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AlphaFoldDB
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P24095
LOXX_SOYBN
Lipoxygenase
Glycine subgen. Soja
MFGIFDKGQKIKGTVVLMPKNVLDFNAITSIGKGGVIDTATGILGQGVSLVGGVIDTATSFLGRNISMQLISATQTDGSGNGKVGKEVYLEKHLPTLPTLGARQDAFSIFFEWDASFGIPGAFYIKNFMTDEFFLVSVKLEDIPNHGTIEFVCNSWVYNFRSYKKNRIFFVNDTYLPSATPAPLLKYRKEELEVLRGDGTGKRKDFDRIYDYDVYNDLGNPDGGDPRPILGGSSIYPYPRRVRTGRERTRTDPNSEKPGEVYVPRDENFGHLKSSDFLTYGIKSLSHDVIPLFKSAIFQLRVTSSEFESFEDVRSLYEGGIKLPTDILSQISPLPALKEIFRTDGENVLQFPPPHVAKVSKSGWMTDEEFAREVIAGVNPNVIRRLQEFPPKSTLDPTLYGDQTSTITKEQLEINMGGVTVEEALSTQRLFILDYQDAFIPYLTRINSLPTAKAYATRTILFLKDDGTLKPLAIELSKPHPDGDNLGPESIVVLPATEGVDSTIWLLAKAHVIVNDSGYHQLVSHWLNTHAVMEPFAIATNRHLSVLHPIYKLLYPHYRDTININGLARQSLINADGIIEKSFLPGKYSIEMSSSVYKNWVFTDQALPADLVKRGLAIEDPSAPHGLRLVIEDYPYAVDGLEIWDAIKTWVHEYVSLYYPTDAAVQQDTELQAWWKEAVEKGHGDLKEKPWWPKMQTTEDLIQSCSIIVWTASALHAAVNFGQYPYGGLILNRPTLARRFIPAEGTPEYDEMVKNPQKAYLRTITPKFETLIDLSVIEILSRHASDEIYLGERETPNWTTDKKALEAFKRFGSKLTGIEGKINARNSDPSLRNRTGPVQLPYTLLHRSSEEGLTFKGIPNSISI
Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. It catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure.
P24095
B7GTU6
GATA_BIFLS
Glutamyl-tRNA(Gln) amidotransferase subunit A
Bifidobacterium
MSNETATLVKLSAAEQAAAIKKGDVTSRELVEAHLKVIEAAEPSIKAFLKVSGDVALEQADAFDAKSAEDKAALPELAGVPIAIKDMIVTKGIETTAASKILEGWVPPYDATVIEKLKAAGMPILGKTNLDEFAQGSSTEHSAYQTTHNPWDTERVPGGSGGGSASAVAAFEAPIALGTDTGGSIRQPGALTGTVGVKPTYGGVSRFGAIAMASSLDQIGPVSRTVLDSALLQEIIGGHDKRDSTSIPEGPRPMVAAAREGAKRDLKGMKVGLIKELGGEGFQPGVEARFGEAVDKLKDMGAEVVEVSCPHIGYSLGAYYIIMPSEVSSNLARYDGMRYGLRVMPPAGVPQTAANMMAYTREAGFGDEVKRRIILGTYALSAGYYDAWYGSAQKVRTLIIEDFKKAFEQVDVLISPTSPSTAFKFGEKMDDPLAMYVNDIATIPANLAGMPAMSIPAGLSDDGLPVGFQFIAPQQRDEVMYKPAAALEAALEDGWNGPIWNDLKTPWLDGLGK
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
B7GTU6
G5ED45
HYL1_CAEEL
Ceramide synthase hyl-1
Caenorhabditis
MWRMSYFWHEPYWLPRNVTWPEVPAKFVDLLVPIYLAIPLVIIRILWESTIGVTYLYFRTNAYASRKNITLLGCMWEHMTGGFASVSRAKKILECFWRFSYYTFAFLYGLYVMKNSSWLYDVKQCWIGYPFHPVPDTIWWYYMIETGFYYSLLIGSTFDVRRSDFWQLMVHHVITIFLLSSSWTINFVRVGTLILLSHDVSDVFLEGGKLVRYDAHNKNMTNFMFVLFFSSWVATRLIYYPFIVIRSAVTEAAALIQPDYILWDYQLSPPYAPRLIVFALILLFFLHIFWTFIILRIAYRTSTGGQAKDVRSDSDSDYDEEEMARRERTRLLKKKKNKVSPSTDDDDDEGEEEKNDRKARHRRAPRKE
Catalyzes the acylation of sphingoid bases to form ceramides. Sphingolipids from Caenorhabditis elegans contain exclusively isosphingoid bases. Exhibits substrate preference for fatty acyl-coA chains containing 24 and 26 carbons.
G5ED45
Q9ZLZ7
SYE1_HELPJ
Glutamyl-tRNA synthetase 1
Helicobacter
MSLIVTRFAPSPTGYLHIGGLRTAIFNYLFARANQGKFFLRIEDTDLSRNSIEAANAIVEAFKWVGLEHDGEILYQSKRFEIYKEYIQKLLDEDKAYYCYMSKEELDALREEQKARKETPRYDNRYRDFKGTPPKGIEPVVRIKVPQNEVIGFNDGVKGEVKVNTNEIDDFIIARSDGTPTYNFVVTIDDALMGITDVIRGDDHLSNTPKQIVLYKALNFKIPNFFHVPMILNEEGQKLSKRHGATNVMDYQEMGYLKEALVNFLARLGWSYQDKEVFSMQELLEWFNPKDLNSSPSCFSWHKLNWLNAHYLKNQSVQELLKLLKPFSFSDLSHLNPAQLDRLLDALKERSQTLKELALKIDEVLTAPIEYEEKVFKKLNQALVMPLLEKFKLALDKTDFNDESALENAMHQIIEEEKIKAGHFMQPLRLALLGKGGGIGLKEALFILGKAESIKRIEEFLKN
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Q9ZLZ7
C1FMV9
RPOB_CLOBJ
Transcriptase subunit beta
Clostridium
MVHPVQVGKRTRMSFSRLKEVGQMPNLIEVQLDSYDWFLKEGLQEVFDDINPIQDYTGNLNLEFVGYKLDLDSIKYSVEECKERDSTYAAPLKVKVRLLNKETGEIKEQEVFMGDFPLMTEQGTFIINGAERVIVSQLVRSPGVYYDMTVDKTGSKLFSATVIPNRGAWLEYETDSNNIIYVRIDKTRKLPITILARALGYGTDAEIIEFFGEDERLKATIEKDNTKTREEALLEIYKRLRPGEPPTVDSAESLIESLFFDAKRYDLSRVGRYKFNKKLAIHLRITNQIADQDIVNPQTGEILVQKGEKIDKDKAIEIQNCGINEVYIKIDDKSFKVIGNHFVDIHSLVPFDISDLNIKEYVFYPVLKEILDNYADEESIKEEIRKNIYRLIPKHIIREDIYATINYELGLSYDIGYKDDIDHLGNRRLRSVGELLQNQFRIGLSRMERVVKERMTIQDQEVITPQALINIRPVAASIKEFFGSSQLSQFMDQTNPLSELTHKRRLSALGPGGLSRERAGFEVRDVHHSHYGRMCPIETPEGPNIGLINSLATFAKVNEYGFIETPYRRIDPKNKRATNDIVYMTADEEDLYVIARSDEPIDENGYFIDDKVTVRAKEEVLVVPVSEVEYMDISPRQLVSVATAMIPFLENDDASRALMGSNMQRQAVPLLKPQAPIVGTGIEYKAATDSGVLPKAKNAGTVVYVSADEIRVRRDSDGGIDKYKLLKFKRSNQGTCINQRPIVSKGEVVAKETLLADGPSTDLGEIALGKNILMGFITWEGYNYEDAMLISEQLVKEDVFTSIHIEEYEAEARDTKLGPEEITRDIPNVGEEALKDIDERGIIRIGAEVRSGDILVGKVTPKGETELTAEERLLRAIFGEKAREVRDTSLRVPHGEAGIIVDVKIFTRENGDELPPGVNKLVRCYIAQKRKISVGDKMAGRHGNKGVISRVLPEEDMPFLPDGRPLQICLNPLGVPSRMNIGQVLEVHLGLAASKLGWHIATPVFDGAIESDIVDCLRKAGYSEDGKTVLYDGRTGEPFDNRVTVGYMYILKLAHLVDDKIHARSTGPYSLVTQQPLGGKAQFGGQRFGEMEVWALEAYGAAHTLQEILTVKSDDVVGRVKTYEAIVKGENIPEPGVPESFKVLIKELQALCLDVKVLNDDNQEIKLKESVDEDADELEVNIEGTENQPEEKEEKEKEDSDEYDDLREEDVEPDLEELSLDDLDLDDFGDEH
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
C1FMV9
Q8D0W8
CYSA_YERPE
Sulfate-transporting ATPase
Yersinia
MSIEINNISKYFGRTKVLNDITLDIPSGQMVALLGPSGSGKTTLLRIIAGLENQNAGRLSFHGTDVSRLHARDRRVGFVFQHYALFRHMTVFDNIAFGLTVLPRRERPNAAAIKQKVGQLLEMVQLGHLAERFPSQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVVSQGNIEQVGTPDEVWREPATRFVLEFLGEVNRLSGEIRGSQLFIGAHHWPLDLAPMHQGSVDLFLRPWEMEVSTQSSDRCPLPVQVLEVSPRGHFWQLTVQPIGWHQDPISVVLPEGNIDAPVRGNRYYVGGLNARLYSGNQLLQPIALAQSA
Part of the ABC transporter complex CysAWTP involved in sulfate/thiosulfate import. Responsible for energy coupling to the transport system.
Q8D0W8
Q59Q46
IMDH_CANAL
Inosine-5'-monophosphate dehydrogenase
Candida
MVFETSKATSYLKDYPKKDGLSVKELIDSTNFGGLTYNDFLILPGLINFPSSAVSLETKLTKKITLKSPFVSSPMDTVTEENMAIHMALLGGIGIIHHNCTSEEQAEMVRKVKKYENGFINDPVVISPEVTVGEVKKMGEVLGFTSFPVTENGKVGGKLVGIITSRDIQFHEDNKSPVSEVMTKDLVVGKKGISLTDGNELLRSSKKGKLPIVDAEGNLVSLISRTDLQKNQDYPNASKSFHSKQLLCGAAIGTIDADRERLDKLVEAGLDVVVLDSSNGSSVFQLNMIKWIKEKYPELQVIAGNVVTREQAALLIEAGADALRIGMGSGSICITQEVMACGRPQGTAVYGVTEFANKFGVPCIADGGIGNIGHITKALALGASCVMMGGLLAGTAETPGDYFYRDGKRLKTYRGMGSIDAMQQTNTNANASTSRYFSEADKVLVAQGVSGSVVDKGSITKFVPYLYNGLQHSLQDIGIKSIDELRENVDNGEIRFEFRTASAQFEGGVHGLHSYEKRLHN
Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
Q59Q46
Q39617
POR_CHLRE
NADPH-protochlorophyllide oxidoreductase
Chlamydomonas
MALTMSAKSVSARAQVSSKAQAAPAVAVSGRTSSRVMPAPALAARSSVARTPLVVCAATATAPSPSLADKFKPNAIARVPATQQKQTAIITGASSGLGLNAAKALAATGEWHVVMACRDFLKAEQAAKKVGMPAGSYSILHLDLSSLESVRQFVQNFKASGRRLDALVCNAAVYLPTAKEPRFTADGFELSVGTNHLGHFLLTNLLLDDLKNAPNKQPRCIIVGSITGNTNTLAGNVPPKANLGDLSGLAAGVPAANPMMDGQEFNGAKAYKDSKVACMMTVRQMHQRFHDATGITFASLYPGCIAETGLFREHVPLFKTLFPPFQKYITKGYVSEEEAGRRLAAVISDPKLNKSGAYWSWSSTTGSFDNQVSEEVADDSKASKLWDISAKLVGLSA
Phototransformation of protochlorophyllide (Pchlide) to chlorophyllide (Chlide).
Q39617
A6WC46
COXX_KINRD
Heme O synthase
Kineococcus
MTVADPRLTDAPAHSRTSLLGRRRGGRPPRFPRAAAYVALTKPRIVELLLITTIPVMLFAAGGLPSGWLILTTFVGGALAAGCANTLNCYFDRDIDALMKRTENRPLVTGEVSPRQALVFATVLGIASTAIFVAFVNVLSAALALGAILLYVVGYTLLLKRRTSQNIVWGGVAGCMQVLIGWTAVRDSLDWAPFVLFGVIFLWTPPHYWPLSVRYREDYANAGVPMLPVVAKPTTVSRQIVLYTIAMVLCSLLLVPLGGAGVVYGAAALVLGIGFLVQTIGLHRRATRFEVETGGRDAGTLEQLKRISPMGVFHGSITYLTLLSAAVAVDPFVRVGWPF
Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
A6WC46
Q8TQ68
SYDND_METAC
Non-discriminating aspartyl-tRNA synthetase
Methanosarcina
MSLANLRTHYTAEVKPESVDNGQKITLAGWIHEVRDLGGICFVVLRDREGKAQVTLVKKKIDKELFDAARRLIRESVISVTGSVKFEEKAPNGYELLPEEIKVLNVAGSPLPMDTTGKVEAELDTRLDSRFIDLRRAETTAVFKIRHEALQAIREYFVKNKFIETATPKVVATATEGGTALFPITYFDREAFLNQSPQLFKQILMGGGFDRVFEIGPIFRAEEHDTRRHLNEATSIDVEVSFADHFDVMEILENLVAHIYTRVIENCKASLEILGVELKVPKTPFLKLTYDEVIEIVNSRCEEKMHWGDDLGTLGEHTVGNYVYETTGESHYFIIDWPTEIKPFYAMPYEDRPEFSKSFDMMHRTMELSSGAQRIHISELLKSRIESQGLNPDGFEFYLKAFEYGMPPHAGWGMGCERFVMTMLGTENIRDTVLFPRDRRRLSP
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Q8TQ68
Q9ZP55
DRP4C_ARATH
Dynamin-related protein 4C
Arabidopsis
MVKKKVATKKNSPSLAIAKKKSRSNKDVVSVEAPIISSYNDRIRPLLDTVDRLRNLNVMREGIHLPTIVVVGDQSSGKSSVLESLAGISLPRGQGICTRVPLVMRLQRSSSPEPEIWLEYNDKVVPTDEEHIAEAIRAATDVIAGSGKGVSDAPLTLHVKKAGVPDLTMVDLPGITRVPVNGQPENIYEQISGMIMEYIEPQESIILNVLSATVDFTTCESIRMSRKVDKTGQRTLAVVTKADMAPEGLLQKVTADDVSIVLGYVCVRNRIGEETYEEARMQEELLFRTHPVLSLIDEDIVGIPVLAQKLMLIQSSMIARCLPKIVSKINQKLDTAVLELNKLPMVMASTGEALMALMDIIGSAKESLLRILVQGDFSEYPDDQNMHCTARLADMLSQFSDSLQAKPKEVAEFLMDEIKILDECKCVGLPNFIPRSAFLAILSQHVDGIQDKPVEFINKIWDYIEDVLSSVTAKRSDNFPQIQSSIKRAGRNLISKIKEQSVNRVMEIVEMEKLTDYTCNPEYMTSWTQKTSAQESFIDAVVKNENIPDYFSVTGFGNVKISHLRKYHAHLLIPAFDMKMRITSYWKIVLRRIVDNLALYLQLSVKSLVNTRFQKEIVAEMVDPRDGGGVEKMLEESPLVASKREKLQNSIKLLKESKDAVAAIVDQNC
Putative microtubule-associated force-producing protein, able to bind and hydrolyze GTP.
Q9ZP55
A1VX91
ILVD_CAMJJ
Dihydroxy-acid dehydratase
Campylobacter
MRSDAIKKGHLKAPNRSLLRACGLKDEDFDKPFIGVANSYIDIIPGHYFLNDYAKIIKDEIRKNGCVPFEFNTIGVDDGIAMGHEGMLYSLPSREIIANSIETVMNAHQLDALICIPNCDKITPGMLMGALRVNVPTIFVSGGPMASGVTKKGEKISLSSVFEAVGAYEAKKISEEEFKDIECSACPSGGSCSGMFTANSMNTLCEAMGIALEGNGTILALSKEREELLRKAARRICEIALDERFKIRNIITQKAVRNAMVVDMAMGGSSNTVLHMLAISREAGVALDIKDLNFISSKVAHIAKIAPSLNSVYMDDIHKAGGVSAVMAEISSRQGHILELDALTITGESLEERLKNAKIKDENIIRKVDNAYSKVGGLAILFGNLAEQGCVIKTAGIIGERKFKGEAVCFNSQDEAIKGIIKGKVKKGNVCVIRYEGPKGGPGMQEMLSPTSLLMGMGLGADVALITDGRFSGATRGLSVGHISPEAAEGGLIGLLKDGDEIEIDVDAYTIHANLSEEEITQRKKEFVLPQKEVPSRWLRMYQKLVSNASKGAVLDME
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.
A1VX91
Q1LLX0
RS18_CUPMC
30S ribosomal protein S18
Cupriavidus
MAFVKRDNKNKKRFQQQNPLFKRKRFCRFTVAGVEQIDYKDLDTLKDFIGDNGKITPARLTGTKAHYQRQLDTAIKRARFLALMPYTDLHKN
Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit.
Q1LLX0
P01877
IGHA2_HUMAN
Ig alpha-2 chain C region LAN
Homo
ASPTSPKVFPLSLDSTPQDGNVVVACLVQGFFPQEPLSVTWSESGQNVTARNFPPSQDASGDLYTTSSQLTLPATQCPDGKSVTCHVKHYTNSSQDVTVPCRVPPPPPCCHPRLSLHRPALEDLLLGSEANLTCTLTGLRDASGATFTWTPSSGKSAVQGPPERDLCGCYSVSSVLPGCAQPWNHGETFTCTAAHPELKTPLTANITKSGNTFRPEVHLLPPPSEELALNELVTLTCLARGFSPKDVLVRWLQGSQELPREKYLTWASRQEPSQGTTTYAVTSILRVAAEDWKKGETFSCMVGHEALPLAFTQKTIDRMAGKPTHINVSVVMAEADGTCY
Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens . The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen . Ig alpha is the major immunoglobulin class in body secretions .
P01877
Q1I2W1
XPT_PSEE4
Xanthine phosphoribosyltransferase
Pseudomonas
MEALQQKIREEGIVLSDQVLKVDAFLNHQIDPALMQLIGDEFARLFADSGVTKIVTIEASGIAPAVMTGLKLGVPVIFARKHQSLTLTENLLTASVYSFTKQTENTVAISPRHLNSSDRVLVIDDFLANGKASQALISIIKQAGATVAGLGIVIEKSFQGGRAELDSQGYRVESLARVKSLEGGVVTFIE
Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis.
Q1I2W1
A1KWK2
SSTT_NEIMF
Na(+)/serine-threonine symporter
Neisseria
MAFGKSLFHAIGRVSLVRQIAAGLALGIVIGSVSPQLGLAAGLFGSLFVGALKAVAPVLVFILVAATIAQHQKGNKAHIRPIIVLYLIGTFSAALTAVIAGMVFPTHIVLAGAGDVSAAPPSGIVEVLKSLLMNLVANPINAIANANYIGILAWALVLGAALRNHGSDVTRQVVADLAEAVSTVVKWIIRFAPLGIFGLVSSTIAETGFGALAGYAKLLAVLLGCMAFIALVVNPAIVWWKIRRNPYPLVFTCLRESGVYAFFTRSSAANIPVNMALAKKLGLHEDTYSISIPLGATVNMGGAAITITVLAMAAAYTQGIQVDFATALLLSLVATVSACGASGVAGGSLLLIPLACSLFGISNDVAMQVVAVGFIIGVIQDSAETALNSSTDVLFTAAADLGRQRNRAE
Involved in the import of serine and threonine into the cell, with the concomitant import of sodium (symport system).
A1KWK2
A0KMH0
LPLA_AERHH
Lipoate--protein ligase
Aeromonas
MSRLRLLLSDSHDPLFNLAVEECIFRQMDPNQRVLFLWRNANTVVIGRAQNPWKECNTRRMEEDGVTLARRSSGGGAVFHDLGNSCFTFMAGKPEYDKSVSTAIVLDALTRLGVEAFASGRNDLLVATPDGERKVSGSAYRETHDRGFHHGTLLLDADLGRLANYLNPDPKKLAAKGISSVRSRVANLCELLPGIDHPQVSEALQEAFFSHYGERVQPEHISPEQMPDLPGFAETFARQRSWEWNFGHAPAFSHQLDERFGWGGVELHFDVEKGVIGRAQIFSDSLDPAPLDALAARLPGTAYRADALYDLLRQWRSEFAAREAELEELSRWLLAALR
Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes.
A0KMH0
Q1GSA0
NDK_SPHAL
Nucleoside-2-P kinase
Sphingopyxis
MAVTRTFSIIKPDATRRNLTGAVTKMLEDAGLRVVASKRIHMTREQAEGFYAVHKERPFFGELVEFMISGPVVVQVLEGEDAVKRNRDVMGATNPADAAEGTIRKTFAESIEANSVHGSDSDENAATEIAYFFKPEEIVG
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Q1GSA0
Q9RVP2
CATNT_DEIRA
CC-adding enzyme
Deinococcus
MATPDGEQVWAQLQPQDRAWLNDLSRRAGPDTELALVGGAVRDALLGQTPLDLDIVVAGQDGQGVEALALASGLPFVFHPAFENATLTLPDGRGADLVRARREHYPQPGRNPEPLPGTLHDDLRRRDFGLNALALRLREDGAPELLDVVGGLRDLERRELRPLHDRSLHEDASRLVRAARLAARLELHPAPELLAQVPDALALADDTPRLWAELKLLLAEPRPGQAARVLDGWGAGTLLPGLPLLEALDVQQNAGTPVQPGTYAAAVLSAAPDAAALAERMALGERPAALLARALSDSYFAPGTPELQLRGLLRPESYLPLTGREVVALGVAPGPAVGRALAHLAGLRQSGAVRSADEERTALRAYLGANPKAT
tRNA nucleotidyltransferase involved in the synthesis of the tRNA CCA terminus. Adds the two cytidine residues to tRNA.
Q9RVP2
Q382H9
COQ4_TRYB2
Coenzyme Q biosynthesis protein 4 homolog
Trypanosoma
MQSRVVSSAVMFLGGIAGAVKSLPAFVTSSFGAIVDPEDGRGSAAFAEITALTALHHMQRLMMADEMGRSILKERPQVTDETLEFAKTQPEGTFGYRYAAFMKRNNFLPSGRAPILHVSDPTLAYVMLRYRQIHDFVHAYVGLGRTIEEELAVKLFEWQHTGLPVGLMAVLGGMPWLRMDQILNMGMYNEWARANAPRQLHGKRFVSCILNVPWEWYLDKPYEQLVDDVGIVPLDAFLKERKSGGLHDS
Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of other COQ polypeptides.
Q382H9
Q72E53
TGT_DESVH
tRNA-guanine transglycosylase
Desulfovibrio
MTTPGTFEIHATDGAARTGCLHTAHGIVRTPIFMPVGTVGSVKAIAPDDLEAIGAEIILGNTYHLYLRPGDELVARRGGLHEFNAWRKPILTDSGGFQVFSLSGLRRIAEEGVEFRSHLDGSKHLFTPEKVVSIQRNLNSDIMMVLDECVPYGADRTYTEKSVGLTTRWAKRCRDAYPKGAAGNLLFGITQGGFFKDLRTRSIGALTDIDFDGFALGGLSVGEPKAEMMDLLYHSAPLLPADKPRYLMGVGTPLDIINGIAAGVDMFDCVLPTRNARNGTLYTSLGKLNIKRREFAEDDGPLDPACSCYTCRTFSRAYLRHLYTAKELLAFRLNSIHNLTYFLDLVRGARAAIAAGRFAEYKRSFEAIYPEEVVA
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Q72E53
Q1LTY2
RPOZ_BAUCH
Transcriptase subunit omega
Candidatus Baumannia
MARITVQDAVEKIGNRFNLVLIAARRARQIQINGKDPLVPEKNDKSTVIALREIEQGLIGNQIID
Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
Q1LTY2
C6DFR6
FMT_PECCP
Methionyl-tRNA formyltransferase
Pectobacterium
MSDSLRIIFAGTPDFAARHLDALLSSGHEVVGVFTQPDRPAGRGNKLTPSPVKVLAEQHNIPIFQPKSLRPAENQAMVQALDADVMVVVAYGLILPQPVLSMPRLGCINVHGSLLPLWRGAAPIQRALWAGDSETGVTIMQMDVGLDTGAMLHKISCPILPQDTSATLYDKLAELGPRGLLETLELLADGSAVAEAQNDALATYAEKLSKEEARLNWQLSAEQLERCIRAFNPWPVSYFTVDEQPVKVWKAEVITTAHSTLPGTILQADKQGIQVATAVGILNIQELQPAGKKVMSAQDLLNSRREWFVPGNTLD
Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
C6DFR6
B4SJS0
ATPG_STRM5
F-ATPase gamma subunit
Stenotrophomonas maltophilia group
MASGREIKTKIKSVQNTRKVTRALEMVSASKIRKAQDRMKTSRPYAQAMKQVIGHLAQASTDYQHPFLVEREQVKRVGFIVISSDRGLAGGLNNNLFRKLLGEAKAWQDKGAEVDMVTIGQKASTFFRRVKVNMVGSVTHIGDVPKLESLIGVIKVMLDAFTEGKIDRVYLVYNRFINTMTQKASFDQLLPLPAAEKQVAHHDWDYLYEPDAATVLEHVMTRYIESLVYQALLENVASEHAARMVAMKSASDNANKLIGDLQLVYNKARQAAITQEISEIVGGAAAV
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.
B4SJS0
A3N2A1
RPIA_ACTP2
Phosphoriboisomerase A
Actinobacillus
MTQQEMKKIAAQAALQFVKPDTIVGVGSGSTVNCFIDALASMKDQIKGAVAASKASEERLRAIGIEVFNANEVSELDVYIDGADEITPQGAMIKGGGAALTREKIVSSLAKKFVCIVDGSKQVDVLGTTFPLPVEVIPMARSYVARQLVALGGSPEYREGVVTDNGNVILDVHNFHIIEPLKMEHTINNIAGVVTNGIFAQRYANVTIVGTPEGAKIIE
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
A3N2A1
A8EZN9
DER_RICCK
GTP-binding protein EngA
belli group
MTKQIIALVGRPNVGKSTLFNRLSIRKKAIVHNLPGVTRDRKYTDGKIGSCEFLLIDTPGLEENPNSMSVRLMEQTTKAILEADLICFMVDCRSGILPDDKLLSSFIRKYNKPAILVVNKCEKAFDFDKEYYQLGFDSMVAISAEHGTGLIDLYDEIIAKLPKEKSIETNIADPVKGDCVQIVISGRPNAGKSTFINALINDERLLTGPEAGITRESIEIDWQYKNNHIKLIDTAGLRKKSTITESLDKLSASDAINSIKFANTVILIIDALSPLKQQDLNIASYVANEGRSIVIVVNKWDLVKESEKEAFQEEFYYQINTHLPQIKGVSVLFISAINKQNIEQVLDACLTIYKNWNKKITTSKLNEWLNFTTEAHPLPLQKGGKRVRIKYMTQIKTRPPTFKLFSNNPEKITNSYTRYLVNNMREAFDMPGIPIRFAYVKTKNPYV
GTPase that plays an essential role in the late steps of ribosome biogenesis.
A8EZN9
P29017
CD1C_HUMAN
T-cell surface glycoprotein CD1c
Homo
MLFLQFLLLALLLPGGDNADASQEHVSFHVIQIFSFVNQSWARGQGSGWLDELQTHGWDSESGTIIFLHNWSKGNFSNEELSDLELLFRFYLFGLTREIQDHASQDYSKYPFEVQVKAGCELHSGKSPEGFFQVAFNGLDLLSFQNTTWVPSPGCGSLAQSVCHLLNHQYEGVTETVYNLIRSTCPRFLLGLLDAGKMYVHRQVRPEAWLSSRPSLGSGQLLLVCHASGFYPKPVWVTWMRNEQEQLGTKHGDILPNADGTWYLQVILEVASEEPAGLSCRVRHSSLGGQDIILYWGHHFSMNWIALVVIVPLVILIVLVLWFKKHCSYQDIL
Antigen-presenting protein that binds self and non-self lipid and glycolipid antigens and presents them to T-cell receptors on natural killer T-cells.
P29017
Q5L686
RUVB_CHLAB
Holliday junction ATP-dependent DNA helicase RuvB
Chlamydia
MTHQVSVLHQDKKFDVSLRPKGLKEFCGQAQLTERLELFLNAAIQRGEVPGHCLFFGPPGLGKTSLAHIVANTVGKGLLVASGPQLVKPSDLLGLLTSLQEGDVFFIDEIHRMGKVAEEYLYSAMEDYKIDITIDSGPGARSVSVDLAPFSLVGATTRSGMLSEPLRARFSFTGRVAYYSDEDLATILRRSSNLLGIDADASALYEIARRSRGTPRLANNLLRWVRDFAQMREGNCINSDVAEKALAMLLIDEWGLNEIDIKLLTTIMNYYQGGPVGIKTLSVAVGEDVRTLEDVYEPFLILKGLLKKTSRGRMVTQLAYNHLKRCSDNLQSLGEEK
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.
Q5L686
Q5U203
UBE2F_RAT
Ubiquitin-conjugating enzyme E2 F
Rattus
MLTLASKLKRDDGLKGSRASASTSDSTRRVSVRDKLLVKEVAELEANLPCTCKVHFPDPNKLHCFQLTVSPDEGYYQGGKFQFETEVPDAYNMVPPKVKCLTKIWHPNITETGEICLSLLREHSIDGTGWAPTRTLKDVVWGLNSLFTDLLNFDDPLNIEAAEHHLRDKEDFRDKVDEYIKRYAR
Accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX2, but not RBX1, suggests that the RBX2-UBE2F complex neddylates specific target proteins, such as CUL5.
Q5U203
Q9FIL1
BSK5_ARATH
Brassinosteroid-signaling kinase 5
Arabidopsis
MGPRCSKLSLCWWPTHLKSTHNEASDLDNGTDDLPSFTEFSFDQLRAATCGFSTDSIVSEHGVKAPNVVYKGRLEDDRWIAVKRFNRSAWPDTRQFLEEAKAVGQLRNERLANLIGFCCEGDERLLVAEFMPFETLSKHLFHWDSQPMKWSMRLRVALYLAQALEYCSSKGRALYHDLNAYRILFDQDGNPRLSCFGLMKNSRDGKSYSTNLAFTPPEYLRTGRVIPESVVYSFGTLLLDLLSGKHIPPSHALDLIRGKNFLMLMDSCLDGHFSNDDGTDLVRLASRCLQYEARERPNVKSLVSSLAPLQKETDIPSHVLMGIPHGAASPKETTSLTPLGDACSRHDLTAIHEILEKVGYKDDEGVANELSFQVWTDQIQETLNSKKQGDAAFKGKDFVTAVECYTQFIEDGTMVSPTVFARRCLCYLMSNMPQEALGDAMQAQVVSPEWPTAFYLQAAALFSLGMDKDACETLKDGTSLEAKKHNNRN
Probable serine/threonine kinase that acts as positive regulator of brassinosteroid (BR) signaling downstream of the receptor kinase BRI1 . Involved in abiotic stress tolerance. Required for salt stress and abscisic acid-mediated drought stress tolerance .
Q9FIL1
Q93Z37
BIG1E_ARATH
Protein BIG GRAIN 1-like E
Arabidopsis
MSMKGISSAESDKLSRRISLTHKRNSEELDVFEAAVYFGYNEASSGDHGHTQKYGYNAAREENPRRWGILGGGRRISLDLPIRCSEQVYHLQQDHHEKHEVTTIKERLGNVRHKQPSSPGGKIASFLNSLFHQAGSKKNKSKSKSKTKPTDPEVEEEIPGGGWMRRRRRSSISHFFSSSRSTSTTTTTTASSSSKSLISSSSSGFRTPPPYLNTPTKNYKQFLNYTSATKQVGEEETKTNKEYSWLDEKLKVMESLSENQRIWSDDEDIDDDRRIKREGEDDGMESDSSSDLFELQNYELSRGGLPVYETTNVANINKTHI
Involved in auxin transport. Regulator of the auxin signaling pathway.
Q93Z37
Q6F1Z6
DEOC1_MESFL
Phosphodeoxyriboaldolase 1
Mesoplasma
MKLNKYIDHTLLKQDATKAEIKQLCDEAIEFDFATVCVNSYWTSYCKELLKGTNVGITNVVGFPLGACTTATKAFEVSEAIKDGATEIDMVLNIGALKDKNYELVLEDMKAVKKAAGSHVVKCIMENCLLTKEEIMKACEIAVEAGLEFVKTSTGFSKSGATFEDVKLMKSVVKDNALVKAAGGVRTFEDAQKMIEAGADRLGTSGGVAIIKGEENNASY
Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Q6F1Z6
D3ZFB6
PRRT2_RAT
Dispanin subfamily B member 3
Rattus
MAASSSEVSEMKGVEDSSNTHSEGPRHSEEGMGPVQVVAENLDQPEALQSGPDTTAAPVDSGPKAELAPETTETPVETPETVQATDLSVNPGEDSKTCPSPKEACQEPASRPEVNREATAEQGAEQQSAAPPEPTSEQALQLNTQSDPQPTSQPPPKPPLQAEPPTQENPTTEVLTESTGEKQENGAVVPLQAGDGEEGPAPQPHSPPSTKTPPANGAPPRVLQKLVEEDRIGRAHGGHPGSPRGSLSRHPSSQLAGPGVEGGEGTQKPRDYIILAILSCFCPMWPVNIVAFAYAVMSRNSLQQGDVDGAQRLGRVAKLLSIVALVGGVLIIIASCVINLGVYK
As a component of the outer core of AMPAR complex, may be involved in synaptic transmission in the central nervous system. In hippocampal neurons, in presynaptic terminals, plays an important role in the final steps of neurotransmitter release, possibly by regulating Ca(2+)-sensing. In the cerebellum, may inhibit SNARE complex formation and down-regulate short-term facilitation.
D3ZFB6
A0RQU7
EFTS_CAMFF
Elongation factor Ts
Campylobacter
MEISASMVKELRESTGAGMMDCKKALQESNGDMQKAVDILREKGLGKAAKKADRLASEGLVSVVVSENNKTATITEINSETDFVAKNATFVDLVKNTTIHVQTNSINTVEELKESSINGVKFEEYFQSQIATIGENLVVRRFETIKAAKGGIVAGYIHSNSRVGVLIGAACDSEETAAKIHDFLRNLCMHAAAMKPQVISYKEFDADFVEKEYLALKGELEKENEELVRLKKPLHKIPEFASRAQLTDDIIAKATENLKAELKKQGKPEAIWDKILPGQIDRYIADNTQLDQRLTLLGQFYVMDDKKTVEQAIADEAKKVGGKVEIVSYVRFEVGEGLEKKSEDFAAEVAAQMA
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.
A0RQU7
Q99R75
CRTM_STAAM
Dehydrosqualene synthase
Staphylococcus
MTMMDMNFKYCHKIMKKHSKSFSYAFDLLPEDQRKAVWAIYAVCRKIDDSIDVYGDIQFLNQIKEDIQSIEKYPYEHHHFQSDRRIMMALQHVAQHKNIAFQSFYNLIDTVYKDQHFTMFETDAELFGYCYGVAGTVGEVLTPILSDHETHQTYDVARRLGESLQLINILRDVGEDFDNERVYFSKQRLKQYEVDIAEVYQNGVNNHYIDLWEYYAAIAEKDFQDVMDQIKVFSIEAQPIIELAARIYIEILDEVRQANYTLHERVFVDKRKKAKLFHEINSKYHRI
Involved in the biosynthesis of the yellow-orange carotenoid staphyloxanthin, which plays a role in the virulence via its protective function against oxidative stress. Catalyzes the head-to-head condensation of two molecules of farnesyl diphosphate (FPP) into the colorless C(30) carotenoid 4,4'-diapophytoene (dehydrosqualene).
Q99R75
B4EXE3
CH10_PROMH
Chaperonin-10
Proteus
MKIRPLHDRVIVKRKEVEAKSAGGIVLTGSAAGKSTRGEILAVGNGRIMENGEVKPLDVKVGDIVIFNDGYGVKSEKIDNEDVLIMSESDILAIVEA
Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel.
B4EXE3
Q9EPQ7
STAR5_MOUSE
START domain-containing protein 5
Mus
MDPSWATQESEAVAEKVLRYRRDASGWKKCREGNGVSISWRPSEEFPGNLYRGEGILCGTPEEVWDCIKPVASGLREKWDDNVSSFEIVQSITDMLCVSRTSTPSAAMKLISPRDFVDLVLVKKYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFCEPLPGDPNKTNLVTFFQTDLSGYLPQSVVDSFFPRSMAEFYPNLQKAVRKFHH
May be involved in the intracellular transport of sterols or other lipids. May bind cholesterol or other sterols.
Q9EPQ7
P81543
FERA_SULME
Seven-iron ferredoxin
Sulfuracidifex
GIDPNYRTSRPEVGTHEGHKVYGPVENPKVLGIHGAIVGVDFDLCIADGSCINA
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
P81543
B2HED8
G6PI_MYCMM
Phosphohexose isomerase
Mycobacterium
MTSEQSIPDITATPAWEALRKHHDQIGETHLRQIFADDPNRGHDLTVTVGDLYIDYSKHRITRDTISLLVDLARTANLEAHRDQMFAGAHINTSEDRAVLHTALRLPRDAELIVDGRNVVEDVHAVLDAMGDFTDRLRSGEWTGATGKRISTVVNIGIGGSDLGPVMVYQALRHYADAGISARFVSNVDPADLIATLADLDPATTLFIVASKTFSTLETLTNATAARRWLTDALGDAAVSQHFVAVSTNRRLVDDFGINTDNMFGFWDWVGGRYSVDSAIGLSVMAAIGREAFADFLSGFHIVDEHFRTAPLESNAPALLGLIGLWYSNFLGAQSRAVLPYSNDLARFAAYLQQLTMESNGKSTRADGTAVTTDTGEIYWGEPGTNGQHAFYQLLHQGTRLVPADFIGFSQPIDDLPTVEGTGSMHDLLMSNFFAQTQVLAFGKTAEEIAAEGTPAAVVPHKVMPGNRPSTSILANRLTPSVLGQLIALYEHQVFTEGVVWGIDSFDQWGVELGKTQAKALLPVITSDGSPQRQSDSSTDALVRRYRTQRGRTG
Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
B2HED8
A8Z668
RL3_SULMW
50S ribosomal protein L3
Candidatus Sulcia
MSGIIGKNIGMTSMYDESGFNVPCSIIEAGPCIVLQIKTKEKDGYDSCQLGFDEKKYKNTNKPLLFFFKKFKSTPKKKIFELPIKGNIKSGNIIKLNCFHENELVNITGFSKGKGFQGVVKRHGFSGVGERSHGQHNRSRAPGSIGAGSDPSRVFKGTRMAGRMGNKKVTLKNRKILKIDLLNNFLIIKGSVPGAKNSYLIIKKLK
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
A8Z668
A0KGR9
MUTL_AERHH
DNA mismatch repair protein MutL
Aeromonas
MPIRILPPILANQIAAGEVVERPSSVVKELVENSLDAGADRVEIDIDKGGAKLIRIRDNGSGVAKDELVLALSRHATSKVATLDDLEGINSLGFRGEALASISSVSRLTFTSRTAEQSEAWQAQAEGREMSVTIKPAAHPVGTTVEVVDLFFNTPARRKFMRSEKTEFAHIDELVRRIALSRFDVTLILRHNGKVVRQYKAANTVAEQERRLAAVCGSPFMHYALAVESEHSDVRLWGWLATPEGARPQNDLQYTYVNGRMMRDKLINHAIRQAYDELLPADRFAAYVLYIELDPRQVDVNVHPAKHEVRFHQARLIHDFIFQALFTALRQQGAASDEPLAETLVELPVSAPIEYPGQAPRAEWYGAEHNYRAPAREVREGSSTGRAGNYQPPEPPSREAMRGMGSLLTTLPAVQGTPLAEAETAPVAAAVPAKAGAWRALTLVEQAYLLLERDNRLALLSLVRAERLLLRHWLLETWGQGLAAQPLLLPVSFKLPKNLVALVEQQDRLLKRMGLELKSGGRDTMILTRVPALLRQTDLVRLLPELLQLIESGSDSDAGQQAEVLCQWLVEQGISREKVYDFATANRLLTELVADFSDQLANVRMVRPLALASVLAEFADGH
This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex.
A0KGR9
Q9LTH3
U76E1_ARATH
UDP-glycosyltransferase 76E1
Arabidopsis
MEELGVKRRIVLVPVPAQGHVTPIMQLGKALYSKGFSITVVLTQYNRVSSSKDFSDFHFLTIPGSLTESDLKNLGPFKFLFKLNQICEASFKQCIGQLLQEQGNDIACVVYDEYMYFSQAAVKEFQLPSVLFSTTSATAFVCRSVLSRVNAESFLLDMKDPKVSDKEFPGLHPLRYKDLPTSAFGPLESILKVYSETVNIRTASAVIINSTSCLESSSLAWLQKQLQVPVYPIGPLHIAASAPSSLLEEDRSCLEWLNKQKIGSVIYISLGSLALMETKDMLEMAWGLRNSNQPFLWVIRPGSIPGSEWTESLPEEFSRLVSERGYIVKWAPQIEVLRHPAVGGFWSHCGWNSTLESIGEGVPMICRPFTGDQKVNARYLERVWRIGVQLEGELDKGTVERAVERLIMDEEGAEMRKRVINLKEKLQASVKSRGSSFSSLDNFVNSLKMMNFM
Possesses low quercetin 3-O-glucosyltransferase and 7-O-glucosyltransferase activities in vitro.
Q9LTH3
P01900
HA12_MOUSE
H-2 class I histocompatibility antigen, D-D alpha chain
Mus
MGAMAPRTLLLLLAAALGPTQTRAGSHSLRYFVTAVSRPGFGEPRYMEVGYVDNTEFVRFDSDAENPRYEPRARWIEQEGPEYWERETRRAKGNEQSFRVDLRTALRYYNQSAGGSHTLQWMAGCDVESDGRLLRGYWQFAYDGCDYIALNEDLKTWTAADMAAQITRRKWEQAGAAERDRAYLEGECVEWLRRYLKNGNATLLRTDPPKAHVTHHRRPEGDVTLRCWALGFYPADITLTWQLNGEELTQEMELVETRPAGDGTFQKWASVVVPLGKEQKYTCHVEHEGLPEPLTLRWGKEEPPSSTKTNTVIIAVPVVLGAVVILGAVMAFVMKRRRNTGGKGGDYALAPGSQSSDMSLPDCKV
Involved in the presentation of foreign antigens to the immune system.
P01900
O79436
NU4M_RABIT
NADH dehydrogenase subunit 4
Oryctolagus
MLKTIIPTIMLIPTVWWSKPHMIWINATVYSLLISLTTLSLLNQPSDTNLNFSTTFFSDALSTPLLMLTTWLLPLMILASQHHLDKETLTRKKIYISLLISLQVFLVMTFSATEFILFYILFEATLIPTLIIITRWGNQTERLNAGTYFLFYTLMGSLPLLVALIYLQNSMGSLNFLLLQLMNKSITTSWSNSLMWLACMMAFLVKMPLYGLHLWLPKAHVEAPIAGSMVLAAILLKLGGYGMMRITILLSPITDYMAYPFLMLSLWGMIMTSSICLRQTDLKSLIAYSSVSHMALVIVAILIQTPWSFMGATALMIAHGLTSSLLFCLANSNYERIHSRTMLLARGLQTILPLMAAWWLVASLTNLALPPTINLLGELLIIMASFSWSNLTIILMGTNVLITALYSLYMLSTTQRGKFTYHTNNISPTFTRENTLMVLHLAPLLLLSISPKIILGLMF
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
O79436
Q6AX58
PHIPL_XENLA
Phytanoyl-CoA hydroxylase-interacting protein-like
Xenopus
MEVPRLSQHMSTPNSPCEEMIKNLSLENIQLCERDGNKSQDSGIAEMEELPVPHNIKISNITCDSFKISWDMDPKSKDRITHYFVDLNKKENKNSNKFKHKDVPTKLVAKAVPLPMTVRGHWFLSPRTEYTVAVQTASKQVDGDYAVSEWSEIIEFCTADYSKVHLTQLMEKAEAIAGRMLKFSVFYRNQHKEYFDYIREHHGNVMQPSPKDNSGSHGSPISAKLEGIFFSCNTEFNTGKPQQDSPYGRYRVEIPAEKLFNPNTNLYFGDFYCMYTAYHYVILVIAPMGSPGDEFCKQRLPQLSLSDNKFLTCTQEHDGLVFHQAQDVILEVIYTDPVDLSWGNVAEIIGHQLMSLSTADAKKDPSCKTCNISVGR
May play a role in the development of the central system.
Q6AX58
A5FPF7
NADA_DEHMB
Quinolinate synthase
Dehalococcoides
MYRELISHKIAELKKERKAIILAHNYQLGEIQDAADFVGDSLELARKAAKVDAGVIVFCGVHFMAETAAILSPEKIVLAPEPRAGCPMADMISGAELREFKSRHPGLPVVCYVNSTAEVKAESDICCTSANAVKVVESLKSDTVLFVPDQYLGAFVKERTSKKIISWPGYCPSHARIKPEDIVNLKKHYPAARVIVHPESRPEVTALADEVLSTGQMVSYATRADVKELIVGTEIGMLYRLRKENPDKLFIPVSEQAVCANMKMTTLPKLLASLENMQTVVSVPEEIRVKAVGAVERMLRVV
Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
A5FPF7
Q5HAY9
ERA_EHRRW
GTPase Era
Ehrlichia
MNHVGRKCSMSAIVGATNAGKSTLVNVLVGQKVAAVTPKVQTTRVRMHAVSNHENVQLIFIDTPGIFSPKTKLEKFLVKHAWMSLKGIENVIVLVDVKNYLNQHLKKIIDRIKHSNLNAILVLNKIDIVHQSIVSEVIEYMYSLYKFSKAFTISALYGIGIDKLVDYLCETSPYGPWLYNDDQISDAPLKFFMAEITREKLFITLRHELPYSLSVVTELVEEKEDNSLIIKQVIYVTKGSHKTIILGKKGEMVKKISMESKSDLENILQVKVHLFLFVKVREFWQNHLNECVGYAE
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.
Q5HAY9
B0CN39
SFMM3_STRLA
O-methyltransferase SfmM3
Streptomyces
MRRMLYAQLPSRALVVVAQLGIADILAEGPADISTLAERTSTDAVALARLLRGLAVFGVFEEGAEQVYSLTPLGEALTSGHPASALPSATLVAGQFGAAWGDLLETVRTGQSPFERSRGVSLFTHMEQDEELRAVFDDSQGRGLALELDEILRAIDFSAYPTVVDVGGSDGTFLRRILSAHPDISGIVFDLPGSTSLQAERPTADPLEGRYSVATGDFFDSLPEGGDLYLLSHILHDWDDDRAVQILRTCRAAMSDDATLMVVDLIAANRGQRDERLHTAALMDLYMLSLFGGNGGQERTAAQVEVLLSKAGFRITRVDSLPSGMNVIRAVRAA
O-methyltransferase that mediates the methylation of 3-hydroxy-5-methyl-L-tyrosine (3-OH-5-Me-Tyr) into 3-hydroxy-5-methyl-O-methyltyrosine (3-OH-5-Me-OMe-Tyr), a core structure of saframycin A, a potent antitumor antibiotic that belongs to the tetrahydroisoquinoline family.
B0CN39
A7HZ38
DNAJ_PARL1
Chaperone protein DnaJ
Parvibaculum
MSKRDFYDVLGVSRNASADELKKAYRSLAKKYHPDQNQGDKEAEQRFKELNEAYDALKDEQSRAAYDQFGHAAFDGGMGARGGPGGMGGFGAGASMSDIFDDLFGEFMGGRGGRGGRRGDGGQTRGHDLRYNMEISLEEAFEGKKAQVRVPGSVACEVCTGTGAAPGSSPITCPTCQGHGKVRASQGFFTIERTCPTCHGRGQTIDKPCTNCHGAGRVEKERTLSVNIPAGVEDGTRIRLSGEGEAGMRGGPAGDLYIFLSVKPHRLFERDGADLFCRVPIAMVTATLGGEIEVPTLGGKKVKVKVPEGAQTGRQFRLRGKGMPVVNSRETGDLYIQITVETPVNLTKKQKELLKEFEQASTPGNNPESAGFFAKVKEFWDGFQN
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
A7HZ38
B6J1Q3
PANB_COXB2
Ketopantoate hydroxymethyltransferase
Coxiella
MIAMNTPDFQRMKKDNKKISMVTCYDYWSACIISQSNVDCILVGDSLAMVMYGHSTTLPATVEIMAQHIQAVSRGAPNKFIIGDMPFCSYRKDLTTSMNAVERLMQAGAQAIKLEGADAHNLKFIHHVVKSGIPVIGHLGLTPQSIYTLGGFKVQGKEPSAAKKLMADAKALAETGCFAMVLECVPSELAELITHSISIPTIGIGAGPATSGQVLVLQDLLGTNNQFQPKYLKKFLNGFELIKKALDDFDQEVKTSTYPHLETHCY
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
B6J1Q3
P84597
DRS1_PITHY
Dermaseptin-H4
Pithecopus
MDILKKSLFIVLFLGLVSLSICEEEKRENEDEEEQEDDEQSEEKRGLWKSLLKNVGVAAGKAALNAVTDMVNQGEQ
Has antimicrobial activity.
P84597
Q3BER1
DIS_ECHOC
Short ocellatusion precursor Eo10c-10
Echis
MIPVLLVTICLAVFPFQGSSIILESGNINDYEIVYPKKVAVLPTGAMNSAHPCYDPVTCQPKEKEDCESGPCCDNCKFLKEGTICKMARGDNMHDYCNGKTCDCPRNPYKGEHDPMEWPAPAKGSVLM
The short monomeric disintegrin ocellatusin inhibits ADP-induced platelet aggregation (IC(50)=168 nM). Inhibits alpha-5/beta-1 (ITGA5/ITGB1) integrin and induces the expression of a ligand-induced binding site epitope on beta-1 integrin subunit. Has a direct chemotactic stimulus on human neutrophils in vitro.
Q3BER1
Q86QV5
KGX32_CENEL
Ergtoxin-like protein
Centruroides
DRDSCVDKSRCAKYGYYQQCEICCKKAGHRGGTCEFFKCKCKV
Blocks Kv11/ERG potassium channels.
Q86QV5
B0KMD1
MDH_PSEPG
Malate dehydrogenase
Pseudomonas
MNKLTIVGAGLVGEAAAQIIARDELCRELVLMDVQGELAQGKALDVWQAAVESGSDTRVYGGAKAEMLDGSDLVVITAGVPRKPGQSRQDVLSINLPILDGIMTDIKHHAPAATVLVVSNPVDVLTYRAWSVSGLGRDKVFGQAGVLDTARMKCFIAEQTGFSAKDITALVLGGHGDSMVPLMRYCQIGSVPLSHFLSSEQIEQIVERTRKGGGEILGLKKMGSACDAPGVAIAQMVDAIANGRNRILPAVAILQGEYGRKDIAMGVPCVLADEGLARVIELPLDAQEQAMFDQSADQVARDIDEMKAL
Catalyzes the reversible oxidation of malate to oxaloacetate.
B0KMD1
P39604
RODA_BACSU
Rod shape-determining protein
Bacillus
MSRYKKQQSPFYQGDLIFIFGVFFIISVVSIYAAGQFGQYGNTDWIQQIVFYLLGAVAITVLLYFDLEQLEKLSLYIFIIGILSLIILKISPESIAPVIKGAKSWFRIGRITIQPSEFMKVGLIMMLASVIGKANPKGVRTLRDDIHLLLKIAGVAVIPVGLILMQDAGTAGICMFIVLVMVFMSGINWKLIAIIAGSGILLISLILLVMINFPDVAKSVGIQDYQIKRVTSWVSASNETQEDSNDSWQVDQAIMAIGSGGILGNGISNLKVYVPESTTDFIFSIIGESFGFIGCAIVVIMFFFLIYRLVVLIDKIHPFNRFASFFCVGYTALIVIHTFQNIGMNIGIMPVTGIPLLFVSYGGSSTLSTLIGFGIVYNASVQLTKYRSYLFNS
Peptidoglycan polymerase that is essential for cell wall elongation . Also required for the maintenance of the rod cell shape .
P39604
Q6ENF3
PSAJ_ORYNI
PSI-J
Oryza
MRDIKTYLSVAPVLSTLWFGALAGLLIEINRLFPDALSFPFFSF
May help in the organization of the PsaE and PsaF subunits.
Q6ENF3
B3QL69
DCUP_CHLP8
Uroporphyrinogen decarboxylase
Chlorobaculum
MLKNDLFLRALKRQSTPRTPIWVMRQAGRYLPEYRAVREKTDFLTLCKTPELACEVTIQPVDLMGVDAAIIFSDILVVNEAMGMDVQIIESKGIKLTPEIRSQADIDKLIDPDVEEKLGYVFDAIRLTKKELNDRVPLIGFSGAAWTLFTYAVEGGGSKNYANAKKMMYREPQMAHQLLQKITTCISNYLIKQVEAGADAIQIFDSWASALSEDDYREFALPYIKQNVAAVKAAYPEVPVIVFAKDMNTILSDVADTGADAVGLGWNIDIAKARKELNDRVCLQGNMDPTVLYGTPEKIKSEAAKILKQFGQHTDCSGHVFNLGHGILPDVDPANLKCLVEFVKEESAKYH
Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
B3QL69
Q2RK09
RSGA_MOOTA
Small ribosomal subunit biogenesis GTPase RsgA
Moorella
MEGTLLRRYGGFYYVESEGRVWTCRLRGRFRLQETVFLPGDRVEIKPVGPGEGVIEDLKPRRTCLKRPAVANVEQVIIVFALREPPPDLELLDRLLFLSGVEDIEAVIVWNKADISKQEYAGLPELYRQIGYRNLITSAHTGQGIDELKALLAGRLSTFAGPSGVGKSSLLNAIQPGLNLRTGEVSSKGGRGRHTTRQAELIRLPDGGWVADTPGFSRLDLPAITREEVAAYFPEMEPLRGRCRYASCLHRKEPGCAVVAAVEAGLIIKHRYEHYLTFLAEVIARERSFS
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit.
Q2RK09
Q5J1T5
CYB_SUSCL
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
Sus
MTNIRKSHPLMKIINNAFIDLPAPSNISSWWNFGSLLGICLIFQILTGLFLAMHYTSDTTTAFSSVTHICRDVNYGWVIRYLHANGASMFFICLFIHVGRGLYYGSYMFLETWNIGVILLFTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTDLVEWIWGGFSVDKATLTRFFAFHFILPFVITALAAVHLLFLHETGSNNPTGISSDMDKIPFHPYYTLKDILGALFMMLILLILVLFSPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVASILILILMPMLHTSKQRSMMFRPLSQCLFWMLVADLITLTWIGGQPVEHPFIIIGQLASILYFLIILVLMPITSIIENNLLKW
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.
Q5J1T5
B4TBB5
PXPA_SALHS
5-oxoprolinase (ATP-hydrolyzing) subunit A
Salmonella
MNIDLNADLGEGCASDSELLTLVSSANIACGFHAGDAQTMLTCVREALKNGVAIGAHPSFPDRDNLGRTAMVLPPETVYAQTLYQIGALGAIVQAQGGVMRHVKPHGMLYNQAAKDPRLAQAIAKAVHDYDPSLILVGLAGSELIRAGERHRLVTRQEVFADRGYQADGSLVPRTQPGALIHDEEQALAQTLDMVQAGRVKSVTGVWTTVTAQTVCIHGDGEYALAFARRLRAAFNARNIHVIA
Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
B4TBB5
Q3T051
RL39_BOVIN
60S ribosomal protein L39
Bos
MSSHKTFRIKRFLAKKQKQNRPIPQWIRMKTGNKIRYNSKRRHWRRTKLGL
RNA-binding component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Q3T051
O24385
CPI7_SOLTU
PCPI-7
Solanum
VLPEVYDQDGEPLRIGERYIIKNPLLGGGAVYLYNIGNLQCPNAVLQHMSIPQFLGKGTPVVFVRKSESDYGDVVRVMTGVYIKFFFKTSKLCVDETVWKVNDEELVVTGGNVGNENDIFKIKKTDLVIRGMKNVYKLLHCRSHLGCKNIGGNFKNGYPRLAAVDDDKDFIPFVFIKA
Inhibitor of cysteine proteases. May protect the plant by inhibiting proteases of invading organisms.
O24385
O30238
Y2433_ARCFU
Putative toxin AF_2433
Archaeoglobus
MRRERYLEKIEYIVEALSEIPERVKTPIEVSGVFYNLLTSIESAMDISAMLVKDLGGRVEDDYSNVEMLKELGIIDEELAEGLKKCNGLRNWLVHRYNRVDKELVLSSVEEVKALLLKFIQRVEDVLEKIEP
Probable toxic component of a putative type VII toxin-antitoxin (TA) system, probably an RNase. Probably neutralized by cognate antitoxin AF_2432. Neutralization may be due to AMPylation by AF_2432.
O30238
Q3IYY8
TTCA_CERS4
tRNA 2-thiocytidine biosynthesis protein TtcA
Cereibacter
MFDDQDEIHPLLAGAPQTTEFRKLRKRIVREVREAIETYGMVERGARWLVCLSGGKDSYTLLAVLHELKWRGLLPVDLLACNLDQGQPGFPATVLPEFLSRMGVPHRIEYQDTYSIVMDKIPQGRTYCALCSRLRRGNLYRIAREEGCSAVVLGHHRDDILETFFMNLFHGGRLATMPPKLVNEDGDLFVYRPLAFVAEADCEKFARDMAYPIIPCDLCGSQEGLQRQQVKQILDGWEARSPGRRQVMFRALMNARPSHLLDPGLFDFLGLATAPRASEERQDEPPHLRGEA
Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system.
Q3IYY8
P06632
DKGA_CORSC
AKR5C
unclassified Corynebacterium
MTVPSIVLNDGNSIPQLGYGVFKVPPADTQRAVEEALEVGYRHIDTAAIYGNEEGVGAAIAASGIARDDLFITTKLWNDRHDGDEPAAAIAESLAKLALDQVDLYLVHWPTPAADNYVHAWEKMIELRAAGLTRSIGVSNHLVPHLERIVAATGVVPAVNQIELHPAYQQREITDWAAAHDVKIESWGPLGQGKYDLFGAEPVTAAAAAHGKTPAQAVLRWHLQKGFVVFPKSVRRERLEENLDVFDFDLTDTEIAAIDAMDPGDGSGRVSAHPDEVD
Catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates. 25DKGR-A exhibits a greater selectivity for the substrate and higher thermal stability than 25DKGR-B.
P06632
Q796Y8
BCP_BACSU
Thioredoxin-dependent peroxiredoxin Bcp
Bacillus
MTIEIGQKAPDLELKGDHGETVKLSDYKGKYIVLYFYPKDMTPGCTTEACDFRDSHESFAELDAVIIGVSPDSQEKHGKFKEKHNLPFLLLVDDEHKLAEAFDVWKLKKNFGKEYMGIERSTFLIDKEGRLIKEWRKVKVKDHVAEALQTLKDMSEK
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events.
Q796Y8
Q3ZW88
NADD_DEHMC
Nicotinate mononucleotide adenylyltransferase
Dehalococcoides
MVSLKTGILGGTFDPIHTGHLILADEVKNRLGLDEVIFIPTGQPYYKADKTISPAEDRLNMVKLAISDKPYFRVMDIEIKRSGPTYTADTLNDLKTILPEKTELYFMLGWDNLEALPRWHKASEIIRLCRLVAAPRIGQVKPDVDELDDKLPGLQQSLILLSKPEVDISSSLVRERVENGQGVEHLVPAAVASYIKEHNLYCRK
Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Q3ZW88
O19084
CDSN_PIG
S protein
Sus
GKPCPPITSVDKFGSYEVVGGSSDSYLVPGMTYSGGKIYPVGYFTKDNPVKGSPGAPSFAAGPPISEGKYFSSNPIIPSHSSSSSNIYQSGASSAIVFQPVGSGGVQPCGVGSSGSKGPCSLSGSGVHSSSSISSSSGSSFHPCGTVSQGPCSPPGTGSFSGSSSSKSGGKIILQPCGSKSSSSGHPCISVSSSTLSGGPDGSPQPDPSAGAKPCGSGSSGKIPC
Important for the epidermal barrier integrity.
O19084
B4RS82
ATPG_ALTMD
F-ATPase gamma subunit
Alteromonas
MASGKEIKGKIGSIKNTQKITSAMEMVAASKMKKAQERMASGRPYAQNMLKVIGHIANGNLEYRHPYLEEREVKRVGYIVISTDRGLCGGLNTNEFKLVTQDVKKWREQGVEVDFAALGSKACSFFNRFGGKLLAAESGLGDKPSVSDVVGVVRVMLKAYDEGQIDRVFLVFNDFVNTMTQKPVINQLLPLPKSEDEEYQHRWDYIYEPDPKEILEALMVRYIESQVYQGVVENAASEQAARMVAMKAATDNAGNLIDELQLVYNKARQAAITQEISEIVSGAAAV
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.
B4RS82
A6T3X6
KUP_JANMA
Probable potassium transport system protein kup
Janthinobacterium
MASPDKKSSLAALTLAAVGIVYGDIGTSPLYTMKEVFSKEHGLALTPENLLGVVSLIVWGLIIIVSLKYVTLVLRANNRGEGGIMALMALALSSVTRNSRWYFPLLVMGLFGATLFYGDSVITPAISVLSAIEGLSVATETFDPYVVPLTVAVLVGLYSVQARGTAGIGKWFGPIMVVWFATLAVMGVVNIIDAPEILYALNPWHALHFLDGNRFLAFIALGAVVLAFTGAEALYADMGHFGAKPIRMAWFLVAFPALALNYLGQGALLLMHPDAVTNPFYQQLGAWSIYPLVALSTMAAIIASQATISGTFSMTKQAIALGFLPRMKIEFTSASQIGQIYIPAVNWLQMAVVVMAVVGFGSSSDLAAAYGIAVTATMLVTTILTFFVIRYRWKYNLLLCLASTGFFLVIDLSLFSANMLKLFHGGWFPLLLGTILFTLMLTWKRGRELVFENLQKHAIPLEDFLASLFISPPTRVPGTAIFLRGESDGVPHAMLHNLSHNKVLHERVVFLTVRMMEVPYVPTTDQVRIHLLGDDCYQMDVTYGFKNVPDIPAALELAKDQGLEFEMMETSFFIARQTVVANPVRGMALWREHIFVAMSRHARGAADYYQIPSNRVIELGTKVEI
Transport of potassium into the cell.
A6T3X6
Q1MN40
RBFA_RHIL3
Ribosome-binding factor A
Rhizobium
MTRPTSSAPSQRMLRIGEQVRAAITQVLQRGEVRDDVIEATVISVSEVRMSPDLKIATAYVTPLGVSDHSIVIEALNRHARFIRGRLGPQLRQMKYMPEVRFRDDTSFDNYKKIDELLRSPEVSRDLDGDNDEQ
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA.
Q1MN40
Q1CUR4
SYP_HELPH
Prolyl-tRNA synthetase
Helicobacter
MLFSKLFAPTLKEPPKDAVLKSHKHLAQAGYIYQVGSGIYNFLPLAKKVLDKIENITHKRMQEHGAQNILMSFVVLASLWEKSGRLDKYGKELLVFKDRKDNDFVLSPTLEENITEIAANFIKSYKQLPVHLYQIHTKFRDEIRPRFGLVRAREFIMKDGYSFHEDAESLDKEFLNTQSAYKEILNDLGLDFRIVEADSGAIGGSKSKEFVVLTECGEDTIVVCKNCDYAANIEIAKRSKRPEPLNVPKAQLAKFPTPNTTSAQSVAEFFKTEPYFVLKALVRKVIHKDKETLACFFVRGDDNLEEVKALNALNIIGANALELREASQKDLDSAGLIAGFIGPYGLKKHVPYIIFDEDLKEGDCLITGANEKDFHAVGVDLKGFENLVYADIVQVKESDHCPNCQGALKYHKSLEVGHIFKLGQGYAKSLRASFLDKNGKEQFFEMGCYGIGISRLLSAILEQKSDDLGCVWTKNTAPFDVVIVVSNWKDEAQKKLAFEVYERLLQKGVDALLDDRDARFGAKMRDFELIGERLALIIGKQTLENKEFECIKRANLEKQTIKDIELEEKILEMLASE
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
Q1CUR4
Q0C444
PANB_HYPNA
Ketopantoate hydroxymethyltransferase
Hyphomonas
MSKQTQTTRKTVKDIAAAKGATPLVMLTAYDAPTAAILDPHCDILLVGDSLGMVVHGLPSTVGVTMEMMILHGQAVMRGASQAMVVVDMPFGSYETNADQAFLNAVRIMKETGCQAIKIESGAYAAGQIAHLVERGIPVMGHIGLRPQAINVDGGFRAKGRTEDERDRVIAEARAAADAGAFCIVIEGVAEDLAAAITAEVSCPTIGIGASAACDGQVLVTQDMLGLFDWTPKFVRRYADLREVVDKAAAEYAADVRARRFPGTAETYSLRKQGS
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Q0C444
P00018
CYC_DRONO
Cytochrome c
Dromaius
MGDIEKGKKIFVQKCSQCHTVEKGGKHKTGPNLNGLFGRKTGQAEGFSYTDANKNKGITWGEDTLMEYLENPKKYIPGTKMIFAGIKKKSERADLIAYLKDATSK
Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
P00018
Q1EN13
DRS11_PHYSA
Dermaseptin-S11
Phyllomedusa
MAFLKKSLFLVLFLGMVSLSICEEEKRENEDEEEQEDDEQSEEKRALWKTLLKGAGKVFGHVAKQFLGSQGQPES
Antimicrobial peptide with activity against Gram-positive and Gram-negative bacteria, and fungi. Has hemolytic activity.
Q1EN13
Q0SZX2
TUSD_SHIF8
tRNA 2-thiouridine synthesizing protein D
Shigella
MRFAIVVTGPAYGTQQASSAFQFAQALIAEGHKLSSVFFYREGVYNANQLTSPASDEFDLVRGWQQLNAQHGVALNICVAAALRRGIVDETEAGRLGLASSNLQPGFTLSGLGALAEASLTCDRVVQF
Part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. Accepts sulfur from TusA and transfers it in turn to TusE.
Q0SZX2
B0JII8
MEND_MICAN
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
Microcystis
MSIDFRNLNTLWGSILVETLARLGLKIGVVSPGSRSTPLTIALARHPQIEAIPILDERSAAFFALGLAKQLYQPVVLVCTSGTATANFYPAVIEAKESHVPLLILTADRPPELRHAHAGQTIDQVKLYGNYPNWQAEISCPSANIERLRYLRQTIIHAWWRCLDPVPGVVHLNLPFRDPLAPTPDLEINNLEANFDQEAFFSHISRQNIAINHSILQINSLPSKGIIIAGLASPQNPESYCQAIADLARSQQYPILAEALSPLRNYAGLNPHLITTYDLLLRNPALRTQLTPDVVLQIGELPTSKELRTWLEEIDCPRWIIDPHPDNYDPLQGKTGHLRVNIEQLGDLFPDKTDNNREYRQLWQKFDQQARLTIDRLLAAETKLIEGKIPWLLSQYLPPRTPIFISNSMPVRYAEFFNPPSDRQIRPYFNRGANGIDGNLSTAIGIAYKNVPSLLLTGDLALLHDTNGFLIKKYFVGSLTIILINNKGGGIFQMLPIAKFDPPFEEFFATPQNIDFCQLCRTYGIDYHLISDWTDFEQKIAVLPESGIRLLEISCDRAFNTQWFLSNYV
Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
B0JII8
B1XYF6
RISB_LEPCP
6,7-dimethyl-8-ribityllumazine synthase
Leptothrix
MKNADRGVAAELDGSDLRVAIVQARFNAAITEQLASSCIAELEALGVLAKHIKHVTVPGALEVALALQALAEQKDHDALIALGCIIRGETYHFELVANESGAAVTRVSLEHGVPIANAILTVENEAQAWARADEKGRDAARVAVEMANLMEDLS
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
B1XYF6
Q1QTQ8
ASTB_CHRSD
N-succinylarginine dihydrolase
Chromohalobacter
MSQDVREVNFDGLVGPTHNYAGLAHGNVASMRHGGLTANPREAALQGLAKMKSLMEAGFAQGVLPPQQRPDLGALRDLGFTGDDAGVLAQAARQAPQLLRAVCSASSMWTANAATVTPSLDAPDGRVHFTAANLQSSFHRYLEPRTTARVLAAMFHDPAHFAHHPVLPATPTFSDEGAANHTRLCGDHDEPGVHLYVYGRQAFGGEHGPKRYPARQTLEASQAIARQHGLDDTRTVFAQQHPDAIDAGVFHNDVIAVGNGPVLLYHEMAFRDETATLEALRARMSTPLIPVRVPSEAISLEDAVATYLFNSQLLSNPDGSMTLVVPGECQENETVWRTIQDLLLGGNNPISEVLVKDVKQSMRNGGGPACLRLRVALAARERQALTGRVLLDEALHDDLAAWVERHYRDRLAPEDLADPLLVRESLTALDELTQLLGIGAVYPFQLN
Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-succinylornithine, ammonia and CO(2).
Q1QTQ8
A8MLF4
RS8_ALKOO
30S ribosomal protein S8
Alkaliphilus
MTMTDPIADMLTRIRNGNMAKHETIDIPASNMKKEIANILLEEGFIKGFDVIEDGKQGIIRMQLKYGKNKEKVITGIKKISKPGLRVYAKKDEIPRVLGGLGIAIISTSRGIITDKVARKEGVGGEVIAYIW
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.
A8MLF4
Q7VDW9
OBG_PROMA
GTP-binding protein Obg
Prochlorococcus
MQFIDQARITVKAGRGGDGIVAFRREKYVPAGGPSGGDGGNGGNVVFQADSNLQTLLDFKFKQIILAENGRRGGPNKCTGASGNNIVLKVPCGTEVRHLETGIIFGDLTIDGESLVVAFGGIGGLGNAHYLSNRNRAPEKFTEGKDGEEWLLHLELKLLAEVGIIGLPNAGKSTLISVLSSARPKIADYPFTTLIPNLGVVRKPSGDGTVFADIPGLIEGAAEGIGLGHEFLRHIERTRLLIHLVDASALNPLEDIEIVENELSAYGHSLIDRPRILVLNKKELLDAKNLKKLERKLNQGSISEVISISAIMSNGLDILLNKIWSKLEI
An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
Q7VDW9
B0JYW5
ANM6_XENTR
Histone-arginine N-methyltransferase PRMT6
Silurana
MAMLKKRKHERTEQDCEYFQCYSDVSVHEEMIADTVRTNAYKLALLRNHSSLQGKTVLDVGAGTGILSVFSVQAGAQAVYAVEASSMSQLACQVVKSNDMENKVKVLNSSVESAEIPEQVDAIVSEWMGYALMYESMLPSVIYARDKWLKPGGLILPSCADLFIAPVNDLIVESRLDFWSEVKGMYGVDMSCMQSFARSCIMNKEMAVNLVSPEDVLSFPVRFASLDLNVCTQEEVRNLHGSFQFSCFGSSLLHGFAVWFSVTFPGENSVTLSTSPYGEETHWKQTLLYLDEEVQVEQDTEITGDVTLSPSDINPRHLRVLLNYSIGGGLRRTKQFQMGS
Arginine methyltransferase that can catalyze the formation of both omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA), with a strong preference for the formation of aDMA. Preferentially methylates arginyl residues present in a glycine and arginine-rich domain and displays preference for monomethylated substrates. Specifically mediates the asymmetric dimethylation of histone H3 'Arg-2' to form H3R2me2a. H3R2me2a represents a specific tag for epigenetic transcriptional repression and is mutually exclusive with methylation on histone H3 'Lys-4' (H3K4me2 and H3K4me3). Acts as a transcriptional repressor of various genes such as HOXA2, THBS1 and TP53. Repression of TP53 blocks cellular senescence. Also methylates histone H2A and H4 'Arg-3' (H2AR3me and H4R3me, respectively). Acts as a regulator of DNA base excision during DNA repair by mediating the methylation of DNA polymerase beta (POLB), leading to the stimulation of its polymerase activity by enhancing DNA binding and processivity. Methylates HMGA1. Regulates alternative splicing events. Acts as a transcriptional coactivator of a number of steroid hormone receptors including ESR1, ESR2, PGR and NR3C1.
B0JYW5
O28294
ILVC_ARCFU
Ketol-acid reductoisomerase type I
Archaeoglobus
MAKIYRDADADLKYLDGKTVCIIGYGSQGHAHALNLKDSGVNVVVGLPEWDKATWERAEKDGMVVKKLSEAADGADVIAMLIPDMVQPAVYREHIQDKLKEGAMLMFAHGFNIHYNQIVPPEYVDVAMVAPKGPGPLVRRMYVEGKGVPSLVAVEQNYTGKALEVALAYAKGIGATRAGVIETTFKEETETDLFGEQVDLCGGVAEMIKMSFETLVEAGYQPEIAYFEVLHELKLIVDLIYEGGIYNMWSAVSETAKYGGMTRGKRIFTEQTREEMRKILKEIQTGEFAREWILENMAGRPVYNKLLQMEREHPIEKIGKELRAMMPWLKKD
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 or NADH to yield (R)-2,3-dihydroxy-isovalerate. It is able to use both NADPH and NADH, but has a preference for NADH.
O28294
Q96C57
CSTOS_HUMAN
Protein CUSTOS
Homo
MAAPSGTVSDSESSNSSSDAEELERCREAAMPAWGLEQRPHVAGKPRAGAANSQLSTSQPSLRHKVNEHEQDGNELQTTPEFRAHVAKKLGALLDSFITISEAAKEPAKAKVQKVALEDDGFRLFFTSVPGGREKEESPQPRRKRQPSSSSEDSDEEWRRCREAAVSASDILQESAIHSPGTVEKEAKKKRKLKKKAKKVASVDSAVAATTPTSMATVQKQKSGELNGDQVSLGTKKKKKAKKASETSPFPPAKSATAIPAN
Plays a role in the regulation of Wnt signaling pathway during early development.
Q96C57
P31382
PMT2_YEAST
Dolichyl-phosphate-mannose--protein mannosyltransferase 2
Saccharomyces
MSSSSSTGYSKNNAAHIKQENTLRQRESSSISVSEELSSADERDAEDFSKEKPAAQSSLLRLESVVMPVIFTALALFTRMYKIGINNHVVWDEAHFGKFGSYYLRHEFYHDVHPPLGKMLVGLSGYLAGYNGSWDFPSGEIYPDYLDYVKMRLFNASFSALCVPLAYFTAKAIGFSLPTVWLMTVLVLFENSYSTLGRFILLDSMLLFFTVASFFSFVMFHNQRSKPFSRKWWKWLLITGISLGCTISVKMVGLFIITMVGIYTVIDLWTFLADKSMSWKTYINHWLARIFGLIIVPFCIFLLCFKIHFDLLSHSGTGDANMPSLFQARLVGSDVGQGPRDIALGSSVVSIKNQALGGSLLHSHIQTYPDGSNQQQVTCYGYKDANNEWFFNRERGLPSWSENETDIEYLKPGTSYRLVHKSTGRNLHTHPVAAPVSKTQWEVSGYGDNVVGDNKDNWVIEIMDQRGDEDPEKLHTLTTSFRIKNLEMGCYLAQTGNSLPEWGFRQQEVVCMKNPFKRDKRTWWNIETHENERLPPRPEDFQYPKTNFLKDFIHLNLAMMATNNALVPDPDKFDYLASSAWQWPTLNVGLRLCGWGDDNPKYFLLGTPASTWASSVAVLAFMATVVILLIRWQRQYVDLRNPSNWNVFLMGGFYPLLAWGLHYMPFVIMSRVTYVHHYLPALYFALIILAYCFDAGLQKWSRSKCGRIMRFVLYAGFMALVIGCFWYFSPISFGMEGPSSNFRYLNWFSTWDIADKQEA
Protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Forms a heterodimeric complex with PMT2 and more rarely with PMT5 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. The PMT1-PMT2 complex participates in oxidative protein folding, ER-associated protein degradation (ERAD), as well as ER export.
P31382
Q9JME2
CHSTB_MOUSE
Chondroitin 4-sulfotransferase 1
Mus
MKPALLEVMRMNRICRMVLATCFGSFILVIFYFQSMLHPVMRRNPFGVDICCRKGSRSPLQELYNPIQLELSNTAILHQMRRDQVTDTCRANSAMSRKRRVLTPNDLKHLVVDEDHELIYCYVPKVACTNWKRLMMVLSGRGKYSDPMEIPANEAHVSANLKTLNQYSIPEINHRLKSYMKFLFVREPFERLVSAYRNKFTQKYNTSFHKRYGTKIIRRQRKNATQEALRKGDDVKFEEFVAYLIDPHTQREEPFNEHWQTVYSLCHPCHIHYDLVGKYETLEEDSNYVLQLAGVSGYLKFPTYAKSTRTTDEMTTEFFQNISAEHQTQLYEVYKLDFLMFNYSVPNYLKLD
Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Can also sulfate Gal residues in desulfated dermatan sulfate. Preferentially sulfates in GlcA->GalNAc unit than in IdoA->GalNAc unit. Does not form 4, 6-di-O-sulfated GalNAc when chondroitin sulfate C is used as an acceptor.
Q9JME2
A0RMM6
EX7L_CAMFF
Exodeoxyribonuclease VII large subunit
Campylobacter
MTVSELNEQAKALLETHFSFVEVTGEISRLIRHSSGHWYFSLKDEKSVISSAMYKFSNQQVKFEVKDGMQVTIYGKLTIYPPSGSYQLLANKMLPVGIGELELAFNQLKSKLENEGLFDIKFKKPLPKFPKKIAIVTSLTSAAYQDMLKVINSRYKLCEFIAFNTLVQGEMAAANIIQMLQKADKMGFDAIVLARGGGSKEDLWCFNDENLARVIFTLKTPIVSAVGHEIDYCISDFVSDHRSLTPTAAMVDLLPDANTILQSLDIAFDKFESFIDGKFQNSFNILNLINQSLKNQAISQKIEKANLTLENKKANLENLITSKINNLAHKIKEFELVFDRQEQFFKATKNMVQIEKNGKIMPLHELQIGDEISIYSQITKKNAIIKS
Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
A0RMM6
P20601
ATPF_PRIM1
F-type ATPase subunit b
Priestia
MAVSNMFVLGAAGINGGDILFQLVMFLILLALLQKFAFGPVMGIMKKREEHIAGEIDEAEKQNEEAKKLVEEQREILKQSRQEVQVMMENARKSAEDKKEEIVAAAREESERLKAAAKQEIEQQKDQAVAALREQVASLSVLIASKVIEKELSEQDQEKLIHEYIQEVGDVR
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
P20601
P44433
RLUC_HAEIN
rRNA-uridine isomerase C
Haemophilus
MTKQNEKIINSSVKMLTISEDESGQRIDNYLLAKLKGVPKSLIYRIVRKGEVRVNKGRIKPEYKLQTGDVVRIPPVRVAEKNDAPISKNLNKVAALENQILFEDDCLIILNKPSGIAVHGGSGLNFGVIEALRALRPEARFLELVHRLDRDTSGILLIAKKRSALRNLHEQLRVKTVQKDYLALVRGQWQSHIKVIQASLLKNELSSGERIVRVSEQGKPSETRFSIEERYINATLVKASPVTGRTHQIRVHTQYAGHPIALDDKYGDKDFDKQMNELGLNRLFLHAFSIRFEHPKNGETLRFNASLDHQMKAILQKLRESK
Responsible for synthesis of pseudouridine from uracil at positions 955, 2504 and 2580 in 23S ribosomal RNA.
P44433
Q03341
ACT2_ECHGR
Actin-2
Echinococcus granulosus group
MADEDTAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNCPAMYVAIQAVLSLYASGRTTGVVLDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDHLVKIMTERGYNFTTTAEREIARDIKEKLCYVALDFEQEMITSTSSAILERSYELPDGQLITIGNERFRCPEALFQPGFLGLEATGIHETTYNSIMKCDVDIRKDLYSNTVLSGGSTMFQGIAERMQREISSLAPTTVKIRIAAPPERKYSVWIGGSILASLSTFQQMWISKVEYEEIGPSIVHRKCF
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Q03341
A4Y2P1
LPXC_SHEPC
UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase
Shewanella
MIFQRTVQKMVKATGVGLHSGNKVTLSIMPAPVNTGIVLVRTDLSPAVAIPAKAEQVRETTMCTALVNDEGIRISTIEHLFAALAGLGIDNAVIEVDAPEIPIMDGSASPFVFLLQSAGIKEQAAPKKYLKIKRPVRVEDGDKWAELKPFKGFRVNFKIDFAHPEIARSQQHVVMDFSTSAFVKEISRARTFGFMRDIEYLRANNLALGGSMENAVVLDEYRVLNPDGLRYEDEFVKHKILDAFGDLYVAGHAILGEFTAYKTGHALNNQLVRALLAQQDAWELVSFEKEADVPVSFSVPSGAVFA
Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.
A4Y2P1
Q8E5X0
THIM_STRA3
4-methyl-5-beta-hydroxyethylthiazole kinase
Streptococcus
MYLEQLKEVNPLTICITNNVVKNFTANGLLALGASPAMSECIEDLEDLLKVANALLINIGTLTKESWQLYQEAIKIANKNQVPVVLDPVAAGASRFRLEVSLDLLKNYSISLLRGNGSEIAALVGEKQASKGADGGKVADLESIAVKANQVFDVPVVVTGETDAIAVRGEVRLLQNGSPLMPLVTGTGCLLGAVLAAFIGSSDRSDDLACLTEAMTVYNVSGEIAEKVAKGKGVGSFQVAFLDALSQMKSEMIMDK
Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
Q8E5X0
P39928
SLN1_YEAST
Tyrosine phosphatase-dependent protein 2
Saccharomyces
MRFGLPSKLELTPPFRIGIRTQLTALVSIVALGSLIILAVTTGVYFTSNYKNLRSDRLYIAAQLKSSQIDQTLNYLYYQAYYLASRDALQSSLTSYVAGNKSADNWVDSLSVIQKFLSSSNLFYVAKVYDSSFNAVLNATNNGTGDLIPEDVLDSLFPLSTDTPLPSSLETIGILTDPVLNSTDYLMSMSLPIFANPSIILTDSRVYGYITIIMSAEGLKSVFNDTTALEHSTIAIISAVYNSQGKASGYHFVFPPYGSRSDLPQKVFSIKNDTFISSAFRNGKGGSLKQTNILSTRNTALGYSPCSFNLVNWVAIVSQPESVFLSPATKLAKIITGTVIAIGVFVILLTLPLAHWAVQPIVRLQKATELITEGRGLRPSTPRTISRASSFKRGFSSGFAVPSSLLQFNTAEAGSTTSVSGHGGSGHGSGAAFSANSSMKSAINLGNEKMSPPEEENKIPNNHTDAKISMDGSLNHDLLGPHSLRHNDTDRSSNRSHILTTSANLTEARLPDYRRLFSDELSDLTETFNTMTDALDQHYALLEERVRARTKQLEAAKIEAEAANEAKTVFIANISHELRTPLNGILGMTAISMEETDVNKIRNSLKLIFRSGELLLHILTELLTFSKNVLQRTKLEKRDFCITDVALQIKSIFGKVAKDQRVRLSISLFPNLIRTMVLWGDSNRIIQIVMNLVSNALKFTPVDGTVDVRMKLLGEYDKELSEKKQYKEVYIKKGTEVTENLETTDKYDLPTLSNHRKSVDLESSATSLGSNRDTSTIQEEITKRNTVANESIYKKVNDREKASNDDVSSIVSTTTSSYDNAIFNSQFNKAPGSDDEEGGNLGRPIENPKTWVISIEVEDTGPGIDPSLQESVFHPFVQGDQTLSRQYGGTGLGLSICRQLANMMHGTMKLESKVGVGSKFTFTLPLNQTKEISFADMEFPFEDEFNPESRKNRRVKFSVAKSIKSRQSTSSVATPATNRSSLTNDVLPEVRSKGKHETKDVGNPNMGREEKNDNGGLEQLQEKNIKPSICLTGAEVNEQNSLSSKHRSRHEGLGSVNLDRPFLQSTGTATSSRNIPTVKDDDKNETSVKILVVEDNHVNQEVIKRMLNLEGIENIELACDGQEAFDKVKELTSKGENYNMIFMDVQMPKVDGLLSTKMIRRDLGYTSPIVALTAFADDSNIKECLESGMNGFLSKPIKRPKLKTILTEFCAAYQGKKNNK
Histidine kinase that acts as an osmosensor at the plasma membrane. Part of the bifurcated SLN1-YPD1-SKN7/SSK1 two-component regulatory system, which controls activity of the HOG1 pathway and gene expression in response to changes in the osmolarity of the extracellular environment. Under normal osmotic conditions, the histidine kinase autophosphorylates His-576. This phosphate is subsequently transferred to Asp-1144, from where it is relayed to 'His-64' of the phosphorelay intermediate protein YPD1. Under high osmolarity conditions, the histidine kinase is no longer active.
P39928
Q2KYL9
GCSH_BORA1
Glycine cleavage system H protein
Bordetella
MSLPTDRKYTTSHEWVKAEGDVFVVGITENAQDQLGDLVFVGDVSVGANLKAGETAGVVESVKAASDIYAPVDGVIVAFNDELEANPNLINESAFTAWIFKIKPLNAADADKLLDAAGYEAVANG
The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
Q2KYL9
P42366
TPX_STRGN
Thioredoxin-dependent peroxiredoxin
Streptococcus
MTTFLGNPVTFTGKQLQVGDTAHDFSLTATDLSKKTLADFAGKKKVLSIIPSIDTGVCSTQTRRFNQELSDLDNTVVITVSVDLPFAQGKWCAAEGIENAVMLSDYFDHSFGRDYAVLINEWHLLARAVLVLDENNTVTYAEYVDNINTEPDYDAAIAAVKNL
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
P42366
B3TN75
PSBB_BRADI
Protein CP-47
Brachypodium
MGLPWYRVHTVVLNDPGRLLAVHIMHTALVSGWAGSMALYELAVFDPSDPVLDPMWRQGMFVIPFMTRLGITDSWGGWSISGGTVTNPGIWSYEGVAGTHIVFSGLCFLAAIWHWVYWDLAIFSDDRTGKPSLDLPKIFGIHLFLAGVACFGFGAFHVTGLYGPGIWVSDPYGLTGKVQAVNPAWGAEGFDPFVPGGIASHHIAAGTLGILAGLFHLSVRPPQRLYKGLRMGNIETVLSSSIAAVFFAAFVVAGTMWYGSATTPIELFGPTRYQWDQGYFQQEIYRRVSNGLSENLSLSEAWSKIPEKLAFYDYIGNNPAKGGLFRAGSMDNGDGIAVGWLGHPVFRDKEGRELFVRRMPTFFETFPVVLVDEEGIVRADVPFRRAESKYSVEQVGVTVEFYGGELNGVSYSDPATVKKYARRSQLGEIFELDRATLKSDGVFRSSPRGWFTFGHATFALLFFFGHIWHGARTLFRDVFAGIDPDLDAQVEFGTFQKVGDPTTRKQAV
One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation.
B3TN75
B0RDN5
RL9_CLAMS
50S ribosomal protein L9
Clavibacter
MSKVILTTEVSGLGSPGDVVEVKNGFSRNYLVPQGFAVIWSRGGEKQIEQIKAARAAREHATIEEAQDLKSRLEAKIVKLTVKAGQGGRLFGSVKTSDIAKAVEESGIGQVDKRKIEIPNPIKGTGNHEATIRLRDDIVATISLQVVAAK
Binds to the 23S rRNA.
B0RDN5
P73002
CBIA_SYNY3
Cobyrinic acid a,c-diamide synthetase
unclassified Synechocystis
MTVIIAGERSGAGKTTITLAMLAYLARQKLRVQSFKVGPDYIDPMFHSQITGRPCRNLDPFLTSEAYVQRCFHYHSQGTPYSLIEGVMGLFDGVPYQGLTDYSSTAHIARLLNLPIVFVMDCQRLSGSVAAIVQGYRHWQPGVNLVGVILNRVGGDRHLELLKIALEPLRIPILGVFFRQQDLTLPDRHLGLVPCGELPQIQQYFDQLAHVAAQQLDWPKLLPLLETPRNLPSPMSLFDVPQKSPQARLAIAQDQAFNFYYADNLDLLTHCGFELIPFSPLEDTELPPAIDGVYLGGGFPELFAEQLSQNQALKDQLKTLIHQGLPTYGECGGLMYLSQSLTNFEGQIFPMLEMLPTAVTMGGKLSLGYRQAQVVNSHSWLWQTESLRGHEFHRSQMTKLPNQALYRQRGLLAIDQNTTDGWCVGSVQASYLHLHWGSQISTVEKFRAACLAFQKKLSYLGKHPPFKSVPLRNTGGDAHGRE
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
P73002
Q3U507
GP174_MOUSE
Probable G-protein coupled receptor 174
Mus
MTDNFTCNKTDGDNTDFRYFIYAVTYTVILVPGLIGNILALWVFYGYMKETKRAVVFMINLAIADLLQILSLPLRIFYYLNHDWPFGPGLCMFCFYLKYVNMYASIYFLVCISVRRFWFLMYPFRFNDCKQKYDLYISIIGWLIICLACLLFPLLRTNDDTPGNRTKCFVDLPIRNVNLAQSVAMITIGEVVGFVTPLMIVLYCTWKTALSLQNKYPISQHLGEKKKALKMILTCAGVFLVCFVPYHFSFPLDFLVKSNEIKSCFARRVILIFHSVALCLASLNSCLDPVIYYFTTNEFRRRLSRQDLPDNIQLHTKSYKIASNHATSTVAAELC
Putative receptor for purines coupled to G-proteins.
Q3U507
Q82ZE1
RSGA_ENTFA
Small ribosomal subunit biogenesis GTPase RsgA
Enterococcus
MVYLKGQIRKALSGFYYVYADGETYQTRARGNFRNRKITPLVGDEVLFESDNLTDGYVLEILPRRNELVRPPVANVDLGVVVMSMVSPNFSFNLLDRFLVSLEYKDIEPVIYLTKVDLLDEPQRQQVTEIKQIYEALGYAVIASEDVEATKELERFFPERLTVFMGQSGAGKSTLLNQISPELQLATAEISQSLGRGKHTTRHVELIPLYDGLVADTPGFSAIDFLEMEAVELPKQFPEFVAAASHCKFRECMHHKEPGCEVKRQVEAGTIATSRYENYLQFLMEIENRRPVYKKKS
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit.
Q82ZE1