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 |
|---|---|---|---|---|---|---|
Q31Z75 | GLPB_SHIBS | Anaerobic glycerol-3-phosphate dehydrogenase subunit B | Shigella | MRFDTVIMGGGLAGLLCGLQLQKHGLRCAIVTRGQSALHFSSGSLDLLSHLPDGQPVADIHSGLESLRQQAPAHPYSLLGPQRVLDLACQAQALIAESGAQLQGSVELAHQRITPLGTLRSTWLSSPEVPVWPLPAKKICVVGISGLMDFQAHLAAASLHELDLSVETAEIELPELDVLRNNATEFRAVNIARFLDNEENWPLLLDALIPVANTCEMILMPACFGLADDKLWRWLNEKLLCSLMLLPTLPPSVLGIRLQNQLQRQFVRQGGVWMPGDEVKKVTCKNGVVNEIWTRNHADIPLRPHFAVLASGSFFSGGLVAERNGIREPILGLDVLQTATRGEWYKGDFFAPQPWQQFGVTTDETLRPSQAGQTIENLFAIGSVLGGFDPIAQGCGGGVCAVSALHAAQQIAQRAGGQQ | Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses fumarate or nitrate as electron acceptor. | Q31Z75 |
Q0VS73 | GATB_ALCBS | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B | Alcanivorax | MSWEIVIGLEVHVQLNTASKLFSGSKLSTGAEPNTQASLVDLGLPGTLPVVNREAVRKAALFGLAIDADICRHSVFERKNYFYPDLPKGYQTTQLAEPIVGAGTVEIQLDNGEKKSIRIHHAHLEEDAGKSLHEDFHGMTGIDLNRAGTPLIEIVSEPDMANAEEAVAFARKLHAIVTSIGICDGDMSQGNMRFDVNISVRKPGEPLGTRTETKNLNSFRFMEKAIALEVERQIDVLEDGGEIVQETRLYNGDTHTARSMRSKEDANDYRYFPCPDLLPVAITDADIEELKAAMPELPDSRKARFTNDYQLSEYDADLLSGSIATAAFFEAAAKSGGDAKLAANWVMGELAAKLNAEEKSITDSPVSAEQLGQLIARLKDGTISSKIAKQVFEACWAGEGNPDEIIEAKGLKQMSDTGELEKIVDDIIANNAAQADDYRNSDDAKKKKKIGFFVGQAMKATQGKANPQQLNKLLQEKLQ | Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln). | Q0VS73 |
Q79FL8 | PG30_MYCTU | PE-PGRS family protein PE_PGRS30 | Mycobacterium tuberculosis complex | MSFLLVEPDLVTAAAANLAGIRSALSEAAAAASTPTTALASAGADEVSAAVSRLFGAYGQQFQALNARAATFHAEFVSLLNGGAAAYTGAEAASVSSMQALLDAVNAPTQTLLGRPLIGNGADGVAGTGSNAGGNGGPGGILYGNGGNGGAGGNGGAAGLIGNGGAGGAGGAGGAGGAGGAGGTGGLLYGNGGAGGNGGSAAAAGGAGGNALLFGNGGNGGSGASGGAAGHAGTIFGNGGNAGAGSGLAGADGGLFGNGGDGGSSTSKAGGAGGNALFGNGGDGGSSTVAAGGAGGNTLVGNGGAGGAGGTSGLTGSGVAGGAGGSVGLWGSGGAGGDGGAATSLLGVGMNAGAGGAGGNAGLLYGNGGAGGAGGNGGDTTVPLFDSGVGGAGGAGGNASLFGNGGTGGVGGKGGTSSDLASATSGAGGAGGAGGVGGLLYGNGGNGGAGGIGGAAINILANAGAGGAGGAAGSSFIGNGGNGGAGGAGGAAALFSSGVGGAGGSGGTALLLGSGGAGGNGGTGGANSGSLFASPGGTGGAGGHGGAGGLIWGNGGAGGNGGNGGTTADGALEGGTGGIGGTGGSAIAFGNGGQGGAGGTGGDHSGGNGIGGKGGASGNGGNAGQVFGDGGTGGTGGAGGAGSGTKAGGTGSDGGHGGNATLIGNGGDGGAGGAGGAGSPAGAPGNGGTGGTGGVLFGQSGSSGPPGAAALAFPSLSSSVPILGPYEDLIANTVANLASIGNTWLADPAPFLQQYLANQFGYGQLTLTALTDATRDFAIGLAGIPPSLQSALQALAAGDVSGAVTDVLGAVVKVFVSGVDASDLSNILLLGPVGDLFPILSIPGAMSQNFTNVVMTVTDTTIAFSIDTTNLTGVMTFGLPLAMTLNAVGSPITTAIAFAESTTAFVSAVQAGNLQAAAAALVGAPANVANGFLNGEARLPLALPTSATGGIPVTVEVPVGGILAPLQPFQATAVIPVIGPVTVTLEGTPAGGIVPALVNYAPTQLAQAIAP | Mediates suppression of pro-inflammatory immune response in macrophages via modulation of host cytokine response . Required for full virulence. Involved in inhibition of phago-lysosome fusion . | Q79FL8 |
Q5G290 | PA2A6_NAJSG | Phospholipase A2 molecule B | Naja | SNRPMPLNIKQFNNMIQCTVPARSWWDFADYGCYCGSGSGSPVDDLDRCCQVHDNCYNAGGGVTGCAPKSKTYTYECSQGTLTCSGENSACAATVCDCDRLAAICFAGAPYNDNNYNIDLKSRCQ | PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. | Q5G290 |
A9G7Z8 | Y5766_SORC5 | Nucleotide-binding protein sce5766 | Sorangium | MSNGGDQQQHGLLGPDGAPGRVVVVTGLSGAGKSTALHALEDLGFFCVDNLPTSLVQPAVEACESGGITRIGLGIDVRVGSFLAGATAALDSIRTGRDVVILFLDASDETLLRRFSETRRPHPLTTGGSGAIAMLDGVLLERERLASLRARATIELDTTRLSTHDLRRVVIERLRPARVEVPRMSTRFVSFGYKYGIPLDADLLFDVRFLDNPYFVHGLRELTGNDEPVREYILKNPDALEFICRTEQLLSFCMPRYASEGKSYLTVGIGCTGGRHRSVVLTNALSDSLRRKTGLPITVVHRDVARVSTSGVPSGVGEGMAGAPGVDLRLAQPGATPSEPRPASDTSVTGGER | Displays ATPase and GTPase activities. | A9G7Z8 |
Q9SZD4 | PRS4A_ARATH | Regulatory particle triple-A ATPase subunit 2a | Arabidopsis | MGQGPSGGLNRQGDRKPDGGDKKEKKFEPAAPPARVGRKQRKQKGPEAAARLPTVTPSTKCKLRLLKLERIKDYLLMEEEFVANQERLKPQEEKAEEDRSKVDDLRGTPMSVGNLEELIDENHAIVSSSVGPEYYVGILSFVDKDQLEPGCSILMHNKVLSVVGILQDEVDPMVSVMKVEKAPLESYADIGGLEAQIQEIKEAVELPLTHPELYEDIGIKPPKGVILYGEPGTGKTLLAKAVANSTSATFLRVVGSELIQKYLGDGPKLVRELFRVADDLSPSIVFIDEIDAVGTKRYDAHSGGEREIQRTMLELLNQLDGFDSRGDVKVILATNRIESLDPALLRPGRIDRKIEFPLPDIKTRRRIFQIHTSKMTLSEDVNLEEFVMTKDEFSGADIKAICTEAGLLALRERRMKVTHPDFKKAKEKVMFKKKEGVPEGLYM | The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (Probable). Interacts with transit peptides of proteins targeted to the chloroplast, and may be involved in the degradation of unimported plastid protein precursors . Is required for the maintenance of postembryonic root and shoot meristems . Has a specific role in the regulation of organs size . Acts redundantly with RPT2B in the regulation of gametogenesis . With RPT2B plays a critical role in 26S proteasome assembly . Acts as an upstream signaling component for inducing both defense and morphological phenotypes in the constitutive active uni-1D mutant . Acts as negative regulator of endoreduplication in trichome cells . May function after the completion of the third endoreduplication step (8C to 16C) mediated by RHL1 . Acts as negative regulator of transcriptional gene silencing (TGS) at specific endogenous genes through DNA methylation . Promotes post-transcriptional gene silencing (PTGS) by limiting the degradation of transgene aberrant RNAs by the RNA quality control (RQC) machinery, thus favoring their entry into cytoplasmic siRNA bodies where they can trigger PTGS . Involved in tolerance to zinc deficiency, possibly through alleviation of oxidative stresses or processing of poly-ubiquitinated proteins . Required for resistance to the fungal pathogen Golovinomyces cichoracearum . | Q9SZD4 |
Q31AR4 | TPIS_PROM9 | Triose-phosphate isomerase | Prochlorococcus | MRKSVIAGNWKMHMTCAEAKSYLEEFIPLIKNIRDDRKVVIAPPFTAISTFSKHSDFDYLDISSQNIHWEDEGAFTAEISPKMLIEHGVSYAIVGHSEPRKYFSESDEQINKRAVFAQCSGLTPIVCVGETLEQRERGEADRVITRQVEQGLENTDPSNLIVAYEPIWAIGTGKTCEAKDANNICSLIRKLIGFDDVIIQYGGSVKPNNIDEIMSMSDIDGVLVGGASLDPNSFARIANYQ | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | Q31AR4 |
Q9CZD5 | IF3M_MOUSE | Translation initiation factor IF-3, mitochondrial | Mus | MAVLLMRLMLQTTKLDHNLIGRCLQRHAVKPDPAQLSLSASTPKLLYLTSAKGFSTAGDPQGERKQKRRDAFSNTGRKISERIIRVLDEKGMDLGMMHRADVIRLMNKQDLRLVQRNTSSEPPEYQLMTGEQIHQERLKLREQEKAKPKTGPTMTKELVFSSNIGQHDLDTKSKQIQQWIEKKYHVQVTIKRRKDAEQSEEETEEIFNQILQTMPDIATFSSRPKAIRGGTASMCVFRHLSKKEEKAYRESQESQRRDTLSKDDDGNSKESDVVCQ | IF-3 binds to the 28S ribosomal subunit and shifts the equilibrum between 55S ribosomes and their 39S and 28S subunits in favor of the free subunits, thus enhancing the availability of 28S subunits on which protein synthesis initiation begins. | Q9CZD5 |
Q8YG94 | RSMA_BRUME | S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase | Brucella | MSIDSLPPLREVIERHDLMPKKSLGQNFLFDLNLTSKIARQAGDLRDQPVIEVGPGPGGLTRALLAQGAYVTAIERDDRCLEALAEIAAHYPGRLRIIAGDALEQDFTALFPEGPKPRIVANLPYNVGTQLLLNWLLVEPWPPFYSSMTLMFQREVAERIVAKLDSDHYGRLGVLAGWRTQAKIAFDVPPQAFTPPPKVMSSVVHIVPRETPLPCRAEALGQITQAAFGQRRKMLRQSLKSIGGAALLEKTGIDGTRRAETLSVEEFVALANACLP | Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits. | Q8YG94 |
A7MB89 | FEM1C_BOVIN | FEM1-gamma | Bos | MDLKTAVFNAARDGKLRLLTKLLASKSKEEVSSLISEKTNGATPLLMAARYGHLDMVEFLLEQCSASIEVGGSVNFDGETIEGAPPLWAASAAGHLKVVQSLLNHGASVNNTTLTNSTPLRAACFDGHLEIVKYLVEHKADLEVSNRHGHTCLMISCYKGHKEIAQYLLEKGADVNRKSVKGNTALHDCAESGSLDIMKMLLMYCAKMEKDGYGMTPLLSASVTGHTNIVDFLTHHAQTSKTERINALELLGATFVDKKRDLLGALKYWKKAMNMRYSDRTNIISKPVPQTLIMAYDYAKEVNSAEELEGLIADPDEMRMQALLIRERILGPSHPDTSYYIRYRGAVYADSGNFKRCINLWKYALDMQQNNLDPLSPMTASSLLSFAELFSFMLQDRAKGLLGTTVTFDDLMGILCKSVLEIERAIKQTQCPADPLQLNKALSIILHLICLLEKVPCTLEQDHFKKQTIYRFLKLHPRGKNNFSPLHLAVDKNTTCVGRYPVCKFPSLQVTAILIECGADVNVRDSDDNSPLHIAALNNHPDIMNLLIKSGAHFDATNLHKQTASDLLDEKEIAKNLIQPINHTTLQCLAARVIVNHRIYYKGHIPEKLETFVSLHR | Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms. The CRL2(FEM1C) complex specifically recognizes proteins with an arginine at the C-terminus: recognizes and binds proteins ending with -Lys/Arg-Xaa-Arg and -Lys/Arg-Xaa-Xaa-Arg C-degrons, such as SIL1 or OR51B2, leading to their ubiquitination and degradation. The CRL2(FEM1C) complex mediates ubiquitination and degradation of truncated MSRB1/SEPX1 selenoproteins produced by failed UGA/Sec decoding. | A7MB89 |
A5VJ98 | UVRC_LIMRD | Excinuclease ABC subunit C | Limosilactobacillus | MASEHLEHKLALLPDKPGCYLMKNINDQIIYVGKAKNLKNRVRSYFKSSHTGKVAKMVSEVADFETIVTSTNKESFLLEITLIQKHQPYFNIKLKKGTGYPYIKITNERDPQIKIVSKIKKDGGYYFGPYPNVYAAEETMHFIQKVYPLRRCNGYQGRPCLYYHMGQCLGACFKEVPKSDYEEQIKKIKSFLSGNTATVKRQLTKKMQRAAENMEFERAAEIRDQLHYIEVTVEKQKIISNDKTPRDLFNFYMDKGWLSIQIFFIRQARLMKREKRLFPIVDTAVEEMTSFILQFYNRRNNILPHEILLPKGLPNKEISEILGVPVRTPVRGEKRDLLAMAHENAQLSLDEKFRLLEMDQSKTTGAMKEITDALGLPEGHRIEAFDHSHIQGADPVSAMVVFINGEPAKNFYRKYKLKTVINHADEAASTREVIRRRYSRLLKENKPMPDMIFMDGGEIQMDAAKDVLENELGLEIPVVGMVKNDKHQTADLLFGDDDHHINLNPRSQGFYLVQRIQDEVHRFAITFHRRVHTKHSLSSRLDEIKGVGPRTRTKLLKKYGSITKIAQASVDEIHSLGINRPTAQLIKVSLQKNAEVAKGSSHD | The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. | A5VJ98 |
Q8BUM3 | PTN7_MOUSE | Hematopoietic protein-tyrosine phosphatase | Mus | MVQACEGRSRAQLPTLSLGADMTQPPPTKAPAKKHVRLQERRGSSVALMLDVQSLGTVEPICSVNTPREVTLHFLRTAGHPLTRWTLQHQPPSPKQLEEEFLKIPSNFVNPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDSDYINANYIRGYDGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLREGKEKCVHYWPTEEEAYGPFQIRIQDMKEHPEYTVRQLTIQHQQECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLALYAAQLPPEPNP | May play a role in the regulation of T and B-lymphocyte development and signal transduction. | Q8BUM3 |
O07592 | YHDW_BACSU | Putative glycerophosphodiester phosphodiesterase YhdW | Bacillus | MYIIAHRGASGYAPENTIAAFDLAVKMNADMIELDVQLTKDRQIVVIHDDRVDRTTNGSGFVKDFTLEELQKLDAGSWYGPAFQGERIPTLEAVLKRYHKKIGLLIELKGHPSQVGIEEEVGQLLGQFSFSINNIVQSFQFRSVQRFRELYPSIPTAVITRPNFGMLSRNQMKAFRSFANYVNIKHTRLNRLMIGSINKNGLNIFAWTVNNQKTAAKLQAMGVDGIVTDYPDFIIKDGKHENI | Glycerophosphoryl diester phosphodiesterase hydrolyzes deacylated phospholipids to sn-glycerol 3-phosphate (G3P) and the corresponding alcohols. | O07592 |
A6SVP5 | ILVD_JANMA | Dihydroxy-acid dehydratase | Janthinobacterium | MAFNRRSKNITQGISRSPNRSMYYAMGYEKEDFDKPMVGVANGHSTITPCNSGLQKLADIAIKTIKDSGGNPQVFGTPTISDGMSMGTEGMKYSLISREVIADCIETAVNGQWMDGVLVIGGCDKNMPGGMIAMLRTNVPSIYVYGGTIKPGNWKGKDLTIVSAFEAVGEFTAGRMSQEDFDGIERNACPSAGSCGGMYTANTMSSSFEALGLALPYSSTMANPDDEKVGSAAESARVLIEAIKNDLKPRDIVTRKAIENAVAVIMATGGSTNAVLHFLAIAHAAEVEWTIDDFERMRKKVPVICDLKPSGKYVATDLHKAGGIPQVMKVLLDAGLLHGDCMTITGQTVAEALAHIPSVPRADQHVIHPIKDALYEQGHLAILKGNLSPEGCVAKITGLKNPVITGPARVFDDEYSAMDAIMANKIVAGDVLVMRYLGPKGGPGMPEMLAPTSALVGQGLGESVGLITDGRFSGGTWGMVVGHVSPEAFVGGLIGLVEEGDSVTIDAHKLLIQLNVPEEEIARRRANWKQPAPRYTRGVLSKFAALASSASKGAVTG | 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. | A6SVP5 |
Q9FMZ0 | BKI1_ARATH | BRI1 kinase inhibitor 1 | Arabidopsis | METNLQQVKNSSQTFSEKQNPKQEASPSPISSTCSSPSHDFSFTISLQPLSSSSKHISPTLRSPSKTTSSYQQTDPFAVDLSPADEIFFHGHLLPLHLLSHLPVSPRTSTGSYNDGFTLPVKDILPDQPTNNNNNTENAITNISTEAKDDNTEDKAEGEIRVKTKPIKSFSLFGLSKWRKGFESNEREQEQQQQKIKKPMSLDLSHAVKKYIRMLFQKRGNGTQFWNRRQTSSYSFSSSLMGPNGNSKTMINGSYNKRDLIRGRRGELFSAPASMRTSPTNSGHLRVSTAGLSSSSGSTSSSSSDSTMEELQAAIQAAIAHCKNSSAVDRDDKVKDS | Negative regulator of brassinosteroid signaling. When associated to the membrane, limits the interaction of BRI1 with BAK1 by binding to the kinase-inactive form of BRI1. | Q9FMZ0 |
Q74KS4 | METK_LACJO | Methionine adenosyltransferase | Lactobacillus | MKKEKRLFTSESVSEGHPDKVADQISDAILDAILAKDPDGRVACETTVTTGLVLVVGEISTSAYVDIQSVVRKTILEIGYNRPELGFDGNNCAILVDIDEQSSDIADGVNESLETRENQQDKDDLDKIGAGDQGLMFGFAIKETPELMPLPISLAHSLMRRVASLRKEGRLDWLRPDAKAQVTVEYDDENKPKRIDTVVISTQTDATVSNDEIREAMIDMVIKKVIPSQYLDKDTKFLINPSGRFVIGGPKGDSGLTGRKIIVDTYGGYARHGGGAFSGKDLTKVDRSASYAARYVAKNIVAAGLAYQCEIQLAYAIGVAHPVSIMVDTHGTSKVSEDLLVEAVRNVFDLRPAGIIEMLNLKRPIYRQTAAYGHFGRTDVDLPWEHTDKVEALKTYVSEHAE | Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. | Q74KS4 |
Q9VZ09 | SISA_DROME | Protein sisterless A | Sophophora | MERSHLYLPTLSYAAMGHVYAPYRGSSSPALSTASSTSSKPEQIEELVSQQLHHLKMHYADEEQRYVDQMLLENPIVVERRAPPPLKTELAMDCRGSGSGSGSGSGSDVKDAQRQRAESCRKSRYNNKIKKAKLRFRHKFVSGQLKKSAVMLDTMRDVIAQAERQLLERGYPAATLERMRATFGLEMEQ | Involved in sex determination and dosage compensation. Required for proper expression of Sxl in embryonic somatic cells. Also has an essential function in the yolk nuclei. Involved in endoderm migration and midgut formation. | Q9VZ09 |
A0A126GUP6 | MP1_DROME | Melanization protease 1 | Sophophora | MEPHFFFTVLWMLLMGTSSTYAQEIFGYCRTPDENSGTCINLRECGYLFELLQSEEVTEQDRRFLQASQCGYRNGQVLEKHFCFTNVQICCANSRMRNQQPQWGNHPQPTQTTKPTKRSGTKLLPMAPNCGENFGDRVVGGNETTKREFPWMALIEYTKPGNVKGHHCGGSLINHRYVLTAAHCVSAIPSDWELTGVRLGEWDASTNPDCTVGKNGRRDCNEPYVDYPVEERIPHPQYPGNSRDQLNDIALLRLRDEVQYSDFILPVCLPTLASQHNNIFLGRKVVVAGWGRTETNFTSNIKLKAELDTVPTSECNQRYATQRRTVTTKQMCAGGVEGVDSCRGDSGGPLLLEDYSNGNSNYYIAGVVSYGPTPCGLKGWPGVYTRVEAYLNWIENNVRA | Serine protease which plays an essential role in the melanization immune response by acting downstream of sp7 to activate prophenoloxidase (PPO1) . May function in diverse Hayan-dependent PPO1-activating cascades that are negatively controlled by different serpin proteins; Spn27A in the hemolymph and Spn77BA in the trachea . Regulation of melanization and PPO1 activation appears to be largely independent of the Toll signaling pathway . | A0A126GUP6 |
Q8NT90 | HEM3_CORGL | Pre-uroporphyrinogen synthase | Corynebacterium | MTLKIGTRGSKLATTQAGTIRDQLKHYGRDAELHIVTTPGDVNMSPVERIGVGVFTQALRDVLHSGECDVAVHSMKDLPTATDPRFHLVVPTRADSREALIARDGLTLAELPEGAKVGTSAPRRISQLKAIRPDLEILPLRGNIDTRMGKVTSGELDAVMLAYAGLTRVGMQDRATEVFDADIIMPAPAQGALAIECRADDTETVRALNMLMHADTFVSAVAERTVLNRLEAGCTAPVAAHATLDGYSGDTMTLTAGVYALDGSDQLVFSAEGDGARPEELGELVAQQLIDAGAANLLGDRS | Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. | Q8NT90 |
Q4ZWR7 | FABZ_PSEU2 | Beta-hydroxyacyl-ACP dehydratase | Pseudomonas syringae | MMDIKEIREYLPHRYPFLLVDRVTELDIENKNIRAYKNVSVNEPFFNGHFPEHPIMPGVLIIEAMAQAAGILAFKMLDSKPSDGTLYYFVGSDKLRFRQPVLPGDQLVLEAKFLSSKRQIWKFECKATVDGKAVCSAEIICAERKL | Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs. | Q4ZWR7 |
A1VTF8 | RPOB_POLNA | Transcriptase subunit beta | Polaromonas | MAYSFTERKRIRKSFGNRESVLTVPYLLQMQKDAYIAFLQADRAPQKRMVEGLQAAFQNAFPIVSHNGFVEMKFIEYNLAKPAFDVRECQTRGLTFASAVRAKVQLIIYDRESSTSQSKVVKEVKEQEVYMGEVPLMTDKGSFVINGTERVIVSQLHRSPGVFFEHDKGKTHSSGKLLFSARIIPYRGSWLDFEFDPKDILYFRVDRRRKMPVTILLKAIGLNHESILANFFVFDNFRLMDSGAQMEFVAERMRGEVARFDLTDKAGKVVVAKDKRITVRHTRELEQSGTTSISVPEDFLIGRVVAKNIIDTDTGEIIAKANDELTELLLKKLRTAGIQNLQVLYTNELDQGAYISQTLRADETADEFAARVAIYRMMRPGEPPTEDAVQALFQRLFYNPDTYDLSRVGRMKFNARVGRDESTGPMVMTNEDILAVVKILVDLRNGNGEVDDIDHLGNRRVRCVGELAENQYRTGLARIEKAVKERLGQAEQEPLMPHDLINSKPISAALKEFFGASQLSQFMDQTNPLAEITHKRRVSALGPGGLTRERAGFEVRDVHVTHYGRVCPIETPEGPNIGLINSLALYARLNEYGFIETPYRRVADSKVTMEIDYLSAIEEGKYVIAQANAALDNEGRLTGDLVSAREKGESILVSAERVQYMDVSPAQIVSVAASLVPFLEHDDANRALMGANMSRQAVPVLRPEKPLVGTGIERVAAVDSGTVVTATRGGVVDYVDATRIVVRVNDAEALAGEIGVDIYNLIKYQRSNQNTNIHQRPIVKMGDKLAKGDVVADGASTDLGEIAIGQNMLIGFMPWNGYNFEDSILISERVVAEDRYTSIHIEELVVMARDTKLGSEEITRDIPNLSEQQLNRLDESGIIYVGAEVQPGDTLVGKVTPKGETTLTPEEKLLRAIFGEKASDVKDTSLRVSQGSSGTVIDVQVFTREGITRDKRAQQIIDDELKRYRLDLNDQLRIVEADAFDRIEKLLIGKIANGGPKKLAKGTKLDKAYLTDVEKYHWFDIRPADDEVASQLESIKNSMEQTRHSFDLSFEEKRKKLTQGDELPSGVLKMVKVYLAVKRRLQPGDKMAGRHGNKGVVSKIVPVEDMPHMADGTPCDIVLNPLGVPSRMNVGQVLEVHLGWAAKGLGQRIGDMLQAESKVAELRQFMDTLYNKSGRTEDLASLSDEQVVEMAQNLTTGVPFATPVFDGASEADIMTMLQLAYPDAVAKAKGLTPTRTQAQLYDGRTGDAFERTTTVGYMHFLKLHHLVDDKMHARSTGPYSLVTQQPLGGKAQFGGQRFGEMEVWALEAYGAAYVLQEMLTVKSDDVVGRTKVYESIVKGEHAITAGMPESFNVLVKEIRSLGIDMELERS | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | A1VTF8 |
Q87KA9 | ATPE_VIBPA | F-ATPase epsilon subunit | Vibrio | MAPITFHLDVVSAEKRIFSGRVETFQVTGSEGELGIFHGHTPLLSAIKPGMVRIVKQHGHEEFIYVSGGMVEVQPGTATVLADTAIRGEDLDAAKAEEAKRRAEEKIQNQHGDMDFAQAASELAKAIAQLRVIELTKKRR | Produces ATP from ADP in the presence of a proton gradient across the membrane. | Q87KA9 |
A8MC69 | AROC_CALMQ | 5-enolpyruvylshikimate-3-phosphate phospholyase | Caldivirga | MSSIGVVFRVTTFGESHGPAVGVVIDGVPAGIQLNEDYIRRELNRRRFCHIPVLNPRCEDEDFQILSGIKDGLTTGTPIAIVVWNKRAVSNYYMDIWMKPRPGHADLAWYLKFGKLYDFRGGGRASGRETVARIAAGAVAKAILKQTIDVDVSSHLIELGGVSISRDDYTFNDVAKSWEKPLPMIDDEAIEKAIKVLINAATEGDSVGGIGEVLTTEVPPGLGEPVFDKLKADLAKAVMSIPSTTGIEFGLGFKLARMRGSEANDQIVLRNGKPRLETNRVGGMLGGMSIGEPIRFRVAFKPTPSIRRPQRTVDLEKITETTITFTGRYDISTAPKAILAAEAMTAIILVDHAIRAGLIPRIIRK | Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | A8MC69 |
Q6EJ97 | ISPS_PUEML | Isoprene synthase, chloroplastic | Pueraria | MATNLLCLSNKLSSPTPTPSTRFPQSKNFITQKTSLANPKPWRVICATSSQFTQITEHNSRRSANYQPNLWNFEFLQSLENDLKVEKLEEKATKLEEEVRCMINRVDTQPLSLLELIDDVQRLGLTYKFEKDIIKALENIVLLDENKKNKSDLHATALSFRLLRQHGFEVSQDVFERFKDKEGGFSGELKGDVQGLLSLYEASYLGFEGENLLEEARTFSITHLKNNLKEGINTKVAEQVSHALELPYHQRLHRLEARWFLDKYEPKEPHHQLLLELAKLDFNMVQTLHQKELQDLSRWWTEMGLASKLDFVRDRLMEVYFWALGMAPDPQFGECRKAVTKMFGLVTIIDDVYDVYGTLDELQLFTDAVERWDVNAINTLPDYMKLCFLALYNTVNDTSYSILKEKGHNNLSYLTKSWRELCKAFLQEAKWSNNKIIPAFSKYLENASVSSSGVALLAPSYFSVCQQQEDISDHALRSLTDFHGLVRSSCVIFRLCNDLATSAAELERGETTNSIISYMHENDGTSEEQAREELRKLIDAEWKKMNRERVSDSTLLPKAFMEIAVNMARVSHCTYQYGDGLGRPDYATENRIKLLLIDPFPINQLMYV | Lyase that catalyzes the formation of isoprene from dimethylallyl diphosphate. | Q6EJ97 |
Q03957 | CTK1_YEAST | CTD kinase subunit 1 | Saccharomyces | MSYNNGNTYSKSYSRNNKRPLFGKRSPNPQSLARPPPPKRIRTDSGYQSNMDNISSHRVNSNDQPGHTKSRGNNNLSRYNDTSFQTSSRYQGSRYNNNNTSYENRPKSIKRDETKAEFLSHLPKGPKSVEKSRYNNSSNTSNDIKNGYHASKYYNHKGQEGRSVIAKKVPVSVLTQQRSTSVYLRIMQVGEGTYGKVYKAKNTNTEKLVALKKLRLQGEREGFPITSIREIKLLQSFDHPNVSTIKEIMVESQKTVYMIFEYADNDLSGLLLNKEVQISHSQCKHLFKQLLLGMEYLHDNKILHRDVKGSNILIDNQGNLKITDFGLARKMNSRADYTNRVITLWYRPPELLLGTTNYGTEVDMWGCGCLLVELFNKTAIFQGSNELEQIESIFKIMGTPTINSWPTLYDMPWFFMIMPQQTTKYVNNFSEKFKSVLPSSKCLQLAINLLCYDQTKRFSATEALQSDYFKEEPKPEPLVLDGLVSCHEYEVKLARKQKRPNILSTNTNNKGNGNSNNNNNNNNDDDDK | Catalytic subunit of the CTDK-I complex, which hyperphosphorylates the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit. CTDK-I phosphorylates 'Ser-5' if the CTD substrate is not phosphorylated at 'Ser-5', but will phosphorylate 'Ser-2' of a CTD substrate if 'Ser-5' is already phosphorylated. CTDK-I is also more reactive toward substrates that are prephosphorylated at 'Ser-2' or 'Ser-5' compared with an unphosphorylated CTD substrate, therefore efficiently creating doubly phosphorylated CTD repeats. Involved in RNA polymerase II transcriptional elongation, and through PTI1, pre-mRNA 3'-end processing. Participates in both positive and negative regulation of CTD phosphorylation. Required for DNA damage induced transcription, including the expression of the RNR genes, and reprogramming of gene expression upon amino acid starvation. Required for SET2 mediated H3K36 methylation. Also regulates H3K4 methylation. Controls the maintenance of suppressive chromatin in the coding regions of genes by both promoting H3K36 methylation, which leads to histone deacetylation, and catalyzing phosphorylation of the CTD required to localize H3K4 chromatin modification specifically to the 5' ends of genes, thereby creating a boundary for H3K4 methylation that prevents a mark associated with transcriptional initiation from spreading into the bodies of genes. Involved in RNA polymerase I transcription. Involved in telomere maintenance. Acts together with SNF1 to induce GSY2 transcription in response to glucose limitation. Involved in the adaptation to alternative carbon sources, including galactose, glycerol and ethanol, but not raffinose. Required for the integrity of the rDNA locus. Functions in translation elongation by enhancing decoding fidelity. Needed for translational accuracy by phosphorylating RPS2. | Q03957 |
Q5FG65 | PYRH_EHRRG | Uridine monophosphate kinase | Ehrlichia | MSENSANELKYSRVLLKVSGEALMGDKGFGWDIETIDNLSHDLKEVHDLGVQLCLVVGGGNIFRGASASAPFGFERASNDYIGMLATMMNALSLQNSLEKINVQSRVLSAVSITAVCETYIRRRAIRHLEKGRIVICAAGVGNPFFTTDTAAALRGIEMGCNVIFKGTQVDGVYSADPKKVADAVRYDKISYRELLSLDLKIMDVAAVSLARDHSIPIIVFNLGKRGALADIICGGGLYTTIYN | Catalyzes the reversible phosphorylation of UMP to UDP. | Q5FG65 |
A8AB83 | RADA_IGNH4 | DNA repair and recombination protein RadA | Ignicoccus | MGQVATEEKRPTSVAELPGVGPSTAAKLIDAGYGTIEALAVATPEELVAIGIPLTTAQKIIRAARQMLDIRFRTAKEVKLERMNLRKITTGSKNLDDLLGGGIETKTITEFFGEFGSGKSQLCHQASVNVQLPLEQGGLSEGDKVAKAVYVDTEGTFRWERIEQMAKCLGLDPDQVMDNIYYIRAVNSDHQMAIVEELFNLVPKENVKLIVVDSVTSHFRAEYPGRENLAVRQQKLNKHLHQLGKLAEVYNTAVIITNQVMARPDVFYGDPTQAVGGHVLYHAPGVRVQLKKARGNKRIARVVDAPHLPEAEAVFAITDCGIRDPED | Involved in DNA repair and in homologous recombination. Binds and assemble on single-stranded DNA to form a nucleoprotein filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules. | A8AB83 |
Q1LI29 | EFG1_CUPMC | Elongation factor G 1 | Cupriavidus | MARKTPIERYRNIGISAHIDAGKTTTTERILFYTGVNHKIGEVHDGAATMDWMEQEQERGITITSAATTAFWKGMGGNYPEHRFNIIDTPGHVDFTIEVERSMRVLDGACMVYCAVGGVQPQSETVWRQANKYGVPRLAFVNKMDRTGANFFKVYDQLKTRLKANPVPVVVPIGAEDGFQGVVDLLEMKAIVWDEASQGVKFEYQDIPAELQATADEWREKMVESAAEASEELMEKYLGGEELTRAEIVKALRDRTIACEIQPMLCGTAFKNKGVQRMLDAVIDFLPSPVDIPPVKGVDESDDEKKLERKADDNEKFSALAFKIMTDPFVGQLIFFRVYSGKINSGDTVYNPVKQKKERLGRILQMHANQREEIKEVLAGDIAAAVGLKDATTGDTLCDPAAPIVLERMVFPEPVISQAVEPKTKADQEKMGIALNRLAAEDPSFRVRTDEESGQTIISGMGELHLEILVDRMKREFGVEANIGAPQVAYRETIRKKAEDVEGKFVKQSGGRGQYGHAVITLEPQEPGKGFEFIDAIKGGVIPREYIPAVEKGIVDTLPAGILAGFPVVDVKVTLTFGSYHDVDSNENAFRMAGSMAFKEAMRKASPVLLEPMMAVEVETPEDYTGTVMGDLSSRRGIVQGMDDMVGGGKIIKAEVPLSEMFGYSTALRSATQGRATYTMEFKHYAEAPKNIAEAVMTAKGKQ | 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. | Q1LI29 |
Q9CAH0 | MORF7_ARATH | RNA editing-interacting protein 7 | Arabidopsis | MARIIRRPLNLTAAVRFRLSPLSPFSGNSGSINSETTSWSELIRVPSLVEGCDYKHWLVLMKPPNGYPTRNHIVQSFVETLAMALGSEEEAKRSIYSVSTKYYYAFGCRIHEPLTYKIRSLPDVKWVLPDSFIVDGDNRYGGEPFVDGEVVPYDEKYHADWLRDQTDEDAKSGVVKKKHRRKRKKKLI | Involved in organellar RNA editing. Required for the processing of few RNA editing sites in mitochondria. | Q9CAH0 |
A1T9N3 | UREF_MYCVP | Urease accessory protein UreF | Mycolicibacterium | MSSLATLLVLSDSRLPTGGHVHSGGVEEAVSSGLVVDLATLRAYLTRRIRTSGLVTASLAAAVHRGSLPAAAGEAGDAETDARTPSPAARAASRAQGRGLVRLARRVWPEQDWDGLGATPHLAVAAGVAGRAGGLAPDHTALSVVYTTMTGSATAAQRLLALDPGDVAAVTFALSPLCEHTAAEAAKELADLSDPLLDVLAQRHLERERPLFAS | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | A1T9N3 |
B1J265 | GLMM_PSEPW | Phosphoglucosamine mutase | Pseudomonas | MSRKYFGTDGIRGRVGEYPITPDFMLKLGWAAGMAFRKQGNCRVLVGKDTRISGYMFESALEAGLSAAGADVLLLGPMPTPAIAYLTRTFHAEAGIVISASHNPHDDNGIKFFSGQGTKLPDEIELMIEELLDQPMTVVDSSKLGKVSRINDAAGRYIEFCKSSVPTSTGFEGLKLVVDCAHGATYKVAPSVFRELGAEVTVLHAQPDGLNINENCGSTHIESLQAAVLVGHADLGIAFDGDGDRVLMVDHTGAIVDGDELLFIIARDLHERGKLQGGVVGTLMSNLGLELALKDLDIPFVRAKVGDRYVMAELLERGWLVGGENSGHVVCCNHTTTGDAIIAALQVLLALRRRGETLAQARQALRKCPQVLINVRFGASKVDPLEHPAVKEASARVTEDMAGRGRVLLRKSGTEPLVRVMVEGDDENQVRTHAEALAKLVAEVCV | Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. | B1J265 |
Q39JU3 | SYP_BURL3 | Prolyl-tRNA synthetase | Burkholderia cepacia complex | MKASRFFIGTLKEAPADAEIVSHKLMVRAGMIRRVAGGIYNYLPVGLRSIRKVEAIVREEMNRAGGIELLMPAVQPAELWQESGRWEQYGPELLRFKDRKDNDFVIGPTHEEVITDIARNQIKSYRQMPVNFYQIQTKFRDEIRPRFGVMRGREFIMKDAYSFDKDAAGLNESYRKMYDAYVRIFTRLGLEFRAVAADSGSIGGNFSHEFHVIADTGEDAIAYCPTSEFAANIEAAEALPLIAERAAPAEAMEKVATPGKAKCEAVAELLAIPLERTIKSIVLATDNEGAEPTIWLVMLRGDHDLNEIKVSKLPGLKNHRFATEQEIVEWFGTPPGYLGPVGTKKPVKVIADRTVANMSDFVVGANEVDYHIAGVNWGRDLPEPDVADVRNVKKGDPSPDGKGVIDICRGIEVGHVFQLGTKYSEAMGATFLDESGKPQPMLMGCYGVGVTRILGAAIEQNFDDKGIIWPESIAPFEVVLCPMGYDRSDMVRETADKLYAELVAAGIDVILDDRGERPGVMFADWELIGVPHRLVIGERGLKEGKIEYQGRRDAEATLLPADAAAATVAEKIRAALAR | 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. | Q39JU3 |
Q47ZY2 | QUEC2_COLP3 | Queuosine biosynthesis protein QueC 2 | Colwellia | MKKLVVIYSGGMDSFTALNKAVKEGFDVYALSFDYGQKHNKELIYAQNVCNELNVPHKILDIKSISTLFTSSSLVSDDINVPDGHYEADNMKSTVVPNRNMILISLAIGYAVDIEAEGVWYGAHSGDHLIYPDCRPEFVKVMDQASKVANFEPVYVHAPYLNTDKIGILKDGIKMGLDYSKTWTCYQGKEKACGTCGSCVERLEAFQANNIDDPVQYSI | Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). | Q47ZY2 |
Q83CP8 | SCPA_COXBU | Segregation and condensation protein A | Coxiella | MENQEVVNQLAGFEVKVSGQPLSKLPEDLYIPPDALRVFLEAFEGPLDLLLYLIKKHNIDILDIPIAEITRQYMQFVDLMREMRIELAAEYLVMAAMLAEIKSRLLLPRPVVEEENEQDPRAELVRRLQEYERYKKAAYDLDQLPRVGRDTFIADAAVPPMNTAKIHPTAELPELLNALKDVLQRASLYNAHSIAREPLSIRERMSRILSLVDKENFIAFTRLFTVEEGRMGVVVTLIATLELIRQSVIELVQAEPFALIHIRAKG | Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpB that pull DNA away from mid-cell into both cell halves. | Q83CP8 |
A8HT29 | GCSPA_AZOC5 | Glycine dehydrogenase (aminomethyl-transferring) subunit 1 | Azorhizobium | MRYLPLTPEDRTEMLARIGAPSVDALFADIPAAKLDPALADLPAHKTELSVERTLGALSAQNVPAGSVPFFVGAGAYRHHVPATVDHLIQRSEFLTSYTPYQPEIAQGTLQYLFEFQTQVGELTGMEVANASMYDGSTAAAEAVLMAHRVTKRRKAVVAGNVHPHYRETIATLSLYADDAVVALSPVPQGGEDILSAIDGETSCVVVQSPDVFGNIVDLKPIAEKAHAAGALLIAVFTEVVSLGLIEPPGAQGADIVVGEGQSIGNPLTFGGPYVGLFATRQKYVRQMPGRLAGETVDASGKRGFVLTLSTREQHIRREKATSNICTNSGLCALAFTIHLTLLGETGLRKLARLNHANACKLADKLAAVPGVQVLNSAFFNEFTLRVPGKAVDVIEKLAAKGVLGGVPYARLAPKAGLDDLILVAATEINTDEDRAAYAAALKEVLA | The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein. | A8HT29 |
Q2GH18 | PLSX_EHRCR | Phosphate-acyl-ACP acyltransferase | Ehrlichia | MSIISIAVDAMGGDFAPEAVVSGLDFALTNLLDDQNVSFNIYGQGSQVLPILDKYKDLKEHSVFIDTPEVVLANDKPSFALRKRRSSSMWCAIDSIKSGVTSGVVSSGNTGALMAISRFLLGTLPNIDRPAICTALPSRGEEYFVLLDLGANIESSSNALFQFAIMGSAFAKAVLNIASPKVALLNVGQEEVKGTDVIREAFLLLKQAEGRINFCGYIEPIDILGDKVDVVVTDGFCGNIVLKVAESIAYTFKSVFEKSVTSSIISKFAGLLLKSQMKKDFMRFNPKMYNGAMLLGLNGVVVKSHGNADKVAFAHAIKVTVNAVRNDINAKIIHELS | 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. | Q2GH18 |
Q89Z26 | MNME_BACTN | tRNA modification GTPase MnmE | Bacteroides | MNQDTICAIATAQGGAIGSIRVSGPEAISITSRIFQPAKAGKLLSEQKPYTLTFGRIYNGEEVIDEVLVSLFRAPHSYTGEDSTEITCHGSSYILQQVMQLLIKNGCRMAQPGEYTQRAFLNGKMDLSQAEAVADLIASSSAATHRLAMSQMRGGFSKELTDLRSKLLNFTSMIELELDFSEEDVEFADRSALRKLADEIEQVISRLVHSFNVGNAIKNGVPVAIIGETNAGKSTLLNVLLNEDKAIVSDIHGTTRDVIEDTINIGGITFRFIDTAGIRETNDTIESLGIERTFQKLDQAEIVLWMVDSSDASSQIKQLSEKIIPRCEEKQLIVVFNKADLIEEMQKEELSALLKNFPKEYTKSIFISAKERRQTDELQKMLINAAHLPTVTQNDIIVTNVRHYEALSKALDAIHRVQDGLDSHISGDFLSQDIRECIFFISDIAGEVTNDMVLQNIFQHFCIGK | Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34. | Q89Z26 |
Q31ZN0 | DADA_SHIBS | D-amino acid dehydrogenase | Shigella | MRVVILGSGVVGVASAWYLNQAGHEVTVIDREPGAALETSAANAGQISPGYAAPWAAPGVPLKAIKWMFQRHAPLAVRLDGTQFQLKWMWQMLRNCDTSHYMENKGRMVRLAEYSRDCLKALRAETNIQYEGRQGGTLQLFRTEQQYENATRDIAVLEDAGVPYQLLESSRLAEVDPALAEVAHKLTGGLQLPNDETGDCQLFTQNLARMAEQAGVKFRFNTPVDQLLCDGEQIYGVKFGDEVIKADAYVMAFGSYSTAMLKGIVDIPVYPLKGYSLTIPIAQEDGAPVSTILDETYKIAITRFDNRIRVGGMAEIVGFNTELLQPRRETLEMVVRDLYPRGGHVEQATFWTGLRPMTPDGTPVVGSTRFKNLWLNTGHGTLGWTMACGSGQLLSDLLSGRTPAIPYEDLSVARYSRGFTPSRPGHLHGAHS | Oxidative deamination of D-amino acids. | Q31ZN0 |
Q13VN6 | EFP_PARXL | Elongation factor P | Paraburkholderia | MKTAQELRTGNVVMIGADAMVVQKAEYNKSGRNSAVVKMKFKNLLTGAGMESVYKADDKFDVVVLERKEVTYSYFADPMYVFMDADYNQFEVESEMMGDALHYLEDGMACEVVFYNDKAISVELPTTLVREIIYTEPAVKGDTSSGKVLKNAKLNTGFELQVPLFCNIGDKIEIDTRTHEYRSRA | Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase. | Q13VN6 |
Q7TT23 | DAAF9_MOUSE | Dynein axonemal assembly factor 9 | Mus | MDSFDPQQLGLSPARFAGTFGSGAASVSCSRLRQVQSVLTQSSKSQPDGILCILGIDSRYNEGCRELANYLLFGLYSQNATDFEKTGFSEEILDDVILLIKSDSVHLYCNPVNYRYLLPYVAHWRNLHFHCMTENEYEDEEAAEEFKISSFVDMVRDCSRIGIPYSSQGHLQIFDMFVVEKWPIVQAFALEGIGGDGFFTMKYELQDVSLSLWNVYSRMDPASLENMLSEDLAVFEHQWTSFFANFDTEIPFLLELSESQAGEPFRSYFGHGMLSSHITENSPHRQPFVLFGNHSTRDNLSAGSFNFPSEGHLVRNTGPAGSFAKHMVAQCVSPKGPLACSRTYFFGATHVPYLGDNEKLPRTTEQIRLLSQIYAAVIEAVLAGIACYAKTCSLAKAKEVAEHTLESGLVFTELVPFKADLRSKVTFHIHAVNNQGRIVPLNNEDSLSFVKTARMTVYDIPDLLGGGGGGCLGSVVFSESFLTSRILVKEKDGTITPETSYIILTAAIPRFCSWLVEDSEIKLSEKTLQATKGDDCCLGTLLTGGKGAYLYSNSPQSGPEEGSAYFFSGGLLFSHRHHGSIVIAKEHVDAFSFYDGDSTSVVAALLIHFRSSILPHLPVHFHGSSNFLMLALFPKSKIYQAFYSEVFSPWQQQDNSGLSLKVIQEDGLSAEQKRLHSNAQKLFSALSPPAQDWSSPKLLSGKLPELDRFLQHFAIGSIGQEPVMRAHLVGLLQQPEMSPAHEVESDKVVISIVTGLPGCHASKLCAFLITLHKEYGRWMVYRQIMDSSECFHAAHFQKYLSSALEAQQNRSARQSAYIRKKTRLLVVLQGYTDVIDVVQALQTHPDPNVRSYFTIGAVTVCVEPLSCYMEHRFLFPKCLDQCSQGVVSNVVFTSHTAEQKHPLLVQLQTLIRASNPTAAFILAENGIVTRNEDIELILSENSFSSPQMLRSRYLLFPGWYEGKFDAGSVFPLMVQICVWFDCPLEKTRFVSRCRAIQSSIKPSPFSGNIYHILGKVKFSDSEKTMEVCHNTLTNSLTIVPVLEGPTPPPNSRSSPQDNGQPECYLVFIGCSLKEDSLKDWLRQSAKQRPQRKALKTRGMLTQQEIKNIHVKRHLDPLPAGYFYNGTQFVNFFGDKTDFHPLMDQFMNDYVEEANREIERYNRELEQQEYRDLFEQKPKP | May act as an effector for ARL3. | Q7TT23 |
A9IW26 | RL4_BART1 | 50S ribosomal protein L4 | Bartonella | MDLVIKTLDGHEAGKLKVSESIFDLVPREDILQRVVRWQLARRQQGTHQSQGRSDVSRTGAKMFKQKGTGRARHSSARAPQFRGGGKAHGPVFRSHAHDLPKKIRALGLRLALSAKLKAKDLIVVDELAVKDAKTKKLVSHFSKLGFNNALLIGGQEIDINFFRAASNIPNIDVLPIQGINVYDILRRSKLVLSKAAVEALEERFR | Forms part of the polypeptide exit tunnel. | A9IW26 |
Q5XDG5 | YBEY_STRP6 | Endoribonuclease YbeY | Streptococcus | MYIEMIDETGQVSQEIMEQTLDLLNFAAQKTGKEEKEMSVTFVTNERSHELNLEYRDTDRPTDVISLEYKPETPILFSQEDLAADPSLAEMMAEFDAYIGELFISIDKAREQSQEYGHSFEREMGFLAVHGFLHINGYDHYTLEEEKEMFTLQEEILTAYGLTRQ | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | Q5XDG5 |
B1WZT9 | RS20_CROS5 | 30S ribosomal protein S20 | Crocosphaera subtropica | MANSKSALKRIRTSERNRLRNKSYKSAVRTLMKKYLQAVEEYAASPTPENKAVVDQRMSAAYSKIDKAVKRSVLHRNNGARKKARLAKALQQVASAS | Binds directly to 16S ribosomal RNA. | B1WZT9 |
Q9D011 | MPLKI_MOUSE | TTD non-photosensitive 1 protein homolog | Mus | MHRPNFRPPTPPYPSPGIGGWGGGNNFRGALGGGPRPPSPRDGYGSPHHTPPCGPRARPYGSSQSPRHGGNFSGARFGSPSPGGYPGSYSRSPAGSQHQFGYSPGQQQTYPQGSPRTSTPFGSGRGREKRMSNELESYFKPSMLEDPWAGLEPVSVVDISQQYSNTQTFTGKKGRYFS | May play a role in maintenance of cell cycle integrity by regulating mitosis or cytokinesis. | Q9D011 |
Q602E7 | MNMG_MESH2 | Glucose-inhibited division protein A | Mesomycoplasma | MSKKSKNSSIEFDAIVVGGGHAGIEAVYALLKKKLKVVLITLDKKKLASMPCNPAIGGPAKGIITREIDALGGVQGKLSDLAMIQIKYLNESKGPAVLAIRAQIDKEKYSKLILKDLKKQENLLIIEDLVSELLVEKNRVFGLKTAKKQVFFSKTVIITTGTYMDSKVLRGSLAIPSGPDGQQTSNLLSNNLKTLGFELQRLKTGTPPRIFTSSIDFSKVEKEVLPVYNINFSFQSKHKLKKQISCYLTYTTAKTHDIINKNLGKSSMYSGLISGVGPRYCPSIEDKIVRFSEKPRHQIFFEPETKKQDIMYINGLSTSMPEDVQLEMVKTIPGLENAKIAKFGYAIEYDALNPLELKKSLETKRVKGLFMAGQINGTSGYEEAAAQGLVAGINAGQFVLGKKPVEILRNDGYIGVLIDDLVTKGTKEPYRMLTSRAEYRLILRNDNADIRMAKYALKSGLISKKEYLKIKAKYAKIDRKILELSKEFVSPKDELAKKYNLEKRISKLKLISWPNVNFKDILPDFEFGYELTVMARLKGYIQKQNSEAQKMIRLEKLLIPGELNYEKVANLSSEALDKFQKVRPKTIGEASRISGVNPADIQMLLFHIKVLKMQKVSKI | NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34. | Q602E7 |
Q71E89 | CYB_MUNMN | Ubiquinol-cytochrome-c reductase complex cytochrome b subunit | Mungos | MTNIRKSHPLIKIINESFIDLPAPSNISAWWNFGSLLGACLILQILTGLFVAMHYTSDTTTAFSSVTHICRDVNYGWIIRYMHANGASMFFICLFMHIGRGMYYGSYSFMETWNIGIILLFTVMATAFMGYVLPWGQMSFWGATVITNLLSAVPYIGTNLVEWIWGGFSVDKATLTRFFAFHFILPFVISALAAVHLLFLHETGSNNPSGIPSDSDKIPFHPYYTIKDMLGLLIMFTALMTLVLFSPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPYKLGGVLALILSITILAIVPLLHTSNQRSMMFRPLSQCLFWLLAADLLTLTWIGGQPVEYPFIIIGQLASILYFLIILVLMPISGIIENHLLKW | 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. | Q71E89 |
P51465 | HBAB_LITCT | Hemoglobin alpha-B chain | Lithobates | MPFSASDRHDITHLWEKMAPNVEFLGEEAMERLFKSHPKTKTYFSHLNVEHGSAAVRAQGAKVLNAIGHASKNLDHLDEALSNLSDKHAHDLRVDPGNFHLLCHNILVVLAIHFPEDFTPRAHAAFDKFLAAVSETLYSKYR | The alpha-B chain is a component of adult hemoglobin B. | P51465 |
Q9V8F5 | BM23_DROME | Immune-induced peptide 23 | null | MKCLILSFAIFVVLASQATAGNVIIGGVCQDCSPPVAENVVVGGQSYRTGRPGQGTVYINSPGAYLGALDGPIRRTGAGGGGGGGAQYPDGYSGRLPGGTYLHNKDCVGCSISGGGD | Secreted immune-induced peptide induced by Toll signaling . Has a role in resistance to bacterial and fungal infections . | Q9V8F5 |
Q475N7 | MIAB_CUPPJ | tRNA-i(6)A37 methylthiotransferase | Cupriavidus | MKKVFVKTYGCQMNEYDSDKMVDVLNASQGLEPTDNVEDADVILFNTCSVREKAQEKVFSELGRMKALKAVKPDLVIGVGGCVASQEGASIVSRAPYVDVVFGPQTLHRLPDLIARRQRTGQSQVDISFPEIEKFDHLPPARVEGPSAFVSIMEGCSKYCSYCVVPYTRGEEVSRPFEDVLAEVAGLAEQGVREVTLLGQNVNAYRGAMGGTSEIADFALLIEYVAEIPGIERIRYTTSHPKEFTSRLVELYGRCDKLVNHLHLPVQHASDRVLMAMKRGYSVLEYKSIIRRLRMLRPDMSMSSDFIVGFPGETDADFDKLMALIEEVGYDTSFSFIFSPRPGTPAANLHDDTPHEVKLRRLQHLQATIEENVQRISRNMVGSVQRILVEGPSRKDPTELHGRTENNRVVNFALPGVPQAQRDRMIGQMVDVSITQAFPHSLRGEIVVRQ | Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | Q475N7 |
B9MLD4 | FABZ_CALBD | Beta-hydroxyacyl-ACP dehydratase | Caldicellulosiruptor | MYNIDKILEIIPHRYPFLLVDRIIEVEEGKRAKGIKNVTINEPFFQGHFPSNPVMPGVLIVEAMAQVGAVAMLLKEEFKGKTPFFAGIDKVRFKKVVKPGDVLVIETELISLKGSIGKAKAVAMVDGEVVCEGELLFAIK | Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs. | B9MLD4 |
A7EWL8 | THI4_SCLS1 | Thiazole biosynthetic enzyme | Sclerotinia | MAPPSAVEANSPIDGVHLKSAFEVKAVHAQTASQGKTLAELAEKWDQGFTFAPIRESQVSRAMTRRYFKDLDTYAESDVVIVGAGSCGLSTAYMLGKARPDLKIAIIEASVSPGGGAWLGGQLFSAMVMRKPADAFLIDLGVPFEDEGDFVVVKHAALFTSTLLSKVLAFPNIKLFNATSVEDLITRQTADGNIRIAGVVTNWTLVTMHHDDQSCMDPNTINAPIVISTTGHDGPFGAFCVKRLVSMNQIKELGGMRGLDMNVAEDAIVKKTREIVPGLIVGGMELSEVDGANRMGPTFGAMALSGVKAAEEALKVFDERKAQNAY | Involved in biosynthesis of the thiamine precursor thiazole. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an adenylated thiazole intermediate. The reaction includes an iron-dependent sulfide transfer from a conserved cysteine residue of the protein to a thiazole intermediate. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. May have additional roles in adaptation to various stress conditions and in DNA damage tolerance. | A7EWL8 |
Q7VRV8 | NUOH_BLOFL | NDH-1 subunit H | Candidatus Blochmannia | MNISFEKFLECLSIFMHSFFVLLMVVMCGAYMSFVERRLLALFQNRYGPNRVGWNGSLQLLADLIKIMFKEDWIPPFSDRYIFVLAPAIAFIISLMIIPVIPFTPSSVILHCNVGVLFFLMISALTVYSVLLAGWSSNNKYALIGAVRSIAQTLSYEVFLGLSLMGIVAKSGSFDLLNIVQDQKYLWNIVPQFLGFVVFFISGMALCHRHPFDQPESEQELVAGYHIEYSGMKFSLFFISEYISVISISSFMVTLFFGGWYGPWFPPVVWFIIKTFMIVLFFVLIRASLPRPRYDYVMLVGWKFLLPIALLNLLVTAGYILI | NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. | Q7VRV8 |
A4VXL3 | ILVC_STRSY | Ketol-acid reductoisomerase type I | Streptococcus | MTVTMQYEKDVTVAALDGKRIAVIGYGSQGHAHAQNLRDTGHDVIIGVRAGKSFDKAKEDGFETFEVAEAAKQADVIMILAPDEIQADLYNEEIAPNLEAGNALGFAHGFNVHFEFIKVPADVDVFMCAPKGPGHLVRRTFEEGFGVPALYAVYQDATGNAKHIAMDWAKGVGSARVGLLETTFKEETEEDLFGEQAVLCGGLTALMQAGFEVLTEAGYAPELAYFEVLHEMKLIVDLVYEGGFKKMRQSISNTAEFGDYVSGPRVITDQVKENMKAVLADIQSGKFANDFVNDYKAGRPRMEAYRKEAENLEIEKVGAELRKAMPFVGRNDDDAFKIYN | Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | A4VXL3 |
Q15W54 | RF3_PSEA6 | Peptide chain release factor 3 | Pseudoalteromonas | MSNALVPQEVSRRRTFAIISHPDAGKTTITEKVLLFGNALQRAGTVKGKKSGQHAKSDWMEMEKERGISVTTSVMQFPYSDCLVNLLDTPGHEDFSEDTYRTLTAVDSCLMVIDAAKGVEARTIKLMEVTRLRDTPIITFMNKLDRDTRDPIDLLDEVESVLNIKCAPITWPIGMGKEFKGVYHLLRDETILYSTGQGHTIQEKRVIKGLDNPELDTAIGDYAEELRDMLDLVKGASHEFNHEEFIAGELTPVFFGTAMGNFGVDHMLDGLVDWAPSPQGRETDQGKVEAKDEKFSGFVFKIQANMDPKHRDRIAFCRIVSGKYQKGMKMHQSRIGKDVRISDALTFLAGDRELLEEAYAGDIIGLHNHGSIQIGDTFTSGDKFRFAGIPNFAPELFKRIRLRDPLKQKQLLKGLIQLSEEGAVQVFRPLQNNDLIVGAVGVLQFDVVVARLKGEYNVDAMYEHINVATARWIYGKDERKVDEFRRKAEANLALDGGDNLTYIAPTMVNLSLAQERYPEIEFHQTREH | Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP. | Q15W54 |
Q8FQ22 | ATPA_COREF | F-ATPase subunit alpha | Corynebacterium | MAELTISSDEIRSAIANYTSSYSAEASREEVGVVISAADGIAQVSGLPSVMANELLEFPGGVIGVAQNLDTDSVGVVVLGNYELLKEGDQVRRTGDVLSIPVGEKFLGRVINPLGQPIDGLGEIVAEEDRVLELQAPSVLERQPVEEPMATGIKAIDAMTPIGRGQRQLIIGDRKTGKTAVCVDTILNQKANWETGDKTKQVRCIYVAIGQKGSTIAALRKTLEEQGALEYTTIVAAPASDAAGFKWLAPFAGAALAQHWMYQGNHVLVIYDDLTKQAEAYRAISLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDDLGAGSITALPIIETKANDVSAFIPTNVISITDGQVFLESDLFNRGVRPAINVGISVSRVGGAAQTKGMKKVAGSLRLDLAAYRDLEAFATFASDLDAASKAQLERGQRLVQLLIQSENAPQAVEYQIISLWLAGEGAFDNVPVDDVRRFETELHEYLGSNAPQVYEQIAGGAVLSDESKETLLQATEQFKGTFQTTDGTRIINEPEVDALDAGQVRKDQLTVSRKVGK | Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | Q8FQ22 |
Q94570 | TBA2_HOMAM | Alpha-II tubulin | Homarus | MRECISIHVGQAGVQMGNSCWELYCLEHGIQPDGQMPSDKTVGVCNDSFNTFFTETGSGKHVPRAVFVDLEPSVIDEVRSGIYRQLFHPEQLISGKEDAANNYARGHYTIGKEYVDIVLDRIRKLADQCTGLQGFLIFRSFGGGTGSGFASLLMERLSVEYGKKSKLEIAIYPAPQSATSVVEPYNSILTTHTTLEHSDCCFMVDNEAIFDICQRNLDVSRPTYTNLNRLIGQIVSSITASLRFEGALNVDLTEFQTNLVPYPRIHFPLTTYSPIISAEKAYHEQLSVGEITSACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVTASIANVKTKRTIQFVDWCPTGFKVGINYQPPTVVPGADLAKVSRAVCMLSNTTAIAEAWARLDHKVDLMYAKRAFVHWYVGEGMEERQFSEAREDLATLEKDYEEVGIDTADGEDDEEANDY | Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. | Q94570 |
P02415 | RL16_MYCCT | 50S ribosomal protein L16 | Mycoplasma | MLQPKRTKYRKPHRVSYEGKAKGAKEINFGEFGLMALDGAWIDNHQIEAARIAMTRYMKRDGKIWMRIFPHMAMTKKPAEVRMGSGKGNPEKWVAVVKKGTIMFEVAQVNEQVAREALRLAMHKLPIRCKFVKRGEN | Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs. | P02415 |
B7IYH2 | LEPA_BACC2 | Ribosomal back-translocase LepA | Bacillus cereus group | MNKEERAKRQSKIRNFSIIAHIDHGKSTLADRILEKTNALTQREMKAQLLDSMDLERERGITIKLNAVQLNYKAKDGEEYILHLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNNLEILPVINKIDLPSADPERVRQEVEDVIGLDASEAVLASAKAGIGIEEILEQIVEKVPAPAGDSEEPLQCMIFDSLYDPYRGVIAYIRVVNGTVKVGDKVRMMATGKEFEVTEVGVFTPKTTQRDELTVGDVGFLAASIKNVGDTRVGDTITHAKRPAAEALPGYRKLNPMVFCGLYPIDSARYNDLRDALEKLELNDSALEFEPETSQALGFGFRCGFLGLLHMEIIQERIEREFKIDLITTAPSVIYKVYLTNGEDVIVDNPSNMPDPQSIDRVEEPFVKASIMVPNDYVGAVMEICQGKRGTFIDMQYLDETRVTLTYEIPLSEIVYDFFDQLKSNTKGYASFDYELIGYKPSKLVKMDILLNNEQVDALSFIVHRDSAYDRGKVIVEKLKELIPRQQFEVPIQATIGNKVVARSTIKAMRKNVLAKCYGGDISRKRKLLDKQKEGKKRMKSVGSVEVPQEAFMAVLKMDDN | 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. | B7IYH2 |
A4TDU4 | NRDI_MYCGI | Protein NrdI | Mycolicibacterium | MANIVYFSSVSENTHRFVQKLELPAIRIPLKDRIRVEEPYVLILPTYGGGHANGPDPDRGGYVPKQVIAFLNDEHNRSLIRGVIAAGNTNFGAEFGYAGVVVSRKCDVPFLYRFELMGTTDDVFAVRAGLQDFWKDQSCPQPSQLQNR | Probably involved in ribonucleotide reductase function. | A4TDU4 |
Q6NHJ8 | COAD_CORDI | Pantetheine-phosphate adenylyltransferase | Corynebacterium | MRKAVCPGSFDPVTMGHLDIIGRAAQQYDEVTVLVTANPNKPSGMFTVDERLALIKESTAHFVNVKVDNWAGLLVDYTTANGIDAIVKGLRTALDYEYELPMAQMNRKLAGVDTLFLMTDPQYGYISSTLCKEVTKYGGDVSDMLPPAVAAAIVEKVKS | Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. | Q6NHJ8 |
O17386 | CED8_CAEEL | Cell death abnormality protein 8 | Caenorhabditis | MFLKKHKSKLLLVPRDEEQEDAGIVAVLTDRIPSVLLVRWFDLFCFGFAMCSYALDFFSDIGIAIFHFWAGRYLSGSLVLAFALLPSVIINIISMVWMLDDEMHWKRRAHPRRTGTFELNQKRFIPLSKMIVLCICQMGPLFWYYKALYYGWMFRKSSNENTDGEKRKCFSKMVEAERDATLLRFFEAFLESAPQLIIQGSIAASYFQNYYQTGTYPYWLYFQAASLLLSIISISWSVVVQNRSLRMIRDDKVNIWPHEAVLQFCWRFLTILARIITLVALVLIFGINVVPLISVHLLVTLVHVIFLQAIHIDACTHIEKLLLLINTFIHIFIPFNMVEGNTRWRYLTAYSVEFIEMMLVCWLLPLSLNTFPYIEKVQVGVPISFIAGIAIMMMYYQFFHPNRRQLIVTQSQEDLSLNVQKSVETLTPKLESSLEISGEQNTSQDLVSELLLDVEHEN | Phospholipid scramblase that acts downstream of ced-9 and caspase ced-3 to promote phosphatidylserine exposure on apoptotic cell surface . Phosphatidylserine is a specific marker only present at the surface of apoptotic cells and acts as a specific signal for engulfment . Regulates apoptosis kinetics during embryonic development . Not required for engulfment of germ cell corpses . | O17386 |
Q92BX2 | IDI2_LISIN | Type 2 isopentenyl diphosphate isomerase | Listeria | MQKNDDLLRERRKDEHVALGVKQNENLAPSSLEDIQLIGTSIPRYNVKDIDLTTTFLGATVPFPFYINAMTGGSRHTKRINAELAEIAREVAIPMAVGSQSAALKNSSLIDTYQVVREVNPKGIILANVSPEVDIQDGIRAIEMLEADALQIHINPAQELVMQEGDRSFSHWLSRIEAYVKNSPVPVVVKEVGFGMTRETVKTLAEIGVTTVDLAGKGGTNFAQIENDRRRDQAYNFLLDWGISTGQALIDMQHADAPKIAYLASGGIRNPLDIVKALALGADSVGMAGQIISSLKKDGVSKTIEKLELWKEQLRGLFVLANAKNIAELKETPLIVSGELAKWGSLREIDLVQLANRK | Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP). | Q92BX2 |
B6J630 | DAPF_COXB1 | PLP-independent amino acid racemase | Coxiella | MKVNFTKMQGSGNDFVVIDATKTPFQLTTSQIQKMANRRFGVGFDQLLVIEPPKNNSVDFHFRIFNADGSEVGQCGNGARCIARFIRAHQLSDREELRVSTLNEVLELKIQPDGKVSVKMGVPRFEPTEIPFIASGVANFYDIAVDNQIVKLGVVNIGNPHAIIPVERINAEEVGKLGARLSVHECFPEGANVGFMQVIDPQNIRLRVYERGTGETLACGSNACAAVAVGRRCGLLQERVVVSQPGGSLTIDWQGPLTPVTMTGPATTVFCGEWLD | Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan. | B6J630 |
Q4ADG7 | MX1_OTABY | Myxovirus resistance protein 1 | Otaria | MVNSKGKITDSDPGSSHLLLNGLADKAGKNQDTEPENSLCSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLKKLLNKDEWRGKVSYQDFEMEISDPSEVEVEINKAQNAIAGEGQGISHELISLEVSSPHVPDLTLIDLPGITRVAVGNQPADIGHQTKKLIKKYILKQETINLVVVPCNVDIATTEALSMAQEVDPDGDRTIGILTKPDLVDRGTESKVVDVAQNLVCHLKKGYMIVKCRGQQDIQDQVTLTEALQKERDFFEDHPHFRVLLEEGRATVPCLADRLTSELITHICKTLPLLEKQIKENYEKITEELQKYGSDVPEEEHEKMFFLIEKINAFNHDITSLTEGEEFVGEDECRLFTKIRNEFHKWSLVIEKRFQQGYKAICKQIERFENRYRGRELPGFVNYKTFEIIIKQQIKELEEPAVYMLHTITDMVQAAFTDISEANFAEFFNLYRTTKSKIEDIKFELEKEAEKSIRLHFQMEQIVYCQDQVYQCALQRVREESDKEKDKKINSMCSKEVSSVNISLSDIFEHLLAYRQEATNRISSHIPLIIQYFILQVYGQKLQKDMLLLLHDKDTHNWLLKERSDTRDKRKLLKERLARLAQARRRLAKFPG | Interferon-induced dynamin-like GTPase with antiviral activity. | Q4ADG7 |
Q8VXG7 | PALY_MAIZE | Bifunctional phenylalanine ammonia-lyase | Zea | MAGNGAIVESDPLNWGAAAAELAGSHLDEVKRMVAQARQPVVKIEGSTLRVGQVAAVASAKDASGVAVELDEEARPRVKASSEWILDCIAHGGDIYGVTTGFGGTSHRRTKDGPALQVELLRHLNAGIFGTGSDGHTLPSEVTRAAMLVRINTLLQGYSGIRFEILEAITKLLNTGVSPCLPLRGTITASGDLVPLSYIAGLITGRPNAQAVTVDGRKVDAAEAFKIAGIEGGFFKLNPKEGLAIVNGTSVGSALAATVMYDANVLAVLSEVLSAVFCEVMNGKPEYTDHLTHKLKHHPGSIEAAAIMEHILDGSSFMKQAKKVNELDPLLKPKQDRYALRTSPQWLGPQIEVIRAATKSIEREVNSVNDNPVIDVHRGKALHGGNFQGTPIGVSMDNARLAIANIGKLMFAQFSELVNEFYNNGLTSNLAGSRNPSLDYGFKGTEIAMASYCSELQYLGNPITNHVQSADEHNQDVNSLGLVSARKTAEAIDILKLMSSTYIVALCQAVDLRHLEENIKASVKNTVTQVAKKVLTMNPSGELSSARFSEKELISAIDREAVFTYAEDAASASLPLMQKLRAVLVDHALSSGERGAGALRVLQDHQVRGGAPRGAAPGGGGRPRGVAEGTAPVANRIADSRSFPLYRFVREELGCVFLTGERLKSPGEECNKVFVGISQGKLVDPMLECLKEWDGKPLPINIK | Catalyzes the non-oxidative deamination of L-phenylalanine and L-tyrosine to form trans-cinnamic acid and p-coumaric acid respectively with similar efficiencies. Facilitates the commitment step in phenylpropanoid pathways that produce lignins, coumarins and flavonoids. | Q8VXG7 |
B5EQ29 | CLPX_ACIF5 | ATP-dependent Clp protease ATP-binding subunit ClpX | Acidithiobacillus | MAGKHEGSGEKTLYCSFCGKSQHEVRKLIAGPSVFICDECIELCNDIVKDEILDDHSEAQDKLPKPMEIRKTLDDYVIGQDVAKKVLSVAVYNHYKRLEHGGKDNEVELDKSNILLIGPTGSGKTLLAQTLARLLNVPFAMADATTLTEAGYVGEDVENIIQKLLQKCDYDVEKAQTGIVYIDEIDKITRKSENPSITRDVSGEGVQQALLKLIEGTVASVPPQGGRKHPQQEFLQVDTRHILFICGGAFAGLEKSVSARLEKGGMGFNAPLKRRDKEATAAMLMQNLEPEDLVRYGLIPEFVGRLPILALLEELDEEALISILTDPKNALVKQYQKLFALEGVTLEFRTEALRAIAKKALARKTGARGLRSILEQILLDTMYELPSMSGVKKVVVDAAVVESGTKPLLVYDDAAKVDMSHPA | ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | B5EQ29 |
Q2SWD1 | KUP_BURTA | Probable potassium transport system protein kup | pseudomallei group | MTDTNHSSMRQHSLQSLAIAAIGVVFGDIGTSPLYSLKEAFSPAHGIPLTPSAILGVISLLFWAIILVVGIKYVLFVMRADNNGEGGVLALMALSLRPLNPKSRITGLMMALGIFGACMFYGDAVITPAISVMSAVEGLEVATPQLSHLVLPITIVILIALFWIQRHGTATVGKLFGPIMVIWFVTIAALGVYHIARAPMIVSAINPYYAFSFMSEHVLLAYVVLGSVVLVLTGAEALYADMGHFGAKPIRLAAYVLVMPSLVLNYFGQGALLLLDPKAIENPFFLLAPQWAALPLVVLSTVATVIASQAVISGAYSLTSQAIQLGYVPRMKILHTSELAIGQIYVPVVNWLLLFVILCIVIGFKSSDNLAAAYGIAVTATMVITTILAAVVMVKVWNWNKLLVAMIIGVFLVIDLGFFGANLLKVEQGGWLPLGIGALLFFLLMTWYKGRHIVKERTAADGIPLAPFLQGLLAHPPHRVSGTAIYLTGNDTLVPVSLLHNLKHNKVLHERTIFMTFVTRDIPYVKDDERVTVHDAGEGLYIVKAEYGFNETPDVKAVLEEVSCQRAMTFELMDTSFFLARETVVPTHLPGMSIWRERVFAWMHQNAAKPTDFFAIPANRVVELGTKIEI | Transport of potassium into the cell. | Q2SWD1 |
Q0HLE9 | TYPH_SHESM | TdRPase | Shewanella | MFLAQEIIRKKRNGLALSAEEIQFFVKGITTNAVSEGQIAALGMAVYFNDMNMDERIALTTAMRDSGTVLNWQSLGLNGPVIDKHSTGGVGDVISLMLGPMAAACGGYVPMISGRGLGHTGGTLDKFDAIPGYQTEPSSELFRKVVKDVGVAIIGQTGDLVPADKRFYSIRDNTATVESISLITASILSKKLACSLDALAMDVKVGSGAFMPTYEASEELARSIAAVANGAGTKTTALLTDMNQVLASCAGNAVEVKEAIDFLTGAYRNPRLYAVTMGLCAEMLLLGGLATDEADARAKLNRVLDNGRAAEIFGKMVSGLGGPVDFVENYSKYLPQSQIIRPVFADTQGYAHSMDTRELGLAVVTLGGGRRKPGDALDYSVGLTQVCALGDKIDASTPIAVIHAQSEDAFAQAEEAVKKAIRIDEVAPEKTPEIYAYIRAADL | The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis. | Q0HLE9 |
A1UKU2 | ECTC_MYCSK | N-acetyldiaminobutyrate dehydratase | unclassified Mycobacterium | MIVRTTQAITGTERDVAAKDWRSKRIVLADDGVGFSFHETTINANSVSEFHYRHHVEAVWVVEGSGTLTDHETGEEFPLLPGTMYLLDGHERHRVTCHEQLRMLCVFNPPVTGQEVHDESGAYPAPVAS | Catalyzes the circularization of gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) to ectoine (1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid), which is an excellent osmoprotectant. | A1UKU2 |
A0Q1U7 | NADA_CLONN | Quinolinate synthase | Clostridium | MEIDLKDKIMKLKKEKNAVILAHFYQPKDVQEVADYIGDSYFLIDVGEKCKEDTIVFCGVKFMAESAKILSPNKKVIFPTPKAICPMANMITKEDVLKLKEKHPNAKVVCYINSTAEVKSVVDVCCTSSNAIEIVNNLESNEIIFLPDKNLGSYIQENTPNKKIILWDGYCYVHNKIKASDIIKAKEEYGNDINVLVHPECRKEVRELADYIGSTKGIINFAQNSNSKKYLIVTECGVIHELKKKNPDKEFYMLDMHCSNMKMNSIKEIYTCLKNYNNEVKIDENIKRKAVRALEKMHSL | Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. | A0Q1U7 |
Q9VAN6 | SLBP_DROME | Histone stem-loop-binding protein | Sophophora | MLCEDQHMSVENTPQKGSGSLNSSASSISIDVKPTMQSWAQEVRAEFGHSDEASSSLNSSAASCGSLAKKETADGNLESKDGEGREMAFEFLDGVNEVKFERLVKEEKLKTPYKRRHSFTPPSNENSRSNSPNSSNSSANGDAAAPKGGNNPHSRNSKKSGNFRAHKEEKRVRHNSYTSSTSSSSSYTEADPAILSRRQKQIDYGKNTAAYERYVEMVPKDERTRDHPRTPNKYGKYSRRAFDGLVKIWRKSLHIYDPPTQARDTAKDSNSDSDSD | Involved in histone pre-mRNA 3' processing and couples histone mRNA production with the cell cycle. Both maternal and zygotic proteins play an essential and vital function for development. | Q9VAN6 |
Q83HW8 | NADE_TROW8 | NH(3)-dependent NAD(+) synthetase | Tropheryma | MCCDISKTLCVKPFIDPEEEISHRVSFLADYLRHSRASGYVLGISGGQDSALAGRLCQIAVESVRSIGFDATLWAIRLPYGQQFDESDAQTAMQFISPDEELSFDIRSATDNLCVDLNRSLGSKISDFNRGNIKARLRMVVQYAVAAHHDALVVGTDHAAEAVTGFFTKFGDGAADILPLYGLTKGQGRALLKALGACDSIIEKVPTADLLDDLPCLPDETELGLQYRDIDAFLEGKPVSEDITMAITERYKSTLHKRMPPITPHSTWWRK | Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. | Q83HW8 |
Q1QV22 | YBEY_CHRSD | Endoribonuclease YbeY | Chromohalobacter | MTPDIDRQVALETATELLPTQADLEAWVGAVLARHPDTDRHELSVRFVTADESQALNRDYRGKDKPTNVLSFPFEAPPGLPLALLGDLAICHAVVVDEAAEQGKPLAHHYAHMVIHGTLHLLGYDHIDDREAEEMEALERELLAHFAIGDPYAE | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | Q1QV22 |
A8F4Q6 | RS12_PSELT | 30S ribosomal protein S12 | Pseudothermotoga | MPTINQLIRLGRERKVEKPKAPALQGNPQKRGVCVRVTTMTPKKPNSALRKIARVRLSNGIEVTAYIPGIGHNLQEHSVVLVRGGRVKDLPGIRYKIIRGTLDTAGVENRKQSRSKYGAKRPKK | Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit. | A8F4Q6 |
A4FLW9 | RHMD_SACEN | L-rhamnonate dehydratase | Saccharopolyspora | MKIRQVRALTVTGGGADYHDQAEDHWIDDHVATPMAKYPEYRASRQAFGINVLGTLVVEVEAEDGTVGVGVTTAGEPGAYIVEKHLARFVEGASVTDVEKIWDQMFNATLYYGRKGLVLNAISAVDLALYDLLGKIRQEPVYALLGGPVRDELQCYATTGRPDVAKELGFLGGKMTLQHGPAEGVEGLHANIERLRKMREQVGPDFWLMFDCWMALDVEYATRLAHAAAEYDLKWLEEALIPDDYWGYGELRRRMPSTMLMTTGEHEHTRYGFRLLLEMGRPDIIQPDVNWCGGITELIKISALADAHGAMVVPHGSSVYSYHFVITRHNSPFTEFLMMHPQATEVVPMFSPLLLDEPVPVGGRLRLPETPGFGVRLNPEVELRRPYDHD | Catalyzes the dehydration of L-rhamnonate to 2-keto-3-deoxy-L-rhamnonate (KDR). | A4FLW9 |
B5XYH9 | UBIB_KLEP3 | Ubiquinone biosynthesis protein UbiB | Klebsiella | MTPGELRRLYFIIHTFLSYGLDELIPKIRLTLPLRIWRRMLFWMPNRHQDQPLGTRLRLALQELGPVWIKFGQMLSTRRDLFPPHIADQLALLQDRVAPFEGKLAQQQIEKAMGGLPVDAWFDDFSVEPLASASIAQVHTARLKENGKEVVIKVIRPDILPIIKADMKLIYRLARWVPRLLPDGRRLRPQEVVREYEKTLLDELNLLRESANAIQLRRNFEDSPMLYVPEVYPDYCSESMMVMERIYGIPVSDVEALEAQGTNMQLLAERGVQVFFTQVFRDSFFHADMHPGNIFVSYEHPEDPQYIGIDCGIVGSLNKEDKRYLAENFIAFFNRDYRKVAELHVDSGWVPPDTNVEEFEFAIRTVCEPIFEKPLAEISFGHVLLNLFNTARRFNMEVQPQLVLLQKTLLYVEGVGRQLYPQLDLWKTAKPFLESWIKDQVGIPALVRAFKDKAPFWIERMPEIPELVYQSLQQSKQLQTSVDTIVRDMHVRHVRQGQSRYLFGIGAVLLLSGTLLFIHRPEWGMMPGWLMAGGVVTWLIGWRKTH | Is probably a protein kinase regulator of UbiI activity which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis. | B5XYH9 |
Q9NFZ3 | GBGE_DROME | Guanine nucleotide-binding protein subunit gamma-e | Sophophora | MDPSALQNMDRDALKKQIENMKYQASMERWPLSKSIAEMRSFIEENEKNDPLINAPDKKNNPWAEKGKCVIM | Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. This subunit functions in visual transduction in the compound eye. | Q9NFZ3 |
C3K1P8 | CHED_PSEFS | Probable chemoreceptor glutamine deamidase CheD | Pseudomonas | MKKPVGTTEVILAPGQVSFATRPTRLRTLLGSCVAITFWHPQRLIGGMCHFMLPGRLRKHQPLDGRYADEALELLLRHAQVNGTHARDYQVKLFGGGEMFPDLHRRLPTQDVASLNIRAALALAERYHLHLTAQDMGSTGYRTIMFDLWNGNVWVRHQPMGLLQEDAYQKNQCAGGR | Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis. | C3K1P8 |
A3P027 | HIS6_BURP0 | ImGP synthase subunit HisF | pseudomallei group | MALAKRIIPCLDVTAGRVVKGVNFVELRDAGDPVEIARRYDAQGADELTFLDITATSDGRDLILPIIEAVASQVFIPLTVGGGVRAVEDVRRLLNAGADKVSMNSSAVANPPLVRDAADKYGSQCIVVAIDAKRVSADGEPPRWEVFTHGGRKGTGLDAVEWARKMAELGAGEILLTSMDRDGTKAGFDLALTRAVSDAVPVPVIASGGVGSLEHLAAGITEGHADAVLAASIFHYGEHTVGEAKRFMAERGIAVRL | IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit. | A3P027 |
Q02ML8 | CAS3_PSEAB | CRISPR-associated nuclease/helicase Cas3 subtype I-F/YPEST | Pseudomonas | MNILLVSQCEKRALSETRRILDQFAERRGERTWQTPITQAGLDTLRRLLKKSARRNTAVACHWIRGRDHSELLWIVGDASRFNAQGAVPTNRTCRDILRKEDENDWHSAEDIRLLTVMAALFHDIGKASQAFQAKLRNRGKPMADAYRHEWVSLRLFEAFVGPGSSDEDWLRRLADKRETGDAWLSQLARDDRQSAPPGPFQKSRLPPLAQAVGWLIVSHHRLPNGDHRGSASLARLPAPIQSQWCGARDADAKEKAACWQFPHGLPFASAHWRARTALCAQSMLERPGLLARGPALLHDSYVMHVSRLILMLADHHYSSLPADSRLGDPNFPLHANTDRDSGKLKQRLDEHLLGVALHSRKLAGTLPRLERQLPRLARHKGFTRRVEQPRFRWQDKAYDCAMACREQAMEHGFFGLNLASTGCGKTLANGRILYALADPQRGARFSIALGLRSLTLQTGQAYRERLGLGDDDLAILVGGSAARELFEKQQERLERSGSESAQELLAENSHVHFAGTLEDGPLREWLGRNSAGNRLLQAPILACTIDHLMPASESLRGGHQIAPLLRLMTSDLVLDEVDDFDIDDLPALSRLVHWAGLFGSRVLLSSATLPPALVQGLFEAYRSGREIFQRHRGAPGRATEIRCAWFDEFSSQSSAHGAVTSFSEAHATFVAQRLAKLEQLPPRRQAQLCTVHAAGEARPALCRELAGQMNTWMADLHRCHHTEHQGRRISFGLLRLANIEPLIELAQAILAQGAPEGLHVHLCVYHSRHPLLVRSAIERQLDELLKRSDDDAAALFARPTLAKALQASTERDHLFVVLASPVAEVGRDHDYDWAIVEPSSMRSIIQLAGRIRRHRSGFSGEANLYLLSRNIRSLEGQNPAFQRPGFETPDFPLDSHDLHDLLDPALLARIDASPRIVEPFPLFPRSRLVDLEHRRLRALMLADDPPSSLLGVPLWWQTPASLSGALQTSQPFRAGAKERCYALLPDEDDEERLHFSRYEEGTWSNQDNLLRNLDLTYGPRIQTWGTVNYREELVAMAGREDLDLRQCAMRYGEVRLRENTQGWSYHPYLGFKKYN | In this bacteria Y.pestis-subtype CRISPRs do not confer resistance to phage DSM3 or MP22, but instead are required for DMS3-dependent inhibition of biofilm formation and possibly motility. | Q02ML8 |
B6YS29 | MRAY_AZOPC | UDP-MurNAc-pentapeptide phosphotransferase | Candidatus Azobacteroides | MLYSLFYFLSSLNVPGARLFRYISFRSVLSFSLSLIISVLIGERIIRFLQRHQAGETIRNLGLEGQIQKKGTPTMGGIIIIIAILIPVLLLARLSNIYVLLMLITTIWLGILGLIDDCIKVIWKHKEGLSGKIKIIAQVGLGLIVGLIVYLSPNIVMYENVEIRQQGGRKTVSYTPPLKSTQTTVPFFKNNNLDYRDLTAFMTNHRTAATWILFVLITVFIVTAVSNGANLTDGLDGLTAGSSAIIGVVLGILAYVSANLGFAAYLNIMYIPGCGELTVFASAFVGACMGFLWHNAFPAQVFMGDIGSLTLGGIIAVFAIIIHKELLLPMLCGIFFTESLSVMIQVAYFKYSKRKTGMGKRIFKMTPIHHHFQKGGSEEVNVIIQKPLNAIPESKIVVRFWLIGILLAALTVVTLKIR | Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I. | B6YS29 |
Q8WV07 | LTO1_HUMAN | Tumor-amplified and overexpressed sequence 1 | Homo | MAGSQDIFDAIVMADERFHGEGYREGYEEGSSLGVMEGRQHGTLHGAKIGSEIGCYQGFAFAWKCLLHSCTTEKDSRKMKVLESLIGMIQKFPYDDPTYDKLHEDLDKIRGKFKQFCSLLNVQPDFKISAEGSGLSF | The complex LTO1:YAE1 functions as a target specific adapter that probably recruits apo-ABCE1 to the cytosolic iron-sulfur protein assembly (CIA) complex machinery . May be required for biogenesis of the large ribosomal subunit and initiation of translation . May play a role in the regulation of proline metabolism and ROS production . | Q8WV07 |
Q7WRB8 | RL16_BORBR | 50S ribosomal protein L16 | Bordetella | MLQPSRRKYRKEQKGRNTGLASRGTHVSFGEFGLKATGRGRLTARQIEAARRAINRHIKRGGRIWIRIFPDKPISQKPAEVRMGNGKGNPEYWVAEIQPGKVLYEMEGVSEELAREAFRLAAAKLPISTTFVARHIGA | Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs. | Q7WRB8 |
Q6LXB7 | SECE_METMP | Protein transport protein Sec61 gamma subunit homolog | Methanococcus | MQKSKLNTTLNGLKDFLHQCRRVLMISRKPTRQEYITISKVTGLGICLLGFVGFVIHVPITYLKALIKP | Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation. | Q6LXB7 |
P10251 | KAD_MYCCT | Adenylate monophosphate kinase | Mycoplasma | MNIMLLGAPGCGKGTQAEQLVNKLNFIQVSTGDLMRKEISLNTTLGLKCQEYMNAGKYVPDQIVNQIVNQFLQYNNDKLIFDGYPRTLEQAKSLEKMLDLYNKKIDYVFYIDVNEQILIKRITNRLVCPLCKASFNLETRKPKQEGLCDFDNTKLVKRSDDSLDKVKIRLQTYKEQTLPLIDYFKTNSKFIEIKADNLSAEQVFNQIKGELKI | Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. | P10251 |
P95200 | NDHA_MYCTU | Type II NADH dehydrogenase NdhA | Mycobacterium tuberculosis complex | MTLSSGEPSAVGGRHRVVIIGSGFGGLNAAKALKRADVDITLISKTTTHLFQPLLYQVATGILSEGDIAPTTRLILRRQKNVRVLLGEVNAIDLKAQTVTSKLMDMTTVTPYDSLIVAAGAQQSYFGNDEFATFAPGMKTIDDALELRGRILGAFEAAEVSTDHAERERRLTFVVVGAGPTGVEVAGQIVELAERTLAGAFRTITPSECRVILLDAAPAVLPPMGPKLGLKAQRRLEKMDVEVQLNAMVTAVDYKGITIKEKDGGERRIECACKVWAAGVAASPLGKMIAEGSDGTEIDRAGRVIVEPDLTVKGHPNVFVVGDLMFVPGVPGVAQGAIQGARYATTVIKHMVKGNDDPANRKPFHYFNKGSMATISRHSAVAQVGKLEFAGYFAWLAWLVLHLVYLVGYRNRIAALFAWGISFMGRARGQMAITSQMIYARLVMTLMEQQAQGALAAAEQAEHAEQEAAG | Alternative, nonproton pumping NADH:quinone oxidoreductase that delivers electrons to the respiratory chain by oxidation of NADH and reduction of quinones. | P95200 |
Q8M9Y1 | TILS_CHAGL | tRNA(Ile)-lysidine synthetase | Chaetosphaeridium | MNHFNLKLIKRIQNDLIKYNLLKPKKSILIAISGGQDSIVLLKILSILQIQWKWKLSIIYCDHQWNIYSKNQAFHLYKVSFQMGIPFYHGVTIKPLRTEKSARIWRYSVFQRIASISKFNVIVTAHSSTDRVETFLYNLFRGTGVQGLQSLTWKKNIQFEILPNFARSKKSFDLKILSLESKNGIQTYSDYNKLQLIRPLLNITRTELGKFCSNENLPLWPDLTNYNLSIIRNRIRYQTMPYLKIYFNCNLEKILAQIAEILYSENLYFENLSKKIMLKISFEEINSKKLSLSLFKILPLALQRRIIKFFFENHFSKILDFRDIEEIRYYILNLSNNSKFL | Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. | Q8M9Y1 |
Q6NY82 | UBE2F_DANRE | Ubiquitin-conjugating enzyme E2 F | Danio | MLTLASKLKREEGVRAGRTPAGSNDAAHRVSIRDRLLIKEVAELEANLPSTCKVTFPDENKLCHFQLAISPDEGYYLGGKFQFEIEVPEAYNMVPPKVKCLTRIWHPNIAETGEICLSLLREHSIDGTGWAPTRTLKDVVWGLNSLFTDLLNFDDPLNIDAAEHHLRDKEDFRNKVQDFIKNYAR | 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. | Q6NY82 |
B2I6G9 | NAGZ_XYLF2 | N-acetyl-beta-glucosaminidase | Xylella | MLLIGVAGTTLSAQEVDWLQDDAVAGVVLFKRNFASRAQIVELSAALREAAPRPLLLAVDQEGGRVQRFHEGYSALPPLQGIGALYVRDPEAALELAFEHAWLMASEVRASGVDLSFAPVVDLGRGNRAIGDRAFSDDPHVVAAFAKAYVQGMHAAGMPVTLKHFPGHGSVLEDTHVDLAVDVRALETLESEDLVPFAAGIAAGADAVMMAHVVYPNVAPEPAGFSAHWIEVILRGRMGFRGVVFSDDIGMAAVRGVGGVVGCVHAHLDAGCDVVLVCHPELVNDALSAVAGRRSNTAALIGLIGRGVLGWDGLLADVRYGSIQSHLFERFGTST | Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides. | B2I6G9 |
Q7CNU3 | OMP2A_BRUME | Porin Omp2a | Brucella | MNIKSLLLGSAAALVAASGAQAADAIVAPEPEAVEYVRVCDAYGAGYFYIPGTETCLRVHGYVRYDVKGGDDVYSGTDRNGWDKGARFALMFNTNSETELGTLGTYTQLRFNYTSNNSRHDGQYGDFSDDRDVADGGVSTGTDLQFAYITLGGFKVGIDESEFHTFTGYLGDVINDDVVAAGSYRTGKIAYTFTGGNGFSAVIALEQGGEDVDNDYTIDGYMPHVVGGLKYAGGWGSIAGVVAYDSVIEEWATKVRGDVNITDRFSVWLQGAYSSAATPNQNYGQWGGDWAVWGGAKFIAPEKATFNLQAAHDDWGKTAVTANVAYQLVPGFTITPEVSYTKFGGEWKDTVAEDNAWGGIVRFQRSF | Forms passive diffusion pores that allow small molecular weight hydrophilic materials across the outer membrane. | Q7CNU3 |
E0SHN8 | LPOB_DICD3 | Penicillin-binding protein activator LpoB | Dickeya | MKKYLGIVLMALVIAGCTSRVPQTEQPATIEPAVPTPSKPQLPPSESQPLPTPPKIQVPVLDWSAAVTPLVGQMVKTDGIARGSILLLNKLKNNTNGSLQTAQATTALYNALASSGQFTMVSREQLGVARQSLGLSEEDSLESRSKAVGLARYVGAQYVLYADASGDVKSPELSMQLMLVQTGEIVWSGNGTVRQQ | Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1B (PBP1b). | E0SHN8 |
Q74JK1 | RNH2_LACJO | Ribonuclease HII | Lactobacillus | MTITEIKNLLQGEVSKEQLEELKADERKGVQKLLISYEKRQAKYAKALAQFQSRFSYEKEFWQKDQLVAGVDEVGRGPLAGPVVTAAVILPHDFDLIDVNDSKKLSPKKRQALFPKILEKAVSVSVGLANNDVIDQINIYEADRLAMAHAVQGLKVKPDALLVDAMNVPLNIPQVKLIHGDAKSNSIAAASIVAKVFRDNLMDAYGELYPEYDFKHNAGYGTREHMEALEKYGPTPIHRRSFAPVSEYEK | Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. | Q74JK1 |
Q09768 | GSH1_SCHPO | Gamma-glutamylcysteine synthetase | Schizosaccharomyces | MGLLVLGTPLDWPESKKYCDYVRENGIMQFLHMYDTYISKKQDVLLWGDEIECIVVSMDDKSKKARVSLRQEDILNALGKYEETFRHVDFGPVYAALRNETCPKKIDAILSEVAKNPADYVERIGGNSNKDTIEITSSTKPHAQNAVPTFHPEYGRYMLESTPGAPYGSTLKDFTFVEYNMRLRRKIIENHLLPNELPLTITNFFRLGTPGFTDPEVEANGAISRSFFLPDDVINTHVRFPTLTANIRQRRGRKVAMNVPIFFDKNTIKPFHDPTVPWDRNLFPEDANARDGAALDNHIYMDSMGFGMGCCCLQITFQAKSCDEARLLYDQLTPITPLMLALSAGTPAFRGYLADQDCRWNVIAGAVDDRTEEEMKTVPKSRYDSVDLYISNDKRNLPEYNDVPVVINQDCYDKLIKDCIDERLAKHMAHIFSRDPLVIFSDSILQDNSVSNAHFENLNSTNWQSMRFKPPPPGSDIGWRVEFRSMEIQITDFENAAYSIFVVMLSRAILSFNLNLYMPISLVDENMKAAHARDAIHRKKFWFRCNPFPDASTDDESGQFRQLTIDELFNGEHRENGFPGLITIVRSYLYSCNPDAKTICLIERYIRLISQRANGQCLTAASWIRNFITTHPSYKQDSVVNDEINYDLIRRIAKIVDGDYDDTLLGKCS | Catalyzes the ATP-dependent ligation of L-glutamate and L-cysteine and participates in the first and rate-limiting step in glutathione biosynthesis. | Q09768 |
A5EKQ4 | YQGF_BRASB | Putative pre-16S rRNA nuclease | unclassified Bradyrhizobium | MPAPILPLIEAASRWPERGALVGLDLGTKTIGVAVSDPDRRLATGVETIQRKAFKADAARLLAISSERKVVGFVLGLPINMDGSEGPRAQSTRAFARNLANLTDLPIGLWDERLSTAAVERELIGMDVSRARRAEVIDTHAAIFILQGALDRLATLRRSGQ | Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. | A5EKQ4 |
A8CG89 | PA2B1_DABRR | Phosphatidylcholine 2-acylhydrolase | Daboia | MRTLWIVAMCLIGVEGNLFQFARMIDAKQEAFSFFKYISYGCYCGWGGQGTPKDASDRCCFVHDCCYARVKGCNPKLVEYSYSYRTGKIVCETYNRCKRAVCECDRVAAICLGQNVNTYNKGYMFLSSYYCRQKSEQC | Exhibits high hydrolytic activities and shows strong preference for the anionic micelles (dPPC with deoxycholate) to the zwitterionic micelles (dPPC with Triton X-100). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. | A8CG89 |
Q3IGW5 | SUCC_PSET1 | Succinyl-CoA synthetase subunit beta | Pseudoalteromonas | MNLHEYQAKQLFAEYGLPVSTGYACDTPEEAAAAAEKIGGDMWVVKTQVHAGGRGKAGGVKLVKTIDEVKAFAANWLGKNLVTYQTDEKGQPVAKILVESCTDIANELYLGAVVDRASRKVVFMASTEGGVEIETVAEETPELIHKAEIDPLVGPQAYQARELGFKLGLNPVQMKQFVKIFMGLGKMFTDFDFALLEINPLVITDEGNLHCLDGKIGIDGNALYRQPKIREFHDPSQEDSREAHAASFELNYVALDGNVGCMVNGAGLAMGTMDIVNLHGGKPANFLDVGGGATKERVSEAFKIILSDDNVKAVLVNIFGGIVRCDMIAEGIIGAVKEVGVNVPVVVRLEGTNAELGREVLKNSGLDIIAAESLTDAAEKVVAAAEGK | Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. | Q3IGW5 |
B4RBP5 | BIOB_PHEZH | Biotin synthase | Phenylobacterium | MNAHVRPVDPANVDPAQPRHDWTLEEVEALFELPFTELVFRAAEVHRRWFDPTELQLSQLLSVKTGGCPEDCGYCAQSQKFKTGLAASKLMEAETVIAAAAEAKAGGAQRFCMGAAWRDLKDRDLPKVAAMISGVKALGLETCATLGMLTADQAKALKAAGLDYYNHNLDTGPDYYDKVVTTRTYQDRLDTLAAVRDAGMATCCGGIVGMGETRRDRAGLLHQLATLPAHPDSLPINDLMPIPGTPLGDSKAVDPLEFVRMIAVARIVCPKSMVRIAAGREHMTKELQALCFLAGANSIFVGARLLTTDNPEKTADEALLADLKMKPMAMA | Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism. | B4RBP5 |
Q40611 | ATPA_OCHNE | F-ATPase subunit alpha | Ochrosphaera | MINIRPDEISNIIRQQIESYDQEVQIDNVGTVLQVGDGIARVYGLEQVMAGELLEFEDKTVGIALNLENDNVGVVLMGPGLDILEGGSVRSTGKIAQIPVGDGFLGRVVDSLARPIDGKGDIDATESRLVESMAPGIITRKSVCEPVQTGITAIDSMIPIGRGQRELIIGDRQTGKTSVAIDTIINQKSEDVICVYVAIGQKASSVASIVTTLEEKGALGYTIVVASNADDPATLQYIAPYTGAALAEYFMYKGKATLIIYDDLSKQASAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDALGGGSMTALPIIETQAGDVSAYIPTNVISITDGQIFLSGDLFNAGIRPAINVGISVSRVGSAAQTKAMKQVAGKLKLELAQFAELEAFSQFASDLDAATQAELARGQRLREMLKQPQNSPIPVEEQVALI | Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | Q40611 |
Q5NPY8 | AROB_ZYMMO | 3-dehydroquinate synthase | Zymomonas | MSSEVSKTVTVPIDLGNHSYKIDIGAGLYQQAVSILTPYVRNRRFIVITDENVARCQLPEFEKSFHEAGVTVDSIILPAGEATKSWHHLAELCDQLIRRGVERRDAIIALGGGVIGDLVGFAAAILKRGCQFIQIPTSLLAQVDSSVGGKTAINCEAGKNLIGAFHQPVFVLIDPDALQTLPARQLRAGYGEIIKYGLIDDPDFFAWCEEHGAALIEGDKASRLYAIEHSIRAKALIVADDEKEISGKRALLNLGHTFGHALEADTGFSDKLFHGEAVAAGSALAFGFSYVKNLASKEDIQRIIKHLRETGLPASLEEAGVKASGKELVAHMMHDKKMEAGRLPFLLARGIGKSFLDKEVNLEEIAAFLDSPLARKGTI | Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). | Q5NPY8 |
B1AXV0 | FRS1L_MOUSE | Ferric-chelate reductase 1-like protein | Mus | MAGQPLRRPAWVPLLLRLLLAGIAACDASPADDSAGPGGRGPRGRARGDAGADEAVPRHDSSYGTFASEFYDLRYLSEEGYPFPTAPPVDPFAKIKVEDCGRTKGCFRYGKPGCNAETCDYFLSYRMIGADVEFELSADTDGWVAVGFSSDKKMGGDDVMACVHDDNGRVRIQHFYNVGQWAKEVQRNPARDEEGVFENNRVTCRFKRPVNVPRDETIVDLHLSWYYLFAWGPAIQGAITRHDIDSPPASERVVSIYKYEDIFMPSAAYQTFSSPFCLLLIVALTFYLLMGTP | Important modulator of glutamate signaling pathway. | B1AXV0 |
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