UniProt ID stringlengths 6 10 | Protein Sequence stringlengths 5 15.6k | Functional Description stringlengths 6 12.4k |
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Q10731 | MASKNLFVLFFIFALFAANIAALQCPKNSEVRNSPCPRTCNDPYGQNSCITVIRETCHCKGELVFDSDSICVPISQC | Highly specific for fungal protease and subtilisin. Hemolymph. Belongs to the protease inhibitor I40 family. |
A5GFQ0 | MAEEEQRKKIPLVPENLLKKRKAYQALKATQAKQALLQKKEQRKGKELKFKRLEWFLHDSWRQLRDRVRLRRLEVKPHGLEVPDKHSLAFVVRIERISGVSSVVQRTIARLRLKKIFSGVFMQVTPQTIKTLRIVEPYVTWGFPNLKSVRELILKRGQAKVKNKIIPLTDNTVIEEHLGKFGVICLEDLIHEIAFPGKNFQAISGFLRPFQLSVARHATKNRVGFLKEVGSPGYRGERINQLIRQLN | Belongs to the universal ribosomal protein uL30 family. |
D6W0Q2 | MIVWQALFVVYCLFTTSIHGLFQDFNPFANKNISLKFPSLNRWEKNVMATGQQTIINSDSIYEWTPILSNITAGKKDSFVFTIDAEASGYGFAPTYEVLMFISGNICQMPMNRSDVDLTIYYSFNETVLENPNIGQSAVFQDGYIQALAISPVQSSSSNATSTYSNLYVVAELVNSTTEQPLSSSDASENWEYRLSISENDLVFQWDVRPWVEVLDTDMNSALLSTGNVTADAKVYHNYSIYDPSLYDLYVYSYEDSVQLNQNYNLSLCAVKNGPYLVSSQNTSNATVTSNSTNPLERTDLAIQKKITEYGGSVTEMFYV... | Calcium-permeable, cation-selective stretch-activated channel (SAC). Required for calcium influx and for vitality of MATa cells in a late, pheromone-induced event of the mating process requiring calcium induced signaling. Functions together with CCH1 to ensure that adequate levels of Ca(2+) are supplied to PMR1 to sust... |
Q1MFZ8 | MSQNSLRLVEDKSVDKSKALEAALSQIERSFGKGSIMKLGSNENVVEIETISTGSLGLDIALGVGGLPRGRIIEIYGPESSGKTTLALQTIAEAQKKGGICAFVDAEHALDPVYARKLGVDLQNLLISQPDTGEQALEITDTLVRSGAVDVLVVDSVAALTPRAEIEGEMGDSLPGLQARLMSQALRKLTASISKSNTMVIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRIGAVKEREEVIGNQTRVKVVKNKMAPPFKQVEFDIMYGEGVSKTGELVDLGVKAGIVEKSGAWFSYNSQRLGQGRENAKTFL... | Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage. Belongs to the RecA f... |
Q8SQ79 | MSVLTPLLLRGLTGSARRLPVPRAKIHSLPPDEKLGIMELAVGLTSCFVTFLLPAGWILSHLETYRRPE | Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CII... |
B2K814 | MTLKELVVGFGTQVRSLWMIGLHAFHKRETLMYPEEPVYLPPRYRGRIVLTRDPDGEERCVACNLCAVACPVGCISLQKAEQKDGRWYPEFFRINFSRCIFCGLCEEACPTTAIQLTPDFEMGEFKRQDLVYEKEDLLISGPGKYPEYNFYRMAGMAIDGKQKGEAENEAKPIDVKGLMP | NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are t... |
Q470E8 | MTAAEIDIRQILKLLPHRYPMLLVDRVLEFEPQKRIKTLKNVTINEPFFQGHFPGQPVMPGVMILEALAQSAGLLTFGADMERKEGALYYFVGIDGARFKQVVYPGDQLHMNVTVERYIRGIWKFKAFATVDEKVACEAELMCTVKQADA | Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs. a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O Belongs to the thioester dehydratase family. FabZ subfamily. |
A1DMR2 | MKDQLLVPLRRRPWTCRKCLQRLQLLPQHQTRRSFETAASPFPRQLDSLPADYSRTKTVDDDTLRRVFDSQQFWREFSQQRSAQPKPTGLVQNQYLTSPDGFRTFANVSLQKCQAIVSKVLAASTLEEYRTMARDLDRLSDLLCRVIDLSDFIRVIHPDPQVQEAATQAYALMFEYMNVLNTTTGLNDQLKKAAANPEVTSQWSDEEKIVAQILIKDFSNSAIHMPPHERQRFVNLSNDISQLGSSFVNGAEPAKSHVSVATNNLRGLDPILVQQIKRWNRTAAVPTTGMIPRLALRSVHDENVRREVYLASRTSSKRQL... | Cleaves proteins, imported into the mitochondrion, to their mature size. While most mitochondrial precursor proteins are processed to the mature form in one step by mitochondrial processing peptidase (MPP), the sequential cleavage by MIP of an octapeptide after initial processing by MPP is a required step for a subgrou... |
P13278 | MSNKESNVALQTLRVTKDMKDFLSHRIVGEPPANIKIEYQKIHRYRTCVCPSTGHISELCPSGDLILSLGAHRNVIAAATVYDVVKNKIKSTTSKAGTSSTLSSLGLSGFQKPKIGSKNKKTMFSKQNNSTNESDESGGEEGSSLNDLPKSDLINAIMELASQGRNNSKGKGKRGGKR | Constituent of viral factories. Binds to ssRNA and dsRNA (By similarity). Constituent of spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging. Belongs to the phytoreovirus RNA-binding protein family. |
Q39QQ5 | MPSFDIVSKVDMQEVDNAVNQAVKEIGQRYDFKGSKSEVTLEKDAIKILADDDFRLKAIVDILQSKFIKRGISPKALQYGKAETASGGMVRQIITVQQGISKEKGKEVVAVIKDTKLKVQGQIQDDQVRVTGKNRDDLQEAIRTLKGKDLGIELQFVNFRD | Belongs to the UPF0234 family. |
B2TZL3 | MSLFDKKHLVSPADALPGRNTPMPVATLHAVNGHSMTNVPDGMEIAIFAMGCFWGVESLFWQLPGVYSTAAGYTGGYTPNPTYREVCSGDTGHAEAVRIVYDPSVISYEQLLQVFWENHDPAQGMRQGNDHGTQYRSAIYPLTPEQDAAARASLERFQAAMLAADDDRHITTEIANATPFYYAEDDHQQYLHKNPYGYCGIGGIGVCLPPEA | Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein] [thioredoxi... |
B4L760 | MSGGLDILSLKEDDITKMLVATTHLGSENVNFQMEQYVFKRRADGVNIINLGKTWEKLVLAARAIVAIENASDVFVISSRPIGQRAVLKFAKYTDTTPIAGRFTPGAFTNQIQPAFREPRLLVVTDPNTDHQPIMEASYVNIPVIAFTNTDSPLRYIDIAIPCNNKSPHSIGLMWWLLAREVLRLRGTISRTTEWPVVVDLFFYRDPEEAEKEEAAAAKELLPPPKIEEAVDHPVEETTNWADEVAAETVGGVEDWNEDTVKTSWGSDGQF | Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Required during oogenesis and imaginal development. Component of the small ribosomal subunit. Mature ribosomes con... |
Q8SWR5 | MNDLKPATSYRSTSLHDAVKLRLDEPSSFSQTVPPQTIPEFFKESCEKYSDLPALVWETPGSGNDGWTTLTFGEYQERVEQAALMLLSVGVEERSSVGILAFNCPEWFFAEFGALRAGAVVAGVYPSNSAEAVHHVLATGESSVCVVDDAQQMAKLRAIKERLPRLKAVIQLHGPFEAFVDHEPGYFSWQKLQEQTFSSELKEELLARESRIRANECAMLIFTSGTVGMPKAVMLSHDNLVFDTKSAAAHMQDIQVGKESFVSYLPLSHVAAQIFDVFLGLSHAGCVTFADKDALKGTLIKTFRKARPTKMFGVPRVFEK... | Mediates activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation (PubMed:26893370, PubMed:29739804). Probably by regulating lipid storage and catabolism, plays a role in neuronal function (PubMed:25409104). a long-chain fatty acid + ATP + CoA = a long-chain fatty a... |
Q6IB09 | MEEASEGGGNDRVRNLQSEVEGVKNIMTQNVERILARGENLEHLRNKTEDLEATSEHFKTTSQKVARKFWWKNVKMIVLICVIVFIIILFIVLFATGAFS | SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. VAMP8 is a SNARE involved i... |
Q39CT5 | MVVAVYPGTFDPLTRGHEDLVRRASSIFDTLVVGVADSRAKKPFFSLEERLTIANEVLGHYPNVKVMSFTGLLKDFVRTNNARVIVRGLRAVSDFEYEFQMAGMNRYLLPDVETMFMTPSDQYQFISGTIVREIAQLGGDVSKFVFPSVEKWLTEKVAAMGGPVA | Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. Homohexamer. Belongs to the bacterial C... |
P11818 | MKRARPSEDTFNPVYPYDTETGPPTVPFLTPPFVSPNGFQESPPGVLSLRLSEPLVTSNGMLALKMGNGLSLDEAGNLTSQNVTTVSPPLKKTKSNINLEISAPLTVTSEALTVAAAAPLMVAGNTLTMQSQAPLTVHDSKLSIATQGPLTVSEGKLALQTSGPLTTTDSSTLTITASPPLTTATGSLGIDLKEPIYTQNGKLGLKYGAPLHVTDDLNTLTVATGPGVTINNTSLQTKVTGALGFDSQGNMQLNVAGGLRIDSQNRRLILDVSYPFDAQNQLNLRLGQGPLFINSAHNLDINYNKGLYLFTASNNSKKLE... | Forms spikes that protrude from each vertex of the icosahedral capsid. Interacts with host coxsackievirus and adenovirus receptor CXADR located at the cell tight junctions to provide virion initial attachment to target cell. The fiber protein binds to CXADR with a higher affinity than CXADR binds to itself, thereby blo... |
P0A5K8 | MLKGFKEFLARGNIVDLAVAVVIGTAFTALVTKFTDSIITPLINRIGVNAQSDVGILRIGIGGGQTIDLNVLLSAAINFFLIAFAVYFLVVLPYNTLRKKGEVEQPGDTQVVLLTEIRDLLAQTNGDSPGRHGGRGTPSPTDGPRASTESQ | Channel that opens in response to stretch forces in the membrane lipid bilayer. The force required to trigger channel opening depends on the nature of the membrane lipids; the presence of phosphatidylinositol enhances mechanosensitivity of the channel. May participate in the regulation of osmotic pressure changes withi... |
Q5WAV8 | MKRYIEICKPLWTLLPEGTIHEDERLCKHTYTQMGGAADLFITPQSYEETQTVLKFAHEHRVPVTLLGNGSNVIVKDGGIRGITLSLKKLNTITCTGVELVAQTGATIIEASRRARDAELTGLEFACGIPGTVGGAFYMNAGAYGGQIADVLESVLVLTEQGEFKTLSKEEFDFDYRKSVFSAKRYIALEGTFRLQKGDMAQIQAKMDELTIARETKQPLEYPSCGSVFKRPPGMFAGKLIQDSGLQGTRIGGAEVSKKHAGFIVNVDNATATEYMSLVRHVQQTVKDKFGVELETEVITIGEDIEEPVSD | Cell wall formation. NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine Cell wall biogenesis; peptidoglycan biosynthesis. Belongs to the MurB family. |
B0SCV6 | MSHSHRDALFQWMKTYVYRHSETPFRLASGLESQHYFNCKEITLHPERLSILAECFIEEIIPKLNIEFQAVGGLTLGADPIAYAISLGYQKRGKNVFPLVVRKESKGHGTGQQIEGFWKDIKTCLVVDDVITTGGSTLKAVKVLREVGINVTKGICILDREEGGSENLQTENVTMTSIFAKSEFF | Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orot... |
P96848 | MALDLTAYFDRINYRGATDPTLDVLQDLVTVHSRTIPFENLDPLLGVPVDDLSPQALADKLVLRRRGGYCFEHNGLMGYVLAELGYRVRRFAARVVWKLAPDAPLPPQTHTLLGVTFPGSGGCYLVDVGFGGQTPTSPLRLETGAVQPTTHEPYRLEDRVDGFVLQAMVRDTWQTLYEFTTQTRPQIDLKVASWYASTHPASKFVTGLTAAVITDDARWNLSGRDLAVHRAGGTEKIRLADAAAVVDTLSERFGINVADIGERGALETRIDELLARQPGADAP | Catalyzes the transfer of the acetyl group from acetyl coenzyme A to the free amino group of arylamines and hydrazines (PubMed:18795795). Is able to utilize not only acetyl-CoA, but also n-propionyl-CoA and acetoacetyl-CoA as acyl donors, although at a lower rate (PubMed:19014350). As acetyl-CoA and propionyl-CoA are p... |
Q6DH95 | MAGDMLLLMRGLARLSQAVIETQANSLRSGGVQTMQMTAEQAMGVAMQKIQEFTGSQQSVSDFSADMDSKYDFTASEQNFESAAHGGLDSDSVFRDANTGAANTYSQAQGKSKLFDGYKDPTSQFTGHTRSYHQDHSSVGGITAEDIEKAREAKQNGSKPHKQMLSERARERKVPVTRLGRLANFGGLAVGLGIGALAEVAKKSLRSEDKNGNKKAVLDSSPFLSEANAERIVRTLCKVRGAALKLGQMLSIQDDAFINPQLAKIFERVRQSADFMPIKQMTKALSNDLGPNWRDKLEMFEERPFAAASIGQVHLARMKD... | Atypical kinase involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration. Its substrate specificity is unclear: does not show any protein kinase activity. Probably acts as a small molecule kinase, possibly a lipid kinase that pho... |
Q17551 | MSFFLREIDGERVCSTSTETSIPEDRKSARRLRKLLYKCAENTCKPDILRVPAHCGKLDKEEEKSKTPLDQQQQINFHDILNSKFVVGPPSPFALVAIAKSILARFGNPEEVSEKEDGSEEEAGTSGADEEGKQYKNTDQLVGASLTCIFEVLEQLSRRDAELCVQALESLLSLIQSMPIDCLQSENRLSMSAMMHVLKTLREDACPSVSSKATSCLVALSVACGEPEHLGSTIRSLICMKKNIRMSADSTYDMIQMPENLRKLLLKVRRKALGGDNTANSPPNWAMVDVHEHSVASSFSLPSLPDSSPSSDTPDDDNRI... | Atypical E3 ubiquitin-protein ligase which specifically mediates ubiquitination of threonine and serine residues on target proteins, instead of ubiquitinating lysine residues (By similarity). Shows esterification activity towards both threonine and serine, with a preference for threonine, and acts via two essential cat... |
A9IJ22 | MKALLDLFKQVSQDEQFDAIKIGIASPEKIRSWSYGEVRKPETINYRTFKPERDGLFCSKIFGPIKDYECLCGKYKRLKHRGVICEKCGVEVTVAKVRRERMGHIELASPVAHIWFLKSLPSRLGMVLDMTLRDIERVLYFEAWCVIEPGMTPLKRGQIMSDDDFLAKTEEYGDDFRALMGAEAVRELLRTIDIDREVETLRGELKATSSEAKIKKISKRLKVLEGFQKSGIKAEWMVMEVLPVLPPDLRPLVPLDGGRFATSDLNDLYRRVINRNNRLKRLLELKAPEIILRNEKRMLQEAVDSLLDNGRRGKAMTGAN... | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1) Binds 1 Mg(2+) ion per subunit. Binds 2 Zn(2+) ions per subunit. The RNAP catalytic core consists of 2 alpha, 1 beta, 1 b... |
Q39578 | MPALSPAKKGTDKGKTGKKTGKQEQNAQDYIPPPPPMPGDEAFAMPIREIVKPDNQLWLSEADLNEEVAKMLTANNPAAPKNIVRFNMKDKVFKLEPMVEQTVVHYATDGWLLHKSSDEAKRQMDMEKMEQEASARFQADIDRASHEHKDHGDVEPPDDSRQLRNQFNFSERAAQTLNYPLRDRETFTEPPPTATVSGACTQWEIYDEYIKDLERQRIDEAMKSKGGKKAAAAARAAGAAHRQRNEHVPTLQSPTLMHSLGTLDRMVNQNMYEEVAMDFKYWDDASDAFRPGEGSLLPLWRFVSDKSKRRQVTSVCWNPL... | Is essential for arm assembly or attachment to the outer doublet microtubule. Consists of at least 3 heavy chains (alpha, beta and gamma), 2 intermediate chains and 8 light chains. Belongs to the dynein intermediate chain family. |
B4T5B9 | MQQFEWIHGAWLGLAIMLEIAANVLLKFSDGFRRKCYGILSLAAVLAAFSALSQAVKGIDLSVAYALWGGFGIAATLAAGWVLFGQRLNPKGWVGVILLLAGMVMIKFA | Catalyzes the excretion of spermidine. Forms a complex with MdtJ. Belongs to the drug/metabolite transporter (DMT) superfamily. Small multidrug resistance (SMR) (TC 2.A.7.1) family. MdtI subfamily. |
Q0AUM4 | MIVSAMEKAEILVEALPYIKDFYGRRVVIKYGGAAMTDCELKQKVMQDIVLMKFVGMHPIVVHGGGPEINQMLSRLGIQSEFVNGFRVTDAATMEIVEMVLGGKVNKEIVAGIHASGGKAVGISGKDGMLIQAHPADGSGKMGFVGEVQYVNPELIEKVIENGYIPVIAPIGIGEDQQSYNINADLVAAAIAVSMKADKLVLLTDVPGLMMNPADSNSLISVLKVSEVENYVQEGIIAGGMVPKVQCCVEAVTGGVGRTHIIDGRVPHSILLEIFTDEGIGTMVVNE | Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. Belongs to the acetylglutamate kinase family. ArgB subfamily. |
A7ZW80 | MIRTMLQGKLHRVKVTHADLHYEGSCAIDQDFLDAAGILENEAIDIWNVTNGKRFSTYAIAAERGSRIISVNGAAAHCASVGDIVIIASFVTMPDEEARTWRPNVAYFEGDNEMKRTAKAIPVQVA | Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. H(+) + L-aspartate = beta-alanine + CO2 Binds 1 pyruvoyl group covalently per subunit. Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1. Heterooctamer of four alpha and four beta subunits.... |
A6X570 | MAEPGFLSLTLIGALVFGYFLGSIPFGLILTRLAGLGDVRSIGSGNIGATNVLRTGNKKLAAATLIFDMLKGTVAVLVASRYGPDAAIGAGFGAFIGHLFPVWIGFKGGKGVATYLGVLIGLAWPGALVFAAVWIVTALLTRYSSLAALIASIVVPIALYSRGYPAIAVLFAIMTVIVIFKHKANITRLLNGTESKIGAKG | Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP. an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate Lip... |
B8ZQ12 | MDIKSEVIEIIDELFMEDVSDMMDEDLFDAGVLDSMGTVELIVEIENRFDIRVPVTEFGRDDWNTANKIIAGIVELQNA | Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC-carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester bond, proba... |
Q5KIP8 | MGGGDLNMKKSWHPVLLVNQERVWKAEKVANEEKKMLAQLRKEREEERQLEELHRLQEASTGKKRVEKLDWMYAAPSTEGGALGGARIGERDMEEYLLGKKRVDEVLGQGDKNIGAASREFIALQNANTARDTAAKIREDPLLAIKKQEQAALAALMNRPDIRKQLRAAKKAKETKGREGESKEERKARKRAEKEERRKSKHRYHDSRSPPSDYYDDRDHRRHRDSYDSQDRENRRTYRDRSDRSRTRSESPKREKKEKDYSNRDRDYRRRNDTTRGSFDESPRKGGGNRWGSHGPDGYRRSDHRDDGFRERQRGDRIPP... | Involved in pre-mRNA splicing. Associated with the spliceosome. Belongs to the CWC25 family. |
D6VRT0 | MTIAPITGTIKRRVIMDIVLGFSLGGVMASYWWWGFHMDKINKREKFYAELAERKKQEN | Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CII... |
Q11AV8 | MPELPEVETVRRGLEPVMEGARIIHVEQRRADLRFPFPAGFSEHVKGCRIEALGRRAKYLLLHLENGRVLVSHLGMSGSFRIEESGSDKLRGDFHYARSKAEKHDHVVFHLARHEGGSARVIYNDPRRFGFMLLLDSADLEAHPLFAGLGVEPTGNALDGALLARLLAGKRAPLKAALMDQRLVAGLGNIYVCEALWRAGLSPRRIAATIATREGKSTGRSERLAGAIRTVIAEAIAAGGSSLKDYVQADGSLGYFQHSFSVYDREGKPCRKEGCSGTIQRFVQGGRSTFYCPICQR | 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. ... |
B0UIW7 | MNSLDLPKAPQDTRVVVAMSGGVDSSVVAGLLRRQGYDVVGITLQLYDHGAATHRRGACCAGQDIHDARRAAETLGIPHYVLDYEDRFREAVIDRFAESYIHGETPIPCVECNRSIKFRDLLATALDLGADALATGHYVASRARPGGGRALYRALDPARDQSYFLYATTPEQLDVLRFPLGELPKDETRRLAREFGLAVADKPDSQDICFVPQGRYQDVIARLRPDAARPGEIVHLDGRTLGRHEGIIGFTVGQRRGLGLATGEPLYVVRLDPETARVVVGPREALATSVIRIAETNWLGDEPLADLDGMPVAVRVRSTR... | Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein] Belongs to the MnmA/TRMU family. |
P16266 | MPHHEFECSKVIPERKKHAVIKGKGETLADALPQGYLNTIPGSISERGCAYCGAKHVIGTPMKDVIHISHGPVGCTYDTWQTKRYISDNDNFQLKYTYATDVKEKHIVFGAEKLLKQNIIEAFKAFPQIKRMTIYQTCATALIGDDINAIAEEVMEEMPEVDIFVCNSPGFAGPSQSGGHHKINIAWINQKVGTVEPEITGDHVINYVGEYNIQGDQEVMVDYFKRMGIQVLSTFTGNGSYDGLRAMHRAHLNVLECARSAEYICNELRVRYGIPRLDIDGFGFKPLADSLRKIGMFFGIEDRAKAIIDEEVARWKPELD... | This iron-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation. Other nitrogenase complexes utilize a molybdenum-iron protein or a vanadium-iron protein. 16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]-[ferredoxin] = 16 ADP + 6 H(+) + H2 + 2 NH4(+) + 8 oxidized [2Fe-... |
Q7MAX1 | MNTTDTIVAQATPPGRGGVGILRVSGPKAAQVAEVVLGKLPKPRYADYLPFRDVDGQILDQGIAIYFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTLSGVRIANPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSAMNSLQGAFSTQVHQMVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAKLDEVIVELERVRSQARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDSTTTNAVEPVEIWPEF... | Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34. Binds 1 potassium ion per subunit. Homodimer. Heterotetramer of two MnmE and two MnmG subunits. Belongs to the TRAFAC cla... |
Q660I8 | MKIAVLLSGGVDSSIALYKVINKGYTNIKCYYLKIWLEDELSYIGNCPWQEDLNYVEAVCNKFNIPYEIINFQKEYYNKVVIYTIEELKNGNTPSPDIFCNQRIKFGAFFEKINEQYDLVVTGHYARIQIKEKKFFLKQAKDKIKDQSYFLSHLSQEQMSKLYFPLGTLFKSEVRQIAKSINLPNKDRKDSQGICFLGKIKYNEFIKYHLGEKKGNIVEKETGKIIGIHNGYWFFTVGQRRGIKLSNGPWFVIEKDLEKNIIYISHNENYLKQAKRKFLVHEIHWINGMPSDFENFKIKIRHGEKKYSCKLRLITNNLIE... | Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein] Belongs to the MnmA/TRMU family. |
Q7MCS5 | MRIAILSRNENLYSTMRLKQAGEARGHEVDVIDTLHCYMDITSNNPKIRYKGEELPQYDAIIPRIGASVTFYGTAVVRQFEMMGTFVVNESVAISRSRDKLRSLQLLSRKGIGLPRTGFAHHPDNIQDVIRNVGGAPLVIKLLEGTQGIGVVLAETNKAAESVIEAFMGLKANIMVQEFIEEAKGADIRCFVVGNKVIAAMKRQAKEGEFRSNLHRGGSAQLVRLSKEERATAINAAKVMGLNLCGVDILQSKNGPVVMEVNSSPGLEGIEQATNKDVAGMIYEFIEKNAKPNSNRTKGRG | Binds 2 magnesium or manganese ions per subunit. Belongs to the RimK family. |
Q8EWT2 | MSKNKLLLGSHVGFKAKNYLVGSVLETLEYDGNCFMVFTGPPQNFMRKELDQNLIDEAVKLMKEKNPLLLENIVVHAPYLINLGSPKESTRSLGLNQLIVEINRTNQIHSKLIVLHPGSALDSDRNVAINHIADNLNKAIEATDNDVIICVETMAGKGSEVGINFEEVSKIVSGVKNKKRIGVCLDTCHMHDSGIDISDPDQTLEEFSKYLDLSYIKVIHLNDSKNEIGSRKDRHDNIGYGKVGFDYLVKWAHNEKLANVPKILETPYRDDKPIYKQEIINLNSKEWKE | Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate. Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products. Binds 3 Zn(2+) ions. Belongs to the AP endonuclease 2 family. |
A1V5Z5 | MDFSIKGCDWSKGTANGFLTGKSDCIVLGVFEAQTLSGAALDIDEATKGLVSRVIKAGDIDGKLGKTLFLHEVSGIGASRVLLVGLGRQDAFSQKAYGDAAKVAWRALLGTKVVQVTFTLAQLPVPERASDWGVRAAILALRNETYKFTQMKSKPDAGAPALKRVVFSVDPADDKAAKVAAKQAVALANGMDLTRDLGNLPGNVCTPTYLANTAKKIAKDWGLKVDVLGLKQIQALKMGSFLSVAKGSVEPPQFIVLQYRGAAAKAAPVVLVGKGITFDSGGISLKPGEGMDEMKYDMCGAGSVLGTMRAVAEMGLKVNV... | Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, ... |
B4TZP6 | MSKLFWAMLAFISRLPVPSRWSQGLDFEQYSRGIVMFPFIGLILGGVSGLIFILLQSWCGIPLAALFCILALALLTGGFHLDGLADTCDGIFSARRRERMLEIMRDSRLGTHGGLALIFVLLAKILVVSELALRGTPMLAALAAACAAGRGSAVLLMYHHRYARDEGLGNVFIGKVSGRQTCITLGLAVIVATVLLPGMQGLAAMVVTLAAIFILGQLLKRTLGGQTGDTLGAAIELGELIFLLALL | Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate. adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+) adenosylcob(III)inamide-GDP + alp... |
Q58967 | MKEIYRLVDVSYKYPNGSIALDNVNLNIYKNEVVAILGPNGAGKTTLLKILDGLVFPDKGEVYFEGKKLTDEILRDKELMKEFRRKVGFVFQNPDVMLFNPTVWDEVAFSPLHLYSKEKAIEVTDKTLKDMKIYHLKDRHPYNLSGGEKKKVSISCILSVEPEVILMDEPTSALDPKSRAEIMNLIKSFKECGKTVVLVTHDLNLACLADRCYVLNKKVIFEGKVKDLFSLNLDELNLDVPEISKLFIKLKNMGYNINEIPVTLDEAVNIISKLFQKY | Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system (By similarity). Belongs to the ABC transporter superfamily. |
B4F040 | MKNSIIKSAITCLLLLSPSTFAATDIIGGEMEFKGVVVAHGCTIVAGDENKVIDFKQISAKDLYSLQKSNPVAFSISLENCSQDIYKSVTITLDGQAHSTMPNHIAVTGSGSEDPKSIGIAFTDKAHNIIELKKPSAPQQLNNKRVQFNFMAYVEATSSAIQNQTILTGPFQAQATYTLNYQ | Belongs to the fimbrial protein family. |
B0TXF5 | MNWSDILAEEKQKPYFKKILEFLANEALVGKTIFPTKANIFNAFKYTRLDNLKVVILGQDPYHNYNQAHGLAFSVQQGVDIPPSLRNIYKELERSITEFKIPEHGCLINWAKQGVFLLNTTLTVEAHKANSHKDIGWEIFTDAVIQKISNNKPNVVFMLWGSHARKKKNLIDTAKHLVLESSHPSPLSVYRGFDGCDHFVKANQYLTSKDLDIIDWRL | Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil. Belongs to the uracil-DNA glycosylase (UDG) superfamily.... |
Q14FN3 | MTNRYTTLFANLEKRNEGAFIPFVTIGDPNKALSFEIIDTLVSSGADALELGIPFSDPLADGPTIQEANIRALESGITPKDCFDILTKIRAKYPHIPIGLLLYANLVYANGIENFYQKCLDAGVDSILIADVPAHESKEFRDIAKKVGIAQIFIAPPDASESTLKQISELGSGYTYLLSRVGVTGTETAANMPVEDVLTKLREYNAPKPVLGFGISKPEQVQQAIKAGAAGAISGSATVKIIQNNISNKQKMLNELTYFVKEMKAATLN | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step... |
B0C9E9 | MNQLKTASLLGLLSALLIGSSYALLGGSGGMVMGIGLAALTNLGAWYYSDQIALSAYQAQLVRPNQAPHLYAVVQRLAQRANLPMPRLYIIPSSAANAFATGRDPDHAAIAVTEGLLRMLPAAELEGVLAHELAHIQNRDTLTQAVAATLAGAIAFLAQMVSYSFWFFGSRGNDRESNPIGALLMIVLAPLSATILQLGISRTREFSADETAARLTGQPRALAQALSRLESNAQRNALGGNPAFAPLLIINPPVRQWLSNLFTTHPSTQDRINRLLKLEQQLQRRPSIAFTSL | Binds 1 zinc ion per subunit. Belongs to the peptidase M48B family. |
P55548 | MVRYNAVEDPLCYPGTHVLRNRANIPDQNELDEFEQLMFDSRAREALPDGDLDFAHYRALHRHFFQDVYEWAGQTRIIRTGKGENWFCYPEYIEREANRLFAELAARDHLARTESKEAFAKGASWFLAEINAIHPFREGNGRTQLVFLTMLTRYAGYELDESKLEPKRFLDAMIRSFSGDLAPLAAEIRRMI | Probable adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins. ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein] ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-[protein] + diphosphate Belongs to the fic family. |
A5CC63 | MSITVERKKALISEYADLENNTGSVEVQCAILTERIINLTQHCKINFKDFHSKRGLLMLVSSRRKLLSYLKKKDLNRYTQLINRLGLRK | One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform of the 30S subunit by binding and bridging several RNA helices of the 16S rRNA. Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome. Part of the 30S ribosoma... |
Q6ZST0 | MGFLEEEGRWNLSFSGAGYLGAHHVGATECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSVDFCCSHLLGMVGQLERLSLSILHPAYAPIEHVKQQLQDALPPDAHVLASQRLGISLTRWPDGRNFLVTDFATCDELIQALVCTLYFPFYCGLIPPEFRGERYIDGALSNNLPFADCPSTITVSPFHGTVDICPQSTSPNLHELNVFNFSFQISTENFFLGLICLIPPSLEVVADNCRQGYLDALRFLERRGLTKEPVLWTLVSKEPPAPADGNWDAGCDQRWKGGLSLNWKVPHVQVKDVPNFEQLSPELEAALKK... | Has abundant triacylglycerol lipase activity. a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+) Expressed in brain and pituitary gland. No differential expression during adipocyte differentiation. |
Q9V3Q8 | MSDDWDDEPIVDTRGARGGDWSDDEDTAKSFSGEAEGDGVGGSGGEGGGYQGGNRDVFGRIGGGRGGGAGGYRGGNRDGGGFHGGRREGERDFRGGEGGFRGGQGGSRGGQGGSRGGQGGFRGGEGGFRGRLYENEDGDERRGRLDREERGGERRGRLDREERGGERGERGDGGFARRRRNEDDINNNNNIVEDVERKREFYIPPEPSNDAIEIFSSGIASGIHFSKYNNIPVKVTGSDVPQPIQHFTSADLRDIIIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPHELELGRPQ... | Involved in translational control mechanisms operating in early stages of oogenesis. Required maternally in many stages of oogenesis, including cystocyte differentiation, oocyte differentiation, and specification of anterior-posterior polarity in the developing cysts. Essential for the formation and/or structural integ... |
Q46669 | MKKYIISLIVFLSFYAQADLTDFRVATWNLQGASATTESKWNINVRQLISGENAVDILAVQEAGSPPSTAVDTGTLIPSPGIPVRELIWNLSTNSRPQQVYIYFSAVDALGGRVNLALVSNRRADEVFVLSPVRQGGRPLLGIRIGNDAFFTAHAIAMRNNDAPALVEEVYNFFRDSRDPVHQALNWMILGDFNREPADLEMNLTVPVRRASEIISPAAATQTSQRTLDYAVAGNSVAFRPSPLQAGIVYGARRTQISSDHFPVGVSRR | Part of the tripartite complex that is required for the CDT activity. CdtB exhibits a DNA-nicking endonuclease activity, and very probably causes DNA damage in intoxicated cells. This damage induces G2/M cell cycle arrest, chromatin fragmentation, cell distention and nucleus enlargement. Heterotrimer of 3 subunits, Cdt... |
Q8C8C1 | MRIFRPWRLRCPALHLPSFPTFSIKCSLPPLPTDEDMCKSVTTGEWKKVFYEKMEEVKPADSWDFIIDPNLKHNVLAPGWKQYLELHASGRFHCSWCWHTWQSPHVVILFHMYLDKAQRAGSVRMRVFKQLCYECGTARLDESSMLEENIESLVDNLITSLREQCYGERGGHYRIHVASRQDNRRHRGEFCEACQEGIVHWKPSEKLLEEEATTYTFSRAPSPTKPQAETGSGCNFCSIPWCLFWATVLMLIIYLQFSFRTSV | Specifically promotes functional cell surface expression of olfactory receptors, but not of other GPCRs. Interacts with olfactory receptors. Effective cell surface expression depends upon interaction with olfactory receptors. Predominantly expressed in olfactory and vomeronasal organs, in mature olfactory sensory neuro... |
Q6LUH3 | MYLPQEIIRKKRDNVELTADEINFFIQGIAKETMSEGQIAAFAMAIYFNDMTMDERVALTCAMRDSGMVIDWSHMNFDGPIVDKHSTGGVGDVTSLMLGPMVAACGGFVPMISGRGLGHTGGTLDKLESIPGYNITPTNDVFGQVTKDAGVAIIGQTGDLAPADKRVYATRDVTATVDNISLITASILSKKLAAGLGSLVMDVKVGSGAFMPTYEASEDLAKSIVAVANGAGTKTTALLTDMNQVLASTAGNALEVREAVQFLTGEYRNPRLFEVTMALCAEMLVNSGLASDIEQAREQLQAVLDNGKAATCFGKMVAGL... | The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis. phosphate + thymidine = 2-deoxy-alpha-D-ribose 1-phosphate + thymine... |
B1LNN7 | MTTIVSVRRNGHVVIAGDGQATLGNTVMKGNVKKVRRLYNDKVIAGFAGGTADAFTLFELFERKLEMHQGHLVKAAVELAKDWRTDRMLRKLEALLAVADETASLIITGNGDVVQPENDLIAIGSGGPYAQAAARALLENTELSAREIAEKALDIAGDICIYTNHFHTIEELSYKA | Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. ATP-dependent cleavage of peptide bonds with broad specificity. Allosterically activated by HslU binding. A double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. The... |
P0C569 | MSKDLVHPSLIRAGIVELEMAEETTDLINRTIESNQAHLQGEPLYVDSLPEDMSRLRIEDKSRRTKTEEEERDEGSSEEDNYLSEGQDPLIPFQNFLDEIGARAVKRLKTGEGFFRVWSALSDDIKGYVSTNIMTSGERDTKSIQIQTEPTASVSSGNESRHDSESMHDPNDKKDHTPDHDVVPDIESSTDKGEIRDIEGEVAHQVAESFSKKYKFPSRSSGIFLWNFEQLKMNLDDIVKAAMNVPGVERIAEKGGKLPLRCILGFVALDSSKRFRLLADNDKVARLIQEDINSYMARLEEAE | Non catalytic polymerase cofactor and regulatory protein that plays a role in viral transcription and replication. Stabilizes the RNA polymerase L to the N-RNA template and binds the soluble protein N, preventing it from encapsidating non-genomic RNA. Also inhibits host IFN-alpha and IFN-beta signaling by binding and r... |
A8ESV2 | MTHKREIQGVVVKKSGDKTASVLVTRSVLHPKYHKTVKRFKKYLIHDEKNELNVGDSVIAIECRPLSKTKSFRLKTIVATGVK | One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. Part of the 30S ribosomal subunit. Belongs to the universal ribosomal protein uS17 family. |
O66468 | MDIQEIMEILPHRYPILLVDKILEIEEGKRIIGLKNVSVNEPVFQGHFPGFPLFPGVYILEAMAQVGGILMIKSLNLEIGKYAVVFAGIDDARFKKPVYPGDQLILELEVISLKKALSKMKGVAKVDGEVVAQATLMAAARKLEDIKRNA | Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs. a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O Belongs to the thioester dehydratase family. FabZ subfamily. |
Q06SH6 | MGIRFLRSYTPGTRNRSVSDFNEITINKPEKSLTFSHHRCKGRNHRGIITCRHRGGGHKRLYRQIDFQRDKTKVPAQVLSIEYDPNRNARIALLRYPDGEKRYILHPRGLKIGETVISDVNASIQTGNTLPLRNIPLGTEVHNVEFQPGSGGQLARSAGTLVELLAKEGDFVTLRLPSKEIRLISRHCWATIGQVGHVEAYSIVVGKAGRTRWLGIRPTVRGSVMNPVDHPHGGGEGRAPIGRSRPVTPWGKPALGQKTRKPKKQSNKLILRKRKK | Part of the 50S ribosomal subunit. Belongs to the universal ribosomal protein uL2 family. |
C5E1G5 | MVLDPSRYQDHRTWKMTPGLIRARQPFFKKNMIGLAILAGVSAGIYTYTYSFLHKDNDFADVPIPPIDEKELEKLKKEYEQHKQERQ | Required for assembly of cytochrome c oxidase (complex IV). Component of 250-400 kDa complexes called cytochrome oxidase assembly intermediates or COA complexes. Belongs to the COA3 family. |
Q110D1 | MAQFHYECVESKTDKDRSQYGKFIIEPLARGQGTTVGNALRRVLLSNLEGTAITSVRIAGVNHEFATIKGVREDVLEILLNMKEVVLKSYSEQPQIGRLRVEGPATVTADRFDVPSEVEVIDRSQYIATLSPGSILEMEFRIEKGTGYKAVDRTRDDVATLDFLQIDAIFMPVRKVNYTIEDAHIGSSLEQDRLIMDIWTNGSYTPQDALSNAAGILMSLFEPLKDITNMADIPSGETTDPTSQIPIEELQLSVRAYNCLKRAQINSVADLLDYSQEDLLEIKNFGQKSAEEVIEALQKRLGITLPQEKVAKAT | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1) In cyanobacteria the RNAP catalytic core is composed of 2 alpha, 1 beta, 1 beta', 1 gamma and 1 omega subunit. When a sig... |
C5CPF1 | MMDKGAPRGTRTGFTTGACSAAAARAAVIGLVTGQVPDHVECLLPNGDLVRFAVHDGRVDSASAHAMVIKDAGDDPDCTDKAHLTADVRLLPDLAGQVVLAGGTGVGTVTMPGLGLAVGGPAINPVPRRNIEANVRAVGAALLDEVGLEVAISVPQGEEMAKKTLNARLGILGGISILGTTGIVKPYSTAAYRASVVQGVQVAGTLGHGVVVLTTGGRTEKFVMAEMPELPEPAFVQMGDFLRYAMGAAVKAGIRKVVIGGMVGKLTKIAQGETITHAGRAEVDTGLLADLAAGLGAPPDVCDAIRGNETARYAGERMDA... | Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A. Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10. Belongs to th... |
Q9VFZ5 | MGKIPAIGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFNETERLIGDPAKNQVAMNAKNTVFDAKRLIGRKFDDKKIQEDLKLWPFKVINEKGKPKIEVEFKGERKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGSIAGLNVLRIINEPTAAALAYGLDKNLKGERNVLIFDLGGGTFDVSVLSIDEGSLFEVKATAGDTHLGGEDFDNRLVNHFAEEFKRKHKSDIKGNARALRRLRTACERAKRTLSSSTEASLEIDALHEGIDFYSKISRARFEELNMDLFRSTMQPVER... | Heat shock cognate proteins are expressed constitutively during normal development. Belongs to the heat shock protein 70 family. |
B5XL29 | MSEKIRVLLYYKYVSIENAQEYAAKHLEFCKSIGLKGRILIADEGINGTVSGDYETTQKYMDWVHSDERFADLWFKIDEENQQAFRKMFVRYKKEIVHLGLEDNNFDSDINPLETTGEYLNPKQFKEALLDEDTVVLDTRNDYEYDLGHFRGAIRPDIRNFRELPQWVRDNKDKFMEKRVVVYCTGGVRCEKFSGWMVREGFKDVGQLHGGIATYGKDPEVQGELWDGAMYVFDDRISVPINHVNPTVISKDYFDGTPCERYVNCANPFCNKQIFASEENETKYVRGCSPECRAHERNRYVQENGLSRQEWAERLEAIGE... | Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs. AH2 + O2 + uridine(34) in tRNA = 5-hydroxyuridine(34) in tRNA + A + H2O Belongs to the TrhO family. |
Q49WD6 | MRYTILSKGDSKSNALKHKMINHMKDFQMVEDPDNPEIVISVGGDGTLLQAFHQYSYMLSRCAFVGIHTGHLGFYADWLPHEVEKLIIEINNSEFQVIEYPLLEIIVRYNDNGYETRHLALNEATMKTENGSTLVVDVNIRGNQFERFRGDGLCISTPSGSTAYNKALGGALIHPSLEAMQIAEIASINNRVFRTVGSPLVLPKHHTCLITPVNQDTILTTIDHVSIKHKNVNAIQYRVANEKIRFARFRPFPFWKRVHDSFISSGDDE | Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP. ATP + NAD(+) = ADP + H(+) + NADP(+) Belongs to the NAD kinase family. |
B6YV12 | METGAVTGILNTTLAVVFTWVGYKTARIVWKYTPYSYPNARIKAMEAKLLSEQRFNELAESRTLNNFVVSLEDTDYKDYLASVSNYTVEEIERALERALAGTYELMVTILPKRVNPFFRLLLEEWDVRNITSVIKAKMVNEPASDYVVEIGTMLPKVKAMAEAKTMEEILVILEGTPYEEPYQKLLLGEISLKEFETELYRMYYAKLLNYALSKKEDERVILEEFVRLKIDKTNILTLLRAKAAKMGAEEIKPLIIPGGTIKLDSILHVDDLSMALAELDSTRYGAVIRDVREEVERDLSVLERALDRHIRERMNELTRF... | Produces ATP from ADP in the presence of a proton gradient across the membrane. Belongs to the V-ATPase V0D/AC39 subunit family. |
Q2FWZ2 | MRKRARIIYNPTSGKELFKRELPDALIKLEKAGYETSAYATEKIGDATLEAERAMHENYDVLIAAGGDGTLNEVVNGIAEKPNRPKLGVIPMGTVNDFGRALHIPNDIMGALDVIIEGHSTKVDIGKMNNRYFINLAAGGQLTQVSYETPSKLKSIVGPFAYYIKGFEMLPQMKAVDLRIEYDGNVFQGEALLFFLGLTNSMAGFEKLVPDAKLDDGYFTLIIVEKSNLAELGHIMTLASRGEHTKHPKVIYEKAKAINISSFTDLQLNVDGEYGGKLPANFLNLERHIDVFAPNDIVNEELINNDHVDDNLIEE | Catalyzes the phosphorylation of diacylglycerol (DAG) into phosphatidic acid. Is a key enzyme involved in the production of lipoteichoic acid by reintroducing DAG formed from the breakdown of membrane phospholipids into the phosphatidylglycerol biosynthetic pathway. a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glyc... |
B6JKY3 | MALNLEKKQEIIKAFATKENDTGSCEVQVALLNERIKLLTEHLKANPKDHSSRLGLLKLVAQRRNLLKYIKRTAHARYVVLIEKLGIKDR | One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform of the 30S subunit by binding and bridging several RNA helices of the 16S rRNA. Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome. Part of the 30S ribosoma... |
Q2W015 | MKKVGVIGGGAWGTALALTARRAGRDVVLWAREPQVVDDINVRHVNSDFLPGIDLDPALRATVDLADAADADAVLLVSPAQHLRAAARALAPHWRAGVPAVICSKGIELSTCALMQDAIAAELPQAPIAVLSGPTFAIEVARGLPTAITLACAAPELGRKLVEALGTASFRPYLSDDLVGAQIGGAVKNVLAIACGIVEGRGLGDNARAALITRGLAEMTRLAMAKGGRPETLMGLSGLGDLILTASSTQSRNYSWASPWARAAPWPTSWASAIR | NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH NADP(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADPH Membrane lipid metabolism; glycerophospholipid metabolism. Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family. |
B2HKQ2 | MAKKSKIVKNNKRRDIVARYAQRRAELKQIIQSPTSSYEQRLDAQRALSRQPRDASAVRLRNRDAIDGRPRGHLRKFGLSRVRVRELAHAGQLPGVRKASW | Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site. Part of the 30S ribosomal subunit. Contacts proteins S3 and S10. Belongs to the universal ribosomal protein uS14 family. |
A3PD39 | MRKSVIAGNWKMHMTCAEAKSYLEEFIPLIKNIKDDRKVVIAPPFTAISTFSDHSDFEYLDISSQNIHWEDQGAFTAEISPKMLLEHGVSYAIVGHSEPRKYFSESDEQINKRAVFAQSSGLTPIVCVGETLEQRERGEADRVITRQVEQGLENTDPSNLIVAYEPIWAIGTGKTCEAEDANKICSLIRKLIGFDDVIIQYGGSVKPNNIDEIMSMSDIDGVLVGGASLDPNSFARIANYQ | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate Carbohydrate biosynthesis; gluconeogenesis. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphat... |
A8HAG8 | METVISFTAIAVAIMIGLAALGTGIGFAILGGKFLEASARQPELAPALQTKMFIVAGLLDAISMIAVGVALFFVFANPFLGQLAG | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ... |
Q0TQU5 | MELNTLKSTFINNFGKEPTSLFFSPGRINLIGEHIDYNGGFVFPCPITLGTFAAASLREDRICRAYSLNFESLGVIEFSLDDLSYKKEDNWTNYLKGVLKVLIEKGYKIDKGIDLVINGNLPNGAGLSSSASLEMLIVKILDTFFSLNISKVDAALIGKEVENTYIGVNSGIMDQFAISLGEKDKAILLDCNSLYYEYVPLNLGDNSIIIMNTNKRRELADSKYNERRKECDDSLDTLKKYTNISSLCELTSLEFETYKDKIEDSNKLRRCVHAISENERVKDAVKALKENNLELFGQLMNQSHISLRDDYEVTGKELDT... | Catalyzes the transfer of the gamma-phosphate of ATP to D-galactose to form alpha-D-galactose-1-phosphate (Gal-1-P). alpha-D-galactose + ATP = ADP + alpha-D-galactose 1-phosphate + H(+) Carbohydrate metabolism; galactose metabolism. Belongs to the GHMP kinase family. GalK subfamily. |
Q31M81 | MSRLVLAIGNSRWHWGIFSRDQAPQFWDAIAPHQPFSRSDLATFLQAQDPAIVADTPIAIASVVPQQLALLPEDWPQRRLQLRDVPLTNCYPQLGLDRAIALYEAGCQAGWPVLMIDCGTAITINAGDAEGQFAGGAILPGVTLQLRSLAQGTAALPSVEISAEGDRWGMDTQSAIASGVIYGIAGALRGFIEDWRSHHPQRPIYFTGGDGELLAKLLTDLPDIRVEPHLLLHGIDRLAQAMMTDPD | Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+) A monovalent cation. Ammonium or potassium. Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5. Homodimer. Belongs to the type III pa... |
Q9BZP8 | MAVNVYSTSVTSENLSRHDMLAWVNDSLHLNYTKIEQLCSGAAYCQFMDMLFPGCVHLRKVKFQAKLEHEYIHNFKVLQAAFKKMGVDKIIPVEKLVKGKFQDNFEFIQWFKKFFDANYDGKDYNPLLARQGQDVAPPPNPGDQIFNKSKKLIGTAVPQRTSPTGPKNMQTSGRLSNVAPPCILRKNPPSARNGGHETDAQILELNQQLVDLKLTVDGLEKERDFYFSKLRDIELICQEHESENSPVISGIIGILYATEEGFAPPEDDEIEEHQQEDQDEY | Plus-end tracking protein (+TIP) that binds to the plus-end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth. May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes. Also acts as a regulator of minus-end microtubule organi... |
B7HYU3 | MKKYILSLDQGTTSSRAILFNKKGEIVHSAQKEFTQHFPKPGWVEHNAQEIWGSILAVIATCLSEADVKPEQIAGIGITNQRETAVVWDKTTGKPIYNAIVWQSRQTAEICDELKEKGYSEMVREKTGLLIDAYFSGTKVKWILDNVEGAREKAENGDLLFGTIDTWLVWKLSGGKAHVTDYSNASRTLMFNIHDLQWDDELLDMLTVPKSMLPEVRPSSEVYGETIDYHFFGQNVPIAGVAGDQQAALFGQACFGEGMAKNTYGTGCFMLMNTGEKAVASEHGLLTTIAWGIDGKVNYALEGSIFVAGSAIQWLRDGMR... | Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate. ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate Activated by phosphorylation and inhibited by fructose 1,6-bisphosphate (FBP). Polyol metabolism; glycerol degradation via gly... |
P39845 | MSEHTYSLTHAQRRVWFTELLEPDTSICNLTACVKFKGNIELDTLEGALNHSISRNDAIRFQLLEGEELEPRLHLTEYKYYPLRIIDFSNVEMIEIEQWIQDQASIPFKLFNSPLFQFYLLRIDSHEVWLFAKFHHIIMDGISLNVMGNQIIDLYQKMKKKDPLPDQPEPSYLSYIEKESQYLQSPRFAKDRLFWTQTFEHPLEYHSLADQTSLQKQSTSASRDTIILSPDLEQTIRIFCEEHKINIISLFMASFYICISRITSKKDLAIGTYYGNRGSKAEKEMLGMFVSSLPIRITVDPDTDFLSFVRTIGREQLSVM... | This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Glu and Orn as part of the biosynthesis of the lipopeptide antibiotic lipastatin. The Orn residue is further epimerized to the D-isomer form. The activation sites for these amino acids consist of individual domains. Binds 2 phosph... |
Q10558 | MDFVIQWSCYLLAFLGGSAVAWVVVTLSIKRASRDEGAAEAPSAAETGAQ | Required for wild-type expression of ArfA and ammonia secretion, not however part of an ammonia transporter. Part of the arfA-arfB-arfC operon. Upon operon disruption no reduction of serine uptake at pH 6.9, no visible effect on outer membrane permeability, however severe delays in ammonia secretion, medium pH neutrali... |
A7M6E8 | MATAQSNSPRVFCIGTADTKFDELRFLSEHVRSSLNSFSNKSSFKVGVTVVDVSTSRKETNSCADFDFVPSKDVLSCYARGEGTVGRFPDIRGQAIAIMNKALETFLSKANGEQNLAGVIGLGGSGGTSLLSSAFRSLPIGIPKVIISTVASGQTESYIGTSDLVLFPSVVDICGINNVSKVVLSNAGAAFAGMVIGRLESSKEHSITNGKFTVGVTMFGVTTPCVNAVKERLVKEGYETLVFHATGVGGRAMEDLVRGGFIQGVLDITTTEVADYVVGGVMACDSSRFDAILEKKIPLVLSVGALDMVNFGPKTTIPPE... | Inhibitor of viral RNA replication which confers resistance to some tobamoviruses including tobacco mild green mosaic virus (TMGMV) and pepper mild mottle virus (PMMoV), but not to tomato mosaic virus (ToMV strains L, ToMV0 and ToMV1-2) and tobacco mosaic virus (TMV) (PubMed:17699618, PubMed:3686829, PubMed:17238011, P... |
Q2YYM7 | MRILVEIAYQGNNFLGFQIQQNGRTVQQQFEKLLQRMHKRHVRIHPSSRTDRGVHAIQQYFHFDTELNIPMSQWQYAMNRTLPVDIYVNNVVTVDDDFHCRYDCVGKRYRYKVYQAQHRDPFQRGLKTFIPEPLDLDKMNRAAQQFIGTHDFTGFCSQKTEVESKVRTLYQSEIVKTDDGFDYIVTGSGFLYNMVRVLVAFLIEVGKGRHEVSDVPKLLESKNRKNVPFTAPAEGLYLEKIYLDENELLKDFGNDIKIHRKKSLQND | Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA Homodimer. Belongs to the tRNA pseudouridine synthase TruA family. |
Q19LH4 | MSTETMIQDVELAEEALPKTRGPQGSKRRLFLSLFSFLLVAGATALFCLLHFGVIGPQKDELSKDFSLISPLALAVRSSSRIPSDKPVAHVVANPQAEGQLQWLNRRANALLANGVELRDNQLVVPSEGLYLVYSQVLFKGQGCPSNFMLLTHSISRIAVSYQAKVNLLSAIKSPCQRETPQGAKTNPWYEPIYLGGVFQLEKGDRLSAEINLPDYLDLAESGQVYFGIIGL | Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions ... |
Q54C71 | MELSEPKQRFESLLSLFEDVANKRYSGDFSVKKNINAPQVPPRSYSLFNVTGGNVSSYNNQQQQQNNNNNNNNNNNNNNNNNNNNNNNNNNSGEISSNNSTPSILFSPTPTSTAPPAPPQPTTPPNTGFHNRPLSININQQPIGGVNNNNNNNNKDSPSNKPLRLSGSPPTASINGNQIEQLQRELRNEKEAHQQTKYLLNSFADENKKLSNDCQLWRAKYFKLLTKNTKLKVIFDHFQSIMNESDSVPGEGSLVHSTSYNSSSSSSSGGGGNITPRKLSLAGGGKFDDAPQSASALLKIHHQRNQSTGSAFSNTIYNGE... | ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. |
A9ISK1 | MSVTAAQVKELRELSGAGMMDCKAALAETNGDMDAAVDWLRKKGIAKADKKAGRTAAEGLIGVVSKDSHAVLVEINSETDFVARNDGFQDIVRNVATAALDTPGDVESVSVSLYPGSEKTVELTIKDAIGTIGENMTFRRSAKLSVENGVVATYIHNSVSDGLGKLGVLVAIETTGNKEAALAFGRQVAMHIAATNPLALTAQDVDAGAVEREKAIFSDQARQSGKPENIIEKMVEGRMRKFFEEVVLLSQAFVMNPDMTVEAALKDAEKSIGAPAKITGFIRFALGEGVEKEETDFAAEVAAAVKG | Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. Belongs to the EF-Ts family. |
Q3TA07 | MPRGDSEQVRYCARFSYLWLKFSLIIYSTVFWLIGGLVLSVGIYAEAERQKYKTLESAFLAPAIILILLGVVMFIVSFIGVLASLRDNLCLLQSFMYILGICLVMELIGGIVALIFRNQTIDFLNDNIRRGIENYYDDLDFKNIMDFVQKKFKCCGGEDYRDWSKNQYHDCSAPGPLACGVPYTCCIRNTTDVVNTMCGYKTIDKERLNAQNIIHVRGCTNAVLIWFMDNYTIMAGLLLGILLPQFLGVLLTLLYITRVEDIILEHSVTDGLLGPGAKSRTDTAGTGCCLCYPD | Regulates maturation and trafficking of the transmembrane metalloprotease ADAM10 (PubMed:23035126, PubMed:26668317). Promotes ADAM10-mediated cleavage of (CDH2) (PubMed:26668317). Negatively regulates ligand-induced Notch activity probably by regulating ADAM10 activity (By similarity). Interacts with ADAM10; the intera... |
A4TSE5 | MNILNLKIIMFLLISNTIVVGGAWATSTCPDWPATRIAVEINALEQQLNKWSAAYHQQGHSPVTDDIYDQLQDKLRVWQSCRGLPDKTESQPIPGKGQFLHPVAHTGLKKLKDETALTRWMAGRKNLWVQPKVDGVAVTLVYHGGKLVQLLSRGNGVKGQNWTEKAPFISAIPQYIANAPALLTLQGELFLLMDGHQQAKSGGVNARSTVAGALMRKSPSPLLAQVGVFIWAWPDGPTTMKEKVALLQVMGFPFTAKYSEPVMSHLDVVQWRQFWFQAPLPFVTDGVVVRQEEEPAGRYWQATPGQWSMAWKYPPLQHIA... | Catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D... |
Q58232 | MAMSLKKIGAIAVGGAMVATALASGVAAEVTTSGFSDYKELKDILVKDGQPNCYVVVGADAPSTMDVVSAADIAAKIGSLCYKEGTVEDGSADITVHAEANSDDFDLKKDWNNSAMPANAYALFVAASDGDYSEKFENDTGKPSFMDNGVLGDADKINKTVDLGDIATMMKVDDVDPSDWYDSDDDAGEIVMVELKNDTSDGFTVYKKNMLYETLVYKDDEENFANTTKMEEGMRIPFLGKEMVVVDIDKDDDAIYLGTPVYDGIIKEGETYDLGNGYQVKIKAILKTTVNNTDVYKVDVQILKDGKVVAEKYDKAPLEL... | S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of the cell. Belongs to the Mj S-layer protein family. |
Q6NTH6 | MYRVPEFYARRKRLGGQTPYLMDQLGLRLGMWYWKDETRTLEFRRFAAEDSVQWLLKHHPHFTPAAEVKEKGKKGKAVHFAETDGPASDRLTDKRLAAKDDKSAKAVEKRGQQGTITLDDVKFVTLLLLQDTEMQRICSFTTFMRNKNLDNFLMALLYYLSHYLEKNSLEKKPKSYMVGLVEKKEMELVLSELEAAQRYLAQKYCILVLGLAVPDKHHMCCGKEKISDTQKDWKFFESFYTFCTYVAWIVFRRQHLTEIEEEVGRLFRTNMFNIPRRRREDEESGGEKKRMTFVQFRRMMAKRPAIKKAINMRSPVMSTL... | Inhibits phosphatase activity of protein phosphatase 1 (PP1) complexes. Interacts with PPP1CA. |
Q0T6Q2 | MQEQYRPEEIESKVQLHWDEKRTFEVTEDESKEKYYCLSMLPYPSGRLHMGHVRNYTIGDVIARYQHMLGKNVLQPIGWDAFGLPAEGAAVKHHTAPAPWTYDNIAYMKNQLKMLGFGYDWSRELATCTPEYYRWEQKFFTELYKKGLVYKKTSAVNWCPNDQTVLANEQVIDGCCWRCDTKVERKEIPQWFIKITAYADELLNDLDKLDHWPDTVKTMQRNWIGRSEGVEITFNVNDYDNTLTVYTTRPDTFMGCTYLAVAAGHPLAQKAAENNPELAAFIDECRNTKVAEAEMATMEKKGVDTGFKAVHPLTGEEIPV... | ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu) Belongs to the class-I aminoacyl-tRNA synthetase family. |
Q7TT91 | MAKGKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLSNKFGGEARGYDQIDAAPEEKARGITINTSHVEYETETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLSRQVGVPYIIVFLNKADMVDDAELLELVEMEVRELLSKYDFPGDDTPIVKGSAKLALEGDKGELGEQAILSLAQALDTYIPTPERAVDGAFLMPVEDVFSISGRGTVVTGRIERGVVKVGEEIEIVGIKPTVKTTCTGVEMFRKLLDQGQAGDNVGILLRGTKREDVERGQVLAKPGSINPHTDFTAEVYILSKEEGG... | This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. Monomer. Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily. |
Q03Z44 | MAEEKALNDQMLARRQKLATIVSDLHLDPFGKRFERTAKAQELHNLYDASSLEELENAKHEVVIAGRMVAKRGAGKVIFADFRDVSGKIQVYARRDDLADNYPIIKRADLGDFLGIKGIMMKTEAGELTVLATELTHLSKALRPMPDKFHGISDVETRYRKRYLDLIANEDSFKKFQERSHIISAIRAYMDRNDFLEVETPILQTEAGGAAARPFITHHNALNIDMYMRIATELYLKRLVVGGMERVYEIGRIFRNEGMDPKHNPEFTTMESYAAYMDFTDVMDETEGIFKAAASVVSDDLKITYQGTEIDLGTKFARKH... | ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys) Binds 3 Mg(2+) ions per subunit. Homodimer. Belongs to the class-II aminoacyl-tRNA synthetase family. |
Q10T06 | MREILHIQGGQCGNQIGAKFWEVVCAEHGIDATGRYDGDSDLQLERVNVYYNEASCGRFVPRAVLMDLEPGTMDSVRSGPYGHIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDAVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGK... | Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 1... |
Q04KW8 | MPKQKTHRASAKRFKRTGSGGLKRFRAYTSHRFHGKTKKQRRHLRKASMVHSGDYKRIKAMLTRLK | Belongs to the bacterial ribosomal protein bL35 family. |
A1JNQ2 | MSTLFIADLHLSVQEPAITAGFLHFIQREAIHADALYILGDLFESWIGDDDPEPLYRQIAAALKSLQQHGVPCYFIHGNRDFLLGKRFAVESGMTLLPEEKVVDLYGRKIVILHGDTLCTDDADYQHFRRRVHNPIIQKLFLWLPLRFRLRIAAYMRNQSQQNNSGKSQLIMDVNPHAVVETFERNSVSWMIHGHTHRPAVHTVELASTTAHRVVLGAWHVEGSMVKVTADKVELIKFPF | Hydrolyzes the pyrophosphate bond of UDP-2,3-diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. H... |
Q9ZH28 | MKTGIHPEYRPVVFVDTSTDFKFLSGSTKSSSETIKWEDGNEYPLLRVEISSDSHPFYTGKQKHATADGRVDRFNKKYGLK | Part of the 50S ribosomal subunit. Belongs to the bacterial ribosomal protein bL31 family. Type B subfamily. |
Q1IDJ5 | MLPFWIALQFLSSLPVRLPGMPTPNEMGRSLLFYPVVGLLFGLLLWLASHLLQGAPAPLHAALLLALWVLLSGALHLDGLADSADAWLGGFGDRERTLQIMKDPRSGPIAVVVLVLVLLLKFCALWVLVERGTGGWLVLAPVVGRAAMLGLFMGTPYVRKGGLGAALAEHLPRRAAGWVLLGSVLGCVVLGGSPGLWMLLLSLGVFLWLRRLMCKRLGGTTGDTAGAMVELLELAVLVGLALMV | Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate. adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+) adenosylcob(III)inamide-GDP + alp... |
Q0HHI5 | MQDRFIRSITQLPTPLADALIPLLHQNFAGHIDAQQLAELVQSSKMTEAEVLLALLPIAAALAKPPISEFYVGAIAKGKSGDIYMGANLELPGEALFHSVHAEQSAISHAWLSGESQIVDMIVNASPCGHCRQFMNELVEGGQIKIHLPSQDSHLLSYYLPYAFGPKDLNVQSPLLVKHETEFALDSSDPMVIEALDHAGLSYAPYTQSYAAVVLETSDGATYCGRYAENAAFNPSMLPMQMALSNLTRHNRDFGEIRRAVLVESSQGKISLVGATMDALHAVAAIELEHIVVDPV | This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. cytidine + H(+) + H2O = NH4(+) + uridine 2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+) Binds 1 zinc ion. Homodimer. Belongs to the cytidine and deoxycytidylate deaminase family. |
B1JK10 | MTTNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPTQHGEVFVTEDGAETDLDLGHYERFIRTKMTRRNNFTTGRIYSEVLRKERRGDYLGATIQVIPHITNAIKERIIEGGEGHDVVLVEIGGTVGDIESLPFLEAIRQMAVDVGREHTLYMHLTLVPYLAAAGEVKTKPTQHSVKELLSIGIQPDVLICRSDRAVPANERAKIALFCNVPEKAVISLKDVDSIYKIPGLLKSQGLDDYICKRFSLTCPEANLAEWEQVLYEESNPGGEVTIGMIGKYVELPDAYKSVIEALKHGGLKNR... | Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate H2O + L-glutamine = L-glutama... |
Q317H9 | MRSKKMTHGLEKAPHRSLLYALGLTREELSRPLVGVVNSANEVVPGHIHLHTIAEAVKAGVRAAGGTPMEFPAIAVCDGLAMNHEGMRFSLPSREIIADSIEIMATAHPFDALVFIPNCDKSVPGMLMAMLRMNVPSILISGGPMMAGTGNGKAADLITVFEGVGMVRQGRMTEDELEQLSETACPGCGSCAGMFTANSMNCLSETIGLALPGNGTTPANSAARVRLAKHAGMRVMELLERDIKPRDIVTEKAVANAVAADMALGCSTNTVLHLPAVFAEAGLDLTLGIFDEVSRKTPNLCKLSPAGDQHIQDLHRAGGI... | Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (... |
A4W5T0 | MTNRLVLSGTVCRTPLRKVSPSGIPHCQFVLEHRSVQEEAGFHRQAWCQMPVIISGHENQAITHSITVGSAVTVQGFISCHKAKNGLSKMVLHAEQIDLIDSGD | Binds single-stranded DNA at the primosome assembly site (PAS). Component of the preprimosomal complex composed of PriA, PriB, PriC, DnaB and DnaT. Upon transient interaction with DnaG it forms the primosome. Belongs to the PriB family. |
Q0SX03 | MTKSELIERLATQQSHIPAKTVEDAVKEMLEHMASTLAQGERIEIRGFGSFSLHYRAPRTGRNPKTGDKVELEGKYVPHFKPGKELRDRANIYG | This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control. Heterodimer of an alpha and a beta chain. Belongs to the bacterial histone-like protein family. |
P14745 | MDKFWWRAAWGLCLVQLSLAQIDLNITCRFEGIYHVEKNGRYSISRTEAADLCKAFNSTLPTMAQMEKALSIGFETCRYGFIEGHVVIPRIHPNSICAANNTGVYILTSNTSQYDTYCFNASAPPGEDCTSVTDLPNAFDGPITITIVNRDGTRYVKKGEYRTNPEDINPSSPTDDDVSSGSSSERSSTLGGYIFYNHFSTSPPIPDEDGPWITDSTDRTPATRDQGAFDPSGGSHTTHGSESAGHSHGSREGGANTTSGPLRTPQIPEWLIILASLLALALILAVCIAVNSRRRCGQKKKLVINNGNGAVEDRKSSGLN... | Cell-surface receptor that plays a role in cell-cell interactions, cell adhesion and migration, helping them to sense and respond to changes in the tissue microenvironment. Participates thereby in a wide variety of cellular functions including the activation, recirculation and homing of T-lymphocytes, hematopoiesis, in... |
A0KIC6 | MNAVTAGAHALRHDWTLAEVQALFALPFNDLLFQAQTVHRAHFDPNEVQVSTLLSIKTGACPEDCKYCPQSARYHTGLEAERLMEVEKVLERAREAKANGSSRFCMGAAWRNPKEKDMPYILRMIEEVRGLGMETCMTLGMLTADQAARLGAAGLDYYNHNLDTSPEFYGDIITTRTYQDRLDTLAYVRGAGMKVCSGGIVGMGEQAKDRAGLLMALANLPRHPESVPINMLVKVKGTPLENQENLDPFEFIRTIAVARIMMPASHVRLSAGREKMNEQMQAMCFMAGANSIFYGCKLLTTPNPDENSDMQLFKRLGIRP... | Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism. (4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 ox... |
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