | 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. | A1URK5 |
A6TVF1 | WHIA_ALKMQ | Probable cell division protein WhiA | Alkaliphilus | MSYSSNTKNELARIEGEQSCCVRAELAALIRMSGTLQLVGSQKLNIKVTTENPAIARRLFKIIKKQYNIHAEVMIRRNARLKKNNYYLLVITHSMGSSEVLADLGIMKKVDDSFDITYRIPQELTQNRCCKRAYLRGAFLGGGSVSDPEKTYHLEFVTHHKELSEGLRDLINSFDLNAKVVERKGNYVVYLKEGDQVVDLLNIVGAHSALLDLENIRVYKEMRNNVNRIVNCETANLSKTVDASIRQIQNIQYIEGSIGINRLPDNLREVAELRVEYQDATLKELGEMINPPIGKSGVNHRLRKLDQIADRERGKSI | Involved in cell division and chromosome segregation. | A6TVF1 |
Q9RC23 | MRSD_BACSY | Mersacidin-modifying enzyme MrsD | Bacillus | MSISILKDKKLLIGICGSISSVGISSYLLYFKSFFKEIRVVMTKTAEDLIPAHTVSYFCDHVYSEHGENGKRHSHVEIGRWADIYCIIPATANILGQTANGVAMNLVATTVLAHPHNTIFFPNMNDLMWNKTVVSRNIEQLRKDGHIVIEPVEIMAFEIATGTRKPNRGLITPDKALLAIEKGFKERTKHPSLT | Catalyzes the oxidative decarboxylation of the C-terminal cysteine residue of mersacidin to an aminoenethiol residue. | Q9RC23 |
C7LYP4 | ARC_ACIFD | Proteasomal ATPase | Acidimicrobium | MPRDETPEREHAEQQSRQALEEEVRELRRRVEEAPSRVRALEEKLLEVSGALAQTQAKNEKLTFTLQQAREHIQNLREEVEKLTQPPSAYGVYLAANQDGTADVFTTGRKMRVAVHPEIDLAAVRVGQEVVLNESFAIVSVRGSDVIGEVATVKDVLDDGSRVILLGRADEERVAQVAGHLQHPPLRVGDSVMVDPRSAMVLERLPRPEVSELALEEVPDITYHDIGGLDRQIEEIQDAVELPFLYRELFGDYRLPAPKGILLYGPPGCGKTLIAKAVANSLAKKVEQVSGRSVRSYFLNVKGPELLNKYVGETERQIRLIFQRAREKAEEGVPVIVFFDEMDSLFRTRGSGISSDMESTVVPQLLAEIDGVEALRNVIVIGASNREDLIDPAILRPGRLDVKIKIERPDEQAAREIFARYLTPEVPIDAGEVTTLGGGDAEKAIAVMIERTVERMYATSDENRFLEVTYQNGEKEILYFKDFSSGAMIENIVRRAKKLAIKREIAGGSRGICLDDLLASIAKEFKEHEDLPNTTNPDDWAKISGRKGERIVFMRILLHEEEGQTGGRAIERVATGQYL | ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. | C7LYP4 |
Q2S1N5 | RIMP_SALRD | Ribosome maturation factor RimP | Salinibacter | MNPTQQHLADRVSGLTEEVIVGTDYFLVDVEVRGHKGTRVVEVYIDSEEEVGHDDLALISKEIGFLLDVEDVVDGSYKLELSSPGIKRPLTMPAQYRKNVGRTLRVRFESDGDEEIVVGDLTDADDEEIELELPSAERLQLPYTTITQARIELPW | Required for maturation of 30S ribosomal subunits. | Q2S1N5 |
A7GGI2 | GLYA_CLOBL | Serine hydroxymethyltransferase | Clostridium | MDFTNLKNTDPELLDMIKKEEERQEYNIELIASENFTSLSVMEAMGSLLTNKYAEGYPHKRYYGGCEFVDEVEDLARERLKKLFAAEHANVQPHSGSQANMAVYMSVLQTGDTILGMDLSHGGHLTHGSPVNFSGKLYNFISYGVDKETETIDYDQLKKIALENRPKMIVSGASAYPRIIDFEKIREICDEIDAYMMVDMAHIAGLVATGLHPSPVPYADFVTTTTHKTLRGPRGGAILCKEKYAKAVDKAIFPGIQGGPLMHTIAAKAVCFREALREDYKEYMQQVVKNTKVLGEELKNYGFRLISGGTDNHLLLIDLTNKNITGKDAEKLLDSVGITVNKNTIPFETLSPFITSGIRIGTPAVTTRGFKEEEMKKIAYFMNYSIEHREENLSQIKEQIKEICKKYPLYQNA | Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | A7GGI2 |
Q3BWP3 | RNH_XANC5 | Ribonuclease H | Xanthomonas | MKFIEVHTDGSCLGNPGPGGWAALLRYNGREKELAGGEAVSTNNRMELMAAIMALETLTEPCQIVLHTDSQYVRQGITEWMPGWVRRNWKTAGGDPVKNRELWERLHAATQRHRIDWRWVKGHNGDPDNERVDVLARNQAIAQRDGLATS | Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. | Q3BWP3 |
Q8Z227 | MALT_SALTI | ATP-dependent transcriptional activator MalT | Salmonella | MLIPSKLSRPVRLDHTVVRERLLAKLSGANNFRLLLVTSPAGYGKTTLVSQWAAGKNELGWYSLDEGDNQQERFASYLIAAIQQATGGHCSTSEAMAQKRQYASLTSLFAQLFIELAQWHRPLYLVIDDYHLITNPVIHDAMRFFLRHQPENFTLVVLSRNLPQLGIANLRVRDQLLEIGSQQLAFNHQEAKQFFDRRLSSPIEAAESSRMCDDVAGWATALQLIALSARQNHTSAHHSARRLAGINASHLSDYLVDEVLDNVDVSTRHFLLKSAILRSMNDALIVRVTGEENGQMRLEEIERQGLFLQRMDDTGEWFSYHPLFGSFLRQRCQWELAAELPEIHRAAAESWMEQGFPSEAIHHALAAGDAQMLRDILLNHAWGLFNHSELALLEESLKALPWESLLENPRLVLLQAWLMQSQHRYSEVNTLLARAEQEIKGVMDGTLHAEFNALRAQVAINDGNPEEAERLAKLALDELPLAWFYSRIVATSVHGEVLHCKGNLSQSLSLMQQTEQMARHHDVWHYALWSLIQQSEIQFAQGFLQAAWETQERAFQLIKEQHLEQLPMHEFLVRIRAQLLWAWARLDEAEASARSGIAVLSTFQPQQQLQCLTLLVQCSLARGDLDNARSQLNRLEKLLGNGRYHCDWISNADKVRVIYWQLTGDKKSAANWLRHTPKPAFANNHFLQGQWRNIARAQILLGEFEPAEIVLEELNENARSLRLMSDLNRNLLLLNQLYWQSGRKNDAQRVLLDALQLANRTGFISHFVIEGEAMAQQLRQLIQLNTLPEMEQHRAQRILRYINQHHRHKFAHFDEGFVERLLNHPDVPELIRTSPLTQREWQVLGLIYSGYSNEQIAGELAVAATTIKTHIRNLYQKLGVAHRQDAVQHAQQLLKMMGYGV | Positively regulates the transcription of the maltose regulon whose gene products are responsible for uptake and catabolism of malto-oligosaccharides. Specifically binds to the promoter region of its target genes, recognizing a short DNA motif called the MalT box. | Q8Z227 |
Q9GK68 | GDF9_BOVIN | Growth/differentiation factor 9 | Bos | MALPNKFFLWFCCFAWLCFPISLDSQPSRGEAQIVARTALESEAETWSLLKHLDGRHRPGLLSPLLNVLYDGHREPPRLQPDDRALSYMKRLYKAYATKEGTPKSNRSHLYNTVRLFTPCAQHKQAPGDQAAGTLPSVDLLFNLDRVTVVEHLFKSVLLYTFNNSISFPFPVKCICNLVIKEPEFSSKTLPRAPYSFTFNSQFEFRKKYKWIEIDVTAPLEPLVASHKRNIHMSVNFTCVKDQLQHPSARDSLFNMTLLLAPSLLLYLNDTSAQAFHRWHSLHPKRKPSQDPDQKRGLSACPMGEEAAEGVRLSRHRRDQESVSSELKKPLVPASFNLSEYFKQFLFPQNECELHDFRLSFSQLKWDNWIVAPHKYNPRYCKGDCPRAVGHRYGSPVHTMVMNIIHEKLDSSVPRPSCVPAKYSPLSVLAIEPDGSIAYKEYEDMIATKCTCR | Required for ovarian folliculogenesis. | Q9GK68 |
Q30ZH4 | ISPE_OLEA2 | 4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase | Oleidesulfovibrio | MLTVPQQTIRSGCKINLFLEITGVRPDGYHELVTLFYPLSEPFDLMEISPATHGVTVLSERADLCGDKNIICKAWHTFAAAGGTPPPMQVRLAKGVPDGAGLGGGSANAAAVLKLLNTAGGAPRFSDTALAKIAAQVGADVPFFLHNTPCLATGIGEKLVPAPLDLSGWHLVLVCPGVQVSTPWAYNRWDTLYRSGLHHPCGQLPAAHAPAACAQLQTTGPDRPVRAETGCAGRKKNTCRSLTTERQADSKPVSRALWLFNSFETVVFSAYSELRQHKNTLLAHGASAALMSGSGSSLFGLFRDKAQAEAAMLHFCQRSIAVYVHRL | Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. | Q30ZH4 |
A6UVA8 | ASPD_META3 | L-aspartate dehydrogenase | Methanococcus | MLKIGIIGCGTIATMIAKAINYKKINGTIVALYDKHNDKSQDLNKLTNAKICDSIDKLVKEELDIVIECASIKSVEEVATKSLNHKKNVVIMSVGALADKNLFSKLYKIANDNEKKIFVPSGAIAGVDAIKTASIGRIDEVSLITTKPVYGLEDALKNKGIDTTNISEPTVVFEGTVFDAIKEFPQNINVSVVLSIASKIPAKVKIVADPSATSNKHEIIVKGSIGTIKTVVENNPCKDNPKTSALAAYSVIRLLKDLSEPIIVGT | Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate. | A6UVA8 |
Q5R6T1 | PDIA6_PONAB | Protein disulfide-isomerase A6 | Pongo | MALLVLGLVSCAFFLEVNGLYSSSDDVIELTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIFGSNKNRPEDYQGGRTGEAIVDAALSALRQLVKDRLGGQSGGYSSGKQGRSDSSSKKDVIELTDDSFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEVKEQTKGKVKLAAVDATVNQVLASRYGIRGFPTIKIFQKGESPVDYDGGRTRSDIVSRALDLFSDNAPPPELLEIISEDIAKRTCEEHQLCVVSVLPHILDTGAAGRNSYLEVLLKLADKYKKKMWGWLWTEAGAQSELETALGIGGFGYPAMAAINARKMKFALLKGSFSEQGINEFLRELSFGRGSTAPVGGGAFPTIVEREPWDGRDGELPVEDDIDLSDVELDDLGKDEL | May function as a chaperone that inhibits aggregation of misfolded proteins. Negatively regulates the unfolded protein response (UPR) through binding to UPR sensors such as ERN1, which in turn inactivates ERN1 signaling. May also regulate the UPR via the EIF2AK3 UPR sensor. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin. | Q5R6T1 |
Q8W3L1 | MFDR_ARATH | Mitochondrial ferredoxin reductase | Arabidopsis | MSRYLARYMVSRYFSSASSRPLHVCIVGSGPAGFYTADKVLKAHEGAHVDIIDRLPTPFGLVRSGVAPDHPETKIAINQFSRVAQHERCSFIGNVKLGSDLSLSELRDLYHVVVLAYGAESDKDLGIPGESLSGIYSAREFVWWYNGHPDYSSLKPDLKTSDSAVILGQGNVALDVARILLRPTTELASTDIATHALSALKESSIRKVYLIGRRGPVQAALTAKELREVLGIKNLHIRIKQTDLSVTPADEEEMKTSRARKRIYELLSKAAAAAKTSEADPDQRELHFVFFRQPDQFLESDERKGHVSGVNLQKTILESVGTGKQIAVGTGEFEDLNCSMVLKAIGYKSVPVNGLPFDHKKGVVPNVKGRVVSHTSGDISQTEPGLYVCGWLKRGPVGIIATNLYCAEETVGSISEDIEEGVWKSSKAGSKGLMQLLEKRKVKKVEFSGWEKIDAKEKQMGIERNKPREKLVTWEDLLAAAAN | Associates in vitro with the adrenodoxin-like protein MFDX1 to form an efficient low potential electron transfer chain that is able to reduce cytochrome C . Functions as accessory mitochondrial protein involved with BIO2 in the plant biotin synthase reaction . | Q8W3L1 |
Q7Z0Q2 | RNKB_CERCA | Cc RNase | Ceratitis | MKICGPKLSLCGLIISVWGIIQLVLMGLFFYINSVALIEDLPIDEEFNSVEEFYTAATSAYNQNAYNCWIAACIYVLTLLLSAQQFYVNSRATAN | Endoribonuclease which displays activity against poly(C) and poly(U) synthetic substrates, as well as rRNA. | Q7Z0Q2 |
Q8KAN7 | RNC_CHLTE | Ribonuclease III | Chlorobaculum | MSLQFLRSEASDGAGETSDASSADFLLDPQTATHLARLTGRPCNRLIYRTALTHRSVLHDHHSEEHKPESNQRLEFLGDAVLDLLISEHLFKQFPGSDEGHLSSNRAKIVNRKSLAAFALELQLGEHLIIGESADKQKIRTSESALADALEALVGAIYLDQGLAGAERFITNHVIAKVDLHKLVEAEYNYKSRLIEYTQSRQLPPPLYTVITEEGAEHEKTFVVEVSCNGQPLGRGTAPRKKDAEQLAAKEAMKRLESGDLGNLNEPSPQNS | Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism. | Q8KAN7 |
P66901 | DPAL_ECO57 | Alpha,beta-diaminopropionate ammonia-lyase | Escherichia | MSVFSLKIDIADNKFFNGETSPLFSQSQAKLARQFHQKIAGYRPTPLCALDDLANLFGVKKILVKDESKRFGLNAFKMLGGAYAIAQLLCEKYHLDIETLSFEHLKNAIGEKMTFATTTDGNHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILNLGAECIVTDMNYDDTVRLTMQHAQQHGWEVVQDTAWEGYTKIPTWIMQGYATLADEAVEQMREMGVTPTHVLLQAGVGAMAGGVLGYLVDVYSPQNLHSIIVEPDKADCIYRSGVKGDIVNVGGDMATIMAGLACGEPNPLGWEILRNCATQFISCQDSVAALGMRVLGNPYGNDPRIISGESGAVGLGVLAAVHYHPQRQSLMEKLALNKDAVVLVISTEGDTDVKHYREVVWEGKHAVAP | Catalyzes the alpha,beta-elimination reaction of both L- and D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. The D-isomer of serine is degraded to pyruvate, though very poorly; other amino acids (L-serine, D- and L-threonine, D- and L-beta-Cl-alanine) are not substrates. | P66901 |
Q21DK5 | ATPD_SACD2 | F-type ATPase subunit delta | Saccharophagus | MAEFTTLARPYAKAAFIAARDASDLGGWSKALATAAAVSQVDRVKTVLSAPGLTAQQKADAFVALCGEELAEKQQNFIHVLADNRRLALLPEISVLFDLYKANQEKSLDVTVETAFEIDAATEKKLVEALSKKLDREVTLSTAVDKALLGGALIRAGDTVIDGSVRGRLAKLAEAMNV | This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. | Q21DK5 |
Q9SU36 | ORP2B_ARATH | OSBP-related protein 2B | Arabidopsis | MPLTRSKSLPATENGGSDRETLQSGRSVAGILYKWTNYGKGWRSRWFLLRDGILSYSKIRRPENVNLLSPSDDLRLIGDISTDRLLRMKSCSGRSRRKHHKNIGIVHLKVSSYRESKSDHRKFYIFTATKTLHLRTDSRSDRAAWLQALASTRGIVPLQSINGDFSFVSPKDLSISTERLKKRLFEEGMNESLVKECEQIVDSEFCEVQEQIKLLHEERKKLLDALRQLEMANLEAEASGIHDDVYQLRNHKYSSLGRGKYSECSTSASSDDKQEFEDISEEDEASFHDTKESFGEPDVGSVLTHFKRRTKLPDPAEKERGVSLWSMIKDNVGKDLTRVCLPVYFNEPISSLQKCFEDLEYSYLLDQAYEYGKSGKSLLRALNVAAFAVSGYASTEGRHCKPFNPLLGETYEADFPEKGIRFFSEKVSHHPTVIACHCEGKGWKFWGDTNLRSKFWGRSIQLEPVGILTLEFDDGEIFQWSKVTTTIYNILLGKLYCDHHGIMKIRGNRQYSCMLKFKEQSILDRNPHQVNGFVEDVTGKKAATVFGKWNDSLYYVAGDGINKASASLLWKATKAPPNVTRYNFTSFAMTLNELIPGLEEKLPPTDSRLRPDQRHLENGEYEKANEEKQRLERRQRMSRQIQESGWRPRWFEPQGESESYKYTGGYWEARDVKSWDDCPNIFGEFTEEVADCA | May be involved in the transport of sterols. | Q9SU36 |
A0AEN2 | PURA_LISW6 | IMP--aspartate ligase | Listeria | MSSVVVVGTQWGDEGKGKITDFLSENAEAIARYQGGNNAGHTIKFDGETYKLHLIPSGIFYKEKISVIGNGMVVDPKALVEELKYLHDKGVDTSNLRISNRAHIILPYHIRIDEADEERKGANKIGTTKKGIGPAYMDKAARVGIRIIDLLDKETFKEKLEHNLGEKNRLLERFYELEGFKLEDILEEYYGYGQQFKDYVCDTSVVLNDALDDGKRVLFEGAQGVMLDIDQGTYPFVTSSNPIAGGVTIGSGVGPSKINHVVGVAKAYTTRVGDGPFPTELFDSIGDNIREVGREYGTTTGRPRRVGWFDSVVVRHARRVSGLTDLSLTLLDVLTGIETLKICVAYKLDGKTITEFPASLKDLARCEPVYEELPGWTEDITEVKSLDDLPVNCRHYMERIAQLTGVQVSMFSVGPDRAQTHVVKSVWRLA | 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. | A0AEN2 |
Q5N5U2 | CHLN_SYNP6 | Light-independent protochlorophyllide reductase subunit N | Synechococcus | MTTTEAPSALSFECETGNYHTFCPISCVAWLYQKIEDSFFLVIGTKTCGYFLQNAMGVMIFAEPRYAMAELEEGDISAQLNDFAELKRLCTQIKRDRNPSVIVWIGTCTTEIIKMDLEGLAPKLEAEIGIPIVVARANGLDYAFTQGEDTVLAAMPARCPEAATSEADQQERTNAIQRLLQFGKSPAAEQQPASSKHPPLILFGSVPDPVATQLTIELAKQGITVSGWLPAKRYTELPVIAEGSYAIGLNPFLSRTATTLMRRRKCKVIGAPFPIGPDGSRAWIEKICSVLEIEPQGLAEREAQVWDSIEDYRQLVEGKQVFFMGDNLWEISLARFLVRCGMRCPEIGIPYLDRRYLGAELAMLEATCQSMGVPLPRLVEKPDNYNQLQRIEALQPDLVITGMAHANPLEARGISTKWSVEFTFAQIHGFGNARAILELVTRPLRRNLALGTLGGSQWVSEAVTSR | 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. | Q5N5U2 |
P49371 | HUGA_DOLMA | Hyaluronoglucosaminidase | Dolichovespula | SERPKRVFNIYWNVPTFMCHQYGLYFDEVTNFNIKHNSKDDFQGDKISIFYDPGEFPALLPLKEGNYKIRNGGVPQEGNITIHLQRFIENLDKTYPNRNFNGIGVIDFERWRPIFRQNWGNMMIHKKFSIDLVRNEHPFWDKKMIELEASKRFEKYARLFMEETLKLAKKTRKQADWGYYGYPYCFNMSPNNLVPDCDATAMLENDKMSWLFNNQNVLLPSVYIRHELTPDQRVGLVQGRVKEAVRISNNLKHSPKVLSYWWYVYQDDTNTFLTETDVKKTFQEIAINGGDGIIIWGSSSDVNSLSKCKRLREYLLTVLGPITVNVTETVN | Hydrolyzes high molecular weight hyaluronic acid to produce small oligosaccharides. | P49371 |
Q219F8 | PTH_RHOPB | Peptidyl-tRNA hydrolase | Rhodopseudomonas | MRLLVGLGNPGAKYQGNRHNIGFMVLDEMARRHGFSPWRRRFQGETADGSIGGERVTLLKPLTYMNDSGRAVQDAASFFKLGLPDITVVHDEIELPAAKLRVKVGGGIAGHNGLRSISAHVGNDYRRVRIGVGHPGAKELVHGHVLNDFAKSERPWVEAMIEAIVEHAGLLVDGRDSTFQNKVHLALQAKGFLDNNDGSAA | The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. | Q219F8 |
Q38XW7 | PURL_LATSS | Phosphoribosylformylglycinamidine synthase subunit II | Latilactobacillus | MVNNPTAIEIQQTKLYQQWGLTDSEYELICTKILKRLPNYTETGLFSVMWSEHCSYKNSKPILKKFPTNGPHVLQGPGEGAGILDIGDGQAVVFKAESHNHPSAVEPYEGAATGVGGIIRDIFSMGATPIAILDSLRFGELNDNQTKYLVQEVVAGIGGYGNCIGIPTVGGEISFDPCYQANPLVNAMCVGLIEQKDIQQGKARGAGNSVLYVGAKTGRDGIHGATFASDEFAEGKATQRSAVQVGDPFMEKLLMDACLELILQHSDWLVGIQDMGAAGLVSSTAEMAAKAGTGMILDLDQVPQRETDMSAYEIMLSESQERMALCVRAGYEDQVIALFKGYDLDAVRIGEVTTKEQYQLWHQGQLVADLPVAALTDAAPVYHKDQAKPERLATFAAQAPYVPSVTDTQATWLALLKQPTIADKSSFYRHYDAQVKTNTVVLPGSDAAVVRIRGTKKALAMTTDCNGRYLYLDPHVGGQIAVAEAARNIVAAGGQPLGITDCLNYGNPEKPAVFWEFDQSAQGIAAACETFGTPVISGNVSLYNEFNGEAIYPTPMIGMVGLIRDIQDITTQDFKQVDDLIYLIGETDDNYAGSELQKMQQGTISDQLGHFSLATEKANQDLVLKAIQQGLITSAHDLSEGGLAVALSEATFKQGLGYHVQVDLASRQLFAETQSRFIVTVKAANQAAFEQISDQSAQLIGRVTAEPIMHIQTKDEMIDLTVEAAKDAWEAALPCLMKSEA | Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL. | Q38XW7 |
B1WUD1 | RIMO_CROS5 | Ribosome maturation factor RimO | Crocosphaera subtropica | MGNKPTISVSHLGCEKNRIDSEHMLGILAQQGYSIDANEELADYVIVNTCSFIQEAREESVRTLVELAEANKKIIISGCMAQHFQEQLLEELPEAVALVGTGDYQKIAEVIQRVETGERVTEVSQNPTFVADEMTPRYRTTNEAVAYLRVAEGCDYRCAFCIIPHLRGNQRSRSIESIVTEAQQLADQGVQEIILISQITTNYGLDLYGEPKLAELLRALGKVDIPWIRIHYAYPTGLTPKVIDAIRDTPNILPYLDLPLQHSHPAILKAMNRPWQGQVNDNIIERLKQSIPNAILRTTFIVGFPGETEEHFEHLINFVQRHEFDHVGVFTFSPEEETPAYQMPNQVPSEIAQARRNYLMEIQQPIAAKKNQKCVGQTVEVLIEQENPTTQEYIGRSIRFAPEVDGVVYVEGEGQLNSIIPVKITDADVYDLYGKVI | Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12. | B1WUD1 |
Q5YZ84 | GLNE_NOCFA | Adenylyl transferase | Nocardia | MVRPPSARSAVPGVGRLGLLDPTAAASLRELGWDNVESIPVLWALSRAPDADLALNTLMRLREALGSDWQRLDSAIRTDTSLRGRLFALLGSSTALGDHLVAEPAAWEVLRRGDLPDRDELLADLLAAVQATPEAGPHAGPMLFRAGIAGPEAVALLRCRYRDQLMLLAALDLAATVENEPVLPYRVVGRHLTDLADAALTAALAVAVARVCKDQPCPVRLAVIAMGKCGARELNYVSDVDVVFVAEPADATATRLAAEMMSVGSQAFFEVDAALRPEGKQGALVRTLDSHLTYYKRWARTWEFQALLKNRPMTGDLELGREYRDAVMPMVWTASERPDFVPEVQGMRRRVEDLVPAELRERELKLGRGSLRDVEFAVQLLQLVHGRVDENLHVASTVDALSALAAGGYVGRDDAANLTASYEFLRLLEHRLQLQRLKRTHTLPADDDEEGMRWLARAAHIRPDGRQDAMGVLRSEIRRNAVRVRRLHAKLFYRPLLEAVVRMDPDALRLSPDAAVRQLAALGYAAPENAFGHLKALTGGVSRKGRIQALLLPTLLEWLGETPNPDAGLLAYRRVSEALDEQTWFLRELRDEGAVAQRLMIVLGSSEFLPDLLINAPETIRMFADGPHGPLLLGPQPEEVARGILTAAARYDDPNRAVAAARSLRRHELARVASADLLGMLEVPQVCRALSSVWVAVLDAALAAVIRAGEAESGEPAPAAFAVIGMGRLGGMELGYGSDADVLFVCEPRPGVDETKAVKWANTVAERVQRLLGAPSTDPPLHVDAGLRPEGRSGALVRTLSAYQAYYGQWAQSWEVQALLRAHQVAGDQELGVRFLHAVDKVRYPAGGVSEDAVREIRRIKARVDSERLPRGADPATHTKLGRGGLADIEWTVQLLQLRHAHEVESLHNTATLETLAAIEKAELLAAEDVALLRDSWLLATKARNALVLVRGKPSDQLPGPGRLLSAVATVAGWPNNDGGSEFLDHYLRITRRARAVVERVFGS | Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB) which indicates the nitrogen status of the cell. | Q5YZ84 |
A1BD24 | RPOC_CHLPD | Transcriptase subunit beta' | Chlorobium | MIFSQGASPLKGDFSKIKFSIASPESILAHSRGEVLKPETINYRTFKPERDGLMCEKIFGPTKDWECYCGKYKRVRYKGIICDRCGVEVTTKSVRRERMGHISLAVPVVHTWFFRSVPSKIGALLDLSTKELERIIYYEVYVVINPGEPGAKQGIKKLDRLTEEQYFQIITEYEDNQDLDDHDSDKFVAKMGGEAIRLLLKSIDLNETAIHLRKVLKESSSEQKRADALKRLKVVEAFRKSYEPQKKTRKKAVGLFPEDELPEPYVFEGNKPEYMVMEVVPVIPPELRPLVPLEGGRFATSDLNDLYRRVIIRNNRLKKLIDIRAPEVILRNEKRMLQEAVDALFDNSRKANAVKTGESNRPLKSLSDALKGKQGRFRQNLLGKRVDYSGRSVIVVGPELKLHECGLPKSMAIELFQPFVIRRLVERGIAKSVKSAKKLIDKKDQVVWDVLEKVIDGRPVLLNRAPTLHRLGIQAFQPVLIEGKAIQIHPLVCTAFNADFDGDQMAVHVPLSQEAQLEAALLMLSSHNLILPQSGKPVTVPSQDMVLGMYYLTKSRPGDPGEGRIFYSDEDVLIAYNEDRIGLHAQIFVHFNGAVDQKFDPLRVLDTIVDPKSEKYTWLKSQLEKKTILLTTVGRVIFNQNVPDSIGFINRVIDKKVAKELIGRLSSDVGNVETAKFLDNIKEVGFHYAMKGGLSVGLSDAIVPDTKVRHIKNAQKDSTKVVKEYNRGTLTDNERYNQIVDVWQKTSNIVAEESYQKLKKDREGFNPLYMMLDSGARGSREQVRQLTGMRGLIARPQKSMSGQPGEIIENPIISNLKEGLTVLEYFISTHGARKGLSDTSLKTADAGYLTRRLHDVAQDVIVTIEDCGTTRGLHVYRNIEEETSGQIKFREKIRGRVAARDIYDTLNNNVIVKAGEIITEELGDLIQETAGVEEAEIRSVLTCESKIGICSKCYGTNLSVHQIVEIGEAVGVIAAQSIGEPGTQLTLRTFHQGGTAQGGISETETKAFYEGQLEFEDLKTVEHSAITEDGVEEIRIIVVQKNGKINIVDPDSGKILKRYVVPHGAHLHCNAKALVKKDQVLFSSEPNSTQIIAELHGRVKFADIEKGVTYKEEVDPQTGFAQHTIINWRSKLRANETREPRVLIIDESGEVRKNYPVPIKSNLYVEDGQKIVPGDIIAKVPRNLDRAGGDITAGLPKVTELFEARIPSDPAIVSEIDGYVSFGSQRRSSKEIKVKNDFGEEKVYYVQVGKHVLANEGDEVKAGDAMTDGAVSPQDILRIQGPNAVQQYLVNEIQKVYQINAGVEINDKHLEVIVRQMLQKVRVEEPGDTELLPGDLIDRSAFVEANNNVAEKVRVTEKGDAPSRIQEGQLYKTRDITKLNRELRKNSKNLVAFEPALQATSHPVLLGITSAALQTESVISAASFQETTKVLTDAAVAGKIDYLAGLKENVIVGKLIPAGTGLKRYRNLTLTGESVETISHDASDDASTQNGI | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | A1BD24 |
Q3KHC5 | DAPE_PSEPF | N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase | Pseudomonas | MTAHADLSPTLQLAIDLIRRPSVTPVDADCQKQMMQRLGDAGFQLEPMRIEDVDNFWATHGKGDGPVLCFAGHTDVVPTGPVTAWQIDPFNAVIDEHGMLCGRGAADMKGSLASMTVAAERFVADYPDHKGKVAFLITSDEEGPAHHGTKAVVERLAARNERLDWCIVGEPSSTTLVGDVVKNGRRGSLGAKLTVRGVQGHVAYPHLAKNPIHLAAPALAELAAEHWDHGNDFFPPTSFQISNVNSGTGATNVIPGDLVAVFNFRFSTESTVEGLQKRVADILDKHGLDWHIDWALSGLPFLTEPGALLDAVSSSIKDITGRETKASTSGGTSDGRFIATMGTQVVELGPVNATIHQVNERVLAADLDVLTEIYYQTLIKLLA | Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls. | Q3KHC5 |
Q8AXF4 | FBX43_XENLA | Xerp1 | Xenopus | MANLLENFAAHHSMTAGAKKKADHQDTSVSQDSGYSDSLKGFSPDSHKSGNFLETVTEGYENSENIDPTLILSPIKYELSWGADTRESKQLAPLYETPRVGKKEFSLRRRLLISKATSGGNLDFDVSVCSAESCGREKSLRRIPSHEGSLSNSFADSPRDGSYEPIATSTLKTESESGTSCKKWRLSFAQQRSSTLDDSKSDSIPLPEVENISPVQHSLASSTDDSILYEETIFGAPTTPTCNFIVKEEFQTPISNLAANFRFNLCTPDVGHVSDFDISVTEDSAFHSLSLDKSQDSITDHEGSFQELIQKPRETSKAVNNKSRLRKLDRCRRLSTLRERGSQSEVEEEGNEVPVLSSAYKLKVARASVDEENEFSSDESRVHSLLSSDDLTGKPALRVLHEMLLRSTRKRPQQATVQDLLGSSGCFELPEDSLSRLIGRKMGLETFDILAELKNRNLKHILASILDLVNAASICSMCRVSRDWRDVVLQDKSAHQRRKAYIKKLKTEAEQGRQLSFEDSATRLNILSRSALRSVQIQARSAFRTPTSSLTPGDNKSIHSASKHQEYLKVAKTLFTDEALKPCPRCQYPAKYQALKKRGTCSRKDCGFDFCSLCLCTFHGSKECGTGSAKRIPKKEALPGSAQSKRNLKRL | Required to prevent anaphase onset in cytostatic factor-arrested oocytes. Inhibits the anaphase-promoting complex/cyclosome (APC/C) ubiquitin ligase and prevents cyclin degradation. Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. | Q8AXF4 |
B3GXZ4 | LEXA_ACTP7 | LexA repressor | Actinobacillus | MSRKHLTARQQEIFDFVKHHIETTGMPPTRVEIAREIGFKSPNAAEEHLKALARKGYIEMLSGTSRGIRILVDNEETAANDDGLPLIGKVAAGTPIMAIEHVESHYPVNGAMFNPNADYLLKVNGNSMEKIGILDGDLLAVHKTNFARNGQVVVARVDDEVTVKRLEKKGDLIYLHPENDELQPIVVDPRIEYIEIEGIAVGVIRNNAWM | Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair. | B3GXZ4 |
O88516 | DLL3_MOUSE | Drosophila Delta homolog 3 | Mus | MVSLQVSPLSQTLILAFLLPQALPAGVFELQIHSFGPGPGLGTPRSPCNARGPCRLFFRVCLKPGVSQEATESLCALGAALSTSVPVYTEHPGESAAALPLPDGLVRVPFRDAWPGTFSLVIETWREQLGEHAGGPAWNLLARVVGRRRLAAGGPWARDVQRTGTWELHFSYRARCEPPAVGAACARLCRSRSAPSRCGPGLRPCTPFPDECEAPSVCRPGCSPEHGYCEEPDECRCLEGWTGPLCTVPVSTSSCLNSRVPGPASTGCLLPGPGPCDGNPCANGGSCSETSGSFECACPRGFYGLRCEVSGVTCADGPCFNGGLCVGGEDPDSAYVCHCPPGFQGSNCEKRVDRCSLQPCQNGGLCLDLGHALRCRCRAGFAGPRCEHDLDDCAGRACANGGTCVEGGGSRRCSCALGFGGRDCRERADPCASRPCAHGGRCYAHFSGLVCACAPGYMGVRCEFAVRPDGADAVPAAPRGLRQADPQRFLLPPALGLLVAAGLAGAALLVIHVRRRGPGQDTGTRLLSGTREPSVHTLPDALNNLRLQDGAGDGPSSSADWNHPEDGDSRSIYVIPAPSIYAREDWLIQVLF | Inhibits primary neurogenesis. May be required to divert neurons along a specific differentiation pathway. Plays a role in the formation of somite boundaries during segmentation of the paraxial mesoderm. | O88516 |
A1R6G5 | UVRC_PAEAT | Excinuclease ABC subunit C | Paenarthrobacter | MADPASYRPQTGEIPTTPGVYRFRDPHGRVIYVGKAKNLRSRLNSYFANPAGLLPKTHAMVHAASSVEWTVVGSELESLQLEYTWIKEFKPRFNVVFRDDKTYPYLAVTMGEKYPRVQVMRGERRKGTRYFGPYTAGAIRETMDTLLRVFPVRSCSAGVFKRAESSGRPCLLGYIDKCSAPCVGRVTPDEHRGLAEDFCSFMGGEAKRFISRLEKDMAAAVAELDYERAAGLRDDIIALRKVFERNAVVLAEDTDADVFALHEDELEASVQVFHVRGGRVRGQRGWVVEKVEDATTPELIEHLLQQVYGEDSEVQGRIPREVLVPENPSNHAELMEWLGGLRGARVDIRVPQRGDKAALMSTVRENAEQALKLHKTRRAGDITVRSLALQELQEALEIPVPLLRIECFDISHVQGTNVVASMVVVEDGLPKKSDYRKFSITGAAATDDTAAMHDVLTRRFRHYLTDKAAQVPIVSGEIVNPTRAGAKSGTELPPSDLDVPAPKAKFAYPPNLVVVDGGQPQVNAAARALAELGIDDVYVVGLAKRLEEVWLPDSDFPVILPRTSQGLYLLQRIRDEAHRFAITFHRQKRGKAMTVSVLDGVPGLGEAKRKALVAHFGSLKKIKAASVEELTSAKGIGPALAAAVVQHLGSTEDAGERAPAVNMTTGEILES | The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. | A1R6G5 |
Q01323 | OTC_NEIFL | Ornithine carbamoyltransferase | Neisseria | KTSTRTRCAFEVAARDQGAGVTYLEPSASQIGHKESIKDTARVLGRMFDGIEYRGFGQDVVEELAKYAGVPVFNGLTNEFHPTQMLADGLTMREHSDKPLNQIAFAYVGDARYNMANSLLVLAAKLGMDVRISAPKSLWPSENIIEMVQAVAKETGGRILLTENVQEAVKGVDFIHTDVWVSMGEPKEAWQERIDLLKDYRVTPELMAAAENPQVKFMHCLPAFHNRETKVGEWIYETFGLNGVEVTEEVFESEASIVFDQA | Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline. | Q01323 |
Q6D7I3 | KDPA_PECAS | Potassium-translocating ATPase A chain | Pectobacterium | MAADAFLLIFGLLLTVLIVAQPLGSGLARLIEGETGTLLQKFETKTARFFALDTTEMRWQQYAAAILALNLIGIVVLFVLLMAQGNLPLNPENMPGLSWHLALNTAVSFVTNTNWQAYSGENTLSYLSQMVGLTVQNFLSAASGIAVAFALIRAFSRRCVDTLGNAWLDLLRITLYVLLPLSLLLALFFVSQGVLQNLLPYQHLTTLDGAAQTLPMGPVASQEAIKLLGTNGGGFFGANSAHPFENPTALSNIVQMLAILLIPTALCFAFGKAVSDKRQGHALLWAMALIFIVAAAVVMKMEVTGNPHLLALGADSAANLEGKETRFGVLTSSLYAVVTTATSTGAVNAMHDSFTALGGMVPLWLMQIGEVVFGGVGSGLYGMLLFVLLTVFIAGLMIGRSPEYLGKKIEVYEMKMTALAILIPPALVLLGTALALSTEAGRGGILNPGAHGFSEVLYAVSSAANNNGSAFAGLSVNTPFYNVLLAVAMLLGRFAVMVPVLAIAGSLVVKKRQPESKGSLSTRSPLFIGMLIAIVLLIGALTFIPALALGPVAEHLQFGLTH | Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the periplasmic potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel. | Q6D7I3 |
Q32JQ8 | METN_SHIDS | Methionine import ATP-binding protein MetN | Shigella | MIKLSNITKVFHQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVLVDGQELTTLSESELTKARRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEIKRRVTELLSMVGLGDKHDSYPSNLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFIQSTLHLDIPEDYQERLQAEPFTDCVPMLRLEFTGQSVDAPLLSETARRFNVNNNIISAQMDYAGGVKFGIMLTEMHGTQQDTQAAIAWLQEHHVKVEVLGYV | Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system. | Q32JQ8 |
Q8RXS5 | DRL40_ARATH | pNd11 | Arabidopsis | MGGCVSVSISCDQLTKNVCSCLNRNGDYIHGLEENLTALQRALEQIEQRREDLLRKILSEERRGLQRLSVVQGWVSKVEAIVPRVNELVRMRSVQVQRLCLCGFCSKNLVSSYRYGKRVMKMIEEVEVLRYQGDFAVVAERVDAARVEERPTRPMVAMDPMLESAWNRLMEDEIGILGLHGMGGVGKTTLLSHINNRFSRVGGEFDIVIWIVVSKELQIQRIQDEIWEKLRSDNEKWKQKTEDIKASNIYNVLKHKRFVLLLDDIWSKVDLTEVGVPFPSRENGCKIVFTTRLKEICGRMGVDSDMEVRCLAPDDAWDLFTKKVGEITLGSHPEIPTVARTVAKKCRGLPLALNVIGETMAYKRTVQEWRSAIDVLTSSAAEFSGMEDEILPILKYSYDNLKSEQLKLCFQYCALFPEDHNIEKNDLVDYWIGEGFIDRNKGKAENQGYEIIGILVRSCLLMEENQETVKMHDVVREMALWIASDFGKQKENFIVQAGLQSRNIPEIEKWKVARRVSLMFNNIESIRDAPESPQLITLLLRKNFLGHISSSFFRLMPMLVVLDLSMNRDLRHLPNEISECVSLQYLSLSRTRIRIWPAGLVELRKLLYLNLEYTRMVESICGISGLTSLKVLRLFVSGFPEDPCVLNELQLLENLQTLTITLGLASILEQFLSNQRLASCTRALRIENLNPQSSVISFVATMDSLQELHFADSDIWEIKVKRNETVLPLHIPTTTTFFPNLSQVSLEFCTRLRDLTWLIFAPNLTVLRVISASDLKEVINKEKAEQQNLIPFQELKELRLENVQMLKHIHRGPLPFPCLQKILVNGCSELRKLPLNFTSVPRGDLVIEAHKKWIEILEWEDEATKARFLPTLKAFPENIDADGYEISF | Probable disease resistance protein. | Q8RXS5 |
B7GFR5 | CH10_ANOFW | Chaperonin-10 | Anoxybacillus | MLKPLGDRIVIELIQTEEKTASGIVLPDTAKEKPQEGKVVAVGSGRVLDNGERVAPEVSVGDRIIFSKYAGTEVKYDGKEYLILRESDILAVIG | 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 the GroEL ring, thereby capping the opening of the GroEL channel. | B7GFR5 |
Q8VWH2 | RFT1_ORYSJ | FLOWERING LOCUS T-like protein 3 | Oryza sativa | MAGSGRDDPLVVGRIVGDVLDPFVRITNLSVSYGARIVSNGCELKPSMVTQQPRVVVGGNDMRTFYTLVMVDPDAPSPSNPNLREYLHWLVTDIPGTTGATFGQEVMCYESPRPTMGIHRLVFVLFQQLGRQTVYAPGWRQNFSTRNFAELYNLGSPVATVYFNCQREAGSGGRRVYP | Probable mobile flower-promoting signal (florigen) that moves from the leaf to the shoot apical meristem (SAM) and induces flowering. Promotes the transition from vegetative growth to flowering under long day (LD) conditions. Acts upstream of MADS14 and MADS15. May also participate in the promotion of flowering under short day (SD) conditions. | Q8VWH2 |
B2T6J4 | CLPS_PARPJ | ATP-dependent Clp protease adapter protein ClpS | Paraburkholderia | MAIIPDKQDGTVLERQEKKLKPPSMYKVVLLNDDFTPMEFVVMVVQEYFNKDRETATQVMLKVHREGRGVCGVYTRDIASTKVEQVVTHARQAGHPLQCVMEEA | Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation. | B2T6J4 |
Q6EUP4 | 14335_ORYSJ | G-box factor 14-3-3 homolog E | Oryza sativa | MSQPAELSREENVYMAKLAEQAERYEEMVEFMEKVAKTVDSEELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEESRGNEDRCTLIKEYRGKIETELSKICDGILKLLDSHLVPSSTAPESKVFYLKMKGDYYRYLAEFKTGAERKDAAENTMVAYKAAQDIALAELPPTHPIRLGLALNFSVFYYEILNSPDRACNLAKQAFDEAISELDTLSEESYKDSTLIMQLLRDNLTLWTSDISEDAAEEIKEAPKGESGDGQ | Is associated with a DNA binding complex that binds to the G box, a well-characterized cis-acting DNA regulatory element found in plant genes. | Q6EUP4 |
Q330G9 | NU2M_SACBI | NADH dehydrogenase subunit 2 | Saccopteryx | MNPLIFTMIMLTVILGTTIVMMSSHWLMIWMGFEMNMLAVIPLLMKQYNPRSMEAATKYFLTQATASMLLMLAVIINLLYSGQWTFTKLMNPTASIIMTLALGMKMGLAPFHFWVPEVTQGISLSSGLILLTWQKLAPLSVLYVISPAINLDLILLMSMMSIAIGGWGGLNQTQLRKILAYSSIAHMGWMASILVFNPTMTLLNLLLYILMTTTTFMLFMVASATTTLSLSHMWNKMPLITTSTLTIMLSLGGLPPLTGFLPKWMIIQELTKNNNITLATLMAITALLNLFFYMRLTYATSLTMFPTTNNMKMKWQFNNKKQLKCLPVLIILSTITLPLAPAITLLN | 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. Essential for the catalytic activity and assembly of complex I. | Q330G9 |
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