habdine/Prot2Text-Data · Datasets at Hugging Face

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
Q8CWR2	TRUB_STRR6	tRNA-uridine isomerase	Streptococcus	MNGIINLKKEAGMTSHDAVFKLRKILGTKKIGHGGTLDPDVVGVLPIAVGKATRMVEFMQDEGKIYEGEIILGYSTTTEDASGEVVAETPVLSSLDEKLVDEAIASLTGPITQIPPMYSAVKVNGRKLYEYARAGQEVERPERQVIIYQFERTSPISYDGQLARFTFRVKCSKGTYIRTLSVDLGEKLGYAAHMSHLTRTSAAGLQLEDALALEEIAEKVEAGQLDFLHPLEIGTGDLVKVFLTPEEATEVRFGRFIELDQTDKELAAFEDDKLLAILEKRGNLYKPRKVFS	Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.	Q8CWR2
Q83MJ8	TRUB_SHIFL	tRNA-uridine isomerase	Shigella	MSRPRRRGRDINGVLLLDKPQGMSSNDALQKVKRIYNANRAGHTGALDPLATGMLPICLGEATKFSQYLLDSDKRYRVIARLGQRTDTSDADGQIVEERPVTFSAEQLAAALDTFRGDIEQIPSMYSALKYQGKKLYEYARQGIEVPREARPITVYELLFIRHEGNELELEIHCSKGTYIRTIIDDLGEKLGCGAHVIYLRRLAVSKYPVERIVTLEHLRELVEQAEQQDIPAAELLDPLLMPMDSPASDYPVVNLPLTSSVYFKNGNPVRTSGAPLEGLVRVTEGENGKFIGMGEIDDEGRVAPRRLVVEYPA	Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.	Q83MJ8
B6YT21	RS7_THEON	30S ribosomal protein S7	Thermococcus	MAKPLTERFYQPKELKVMGRWSVEDVVVNDPSLRPYINLEPRILPHSHGRHAKKPFGKAQVHIVERLINKVMRSGASSHKVGGHFMRREHRSLMGKKMKAYEVVKEAFMIIERRTKQNPIQVFIRAIENSAPREDTTTIAFGGIRYHMAVDVSPLRRLDIALKNIALGASAKCYRNKTSYAQALAEEIIAAANKDPKSFAYSKKEEIERIAQSSR	One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center.	B6YT21
D0MY11	ITPA_PHYIT	Nucleoside-triphosphate pyrophosphatase	Phytophthora	MSSAKPVLTFVTGNANKLKEVVAILGADFPFELRNQAVDLPELQGEPADIAKEKCRLAAKQVQGAVLVEDTSLCFNALKGLPGPYIKWFLEKTGHDGLNNMLAAYEDKSAYAQCIFAYAPAGAEPQVFVGQTHGKIVPARGPTTFGWDPVFQPDGFEQTYAEMEKVTKNQISHRYKALEALKTHLVKPVDK	Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.	D0MY11
B1JXI7	KYNB_BURCC	N-formylkynurenine formamidase	Burkholderia cepacia complex	MDTLWDISPPVSPATPVWPGDTPVAVERVWRMEAGSPVNVARLTLSPHTGAHCDAPLHYDADGAPIGAVPLDTYLGPCRVIHCIGASPVVRPADVEVALDGVPPRVLLRTYARAAVEQWDSAFCAVAPDTVDLLAAHGVKLIGIDTPSLDPQESKTMDAHHRVRAHRMAILEGIVLDDVPPGDYELIALPLKFATLDASPVRAVLRALPAHAS	Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation.	B1JXI7
Q31UK6	GPPA_SHIBS	pppGpp-5'-phosphohydrolase	Shigella	MGSTSSLYAAIDLGSNSFHMLVVREVAGSIQTLTRIKRKVRLAAGLNSENALSNEAMERGWQCLRLFAERLQDIPPSQIRVVATATLRLAVNAGDFIAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADQRLVVDIGGASTELVTGTGAQTTSLFSLSMGCVTWLERYFADRNLGQENFDAAEKAAREVLRPVADELRYHGWKVCVGASGTVQALQEIMMAQGMDERITLEKLQQLKQRAIHCGRLEELEIDGLTLERALVFPSGLAILIAIFTELNIQCMTLAGGALREGLVYGMLHLAVEQDIRSRTLRNIQRRFMIDIDQAQRVAKVAANFFDQVEKEWHLEAISRDLLISACQLHEIGLSVDFKQAPQHAAYLVRNLDLPGFTPAQKKLLATLLLNQTNPVDLSSLHQQNAVPPRVAEQLCRLLRLAIIFASRRRDDLVPEMTLQANHELLTLTLPQGWLTQHPLGKEIIAQESQWQSYVHWPLEVH	Catalyzes the conversion of pppGpp to ppGpp. Guanosine pentaphosphate (pppGpp) is a cytoplasmic signaling molecule which together with ppGpp controls the 'stringent response', an adaptive process that allows bacteria to respond to amino acid starvation, resulting in the coordinated regulation of numerous cellular activities.	Q31UK6
Q6CMD3	RTC5_KLULA	Restriction of telomere capping protein 5	Kluyveromyces	MGQSTSKEHENARTNESKLKGESLMDFFNDRCLKQLTTAELISFKNNIPEGKELNDYVEVSDISRMYYIPKDSAVMLSVFMNMFHTLANFPLLQDSYEKVTFKTLLKATLLLVKERAIKYTDWKKYNDLKMLFITLSLEKNIKAEPLMDSSALSDCKDWKGVIRSYNGTDFDELKVNANNLLHFLALILALSRCCILNNCKIDNDVLAKSLEDFKHQALNIVRTMNPEIISMSDCLDSSITYTQFSMAVNDVAPNLLNPLKMLMEHVLYMDRDLVDADVLQPISNPTKIVNESELSQLATFLPKEIVFSRFQKLYVGRESGFSMRSFQSKVFKWMAPTILFVEGMRIRDEDDEDGDAYAVKNPRYRNFLQEYGKLKSEDQHLDTLSKKKRKLLFAVCIRDPWKVSNKDLFGDSSTKIIQLHPRQEIFDADPFKTGNVYFNTVGGGIGIGSSQPIIKANGKKYFPGNVSLTIDSSLEFGIFRHLGAGGSFKPGRLISGRGEERNSFEYRFIIQDVEVWGCGGEKELEEQVKQWQWEEAEAKRRQKINLQSMGEDRALLEMAGLVGQHQSGGSI	May be involved in a process influencing telomere capping.	Q6CMD3
Q7CHH5	SCMU_YERPE	*YpCM	Yersinia	MQPTHTLTRLTVIGKLIIASSFFLSLAVQAQQCGQTAPLINERLSYMKDVAGYKAENHLPIEDRIQEEKVINSAMAQAESLGLNGESIKPLMVAQINAAKAIQYRYRADWLSQPEPGWQPKPLDDVRANIGELSTKILEQIAEELKTCKPAEMGDKAHFINTIRQHNLTSADVEAIFSTFNQVKLK	Catalyzes the Claisen rearrangement of chorismate to prephenate. May play some role in the pathogenicity.	Q7CHH5
A6TFK4	SECB_KLEP7	Protein-export protein SecB	Klebsiella	MSEQNSTEMTFQIQRIYTKDISFEAPNAPQVFQKDWQPEVKLDLDTASTQLAEGVYEVVLRVTVTAALGEETAFLCEVQQGGIFSIDGIEGTQMAHCLGAYCPNILFPYARECITSLVSRGTFPQLNLAPVNFDALFMNYLQQQAGEGAEQHQDA	One of the proteins required for the normal export of preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. It also specifically binds to its receptor SecA.	A6TFK4
Q4FQ35	ATPA_PSYA2	F-ATPase subunit alpha	Psychrobacter	MQQLNPAEISNLIKQRIQDLDAGATAKNEGTIVKVSDGIVQIHGLEDAMYGEMIEFEGEVYGMALNLERDSVGAVVLGDFLKLQEGQKAYCTGRILEVPVGPELLGRVVDALGNPIDGKGPINAKMTDKVEKIAPGVIDRQSVDQPVMTGYKSVDTMIPIGRGQRELIIGDRQTGKTAMAIDAIIAQKASGIKCVYVAIGQKRSTIANVVRKLEQTGALEYTTVVVASASEPAALQYIAPYSGCTMGEYFRDRGEDALIVFDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERASRVNAAYVEKFTNGEVVGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLESSLFNSGIRPAVNAGISVSRVGGAAQTKIIKKLSGGIRTALAQYRELAAFAQFASDLDDATREQLDHGERVTELMKQKQYQPMSISEQAAVIYASNEGFLADVPVEKIGSFEEAYLRYMHDEQADLMKEIDDTANYNDDIAGRLKLSLETFKQNHSY	Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.	Q4FQ35
B1VV20	PSD_STRGG	Phosphatidylserine decarboxylase beta chain	Streptomyces	MPDSTSSASRGGVRIARGASPWLLPTVATAALSLARARKSGRWAAVAVPTTALAAGMLWFFRDPEREITDGRVISPADGVVQSIMPWKDGRTRVAIFMSPLNVHVNRAPLAGTVTSVEHIPGGFVPAFNKESENNERVVWHFDTELGDIEMVQIAGAVARRIVPYLPEGTKVEQGERIGLIRFGSRVDIYLPEGIDVAVEVGQATTAGVTRIDRD	Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).	B1VV20
A6BM29	PSBB_GNEPA	Protein CP-47	Gnetum	MGLPWYRVHTVVLNDPGRLIAVHIMHTALVAGWAGSMALYELAVFDPSDPVLDPMWRQGMFILPFMTRLGIKESWGGWSITGESAVNPGLWSYEGVAGAHIVFSGLCFLSAIWHWVYWDLEIFSDPRTGKPSLDLPKIFGIHLFLSGVACFGFGAFHVTGLYGPGIWVSDPFGLTGRIQPVSPAWGAEGFDPFVPGGIASHHIAAGLLGIIAGLFHLSVRPPQRLYRGLRMGNIETVLSSSIAAVFFAAFIVAGTMWYGSATTPIELFGPTRYQWDQGYFQQEIDRRVRAGLTEKLSLSEAWSRIPEKLAFYDYIGNNPAKGGLFRAGAMDNGDGIAVGWLGHPIFRDKEGNELFVRRMPTFFETFPVVLVNKEGIVKADVPFRRSESKYSVEQVGVTVEFYGGELNGVSFSDPAIVKKYARRAQLGEIFELDRATLKSDGVFRSSPRGWFTFGHATFALLFFFGHIWHGARTLFRDIFAGIDPELDAQVEFGAFQKLGDPTTKRQVV	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.	A6BM29
Q3UND0	SKAP2_MOUSE	Src-associated adapter protein with PH and SH3 domains	Mus	MPNPSCTSSPGPLPEEIRNLLADVETFVADTLKGENLSKKAKEKRESLIKKIKDVKSVYLQEFQDKGDAEDGDEYDDPFAGPADTISLASERYDKDDDGPSDGNQFPPIAAQDLPFVIKAGYLEKRRKDHSFLGFEWQKRWCALSKTVFYYYGSDKDKQQKGEFAIDGYDVRMNNTLRKDGKKDCCFEICAPDKRIYQFTAASPKDAEEWVQQLKFILQDLGSDVIPEDDEERGELYDDVDHPAAVSSPQRSQPIDDEIYEELPEEEEDTASVKMDEQGKGSRDSVHHTSGDKSTDYANFYQGLWDCTGALSDELSFKRGDVIYILSKEYNRYGWWVGEMKGAIGLVPKAYLMEMYDI	May be involved in B-cell and macrophage adhesion processes. In B-cells, may act by coupling the B-cell receptor (BCR) to integrin activation. May play a role in src signaling pathway.	Q3UND0
Q9V0N9	PSB2_PYRAB	Proteasome core protein PsmB 2	Pyrococcus	MLQLTEKFKGTTTVGIVCSDGVVLAADRRASLGNIVYAKNVTKIHKIDEHLAIAGAGDVGDILNLVRLLRAEAKLYYAQSGKRMSVKALATLLANMLNGARMLPYLAWFLVGGFDEKPRLYSVDMMGGITEDKYVAAGSGMEFAYSVLDSEYREDLKVREGIKIAVEAINSAIKRDVFSGDGIMVVTITEEGYRELSNSRLKAILRQ	Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.	Q9V0N9
Q6CSC1	IML2_KLULA	Inclusion body clearance protein IML2	Kluyveromyces	MFRVFNALTGAGSPKATELSGEERTKFILQQAHDFEIALQAMDYVLDDNAEVGLKLLADNQATSPGDATVGALAKGVIEFLEATLGFEPEVMKKASTTLAEAEQLSLKSRAKLQKLNIKTSSLYPPGTEYAVTYTESCLLHALLMLFSESMVEGAKALFKLRKAYHMLQDILKEINASEKRKRSSIYLQEINESTASFISSGTCFTSYDIPYKLTPEEEQDKELLDLANKVYSLRRKRLCGAHIGNSPAINRLRDDVGAASLKKGSDEETQEFQLLSDNANINQATMDEFIHSGVNLCFGILQVVLSLIPPAIGAVLSVVGFHGSREEGLRLVWKSTKDRNIHGGIGLLGLLFYYDGPFQFTDIDFDIPAARDDNLPVTEMDRPTLLHPGKILTSALLQARALFPNSALWLLQEARMLSKQGRLKEAVDLLDSIDHNTIEMKQVKALIVFEKATTLVYMHEFERGAETMLIMLSISEWSHALYTYFAGCCYLEMFRKYEMGILNGENAAEKKAYYKERATNLVFESANMVGKKKFMSKILPLDRFLLRKVDQFKKFQNIIKSSDPLDSIGVSPVHELIYFYNGYNRMTMKELNLSLKSLTEYRNPTIDLQNPDQELIKDLLTSLVLRRTGKIEEGCKILDTQVLPQLFTIQNDKVKYIKKTEDPWVYPTAFYERALFSWKLKGMNGLHEAHEWLIRAQNYQDDYELSTRIGMKIKAAKDRVEESI	Inclusion body (IB) resident protein that interacts strongly with lipid droplet (LD) proteins. Involved in LD-mediated IB clearing after protein folding stress, probably by enabling access to the IBs of an LD-stored soluble sterol derivative that acts as chaperone in inclusion clearing.	Q6CSC1
Q2LUK6	RL25_SYNAS	General stress protein CTC	Syntrophus	MEARELKANVRKESGKEQARRMRREGLIPAVLYGPGTDPVSLSVNASDLKTALKGAEENVLIKLIIDDSGRLMEKNSLIRELQIEPLTNNFFHADFYALRMDQESTFDVPIHFEGQPVGIEKGGELQYLKREIKVSCLPSELPDCITVDISRLDVGDAVLIGDLSLSESIRCFDSKDIVLVTIAALHGVNKAEETEEASS	This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance.	Q2LUK6
Q884C9	UVRB_PSESM	Excinuclease ABC subunit B	Pseudomonas	MSEFQLVTRFEPAGDQPEAIRQLVEGIDAGLAHQTLLGVTGSGKTFSIANVISQIKRPTLVLAPNKTLAAQLYGEFKAFFPNNAVEYFVSYYDYYQPEAYVPSSDTFIEKDASINDHIEQMRLSATKALLERKDAIIVTTVSCIYGLGSPETYLRMVLHVDRGDKLDQRALLRRLADLQYTRNDMDFARATFRVRGDVIDIYPAESDLEAIRIELFDDEVESLSAFDPLTGEVIRKLPRFTFYPKSHYVTPRETLVEAMEGIKVELQERLEYLRSQNKLVEAQRLEQRTRFDLEMMLELGYCNGIENYSRYLSGRPSGAPPPTLFDYLPADALLVIDESHVSVPQVGAMYKGDRSRKETLVEYGFRLPSALDNRPMRFDEWEAISPQTIFVSATPGNYEAEHAGRIVEQVVRPTGLVDPQIEIRPALTQVDDLLSEIHKRAALEERVLVTTLTKRMSEDLTDYLSDHGVRVRYLHSDIDTVERVEIIRDLRLGTFDVLVGINLLREGLDMPEVSLVAILDADKEGFLRSDRSLIQTIGRAARNLNGRAILYADRITGSMERAIGETERRREKQIAFNLEHGITPKGVFKDVADIMEGATVPGSRSKKRKGMAKAAEESARYENELRSPSEINKRIRQLEEKMYQLARDLEFEAAAQMRDEIGKLRERLLAV	The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.	Q884C9
C3PFR8	NUCS_CORA7	Endonuclease NucS	Corynebacterium	MRVVIAQCSVDYVGRLDAHLPMADRLILIKADGSVSIHADDRAYKPLNWMTPPCTFEESAIEDIDGEDTGEKLWLVENPKGEQLRITIAQIHQEIDMDLGEDPGLVKDGVEAHLQELLAEHIETLGEKYSLVRREYPTAIGPVDIMAKNSKNEFVAVEVKRRGGIDGVEQLTRYLELLNRDDLLAPVHGVFAAQEIKPQARTLAEDRGIRCVVLDYQELRGIESNELRLF	Cleaves both 3' and 5' ssDNA extremities of branched DNA structures.	C3PFR8
Q1AVW2	RECO_RUBXD	Recombination protein O	Rubrobacter	MALYRSRGIVLRSIRYGEADRILDIYTRDAGLVSCIAKGIRRTRSRFGARLEPFSCVDFMAYRGRTLDTITQAESLRSFRGVRERLDRLQAAAGMAGVLHALSGGTPDRRTFNLLYRALDALEKGEEGFGMIEASFGLKLAVLSGYAPRLDGCAECGGDVPGEGARFAPAAGGFLCRDCRSDAPPDSFPVPPGTLGRLRELAALPLAEAASGRGLEEALRRVVRAHVLAHAPGAASLATPAGTAGGRP	Involved in DNA repair and RecF pathway recombination.	Q1AVW2
Q9HJ56	RL7A_THEAC	Ribosomal protein L8e	Thermoplasma	MEKSYVKFETPEDVSQKALDLVESSYRTGKVKKGTNEVIKSIERGESKLVVIAEDVNPPEVVYYLPSLCEDKKVPYVYVKKKADLGSKVGIASAASVSIVDYGKNEELYKSIVSALEQIKK	Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, the RNA component of RNase P, box H/ACA, box C/D and box C'/D' sRNAs.	Q9HJ56
A4ST47	ENGB_AERS4	Probable GTP-binding protein EngB	Aeromonas	MDTQTLNFNKVHFVTSAPDIRHLPNDGGVEIAFAGRSNAGKSSALNTLTKHKNLARTSKTPGRTQLINLFELEPGKRLVDLPGYGYAQVPLEMKLKWQKSLAEYLQRRESLKGLVILMDIRHPLKDTDMNMLEWSSHRELPVMLLLTKADKLSPGPRNNQVIKVRQAIADLGPQIQVEAFSSLNNIGVEKLAQTLSGWYLAGADEIADNDEQEQVEE	Necessary for normal cell division and for the maintenance of normal septation.	A4ST47
Q6JE37	CITX2_NICBE	Cf-9-interacting thioredoxin 2	Nicotiana	MQAATLSFQPSAPPLQTSAFHFSSKQPNQLKYSLFSYTCPILKRSLLSTQTLSRKSICKPPDVATGKYVREDYLVKKVSAKDIQELIKGERNVPLIIDFYATWCGPCILMAQELEMLAVEYESNALIVKVDTDDEYEFARDMQVRGLPTLYFISPDPNKDAIRTEGLIPIQMMRDIINNDL	Probable thiol-disulfide oxidoreductase that may play a role in proper chloroplast development.	Q6JE37
Q824N2	RS11_CHLCV	30S ribosomal protein S11	Chlamydia	MVKHQTQKKGVKRKQLKNIPSGVVHVKATFNNTIVSITDPAGNTISWASAGKVGYSGSRKSSAFAATMAAQDAAKNAMNSGLKEVEVCLKGTGAGRESAVRALIASGLVVSVIRDETPVPHNGCRPRKRRRV	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.	Q824N2
C5PEI9	PEPA_COCP7	Aspartic protease PEP3	Coccidioides	MQNRPRVFDSAMNLSPNMHFLSLMPGLLLLSLQVHTSPTPLKKTIRSVRIERIRQPNYVPDGPGALKKAYAKFGIIPSGISFDSFEDFTPFSSDNVRNTVSKAMQANETGIVTNTPTNNDVEYLSPVTIGGQKFVMNLDTGSSDTWVFNTQLSEDAKRGHSIFDPAKSKAFSDLEDATFNITYGDASFAFGRVGIDTVDIGGATVQKQAVGLPTDVSGSFILDQASDGLIGLGFDELNTVEPQQQKSFFTNLAANLDEPVLAAQLKKGAPGSYEFGSIDETKFKGDLVTIPVNNSRGFWEVKSTMFKVGKDEQLHRITKGVGSAIADTGTTLMLVNEEIVNSYYDQVDNARSVYAAGGFIFPCNATLPDLYVSLGDTHLARIPGDLMNFSKVGLSTETGEELCFGGVQSNSGSGLQVFGDVLFKAIFVVFDLRGPSLHVAGHA	Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions.	C5PEI9
Q8TX94	LEUD1_METKA	null	Methanopyrus	MRDVIRGRAWVFGDDIDTDQIIPGRYLTTQDPEELAKHVMEGADPEFPEKVREGDVIVAGKNFGCGSSREHAPIALKAAGIACVVTRSFARIFYRNAINLGLPLVVCPGVDDAFEDGQGIEVNLREGYVRNLDTGEELEAKPLPDFMMRILEAGGLVELIKREGPRAFEG	Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.	Q8TX94
B0BUW3	CLPX_RICRO	ATP-dependent Clp protease ATP-binding subunit ClpX	spotted fever group	MVVEADKKALICSFCSKKQHEVKKLIAGPAVFICDECIDLCTDIMKEENKVALKQITSSIPTPQKICGILNDYVVGQDQAKKILAVAVYNHYKRLEYIQSGNNDVELNKSNILLIGPTGSGKTVLAQTLAKILDVPFTMADATSLTEAGYVGEDVENILLRLLIASEFNIAKAQKGIIYIDEVDKIARKSENPSITRDVSGEGVQQALLKIMEGTVASVPPQGGRKHPQQDFVQLDTSNILFICGGAFMGIDSIITSRTNHSSIGFAANVNIDKEKNNSEILKSLEIEDLTKFGLIPEFIGRLPIVTTLDELDKEALITILTKPKNAIVKQYQKQFELDDAELVIDDSALETIAEKALAKKTGARGLRSILEHLLLDSMYKVAELKKQRVTITKEVVNGLVEPIMTSLISTKSNKKQPIIADIPA	ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.	B0BUW3
A0KGL5	RAPA_AERHH	ATP-dependent helicase HepA	Aeromonas	MPFALGQRWISDTETDLGLGTVVAVEGRMVTLLFPATGENRMYAKEEAPVTRVSFNVGDQIASHEDWTMTVEEVQEKDGLLIYVGVRTDNDEPVALKEVFLNNFIKFNKPQDRLFAGQIDRMSRFTLRYEALINQHQRRRNPTRGLAGGRVSLIPHQLYIAHEVGHRYAPRVLLADEVGLGKTIEAGMIIHQQLLSGRAHRVLILLPETLQHQWLVEMLRRFNLHFSLFDEERCIEAFADAENPFETEQLVICSLDFLRKKRRRFEQVLEAEWDLLVVDEAHHLEWSEEAPSRAYEMVEALAEQVPGVLLLTATPDQLGHQSHFARLRLLDPERFYDYDAFLAEEQAYGQVASAAQELLDGETLSDEAKRILASQLEGLDLSDAAARQQAVAKLLDQHGTGRVLFRNSRANIQGFPERHLNVYPMPLPEQYKTAIKVMGMMGGNGGDLQTRALRYLYPEKIFQQFEGDNATWTQFDPRVEWLLELLLSARQQKVLVICSEAATAIALEEALRTREGIRGAVFHEGMSILERDKASAYFAQQEGGAQVLLCSEIGSEGRNFQFASHLVLFDLPLNPDLLEQRIGRLDRIGQQNTVEIHVPYLEGTSQRALQLWYHDGLDAFEQTCPTARPVFEAVRDELFELLAANTGDQAPLDALLVKTRELHEPLKARLEQGRDRLLEIHSSGGAAAQQLVDKLAAEDDDTGMISFALKMFDEIGVNQDDRGENALVLTPGDHMLVSSFPGLPQDGMTITFDRNTALSRDDMALLSWDHPMMRGGIDLILGSEIGATSVALLKNKALPIGSILLELIFVAESAAHPQLYRFMPPTPIRLLMDKNGQNLGEKVAFDAFNRQLTPVNRHLGSKLVTASQPVIHGLIGKGQAIAEELKGGIVDKARAQMAQTLQQDLDRLEALKAVNPNVRDSELDYLRNLQAELHHLIDQTQLKLDAIRFIVVTHN	Transcription regulator that activates transcription by stimulating RNA polymerase (RNAP) recycling in case of stress conditions such as supercoiled DNA or high salt concentrations. Probably acts by releasing the RNAP, when it is trapped or immobilized on tightly supercoiled DNA. Does not activate transcription on linear DNA. Probably not involved in DNA repair.	A0KGL5
B1YHU0	LIPL_EXIS2	Octanoyl-[GcvH]:E2 amidotransferase	Exiguobacterium	MGIELLKQEHYRIFDQTSLGNTFHATQSFAMDDTLCASVATEGAAIRSWVHHETVVLGIQDARLPHLDDGIDVLHAHGFQPVIRNSGGLAVVLDAGVLNISLVLPERGGIDIDSGYEAMLALVRRMFAEETDAINAGEVVGSYCPGSYDLSIAGKKFAGISQRRVRGGVAVQIYLCVNGSGSARAQLVRDFYAAALQGETTKFVYPTVVPETMASLEELLQRPLTVEDCLVRVYRSLMELGATLTPSVLSEVENERFGVNLGRMLDRNEKVLG	Catalyzes the amidotransfer (transamidation) of the octanoyl moiety from octanoyl-GcvH to the lipoyl domain of the E2 subunit of lipoate-dependent enzymes.	B1YHU0
A5UAV8	AROC_HAEIE	5-enolpyruvylshikimate-3-phosphate phospholyase	Haemophilus	MAGNTIGQLFRVTTFGESHGIALGCIVDGVPPNLELSEKDIQPDLDRRKPGTSRYTTPRREDDEVQILSGVFEGKTTGTSIGMIIKNGDQRSQDYGDIKDRFRPGHADFTYQQKYGIRDYRGGGRSSARETAMRVAAGAIAKKYLREHFGIEVRGFLSQIGNIKIAPQKVGQIDWEKVNSNPFFCPDESAVEKFDELIRELKKEGDSIGAKLTVIAENVPVGLGEPVFDRLDADLAHALMGINAVKGVEIGDGFAVVKQRGSEHRDEMTPNGFESNHAGGILGGISSGQPIIATIALKPTSSITIPGRSINLNGKPVEVVTKGRHDPCVGIRAVPIAEAMVAIVLLDHLLRFKAQCK	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.	A5UAV8
P70232	NCHL1_MOUSE	Processed neural cell adhesion molecule L1-like protein	Mus	MMELPLCGRGLILSLIFLLLKLSAAEIPLSVQQVPTIVKQSYVQVAFPFDEYFQIECEAKGNPEPIFSWTKDDKPFDLSDPRIIAANNSGTFKIPNEGHISHFQGKYRCFASNRLGTAVSEEIEFIVPGVPKFPKEKIEPIDVEEGDSIVLPCNPPKGLPPLHIYWMNIELEHIEQDERVYMSQRGDLYFANVEENDSRNDYCCFAAFPKLRTIVQKMPMKLTVNSSNSIKQRKPKLLLPPAQMGSLSAKTVLKGDTLLLECFAEGLPTPHIQWSKPGSELPEGRATIEVHEKTLKIENISYQDRGNYRCTANNLLGKASHDFHVTVEEPPRWKKKPQSAVYSTGSSGILLCEAEGEPQPTIKWRLNGLPIEKHPFPGDFMFPREISFTNLLPNHTGVYQCEASNIHGTILANANIDVIDVIPLIKTKNEENYATVVGYSAFLHCEYFASPKATVVWEVADETHPLEGDRYHTHENGTLEIYRTTEEDAGSYSCWVDNAMGKAVITANLDIRNATKLRVSPKNPRIPKSHVLELYCESQCDSHLKHSLKLSWSKDGEAFEMNGTEDGRIVIDGAYLTISNITAEDQGVYSCSAQTSLDSTSEKTQVTVLGVPDPPGNLHLSERQNRSVRLSWEAGDDHNSKISEYIVEFEGNREEPGKWEELTRVQGEETDVVLSLAPYVRYQFRVTAVNEVGRSHASLPSDHHETPPAAPDKNPQNIRVQASQPKEMIIKWEPLKSMEQNGPGLEYKVSWKPQGAPEEWEEEIVTNHTLRVMTPTVYAPYDVKVQAINQLGSSPDPQPVTLYSGEDYPSTAPVIQRVDVMNSTLVKVTWSSIPKETVHGLLRGYQINWWKTKSLLDGRTHPKEVNILRFSGQRNSGMVPSLDPFSEFHLTVLAYNSKGAGPESEPYIFQTPEGVPEQPSFLKVIKVDKDTATLSWGLPKKLNGNLTGYLLQYQIINDTYELGELNEINVTTPSKSSWHLSNLNSTTKYKFYLRACTSRGCGKPISEEGATLGEGSKGIRKITEGVNVTQKIHPVEVLVPGAEHIVHLMTKNWGDNDSIFQDVIETRGREYAGLYDDISTQGWFIGLMCAIALLTLILLTICFVKRNRGGKYSVKEKEDLHPDPEVQSAKDETFGEYSDSDEKPLKGSLRSLNRNMQPTESADSLVEYGEGDQSIFNEDGSFIGAYTGAKEKGSVESNGSSTATFPLRA	Extracellular matrix and cell adhesion protein that plays a role in nervous system development and in synaptic plasticity. Both soluble and membranous forms promote neurite outgrowth of cerebellar and hippocampal neurons and suppress neuronal cell death. Plays a role in neuronal positioning of pyramidal neurons as well as in regulation of both the number of interneurons and the efficacy of GABAergic synapses. May play a role in regulating cell migration in nerve regeneration and cortical development. Potentiates integrin-dependent cell migration towards extracellular matrix proteins. Recruits ANK3 to the plasma membrane.	P70232
Q0I4M4	LPXA_HAES1	Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase	Histophilus	MIHSTAKIHPSSIIEEGAKIGENVVIGPFCIVGSDVQIGKGTTLHSHVVVKGVTTIGEDNQIFQFASIGEVNQDLKYQGEPTKTIIGHRNRIRESVTIHRGTVQGGGVTRIGDDNLLMINAHIAHDCQIGNRCILANNATLAGHVELGDFVIVGGMSAIHQFVIVGAHVMLGGGSMVSQDVPPYVMAQGNHARPFGVNIEGLKRRGFDKPTLHAIRNVYKLIYRSGKTLEEVIPEIENYAQTESAVSFFLDFFNRSTRGIIR	Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.	Q0I4M4
P32518	DUT_SOLLC	dUTP pyrophosphatase	Solanum subgen. Lycopersicon	MAENQINSPEITEPSPKVQKLDHPENGNVPFFRVKKLSENAVLPSRASSLAAGYDLSSAAETKVPARGKALVPTDLSIAVPQGTYARIAPRSGLAWKYSIDVGAGVIDADYRGPVGVVLFNHSEVDFEVKVGDRIAQLIVQKIVTPEVEQVDDLDSTVRGSGGFGSTGV	This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. It may have as well a metabolic role in merismatic cells.	P32518
B5XY03	G6PI_KLEP3	Phosphohexose isomerase	Klebsiella	MKNINPTQTSAWQALQKHFDEMKDVTISELFAKDSDRFSKFSATFDDLMLVDFSKNRITEETLAKLQDLAKETDLAGAIKSMFSGEKINRTEDRAVLHVALRNRSNTPIVVDGKDVMPEVNAVLEKMKTFSEAIISGSWKGYTGKPITDVVNIGIGGSDLGPFMVTEALRPYKNHLNMHFVSNVDGTHIAEVLKNVNPETTLFLVASKTFTTQETMTNAHSARDWFLATAGDDKHVAKHFAALSTNAKAVGEFGIDTANMFEFWDWVGGRYSLWSAIGLSIILSVGFDNFVELLSGAHAMDKHFSTTPAEKNLPVLLALIGIWYNNFFGAETEAILPYDQYMHRFAAYFQQGNMESNGKYVDRNGHAVDYQTGPIIWGEPGTNGQHAFYQLIHQGTKMVPCDFIAPAITHNPLSDHHPKLLSNFFAQTEALAFGKSREVVEQEYRDQGKDPATLEHVVPFKVFEGNRPTNSILLREITPFSLGALIALYEHKIFTQGAILNIFTFDQWGVELGKQLANRILPELKDGSEVSSHDSSTNGLINRYKAWRA	Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.	B5XY03
A1TAQ3	ARC_MYCVP	Mycobacterial proteasome ATPase	Mycolicibacterium	MSESERSEASEVFGTSPDSRLSSEDAAELEQLRREAAILREQLEDAGGLATSARAARDVHQLEARIDSLAARNAKLMDTLKEARQQLLALREEVDRLGQPPSGYGVLLSVQDDETVDVFTSGRKMRLTCSPNIETKELKKGQTVRLNEALTVVEAGHFESVGEISTLREILSDGHRALVVGHADEERIVWLAEPLVAAEHLPEGSYADEDDLTDDRPRKLRPGDSLLVDTKAGYAFERIPKAEVEDLVLEEVPDVSYNDIGGLGRQIEQIRDAVELPFLHKELYREYSLRPPKGVLLYGPPGCGKTLIAKAVANSLAKKMAEVRGDDAREAKSYFLNIKGPELLNKFVGETERHIRLIFQRAREKASEGTPVIVFFDEMDSIFRTRGTGVSSDVETTVVPQLLSEIDGVEGLENVIVIGASNREDMIDPAILRPGRLDVKIKIERPDAESAQDIFSKYLTEELPIHDDDLAEFSGDRSLTIKAMIEKVVDRMYAEIDDNRFLEVTYANGDKEVMYFKDFNSGAMIQNVVDRAKKNAIKAVLETGQRGLRIQHLLDSIIDEFAENEDLPNTTNPDDWARISGKKGERIVYIRTLVTGKSSSASRAIDTESNLGQYL	ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis.	A1TAQ3
Q12ZV0	RL4_METBU	50S ribosomal protein L4	Methanococcoides	MTTANIIDLSGNSKGEIALPEVFSEIFRPDLIKKAVLSAQANRLQPYGTKLYAGMQTSAHSWGSGRGVAQVPRISNGSRVARIPQAVGGRRAHPPKTETDRTEKINKKEKRLAVRSAIAATIDADLVKARGHKFTAEVPFVADDAIEGLVKIKEVISFLQAAGLYDDIIRAKEGKHIRAGKGKRRGRKYKNRKSVLIVTGEESLLSKAANNLPGVDVATVTALNAELLAPGTHAGRLTVWTQSAITNMEGMFL	Forms part of the polypeptide exit tunnel.	Q12ZV0
Q80VM4	ZN579_MOUSE	Zinc finger protein 579	Mus	MDPQPPPPAQGSPPHRDRGRGRGRGRGRGRGRGRGRGGAGAPRAPLPCPTCGRLFRFPYYLSRHRLSHSGLRPHACPLCPKAFRRPAHLSRHLRGHGPQPPLRCAACPRTFPEPAQLRRHLAQEHAGSEVDLSTQRAVKEEPEASWGPQDEGVEQPATVVVAGAEEEATTQWPAGDSAPAAVPTSTDPRESEAKEAEAGAAELRAELALAAGRQEEKQVLLQADWTLLCLRCREAFATKGELKAHPCLRPEGEQEGEGGPPPRPKRHQCSICLKAFARPWSLSRHRLVHSTDRPFVCPDCGLAFRLASYLRQHRRVHGPLSLLAPLPGAGKKDDKASGGRNSGKGPEGGEGAECGGASEGGEGGHNGGDATPARPPAGEPRFWCPECGKGFRRRAHLRQHGVTHSGARPFQCVRCQREFKRLADLARHAQVHAGGPAPHPCPRCPRRFSRAYSLLRHQRCHRAELERAELERAAALQELQTQASQSPQPPQPLKQEAEGLPLPIAHIKEEPPSPGTPPQSPPAPPVFLSASCFDSQDHSAFEMEDEEMDSKAHLCGLGGLAS	May be involved in transcriptional regulation.	Q80VM4
B2VF78	SLMA_ERWT9	Nucleoid occlusion factor SlmA	Erwinia	MVEKKSAKRNRREEILQALAQMLESSDGSQRITTAKLAANVGVSEAALYRHFPSKTKMFDSLIEFIEDSLITRINLILKDEKETMPRLRLITQLILGFGELNPGLTRILTGHALMFEQDRLQGRINQLFERIELQIRQVMRERKMREGEGFATDEALLATQLLAFCEGLLSRFVRSEFRYRPTVDFDARWPLMAAQLI	Required for nucleoid occlusion (NO) phenomenon, which prevents Z-ring formation and cell division over the nucleoid. Acts as a DNA-associated cell division inhibitor that binds simultaneously chromosomal DNA and FtsZ, and disrupts the assembly of FtsZ polymers. SlmA-DNA-binding sequences (SBS) are dispersed on non-Ter regions of the chromosome, preventing FtsZ polymerization at these regions.	B2VF78
Q0SPQ5	RSMG_CLOPS	16S rRNA 7-methylguanosine methyltransferase	Clostridium	MQYFDLMKKACDSVGMEFNEDKYQKFMLYKDLLKEWNEKINLTAITEDEEIVKKHFIDCIKAFKADEFKKAKTVIDVGTGAGFPGLPIAIMREDVEVTLLDSLNKRINFLNEVVNKLALKNVETIHSRAEDGARKKELRENFDIATSRAVANMCVLSEFCIPYVKVNGNFIALKGPNITEELNDSKNAIGTLGGKLKGITEVEIEGTDLNHNLVIVDKIKSTPKTFPRKAGNVTKKPLK	Specifically methylates the N7 position of a guanine in 16S rRNA.	Q0SPQ5
B2KA77	KDPA_YERPB	Potassium-translocating ATPase A chain	Yersinia	MVASGFLLIASFMVVLFVLSRPLGGFLARLIEGEPFSALQKVEAGLWRCSGVKNAEMNGWQYALAILCFNLLGIVLLFVLLMTQGSLPLNPEHLPGMSWHLALNTAVSFVTNTNWQAYSGENTLSYLSQMAGLTVQNFLSAATGIAVAFALIRAFARHSATTLGNAWVDLVRITLYVLLPIALIIALIFVSQGVLQNLDGYLHITTLEGVQQTLPMGPVASQEAIKVLGTNGGGFFGANSAHPFENPTAFSNFVQMLAIFLIPCALCFAFGQVVGDNRQGHALIWAMSLIFIVAVVVVMYAELAGNPHLSPLGADSNSNMEGKESRFGILATSLYAVVTTAASCGAVNAMHDSFTALGGMIPLWLMQIGEVVFGGVGSGLYGMLLFVLLTVFIAGLMIGRTPEYLGKKIDVFDMKMTALAILVTPTIVLLGTALALCTEAGRAGILNPGAHGFSEVLYAFSSAANNNGSAFAGLSVNTPFYNLLLAAAMFIGRFGVILPVLAIASSLVAKKRQPAGNGTLPTGGPLFIGLLIGTVLLVGALTFIPALALGPVAEHLQVWLAH	Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the periplasmic potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel.	B2KA77
Q5ZTZ8	KGUA_LEGPH	GMP kinase	Legionella	MVSDNSGNLYIVAAPSGGGKTSLVKKLIEMVGEIEVSVSHTTRPMRPGEKEGVDYFFIDEKQFISMVNEGAFIEHAKVFNHWYGTSVAQINKRLQFGIDVVLDIDWQGAEQIRHAYPDAVSVFIIPPSLDALKERLMNRRQDKDHVISERMTKAQDELGHYPEFDYLIVNDDFEKAAMELQSIVIANRLRIEKQVNKQAKLLSFLLSSQ	Essential for recycling GMP and indirectly, cGMP.	Q5ZTZ8
B5Y273	LPLA_KLEP3	Lipoate--protein ligase	Klebsiella	MSTLRLLLSDSYDPWFNLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDHVRLARRSSGGGAVFHDLGNTCFTFMAGKPEYDKTVSTAIVLAALNSLGVTAEASGRNDLVVKTDSGDRKVSGSAYRETIDRGFHHGTLLLNADLSRLANYLNPDQKKLQAKGITSVRGRVANLVELLPGITHQHICEAIQEAFFSHYGERVDAEVISPDNTPDLPNFAETFARQSSWEWNFGQAPAFSHLLDERFRWGGVELHFDVEKGHITRTQAFTDSLNPAPLEALAARLVGCQYRAEVLLQQCEALVGDFPEQEAELKELSAWMAGAVR	Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes.	B5Y273
A1SSY6	NQRD_PSYIN	NQR-1 subunit D	Psychromonas	MAKSNEIKAVLTSPIISNNPITLQILGICSALAVTSKLENAVVMTVAVLFVTAFSNFFISTIRNYIPNSVRIIVQMAIIASLVIVVDQFLRAYAFSISKQLSVYVGLIITNCIVMGRAEAFAMKNKPIASFMDGVGNGLGYGVILILVGAFRELFGSGSLYGFVILPLTSNGGWYQSNGLLLLAPSAFFIVGGIIWAVRTMRPDQVEPKE	NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.	A1SSY6
P04113	MLRA_MIZYE	Myosin regulatory light chain A, smooth adductor muscle	Mizuhopecten	ADKERAQRATSNVFARLPQKLMQEMKEAFTMIDQNRDGFIDINDLKEMFSSLGRTPDDKELTAMLKEAPGPLNFTMFLSIFSDKLSGTDTEETLRNAFAMFDELDTKKLNIEYIKDLLENMGDNFTKDEMRMTFKEAPVTGGKFDYVKFTAMIKGSGEEEA	In molluscan muscle, calcium regulation is associated with myosin rather than with actin. Muscle myosin contains two types of light chains: the catalytic light chain, essential for ATPase activity, and the regulatory light chain, a calcium-binding protein responsible for Ca(2+) dependent binding and Ca(2+) dependent Mg-ATPase activity.	P04113
Q988C8	FHMCD_RHILO	5-formyl-3-hydroxy-2-methylpyridine 4-carboxylate 5-dehydrogenase	Mesorhizobium	MIRNIAIIGLGTMGPGMAARLARGGLQVVAYDVAPAAIERARSMLSVAETVLDALGIALPSAGVGTVRFTDDIGDAVSGADLVIENVPENISIKADVYRTIDGLIGQDTIVASDTSGIPITKLQAHISYPERMVGMHWSNPPHIIPMIEVIAGEKTAPQTVATIRDLIRSIGLLPVVVKKDVPGFVENRVLYALLREAVDLVERGVIDPEDLDTCVSWGIGYKIAVIGPMALLDMAGLDIYKSVSSFLNADLSNRDDVAPMVLEKTSASKFGIKSGEGMFCYTPEQTKALQAERARKLVAVRRILEGRE	Involved in the degradation of pyridoxine (vitamin B(6)). Catalyzes the oxidation of 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate (FHMPC) by NAD(+) to 5-hydroxy-6-methylpyridine-3,4-dicarboxylate (HMPDC) . Can also catalyze the reduction of FHMPC by NADH to 4-pyridoxic acid .	Q988C8
Q46I27	CBID_PROMT	Cobalt-precorrin-6A synthase	Prochlorococcus	MNQFTLPVWVVAAAKSATNILIGNKFRDKERIDLPNNEKSISVPISSSALLDNGKRSLAVSHCQSGLPLDITRGVEIWAYIQLSKGGFQSKGKVRNGFPDWLDFHAGYGVGKFQSSGQPCISQFARDLLCINLYPLLPKGSSIKVEIILPEGKDRASKTSNEAFGVVDGLSLIGTQAEVQISASPDQLKNTKELLHHKCSEAKFDGCLTFVIGENGMDLAMKYGLPANQIIKTGNWLGPLLVAAAENGVKKLLLFGYHGKLIKLSGGVFHTHHHLADGRIEILTSIAFREGISFDLIELISKSTSVENALLTLEVSNPEAVSLIWSRMAKEIEIKSRSYVNRYLSSSMEIGSVLFDRKRQMRWAGLEGLKQINSLGLILKR	Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.	Q46I27
Q9NQG5	RPR1B_HUMAN	Cell cycle-related and expression-elevated protein in tumor	Homo	MSSFSESALEKKLSELSNSQQSVQTLSLWLIHHRKHAGPIVSVWHRELRKAKSNRKLTFLYLANDVIQNSKRKGPEFTREFESVLVDAFSHVAREADEGCKKPLERLLNIWQERSVYGGEFIQQLKLSMEDSKSPPPKATEEKKSLKRTFQQIQEEEDDDYPGSYSPQDPSAGPLLTEELIKALQDLENAASGDATVRQKIASLPQEVQDVSLLEKITDKEAAERLSKTVDEACLLLAEYNGRLAAELEDRRQLARMLVEYTQNQKDVLSEKEKKLEEYKQKLARVTQVRKELKSHIQSLPDLSLLPNVTGGLAPLPSAGDLFSTD	Interacts with phosphorylated C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and participates in dephosphorylation of the CTD by RPAP2. Transcriptional regulator which enhances expression of CCND1. Promotes binding of RNA polymerase II to the CCDN1 promoter and to the termination region before the poly-A site but decreases its binding after the poly-A site. Prevents RNA polymerase II from reading through the 3' end termination site and may allow it to be recruited back to the promoter through promotion of the formation of a chromatin loop. Also enhances the transcription of a number of other cell cycle-related genes including CDK2, CDK4, CDK6 and cyclin-E but not CDKN1A, CDKN1B or cyclin-A. Promotes cell proliferation.	Q9NQG5
Q117R7	METE_TRIEI	Methionine synthase, vitamin-B12 independent isozyme	Trichodesmium	MSISTSTLGYPRIGKNREVKKALESFWQQKISADELLKIVREIEEASWQTQTKAGIERIGIGDATLYDQILDWSFRFGIIPKRFQQFQNLECYFAMARGKDGILALEMTKWFDTNYHYLVPEITPDITPKADFSDFLETVKRAKKIIGKSAVPIIISPITFIRLSRLESVEFDNILAQLLPLYSDLLTKLKKLGISEIQLHEPALVFGDSSNLKKQFEMAYAELAKVGLNIHLVTYFDDLGETYPWVMKLPVTSISLDLTRGQNLELIKSYGFPADKTLGAGVVDARNIWRIRTQEVTSLLEELKGIIPNISVQPSASLQFVPYDVRREVKLPEALRNVLSFAEQKLEETVLLSKALTGKSNKSEIENIEIYWQEFYKFSPANEKVKSQIKALKETDFRRSMSYLERLDNQIKLPAFPTTTIGSFPQTKQVRKLRARYKKGELTQAEYLAQIDANIAYCIGLQEGMGMDVLVHGEFERSDMVEYFGEQLDGYTFTTHGWVQSYGSRYVRPPIIFGDIYRPHAMTIREFEVAQSLTEKPVKGMLTGPVTMLNWSYPRTDISRQEQAFQLALAIREELKDLEKAGAAFIQVDEPAMREGLPLKQQRWHEYLNWAVDAFRLSTAIARPETQVHTHMCYSEFGDIMESIKQLDADVISIEDSRSNNETLMQLTDADYPAQVGPGVYDVHSPSIPTTEYLRESLYKCIQYLPVTQIWVNPDCGLKTRRWEEAIPATRNMVQAAISLRQE	Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.	Q117R7
C5D9H6	MUTL_GEOSW	DNA mismatch repair protein MutL	unclassified Geobacillus	MGKIRKLDDQLSNKIAAGEVVERPASVVKELVENAVDANSTIIEIELEEAGLTKIRVIDNGDGMEEDDCLVAFERHATSKIKDEHDLFRIRTLGFRGEALPSIASVSEVEMKTSTGDGPGTKVVLKGGKLVVHERTTSRKGTDITVSNLFFNTPARLKYMKTIHTELGHVTDVVNRLAMAHPDISFRLRHHGKQLLYTSGNGDVRHVLAAIYGMDVAKKMIPIQAESLDFTVQGYISLPEVTRASRNYISTIVNGRYVRNIPLAKAIEAGYHTLLPIGRYPIVFLSIAMDPILVDVNVHPAKLEVRFSKEAELNELVTQAIRQALQARTLIPEMMIKQKETPKPKAEQTAWTFEHVVKEPFVSPLVHVDEPKQVDEPKQSSPVQEPKEEIPSFLPTVESKQNDVDDELVEMDEQTESSDEQEHVNDRLPPLYPIGQMHGTYILAQNERGLYIIDQHAAQERIKYEYFREKVGEVINEVQELLVPLTFHYPTDEYVLIDAHREELAKCGVFLEPFGHNTFIVRSHPSWFPKGEEAEIIEEMIQQVIDMKKVDMKQLREKAAILMSCKRSIKANEYLRDDEIFALLESLRKTTDPFTCPHGRPIIIHFSTYELEKMFKRVM	This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex.	C5D9H6
Q96GX2	A7L3B_HUMAN	Ataxin-7-like protein 3B	Homo	MEEISLANLDTNKLEAIAQEIYVDLIEDSCLGFCFEVHRAVKCGYFYLEFAETGSVKDFGIQPVEDKGACRLPLCSLPGEPGNGPDQQLQRSPPEFQ	By binding to ENY2, interferes with the nuclear functions of the deubiquitinase (DUB) module of the SAGA complex which consists of ENY2, ATXN7, ATXN7L3 and the histone deubiquitinating component USP22. Affects USP22 DUB activity toward histones indirectly by changing the subcellular distribution of ENY2 and altering ENY2 availability for ATXN7L3 interaction. Regulates H2B monoubiquitination (H2Bub1) levels through cytoplasmic sequestration of ENY2 resulting in loss of nuclear ENY2-ATXN7L3 association which destabilizes ATXN7L3. Affects protein expression levels of ENY2 and ATXN7L3.	Q96GX2
O74870	MUG73_SCHPO	Meiotically up-regulated gene 73 protein	Schizosaccharomyces	MNAKLSSSGMVLKELPEVALQKISSNYYWAVFAVFLLCAIVFPLVSIFSLPQKQTYHRFFSILSLVSCLAYFTMACNYGLKNVFSSASFFREVSVRMVYYVRYIQWLINFPLIIVMLHWTVGVSILEIAYVVCYVLFAIVCLLAAALTSSPYKWAYYGFSFVGYFIALAHSVVLHKKYASRLETSARLGFLWSIVYLHVIWFLYYACWILSEGLNVISPIGEAIFYSILDLFEFGFFGAAFSWMLDLVGIENFKSPQSIPLGACSPADDKFSMCPDMEAQNQADDLAVETRIQISNLPSSPTKNNC	Has a role in meiosis.	O74870
Q2SXD1	LOLD_BURTA	Lipoprotein-releasing system ATP-binding protein LolD	pseudomallei group	MNDRVFEQTMNQNHQGGAARECVLEAHGITKTFMQGGFNVQVLDNAQVSVRRGEKLAIVGASGSGKSTLLHVLGGLDEPSAGQVSLLGKPFTQLAERERNDLRNRALGFVYQFHHLLPEFTALDNVAMPLRIRRMSAEEARHHAREMLEQVGLGARAKHRPGELSGGERQRVAIARALVTKPACVLADEPTGNLDGSTADHVFHLMLELSRTLDTSFVIVTHDPDLAARCDRILRLRDGVLHEEPAVPV	Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner.	Q2SXD1
Q3B5P7	PDXJ_CHLL3	Pyridoxine 5'-phosphate synthase	Pelodictyon	MRLAVNIDHIATLRNARNEGEPDPVAAALLAEESGAAGIVCHLREDRRHIRDNDLKGLRRSVKTKLDLEMAMTEEMQRIAIETVPELITLVPEKREELTTEGGFDIERHFKRLALFIEPIRAAGIEVSLFIEPDSRSIDLAAEAGSDLVELHTGSYALKSGEEQTAEFERIRHAAKYAVDRGLKVVAGHGLNYRNIQPFRQIPEIEEVSIGHALIARAAFVGIPEAVREMLDLIG	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.	Q3B5P7
Q9F1Y5	GPPMT_STRCO	Geranyl diphosphate 2-C-methyltransferase	Streptomyces albidoflavus group	MTTETTTATATAKIPAPATPYQEDIARYWNNEARPVNLRLGDVDGLYHHHYGIGPVDRAALGDPEHSEYEKKVIAELHRLESAQAEFLMDHLGQAGPDDTLVDAGCGRGGSMVMAHRRFGSRVEGVTLSAAQADFGNRRARELRIDDHVRSRVCNMLDTPFDKGAVTASWNNESTMYVDLHDLFSEHSRFLKVGGRYVTITGCWNPRYGQPSKWVSQINAHFECNIHSRREYLRAMADNRLVPHTIVDLTPDTLPYWELRATSSLVTGIEKAFIESYRDGSFQYVLIAADRV	Catalyzes the SAM-dependent methylation of geranyl diphosphate (GPP) to yield (E)-2-methylgeranyl diphosphate (2-MeGPP).	Q9F1Y5
Q7VP34	SYI_HAEDU	Isoleucyl-tRNA synthetase	Haemophilus	MTDYKDTLNLPETGFPMRGDLAKREPAMLKNWYDKNLYQQIRQTSKGKKTFILHDGPPYANGNLHLGHAVNKILKDIIMKSKTASGFDTPYVPGWDCHGLPIELKVESIVGKPNEKISAAEFRQACREYANEQVDRQKADFIRMGVLGDWDNPYLTMNFNTEASIIRTLAKVIANGHLYKGSKPVHWCLDCGSSLAEAEVEYEDKVSPSIYVRFKACDETAIETLFNAKGNGPISAIIWTTTPWTMPSNRAIAIHPELEYALVQLADERVILATELVESVAKAIEAESFDILATVKGETLQLLRFHHPFYAFDVPFIFGDHVTTEGGTGLVHTAPDHGTDDFIIARKNNIEMAGLIGNDGKFKSDVEFFAGLAVFESNEKVIEKLKETGALLKLARIKHSYPHCWRHKTPIIFRATPQWFIGMEKQGLRAQALAEIKTVRWIPNWGEARIDTMVANRPDWCISRQRTWGVPMAMFVHNETEELHPRTLDILELVAQRVEQQGIQAWWDLDPTEVLGEDAQHYHKVPDTLDVWFDSGSTYASVVEQRPEFNGQTADMYLEGSDQHRGWFMSSLMLASATNGKAPYQQVLTHGFVVDEKGRKMSKSIGNVIVPSEVWNKNGADILRLWVASTDYTAEMKVSHGILNSAGDAYRRIRNTARFLLSNLNGFIPARDEVKPNEMIALDRWAVSCALEAQNDIIEAYEHYQFHTVVQRLMRFCSIEMGSFYLDIIKDRQYTTKADSLARRSCQTALWHIAEALVRWIAPILSFTADEIWSHLPTVEGRSEFVFTEQFYSQLFTLNCHDKLDDNYWQQLINIRAEVNRVLEQARNEKTIGAGLEAKVTVYANDEMLPLLHQLGNELRFVLITSQAIVKPLSEADVAEGELAGLAVKVERAEGEKCPRCWHFATDIGTHAEHNAICGRCVENVAGKGEVRRFA	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).	Q7VP34
A4SFY3	GLYA_CHLPM	Serine hydroxymethyltransferase	Chlorobium	MDTDILKMQDREVFEAIALETGRQMETLELIASENFTSRAVMQACGSVMTNKYAEGYPGKRYYGGCEFVDIAENLARDRAKKLFGCEYVNVQPHSGSSANMAVLFSVLKPGDCIMGLDLSHGGHLTHGSSVNFSGQMYKAHAYGVDGETGIIDMNQVEKMALEVRPRLIICGASAYSQGFDFKAFREIADKVGAFLMADIAHPAGLIVSGLLSDPMPHCHFVTTTTHKTLRGPRGGMIMMGKDFENPMGITIKTKNGQRVKMMSEVMDAEVMPGIQGGPLMHIIAGKAVAFGEALRPEFRQYAMQVRSNAAAMSERFLSLGYNIVSGGTKNHLMLLDLRNKDITGKVVENTLHEAGITVNKNMVPFDDKSPFVTSGIRIGTAAMTTRGMNEDDSRLIAELIDRVILSAASPESSSVCRSVKEEIRSLCLRNPLEGYGVTPS	Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.	A4SFY3
A8XDI8	MTNA_CAEBR	Translation initiation factor eIF-2B subunit alpha/beta/delta-like protein	Caenorhabditis	MAPKINKIVNGPIPDSFLADETKRLDSLKFDGQRLEVLDQLLLPHEFKYIPVNDVSDAFNVIKSMQVRGAPLIAVVGSLGLLLEFNKNSELNIETIREKIEYLITSRPTAVDLRNSVTGLIPILETEGITDDEKLAKCQEYLLNVYTAEKLQNRILLWNAYQELLTAFPGKEKFTVMTICNTGSLATVSWGTALGVIRALHSENRLNLAYVLETRPYNQGIRLTATELLHGQVPFKLITDSMAAWAMKNHQLDCVLVGADNVARNGDTANKIGTYMLAVLCKHHNINFYPVVPFTTINKNISSGEEIKIEERAASELLRVNGVLVGNSECPVWNPAFDVTPAHLITKILTDFGNWSPAALEEQIPR	Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).	A8XDI8
P0DN06	VKT1A_ANEVI	AsKC1a	Anemonia	MVFLLCFFLVADVSYGINKDCLLPMDVGRCRASHPRYYYNSSSKRCEKFIYGGCRGNANNFHTLEECEKVCGVRSRDSPKEN	Dual-function toxin that inhibits both the serine protease trypsin (Kd=30 nM) and voltage-gated potassium channels Kv1.2/KCNA2 (IC(50)=2800 nM).	P0DN06
P47116	PTK2_YEAST	Serine/threonine-protein kinase PTK2/STK2	Saccharomyces	MAGNGKDKEVDKSPSVSTLKLLGKRLFNSSSHTDNSSLLLSAEQLGNGRSLRKRPTSPSISGSGSGGNSPSSSAGARQRSASLHRRKNNASVGFSNGSVSSHKSSVALQDLIKHNNNPYLNSPSDILGTGTGIASTRDRDRAVLDREKEKERARNKERNTHHAGLPQRSNSMASHHFPNENIVYNPYGISPNHARPDTAFADTLNTNKENDLSFYMHDGNSKIRMLPLPIANPNDFLPEDMKQYSVHLTDNFVFDTDNKPIGSGGSSEVRKVKSSYRQKDVYALKKLNMIYHESPEKFYKRCSKEFIIAKHLSHNVHITNTFYLLKVPTTTYTTRGWGFIMELGVKDLFQLMERTGWKNVPFNEKYCLFKQVAQGIKFCHDNGIAHRDLKPENVLISKEGICKLTDFGISDWYHVIPHDYTSPVKTCQGMIGSPPYTPPEVMYFDAKKHYPEKFQKPYNPLAMDSYALGIMLITMINNIIPFIDSCNTDARFREFEVSYDNFINHQNPHFRDKGCHKPGPGSEYSLARNFKNTDATRIAWRLADPNPATRYTMDDLFNDPFFQQIETCVEPNDDDLVRVPELRKSTSTNDFSENSLDAPHDQEVIHTSNPFLKKETLTSKPRSMLEIAESPSLKQKSKVKDSAKTKTHDVGDEGGNESTKPKQQDKKENLKKDEVKNGDKDKVIEEATTTNVDSILEKPTPTSTKVEDNLSEDDSTMKELKSMLNSTPTTPTHNGPTPLPAKAGTQLDKRMSDLSLKSETPASTKNFSAPNVSSSSNSLRSLGSPSVSSSKKKKVIHHHLDITNSVTNMSSVSAFISR	Essential determinant for high-affinity spermidine transport. Required for the activation of the plasma membrane proton pump PMA1 via phosphorylation of 'Ser-899'.	P47116
P28604	NODQ_AZOBR	ATP adenosine-5'-phosphosulfate 3'-phosphotransferase	Azospirillum	METGTGRGLLRFLTCGSVDDGKSTLIGRLLHDAGLISDDQLEQARRDSRGRAEEDGGIDFSLLVDGLEAEREQSITIDVAYRYFATDRRSFIVADAPGHEQYTRNMATAASGASLAVLLVDARKGLLTQTRRHAIVASLMGIRHVVLAVNKMDLVEDGETVFAAIRQAFTVFSAPLGFRSVTAIPLSARHGDNVVHRSAAMPWHHGPTLLGHLETAAAEDDPTEDGPLRFLVEWVNRPNLDFRGLSGTLLSGSLETGGAVTVWPSGRSARIARIVTFDGDVTQARAGDAVTVTLDAAVDAGRGDLLSGPDGAPEVADQFAAHLLWMAEEPLIPGRSYLLRAGARWVPATVTALRHAVNVETLEHGAASVLGLNAVGLCNLSTAAPLAFDPYEASRHTGSFILVDRFSNRTVGAGMIRHPLRRAANLHRQELAVSTVERAALKRQRPAVLWFTGLSGSGKSTIANRVERRLHTLGHHTMMLDGDNVRLGLNRDLGFTDADRVENIRRVGEVAKLMTEAGLIVLCAFIAPFRAEREAVRALLPDGAFLEVFVDTPLDECMRRDPKGLYAKARAGTLRNFTGVDSPYEAPDAPELRLDTTAEDADALAERVVELLHRKGIAEA	APS kinase catalyzes the synthesis of activated sulfate.	P28604
A7MLX1	NRDR_CROS8	Transcriptional repressor NrdR	Cronobacter	MHCPFCFAVDTKVIDSRLVGEGSSVRRRRQCLVCNERFTTFEVAELVMPRVVKSNDVREPFNEDKLRSGMQKALEKRPVSSDDVEMAINHIKSHLRATGEREVPSKLIGNLVMEQLKKLDKVAYIRFASVYRSFEDIREFGEEIARLQD	Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.	A7MLX1
P48368	CRTE_CYAPA	Farnesyltranstransferase	Cyanophora	MKPLQTNFNLLTYLYERKEIVEDTLNKSIPRGNPTFIYDSIRYSLSAGGKRIRPILCLASCELAGGTMEMALPTACALEMIHTMSLIHDDLPAMDNDSYRRGKPTNHIIYGEDLAILAGDALLAYAFEFIATQTKNVPADLIVKVIAQVAHSVTTSGLVGGQIIDLSSEGKSDTTLETLNFIHIHKTGALLEAAVLSGALLAGAKEKDMNRFLRYAQNIGLAFQIIDDVLDIISTEEKLGKSIGKDLKTQKATYPSFWGVEESIKQAELLVEEAKEEILYFDNKAIPLIAIADFIVNRNN	Catalyzes the condensation of farnesyl diphosphate (FPP) and isopentenyl diphosphate (IPP) to yield geranylgeranyl diphosphate (GGPP) needed for biosynthesis of carotenoids and diterpenes.	P48368
A8F2U0	ATPB_RICM5	F-ATPase subunit beta	spotted fever group	MAKNIGKITQIISAVVDVKFTNNGELPEILNALECYNDKQRIVLEVAQHIGDDTVRCIAMDSTEGLVRGVEVIDTGSPIRIPVGTETLGRIMNVVGEPIDGKGDIKSSNISSIYKPAPDFTNQSTERNILVTGIKVIDLLAPYTKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYTVFAGVGERTREGNDLYHEMIDSGVINLAEPEKSKVALVYGQMNEPPGARARVALSGLTIAESFRDMNEGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGELQERITSTKYGSITSVQAIYVPADDLTDPAPATSFAHLDATTVLSRQIAELGIYPAVDPLDSNSQVLDPMIVGEEHYSVARQVQQVLQTYKSLQDIIAILGMDELSEEDKLTVVRARKIQRFLSQPFHVAEVFTGAEGKFVNLADTIAGFKGLVEGKYDDLPEAAFYMVGTIDEAIEKAQTLK	Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.	A8F2U0
Q21DL5	GLMU_SACD2	Glucosamine-1-phosphate N-acetyltransferase	Saccharophagus	MLEIIILAAGKGTRMRSDKPKVLHTLAGKPFLEHVLDRSAELNADKVHVIIGHGADMVREALAGRDVNFVEQTEQLGTGHAVLQVLPHLNPESDTLILYGDVPLTKTDTLAELRAKVSDSSMGLLTVNLADPNGYGRIVRTNGSVTAIVEQKDANPEQLKIDEVNTGVMAVKSAHLAKWLPALSNDNAQGEYYLTDIIAMSSADDIAIETAQPKDEYEVLGVNNRLQQAELERIFQRQVAEELMVAGATLLDPARLDCRGSIEVGRDCVIDVNCVFEGKVVLGNNVHIGPNCVISDSTIGDGTVILANSILEESTLAENCNIGPFARLRPGSQLASKAKIGNFVETKKAVIGEGSKVNHLSYVGDAEIGAGVNIGAGTITCNYDGVNKSKTTIEDGAFIGSNSALVAPVTVGKNATVGAGSIVTKNSEEGDLIIARAKQSNIKGWARPVKK	Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.	Q21DL5
Q8K3F7	TDH_MOUSE	L-threonine 3-dehydrogenase, mitochondrial	Mus	MLFLGMLKQVVNGTAQSKASSCRKLVLPLKFLGTSQHRIPADANFHSTSISEAEPPRVLITGGLGQLGVGLANLLRKRFGKDNVILSDIRKPPAHVFHSGPFVYANILDYKSLREIVVNHRISWLFHYSALLSAVGEANVSLARDVNITGLHNVLDVAAEYNVRLFVPSTIGAFGPTSPRNPAPDLCIQRPRTIYGVSKVHTELMGEYYYYRYGLDFRCLRYPGIISADSQPGGGTTDYAVQIFHAAAKNGTFECNLEAGTRLPMMYISDCLRATLEVMEAPAERLSMRTYNISAMSFTPEELAQALRKHAPDFQITYCVDPLRQAIAESWPMILDDSNARKDWGWKHDFDLPELVATMLNFHGVSTRVAQVN	Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate, mediating L-threonine catabolism.	Q8K3F7
C4K7A8	RL14_HAMD5	50S ribosomal protein L14	Candidatus Hamiltonella	MIQQESMLNVADNSGARSVKCIKVLGGSRRRYACVGDIIVISIKEAIPRGKVKKGEVLKAVVVRTSKGVRRPDGSIIRFDTNACVILNKNTEQPIGTRIFGPVTRELRNEKFMKIISLAPEVL	Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.	C4K7A8
Q28013	RASA3_BOVIN	Ins P4-binding protein	Bos	MAVEEEGLRVFQSVKIKIGEAKNLPTYPGPNKMRDCYCTVNLDQEEVFRTKVVEKSLCPFYGEDFYCEIPRSFRHLSFYIFDRDVFRRDSIIGKVAIKKEDLQKYHNRDTWFQLQHVDADSEVQGKVHLELRLSEVITDSGVVCHKLATRILECQGLPIVNGQCDPYATVTLAGPCRSEAKKTKVKKKTNNPQFDEVFYFEVTRPCSYSRKSHFDFEDEDVDKLEIRVDLWNASNLKFGDEFLGELRVPLKVLRQSSPHEAWYFLQPRDNGSKSLKPGDLGSLRLNVVYTEDHVFSSDYYSPLRDLLLKSADVEPVSASAAHILGEVCREKQEAAIPLVRLFLHYGRVVPFISAIASAEVRRTQDPNTIFRGNSLTSKCIDETMKLAGMQYLHVTLKPTIEEICQSHKSCEIDPVRLKDGESLESNMENLRQFVDRVFSVITKSGVSCPTVMCDIFFSLREAAAKRFQDDLDVRYTAVSSFIFLRFFAPAILSPNLFQLTPHHTDPQTSRTLTLVSKTIQTLGSLSKSKSASFKESYMAAFYEFFNEQKYADAVKNFLDLISSSGRRDPKSVQQPILLKEGFMIKRAQGRKRFGMKNFKKRWFRLTNHEFTYQKSKGDPPLYSIPIENILAVEPLEEESFKMKNMFQVIQPERALYIQANNCVEAKAWIDILTKVSQCNQKRLAVYHPSAYLNGHWLCCRASSDTAAGCSPCTGGLPANIQLDIDGDRETERIYSLSSSYMSKLETMQEACGSRSVYDGPEQEEYSTFIIDDPQETYKTLKQVVAGVGALEQEHAQYKRDKFRRTKYGSQEHPIGDKSFQSYIRQQSETPAHSM	Inhibitory regulator of the Ras-cyclic AMP pathway. May bind inositol tetrakisphosphate (IP4).	Q28013
Q9H4K7	MTG2_HUMAN	Protein obg homolog 1	Homo	MAPARCFSARLRTVFQGVGHWALSTWAGLKPSRLLPQRASPRLLSVGRADLAKHQELPGKKLLSEKKLKRYFVDYRRVLVCGGNGGAGASCFHSEPRKEFGGPDGGDGGNGGHVILRVDQQVKSLSSVLSRYQGFSGEDGGSKNCFGRSGAVLYIRVPVGTLVKEGGRVVADLSCVGDEYIAALGGAGGKGNRFFLANNNRAPVTCTPGQPGQQRVLHLELKTVAHAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGHLQIAVADIPGIIRGAHQNRGLGSAFLRHIERCRFLLFVVDLSQPEPWTQVDDLKYELEMYEKGLSARPHAIVANKIDLPEAQANLSQLRDHLGQEVIVLSALTGENLEQLLLHLKVLYDAYAEAELGQGRQPLRW	Plays a role in the regulation of the mitochondrial ribosome assembly and of translational activity. Displays GTPase activity. Involved in the ribosome maturation process.	Q9H4K7
B4HHG8	EI3D2_DROSE	Eukaryotic translation initiation factor 3 subunit 7-2	Sophophora	MSNYAPFIKPYVEYNEHGWGPCEVPELDVPYQPFCKSDRLGKICDWTAMVPEKKFPSKYASTFGNNSQYAYFYEDDDSTFHLVDTTGSKATKPYQRGRYRTNMRNNVRTRGRTGRGTPNIASLGGSTAGGATASTTKYGKGRHTRNTQNVGRRFGRNAPTRIRESSVMVQSNWVSIEEIDFPRLLKLALPNIKEGKDIATCGSLEFYDKLYDRVNLRNEKPLQKMARVVHTVTTTDDPVIRRLSRTMGNVFATDEILSTIMCCTRSNYSWDVVVEKLGTKVFLDKRYNDQFDLLTVNETSVEPPMEEEGSINSAHSLAMEATLINHNFSQQVLRIGDQEQRFMFEEPNPFEEPGVDLASIGYRYRQWDLGNDVVLIARCKHNAVIQGPNGDMQFLSIKALNEWDSKVTNSVEWRQKLDTQRGAVLASELRNNACKLARWTVEAVLAGSDQLKLGYVSRMNPRDHLRHVILGTQQFKPQEFATQINLNMDNSWGVLRCLIDLVMKQPDGKYLIMKDPNKPMIRLYDVPENAFDSDRDEEESSEPLSNSNDN	mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. In the eIF-3 complex, eif3d specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs.	B4HHG8
C1KVP1	EZRA_LISMC	Septation ring formation regulator EzrA	Listeria	MYYMLIGFIIVVIAVIGAGYILKRKHYQRINELEEKKIKLRERPVIDELSKVKKLKLTGQTEALFESWRSSWDEIETRLFPDLEEVLLEAEMNTDRYKFRSATHAENDIEQMLVVIEKQMDQILGGLKELLISEEKNAKESRATKEKFAELRREVLTRGFKLGETLPYIETKLSELSESLNSYDSLTDQGDHLEAREIVIVVQKEMQVIEAQMERIPSLLHETDTILPEEMTKLRAGYEEMVRKGYYLAQMELDKEISRMKNQIDKMKKNVINLDLDEAEQGVEELHNEIDLFYDTLEHEAEARHFVKENHSPTSDKLQRQNAVSDALAEQITEVKQTYHVAEDDLAVYLKTSAKLSEAKENFEQLTALIASGEIAYSAAQDTLKEIDAALITISAEQDKFAEELRSLRKDELEARDDAERMRRAIITLDRKMERERLPGLPEEYLSLREHMGESINALEKRLEEKPLNMKAVSQDWRIAEEDLTHLTEKAEEMMENVRLVEHVIQYANRYRLRNKELADELVQAENHFYNDYQYKKALEIAVTALEKVETGAFKKVEKAYESKVSVDDIE	Negative regulator of FtsZ ring formation; modulates the frequency and position of FtsZ ring formation. Inhibits FtsZ ring formation at polar sites. Interacts either with FtsZ or with one of its binding partners to promote depolymerization.	C1KVP1
B0UXH9	PIRC1_DANRE	UPF0691 protein C9orf116 homolog	Danio	MSTNEIKNDYSAKEETAGPGDSNTSEIKTSDVYKVDKNLPSRFNNPDCFRYSHKTTNPLYRTTNQAYGSKKPTVHEMPTSFNGSRHRFSEHLLKSGMYRDNGFNTMLDKSRLSRPNETSVFYDRINFHSLYHTAGKS	Microtubule inner protein involved in the attachment of outer dynein arms (ODAs) to dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating. Functions at the initial step of left-right asymmetry specification of the visceral organs.	B0UXH9
P53617	NRD1_YEAST	Protein NRD1	Saccharomyces	MQQDDDFQNFVATLESFKDLKSGISGSRIKKLTTYALDHIDIESKIISLIIDYSRLCPDSHKLGSLYIIDSIGRAYLDETRSNSNSSSNKPGTCAHAINTLGEVIQELLSDAIAKSNQDHKEKIRMLLDIWDRSGLFQKSYLNAIRSKCFAMDISNNTANTASQQLSLDPKQRSKQILSNLKKSPPLNLNISLPTDLTSTDPAKQQAALFQVIAALQKHFKTLPSHTSVGTVAPPQAHTITEYGSRRERERERERYNSRRNRSRSPPAPFSQPSTGRKDRYPSVAQDQYSIGAPNTTFGTNNHHLYPDELNVSNNPHYRPKPVSYDSTLPPDHIKVYSRTLFIGGVPLNMKEWDLANVLKPFAEVQSVILNNSRKHAFVKVYSRHEAENVLQNFNKDGALPLRTRWGVGFGPRDCCDYQHGYSIIPMHRLTDADKKWSVSAQWGGTSGQPLVTGIVFEEPDIIVGEGVSSKAISQKMPTDSGRNGPRSGKPNKSGSISSISPVPYGNAPLASPPPQQYVQPMMQQPYGYAPNQPLPSQGPAAAAPPVPQQQFDPTAQLNSLMNMLNQQQQQQQQS	Plays a role in sequence-specific regulation of nuclear pre-mRNA abundance.	P53617
A4FW56	CYDE_METM5	L-cysteine desulfhydrase	Methanococcus	MDDSKRILITKILKNEVTEALGCTEVGLIGYAVSLCNISDPFSIEKIELTLNNGSFKNVYAVGVPNTGKYGLLPAVVGGFLGNSKNKLLIFNDITYSQELEDFTKEKLEIKVINGPLYCSVKIKDNSGKIHESLIKDNHLNVVIPEIKKEKINMEINSSEKEKYKNLELLDFLNYLDEIPEEIIKLVEKTIYTNKNLIKGDFLNYGTDILSNMVNKTTSACNIRMTGENMTAMSVAKSGNMGIMATLPIISYDFSTENNSEKLIKSVLLSMLVTIYSTYNSSYLSSMCGCVSKGGMGAVIGLSHYKNGKNLKKFDSSARTFTANLPGIICDGGKVGCALKLASGCFAAYSSLFVDISYENGIVGKNFKECVENISKISKAMGDLDCDIVEIMSKKEM	Catalyzes the cleavage of L-cysteine to form 2-aminoprop-2-enoate and sulfide. The former then spontaneously hydrolyzes to pyruvate and NH(3). May be responsible for the production of sulfide required for the biosynthesis of iron-sulfur centers in this archaea.	A4FW56
A7FZ65	RS19_CLOB1	30S ribosomal protein S19	Clostridium	MSRSVKKGPYIQEVLLKRINEMNKNGEKKVLKTWSRSSTVFPQMIGHTIAVHDGRKHVPVYITEDMVGHKLGEFVLTRTYRGHDDKSEKSSRLR	Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.	A7FZ65
B1Y8I5	RL23_LEPCP	50S ribosomal protein L23	Leptothrix	MSRAPISRTFTEGRLAQVLVAPIISEKATSIGEKHNQVLFKVLQDATKIEIKAAVELMFKVEVESVQVLNQKGKTKRFGGRTGRRDHLRKAYVSLKAGQELNFSGEAA	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.	B1Y8I5
Q5WL08	G1PDH_ALKCK	sn-glycerol-1-phosphate dehydrogenase	Alkalihalobacillus	MNISALKARIRASKEDLYPLPLEQIVVAEGALREAAAFIAKQAESGVVLVADSHTYKAAGRDLHDHLCQKGVKADWHLLEPNSNGDIIADEVSLISVMLKVEQSTKLLVAVGAGTIHDIVRFVSGKTNKPFVSIPTAPSVDGFTSLGAPIVVQGSKKTYQLVAPIALFADTVVLQHAPPALIAAGFGDMVGKYTSLFDWKIGSLLKNEAYSDLVADLTEEALSTCVDKVADIGKRTSAGVQVLMESLLTSGLAMALFGYSHPASGAEHHLSHYWEMEALRLGKKQLLHGAKVGLSTQIINRFYKNTVLPDVHRFLDDDEAKQVIALVEALPDPDDVKALLEQAGWNEALVPIAPELVEESLQHAYLLRDRYTLLRLYREGTTMKKEGDAHVGRS	Catalyzes the NAD(P)H-dependent reduction of dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1-phosphate (G1P). The G1P thus generated is probably used for the synthesis of phosphoglycerolipids in Gram-positive bacterial species.	Q5WL08
B2TYK2	GRCA_SHIB3	Autonomous glycyl radical cofactor	Shigella	MITGIQITKAANDDLLNSFWLLDSEKGEARCIVAKAGYAEDEVVAVSKLGDIEYREVPVEVKPEVRVEGGQHLNVNVLRRETLEDAVKHPEKYPQLTIRVSGYAVRFNSLTPEQQRDVIARTFTESL	Acts as a radical domain for damaged PFL and possibly other radical proteins.	B2TYK2
O15432	COPT2_HUMAN	Solute carrier family 31 member 2	Homo	MAMHFIFSDTAVLLFDFWSVHSPAGMALSVLVLLLLAVLYEGIKVGKAKLLNQVLVNLPTSISQQTIAETDGDSAGSDSFPVGRTHHRWYLCHFGQSLIHVIQVVIGYFIMLAVMSYNTWIFLGVVLGSAVGYYLAYPLLSTA	Involved in low-affinity copper uptake.	O15432
Q3B2F8	RUVB_CHLL3	Holliday junction ATP-dependent DNA helicase RuvB	Pelodictyon	MRIELLNTPVDAVELRIEDQIRPRRMEDFTGQQRLTDNLKVFISAARMRGDALDHVLLSGPPGLGKTTLAHIIAEEMGGSLKATSGPMLDKAGNLAGILTSLQKGDVLFIDEIHRMPPAVEEYLYSAMEDFRIDIMLDSGPSARAVQLKVEPFTLVGATTRSGLLTAPLRARFGISNRFDYYPPELLETILMRSSTILGIGIERDAASEIAGRSRGTPRIANRLLRRARDFAQVDGMEIISRPTAMKTLDSLEIDEEGLDEMDKKIMDAVVNRFSGGPVGVGSLAVSVGEEQDTIEEVYEPYLIQAGYLSRTPRGRVATQRALLRFSDGSSALRGTLFDGQEHV	The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.	Q3B2F8
B5ZN86	RRF_RHILW	Ribosome-releasing factor	Rhizobium	MTEGIDIKELKRRMDGAVSAFKSDIASLRTGRASANILDPVTIEAYGSRMPLNQVANITVPEPRMLSVSVWDKSMVSAVERGIRESNLGLNPIVDGQSLRIPLPELNEERRKSLVKVAHDYAEKSKVAIRHVRRDGMDGLKKAEKDGVIGQDEGRAQSERVQKMTDETISEIDRLLGEKEKEIMQV	Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another.	B5ZN86
A8NCK6	COX2_COPC7	Alpha-cuprenene oxidase 2	Coprinopsis	MNIVNSLDLSNITTNHVAAAVCAGIAVYAIVAGRNRGKKYPPGPKGHPLIGSLFEMPIQNAHVVYKEWAKTYGDMIFFKVLGQPFLILSSEETITDLLDKRSTIYSSRPRMPMVVELMGWDYTLGLLPYGERWRFLRREFHRFMSPTAVSNYRQIQENSVYTFLNNLVESPEQFSKHLRLFYGSISMKVSYGINVKSAEDQYLLDAEGAMSGFMEAGIPGRFWVDLFPALKYVPSWMPGAEFKRKAARWARLNDISLERPFKHVLDQLKKGVASQSVSATLIEELPDQNSPDRKEKETIARNISATTFLAGIDTIHSTTQAFFYAMAQFPEVQKKAQAEIDAVVGDKRLPTFEDRDQLPYVNALVKELIRWSEVAPLGIYHSTTEDDEYKGYFIPKGTIVMTNAWSILTDPVTYPDPFAFKPERYLKNGVMNPDAPRPEDLAFGRGRRICPGRYLADETLFMTSVGVLAGFNISPPLDKSGKPIKLKNERVGTITLTPPKFECRIEPRSPAIRTMIHDTAESISAL	Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of alpha-cuprenene and oxidized derivatives . The alpha-cuprenene synthase COP6 is the only sesquiterpene synthase identified in C.cinereus that appears to be part of a biosynthetic gene cluster and is highly specific since it catalyzes the cyclization of (2E,6E)-farnesyl diphosphate into only one product, alpha-cuprenene . The cytochrome P450 monooxygenase COX2 then oxidizes the cyclohexadiene ring of alpha-cuprenene at positions 1 and 4, yielding first alpha-cuparene, followed by alpha-cuparophenol and a further yet unidentified compound resulting from one additional oxidation step . The cytochrome P450 monooxygenase COX1 then likely catalyzes the oxidation at position 9 of the pentane ring of alpha-cuprenene to give the corresponding hydroxy or ketone derivatives .	A8NCK6
Q4JV64	DAPA_CORJK	4-hydroxy-tetrahydrodipicolinate synthase	Corynebacterium	MSTGNAATRGSAHFGTISLAMVTPFKKDGSIDLDAGVALAGHFVDEGCDSLVLAGTTGESPTTGATEKLDLLRAVRSELGDSVKLIAGSGSYDTAVTVEMSRASQEAGADSLLVVTPYYSRPSQEGIYQHFTTVADAVDIPVCVYDIPSRSVVPVEPETLHRLADHPQIAAVKDAKGDLAAGMELIENTDLAWYSGDDPLNLPWLAAGATGFISVIGHVATRQLKQLRDAFDAGDIATARSIAVQLQPLQKAQARLGGVTFAKAALKLKGKDVGAPRLPIIEPTAAEMDQLAQDLQAAGV	Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).	Q4JV64
A0AKW5	DCUP_LISW6	Uroporphyrinogen decarboxylase	Listeria	MTKITNDLFLRAARKEQVDKIPVWYMRQAGRSQPEYRKLKEKYSLFEITHQPEICAYVTKLPVDQYGVDAAILYKDIMTPLPGMGIDVEIKSGIGPVIHNPIRTFQDVDKLSIFKPEIEVPYVLDTIKLLADDMLEVPLIGFAGAPFTLASYMIEGGPSKNYHLTKSFMYREPEVWSILMEKLGRMTATYLIAQINAGASAVQLFDSWVGALSRADYTKYIRPVIEMIVREVKAVHPTTPIIMQAVGASHLLEEWETMPLDVVGVDWRETLTGARKKVPSKAIQGNLDPSTLLAPEKCLEEAERIIQEGILKPGYIFNLGHGVFPEVQPEMLKKLTNYIHDRSEILLKKG	Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.	A0AKW5
B8E7D3	OPGG_SHEB2	Glucans biosynthesis protein G	Shewanella	MVSLLRCPSSKPYSSLICSLTLGAVVALSGVAYAEETKPAETVPVVTPPKVISQPATKNQVRFTKTGAFDSDTVVKIAKRLAAKPYVALKDPLPAGLAKLSYDEYRDIRFNPTASIWRDQGVPFQMQMFHRGFYFQDLIEIAIVEGQNATHLAYEPKYFTAGEVITQALPNDDIGYSGFRIHNQLNTNGVFDELMVFQGASYFRALGKGNAYGLSSRGLALKTADAEGEEFPIFRAFWVERPYNDSNLIVVHALLDSPSVAGAYTFSVRPGDNTLIDVEATLFPRVELSKVGLAPSTSMFLHSLNGRHDTDDFRPEVHDSDGLLMLNGRGEHLWRPLANPRQLQVSAFSDNSPQGFGLIQRERDYASYQDLEAHYERRPSLWIEPVGNWGQGSVVLTEIPTESEIHDNIVSYWKPRQPIPAGSEFHFAYRMSWGEEPAAKVGAVHVSRSASGRADIAKATPRRLFVVDYQIEGPMTDEMPVAKVEASGGVVTNVVIARNAAKNGYRLAFELEPEDKELIELRAELKFPTPRQVETWLYRWTL	Involved in the biosynthesis of osmoregulated periplasmic glucans (OPGs).	B8E7D3
Q58T74	M7H1_BOMMX	Maximin-6	Bombina	MNFKYIVAVSFLIASAYARSEENDEQSLSQRDVLEEESLREIRGIGAKILGGVKTALKGALKELASTYVNGKRTAEDHEVMKRLEAVMRDLDSLDYPEEAAERETRGFNQEEIANLFTKKEKRILGPVISTIGGVLGGLLKNLG	Maximin-H1 shows antibacterial activity against both Gram-positive and Gram-negative bacteria. It shows also antimicrobial activity against the fungus C.albicans. Shows strong hemolytic activity.	Q58T74
Q8NSR1	GUAA_CORGL	Glutamine amidotransferase	Corynebacterium	MSLQTNHRPVLVVDFGAQYAQLIARRVREAGIYSEVIPHTATADDVRAKNAAALVLSGGPSSVYAEGAPSLDAEILDLGLPVFGICYGFQAMTHALGGTVANTGKREYGRTDINVAGGVLHEGLEACHKVWMSHGDAVSEAPEGFVVTASSEGAPVAAFENKERKMAGVQYHPEVLHSPHGQAVLTRFLTEIAGLEQNWTAANIAEELIEKVREQIGEDGRAICGLSGGVDSAVAGALVQRAIGDRLTCVFVDHGLLRAGEREQVEKDFVAATGAKLVTVDERQAFLSKLAGVTEPEAKRKAIGAEFIRSFERAVAGVLEEAPEGSTVDFLVQGTLYPDVVESGGGSGTANIKSHHNVGGLPDDVEFKLVEPLRDLFKDEVRAVGRELGLPEEIVGRQPFPGPGLGIRIIGEVTEDRLETLRHADLIARTELTEAGLDGVIWQCPVVLLADVRSVGVQGDGRTYGHPIVLRPVSSEDAMTADWTRLPYEVLEKISTRITNEVPDVNRVVLDVTSKPPGTIEWE	Catalyzes the synthesis of GMP from XMP.	Q8NSR1
L0E155	MALA_MALAU	Malbrancheamide biosynthesis cluster protein A	Malbranchea	MAPTPKYTFTERAAAGNLSDAEILNSNNPTGSELPDESDVVVGGAGIHGLIYALHASKYKPNNLKISVIEKNTRPGYKIGESTLPIFYTWCKLHGISAAYLLRLFGLKDGLCFYFLDRENQGQYTDFCSVGAPGLVLASLQIERPMSELLFTILAQRNGVNVYHGREVDFKSTVVQGGGQGNKIAVSRGKYDSTPKTIDSALFVDATGRFRQFCSKKAPRHRFDGWNCNAFWGYFTAPKDESKIPFDLYEGDHTNHLCFPEGWVWVIRLPSWEGSLIANLMDMVTYILECADAGVPGDELPSSEELARMFGLKFQWVTSIGFAVRNDVKYPEDLSAYGTREAEQKFNYFVQKYELLQQFMSNFELIENLYGPGTTWFIRKTLAYQSPVVSGPGWLAIGDACGFTNPLYSPGINVGMSTSTWAAQLSHRIVEIGKSAPADAAESSIRKLLVPYDDYCKSLVPALEQMNRFNYVCYRDTRLGPQVACLWQFFAGIERYLSDVNIETFAHYAIKWVWGAMVPEYQQVAQKCIEHIETVPLDERLPDAMVDELLAFSNRIKSAAVAADDFSLRWDAILRSFDRSLNFVEGKTSRDIYTRQCSGCGAWLQLRPDWKKCHSCGLLGTEPQTAVTFDPPLTAEEEALLYAAWNTAPKYDPSKELKLPTPTRPAA	Flavin-dependent halogenase; part of the gene cluster that mediates the biosynthesis of malbrancheamide, a dichlorinated fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core . The first step of malbrancheamide biosynthesis involves coupling of L-proline and L-tryptophan by malG, a bimodular NRPS, to produce L-Pro-L-Trp aldehyde through reductive offloading . This compound undergoes spontaneous cyclization and dehydration to give a dienamine which is reverse prenylated at C-2 by malE . The other prenyltransferase present in the cluster, malB, displays modest activity, suggesting that may be a redundant gene in the pathway . Subsequently, a [4+2] Diels-Alder cyclo-addition catalyzed by the bifunctional enzyme malC forms the characteristic bicyclo[2.2.2]diazaoctane ring of premalbrancheamid . Finally, the flavin-dependent halogenase malA catalyzes the iterative dichlorination of the indole ring of premalbrancheamide to yield C-9 monochlorinated malbrancheamide B, C-8 monochlorinated isomalbrancheamide B, and dichlorinated malbrancheamide . MalA is also able to brominate premalbrancheamide at C-9 to yield malbrancheamide C, and, to a lesser extend, at C-8 to yield isomalbrancheamide C . Finally, malA can brominate C-9 monochlorinated malbrancheamide B at C-8 to yield malbrancheamide D, or C-8 monochlorinated isomalbrancheamide B at C-9 to produce isomalbrancheamide D .	L0E155
A5F2Y7	RLMH_VIBC3	rRNA (pseudouridine-N3-)-methyltransferase RlmH	Vibrio	MKIQLIAVGTKMPKWVEEGFQEYRRRFPHDMPLELVEITAGKRGKNADIARILQKEGEAMLAAVPKGNRIVTLDIPGKRWDTEELAVQLESWKLDGRDVSILIGGPEGLAPACKAAADQSWSLSPLTLPHPLVRVVMAESLYRAWSITTNHPYHRE	Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.	A5F2Y7
Q889W6	RL22_PSESM	50S ribosomal protein L22	Pseudomonas	MEVAAKLSGARISAQKARLVADQIRGKKVGEALNLLAFSSKKAAEILKKVLESAVANAEHNEGADVDDLKVSTVFVNEGRSLKRIMPRAKGRADRIVKRSCHITVKVADK	The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.	Q889W6
K7XFK5	KAX3G_MESGB	Tx4	Mesobuthus	MKVFSAVLIILFVCSMIIGISEGKEIPVKCKHSGQCLQPCKDAGMRFGKCMNGKCNCTPK	Potassium channel inhibitor.	K7XFK5
Q189R8	FOLD_CLOD6	Methenyltetrahydrofolate cyclohydrolase	Clostridioides	MSTKGQIIKGKPVADKISEELIKEVDLLVKEGINPKLTIVRVGARSDDLSYERGALKRCQNIGITTEVLELAEDITQEEYIDVLKRVNDDKNVNGILCFRPLPKHLNEEVIKYVIAPEKDVDCFSPINSAKVMEGDKSGFPPCTPTAVVEILKHYNVDLKGSKVTVLGRSMVVGKPVSMLLLSEHATVTICHSKTKNLSGVAAEADVLIAAIGRAKMVDESFVKDGAVVIDVGINVDEEGNLCGDVDTNAVLDKVSMITPVPAGVGSVTTSILAKHVVKACKLQNNK	Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.	Q189R8
Q88YZ2	ACCD1_LACPL	Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta 1	Lactiplantibacillus	MSHYPASGTWQACPKCGRHVHQRQWGTYQQCPYCHYWQRLTTAQRLEQLVDEGSFQPLTMTERPVNQLGFPDYMNKLRRAQRQTGLNEAVVCGTALIEQQPCILAVMDSHFMMGTLNTAVTRRLLHASEQARAQRLPLIIVTASGGARMQEGVYALVGMNLILAELARLAATPLPLITVLTDPTMGGVSASFAFKGDLIIAEAGAKIGFAGARVIQQTLPVKLPADFQTADQLFKNGMVDAVVERPQLRSTLGQALVNYGIGRSAHG	Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.	Q88YZ2
B7VBM9	ARNE_PSEA8	Undecaprenyl phosphate-aminoarabinose flippase subunit ArnE	Pseudomonas	MSAALLLATLLMTGLGQVAQKLTVEHWRLVAADGWTARLRSPWPWLALLALGLGLLCWLLLLQRVEVGSAYPMLALNFVLVTLAARFVFDEPVDRRHLAGLLLIVAGVALLGRSA	Translocates 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol (alpha-L-Ara4N-phosphoundecaprenol) from the cytoplasmic to the periplasmic side of the inner membrane.	B7VBM9
Q9F5Y1	RNFE_AZOVD	Rnf electron transport complex subunit E	Azotobacter	MSHCGAPSVPEPEKKVPWQYFTSALWQYNVALVQMLALCPTLAVTTTATNGLGMGLATTLVLVMTNALISSMRHTISPEVRNPVMIGVIAGVVTLTDMAMNAWMHELYKVLGLFIALIVTNCAVLGRAESFCLRNPVIPSILDGAGMGAGFTAVLVVIGGIREILGSGTLFSQASSLLGSHFKWMEITVIPDFQGILLAILPPGAFIVLGFLLAAKRVIDRKRAERRQQTHGELVVLQ	Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.	Q9F5Y1
P27715	UNC13_CAEEL	Uncoordinated protein 13	Caenorhabditis	MDDVGDYNDDQLSDGMSMRLLCITIKKARLQGAVDEFNSYVTVKLQTVKSTTVAVRGNLPCWEQEFIFETNRPDDGMVLELWAKGVLWDKLIGVHYMPLSEIRYSNAAGSGQWLQMDHELETRNGQTVGTRGPTGHNLLTDVRFELPFDVQGHDEDIQSRLLALNGLIEHDQLGPNNHHRAPFNHSGLSEDSDYTSDVSVPVNHHQLHPNSSAHQYESHLHPHRTRQLLHTREGAASYEDEEDAYHARHQPESDDYNHQDTYDQHSSYYNDEYAPSGSSSQYQRQGYQDQDQQHQNIYEDTVTPVREFGESAVPPAASSSRRQFDQVYGYASSSEERYDTPMSSGRLPRDEPILEHSEPEYVYDQNGYPEEDNYGINPTYSEDHFEGQTNDYSTTHQEPNDFRNDYNSSYQREYWNESEPLSYNSRPPNGHIRTGANTWREPSTSSRPTSSQAWNYQDDTHQYDEVDRGSRVSFTRTPSVDRTDRPSESGGGFYDEMSESGRPGRPDSHHNWRYDSIQEEDNEKDNWKQHVEGYEEGQEEKQKDNQKPNDHSAASPQDHYHRSDSTAQQDFGNNIVRQTIQEEEEKRNYQELWHNAYKRVCADLGIKSSQASLVATTGGTLLQNLFLYRPKLAPAGHGATASQFQSPAGATRFYANHNNNNNNVSKNELDSTTETPPDPSRTPSTSSMNPVPSLAVPMSPGPYLNSDPPSPVSPNPQIKRSIYRIKESYEDRNGGRERIYTTNLVSVYLEKMKPPDELEEGSSGSMRETQNEIKNGTQLHNAESNIFFPQDSVPKSISYNAGNLKNTSITTSKTSSAITNHSSLPPQPPSKPASRDSDPMKQLLTFSKSFKKVRRVRSAMPRRRKRKRVKIKKSRSCPILWKTEKTPHPMKSKSMTCIRIPKKTVIAPLRKEIKIVRMKPPAARCESDSKAHKKKNLLDVYKDMGKSTVLDGNGSSAANAFYKSIDAAPNMNVARTKTSIPLVSELVLKTMATKRAQAGLANAARTTFSDTELKTHVYKKTLQALIYPISATTPHNFATTTFQTPTFCYECEGLLWGLARQGLRCTQCQVKVHDKCRELLSADCLQRAAEKSTKHGEADRTQSLVNVIRDRMKIQEQNKPEVFQMIRTVFDVDENIQKETLKTVKASILEGSSKWSAKITLTVLCAQGLIAKDKTGKSDPYVTAQVGKTKRRTRTIHQELNPVWNEKFHFECHNSTDRIKVRVWDEDNDLKSKLRQKLTRESDDFLGQTVIEVRTLSGEMDVWYNLEKRTDKSAVSGAIRLHINVEIKGEEKLAPYHVQYTCLHEHLFAAHCVDEEVKLPKVRGEDSWKVCFQETGQEIAEEFAMRYGIESIYQAMTHFACLCTRYMCAGVPAVLSTLLANINAYYAHTTATSAVSAPDRFAASNFGKERFVKLLDQLHNSLRIDLSAYRNHFPSSSPAKLQDLKSTVDLLTSITFFRMKVLELASPPRASTVVRECAKACMQQTYQLMFESCAEQFPILDTSVQFWYEFIDYIMRVIEEDQKNYTPALNQFPQELNVGNLSAETLWSMYKNDLKMALEEHAQKKRCKTPEYMNLYFKVKGFYFKYVADLSTYKSSIPEFPAWFIPFVMDWLNENDEHSMDILRNAYNVDKADNFPQTSEHTKFSNSVVDVFTQLNAALKLLKQMDCPNPEVAADMMKRFSKTLNKVLLAYADMVQKDFPKFAHDEKLACILMNNVQQLRVQLEKIYETMGGAELDEHIGQVLTVLQKKLNSVLDRLSAEFVTTLEPHIHEQTIKLGMLLVKIKGPQLQKTQVQPEADAVLEPLMDLLEGSLRRYADQCEKTVLKYILKELWKITIVNMEKRVVLPPLSDKALLKQLPNAKIGDVTKLMSTNIQSIKGMNSVKDMMDMARESEKSLTPRQCTVLDCALDAIKDSFHASGKGLKKSFFEKSPELQSLKYALSLYTQTTEQLIKTFITSQRQQDLPSQEQPVGEVSVQVDLFSHPGTGEQKVTVKILAANDLRWQTSSAFKPFVEVHLVGPHLSDKKRKWSTKTKAGNWAPKFNETFHFFLGNEGEPEHYELMFQVKDYCFARDDRVVGVGVLQLSSVVDQAGSCAMWVQLGTRLHIDETGLILLRILSQRQTDEVAKDFVRLKTECRYETETVMAASASSQNINRT	May form part of a signal transduction pathway, transducing the signal from diacylglycerol to effector functions . One such function could be the release of neurotransmitter from neurons . Probably by regulating neuronal transmission downstream of lin-3 and receptor lin-23 and phospholipase plc-3 and upstream of innexin unc-7 and egl-4/PKG in ALA neurons, involved in the decrease in pharyngeal pumping during the quiescent state that precedes each larval molt, .	P27715
C4K230	ATPD_RICPU	F-type ATPase subunit delta	spotted fever group	MNKGNLIENYAVALFNNAMVDNIQDKIFEEITSINRIITDNFDIREFLFSPIVNKNDKINAVNSLAKNIKISTIVQNFLLLLVKNSRIAILSNIVDAYNTLLYESKNIKIVQVISANKLQPKEQEWIKSRIEKELNQKTEILFDIDNTIIGGIVIKYDSMLQDYSIKGSLEKITKALKTVNIAV	This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.	C4K230
P14117	RL4_XENTR	L1	Silurana	ITLLNVSKLNLLRLALGGHVGRFCIWTESSFRKLDDLYGTWRKSAKLKADYNLPMHKMTNTDLTRILKSQEIQRALRAPNKKVKRRELKKNPLKNL	Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.	P14117
B1XPT3	MTNB_SYNP2	Methylthioribulose-1-phosphate dehydratase	unclassified Synechococcus	MSLENQTQKERLCAVIRQLHTQGKSPATSTNYSFLDEDQVIFVSRSGVDKSQFQPEDFIAVDTMGLPLPPDEGIKPSAETLIHCFIYQNFPGITCVLHTHSVAATLLSGIFAAKQAVTFSGYEVIKGIAGQTTHETAIALPIFANDQDMKSFCQQLAQRQEELNNYGFLIAKHGLYAWGETMAIAKRHLEVWEFMLECELEQLKITPPLAAR	Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).	B1XPT3
Q12X59	G1PDH_METBU	sn-glycerol-1-phosphate dehydrogenase	Methanococcoides	MDVTHDMNGQKKWMQLPRNVVIGNGVINEVRDVCTDLKLIDNALVVTGKSTKGIAGEIVQDSLQDAGQNVELVISESASMKEVERIRKHAIESGTKYFLGVGSGKTIDVAKLAATDLEVPFISVPTAASHDGIVSSRASIKDGKTTTSVQANAPMAVIADTEIIANAPYRLLAAGCGDIISNCTAVLDWQLASRLQNVQFSEYAAALASMTAQILIDSADSIKPELESSVRMVVKALVSSGVAMSIAGSSRPASGSEHMFSHALDRVADEPALHGEQCGVGTILMMYLHGGDWKKISDALKLIGAPTTAKELGIEDKYILEALVLSHTIRPERYTILGTGLTPDAAEIVARKTKVIS	Catalyzes the NAD(P)H-dependent reduction of dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1-phosphate (G1P). The G1P thus generated is used as the glycerophosphate backbone of phospholipids in the cellular membranes of Archaea.	Q12X59
Q9RUF3	SYM_DEIRA	Methionyl-tRNA synthetase	Deinococcus	MQNPPQHPEAQSPETRDREFFITAAIDYANGTPHIGHVYEKILADAIARYQRLAGRDVTFVMGTDEHGEKISKAAAKGGVTPQELVDDLSERAFQGLWKKLGISYDFFIRTTSAKHKKYVQDVLQRVYDAGDIYFAEYEGLYSVGAERYVTEKELVEGPDGVRRFPGDKDPPELRREANYFFNMQKYQPWLLETLQQNPDLIQPAGYRNEVLEMLKEDIGPLSISRPKARVPWGIELPWDTDHVTYVWFDALLSYLTPLVSQGQDASMSGKAWHVIGKDILKPHAVFWPTMLRAAGLPLYRRLVVHSHILAEDGRKMGKSLGNAIDPEELVAAWPVDAIRYALLREASLGADSPFGEGVLVSRLNSDLANDLGNLLSRTVSMIQKYRGGVIPAATEPTDREREIEAAARALPDEVLRLVDELKINMAIDAAMSFVRDLNRYIAESTPWTLAKSPETQGRLDTVLYTAAEGLRVASVALEAVIPTKAKELREQLGLGRQGYPLQAAWGLTPAGTRVQGGAILFPKPEPKADETKNAEAKPPKPQAKKEKKTVTDTAPAKTTEQKPEAAAPAQNDGLISIDDFAKIDLRIAEVVACEAVEKADKLLKLTVKLGDETRTVVSGIRKWYEPEALVGRKVVLVANLKPAKLRGIESQGMILAAEDDAGNLDLVGTELDLPSGTKVR	Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.	Q9RUF3
B1VDE1	MIAA_CORU7	Isopentenyl-diphosphate:tRNA isopentenyltransferase	Corynebacterium	MDYSHSDSPSTAPAGKTPVDQLRPLLIVGPTGAGKSDLSLEVARRLDQPVEIINGDSMQMYRGMDIGTAKLSRAERAEFPHHLFDCLDVDDTASVAAYRDLAGETVEQIQARGARPIIVGGSMMYLQALVDDWQFPPTDAAVRAKWMAEQDRIGVEALHEVLRSKDPDAADIIEEKDPRRIVRALEVIELTGKPFAASQPPKNVPTRWGTRIFGLKAPGNWLNPRLEARVDRMFAAGLVAEVEGLATAGLSRESTAGKAIGYAQVLSALAGECSMEQAREDTVVGTRRYARRQRSWFRRDPRIHWLDATVADPGLLAGQVIDELRETTQG	Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).	B1VDE1

Q8CWR2

TRUB_STRR6

tRNA-uridine isomerase

Streptococcus

MNGIINLKKEAGMTSHDAVFKLRKILGTKKIGHGGTLDPDVVGVLPIAVGKATRMVEFMQDEGKIYEGEIILGYSTTTEDASGEVVAETPVLSSLDEKLVDEAIASLTGPITQIPPMYSAVKVNGRKLYEYARAGQEVERPERQVIIYQFERTSPISYDGQLARFTFRVKCSKGTYIRTLSVDLGEKLGYAAHMSHLTRTSAAGLQLEDALALEEIAEKVEAGQLDFLHPLEIGTGDLVKVFLTPEEATEVRFGRFIELDQTDKELAAFEDDKLLAILEKRGNLYKPRKVFS

Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.

Q8CWR2

Q83MJ8

TRUB_SHIFL

tRNA-uridine isomerase

Shigella

MSRPRRRGRDINGVLLLDKPQGMSSNDALQKVKRIYNANRAGHTGALDPLATGMLPICLGEATKFSQYLLDSDKRYRVIARLGQRTDTSDADGQIVEERPVTFSAEQLAAALDTFRGDIEQIPSMYSALKYQGKKLYEYARQGIEVPREARPITVYELLFIRHEGNELELEIHCSKGTYIRTIIDDLGEKLGCGAHVIYLRRLAVSKYPVERIVTLEHLRELVEQAEQQDIPAAELLDPLLMPMDSPASDYPVVNLPLTSSVYFKNGNPVRTSGAPLEGLVRVTEGENGKFIGMGEIDDEGRVAPRRLVVEYPA

Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.

Q83MJ8

B6YT21

RS7_THEON

30S ribosomal protein S7

Thermococcus

MAKPLTERFYQPKELKVMGRWSVEDVVVNDPSLRPYINLEPRILPHSHGRHAKKPFGKAQVHIVERLINKVMRSGASSHKVGGHFMRREHRSLMGKKMKAYEVVKEAFMIIERRTKQNPIQVFIRAIENSAPREDTTTIAFGGIRYHMAVDVSPLRRLDIALKNIALGASAKCYRNKTSYAQALAEEIIAAANKDPKSFAYSKKEEIERIAQSSR

One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center.

B6YT21

D0MY11

ITPA_PHYIT

Nucleoside-triphosphate pyrophosphatase

Phytophthora

MSSAKPVLTFVTGNANKLKEVVAILGADFPFELRNQAVDLPELQGEPADIAKEKCRLAAKQVQGAVLVEDTSLCFNALKGLPGPYIKWFLEKTGHDGLNNMLAAYEDKSAYAQCIFAYAPAGAEPQVFVGQTHGKIVPARGPTTFGWDPVFQPDGFEQTYAEMEKVTKNQISHRYKALEALKTHLVKPVDK

Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.

D0MY11

B1JXI7

KYNB_BURCC

N-formylkynurenine formamidase

Burkholderia cepacia complex

MDTLWDISPPVSPATPVWPGDTPVAVERVWRMEAGSPVNVARLTLSPHTGAHCDAPLHYDADGAPIGAVPLDTYLGPCRVIHCIGASPVVRPADVEVALDGVPPRVLLRTYARAAVEQWDSAFCAVAPDTVDLLAAHGVKLIGIDTPSLDPQESKTMDAHHRVRAHRMAILEGIVLDDVPPGDYELIALPLKFATLDASPVRAVLRALPAHAS

Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation.

B1JXI7

Q31UK6

GPPA_SHIBS

pppGpp-5'-phosphohydrolase

Shigella

MGSTSSLYAAIDLGSNSFHMLVVREVAGSIQTLTRIKRKVRLAAGLNSENALSNEAMERGWQCLRLFAERLQDIPPSQIRVVATATLRLAVNAGDFIAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADQRLVVDIGGASTELVTGTGAQTTSLFSLSMGCVTWLERYFADRNLGQENFDAAEKAAREVLRPVADELRYHGWKVCVGASGTVQALQEIMMAQGMDERITLEKLQQLKQRAIHCGRLEELEIDGLTLERALVFPSGLAILIAIFTELNIQCMTLAGGALREGLVYGMLHLAVEQDIRSRTLRNIQRRFMIDIDQAQRVAKVAANFFDQVEKEWHLEAISRDLLISACQLHEIGLSVDFKQAPQHAAYLVRNLDLPGFTPAQKKLLATLLLNQTNPVDLSSLHQQNAVPPRVAEQLCRLLRLAIIFASRRRDDLVPEMTLQANHELLTLTLPQGWLTQHPLGKEIIAQESQWQSYVHWPLEVH

Catalyzes the conversion of pppGpp to ppGpp. Guanosine pentaphosphate (pppGpp) is a cytoplasmic signaling molecule which together with ppGpp controls the 'stringent response', an adaptive process that allows bacteria to respond to amino acid starvation, resulting in the coordinated regulation of numerous cellular activities.

Q31UK6

Q6CMD3

RTC5_KLULA

Restriction of telomere capping protein 5

Kluyveromyces

MGQSTSKEHENARTNESKLKGESLMDFFNDRCLKQLTTAELISFKNNIPEGKELNDYVEVSDISRMYYIPKDSAVMLSVFMNMFHTLANFPLLQDSYEKVTFKTLLKATLLLVKERAIKYTDWKKYNDLKMLFITLSLEKNIKAEPLMDSSALSDCKDWKGVIRSYNGTDFDELKVNANNLLHFLALILALSRCCILNNCKIDNDVLAKSLEDFKHQALNIVRTMNPEIISMSDCLDSSITYTQFSMAVNDVAPNLLNPLKMLMEHVLYMDRDLVDADVLQPISNPTKIVNESELSQLATFLPKEIVFSRFQKLYVGRESGFSMRSFQSKVFKWMAPTILFVEGMRIRDEDDEDGDAYAVKNPRYRNFLQEYGKLKSEDQHLDTLSKKKRKLLFAVCIRDPWKVSNKDLFGDSSTKIIQLHPRQEIFDADPFKTGNVYFNTVGGGIGIGSSQPIIKANGKKYFPGNVSLTIDSSLEFGIFRHLGAGGSFKPGRLISGRGEERNSFEYRFIIQDVEVWGCGGEKELEEQVKQWQWEEAEAKRRQKINLQSMGEDRALLEMAGLVGQHQSGGSI

May be involved in a process influencing telomere capping.

Q6CMD3

Q7CHH5

SCMU_YERPE

*YpCM

Yersinia

MQPTHTLTRLTVIGKLIIASSFFLSLAVQAQQCGQTAPLINERLSYMKDVAGYKAENHLPIEDRIQEEKVINSAMAQAESLGLNGESIKPLMVAQINAAKAIQYRYRADWLSQPEPGWQPKPLDDVRANIGELSTKILEQIAEELKTCKPAEMGDKAHFINTIRQHNLTSADVEAIFSTFNQVKLK

Catalyzes the Claisen rearrangement of chorismate to prephenate. May play some role in the pathogenicity.

Q7CHH5

A6TFK4

SECB_KLEP7

Protein-export protein SecB

Klebsiella

MSEQNSTEMTFQIQRIYTKDISFEAPNAPQVFQKDWQPEVKLDLDTASTQLAEGVYEVVLRVTVTAALGEETAFLCEVQQGGIFSIDGIEGTQMAHCLGAYCPNILFPYARECITSLVSRGTFPQLNLAPVNFDALFMNYLQQQAGEGAEQHQDA

One of the proteins required for the normal export of preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. It also specifically binds to its receptor SecA.

A6TFK4

Q4FQ35

ATPA_PSYA2

F-ATPase subunit alpha

Psychrobacter

MQQLNPAEISNLIKQRIQDLDAGATAKNEGTIVKVSDGIVQIHGLEDAMYGEMIEFEGEVYGMALNLERDSVGAVVLGDFLKLQEGQKAYCTGRILEVPVGPELLGRVVDALGNPIDGKGPINAKMTDKVEKIAPGVIDRQSVDQPVMTGYKSVDTMIPIGRGQRELIIGDRQTGKTAMAIDAIIAQKASGIKCVYVAIGQKRSTIANVVRKLEQTGALEYTTVVVASASEPAALQYIAPYSGCTMGEYFRDRGEDALIVFDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERASRVNAAYVEKFTNGEVVGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLESSLFNSGIRPAVNAGISVSRVGGAAQTKIIKKLSGGIRTALAQYRELAAFAQFASDLDDATREQLDHGERVTELMKQKQYQPMSISEQAAVIYASNEGFLADVPVEKIGSFEEAYLRYMHDEQADLMKEIDDTANYNDDIAGRLKLSLETFKQNHSY

Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.

Q4FQ35

B1VV20

PSD_STRGG

Phosphatidylserine decarboxylase beta chain

Streptomyces

MPDSTSSASRGGVRIARGASPWLLPTVATAALSLARARKSGRWAAVAVPTTALAAGMLWFFRDPEREITDGRVISPADGVVQSIMPWKDGRTRVAIFMSPLNVHVNRAPLAGTVTSVEHIPGGFVPAFNKESENNERVVWHFDTELGDIEMVQIAGAVARRIVPYLPEGTKVEQGERIGLIRFGSRVDIYLPEGIDVAVEVGQATTAGVTRIDRD

Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).

B1VV20

A6BM29

PSBB_GNEPA

Protein CP-47

Gnetum

MGLPWYRVHTVVLNDPGRLIAVHIMHTALVAGWAGSMALYELAVFDPSDPVLDPMWRQGMFILPFMTRLGIKESWGGWSITGESAVNPGLWSYEGVAGAHIVFSGLCFLSAIWHWVYWDLEIFSDPRTGKPSLDLPKIFGIHLFLSGVACFGFGAFHVTGLYGPGIWVSDPFGLTGRIQPVSPAWGAEGFDPFVPGGIASHHIAAGLLGIIAGLFHLSVRPPQRLYRGLRMGNIETVLSSSIAAVFFAAFIVAGTMWYGSATTPIELFGPTRYQWDQGYFQQEIDRRVRAGLTEKLSLSEAWSRIPEKLAFYDYIGNNPAKGGLFRAGAMDNGDGIAVGWLGHPIFRDKEGNELFVRRMPTFFETFPVVLVNKEGIVKADVPFRRSESKYSVEQVGVTVEFYGGELNGVSFSDPAIVKKYARRAQLGEIFELDRATLKSDGVFRSSPRGWFTFGHATFALLFFFGHIWHGARTLFRDIFAGIDPELDAQVEFGAFQKLGDPTTKRQVV

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.

A6BM29

Q3UND0

SKAP2_MOUSE

Src-associated adapter protein with PH and SH3 domains

Mus

MPNPSCTSSPGPLPEEIRNLLADVETFVADTLKGENLSKKAKEKRESLIKKIKDVKSVYLQEFQDKGDAEDGDEYDDPFAGPADTISLASERYDKDDDGPSDGNQFPPIAAQDLPFVIKAGYLEKRRKDHSFLGFEWQKRWCALSKTVFYYYGSDKDKQQKGEFAIDGYDVRMNNTLRKDGKKDCCFEICAPDKRIYQFTAASPKDAEEWVQQLKFILQDLGSDVIPEDDEERGELYDDVDHPAAVSSPQRSQPIDDEIYEELPEEEEDTASVKMDEQGKGSRDSVHHTSGDKSTDYANFYQGLWDCTGALSDELSFKRGDVIYILSKEYNRYGWWVGEMKGAIGLVPKAYLMEMYDI

May be involved in B-cell and macrophage adhesion processes. In B-cells, may act by coupling the B-cell receptor (BCR) to integrin activation. May play a role in src signaling pathway.

Q3UND0

Q9V0N9

PSB2_PYRAB

Proteasome core protein PsmB 2

Pyrococcus

MLQLTEKFKGTTTVGIVCSDGVVLAADRRASLGNIVYAKNVTKIHKIDEHLAIAGAGDVGDILNLVRLLRAEAKLYYAQSGKRMSVKALATLLANMLNGARMLPYLAWFLVGGFDEKPRLYSVDMMGGITEDKYVAAGSGMEFAYSVLDSEYREDLKVREGIKIAVEAINSAIKRDVFSGDGIMVVTITEEGYRELSNSRLKAILRQ

Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.

Q9V0N9

Q6CSC1

IML2_KLULA

Inclusion body clearance protein IML2

Kluyveromyces

MFRVFNALTGAGSPKATELSGEERTKFILQQAHDFEIALQAMDYVLDDNAEVGLKLLADNQATSPGDATVGALAKGVIEFLEATLGFEPEVMKKASTTLAEAEQLSLKSRAKLQKLNIKTSSLYPPGTEYAVTYTESCLLHALLMLFSESMVEGAKALFKLRKAYHMLQDILKEINASEKRKRSSIYLQEINESTASFISSGTCFTSYDIPYKLTPEEEQDKELLDLANKVYSLRRKRLCGAHIGNSPAINRLRDDVGAASLKKGSDEETQEFQLLSDNANINQATMDEFIHSGVNLCFGILQVVLSLIPPAIGAVLSVVGFHGSREEGLRLVWKSTKDRNIHGGIGLLGLLFYYDGPFQFTDIDFDIPAARDDNLPVTEMDRPTLLHPGKILTSALLQARALFPNSALWLLQEARMLSKQGRLKEAVDLLDSIDHNTIEMKQVKALIVFEKATTLVYMHEFERGAETMLIMLSISEWSHALYTYFAGCCYLEMFRKYEMGILNGENAAEKKAYYKERATNLVFESANMVGKKKFMSKILPLDRFLLRKVDQFKKFQNIIKSSDPLDSIGVSPVHELIYFYNGYNRMTMKELNLSLKSLTEYRNPTIDLQNPDQELIKDLLTSLVLRRTGKIEEGCKILDTQVLPQLFTIQNDKVKYIKKTEDPWVYPTAFYERALFSWKLKGMNGLHEAHEWLIRAQNYQDDYELSTRIGMKIKAAKDRVEESI

Inclusion body (IB) resident protein that interacts strongly with lipid droplet (LD) proteins. Involved in LD-mediated IB clearing after protein folding stress, probably by enabling access to the IBs of an LD-stored soluble sterol derivative that acts as chaperone in inclusion clearing.

Q6CSC1

Q2LUK6

RL25_SYNAS

General stress protein CTC

Syntrophus

MEARELKANVRKESGKEQARRMRREGLIPAVLYGPGTDPVSLSVNASDLKTALKGAEENVLIKLIIDDSGRLMEKNSLIRELQIEPLTNNFFHADFYALRMDQESTFDVPIHFEGQPVGIEKGGELQYLKREIKVSCLPSELPDCITVDISRLDVGDAVLIGDLSLSESIRCFDSKDIVLVTIAALHGVNKAEETEEASS

This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance.

Q2LUK6

Q884C9

UVRB_PSESM

Excinuclease ABC subunit B

Pseudomonas

MSEFQLVTRFEPAGDQPEAIRQLVEGIDAGLAHQTLLGVTGSGKTFSIANVISQIKRPTLVLAPNKTLAAQLYGEFKAFFPNNAVEYFVSYYDYYQPEAYVPSSDTFIEKDASINDHIEQMRLSATKALLERKDAIIVTTVSCIYGLGSPETYLRMVLHVDRGDKLDQRALLRRLADLQYTRNDMDFARATFRVRGDVIDIYPAESDLEAIRIELFDDEVESLSAFDPLTGEVIRKLPRFTFYPKSHYVTPRETLVEAMEGIKVELQERLEYLRSQNKLVEAQRLEQRTRFDLEMMLELGYCNGIENYSRYLSGRPSGAPPPTLFDYLPADALLVIDESHVSVPQVGAMYKGDRSRKETLVEYGFRLPSALDNRPMRFDEWEAISPQTIFVSATPGNYEAEHAGRIVEQVVRPTGLVDPQIEIRPALTQVDDLLSEIHKRAALEERVLVTTLTKRMSEDLTDYLSDHGVRVRYLHSDIDTVERVEIIRDLRLGTFDVLVGINLLREGLDMPEVSLVAILDADKEGFLRSDRSLIQTIGRAARNLNGRAILYADRITGSMERAIGETERRREKQIAFNLEHGITPKGVFKDVADIMEGATVPGSRSKKRKGMAKAAEESARYENELRSPSEINKRIRQLEEKMYQLARDLEFEAAAQMRDEIGKLRERLLAV

The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.

Q884C9

C3PFR8

NUCS_CORA7

Endonuclease NucS

Corynebacterium

MRVVIAQCSVDYVGRLDAHLPMADRLILIKADGSVSIHADDRAYKPLNWMTPPCTFEESAIEDIDGEDTGEKLWLVENPKGEQLRITIAQIHQEIDMDLGEDPGLVKDGVEAHLQELLAEHIETLGEKYSLVRREYPTAIGPVDIMAKNSKNEFVAVEVKRRGGIDGVEQLTRYLELLNRDDLLAPVHGVFAAQEIKPQARTLAEDRGIRCVVLDYQELRGIESNELRLF

Cleaves both 3' and 5' ssDNA extremities of branched DNA structures.

C3PFR8

Q1AVW2

RECO_RUBXD

Recombination protein O

Rubrobacter

MALYRSRGIVLRSIRYGEADRILDIYTRDAGLVSCIAKGIRRTRSRFGARLEPFSCVDFMAYRGRTLDTITQAESLRSFRGVRERLDRLQAAAGMAGVLHALSGGTPDRRTFNLLYRALDALEKGEEGFGMIEASFGLKLAVLSGYAPRLDGCAECGGDVPGEGARFAPAAGGFLCRDCRSDAPPDSFPVPPGTLGRLRELAALPLAEAASGRGLEEALRRVVRAHVLAHAPGAASLATPAGTAGGRP

Involved in DNA repair and RecF pathway recombination.

Q1AVW2

Q9HJ56

RL7A_THEAC

Ribosomal protein L8e

Thermoplasma

MEKSYVKFETPEDVSQKALDLVESSYRTGKVKKGTNEVIKSIERGESKLVVIAEDVNPPEVVYYLPSLCEDKKVPYVYVKKKADLGSKVGIASAASVSIVDYGKNEELYKSIVSALEQIKK

Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, the RNA component of RNase P, box H/ACA, box C/D and box C'/D' sRNAs.

Q9HJ56

A4ST47

ENGB_AERS4

Probable GTP-binding protein EngB

Aeromonas

MDTQTLNFNKVHFVTSAPDIRHLPNDGGVEIAFAGRSNAGKSSALNTLTKHKNLARTSKTPGRTQLINLFELEPGKRLVDLPGYGYAQVPLEMKLKWQKSLAEYLQRRESLKGLVILMDIRHPLKDTDMNMLEWSSHRELPVMLLLTKADKLSPGPRNNQVIKVRQAIADLGPQIQVEAFSSLNNIGVEKLAQTLSGWYLAGADEIADNDEQEQVEE

Necessary for normal cell division and for the maintenance of normal septation.

A4ST47

Q6JE37

CITX2_NICBE

Cf-9-interacting thioredoxin 2

Nicotiana

MQAATLSFQPSAPPLQTSAFHFSSKQPNQLKYSLFSYTCPILKRSLLSTQTLSRKSICKPPDVATGKYVREDYLVKKVSAKDIQELIKGERNVPLIIDFYATWCGPCILMAQELEMLAVEYESNALIVKVDTDDEYEFARDMQVRGLPTLYFISPDPNKDAIRTEGLIPIQMMRDIINNDL

Probable thiol-disulfide oxidoreductase that may play a role in proper chloroplast development.

Q6JE37

Q824N2

RS11_CHLCV

30S ribosomal protein S11

Chlamydia

MVKHQTQKKGVKRKQLKNIPSGVVHVKATFNNTIVSITDPAGNTISWASAGKVGYSGSRKSSAFAATMAAQDAAKNAMNSGLKEVEVCLKGTGAGRESAVRALIASGLVVSVIRDETPVPHNGCRPRKRRRV

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.

Q824N2

C5PEI9

PEPA_COCP7

Aspartic protease PEP3

Coccidioides

MQNRPRVFDSAMNLSPNMHFLSLMPGLLLLSLQVHTSPTPLKKTIRSVRIERIRQPNYVPDGPGALKKAYAKFGIIPSGISFDSFEDFTPFSSDNVRNTVSKAMQANETGIVTNTPTNNDVEYLSPVTIGGQKFVMNLDTGSSDTWVFNTQLSEDAKRGHSIFDPAKSKAFSDLEDATFNITYGDASFAFGRVGIDTVDIGGATVQKQAVGLPTDVSGSFILDQASDGLIGLGFDELNTVEPQQQKSFFTNLAANLDEPVLAAQLKKGAPGSYEFGSIDETKFKGDLVTIPVNNSRGFWEVKSTMFKVGKDEQLHRITKGVGSAIADTGTTLMLVNEEIVNSYYDQVDNARSVYAAGGFIFPCNATLPDLYVSLGDTHLARIPGDLMNFSKVGLSTETGEELCFGGVQSNSGSGLQVFGDVLFKAIFVVFDLRGPSLHVAGHA

Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions.

C5PEI9

Q8TX94

LEUD1_METKA

null

Methanopyrus

MRDVIRGRAWVFGDDIDTDQIIPGRYLTTQDPEELAKHVMEGADPEFPEKVREGDVIVAGKNFGCGSSREHAPIALKAAGIACVVTRSFARIFYRNAINLGLPLVVCPGVDDAFEDGQGIEVNLREGYVRNLDTGEELEAKPLPDFMMRILEAGGLVELIKREGPRAFEG

Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.

Q8TX94

B0BUW3

CLPX_RICRO

ATP-dependent Clp protease ATP-binding subunit ClpX

spotted fever group

MVVEADKKALICSFCSKKQHEVKKLIAGPAVFICDECIDLCTDIMKEENKVALKQITSSIPTPQKICGILNDYVVGQDQAKKILAVAVYNHYKRLEYIQSGNNDVELNKSNILLIGPTGSGKTVLAQTLAKILDVPFTMADATSLTEAGYVGEDVENILLRLLIASEFNIAKAQKGIIYIDEVDKIARKSENPSITRDVSGEGVQQALLKIMEGTVASVPPQGGRKHPQQDFVQLDTSNILFICGGAFMGIDSIITSRTNHSSIGFAANVNIDKEKNNSEILKSLEIEDLTKFGLIPEFIGRLPIVTTLDELDKEALITILTKPKNAIVKQYQKQFELDDAELVIDDSALETIAEKALAKKTGARGLRSILEHLLLDSMYKVAELKKQRVTITKEVVNGLVEPIMTSLISTKSNKKQPIIADIPA

ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.

B0BUW3

A0KGL5

RAPA_AERHH

ATP-dependent helicase HepA

Aeromonas

MPFALGQRWISDTETDLGLGTVVAVEGRMVTLLFPATGENRMYAKEEAPVTRVSFNVGDQIASHEDWTMTVEEVQEKDGLLIYVGVRTDNDEPVALKEVFLNNFIKFNKPQDRLFAGQIDRMSRFTLRYEALINQHQRRRNPTRGLAGGRVSLIPHQLYIAHEVGHRYAPRVLLADEVGLGKTIEAGMIIHQQLLSGRAHRVLILLPETLQHQWLVEMLRRFNLHFSLFDEERCIEAFADAENPFETEQLVICSLDFLRKKRRRFEQVLEAEWDLLVVDEAHHLEWSEEAPSRAYEMVEALAEQVPGVLLLTATPDQLGHQSHFARLRLLDPERFYDYDAFLAEEQAYGQVASAAQELLDGETLSDEAKRILASQLEGLDLSDAAARQQAVAKLLDQHGTGRVLFRNSRANIQGFPERHLNVYPMPLPEQYKTAIKVMGMMGGNGGDLQTRALRYLYPEKIFQQFEGDNATWTQFDPRVEWLLELLLSARQQKVLVICSEAATAIALEEALRTREGIRGAVFHEGMSILERDKASAYFAQQEGGAQVLLCSEIGSEGRNFQFASHLVLFDLPLNPDLLEQRIGRLDRIGQQNTVEIHVPYLEGTSQRALQLWYHDGLDAFEQTCPTARPVFEAVRDELFELLAANTGDQAPLDALLVKTRELHEPLKARLEQGRDRLLEIHSSGGAAAQQLVDKLAAEDDDTGMISFALKMFDEIGVNQDDRGENALVLTPGDHMLVSSFPGLPQDGMTITFDRNTALSRDDMALLSWDHPMMRGGIDLILGSEIGATSVALLKNKALPIGSILLELIFVAESAAHPQLYRFMPPTPIRLLMDKNGQNLGEKVAFDAFNRQLTPVNRHLGSKLVTASQPVIHGLIGKGQAIAEELKGGIVDKARAQMAQTLQQDLDRLEALKAVNPNVRDSELDYLRNLQAELHHLIDQTQLKLDAIRFIVVTHN

Transcription regulator that activates transcription by stimulating RNA polymerase (RNAP) recycling in case of stress conditions such as supercoiled DNA or high salt concentrations. Probably acts by releasing the RNAP, when it is trapped or immobilized on tightly supercoiled DNA. Does not activate transcription on linear DNA. Probably not involved in DNA repair.

A0KGL5

B1YHU0

LIPL_EXIS2

Octanoyl-[GcvH]:E2 amidotransferase

Exiguobacterium

MGIELLKQEHYRIFDQTSLGNTFHATQSFAMDDTLCASVATEGAAIRSWVHHETVVLGIQDARLPHLDDGIDVLHAHGFQPVIRNSGGLAVVLDAGVLNISLVLPERGGIDIDSGYEAMLALVRRMFAEETDAINAGEVVGSYCPGSYDLSIAGKKFAGISQRRVRGGVAVQIYLCVNGSGSARAQLVRDFYAAALQGETTKFVYPTVVPETMASLEELLQRPLTVEDCLVRVYRSLMELGATLTPSVLSEVENERFGVNLGRMLDRNEKVLG

Catalyzes the amidotransfer (transamidation) of the octanoyl moiety from octanoyl-GcvH to the lipoyl domain of the E2 subunit of lipoate-dependent enzymes.

B1YHU0

A5UAV8

AROC_HAEIE

5-enolpyruvylshikimate-3-phosphate phospholyase

Haemophilus

MAGNTIGQLFRVTTFGESHGIALGCIVDGVPPNLELSEKDIQPDLDRRKPGTSRYTTPRREDDEVQILSGVFEGKTTGTSIGMIIKNGDQRSQDYGDIKDRFRPGHADFTYQQKYGIRDYRGGGRSSARETAMRVAAGAIAKKYLREHFGIEVRGFLSQIGNIKIAPQKVGQIDWEKVNSNPFFCPDESAVEKFDELIRELKKEGDSIGAKLTVIAENVPVGLGEPVFDRLDADLAHALMGINAVKGVEIGDGFAVVKQRGSEHRDEMTPNGFESNHAGGILGGISSGQPIIATIALKPTSSITIPGRSINLNGKPVEVVTKGRHDPCVGIRAVPIAEAMVAIVLLDHLLRFKAQCK

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.

A5UAV8

P70232

NCHL1_MOUSE

Processed neural cell adhesion molecule L1-like protein

Mus

MMELPLCGRGLILSLIFLLLKLSAAEIPLSVQQVPTIVKQSYVQVAFPFDEYFQIECEAKGNPEPIFSWTKDDKPFDLSDPRIIAANNSGTFKIPNEGHISHFQGKYRCFASNRLGTAVSEEIEFIVPGVPKFPKEKIEPIDVEEGDSIVLPCNPPKGLPPLHIYWMNIELEHIEQDERVYMSQRGDLYFANVEENDSRNDYCCFAAFPKLRTIVQKMPMKLTVNSSNSIKQRKPKLLLPPAQMGSLSAKTVLKGDTLLLECFAEGLPTPHIQWSKPGSELPEGRATIEVHEKTLKIENISYQDRGNYRCTANNLLGKASHDFHVTVEEPPRWKKKPQSAVYSTGSSGILLCEAEGEPQPTIKWRLNGLPIEKHPFPGDFMFPREISFTNLLPNHTGVYQCEASNIHGTILANANIDVIDVIPLIKTKNEENYATVVGYSAFLHCEYFASPKATVVWEVADETHPLEGDRYHTHENGTLEIYRTTEEDAGSYSCWVDNAMGKAVITANLDIRNATKLRVSPKNPRIPKSHVLELYCESQCDSHLKHSLKLSWSKDGEAFEMNGTEDGRIVIDGAYLTISNITAEDQGVYSCSAQTSLDSTSEKTQVTVLGVPDPPGNLHLSERQNRSVRLSWEAGDDHNSKISEYIVEFEGNREEPGKWEELTRVQGEETDVVLSLAPYVRYQFRVTAVNEVGRSHASLPSDHHETPPAAPDKNPQNIRVQASQPKEMIIKWEPLKSMEQNGPGLEYKVSWKPQGAPEEWEEEIVTNHTLRVMTPTVYAPYDVKVQAINQLGSSPDPQPVTLYSGEDYPSTAPVIQRVDVMNSTLVKVTWSSIPKETVHGLLRGYQINWWKTKSLLDGRTHPKEVNILRFSGQRNSGMVPSLDPFSEFHLTVLAYNSKGAGPESEPYIFQTPEGVPEQPSFLKVIKVDKDTATLSWGLPKKLNGNLTGYLLQYQIINDTYELGELNEINVTTPSKSSWHLSNLNSTTKYKFYLRACTSRGCGKPISEEGATLGEGSKGIRKITEGVNVTQKIHPVEVLVPGAEHIVHLMTKNWGDNDSIFQDVIETRGREYAGLYDDISTQGWFIGLMCAIALLTLILLTICFVKRNRGGKYSVKEKEDLHPDPEVQSAKDETFGEYSDSDEKPLKGSLRSLNRNMQPTESADSLVEYGEGDQSIFNEDGSFIGAYTGAKEKGSVESNGSSTATFPLRA

Extracellular matrix and cell adhesion protein that plays a role in nervous system development and in synaptic plasticity. Both soluble and membranous forms promote neurite outgrowth of cerebellar and hippocampal neurons and suppress neuronal cell death. Plays a role in neuronal positioning of pyramidal neurons as well as in regulation of both the number of interneurons and the efficacy of GABAergic synapses. May play a role in regulating cell migration in nerve regeneration and cortical development. Potentiates integrin-dependent cell migration towards extracellular matrix proteins. Recruits ANK3 to the plasma membrane.

P70232

Q0I4M4

LPXA_HAES1

Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase

Histophilus

MIHSTAKIHPSSIIEEGAKIGENVVIGPFCIVGSDVQIGKGTTLHSHVVVKGVTTIGEDNQIFQFASIGEVNQDLKYQGEPTKTIIGHRNRIRESVTIHRGTVQGGGVTRIGDDNLLMINAHIAHDCQIGNRCILANNATLAGHVELGDFVIVGGMSAIHQFVIVGAHVMLGGGSMVSQDVPPYVMAQGNHARPFGVNIEGLKRRGFDKPTLHAIRNVYKLIYRSGKTLEEVIPEIENYAQTESAVSFFLDFFNRSTRGIIR

Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.

Q0I4M4

P32518

DUT_SOLLC

dUTP pyrophosphatase

Solanum subgen. Lycopersicon

MAENQINSPEITEPSPKVQKLDHPENGNVPFFRVKKLSENAVLPSRASSLAAGYDLSSAAETKVPARGKALVPTDLSIAVPQGTYARIAPRSGLAWKYSIDVGAGVIDADYRGPVGVVLFNHSEVDFEVKVGDRIAQLIVQKIVTPEVEQVDDLDSTVRGSGGFGSTGV

This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. It may have as well a metabolic role in merismatic cells.

P32518

B5XY03

G6PI_KLEP3

Phosphohexose isomerase

Klebsiella

MKNINPTQTSAWQALQKHFDEMKDVTISELFAKDSDRFSKFSATFDDLMLVDFSKNRITEETLAKLQDLAKETDLAGAIKSMFSGEKINRTEDRAVLHVALRNRSNTPIVVDGKDVMPEVNAVLEKMKTFSEAIISGSWKGYTGKPITDVVNIGIGGSDLGPFMVTEALRPYKNHLNMHFVSNVDGTHIAEVLKNVNPETTLFLVASKTFTTQETMTNAHSARDWFLATAGDDKHVAKHFAALSTNAKAVGEFGIDTANMFEFWDWVGGRYSLWSAIGLSIILSVGFDNFVELLSGAHAMDKHFSTTPAEKNLPVLLALIGIWYNNFFGAETEAILPYDQYMHRFAAYFQQGNMESNGKYVDRNGHAVDYQTGPIIWGEPGTNGQHAFYQLIHQGTKMVPCDFIAPAITHNPLSDHHPKLLSNFFAQTEALAFGKSREVVEQEYRDQGKDPATLEHVVPFKVFEGNRPTNSILLREITPFSLGALIALYEHKIFTQGAILNIFTFDQWGVELGKQLANRILPELKDGSEVSSHDSSTNGLINRYKAWRA

Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.

B5XY03

A1TAQ3

ARC_MYCVP

Mycobacterial proteasome ATPase

Mycolicibacterium

MSESERSEASEVFGTSPDSRLSSEDAAELEQLRREAAILREQLEDAGGLATSARAARDVHQLEARIDSLAARNAKLMDTLKEARQQLLALREEVDRLGQPPSGYGVLLSVQDDETVDVFTSGRKMRLTCSPNIETKELKKGQTVRLNEALTVVEAGHFESVGEISTLREILSDGHRALVVGHADEERIVWLAEPLVAAEHLPEGSYADEDDLTDDRPRKLRPGDSLLVDTKAGYAFERIPKAEVEDLVLEEVPDVSYNDIGGLGRQIEQIRDAVELPFLHKELYREYSLRPPKGVLLYGPPGCGKTLIAKAVANSLAKKMAEVRGDDAREAKSYFLNIKGPELLNKFVGETERHIRLIFQRAREKASEGTPVIVFFDEMDSIFRTRGTGVSSDVETTVVPQLLSEIDGVEGLENVIVIGASNREDMIDPAILRPGRLDVKIKIERPDAESAQDIFSKYLTEELPIHDDDLAEFSGDRSLTIKAMIEKVVDRMYAEIDDNRFLEVTYANGDKEVMYFKDFNSGAMIQNVVDRAKKNAIKAVLETGQRGLRIQHLLDSIIDEFAENEDLPNTTNPDDWARISGKKGERIVYIRTLVTGKSSSASRAIDTESNLGQYL

ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis.

A1TAQ3

Q12ZV0

RL4_METBU

50S ribosomal protein L4

Methanococcoides

MTTANIIDLSGNSKGEIALPEVFSEIFRPDLIKKAVLSAQANRLQPYGTKLYAGMQTSAHSWGSGRGVAQVPRISNGSRVARIPQAVGGRRAHPPKTETDRTEKINKKEKRLAVRSAIAATIDADLVKARGHKFTAEVPFVADDAIEGLVKIKEVISFLQAAGLYDDIIRAKEGKHIRAGKGKRRGRKYKNRKSVLIVTGEESLLSKAANNLPGVDVATVTALNAELLAPGTHAGRLTVWTQSAITNMEGMFL

Forms part of the polypeptide exit tunnel.

Q12ZV0

Q80VM4

ZN579_MOUSE

Zinc finger protein 579

Mus

MDPQPPPPAQGSPPHRDRGRGRGRGRGRGRGRGRGRGGAGAPRAPLPCPTCGRLFRFPYYLSRHRLSHSGLRPHACPLCPKAFRRPAHLSRHLRGHGPQPPLRCAACPRTFPEPAQLRRHLAQEHAGSEVDLSTQRAVKEEPEASWGPQDEGVEQPATVVVAGAEEEATTQWPAGDSAPAAVPTSTDPRESEAKEAEAGAAELRAELALAAGRQEEKQVLLQADWTLLCLRCREAFATKGELKAHPCLRPEGEQEGEGGPPPRPKRHQCSICLKAFARPWSLSRHRLVHSTDRPFVCPDCGLAFRLASYLRQHRRVHGPLSLLAPLPGAGKKDDKASGGRNSGKGPEGGEGAECGGASEGGEGGHNGGDATPARPPAGEPRFWCPECGKGFRRRAHLRQHGVTHSGARPFQCVRCQREFKRLADLARHAQVHAGGPAPHPCPRCPRRFSRAYSLLRHQRCHRAELERAELERAAALQELQTQASQSPQPPQPLKQEAEGLPLPIAHIKEEPPSPGTPPQSPPAPPVFLSASCFDSQDHSAFEMEDEEMDSKAHLCGLGGLAS

May be involved in transcriptional regulation.

Q80VM4

B2VF78

SLMA_ERWT9

Nucleoid occlusion factor SlmA

Erwinia

MVEKKSAKRNRREEILQALAQMLESSDGSQRITTAKLAANVGVSEAALYRHFPSKTKMFDSLIEFIEDSLITRINLILKDEKETMPRLRLITQLILGFGELNPGLTRILTGHALMFEQDRLQGRINQLFERIELQIRQVMRERKMREGEGFATDEALLATQLLAFCEGLLSRFVRSEFRYRPTVDFDARWPLMAAQLI

Required for nucleoid occlusion (NO) phenomenon, which prevents Z-ring formation and cell division over the nucleoid. Acts as a DNA-associated cell division inhibitor that binds simultaneously chromosomal DNA and FtsZ, and disrupts the assembly of FtsZ polymers. SlmA-DNA-binding sequences (SBS) are dispersed on non-Ter regions of the chromosome, preventing FtsZ polymerization at these regions.

B2VF78

Q0SPQ5

RSMG_CLOPS

16S rRNA 7-methylguanosine methyltransferase

Clostridium

MQYFDLMKKACDSVGMEFNEDKYQKFMLYKDLLKEWNEKINLTAITEDEEIVKKHFIDCIKAFKADEFKKAKTVIDVGTGAGFPGLPIAIMREDVEVTLLDSLNKRINFLNEVVNKLALKNVETIHSRAEDGARKKELRENFDIATSRAVANMCVLSEFCIPYVKVNGNFIALKGPNITEELNDSKNAIGTLGGKLKGITEVEIEGTDLNHNLVIVDKIKSTPKTFPRKAGNVTKKPLK

Specifically methylates the N7 position of a guanine in 16S rRNA.

Q0SPQ5

B2KA77

KDPA_YERPB

Potassium-translocating ATPase A chain

Yersinia

MVASGFLLIASFMVVLFVLSRPLGGFLARLIEGEPFSALQKVEAGLWRCSGVKNAEMNGWQYALAILCFNLLGIVLLFVLLMTQGSLPLNPEHLPGMSWHLALNTAVSFVTNTNWQAYSGENTLSYLSQMAGLTVQNFLSAATGIAVAFALIRAFARHSATTLGNAWVDLVRITLYVLLPIALIIALIFVSQGVLQNLDGYLHITTLEGVQQTLPMGPVASQEAIKVLGTNGGGFFGANSAHPFENPTAFSNFVQMLAIFLIPCALCFAFGQVVGDNRQGHALIWAMSLIFIVAVVVVMYAELAGNPHLSPLGADSNSNMEGKESRFGILATSLYAVVTTAASCGAVNAMHDSFTALGGMIPLWLMQIGEVVFGGVGSGLYGMLLFVLLTVFIAGLMIGRTPEYLGKKIDVFDMKMTALAILVTPTIVLLGTALALCTEAGRAGILNPGAHGFSEVLYAFSSAANNNGSAFAGLSVNTPFYNLLLAAAMFIGRFGVILPVLAIASSLVAKKRQPAGNGTLPTGGPLFIGLLIGTVLLVGALTFIPALALGPVAEHLQVWLAH

Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the periplasmic potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel.

B2KA77

Q5ZTZ8

KGUA_LEGPH

GMP kinase

Legionella

MVSDNSGNLYIVAAPSGGGKTSLVKKLIEMVGEIEVSVSHTTRPMRPGEKEGVDYFFIDEKQFISMVNEGAFIEHAKVFNHWYGTSVAQINKRLQFGIDVVLDIDWQGAEQIRHAYPDAVSVFIIPPSLDALKERLMNRRQDKDHVISERMTKAQDELGHYPEFDYLIVNDDFEKAAMELQSIVIANRLRIEKQVNKQAKLLSFLLSSQ

Essential for recycling GMP and indirectly, cGMP.

Q5ZTZ8

B5Y273

LPLA_KLEP3

Lipoate--protein ligase

Klebsiella

MSTLRLLLSDSYDPWFNLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDHVRLARRSSGGGAVFHDLGNTCFTFMAGKPEYDKTVSTAIVLAALNSLGVTAEASGRNDLVVKTDSGDRKVSGSAYRETIDRGFHHGTLLLNADLSRLANYLNPDQKKLQAKGITSVRGRVANLVELLPGITHQHICEAIQEAFFSHYGERVDAEVISPDNTPDLPNFAETFARQSSWEWNFGQAPAFSHLLDERFRWGGVELHFDVEKGHITRTQAFTDSLNPAPLEALAARLVGCQYRAEVLLQQCEALVGDFPEQEAELKELSAWMAGAVR

Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes.

B5Y273

A1SSY6

NQRD_PSYIN

NQR-1 subunit D

Psychromonas

MAKSNEIKAVLTSPIISNNPITLQILGICSALAVTSKLENAVVMTVAVLFVTAFSNFFISTIRNYIPNSVRIIVQMAIIASLVIVVDQFLRAYAFSISKQLSVYVGLIITNCIVMGRAEAFAMKNKPIASFMDGVGNGLGYGVILILVGAFRELFGSGSLYGFVILPLTSNGGWYQSNGLLLLAPSAFFIVGGIIWAVRTMRPDQVEPKE

NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.

A1SSY6

P04113

MLRA_MIZYE

Myosin regulatory light chain A, smooth adductor muscle

Mizuhopecten

ADKERAQRATSNVFARLPQKLMQEMKEAFTMIDQNRDGFIDINDLKEMFSSLGRTPDDKELTAMLKEAPGPLNFTMFLSIFSDKLSGTDTEETLRNAFAMFDELDTKKLNIEYIKDLLENMGDNFTKDEMRMTFKEAPVTGGKFDYVKFTAMIKGSGEEEA

In molluscan muscle, calcium regulation is associated with myosin rather than with actin. Muscle myosin contains two types of light chains: the catalytic light chain, essential for ATPase activity, and the regulatory light chain, a calcium-binding protein responsible for Ca(2+) dependent binding and Ca(2+) dependent Mg-ATPase activity.

P04113

Q988C8

FHMCD_RHILO

5-formyl-3-hydroxy-2-methylpyridine 4-carboxylate 5-dehydrogenase

Mesorhizobium

MIRNIAIIGLGTMGPGMAARLARGGLQVVAYDVAPAAIERARSMLSVAETVLDALGIALPSAGVGTVRFTDDIGDAVSGADLVIENVPENISIKADVYRTIDGLIGQDTIVASDTSGIPITKLQAHISYPERMVGMHWSNPPHIIPMIEVIAGEKTAPQTVATIRDLIRSIGLLPVVVKKDVPGFVENRVLYALLREAVDLVERGVIDPEDLDTCVSWGIGYKIAVIGPMALLDMAGLDIYKSVSSFLNADLSNRDDVAPMVLEKTSASKFGIKSGEGMFCYTPEQTKALQAERARKLVAVRRILEGRE

Involved in the degradation of pyridoxine (vitamin B(6)). Catalyzes the oxidation of 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate (FHMPC) by NAD(+) to 5-hydroxy-6-methylpyridine-3,4-dicarboxylate (HMPDC) . Can also catalyze the reduction of FHMPC by NADH to 4-pyridoxic acid .

Q988C8

Q46I27

CBID_PROMT

Cobalt-precorrin-6A synthase

Prochlorococcus

MNQFTLPVWVVAAAKSATNILIGNKFRDKERIDLPNNEKSISVPISSSALLDNGKRSLAVSHCQSGLPLDITRGVEIWAYIQLSKGGFQSKGKVRNGFPDWLDFHAGYGVGKFQSSGQPCISQFARDLLCINLYPLLPKGSSIKVEIILPEGKDRASKTSNEAFGVVDGLSLIGTQAEVQISASPDQLKNTKELLHHKCSEAKFDGCLTFVIGENGMDLAMKYGLPANQIIKTGNWLGPLLVAAAENGVKKLLLFGYHGKLIKLSGGVFHTHHHLADGRIEILTSIAFREGISFDLIELISKSTSVENALLTLEVSNPEAVSLIWSRMAKEIEIKSRSYVNRYLSSSMEIGSVLFDRKRQMRWAGLEGLKQINSLGLILKR

Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.

Q46I27

Q9NQG5

RPR1B_HUMAN

Cell cycle-related and expression-elevated protein in tumor

Homo

MSSFSESALEKKLSELSNSQQSVQTLSLWLIHHRKHAGPIVSVWHRELRKAKSNRKLTFLYLANDVIQNSKRKGPEFTREFESVLVDAFSHVAREADEGCKKPLERLLNIWQERSVYGGEFIQQLKLSMEDSKSPPPKATEEKKSLKRTFQQIQEEEDDDYPGSYSPQDPSAGPLLTEELIKALQDLENAASGDATVRQKIASLPQEVQDVSLLEKITDKEAAERLSKTVDEACLLLAEYNGRLAAELEDRRQLARMLVEYTQNQKDVLSEKEKKLEEYKQKLARVTQVRKELKSHIQSLPDLSLLPNVTGGLAPLPSAGDLFSTD

Interacts with phosphorylated C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and participates in dephosphorylation of the CTD by RPAP2. Transcriptional regulator which enhances expression of CCND1. Promotes binding of RNA polymerase II to the CCDN1 promoter and to the termination region before the poly-A site but decreases its binding after the poly-A site. Prevents RNA polymerase II from reading through the 3' end termination site and may allow it to be recruited back to the promoter through promotion of the formation of a chromatin loop. Also enhances the transcription of a number of other cell cycle-related genes including CDK2, CDK4, CDK6 and cyclin-E but not CDKN1A, CDKN1B or cyclin-A. Promotes cell proliferation.

Q9NQG5

Q117R7

METE_TRIEI

Methionine synthase, vitamin-B12 independent isozyme

Trichodesmium

MSISTSTLGYPRIGKNREVKKALESFWQQKISADELLKIVREIEEASWQTQTKAGIERIGIGDATLYDQILDWSFRFGIIPKRFQQFQNLECYFAMARGKDGILALEMTKWFDTNYHYLVPEITPDITPKADFSDFLETVKRAKKIIGKSAVPIIISPITFIRLSRLESVEFDNILAQLLPLYSDLLTKLKKLGISEIQLHEPALVFGDSSNLKKQFEMAYAELAKVGLNIHLVTYFDDLGETYPWVMKLPVTSISLDLTRGQNLELIKSYGFPADKTLGAGVVDARNIWRIRTQEVTSLLEELKGIIPNISVQPSASLQFVPYDVRREVKLPEALRNVLSFAEQKLEETVLLSKALTGKSNKSEIENIEIYWQEFYKFSPANEKVKSQIKALKETDFRRSMSYLERLDNQIKLPAFPTTTIGSFPQTKQVRKLRARYKKGELTQAEYLAQIDANIAYCIGLQEGMGMDVLVHGEFERSDMVEYFGEQLDGYTFTTHGWVQSYGSRYVRPPIIFGDIYRPHAMTIREFEVAQSLTEKPVKGMLTGPVTMLNWSYPRTDISRQEQAFQLALAIREELKDLEKAGAAFIQVDEPAMREGLPLKQQRWHEYLNWAVDAFRLSTAIARPETQVHTHMCYSEFGDIMESIKQLDADVISIEDSRSNNETLMQLTDADYPAQVGPGVYDVHSPSIPTTEYLRESLYKCIQYLPVTQIWVNPDCGLKTRRWEEAIPATRNMVQAAISLRQE

Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.

Q117R7

C5D9H6

MUTL_GEOSW

DNA mismatch repair protein MutL

unclassified Geobacillus

MGKIRKLDDQLSNKIAAGEVVERPASVVKELVENAVDANSTIIEIELEEAGLTKIRVIDNGDGMEEDDCLVAFERHATSKIKDEHDLFRIRTLGFRGEALPSIASVSEVEMKTSTGDGPGTKVVLKGGKLVVHERTTSRKGTDITVSNLFFNTPARLKYMKTIHTELGHVTDVVNRLAMAHPDISFRLRHHGKQLLYTSGNGDVRHVLAAIYGMDVAKKMIPIQAESLDFTVQGYISLPEVTRASRNYISTIVNGRYVRNIPLAKAIEAGYHTLLPIGRYPIVFLSIAMDPILVDVNVHPAKLEVRFSKEAELNELVTQAIRQALQARTLIPEMMIKQKETPKPKAEQTAWTFEHVVKEPFVSPLVHVDEPKQVDEPKQSSPVQEPKEEIPSFLPTVESKQNDVDDELVEMDEQTESSDEQEHVNDRLPPLYPIGQMHGTYILAQNERGLYIIDQHAAQERIKYEYFREKVGEVINEVQELLVPLTFHYPTDEYVLIDAHREELAKCGVFLEPFGHNTFIVRSHPSWFPKGEEAEIIEEMIQQVIDMKKVDMKQLREKAAILMSCKRSIKANEYLRDDEIFALLESLRKTTDPFTCPHGRPIIIHFSTYELEKMFKRVM

This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex.

C5D9H6

Q96GX2

A7L3B_HUMAN

Ataxin-7-like protein 3B

Homo

MEEISLANLDTNKLEAIAQEIYVDLIEDSCLGFCFEVHRAVKCGYFYLEFAETGSVKDFGIQPVEDKGACRLPLCSLPGEPGNGPDQQLQRSPPEFQ

By binding to ENY2, interferes with the nuclear functions of the deubiquitinase (DUB) module of the SAGA complex which consists of ENY2, ATXN7, ATXN7L3 and the histone deubiquitinating component USP22. Affects USP22 DUB activity toward histones indirectly by changing the subcellular distribution of ENY2 and altering ENY2 availability for ATXN7L3 interaction. Regulates H2B monoubiquitination (H2Bub1) levels through cytoplasmic sequestration of ENY2 resulting in loss of nuclear ENY2-ATXN7L3 association which destabilizes ATXN7L3. Affects protein expression levels of ENY2 and ATXN7L3.

Q96GX2

O74870

MUG73_SCHPO

Meiotically up-regulated gene 73 protein

Schizosaccharomyces

MNAKLSSSGMVLKELPEVALQKISSNYYWAVFAVFLLCAIVFPLVSIFSLPQKQTYHRFFSILSLVSCLAYFTMACNYGLKNVFSSASFFREVSVRMVYYVRYIQWLINFPLIIVMLHWTVGVSILEIAYVVCYVLFAIVCLLAAALTSSPYKWAYYGFSFVGYFIALAHSVVLHKKYASRLETSARLGFLWSIVYLHVIWFLYYACWILSEGLNVISPIGEAIFYSILDLFEFGFFGAAFSWMLDLVGIENFKSPQSIPLGACSPADDKFSMCPDMEAQNQADDLAVETRIQISNLPSSPTKNNC

Has a role in meiosis.

O74870

Q2SXD1

LOLD_BURTA

Lipoprotein-releasing system ATP-binding protein LolD

pseudomallei group

MNDRVFEQTMNQNHQGGAARECVLEAHGITKTFMQGGFNVQVLDNAQVSVRRGEKLAIVGASGSGKSTLLHVLGGLDEPSAGQVSLLGKPFTQLAERERNDLRNRALGFVYQFHHLLPEFTALDNVAMPLRIRRMSAEEARHHAREMLEQVGLGARAKHRPGELSGGERQRVAIARALVTKPACVLADEPTGNLDGSTADHVFHLMLELSRTLDTSFVIVTHDPDLAARCDRILRLRDGVLHEEPAVPV

Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner.

Q2SXD1

Q3B5P7

PDXJ_CHLL3

Pyridoxine 5'-phosphate synthase

Pelodictyon

MRLAVNIDHIATLRNARNEGEPDPVAAALLAEESGAAGIVCHLREDRRHIRDNDLKGLRRSVKTKLDLEMAMTEEMQRIAIETVPELITLVPEKREELTTEGGFDIERHFKRLALFIEPIRAAGIEVSLFIEPDSRSIDLAAEAGSDLVELHTGSYALKSGEEQTAEFERIRHAAKYAVDRGLKVVAGHGLNYRNIQPFRQIPEIEEVSIGHALIARAAFVGIPEAVREMLDLIG

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.

Q3B5P7

Q9F1Y5

GPPMT_STRCO

Geranyl diphosphate 2-C-methyltransferase

Streptomyces albidoflavus group

MTTETTTATATAKIPAPATPYQEDIARYWNNEARPVNLRLGDVDGLYHHHYGIGPVDRAALGDPEHSEYEKKVIAELHRLESAQAEFLMDHLGQAGPDDTLVDAGCGRGGSMVMAHRRFGSRVEGVTLSAAQADFGNRRARELRIDDHVRSRVCNMLDTPFDKGAVTASWNNESTMYVDLHDLFSEHSRFLKVGGRYVTITGCWNPRYGQPSKWVSQINAHFECNIHSRREYLRAMADNRLVPHTIVDLTPDTLPYWELRATSSLVTGIEKAFIESYRDGSFQYVLIAADRV

Catalyzes the SAM-dependent methylation of geranyl diphosphate (GPP) to yield (E)-2-methylgeranyl diphosphate (2-MeGPP).

Q9F1Y5

Q7VP34

SYI_HAEDU

Isoleucyl-tRNA synthetase

Haemophilus

MTDYKDTLNLPETGFPMRGDLAKREPAMLKNWYDKNLYQQIRQTSKGKKTFILHDGPPYANGNLHLGHAVNKILKDIIMKSKTASGFDTPYVPGWDCHGLPIELKVESIVGKPNEKISAAEFRQACREYANEQVDRQKADFIRMGVLGDWDNPYLTMNFNTEASIIRTLAKVIANGHLYKGSKPVHWCLDCGSSLAEAEVEYEDKVSPSIYVRFKACDETAIETLFNAKGNGPISAIIWTTTPWTMPSNRAIAIHPELEYALVQLADERVILATELVESVAKAIEAESFDILATVKGETLQLLRFHHPFYAFDVPFIFGDHVTTEGGTGLVHTAPDHGTDDFIIARKNNIEMAGLIGNDGKFKSDVEFFAGLAVFESNEKVIEKLKETGALLKLARIKHSYPHCWRHKTPIIFRATPQWFIGMEKQGLRAQALAEIKTVRWIPNWGEARIDTMVANRPDWCISRQRTWGVPMAMFVHNETEELHPRTLDILELVAQRVEQQGIQAWWDLDPTEVLGEDAQHYHKVPDTLDVWFDSGSTYASVVEQRPEFNGQTADMYLEGSDQHRGWFMSSLMLASATNGKAPYQQVLTHGFVVDEKGRKMSKSIGNVIVPSEVWNKNGADILRLWVASTDYTAEMKVSHGILNSAGDAYRRIRNTARFLLSNLNGFIPARDEVKPNEMIALDRWAVSCALEAQNDIIEAYEHYQFHTVVQRLMRFCSIEMGSFYLDIIKDRQYTTKADSLARRSCQTALWHIAEALVRWIAPILSFTADEIWSHLPTVEGRSEFVFTEQFYSQLFTLNCHDKLDDNYWQQLINIRAEVNRVLEQARNEKTIGAGLEAKVTVYANDEMLPLLHQLGNELRFVLITSQAIVKPLSEADVAEGELAGLAVKVERAEGEKCPRCWHFATDIGTHAEHNAICGRCVENVAGKGEVRRFA

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).

Q7VP34

A4SFY3

GLYA_CHLPM

Serine hydroxymethyltransferase

Chlorobium

MDTDILKMQDREVFEAIALETGRQMETLELIASENFTSRAVMQACGSVMTNKYAEGYPGKRYYGGCEFVDIAENLARDRAKKLFGCEYVNVQPHSGSSANMAVLFSVLKPGDCIMGLDLSHGGHLTHGSSVNFSGQMYKAHAYGVDGETGIIDMNQVEKMALEVRPRLIICGASAYSQGFDFKAFREIADKVGAFLMADIAHPAGLIVSGLLSDPMPHCHFVTTTTHKTLRGPRGGMIMMGKDFENPMGITIKTKNGQRVKMMSEVMDAEVMPGIQGGPLMHIIAGKAVAFGEALRPEFRQYAMQVRSNAAAMSERFLSLGYNIVSGGTKNHLMLLDLRNKDITGKVVENTLHEAGITVNKNMVPFDDKSPFVTSGIRIGTAAMTTRGMNEDDSRLIAELIDRVILSAASPESSSVCRSVKEEIRSLCLRNPLEGYGVTPS

Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.

A4SFY3

A8XDI8

MTNA_CAEBR

Translation initiation factor eIF-2B subunit alpha/beta/delta-like protein

Caenorhabditis

MAPKINKIVNGPIPDSFLADETKRLDSLKFDGQRLEVLDQLLLPHEFKYIPVNDVSDAFNVIKSMQVRGAPLIAVVGSLGLLLEFNKNSELNIETIREKIEYLITSRPTAVDLRNSVTGLIPILETEGITDDEKLAKCQEYLLNVYTAEKLQNRILLWNAYQELLTAFPGKEKFTVMTICNTGSLATVSWGTALGVIRALHSENRLNLAYVLETRPYNQGIRLTATELLHGQVPFKLITDSMAAWAMKNHQLDCVLVGADNVARNGDTANKIGTYMLAVLCKHHNINFYPVVPFTTINKNISSGEEIKIEERAASELLRVNGVLVGNSECPVWNPAFDVTPAHLITKILTDFGNWSPAALEEQIPR

Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).

A8XDI8

P0DN06

VKT1A_ANEVI

AsKC1a

Anemonia

MVFLLCFFLVADVSYGINKDCLLPMDVGRCRASHPRYYYNSSSKRCEKFIYGGCRGNANNFHTLEECEKVCGVRSRDSPKEN

Dual-function toxin that inhibits both the serine protease trypsin (Kd=30 nM) and voltage-gated potassium channels Kv1.2/KCNA2 (IC(50)=2800 nM).

P0DN06

P47116

PTK2_YEAST

Serine/threonine-protein kinase PTK2/STK2

Saccharomyces

MAGNGKDKEVDKSPSVSTLKLLGKRLFNSSSHTDNSSLLLSAEQLGNGRSLRKRPTSPSISGSGSGGNSPSSSAGARQRSASLHRRKNNASVGFSNGSVSSHKSSVALQDLIKHNNNPYLNSPSDILGTGTGIASTRDRDRAVLDREKEKERARNKERNTHHAGLPQRSNSMASHHFPNENIVYNPYGISPNHARPDTAFADTLNTNKENDLSFYMHDGNSKIRMLPLPIANPNDFLPEDMKQYSVHLTDNFVFDTDNKPIGSGGSSEVRKVKSSYRQKDVYALKKLNMIYHESPEKFYKRCSKEFIIAKHLSHNVHITNTFYLLKVPTTTYTTRGWGFIMELGVKDLFQLMERTGWKNVPFNEKYCLFKQVAQGIKFCHDNGIAHRDLKPENVLISKEGICKLTDFGISDWYHVIPHDYTSPVKTCQGMIGSPPYTPPEVMYFDAKKHYPEKFQKPYNPLAMDSYALGIMLITMINNIIPFIDSCNTDARFREFEVSYDNFINHQNPHFRDKGCHKPGPGSEYSLARNFKNTDATRIAWRLADPNPATRYTMDDLFNDPFFQQIETCVEPNDDDLVRVPELRKSTSTNDFSENSLDAPHDQEVIHTSNPFLKKETLTSKPRSMLEIAESPSLKQKSKVKDSAKTKTHDVGDEGGNESTKPKQQDKKENLKKDEVKNGDKDKVIEEATTTNVDSILEKPTPTSTKVEDNLSEDDSTMKELKSMLNSTPTTPTHNGPTPLPAKAGTQLDKRMSDLSLKSETPASTKNFSAPNVSSSSNSLRSLGSPSVSSSKKKKVIHHHLDITNSVTNMSSVSAFISR

Essential determinant for high-affinity spermidine transport. Required for the activation of the plasma membrane proton pump PMA1 via phosphorylation of 'Ser-899'.

P47116

P28604

NODQ_AZOBR

ATP adenosine-5'-phosphosulfate 3'-phosphotransferase

Azospirillum

METGTGRGLLRFLTCGSVDDGKSTLIGRLLHDAGLISDDQLEQARRDSRGRAEEDGGIDFSLLVDGLEAEREQSITIDVAYRYFATDRRSFIVADAPGHEQYTRNMATAASGASLAVLLVDARKGLLTQTRRHAIVASLMGIRHVVLAVNKMDLVEDGETVFAAIRQAFTVFSAPLGFRSVTAIPLSARHGDNVVHRSAAMPWHHGPTLLGHLETAAAEDDPTEDGPLRFLVEWVNRPNLDFRGLSGTLLSGSLETGGAVTVWPSGRSARIARIVTFDGDVTQARAGDAVTVTLDAAVDAGRGDLLSGPDGAPEVADQFAAHLLWMAEEPLIPGRSYLLRAGARWVPATVTALRHAVNVETLEHGAASVLGLNAVGLCNLSTAAPLAFDPYEASRHTGSFILVDRFSNRTVGAGMIRHPLRRAANLHRQELAVSTVERAALKRQRPAVLWFTGLSGSGKSTIANRVERRLHTLGHHTMMLDGDNVRLGLNRDLGFTDADRVENIRRVGEVAKLMTEAGLIVLCAFIAPFRAEREAVRALLPDGAFLEVFVDTPLDECMRRDPKGLYAKARAGTLRNFTGVDSPYEAPDAPELRLDTTAEDADALAERVVELLHRKGIAEA

APS kinase catalyzes the synthesis of activated sulfate.

P28604

A7MLX1

NRDR_CROS8

Transcriptional repressor NrdR

Cronobacter

MHCPFCFAVDTKVIDSRLVGEGSSVRRRRQCLVCNERFTTFEVAELVMPRVVKSNDVREPFNEDKLRSGMQKALEKRPVSSDDVEMAINHIKSHLRATGEREVPSKLIGNLVMEQLKKLDKVAYIRFASVYRSFEDIREFGEEIARLQD

Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.

A7MLX1

P48368

CRTE_CYAPA

Farnesyltranstransferase

Cyanophora

MKPLQTNFNLLTYLYERKEIVEDTLNKSIPRGNPTFIYDSIRYSLSAGGKRIRPILCLASCELAGGTMEMALPTACALEMIHTMSLIHDDLPAMDNDSYRRGKPTNHIIYGEDLAILAGDALLAYAFEFIATQTKNVPADLIVKVIAQVAHSVTTSGLVGGQIIDLSSEGKSDTTLETLNFIHIHKTGALLEAAVLSGALLAGAKEKDMNRFLRYAQNIGLAFQIIDDVLDIISTEEKLGKSIGKDLKTQKATYPSFWGVEESIKQAELLVEEAKEEILYFDNKAIPLIAIADFIVNRNN

Catalyzes the condensation of farnesyl diphosphate (FPP) and isopentenyl diphosphate (IPP) to yield geranylgeranyl diphosphate (GGPP) needed for biosynthesis of carotenoids and diterpenes.

P48368

A8F2U0

ATPB_RICM5

F-ATPase subunit beta

spotted fever group

MAKNIGKITQIISAVVDVKFTNNGELPEILNALECYNDKQRIVLEVAQHIGDDTVRCIAMDSTEGLVRGVEVIDTGSPIRIPVGTETLGRIMNVVGEPIDGKGDIKSSNISSIYKPAPDFTNQSTERNILVTGIKVIDLLAPYTKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYTVFAGVGERTREGNDLYHEMIDSGVINLAEPEKSKVALVYGQMNEPPGARARVALSGLTIAESFRDMNEGQDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGELQERITSTKYGSITSVQAIYVPADDLTDPAPATSFAHLDATTVLSRQIAELGIYPAVDPLDSNSQVLDPMIVGEEHYSVARQVQQVLQTYKSLQDIIAILGMDELSEEDKLTVVRARKIQRFLSQPFHVAEVFTGAEGKFVNLADTIAGFKGLVEGKYDDLPEAAFYMVGTIDEAIEKAQTLK

Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.

A8F2U0

Q21DL5

GLMU_SACD2

Glucosamine-1-phosphate N-acetyltransferase

Saccharophagus

MLEIIILAAGKGTRMRSDKPKVLHTLAGKPFLEHVLDRSAELNADKVHVIIGHGADMVREALAGRDVNFVEQTEQLGTGHAVLQVLPHLNPESDTLILYGDVPLTKTDTLAELRAKVSDSSMGLLTVNLADPNGYGRIVRTNGSVTAIVEQKDANPEQLKIDEVNTGVMAVKSAHLAKWLPALSNDNAQGEYYLTDIIAMSSADDIAIETAQPKDEYEVLGVNNRLQQAELERIFQRQVAEELMVAGATLLDPARLDCRGSIEVGRDCVIDVNCVFEGKVVLGNNVHIGPNCVISDSTIGDGTVILANSILEESTLAENCNIGPFARLRPGSQLASKAKIGNFVETKKAVIGEGSKVNHLSYVGDAEIGAGVNIGAGTITCNYDGVNKSKTTIEDGAFIGSNSALVAPVTVGKNATVGAGSIVTKNSEEGDLIIARAKQSNIKGWARPVKK

Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.

Q21DL5

Q8K3F7

TDH_MOUSE

L-threonine 3-dehydrogenase, mitochondrial

Mus

MLFLGMLKQVVNGTAQSKASSCRKLVLPLKFLGTSQHRIPADANFHSTSISEAEPPRVLITGGLGQLGVGLANLLRKRFGKDNVILSDIRKPPAHVFHSGPFVYANILDYKSLREIVVNHRISWLFHYSALLSAVGEANVSLARDVNITGLHNVLDVAAEYNVRLFVPSTIGAFGPTSPRNPAPDLCIQRPRTIYGVSKVHTELMGEYYYYRYGLDFRCLRYPGIISADSQPGGGTTDYAVQIFHAAAKNGTFECNLEAGTRLPMMYISDCLRATLEVMEAPAERLSMRTYNISAMSFTPEELAQALRKHAPDFQITYCVDPLRQAIAESWPMILDDSNARKDWGWKHDFDLPELVATMLNFHGVSTRVAQVN

Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate, mediating L-threonine catabolism.

Q8K3F7

C4K7A8

RL14_HAMD5

50S ribosomal protein L14

Candidatus Hamiltonella

MIQQESMLNVADNSGARSVKCIKVLGGSRRRYACVGDIIVISIKEAIPRGKVKKGEVLKAVVVRTSKGVRRPDGSIIRFDTNACVILNKNTEQPIGTRIFGPVTRELRNEKFMKIISLAPEVL

Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.

C4K7A8

Q28013

RASA3_BOVIN

Ins P4-binding protein

Bos

MAVEEEGLRVFQSVKIKIGEAKNLPTYPGPNKMRDCYCTVNLDQEEVFRTKVVEKSLCPFYGEDFYCEIPRSFRHLSFYIFDRDVFRRDSIIGKVAIKKEDLQKYHNRDTWFQLQHVDADSEVQGKVHLELRLSEVITDSGVVCHKLATRILECQGLPIVNGQCDPYATVTLAGPCRSEAKKTKVKKKTNNPQFDEVFYFEVTRPCSYSRKSHFDFEDEDVDKLEIRVDLWNASNLKFGDEFLGELRVPLKVLRQSSPHEAWYFLQPRDNGSKSLKPGDLGSLRLNVVYTEDHVFSSDYYSPLRDLLLKSADVEPVSASAAHILGEVCREKQEAAIPLVRLFLHYGRVVPFISAIASAEVRRTQDPNTIFRGNSLTSKCIDETMKLAGMQYLHVTLKPTIEEICQSHKSCEIDPVRLKDGESLESNMENLRQFVDRVFSVITKSGVSCPTVMCDIFFSLREAAAKRFQDDLDVRYTAVSSFIFLRFFAPAILSPNLFQLTPHHTDPQTSRTLTLVSKTIQTLGSLSKSKSASFKESYMAAFYEFFNEQKYADAVKNFLDLISSSGRRDPKSVQQPILLKEGFMIKRAQGRKRFGMKNFKKRWFRLTNHEFTYQKSKGDPPLYSIPIENILAVEPLEEESFKMKNMFQVIQPERALYIQANNCVEAKAWIDILTKVSQCNQKRLAVYHPSAYLNGHWLCCRASSDTAAGCSPCTGGLPANIQLDIDGDRETERIYSLSSSYMSKLETMQEACGSRSVYDGPEQEEYSTFIIDDPQETYKTLKQVVAGVGALEQEHAQYKRDKFRRTKYGSQEHPIGDKSFQSYIRQQSETPAHSM

Inhibitory regulator of the Ras-cyclic AMP pathway. May bind inositol tetrakisphosphate (IP4).

Q28013

Q9H4K7

MTG2_HUMAN

Protein obg homolog 1

Homo

MAPARCFSARLRTVFQGVGHWALSTWAGLKPSRLLPQRASPRLLSVGRADLAKHQELPGKKLLSEKKLKRYFVDYRRVLVCGGNGGAGASCFHSEPRKEFGGPDGGDGGNGGHVILRVDQQVKSLSSVLSRYQGFSGEDGGSKNCFGRSGAVLYIRVPVGTLVKEGGRVVADLSCVGDEYIAALGGAGGKGNRFFLANNNRAPVTCTPGQPGQQRVLHLELKTVAHAGMVGFPNAGKSSLLRAISNARPAVASYPFTTLKPHVGIVHYEGHLQIAVADIPGIIRGAHQNRGLGSAFLRHIERCRFLLFVVDLSQPEPWTQVDDLKYELEMYEKGLSARPHAIVANKIDLPEAQANLSQLRDHLGQEVIVLSALTGENLEQLLLHLKVLYDAYAEAELGQGRQPLRW

Plays a role in the regulation of the mitochondrial ribosome assembly and of translational activity. Displays GTPase activity. Involved in the ribosome maturation process.

Q9H4K7

B4HHG8

EI3D2_DROSE

Eukaryotic translation initiation factor 3 subunit 7-2

Sophophora

MSNYAPFIKPYVEYNEHGWGPCEVPELDVPYQPFCKSDRLGKICDWTAMVPEKKFPSKYASTFGNNSQYAYFYEDDDSTFHLVDTTGSKATKPYQRGRYRTNMRNNVRTRGRTGRGTPNIASLGGSTAGGATASTTKYGKGRHTRNTQNVGRRFGRNAPTRIRESSVMVQSNWVSIEEIDFPRLLKLALPNIKEGKDIATCGSLEFYDKLYDRVNLRNEKPLQKMARVVHTVTTTDDPVIRRLSRTMGNVFATDEILSTIMCCTRSNYSWDVVVEKLGTKVFLDKRYNDQFDLLTVNETSVEPPMEEEGSINSAHSLAMEATLINHNFSQQVLRIGDQEQRFMFEEPNPFEEPGVDLASIGYRYRQWDLGNDVVLIARCKHNAVIQGPNGDMQFLSIKALNEWDSKVTNSVEWRQKLDTQRGAVLASELRNNACKLARWTVEAVLAGSDQLKLGYVSRMNPRDHLRHVILGTQQFKPQEFATQINLNMDNSWGVLRCLIDLVMKQPDGKYLIMKDPNKPMIRLYDVPENAFDSDRDEEESSEPLSNSNDN

mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. In the eIF-3 complex, eif3d specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs.

B4HHG8

C1KVP1

EZRA_LISMC

Septation ring formation regulator EzrA

Listeria

MYYMLIGFIIVVIAVIGAGYILKRKHYQRINELEEKKIKLRERPVIDELSKVKKLKLTGQTEALFESWRSSWDEIETRLFPDLEEVLLEAEMNTDRYKFRSATHAENDIEQMLVVIEKQMDQILGGLKELLISEEKNAKESRATKEKFAELRREVLTRGFKLGETLPYIETKLSELSESLNSYDSLTDQGDHLEAREIVIVVQKEMQVIEAQMERIPSLLHETDTILPEEMTKLRAGYEEMVRKGYYLAQMELDKEISRMKNQIDKMKKNVINLDLDEAEQGVEELHNEIDLFYDTLEHEAEARHFVKENHSPTSDKLQRQNAVSDALAEQITEVKQTYHVAEDDLAVYLKTSAKLSEAKENFEQLTALIASGEIAYSAAQDTLKEIDAALITISAEQDKFAEELRSLRKDELEARDDAERMRRAIITLDRKMERERLPGLPEEYLSLREHMGESINALEKRLEEKPLNMKAVSQDWRIAEEDLTHLTEKAEEMMENVRLVEHVIQYANRYRLRNKELADELVQAENHFYNDYQYKKALEIAVTALEKVETGAFKKVEKAYESKVSVDDIE

Negative regulator of FtsZ ring formation; modulates the frequency and position of FtsZ ring formation. Inhibits FtsZ ring formation at polar sites. Interacts either with FtsZ or with one of its binding partners to promote depolymerization.

C1KVP1

B0UXH9

PIRC1_DANRE

UPF0691 protein C9orf116 homolog

Danio

MSTNEIKNDYSAKEETAGPGDSNTSEIKTSDVYKVDKNLPSRFNNPDCFRYSHKTTNPLYRTTNQAYGSKKPTVHEMPTSFNGSRHRFSEHLLKSGMYRDNGFNTMLDKSRLSRPNETSVFYDRINFHSLYHTAGKS

Microtubule inner protein involved in the attachment of outer dynein arms (ODAs) to dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating. Functions at the initial step of left-right asymmetry specification of the visceral organs.

B0UXH9

P53617

NRD1_YEAST

Protein NRD1

Saccharomyces

MQQDDDFQNFVATLESFKDLKSGISGSRIKKLTTYALDHIDIESKIISLIIDYSRLCPDSHKLGSLYIIDSIGRAYLDETRSNSNSSSNKPGTCAHAINTLGEVIQELLSDAIAKSNQDHKEKIRMLLDIWDRSGLFQKSYLNAIRSKCFAMDISNNTANTASQQLSLDPKQRSKQILSNLKKSPPLNLNISLPTDLTSTDPAKQQAALFQVIAALQKHFKTLPSHTSVGTVAPPQAHTITEYGSRRERERERERYNSRRNRSRSPPAPFSQPSTGRKDRYPSVAQDQYSIGAPNTTFGTNNHHLYPDELNVSNNPHYRPKPVSYDSTLPPDHIKVYSRTLFIGGVPLNMKEWDLANVLKPFAEVQSVILNNSRKHAFVKVYSRHEAENVLQNFNKDGALPLRTRWGVGFGPRDCCDYQHGYSIIPMHRLTDADKKWSVSAQWGGTSGQPLVTGIVFEEPDIIVGEGVSSKAISQKMPTDSGRNGPRSGKPNKSGSISSISPVPYGNAPLASPPPQQYVQPMMQQPYGYAPNQPLPSQGPAAAAPPVPQQQFDPTAQLNSLMNMLNQQQQQQQQS

Plays a role in sequence-specific regulation of nuclear pre-mRNA abundance.

P53617

A4FW56

CYDE_METM5

L-cysteine desulfhydrase

Methanococcus

MDDSKRILITKILKNEVTEALGCTEVGLIGYAVSLCNISDPFSIEKIELTLNNGSFKNVYAVGVPNTGKYGLLPAVVGGFLGNSKNKLLIFNDITYSQELEDFTKEKLEIKVINGPLYCSVKIKDNSGKIHESLIKDNHLNVVIPEIKKEKINMEINSSEKEKYKNLELLDFLNYLDEIPEEIIKLVEKTIYTNKNLIKGDFLNYGTDILSNMVNKTTSACNIRMTGENMTAMSVAKSGNMGIMATLPIISYDFSTENNSEKLIKSVLLSMLVTIYSTYNSSYLSSMCGCVSKGGMGAVIGLSHYKNGKNLKKFDSSARTFTANLPGIICDGGKVGCALKLASGCFAAYSSLFVDISYENGIVGKNFKECVENISKISKAMGDLDCDIVEIMSKKEM

Catalyzes the cleavage of L-cysteine to form 2-aminoprop-2-enoate and sulfide. The former then spontaneously hydrolyzes to pyruvate and NH(3). May be responsible for the production of sulfide required for the biosynthesis of iron-sulfur centers in this archaea.

A4FW56

A7FZ65

RS19_CLOB1

30S ribosomal protein S19

Clostridium

MSRSVKKGPYIQEVLLKRINEMNKNGEKKVLKTWSRSSTVFPQMIGHTIAVHDGRKHVPVYITEDMVGHKLGEFVLTRTYRGHDDKSEKSSRLR

Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.

A7FZ65

B1Y8I5

RL23_LEPCP

50S ribosomal protein L23

Leptothrix

MSRAPISRTFTEGRLAQVLVAPIISEKATSIGEKHNQVLFKVLQDATKIEIKAAVELMFKVEVESVQVLNQKGKTKRFGGRTGRRDHLRKAYVSLKAGQELNFSGEAA

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.

B1Y8I5

Q5WL08

G1PDH_ALKCK

sn-glycerol-1-phosphate dehydrogenase

Alkalihalobacillus

MNISALKARIRASKEDLYPLPLEQIVVAEGALREAAAFIAKQAESGVVLVADSHTYKAAGRDLHDHLCQKGVKADWHLLEPNSNGDIIADEVSLISVMLKVEQSTKLLVAVGAGTIHDIVRFVSGKTNKPFVSIPTAPSVDGFTSLGAPIVVQGSKKTYQLVAPIALFADTVVLQHAPPALIAAGFGDMVGKYTSLFDWKIGSLLKNEAYSDLVADLTEEALSTCVDKVADIGKRTSAGVQVLMESLLTSGLAMALFGYSHPASGAEHHLSHYWEMEALRLGKKQLLHGAKVGLSTQIINRFYKNTVLPDVHRFLDDDEAKQVIALVEALPDPDDVKALLEQAGWNEALVPIAPELVEESLQHAYLLRDRYTLLRLYREGTTMKKEGDAHVGRS

Catalyzes the NAD(P)H-dependent reduction of dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1-phosphate (G1P). The G1P thus generated is probably used for the synthesis of phosphoglycerolipids in Gram-positive bacterial species.

Q5WL08

B2TYK2

GRCA_SHIB3

Autonomous glycyl radical cofactor

Shigella

MITGIQITKAANDDLLNSFWLLDSEKGEARCIVAKAGYAEDEVVAVSKLGDIEYREVPVEVKPEVRVEGGQHLNVNVLRRETLEDAVKHPEKYPQLTIRVSGYAVRFNSLTPEQQRDVIARTFTESL

Acts as a radical domain for damaged PFL and possibly other radical proteins.

B2TYK2

O15432

COPT2_HUMAN

Solute carrier family 31 member 2

Homo

MAMHFIFSDTAVLLFDFWSVHSPAGMALSVLVLLLLAVLYEGIKVGKAKLLNQVLVNLPTSISQQTIAETDGDSAGSDSFPVGRTHHRWYLCHFGQSLIHVIQVVIGYFIMLAVMSYNTWIFLGVVLGSAVGYYLAYPLLSTA

Involved in low-affinity copper uptake.

O15432

Q3B2F8

RUVB_CHLL3

Holliday junction ATP-dependent DNA helicase RuvB

Pelodictyon

MRIELLNTPVDAVELRIEDQIRPRRMEDFTGQQRLTDNLKVFISAARMRGDALDHVLLSGPPGLGKTTLAHIIAEEMGGSLKATSGPMLDKAGNLAGILTSLQKGDVLFIDEIHRMPPAVEEYLYSAMEDFRIDIMLDSGPSARAVQLKVEPFTLVGATTRSGLLTAPLRARFGISNRFDYYPPELLETILMRSSTILGIGIERDAASEIAGRSRGTPRIANRLLRRARDFAQVDGMEIISRPTAMKTLDSLEIDEEGLDEMDKKIMDAVVNRFSGGPVGVGSLAVSVGEEQDTIEEVYEPYLIQAGYLSRTPRGRVATQRALLRFSDGSSALRGTLFDGQEHV

The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.

Q3B2F8

B5ZN86

RRF_RHILW

Ribosome-releasing factor

Rhizobium

MTEGIDIKELKRRMDGAVSAFKSDIASLRTGRASANILDPVTIEAYGSRMPLNQVANITVPEPRMLSVSVWDKSMVSAVERGIRESNLGLNPIVDGQSLRIPLPELNEERRKSLVKVAHDYAEKSKVAIRHVRRDGMDGLKKAEKDGVIGQDEGRAQSERVQKMTDETISEIDRLLGEKEKEIMQV

Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another.

B5ZN86

A8NCK6

COX2_COPC7

Alpha-cuprenene oxidase 2

Coprinopsis

MNIVNSLDLSNITTNHVAAAVCAGIAVYAIVAGRNRGKKYPPGPKGHPLIGSLFEMPIQNAHVVYKEWAKTYGDMIFFKVLGQPFLILSSEETITDLLDKRSTIYSSRPRMPMVVELMGWDYTLGLLPYGERWRFLRREFHRFMSPTAVSNYRQIQENSVYTFLNNLVESPEQFSKHLRLFYGSISMKVSYGINVKSAEDQYLLDAEGAMSGFMEAGIPGRFWVDLFPALKYVPSWMPGAEFKRKAARWARLNDISLERPFKHVLDQLKKGVASQSVSATLIEELPDQNSPDRKEKETIARNISATTFLAGIDTIHSTTQAFFYAMAQFPEVQKKAQAEIDAVVGDKRLPTFEDRDQLPYVNALVKELIRWSEVAPLGIYHSTTEDDEYKGYFIPKGTIVMTNAWSILTDPVTYPDPFAFKPERYLKNGVMNPDAPRPEDLAFGRGRRICPGRYLADETLFMTSVGVLAGFNISPPLDKSGKPIKLKNERVGTITLTPPKFECRIEPRSPAIRTMIHDTAESISAL

Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of alpha-cuprenene and oxidized derivatives . The alpha-cuprenene synthase COP6 is the only sesquiterpene synthase identified in C.cinereus that appears to be part of a biosynthetic gene cluster and is highly specific since it catalyzes the cyclization of (2E,6E)-farnesyl diphosphate into only one product, alpha-cuprenene . The cytochrome P450 monooxygenase COX2 then oxidizes the cyclohexadiene ring of alpha-cuprenene at positions 1 and 4, yielding first alpha-cuparene, followed by alpha-cuparophenol and a further yet unidentified compound resulting from one additional oxidation step . The cytochrome P450 monooxygenase COX1 then likely catalyzes the oxidation at position 9 of the pentane ring of alpha-cuprenene to give the corresponding hydroxy or ketone derivatives .

A8NCK6

Q4JV64

DAPA_CORJK

4-hydroxy-tetrahydrodipicolinate synthase

Corynebacterium

MSTGNAATRGSAHFGTISLAMVTPFKKDGSIDLDAGVALAGHFVDEGCDSLVLAGTTGESPTTGATEKLDLLRAVRSELGDSVKLIAGSGSYDTAVTVEMSRASQEAGADSLLVVTPYYSRPSQEGIYQHFTTVADAVDIPVCVYDIPSRSVVPVEPETLHRLADHPQIAAVKDAKGDLAAGMELIENTDLAWYSGDDPLNLPWLAAGATGFISVIGHVATRQLKQLRDAFDAGDIATARSIAVQLQPLQKAQARLGGVTFAKAALKLKGKDVGAPRLPIIEPTAAEMDQLAQDLQAAGV

Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).

Q4JV64

A0AKW5

DCUP_LISW6

Uroporphyrinogen decarboxylase

Listeria

MTKITNDLFLRAARKEQVDKIPVWYMRQAGRSQPEYRKLKEKYSLFEITHQPEICAYVTKLPVDQYGVDAAILYKDIMTPLPGMGIDVEIKSGIGPVIHNPIRTFQDVDKLSIFKPEIEVPYVLDTIKLLADDMLEVPLIGFAGAPFTLASYMIEGGPSKNYHLTKSFMYREPEVWSILMEKLGRMTATYLIAQINAGASAVQLFDSWVGALSRADYTKYIRPVIEMIVREVKAVHPTTPIIMQAVGASHLLEEWETMPLDVVGVDWRETLTGARKKVPSKAIQGNLDPSTLLAPEKCLEEAERIIQEGILKPGYIFNLGHGVFPEVQPEMLKKLTNYIHDRSEILLKKG

Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.

A0AKW5

B8E7D3

OPGG_SHEB2

Glucans biosynthesis protein G

Shewanella

MVSLLRCPSSKPYSSLICSLTLGAVVALSGVAYAEETKPAETVPVVTPPKVISQPATKNQVRFTKTGAFDSDTVVKIAKRLAAKPYVALKDPLPAGLAKLSYDEYRDIRFNPTASIWRDQGVPFQMQMFHRGFYFQDLIEIAIVEGQNATHLAYEPKYFTAGEVITQALPNDDIGYSGFRIHNQLNTNGVFDELMVFQGASYFRALGKGNAYGLSSRGLALKTADAEGEEFPIFRAFWVERPYNDSNLIVVHALLDSPSVAGAYTFSVRPGDNTLIDVEATLFPRVELSKVGLAPSTSMFLHSLNGRHDTDDFRPEVHDSDGLLMLNGRGEHLWRPLANPRQLQVSAFSDNSPQGFGLIQRERDYASYQDLEAHYERRPSLWIEPVGNWGQGSVVLTEIPTESEIHDNIVSYWKPRQPIPAGSEFHFAYRMSWGEEPAAKVGAVHVSRSASGRADIAKATPRRLFVVDYQIEGPMTDEMPVAKVEASGGVVTNVVIARNAAKNGYRLAFELEPEDKELIELRAELKFPTPRQVETWLYRWTL

Involved in the biosynthesis of osmoregulated periplasmic glucans (OPGs).

B8E7D3

Q58T74

M7H1_BOMMX

Maximin-6

Bombina

MNFKYIVAVSFLIASAYARSEENDEQSLSQRDVLEEESLREIRGIGAKILGGVKTALKGALKELASTYVNGKRTAEDHEVMKRLEAVMRDLDSLDYPEEAAERETRGFNQEEIANLFTKKEKRILGPVISTIGGVLGGLLKNLG

Maximin-H1 shows antibacterial activity against both Gram-positive and Gram-negative bacteria. It shows also antimicrobial activity against the fungus C.albicans. Shows strong hemolytic activity.

Q58T74

Q8NSR1

GUAA_CORGL

Glutamine amidotransferase

Corynebacterium

MSLQTNHRPVLVVDFGAQYAQLIARRVREAGIYSEVIPHTATADDVRAKNAAALVLSGGPSSVYAEGAPSLDAEILDLGLPVFGICYGFQAMTHALGGTVANTGKREYGRTDINVAGGVLHEGLEACHKVWMSHGDAVSEAPEGFVVTASSEGAPVAAFENKERKMAGVQYHPEVLHSPHGQAVLTRFLTEIAGLEQNWTAANIAEELIEKVREQIGEDGRAICGLSGGVDSAVAGALVQRAIGDRLTCVFVDHGLLRAGEREQVEKDFVAATGAKLVTVDERQAFLSKLAGVTEPEAKRKAIGAEFIRSFERAVAGVLEEAPEGSTVDFLVQGTLYPDVVESGGGSGTANIKSHHNVGGLPDDVEFKLVEPLRDLFKDEVRAVGRELGLPEEIVGRQPFPGPGLGIRIIGEVTEDRLETLRHADLIARTELTEAGLDGVIWQCPVVLLADVRSVGVQGDGRTYGHPIVLRPVSSEDAMTADWTRLPYEVLEKISTRITNEVPDVNRVVLDVTSKPPGTIEWE

Catalyzes the synthesis of GMP from XMP.

Q8NSR1

L0E155

MALA_MALAU

Malbrancheamide biosynthesis cluster protein A

Malbranchea

MAPTPKYTFTERAAAGNLSDAEILNSNNPTGSELPDESDVVVGGAGIHGLIYALHASKYKPNNLKISVIEKNTRPGYKIGESTLPIFYTWCKLHGISAAYLLRLFGLKDGLCFYFLDRENQGQYTDFCSVGAPGLVLASLQIERPMSELLFTILAQRNGVNVYHGREVDFKSTVVQGGGQGNKIAVSRGKYDSTPKTIDSALFVDATGRFRQFCSKKAPRHRFDGWNCNAFWGYFTAPKDESKIPFDLYEGDHTNHLCFPEGWVWVIRLPSWEGSLIANLMDMVTYILECADAGVPGDELPSSEELARMFGLKFQWVTSIGFAVRNDVKYPEDLSAYGTREAEQKFNYFVQKYELLQQFMSNFELIENLYGPGTTWFIRKTLAYQSPVVSGPGWLAIGDACGFTNPLYSPGINVGMSTSTWAAQLSHRIVEIGKSAPADAAESSIRKLLVPYDDYCKSLVPALEQMNRFNYVCYRDTRLGPQVACLWQFFAGIERYLSDVNIETFAHYAIKWVWGAMVPEYQQVAQKCIEHIETVPLDERLPDAMVDELLAFSNRIKSAAVAADDFSLRWDAILRSFDRSLNFVEGKTSRDIYTRQCSGCGAWLQLRPDWKKCHSCGLLGTEPQTAVTFDPPLTAEEEALLYAAWNTAPKYDPSKELKLPTPTRPAA

Flavin-dependent halogenase; part of the gene cluster that mediates the biosynthesis of malbrancheamide, a dichlorinated fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core . The first step of malbrancheamide biosynthesis involves coupling of L-proline and L-tryptophan by malG, a bimodular NRPS, to produce L-Pro-L-Trp aldehyde through reductive offloading . This compound undergoes spontaneous cyclization and dehydration to give a dienamine which is reverse prenylated at C-2 by malE . The other prenyltransferase present in the cluster, malB, displays modest activity, suggesting that may be a redundant gene in the pathway . Subsequently, a [4+2] Diels-Alder cyclo-addition catalyzed by the bifunctional enzyme malC forms the characteristic bicyclo[2.2.2]diazaoctane ring of premalbrancheamid . Finally, the flavin-dependent halogenase malA catalyzes the iterative dichlorination of the indole ring of premalbrancheamide to yield C-9 monochlorinated malbrancheamide B, C-8 monochlorinated isomalbrancheamide B, and dichlorinated malbrancheamide . MalA is also able to brominate premalbrancheamide at C-9 to yield malbrancheamide C, and, to a lesser extend, at C-8 to yield isomalbrancheamide C . Finally, malA can brominate C-9 monochlorinated malbrancheamide B at C-8 to yield malbrancheamide D, or C-8 monochlorinated isomalbrancheamide B at C-9 to produce isomalbrancheamide D .

L0E155

A5F2Y7

RLMH_VIBC3

rRNA (pseudouridine-N3-)-methyltransferase RlmH

Vibrio

MKIQLIAVGTKMPKWVEEGFQEYRRRFPHDMPLELVEITAGKRGKNADIARILQKEGEAMLAAVPKGNRIVTLDIPGKRWDTEELAVQLESWKLDGRDVSILIGGPEGLAPACKAAADQSWSLSPLTLPHPLVRVVMAESLYRAWSITTNHPYHRE

Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.

A5F2Y7

Q889W6

RL22_PSESM

50S ribosomal protein L22

Pseudomonas

MEVAAKLSGARISAQKARLVADQIRGKKVGEALNLLAFSSKKAAEILKKVLESAVANAEHNEGADVDDLKVSTVFVNEGRSLKRIMPRAKGRADRIVKRSCHITVKVADK

The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.

Q889W6

K7XFK5

KAX3G_MESGB

Tx4

Mesobuthus

MKVFSAVLIILFVCSMIIGISEGKEIPVKCKHSGQCLQPCKDAGMRFGKCMNGKCNCTPK

Potassium channel inhibitor.

K7XFK5

Q189R8

FOLD_CLOD6

Methenyltetrahydrofolate cyclohydrolase

Clostridioides

MSTKGQIIKGKPVADKISEELIKEVDLLVKEGINPKLTIVRVGARSDDLSYERGALKRCQNIGITTEVLELAEDITQEEYIDVLKRVNDDKNVNGILCFRPLPKHLNEEVIKYVIAPEKDVDCFSPINSAKVMEGDKSGFPPCTPTAVVEILKHYNVDLKGSKVTVLGRSMVVGKPVSMLLLSEHATVTICHSKTKNLSGVAAEADVLIAAIGRAKMVDESFVKDGAVVIDVGINVDEEGNLCGDVDTNAVLDKVSMITPVPAGVGSVTTSILAKHVVKACKLQNNK

Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.

Q189R8

Q88YZ2

ACCD1_LACPL

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta 1

Lactiplantibacillus

MSHYPASGTWQACPKCGRHVHQRQWGTYQQCPYCHYWQRLTTAQRLEQLVDEGSFQPLTMTERPVNQLGFPDYMNKLRRAQRQTGLNEAVVCGTALIEQQPCILAVMDSHFMMGTLNTAVTRRLLHASEQARAQRLPLIIVTASGGARMQEGVYALVGMNLILAELARLAATPLPLITVLTDPTMGGVSASFAFKGDLIIAEAGAKIGFAGARVIQQTLPVKLPADFQTADQLFKNGMVDAVVERPQLRSTLGQALVNYGIGRSAHG

Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.

Q88YZ2

B7VBM9

ARNE_PSEA8

Undecaprenyl phosphate-aminoarabinose flippase subunit ArnE

Pseudomonas

MSAALLLATLLMTGLGQVAQKLTVEHWRLVAADGWTARLRSPWPWLALLALGLGLLCWLLLLQRVEVGSAYPMLALNFVLVTLAARFVFDEPVDRRHLAGLLLIVAGVALLGRSA

Translocates 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol (alpha-L-Ara4N-phosphoundecaprenol) from the cytoplasmic to the periplasmic side of the inner membrane.

B7VBM9

Q9F5Y1

RNFE_AZOVD

Rnf electron transport complex subunit E

Azotobacter

MSHCGAPSVPEPEKKVPWQYFTSALWQYNVALVQMLALCPTLAVTTTATNGLGMGLATTLVLVMTNALISSMRHTISPEVRNPVMIGVIAGVVTLTDMAMNAWMHELYKVLGLFIALIVTNCAVLGRAESFCLRNPVIPSILDGAGMGAGFTAVLVVIGGIREILGSGTLFSQASSLLGSHFKWMEITVIPDFQGILLAILPPGAFIVLGFLLAAKRVIDRKRAERRQQTHGELVVLQ

Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.

Q9F5Y1

P27715

UNC13_CAEEL

Uncoordinated protein 13

Caenorhabditis

MDDVGDYNDDQLSDGMSMRLLCITIKKARLQGAVDEFNSYVTVKLQTVKSTTVAVRGNLPCWEQEFIFETNRPDDGMVLELWAKGVLWDKLIGVHYMPLSEIRYSNAAGSGQWLQMDHELETRNGQTVGTRGPTGHNLLTDVRFELPFDVQGHDEDIQSRLLALNGLIEHDQLGPNNHHRAPFNHSGLSEDSDYTSDVSVPVNHHQLHPNSSAHQYESHLHPHRTRQLLHTREGAASYEDEEDAYHARHQPESDDYNHQDTYDQHSSYYNDEYAPSGSSSQYQRQGYQDQDQQHQNIYEDTVTPVREFGESAVPPAASSSRRQFDQVYGYASSSEERYDTPMSSGRLPRDEPILEHSEPEYVYDQNGYPEEDNYGINPTYSEDHFEGQTNDYSTTHQEPNDFRNDYNSSYQREYWNESEPLSYNSRPPNGHIRTGANTWREPSTSSRPTSSQAWNYQDDTHQYDEVDRGSRVSFTRTPSVDRTDRPSESGGGFYDEMSESGRPGRPDSHHNWRYDSIQEEDNEKDNWKQHVEGYEEGQEEKQKDNQKPNDHSAASPQDHYHRSDSTAQQDFGNNIVRQTIQEEEEKRNYQELWHNAYKRVCADLGIKSSQASLVATTGGTLLQNLFLYRPKLAPAGHGATASQFQSPAGATRFYANHNNNNNNVSKNELDSTTETPPDPSRTPSTSSMNPVPSLAVPMSPGPYLNSDPPSPVSPNPQIKRSIYRIKESYEDRNGGRERIYTTNLVSVYLEKMKPPDELEEGSSGSMRETQNEIKNGTQLHNAESNIFFPQDSVPKSISYNAGNLKNTSITTSKTSSAITNHSSLPPQPPSKPASRDSDPMKQLLTFSKSFKKVRRVRSAMPRRRKRKRVKIKKSRSCPILWKTEKTPHPMKSKSMTCIRIPKKTVIAPLRKEIKIVRMKPPAARCESDSKAHKKKNLLDVYKDMGKSTVLDGNGSSAANAFYKSIDAAPNMNVARTKTSIPLVSELVLKTMATKRAQAGLANAARTTFSDTELKTHVYKKTLQALIYPISATTPHNFATTTFQTPTFCYECEGLLWGLARQGLRCTQCQVKVHDKCRELLSADCLQRAAEKSTKHGEADRTQSLVNVIRDRMKIQEQNKPEVFQMIRTVFDVDENIQKETLKTVKASILEGSSKWSAKITLTVLCAQGLIAKDKTGKSDPYVTAQVGKTKRRTRTIHQELNPVWNEKFHFECHNSTDRIKVRVWDEDNDLKSKLRQKLTRESDDFLGQTVIEVRTLSGEMDVWYNLEKRTDKSAVSGAIRLHINVEIKGEEKLAPYHVQYTCLHEHLFAAHCVDEEVKLPKVRGEDSWKVCFQETGQEIAEEFAMRYGIESIYQAMTHFACLCTRYMCAGVPAVLSTLLANINAYYAHTTATSAVSAPDRFAASNFGKERFVKLLDQLHNSLRIDLSAYRNHFPSSSPAKLQDLKSTVDLLTSITFFRMKVLELASPPRASTVVRECAKACMQQTYQLMFESCAEQFPILDTSVQFWYEFIDYIMRVIEEDQKNYTPALNQFPQELNVGNLSAETLWSMYKNDLKMALEEHAQKKRCKTPEYMNLYFKVKGFYFKYVADLSTYKSSIPEFPAWFIPFVMDWLNENDEHSMDILRNAYNVDKADNFPQTSEHTKFSNSVVDVFTQLNAALKLLKQMDCPNPEVAADMMKRFSKTLNKVLLAYADMVQKDFPKFAHDEKLACILMNNVQQLRVQLEKIYETMGGAELDEHIGQVLTVLQKKLNSVLDRLSAEFVTTLEPHIHEQTIKLGMLLVKIKGPQLQKTQVQPEADAVLEPLMDLLEGSLRRYADQCEKTVLKYILKELWKITIVNMEKRVVLPPLSDKALLKQLPNAKIGDVTKLMSTNIQSIKGMNSVKDMMDMARESEKSLTPRQCTVLDCALDAIKDSFHASGKGLKKSFFEKSPELQSLKYALSLYTQTTEQLIKTFITSQRQQDLPSQEQPVGEVSVQVDLFSHPGTGEQKVTVKILAANDLRWQTSSAFKPFVEVHLVGPHLSDKKRKWSTKTKAGNWAPKFNETFHFFLGNEGEPEHYELMFQVKDYCFARDDRVVGVGVLQLSSVVDQAGSCAMWVQLGTRLHIDETGLILLRILSQRQTDEVAKDFVRLKTECRYETETVMAASASSQNINRT

May form part of a signal transduction pathway, transducing the signal from diacylglycerol to effector functions . One such function could be the release of neurotransmitter from neurons . Probably by regulating neuronal transmission downstream of lin-3 and receptor lin-23 and phospholipase plc-3 and upstream of innexin unc-7 and egl-4/PKG in ALA neurons, involved in the decrease in pharyngeal pumping during the quiescent state that precedes each larval molt, .

P27715

C4K230

ATPD_RICPU

F-type ATPase subunit delta

spotted fever group

MNKGNLIENYAVALFNNAMVDNIQDKIFEEITSINRIITDNFDIREFLFSPIVNKNDKINAVNSLAKNIKISTIVQNFLLLLVKNSRIAILSNIVDAYNTLLYESKNIKIVQVISANKLQPKEQEWIKSRIEKELNQKTEILFDIDNTIIGGIVIKYDSMLQDYSIKGSLEKITKALKTVNIAV

This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.

C4K230

P14117

RL4_XENTR

L1

Silurana

ITLLNVSKLNLLRLALGGHVGRFCIWTESSFRKLDDLYGTWRKSAKLKADYNLPMHKMTNTDLTRILKSQEIQRALRAPNKKVKRRELKKNPLKNL

Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.

P14117

B1XPT3

MTNB_SYNP2

Methylthioribulose-1-phosphate dehydratase

unclassified Synechococcus

MSLENQTQKERLCAVIRQLHTQGKSPATSTNYSFLDEDQVIFVSRSGVDKSQFQPEDFIAVDTMGLPLPPDEGIKPSAETLIHCFIYQNFPGITCVLHTHSVAATLLSGIFAAKQAVTFSGYEVIKGIAGQTTHETAIALPIFANDQDMKSFCQQLAQRQEELNNYGFLIAKHGLYAWGETMAIAKRHLEVWEFMLECELEQLKITPPLAAR

Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).

B1XPT3

Q12X59

G1PDH_METBU

sn-glycerol-1-phosphate dehydrogenase

Methanococcoides

MDVTHDMNGQKKWMQLPRNVVIGNGVINEVRDVCTDLKLIDNALVVTGKSTKGIAGEIVQDSLQDAGQNVELVISESASMKEVERIRKHAIESGTKYFLGVGSGKTIDVAKLAATDLEVPFISVPTAASHDGIVSSRASIKDGKTTTSVQANAPMAVIADTEIIANAPYRLLAAGCGDIISNCTAVLDWQLASRLQNVQFSEYAAALASMTAQILIDSADSIKPELESSVRMVVKALVSSGVAMSIAGSSRPASGSEHMFSHALDRVADEPALHGEQCGVGTILMMYLHGGDWKKISDALKLIGAPTTAKELGIEDKYILEALVLSHTIRPERYTILGTGLTPDAAEIVARKTKVIS

Catalyzes the NAD(P)H-dependent reduction of dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1-phosphate (G1P). The G1P thus generated is used as the glycerophosphate backbone of phospholipids in the cellular membranes of Archaea.

Q12X59

Q9RUF3

SYM_DEIRA

Methionyl-tRNA synthetase

Deinococcus

MQNPPQHPEAQSPETRDREFFITAAIDYANGTPHIGHVYEKILADAIARYQRLAGRDVTFVMGTDEHGEKISKAAAKGGVTPQELVDDLSERAFQGLWKKLGISYDFFIRTTSAKHKKYVQDVLQRVYDAGDIYFAEYEGLYSVGAERYVTEKELVEGPDGVRRFPGDKDPPELRREANYFFNMQKYQPWLLETLQQNPDLIQPAGYRNEVLEMLKEDIGPLSISRPKARVPWGIELPWDTDHVTYVWFDALLSYLTPLVSQGQDASMSGKAWHVIGKDILKPHAVFWPTMLRAAGLPLYRRLVVHSHILAEDGRKMGKSLGNAIDPEELVAAWPVDAIRYALLREASLGADSPFGEGVLVSRLNSDLANDLGNLLSRTVSMIQKYRGGVIPAATEPTDREREIEAAARALPDEVLRLVDELKINMAIDAAMSFVRDLNRYIAESTPWTLAKSPETQGRLDTVLYTAAEGLRVASVALEAVIPTKAKELREQLGLGRQGYPLQAAWGLTPAGTRVQGGAILFPKPEPKADETKNAEAKPPKPQAKKEKKTVTDTAPAKTTEQKPEAAAPAQNDGLISIDDFAKIDLRIAEVVACEAVEKADKLLKLTVKLGDETRTVVSGIRKWYEPEALVGRKVVLVANLKPAKLRGIESQGMILAAEDDAGNLDLVGTELDLPSGTKVR

Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.

Q9RUF3

B1VDE1

MIAA_CORU7

Isopentenyl-diphosphate:tRNA isopentenyltransferase

Corynebacterium

MDYSHSDSPSTAPAGKTPVDQLRPLLIVGPTGAGKSDLSLEVARRLDQPVEIINGDSMQMYRGMDIGTAKLSRAERAEFPHHLFDCLDVDDTASVAAYRDLAGETVEQIQARGARPIIVGGSMMYLQALVDDWQFPPTDAAVRAKWMAEQDRIGVEALHEVLRSKDPDAADIIEEKDPRRIVRALEVIELTGKPFAASQPPKNVPTRWGTRIFGLKAPGNWLNPRLEARVDRMFAAGLVAEVEGLATAGLSRESTAGKAIGYAQVLSALAGECSMEQAREDTVVGTRRYARRQRSWFRRDPRIHWLDATVADPGLLAGQVIDELRETTQG

Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).

B1VDE1