accession stringlengths 6 10 | name stringlengths 6 11 | Full Name stringlengths 1 147 ⌀ | taxon stringlengths 3 46 ⌀ | sequence stringlengths 16 2.75k | function stringlengths 6 5.51k | AlphaFoldDB stringlengths 6 10 |
|---|---|---|---|---|---|---|
P40494 | PRK1_YEAST | p53-regulating kinase 1 | Saccharomyces | MNTPQISLYEPGTILTVGSHHAKIIKYLTSGGFAQVYTAEISPPDPYSNANIACLKRVIVPHKQGLNTLRAEVDAMKLLRNNKHVVSYIDSHAARSVNGIAYEVFVLMEFCERGGLIDFMNTRLQNRLQESEILEIMSQTVQGITAMHALQPPLIHRDIKIENVLISHDGLYKVCDFGSVSGVIRPPRNTQEFNYVQHDILTNTTAQYRSPEMIDLYRGLPIDEKSDIWALGVFLYKICYYTTPFEKSGEAGILHARYQYPSFPQYSDRLKNLIRLMLMEAPSQRPNICQVLEEVSRLQNKPCPIRNFYLLRAMNQNANTQLAGEPSSTTYVPTQKFIPVQSLQSINQPPNMMPVTHVSTTPNLGTFPISINDNNKTEVTAHAGLQVGSHSNLTSPLMKTKSVPLSDEFASLYYKELHPFQKSQTFKSVESFQSPQRKSMPPLSLTPVNNDIFDRVSAINRPNNYVDSETQTIDNMAVPNLKLSPTITSKSLSSTKEIAAPDNINGSKIVRSLSSKLKKVITGESRGNSPIKSRQNTGDSIRSAFGKLRHGFTGNSVNNSRSASFDNNNVNGNGNNTNRRLVSSSTSSFPKFNSDTKRKEESDKNQRLEKRRSMPPSILSDFDQHERNNSRTGSRDYYRSHSPVKKTQASAKTTSKPTLIPDNGNVNINQEKKESIQRRVHNLLKSSDDPVTYKSASGYGKYTDIGTETSNRHSSVRITPITEEKFKKTLKDGVLDIKTKSNGKDKSRPPRPPPKPLHLRTEIQKIRNFSRLQSKKLPIERISSEATETIVDVNVDDLEADFRKRFPSKV | Protein kinase involved in the regulation of actin cytoskeleton organization and endocytosis . Phosphorylates PAN1 which disrupts the interaction between PAN1 and END3, and between PAN1 and SLA1 . Phosphorylates SCD5 . Preferentially, phosphorylates substrates on threonine residues in a [L/I/V/M]-x-x-[Q/N/T/S]-x-T-G motif . | P40494 |
P40727 | FLHB_SALTY | Flagellar biosynthetic protein FlhB | Salmonella | MAEESDDDKTEAPTPHRLEKAREEGQIPRSRELTSLLILLVGVCIIWFGGESLARQLAGMLSAGLHFDHRMVNDPNLILGQIILLIKAAMMALLPLIAGVVLVALISPVMLGGLIFSGKSLQPKFSKLNPLPGIKRMFSAQTGAELLKAVLKSTLVGCVTGFYLWHHWPQMMRLMAESPIVAMGNALDLVGLCALLVVLGVIPMVGFDVFFQIFSHLKKLRMSRQDIRDEFKESEGDPHVKGKIRQMQRAAAQRRMMEDVPKADVIVTNPTHYSVALQYDENKMSAPKVVAKGAGLIALRIREIGAEHRVPTLEAPPLARALYRHAEIGQQIPGQLYAAVAEVLAWVWQLKRWRLAGGQRPPQPENLPVPEALDFMNEKNTDG | Required for formation of the rod structure in the basal body of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin. | P40727 |
Q3A6N5 | RL5_SYNC1 | 50S ribosomal protein L5 | Syntrophotalea | MGARLKEVYSTEIAPALVKRLQLKNVMEVPRVEKVVLNMGLGEAIQNIKVLESAVEELTRICGQKPVVTKAKKSIAQFKLREGMPIGCMVTLRRDKAYEFLDRLINVALPRVRDFKGVSKKGFDGRGNYTLGIREQLIFPEIDLEKVDKVKGLNVTIVTTAKNDEEGYALMEAIGMPFPKKAQD | This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs. | Q3A6N5 |
P97051 | NHAA_PSEPU | Nitrile hydratase subunit alpha | Pseudomonas | MGQSHTHDHHHDGYQAPPEDIALRVKALESLLIEKGLVDPAAMDLVVQTYEHKVGPRNGAKVVAKAWVDPAYKARLLADATAAIAELGFSGVQGEDMVILENTPAVHNVFVCTLCSCYPWPTLGLPPAWYKAAAYRSRMVSDPRGVLAEFGLVIPANKEIRVWDTTAELRYMVLPERPGTEAYSEEQLAELVTRDSMIGTGLPTQPTPSH | NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. Industrial production of acrylamide is now being developed using some of the enzymes of this class. | P97051 |
Q9FKG6 | PUB52_ARATH | Serine/threonine-protein kinase | Arabidopsis | MEEKKVVRALSEHLSLPPPPSPSVAVAINGKKKSKYVVFWALEKFIPEGFTDFKLLYVRPPVSYIPTPMGIAVAVSELREDVVSAYKQELDWSANEMLRPYKKMFERRKVQVEVLLLDSLEPAAAIAEEIAGTGVTKLVIGMSLRGFFSRKIDMSSLIATAVPRFCTVYVISKGKLASVRPSESDASGSIRFERSSSTSGSTDSPRLPPEYQDFLSAVSEAQSRVSPFSPALKHSMGSNAVAQMDTSSSGTDQEEVSTGRGMEIVHSGIEGKKNKDESFSASFPMGTEAYNSMSWTSKWRDHEDRREMRSSSSSNNHDLVNMDWGAVVPENYSWVSHTASHMSDGLLSVHSITDNQVNLNFEIEKLRAELKHVQEMYAMAQTETVGASKKLTELNQRRFEESEKLVELKEKEEVAKDTASKEKQRYEEAMKEAEKVKELMMKEALHRREAEFKAERDAREKDKLQASLVSPGVQYQHYTWEEIAAATSDFAENLKIGIGAYGSVYKCNLHHTTGAVKVLHAGETQLSKQFDQELEILSKIRHPHLVLLLGACPERGCLVYEYMDNGSLDDRLMLVNDTPPIPWFERFRIALEVASALVFLHKSKPRPIIHRDLKPGNILLDHNFVSKLGDVGLSTMVNQDDVSSRTIFKQTSPVGTLCYIDPEYQRTGIISPKSDVYSLGVVILQLITAKPAIAITHMVEEAIGDDAEFMAILDKKAGSWPISDTRELAALGLCCTEMRRRDRPDLKDQIIPALERLRKVADKAQNLLSRTPSGPPSHFICPLLKGVMNEPCVAADGYTYDREAIEEWLRQKDTSPVTNLPLPNKNLIANYTLYSAIMEWKSNKR | Functions as an E3 ubiquitin ligase. | Q9FKG6 |
A8LY23 | RPOZ_SALAI | Transcriptase subunit omega | Salinispora | MGTIATNPEGITNPPIDELLEKTTSKYALVIFAAKRARQVNAYYSQLGEGLLEYVGPLVETTPQEKPLSIAMREINGGLLTAEPTDQP | 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. | A8LY23 |
E0SNQ8 | PUS10_IGNAA | tRNA pseudouridine 54/55 synthase | Ignisphaera | MSIIDIANNILRKYCLCDRCLGRLFASLGRGLSNDERGKAIKIALVLELHKRYLDGDKDSLKQLVELSPNIGPIAVNLIKNLGIEIEYTPRTCFICDNKINDIIDTYSQRIADIINERHINSFVLGIRGVTSYIRKEESIANEFKLLYWENIKRELKREIGKKIQMMTNAKVDFLNPEAMIIIDIDRDRIYIESPSLLIYGRYWKLGRMISQNIWLTKNGVKKYPLSIEEIAKMLVKDGFGDDVVLHIAGREDVDVRTLGSGRPFVLEIKRPRKRNIDIKDIENRLNSISRWLKFELNMFVDRDFVSRVKKGCRTSYKIYRAIVVADRDIGIEDIKRLEEFFRDRIIEQRTPTRVLRRKKDVLRRRKVFEIKTRVISPRVFEALIKCEGGLYVKELISGDNGRTVPSFSSVLNANTLCLTLDALYVHEYI | Responsible for synthesis of pseudouridine from uracil-54 and uracil-55 in the psi GC loop of transfer RNAs. | E0SNQ8 |
Q604W0 | DDL_METCA | D-alanylalanine synthetase | Methylococcus | MEKRIQQASKFGKVAVLMGGSAAEREISLKSGKAVLEALRSGGIDAEGIDVGRDLIAPLLERRFDRVFNVIHGRGGEDGVLQGALACLRVPCTGSGVLASALSMDKLRTKLCWTGAGLPTPPWLRLDSPDDLERCRQALGFPVIVKPAEEGSSIGMSRAATAEELAQAWERASGYGCAVFAERWIDGVEYTGGMLKGVPLPLIRLETPHAFYDFDAKYRADTTRYHCPCGLDTGREAELQALVLRACQIVGVSGWGRVDLLVDRSGQPWLIEVNTVPGMTDHSLVPMAAKAAGIDFQELVWHILETSFA | Cell wall formation. | Q604W0 |
Q2ITM9 | SYA_RHOP2 | Alanyl-tRNA synthetase | Rhodopseudomonas | MSGVNDIRSAFLNYFAKNGHDIVPSSPLVPRNDPTLMFTNAGMVQFKNVFTGLEKRPYQRATTSQKCVRAGGKHNDLDNVGYTARHLTFFEMLGNFSFGDYFKERAIELAWNLITKEYGLKKDKLLVTVYHTDDEAASYWKKIAGFSDDRIIRIPTSDNFWAMGDTGPCGPCSEIFIDQGEHIFGGPPGSPEEDGDRFLEFWNLVFMQYEQVTKDERLPLPRPSIDTGMGLERMANILQGVDSVFETDLFRSLIDATSSALGRGPGEEDAASFRVIADHLRSSSFLIADGVLPSNEGRGYVLRRIMRRAMRHAQLLGASEPLMWRLVWALVREMGQAYPELVRAEAMIEETMRLEETRFRKTLDRGLAILDEKSASLKKGDMFDGDTAFTLYDTYGFPLDLTQDALRNRGISVDIASFTDAMDRQRAKARASWAGSGEAATETVWFGLREKLGATEFLGYDTETAEGVVTALVADGKEVDALKAGDSGAIVLNQTPFYAESGGQVGDTGVLSGDGVRFRVTDTLKKAGDLFVHFGTVEEGAIKRDAALQLDVDHARRSSIRANHSATHLLHEALRQVLGDHIAQKGSMVAPDRLRFDFVHQKPITPDELRRVEDIANDIVLENDEVTTRLMAVDDAREAGARALFGEKYGDEVRVVSMGKTARDSGSNALGWSVELCGGTHVKRTGDIGLVSITGESAVASGVRRIEALTGRYARQSANAAINTAKQAAAELRTTVDDMPARIAALMEERKKLERELSDARKKLAMGGGGAAGAADGGADVREVGGVKLMARAVEGIEIKDLKSLVDQGKKQLGSGVIALVATSEDGKGSIVVGVTPDLVARFSAVDLVRTASVVLGGKGGGGKPDMAQAGGPDGSKAQAALDAIAAAIGG | Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | Q2ITM9 |
Q5E6Y8 | EX7S_ALIF1 | Exodeoxyribonuclease VII small subunit | Aliivibrio | MAVKKPENLSFEAAIEELDSVVNQLESGDLPLEDALKKFERGISLARAGQEKLTQAEQRVEILLQADDNAELTPFDGQDD | Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. | Q5E6Y8 |
Q46HL3 | NU1C_PROMT | NDH-A | Prochlorococcus | MNSGIDLEMSFTQGVQNLGLSHELAHLLWIPLPMLLVLVSAVIGVLVTVWLERKISAAAQQRIGPEYAGALGILQPMADGLKLLVKEDIIPARADSVLFTVGPILVLVPVILSWLIVPFGQNLLISNVGIGIFLWIALSSIQPIGLLMSGYSSNNKYSLLGGLRAAAQSISYEIPLALAVLAIVMMSNSLSTVDIVEQQNTAGFLSWNIWRQPVGFIIFWICALAECERLPFDLPEAEEELVAGYQTEYSGMKFALFYLAGYINLVLSALLVSVLYLGGWGFPISIDWFSSFIGLSIDNPLVQIIAASLGIVMTILKAYLLVFLAILLRWTTPRVRIDQLLDLGWKFLLPISLVNLLVTASLKLAFPMTFGG | NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. | Q46HL3 |
K4CEE8 | C7A46_SOLLC | Cytochrome P450 716A46 | Solanum subgen. Lycopersicon | MELFYASLVCLFVLLLSLSFLFLFNKKNKSMILSCPLPPGNSGWPVIGETLEFLSTGWKGHPEKFIFDRISKYKSSIFKTHLLGEKAVVFCGASSNKFLFSNENKLVQTWWPSSVDKVFPSSTQTSSKEEAIKMRKMLPNFLKPEALQRYIRIMDHIAQKHFQSWENQQEVVVFPLAKRYTFWLACRLFVSVEDPNHVARLADPFDVLASGLISIPINLPGTPFNRAIKASNFIRKELVAIIKQRKIDLTEGKASDSQDILSHMLLTSDENGKFMHELDIADKILGLLIGGHDTASSACAFIVKYLAELPEIYDQVYKEQIEIAKSKGPGELLSWEDIKKMKYSWNVACEVLRLAPPLQGAFREALVDFTFNGFSIPKGWKIYWSANSTHINPEVFVDPLKFDPSRFEGNGPAPYTFVPFGGGPRMCPGKEYARLEILVFMHHLVKRFSWKKIIRDEKIVVNPMPIPANGLPIRLYPHHVKT | Catalyzes the carboxylation of beta-amyrin at the C-28 position to form oleanolate . Catalyzes the carboxylation of alpha-amyrin at the C-28 position to form ursolate . | K4CEE8 |
Q47UB2 | RPOZ_COLP3 | Transcriptase subunit omega | Colwellia | MARVTVEDAVDKVGNRFDLVLVASRRARQIATGGKDPLVDVENDKPTVIALREIEAGLITTDIMNTSDRAQQIQQDTAELDAVAAIVGGQQEELS | 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. | Q47UB2 |
Q18CD1 | ISPD_CLOD6 | MEP cytidylyltransferase | Clostridioides | MYSVIIVAAGSGRRMNLDINKQFIKLREKEIIAHTIQVFYENINIDEIVVCIKKEEEDFFKENIINKYNFKNIKIAYGGKERQDSIYNGLKKLDKNCDIVLIHDGARPFVDHRIINESIKVAKEKKAVVVGVPVSDTIKIVSDGTVKETPERNLLWAAQTPQTFEYNLIIDAYEQAYKNNYYGTDDSMLVENIGQSVTMVMGSYENIKITSPEDLNIAEQILNMEKRDEVNSRRRII | Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). | Q18CD1 |
Q2G5S0 | PLSX_NOVAD | Phosphate-acyl-ACP acyltransferase | Novosphingobium | MSLPRIAVDAMGGDEGVRVMVEGAALARRRHDRFKFLLVGDEARIKQALENHPNLRGASEILHAPDIVSGDEKPTQALRRAKTTSMGMAINAVKRGEAGAAVSAGNTGALMAMAKLALRTLPGIDRPALSALLPTLGDNDLVMLDLGANTECDARNLVQFAIMGAAYARIVNGLDAPRVRLLNIGTEETKGTDSLRDAATELKALAGDLALSFDGFTEADKLSRGDVDVVVTDGFSGNIALKSMEGAARFVADLLRRSFSSSLRSKLGFLISRPATELLKHHLDPNNHNGAVFLGLNGIVVKSHGGASALGVANAVAVTARLLEENLTERIKADLARVGAEAIRTSGRSGGKSKSSAAREDGAA | Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA. | Q2G5S0 |
I1S3T9 | XYNC_GIBZE | 1,4-beta-D-xylan xylanohydrolase C | Fusarium | MKFSSLLFTASLVAAMPASIEPRQAQESINKLIKAKGKLYYGTITDPNLLQSQQNNAVIKADFGQVTPENSMKWDATEPQQGKFNFGGGDQVVNFAAQNGLKVRGHALVWHSQLPQWVHNIKDKTQMKNAIENHIKNVAGHFKGKVYAWDVLNEIFDWDGSLRKDSPFTQVLGEEFVGIAFRAARAADPNAKLYINDYSIDDPNAAKLKAGMVAHVKKWVSQGIPIDGIGSQTHLDPGAANGVQAALQQMASTGVKEVAITELDIRSAPAADYATVTKACLNVPKCVGITVWGVSDKDSWRKEKDSLLFNAQYQAKPAYTAVVNALR | Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Plays an important role in causing fusarium head blight (FHB) on cereal crops. | I1S3T9 |
Q8DD21 | RL7_VIBVU | 50S ribosomal protein L7/L12 | Vibrio | MSITNEQILDAIAEMSVTQVVELISAMEEKFGVTAAAAVVAGGAAAGAAVEEQTEFNVILASAGANKVAVIKAVRGATGLGLKEAKALVDGAPAALKEGVEKAEAEALKKELEEAGATVEIK | Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation. | Q8DD21 |
P70313 | NOS3_MOUSE | NOS type III | Mus | MGNLKSVGQEPGPPCGLGLGLGLGLCGKQGPASPAPEPSQAPAPPSPTRPAPDHSPPLTRPPDGPRFPRVKNWEVGSITYDTLSAQAQQDGPCTSRRCLGSLVFPRKLQSRPTQGPSPTEQLLGQARDFINQYYNSIKRSGSQAHEQRLQEVEAEVAATGTYQLRESELVFGAKQAWRNAPRCVGRIQWGKLQVFDARDCRTAQEMFTYICNHIKYATNRGNLRSAITVFPQRCPGRGDFRIWNSQLIRYAGYRQQDGSVRGDPANVEITELCIQHGWTPGNGRFDVLPLLLQAPDEPPELFTLPPEMVLEVPLEHPTLEWFAALGLRWYALPAVSNMLLEIGGLEFPAAPFSGWYMSSEIGMRDLCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDHHAATASFMKHLENEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQPDPWKGSAAKGAGITRKKTFKEVANAVKISASLMGTVMAKRVKATILYGSETGRAQSYAQQLGRLFRKAFDPRVLCMDEYDVVSLEHEALVLVVTSTFGNGDPPENGESFAAALMEMSGPYNSSPRPEQHKSYKIRFNSVSCSDPLVSSWRRKRKESSNTDSAGALGTLRFCVFGLGSRAYPHFCAFARAVDTRLEELGGERLLQLGQGDELCGQEEAFRGWAQAAFQAACETFCVGEDAKAAARDIFSPKRSWKRQRYRLSTQAESLQLLPGLTHVHRRKMFQATILSVENLQSSKSTRATILVRLDTGGQEGLQYQPGDHIGVCPPNRPGLVEALLSRVEDPPPSTEPVAVEQLEKGSPGGPPPGWVRDPRLPPCTLRQALTYFLDITSPPSPRLLRLLSTLAEESSEQQELEALSQDPRRYEEWKWFSCPTLLEVLEQFPSVALPAPLILTQLPLLQPRYYSVSSAPSAHPGEIHLTIAVLAYRTQDGLGPLHYGVCSTWMSQLKAGDPVPCFIRGAPSFRLPPDPNLPCILVGPGTGIAPFRGFWQDRLHDIEIKGLQPAPMTLVFGCRCSQLDHLYRDEVLDAQQRGVFGQVLTAFSRDPGSPKTYVQDLLRTELAAEVHRVLCLEQGHMFVCGDVTMATSVLQTVQRILATEGGMELDEAGDVIGVLRDQQRYHEDIFGLTLRTQEVTSRIRTQSFSLQERQLRGAVPWSFDPPGPEIPGS | Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets. May play a significant role in normal and abnormal limb development. | P70313 |
A9I0G7 | PYRE_BORPD | Orotate phosphoribosyltransferase | Bordetella | MAAASATSTDFVRFALDEGVLRFGSFKVKSGRTSPYFFNAGLFNSGASVGRLAQFYAQALVDSGIAFDMLFGPAYKGIPLATATAVALAGHPAMQGRDVPFAFNRKEAKDHGEGGTLVGAPLQGRVVIIDDVITAGTSVRESVEIIRAAGAEPAAVLIALDRQERAGPDDALSPHSAVQDVAKTYGMPVVSIASLADILALLQGDAQFAGNREAVLAYRGKYGVV | Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). | A9I0G7 |
Q04SI9 | ENO_LEPBJ | 2-phosphoglycerate dehydratase | Leptospira | MSHNSQIQKIQAREIIDSRGNPTVEVDVTLMDGSFGRAAVPSGASTGEYEAVELRDGDKQRYLGKGVLKAVEHVNVKIQEILKGQDALDQNRVDQLMLDADGTKNKGKLGANAILGTSLAVAKAAAFHSKLPLYRYIGGNFARELPVPMMNIINGGAHADNNVDFQEFMILPVGAKNFREGLRMGAEVFHSLKSVLKGKKLNTAVGDEGGFAPDLTSNVEAIEVILQAIEKAGYKPEKDVLLGLDAASSEFYDKSKKKYVLGAENNKEFSSAELVDYYANLVSKYPIITIEDGLDENDWEGWKLLSEKLGKKIQLVGDDLFVTNIEKLSKGITSGVGNSILIKVNQIGSLSETLASIEMAKKAKYTNVVSHRSGETEDVTISHIAVATNAGQIKTGSLSRTDRIAKYNELLRIEEELGKSAVYKGKETFYNL | Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. | Q04SI9 |
A1AG46 | KBAY_ECOK1 | Tagatose-bisphosphate aldolase | Escherichia | MSIISTKYLLQDAQANGYAVPAFNIHNAETIQAILEVCSEMRSPVILAGTPGTFKHIALEEIYALCSAYSTTYNMPLALHLDHHESLDDIRRKVHAGVRSAMIDGSHFPFAENVKLVKSVVDFCHSQDCSVEAELGRLGGVEDDMSVDAESAFLTDPQEAKRFVELTGVDSLAVAIGTAHGLYSKTPKIDFQRLAEIREVVDVPLVLHGASDVPDEFVRRTIELGVTKVNVATELKIAFAGAVKAWFAENPQGNDPRYYMRVGMDAMKEVVRNKINVCGSANRISA | Catalytic subunit of the tagatose-1,6-bisphosphate aldolase KbaYZ, which catalyzes the reversible aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to produce tagatose 1,6-bisphosphate (TBP). Requires KbaZ subunit for full activity and stability. | A1AG46 |
A0A087WT02 | TVA92_HUMAN | T cell receptor alpha variable 9-2 | Homo | MNYSPGLVSLILLLLGRTRGDSVTQMEGPVTLSEEAFLTINCTYTATGYPSLFWYVQYPGEGLQLLLKATKADDKGSNKGFEATYRKETTSFHLEKGSVQVSDSAVYFCALS | V region of the variable domain of T cell receptor (TR) alpha chain that participates in the antigen recognition . Alpha-beta T cell receptors are antigen specific receptors which are essential to the immune response and are present on the cell surface of T lymphocytes. Recognize peptide-major histocompatibility (MH) (pMH) complexes that are displayed by antigen presenting cells (APC), a prerequisite for efficient T cell adaptive immunity against pathogens . Binding of alpha-beta TR to pMH complex initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn ZAP70 phosphorylates LAT, which recruits numerous signaling molecules to form the LAT signalosome. The LAT signalosome propagates signal branching to three major signaling pathways, the calcium, the mitogen-activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB) pathways, leading to the mobilization of transcription factors that are critical for gene expression and essential for T cell growth and differentiation . The T cell repertoire is generated in the thymus, by V-(D)-J rearrangement. This repertoire is then shaped by intrathymic selection events to generate a peripheral T cell pool of self-MH restricted, non-autoaggressive T cells. Post-thymic interaction of alpha-beta TR with the pMH complexes shapes TR structural and functional avidity . | A0A087WT02 |
Q57HG9 | RHAB_SALCH | Rhamnulose kinase | Salmonella | MTFRHCVAVDLGASSGRVMLARYDSKHRTLTLREIHRFVNCLQKTDGFDTWDIDSLEKDIRLGLKKVCNEGILIDSIGIDTWGVDYVLLDKQGQRVGLPVSYRDNRTTGIMPQALVQIGKSEIYRRSGIQFLPFNTIYQLRALTKQQPELTAQVAHALLMPDYFSYRLTGEMNWEYTNATTTQLVNINTDDWDDTLLAWTGAKKSWFGRPSHPGNVIGDWICPQGNRIPVVAVASHDTASAVIASPLANKHSAYLSSGTWSLMGFESKMPYTTDEALAANITNEGGAEGRYRVLKNIMGLWLLQRVLKERRITDLPALIAQTEALPACRFLINPNDDRFINPDDMRAEIQAVCRETDQPVPVSDAELARCIFDSLALLYADILHELANLRGEKFTQLHIVGGGCQNSLLNQLCADACGIRVIAGPVEASTLGNIGIQLMTLDELNNVDDFRQVVSANYDLTTYIPNPDSEIARHVAQFQPKRQTKELCA | Involved in the catabolism of L-rhamnose (6-deoxy-L-mannose). Catalyzes the transfer of the gamma-phosphate group from ATP to the 1-hydroxyl group of L-rhamnulose to yield L-rhamnulose 1-phosphate. | Q57HG9 |
Q40253 | L6_LINUS | NADP(+) hydrolase L6 | Linum | MSYLREVATAVALLLPFILLNKFWRPNSKDSIVNDDDDSTSEVDAISDSTNPSGSFPSVEYEVFLSFRGPDTREQFTDFLYQSLRRYKIHTFRDDDELLKGKEIGPNLLRAIDQSKIYVPIISSGYADSKWCLMELAEIVRRQEEDPRRIILPIFYMVDPSDVRHQTGCYKKAFRKHANKFDGQTIQNWKDALKKVGDLKGWHIGKNDKQGAIADKVSADIWSHISKENLILETDELVGIDDHITAVLEKLSLDSENVTMVGLYGMGGIGKTTTAKAVYNKISSCFDCCCFIDNIRETQEKDGVVVLQKKLVSEILRIDSGSVGFNNDSGGRKTIKERVSRFKILVVLDDVDEKFKFEDMLGSPKDFISQSRFIITSRSMRVLGTLNENQCKLYEVGSMSKPRSLELFSKHAFKKNTPPSYYETLANDVVDTTAGLPLTLKVIGSLLFKQEIAVWEDTLEQLRRTLNLDEVYDRLKISYDALNPEAKEIFLDIACFFIGQNKEEPYYMWTDCNFYPASNIIFLIQRCMIQVGDDDEFKMHDQLRDMGREIVRREDVLPWKRSRIWSAEEGIDLLLNKKGSSKVKAISIPWGVKYEFKSECFLNLSELRYLHAREAMLTGDFNNLLPNLKWLELPFYKHGEDDPPLTNYTMKNLIIVILEHSHITADDWGGWRHMMKMAERLKVVRLASNYSLYGRRVRLSDCWRFPKSIEVLSMTAIEMDEVDIGELKKLKTLVLKFCPIQKISGGTFGMLKGLRELCLEFNWGTNLREVVADIGQLSSLKVLKTTGAKEVEINEFPLGLKELSTSSRIPNLSQLLDLEVLKVYDCKDGFDMPPASPSEDESSVWWKVSKLKSLQLEKTRINVNVVDDASSGGHLPRYLLPTSLTYLKIYQCTEPTWLPGIENLENLTSLEVNDIFQTLGGDLDGLQGLRSLEILRIRKVNGLARIKGLKDLLCSSTCKLRKFYITECPDLIELLPCELGGQTVVVPSMAELTIRDCPRLEVGPMIRSLPKFPMLKKLDLAVANITKEEDLDAIGSLEELVSLELELDDTSSGIERIVSSSKLQKLTTLVVKVPSLREIEGLEELKSLQDLYLEGCTSLGRLPLEKLKELDIGGCPDLTELVQTVVAVPSLRGLTIRDCPRLEVGPMIQSLPKFPMLNELTLSMVNITKEDELEVLGSLEELDSLELTLDDTCSSIERISFLSKLQKLTTLIVEVPSLREIEGLAELKSLRILYLEGCTSLERLWPDQQQLGSLKNLNVLDIQGCKSLSVDHLSALKTTLPPRARITWPDQPYR | TIR-NB-LRR receptor-like protein that confers resistance to the flax rust phytopathogenic fungus (M.lini) . Acts as a NAD(+) hydrolase (NADase): in response to activation, catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide; NAD(+) cleavage triggering a defense system that promotes cell death . Also able to hydrolyze NADP(+), but not other NAD(+)-related molecules . | Q40253 |
P0CD31 | NU2C2_PIPCE | NADH-plastoquinone oxidoreductase subunit 2 B | Piper | MIWHVQNENFILDSTRIFMKAFHLLLFHGSFIFPECILIFGLILLLMIDSTSDQKDIPWLYFISSTSLVMSITALLFRWREEPMISFSGNFQTNNFNEIFQFLILLCSTLCIPLSVEYIECTEMAITEFLLFVLTATLGGMFLCGANDLITIFVAPECFSLCSYLLSGYTKRDVRSNEATTKYLLMGGASSSILVHGFSWLYGSSGGEIELQEIVNGLINTQMYNSPGISIALIFITVGIGFKLSPAPFHQWTPDVYEGSPTPVVAFLSVTSKVAASASATRIFDIPFYFSSNEWHLLLEILAILSMILGNLIAITQTSMKRMLAYSSIGQIGYVIIGIIVGDSNDGYASMITYMLFYISMNLGTFACIVLFGLRTGTDNIRDYAGLYTKDPFLALSSALCLLSLGGLPPLAGFFGKLYLFWCGWQAGLYFLVSIGLLMSVVSIYYYLKIIKLLMTGRNQEITPHMRNYRRYPLRSNNSIELSMILCVIASTIPGISMNPIIAIAQDTLF | NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. | P0CD31 |
A9QC94 | PSBB_TRACE | Protein CP-47 | Trachelium | MGLPWYRVHTIVLNDPGRLLAVHIMHTALVAGWAGSMALYELAVFDPSDPVLDPMWRQGMFVIPFMTRLGIINSWGGWGITGGTITYPGIWSYEGVAGAHIVFSGLCFLAAIWHWVYWDLEIFTDERTGKPSLDLPKIFGIHLFLAGVACFGFGAFHVTGLYGPGIWVSDPYGLTGKVQYVNPAWGVEGFDPFVPGGIASHHIAAGTLGILAGLFHLSVRPPQRLYKGLRMGNIETVLSSSIAAVFFAAFVVAGTMWYGSATTPIELFGPTRYQWDQGYFQQEIYRRVSTGLAKNQSLSEAWSKIPEKLAFYDYIGNNPAKGGLFRAGSMDNGDGIAVGWLGHPIFRDKEGRELFVRRMPTFFETFPVVLVDGAGIVRADVPFRRAESKYSVEQVGVTVEFYGGELNGVSYNDPATVKKYARRAQLGEIFELDRATLKSDGVFRSSPRGWFTFGHASFALLFFFGHIWHGARTLFRDVFAGIDPDLDAQVEFGAFQKLGDPTTRRQVV | 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. | A9QC94 |
C3P1G4 | UPP_BACAA | UPRTase | Bacillus cereus group | MGKLYVFDHPLIQHKITYIRDKNTGTKDFRELVDEVASLMAFEITRDLPLKDIEIETPVSKATTKVIAGKKLGLIPILRAGLGMVDGILKLIPAAKVGHVGLYRDPKTLQPVEYYVKLPTDVEERDFIVLDPMLATGGSAAEAINSLKKRGAKQIKLMCIVAAPEGVKVVQEEHPDVDIYVAALDEKLNDHGYVVPGLGDAGDRLFGTK | Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate. | C3P1G4 |
Q8XBR9 | PAGP_ECO57 | Lipid A acylation protein | Escherichia | MNVSKYVAIFSFVFIQLISVGKVFANADEWMTTFRENIVQTWQQPEHYDLYIPAITWHARFAYDKEKTDRYNERPWGGGFGLSRWDEKGNWHGLYAMAFKDSWNKWEPIAGYGWESTWRPLADENFHLGLGFTAGVTARDNWNYIPLPVLLPLASVGYGPVTFQMTYIPGTYNNGNVYFAWMRFQF | Transfers a palmitate residue from the sn-1 position of a phospholipid to the N-linked hydroxymyristate on the proximal unit of lipid A or its precursors. | Q8XBR9 |
A0Q2Z4 | ATPB_CLONN | F-ATPase subunit beta | Clostridium | MPDNNVGRVVQVIGPVIDIKFDSDCLPNIYNAIEIDMGDRILITEVEQHIGDDVVRTIAMESTEGLKRGMKAVNTEKPISVPVGSEILGRLFNVLGKTIDEEGEFKAEEYYPIHRPAPTFEEQSVEPEMFETGIKVIDLIAPYQKGGKIGLFGGAGVGKTVLIQELINNIAKEHGGLSVFTGVGERTREGNDLYYEMKESGVINKTALVFGQMNEPPGARMRVALTGLTMAEYFRDQGQNVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGALQERITSTKHGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRSIAELGIYPAVDPLESTSRILDPRVIGQEHYDVAINVKHILERYKELQDIIAILGVDELSEEDKLVVSRARKVQRFLSQPFTVAEQFTGMKGKFVPVKETVRGFKEIIEGKYDDVPEAAFLFVGSIEEALEKAKTMS | Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | A0Q2Z4 |
C3MZM9 | RPO1C_SULIA | DNA-directed RNA polymerase subunit A'' | Sulfolobus | MIDEKDKSYLEEKVKQASNILPQKIVEDLKNLISNKEVLVTRDEIDKIFDLAIKEYSEGLIAPGEAIGIVAAQSVGEPGTQMTLRTFHFAGIRELNVTLGLPRLIEIVDAKKVPSTPMMTIYLTDEYKHDKEKALEVARKLEYTKIENVVSSTSIDIASMSIILQLDNEMLKDKGVTVDDVKKAINRLKLGEFVIDESEGNTLNISFANIDSIAALFKLRDKILNTKIKGIKGIKRAIVQKKGDEYIILTDGSNLSGVLSVKGVDIAKVETNNIREIEEVFGIEAAREIIIREISKVLAEQGLDVDMRHILLVADVMTRTGVVRQIGRHGVTGEKNSVLARAAFEVTVKHLLDAAARGDVEEFKGVVENIIIGHPIKLGTGMVELTMRPILR | DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Forms part of the jaw domain. | C3MZM9 |
Q0WQE7 | AUG3_ARATH | AUGMIN subunit 3 | Arabidopsis | MSSARLCSLVAELGYEGAGKLDPDSFEWPFQYDDARPILDWICSSLRPSNVLSLAELSLYEQFQRDGKLLEGDDLDQAYDSISAFSSRRNNQEAVFGAEESIKEVRDATLAHKAEALELQRQLRRLQTQYDLLTGQSSALIQGRRARVAATSAVSGQITAIEDSLSARNLQMNGVLGRLASTSQELAHYHSGEEDGIYLAYSDFHAYLAGDSACTKELNQWFAKQLDTGPYRLVAEEGKSKCSWVSLDDTSNMLRDLEKSQHQRVAELQRLRSIFGTSERQWIEAQVENAKQQAILLTLKSQVTSVEAHIHFDLHSLRRKHADLVEEISTLYQKEEKLLSETIPELCWELAQLQDTYILQGDYDLKVMRQELYISKQKVFINHLVNQLARHQFLKLACQLEKKNMLGAFSLLKVIESELQGYLSATRSRVGRCSALIQAASDVQEQGAVDDRDSFLHGVRDLLSIHSNTQAGLSTYVSAPAIIQQIVALQSDLSSLQSDLENSLPDDRNRCINELCTHIQNLQQLLFASSTTAQPILTPWPLMKELDEMGKINSKLSTAVEEVTLEHRNKREIVKHHAKDVELQRRVFVDFFCNPERLRNQVRELNALVRARQASSS | Involved in microtubules reorganization during spindle and phragmoplast development. Required for gamma-tubulin localization during mitosis. | Q0WQE7 |
Q5WSK5 | LPXD2_LEGPL | UDP-3-O-acylglucosamine N-acyltransferase 2 | Legionella | MSNYQFTKPAGPFYLAELAEISGSTLYEGKGEAFTVSGLAKLSEATTHNLVMLHQKKYLKELKNTAARACIIGPEYVKFAPDSMYLLVHPNPYKAFALIAQAFYPSEKPAGFIASSAAIETSAVIGSNCYIAHGVYIGNNAKIGSGCQIGVNTYIGDGVTIGDDCLIEDNVSIRHAVIGKHVVIYPGARIGQDGFGFASDASGHYKIPHAGGVIIGNHVEIGANTCIDRGSLDNTVIEDWCRLDNLVQVGHNVKIGKGSIIVAQVGIAGSTELGEYVTLAGQAGVIGHLKIGKGATVLASGKVYKNVKSGDRVGGHPAVSISDWQKQIRFLKTAIKPKKSPKS | Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. | Q5WSK5 |
P13079 | CARB_STRTH | Carbomycin-resistance protein | Streptomyces | MAALLKRILRRRMAEKRSGRGRMAAARTTGAQSRKTAQRSGRSEADRRRRVHGQNFLVDRETVQRFVRFADPDPGEVVLEVGAGNGAITRELARLCRRVVAYEIDRHFADRLREATAEDPRIEVVAGDFLKTSQPKVPFSVVGNIPFGNTADIVDWCLNARRLRTTTLVTQLEYARKRTGGYRRWSRLTVATWPEVEWRMGERISRRWFRPVPAVDSAVLRLERRPVPLIPPGLMHDFRDLVETGFTGKGGSLDASLRRRFPARRVAAGFRRARLEQGVVVAYVTPGQWITLFEELHGR | Probable RNA methylase. Confers resistance to carbomycin and several other macrolides, lincomycin and vernamycin B, but not to all macrolide-lincosamide-streptogramin B antibiotics. | P13079 |
O51723 | NADD_BORBU | Nicotinate mononucleotide adenylyltransferase | Borreliella | MRIAILGGTYNPVHIGHIFLAKEIEYLLNIDRVIFIPTCNPAHKLIDENVSVSNRIDMLKLALENEDKMFIDDCDIINGGITYTVDTISCVKKKYKNDKLFLIIGDDLFQNFDSWKDPQSIVSSVELVVAHRIYKERLKSSFKHIYIDNKIIPISSSEIRNRIVNGLPVSYLLPFGVLKYIKDNNLYVKKVNV | Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). | O51723 |
O32445 | NAGA_VIBCH | N-acetylglucosamine-6-phosphate deacetylase | Vibrio | MYALTNCKIYTGNDVLVKHAVIINGDKIEAVCPIESLPSEMNVVDLNGANLSPGFIDLQLNGCGGVMFNDEITAETIDTMHKANLKSGCTSFLPTLITSSDENMRQAIAAAREYQAKYPNQSLGLHLEGPYLNVMKKGIHSVDFIRPSDDTMIDTICANSDVIAKVTLAPENNKPEHIEKLVKAGIVVSIGHTNATYSEARKSFESGITFATHLFNAMTPMVGREPGVVGAIYDTPEVYAGIIADGFHVDYANIRIAHKIKGEKLVLVTDATAPAGAEMDYFIFVGKKVYYRDGKCVDENGTLGGSALTMIEAVQNTVEHVGIALDEALRMATLYPAKAIGVDEKLGRIKKGMIANLTVFDRDFNVKATVVNGQYEQN | Involved in the first committed step in the biosynthesis of amino-sugar-nucleotides. Catalyzes the hydrolysis of the N-acetyl group of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to yield glucosamine 6-phosphate and acetate. | O32445 |
A4Y9B5 | PNP_SHEPC | null | Shewanella | MNPIVKSFEYGQHTVTLETGVIARQADAAVLASMGDTTVLVTVVGKKEAEAGRDFFPLTVNYQEKTYAAGKIPGGFFKREGRPSEDETLIARLIDRPIRPLFPNGFKNEVQVIITVVSVDPQIEPDIISMIGTSAALAISGIPFSGPLGAARVGYINGEYVLNPTVAQIETSQLNLVVAGTASAVLMVESEAQALPEEVMLGSVVYGHDQQQVVINAIAEFKAEAGKPMWDWTAPVQDETLVAQIKELAEAGLGDAYKIQVKQDRYAQVAVVKAATKEALLASNPNIDLREVDNLLGSLEKKVVRGRIIRGEPRIDGREPDMIRALSVLAGVLPRTHGSALFTRGETQALVTCTLGTERDAQKIDSIMGERTNRFMLHYNFPPYSVGETGMVGSPKRREIGHGKLAWRGINAVMPSAEEFPYSVRVVSEITESNGSSSMASVCGTSLALMDAGVPIKTSVAGIAMGLVKEGDDFVVLSDILGDEDHLGDMDFKVAGTRGGITALQMDIKIEGITKEIMEIALQQAYGARVHILNVMDQAIGSHRDDISDHAPRITTIKINPEKIRDVIGKGGAVIRALTEETGTTIELEDDGTVRIASSNGEATKEAIRRIEEITSEVEVGRIYNGKVIRIVDFGAFVNILPGKDGLVHISQISDERVANVSDHLELNQEVAVKVMEVDRQGRVRLSIKEAQTKEAAAE | Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. | A4Y9B5 |
Q602B7 | SYI_MESH2 | Isoleucyl-tRNA synthetase | Mesomycoplasma | MDKNFYKNSLNIFNSNFSMKANLSEKDKFYADFWEKNQIYQQILRKRRGNPRFILHDGPPYANGDIHIGHALNKILKDIIVRYKTMAGFYSPFVPGWDTHGLPIENKIINQIGSKSTLEIRRKSNDFANSQILAQMKQFKKLNLLTDFKQIYQTNTPNYEAKQLKLFKKMVSRGLVYRALKPVYWSPSSQSALAEAEIEYLEYRSPSLFTSFDIKKGNNFVAENDKLIIWTTTPWTLIANSGVAVGENFDYVRIKNGENFYVLAANLLEKLAVIFDWKHYEIIDNFPGKSILGIKYLHPIFEKICPIVSGNHVSLDVGSGLVHLAPLFGEDDYWIGRENNLEMVMHVNDDGKFNENAGQFSGQFYADSNKLITEFLEKKSKILHLSFIDHSFPHDWRTLKPVIYRGTPQWFVSIEKIKKDLEKAIEEIEFPENWLKKRLTKMVVERKDWLISRQRSWGIPLIIFYDQNKEPVLDKPEIFDYIISLVEKFGSRIWYEKTTDELLPEKYQNLGWTKENDILDVWFDSGVSFFAANISDEKPPFDIYFEGSDQYRGWFNSSLINSVIYFGFSPYKKLLSHGFVVDAKGNKMSKSRGNGVDPLVILSKYGCDIFRLWVANSEYYNDIVYSEAIFEQNVEIYRKIRNTVRFLITNLADFKPKKYELTEVDLYIFNKIQKLKNEIIQNYDQNRFVRVVKIINNFIIEFSNFYLSIVKDILYADKEESLKRRQVQYNLYELLQVLNIAIAPIMPTTAEEIYSFIQKNNKQISVHMEEFFKKSHFDEELDAKWDEFFQIKDSVYQLIEQKIKSKEIKRPNEVGVLLKTDSDFIKSIDLEKLLMVAKVEFSNEKTEILQLNWEKCPRCWNHFEKINKVCARCFEVLNEIVPEKNS | Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). | Q602B7 |
P43263 | NPRE_BREBE | Neutral protease | Brevibacillus | MKKSYLATSLTLSIAVGVSGFTSVPAFAKTKIDYHKQWDTPQYIGEVWEPEGAKGDDVVWSYLEKYKDEFRIQGNVEDHFEIVNEARNKETDTKHYRLQEVYNGIPIYGFQQTVHIDADGNVTSFLGQFIPDLDSNKQLKKKPKLNEQKAVKQAIKDVEGEVGEKPDFIQDPEAKLYIYVHEDESYLAYAVELNFLDPEPGRWMYFIDAHSGDVINKYNMLDHVTATGKGVLGDTKQFETTKQGSTYMLKDTTRGKGIETYTANNRTSLPGTLMTDSDNYWTDGAAVDAHAHAQKTYDYFRNVHNRNSYDGNGAVIRSTVHYSTRYNNAFWNGSQMVYGDGDGTTFLPLSGGLDVVAHELTHAVTERTAGLVYQNESGALNESMSDIFGAMVDNDDWLMGEDIYTPGRSGDALRSLQDPAAYGDPDHYSKRYTGSQDNGGVHTNSGINNKAAYLLAEGGTHYGVRVNGIGRTDTAKIYYHALTHYLTPYSNFSAMRRAAVLSATDLFGANSRQVQAVNAAYDAVGVK | Extracellular zinc metalloprotease. | P43263 |
A7MKJ6 | EFG_CROS8 | Elongation factor G | Cronobacter | MARTTPIARYRNIGISAHIDAGKTTTTERILFYTGVNHKIGEVHDGAATMDWMEQEQERGITITSAATTAFWSGMAKQYEPHRINIIDTPGHVDFTIEVERSMRVLDGAVMVYCAVGGVQPQSETVWRQANKYKVPRIAFVNKMDRMGANFLKVVGQIKTRLGANPVPLQLAIGAEEGFTGVVDLVKMKAINWNDADQGVTFEYEDIPADMQDLADEWHQNLIESAAEASEELMEKYLGGEELTEEEIKKALRQRVLNNEIILVTCGSAFKNKGVQAMLDAVIDYLPSPVDVPAINGILDDGKDTPAERHASDEEPFSALAFKIATDPFVGNLTFFRVYSGVVNSGDTILNSVKSARERFGRIVQMHANKREEIKEVRAGDIAAAIGLKDVTTGDTLCNPDHPIILERMEFPEPVISIAVEPKTKADQEKMGLALGRLAKEDPSFRVWTDEESNQTIIAGMGELHLDIIVDRMKREFNVEANVGKPQVAYREAIRSKVTDIEGKHAKQSGGRGQYGHVVIDMYPLEPGSNPKGYEFINDIKGGVIPGEYIPAVDKGIQEQLKSGPLAGYPVVDIGIRLHFGSYHDVDSSELAFKLAASIAFKEGFKKAKPVLLEPIMKVEVETPEENTGDVIGDLSRRRGMLRGQESEVTGVKIHAEVPLSEMFGYATQLRSLTKGRASYTMEFLKYDDAPNNVAQAVIEARGK | Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. | A7MKJ6 |
A5FJ95 | PDXJ_FLAJ1 | Pyridoxine 5'-phosphate synthase | Flavobacterium | MTKLSVNINKIATLRNARGGNVPDLLKVAADIQRFGGQGITIHPRPDERHIRYQDARDLKAIVTTEYNIEGNPQHNFIDLVLECKPDQVTLVPDAIGAITSSAGWDTIKNQEYLKEVIQEFQRNGIRTSIFVDPVLEMIEGAKKTGTDRIELYTEAFAHQYDLGNKNGIDPYVKAAELANELGLGINAGHDLSLDNIQFFKQNIPGLLEVSIGHALISEALYLGLDNVVNMYLKKLK | Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate. | A5FJ95 |
Q9C8T9 | DRL19_ARATH | Putative disease resistance protein At1g63350 | Arabidopsis | MGISFSIPFDPCVNKVSQWLDMKVSYTHNLEKNLVALETTMEELKAKRDDLLRKLKREEDRGLQTLGEIKVWLNRVETIESRVNDLLNARNAELQRLCLCGFCSKSLTTSYRYGKSVFLKLREVEKLERRVFEVISDQASTSEVEEQQLQPTIVGQETMLDNAWNHLMEDGVGIMGLYGMGGVGKTTLLTQINNKFSKYMCGFDSVIWVVVSKEVNVENILDEIAQKVHISGEKWDTKYKYQKGVYLYNFLRKMRFVLFLDDIWEKVNLVEIGVPFPTIKNKCKVVFTTRSLDVCTSMGVEKPMEVQCLADNDAYDLFQKKVGQITLGSDPEIRELSRVVAKKCCGLPLALNVVSETMSCKRTVQEWRHAIYVLNSYAAKFSGMDDKILPLLKYSYDSLKGEDVKMCLLYCALFPEDAKIRKENLIEYWICEEIIDGSEGIDKAENQGYEIIGSLVRASLLMEEVELDGANIVCLHDVVREMALWIASDLGKQNEAFIVRASVGLREILKVENWNVVRRMSLMKNNIAHLDGRLDCMELTTLLLQSTHLEKISSEFFNSMPKLAVLDLSGNYYLSELPNGISELVSLQYLNLSSTGIRHLPKGLQELKKLIHLYLERTSQLGSMVGISCLHNLKVLKLSGSSYAWDLDTVKELEALEHLEVLTTTIDDCTLGTDQFLSSHRLMSCIRFLKISNNSNRNRNSSRISLPVTMDRLQEFTIEHCHTSEIKMGRICSFSSLIEVNLSNCRRLRELTFLMFAPNLKRLHVVSSNQLEDIINKEKAHDGEKSGIVPFPKLNELHLYNLRELKNIYWSPLPFPCLEKINVMGCPNLKKLPLDSKSGKHGGNGLIITHREMEWITRVEWEDEATKTRFLANRSSFSSSLICFSNDLVSRDMNCFHL | Potential disease resistance protein. | Q9C8T9 |
A3PU80 | MURB_MYCSJ | UDP-N-acetylmuramate dehydrogenase | unclassified Mycobacterium | MTGQELAGAEVEADVALAPLTTLRVGPVARRLITATSTEQLVAALRAPVGRDALILAGGSNVVLADDMADLTVIRVANSEITVHDGIVRAEAGANWDDVVVTALAHGLGGLECLSGIPGSAGATPVQNVGAYGSEVADTIRRVRLFDRRTGRDDWVTPQDMAFGYRTSVLKHSDHAVVLEVEFALDVGGRSAPLRYGELARALDVEPGGRADPVAVRDAVLALRRGKGMVLDEPDRDTWSVGSFFTNPVVTTADHERLAAEVDGPVPSYPAPDGVKLAAGWLVEHAGFGKGYPGDDAPARLSTKHALAVTNRGHATTADVIALARTVRDGVRTTFGIELTPEPTLVGCTL | Cell wall formation. | A3PU80 |
G3XDA7 | FTSQ_PSEAE | Cell division protein FtsQ | Pseudomonas | MNGVLLRHQQPGGLGRAPRKPMPRGASRLVAKEPLSVRLPKADFSFLKYLAWPLLLAVLGYGAYRGAEYILPYADRPIAKVSVEGDLSYISQRAVQQRISPYLAASFFTIDLAGMRGQLEQMPWIAHAEVRRVWPDQVVIRLDEQLPIARWGDEALLNNQGQAFTPKELANYEHLPRLHGPQRAQQQVMQQYQLLSQLLRPLGFSIARLEMSDRGGWALTTAQGVEIQIGRDHVVDKIRRFVSIYDKALKDQISNIARIDLRYPNGLAVAWREPVTPATVATASAVQ | Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. May control correct divisome assembly. | G3XDA7 |
Q8UF87 | SSB_AGRFC | Single-stranded DNA-binding protein | Agrobacterium tumefaciens complex | MAGSVNKVILIGNVGADPEIRRTQDGRPIANLRIATSETWRDRNSGERKEKTEWHTVVVFNEGLCKVVEQYVKKGAKLYIEGQLQTRKWQDQTGNDRYSTEIVLQGFNSTLTMLDGRGEGGGGRSGGGDFGGGNDYGSGGGYDQQSSPRGGSSRGGGQPSGGFSNDMDDDIPF | Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism. | Q8UF87 |
Q977U8 | RS8_METTL | 30S ribosomal protein S8 | Methanothermococcus | MSLMDPLANALNHISNCEGVGKSVAYVKPASKLIGRVLNVMQDHGYIGNFEYIEDGRAGIYKVELIGQINKCGAVKPRYAVKKQEFEKFEKRYLPAKGFGLLIVSTPKGLMTHDEAKNQGLGGRLISYVF | 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. | Q977U8 |
P02238 | LGBA_SOYBN | Nodulin-2 | Glycine subgen. Soja | MVAFTEKQDALVSSSFEAFKANIPQYSVVFYTSILEKAPAAKDLFSFLANGVDPTNPKLTGHAEKLFALVRDSAGQLKASGTVVADAALGSVHAQKAVTDPQFVVVKEALLKTIKAAVGDKWSDELSRAWEVAYDELAAAIKKA | Provides oxygen to the bacteroids. This role is essential for symbiotic nitrogen fixation. | P02238 |
Q5WWW0 | ERPA_LEGPL | Iron-sulfur cluster insertion protein ErpA | Legionella | MASVDVSQNTSDINFSVSAADKVAELIKEEDNSDLNLRVSITGGGCSGFQYGFSFDEQINDDDTVIIQQCSDGKSSVKLLIDSMSYQYLHDAEIDYIKGIQGEQFVIRNPNAKTTCGCGSSFSIGDEDDL | Required for insertion of 4Fe-4S clusters for at least IspG. | Q5WWW0 |
Q2HXL0 | RBOHC_SOLTU | StRBOHC | Solanum | MQNSENHHPHHHHHHSDTEIIGNDRASYSGPLSGPLNKRGGKKSARFNIPESTDIGTSAGAGAKSNDDAYVEITLDVREDSVAVHSVKTAGGADVEDPELALLAKGLEKKSTLGASLVRNASSRIRQVSQELKRLASLNKRPIPTGRFDRNKSAAAHALKGLKFISKTDGGAGWAAVEKRFDEITAPTTGLLPRAKFGECIGMNKESKEFAGELYDALARRRNITTDSINKAQLKEFWDQVADQSFDTRLQTFFDMVDKDADGRITEEEVREIIGLSASANRLSTIQKQSDEYAAMIMEELDPNNLGYIMIENLEMLLLQAPNQSVQRGGESRNLSQMLSQKLKHTQEPNPLVRWYKSFMYFLLDNWQRVWVLLLWIGIMAVLFTWKYIQYKQKAAYDVMGPCVCLAKGAAETIKLNMAIILLPVCRNTITWLRNKTRLGSAVPFDDNLNFHKVIAVAIALGVAIHGLAHLTCDFPKLLNASEEAYEPMIYYFGEQPESYWWFVRGVEGVTGIIMVVLMAIAFTLATPWFRRGRVSFPKPFHKLTGFNAFWYSHHLFIIVYTLLIVHGEKLYITKDWYKRSTWMYLTVPLVLYAGERLLRAFRSSIKAVKILKVAVYPGNVLALHMSKPQGYKYKSGQYMFVNCAAVSPFEWHPFSITSAPGDDHLSVHIRTLGDWTRQLKTVFSEVCQPPPNGKSGLLRADYLQGENNPNFPRVLIDGPYGAPAQDYKQYEVVLLVGLGIGATPMISIVKDIVNNMKAMDEEENSLENGNGMSNAAQNASPNMAQKRGKSSSASGGNSFNTRRAYFYWVTREQGSFDWFKGIMNEAAEMDHKGVIEMHNYCTSVYEEGDARSALITMLQSLHHAKSGVDIVSGTRVKSHFAKPNWRNVYKRIALNHPEAKVGVFYCGAPALTKELKQHALNFSHKTSTKFDFHKENF | Calcium-dependent NADPH oxidase that generates superoxide. May be responsible for the oxidative burst in response to pathogen attack in the leaves. | Q2HXL0 |
A9VFD5 | MTNA_BACMK | S-methyl-5-thioribose-1-phosphate isomerase | Bacillus cereus group | MSTIITIPRSVSWKGDAIAVLNQTKLPHVTEYKTLTNIEDVWKSIIMLEVRGAPAIGIVAAFGLALAAKKYDAINIYEFQKKFNRDCNYLGTSRPTAVNLFWAIDRMRESIREITTIKEAQKILEEEALHIQQEDEMVCRSIGEHALTCFKDGDKILTICNAGSIATARYGTALAPFYIGKEKGVRLHAYACETRPVLQGGRLTTWELKQADIDVTLITDNTAAHAIRTKEINAIIVGADRIVENGDTANKIGTLNLAILAKYFGIPFYVAAPLSTFDTTKQTGAEIVIEERDETEVTKIFGKQVAPLGTPVFNPAFDVTPHELITGIITEKGILRGDYKQEITSLFEK | Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P). | A9VFD5 |
Q5FGD5 | ARGC_EHRRG | N-acetyl-glutamate semialdehyde dehydrogenase | Ehrlichia | MSYQVSVAVVGATGYVGVELVRLLLFHPMVKIKYLCATQSIGSLLSSHYDHVLKDSIPVSISCFSSIDLSKVDVIFLCLPHGQSNEIVKKIHNEVKIIIDLSADFRIKDIDTYKEWYGAHCCPDLIQDFVYGLTEIYWEEIKKSRFVACPGCYATSALVPLFPLLRLRLVKSQNIIVDAKSGVSGAGRSVDQKKLFCEIHDVIKSYNISKHRHIPEIEQELCFAACQENINVQFVPNLIPVKRGMLSSIYLELEEGVSPIDIREALLVFYKDSKFIFIDEEKAITTKSVIGTNYCYIGVFPGRIPNTVIIVCNIDNLLKGASGQAVQNFNIMMSCDETTALLNIPYL | Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. | Q5FGD5 |
A5WDY5 | COQ7_PSYWF | 2-nonaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase | Psychrobacter | MAKNLSIIDRAIVGFDSSLRAIIPHSNQTARPLPVSSDALPQLSITESRHVAGLMRINHTGEVCAQGLYHGQAFTAKDDLVKQAMQHSADEEIDHLVWCETRLDELGSHPSVFTPVWYGLSFGLGAIAGIISDEFSLGFVAETEAQVSEHLQDHIDQLPEQDTRSKEILAQMNIEELEHREAALNHGGKALSAPVRISMRWMANRMKNLAYHL | Catalyzes the hydroxylation of 2-nonaprenyl-3-methyl-6-methoxy-1,4-benzoquinol during ubiquinone biosynthesis. | A5WDY5 |
Q86SQ6 | AGRA1_HUMAN | G-protein coupled receptor 123 | Homo | MDLKTVLSLPRYPGEFLHPVVYACTAVMLLCLLASFVTYIVHQSAIRISRKGRHTLLNFCFHAALTFTVFAGGINRTKYPILCQAVGIVLHYSTLSTMLWIGVTARNIYKQVTKKAPLCLDTDQPPYPRQPLLRFYLVSGGVPFIICGVTAATNIRNYGTEDEDTAYCWMAWEPSLGAFYGPAAIITLVTCVYFLGTYVQLRRHPGRRYELRTQPEEQRRLATPEGGRGIRPGTPPAHDAPGASVLQNEHSFQAQLRAAAFTLFLFTATWAFGALAVSQGHFLDMVFSCLYGAFCVTLGLFVLIHHCAKREDVWQCWWACCPPRKDAHPALDANGAALGRAACLHSPGLGQPRGFAHPPGPCKMTNLQAAQGHASCLSPATPCCAKMHCEPLTADEAHVHLQEEGAFGHDPHLHGCLQGRTKPPYFSRHPAEEPEYAYHIPSSLDGSPRSSRTDSPPSSLDGPAGTHTLACCTQGDPFPMVTQPEGSDGSPALYSCPTQPGREAALGPGHLEMLRRTQSLPFGGPSQNGLPKGKLLEGLPFGTDGTGNIRTGPWKNETTV | Orphan receptor. | Q86SQ6 |
O36051 | RR4_NEOSP | 30S ribosomal protein S4, chloroplastic | unclassified Neomarica | RFKKIRRLGALPGLTSKRPRSGSDLKNQLRSGKRSQYRIRLEEKQKLRFHYGLTERQLLKYVHIAGKAKGSTGQVLLQLLEMRLDNILFRLGMASTIPGARQLVNHRHILVNGRIVDIPSYRCKPRDIITTKDKERSKVLIQNYIASSPHEELPNHLTIDPLQYKGLVNQIIDSKWVGLKIN | With S5 and S12 plays an important role in translational accuracy. | O36051 |
Q8TT89 | RIBB_METAC | 3,4-dihydroxy-2-butanone 4-phosphate synthase | Methanosarcina | MNESTVYECLKYGNENINRALEVLRAGKMIQIYDSDSREGETDLVIPAKAVTYKDVKWMRKDAGGLICVAVDPVASKQLKLPFMADLVREASRTSESLGEVVEKDGDLKYDSHSSFSIWVNHRDTRTGIPDLERALTIRKIGEITEKSLSGNGIRFGNEFRTPGHVALLRAAEGLLDERMGQTELSVALARMAGITPAMVVCEMLDDESGRALSKENSKDYGKDHGLVFLEGQEILEAYMLWTGSEC | Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate. | Q8TT89 |
B5Y342 | PSD_KLEP3 | Phosphatidylserine decarboxylase beta chain | Klebsiella | MLNDLKLSLQYILPKLWLTRLAGWGASKRAGWLTKLVIDLFVKYYKVDMKEAQKPDTAAYRTFNDFFVRPLRDDVRPLNTDPNVLVMPADGVISQLGAIEDDKILQAKGHDYSLEALLAGNYQMAGLFRNGSFATTYLSPRDYHRVHMPCNGILREMIYVPGDLFSVNHLTAQNVPNLFARNERVICLFDTEFGPMAQILVGATIVGSIETVWSGTVTPPREGIIKRWTWPAGDSEGSVALLKGQEMGRFKLGSTVINLFAPGQVKLVDSLQSLSVTKIGQPLATAVEASTAAEPAPLPEEEIRAEHRASPLVDDTQDQG | Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). | B5Y342 |
Q6F7T4 | RS13_ACIAD | 30S ribosomal protein S13 | Acinetobacter | MARIAGVNIPDNKHAVISLTYIFGVGRHTAKSILAAVGIGPTTKIRELDDAQLDAIRAEVAKVPTEGDLRREISMNIKRLMDLGCYRGLRHRRSLPVRGQRTKTNARTRKGPRKPIKK | Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites. | Q6F7T4 |
B8DA57 | HIS1_LISMH | ATP phosphoribosyltransferase | Listeria | MKALKIALTKGRLEKDAVALLEKAGIDCSSMTDKKRKLIFHSSTQPISFILVKAVDVMTYVKHGVADIGIVGKDVLMEASKSHYEMLDLEIGKCQFCLASTPDFDPSSYRRKIIATKYPTVASKFFREKGEDVEIIKIEGSVEIAPVLGLADAIIDIVETGSTLKENGLLIYEKMYPISARLIVNKASLKQNKTQIFQLIDQLEQAIKEERIE | Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. | B8DA57 |
P0C092 | CSEN4_MOUSE | Calsenilin isoform 4 | Mus | MRQLPAGPSSLACSGCKAGRLVTVPFSSRDAEDQGSREGIGWQPPGRSWAHTTEQEGKHQVAKATVHPPGPDALLLNQVDPVQCCPTRL | Unknown for isoform 4. Csen is involved in calcium-dependent transcriptional repression, regulation of potassium channels, and perhaps in processing of PSEN2 and apoptosis. | P0C092 |
Q034Y5 | RL23_LACP3 | 50S ribosomal protein L23 | Lacticaseibacillus | MEARDIILRPIVTEQSMAEMDNRKYTFEVALHATKPQVRKAVEEIFGVKVVNVNIANVRGKKKRQGRYEGMTRRRRKALIALSADSKEIKIFADEDNDKK | One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome. | Q034Y5 |
C5FNB5 | LAP5_ARTOC | Probable leucine aminopeptidase MCYG_04170 | Microsporum | MKVLAALALSALALAKPTPPMPGMSLIQTGPQETRWVTDAEKLELTMNNVGFFDITDMPVTASSVTKPKSYAFPGNVSHQADVKPLLGKLSSDHLMSNLQKFSDFPNRYYQADTGVQSAEWVLSQVQGVIGKIQGAKAEKIEHKWKQPSIRAIIPGKSEKIVVVGAHQDSINGQNPKAAAPGADDNGSGSMTILEALTALVSDQKIAGGQATNTIEFHWYAGEEAGLLGSQAVFQQYKQAGKEVVAMLNQDMTGYGKTMGIITDNSDSALTTFTKMILDTYTTAKYADSECGYACSDHASANKAGYPSAFVYEAVLGQDNPAIHSPDDTIDKLDPAKMLEHAKLVVGFAYELAFANL | Probable extracellular aminopeptidase which contributes to pathogenicity. | C5FNB5 |
Q2YIQ4 | ERYD_BRUA2 | Erythritol catabolism regulatory protein EryD | Brucella | MADADDSLALRAAWLHFVAGMTQSAVAKRLGLPSVKAHRLIAKAVADGAVKVTIDGDITECIDLENRLADLYGLDYCEVAPDIGEEGLPLMALGHAGANFMRREIEHGDHEVIGIGHGRTLSAAVGYMPRVMANDLRFVSLLGGLTRNFAANPHDVMHRIAEKTGMPAYVMPVPFFANTAEDREVLLAQRGVTTVFDMGCRAELKIVGIGTVDAQAQLVTSGMIELGEVEEIANLGGVGEMLGHFFNANGQWLETALTGRTIAASVENADMSRIVALAGGLSKVDAIRAVLKSGRLYGLITDERTAKALIGQPNGK | Represses the expression of the eryABCD operon, which is involved in erythritol catabolism. | Q2YIQ4 |
Q4WJ81 | CRZA_ASPFU | C2H2 finger domain transcription factor crzA | Aspergillus subgen. Fumigati | MASQEMFPELGQSPAPGVKSRGVSRSPHPHQQQQQQQHQQHQGQFTGTVTGLDLDSSIATASSFANSSFDPNSNNVSPSAESYGYTAAGYLSGTPASQTDQNYANSLQIPQSYGTGLVPQFNESRGLPIQQQSQQQHHQQPSLDDNFSDLLNSNATEYDFNTVYQTHSPSSNTAPEYDSSLLLDPQVHQQSHPTQIPSSHSSTSPQISPLEQQQHSSPGPMSTQGSTTVAYYTPQHSRHASLDPATAAFLTSNTHPDWQAVMGNSAAFQGHRRAPSEVSEISSAAPSPYLSQHESFDGVDNNPSPLLAPQNDPSLYDSALGIENFTLSEQHQQHQGFSPAHSPYISPRLMPQQGQEMMPNVPYLSGPAPNTQYPTPPNDMYGNGAEGMMNMSQGTHPSVDIGQASQMAPPSINVEFAPPSRIPSFGPSKPASNLDSLSPPPSSTRSRGRSKSDPYAHPSTSRLRSSSTSSSLDPLAPTTPRSLSPFDSFGRQQQSNPSSRDPSPSRSNRRLSTSSIDSRNYILGLADPQRPGASPNDSKRVQKHPATFQCNLCPKRFTRAYNLRSHLRTHTDERPFVCTVCGKAFARQHDRKRHEGLHSGEKKFVCQGELSRGGQWGCGRRFARADALGRHFRSEAGRICIKPLLDEESQERERSLMDQQQHHLQPLPQQVMVPVDNPHAGNFVLPAALLAQYPALQTLQWDQIAASADDPSDIGGRSSFDASSGNEFGFEDDDSGLSSVSGINAGYSAAGNFY | Transcription factor involved in the regulation of calcium ion homeostasis . Regulates genes encoding calcium transporters, transcription factors and genes that could be directly or indirectly involved in calcium metabolism . Supports especially pmcA, pmcB and pmcC expression encoding for calcium-translocating P-type ATPases . Binds target promoters at motif A[GT][CG]CA[AC][AG] . Plays an essential role germination, radial growth, and asexual development . Also plays a major role in proper chitin and glucan incorporation into the cell wall . Involved in the high-osmolarity glycerol response (HOG) signaling pathway . Required for pathogenicity in an experimental murine model of invasive pulmonary aspergillosis . | Q4WJ81 |
B4TRX1 | RLMKL_SALSV | rRNA (guanine-N(7)-)-methyltransferase RlmK | Salmonella | MNSLFASTARGLEELLKTELEKLGAVGCQVVQGGVHFQGDTRLIYQSLMWSRLASRIILPMGECKVYSDLDLYLGVQAINWTEIFNPGATFAVHFSGLNDTIRNSQYGAMKVKDAIVDAFTRKNLPRPNVDRESPDLRINVWLNKETASIALDLSGDGLHLRGYRDRTGLAPIKETLAAAIVMRSGWQPGTPLLDPMCGSGTLLIEAAMWATDRAPGLHRGHWGFSGWAQHDEAIWQEVKAEAQTRARKGLAEYSSHFYGSDSDARVIERARSNARRAGIGELITFEVKDVAQLSNPLPKGPYGTVISNPPYGERLDSEPALIALHSLLGRTMKNQFGGWNLSLFSASPDLLGSLQLRADKQFKAKNGPLDCVQKNYHIAETTADSKPATVAEDYANRLRKNLKKLEKWARQEGIECYRLYDADLPEYNVAVDRYGDWAVIQEYAPPKTVDAQKARQRLFDIIAATLSVLGIPPNKLVLKTRERQKGKNQYQKMSEKGEFLEVSEYNARLWVNLTDYLDTGLFLDHRIARRMLGEMSKGKDFLNLFSYTGSASVHAGLGGARSTTTVDMSRTYLEWAERNLRLNGLSGRAHRLIQADCLGWLREANEQFDLIFIDPPTFSNSKRMEESFDVQRDHVALMKDLKRLLRKGGTIMFSNNKRGFRMDLEGLAELGLTAQEITQKTLSPDFARNRQIHNCWLIRAA | Specifically methylates the guanine in position 2445 (m2G2445) and the guanine in position 2069 (m7G2069) of 23S rRNA. | B4TRX1 |
Q6A6V2 | TSAD_CUTAK | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Cutibacterium | MSEPLILGIESSCDETGVGIVRGNDLLANEVASSMEQHVRFGGVVPEVASRAHLEAIVPVLDKAASTAGVDLSELDGIAVTAGPGLAGALVVGLSAAKALASWLNKPLYGVNHLAGHVAVDLLEHGELPMPCGALLVSGGHTSLLWVNDIATDIIEVGSTIDDAAGEAYDKVARVLGLPYPGGPVIDKAAAEGDPTAIRFPRGLTARHDMVKHRFDYSFSGLKTAVSRWVETQQRDGVEFRIADVAASFQEAVADVLTAKAVDMCQEYGLTHFLIGGGVAANSRLRTLLAERMADAGVELRRPRPGLCTDNGAMIAALGVQVVKAGLPASAMDISADSGLPIETVLV | Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction. | Q6A6V2 |
P22940 | TSAG_ORITS | TSG56 | Orientia | MKKIMLIASAMSALSLPFSASAIELGEEGGLECGPYGKVGIVGGMITGAESTRLDSTDSEGKKHLSLTTGLPFGGTLAAGMTIAPGFRAELGVMYLRNISAEVEVGKGKVDSKGEIKADSGGGTDTPIRKRFKLTPPQPTIMPISIADRDVGVDTDILAQAAAGQPQLTVEQRAADRIAWLKNYAGIDYMVPDPQNPNARVINPVLLNITQGPPNVQPRPRQNLDILDHGQWRHLVVGVTALSHANKPSVTPVKVLSDKITKIYSDIKPFADIAGIDVPDTGLPNSASVEQIQSKMQELNDVLEDLRDSFDGYMGNAFANQIQLNFVMPQQAQQQQGQGQQQQAQATAQEAVAAAAVRLLNGNDQIAQLYKDLVKLQRHAGVKKAMEKLAAQQEEDAKNQGEGDCKQQQGASEKSKEGKGKETEFDLSMIVGQVKLYADLFTTESFSIYAGVGAGLAHTYGKIDDKDIKGHTGMVASGALGVAINAAEGVYVDLEGSYMHSFSKIEEKYSINPLMASVGVRYNF | May be an adherent factor for rickettsial adsorption to the host-cell surface and a determinant of virulence of individual rickettsial strain. It is the major outer membrane protein. | P22940 |
C4PZQ3 | LIAS_SCHMA | Lipoic acid synthase | Schistosoma | MGLLLPRGSYVFPVLASVSAATKRRAEWSYIKINITHSYSSNDKSSEFEEDNPTQKLSPEFQKAIAHGPSLSEFIKLSNNNQSTKEDFFSSPSSVNKSGKSLRLPEWLKTEIPCGGSVARLQKQLRSLNLHTVCEEARCPNISECWTAGKSTAATATIMIMGDTCTRGCRFCSVKTSPNPPPLDPDEPVNTAEAISKWDVDYIVITSVDRDDLGDGGARHIAKTIRQIKVRKPSIIVECLVPDFRGCTDSIHTVVRASPEVYAHNIETVESLQRVVRDHRAGYIQSLRSLETAKERSNRLVSSGDADFLVVTKSSIMLGLGEKEKEVMIALKDLRQAGVDCVTIGQYVQPTKRHLKVKEYIHPDKFDYWAKIGNDLGFLYTASGPLVRSSYRAGEYYIKHIIDQRKRKNI | Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | C4PZQ3 |
A0A1U8QIH0 | CICD_EMENI | Cichorine biosynthesis cluster protein D | Aspergillus subgen. Nidulantes | MVGSRHPDQCAKRWHHSLDPNVKRGPWTMEEDSSLLEAVQKIGRDWKEIGRELFPSRSTTDIKNRYVILSRRRGPSPAIPENCSSIDIETHSSSLADSKPPIPAELLTPEVDFSIANTPCELDSSNLAPDTLSINMTLPSDLPSYLSLPLPDTAETDHALDESSTAWEIPDWTAFDNQCLFTPGASELEGSFTSRNHEEPPQPLPVPDIPGPSTLVLEDLRPETVNLVIDTLLRTNSKFGMRMYNTGS | Transcription factor that regulates the expression of the gene cluster that mediates the biosynthesis of cichorine, a phytotoxin active against knapweed, corn, and soybeans. | A0A1U8QIH0 |
Q88M95 | COBT_PSEPK | N(1)-alpha-phosphoribosyltransferase | Pseudomonas | MTQAWWRDACQPLDNAAMDQARARQQQLTKPAGSLGQLEALAIQLAGLQGLERPTLDQVAITIFAGDHGVVEEGISAYPQAVTGQMLRNFVGGGAAISVLARQLQASLDVVDLGTIDAQLELPGVRHLRLGTGTANFARQPAMTENQLQAALQAGRDSAQRAAEQGAQLFIGGEMGIGNTTAAAALASVLLGCPASELSGPGTGLDNAGVQHKAEVIERALRLHGLRAEDPLQALACVGGFEIAALAGAYLGCAQAGVTVLVDGFICSVAALVAVRLNPQCRAWLLFAHQGAEPGHKTLLAALQAEPLLALGLRLGEGSGAALAVPLLRLACALHGQMATFAEAAVADRPA | Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB). | Q88M95 |
A8GW74 | FOLD_RICB8 | Methenyltetrahydrofolate cyclohydrolase | belli group | MNNVIDGKALANEILSELKHEVQRLKDKTGESPKLAIVLVGDNPASIIYVKNKIKHANKIGIDTLLLNLPITIKTEDLIAKISELNLDQNVSGIIVQLPLPDSIDKNKILSAISPSKDVDGFHPLNVGYLHSGIDNGFVPCTSLGCLEVIKKHEPNLSGKNAIIVGRSNIVGKPLSALLLKENCSVTICHSKSQNLSSITSKADIVVAAIGSPLKLTSGYFKPDAIVIDVGINRIGGNKIVGDVDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVQAFKIYS | Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate. | A8GW74 |
C1A6H2 | DNLJ_GEMAT | Polydeoxyribonucleotide synthase [NAD(+)] | Gemmatimonas | MTASSGTPPHQTVERARELREQLGTAQHEYYVLDRPTLSDQEYDRLFRELQGIEAEYPTLCTEDSPTRRVGAPVQSAFSPHRHLVRMLSLDNAFDLSELEDFEQSLKRVVGDAIHTSGYTVELKIDGAAVALTYREGVLVTAATRGDGTDGEDVTANVRTIRGVPLRLHGDNHPPLMEVRGEVYLPFAGFERMNEARVAAGEPVYVNPRNAAAGSMRQLDSANTAARPLRFFGYAAVLPDGSAPARSQWELLEQLSAWGVPVAPHRQRCHTIQEAEAWATVVEHETRATLGFAIDGGVVKVNDMALQDELGIRADRTPRWGVARKFAPDMALTKLRRIDVNVGRTGVLTPFAVLEPVDVGGATVTFASLHNADQIAAKDLREGDTVQVVRAGDVIPYVLGPVPEQRDGSQQPWSMPTQCPRCNTPVERYGDDVAVYCPNVACPGRQLEGLVHFSSKDALDIDGLSYARIQQLLDAGLVHDVADLFDITVDQLTSLERFAKKSAENLVAAIAAAKQQPLSRLMFGLGIRHVGAQAAQLLSRQYGSLDALMNATAEQLGAVRGIGSIIAQSVASYFADPTTRALMERLRARGLRFDEPNAVQADGVLTGATVVLTGTLPSLSRGEATALVEQAGGRVTSSVSKKTTFVVAGEEAGSKLDKAKELGVTVLTEAELLEKLSGASADASADASA | DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. | C1A6H2 |
Q03AR1 | GUAC_LACP3 | Guanosine 5'-monophosphate oxidoreductase | Lacticaseibacillus | MNNGMQIFDYEDIQMIPNKCVVQSRKEVDTSVKFGPHTFKIPVVPANMQTIIDEPLAIWLAEHDYFYIMHRFQPERRMDFVRDMKKRGLIASISVGVKDDEFDFIEALAANELTPDYITIDIAHGYAQVVIDMIQHIKHYLPNAFVIAGNVGTPEAVRELENAGADATKVGIGPGKVCITKLKTGFGTGGWQLAAVRWCAKAARKPIIADGGIRNNGDIAKSIRFGATMCMIGSLFAGHEETPGKHVNIDGKEYQEYYGSASEYQKGTHHNVEGKKILLPVKGKIGDTLKEMQEDLQSAVSYAGGRDLESLTKVDYVIVKNSIFNGDQY | Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides. | Q03AR1 |
Q85FH0 | NU1C_ADICA | NADH-plastoquinone oxidoreductase subunit 1 | Adiantum | MINSTEFCRNKLIHLFDELEITMNLSKSIWIFASTLLLVLGVTMGVLVIVWLERKVSAGVQQRIGPEYAGPLGIIQSLADGIKLLLKEDIIPAKGNAWLFAAGPAVVVTPVFITYLVIPFGQHIILSDLGIGVFFWIAISSIVPLGLLVAGYGSNNKYSFLGGLRAAAQSISYEIPLALCVLSISLLSGSLSTVDIVETQSKYGFWGWNLWRQPIGFIAFFISSLAECERLPFDLPEAEEELVAGYQTEYSGIKFGLFYVGSYLNLLASSLFVVVLYLGGWDFSIPFVENFGQIVSTSSVIDKSLDTLKPIVEVATTLSKSYFYLFFSILTRWTLPRVRMDQLLDLGWKFLLPIALGNLLLTASFRILLIS | NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. | Q85FH0 |
B2J0M4 | LEPA_NOSP7 | Ribosomal back-translocase LepA | Nostoc | MTDVPAVRIRNFCIIAHIDHGKSTLADRLLQATGTVEDRKMKEQFLDNMDLERERGITIKLQAARMNYTAKDGQQYVLNLIDTPGHVDFSYEVSRSLVACEGALLVVDASQGVEAQTLANVYLALENNLEIIPVLNKIDLPGAEPERVIGEIEEIIGLDCSGAILASAKEGLGIDEILEAVVERIPPPPNTINERLRALIFDSYYDSYRGVIVYFRVMDGTVRKGDRIHLMASGKEFEIDELGVLSPTQKQVEELHAGEVGYLGAAIRAVADARVGDTITLSKAKAESPLPGYAEANPMVYCGMFPIDADQFEDLREALEKLELNDAALHYEPETSSAMGFGFRCGFLGLLHMEIVQERLEREYNLDLIITAPSVVYKVITLKGEELYIDNPSRLPSPNDRQRIEEPYVQVEMITPETYVGSLMELSQNRRGIFKDMKYLAQGRTTLTYELPLAEVVTDFFDQMKSRSRGYASMEYHLIGYRENPLVKLDIMINGDPVDSLAMIVHRDKAYNVGRAMAEKLKELIPRHQFKVPIQASIGSKVIASEHIPALRKDVLAKCYGGDISRKKKLLQKQAKGKKRMKSVGTVDVPQEAFMAVLRLDQS | Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner. | B2J0M4 |
A8ARK8 | HLDD_CITK8 | ADP-L-glycero-beta-D-manno-heptose-6-epimerase | Citrobacter | MIIVTGGAGFIGSNIVKSLNDKGITDILVVDNLKDGTKFVNLVDLNIADYMDKEDFLIQIMAGEEFGDIEAVFHEGACSSTTEWDGKYMMDNNYQYSKELLHYCLERDIPFLYASSAATYGGRTSDFIESREYEKPLNVYGYSKFLFDEYVRQILPEASSQIVGFRYFNVYGPREGHKGSMASVAFHLNTQLNNGETPKLFEGSENFKRDFVYVGDVADVNLWFWENGVSGIFNLGTGRAESFQAVADAALAYHKKSDLEYIPFPEKLKGRYQAFTQADLTNLRAAGYDKPFKTVAEGVTEYMAWLNRDA | Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose. | A8ARK8 |
Q2UCB7 | MCA1B_ASPOR | Metacaspase-1B | Aspergillus subgen. Circumdati | MYHPNYNYPPPQPGWGGGYYPPPQQHQQQQQWSPPPPQPYYSNGYPPPSQSPHSYSPPQYPPHGQYEYGHHTPTPPPSSGSQYRSYHSHSPSWGQMPPRPPMEAQQFGKGAPSNYRFQYSACTGRRKALLIGINYAGQPNALRGCINDVTNMSTFLHERYGYRREDMVILTDDQQNPMSVPTKANILRAMQWLVKDAQRNDSLFIHFSGHGGRTPDLDGDEEDGYDDVIYPVDYRTAGHIVDDDMHAIMVRPLQPGVRLTAIFDSCHSGTALDLPYVYSTQGILKEPNLAKEAAQDLFSAITSYGQGDFASVAQTAIGFLKKAALGESARERTVKTKTSPADVVMFSGSKDTQTSADTFQDGQARGALSWAFIKTLQARPNQSYLQLLNSIRSELEGKYSQKPQLSCSHPLDTNLLFVM | Involved in cell death (apoptosis). | Q2UCB7 |
Q9Y7M3 | PIB2_SCHPO | Glutamine sensor pib2 | Schizosaccharomyces | MTTVHQLSGHGPLSRLNIYSGASPYTQRVRPSYELIEAPTRQATNGTGSVSGSPNSSSNSTPANQGSLPSHTNPQLYSSITRKERPELFRSYSGNPRLSKPYASSKLAASSRTASYQAMSYSVSPTSTNSSVATSLNYQSSRETGISKDHWKPDSDVSVCSFPSCSVRFGLFDRRHHCRRCGDIFCALHCDRNIPLTMDVKFCLAGSLYRSCVSCFYEYLKWKQSIDLASSNDITVIESTIAPQQATTHPPSQPKNAVSVPIPKMDSTDSKGELPSESLVLGTVPDNWVWSTF | Functions as an intracellular glutamine sensor that directly activates the TORC1 signaling pathway, to promote cell growth when glutamine is available. | Q9Y7M3 |
O07015 | RSBQ_BACSU | Sigma factor SigB regulation protein RsbQ | Bacillus | MNEAILSRNHVKVKGSGKASIMFAPGFGCDQSVWNAVAPAFEEDHRVILFDYVGSGHSDLRAYDLNRYQTLDGYAQDVLDVCEALDLKETVFVGHSVGALIGMLASIRRPELFSHLVMVGPSPCYLNDPPEYYGGFEEEQLLGLLEMMEKNYIGWATVFAATVLNQPDRPEIKEELESRFCSTDPVIARQFAKAAFFSDHREDLSKVTVPSLILQCADDIIAPATVGKYMHQHLPYSSLKQMEARGHCPHMSHPDETIQLIGDYLKAHV | Positive regulator required for energy stress activation of the sigma-B transcription factor. Could be required for RsbP phosphatase activity. | O07015 |
A3CQU5 | PURA_STRSV | IMP--aspartate ligase | Streptococcus | MTSVVVVGTQWGDEGKGKITDFLSANAEVIARYQGGDNAGHTIVIDGKKYKLHLIPSGIFFPEKISVIGNGMVVNPKSLVKELNYLHEEGVTTDNLRISDRAHVILPYHIELDRLQEEAKGDNKIGTTIKGIGPAYMDKAARVGIRIADLLDKDIFRERLERNLTEKNRLFEKLYDSTAISFDDIFEEYYEYGQQIKQYVTDTSVILNDALDQGKRVLFEGAQGVMLDIDQGTYPFVTSSNPVAGGVTIGSGVGPSKIDKVVGVCKAYTSRVGDGPFPTELFDEVGNRIRDIGHEYGTTTGRPRRVGWFDSVVMRHSRRVSGITNLSLNSIDVLSGLDTVKICVAYDLDGQRIDHYPASLEQLKRCKPIYEELPGWPEDITGVRSLEDLPENARNYVRRVSELVGVRISTFSVGPGREQTNILESVWSNL | Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. | A3CQU5 |
A1R1C6 | UREE_PAEAT | Urease accessory protein UreE | Paenarthrobacter | MIIEKILGNLHQQPDAYASHHKEKVVLPSTLLVKRIQRVTTDHGKELGIRLPAGTGDLRDGDILAIDQHNIIVVSVLPTDVLVIKARTIHEMGVVAHSLGNRHLQAQFFDGSSEYGAEVMVCQYDHTVEDYLKSVGVPYDRQERVMPVPFRHAEHSH | Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly. | A1R1C6 |
Q4WLM9 | TPS1A_ASPFU | UDP-glucose-glucosephosphate glucosyltransferase | Aspergillus subgen. Fumigati | MPSLENSTQNEARLLLVSNRLPITIKRSEDGKYDFSMSSGGLVSGLSGLSKSTTFQWYGWPGLEVPEEEIPVVKQRLKDEYGAIPVFIDDELADRHYNGFSNSILWPLFHYHPGEITFDESAWEAYKEANRLFAKAVAKEVQDGDLIWVHDYHLMLLPEMLREEIGDSKENVKIGFFLHTPFPSSEIYRILPVRNELLLGVLHCDLIGFHTYDYTRHFLSACSRLLGLATTPNGIEFQGKVIACGAFPIGIDPEKFQEGLKKEKVQKRIAQLEQKFQGVKLMVGVDRLDYIKGVPQKLHALEVFLSDHPEWVGKVVLVQVAVPSRQDVEEYQNLRAVVNELVGRINGKFGTVEFMPIHFLHKSVNFDELIALYAVSDACIVSSTRDGMNLVAYEYIASQQKRHGVLVLSEFAGAAQSLNGSIIINPWNTEELAGAYQEAVTMSDEQRALNFSKLDKYVNKYTSAFWGQSFVTELNRISAHSAGKFQSRKAKLPESADAEKPMNGSGESEESQTTQ | Synthase catalytic subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-alpha-D-glucose in a two step process . The disaccharide trehalose serves as a storage carbohydrate that is mobilized during conidial germination . Regulates the level of trehalose as a protectant for cell integrity during thermal and oxidative stress . | Q4WLM9 |
Q8NZ45 | HUTG_STRP8 | Formiminoglutamate hydrolase | Streptococcus | MLEDYYPSTTSYYHGGIDDDLYTAKWGMVMTFLDLNDSSLTPFEGTHFALIGFKSDKGVYINNGRVGAVESPAAIRTQLAKFPWHLGNQVMVYDVGNIDGPNRSLEQLQNSLSKAIKRMCDLNLKPIVLGGGHETAYGHYLGLRQSLSPSDDLAVINMDAHFDLRPYDQTGPNSGTGFRQMFDDAVADKRLFKYFVLGIQEHNNNLFLFDFVAKSKGIQFLTGQDIYQMGHQKVCRAIDRFLEGQERVYLTIDMDCFSVGAAPGVSAIQSLGVDPNLAVLVLQHIAASRKLVGFDVVEVSPPHDIDNHTANLAATFIFYLVQIMAQHS | Catalyzes the conversion of N-formimidoyl-L-glutamate to L-glutamate and formamide. | Q8NZ45 |
Q8LNW4 | FLOT2_ORYSJ | Nodulin-like protein 2 | Oryza sativa | MARFVVAGPSEYLAITGWGIDDVKLAKKAWVFAGQKCSRFDISPVNYEFNVEAMSSEKLAFNLPAVFTIGPKITPAPAPEVDGASNQRRVLMPESEEKLLLYAKLIAPHDHASNHVKQLVKGVIEGETRVLAASMTMEEIFQGTKKFKQEVFDQVQLDLNKFGLYIYNANVKQLVDEPGHEYFSYLGKKTQQEAANKAKVDVAEERMKGEVGAKEREGLTRQNAAKVDAETKVVSVRQQGIGLREEAKVKAEVQVYENEREAEIAAAQAGLAMKKAGWEKQSKVAQVEAVKAVAIREAELQMEVERKNALRLTEKLKAEQLSKATVQYETQVQESNAALYNRQKAADATLYEQVKSAEARKAQADAMFFEQKLAEDARLYAKQKEAEALAMVGKAKVEYVTSMLQALGGDYGALRDYLMIDGGMYQEMARVNASAVSGMQPKISIWSGADGAAGEAGAGAMQQVAGVYKMLPPLLSTVHEQTGMQPPAWMGSLPKDGAN | May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles. | Q8LNW4 |
Q9HA65 | TBC17_HUMAN | TBC1 domain family member 17 | Homo | MEGAGYRVVFEKGGVYLHTSAKKYQDRDSLIAGVIRVVEKDNDVLLHWAPVEEAGDSTQILFSKKDSSGGDSCASEEEPTFDPGYEPDWAVISTVRPQLCHSEPTRGAEPSCPQGSWAFSVSLGELKSIRRSKPGLSWAYLVLVTQAGGSLPALHFHRGGTRALLRVLSRYLLLASSPQDSRLYLVFPHDSSALSNSFHHLQLFDQDSSNVVSRFLQDPYSTTFSSFSRVTNFFRGALQPQPEGAASDLPPPPDDEPEPGFEVISCVELGPRPTVERGPPVTEEEWARHVGPEGRLQQVPELKNRIFSGGLSPSLRREAWKFLLGYLSWEGTAEEHKAHIRKKTDEYFRMKLQWKSVSPEQERRNSLLHGYRSLIERDVSRTDRTNKFYEGPENPGLGLLNDILLTYCMYHFDLGYVQGMSDLLSPILYVIQNEVDAFWCFCGFMELVQGNFEESQETMKRQLGRLLLLLRVLDPLLCDFLDSQDSGSLCFCFRWLLIWFKREFPFPDVLRLWEVLWTGLPGPNLHLLVACAILDMERDTLMLSGFGSNEILKHINELTMKLSVEDVLTRAEALHRQLTACPELPHNVQEILGLAPPAEPHSPSPTASPLPLSPTRAPPTPPPSTDTAPQPDSSLEILPEEEDEGADS | Probable GTPase-activating protein for Rab8; its transient association with Rab8 is mediated by OPTN. Inhibits Rab8-mediated endocytic trafficking, such as of transferrin receptor (TfR) and reduces Rab8 recruitnment to tubules emanating from the endocytic recycling compartment (ERC). Involved in regulation of autophagy. Mediates inhibition of autophagy caused by the OPTN variant GLC1E LYS-50; the function requires its catalytic activity, however, the involved Rab is not known. | Q9HA65 |
Q21EF2 | PYRE_SACD2 | Orotate phosphoribosyltransferase | Saccharophagus | MQAYQKDFIQLALKAQALKFGEFTLKSGRVSPYFFNAGQFQTGSALASLGRFYAQALVDAGVEFDMIFGPAYKGIPLATTTATALADHHQKDMPFAYNRKEVKAHGEGGTLVGAPIKGRVAIIDDVITAGTAVREVLSLIDAAGAKPAAIVVGLNRQEKGQGELSAIQELEQETGVPVISIINLNHVLQYLETQGDSENLAKVTAYRQQYGVE | Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). | Q21EF2 |
Q87SF9 | LPXC_VIBPA | UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase | Vibrio | MIRQRTLKEIVKTTGVGLHSGRKVTLTLRPAAANTGIIYRRTDVNPPVDFPADPASVRDTMLCTALVNDEGVRISTVEHLNAALAGMGIDNIIVEVDAPEIPIMDGSASPFVYLLQQAGIEMQNVPKRFIRIKKPVRFEDGDKWAEFVPFNGFRMDFEIDFNHPAIESDEQRLLFDFSSQGFVREISRARTFGFMRDIEYLQSQNLVLGGSFDNAIVLDDYRILNEEGLRFENEFVTHKVLDAIGDLYMCGHPIIGEFRAYKSGHGLNNQLLRAVLADQEAWEWTTFEEEVGSPVAFAEPNMVLA | 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. | Q87SF9 |
Q53T59 | H1BP3_HUMAN | HS1-binding protein 3 | Homo | MQSPAVLVTSRRLQNAHTGLDLTVPQHQEVRGKMMSGHVEYQILVVTRLAAFKSAKHRPEDVVQFLVSKKYSEIEEFYQKLSSRYAAASLPPLPRKVLFVGESDIRERRAVFNEILRCVSKDAELAGSPELLEFLGTRSPGAAGLTSRDSSVLDGTDSQTGNDEEAFDFFEEQDQVAEEGPPVQSLKGEDAEESLEEEEALDPLGIMRSKKPKKHPKVAVKAKPSPRLTIFDEEVDPDEGLFGPGRKLSPQDPSEDVSSVDPLKLFDDPDLGGAIPLGDSLLLPAACESGGPTPSLSHRDASKELFRVEEDLDQILNLGAEPKPKPQLKPKPPVAAKPVIPRKPAVPPKAGPAEAVAGQQKPQEQIQAMDEMDILQYIQDHDTPAQAAPSLF | May be a modulator of IL-2 signaling. | Q53T59 |
Q5AU92 | AGALC_EMENI | Melibiase C | Aspergillus subgen. Nidulantes | MFRSTATVAAATAMGLLTATGHGSLAIAQGTTGSNAVVVDGTNFALNGASMSYVFHANSTTGDLVSDHFGATISGAIPAPKEPAVNGWVGMPGRIRREFPDQGRGDFRIPAVRIRQTAGYTVSDLQYQGHEVVDGKPALPGLPATFGEAGDVTTLVVHLYDNYSAVAADLSYSVFPEFDAVVRSVNVTNKGKGNITIENLASLSVDFPLEDLDLVSLRGDWAREANRERRRVEYGIQGFGSSTGYSSHLHNPFFALVHPSTTESQGEAWGFNLVYTGSFSAQVEKGSQGLTRALIGFNPDQLSWNLGPGETLTSPECVSVYSKDGIGGMSRKFHRLYRKHLIRSKFATSDRPPLLNSWEGVYFDFNQSSIETLAEQSAALGIRLFVMDDGWFGDKYPRTSDNAGLGDWTPNPDRFPNGLEPVVEEITNLTVNDTSAEKLRFGIWVEPEMVNPNSSLYREHPDWALHAGAYARTERRNQLVLNLALPEVQEYIIDFMTDLLNSADISYIKWDNNRGIHEAPSPSTDHEYMLGVYRVFDTLTARFPDVLWEGCASGGGRFDAGVLHYFPQIWTSDNTDGVDRVTIQFGTSLAYPPSAMGAHLSAVPNHQTGRTVPLEFRAHVAMMGGSFGLELDPATLQDDPDVPELIQMAEKVNPLVLNGDLYRLRLPEESQWPAALFVAEDGSQAVLFYFQLSPNVNHAAPWVRLQGLDPEASYTVDGDKTYTGATLMNLGLQYTFDTEYGSKVVFLERQ | Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides. Active on paranitrophenyl-alpha-galactoside, raffinose, locust bean gum and gum guar. | Q5AU92 |
B7LEY2 | FUCI_ECO55 | FucIase | Escherichia | MKKISLPKIGIRPVIDGRRMGVRESLEEQTMNMAKATAALLTEKLRHACGAAVECVISDTCIAGMAEAAACEEKFSSQNVGLTITVTPCWCYGSETIDMDPTRPKAIWGFNGTERPGAVYLAAALAAHSQKGIPAFSIYGHDVQDADDTSIPADVEEKLLRFARAGLAVASMKGKSYLSLGGVSMGIAGSIVDHNFFESWLGMKVQAVDMTELRRRIDQKIYDEAELEMALTWADKNFRYGEDENNKQYQRNAEQSRAVLRESLLMAMCIRDMMQGNSKLADIGRVEESLGYNAIAAGFQGQRHWTDQYPNGDTAEAILNSSFDWNGVREPFVVATENDSLNGVAMLMGHQLTGTAQVFADVRTYWSPEAIERVTGHKLDGLAEHGIIHLINSGSAALDGSCKQRDSEGNPTMKPHWEISQQEADACLAATEWCPAIHEYFRGGGYSSRFLTEGGVPFTMTRVNIIKGLGPVLQIAEGWSVELPKDVHDILNKRTNSTWPTTWFAPRLTGKGPFTDVYSVMANWGANHGVLTIGHVGADFITLASMLRIPVCMHNVEETKVYRPSAWAAHGMDIEGQDYRACQNYGPLYKR | Converts the aldose L-fucose into the corresponding ketose L-fuculose. | B7LEY2 |
Q2IV75 | GUAA_RHOP2 | Glutamine amidotransferase | Rhodopseudomonas | MTAPSTPSASSVVPSGADTSPHVAAIHEKILIVDFGSQVTQLIARRVREEGVYSEIVPFQKAEAAFAEMKPKAVILSGGPASVLDADAPAAPMAILEAGVPVLGICYGEQTLAKQLGGTVEAGHHREFGRATIEITDDCALFDGVWQKGGTYDVWMSHGDRVTKLPDGFRGVAKAPGSPISVIADDKRKFYATQFHLEVVHTPDGAKILRNFVRKVAGLTGDWTMRAFREEAIEKIRAQVGTGKVICGLSGGVDSAVAAVLIHEAIGDQLTCVFVDHGMLRKDEAKTVVDLFRHHYNIPLVHVDASETFLGALSGVTDPEQKRKIIGKLFIDVFDAEAKVVGGADYLAQGTLYPDVIESVSFTGGPSVTIKSHHNVGGLPERMNMKLVEPLRELFKDEVRALGRELGLPEIFVGRHPFPGPGLAIRCPGEITAEKLDILRNADAVYIDQIRKAGLYDAIWQAFAVLLPVKTVGVMGDGRTYEYVVGLRAVTSTDGMTADYYPFDMAFLGATATRIINEVKGVNRVVYDVTSKPPGTIEWE | Catalyzes the synthesis of GMP from XMP. | Q2IV75 |
P21841 | PSPC_MOUSE | SP5 | Mus | MDMSSKEVLMESPPDYSAGPRSQFRIPCCPVHLKRLLIVVVVVVLVVVVIVGALLMGLHMSQKHTEMVLEMSIGAPETQKRLAPSERADTIATFSIGSTGIVVYDYQRLLTAYKPAPGTYCYIMKMAPESIPSLEAFARKLQNFRAKPSTPTSKLGQEEGHDTGSESDSSGRDLAFLGLAVSTLCGELPLYYI | Pulmonary surfactant associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces. | P21841 |
Q5HPC6 | ODO1_STAEQ | Alpha-ketoglutarate dehydrogenase | Staphylococcus | MTKNKKEFTEAPVNFGANLGLMLDLYDDYLQDPSSVPEDLQVLFSTIKTGEAHIEAKPTTDGGGSQAGDSTIKRVMRLIDNIRQYGHLKADIYPVNPPERQNVPKLEIEDFDLDKETLEKISSGIVSEHFKDIYDNAYDAIVRMERRYKGPIAFEYTHINNNKERVWLKRRIETPYKASLNDNQKKELFKKLAHVEGFEKYLHKNFVGAKRFSIEGVDTLVPMLQHTITLAGNEGIKNIQIGMAHRGRLNVLTHVLEKPYEMMISEFMHTDPMKFLPEDGSLELTSGWTSDVKYHLGGVKTTNSYGIEQRISLANNPSHLEIVAPVVAGKTRAAQDNTHQVGGPSTDFHKAMPIIIHGDAAYPGQGINFETMNLGSLKGYSTGGSLHIITNNRIGFTTEPFDGRSTTYSSDVAKGYDVPILHVNADDVEATIEAIEIAMEFRKEFHKDVVIDLVGYRRYGHNEMDEPSITNPVPYQNIRKHDSVEILYGKKLVDEGIISEDEMNEVIDSVQKEMRTAHDKIDKNDKMNNPDMEKPESLQLPLQSDTKDFSFDHLKEINDAMLDYPKDFHVLKKLNKVLEKRREPFEKEGGLVDWAQAEQLAFATILQDGTSIRLTGQDSERGTFSHRHAVLHDEENGNTFTPLHHVPQQQATFDIHNSPLSEAAVVGFEYGYNVENKGNFNIWEAQYGDFSNMSQMMFDNFLSSSRAKWGERSGLTLFLPHAFEGQGPEHSSARLERFLQLAAENNSTVVNLSSASNYFHLLRAQAASLDTLEMRPLIVMSPKSLLRNKTVAKPIDEFTSGGFKPIITEDIDEQKVKKVILASGKMYIDLKEYLAKNPNDSILLIAVERLYPFPEEEIKEVLKSLPHLENVSWVQEEPKNQGAWLFVYPYLKALVANKYDLTYHGRIQRAAPAEGDGEIHKLVQTKIIESSINN | E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2). | Q5HPC6 |
Q9VRX2 | VPS8_DROME | Vacuolar protein sorting 8 | Sophophora | MSELKAPSLQSLLESERGSTDSLLAESLQLDFEDLDDAEFAIPPTDVLPTLEAVLSEFEADSDVASEFGMPVPHATPTPSIGEDSTIRTDGRGGGGSIMRYTLLHGISAQLSSAAERVNAGAASSCAVAAFIAIGTSHGHILNFDVTQTLRWAHQDKHGQGAVASLAFNADSTRLLAGFSRGLVAMLDTHTGDVLRELFDVITPNTGVLHVKWTSRSSLALCADAGGSVWSLSFTRKLGIRGCQSRCLFSGARGEVCAVEPLIMDSQGRHELDQYCIVALATLSKYFIVTVRPRLRVIKYHVLQGPPDCLPLLAWHLVLIQAADTSRSVDPVIVVGRGNQLFFHQLFVSNGRITLLYLRHVQLQGSLLSAHWLGPKCVASLDTAEILHLVDVRSSKELECMDMANAGLVYGSAQFKGLATGGNVSPAFALAGSNACYNSVVSRGTQLYVLGARSLHIIGVRTWSERISFLVKHHRWQEACQLALDGYIASVDRPRKRAQAKERIIMLFKEYIANSARAPEYCLGAIVNCLITVGELDLLWTQLWEKLHNSSTELFLQHISEHIEKETIHSVNPVISQALVDYWLEHSPAKLEQLILKLDWMCLDLNQVLKAVKKHRLFRAQIYLNTQALNDYTAALTELLPLVTPDETDLGNCLLVYVSSCLAGREYPSGEIPVELVHQVKHDVLRCLTSQHSKENAGDELPYPYLRALLKFDTRETLNVISLAFQEREFSNELGISHRKRIINLLLEIMSPENATWAEIGCLLNFIAQQISMQCLPRDRQLLERVLSHLAQEEIANESSRQHSERENAWHELLSSNCLAEISSDEEQLRLAEKAKCYCVVEYLLEKLERYDTILDSYIRNEARHETMFAYMERHVASPKRSIFRQLKRNLRELLTINAKETTRLLSLHYPEKINELLDNLRREENLLYLFLKCLNDRKSELEASQMELLLELYCKMESSSTVEEFLRSNSGYRLENAIAIAESHHLNRSVIYLYEKQESYAKAFELSMELLKSAAGEEAAKEAQTISALLARSVETLPAQELERCWFALLQYILPHQELQSITKSLLHEASQHIDLHNLVQLIMNTHNVSTSFGDIKDLLMGMLDSSRHKTEALRASAGALCQDLHLKFVKRYQHAHRGLWVTTTKCSMCRQRLYDHSQVLIFGGCGHGIHEQCMEESETQFEECPRCFTAIPDQSIGLPRPNKNLISISSSLEMGALQLKAPPRRFI | Plays a role in vesicle-mediated protein trafficking to lysosomal compartments and in membrane docking/fusion reactions of late endosomes/lysosomes probably as part of the class C core vacuole/endosome tethering (CORVET) complex. Specifically required for endocytic trafficking in a subset of cells, such as hemocytes and nephrocytes, which are highly active in endocytosis. | Q9VRX2 |
Q43714 | DCS3_GOSAR | (+)-delta-cadinene synthase isozyme A | Gossypium | MASQASQVLASPHPAISSENRPKADFHPGIWGDMFIICPDTDIDAATELQYEELKAQVRKMIMEPVDDSNQKLPFIDAVQRLGVSYHFEKEIEDELENIYRDTNNNDADTDLYTTALRFRLLREHGFDISCDAFNKFKDEAGNFKASLTSDVQGLLELYEASYMRVHGEDILDEAISFTTAQLTLALPTLHHPLSEQVGHALKQSIRRGLPRVEARNFISIYQDLESHNKSLLQFAKIDFNLLQLLHRKELSEICRWWKDLDFTRKLPFARDRVVEGYFWIMGVYFEPQYSLGRKMLTKVIAMASIVDDTYDSYATYDELIPYTNAIERWDIKCMNQLPNYMKISYKALLNVYEEMEQLLANQGRQYRVEYAKKAMIRLVQAYLLEAKWTHQNYKPTFEEFRDNALPTSGYAMLAITAFVGMGEVITPETFKWAASDPKIIKASTIICRFMDDIAEHKFNHRREDDCSAIECYMKQYGVTAQEAYNEFNKHIESSWKDVNEEFLKPTEMPTPVLCRSLNLARVMDVLYREGDGYTHVGKAAKGGITSLLIDPIQI | Responsible for the cyclization of trans,trans-farnesyl diphosphate (FPP) to (+)-delta cadinene. | Q43714 |
Q20Z46 | NUOI2_RHOPB | NDH-1 subunit I 2 | Rhodopseudomonas | MIGWLEALLRVGRKLAAKTVTVQYPEVKPQLPPRSRGRIVLTRDPDGQERCVACNLCAVACPVGCIDLSKAVAEDGRWYPEHFRINFARCIFCGYCEEACPTAAIQLTPDFELSEWRRDALVYDKKDLLIAGEGKVRGYRYWSVAGKAITGKDKGDAEHEAPPVDLKGLRP | 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. | Q20Z46 |
P42636 | TPM1_BIOGL | Tropomyosin I | Biomphalaria | MDAIKKKMLAMKMEKENAIDRAEQMEQKLRDVEETKNKLEEEFNNLQNKFSNLQNDFDTANEGLTEAQTKLEASEKHVAELESDTAGLNRRIQLLEEDLERSEERLQSATEKLEEASKAADESERGRKVLESRSLADDERLDGLEAQLKEAKYIAEDAERKYDEAARKLAITEVDLERAEARLEAAEAKVWELDEELHIVGNNIKTLSIQNDQASQREDSYQETIRDLTQRLKDAENRATEAERTVSKLQKEVDRLEDELLAEKERYKSISDELDSTFAELAGY | Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction. | P42636 |
Q5VWK5 | IL23R_HUMAN | Interleukin-23 receptor | Homo | MNQVTIQWDAVIALYILFSWCHGGITNINCSGHIWVEPATIFKMGMNISIYCQAAIKNCQPRKLHFYKNGIKERFQITRINKTTARLWYKNFLEPHASMYCTAECPKHFQETLICGKDISSGYPPDIPDEVTCVIYEYSGNMTCTWNAGKLTYIDTKYVVHVKSLETEEEQQYLTSSYINISTDSLQGGKKYLVWVQAANALGMEESKQLQIHLDDIVIPSAAVISRAETINATVPKTIIYWDSQTTIEKVSCEMRYKATTNQTWNVKEFDTNFTYVQQSEFYLEPNIKYVFQVRCQETGKRYWQPWSSLFFHKTPETVPQVTSKAFQHDTWNSGLTVASISTGHLTSDNRGDIGLLLGMIVFAVMLSILSLIGIFNRSFRTGIKRRILLLIPKWLYEDIPNMKNSNVVKMLQENSELMNNNSSEQVLYVDPMITEIKEIFIPEHKPTDYKKENTGPLETRDYPQNSLFDNTTVVYIPDLNTGYKPQISNFLPEGSHLSNNNEITSLTLKPPVDSLDSGNNPRLQKHPNFAFSVSSVNSLSNTIFLGELSLILNQGECSSPDIQNSVEEETTMLLENDSPSETIPEQTLLPDEFVSCLGIVNEELPSINTYFPQNILESHFNRISLLEK | Associates with IL12RB1 to form the interleukin-23 receptor. Binds IL23 and mediates T-cells, NK cells and possibly certain macrophage/myeloid cells stimulation probably through activation of the Jak-Stat signaling cascade. IL23 functions in innate and adaptive immunity and may participate in acute response to infection in peripheral tissues. IL23 may be responsible for autoimmune inflammatory diseases and be important for tumorigenesis. | Q5VWK5 |
B1AJD7 | RS4_UREP2 | 30S ribosomal protein S4 | Ureaplasma | MSRYTGSIYKKSRRLGFSLLENNKEFNSGKKRTYGPGQHGNKKVKLSNYGQQLVEKQKLMFLYGLNDRQFRRLYRVALGRPGVLTLNLLQVLESRLDSLVYRAGFAPTRRAARQLVNHSHVLVNNKKVNIPSALVEVGSTIALKAKSLEIPLIKNTLNKPADFIELIDKEKKVAKLARLPERNELPADVNEAYVVEWYNRLM | With S5 and S12 plays an important role in translational accuracy. | B1AJD7 |
Q9ZL09 | DER_HELPJ | GTP-binding protein EngA | Helicobacter | MNTSHKTLKTIAILGQPNVGKSSLFNRLARERIAITSDFAGTTRDINKRKIALNGHEVELLDTGGMAKDALLSKEIKALNLKAAQMSDLILYVVDGKSIPSDEDLKLFREVFKTNPNCFLVINKIDNDKEKERSYAFSSFGTPKSFNISVSHNRGISALIDAVLNALNLNQIIEQDLDADILESLETPNNALEETKEEEIIQVGIIGRVNVGKSSLLNALTKKERSLVSSVAGTTIDPIDETILIGDQKICFVDTAGIRHRGKILGIEKYALDRTQKALEKSHIALLVLDVSAPFVELDEKISSLADKHSLGIILILNKWDIRYAPYEEIMATLKRKFRFLEYAPVITTSCLKARHIDEIKHKIIEVYECFSKRIPTSSLNSVIFQATQKHPLPSDGGKLVKVYYATQFATKPPQISLIMNRPKALHFSYKRYLINTLRKEFNFLGTPLILNAKDKKSVQQN | GTPase that plays an essential role in the late steps of ribosome biogenesis. | Q9ZL09 |
A5UUP4 | LEUD_ROSS1 | Isopropylmalate isomerase | Roseiflexus | MQPISVITGRIVALPVQDIDTDQIIPARYLKVTDKSGLAEGLFYAWRFDADGKPNPDFVLNRPETQGATILVAGRNFGCGSSREHAPWALLGYGFKAVISPYFADIFRNNALKNGLLTVQVDDETYQQLVSLFDEDPTTTVTIDLAAQTVTLPDGRGVHFPIDPFTKHCLLHGVDQMGFLLNEEAAISAYEASRPARVVTTARS | Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. | A5UUP4 |
C5CGH6 | RS11_KOSOT | 30S ribosomal protein S11 | Kosmotoga | MARNRSSRTKKRKKLNIDRGVVHIKSTFNNTIITLSDLDGNTILWASGGTVGYSGSKKSTPYAAQLAADKIAKEALKLGLTRVSIEVKGPGAGREAAIRTIQAAGLVVDSIKDITPIPHNGCRPRRRRRV | Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome. | C5CGH6 |
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