Datasets:
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Full Name
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⌀
taxon
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sequence
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2.75k
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5.51k
AlphaFoldDB
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10
B9MEL5
NUOB_ACIET
NDH-1 subunit B
null
MIEGVMKEGFITTSYDSVVNWAKTGSLWPMTFGLACCAVEMMHAAAARYDLGRFGAEVFRASPRQSDLMIVAGTLCNKMAPALRKVYDQMAEPRWVISMGSCANGGGYYHYSYSVVRGCDRIVPVDVYVPGCPPTAEALIYGIIQLQQKIRRTHTIARA
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.
B9MEL5
Q07002
CDK18_HUMAN
Serine/threonine-protein kinase PCTAIRE-3
Homo
MIMNKMKNFKRRFSLSVPRTETIEESLAEFTEQFNQLHNRRNENLQLGPLGRDPPQECSTFSPTDSGEEPGQLSPGVQFQRRQNQRRFSMEDVSKRLSLPMDIRLPQEFLQKLQMESPDLPKPLSRMSRRASLSDIGFGKLETYVKLDKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAIREVSLLKNLKHANIVTLHDLIHTDRSLTLVFEYLDSDLKQYLDHCGNLMSMHNVKIFMFQLLRGLAYCHHRKILHRDLKPQNLLINERGELKLADFGLARAKSVPTKTYSNEVVTLWYRPPDVLLGSTEYSTPIDMWGVGCIHYEMATGRPLFPGSTVKEELHLIFRLLGTPTEETWPGVTAFSEFRTYSFPCYLPQPLINHAPRLDTDGIHLLSSLLLYESKSRMSAEAALSHSYFRSLGERVHQLEDTASIFSLKEIQLQKDPGYRGLAFQQPGRGKNRRQSIF
May play a role in signal transduction cascades in terminally differentiated cells.
Q07002
Q16IW3
RU1C_AEDAE
U1 small nuclear ribonucleoprotein C
Stegomyia
MPKYYCDYCDTYLTHDSPSVRKTHCTGRKHKDNVKFYYQKWMEEQAQHLIDATTAAFKAGKIAQNPFSAGPPKPNVAIPPPSMGMPARPGMIPGMPAGAPPLLMGPGPMGMRPPMMMPMGMPPMGMGMRPPMMNGPPPQMNQKVYHNTDRRYHR
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.
Q16IW3
B2I663
AROQ_XYLF2
Type II DHQase
Xylella
MAHLLLLHGPNLNLLGTREPEIYGRITLPQIDAALAERAATAGHGLSSLQSNAEHVLIERIHATREDGTAFILINPGAFTHTSVALRDALLAVALPFVEIHLSNPHTREPFRHHSYLADKALGVVCGFGVDSYRIALEGVIARLGSDV
Catalyzes a trans-dehydration via an enolate intermediate.
B2I663
Q3IF87
NADE_PSET1
NH(3)-dependent NAD(+) synthetase
Pseudoalteromonas
MRAEIMAAMKVQPVIDVNAEISRRVNFIKARLIAAHATSLVLGISGGVDSSVCGRLCQLAVNELNQEQSTTDYKFVAVRLPYGVQADENEAQLAVDFIQPSSRMTVNIKPATDALHEQTMAAIVGNGESLPEQEKIDFIKGNVKARQRMIAQYEIAAFCQGLVVGTDHSAENITGFYTKFGDGACDLAPLFGLSKRQVRALGSTLGASSVLVNKAPTADLESDRPGLTDEEALGLSYEQIDDFLEGKPVTQQVEQTLSAIYQRTQHKRQPVPTIYDEL
Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Q3IF87
P52406
CHI4_SOLTU
Endochitinase 4
Solanum
EFTALSLLFSLLLLTASAEQCGKQAGGARCAAGLCCSNFGWCGNTNDYCGPGKCQSQCPSGPSPKPPTPGPGPSGGDIGSVISNSMFDQMLKHRNDNACQGKNNFYSYNAFINAARSFGGFGTTGDTTARKREIAAFFAQTSHETTGGWPTAPDGPYAWGYCFLREQGSPGDYCTPSGQWPCAPGRKYFGRGPIQISHNYNYGPCGRAIGVDLLNNPDLVATDPVISFKSAIWFWMTPQSPKPSCHDVIIGRWQPSAADRAANRLPGFGVITNIINGGLECGRGSDSRVQDRIGFYRRYCGI
Defense against chitin-containing fungal pathogens.
P52406
Q6MDZ8
Y477_PARUW
Nucleoid-associated protein pc0477
Candidatus Protochlamydia
MGTGFSKKKKEARLIQQQMSLVQNELQNLEVVGVAGSGLVTITLTGDGEMKQVKIKPECVDVEDLEGLEMLIRAAHADAHKRLKEQSPPIPGFPGFLA
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
Q6MDZ8
A5U2R1
FRDC_MYCTA
Quinol-fumarate reductase subunit C
Mycobacterium tuberculosis complex
MSAYRQPVERYWWARRRSYLRFMLREISCIFVAWFVLYLMLVLRAVGAGGNSYQRFLDFSANPVVVVLNVVALSFLLLHAVTWFGSAPRAMVIQVRGRRVPARAVLAGHYAAWLVVSVIVAWMVLS
Anchors the catalytic components of the fumarate reductase complex to the cell membrane, binds quinones.
A5U2R1
B2IME4
IF2_STRPS
Translation initiation factor IF-2
Streptococcus
MSKKRLYEIAKELGKESKEVVARAKELGLDVKSHSSSVEEAVAAKIAASFKPAAAPKVEAKPAAPKVSAEKKAEKSEPAKPAVAKEEAKPAEPVAPKTEKVAAKPQSRNFKAEREARAKEQAERRKQNKGNNRDQQQNGNRQKNDGRNGGKQGQSNRDNRRFNDQAKKQQGQQKRRNERRQQEDKRSNQVAPRIDFKARAAALKAEQNAEYARSSEERFKQYQAAKEALAQANKRKEPEEIFEEAAKLAEQAQQVQAVVEVVPEKKEPAVDTRRKKQARPDKNRDDYDHEEDGPRKQQKNRSSQNQVRNQKNSNWNNNKKNKKGNNKNNRNQTPKPVTERKFHELPTEFEYTDGMTVAEIAKRIKREPAEIVKKLFMMGVMATQNQSLDGETIELLMVDYGIEAKQKVEVDNADIERFFVEDGYLNEDELVERPPVVTIMGHVDHGKTTLLDTLRNSRVATGEAGGITQHIGAYQIVENGKKITFLDTPGHAAFTSMRARGASVTDITILVVAADDGVMPQTIEAINHSKAANVPIIVAINKIDKPGANPERVIGELAEHGVMSTAWGGDSEFVEISAKFNQNIEELLETVLLVAEIQELKADPTVRAIGTVIEARLDKGKGAVATLLVQQGTLNVQDPIVVGNTFGRVRAMTNDLGRRVKVAGPSTPVSITGLNEAPMAGDHFAVYEDEKSARAAGEERAKRALMKQRQATQRVSLENLFDTLKAGELKSVNVIIKADVQGSVEALSASLQKIDVEGVKVTIVHSAVGAINESDVTLAEASNAFIVGFNVRPTPQARQQAEADDVEIRLHSIIYKVIEEMEEAMKGMLDPEFEEKVIGEAVIRETFKVSKVGTIGGFMVINGKVARDSKVRVIRDGVVIYDGELASLKHYKDDVKEVTNGREGGLMIDGYNDIKMDDVIEAYVMEEIKR
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
B2IME4
A6TDQ4
AC4CH_KLEP7
N(4)-acetylcytidine amidohydrolase
Klebsiella
MQANDITFFQRFQDDILAGRKTITIRDAAESHFKPGDVLRVGRYEDDGYFCTIAVTATSTVTLDTLTEQHAQQENMTLGQLRQVISDIYPGESQFYVIEFKTL
Catalyzes the hydrolysis of N(4)-acetylcytidine (ac4C).
A6TDQ4
Q83NT4
SECA_TROW8
Protein translocase subunit SecA
Tropheryma
MSVKLLERILRAGEGRTLKRLRNIAHTVNAIEDEYKGCTDGELRTFAFDLKVRHQNGESLDSILPEAFAMVREASSRTLGLRHFDVQIMGGAALHMGYIAEMFTGEGKTLVATLPAFLNSLSGNGVHIVTVNDYLAGYHSQQMGRVYKVLGLETGVILADQDPSTRAQQYRADITYGTNNEFGFDYLRDNMAWSCAERVQRGHNFVILDEVDSILIDEARTPLIISGSSSGEVSRWFVEFAGIARALTAGEDYDVDERKHTVGVLEPGIAKVEDLLGISNLYESVNTPLISFLNNSIKAKELFKRDRDYVVLDGEVMIVDEHTGRILSGRRYNEGLHQAIEAKEGVEIKAENQTLATVTLQNYFRLYKKISGMTGTAVTEASEFMSTYKLPVVSIPTNKPNIRKDHPDVVYKNEQIKFENLADHVRECYTRGQPVLIGTTSVEKSEYVSKLLSKRGVRHEVLNAKNHAKEARIVAEAGRLRAVTVATNMAGRGTDIILGGNPEVLTAVELRRKGLDPSKDPERYEQAWSSAFPKLHRRTREEAEKVIEAGGLMVIGTERHESRRIDNQLRGRSGRQGDPGESRFYLSLTDDLMRKFNPGAASALAARVPDDTAIESKLVSRAIRSAQAQVESLNAETRKNVLKYDDVLNRQRAAIYTDRSRILEGGDIADRVQAFLSDAIEEIINSHAVTAWDFDALWADLKTIYPVGISIEELTDEAGGMGRITPDFVMREILSDAKFAYEKRESEIGPESMRDLERKVVLSVIDRCWRDHLYEMEYLKEGIGLRAMAQRDPLVEYQKEGFDMFEAMMGRIREESIGYLFNIDAQVSSNSPSDARNRPIEHDDNAV
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Q83NT4
A1SBV0
RSMG_SHEAM
16S rRNA 7-methylguanosine methyltransferase
Shewanella
MLAEKLSQDLAKAGLQVDAQQQQQLLAFVALLDKWNKAYNLTSVREPAQMLTRHILDSLVVSPHLVGSRFIDVGTGPGLPGIPLAIINPDKEFVLLDSLGKRIRFQKQVAVELGLKNISSVESRVELYQPEQGFDGVLSRAFASVGDMLSWCHHLPAENGSFYALKGQLGDEEMAGIPEGFKLIETIRLTVPGLDEQRHLLKLVKA
Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
A1SBV0
Q81DT1
PRSA3_BACCR
Foldase protein PrsA 3
Bacillus cereus group
MKKKKIFIGTIISCVMLALSACGSSDNVVTSKVGNVTEKELSKELRQQYGESTLYQMMLSKALLDKYKVSDEEAKKKVEEAKDKMGENFKSTLEQLGLKNEDELKEKMKPEIAFEKAIKATVTDKDVKNNYKPEMKVSHILVKDEKTAKEIKEKVNNGEDFAALANQYSEDTGSKEQGGEISGFAPGQTVKEFEEAAYKLDAGQVSDPVKTTYGYHIIKVTDKKELKPFDEVKDKIRKDIEQQRLQDTTGKWKQQVVNDLLKDADIKVNNKEFKDTFKFLEKK
Plays a major role in protein secretion by helping the post-translocational extracellular folding of several secreted proteins.
Q81DT1
Q9QYH6
MAGD1_MOUSE
Neurotrophin receptor-interacting MAGE homolog
Mus
MAQKPDGGAGLRGFQAEASVEDSALLVQTLMEAIQISEAPPTSQATAAASGPNASPQSSQPPTANEKADTEVSAAAARPKTGFKAQNATTKGPNDYSQARNAKEMPKNQSKAAFKSQNGTPKGPHAASDFSQAAPTGKSAKKSEMAFKGQNSTKAGPGTTYNFPQSPSANEMTNNQPKTAKAWNDTTKVPGADAQTQNVNQAKMADVGTSAGISEADGAAAQTSADGSQTQNVESRTIIRGKRTRKVNNLNVEENNSGDQRRASLASGNWRSAPVPVTTQQNPPGAPPNVVWQTPLAWQNPSGWQNQTARQTPPAARQSPPARQTPSAWQNPVAWQNPVIWPNPVIWQNPVIWPNPIVWPGPIVWPNPMAWQSTPGWQSPPSWQAPPSWQSPQDWQGPPDWQVPPDWSMPPDWSFPSDWPFPPDWIPADWPIPPDWQNLRPSPNLRSSSNSRASQNQGPPQPRDVALLQERANKLVKYLMLKDYTKVPIKRSEMLRDIIREYTDVYPEIIERACFVLEKKFGIQLKEIDKEEHLYILISTPESLAGILGTTKDTPKLGLLLVILGIIFMNGNRATEAVLWEALRKMGLRPGVRHPLLGDLRKLLTYEFVKQKYLDYRRVPNSNPPEYEFLWGLRSYHETSKMKVLRFIAEVQKRDPRDWTAQFMEAADEALDALDAAAAEAEARAEARNRMGIGDEAVSGPWSWDDIEFELLTWDEEGDFGDPWSRIPFTFWARYHQNARSRFPQAFTGPIIGPSGTATANFAANFGAIGFFWVE
Involved in the apoptotic response after nerve growth factor (NGF) binding in neuronal cells. Inhibits cell cycle progression, and facilitates NGFR-mediated apoptosis. May act as a regulator of the function of DLX family members. May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. Plays a role in the circadian rhythm regulation. May act as RORA coregulator, modulating the expression of core clock genes such as ARNTL/BMAL1 and NFIL3, induced, or NR1D1, repressed.
Q9QYH6
Q4UMQ8
KAD_RICFE
Adenylate monophosphate kinase
spotted fever group
MIVIFLGPPGAGKGTQGKKIAKKIDLPHIAIGDIFRTIIKTSTSEAELINNYVKQGELIPNEIVNQVIKNFLLSSEYKNGYILDGYPRNLEQAKFFESFIKEKIKIIYFDVSDELLIKRVLGRYSCKNCGKIYNSYFLQPKTDNVCDVCGSSTFDYRKDDNEEVIKKRIEVYKTETYPLIDYYKNSGNFYIVDGSKNEQEIEIDIQKILKIN
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Q4UMQ8
Q89AZ6
FLIJ_BUCBP
Flagellar FliJ protein
Buchnera
MYKKKRCFTLLKYLDVKSNYHIVLNLKKILSGIIQVKAQLDILMSYQCEYLKCLDQELKFYISGTRLAHYYNFIAFLIDGVNKQNDTMCKLYKQYNEYIYLWKKKQKKIKMWNNINSRLLLNRFKLSQLDDQDLLDSCCTYKYLLKNDREDTDYV
Flagellar protein that affects chemotactic events.
Q89AZ6
P57402
ZNUB_BUCAI
High-affinity zinc uptake system membrane protein ZnuB
Buchnera
MFELIFPGWLAGVLLSLTTGPLGSFIVWRRMSSFGDTLSHSSLLGIALSIAFNINSFYAILILMSFIAIILAWLEELLPVSLDTVLNIISHSSLSLGMVFISLISSKKEINITNYLFGDLLSVTKNDLITISISSILILSILLFRWHSILSSTINEELSQIDGINVLYARLTIMLMTAFTIAIAIKFVGALLITSLLIIPPATAQHFSGSPEKMVIIAIIVSILSVTGGISLSVFYNTPASPSIVLCSSFLCLISNIKKHFY
Involved in the high-affinity zinc uptake transport system.
P57402
A4Y1N1
RLMF_SHEPC
rRNA adenine N-6-methyltransferase
Shewanella
MPKPPRSTQILSCNAPNGKPKTQHPSARAKVKRTPVNTRSIAEIKKALHPRNVHINGYDFNALIKAFPRLNAFVRPTSFGGLSIDFADPEAVKTLNTALLKHHYGIDFWDIPKGALCPPIPGRVDYLHYLADLLAEGDHHLVMDRVSVLDIGTGANGIYPILGCQVFGWHFVASDINSISLANVQGIIAQNPALHGRLNLRLQGDESAIFKGVIQPQERFELTLCNPPFHASLAEAAEGSLRKVRNLQLNRGRTAKPVAKLNFGGQGAELWCQGGEPQFLATMIDESQAFADQCLWFTSLVSKKENLKPCYQALAKLAVDTVKTIEMQQGNKMTRILAWSFQSAAKRKIWRNAHLSD
Specifically methylates the adenine in position 1618 of 23S rRNA.
A4Y1N1
Q96553
METK3_CATRO
Methionine adenosyltransferase 3
null
METFLFTSESVNEGHPDKLCDQVSDAILDACLEQDPESKVACETCTKTNMVMVFGEITTKATVNYEKIVRDTCRGIGFTSPDVGLDADNCKVLVNIEQQSPDIAQGVHGHLTKKPEEIGAGDQGHMFGYATDETPELMPLTHVLATKLGAKLTEVRKNKTCPWLRPDGKTQVTVEYRNEGGAMVPIRVHTVLISTQHDETVTNEQIAQDLKEHVIKPVIPAQYLDDQTIFHLNPSGRFVIGGPHGDAGLTGRKIIIDTYGGWGAHGGGAFSGKDPTKVDRSGAYIVRQAAKSVVASGLARRCLVQVSYAIGVAEPLSVFVDTFKTGKIPDKDILALIKENFDFRPGMIAINLDLKRGGNFRYQKTAALGHLGRDDPDFTWETVKILKPKA
Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.
Q96553
B3GXZ9
RLMC_ACTP7
23S rRNA(m5U747)-methyltransferase
Actinobacillus
MILNCPHFQQQDCVSCQWLEKPYATQLTDKEIDLKRLISPFILQNFTEILPPVQSSQKQFRNKAKMVVSGSVERPILGILKDQTDPQSGIDLCDCPLYPTEFEALFPILKDFIARAGLVPYNIAKKKGELKYILLTQSRYNQSIMLRFVLKSEQKRPLVERELPNLLAKLPKDSVVSLNIQPQHAAILEGETEIFLTEKTTIEENFNDIPLFIRPQGFFQTNPNVASQLYATAQNWIKDLAIQQFWDLFCGVGGFGLHCAKALQEKNENVQLTSIEISASAIASATKSAEQLQLKNITFASLDSAQFALNEKSATPDLVIVNPPRRGIGKPLAEFLNQLGTPYLIYSSCNARTMAQDFEALSNYSLQKVQLFDMFPHTSHYEVLTFLVKKS
Catalyzes the formation of 5-methyl-uridine at position 747 (m5U747) in 23S rRNA.
B3GXZ9
A7UKV6
SUB4_TRIEQ
Subtilisin-like protease 4
Trichophyton
CLKTLSVFLAAFAAADARAVFKTQGHKNSEMIPDNYIVVMKDGVSQDDFKAHVSSVASIHSTNKAKRGTNTEGMKREFDIMNWRGYHGHFDRDTLEEILNDSKVDYVEQDQVVRISGLVTQRGAPSWGLGRVSHRQAGSRDYVFDDSAGRGVTIYGVDTGIDINHQDFRGRARWGTNTADRDNADRHGHGTHTASTFAGTAYGIAKNANIVAVKVLSSDGSGSTSGIIAGINYCVQDAQQRGILGKAAMNLSLGGGFSQANNDAVTRAQNAGIFVAVAAGNDNRDARNYSPASAPAVCTVASSTINDSKSSFSNWGPVVDIYAPGSDIIAARPGGGSTTMSGTSMASPHVAGMGAYMIGLGADPRSLCDRLKQLATPAIRNPGSSTTNRLLYNG
Secreted subtilisin-like serine protease with keratinolytic activity that contributes to pathogenicity.
A7UKV6
Q8NT75
DCUP_CORGL
Uroporphyrinogen decarboxylase
Corynebacterium
MSALTIPAARRTLNNAPIIDAANGKTPTRTPVWFMRQAGRSLPEYKKVREGISMLDSCFMPELLAEITLQPVRRHDVDAAILFSDIVVPLRAAGVGVEIVAGRGPVLDAPVRSRGDVLNLPILEGNVPEVEQGIGIILDELSDSQALIGFAGAPFTLASYLVEGGPSKNHEKTKAMMHGDPETWHALMARLVPTIVNSLKSQIDAGIDAVQLFDSWAGFLTERDYTEFVLPYSTEILEEVGKYQLPRIHFGVGTGELLGAMSKAGSEVMGVDWRVPLDKAAERIAAVSGPKVLQGNLDPALLFAGRAPLTKEIERIKAEAQTAVDAGHATGHIFNLGHGVLPNTVAEDITEAVSIIHS
Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Q8NT75
Q3SKH1
EFP_THIDA
Elongation factor P
Thiobacillus
MKIAQELRAGNVVMIGKDPMVVQKAEFSKSGRNASVVKMKLKNLLTGAGMESVYRADDKFDTVTLDRKECTYSYFADPLYVFMDSDYNQYEVEGDNLGDALNYLDDGMPVEVVFYEGKAISVEMPTTVIREVEYTEPAVRGDTSGKVMKPARIKPTGFELPVAAFVEIGDMIEIDTRTNEFKRRAN
Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
Q3SKH1
A1AW12
GATC_RUTMC
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C
Candidatus Ruthia
MSLSEKQINQIAYLARLSLNEVQLKNNTQDLNAIFSLIEQLANIETDGIEPMLHPLHMFQRLRKDVVIEKEQSVLFQSVAPKTRNGYYLVPTVIE
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
A1AW12
A6W216
ILVC_MARMS
Ketol-acid reductoisomerase type II
Marinomonas
MANYFNTLPLREQLAQLAKCRFMDSSEFADGVEALKGKKMVVIGCGAQGLNQGLNLRDSGLDVSYALRPEAIAQKRQSWKNATENGFVVGTYEELIPTADVVLNLTPDKQHTPVVKAVMPLMKEGACLSYSHGFNIVEEGMQIREDLTVIMVAPKCPGSEVRAEYVRGFGVPTLIAVHEDNDPKGEGLALAKAYAVGTGGHKAGVLMSSFIAEVKSDLMGEQTILCGMLQTGSILCFDKMVEEGIDAGYASRLIQYGWETITEALKYGGVTNMLDRLSNPAKIKAFDLSEELKVIMRPLYNKHQDDIISGHFSQTMMEDWANDDKNLLQWRADTAETNFEKTPAGDVEISEQEFFDNGILMVAMVKAGVELAFETMTAAGIIAESAYYESLHETPLIANTIARKKLYEMNATISDTAEYGCYLYNHACVPLLADFMKDIKTDVIGKGLSVEDNGVDNARLIEVNKALRSHPVEAVGAVLRGHMADMKKIV
Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
A6W216
Q6FCN1
THIG_ACIAD
Thiazole synthase
Acinetobacter
MQDSPLIIGSRQFQSRLLVGTGKYKDLNETDLAIQASGAEIVTVAIRRVNIGQHADQPNLLSVIPPEKYTILPNTAGCFDADSAIRTCMLARELLDGHNLVKLEVLGDQDTLYPNITETLKAARTLIDDGFEIMVYTSDDPIVAKELESMGCVAIMPLGSLIGSGLGILNPHTISIIKENAKVPVLVDAGVGTASDAAIAMELGCDGVLMNTAIAAAQHPVLMASAMKKAIEAGREAFLAGRMPRKRMANASSPETGYFFK
Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
Q6FCN1
Q863Y8
S52A2_PAPHA
Riboflavin transporter 1
Papio
MAAPTLGHLVLTHLLVALLGMGSWAAVNGIWVELPVVVKHLPEGWSLPSYLSVVVALGNLGLLVVTLWRRLAPGKGERVPIQVVQVLSVVGTALLAPLWHHVAPVAGQLHSVAFLTLALVLALACCTSNVTFLPFLSHLPPPFLRSFFLGQGLSALLPCVLALVQGVGRLECSPAPTNGTSGPPLNFPERFPASTFYWALTALLVTSAAAFQGLLLLLPSLPSVTTGGAGPELPLGSPGAEEEEKEEEEALPLQEPPSQAAGTIPGPDPEAHQLFSAHGAFLLGLLAITSALTNGVLPAVQSFSCLPYGRLAYHLAVVLGSAANPLACFLAMGVLCRSLAGLVGLSLLGMLFGAYLMVLAILSPCPPLVGTTAGVVLVVLSWVLCLCVFSYVKVAASSLLHGGGRPALLAAGVAIQMGSLLGAGTMFPPTSIYHVFQSRKDCVDPCGP
(Microbial infection) In case of infection by retroviruses, acts as a cell receptor to retroviral envelopes similar to the porcine endogenous retrovirus (PERV-A).
Q863Y8
C5WIT0
ACCD_STRDG
Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
Streptococcus
MALFRKKDKYIRITPNNSLKGSVSQVIPEVPDELFAKCPACKHMIYKKDLGLAKICPTCSYNFRISAQERLTLTVDEGSFQELFTSIETKDPLRFPGYQEKLQKAKETTGLHEAVLTGKAMVKEQKIALAIMDSHFIMASMGTVVGEKITRLFELAIEENLPVVIFTASGGARMQEGIMSLMQMAKVSAAVKRHSNAGLFYLTILTDPTTGGVTASFAMEGDIILAEPQSLVGFAGRRVIETTVRENLPDDFQKAEFLQDHGFVDAIVKRTELRDKVAHLVAFHGGGQ
Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
C5WIT0
B3M269
MOC2A_DROAN
Sulfur carrier protein MOCS2A
Sophophora
MSADGPVVNVHVLFFAKSRELAQTPRSKVDVPSQIVASDLLDQLVTRFDLASIKDNLILAHNESYIENLSDKILFREGDELAVIPPLSGG
Acts as a sulfur carrier required for molybdopterin biosynthesis. Component of the molybdopterin synthase complex that catalyzes the conversion of precursor Z into molybdopterin by mediating the incorporation of 2 sulfur atoms into precursor Z to generate a dithiolene group. In the complex, serves as sulfur donor by being thiocarboxylated (-COSH) at its C-terminus by MOCS3. After interaction with Mocs2B, the sulfur is then transferred to precursor Z to form molybdopterin.
B3M269
P61604
CH10_HUMAN
Early-pregnancy factor
Homo
MAGQAFRKFLPLFDRVLVERSAAETVTKGGIMLPEKSQGKVLQATVVAVGSGSKGKGGEIQPVSVKVGDKVLLPEYGGTKVVLDDKDYFLFRDGDILGKYVD
Co-chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp60, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix . The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable).
P61604
P9WKC9
TGS1_MYCTU
Probable triacylglycerol synthase tgs1
Mycobacterium tuberculosis complex
MNHLTTLDAGFLKAEDVDRHVSLAIGALAVIEGPAPDQEAFLSSLAQRLRPCTRFGQRLRLRPFDLGAPKWVDDPDFDLGRHVWRIALPRPGNEDQLFELIADLMARRLDRGRPLWEVWVIEGLADSKWAILTKLHHCMADGIAATHLLAGLSDESMSDSFASNIHTTMQSQSASVRRGGFRVNPSEALTASTAVMAGIVRAAKGASEIAAGVLSPAASSLNGPISDLRRYSAAKVPLADVEQVCRKFDVTINDVALAAITESYRNVLIQRGERPRFDSLRTLVPVSTRSNSALSKTDNRVSLMLPNLPVDQENPLQRLRIVHSRLTRAKAGGQRQFGNTLMAIANRLPFPMTAWAVGLLMRLPQRGVVTVATNVPGPRRPLQIMGRRVLDLYPVSPIAMQLRTSVAMLSYADDLYFGILADYDVVADAGQLARGIEDAVARLVAISKRRKVTRRRGALSLVV
Upon expression in E.coli functions as a triacylglycerol synthase, making triacylglycerol (TG) from diolein and long-chain fatty acyl-CoA. Prefers C(26:0)-CoA over C(18:1)-CoA. TG synthesis activity increases in M.tuberculosis upon oxygen depletion and NO treatment, with concomitant accumulation of TG in inclusion bodies. As disruption of the gene encoding this protein obviates TG synthesis this seems to be the major enzyme involved in production of TG. Has no wax synthase activity to produce wax esters.
P9WKC9
Q6L5Q5
WEFF_STRMT
Stealth protein WefF
Streptococcus
MVEKIDFVVAWVDGNDPVWRKKKAQYDGTINTSKEGMNSDKAYREWGTFKYWFRGVEKFAPWVNKVYLVTDNQKPSWLELNSDKLVLVDHTEIICNDYLPVFSANPIESNIHRIPGLSECFVFFNDDVYLTAPVEPTDFFSDDGLPKYVTALAPITTERYGTGHFQMNDMGIITTHFTREEILKNGKFFSIKQGVKGIAKSLLYRHSKFICGFWENHLTHPLLKSTMELVWEKEKDVLEKTSASRFRSPSDTNVWLFKYWQIASGQYAIGNPKLGGLFSLDNAGPDFWKLLNSRKYKVMCINDGFNVQNENQVMDDFIKAMNQLFPDKSSFEI
Part of the type 2G receptor polysaccharide (RPS) biosynthesis locus. Essential for cell surface RPS production, and the host-like Gal beta 1-3GalNAc (G) motif of the RPS. Probably encodes a 1-3GalNAc alpha transferase.
Q6L5Q5
O43555
GON2_HUMAN
GnRH-associated peptide II
Homo
MASSRRGLLLLLLLTAHLGPSEAQHWSHGWYPGGKRALSSAQDPQNALRPPGRALDTAAGSPVQTAHGLPSDALAPLDDSMPWEGRTTAQWSLHRKRHLARTLLTAAREPRPAPPSSNKV
Stimulates the secretion of gonadotropins; it stimulates the secretion of both luteinizing and follicle-stimulating hormones.
O43555
Q8K9T5
SPEE_BUCAP
Spermidine synthase
Buchnera
MINEKIWHEKLHRHVGQYFSIDKILYQKKNKYHDIIIFQNSIMGRIMAIDGVVQTTEKDEFIYHEMLTHVPIFYHGLIKNVLIVGGGDGGILREICRHKSIENITMVEIDLNIIDLCKQFFPKHNNNAYKDPRLKIVIDNGLNFVQKTKEKFDLIISDSTDPIGCGKDLFLSDFYFHCKNCLVKNGIFVGQNGVFFLQKNDINQSYKNLKKNFHDVSFYQATIPSYYGGTMMFSWGTDNIDFRQINIKNLEKRIKDKKLTFNYYNSNIHISSFYLPQYIINTLDKS
Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
Q8K9T5
Q29499
ACES_RABIT
Acetylcholinesterase
Oryctolagus
AEGREDPELLVTVRGGRLRGLRLKAPGGPVSAFLGIPFEEPPVGPRRFLPPEPKRPWAGVLDATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYYGRFLVQAEGTVLVAMNYRVGAFGFTCLPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPASVTLFGESAGAASVGLHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVVCPPGGAGGNDTELVACLRTRPAQDLVDHEWRVLPQESIFRFSFVPVVDGDFLSDTPEALINAGDFQGLQVLVGVVKDEGTYFLVYGAPGFSKDNESFISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLRDALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTEEERIFAQRLMRYWANFARTGDPNEPRDAKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL
Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft.
Q29499
P29899
CYCL_PARDE
Cytochrome c552
Paracoccus
MTKPRILAAFAMTLIIPVAAMAAPQFFNIIDGSPLNFDDAMEEGRDTEAVKHFLETGENVYNEDPEILPEAEELYAGMCSGCHGHYAEGKIGPGLNDAYWTYPGNETDVGLFSTLYGGATGQMGPMWGSLTLDEMLRTMAWVRHLYTGDPKDASWLTDEQKAGFTPFQPKSSGEDQS
Electron acceptor for MDH. Acts in methanol oxidation.
P29899
P53258
GYP2_YEAST
Protein MIC1
Saccharomyces
MSFFDSLRQKAPFLDKLADSFTPTLTRDEKFRLKYKLPANENILEDTNAEVSFATSIKDGKGHSDRVNNKGRKTAYVYSGRLFLTPHFLVFRDAFDHSSCVLILNISTIKRVERSPSESYEFALLVTLYTGAKVLIQFIGIRYRSEQFCDKLKLNLKENIPNAKTLPAFLETSYSEFLIAKNILGKKDITVPRAGLGQHFKYPGNPTMVKEKAKLRLWFDYFRENGRNLAVVQTPMFRKLIRIGVPNRMRGEIWELCSGAMYMRYANSGEYERILNENAGKTSQAIDEIEKDLKRSLPEYSAYQTEEGIQRLRNVLTAYSWKNPDVGYCQAMNIVVAGFLIFMSEEQAFWCLCNLCDIYVPGYYSKTMYGTLLDQRVFESFVEDRMPVLWEYILQHDIQLSVVSLPWFLSLFFTSMPLEYAVRIMDIFFMNGSITLFQVALAVLKINADDILQADDDGMFIAIIKHYFQTLGQSAHPDSSDIKYRQITKFQELLVTAFKEFSVISEEMAMHARHKYEKGIFQNIETFMKRTQLRHMPKTFNLSSDDLSNIYDMFYQSIETYKISMGTGSSNMGFEVFIQFLSKFCDSCRPCEKDKDPAFRKQKRNFLQRLFDNWDSAHIGELTLNDVVTGLDKLVTVDLLQAINYFFSLYDTDGDGELHREEVLQLSEGLLLLTEPWKSGRYVDLLTKKRIEDDIAENIIKESGGEIATMNQIELPTGVTIDEEKYKVEQAERYLKAASNFLQRSFEYAKAVDLAEEVNLIDLSDDEGEEKRTVKQKQLESIKANAALDPTHPKVIDLPTFRMIILADETYELFFSNTLRSSVHVDEHVNIDNKNKVLRSMFDGILADGKRVAEQVRRRVDSVATRSSIASVESTPTAAASSITTKEEKYDDLDDFTSEHQPENEELLQSSWFEIDDANETSTKAIQERSFEPLSANSSEEKSNLIEFEA
Stimulates specifically the GTPase activity of SEC4, YPT6 and YPT36. Inactivates YPT6 during recycling between the endosome and the Golgi compartments.
P53258
B8DBV7
DPO4_LISMH
DNA polymerase IV
Listeria
MDTSRKIIHIDMDAFYASVEQRDHPEFRGKPLIIGGDPNKRGVVSTCSYEARKYGVHSAMPTRQAAKLCPNGIFIHGNMAHYVEVSSQIREIFSRYTDVIEPLSLDEAYLDVTENKKGMKSATMVARDIQQTIYRELGLTASAGVSFNKFIAKIASDFKKPAGITVVAPEEAEAFLEQIPVTKFYGVGKVTAEKLHRLGIETGADLKKWSEWDLIRELHKHGYQLYRHVRGRSNNIVNPHRDRKSVGKETTFEFNVLDNRILEQSLMKFAKKVEERLIKLQKHGKTVVLKLRYSDFTTITKRLTLNEYTNDANQIYQAAALLLRESYKGQDSIRLIGLTVTNLKPVYFENLRLEGL
Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
B8DBV7
Q9Y5X9
LIPE_HUMAN
Phospholipase A1
Homo
MSNSVPLLCFWSLCYCFAAGSPVPFGPEGRLEDKLHKPKATQTEVKPSVRFNLRTSKDPEHEGCYLSVGHSQPLEDCSFNMTAKTFFIIHGWTMSGIFENWLHKLVSALHTREKDANVVVVDWLPLAHQLYTDAVNNTRVVGHSIARMLDWLQEKDDFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRITGLDPAGPMFEGADIHKRLSPDDADFVDVLHTYTRSFGLSIGIQMPVGHIDIYPNGGDFQPGCGLNDVLGSIAYGTITEVVKCEHERAVHLFVDSLVNQDKPSFAFQCTDSNRFKKGICLSCRKNRCNSIGYNAKKMRNKRNSKMYLKTRAGMPFRVYHYQMKIHVFSYKNMGEIEPTFYVTLYGTNADSQTLPLEIVERIEQNATNTFLVYTEEDLGDLLKIQLTWEGASQSWYNLWKEFRSYLSQPRNPGRELNIRRIRVKSGETQRKLTFCTEDPENTSISPGRELWFRKCRDGWRMKNETSPTVELP
Exerts both phospholipase and triglyceride lipase activities . More active as a phospholipase than a triglyceride lipase . Hydrolyzes triglycerides, both with short-chain fatty acyl groups (tributyrin) and long-chain fatty acyl groups (triolein) with similar levels of activity toward both types of substrates . Hydrolyzes high density lipoproteins (HDL) more efficiently than other lipoproteins .
Q9Y5X9
Q6NGK6
PYRH_CORDI
Uridine monophosphate kinase
Corynebacterium
MTEGVQNERTGYKRVMLKLGGEMFGGGAVGIDPDVVQNVARQIASVARTGAEIAVVIGGGNFFRGAQLQQRGLDRNRSDYMGMLGTVMNCLALQDFLEQEGIDCRVQTAINMAQVAEPYLPLRAKRHLEKGRVVIFGAGMGMPYFSTDTTAAQRALEIDCEVLLMAKAVDGVYDDDPRTNPDAQLFHQITPREVIEKGLKVADATAFSLCMDNKMPILVFNLLTEGNIARAVAGEQIGTLVQS
Catalyzes the reversible phosphorylation of UMP to UDP.
Q6NGK6
A4Z0D8
GLMM_BRASO
Phosphoglucosamine mutase
unclassified Bradyrhizobium
MSRNYFGTDGIRGRANGLITPELALKVGQAAGLLFQRGEHRHRVVIGKDTRLSGYMIEYAMVAGFTSVGMDVLLVGPMPTPAVAMLTKSMRADLGVMISASHNLFEDNGIKLFGPQGFKLSDDVEKQIEQLLDESLDKKLAQSASLGRARRIDGVHDRYIEFAKRTLPRDLSLDGLRVVVDCANGAAYKVVPEALWELGADVISIGVEPDGFNINKECGSTSPEALCRKVREMRADIGIALDGDADRVILVDERGHIVDGDQLLAVIAQSWKEDGRLSRPGIVATVMSNLGLERFLQGQGLELVRTPVGDRYVLERMLADGYNLGGEQSGHIILSDYATTGDGFVAALQVLATVQKLRRPVSEVCHKFDPLPQILKNVRYRSGKPLDTDAVKSAIDTGQKRLNGHGRLLVRSSGTEPVIRVMGEGDDRNLVEEVVDDIVTAVGNAAAAA
Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
A4Z0D8
Q46ZK2
FETP_CUPPJ
Probable Fe(2+)-trafficking protein
Cupriavidus
MARMVQCIKLNKEAEGLDFPPLPGELGKKIWQSVSKEAWAGWLKHQTMLINENRLNMADARARQYLLKQTEKYFFGEGADEAAGYVPPQA
Could be a mediator in iron transactions between iron acquisition and iron-requiring processes, such as synthesis and/or repair of Fe-S clusters in biosynthetic enzymes.
Q46ZK2
A7FF08
ARGO_YERP3
Arginine exporter protein ArgO
Yersinia
MLAVYLHGFILSAAMILPLGPQNVFVMNQGIKRQHHLMSASLCALSDIILICAGIFGGSALLSRSPLLLALVTWGGVAFLMWYGWGALMAAWRGDGVASSATSVTQGRWRILVTLLAVTWLNPHVYLDTFVVLGSLGGQLLPDIRPWFALGAVTASIVWFFALALLAAWLSPWLNRPVAQRIINLFVGGVMGFIAFQLARQGFGL
Involved in the export of arginine. Important to control the intracellular level of arginine and the correct balance between arginine and lysine.
A7FF08
Q609Z8
PSTB_METCA
Phosphate-transporting ATPase
Methylococcus
MCRDVNVYYGEKHAIQNVSLDVGHNEVIALIGPSGCGKSTFLRCLNRMNDTIVGCRVTGSIRLDGQDIYDGGLDVVPLRAQVGMVFQKPNPFPKSIYENVAYGPKIHGLANSKAELEEIVESSLRRAGLWDEVKDDLAKPGTSLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKIEQLIDELRELYTIAIVTHSMQQAARVSQRTAYFHLGRLIEVGDTAQVFTNPRHPLTEDYITGRFG
Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Q609Z8
Q9PN35
RECR_CAMJE
Recombination protein RecR
Campylobacter
MVKGLEKFNELVESFANLPTIGKKTAIRLAYHLCINNQIDGMKLAHNIENAIRFIKPCEQCGALSENELCEICSDKERNKNILCIVESPKDILTLEESQSYNGLYFVLDELNEEKLEKLKQIILKLNISELIFALTHSINSDATIFFIEDKFKGLNLTFSKIAQGIPSGVNLENVDLISLNKAMNFRTKI
May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.
Q9PN35
C6CG41
TRMA_DICC1
tmRNA (uracil(341)-C(5))-methyltransferase
Dickeya
MTPEILPIDQYDAQLEEKTGRLGAMMAPFDAPAPAVFRSPVSHYRMRAEFRIWHDGDDLYHIMFDQQTKQRIRVDQFPAASELINRLMPVLLNALRAEPVLRRKLFQLDYLSTLSGEIAVSLLYHKALDDEWRQRARELCDELRAQGFALQLIGRATKTKICLDRDYVDECLPVAGRQMIYRQVENSFTQPNAMMNIQMLEWALSVTQGSTGDLLELYCGNGNFSLALARNFERVLATEIAKPSVAAAQYNIAANQIDNVQIIRMAAEEFTQAMNGVRQFNRLQGIDLAGYRCETIFVDPPRSGLDDGTAKLVQAYPRILYISCNPETLCANLETLSQTHRISQLALFDQFPYTHHMECGVLLEKRQ
Dual-specificity methyltransferase that catalyzes the formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, and that of position 341 (m5U341) in tmRNA (transfer-mRNA).
C6CG41
C5DA20
HUTI_GEOSW
Imidazolone-5-propionate hydrolase
unclassified Geobacillus
MRPLFIRNASQLVTLAGSSTAPLVKEKMNELHIIENGSVWVEDGKIAAVGTDEELSQQFQERIAEAEIVDATGKTVTPGLVDPHTHFVYAGSRESEFAMRLSGATYMEIMNAGGGIHATTKATREASKETLYEESKRRLDQFLLHGVTTVEAKSGYGLSIEHEVKQLTVAKQLDETHPVDVVSTFMGAHAVPAEWKDNPDGFVRVIVEEMIPKVSELGLAEFNDVFCERGVFTPEQARIILEAGKAYGLMPKIHADEIEPYGGAELAAEVGAVSADHLLRASDEGIRRMAEKGVIAVLLPGTAFFLMTKAANARKIIDAGAAVALSTDCNPGSSPTVSLPLIMNLGCLQMGMTPAEALAAVTINAAHAINRGHEIGSIEVGKKADLVLFDVPNYMQLIYHYGMNHTDTVVKNGRVVVKSGRLCY
Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
C5DA20
Q8R3F9
STPAP_MOUSE
U6 snRNA-specific terminal uridylyltransferase 1
Mus
MAAVDSDVVSLPRGRFRCCLCDVTTANRPSLDAHLKGRKHRDLVQLRATRKAQGLRSVFVSGFPRDVGSAQLSEYFQTFGPVANIVMDKDKGVFAIVEMGDISAREAVLSQPKHSLGGHGLRVRPREQKEFQSPASKSPKGVDSSSHQLVQALAEAADVGAQMVKLVELRELSEAERQLRNLVVALMQEVFTEFFPGCVVHPFGSTVNSFDVHGCDLDLFLDMGDMEETEPDPKAPKVPETSSLDSALASSLDPQALACTPASPLDSLSPTSVQESESLDFDTPSSLAPQTPDSALGSDTVTSPQSLPPVSPLQEDRKEGKQGKELELAEEASKDEKEEAAAVLELVGSILRGCVPGVYRVQTVPSARRPVVKFCHRPSGLHGDVSLSNRLALYNSRFLNLCSEMDGRVRPLVYTLRCWAQHNGLSGGGPLLNNYALTLLVIYFLQTRDPPVLPTVAQLTQRAGEGEQVEVDGWDCSFPKDASRLEPSTNVEPLSSLLAQFFSCVSCLDLSGSLLSLREGRPLMVAEGLPSDLWEGLRLGPMNLQDPFDLSHNVAANVTGRVAKRLQSCCGAAASYCRSLQYQQRSSRGRDWGLLPLLQPSSPSSLLSAKLIPLPSAPFPQVIMALVDVLREALGCHIEQGTKRRRSEGARIKDSPLGGVNKRQRLGGQEKSFEEGKEEPQGCAGDHSENEVEEMVIEVRETPQDWALLHSGPPEEELPLMTANCLDKAAEHNPMKPEVAGEGSQGETGKEASHPSSVSWRCALWHQVWQGRRRARRRLQQQTKEEGRGGPTTGAEWLAMEARVTQELKGPNSEQERPPGEPLLSFVASASQAEQTLTVAPLQDSQGLFPGLHHFLQGFIPQALKNLLK
Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs. Localizes to nuclear speckles together with PIP5K1A and mediates polyadenylation of a select set of mRNAs, such as HMOX1. In addition to polyadenylation, it is also required for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted pre-mRNAs and promotes the recruitment and assembly of the CPSF complex on the 3'UTR of pre-mRNAs. In addition to adenylyltransferase activity, also has uridylyltransferase activity. However, the ATP ratio is higher than UTP in cells, suggesting that it functions primarily as a poly(A) polymerase. Acts as a specific terminal uridylyltransferase for U6 snRNA in vitro: responsible for a controlled elongation reaction that results in the restoration of the four 3'-terminal UMP-residues found in newly transcribed U6 snRNA. Not involved in replication-dependent histone mRNA degradation.
Q8R3F9
G4NAZ1
CE12A_MAGO7
Endo-1,4-beta-glucanase cel12A
Pyricularia
MKTSAALLFLVSLASAAPMTPSPAAEAAAVLEGRQIQTLCDQYGYWSGNGYYVNNNMWGKDSGSGSQCTYIDSSSANHVSWRSTWQWSGGQNNVKSYPYSGRTIQRGRTIASINSMPSVVQWNYNNGNIRANVAYDLFTSTDPNRDNTHGDYELMVWLGRYGDVQPIGSQIGNANVGGRNWQLWSGLNNGMRVYSFVTTQGAITYFNADIKQFFTYLQQSQGFPASQQYLTTFQFGTEPFTGGQTTFQVNSFGANVQ
Endoglucanase that functions in part to hydrolyze 1,3-1,4-beta-glucan during infection and spore formation. Shows preferential hydrolysis of barley beta-glucan and lichenan.
G4NAZ1
Q6D2A2
YEGS_PECAS
Probable lipid kinase YegS-like
Pectobacterium
MEKNPITLLILNGKSAGNDELREAIGELRKDGYTLHVRVTWEYGDAKRYVEEAIQLKADNVIAAGGDGTVNEVAAALAVQPEAVRPCLGIVPLGTANDFATSCQIPMEMHNALTLAIKGRATAIDIAKVNDGHYFINMATGGFATRITTETPAKMKAALGSASYVLHALFRMDMLQAERCEIHGPDFHWSGDTLVIAVGNGRQAGGGQQLCPEALINDGLLELSVLSATELLPNMLQAWFTGSENQNMISATLPWLEISAPDDMTFNLDGEPLTAKRFRIEVLPAAIHCRLPPQCSLLE
Probably phosphorylates lipids; the in vivo substrate is unknown.
Q6D2A2
Q9K4M4
SOXA_PSESE
Thiosulfate-oxidizing multienzyme system protein SoxA
Pseudaminobacter
MTVSKRFLAPVFAMVGGLVLAFSANADPVDEELVIDDIPMVTRAAAPEGHPFDEGLSGWLFREAETRETEADSFANPGMLAVERGADIWNTVEGSAGKSCASCHDDAATSMKNVGAQYPKWDADAKRPINIELQIDKCRVENMGAEPYKFDAEGQVALTSYIKHQSLGTPVKMDLSDGELQDWWEKGKELYYTRTGQLNFACASCHEDSMGKYIRADHLSQGQANGFPTYRFNTGGMVSLHNRFRGCIRDTRAEMPKAFSDELMALEVYVTWRGTGLSVETPAVRQ
C-type diheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the liberation of two electrons, which may be transferred from the SoxAX complex to another cytochrome c that then channels them into the respiratory electron transport chain. Some electrons may be used for reductive CO(2) fixation.
Q9K4M4
A8Z3R9
RNC_STAAT
Ribonuclease III
Staphylococcus
MSKQKKSEIVNRFRKRFDTKMTELGFTYQNIDLYQQAFSHSSFINDFNMNRLDHNERLEFLGDAVLELTVSRYLFDKHPNLPEGNLTKMRATIVCEPSLVIFANKIGLNEMILLGKGEEKTGGRTRPSLISDAFEAFIGALYLDQGLDIVWKFAEKVIFPHVEQNELLGVVDFKTQFQEYVHQQNKGDVTYNLIKEEGPAHHRLFTSEVILQGEAIAEGKGKTKKESEQRAAESAYKQLKQIK
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.
A8Z3R9
B5ZAW9
ATPL_UREU1
Lipid-binding protein
Ureaplasma
MSSFIDITNVISSHVEANLPAVSAENVQSLANGAGIAYLGKYIGTGITMLAAGAVGLMQGFSTANAVQAVARNPEAQPKILSTMIVGLALAEAVAIYALIVSILIIFVA
Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.
B5ZAW9
Q63HQ0
AP1AR_HUMAN
Gamma-A1-adaptin and kinesin interactor
Homo
MGNCCWTQCFGLLRKEAGRLQRVGGGGGSKYFRTCSRGEHLTIEFENLVESDEGESPGSSHRPLTEEEIVDLRERHYDSIAEKQKDLDKKIQKELALQEEKLRLEEEALYAAQREAARAAKQRKLLEQERQRIVQQYHPSNNGEYQSSGPEDDFESCLRNMKSQYEVFRSSRLSSDATVLTPNTESSCDLMTKTKSTSGNDDSTSLDLEWEDEEGMNRMLPMRERSKTEEDILRAALKYSNKKTGSNPTSASDDSNGLEWENDFVSAEMDDNGNSEYSGFVNPVLELSDSGIRHSDTDQQTR
Necessary for adaptor protein complex 1 (AP-1)-dependent transport between the trans-Golgi network and endosomes. Regulates the membrane association of AP1G1/gamma1-adaptin, one of the subunits of the AP-1 adaptor complex. The direct interaction with AP1G1/gamma1-adaptin attenuates the release of the AP-1 complex from membranes. Regulates endosomal membrane traffic via association with AP-1 and KIF5B thus linking kinesin-based plus-end-directed microtubular transport to AP-1-dependent membrane traffic. May act as effector of AP-1 in calcium-induced endo-lysosome secretion. Inhibits Arp2/3 complex function; negatively regulates cell spreading, size and motility via intracellular sequestration of the Arp2/3 complex.
Q63HQ0
P19982
MDH_STRAR
Malate dehydrogenase
Streptomyces
TRTPVNVTVTGAAGQIGYALLFRIASGHLLG
Catalyzes the reversible oxidation of malate to oxaloacetate.
P19982
P23224
PRTA_LISMO
Zinc metalloproteinase
Listeria
MKSKLICIIMVIAFQAHFTMTVKADSVGEEKLQNNTQAKKTPADLKALPDSCEAKDFYKNFKILDMTKDKLGVTHYTLALSSGGYLTDNDEIKVHVTPDNKITFINGDLQQGQLRITNQIKITEKNAIEKAFEAIGQSEAHVKSYVGNPVKEKEIILNSRTKRLVYNIKLIFAEPEVASWIVQVDVETGAILKKQNMLSEVERADTHKDFQALGKGANRLLQRPLHVMKINDLFYLVDRTHKGLIRTFDLKHNTDTSFGKVVSNKTNMFTDPEFSSAVDAHFYASEVYEYYKNVHQLESLDGKGGEIDSFVHYGLNCNNAFWDGQEILYGDGDKKNFKPFSCAKTIVGHELTHAVIQYSAGLEYEGQSGALNESFADVFGYFIAPNHWLIGEDVCVRGSRDGRIRSIKDPDKYNQAAHMKDYESLPLTEEGDWGGVHYNSGIPNKAAYNTITKLGKEKTEQLYFRALKYYLTKKSQFTDAKKALQQAAKDLYGEDASKKVAEAWEAVGVN
Probably linked to the pathogenesis of listerial infection.
P23224
B2B3P6
LAP1_PODAN
Leucyl aminopeptidase 1
Podospora anserina
MKASLLALLLPAVSARNVNLAGDTQRPMTHEEAAAATYHIEISPGNTRWVTEDEKWALRRKGINFFDITDHPDLGATINTLVGPPKKKAVFPKKPTYQDAVKPLFTNLSKSHLEENLEKFTSFHTRYYKSDWGRQSSEWLLGKVQETIKEAGAEKYVTAKHFKHPWGQNSIIATIPGKTNQTVVIGAHQDSINLFLPSILAAPGADDDGSGTVTILEALRVILQSKDIVKGKHPNTLEFHWYSAEEGGLLGSQAIFSAYEKERRDVKAMLQQDMTGFITRTIQAGLPESVGVIVDFVDPKLTEFIKKIITEYCDIPFVETKCGYACSDHASASKAGYPSAFVIESAFEYSDNHIHTTDDLIKYLSFDHMIQHAKLTLAFAYELAFADFPALEKGK
Extracellular aminopeptidase that allows assimilation of proteinaceous substrates.
B2B3P6
Q86UE4
LYRIC_HUMAN
Metastasis adhesion protein
Homo
MAARSWQDELAQQAEEGSARLREMLSVGLGFLRTELGLDLGLEPKRYPGWVILVGTGALGLLLLFLLGYGWAAACAGARKKRRSPPRKREEAAAVPAAAPDDLALLKNLRSEEQKKKNRKKLSEKPKPNGRTVEVAEGEAVRTPQSVTAKQPPEIDKKNEKSKKNKKKSKSDAKAVQNSSRHDGKEVDEGAWETKISHREKRQQRKRDKVLTDSGSLDSTIPGIENTITVTTEQLTTASFPVGSKKNKGDSHLNVQVSNFKSGKGDSTLQVSSGLNENLTVNGGGWNEKSVKLSSQISAGEEKWNSVSPASAGKRKTEPSAWSQDTGDANTNGKDWGRSWSDRSIFSGIGSTAEPVSQSTTSDYQWDVSRNQPYIDDEWSGLNGLSSADPNSDWNAPAEEWGNWVDEERASLLKSQEPIPDDQKVSDDDKEKGEGALPTGKSKKKKKKKKKQGEDNSTAQDTEELEKEIREDLPVNTSKTRPKQEKAFSLKTISTSDPAEVLVKNSQPIKTLPPATSTEPSVILSKSDSDKSSSQVPPILQETDKSKSNTKQNSVPPSQTKSETSWESPKQIKKKKKARRET
Down-regulates SLC1A2/EAAT2 promoter activity when expressed ectopically. Activates the nuclear factor kappa-B (NF-kappa-B) transcription factor. Promotes anchorage-independent growth of immortalized melanocytes and astrocytes which is a key component in tumor cell expansion. Promotes lung metastasis and also has an effect on bone and brain metastasis, possibly by enhancing the seeding of tumor cells to the target organ endothelium. Induces chemoresistance.
Q86UE4
B8DBN0
PPAX_LISMH
Pyrophosphatase PpaX
Listeria
MTGKITTLLFDLDGTLINTNELIIKTFQVTLQEFLPDRVFTREDILPFIGPSLMETFREINPAHADEMRAFYREYNLKHHDDLILEYDGVYEAIRALYEEDYKLGIVSTKMYDTIMRGLKVTGLDKFFQVVIGLDQVSNAKPDPEGIEMALSLLNATKEEAIMIGDNYHDIEAGKNAETLTAGVAWAIKGPEHLAQFQPDFMLEKMSDLLAIVRDEE
Hydrolyzes pyrophosphate formed during P-Ser-HPr dephosphorylation by HPrK/P. Might play a role in controlling the intracellular pyrophosphate pool.
B8DBN0
Q9CK40
TORD_PASMU
Chaperone protein TorD
Pasteurella
MMPFSREERQFVYTWLSNMLGHELSASQLAQYQQGLFDDFFAFLTEQGFQAQVEGIQQQLQQLKTVELAHLELAADYTQLFLLDGSSSALPYASVYLPEAQLTCHFTFLEALLVRFQLQLNRDKPEPSDHLCVYLELLRQLAEVDDMKTYRQLIQDALLPWLLPFNDKVQRVKTRTTFYQQVVVLLILLLQADCQN
Involved in the biogenesis of TorA. Acts on TorA before the insertion of the molybdenum cofactor and, as a result, probably favors a conformation of the apoenzyme that is competent for acquiring the cofactor.
Q9CK40
P10065
CRGA_RAT
Gamma-crystallin 1-1
Rattus
MGKITFYEDRGFQGRCYECSSDCPNLQTYFSRCNSIRVDSGCWMLYERPNYQGYQYFLRRGDYPDYQQWMGFSDSIRSCRSIPYTSSHRIRLYERDDYRGLVSELTEDCSCIHDRFRLNEIYSMHVLEGSWVLYEMPNYRGRQYLLRPGDYRRYHDWGAMDAKVGSLRRVMDLY
Crystallins are the dominant structural components of the vertebrate eye lens.
P10065
Q9VDD3
SNMP1_DROME
Sensory neuron membrane protein 1
Sophophora
MQVPRVKLLMGSGAMFVFAIIYGWVIFPKILKFMISKQVTLKPGSDVRELWSNTPFPLHFYIYVFNVTNPDEVSEGAKPRLQEVGPFVFDEWKDKYDLEDDVVEDTVSFTMRNTFIFNPKESLPLTGEEEIILPHPIMLPGGISVQREKAAMMELVSKGLSIVFPDAKAFLKAKFMDLFFRGINVDCSSEEFSAKALCTVFYTGEIKQAKQVNQTHFLFSFMGQANHSDSGRFTVCRGVKNNKKLGKVVKFADEPEQDIWPDGECNTFVGTDSTVFAPGLKKEDGLWAFTPDLCRSLGAYYQHKSSYHGMPSMRYTLDLGDIRADEKLHCFCEDPEDLDTCPPKGTMNLAACVGGPLMASMPHFYLGDPKLVADVDGLNPNEKDHAVYIDFELMSGTPFQAAKRLQFNLDMEPVEGIEPMKNLPKLILPMFWVEEGVQLNKTYTNLVKYTLFLGLKINSVLRWSLITFSLVGLMFSAYLFYHKSDSLDINSILKDNNKVDDVASTKEPLPSANPKQSSTVHPVQLPNTLIPGTNPATNPATHHKMEHRERY
Plays an olfactory role that is not restricted to pheromone sensitivity. Has a role in detection and signal transduction of the fatty-acid-derived male pheromone 11-cis vaccenyl acetate (cVA). Not required for sensitivity to general odorants. Acts in concert with Or67d and lush to capture cVA molecules on the surface of Or67d expressing olfactory dendrites and facilitate their transfer to the odorant-receptor Orco complex. Essential for the electrophysiological responses of these olfactory sensory neurons (OSNs) to cVA. Not required for the development of trichoid OSNs and support cells.
Q9VDD3
Q6UR32
UREE_YERRO
Urease accessory protein UreE
Yersinia
MILIEHILGNVKKDPVWQAKLKNATFDLLVLDQREAQKSRCRKSSTQGLDLGISLDRHVVLADGDVLAWDEKTNVAVVVQINLRDVMVIDLSELKTRSPDELIKTCFELGHALGNQHWKAVTKNNEVYVPLTVATTMMDSVMRTHGFQHLPFRFVKGAEILPRLSNSEARLLFGGAEDTDTHVHVASPLDEPHGSGLHIHGIHSHGDGHSHSHDDHDHDHNHDHDHKH
Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly.
Q6UR32
Q54J47
PDX1_DICDI
Probable pyridoxal 5'-phosphate synthase subunit pdx1
Dictyostelium
MENLTENQATNNNSPFRIKSSLAQMLKGGVIMDVVTPEQARIAEEAGACAVMALEKIPADIRHFGGVARMSDPGMIKEIMNAVTIPVMAKVRIGHFVEAQILQEIGVDYIDESEVLTIADNENHIDKSEFKVPFVCGCRNLGEALRRISEGAAMIRTKGEAGTGDVVEAVRHARAVNKEIKKIQNMDPHELYTYAKEIQAPLELVKEVKRLGRLPVVNFAAGGVATPADAAMMMQLGMDGVFVGSGIFKSGDPAKRAKAIVQAVTHFNNPQIVAKVSENLGEAMVGINVDTLKDKENQNWSTKEK
Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by pdx2. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively.
Q54J47
B2FJN5
AROQ_STRMK
Type II DHQase
Stenotrophomonas maltophilia group
MAKLLVLHGPNLNLLGTREPEVYGHTTLADIDQALASQASAAGHAVESLQSNAEHVLVDRVQAARDDGTAFILINPAAFTHTSVALRDALAAVAVPFIEIHLSNPHTREPFRQHSYFSDKAVGVVCGFGADSYRYAMDAALLRVSAT
Catalyzes a trans-dehydration via an enolate intermediate.
B2FJN5
A4SHP4
OTC_AERS4
Ornithine carbamoyltransferase
Aeromonas
MAFNLRNRNFLKLLDFTPREIQYMIDLAIDLKKAKYGGYERKHLTGKNIALIFEKTSTRTRCAFEVAAFDQGAQVSYLGPSGSQIGHKESMKDTARVLGRMYDGIEYRGYGQEIVEELGAYAGVPVWNGLTNEFHPTQILADFMTMLEHGKGKRLDQIKFAYLGDARNNMGNSLMVGAAKMGMDIRLVAPKAFWPEEDLVAKCRLIAEETGACITLTEDVKEGVLGTDFLYTDVWVSMGEAKEAWDQRVKLMTPYQINMDVINATKNPDVKFMHCLPAFHNDETTMGKEVADKYGMKGLEVTEDVFESEHSIVFDEAENRMHTIKAVMVATLGD
Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
A4SHP4
Q678S5
CYB_MIRAN
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
Mirounga
MANIRKTHPLAKIINNSFIDLPTPPNISAWWNFGSLLGICLILQILTGLFLAMHYTSDTTTAFSSVTHICRDVNYGWIIRYMHANGASMFFICLYMHMGRGLYYGSYTFTETWNVGIILLFTIMATAFMGYVLPWGQMSFWGATVITNLLSAVPYVGNDLVQWIWGGFSVDKATLTRFFALHFILPFVALALAAVHLLFLHETGSNNPSGIPSDSDKIPFHPYYTIKDILGALLLILTLMLLVLFSPDLLGDPDNYIPANPLSTPPHIKPEWYFLFAYAILRSIPNKLGGVLALILSILILAIIPLLHTSSQRGMMFRPISQCLFWLLVADLLTLTWIGGQPVEHPYIIIGQLASILYFMILLVLMPITSIIENHILKW
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Q678S5
P51123
TAF1_DROME
Transcription initiation factor TFIID 230 kDa subunit
Sophophora
MEMESDNSDDEGSIGNGLDLTGILFGNIDSEGRLLQDDDGEGRGGTGFDAELRENIGSLSKLGLDSMLLEVIDLKEAEPPSDDEEEEDARPSAVSASEGMSAFDALKAGVKREDGAVKAQDDAIDYSDITELSEDCPRTPPEETSTYDDLEDAIPASKVEAKLTKDDKELMPPPSAPMRSGSGGGIEEPAKSNDASSPSDDSKSTDSKDADRKLDTPLADILPSKYQNVDVRELFPDFRPQKVLRFSRLFGPGKPTSLPQIWRHVRKRRRKRNQSRDQKTTNTGGSDSPSDTEEPRKRGFSLHYAAEPTPAECMSDDEDKLLGDFNSEDVRPEGPDNGENSDQKPKVADWRFGPAQIWYDMLEVPDSGEGFNYGFKTKAASTSSQPQLKDERRVKSPEDDVEDPSIADDAFLMVSQLHWEDDVVWDGNDIKAKVLQKLNSKTNAAGWLPSSGSRTAGAFSQPGKPSMPVGSGSSKQGSGASSKKAQQNAQAKPAEAPDDTWYSLFPVENEELIYYKWEDEVIWDAQQVSKVPKPKVLTLDPNDENIILGIPDDIDPSKINKSTGPPPKIKIPHPHVKKSKILLGKAGVINVLAEDTPPPPPKSPDRDPFNISNDTYYTPKTEPTLRLKVGGNLIQHSTPVVELRAPFVPTHMGPMKLRAFHRPPLKKYSHGPMAQSIPHPVFPLLKTIAKKAKQREVERIASGGGDVFFMRNPEDLSGRDGDIVLAEFCEEHPPLINQVGMCSKIKNYYKRKAEKDSGPQDFVYGEVAFAHTSPFLGILHPGQCIQAIENNMYRAPIYPHKMAHNDFLVIRTRNNYWIRSVNSIYTVGQECPLYEVPGPNSKRANNFTRDFLQVFIYRLFWKSRDNPRRIRMDDIKQAFPAHSESSIRKRLKQCADFKRTGMDSNWWVIKPEFRLPSEEEIRAMVSPEQCCAYFSMIAAEQRLKDAGYGEKFLFAPQEDDDEEAQLKLDDEVKVAPWNTTRAYIQAMRGKCLLQLSGPADPTGCGEGFSYVRVPNKPTQTKEEQESQPKRSVTGTDADLRRLPLQRAKELLRQFKVPEEEIKKLSRWEVIDVVRTLSTEKAKAGEEGMDKFSRGNRFSIAEHQERYKEECQRIFDLQNRVLASSEVLSTDEAESSASEESDLEELGKNLENMLSNKKTSTQLSREREELERQELLRQLDEEHGGPSGSGGAKGAKGKDDPGQQMLATNNQGRILRITRTFRGNDGKEYTRVETVRRQPVIDAYIKIRTTKDEQFIKQFATLDEQQKEEMKREKRRIQEQLRRIKRNQERERLAQLAQNQKLQPGGMPTSLGDPKSSGGHSHKERDSGYKEVSPSRKKFKLKPDLKLKCGACGQVGHMRTNKACPLYSGMQSSLSQSNPSLADDFDEQSEKEMTMDDDDLVNVDGTKVTLSSKILKRHGGDDGKRRSGSSSGFTLKVPRDAMGKKKRRVGGDLHCDYLQRHNKTANRRRTDPVVVLSSILEIIHNELRSMPDVSPFLFPVSAKKVPDYYRVVTKPMDLQTMREYIRQRRYTSREMFLEDLKQIVDNSLIYNGPQSAYTLAAQRMFSSCFELLAEREDKLMRLEKAINPLLDDDDQVALSFIFDKLHSQIKQLPESWPFLKPVNKKQVKDYYTVIKRPMDLETIGKNIEAHRYHSRAEYLADIELIATNCEQYNGSDTRYTKFSKKILEYAQTQLIEFSEHCGQLENNIAKTQERARENAPEFDEAWGNDDYNFDRGSRASSPGDDYIDVEGHGGHASSSNSIHRSMGAEAGSSHTAPAVRKPAPPGPGEVKRGRGRPRKQRDPVEEVKSQNPVKRGRGRPRKDSLASNMSHTQAYFLDEDLQCSTDDEDDDEEEDFQEVSEDENNAASILDQGERINAPADAMDGMFDPKNIKTEIDLEAHQMAEEPIGEDDSQQVAEAMVQLSGVGGYYAQQQQDESMDVDPNYDPSDFLAMHKQRQSLGEPSSLQGAFTNFLSHEQDDNGPYNPAEASTSAASGADLGMDASMAMQMAPEMPVNTMNNGMGIDDDLDISESDEEDDGSRVRIKKEVFDDGDYALQHQQMGQAASQSQIYMVDSSNEPTTLDYQQPPQLDFQQVQEMEQLQHQVMPPMQSEQLQQQQTPQGDNDYAWTF
TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. Largest component and core scaffold of the complex. Contains N- and C-terminal Ser/Thr kinase domains which can autophosphorylate or transphosphorylate other transcription factors. Possesses DNA-binding activity. Essential for progression of the G1 phase of the cell cycle. Negative regulator of the TATA box-binding activity of Tbp.
P51123
P71499
GRPE_MYCCT
HSP-70 cofactor
Mycoplasma
MTEELKNKKNNKNYYSQNKNKTKAEFQKPHVKKNQYLKLKTKLDTALLEVQNLKDLNETLKKDIESERQLNLAEISNLTKKYNQKEIEIQKYGASKLARDLIQPLEILKKVVNAPNNNEVVQAYVKGFEMIVSQINNVLESHHIKAMNVKVGDMFNPHLHDANEAVESDEYKTNQIVGVLSDGYMIHDKVLIYAIVKVAK
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
P71499
Q7VAR8
ILVC_PROMA
Ketol-acid reductoisomerase type I
Prochlorococcus
MAKLFYDSDADLQLLSQKTVAIIGYGSQGHAHALNLKDSGIDVVVGLYEGSRSASKASSDGLEVMSVADASAKADWIMILVPDEFQRDIYAKEVAPHLKPGKILSFAHGFNIRFGLIEPPSFVDVVMIAPKGPGHTVRWEFQNGQGVPALFAIEQDASGQARSLAMAYAKGIGGTRAGILETNFKEETETDLFGEQAVLCGGLSALVKAGFETLVEAGYQPELAYFECLHEVKLIVDLMVKGGLTAMRDSISNTAEYGDYVSGPRLINADTKKEMKKILADIQDGTFAKNFVAECEAGKPEMKRIREEDSLLPIEKVGKGLRAMFSWLKTD
Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
Q7VAR8
A8G4F2
ILVD_PROM2
Dihydroxy-acid dehydratase
Prochlorococcus
MNKLRSSAITQGVQRSPNRSMLRAVGFNDEDFNKPIIGVANGYSTITPCNIGLNKLALKAEESIRRSGGMPQKFGTITVSDGISMGTEGMKYSLVSREVIADSIETACNAQSMDAVLAIGGCDKNMPGAMIAIARMNIPSIFIYGGTIKPGKLHGEDLTVVSAFEAVGQLTSGKINEKRLIEVEKNCIPGAGSCGGMFTANTMSAVIEVLGLSLPHSSTMAAEDLEKELSAEKSAEILVSAIKKNIRPLDLMTKKAFENAISVIMAVGGSTNAVLHILAIANTAGIDINIDDFERIRQKVPVICDLKPSGKFVTVDLHNAGGIPQVMKILLNAGLIHGECKNIEGKTITEYLQNIPDKPPSNQNVIRGIDYPLYKKGHLAILKGNLAKEGSVAKISGVKNPVLTGPAKIFESEEDCLKAILNNEIIAGDVVVVRNEGPVGGPGMREMLSPTSAIVGQGLGEKVALITDGRFSGGSYGLVVGHIAPEAAVGGNIALIKEGDLITVDAVKQLIEVDLSDEELEKRKNNWVKPKPKYKRGILSKYSKIVSTSSLGAVTDL
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 (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
A8G4F2
Q30YQ5
YIDC_OLEA2
Membrane protein YidC
Oleidesulfovibrio
MENKRPIIAVVLSLFVLIGWSYLSEFMGWTPAPAPVEQNATAVQQKASEPVAQPVQTASAPAASSFAPTEGREVKVDTPLYTAVFQSQGGVLKHFRLKKYTESIEEGAPLVELVTPEAAGKAPMGLLLNGQPTWKLAAWQFEGDDLKLDGSGKGELVFVGEMDGVRFERTLSFDPETYLISEKVRLTDTAGVSRDVRLGMTLSTTSLSPEGGAYNLTRMAWYQDGFHQETSADDLRETGVKVDEGVNWGGVMCNYFMAVMAPAEGALPFKGVLEGGVYRSVVENSSLSIASGSSAEFGIGYYIGPKESDRLAAMPYHLDEALNYGWFTFLAKPLVSGLKFFYSYAGNYGVAIIILTILVKLLFWPLSQKSYKSMEQMKKLQPMVQKIKEKYGDDRQRMNQEVMELYKTYKVNPAGGCLPMLLQIPVFLGLYQGLLNAIELRHAPFIAHLPFTDIVWLADLSAKDPFYITPVVMGATMLLQQRLTPAPADPTQAKIMMFMPVVFTFMFLNFPAGLVVYWLVNNVLSIGQQWWMLRKS
Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins.
Q30YQ5
Q74M64
DNLI_NANEQ
Polydeoxyribonucleotide synthase [ATP]
Nanoarchaeum
MEFEKLANLFSKLETISDKTRKVQYIARFLKELKDQYKETLLLLQGTVFYPWEQKNLGIAEKGVIRAISIAYGIEKQKVEELFIKYGDLGIVAEKACEMRKQKPLLLKPLTVKDVYQTLRKIADIEGEGSQDKKIITFAKLLVNAKPKEAKYIVRLALEELRIGVGEGIIRDAIAIAFSVTPEAVEYAYSILLDFGEVVRIAKEQGEQGLWQVKLQVGRPFRVMLAIRARNVQEAFDIVGRPAMIEAKYDGFRLQIHKKGDQVWLWTRRLEDVTRQFPDVVNIVRNRVKANEIIFEAEAVGYDKKTNKFLPFQKISQRVKRKYDIEKMAKEIPVELHAFDIVYLEGEQLMKKPFKERRALLEKVIDEKEHEIQLSIGIIEKDDKKAYQFYQDCLNKGLEGVMFKNLNAPYQPGRRVGYMVKLKPTLETLDLVIVAAEWGEGKRSGWLTSFTVAALDKDTGNYLEVGEVGTGIKEKKERAEDITFEELTELLKPYIYKQEGKKVYVKPKIVVEVAYEEIQESPRYKSGFALRFPRIVRIRFDRSPKEIDTIDRIKQIYEMQRGGIHKQ
DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.
Q74M64
A1U0D8
DABA_MARN8
Probable inorganic carbon transporter subunit DabA
Marinobacter
MNAPVTYSASCEQVIPELVNEACERIAPIWPLDRWIAVNPWWGSRTGPVEKVSRELDNLFGAGLLMPPAFYREAWDGGRIQRPHLEEAAREAGLKDDSQALLAQLSGAASNQPGFVSALGYTRRGQQEPPLEEVREEIGRACARYFDLRQNRWRVSGTKQDLYQFWLSQSGRSLARKASVEMLLKPDWQEAAATVARELPYSSRQLPLVIHHLLGHLLGWASWCRGVDWRAALGDPHESGTEHFCAQLATIWLIHEAHALINMTEAERESWQNRYVNAFDLAPASANEQALWIWHRAYELAWQSRFLDDIRSSERSSLAEPDPVAEVQAAFCIDVRSEVIRRQLEKVYPEIRTLGVAGFFGMPIVHHRHGPTDDEARLPGLLAPVYRYSETLGSPSEDRELDRKLDSREQVRESVRRAKYSSLSTFTLVETTGLAWAWKLVRDSLNRNSAKAEAVEPGRLHHCVDGYPLSDPERVNLAEGLLRAMSLTKGFASVLLLVGHGAHTDNNPNEAGLACGACGGKNGGVNARVAAELLNDRQVRAGLAERGIVMPESTIALAAEHCTITDRITIYGRDQVPDSHQRVFNTLVEKLEAAGQACRRERATSLGLNGKTDDDLLAELKRRTRNWAEVRPEWGLANNAGMVIGPRSLTRSLDLGGRCFLHDYDPSQDPSGEVLTLLMSAPMVVANWINLQYFGSVARPDIFGAGNKLLHSVVGGNLGVVEGNGVDLKIGLPLQSVFDGEHWRHEPMRLAVVVDAPAERIEAVIRGNADVRALVENRWLWLHRVEGDQTLRYDDGRWVTT
Part of an energy-coupled inorganic carbon pump.
A1U0D8
P0A0I1
SECE_STAAM
Protein translocase subunit SecE
Staphylococcus
MAKKESFFKGVKSEMEKTSWPTKEELFKYTVIVVSTVIFFLVFFYALDLGITALKNLLFG
Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
P0A0I1
B4TBH3
MENC_SALHS
o-succinylbenzoic acid synthase
Salmonella
MRSAQVYRWQIPMDAGVVLRDRRLKTRDGLYVCLRDGEREGWGEISPLPGFSQETWEEAQTALLTWVNDWLQGSEGLPEMPSVAFGASCALAELTGVLPEAADYRAAPLCTGDPDDLVLRLADMPGEKIAKVKVGLYEAVRDGMVVNVLLEAIPDLHLRLDANRAWTPLKAQQFAKYVNPDYRARIAFLEEPCKTRDDSRAFARETGIAIAWDESLREADFTFEAEEGVRAVVIKPTLTGSLDKVREQVAAAHALGLTAVISSSIESSLGLTQLARIAAWLTPGTLPGLDTLHLMQAQQIRPWPGSALPCLKREELERLL
Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 2-succinylbenzoate (OSB).
B4TBH3
A2BRQ6
SASA_PROMS
Synechococcus adaptive sensor protein A
Prochlorococcus
MNDKKELKLILVAARNQLSSNDIKCLIAYLESDDCEFETSLQISEPKEQPELLELHRLVAIPALIKVSPAPKQIFAGSNIFSQLQKWLPRWSQEGLTKNLGINLQPSKIDSTRTQKEFLLEDELLVLRQENETLTKRIESQERLLRMVAHELRTPLTAATLAVQSQKLGQIDISKLQEVIKRRLEEIELLSQDLLEVGTTKWEALFNPQKIDLGNISAEVILELEKFWRIRNIEIDTDIPSDLPSVFADQRRMRQVFLNLIENAIKFSKDSGSIKITMIHKTNQWVEITICDKGAGIPLSEQKRIFLDRVRLPQTSEGTSGFGIGLSVCRRIVQVHGGRIWVVSEVGVGSCFHFTVPVWQGQNKEQQNLTKG
May be involved in signal transduction. Participates in the KaiABC clock protein complex, which constitutes the main circadian regulator in cyanobacteria, via its interaction with KaiC. Required for robustness of the circadian rhythm of gene expression and is involved in clock outputs.
A2BRQ6
P70708
PADI3_RAT
Protein-arginine deiminase type III
Rattus
MSLQRTVRVSLEHPTSAVCVAGVETIVDIYGSVPEGTDMFEVYGTPGVDIYVSPSMERNRERADTRRWCFNKGLEIIVVMNSPSNDLNDSHVQIAYHSSHEHLPLAYAVLYLTCVDITLDCDMNCADRQDRSFVDKRQWMWGPDGYGAILLVNCDRDEVSSDAQDNCDQCVRCLQDLEDMSVMVLRTQGPESLFDDHRLILHTSSCDAERARVFHVCGPEDSCEAYRCVLGPDRMSYEVPRLKGYEERFYVEGLSFPDAGFPGILSFHITLLDDSNEDYSETPIFTDTVVFRVAPWIMTPSTLPPLEVYVCQVRNNTCFVEAVEELARKAGCKLTICPQAENRNDRWIQDEMELGYTQAPHKTLPVVFDSPRNGELQGFPYKRILGLDFGYVTREPPDSSVSGLDSFGNLEVSPPVVANGKEYPLGRILIGGNLPGSRGRRVTQVVRDFLHAQKVQPLVELFVDWLAVGHVDEFLSFVPAPDGKGFRLLLASPGACFRLFQEKQKWGHGRSLLFEGVIGDRRVQTISINQVLSNQSLINFNKFAQSCIDWNREVLKRELGLGESDIIDIPQLFKSEKRKAVAFFPDLVNMLVLGKHLGIPKPFGPIINGRCCLEEKVRSLLEPLGLHCTFIDDFTPYHMLHGEVHCGTNVRREPFAFKWWHMVP
Catalyzes the deimination of arginine residues of proteins.
P70708
A8AUV1
IDI2_STRGC
Type 2 isopentenyl diphosphate isomerase
Streptococcus
MSQNRKDDHIKYALEQRPGYNSFDEMELVHRSLPKYDLAEIDLSTHFAGRDWEFPFYINAMTGGSQKGSQINEKLAQVAESCGLLFVTGSYSAALKNPSDTSYQVATGRPNLLLATNIGLDKPYQAAQQAVADLQPLFLQIHVNLMQELLMPEGEREFRSWRQHLTDYSQRLDLPLILKEVGFGMDRSTVEEARSLGIQTFDISGRGGTSFAYIENQRGGNRDYLNDWGQSTLQSLLALQPMRDEVELLASGGVRHPLDMIKALVLGAKAVGLSRAMLDLVKNYSVEEVIDIVEGWKSDLRLIMCALSCRNLQELKNVPYLLYGRLKEAQEQIK
Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
A8AUV1
Q01909
ATPG2_ARATH
F-ATPase gamma subunit 2
Arabidopsis
MTGSISTSWLLSSPSNSNSASSSESYSFIATLKPVRYYPFQSLTPNRISSRSPLPSIQIRAGIRELRERIDSVKNTQKITEAMRLVAAARVRRAQDAVIKGRPFTETLVEILYSINQSAQLEDIDFPLSIVRPVKRVALVVVTGDKGLCGGFNNAVTKKATLRVQELKQRGIDCVVISVGKKGNAYFSRRDEFDVDKCIEGGGVFPTTKEAQVIADDVFSLFVSEEVDKVELVYTKFVSLVKSDPVIHTLLPLSMKGESCDVKGECVDAIEDEMFRLTSKDGKLAVERTKLEVEKPEISPLMQFEQDPVQILDAMMPLYLNSQILRALQESLASELASRMNAMSNATDNAVELKKNLTMAYNRARQAKITGELLEIVAGAEALRES
Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Q01909
Q5N3N6
RL7_SYNP6
50S ribosomal protein L7/L12
Synechococcus
MSAKTDEILESLKTLTLLEAAELVKQIEEAFGVSAAAPVGGVVVAAAAGAAAEAVEEKTEFDVVLEEVPADKKIAVLKVVRGITGLGLKEAKDLVEAAPKPIKEGVSKDDAEAAKKELEEAGAKVSVK
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
Q5N3N6
Q735N3
PXPA_BACC1
5-oxoprolinase (ATP-hydrolyzing) subunit A
Bacillus cereus group
MTTIDLNCDLGESFGAYKMGNDDEILPFVSSINVACGFHAGDPSVMRQTVEKALQHNVAIGAHPGFPDLIGFGRRNMNVSASEVYDYVLYQIGALDAFVKAAGGKMQHVKPHGALYNMAATNPEIADAIAKAIYHSNPNLLLYGLANSEAFIQAAEKYNITLVQEAFADRTYKQDGTLTSRTEENALIKNEDEAIKQVLQMVKEGYVNSVNGEKVEVQAKTICLHGDSEKAVQFAERIYRTFELNGISICAPK
Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
Q735N3
Q6FFQ0
KGSDH_ACIAD
2,5-dioxovalerate dehydrogenase
Acinetobacter
MSENNGKQFINGQRVAANAPTIESINATDYQPTGYLFSQATLDEVDQAAQAAYQAFLKYQHTTQQQRADFLDEIAIQIENLGSKLQEVAAQETGLPLVRLQGETGRVTGQLRLFAELLRRGDFYGARIDTALPERKPLPRVDLRQYKIGVGPVAVFGASNFPLAFSTAGGDTVAALAAGCSVVFKAHSGHMATAELVAQAIEKAILNSGIPSGTFNMIFGSRVGANLVEHPLIQAAGFTGSLEGGMALFNLAQNRPQPIPFFAEMSSVNPVIVMPEALNARGEKVAQDTVASFNMGCGQFCTKPGLIIGIKSPAFDQFVTALIDTTRTAVPQIMLNQGTLKSYQQGIDALLNEQGFKCIASGQAPELISQAQPHLFQADQSVLLSGNPKLQHEVFGPMSIVIAVDDEATLLNGLEKLAGQLTATIIADESDLPQAKELLNLLTRKAGRVLFNGFPTGVEVSDAMVHGGPFPATSDSRGTSVGTGAIERFLRPVCYQNTSQVLLPDVLKDGNPLHITRLVNGVLTQN
Catalyzes the NAD(P)(+)-dependent oxidation of alpha-ketoglutaric semialdehyde (alphaKGSA) to alpha-ketoglutarate in the D-glutarate degradation pathway.
Q6FFQ0
B0KCM7
RS4_THEP3
30S ribosomal protein S4
Thermoanaerobacter
MGRYTGPTCRLCRREGMKLYLKGDKCYTDKCPFARRGYAPGQHGQEKKKLTNYGMQLREKQKLKRYYGVLERQFERLYEEAERMKGITGENLLQLLERRLDNVVFRLGFAASRPQARQLVSHGHIEVNGKKVDIPSFLVKPGDVISVREKSRSMELIKNNLEVSRNVPDWLELNKDAFEGRVVSLPRREHIDLPIQEHLIVELYSK
With S5 and S12 plays an important role in translational accuracy.
B0KCM7
Q1CRT7
RNH2_HELPH
Ribonuclease HII
Helicobacter
MTLGIDEAGRGCLAGSLFVAGVACSEKTALEFLKMGLKDSKKLSQKKRFFLEDKIKTHGEVGFFVVKKSAEAIDSLGLGACLKLAIEEILENGCSLANEIKIDGNTAFGLNKRYPNIQTIIKGDETIAQIAMASVLAKAAKDREMLELHALFKEYGWDKNCGYGTKQHIEAIIKLGATPFHRHSFTLKNRILNPKLLEVEQRLV
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Q1CRT7
Q2KD99
GRPE_RHIEC
HSP-70 cofactor
Rhizobium
MTDETTKNGPDATAADAAADAAANVEIDNSVQEEAKQPDPLELLKAENAELRDRYLRLAAEMDNLRRRTEREVKDAKSYSVAGFARDMLAVSDNLRRALDAISPEAKATADAGLTTLIEGVEMTERSMLSALERHGVRKLEPVGQKFDPNFHQAMFEVPNSEVPNNTVVQVVQAGFTIGERVLRPAMVGVAKGGPKPVEAEINSVFDEKDA
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
Q2KD99
B3EB70
NRDR_TRIL1
Transcriptional repressor NrdR
Trichlorobacter
MKCPFCGHPDSKVVDSRPDKGGAVIRRRRECEECARRFTTYERVEEMLPLVCKKDGRREHFDRMKVVSGIKKACEKRPVSVEDIERMADRLETRLQECGEREVPASRIGEWIMNELHAVDQVAYVRFASVYRSFKDINEFMVELQDLLKK
Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
B3EB70
B8CNY1
RUVB_SHEPW
Holliday junction ATP-dependent DNA helicase RuvB
Shewanella
MIEADRLIQPQVIEPDEVVDRAMRPKLLDEYTGQDDTRAQLKIFIEAAQKRGEALDHMLIYGPPGLGKTTLAMIVANEMGVNIKSTSGPVLEKAGDLAALLTNLEENDVLFIDEIHRLSPVVEEILYPAMEDYQLDIMIGEGPAARSIKLDLPPFTLVGATTQAGSLTSPLRARFGIPLRLEFYNIKDLSTIVIRSAKVMELEIDEEGAIEIARRSRGTPRIANRLLRRVRDFAEVKHSGAVTKVVAELALDMLDVDAEGFDYMDRKLLLAIIDKFMGGPVGLDNLAAAIGEERETIEDVLEPFLIQQGFVQRTPRGRIATQRAYNHFNLIQPEAK
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.
B8CNY1
Q9Z439
UBIE_PSEPU
Demethylmenaquinone methyltransferase
Pseudomonas
MNDQRKGDHAEPTTHFGYQDVPESQKAKKVAEVFHSVAAKYDLMNDVLSGGMHRLWKRFTIELSGVRAGNRVLDIAGGTGDLAAKFSRLVGPTGQVVLADINESMLKVGRDRLLDRGVAGNIEFVQADAEKLPFPDNHFDCVTIAFGLRNVTHKDEAIRSMLRVLKPGGRLLVLEFSKPTNKLMSKAYDAYSFAFMPLAGKLITNDSESYRYLAESIRMHPDQETLKAMMVEAGFDRVTYHNMTSGIVAVHRGIKP
Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
Q9Z439
Q601F2
RL21_MESH2
50S ribosomal protein L21
Mesomycoplasma
MFAIIKTSGRQLKVEKDQTIFVEKIDKNEGETITFTDILFINGKIGTPYVENASVTGIIEKQGKAKKIVVYRHNPKSTHKRKLGHRQLFTKVKITELKG
This protein binds to 23S rRNA in the presence of protein L20.
Q601F2
Q8UJ45
RECR_AGRFC
Recombination protein RecR
Agrobacterium tumefaciens complex
MAKRVTGPEIEKLIQLLAKVPGLGPRSARRAALHLIKKKEQLLGPLGHAMGEAYDKVKICSCCGNVDTIDPCTVCADDRRDQSVIIVVEDVSDLWALERAGAMNTAYHVLGGTLSPLDGVGPEDLNIKGLIDRVSAGGIRELIIAVNATVEGQATAHYITDRLSGLGIKITRLAHGVPVGGELDYLDEGTLTAALRARTTI
May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.
Q8UJ45
P27689
FMA3_DICNO
Serogroup B1/AC293
Dichelobacter
MKSLQKGFTLIELMIVVAIIGILAAFAIPAYNDYIARSQAAEGVSLADGLKVRIAENLQDGECKGPDADPQSGVVGNEDKGKYGLAKIEGDYDASKTEAGDPNGCKVEITYGQGTAGDKISKLITGKKLVLDQLVNGSFVQGDGTDLADKFIPNAVKAKKP
Major component of the type IV fimbriae that plays an essential role in twitching motility, natural transformation, and protease secretion.
P27689
A0A0H4ADX3
PKS19_PHANO
Alternariol synthase
Parastagonospora
MTRAKVIYFSGEIPQGDPEGDQRNLFRKLHLLSKERDYPILASFLETVTWAMKEEHRRLVRAQRDLLPTFESILDLTDHVVELRKTSLGGAIERVLVLAFQLGSFIAYHEAHPLEYNFQASDTFLIARGPGMLSAAAVALCPSLPMISSISADITRVAFRFGLVVDQVCRSLEVSPDEINSAGAWIYCVYGVDPQKAHEAVTRFNAEKAYAETSMASVFNDDGKSVSIGGPPSTLKTLFTECDFFKRTKNVPMKKVQGMWHTGKVYGTEHVHQIIPKIHQKHQLYLPLFSPVKGQPLEAASATDLLEQIMEEMLTQRIRWDRTIQNVTERLKQASPESTQLIAIQPSQYVESLIGQWRADMPTTTHTTEDMMSAVMDLPLGNSRAKDAKSSKIAVVGMACRFPGGADNAEKFWELLAQGRDVHSPIPSDRFNIETHVDPAGKVPNTSKTPYGCFVDNPGLFDAMFFGMSPREAEQTDPMQRLALVTAYEALEHSGYVHGRGIHARRVGTFYGQASDDYREVNSGQDVGTYFIPGGCRAFGPGRINYFFKFWGPSFSVDTACSSSLAAIQAACTSLWSGDVDMAITGGMNIITNSDVYAGLSNGHFLSPTGGCKTWDEGADGYCRADGVGSVVLKRLEDAEADNDNILGVVLAAATDHSAEAVSITHPHDVAQAHLYNQVARRAGIDPLAVGYVEMHGTGTQAGDSNEMKSVTNVFAPSTGHIRDRDSPLHIGTVKSNMGHGEAAAGIMAFVKTMLVFQKGIIPPHIGIKTRFNPALPEDLAKRNVVIPVTAAIWVRNSDRKRLAMVNNFGAAGGNTSIIIEEAAPRPRTSEDVRKAQVITVSAKTANSLQENLKALVDYIEARSELSVADLAYTLSARRNHYNYRVSVLATSTAEAASLLRPHIKTSLSQTPHSGKQVPIAFAFTGQGTFYIGIGAQLYRDSHEFRKHIDQLDSLVRRQNFASFLPVVSGNVQPEDVSIVTMNLAIVCVEIALARLWESFGIKPSMVIGHSLGEYAALAVAGVLSDSAAIFLVGTRARLLTSKCTSRTHGMLSVRASAADIKHAGGDIPFEVSCINGPNETVLGGTLSNMEALSATLAAAGYRTFKLDLPHAYHTYQMDTIVDELVKQTETVVCKKTTIPIISPRFSRVMTSEDSIDVSYLIGATRETVDFAGALDDAWQSGLVNESTIWLEMGHHPTCSGFISRTLSSTRMALPSLQRDTDNWLTLAKTLCSLYSAGIPIDWNEYHRPFEQALRLIDAPTYAWTNKNYWIQYRGDWNLTKGRAMPKLDPTTTVVPVSKRFQTSSIHRLISEQYTDGKAILSAESSITDPSLQGVVDGHAMNGYGVASSFLHAEMAFTLAKRVSDKSFASAVSFGINVADFEYHEPVVKLINTSEPQPILVSAEADLEKMEVHVKWFNPAKEIWYCHATVFYEDPSSWLSTWSRSTKLITSRIDALNDMAVTGKASKLTTDLAYSLFGKLVGYSKLYQTMQSVILNEDEAMAEVQFPEDTGGSWTVPPHFIDGLISLSGFILNGGTHFDNTNNFFITPSWKSMRFARPLTPGGRYTAYVRMVPSDNHSFVGDVYVLQGSEIVGVVEAILFLQWPRVMLNRFFRPADVTAKPAAKVPGKSEPSTRPHFKPHHVSRHKPTLTPRSPDEGSENSDSSGVIISRPGGYSSSDQDMEELPSPPAGMNDDMEKALALVAEELAVDIGLLTDDALIADLGLDSLMSLVMSQRLREELGLEIRDAFFLEITTIQDLKALLR
Non-reducing polyketide synthase that mediates the biosynthesis of alternariol (AOH), a micotoxin that seems not to be involved in virulence and oxidative stress tolerance . PKS19 alone is sufficient for AOH synthesis which is initiated by priming with acetyl-CoA, followed by sequential condensations of 6 malonyl-CoA units .
A0A0H4ADX3
Q985A5
ERA_RHILO
GTPase Era
Mesorhizobium
MERGMTDIETAETPATHSGFVALIGAPNAGKSTLVNQLVGAKVSIVTHKVQTTRAIVRGIATHDNAQIVFVDTPGIFKPKRRLDTAMVTTAWGGAKDADIVLLLIDAERGIRGDADAILERLKDVRQPMALILNKVDRVKHETLLALSAAANEKVPFKRTFMVSALTGSGCKDLLDYLAQALPAGPWYYPEDQISDLPMRQLAAEITREKLYLRLHQELPYSSHIETEKWEEKPDGSVRIDQTIYVERDSQKKIVLGHKGETIRAIGQAARMEIAGILEQKVHLFLFVKVRENWGDDPERYREMGLEFPH
An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Q985A5
A8G9V3
MTNN_SERP5
S-adenosylhomocysteine nucleosidase
Serratia
MKVGIIGAMEQEVTLLRDQIENRQTIQRAGCEIYTGQIGGVDVALLKSGIGKVSAAMGTTLLLEHCKPDLVINTGSAGGLASTLKVGDIVVSEEVRYHDADVTAFGYEPGQMAGCPAAFVADDALIALAESCIKQLNLNAVRGLICSGDAFINGAEPLARIRATFPNVAAVEMEAAAVGHVCHLFGTPFVVVRAISDVADSESHMSFEEFLVVAAKQSTLMVNAMLQTLAKRG
Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. Also cleaves 5'-deoxyadenosine, a toxic by-product of radical S-adenosylmethionine (SAM) enzymes, into 5-deoxyribose and adenine. Thus, is required for in vivo function of the radical SAM enzymes biotin synthase and lipoic acid synthase, that are inhibited by 5'-deoxyadenosine accumulation.
A8G9V3
C0ZW40
RS8_RHOE4
30S ribosomal protein S8
Rhodococcus erythropolis group
MTMTDPIADFLTRLRNANTAYHDEVKLPHSKIKANIAEILKREGYISDFRTEDAEVGKTLIVDLKYGPSRERSLAGVRRVSKPGLRVYAKSTNLPKVLGGLGVAIISTSSGLLTDRQAANQGVGGEVLAYVW
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
C0ZW40
P0C1Z4
KKX23_OPIMA
Toxin OmTx3
Opisthacanthus
NDPCEEVCLQHTGNVKACEEACQ
Decreases the amplitude of the potassium current of the rat channels Kv1.1/KCNA1 by 33% and Kv1.2/KCNA2 by 8% as well as human Kv1.3/KCNA3 by 70%.
P0C1Z4
Q3AHI9
CCS1_SYNSC
Cytochrome c biogenesis protein CcsB
unclassified Synechococcus
MASGMGPLKRLAAWFSDLRLAIVLLLLIALASAVGTGIPQGDPPSSYIDAYSDTPWLGLLHGEQVLQLQLDHVYSSGWFLALLAWLGLALILCSWRRQWPALMAARRWIDYRTTRQLSKLAIAESQPCPDTSQGLTQLETVLRASGWQVQRKPQRLAARRGAIGRVGPLLVHTGLVLLMLGAAWGALAGNRLERFLAPGRSLDLLDRDGTSQLTITLDRFAIDRDPAGRTEQFRSALKLQGPNQSLDAEISVNHPLRHRGITVYQADWSLATISLQIGRSPVLELPLQTYPELGDQIWGLVLPTRPDGTEPVFLSLESEQGPATVFDADGQQLARLRPGGPSAEVKGLPMRVDAVLPASGLLLKRDPGVPLVYLGFAVLLVGGGLSLVATRQLWAIAADGTLSVGGLCNRNLAAFATELPQLLQQVVVDQQG
Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment.
Q3AHI9
Q54PQ4
GEFA_DICDI
RasGEF domain-containing protein A
Dictyostelium
MITPTSFEPVELLYSKKKVNRTNWKKNVLKSNPEINNLCERIYPINRAIQFGKQFHPGKAEVKQKLDKTAIIQLILQHLSTKGLKQTKQTLEKEARTTTPIVEGLNESRLVTYIRNALKDTDRIYDLSMEHTEYSKEERQSKITEREELLFQMDLLEDEDEDDGVNIWDEPTENIITEKVHTTEYDINKSKENKDDQDDEVVKFASLNKLVEHLTHDSKHDLQFLKTFLMTYQSFCTPEKLMSKLQQRYNCPSGHDEMATRNIQIRVINVLKGWVDNYYSDFDDKLIAMLRTFIDQIQIKFPAPASAVNKSLTKMVEKLSPVNDSKHIFNEKTPEPMVPKNIFSNNLSIYDIDEEEIARQLTLIEFEIYRNIKPPELLNQSWNKTKLKSRAPNVLKMIDRFNSVSMWVATMIIQTTKVKARARMMTRFIKIADHLKNLNNYNSLMAIIAGLNFSSVYRLKYTREELSAQTMRTYSDLEKIMNSEGSFKTYRTRLQNVPPMLPYLGVHLTDLTFIDENPNNFVTDVGGKQVSLINFTKRTLVFKIISLIQETQVVPYNLQPVHQIQEFLLNIRSDLKAHTLDQYQQELYRESLKREPKKAQRSDVL
Ras-bound GDP/GTP exchange factor required for normal activation of adenylyl cyclase . Component of the Sca1 complex, a regulator of cell motility, chemotaxis and signal relay . The Sca1 complex is recruited to the plasma membrane in a chemoattractant- and F-actin-dependent manner and is enriched at the leading edge of chemotaxing cells where it regulates F-actin dynamics and signal relay by controlling the activation of rasC and the downstream target of rapamycin complex 2 (TORC2)-Akt/protein kinase B (PKB) pathway .
Q54PQ4
A5UHY5
EPMA_HAEIG
EF-P-lysine lysyltransferase
Haemophilus
MTALNHWQPSADIKNLLKRAKIIAEIRQFFTERGLLEVETPVLSEFGVTDLHLSTFSTEFLAPFGEQSKTLWLSTSPEYHMKRLLAAGSGPIFQISKVFRNEEAGNRHNPEFTMLEWYRPHFHMHRLINEVDDLLQQILDCPPAESLSYQFVFQEYVGLDPLSAERSELIEAARKHNFMAEDNEDRDTLLQFLFSEVVEPQIGKERPIAVYHFPSTQAALAQVSPEDQRVAERFEFYYKGLELANGFHELADAQEQRHRFELDNQQRQKCELPTREIDERFLAALEAGMPDASGVALGIDRLMMIALDCEKINDVISFAVDNA
With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.
A5UHY5