entry stringlengths 6 10 | entry_name stringlengths 5 11 | protein_name stringlengths 3 2.44k | sequence stringlengths 2 35.2k | function stringlengths 7 11k |
|---|---|---|---|---|
B6CVD7 | ERO1A_PIG | ERO1-like protein alpha (ERO1-L) (ERO1-L-alpha) (EC 1.8.4.-) (Endoplasmic reticulum oxidoreductase alpha) (Endoplasmic reticulum oxidoreductin-1-like protein) (Oxidoreductin-1-L-alpha) | MGHRWGFLIVFLGAVGLLGSGYGRQQPSETAAQRCFCQVSGYLDDCTCDVETIDRFNNYRLFPRLQKLLESDYFRYYKVNLKRPCPFWNDINQCGRRDCAVKPCQSDEIPDGIKSASYKYSEEANNLIEECEQAERLGAVDESLSEETQKAVLQWTKHDDSSDNFCEADDIQSPDAEYVDLLLNPERYTGYKGPDAWKIWNVIYEENCFKPQTIKRPLNPLASGQGKSEENTFYSWLEGLCVEKRAFYRLISGLHASINVHLSARYLLQDTWLEKKWGHNITEFQQRFDGILTEGEGPRRLKNLYFLYLIELRALSKVVPFFERPDFQLFTGNKVQDAENKMLLLDILHEIKSFPLHFDENSFFAGDKKEANKLKEDFRLHFRNISRIMDCVGCLKCRLWGKLQTQGLGTALKILFSEKLIANMPESGPSYEFHLTRQEIVSLFNAFGRISTSVKELENFRNLLQNIH | Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins. Plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1. |
B6D434 | CAMP_BUNFA | Cathelicidin-related antimicrobial peptide Bf-CRAMP (Cathelicidin-BF) (Vipericidin) | MEGFFWKTLLVVGALAIAGTSSLPHKPLIYEEAVDLAVSIYNSKSGEDSLYRLLEAVSPPKWDPLSESNQELNFTMKETVCLVAEERSLEECDFQEDGVVMGCTGYYFFGESPPVVVLTCKPVGEEGEQKQEEGNEEEKEVEEEEQEEDEKDQPRRVKRFKKFFRKLKKSVKKRAKEFFKKPRVIGVSIPF | Potent antimicrobial peptide against most of Gram-negative bacteria, some Gram-positive bacteria (Bacillus) and some fungi (C.albicans, P.pastoris, A.terreus, A.nidulans, and C.globosum). Adopts an amphipathic alpha helical conformation, that may allow to partition into the target membrane. No hemolytic and cytotoxic activities have been observed on mammalian cells. |
B6DMK2 | MER3_ORYSJ | ATP-dependent DNA helicase MER3 homolog (EC 3.6.4.12) (Protein RICE MEIOTIC CROSSOVER 1) | MAAMGHLGDPYALRSVADLPPPFRSVFGFRYFNSLQSECFPACFLSDVNMVISAPTGSGKTVLFELCILRLLSRFLSSEWRFNLIKGTLKTIYIAPMKALVQEKLRDWNMKLGSLGISCLEMTGDNEFYNTKSIHDADLILTTPEKFDSVSRHGIRDGGLGFFSDIALVLIDEVHLLNDPRGAALEAIVSRIKMLSRLGTMKIAPLANVRFIAVSATIPNIEDIAEWLAVPSEGIKRFGEEMRPVKLTTKVFGYAPARNDFLFERRLQSFIFDILMQHSRGKSALVFCSTRKGAQEAAQCLSQTASSLGYSNPFMKSMQQYEHLKEAALTCSDKQLQACLVHGVGYHNGGLCLKDRSVVEGLFLKGDIQILCTTNTLAHGINLPAHTVVIKSTQFFNKEKGLYVEYERSMVLQMCGRAGRPPFDDTGTIIIMTRRETVHLYENLLNGCEMVESQLLPCAVEHLNAEIVQLTVSDITLAIEWLKCSYLYIRIKKNPQHYGIKKEIPRELLEKQMKDICVEKIHELGEYGLIWTDEDGFLLKPLEPGRLMTKFYLKFDTMKLIVKASACCTLEDLLHIICHSAEITWIQLRRNEKKLLNEINADKEGRLWFHVVGANGKRKKRIQTREEKIFILANDCLTGDPLVHDLSLNQEMNSICSNGCRVAKCMREYFIYKKNYKSAISSMLLAKCLHQKLWESSPFLLKQLPGIGIVTAKALKTAGIDSFESLATADARKIESVTGRNYPFGDSIKSYLPSLGPKIDINIEDAGNRQGKSTIIVTLTRLSQAVGSSKQNYADMVVGSEEDNAILFHEKIKTQEFSSPYSVKLYVPCPPNARATLKVDVIFEEYVGLDIHKKHVVSREDFHVTKVFGIKKAEPLYNLPAESCLVSSKTTRTNQSKYHNGQNPLSKEVCVIEDDFRAKAPDKDDNDLEILGTREYNNLASLEAPSFTLLHEEDYEDVPDVLASEPVEAECKSATNNTIFDHIRKKSRDFPNLMLSKSMDSSYEPLILKKMKTSGDQFGLDQSSLHAYEVTPMVFDRTEARVSPNNTDERCRNILTRTAETRSFQFTGKMDSISQKSEILNRTQGKNSTQLAGKKAFEKSKTPDENSLHFVGKRDSSSEKSKALSKTPDENSLQFLGKMDSSSEKSKFCFSSPLADFQPMQCTKQVAASVQPLTIQDYCKDILASAKSSGTGASFLDVKSVFSFL | DNA helicase required for crossover formation, complete synapsis of homologous chromosomes and bivalent formation during meiosis. Is specific to recombination events resulting in interference-sensitive crossovers (class I meiotic crossover). Works cooperatively with ZIP4 to promote crossovers. |
B6E2X2 | MCAL_RHOCA | L-malyl-CoA/beta-methylmalyl-CoA lyase (EC 4.1.3.24) ((3S)-malyl-CoA/beta-methylmalyl-CoA lyase) | MSFRTQPPAPARLNRCQLFGPGSRPAIFEKMAQSAADVINLDLEDSVAPDDKPQARRNIIEASHNIDWGNKYLSVRINGLDTPFWYRDVVELLEDGSERIDQIMIPKVGCAADVYAVDALVTAIEAAKGRKKRISLEVIIESAAGIAHVEEIAAASPRLQAMSLGAADFAASMGMATTGIGGTQENYYMLHAGVKHWSDPWHWAQAAIVAACRTHGILPVDGPFGDFSDDEGFRAQALRSATLGMVGKWAIHPKQVALANEVFTPSDAAVAEAREILAAMEKAKAEGAGATVYKGRLVDIASIRQAEVIVRQAEMAKV | Involved in the ethylmalonyl-CoA pathway for acetate assimilation. Catalyzes the reversible condensation of glyoxylate and acetyl-CoA to L-malyl-CoA and the reversible condensation of glyoxylate and propionyl-CoA to beta-methylmalyl-CoA. |
B6ECN9 | AADH2_SOLLC | Aminoaldehyde dehydrogenase 2 (SlAMADH2) (EC 1.2.1.-) (4-trimethylammoniobutyraldehyde dehydrogenase AMADH2) (EC 1.2.1.47) (Aminobutyraldehyde dehydrogenase AMADH2) (EC 1.2.1.19) (Gamma-guanidinobutyraldehyde dehydrogenase AMADH2) (EC 1.2.1.54) | MAIPNIRIPCRQLFIDGEWREPLKKNRLPIINPANEEIIGYIPAATEEDVDMAVKAARSALRRDDWGSTTGAQRAKYLRAIAAKVLEKKPELATLETIDNGKPWFEAASDIDDVVACFEYYADLAEALDSKKQTEVKLHLDSFKTHVLREPLGVVGLITPWNYPLLMTTWKVAPALAAGCAAILKPSELASITSLELGEICREVGLPPGALSILTGLGHEAGSPLVSHPDVDKIAFTGSGPTGVKIMTAAAQLVKPVTLELGGKSPIVVFDDIHNLDTAVEWTLFGCFWTNGQICSATSRLIIQETIAPQFLARLLEWTKNIKISDPLEEDCKLGPVISRGQYEKILKFISTAKDEGATILYGGDRPEHLKKGYYIQPTIITDVDTSMEIWKEEVFGPVLCVKTFKIEEEAIELANDTKFGLGAAILSKDLERCERFTKAFQSGIVWINCSQPCFWQPPWGGKKRSGFGRELGEWSLENYLNIKQVTQYVTPDEPWAFYKSPSKL | Dehydrogenase that catalyzes the oxidation of several aminoaldehydes. Metabolizes and detoxifies aldehyde products of polyamine degradation to non-toxic amino acids (Probable). Catalyzes the oxidation of 4-aminobutanal and 3-aminopropanal to 4-aminobutanoate and beta-alanine, respectively. Catalyzes the oxidation of 4-(trimethylamino)butanal and 4-guanidinobutanal to 4-trimethylammoniobutanoate and 4-guanidinobutanoate, respectively. |
B6EGU2 | FADB_ALISL | Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)] | MIYQGENLSVDYIENGIAHLVFNAAGSVNKLNIATLRSLGEAIDVLYKQKDLQALLLSSGKSAFIVGADITEFLGLFDTPEEELSDWLHQANVIFSRLEDLPVPTLSAITGFALGGGCECVLATDFRLADDTASIGLPETQLGIMPGWGGSVRLPRLIGADPAMEVITTGKPKRAKDALKIGMVDGIVSRETLIDASVSMLKQAIDGQLNWQQRREQKKAPIQLSPLEAAMSFNVAKGMIMKMAGKHYPAPLTAVKSIEQSANMHRDDALAIENKHFVALTRTDVAKSLVGIFLNDQLVKSKAKQAVKNSEPVKNAAVLGAGIMGGGIAYQSASKGVPVLMKDIAQASLDLGMNEASKLLNKQLERGRLSGLKMAQVLSSITPSLNYGGIETKDVIVEAVVENPTIKAAVLAEVENEVNEHAILASNTSTIPISLLAKSLKRPENFCGMHFFNPVHRMPLVEVIRGEKTSQQTIDRVVAYASQMGKTPIVVNDCPGFFVNRVLFPYFAGFSLLLRDGGNYQQIDKVMEKEFGWPMGPAYLLDVVGIDTAHHAQAVMAQGFPERMAKNGRDVIDAMFEDDRYGQKNGIGFYAYALDKKGKPKKNIDEKTNAIIATITDSTQPYTSEQISARMMIPMINEVIRCLDEGIIASPAEADMALVYGLGFPPFKGGVFRYLDSIGLDTYLDMAKEFEQLSPVYQVPDSIKQKAAAGECYYPAPKSSVSSPSV | Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}. |
B6EU02 | JBP2_LEITA | Bifunctional helicase and thymine dioxygenase JBP2 (J-binding protein 2) (LtJBP2) [Includes: Probable DNA helicase JBP2 (EC 3.6.4.12); Thymine dioxygenase JBP2 (EC 1.14.11.6)] | MLNGLTRVSTSSELESILDIVQSSGEIAVVFISPSIGDLETITSETQRRQLRIAGIPRGGYTILPAIPLYDDELLQMCERYTAANDYEKAQIRDSLFMREYPLFAYSVRNHKALFHPADYVSRILQFCSYYVQAPDADVLSLLDRSPFLHISPIKEICTHIRLIARGTPLAPEDSESPAPEQLRFHAESDAEKLAAERAGAMSIATSSGGASETEQLSLFSGVVPSALFQKDAVEEVDKDTEETMVDLTGEETVDAVHSFQAEYLTLDGLELVTKAAIFYDREGEGQRIVAVYIPGGVPEDTCRAAAAVLEPAATKKNLRALTNGGLPPDTGLVGYYDYLTNPTRHKCRETEFSRRNWGLLAQSEPLLKHLDKLYSQLAPMHHHLQKVAIPSQYQLCGTVFSTITVNRNFRTAVHTDKGDFRSGLGVLSVINGEFEGCHLAIKKLKKAFQLKVGDVLLFDTSLEHGNTEVINPEIHWQRTSIVCYLRTGLMSSVCEMERRKHLNRLILQQLRNTEVLNTTVNINGADSSLPPLFVPTRLASHLAPVQLAALGFIVERTEKQSGCVVAMTMGLGKTLVALTLCFSQLHLAPQADILILTPKPIISHWVDEKNKWAMHGLHFPHFVASDGLNSLEFEQQLLEYERQKNNEKPKLGHVFVINGEYLAGFLRRFKRFTPLLIIVDEGHRVAAKGNKLTESLDRLRCNLRIVLSGTPLQNDASELYRLVGWVNKGVGRVLPPKRFQELANDINQFVEGDDGAFYNAVMAQEYIQDWMRGFVFREMENDLPPLHDYLLICGSSDVQREYEEKLGLTETTMTALKATEHRPHHLSTHPACYLAFISDSYQSMVSGWTVRAQANTSRMRVSQLEEIDTMRLEHYVQMVENEQLDTFIDLSGKMRVLVDIVLRVQARKEKLIIFSLYVGSQDLIHRTLTALRVCTFTVRGRDSQDRRRRAMQEFSENKDLIVLVLSTKIAAYGLDFTAANHVVLFDSWWNPQVDAQAIARAYRRNQRKPVTVYRLISATENKFVLSSQTRKIALFKCILHERTSRQALPDELEDCAANEKDEERRSFWAKLKTTLLAGGTRALLNVYRYQESVRESE | Dioxygenase that catalyzes the first step of DNA base J (beta-d-glucosyl-HOMedU) biosynthesis by converting thymine to 5-hydroxymethyluracil (HOMedU). DNA base J is a hypermodified thymidine residue found in the genome of kinetoplastid parasites, which is localized primarily to repetitive DNA, namely the telomeres, and is implicated in the regulation of antigenic variation. Probably also acts as a DNA helicase. Recognizes and binds specific regions of the genome, hydrolyzes ATP and allows the DNA base J de novo synthesis. Involved in initial synthesis of DNA base J, JBP1 being able to act via the basal level of DNA base J and propagate further synthesis. In contrast to JBP1, it does not specifically bind DNA base J, however it binds chromatin. |
B6EUA9 | PR40A_ARATH | Pre-mRNA-processing protein 40A (AtPRP40a) | MANNPPQSSGTQFRPMVPGQQGQHFVPAASQPFHPYGHVPPNVQSQPPQYSQPIQQQQLFPVRPGQPVHITSSSQAVSVPYIQTNKILTSGSTQPQPNAPPMTGFATSGPPFSSPYTFVPSSYPQQQPTSLVQPNSQMHVAGVPPAANTWPVPVNQSTSLVSPVQQTGQQTPVAVSTDPGNLTPQSASDWQEHTSADGRKYYYNKRTKQSNWEKPLELMTPLERADASTVWKEFTTPEGKKYYYNKVTKESKWTIPEDLKLAREQAQLASEKTSLSEAGSTPLSHHAASSSDLAVSTVTSVVPSTSSALTGHSSSPIQAGLAVPVTRPPSVAPVTPTSGAISDTEATTIKGDNLSSRGADDSNDGATAQNNEAENKEMSVNGKANLSPAGDKANVEEPMVYATKQEAKAAFKSLLESVNVHSDWTWEQTLKEIVHDKRYGALRTLGERKQAFNEYLGQRKKVEAEERRRRQKKAREEFVKMLEECEELSSSLKWSKAMSLFENDQRFKAVDRPRDREDLFDNYIVELERKEREKAAEEHRQYMADYRKFLETCDYIKAGTQWRKIQDRLEDDDRCSCLEKIDRLIGFEEYILDLEKEEEELKRVEKEHVRRAERKNRDAFRTLLEEHVAAGILTAKTYWLDYCIELKDLPQYQAVASNTSGSTPKDLFEDVTEELEKQYHEDKSYVKDAMKSRKISMVSSWLFEDFKSAISEDLSTQQISDINLKLIYDDLVGRVKEKEEKEARKLQRLAEEFTNLLHTFKEITVASNWEDSKQLVEESQEYRSIGDESVSQGLFEEYITSLQEKAKEKERKRDEEKVRKEKERDEKEKRKDKDKERREKEREREKEKGKERSKREESDGETAMDVSEGHKDEKRKGKDRDRKHRRRHHNNSDEDVSSDRDDRDESKKSSRKHGNDRKKSRKHANSPESESENRHKRQKKESSRRSGNDELEDGEVGE | Binds the phosphorylated C-terminal domain (CTD) of the largest subunit of RNA polymerase II and functions as a scaffold for RNA processing machineries (Probable). May be involved in pre-mRNA splicing (Probable). |
B6EUB3 | PDS5A_ARATH | Sister chromatid cohesion protein PDS5 homolog A (Precocious dissociation of sisters protein 5-A) (AtPDS5A) (PDS5) | MAQKPEEQLKELGSKLDLAPVSKDSLLKLLKEAAVCLSELEQSPPPAVLKSIQPFLDAVIKPEILNHQDKDVKLLVASCVSEITRITAPEAPYSDNIMKDIFQLIVSAFAGLNDVSGPSFGRRVLILETVAKYRSCVVMLDLECDDLVKEVFTTFLDVARDDHPEIVFSSMQNIMIVLLEESEDVQEHLLLILLSKLGRNRSDVRDAARRLAMKVIEHCAPKVESDIKQFLISSMSGDSRFSSSQIDYHEVIYDLYRCAPQALSGVAPYLTGELLADKLETRLKVVGLVGELFSLPGRVISEEFDSIFLEFLKRLTDRVVEVRMAILDHIKDCLLSDPLRAEASQIISALCDRLLDYDENIRKQVVAVICDVSVSALTSIPVDTMKLVAERLRDKAILVKTYTMERLTELFRVYCLRCADGKVDTGDFNWIPGKILRCLYDKDFRSDTIEYILCSSLFPSDFSVRDKVKHWIQIFSGFDKVETKAFEKILEQRQRIQQEMQRYLSIKQTQQTADAPEIQKKILFGFRVMSRAFSDPPKTEQNFLILDQLKDANIWKILTNLLDPNTSITQASRIRDDMLKILSEKHSLYDFLSTLSIKCSYLLFSKEYVKEILAEVSVRKSSKNTLGIQPCMDFLGLLACFCPSLFDGAEEELISFLKDDDEMMKEGTLKILAKAGGTIRENLIVLASSVDLLLERICVEGNRKQAKYAVHALASITKDDGLKSLSVLYKRLVDMLEDKRYQPAVLQCLGCIAQIAMPVYETRESEVVEFIRSKILKLKSETVDDKKLSWDDKSEICQLKIYGIKTLVKSYLPFKDAQLRAGVDDLLGILKNILSFGEVSEDLESSSVDKAHLRLAAAKAVLRLSRHWDDKIPIEIFHLTLKTPEIPFPTAKKIFLGKVHQYVKDRVLEMKYACSFLFDITGSNVLESEEDKHNLADIIQHSYQTKVRKISAQTDANSVTLYPHHILPYLVHALAHHSCPDVEKCKDVKEYEMIYRQLYLIISMLLHKEEDGKTEDIDKEREYVPTIILIFHSIKQSEDVTDATKSKNSHAICELGLSIINHLTQKEPDLQGEITPVSLPPTLYKPSEKVEGDKSQVGEEKLWLADETVLLHFRALKLESHADASVIPQTSENEVMIDGESDGNEIPLGKIVERLRAQGTKTRKGKKNKSVPAEDENGKNDVDVLKMVREINLDHLQMLDKFESSNGHKHSPSERAEICQRDQKGNKRNVGDATSVVSVPKRRRSSSGHSPYKFSNSGPKVQLKASEDELHLESDMDKNVSLDSHDENSDQEKMLESISPRKRKKSLSSKLKITESDWALTDVERSRSAGGGDSKLKSASGSMKKRKNVSGLAKCSTKENKLVNDELIGCRIEVWWPMDKRFYEGTVKSYDSTKQRHVILYEDGDVEVLNLKKEQWELIDTGGKTAKKSRTSKGNSKKKRSSGSKPKNPDGVQRDEDPVTTTPKGKRTPKKNLKQLHPKDTPKSLSLEHEKVESRNKKRRSSALPKTEYSGEAGEEKSESEGKSLKEGEDDEEVVNKEEDLQEAKTESSGDAEGKEAEHDDSDTEGKQENNEMEREAEENAETSDNETLGAWKSKVGKSISRTAI | Cohesin cofactor dispensable during the meiotic division but playing an important role in DNA repair by homologous recombination (HR) probably by helping SMC5/SMC6 complex. Regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin. May couple sister chromatid cohesion during mitosis to DNA replication (By similarity). Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. |
B6F209 | CPAS_ASPOZ | Cyclo-acetoacetyl-L-tryptophan synthase (EC 2.3.1.-) (Cyclopiazonic acid biosynthesis cluster protein A) (Polyketide synthase-nonribosomal peptide synthetase cpaA) (PKS-NRPS cpaA) | MKTPIAVVGTACRFPGDISSPSQLWELLSNPKDVLRDLNPKRLNLTGFNHHNAEHHGATNVPNKSYILDDDVYRFDAAFFNISAAEAEAMDPQQRLLLETTYEALESAGYTLKQMRGSSTSVFIGAMTSDYHDIQARDLDTISRWHATGTSPSILSNRISYFFDLKGPSMTVNTACSSSLVALHQAVQSLRNGDCTAAIVGGVNLLLDPEVYISHSNLHMLSPTSRCRMWDRDADGYARGEGCTSIMIKTLDQALKDGDDVECIIRETAVNSDGRSAGITMPSPEAQATLIRETYERSGLDPVRDRCQYFECHGTGTQAGDPVEAQAIQQTFYPKNAVFSPDDKLYVGSIKTLIGHLEGCAGLAGVMKAIMCLKNRTITPNMFFDNLNPNISPFYDHLRIPTNTVPWPPVAHGCPLRASVNSFGFGGTNAHAIIESYVPSQPKRQASYCKESNRQKYTNSGPFVFSAHTQESLYSNIERTARYVRSNEALDLGHLAWTLAKRTVLPFKVAITALSREELLGNIDKAIVEYKASKASAQGPSPWKHPPEPHRIMGIFTGQGAQWAGMGRELLLASTVFRKSIERCEHALATLHDGPSWSLQEELLADKPSSRLSNPAISQPVTTAIEIAAYDLLCTSGVNVDVVVGHSSGEIVAAYALSIISAEDAMKIAYYRGLHTKPARSGRMLAVSLSFHDARELCSWPSFSGRVVVAASNGPASTTLSGDYDAILEVKALLDRKKTFARTLQVDVAYHSHHMVPCSAAYLESLRACNIQVKSPRSGCTWISSVTGRNAILDGDIQSFSATYWVDNMVKPVLFSQALDKSLCGTQDLGVCIEFGPHPALRGPVLDTLKSKGTSSVHYTSLLRRGQNDLNAASSAVGYLWERMADRVDLASFLQGFRSQALQLIKGLPGYSWDHGRRYWRESRISRRYRLEGTQLHPLLGRRSADEFPNEFCWKNMLHLKEMPWAQGYKEEGRVVLSAAFYLCSLLSAASSAAVCQRLVVLELNNFVVMEPITLEEYGNGVEYITTIRFDNEDFRTISSTILHAEASCHACKSDESVLTKVCTARLTLHLGDARGPDCDCLPPRGQRNDLLAPVDVADLYDSFEQAGMSYTGPFRSITSIQRSLGEATASVAWAVDTTMPESVLNPAMVEASFQAIMCAFASPLTEELRTPFHAKEIRRVLVTPRLALGGVSCDIDAFVTGVDCGGVEGDVSLYKPDGNAMIQIEGLVMKSVPQPDTSSDRNLFSHVVWESDPFGYSLISYPTPNEDMGWKRAADIVALYHLRRTVEEIDPLESAGFTPHHQLLYREISHIAAAGRGSEYYITHPDCAQTSEEIILAMIDKYAGIVDLQSLHSFGKALPAILRGELDLHNTPNEPDTLEGFTHDAAMFSQLSKDICSIVRRIVHKHPHMNVLGLDPGPSVITHQILEALDDKHTSYCLGSADPVILNKTLARLSAQHRNLYSKVIDLTTVNAGEHGSDKYDMVIAANPLHGTDTSANLFEVCRAMLKPGGYLVFVRVTGRVSMSLLCTCGWLPQWWQGYDQDARSWTDMSTVRYDSHLRSKGFSGIDHIFHDSMNSNGDGLSVMVTQAVNDTVMMLREPMNSTGLAPLTETVVFVGGKTLSVARLLQSIRRIVAASGTATTVVEDIDRLEMNGLTKQHSIISLVELDEPFFSRGAFHERLLAFKELVARSKHVLWLTTRNMTSISVAIGRAMRSERGADISLQFLGLSTVANISPSAVVEVFLRLTWSFVPVLTDGEVLWTNEPELQWDGSTLRIPRLVWDHKRNKRYNYRHRQGRPEAGLPQTAVPLSPRVSTNSVAVQIKYSCLVCTDVYLWVGARIDGQGNVVGISDHVSFVIHARLDHVHNLSDEHDLSPDALRATASFTLAYLLIKSLSGPILLYEPDELLAAAVEQDREPEQTVYFVTSKYNDCSRGWITVHPHASRRMVERMLPRKVSAFVDLSSSDDHVVTTLRDIYSHARIQAVELYRRAFAASPGQLIADSYTQACTSLSILSHTALEVTSSTEASTNIASVAYPKVVNWTSPAPIASPGDMISATTMFSSSGTYFMIDMATPLGLSILKWMATNGARKFVLAGRNPRMHEAWLEEMSRLGATVKPLKMDVSNKESILSAFTQIKEALPPIVGVCYAPLALSDQGFEYTVEDAGGLAATAMINAAKYLDELFPTPTLDFFVILTSLVSVIGTPKQVAYHAPSLFMTDLIQRRRLRGLVGSVMALGMVVDAGYFSRQGKEVIQRMMHHGYAPLSESDLHHAFGEVVAAGVPEAEGNAEIFFGLQLIDSQIDQSRESTSVSNHLLSHFITSRSGTKEGQYAEQEDSPSLLVPDEQLQESGPGRNKYDDLLARLSGKVRSILRLGDQALDVHTPLLDLGCDSLLAVDIQAWVAKEFDIDITPMDALLDTVAGLCEKAVPKPNAPGFVVEKEEQLVKELDFIDVATTASRSEHSSSVQDIPLDSTSSESSCVLCPSDSGFEQVRNDLEPRFTRIEKMSPHQSQIWFAGHWMRDPTQYNVVISYNVEGRFPVDRFKEALEHAVSMHESLRTAFFSDPNNGDLLQGVLKVPPPFLEHVRTPSAASVSQEFDKLASYQWRLEDGEVMRVTVVSIGKDQHTVIFGYHHIVMDGASWSTFLHDLKCIYEQRPRREVAQYVDYSLMLNRDIHNGTFAKELEFWKSELLPPPEMMPVLPLAKEKTRIPTDNFKVHTSTRHISIEATERIKQASRSLRGTPFHFYLATLQVFLAGLLKIESLCIGMSDANRKHQQFTGTVGYFLNMLPLRFEVQQTDSFANVFQKTSSKVLTALLNSSIPSNLVVDALNIPRVSNVTPLFQVAINYRVGEITRMSVDDFALNYDRSVMGNAPYDISFHVTPCANGTSIVEVNCRDYLYSPKATERIIDEYVRLLEIMSSNPLISVQSSVATSAPINEDGLSVQRGPRISHGWPATLPERFQDMVDQYGDRIAITDQGRDFSYLQLQAQSTRIGEALLQKGVRSGDTVAVLCPPSMNSVASMLAILRISAVYVPLDLSLPAARHKAMILASPVRALVCVSSTVEKVLELGVSTILNLSEIPDIRAPSTRFTNSAKGDSLAILLYTSGSTGQPKGVCLPQSGFINYLAAKRKELGLDSSTVVLQQSSLGFDMGLAQTLNAIMNGGKLVIVPQELRGDSIEIARIIRDQKVTFTLATPSEYLVMLQHGREYLHNYAGWRHACLGGEPFTDQLKREFVRLGKNCPVVQDSYGVTEISACTTFETMTASQLEEARSVGRTIPNTSLYIVDADCNLVATGEPGEICISGAGVALGYLNEEQTRLKFVQDPFALPDDIARGWTRVYRTGDKAKLLDDGSLILLGRMDGNTEVKVRGLRIDLEDVASTMVNCHPDLLSSAIVCVKGQGVSETLVAFVAMMPGQTASDVELQHLACNLPLPQYMRPSTVICLDELPRNANGKIDRKRIDAMPWTAPTTLSQSSKRLTLGEGELKLLWQVLLPGKHIQPESDFFLLGGNSTLLVRLQGAIRTSIGVSLTLREMYGASTLAQMALKVDARKAESPSMTINWLAETAIPQHILDRASSTSNLNLPKHCQGSGCQILLTGSTSFLGRVLVQLLLQVPEVERVHCIAVEKEQEHVPPTSDKVSLYYGSLLDPNLGLSTAEWASLQDRVDVVIHNGSNGHCLNTYNSLKGPNLGSTHRLAEFALQSQVPLHYISSGRVILQSGQTALGPTSVSFHPPPLDGSDGLTATKWAGEVFLERLAEHTDISISIHRPCTPIGDQAPAQDALNSLLRYSVNLGATPRLTRMEGYLDFQKVEIIAEEIATLVTSRFTKRSNTSSFTTRGVSFFHHSSNIKVPVKSFKEYMEKVHGRPFQELNLREWSSLALEQGIEPLIPSFLEAVDDNEETLRYPYLGN | Hybrid PKS-NRPS synthetase part of the gene cluster that mediates the biosynthesis of the fungal neurotoxin cyclopiazonic acid (CPA), a nanomolar inhibitor of Ca(2+)-ATPase with a unique pentacyclic indole tetramic acid scaffold. The hybrid two module polyketide synthase-nonribosomal peptide synthetase (PKS-NRPS) cpaS incorporates acetyl-CoA, malonyl-CoA, and tryptophan (Trp) and utilizes a C-terminal redox-incompetent reductase domain to make and release the tryptophan tetramic acid, cyclo-acetoacetyl-L-tryptophan (c-AATrp), as the first intermediate in the pathway. CpaS catalyzes a Dieckmann-type cyclization on the N-acetoacetyl-Trp intermediate bound in thioester linkage to the phosphopantetheinyl arm of the T domain to form and release c-AATrp. CpaD then regiospecifically dimethylallylates c-AATrp to form beta-cyclopiazonic acid. CpaD discriminates against free Trp but accepts tryptophan-containing thiohydantoins, diketopiperazines, and linear peptides as substrates for C4-prenylation and also acts as regiospecific O-dimethylallyltransferase (DMAT) on a tyrosine-derived tetramic acid. The beta-cyclopiazonate dehydrogenase cpaO then carries out the dehydrogenation of beta-CPA to yield an unstable enimine product, which is captured by intramolecular cyclization to create the pentacyclic fused scaffold of alpha-cyclopiazonate. Finally, the cytochrome P450 monooxygenase cpaH mediates the conversion of CPA into the less toxic 2-oxocyclopiazonic acid, the end product of the CPA pathway in A.oryza. |
B6HAA7 | ARO1_PENRW | Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)] | MSEPTKISILGRESIVADFGLWRNFVAKDLISDLSSTTYVLVTDTNLGSLYTPTFQKTFEAAAASITPAPRLLIHHVAPGESSKSRQTKADIEDWMLSQNPPCGRDTVIIALGGGVIGDLIGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGSIWQPSRIYIDLEFLETLPVREFINGMAEVIKTAAISSEEEFTALEDNADLILAAVRSEPKAGQGRFGGIRDILKARILASARHKAFVVSADEREGGLRNLLNWGHSIGHAIEAILTPQILHGECVAIGMVKEAELARHLGILKGVAVARVVKCISAYGLPTSMKDARVRKLTAGKHCSVDQLLFNMALDKKNDGPKKKVVLLSAIGRTHEPKASVVSNDDIGVVLAPSVEVHPGVPKSLNVTCAPPGSKSISNRALVLAALGSGTCRVKNLLHSDDTEVMLNALERLGAATFSWEEEGEVLVVNGKGGKIIASPTPLYLGNAGTASRFLTTVATLATPSSVDSSVLTGNNRMKQRPIGDLVDALTVNGAGVEYMESKGCLPLKIAASGGFAGGKINLAAKVSSQYVSSLLMCAPYAKEPVTLKLVGGKPISQPYIDMTTAMMRSFGIDVKKSTTEEHTYHIPQGHYVNPAEYIVESDASSATYPLAIAAVTGTTCTVPNIGSKSLQGDARFAVDVLRPMGCSVVQTDTSTTVTGPTDGVLQPLPDVDMEPMTDAFLTASVLAAVAQGKGANHTTRIYGIANQRVKECNRIKAMKDELAKFGVICREHDDGLEIDGIERSSLRQPSGGVFCYDDHRVAFSFSVLSLIAPQSTLILEKECVGKTWPGWWDALKQMFSVNLNGKELAEAEHAASSDEKRSSASVFIIGMRGAGKTTTGNWVAKALDRRFIDLDTELETSEGMTIPDIIKTRGWEGFRDAELAVLKRVLKDHPTGYVFACGGGVVEMPEARKLLTDYHKSKGNVLLIMRDIKLVMDFLQIDKTRPAYVEDMMGVWLRRKPWFQECSNIQYYSQHSTSTELALASEDFTRFMRVVTGQVDSLSLIKKKKHSFFVSLTLPDVEPSGDIITEACVGSDAVELRVDLLKDPAVDGDIPSIDYVNEQMSLLRRRTTLPVIFTIRTKSQGGRFPDDAHDAAMQLYRLAFRCGCEFVDLEIAFPDAMLRAVTEMKGYSKIIASHHDPKGTLSWANMSWIPSYNRALEYGDVIKLVGVANTLDDNNALRKFKTWAEEAHDVPLIAINMGDSGQLSRILNGFMTPVSHPSLPFKAAPGQLSAAEIRRGLSLMGEIKAQKFAIFGSPVSGSRSPALHNTLFAKMGLPHDYSRLETTKVEDVKDFIRAPDFGGASVTIPLKLDIMPLLDEVAQEAEIIGAVNTIVRVSNGNNPPRLIGYNTDWQGMIRCMRNAGVYGSTGSQSAVVIGGGGTARAAIFALHNMGFSPIYVVGRTASKLESMVSTFPTNYNIRVVDNRAQLDTVPQVAIGTIPADRPIDPVMRETLCHMFERAQEIDGTLIGKSSDTSKHRVLLEMAYKPAVTALMQLASDAGWSTIPGLEVLVGQGVHQFVHWTGITPLYHEARVSKHLDYFLSF | The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. |
B6HLU1 | ACVA_PENRW | N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase (ACV synthetase) (ACVS) (EC 6.3.2.26) (Delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) (Nonribosomal peptide synthetase acvA) (Penicillin biosynthetis cluster protein acvA) | MGPSNPAMAYFKPSTRDTMDPCSGNAADGSIRVRFRGGIERWKECVNQVPERCDLSGLTTDSTRYQLASTGFGDASAAYQERLMTVPVDVHAALQELCLERRVSVGSVINFSVHQMLKGFGNGTHTITASLHREQNLQNSSPSWVVSPTIVTHENRDGWSVAQAVESIEAGRGSEKESVTAIDSGSSLVKMGLFDLLVSFVDADDARIPCFDFPLAVIVRECDANLSLTLRFSDCLFNEETICNFTDALNILLAEAVIGRVTPVADIELLSAEQKQQLEEWNNTDGEYPSSKRLHHLIEEVVERHEDKIAVVCDERELTYGELNAQGNSLARYLRSIGILPEQLVALFLDKSEKLIVTILGVWKSGAAYVPIDPTYPDERVRFVLDDTKARAIIASNQHVERLQREVIGDRNLCIIRLEPLLASLAQDSSKFPAHNLDDLPLTSQQLAYVTYTSGTTGFPKGIFKQHTNVVNSITDLSARYGVAGQHHEAILLFSACVFEPFVRQTLMALVNGHLLAVINDVEKYDADTLLPFIRRHSITYLNGTASVLQEYDFSDCPSLNRIILVGENLTEARYLALRQRFKNRILNEYGFTESAFVTALKIFDPESTRKDTSLGRPVRNVKCYILNPSLKRVPIGATGELHIGGLGISKGYLNRPELTPHRFIPNPFQTDCEKQLGINSLMYKTGDLARWLPNGEVEYLGRADFQIKLRGIRIEPGEIETMLAMYPRVRTSLVVSKKLRNGPEETTNEHLVGYYVCDSASVSEADLLSFLEKKLPRYMIPTRLVQLSQIPVNVNGKADLRALPAVDISNSTEVRSDLRGDTEIALGEIWADVLGARQRSVSRNDNFFRLGGHSITCIQLIARIRQRLSVSISVEDVFATRTLERMADLLQNKQQEKCDKPHEAPTELLEENAATDNIYLANSLQQGFVYHYLKSMEQSDAYVMQSVLRYNTTLSPDLFQRAWKHAQQSFPALRLRFSWEKEVFQLLDQDPPLDWRFLYFTDVAAGAVEDRKLEDLRRQDLTERFKLDVGRLFRVYLIKHSENRFTCLFSCHHAILDGWSLPLLFEKVHETYLQLLHGDNLTSSMDDPYTRTQRYLHAHREDHLDFWAGVVQKINERCDMNALLNERSRYKVQLADYDQVQEQRQLTIALSGDAWLADLRQTCSAQGITLHSILQFVWHAVLHAYGGGTHTITGTTISGRNLPILGIERAVGPYINTLPLVLDHSTFKDKTIMEAIEDVQAKVNVMNSRGNVELGRLHKTDLKHGLFDSLFVLENYPNLDKSRTLEHQTELGYSIEGGTEKLNYPLAVIAREVETTGGFTVSICYASELFEEVMISELLHMVQDTLMQVARGLNEPVGSLEYLSSIQLEQLAAWNATEAEFPDTTLHEMFENEASQKPDKIAVVYEETSLTYRELNERANRMAHQLRSDVSPNPNEVIALVMDKSEHMIVNILAVWKSGGAYVPIDPGYPNDRIQYILEDTQALAVIADSCYLPRIKGMAASGTLLYPSVLPANPDSKWSVSNPSPLSRSTDLAYIIYTSGTTGRPKGVTVEHHGVVNLQVSLSKVFGLRDTDDEVILSFSNYVFDHFVEQMTDAILNGQTLLVLNDGMRGDKERLYRYIEKNRVTYLSGTPSVVSMYEFSRFKDHLRRVDCVGEAFSEPVFDKIRETFHGLVINGYGPTEVSITTHKRLYPFPERRMDKSIGQQVHNSTSYVLNEDMKRTPIGSVGELYLGGEGVVRGYHNRADVTAERFIPNPFQSEEDKREGRNSRLYKTGDLVRWIPGSSGEVEYLGRNDFQVKIRGLRIELGEIEAILSSYHGIKQSVVIAKDCREGAQKFLVGYYVADAALPSAAIRRFMQSRLPGYMVPSRLILVSKFPVTPSGKLDTKALPPAEEESEIDVVPPRSEIERSLCDIWAELLEMHPEEIGIYSDFFSLGGDSLKSTKLSFMIHESFNRAVSVSALFCHRTVEAQTHLILNDAADVHEITPIDCNDTQMIPVSRAQERLLFIHEFENGSNAYNIDAAFELPGSVDASLLEQALRGNLARHEALRTLLVKDHATGIYLQKVLSPDEAQGMFSVNVDTAKQVERLDQEIASLSQHVFRLDDELPWEARILKLESGGLYLILAFHHTCFDAWSLKVFEQELRALYAALQKTKSAANLPALKAQYKEYALYHRRQLSGDRMRNLSDFWLRKLIGLEPLQLITDRPRPVQFKYDGDDLSIELSKKETENLRGVAKRCKSSLYVVLVSVYCVMLASYANQSDVSVGIPVSHRTHPQFQSVIGFFVNLVVLRVDISQSAICGLIRRVMKELVDAQLHQDMPFQEVTKLLQVDNDPSRHPLVQNVFNFESRANGEHDARSEDEGSLAFNQYRPVQPVDSVAKFDLNATVTELESGLRVNFNYATSLFNKSTIQGFLHTYEYLLRQLSELSAEGINEDTQLSLVRPTENGDLHLPLAQSPLATTAEEQKVASLNQAFEREAFLAAEKIAVVQGDRALSYADLNGQANQLARYIQSVSCIGADDGIALMLEKSIDTIICILAIWKAGAAYVPLDPTYPPGRVQLILEEIKAKAVLVHSSHASKCERHGAKVIAVDSPAIETAVSQQSAADLPTIASLGNLAYIIFTSGTSGKPKGVLVEQKAVLLLRDALRERYFGRDCTKHHGVLFLSNYVFDFSVEQLVLSVLSGHKLIVPPAEFVADDEFYRMASTHGLSYLSGTPSLLQKIDLARLDHLQVVTAAGEELHATQYEKMRRRFNGPIYNAYGVTETTVYNIIAEFTTNSIFENALREVLPGTRAYVLNAALQPVPFDAVGELYLAGDSVTRGYLNQPLLTDQRFIPNPFCKEEDIAMGRFARLYKTGDLVRSRFNRQQQPQLEYLGRGDLQIKMRGYRIEISEVQNVLTSSPGVREGAVVAKYENNDTYSRTAHSLVGYYTTDNETVSEADILTFMKARLPTYMVPSHLCCLEGALPVTINGKLDVRRLPEIINDSAQSSYSPPRNIIEAKMCRLWESALGMERCGIDDDLFKLGGDSITSLHLVAQIHNQVGCKITVRDIFEHRTARALHDHVFMKDSDRSNVTQFRTEQGPVIGEAPLLPIQDWFLSKALQHPMYWNHTFYVRTPELDVDSLSAAVRDLQQYHDVFRMRLKREEVGFVQSFAEDFSPAQLRVLNVKDVDGSAAVNEILDGWQSGFNLENGPIGSIGYLHGYEDRSARVWFSVHHMAIDTVSWQILVRDLQTLYRNGSLGSKGSSFRQWAEAIQNYKASDSERNHWNKLVMETASSISALPTSTGSRVRLSRSLSPEKTASLIQGGIDRQDVSVYDSLLTSVGLALQHIAPTGPSMVTIEGHGREEVDQTLDVSRTMGWFTTMYPFEIPRLSTENIVQGVVAVSERFRQVPARGVGYGTLYGYTQHPLPQVTVNYLGQLARKQSKPKEWVLAVGDNEFEYGLMTSPEDKDRSSSAVDVTAVCIDGTMIIDVDSAWSLEESEQFISSIEEGLNKILDGRASQQTSRFPDVPQPAETYTPYFEYLEPPRQGPTLFLLPPGEGGAESYFNNIVKRLRQTNMVVFNNYYLHSKRLRTFEELAEMYLDQVRGIQPHGPYHFIGWSFGGILAMEMSRRLVASDEKIGFLGIIDTYFNVRGATRTIGLGDTEILDPIHHIYNPDPANFQRLPSATDRIVLFKAMRPNNKYESENQRRLYEYYDGTRLNGLDSLLPSDSDVQLVPLTDDTHFSWVGNPQQVEQMCATIKEHLARY | Nonribosomal peptide synthetase part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic. The first step of the pathway is performed by the trimodular NRPS acvA that produces the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine (LLD-ACV or ACV) via condensation of the 3 residues L-2-aminoadipate, L-cysteine and L-valine. The precursor amino acids for penicillin biosynthesis are withdrawn from the vacuolar amino acid pool by the MFS-type transporter penV. Each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. The tripeptide ACV is then cyclized to form isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus. Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase aatA to yield penicillin. This step occurs in the peroxisomal matrix and the penM and paaT transporters are involved in the isopenicillin N and phenylacetic acid import into the peroxisome, respectively. |
B6I112 | HCHA_ECOSE | Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase) | MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDIAGRVHKDRKVLTGDSPFAANALGKLAAQEMLAAYAG | Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}. |
B6JVD0 | ARO1_SCHJY | Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)] | MSQDTDVVSVPILGKEAVFVGFNLERRVCDFLIENAKSSAYVIVTDTNIAPHYLEKYTTALSEAAKRHGVAPRILTRVIPPGETSKCRSMKAEIEDWMLSQSCTRDTVLVAMGGGVIGDMAGYVAATFMRGIRFIQLPTTLLAMVDSSIGGKTAIDTPNGKNLVGAFWQPLAVFADLNFLETLEPRQFINGMGEVIKTAAMWNEKDFCLLEQNPTVILEAVHRPRVPGQFKFENIRNLLQKIILASVRTKCEVVTLDEREGGLRNLLNFGHSIGHAYEAILFPQILHGECVSIGMVKELELSRYLGILKPNAVGRVTKCLMSYTLPVSVHDAHIKKYAGYKKCPVDKLIRIMAVDKKNQGLQKRVVILKAVGETYEKHATVVSDEDIRVVLSHDIQVSPFDNSVSDVVVTPPGSKSISNRALILAAMAKGTTKLTNMLHSDDTQVMMAALEELGAATFSWEDNGETLVVNGGGKFKTPSKELYLSNAGTAARFLTTVAALVGENEQGGEVVLTGNHRMKVRPIGPLVDALRANGCSISYLEREGSLPLKMIPQNGLRGGVIELAATVSSQYVSSILMCAPYAQEPVTLKLVGGKPISQLYVDMTIAMMKGFGVNVVKSETEAYTYHIPKANYTSPGDYEIESDASSATYPLAFAAITGTKCTVPNIGSASLQGDARFARDVLAPMGCTVEQTPTSTTVQGPPMGQLKPLESVDMETMTDAFLTATALAAVACNSSGNEHITRITGIANQRVKECNRIAAMVHELAKFGVKAGELEDGIFIHGQSYKDLKTPEEGIYTYDDHRVAMAFSILTLVTPKPTVILDKACVVKTWPYWWDVLRNSFKIKLAGVESKETVKSVKLTRSRASVILIGMRGAGKTTIGSIIAGQLNMKFLDLDQELEKKLNTTIPDLVNTRGWDDFRQEELQVLQEFIDTKSSDFVAACGGGIVETPAARELLCKYVKEGGIVLHIHRNLDQVLSYLSIDKSRPAYADRESTKNVYLRRHQWYLDCRSHDFVSPTIESGNVQSKLETSMSRFLRVVTGKSTWFEKAIQKPHSFFLSLTFPNINDAISFLPEAIIGCDAVELRADLLEDPNSTTGYPSVEFVAEQFATLRAAIDLPIIFTVRSKDQGGRFPNANESEAVELMLAALRWGVDVLDLELGWSTESLQAIYARKENTKIITSWHDTAQRCSWAQPDEWLQKLDMATAFGDVVKFVGIAKSMQDNFDLEKFRKSFKGYTNKPLIAINMGTVGQLSRVFNNVLTPVTSPALPYKAAPGQLSVRQIITALSLMGSISPKKFYLFGTPIQHSKSPILHKTCYDLTGLPYTYDLFETESVEGVKDVLSQPDFGGANVTIPYKLDILQYLDELSDEARFLGAVNTVVPISENGKRKLRGDNTDWRGIVRTFVRAGANNLNGKNALVIGAGGTSRAAIFAMHKLGAKNIYLLNRTLVNAEKVKAVFPEEYNVKVIDHTKQSEISEWTKLQVAAVVSTVPADRPLPESVSKVIDALLSEIPAQKKEQYVFLDMAYKPLNTPLMSVASKHGYTCINGLEVLLQQGLASFEIWTGLAVPFEHVFGLYMVLCAKEHN | The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. |
B6KAM0 | AMA1_TOXGV | Apical membrane antigen 1 (TgAMA-1) (TgAMA1) [Cleaved into: Apical membrane antigen 1, soluble form] | MICSIMGGLRSLRAARPYSHQSNTETKHMGLVGVASLLVLVADCTIFASGLSSSTRSRESQTLSASTSGNPFQANVEMKTFMERFNLTHHHQSGIYVDLGQDKEVDGTLYREPAGLCPIWGKHIELQQPDRPPYRNNFLEDVPTEKEYKQSGNPLPGGFNLNFVTPSGQRISPFPMELLEKNSNIKASTDLGRCAEFAFKTVAMDKNNKATKYRYPFVYDSKKRLCHILYVSMQLMEGKKYCSVKGEPPDLTWYCFKPRKSVTENHHLIYGSAYVGENPDAFISKCPNQALRGYRFGVWKKGRCLDYTELTDTVIERVESKAQCWVKTFENDGVASDQPHTYPLTSQASWNDWWPLHQSDQPHSGGVGRNYGFYYVDTTGEGKCALSDQVPDCLVSDSAAVSYTAAGSLSEETPNFIIPSNPSVTPPTPETALQCTADKFPDSFGACDVQACKRQKTSCVGGQIQSTSVDCTADEQNECGSNTALIAGLAVGGVLLLALLGGGCYFAKRLDRNKGVQAAHHEHEFQSDRGARKKRPSDLMQEAEPSFWDEAEENIEQDGETHVMVEGDY | Essential microneme protein that plays an important role in host cell invasion. Part of the moving junction (MJ) complex, a ringlike structure formed between the plasma membranes of the apical tip of the parasite and the target host cell. During invasion, the MJ migrates from the anterior to the posterior of the parasite, leading to internalization of the parasite into a parasitophorous vacuole (PV). |
B6KV60 | RON2_TOXGM | Rhoptry neck protein 2 (145 kDa AMA1-associated protein) (AAP145) | MTKRAGLPLGRAFLVLILLSAADSLFFSSFPRSALQLFSSVLFTDAAEPDSDATPGLRPQPSPRTFRPTGYQRIEVKTVDEELPEDLKVYTASTRGSSSRTFEVRNAGGRQEGFTLSVLTAGGPLPHGSWSWSGTPPEVQTTGGSQISFGWVPDTETPSLPERNLLQLKRMLRDEGLIEAVQLRAAEKGCPVAVLHNLRQLPVNFREVLHEEYESRSNPAKMYEVANSYVQQRGSDAARWSVSQSVELSLLEMHATSTTDPRGSSAVPSFLETGPQVRVAMTDAVPSGIRVYATPPAPRPVPVQSNQTEKERSPTSKRLVGMQLGLYLICKLAALFGHPTLFLNPYYTEQQLLEAVAQALGIAPPHRGDFENEGNEAQATANQHNGSADQLLAAIEIFRLGPNPYTIGHVLTLMIAYLDYESFFGASPSKPFHSWVSLAASAGNNTGFAMLDEMCDNHRGPKRRGQKHWYQTGGARKHKNRDMLPLHRQLCDALELVLNGVQQIQIDLMDELGKYKTGVEPLVDPATNSARIHTRTCRGLSPVCDYEATILAPVRALEPHEQQDSLRTKKAFNLVTGYGSGHVGQITGSIAEPFSHSWRTRWGKVVADPTAYGEIFERTLWFDDRELMAKSSGALFRQYDRIAKDSMSFGVFMNVENGLLKKDMRSKLEAYISQRKSFVEKRQQSRFAKLRKKIPENDPYALRAAIFLALNSRTFCAQPTSFLSSFRTFLTNQYHKLSQGRNLPRSQRSLMAFMRTGQVKFFQEWCSFDPLAVNALFLFRFAVSGTDPAALHDRQHTRVSRNKKTMRILNSKWTPAVLKKLMRKVNHKHMAREAKALLLRSLDPTVLSSIVTAFDFITHTQANLEVNQNAFMYHEVRAREVSRQSAAEKGSHRLHERGLVRETDDMIKRWAEHGIPGDIKRRLARGEKLPEGMSFGGIPIPNLTNWDAQLNSKWLEAYNAYLRHPYGRAALNARDPVALLVKDSRDRLQAEAEGTIFLGRIAKRVHQSKNLLRRAGRALKTFFLSLLRENERSEYAVWFGVKVDMRQVIQTCRQINSVAEVVKNDRLYDFITDGWMELVKDVVAGYTKASVRVPGFDTISAANEQLRKEGVAAATARNQGFLSIHYDYANLPEEERKKEFQRSMCMEQCEALWKLVMAFVMPNLQNPKKLKGYEKDFSGAKEIEKLNSPHHVNAFRFSLSVQIDFFDNMLDKTSKKNLKAMKFGASTWFTYAMKLAGQVNSEMGNPNLGTALYMQAAYYGNYIRKWMEQRRKSRKQAIIGVLTLGMMGLYALLNVADIVQHMEDIGGAPPVSCVTNEILGVTCAPQAIAKATTSAARVATQDFLKVGLFAGMAPYLMLPMAVVSVWNILKSEIKVLLQFEMALKHTFTRLKRWLAAPFKNWWAKRGRLKDALFRRASQTYRKTEQETKQPPRPRNLHNPSSWGDTELDSLGVPPEPFVQDFEIKYTTPVFPMSAPLIKA | Essential rhoptry neck protein that plays an important role in host cell invasion. Upon host invasion by tachyzoites, the protein is injected into the host cell where it functions as a receptor for apical membrane antigen 1 (AMA1) on the parasite. Part of the moving junction (MJ) complex, a ringlike structure formed between the plasma membranes of the apical tip of the parasite and the target host cell. During invasion, the MJ migrates from the anterior to the posterior of the parasite, leading to internalization of the parasite into a parasitophorous vacuole (PV). |
B6QCA7 | ARO12_TALMQ | Pentafunctional AROM polypeptide 2 [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)] | MAEPTKISILGRESIVAEYGIWGTYIVQDLLTNLPSTTYVLVTDTNLGSIYREKFAKVFNEAAAALSPAPRLLTKEIPPGENSKSRQGKADIEDWMLQQTCGRDTVIIALGGGVIGDLLGFVASTYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDIDFIDTLPEREFINGMAEVIKTAAISDEKEFAALEQHADAILKAARSKAGKGRFDSVRQVLKDRIVASARHKAYVVTADEREGGLRNLLNLGHSIGHAIEAILSPQVLHGECVAIGMVKELELARYLGILKPIAVSRMVKCLSKYGLPTSLKDARVRKHTAGKHCSLEQLMANMALDKKNDGPKKKVVLLSAIGKTYEPKASVVSNEDIRVVLAPSIEVIPGVPKNLNVVCAPPGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGAATFAWEDEGEVLVVNGNGGKMQASPTELYLGNAGTASRFLTSVATLSGKGSVDYNILTGNNRMKQRPIGDLVDALTVNGAQVEYLEKAGSLPLKIAASGGFKGGRINLAAKVSSQYVSSLLMCAPYAKEPVTLKLVGGKPISLSYIEMTTAMMRSFGIDVQKSTTEEWTYHIPQGSYTNPPEYVIESDASSATYPLAIAAVTGTTCTVPNIGSASLQGDARFAVEVLRPMGCNVEQTATSTTVTGPADGVLRPLPNVDMEPMTDAFLGASVLAAIAQGKGGNNTTRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGINRSSLRHPAGGVFCYDDHRVAFSFSILSLVAPTSTLILEKECVGKTWPTYWDALKQKFGVQLEGKELAESEVTHGSADRSNASIIIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWQGFRDAELSLFKRALAERPTGHVFACGGGIVEIAEARKILVDYHKNKGNVLLVMRDIKKVMEFLNIDKTRPAYIEDMMSVWLRRQPWYQECSNVQYYSRHSSSPELALAMDDFGRFIQFVSGQTDYLAAIRKKHLSFFVSLTLPDLRESGDLLRTVASGSDAVELRVDLLKDPSSDSVIPSAEYVAEQISFYRSRVSLPIVFTIRTVSQGGKFPDDAHDAALELIMLAIRSGCEFIDLEITFPEDLLRKVTESKAHAKIIASHHDPRGKLNWANGSWIQYYNKALQYGDIIKLVGVAETLKDNTSLKDFKDWAEQAHPDVPVIAINMGDKGQLSRMLNGFLTPVSHPALPFKAAPGQLSAAEIRRGLSIMGEIPAKKFAVLGKPVSASRSPPMHNTLFEQNGLPHVYTRLETDKAQDVKEFIRSPDFGGASVTIPLKLDIIPLIDEILNEAEIIGAVNTIIPVEGKDGSTRLVGRNTDWSGIVRCLREAGAHSNEGKSSALVIGGGGTARAAIYALHHMGFSTIYVLGRSPEKIQNMASTFPTGFDIRVLEHANDVESIPRVAVGTIPGDKPIESNIREILCTIFQRSGSAGDESGVLLEMAYKPSVTPLIQLASDYGWTTIPGLEALVGQGVYQFEYWTGITPVYEVARNAVLGTNETK | The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. |
B6QWH9 | ARO11_TALMQ | Pentafunctional AROM polypeptide 1 [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)] | MAEPTKISILGRESIVADCGIWGTYIVQDLLTNLPSTTYVLVTDTNLGSIYREKFAKIFNEAAAALSPAPRLLTKEIPPGENSKSRQGKADIEDWMLQQTCGRDTVIIALGGGVIGDLLGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDIDFIDTLPEREFINGMAEVIKTAAISDEKEFAALEQHADAILKAARSKPGKGRFDLVRQVVKDRIVASARHKAFVVTADEREGGLRNLLNLGHSIGHAIEAILSPQVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKCLSKYGLPTSLKDSRVRKHTAGKHCSLEQMMANMALDKKNDGPRKKVVLLSAIGQTYEPKASVVSNEDIRAVLAPSIEVIPGVPKDLNVVCAPPGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGAATFAWEDEGEVLVVNGNGGKMQASPTELYLGNAGTASRFLTSVATLSGKGSVDYNILTGNNRMKQRPIGDLVDALTINGAQVEYLEKAGSLPLKIAASGGFKGGRINLAAKVSSQYVSSLLMCAPYAKEPVTLKLVGGRPISLSYIEMTTAMMRSFGIDVQKSTTEEWTYHIPQGSYNNPPEYVIESDASSATYPLAIAAVTGTTCTVPNIGSASLQGDARFAVEVLRPMGCKVEQTATSTTVTGPADGVLRPLPNVDMEPMTDAFLGASVLAAIAQGEGGNHATRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGIDRSTLRHPAGGVFCYDDHRVAFSFSILSLVAPTPTLILEKECVGKTWPTYWDALKQKFGVSLKGKELAESEITHGPADRSDASIVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWKGFRDAELSLFKRALTERPTGHVFACGGGIVEIAEARNILIDYHKNKGNVLLVMRDIKKVMEFLNIDKTRPAYIEDMMSVWLRRKPWYQECSNVQYYSRHSSSPELALAMDDFDRFIQFVSGKTDYLAAIRRKRLSFFMSLTLTDLRDSGDLLRTVASGSDAVELRVDLLKDPSSGNGIPSAEYVAEQISFYRSRVSLPIVFTIRTVSQGGKFPNDAHDAALELIMLAIRSGCEFIDLEITFPEDLLRKVAESKAHAKIIASHHDPQGKLNWANGSWIQYYNKALQYGDIIKLVGVAETLKDNTALREFKDWAEQAHPDVPVIAINMGDKGQLSRMLNGFLTPVSHPALPFKAAPGQLSAAEIRKGLSIMGEIPAKKFAIFGKPVSVSRSPAMHNTLFEQNGLPYVYTRLETDQAQDVKEFIRSPDFGGASATIPLKLDIIPLIDEVLNEAEIIGAVNTIIPVEGKDGSTRLIGRNTDWSGIVRCLREAGAHSNEGESSALVIGGGGTARAAIYALHNMGFSTVYVLGRSPEKIQNMASTFPTGFDIRVLENASDIENIPRVAVGTIPGDRPIEANMREILCTIFERSGRAADGKSAAVLLEMAYKPSVTPLMQLASDSGWTTIPGLEALVGQGVYQFEYWTGITPVYEVARNAVLGTDETK | The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. |
B6RAL1 | PATM_PENEN | ABC transporter patM (Patulin biosynthesis cluster protein M) | MVDNYHSSLDVAKTPIQSDADAQKSEAETEGPSSKSSQIAAGESIADSVRNFLELRQGGIPDDTGVVFDKISAVGSGTGSQDAPTVTSAAQSAFGLLSPLQNRQRKQYSRPILSGFSGTINPGEMLLVLGKPGSGCTTFLKTLSGLWDEYKEIQGELTLGGHPLLDVMKQRPQDILFCAESDDHFPTLTVAETLRFATRARCGPQVSAREIDTMVTQLAKLVGLGNVLNTKVGDAKIRGVSGGERRRVSLAEALATCARLICLDNPTHGLDSSTAVEFMEMMREWTTQSRCVAAMSVYQASDAIVSYFDKVLIINSGRQIYYGPVRDAKAYFEDLGFECLSTTTVADFLNVMSADPDVRRAQENRENQVPRTAEEFERAFSASPIYQEMQKSVQVAKERFQTNPSPLVKTSAFALPIWHQIWYCAGRQFRIVTSDYSLWAVELATIVVQSLVLGTLFRNQQRTTSSLFIFASALFYSVLVPALQSMAEFGNGFAQRPLILKQKRYQISRPIAYALGLVTTDVVWKVAAICYNIPLYFLTGFQRTAGNFFTWFLIIYLEHLALSMFFRSVAIFSPNMHRAVLPVGIFFNMYVLYTGLYVPAPQMQVWLGWLRYLNPLYYAFESVMVNEFRDLSYQCSASDPVPSGLGYNDMAHQVCAVVGSEPGDRLLSGASYIHAQYGFKTSHLWRNVGINAALFVFFALCSGIGMEMLKTPAGQLATVFYKSSPGVTHRRDKIDSETGQDQGNESSEMSAGQSNDALRLQEHQGPDKSHNLAWTNLCLDIKTKEGDQRLLNNLSGSVKSGQLKALMGVSGAGKTTLLNALAGRSTIGNLTGTLALNGQVLPTFFRSRMGYVQQQDIHLPTQTVREALQMTARLRRPESISVADKNAYVEKVIEWLSMEHIADALVGVPGAGLNLEQRKKVSIGVEMASKPEILFLDEPTSGLDGQSAMLIARLLRRLADSGQAILCTIHQPAAELIDQFDKLYLLSRGGNLVYDGSLGTRCHEAIQYFQPRSRPCGPEENPAEYFLAVIGAGSRNDAHMDWASLWNDSEQGKEREKAEESLVPAAEQAPQLEQQSLYSVPFHVQLWVVVQRTWLYYWREPDYVNSKLWMSVGNSLLNSLTHLQSPNTERGAYNRVFSAFMSLIVGPPLGLQVQPRFVTLRDIFVHRERESLTYHWLAFVLSAFIVELPFTFLSSLVYWLLWYFPVGYFNAPSRAGYSFLMYELFGVFATSLAQLCASLMPNIEAAFAANGFFFMFCNTFAGTLSPKPVTPSGWRWFYNISPLFYLGEGVTVDVLQDLPIRCEESEVSIFYAVNGTTCGQYAQDFLKTATGYLLNPASTTECQYCRYRDGQSYFQQYGYEFAHRHRNIGVFICFIAFNFTMVLVMTYLTKTRRH | ABC transporter part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (Probable). May be involved in the secretion of E-ascladiol to be converted to patulin by the secreted patulin synthase patE (Probable). |
B6SFA4 | MAA3_ARATH | Probable helicase MAGATAMA 3 (EC 3.6.4.-) (SEN1-like protein) | MAIDNGKLQEEEASSVTRFYNIILGWDYKQLTKENERKNRKDSKEKLNVVKNTYKDVDDYFETFEPLLFEEVKAQILQNKDGEEASVCKMRLVMECNEGEGFHFLLVTYEHEEDEYLAQNDLLLLSKEEVKGNSFPSSYGFAVVEHRQNNLLRLRMYLAEDIVQITKNTKSSRTKSFIQALSNMRSLITSSASPIDKRVFSLKLCGLSTIIREYIALRSVSSLPFKDLIFTAAEKSCGFGDEAWKISGPLNEFFNENLNKSQKEAIDVGLSRKSFVLIQGPPGTGKTQTILSILGAIMHATPARVQSKGTDHEVKRGIQMTIQEKYNHWGRASPWILGVNPRDAIMPEDGDDGFFPTSGNELKPEVVNASRKYRLRVLVCAPSNSALDEIVLRLLSSGLRDENAQTYTPKIVRIGLKAHHSVASVSLDHLVAQKRGSAIDKPKQGTTGTDIDSIRTAILEEAAIVFATLSFSGSALLAKSNRGFDVVIIDEAAQAVEPATLIPLATRCKQVFLVGDPKQLPATVISTVAQDSGYGTSMFERLQKAGYPVKMLKTQYRMHPEIRSFPSKQFYEGALEDGSDIEAQTTRDWHKYRCFGPFCFFDIHEGKESQHPGATGSRVNLDEVEFVLLIYHRLVTMYPELKSSSQLAIISPYNYQVKTFKDRFKEMFGTEAEKVVDINTVDGFQGREKDVAIFSCVRANENGQIGFLSNSRRMNVGITRAKSSVLVVGSAATLKSDPLWKNLIESAEQRNRLFKVSKPLNNFFSEENLETMKLTEDMEIPDAPLYEDESLPVAPYGGDDDFGDGDADQDDVAMAGED | Probable helicase that may regulate RNA molecules involved in nucleolar organization and pollen tube guidance. |
B6ULW4 | BTDA_PAPAN | Theta defensin subunit A (BTD-a) (BTD-1 subunit 1) (BTD-3) (BTD-4 subunit 1) (BTD-7 subunit 1) | MRTFALLTAMLLLVALHAQAEARQARADEAAAQQQPGADDQGMAHSFTWPENAALPLSESAKGLRCVCTRGFCRLL | BTD-1, BTD-3, BTD-4 and BTD-7 have antimicrobial activity against the Gram-negative bacterium E.coli ML35, the Gram-positive bacterium S.aureus 502a, and the fungus C.albicans 16820. BTD-3 is more effective against E.coli than BTD-1, BTD-4 and BTD-7. |
B6ULW5 | BTDB_PAPAN | Theta defensin subunit B (BTD-b) (BTD-1 subunit 2) (BTD-2) | MRTFALLTAMLLLVALQPQAEARQARADEAAAQQQPGADDQGMAHSFTRPENAALPLSESAKGLRCVCRRGVCQLL | BTD-1 and BTD-2 have antimicrobial activity against the Gram-negative bacterium E.coli ML35, the Gram-positive bacterium S.aureus 502a, and the fungus C.albicans 16820. BTD-2 is more effective against E.coli than BTD-1. |
B6ULW7 | BTDD_PAPAN | Theta defensin subunit D (BTD-d) (BTD-7 subunit 2) | MRTFALLTAMLLLVALQAQAEARQARADEAAAQQQPGADDQGMAHSFTRPENAALPLSESAKGLRCFCRRGVCQLL | BTD-7 has antimicrobial activity against the Gram-negative bacterium E.coli ML35, the Gram-positive bacterium S.aureus 502a, and the fungus C.albicans 16820. |
B6V6V5 | KSHA4_RHORH | 3-ketosteroid-9-alpha-monooxygenase, oxygenase component (3-ketosteroid-9-alpha-hydroxylase, oxygenase component) (KSH) (Androsta-1,4-diene-3,17-dione 9-alpha-hydroxylase) (EC 1.14.15.30) (Rieske-type oxygenase) (RO) | MTVPQERIEIRNIDPGTNPTRFARGWHCIGLAKDFRDGKPHQVKVFGTDLVVFADTAGKLHVLDAFCRHMGGNLARGEIKGDTIACPFHDWRWNGQGRCEAVPYARRTPKLGRTKAWTTMERNGVLFVWHCPQGSEPTPELAIPEIEGYEDGQWSDWTWTTIHVEGSHCREIVDNVVDMAHFFYVHFQMPEYFKNVFDGHIAGQHMRSYGRDDIKTGVQMDLPEAQTISDAFYYGPSFMLDTIYTVSEGTTIESKLINCHYPVTNNSFVLQFGTIVKKIEGMSEEQAAEMATMFTDGLEEQFAQDIEIWKHKSRIENPLLTEEDGPVYQLRRWYNQFYVDLEDVTPDMTQRFEFEVDTSRALESWHKEVEENLAGTAE | In vitro, catalyzes the introduction of a 9alpha-hydroxyl moiety into the ring B of 3-ketosteroid substrates such as 1,4-androstadiene-3,17-dione (ADD), 4-androstene-3,17-dione (AD), 4-androstene-17beta-ol-3-one (testosterone), 4-pregnene-3,20-dione (progesterone), 19-nor-4-androstene-3,17-dione (nordion), 1-(5alpha)-androstene-3,17-dione, 5alpha-androstane-3,17-dione and 5beta-androstane-3,17-dione. KSH has the highest activity with 3-keto-delta4 steroid substrates. |
B6V6V6 | KSHB_RHORH | 3-ketosteroid-9-alpha-monooxygenase, ferredoxin reductase component (3-ketosteroid-9-alpha-hydroxylase, ferredoxin reductase component) (KSH) (Androsta-1,4-diene-3,17-dione 9-alpha-hydroxylase) (EC 1.14.15.30) (Rieske-type oxygenase) (RO) | MTTVEVPHGSRSVILTVSAVVEETADTRSIVFAVPDELRDKFAYRPGQFLTLRIPSDRTGSVARCYSLASSPFTDDAPKVTVKRTSDGYGSNWLCDNIATGQTLEVLPPAGVFTPKSLDHDFLLFGAGSGITPVISILKSALTQGGGKVVLVYANRDEKSVIFAEELRALAEKYPTRLTVVHWLESVQGLPTADQLAAIAAPYESYEAFMCGPGPFMDTVHQALNTVGMPRARVHAEVFNSLSGDPFADQAPVEVSDEDAADAATVEVELDGEVHKLSWPRKQTLVDIMLAKGIDVPYSCQEGECGSCACTVLEGKVEMENCDVLDPEDIEAGYILGCQARPVTDHLKIEF | Probably involved in the degradation of cholesterol. In vitro, catalyzes the introduction of a 9alpha-hydroxyl moiety into the ring B of 3-ketosteroid substrates such as 1,4-androstadiene-3,17-dione (ADD), 4-androstene-3,17-dione (AD), 4-androstene-17beta-ol-3-one (testosterone), 4-pregnene-3,20-dione (progesterone), 19-nor-4-androstene-3,17-dione (nordion), 1-(5alpha)-androstene-3,17-dione, 5alpha-androstane-3,17-dione and 5beta-androstane-3,17-dione. KSH has the highest activity with 3-keto-Delta4 steroid substrates. |
B6V8E6 | CTNB1_CANLF | Catenin beta-1 (Beta-catenin) | MATQADLMELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEEEDVDTTQVLYEWEQGFSQSFTQEQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMAWNETADLGLDIGAQGEPLGYRQDDPSYRSFHSGGYGQDALGMDPMMEHEMGGHHPGADYPVDGLPDLGHAQDLMDGLPPGDSNQLAWFDTDL | Key downstream component of the canonical Wnt signaling pathway (By similarity). In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes (By similarity). Involved in the regulation of cell adhesion, as component of an E-cadherin:catenin adhesion complex (By similarity). Acts as a negative regulator of centrosome cohesion. Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2. Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML (By similarity). Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle. Involved in chondrocyte differentiation via interaction with SOX9: SOX9-binding competes with the binding sites of TCF/LEF within CTNNB1, thereby inhibiting the Wnt signaling (By similarity). |
B6VQ60 | BRCA1_CAEEL | Breast cancer type 1 susceptibility protein homolog (EC 2.3.2.27) (RING-type E3 ubiquitin transferase BRCA1) | MADVALRITETVARLQKELKCGICCSTYKDPILSTCFHIFCRSCINACFERKRKVQCPICRSVLDKRSCRDTYQITMAVQNYLKLSEAFKKDIENMNTFKSLPPEKMFMESQMPLDITIIPENDGKRCAPDFAIPFLPVRRKRPSRPQPPSAFAEEPAEPVEPPEPATKQPVELQSRVFPLEKLKKDVETSTETYKISREELKNVDIEEYINTLRENSTEIDEIDALFQLMPTMRQFLRNNINQLMEKFHVAPPKKSEKPANRRVSFASSQDLENIKIMTASESLETPPEPIQKLAQKPEVFKSTQNLIDLNLNTAVKKPVVVASDDDEVVEDSEGELQIDEDDLANVTCATSSTTLDADRTPKAIQDDEDRIDDELSQVPKTIVCSRIHNDADEVVGLELLSDFYHKFLSNACRFAEDVNEHTTHLVMMNSEGRSISQKSTAYLYAIARKCVIVGRQWLVDCITTGLLLSEADYTITSCSSTIPVKIPPSIGSEMGWLRSRNDEHGKLFAGRRFMILRKFTMNPYFDYKQLIELVQQCGGEILSCYENLSPEKLYIIFSKHSKAIEESKNIENLYKCDVVTMEWVLDSISEYLILPTQPYKAVDSIGCLQD | E3 ubiquitin-protein ligase that specifically mediates the formation of polyubiquitin chains and plays a central role in DNA repair. Plays a role in triggering cellular responses at damage sites in response to DNA damage that may be induced by UV and ionizing radiation for example. Functions in double-strand break repair, and is required for homologous recombination between sister chromatids in meiotic and mitotic cells. In particular, protects against chromosome non-disjunction and nuclear fragmentation during meiotic double-strand break repair to ensure sister chromatid recombination and aid chromosome stability. Required for normal cell cycle progression. Along with brap-2 modulates the expression of cell cycle arrest protein cki-1 in response to increased levels of reactive oxygen species. Constituent of the CeBCD complex that possesses E3 ubiquitin-protein ligase activity. When bound to chromatin, the brc-1-brd-1 heterodimer within the CeBCD complex is inactive during normal conditions, but in response to DNA damage, the brc-1-brd-1 heterodimer associates with other proteins such as the recombinase rad-51 or the E2-ubiquitin-conjugating enzyme let-70, which activate the CeBCD complex as an E3-ubiquitin ligase. Moreover, association between the brc-1-brd-1 heterodimer and rad-51 and let-70, probably requires DNA checkpoint proteins such as atl-1 and mre-11 in order to induce ubiquitination at DNA damage sites. To this end, the brc-1-brd-1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. |
B6VQA1 | DIMM_DROME | Protein dimmed | MDATQLTELMGSHDFMQLQHQLHHNNNNYNTDGHNGLSSESAEGSSRPVRRATRRTSQLSNNTYDLEMTDSSSQSDDTSGGGGSSNGGGSTTNTGHPSGCSLGGQGPSGRGRVQQASSGACPSTIAPNSTSSNSSNANGNASRRRKGALNAKERNMRRLESNERERMRMHSLNDAFQSLREVIPHVEMERRLSKIETLTLAKNYIINLTHIILSKRNEEAAALELNSGAVGGVLLSNLSSESGGPVASGIPANSNAATICFEDTLASGGAFDCAILAATDGSLLNAATVTTSPAMQSIQSQAIHLQTPMEQQQQQASHLPHHQQAMHGHGHLGASIQSQQQPSLVLNGTTSVGLGIGIGVGVGVGVGVCNNAPSFADINDNFDEPFREFL | Transcription factor that regulates neurosecretory (NS) cell function and neuroendocrine cell fate. Acts as a master regulator of common NS functions such as Phm expression and neuropeptide production. Plays a role as a regulator of peptide-containing large dense-core vesicle (LDCV) production and peptidergic cell differentiation. Controls transcription of FMRFamide in Tv neuronal cells and Fur1 in Ap-let cells (Tvb and dorsal apterous cells). Also required for up-regulation of Phm in Tv and Ap-let cells, and expression of three neuropeptide genes, Ms, FMRFamide and Lk. Influences both regulated and constitutive secretory activity in neuroendocrine cells at embryonic and postembryonic level. Loss of function studies show reduced cellular levels of various neuropeptides and neuropeptide biosynthetic enzymes. |
B6YWB8 | CAS10_THEON | CRISPR system single-strand-specific deoxyribonuclease Cas10/Csm1 (subtype III-A) (ssDNase Cas10) (EC 3.1.-.-) (Cyclic oligoadenylate synthase) (EC 2.7.7.-) (ToCsm1) | MEIDELTALGGLLHDIGKPVQRAGLYSGDHSTQGARFLRDLAENTGRAEYELLSLFSEFHHKGHMKNDELMIRRIKELSPERFGLTMEDVLNALWIVYEADNLASGEREEGQPQASRPLYSVFNPGKAYPWAELDFEKELPVPGDVFSIRSQDYRELVKRLWEELSKAKLRSDRLLPVLEKYLTFVSSVTSEGNIISLYDHMRMTSAIALAMLRAGCTAEDVRSGRCRKEKRFLLIEGDFSGIQDFIYRVSGKGTLKYLRARSAYLELIGWDVVLEILSRLGLTRANVVFNAGGHFMIIAQNTPDAVKELEEIRAKAVEWLYREFESDLYLAIEWEPVSGREFGREGGKNLFAEARKRLKHKLTVRKLKRFGEIKGLFEHGHTERLAECPVCGRELPEGKLEPSASDPETKVCPTCNRLVSLGGNLPKLLGFGRTAKNDAGVLVEGPFSGFVPYLQGGRPVGEQILVKNTLNPGEIPESAQFVPYFVADYFKKDPKGGVATFEELSMASTGTRRLGVMKGDVDRLGEFFSSMDSPSKLATASRFMDYFFKGYIGAIIEGKFGYIIGDVPSLRDWPEEPDIVVVYAGGDDFFIVGAWDQIFELAFRVRRAFNAYTGGKLTLSVGLGYFDERTPIYRMADVVSERLDTAKDEGRNRVFVVGRSRPLDGKHKLSYEWNHYEELWRTYAPRIYAGNGRLKGKLESKKGLLWKLLEIRELYVRDPNDVRWAYLTAYLLGRHGLSDLFPELVGIDTKAVERKEPQPVYWVDGVLKIVLMAVRR | CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The type III-A Csm effector complex binds crRNA and acts as a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase binding of target RNA cognate to the crRNA is required for all activities. A single-strand deoxyribonuclease (ssDNase) which digests linear and circular ssDNA has 5'-3' and 3'-5' exonuclease activity as well as a less efficient endonuclease activity. Has a minimal size requirement 100 nucleotide ssDNA (nt) is more efficiently digested than 50 or 25 nt ssDNA, while 14 nt ssDNA is not cleaved at all. It has no activity on dsDNA or ssRNA. ssDNase activity is stimulated in the ternary Csm effector complex binding of cognate target RNA activates the ssDNase, as the target RNA is degraded ssDNA activity decreases. When associated with the ternary Csm effector complex (the crRNA, Cas proteins and a cognate target ssRNA) synthesizes cyclic oligoadenylates (cOA) from ATP. cOAs are second messengers that stimulate the ssRNase activity of Csm6, inducing an antiviral state important for defense against invading nucleic acids. |
B6ZK72 | LSD19_STRLS | Epoxide hydrolase LasB (EC 5.5.1.-) (Lasalocid biosynthesis protein Lsd19) | MPAETVRKEVALEYCRRVNAGELEGVLQLFAPDALLVDPLGTEPVVGRAALAARLAPALRGAVHEEPGRPYAAHDGTSVVLPATVTVGAPGAPPQRRGRTRVMGVIEVGEDGLIREMRVMWGVTDSSWTARPAPDEERRKELAREHCLRINDGDVDGLLKLYSPRIRFEDPVGSWTRTGLEALRAHATMAVGSNVRETAGLTVAGQDGRHAAVTVSATMDYLPSGPLLARHHLMTLPAPADPHRALIGIEYVMVIGVDADGLIDEMRAYWGATDVSLLDPAA | Epoxide hydrolase responsible for the double epoxide-opening cyclization of bisepoxyprelasalocid A to form lasalocid A, a polyether antibiotic. In vitro, accepts various substrate analogs differing in the left segment of lasalocid and epoxide stereochemistry to afford products with excellent regioselectivity. |
B6ZK77 | IRL1B_DANRE | Interleukin-1 receptor accessory protein-like 1-B (EC 3.2.2.6) | MRSRVPLQILLYAAVIRSLKVVSKRGSVDGCTDWSVDYLRYRVLLGEPVRIKCALFYGYIRANYTHAQSAGLSLMWYRSATHTDHEEPITLDGTRTLKEEDALWFRPAQLQDSGHYSCVLRNSSYCMKVSMALTVAENSSGLCYNSKMRRLEKAELSKSKDILCPDIQDYTPAGSEPHVTWYKECRPKQWRSSIIRTADLLSIRDVREDDIGNYTCEIQFGRFLVRRTTELTVTAPLTDKPPKILQPPEHKLSVMELQLGGPVNLTCRAFFGYSGDVSPLIYWMKGEKFIEDLDETRIRESEIKMVREHLGEQEVSVSLTIDSLQEEDLGNYSCYVENGHGRRHAIIQLSRRELMYTVELAGGLGAILLMLIFLVSLYKCYRIELMLFYRNHFGSEDVDGENKDYDAYVSYTKVDPDQWSQETREEEHFALEILPDMLEKHYGYKLFIPDRDLIPTGTYIEDVARCVDQSKRLIIVMTPNYVVRRGWSIFELETRLRNMLVSGEIKVILIECSDLRGIMNYQEVEALKHTIKLLTVIRWPGPGSSKPNSRFWKQLQYEMPFRRPEPKLSHEQVLDASEQGPFGELQTVSALSMVSATSTAMATAHPDLRSGFHNTYNTQLRQKHYYRGYEYDIPSSGTLPPLATMGSQHTYCNIPMSLLNGQRPPGQPAHGQQQSLEEQQVNNALLPLLPRETSISSVIW | May regulate secretion and presynaptic differentiation through inhibition of the activity of N-type voltage-gated calcium channel. During presynaptic differentiation may regulate both synaptic vesicle accumulation in axon terminals and subsequent axon terminal remodeling. |
B6ZLK2 | CHD1_CHICK | Chromodomain-helicase-DNA-binding protein 1 (CHD-1) (EC 3.6.4.12) (ATP-dependent helicase CHD1) | MNGHSDEESVRNSSGESRSDDDSGSASGSGSGSSSGSSSDGSSSQSGSSDSESGSESGSQSESESDTSREKKQVQAKPPKADGSEFWKSSPSILAVQRSAVLKKQQQQQKAASSDSGSEEDSSSSEDSADDSSSETKKKKHKDEDWQMSGSGSVSGTGSDSESEEDGDKSSCEESESDYEPKNKVKSRKPPSRIKPKSGKKSTGQKKRQLDSSEEEEDDDEDYDKRGSRRQATVNVSYKEAEETKTDSDDLLEVCGEDVPQTEEDEFETIEKFMDSRIGRKGATGASTTIYAVEVDGDPNAGFEKSKELGEIQYLIKWKGWSHIHNTWETEETLKQQNVKGMKKLDNYKKKDQETKRWLKNASPEDVEYYNCQQELTDDLHKQYQIVERIIAHSNQKSAAGYPDYYCKWQGLPYSECSWEDGALIAKKFQARIDEYFSRNQSKTTPFKDCKVLKQRPRFVALKKQPSYIGGHESLELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWAPQMNAVVYLGDITSRNMIRTHEWMHPQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGREYGYASLHKELEPFLLRRVKKDVEKSLPAKVEQILRMEMSALQKQYYKWILTRNYKALSKGSKGSTSGFLNIMMELKKCCNHCYLIKPPDDNEFYNKQEALQHLIRSSGKLILLDKLLIRLRERGNRVLIFSQMVRMLDILAEYLKYRQFPFQRLDGSIKGELRKQALDHFNAEGSEDFCFLLSTRAGGLGINLASADTVVIFDSDWNPQNDLQAQARAHRIGQKKQVNIYRLVTKGSVEEDILERAKKKMVLDHLVIQRMDTTGKTVLHTGSTPSSSTPFNKEELSAILKFGAEELFKEPEGEEQEPQEMDIDEILKRAETRENEPGPLTVGDELLSQFKVANFSNMDEDDIELEPERNSRNWEEIIPESQRRRIEEEERQKELEEIYMLPRMRNCAKQISFNGSEGRRSRSRRYSGSDSDSITERKRPKKRGRPRTIPRENIKGFSDAEIRRFIKSYKKFGGPLERLDAVARDAELVDKSETDLRRLGELVHNGCIKALKDNSSGQERAGGRLGKVKGPTFRISGVQVNAKLVISHEEELAPLHKSIPSDPEERKRYVIPCHTKAAHFDIDWGKEDDSNLLVGIYEYGYGSWEMIKMDPDLSLTQKILPDDPDKKPQAKQLQTRADYLIKLLNKDLARKEAQRLAGAGNSKRRKTRNKKNKMKASKIKEEIKSDSSPQPSEKSDEDDDEEDNKVNEIKSENKEKSKKIPLLDTPVHITATSEPVPISEESEELDQKTFSVCKERMRPVKAALKQLDRPEKGLSEREQLEHTRQCLIKIGDHITECLKEYTNPEQIKQWRKNLWIFVSKFTEFDARKLHKLYKHAIKKRQESQQHNDQNISSNVNTHVIRNPDVERLKETTNHDDSSRDSYSSDRHLSQYHDHHKDRHQGDAYKKSDSRKRPYSAFSNGKDHRDWDHYKQDSRYYSDSKHRKLDDHRSRDHRSNLEGNLKDSRGHSDHRSHSDHRIHSDHRSTSEYSHHKSSRDYRYHSDWQMDHRASGSGPRSPLDQRSPYGSRSPLGHRSPFEHSSDHKSTPEHTWSSRKT | ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. Regulates polymerase II transcription. Also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. Regulates negatively DNA replication. Not only involved in transcription-related chromatin remodeling, but also required to maintain a specific chromatin configuration across the genome. Required for maintaining open chromatin and pluripotency in embryonic stem cells (By similarity). Required for centromeric localization of CENPA. |
B7FAS6 | SAM10_CAEEL | Single-stranded DNA-binding protein homolog sam-10 (Synaptic vesicle tag abnormal in mechanosensory neurons) | MPPQVIQQQQQSLASEMTARDRLTSYIYEYLQQTGASKTAETFKEEVLSTNPAAGLAAANSTKLSDKSFLLEWWLLFWDLYSAAPERRDAGGDPFSAEAKYFHEAMIGMPPGMNGHFAPPPMGMEMMGGHPGAFGGRFAPGRMPPGAMAPGGMPPGAFPMFPPDPRLQRMAPNQGMRMPPPPVGQPFPGAVGMPRPVGPGAPMDMSGMQRFDFMGGPPPGGGAQPFPGASGSGGMMPNGAHPHMSLNSPSMGVPPADMPPFMGMPPMPPTSSSAMPFGMSSDHQPMSAGPAAAAPGATTAGGPGTPGMIGSVPGPGSVPQVATTSVGSVGTPSSIGQQLHQPKQEITTNGEEIMKTEALTPTGGGGGGSVPPPPPAATAAVSMNGGGPGSAPGSAHSVNNNVNPGTPGSNPLSNPMSNPPLSSGPPPPGSNDAFGKDDNGEISKIREGLLDGFCA | Involved cell autonomously in PLM neuron pre-synaptic differentiation by negatively regulating prk-2 expression and in neurite branch positioning. |
B7FDP2 | SCX39_CENSU | Toxin Css39.8 | MNSLLMITACFFLIGTVWAKEGYLVNKSTGCKYGCLLLGKNEGCDKECKAKNQGGSYGYCYAFGCWCEGLPESTPTYPLPNKSCSKK | Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. This toxin is lethal to crustaceans (freshwater crayfish (Cambarellus montezumae spp.)), it provokes a reversible paralysis to insects (crickets (Achaeta spp.)), but is not toxic to mice. At high concentrations, it does displace the (beta) mammal-specific toxin Cn2 from rat brain synaptosomes. |
B7FXW1 | SQLE_PHATC | Alternative squalene epoxidase (AltSQE) (EC 1.14.19.-) (Alternative squalene monooxygenase) | MLVDRVENNEKQQQQMASSSDAMSDSSLSDDEIIEHVVHGKEPKSTYELSWVSNAIAWSGALVWPLMLTVPLLLSSMYSPISYRQVFPESWYVYDTLSNCAPKPLGLVLGILAVAVGQVFVWIFFYLFKFGYLGTDPRSIQSKGAREYIFREGLLTHIGQPEGFVLLIGYLAITWMLKLMPQSYYSFEGTIQYKELFMCLVLQDGIQYTMHVLEHIVSPAFYQMSHKPHHRFTNPRLFDAFNGSLMDTFCMIIIPLFVTANLVRHCNVWTYMAFGSSYACWLTLIHSEYVFPWDGIFRKLGLGTPADHHVHHKFFKFNYGHLFMWFDQLGGTYRDPSGFAPRVFRENV | Catalyzes the stereospecific epoxidation of squalene at the terminal double bond to form (S)-2,3-epoxysqualene, the first oxygenation step in sterol biosynthesis. |
B7G620 | IDH1_PHATC | Isocitrate dehydrogenase [NAD(+)] 1, mitochondrial (PtIDH1) (EC 1.1.1.41) | MSSLSTLRILHSTAGRRWASYYGIYPKSAACSSSSVAIARFFSTAADRPPKHAMLSVENKVVAPPMVYIAGEEMTRYACDLVVKSWLEPYFDLSQWEYFDLSCVNRDNTNDQVLRDAVTAGQRIGAIFKEPTITPSAIQKKAFGLKNSLGSPNGAMRAGWNGITISRDTIHIDGIELGYKRPVFFERHAVGGEYGAGWSKVGRGTLLTTYLPSDGRDPFVVDKRDLTDQHNVVVTYHNPYDNVEPLAHLFFQRCLDANITPYVVTKKTVFKWQEGFWAVMKDVFDEHYKSRFEEKGLLQACGGDLQHLISDAATMQLIRWTDGGFGMAAHNYDGDMLTDQIAQVHRSPGFITSNLVGKAPDGSLIKEFEASHGTVSDLWNDHLAGKETSLNPLGLVEAIVGALQHAAVLDAEKNPDDEHKVKARDQIFNFTTTLRTAMHNTFRYGQGTRDMSGPSGYTTEDFVRKVAWRLQRYLDAQYDEAPPPQLGEPSRKLRRNYDIDEEAINGLFQKYDKNGDGFIDFEEFTRMLVKMNLAPLLTKKEKEKKPDV | Performs an essential role in the oxidative function of the tricarboxylic acid cycle and respiration (By similarity). Catalyzes the decarboxylation of isocitrate to produce 2-oxoglutarate and generate NADH to provide electrons for energy production. No activity with NADP(+). |
B7G6D3 | MCA3C_PHATC | Metacaspase III c (PtMCA-IIIc) (EC 3.4.22.-) [Cleaved into: Small subunit p10; Large subunit p20] | MGFLRRQLREQFEKKKPEALQADIRMISGCQDVQTSADVSNVSSFQLPDPAGNAGGACTSTLLNVLYKDHQTPEDTMSFVELLNKMRENLEAKGFSQVPQLTASHPIDVNDDFDLVPPAATGTRRALLIGINYVGHEQGVLRGCHNDVKNMVEYIKAVHGFEDENITILMDDGEHTAPTHANMIAAYKKIVALSKADDALFCHFSGHGAKIRDDDRGEEDDGYDETLVPIDYHENGMIRDDDLYDILIKPLVQGVHLVCLMDCCHSGTVLDLPYVYKADGNFTEMEIDENFDFKKLLGKFGIDDFDKFGGEALGKINGDALGKVGKDALGKLNKFFG | Cysteine protease that cleaves specifically after arginine residues. |
B7IE18 | MURJ_THEAB | Lipid II flippase MurJ | MSILFSSILFSIATFFSRILGLFRDVLFAKYFGVSYELDAYFIAIMFPFFLRKVFGEGAMSSAFVPLYSEKSGEEKDKFLSSVINGFSLIILALVILSYFFPELIINLFGAGSSHETKILAKKLLLITSPSIYFIFLWAISYSILNTNNKFFWPALTPSISNITIIIGTFLSTKYGIISPTIGFLIGSILMFFSIIKSIIKHKYYFTIKHFPHFLKLFFPTFMTMVVSQINTVVDMNVVSFYDKGSISYLQYASRFYLLPYGLFAVSVSTVVLSKISNDRKNFNYHLNDALKTTLFFTIPSMVGLIFLSTPIIRFFYEHGAFTSKDTLITSKILIAYTLGLPFYGIYSTISRSYHAIKNTKTPFIAATIVSLSNIILDIIFGLKYGPIGVALATSIAGIIGVLYLLFSVKTFPIKDFLKISLNSLIMLFVIYLTDFTDNEFWFLIQILIGILVYLIFSSIFYRDLIRRFLYARKK | Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane. {ECO:0000255|HAMAP-Rule:MF_02078, ECO:0000305|PubMed:28024149}. |
B7JBP8 | SQRD_ACIF2 | Sulfide-quinone reductase (SQR) (EC 1.8.5.4) (Sulfide:quinone oxidoreductase) | MAHVVILGAGTGGMPAAYEMKEALGSGHEVTLISANDYFQFVPSNPWVGVGWKERDDIAFPIRHYVERKGIHFIAQSAEQIDAEAQNITLADGNTVHYDYLMIATGPKLAFENVPGSDPHEGPVQSICTVDHAERAFAEYQALLREPGPIVIGAMAGASCFGPAYEYAMIVASDLKKRGMRDKIPSFTFITSEPYIGHLGIQGVGDSKGILTKGLKEEGIEAYTNCKVTKVEDNKMYVTQVDEKGETIKEMVLPVKFGMMIPAFKGVPAVAGVEGLCNPGGFVLVDEHQRSKKYANIFAAGIAIAIPPVETTPVPTGAPKTGYMIESMVSAAVHNIKADLEGRKGEQTMGTWNAVCFADMGDRGAAFIALPQLKPRKVDVFAYGRWVHLAKVAFEKYFIRKMKMGVSEPFYEKVLFKMMGITRLKEEDTHRKAS | Catalyzes the oxidation of hydrogen sulfide, with the help of a quinone. Consecutive reaction cycles lead to the accumulation of a polysulfide product on the active site Cys residues these products are released when they exceed a critical length, typically as cyclooctasulfur. |
B7L8Y4 | HCHA_ECO55 | Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase) | MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGTLIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKLLTGDSPFAANALGKLAAQEMLAAYAG | Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}. |
B7L9A7 | FADB_ECO55 | Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)] | MLYKGDTLYLDWLEDGIAELVFDAPGSVNKLDTATVASLGEAIGVLEQQSDLKGLLLRSNKAAFIVGADITEFLSLFLVPEEQLSQWLHFANSVFNRLEDLPVPTIAAVNGYALGGGCECVLATDYRLATPDLRIGLPETKLGIMPGFGGSVRMPRMLGADSALEIIAAGKDVGADQALKIGLVDGVVKAEKLVEGAKAVLRQAINGDLDWKAKRQPKLEPLKLSKIEATMSFTIAKGMVAQTAGKHYPAPITAVKTIEAAARFGREEALNLENKSFVPLAHTNEARALVGIFLNDQYVKGKAKKLTKDVETPKQAAVLGAGIMGGGIAYQSAWKGVPVVMKDINDKSLTLGMTEAAKLLNKQLERGKIDGLKLAGVISTIHPTLDYAGFDRVDVVVEAVVENPKVKKAVLAETEQKVRPDTVLASNTSTIPISELANALERPENFCGMHFFNPVHRMPLVEIIRGEKSSDETIAKVVAWASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDGADFRKIDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAAGFPQRMQKDYRDAIDALFDANRFGQKNGLGFWRYKEDSKGKPKKEEDAAVEDLLAEVSQPKRDFSEEEIIARMMIPMVNEVVRCLEEGIIATPAEADMALVYGLGFPPFHGGAFRWLDTLGSAKYLDMAQQYQHLGPLYEVPEGLRNKARHNEPYYPPVEPARPVGDLKTA | Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}. |
B7LTY9 | FADB_ESCF3 | Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)] | MLYKGDTLYLDWLEDGIAELVFDAPGSVNKLDTATVASLGEAIGVLEQQSDLKGLLLRSNKAAFIVGADITEFLSLFLVPEEQLSQWLHFANSVFNRLEDLPVPTIAAVNGYALGGGCECVLATDYRLATPDLRIGLPETKLGIMPGFGGSVRMPRMLGADSALEIIAAGKDVGADQALKIGLVDGVVKAEKLVEGAKAILRQAINGDLDWKAKRQPKLEPLKLSKIEATMSFTIAKGMVAQTAGKHYPAPITAVKTIEAAARFGREEALNLENKSFVPLAHTNEARALVGIFLNDQYVKGKAKKLTKDVETPKQAAVLGAGIMGGGIAYQSAWKGVPVVMKDINDKSLTLGMTEAAKLLNKQLERGKIDGLKLAGVISTIHPTLDYAGFDRVDVVVEAVVENPKVKKAVLAETEQKVRPDTVLASNTSTIPISELANALERPENFCGMHFFNPVHRMPLVEIIRGEKSSDETIAKVVAWASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDGADFRKIDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAAGFPQRMQKDYRDAIDALFDANRFGQKNGLGFWRYKEDSKGKPKKEEDAAVDDLLAEVSQPKRDFSEEEIIARMMIPMVNEVVRCLEEGIIATPAEADMALVYGLGFPPFHGGAFRWLDTLGSAKYLDMAQQYQHLGPLYEVPEGLRNKARHNEPYYPQVEPARAVGDLKTA | Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}. |
B7M3A5 | HCHA_ECO8A | Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase) | MTVQKSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDIAGRVHKDRKVLTGDSPFAANALGKLAAQEMLAAYAG | Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}. |
B7MCM0 | HCHA_ECO45 | Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase) | MTVQKSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESEDVAAALQWAIENDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKVLTGDSPFAANALGKLAAQEMLAAYAG | Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}. |
B7MWF3 | HCHA_ECO81 | Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase) | MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKVLTGDSPFAANALGKLAAQEMLAAYAG | Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}. |
B7NBV8 | HCHA_ECOLU | Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase) | MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKVLTGDSPFAANALGKLAAQEMLAAYAG | Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}. |
B7NFE7 | FADB_ECOLU | Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)] | MLYKGDTLYLDWLEDGIAELVFDAPGSVNKLDTATVASLGEAIGVLEQQSDLKGLLLRSNKAAFIVGADITEFLSLFLVPEEQLSQWLHFANSVFNRLEDLPVPTIAAVNGYALGGGCECVLATDYRLATPDLRIGLPETKLGIMPGFGGSVRMPRMLGADSALEIIAAGKDVGADQALKIGLVDGVVKAEKLVEGAMAILRQAINGDLDWKAKRQPKLEPLKLSKIEATMSFTIAKGMVAQTAGKHYPAPITAVKTIEAAARFGREEALNLENKSFVPLAHTNEARALVGIFLNDQYVKGKAKKLTKDVETPKQAAVLGAGIMGGGIAYQSAWKGVPVVMKDINDKSLTLGMTEAAKLLNKQLERGKIDGLKLAGVISTIHPTLDYAGFDRVDIVVEAVVENPKVKKAVLAETEQKVRPDTVLASNTSTIPISELANALERPENFCGMHFFNPVHRMPLVEIIRGEKSSDETIAKVVAWASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDGADFRKIDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAAGFPQRMQKDYRDAIDALFDANRFGQKNGLGFWRYKEDSKGKPKKEEDAAVDDLLAEVSQPKRDFSEEEIIARMMIPMVNEVVRCLEEGIIATPAEADMALVYGLGFPPFHGGAFRWLDTLGSAKYLDMAQQYQHLGPLYEVPEGLRNKARHNEPYYPPVEPARPVGDLKTA | Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}. |
B7NRB5 | HCHA_ECO7I | Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase) | MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHSDNPLNGYSICAFPDAADKQTPDIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKLLTGDSPFAANALGKLAAQEMLAAYAS | Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}. |
B7NV20 | FADB_ECO7I | Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)] | MLYKGDTLYLDWLEDGIAELVFDAPGSVNKLDTATVASLGEAIGVLEQQSDLKGLLLRSNKAAFIVGADITEFLSLFLVPEEQLSQWLHFANSVFNRLEDLPVPTIAAVNGYALGGGCECVLATDYRLATPDLRIGLPETKLGIMPGFGGSVRMPRMLGADSALEIIAAGKDVGADQALKIGLVDGVVKAEKLVEGAMAILRQAINGDLDWKAKRQPKLEPLKLSKIEATMSFTIAKGMVAQTAGKHYPAPITAVKTIEAAARFGREEALNLENKSFVPLAHTNEARALVGIFLNDQYVKGKAKKLTKDVETPKQAAVLGAGIMGGGIAYQSAWKGVPVVMKDINDKSLTLGMTEAAKLLNKQLERGKIDGLKLAGVISTIHPTLDYAGFDRVDIVVEAVVENPKVKKAVLAETEQKVRPDTVLASNTSTIPISELANALERPENFCGMHFFNPVHRMPLVEIIRGEKSSDETIAKVVAWASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDGADFRKIDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAAGFPQRMQKDYRDAIDALFDANRFGQKNGLGFWRYKEDSKGKPKKEEDAVVDDLLAEVSQPKRDFSEEEIIARMMIPMVNEVVRCLEEGIIATPAEADMALVYGLGFPPFHGGAFRWLDTLGSAKYLDMAQQYQHLGPLYEVPEGLRNKARHNEPYYPPVEPARPVGDLKTA | Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}. |
B7QK46 | QPCT_IXOSC | Glutaminyl-peptide cyclotransferase (EC 2.3.2.5) (Glutaminyl cyclase) (QC) (Glutaminyl-tRNA cyclotransferase) | MLFPVLLLLKLVIGALIIDASALSWHDLKWPRDLRPLAHHDLLYMGQISEEDRGDFNATLRNFLVPRVVGSQKHREVREFIVRSLKDLDWDVEEDCFDGQTPHGIKPFCNVIATLNPSACHRLVLACHYDSLLHKEGTFIGATDSAVPCAQLLYLARSLNGKLQNQKTRGDGLTLQLVFFDGEEAFERWSSHDSLYGSRHLAQKWHEDRTSAERLESCLERSEIANQIDRMEVMVLLDLLGAENPRFYSYFGETQPVYRRLVNIESRLNDAGLMELPRRRRRTNYFSNSSTVGFIEDDHIPFLKRSVPIVHIIPSPFPDVWHTLDDNEQNLHHPTISNLNKIFKAFVSEYLQL | Responsible for the biosynthesis of pyroglutamyl peptides. Seems to have a preference for substrates with neutral or hydrophobic amino-acid residues at the second and third positions. Shows activity towards the peptides [Gln-1]-corazonin, [Gln-1]-periviscerokinin and [Gln-1]-sulfakinin. |
B7S4N9 | VKT_OXYSC | Kunitz-type serine protease inhibitor taicotoxin (Taicatoxin, serine protease inhibitor component) (TCX) (TSPI) (Venom protease inhibitor 1) (Venom protease inhibitor 2) | MSSGGLLLLLGLLTLWEVLTPVSSKDRPKFCHLPPKPGPCRAAIPRFYYNPHSKQCEKFIYGGCHGNANSFKTPDECNYTCLGVSLPK | Heterotrimer: blocks the voltage-dependent L-type calcium channels (Cav) from the heart, and the small conductance calcium-activated potassium channels (KCa) in the chromaffin cells and in the brain. Is very toxic to mice. Monomer: serine protease inhibitor that inhibits plasma kallikrein (Ki=0.057 nM), tissue kallikrein (Ki=0.23 nM), trypsin (Ki=0.31 nM), plasmin (Ki=6.1 nM), elastase (Ki=201 nM), factor Xa (Ki=871 nM), alpha-factor XIIa (Ki=2380 nM). Does not inhibit APC, urokinase-type plasminogen activator (uPA/PLAU), tissue plasminogen activator (tPA/PLAT), thrombin and factor VIIa. In addition, the monomer inhibits fibrinolysis in whole blood and prolonged the intrinsec clotting time. |
B7SBD2 | TOX3_RAT | TOX high mobility group box family member 3 (Trinucleotide repeat-containing gene 9 protein) | MDVRFYPAAAGDPAGLDFAQCLGYYGYSKLGNNNYMNMAEANNAFFAASEQTFHTPSLGDEEFEIPPITPPPESDPTLGMPDVLLPFQTLSDPLPSQGNEFTPQFPPQSLDLPSITISRNLVEQDGVLHSNGLHMDQSHTQVSQYRQDPSLVMRSIVHMTDAARSGIMPPAQLTTINQSQLSAQLGLNLGGASVPHTSPSPPASKSATPSPSSSINEEDADETNRAVGEKRTAPDSGKKPKTPKKKKKKDPNEPQKPVSAYALFFRDTQAAIKGQNPNATFGEVSKIVASMWDSLGEEQKQVYKRKTEAAKKEYLKALAAYRASLVSKAAAESAEAQTIRSVQQTLASTNLTSSLLLNTSLSQHGTVPASPQTLPQSLPRSIAPKPLTMRLPMSQIVTSVTIAANMPSNIGAPLISSMGTTMVGSVSSTQVSPSVQTQQHQLQLQQQQQQQQQQMQQMQHQQLQQHQMHQQIQQQMQQQHFQHHMQQHLQQQQQQHLQQQISQQQLQQQLQQHLQLQQQLQHMQHQSQPSPRQHSPVTSQITSPIPAIGSPQPASQQHQPQIQSQTQTQVLPQVSIF | Transcriptional coactivator of the p300/CBP-mediated transcription complex. Activates transactivation through cAMP response element (CRE) sites. Protects against cell death by inducing antiapoptotic and repressing pro-apoptotic transcripts. Stimulates transcription from the estrogen-responsive or BCL-2 promoters. Required for depolarization-induced transcription activation of the C-FOS promoter in neurons. Associates with chromatin to the estrogen-responsive C3 promoter region. |
B7SXM5 | IER2_DANRE | Immediate early response gene 2 protein | MDVTAEAKQIMVQALGKMYSSRSQRGGLRLHRSLLLTLVMKSARDIYHSARLMSEKSGQSVTEECTSHTQEPMDTSSSTATPLRETSGQSSEDGQRSGLEGHPHPLNPAADKENCGPSRPDRHSRKRRSKTATDSDFIPCKKAKLECAEVRGVLQNSSANCGRALDSLSLVPMPRTIVTF | DNA-binding protein that seems to act as a transcription factor (By similarity). Mediates with FIBPB FGF-signaling in Kupffer's vesicle ciliogenesis and in the establishment of laterality in the embryo. |
B7TB45 | SPZ2_DROME | Neurotrophin 1 (Neurotrophic factor 1) (Protein spaetzle 2) (Protein spatzle 2) | MKAGRAFGCLFWALLYCVLYLDLVSGNSADDELMDFDFADSNDAAMEDWQLDDLEEAKKAEQAEKKLESNMLDFSVDLDEPEPEKQLPPFDWRERVLRNALAKALADEGLRQKFAEVLPILRMLSSQQRLALSALISAQMNAKKGHELKFEQVRMMFGNEKKLLLPIVFDIANLIKSSTRKYINLGSDLASSALYHTPINRREDDLTPEESQQDDQLGTIAVEVEPKKVSTEEVQLESLEDFFDEMGSEVLDPQMINEALTGDLHDNKTKTFKPENHGQRVRRSANEFVHKLTRSVPASVTEQQLLGGIAGRTIKLNTTAFQQPSSQEEEKMASSNGGQSYSEVEDLAFAGLNGTEIPLSADERLDLQRNSAEETEEPLPSPEELIAGPRYRLGKRPLPGQKSGSPIKRKRVTSSLRGRPKTAASSHKPVVTPPNKKCERFTSNMCIRTDDYPLEQIMGSIRRHKNAMSALLAEFYDKPNNNLEFSDDFDDFSLSKKRREDEGSAGGMCQSVVRYARPQKAKSASGEWKYIVNTGQHTQTLRLEKCSNPVESCSYLAQTYRSHCSQVYNYHRLLSWDKVRGLHVDIFKVPTCCSCQVDGYRQQFPPLSSIQAKDYSPQSPVINHSHNGYSTINEEDLDYAEESEEDELGLRYPSFNNRETNELYSSSNKVRVKLPGISSSVGPYLSPPDDDEDRYGGYKSSSSSSKKYYSQVSRRRPQHSEARLDLDLAPSETHSDQEPPPPQHHQHHHLQYHRPQEELPSAYDFHRPQVYQPEREQLPLVRDPALSPVSAPVLASPAPPLPMPPMPIKQVPSHHQAHHQQPHHHLHQSTGKVAANRDPASMHHQPPRRPTQQWLPGQRRPFRPSAPLSGSGISRRHYHNRRQSIQ | Neurotrophin which may function as a ligand for the Toll-related receptors Toll-7 and Tollo. Binds to Toll-7 and probably acts as its ligand in promoting motor axon targeting and neuronal survival in the central nervous system (CNS). Involved in synaptic targeting of ISNb/d motorneurons and also some SNa motorneurons. In larvae, involved in the negative regulation of the tracheal immune response to bacterial infection perhaps by acting as a ligand for the Toll-related receptor Tollo. May be involved in the normal development of specific neurons at the neuromuscular junction. |
B7U179 | ABAP1_ARATH | ARMADILLO BTB ARABIDOPSIS PROTEIN 1 (ABAP1) | MIISKSFKAPLKFSVKSSTAPVISNHPPMENHPKRQRTTRLAARNLKRKLSHNTDGAPIVTQLIDIDDEPIDLVVAIRRHVEVLNSSFSDPDFDHEAVKEAAADIADLAKIDENVEIIVENGAIPALVRYLESPLVVCGNVPKSCEHKLEKDCALALGLIAAIQPGYQQLIVDAGAIVPTVKLLKRRGECGECMFANAVIRRAADIITNIAHDNPRIKTNIRVEGGIAPLVELLNFPDVKVQRAAAGALRTVSFRNDENKSQIVELNALPTLVLMLQSQDSTVHGEAIGAIGNLVHSSPDIKKEVIRAGALQPVIGLLSSTCLETQREAALLIGQFAAPDSDCKVHIAQRGAITPLIKMLESSDEQVVEMSAFALGRLAQDAHNQAGIAHRGGIISLLNLLDVKTGSVQHNAAFALYGLADNEENVADFIKAGGIQKLQDDNFTVQPTRDCVVRTLKRLQNKIHGPVLNQLLYLMRTAEKTVQIRIALALAHLCDPKDGKLIFIDNNGVEFLLELLYFSSNKQQRYSSSALYELAKKATSFAPEDSAPCSPTQQVFLGEKFVNNPTMSDVTFLIDGKQFYAHKIGLVASSDIFRAMFDGLYKERNAQNVEIPNIRWEVFELMMKFIYSGRINIAKHLAKDLLVAADQYLLEGLKRQCEYTIAQEICLDNIPEMYELADTFNASALRRACTLFVLEHFTKLSSQLWFAKFVKQIIPEIRSYMTDILTRPVEASPPTVV | May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). In association with TCP24, exerts a negative role in cell proliferation in leaves, possibly by inhibiting mitotic DNA replication. {ECO:0000250, ECO:0000269|PubMed:18818695}. |
B7U540 | KCJ18_HUMAN | Inward rectifier potassium channel 18 (Inward rectifier K(+) channel Kir2.6) (Potassium channel, inwardly rectifying subfamily J member 18) | MTAASRANPYSIVSLEEDGLHLVTMSGANGFGNGKVHTRRRCRNRFVKKNGQCNIAFANMDEKSQRYLADMFTTCVDIRWRYMLLIFSLAFLASWLLFGVIFWVIAVAHGDLEPAEGHGRTPCVMQVHGFMAAFLFSIETQTTIGYGLRCVTEECLVAVFMVVAQSIVGCIIDSFMIGAIMAKMARPKKRAQTLLFSHNAVVALRDGKLCLMWRVGNLRKSHIVEAHVRAQLIKPRVTEEGEYIPLDQIDIDVGFDKGLDRIFLVSPITILHEIDEASPLFGISRQDLETDDFEIVVILEGMVEATAMTTQARSSYLANEILWGHRFEPVLFEEKNQYKIDYSHFHKTYEVPSTPRCSAKDLVENKFLLPSANSFCYENELAFLSRDEEDEADGDQDGRSRDGLSPQARHDFDRLQAGGGVLEQRPYRRGSEI | Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. |
B7UI21 | NLEB1_ECO27 | Protein-arginine N-acetylglucosaminyltransferase NleB1 (Arginine GlcNAcyltransferase NleB1) (EC 2.4.1.-) (Non-LEE-encoded type III effector B1) | MLSSLNVLQSSFRGKTALSNSTLLQKVSFAGKEYSLEPIDERTPILFQWFEARPERYEKGEVPILNTKEHPYLSNIINAAKIENERIIGVLVDGNFTYEQKKEFLNLENEHQNIKIIYRADVDFSMYDKKLSDIYLENIHKQESYPASERDNYLLGLLREELKNIPEGKDSLIESYAEKREHTWFDFFRNLAILKAGSLFTETGKTGCHNISPCSGCIYLDADMIITDKLGVLYAPDGIAVHVDCNDEIKSLENGAIVVNRSNHPALLAGLDIMKSKVDAHPYYDGLGKGIKRHFNYSSLHNYNAFCDFIEFKHENIIPNTSMYTSSSW | Protein-arginine N-acetylglucosaminyltransferase effector that disrupts TNF signaling in infected cells, including NF-kappa-B signaling, apoptosis and necroptosis. Acts by catalyzing the transfer of a single N-acetylglucosamine (GlcNAc) to a conserved arginine residue in the death domain of host proteins FADD, TRADD, FAS, TNFRSF1A/TNFR1, TNFRSF25/DR3 and RIPK1: arginine GlcNAcylation prevents homotypic/heterotypic death domain interactions and assembly of the oligomeric TNF-alpha receptor complex, thereby disrupting TNF signaling. Has preference for host FADD as substrate compared to other death domain-containing proteins. Also acts on host proteins without a death domain: catalyzes arginine GlcNAcylation of HIF1A, thereby regulating host glucose metabolism. Also displays intra-bacterial activity by mediating GlcNAcylation of glutathione synthetase GshB. Catalyzes auto-GlcNAcylation, which is required for activity toward death domain-containing host target proteins. Shows a higher enzymatic activity than NleB2. |
B7UI22 | NLEE_ECO27 | Cysteine S-methyltransferase NleE (EC 2.1.1.-) (Effector protein NleE) (Non-LEE-encoded type III effector E) | MINPVTNTQGVSPINTKYAEHVVKNIYPKIKHDYFNESPNIYDKKYISGITRGVAELKQEEFVNEKARRFSYMKTMYSVCPEAFEPISRNEASTPEGSWLTVISGKRPMGQFSVDSLYNPDLHALCELPDICCKIFPKENNDFLYIVVVYRNDSPLGEQRANRFIELYNIKRDIMQELNYELPELKAVKSEMIIAREMGEIFSYMPGEIDSYMKYINNKLSKIE | Cysteine methyltransferase effector that inhibits host cell NF-kappa-B activation by preventing nuclear translocation of host protein RELA/p65. Acts by mediating cysteine methylation of host proteins TAB2 and TAB3: methylation of a conserved cysteine residue of the RanBP2-type zinc finger (NZF) of TAB2 and TAB3 disrupts zinc-binding, thereby inactivating the ubiquitin chain-binding activity of TAB2 and TAB3, leading to NF-kappa-B inactivation. Also mediates cysteine methylation of host protein ZRANB3, inactivating its ability to bind ubiquitin chains. |
B7UM99 | TIR_ECO27 | Translocated intimin receptor Tir (Secreted effector protein Tir) | MPIGNLGNNVNGNHLIPPAPPLPSQTDGAARGGTGHLISSTGALGSRSLFSPLRNSMADSVDSRDIPGLPTNPSRLAAATSETCLLGGFEVLHDKGPLDILNTQIGPSAFRVEVQADGTHAAIGEKNGLEVSVTLSPQEWSSLQSIDTEGKNRFVFTGGRGGSGHPMVTVASDIAEARTKILAKLDPDNHGGRQPKDVDTRSVGVGSASGIDDGVVSETHTSTTNSSVRSDPKFWVSVGAIAAGLAGLAATGIAQALALTPEPDDPTTTDPDQAANAAESATKDQLTQEAFKNPENQKVNIDANGNAIPSGELKDDIVEQIAQQAKEAGEVARQQAVESNAQAQQRYEDQHARRQEELQLSSGIGYGLSSALIVAGGIGAGVTTALHRRNQPAEQTTTTTTHTVVQQQTGGNTPAQGGTDATRAEDASLNRRDSQGSVASTHWSDSSSEVVNPYAEVGGARNSLSAHQPEEHIYDEVAADPGYSVIQNFSGSGPVTGRLIGTPGQGIQSTYALLANSGGLRLGMGGLTSGGESAVSSVNAAPTPGPVRFV | Multifunctional protein that is required for efficient pedestal formation in host epithelial cells during infection. The extracellular region acts as a receptor for bacterial intimin, allowing the bacterium to attach tightly to the host-cell surface. Simultaneously, the intracellular region initiates a signaling cascade in the host cell, which leads to actin polymerization and formation of actin pedestals at the sites of bacterial adhesion. In strain E2348/69, acts mainly via the host adaptor proteins NCK1 and NCK2. Once clustered and phosphorylated at Tyr-474, Tir binds to NCK proteins, which in turn bind and activate host WASL/N-WASP, leading to actin polymerization. Can also trigger an inefficient, NCK-independent pedestal formation. This pathway involves phosphorylation of Tyr-454 and probably a putative host adaptor. Acts also via direct binding to the host cytoskeletal protein alpha-actinin in a NCK- and phosphotyrosine-independent manner. This interaction may stabilize the pedestal, but is not essential for its formation. |
B7UX51 | HCHA_PSEA8 | Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase) | MSNERDTSRTPTPDHAEHNAFFPSPYSLSQYTSAKTDFDGADYPTPYKGGKKVLMIGTDERYILMQNGSMFSTGNHPVEMLLPMYHLDKAGFEFDVATLSGNPVKLEMWAMPGEDEAVKSIYAKYLPKLKAPQKLADLLEQAVADDSPYAAVFVPGGHGVLAGIPHSREVKRLLNAFLAKDRYIITLCHGPACLLAPAVEEKPEDYPFKDYEICVFPDALDTGANLEIGYMPGPLPWLVGENLQKLGVKILNKGITGQVHRDRKLLTGDSPLASNNLGKLAAKTLLEAFAR | Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}. |
B7VGL4 | FADB_VIBA3 | Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)] | MIYQANTLQVKELQDGIAELSFCAPASVNKLDLATLESLDKALDALNAHAGLRGLILTSNKDAFIVGADITEFLGLFAKPEAELDEWLRFANSIFSKLEDLPVPTLSMMRGHALGGGCECVLATDFRIGDKTTSIGLPETKLGIMPGFGGCVRLPRVIGADSAMEIITQGKACRADEALKVGLLDAIVETDQLLESAINTVSLAANEKLDWQLRRKQKTSALSLSKLEAMMSFTMAKGLVAQKAGPHYPAPITSVIAIEEAARSDRDAALDIERKHFVKLAKSEEAKALVGLFLNDQYIKGLAKHAGKSANKATERAAVLGAGIMGGGIAYQSALKGVPVMMKDIAQASLELGMNEASKLLNKRLSRGRLDGFKMAGILSSITPSLHYAGVEQSDVIVEAVVENPKVKAAVLSEVEGLVGEDTVLTSNTSTIPINLLAKSLKRPENFCGMHFFNPVHRMPLVEIIRGEHTSEETINRVVAYAAKMGKSPIVVNDCPGFFVNRVLFPYFGGFSMLLRDGADFTKIDKVMERKFGWPMGPAYLLDVVGLDTAHHAQAVMAQGFPERMGKEGRDAIDALYVAEKYGQKNGSGFYTYSVDKRGRPKKTFSEDILPILADVCQQPQDFDDQTIIQRVMIPMINEVVLCLEEGIIATPQEADMALVYGLGFPPFRGGVFRYLDSVGIGNFVEMAKSYQDLGAMYQVPQLLLDMAAKGESFYDGQQASSL | Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}. |
B7WN72 | SHANK_CAEEL | Protein shank | MNQEEDTVNLQIFVPELNVRKFLAVTQNDFIWDVKRKLLATLPQALPQAFNYGLFLPPCDGRAGKFLLEDRTIRDYPFTDCVPYLELKYKKRVYKMLNLDEKQLKAMHTKGQLKKFMDYVQQKNNEKVEKMCSQGLDANFHDAQGETPLTLAAGIPNNRAVIVSLIGGGAHVDFRNSEGQTAMHKAAFLSSFENVKTLIELGASPNYRDPIGLTPLYYNMLTADSNDQVAEILLREAADIGVTDMHGNHEIHQACKNGLTKHVEHLLYFGGQIDAENVNGNSPLHVCAVNNRPECARVLLFRGADHLAVNKQGQTALHVSHIVGNPGVADVVQAHNPKSSVPYRGTPQYSTRRRLSSTITRRRSMSQSSICSQDVYRTPQSVRKGPMSAAPSPSPSRSSRTTITPSEYGTMRRSGMDSMRGGGMIAAGHETNIARILVIPRGVKGFGFILRGAKHVAMPLNFEPTAQVPALQFFEGVDMSGMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLKVITVDVADMSRGGTIVHRPPTASSRHSLVFTPTPSAIYSSTKASSVYRMRFDTHDAHGVDYYAPNEIRNAYSESRHASVRQRPGSGRRISAAELENLMVRQRVPSVQGSPYQMQYDQESLNGGYSSKKYNSVSDMKRRKGQRNVVASSAGLNRSTFEQAAPTTSTFEYNCSSRSTPQLSRMDSFDSFDDEDEMPAPPPASYISPDLQRDSSMQRSEYSRPFRPTSRPKTPPPPPPMQHQNHQNHQYQQQHPSLPRSASTPQPIQQQQSSIPPPPPPPPPPHCEPTMVHVEFTPPSTSSVPPPPPPLPPISSGAPPPPPPPPPGGLMHVAASAPVLMSNSKGISADALKSVQLKKAEPRETSAASVSNNNNNNNNSTTDFQMDLKNALAKRRSKVAHDVDEDEERESRFEGLSLRETVRENVVERGKGIQNIGIVNKKDSGYTSSRTSLEPSESEEKDHRPHFSLDHSPNVQRVTLISQHLEDNYGQKDNMSVASSSTASSSSTVDLTKPGCFVVPSHVIPPVDYDDDPDSGTGDSDGEIRCSEISFEHKKVDVWSVDDVIGWLSSLHLSEYTPAFRSQRINGRCLRQCDRSRFTQLGVTRIAHRQIIESALRGLLQ | Scaffold protein that most likely acts in the postsynaptic density (PSD) of excitatory synapses which orchestrates synapse formation and maintenance at neuromuscular junctions. Associates with and trafficks the L-type calcium channel egl-19 to the cell surface of body wall muscles to ensure the function of the calcium channel and therefore maintain the Ca(2+) current density. The maintenance of Ca(2+) also allows for the downstream regulation of Ca(2+)-induced expression of genes such as gem-4. Plays a role in the regulation of the defecation cycle, and this may be in association with the inositol trisphosphate (IP3) receptor itr-1, which in turn mediates periodic calcium release and muscle contractions. Required for normal fertility and pharyngeal pumping. |
B7WN96 | ELT3_CAEEL | Transcription factor elt-3 | METANYYLPSPPYSSTSSSDSRESRMNTPIPTTYSEENVNSLFHLMPDNTDQWMTSQKNFWQEGSPSSSEYLHQQAVQPSQQARLPGISNFMKDSQLSVKPAAYYCSPTMNDYRVEKVANTLLDPYVQLDQPTYADFTNAQVLNHQQEMLQMNFPTPLSTSYMNTAQVTQTHQMPFNIFELNLSNFATFQPACDTPLPLLNSSPTHPYTTMSNFTPPPQDPLVAEPKPMKKRMAAVQCHQNSICSNCKTRETTLWRRNGEGGVECNACNLYFRKNNRKRPLSLRKDGIMKRNRRPRNESPNSAIRNTHQRHGHAAAC | Transcription factor. Required, in concert with signal transducer and transcription factor sta-2, for up-regulation of the vacuolar H(+)-ATPase and acceleration of lysosome maturation at molt. Involved in regulating hypodermal development, perhaps acting downstream of transcription factor elt-1. Modulates environmentally induced changes in collagen gene expression, including rol-6, sqt-1, lon-3, and dpy-13. Involved in regulating expression of various genes, including gst-4, sod-3, ugt-9, and col-144. In response to oxidative stress, required to up-regulate expression of gst-4 mRNA. Regulated by the Insulin/IGF-1-like signaling (IIS) mediated pathway. Plays a role in longevity. May regulate the expression of genes that control sensitivity to osmotic stress, in conjunction with the GATA region-binding transcription factor elt-2. May form a transcriptional circuit with GATA factors egl-18 and elt-6. |
B7XDF1 | DSCR6_XENLA | Protein ripply3 (XRipply3) (Down syndrome critical region protein 6 homolog) | MDSSQYMLKATLTQMCLCSRGVRNVHSEHPQQQDSSLTLWRPWLLGAGDRELDGQQRRSGEADGVPTNTGPKGALGFQHPVRLYMPKSKTSEYLQHMGRKVLASFPVQATIHFYNDDSDSEEEDEEEEMEFYNYYQNCAANGVDSSRGSSDNYSVQGGPKRNIGSHAGSA | Acts as a transcriptional corepressor. Negative regulator of the transcriptional activity of tbx1 that plays a key role in pharyngeal development. Plays a role in the formation of the anteroposterior (AP) axis during embryonic development required to establish the posterolateral border of the pre-placodal ectoderm (PPE) acting downstream of the retinoic acid receptor (RAR) signaling. |
B7YZU2 | LINT_DROME | Serine protease filzig (EC 3.4.21.-) (Lumens interrupted) | MFKWVTPASTATLSRCTLPATTAATTTTTAMAATRTATTTTRTTRPQLLSIALTSLIIIVASFVPTTSGFRSIETNGGGRKLFGGYRITPKHCRATKTLPSSDPRANGPTICMFNHECAQRGGEVVGACMDGFLFGACCQIPPTHELASTLINEAQNAYFQQHQQQTKLQQSAAQSSFESYGEQQQSLSEEQVAQQPSQNIYDQQNLDKVYQQLDSSSSISPPNGAYGDEPQQQEYQSESEQPVRDENAYPTSSSSTEATQSQSSSASVEFEQEPSQPADASNDQTTQKINKQPVQPPNFHVHKHSVTINSPSSPPQNDDFVMQVLSTLPPEHADDHHIVFTTEVPTKITSGLQDQTSSESNSFEEVSSTPAATQKPKPKPTQMPTQKTTQKATQKPTPKPTQKAKPKPVPQLAESMKRPIQQKPQQVAKPKPSPKPAQSTNNHHHNHLILDGGEFTHSDITHPGADADLVEDLQFSTGYGPQPVYAEPPKQQQQQQPAEQSYISSSTSAKRPTTGHNSPTTVSSITTHVDSIESIILQLNNTSHGPSYNVVSQQTPSYGYPGAAVVQTEPAAQNPTFYQENESEKVQESDSQSDYGYTTTVNYESFYDKVSDEQDASAAVSQSAEMPTARPGYGEDVSAVLEDHTMPANGYHDAEAPVAPQTSEFNKMPVMGIAYPVDMSYMEEEGNLPATAAGYGQMSSDSYEASTESTYQKLSTVQTEEPQPTYVRPTTNANKQNRPVASYIGMVTMQHYNPQPGNGDYQAQVPPEVSVSSHTTKVQEQMDETSNGYQQSETTSGYVSPPTAVPAPAQRPQYDAVQGDASSERPVLVTASPRPRPKPSTKRPAVKRPISGESTKKKPQPQPSAGAYNQEKISEHSTRKPVSNGYDKVPESPITHIQIKKPSATQHKEQEQTGYPRPASPAGYEQTTAAAPAPAAPSLNYDKPDAPPSQYDQPSAPSASYDQLAPMPSLNYNEQHASSPGRKPSTAKPISTSYVTGPSTPRPPATVDYHYDNVPPLFMADDKLDAFIQSTAENIVGSTPGNYQPPLVATASTPAYAHRPTSSGSYGHKKPGFVQINGTPKPPRPTVLITPKPTAINLVTYSSLSDDSNKLASSTSSYVTGRPGVQGVSSNDFKDPGYFGSSPVHVAFTQSTTEAVYAVPSDDKPAFPGYFGPTPSYPAFSVPGEKVGQNVMEETYTSPNDFVNFPPVRNPNLNMSAASSAVTSDLDLSTPAFVEDVVLKDKMHTLVHKLVASLQGNFEALADMIEEPGSNKTVATYQAGAGGTAKPVRVVTTRKPVRTATTTRPKVTTKKPVTRVTTKAPNKKTSAVSTTTRKPATRRTTVAAKVTTTTRRPATKKPTRRVSSTVKTTTVSSARPADDEIVDEEDEEDVNPNPSDNEIDQGATLSSYGGANGRKIHSTSRTLPTPNLAFHSPSTECGVRPHVKSGRIVGGKGSTFGAYPWQVLVRESTWLGLFTKNKCGGVLITSRYVITAAHCQPGFLASLVAVMGEFDISGDLESKRSVTKNVKRVIVHRQYDPATFENDLALLELDSPVQFDTHIVPICMPNDVADFTGRMATVTGWGRLKYGGGVPSVLQEVQVPIIENSVCQEMFHTAGHNKKILTSFLCAGYANGQKDSCEGDSGGPLVLQRPDGRYELAGTVSHGIKCAAPYLPGVYMRTTFYKPWLRSITGVK | Probable endopeptidase. In tracheal terminal cells, acts downstream of ich to regulate seamless tube growth and/or maintenance probably by processing lumenal matrix proteins. |
B7YZV4 | PDE1_DROME | Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1 (PDE1) (EC 3.1.4.17) | MQPSSPNATNYLADNIQISSANLSQTEMVVGRDSADYTAMHSINVGVGNSFLRGDTDIPQESGHSFETPSNMSFTAGQWDTESLPPVDTPDALNKAAGRIRSLLRRMDHETVAYEDMQRNLHYAARVLEAVFIDESREGCNGNCKNLNCSRHSHGRDDQQQDNNNSNRSCSLQEASPGGAGAGVTPGADNQDSIESRTKGVSQAPQTHSGPTGPPSNTSSETIAQPAPKLQPALETVRESVMEESPSKDPGDKGPPPPASTSTLTSQTTTSSSATAEPSAKAAESQAGSAGSSGSCSNPAAVHRQRRLRTPTWARSMSTNKTRLADEDDELSEVQPDAVPPEVREWLASTFTRQMATSRRKSDEKPKFRSVAHAIRAGIFVDRMYRRVSSSALTAFPPDVVRLLKNLDDWTFDVFALTEAASGQVVKYVAYELFNRYGSIHKFKIAPGILEAFLHRVEEGYCRYRNPYHNNLHAVDVMQTIHYCLCNTGLMNWLTDLEIFASLLAALLHDYEHTGTTNNFHVMSGSETALLYNDRAVLENHHASASFRLLREDEYNILSHLSREEFRELRGLVIEMVLGTDMTNHFQQMKAMRQLLTLQEATIDKQKVLSLVLHCCDISHPAKQWGVHHRWTMLLLEEFFRQGDLEKELGLPFSPLCDRNNTLVAESQICFIDFIVEPSMGVMSDMLELILAPIAPMNKSKPATLVEHETTANSTTNSAIVIPNSGITPSMDKPRDHRTEAKTTAAECLARKSVTGTTASKFNIPKPWLTCLVENKRIWKEQAVKDAEARALATAAEEAAAAAAAEAEESKPETETADGEQSEPAAEPADGAAA | Cyclic nucleotide phosphodiesterase with a dual specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Required for male fertility and male mating behavior. |
B7ZAQ6 | GPHRA_HUMAN | Golgi pH regulator A (Protein GPR89A) (Putative MAPK-activating protein PM01) (Putative NF-kappa-B-activating protein 90) | MSFLIDSSIMITSQILFFGFGWLFFMRQLFKDYEIRQYVVQVIFSVTFAFSCTMFELIIFEILGVLNSSSRYFHWKMNLCVILLILVFMVPFYIGYFIVSNIRLLHKQRLLFSCLLWLTFMYFFWKLGDPFPILSPKHGILSIEQLISRVGVIGVTLMALLSGFGAVNCPYTYMSYFLRNVTDTDILALERRLLQTMDMIISKKKRMAMARRTMFQKGEVHNKPSGFWGMIKSVTTSASGSENLTLIQQEVDALEELSRQLFLETADLYATKERIEYSKTFKGKYFNFLGYFFSIYCVWKIFMATINIVFDRVGKTDPVTRGIEITVNYLGIQFDVKFWSQHISFILVGIIIVTSIRGLLITLTKFFYAISSSKSSNVIVLLLAQIMGMYFVSSVLLIRMSMPLEYRTIITEVLGELQFNFYHRWFDVIFLVSALSSILFLYLAHKQAPEKQMAP | Voltage dependent anion channel required for acidification and functions of the Golgi apparatus that may function in counter-ion conductance. Plays a role in lymphocyte development, probably by acting as a RABL3 effector in hematopoietic cells (By similarity). |
B7ZC96 | KCMA1_DANRE | Calcium-activated potassium channel subunit alpha-1a (BK channel) (Potassium large conductance calcium-activated channel, subfamily M, alpha member 1a) (Slo1a) (Slowpoke homolog) | MSNNINFNKNPDSSVSISKMDVIIPFTPDVPCDNNGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCHCNIKNKEAQKVNNPITIQADGTTKTGNEKEEAPASEVGWMTSVKDWAGVMISAQTLTGRVLVVLVFALSIGALGIYFIDSSDPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKLWFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKLVNLCSIFISTWLTAAGFIHLVENSGDPWENFQNSQPLSYWECVYLLMVTMSTVGYGDVYARTTLGRLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVNGRKHIVVCGHITLESVSNFLKDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVKIESADACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSWNWKEGDDAICLAELKAGFIAQSCLAQGLSTMLANLFSMRSYIKIEEDTWQKYYLEGVANEMYTEYLSSAFVGLSFPTVCELCYVKLKLLLIAIEYKSEQRESSILINPGNHVKMQEGTLGFFIASDAKEVKRAFFYCKACHDDITDPKRIKKCGCKRIEDEHPSTLSPKKKQRNGGMRNSPNCSPKMMRHDPLLIPGNEQIESMDANVKRYDSTGMFHWCPSKEIEKVILTRSEASMTVLSGHVVVCIFGDVTSALVGLRNLVMPLRASNFHYHELKPIVFVGSLDYLRREWETLHNFPKVFILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDASLQDKECILASLNIKSMQFDDSIGVLQANSQGFTPPGMDRSSPDNSPVHGLVRQASVTTGSNIPIITELVNDSNVQFLDQDDDDDPDTELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGGATPELEALLAEENALRGGYSTPQTLANRDRCRVAQLALYDGPFADLGDGGCYGDLFCKALKTYNMLCFGIYRLRDAHLGAPSQCTKRYVITNPPYEFEMVPTDLIFCLMQFDHNAGQSRASLSHSSHSSHSSSKKSSSVHSIPATNRQNRSSKAREARDKQNATRMNRMGPEKRWFTDEAENAYPRNIQIKPMSTHMANQVNQYKSTSSLIPPIREVEDEC | Potassium channel activated by both membrane depolarization or increase in cytosolic Ca(2+) that mediates export of K(+). It is also activated by the concentration of cytosolic Mg(2+) (By similarity). Its activation dampens the excitatory events that elevate the cytosolic Ca(2+) concentration and/or depolarize the cell membrane (By similarity). It therefore contributes to repolarization of the membrane potential (By similarity). Involved in determining peripheral auditory sensitivity. |
B7ZNG0 | KIF7_MOUSE | Kinesin-like protein KIF7 | MGLEAQRLPGAEEAPVRVALRVRPLLPKELLHGHQSCLRVEPERGRITLGRDRHFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFNATVFAYGQTGSGKTYTMGEASVASLHEDEQGIIPRAMAEAFKLIDENDLLDCLVHVSYLELYKEEFRDLLEVGTASRDIQLREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTPSRLPRPAAGHLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRRGSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSSSDFDETLNTLNYASRAQNIRNRATVNWHPEAERVPEEQAAGARGPPRHRSETRIIHRGRRVPCPAVGSAAVAAGLGAECARCRARTSAAYSLLRELQAEPGLPGAAARKVRDWLCAVEGERSTLSSASGPDSGIESAPAEDQAAQGTSGRKGDEGTQQLLTLQSQVARLEEENRDFLAALEDAMEQYKLQSDRLREQQEEMVELRLRLELAQPGWGAPGLLQGLPPGSFVPRPHTAPLGGAHTHMLGMMPSTCLPGEEVSSEQQVVSGKEVKAEVLAQADKLRSASSTTSEEEGEEEEEEEEEEEEPPRRTLYLRRNGISNWSQRAGLSPGSPPDRKGPEVCPEEPAAAIPAPQAVGSGKVPVQTRQAPAAMASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQDASERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNVQLLLQQGRDHLGEGLADSKRQYEARIHALEKELGRHMWINQELKQKLSAGSTAGQSQGCERRSLCLENRQCLGNEDGLHPAAPEPLWQSSLLEGVSRVWDESRDLVHAPLPLTWKRSSLCSEQGSSEESRVRETTEPPVGRVLPMGEVGLSWNFGPLPKPRWEPRRTSPGMIDVRKNPL | Essential for hedgehog signaling regulation: acts as both a negative and positive regulator of sonic hedgehog (Shh) and Indian hedgehog (Ihh) pathways, acting downstream of SMO, through both SUFU-dependent and -independent mechanisms. Involved in the regulation of microtubular dynamics. Required for proper organization of the ciliary tip and control of ciliary localization of SUFU-GLI2 complexes. Required for localization of GLI3 to cilia in response to Shh. Negatively regulates Shh signaling by preventing inappropriate activation of the transcriptional activator GLI2 in the absence of ligand. Positively regulates Shh signaling by preventing the processing of the transcription factor GLI3 into its repressor form. In keratinocytes, promotes the dissociation of SUFU-GLI2 complexes, GLI2 nuclear translocation and Shh signaling activation. Involved in the regulation of epidermal differentiation and chondrocyte development. |
B7ZQJ9 | GT2D1_XENLA | General transcription factor II-I repeat domain-containing protein 1 (Binding factor for early enhancer) (BEN) (XBEN) (GTF2I repeat domain-containing protein 1) (Williams-Beuren syndrome critical region 11-like protein) (XWBSCR11) | MALAGKQYEGSLNNSRPNLWPSSIPGGKNEIITSLVTALDSMCTALSKLNTEVACIALHEESAFVVGTEKGRCFLNSRKELQADFQRFCIGAHKKDQENEVKRRNRDGIQNIQHVPLGPTSDIYLLRKMVEEIFEVLYSEALGKSNIVPVPYVKVMKEPGSVVVLGLPDGISFRKPAEYDLKSLMLILKHSHNIRFKLRIPTEESIREPKSCSELNSPPTSATKVIPETSQCHRLPIQEHPSSASNFPYSVSQPNQISLEPKQEVHSNMLGTNAVNQMLVQRPSAENNHDLSDCCGQQSPVAGSSLRQNVLASKHLLFSIVHDKTDKWDSFLRETEDINILRECVQILFNSRYAGALGLDHMVPVPYRKIACHPEAVEINGFPDKIPFKRPCTYGVPKLKRILEERHNIHFTIKSMFDQRIFDGTTFTKETTKSDSSSLGEEACSENQKAAALDMLGFPTGSRSEKSSISDECEPGTSSETTGVKLIKLEAEDPDIMQIAVPGTSSETSGVKIIKLESEDPDLIQITVPGTSNETSGVKPKLESEDPDLIQIAVPDRLAECVKNHLAPEDPSYVLDTGKVCDDRPCGVLRNENKHLDGIGDIIRQLRKHVENLFNRKYAKAIGASGPVKVPYAKFLMYPEDLFVLGLPEGVAFRRPNCFGITKLRRILEYSDGIQFVVKRPELISEGLEDCVVGSPGTLGFNDKSNEVILDETNTRPSFQESFDARLSRIDIANTLREQVQVLFNKKYGEALGIKYPVQVPYKRIKNNPGSVIIEGLPPGIPFRKPCTFGSQNLERILAVADKIRFTVTRPFQGLIPRPDDEDANRLGEKVILREQVKELFNEKYGKALGLDQPALIPYKLIRDNPDAVEVRGMPNDIPFRNPNSYDLHRLENILKAQDQIQMVVIKQLEPFPEICSEPPKIKNGNTGPKRKRKRVSEGNSISSASSNCSSSSSSSSNMDPISSAHHVSLVQWPMYMLDYGGLNMQLPGPINY | Transcription factor that activates a subset of organizer-specific genes. Binds to the distal element (DE) of the gsc promoter to regulate its expression. In the presence of pou5f1.1/oct-25, forms a repression complex on the promoter of the gsc and mix2 genes to inhibit their transcription. |
B7ZR30 | STK10_XENLA | Serine/threonine-protein kinase 10-A (EC 2.7.11.1) (Polo-like kinase kinase 1) (XPlkk1) | MAFANFRRILRLPNFEKKRLREYEHVRRDVDPNQVWEIIGELGDGAFGKVYKAKNRETGILAAAKVIETKNEEELEDYMVEIEILATCNHHFIVKLLGAFYWEGKLWIMIEFCPGGAVDAVMLELDRGLKEPEIKTICRQMLEALAYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKTLQRRDSFIGTPYWMAPEVVMCETMKDAPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLSSLSKWSPEFHSFLKTALDKNPETRPSAAQLLEHPFVKKASGNKPLRDLVAEAKAEVLDEIEEQGEAEEEEDSDMLSPKTKGVSQSTHVEIGKDIEREQVGNGIKPHSATSPQKTDSQADNYSQRRNNEVKNCPENGRPDAVNGKPDIIILNPLSSNLEPKRNSTAESYRGEEHSSASSQRQRSAQSAELVPNGSFDSPTRYFTNWSKRDSDSGSNSASESMDISMNLSADLSMNKETGFLSHRENRLHKKTLKRTRRFVVDGVEVSITTSKIIGDDEKKDEEMRFLRRQELRELRLLQKEEHRHQAQLTSKHSFQLEQMSRRFEQEMNSKRKFYDTELETLERHQKQQIVWMEQEHAFRRRDEAKHIKTEQERDHIKFLEQLKLRKKELKAHVEKLPRQQRRETMKVQMDGFAHKKQTEEQQFVNRQKEDLNLAMRVIVLENRKEIYNKEREFLNKKQQLLRDRESVIWELEERHLQERHQLVKQQLKDQYFLQRHELLRKHEKEQEQMQRYNQRMMEQLRLRQQQEKVRLPKNQKAEAKTRMTMFKKSLHISPSGSAAEQRDKIKQFSLQEEKRQKAERLQQQQKHEHQLMEMLAECDCNVRDLLQMQNEKCHLLVEHETQKLKSLDEHHIQLIREWRENIRPRKKAFEDELELKKEAQEMFFRLNEEVAGDPFLSNKPTRFYSFSSPEAS | May act as a polo kinase kinase by mediating phosphorylation of plk1/plx1 and subsequent activation of plk1/plx1 during oocyte maturation. |
B7ZR65 | SOX9A_XENLA | Transcription factor Sox-9-A | MNLLDPFMKMTEEQDKCMSGAPSPTMSDDSAGSPCPSGSGSDTENTRPQENTFPKGDQELKKETEDEKFPVCIREAVSQVLKGYDWTLVPMPVRVNGSSKNKPHVKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLNEGEKRPFVEEAERLRVQHKKDHPDYKYQPRRRKSVKNGQTEQEDGAEQTHISPNAIFKALQADSPHSSSSMSEVHSPGEHSGQSQGPPTPPTTPKTDIQPGKPDLKREGRPLQENGRQPPHIDFRDVDIGELSSEVISTIETFDVNEFDQYLPPNGHPGVGSTQASYTGSYGISSTPSATTGAGPAWMSKQQQQQPQQHSLSTLNSEQSQSQQRTHIKTEQLSPSHYSDQQQQHSPQQLNYSSFNLQHYSSSYPTITRAQYDYTEHQGSSTYYSHASGQNSGLYSTFSYMNPSQRPLYTPIADTTGVPSIPQTHSPQHWEQPVYTQLTRP | Transcription factor that plays a key role in chondrocytes differentiation and skeletal development (By similarity). Specifically binds the 5'-ACAAAG-3' DNA motif present in enhancers and super-enhancers and promotes expression of genes important for chondrogenesis, including COL2A1 (By similarity). Plays a central role in successive steps of chondrocyte differentiation (By similarity). Absolutely required for precartilaginous condensation, the first step in chondrogenesis during which skeletal progenitors differentiate into prechondrocytes (By similarity). Together with SOX5 and SOX6, required for overt chondrogenesis when condensed prechondrocytes differentiate into early stage chondrocytes, the second step in chondrogenesis (By similarity). Later, required to direct hypertrophic maturation and block osteoblast differentiation of growth plate chondrocytes: maintains chondrocyte columnar proliferation, delays prehypertrophy and then prevents osteoblastic differentiation of chondrocytes (By similarity). Also required for chondrocyte hypertrophy, both indirectly, by keeping the lineage fate of chondrocytes, and directly, by remaining present in upper hypertrophic cells (By similarity). Low lipid levels are the main nutritional determinant for chondrogenic commitment of skeletal progenitor cells: when lipids levels are low, FOXO transcription factors promote expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). In addition to cartilage development, also acts as a regulator of proliferation and differentiation in epithelial stem/progenitor cells (By similarity). Involved in development of the cranial neural crest, which is fated to form skeletal elements. Also required for otic placode specification during inner ear development. |
B7ZRU9 | EVI1A_XENLA | MDS1 and EVI1 complex locus protein EVI1-A (Ecotropic virus integration site 1 protein homolog-A) (Evi-1) (xEvi-1) | MKSEDYSYARMAPDIHEERQYRCEECDQLFESKTELSDHQKYPCVTPHSAFSLVENSFPPSLNDDSDLTEMQHTHECKECDQVFPDMQSLEKHLLSHTEEREYKCDQCPKAFNWKSNLIRHQMSHDTGKHYECENCSKQVFTDPSNLQRHIRSQHVGARAHACSDCGKTFATSSGLKQHKHIHSSVKPFVCEVCHKSYTQFSNLCRHKRMHADCRTQIKCKDCGQMFSTTSSLNKHRRFCEGKNHFAAGGLFGQGISLPGTPAMDKASMISMNHANAGLADYFGASRHTAGLTFPTAPGFPFSFPGLFPSSLYHRPPFIPPASPVKGLPGVEQSSKSQSPHVNQPQVLPATQDILKALSKHPSVDENKALEFITESNLNQRPHEKISDHSESSDLDDVSTPSGSDLETTSGSDLESDIESDKDKLKENGKLYKDKMSPLQSLAALNSKREYNNHSVFSPCLEEQTAVTGAVNDSIKAIASIAEKYFGSTGLVGLPDKKGTTLPYPSMFPLPFFPAFSQSMYTFPDRDVRPVPLKIEPESPKETKKVQKGKTESPFDLTTKRKEEKASPNVPSKSGAPTSSNHDQPLDLSMGSRSRAATTKQTEPRKNHIFNEKKDMDPELPKTSEHCLQHARPAPFFMDPIYRVEKRKPMDPLEILKEKYLRPSPGFLFHPQFPMPDQRTWMSAIENMAEKLESFNALKPEANNLIQSVPSMFNFRASSSALPENLLRKGKERYTCRYCGKIFPRSANLTRHLRTHTGEQPYRCKYCDRSFSISSNLQRHVRNIHNKEKPFKCHLCDRCFGQQTNLDRHLKKHENGNLSGTAASSPHSEIEGTGPILDEKEDSYFNEIRNFIGNSSHNKQSPLNSDERINGSHDKIMLAGQNSDILDDDEDEAILDEDDEESDIAVKVMKEPNTSVMLEKCSVDEYEEGGKSEVNSKVSPSRYDDEDDDDDEEEDFKKSLSALDHIRHFTDSLKMRKMDDGQFNDAELSAFTASHLTDDLKHPLYRKSKSQAYAMMLSLSDQESLHPTTHTSSSMWHNLARAAAESTALHSVSHV | Transcriptional repressor during pronephros development. Plays a role in regionalization of the pronephros may promote formation of the distal tubule and duct over formation of the glomus and proximal tubule. |
B7ZS96 | TTHY_XENLA | Transthyretin (xTTR) (Prealbumin) | MASFKSFLLLALLAIVSEAAPPGHASHGEADSKCPLMVKVLDAVRGIPAANLLVNVFRQTESGKWEQITSGKTTELGEIHNLTTDEQFTEGVYKIEFATKAFWGKLGLSPFHEYVDVVFTANDAGHRHYTIAVLLTPYSFSSTAIVSEPHDDL | Thyroid hormone-binding protein, with a much higher binding affinity for triiodothyronine (T3) than for thyroxine (T4). Probably transports triiodothyronine from the bloodstream to the brain. |
B7ZSG3 | WT1A_XENLA | Wilms tumor protein homolog A (XWT1a) (xWT1) | MGSDVRDMNLLPPVSSLSGNSSCNMPVSSSAQWAPVLDFPPGAPYSSLTPHSFIKQEPTWNPDPHEDQCLSAFTVHFSGQFTGTAGACRYGPFGAPTPSQATTGQARMFSNAPYLSNCLDNQQGMRNQGYSAVAFDGTPSYGHTPSHHTSQFTNHSFKHEDPLSQQTSLGEQQYSVPPPVYGCHTPTDTCTGSQALLLRTPYNSDNLYPMTSQLDCMTWNQMNLGSSLKSHGTSYENDSHSSPMLYNCGGQYRIHTHGVFRGIQDVRRVPGVTPAIVRSTEANEKRPFMCAYPGCNKRYFKLSHLQMHSRKHTGEKPYQCDFKDCERRFSRSDQLKRHQRRHTGIKPFQCKTCQRKFSRSDHLKTHTRTHTGKTSEKPFSCRWPSCQKKFARSDELVRHHNMHQRNMTKLQLAL | Transcription factor required for development of the vascular component of the pronephric kidney, the glomus may repress tubule-specific gene expression in the portion of the pronephros fated to form the glomus. Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3' (By similarity). Inhibits Wnt-signaling during embryonic development. Function may be isoform-specific: the isoform containing the KTS motif is less effective in inhibiting wnt signaling. |
B7ZSK1 | NMDE1_XENLA | Glutamate receptor ionotropic, NMDA 2A (GluN2A) (N-methyl D-aspartate receptor subtype 2A) (NMDAR2A) (NR2A) | MGMFVLLLYTFLYAGDLGHGAEKSFPVLNIAVILGRTRYITERDIRSLWTRDMSLDFDVNVVTLLVNQTDPKSIITHVCDLMSGTKIHGVVFGDDTDQEAIAQILDFVSSQTFIPILGIHGGSSMIMADKDEMSTFFQFGASIKQQATVMLNIMEEYDWHVFSVITSNFPGYRDFISFIKTTVDNSFVGWEVQNYITLDTSYTDAQTLTQLKKIHSSVILLYCSKDEATYIFEEARSLGLMGYGFVWIVPSLVTGNTDIIPYEFPSGLVSVSYDDWDYGIEARVRDGLGIITTAASAMLEKHSVIPEAKTSCYGQNERNDPPLHTLHNFMINVTWDGKDLSFTEDGYQANPKLVVLLLNMEREWEKVGKWENKSLNMKYPVWPRITASLDSDHDDNHLSIVTLEEAPFVIVENIDYLTGTCVRNTVPCRKYFRLNNSTTEGTSVKKCCKGFCIDILKKLSKTVKFTYDLYLVTNGKHGKKIKNVWNGMIGEVVYKRAVMAVGSLTINEERSVAVDFSVPFVETGISVMVSRSNGTVSPSAFLEPFSASVWVMMFVMLLLVSAMAVFIFEYFSPVGYNRNLAQGKDPHGPSFTIGKAVWLLWGLVFNNSVPVQNPKGTTSKIIVSIWAFFAVIFLASYTANLAAFMIQEEFVDQVTGLSDNKFQRPHDYSPPFRFGTVPNGSTERNIRNNYPDMHQYMVKFHQKGVQDALVSLKTGKLDAFIYDAAVLNYMAGRDEGCKLVTIGSGYIFATTGYGIALQKGSRWKRPIDLALLQFVGDGEMEELEKLWLTGICHTEKNEVMSSQLDIDNMAGVFYMLAAAMALSLITFVWEHLFYWKLRFCFTGVCTGTPGLLFSISRGIYSCIHGVHIEEKKKSPDFSFTASQTNMLKLLRASKNIANLSNLNQSQCNSPKRTSDYIQRNSLLTDMVLDKGNLTYSDNRPFQQKDIYSENTYDLAMLSANCPKDNLNNYVFQGQHPLTLNESNPNTVEVAVSAEAKVNTRPRQLWKKSVETLRQTQGSVNENGTEESKSSIKNQRFLPEDGHFSDVSEASSRATCHIDSENNNKHRKSKDNLKKRPVSAKYARECSEVELSYLKIKHGPNRDKVYTIDGDKEPSFIMDQPKYSENSPDQDDEDYPDVYQDHNDNYRKTEPLQSDRTPLHSEGRLPNNDIQYKLFSKHYNLKEKNTSMSDANDRHRQNSTHCRSCLSNMPNYTGHYTARSPYKCDDCLHTGKLYDIDEDQMLHEAANSMHSEDFYEHNWLENNALHFQKKNKLRINRQHSCDNINKPREHDLGRPPRSLSLKEKERYIQENPFAKFVIVPPEKLLGNNASLFTDSLKDSKRSKSLYPDNSSDNPFLHSYQETQKLSHGRSSSDIYKQSSLPKARNDNYLRSSIKSTTSYSSRDGRVPDDMCVSEYALPYVTSNNSVYSAPRVVNSCSNRRVFKKMPSLESDV | Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+). Sensitivity to glutamate and channel kinetics depend on the subunit composition (Probable). Plays a role in dendritic branching in brain neurons and in synaptic plasticity. |
B7ZWR6 | OEP61_ARATH | Outer envelope protein 61 (Tetratricopeptide repeat domain-containing protein 7) | MFNGLMDPEMIRLAQDQMSRMTPADFARIQQQMMSNPDLMNMATESMKNMRPEDLKQAAEQLKHTRPEDMAEISEKMAKASPEDIAAMRAHADAQFTYQINAAQMLKKQGNELHSRGNFSDAAEKYLRAKNNLKEIPSSKGGAILLACSLNLMSCYLKTNQHEECIKEGSEVLGYDARNVKALYRRGQAYRDLGLFEDAVSDLSKAHEVSPEDETIADVLRDVKERLAVEGPGKASRGVVIEDITEENNVTSGENKKPSKEANGHAQGVKTDVDGLQALRDNPEAIRTFQNFISKTDPDTLAALSGGKAGDMSPDMFKTASSMIGKMSPEEIQKMVQTASSFKGDNPFAPTAPSTENGFTPTPDMLKLASDMMGKMSPEERERMFNMASSLKANAPASTSYGNAEASEPRESLGASGSSSGNSFVAPRSGFEPSIPSAPPADLQEQMRNQMKDPAMRQMFTSMIKNMNPEMMASMSEQFGMKLSQEDAAKAQQAMASLSPDALEKMMRWADRAQTGMEKAKKAKKWLFGKGGLIFAILMLVLAMVLHRLGYIGN | Plays a role in protein import into the endoplasmic reticulum (ER). May function as chaperone docking protein during post-translational protein translocation into the ER. Chaperone receptor mediating Hsp70-dependent protein targeting to chloroplasts. Interacts specifically with some chloroplast precursors, but not with mitochondrial precursors. Able to select precursors for delivery to the chloroplast translocase independently of Hsp70. |
B8A4F0 | ZD16A_DANRE | Palmitoyltransferase ZDHHC16A (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 16A) (DHHC-16A) | MHPCSSVLHLLLRCMRGCCRHTRSRVPRRLRRHVSYIRLIFKSLYFNSLTNSDVVTDSILEPVFWMVEVVTRWFGMVFVFLVVALTSSVVFIAYFCLLPLVLHTYSPGWMIWHICYGHWNLVMIVFHYYKATKTPPGYPPKMKTDVPFVSVCKKCIIPKPARSHHCGICKTCILKMDHHCPWLNNCVGHFNHRYFFSFCLFLTLGCMYCSVSGRHLFIDAYNTIDQLKHLEAEKQGVPVTGIGLLIGIVPSAGVAGKAVQVAQEVSQPPYTYKDRMFHKSVIYMWVLTSTVSVALGALTLWHALLITRGETSIERHINGKEAKRLAKRGRVYRNPFSYGKLNNWKVFFGVEKRSHWLTRVLLPSGHAPYGDGLTWDIYPLKKDMMPV | Palmitoyl acyltransferase that mediates palmitoylation of proteins and is required during embryonic heart development. Involved in the proliferation of neural stem cells by regulating the FGF/ERK pathway (By similarity). Involved in the proliferation of neural stem cells by regulating the FGF/ERK pathway. |
B8A4W9 | LOX3B_DANRE | Lysyl oxidase homolog 3B (EC 1.4.3.-) (EC 1.4.3.13) (Lysyl oxidase-like protein 3B) | MELHQWCRHIIVFLLNVWIPSCFAQTTPPARSSPTPTPQTADNPDSLKFRLSGFPRKHNEGRIEVFYKGEWGTICDDDFSLANAHVLCRQLGFVSATGWTHSAKYGKGAGKIWLDNVQCSGSERSVSVCKSRGWGNSDCTHDEDAGVICKDERLPGFVDSNVIEVQVDENRVEEVRLRPVFTTATKRMPVTEGVVEVKNKDGWAQICDIGWTPKNTHVVCGMMGFPHEKKVNKNFYKLYAERQKNFFLVHSVACLGTEVHLAACPLEFNYGNATESCPGGMPAVVSCVPGPLYTQSPTMKKKLKMPPTTRLKGGAKYGEGRVEVLKGSEWGTVCDDRWNLVSASVVCREMGFGSAKEALTGASMGKGLGPIHMNEVQCTGNERSLWSCRYKNITAEDCKHTEDASVRCNVPYMGYEKTVRILGGRTRYEGRVEVLHREADGTLRWGLICGEGWGTQEAMVLCRQLGLGYANHGLQVRLSGGRSPYEGRVEVRVGQRWGSVCSEGWSTKEAMVLCRQLGLGFSMHAITETWYWDSSNVTDMVMSGVKCTGDEMSISQCQHHRTVNCQKAAARFAAGVICSETASDLVLNAPLVQQTTYIEDRPLHMLYCAAEEDCLSKSAASANWPYGHRRLLRFSSQIHNIGRADFRPKAGRHSWVWHACHGHYHSMDIFTHYDLMSANGTKVAEGHKASFCLEDTDCDEGVSKRYKCANFGEQGITVGCWDLYRHDIDCQWIDITDVKPGNYILQVVINPNYEVSESDFTNNAMKCNCKYDGHRIWVHNCHIGDAFSEEAEKKFEKYPGQLNNQIS | Protein-lysine 6-oxidase that mediates the oxidation of peptidyl lysine residues to allysine in target proteins (By similarity). Catalyzes the post-translational oxidative deamination of peptidyl lysine residues in precursors of elastin and different types of collagens, a prerequisite in the formation of cross-links between collagens and elastin (By similarity). Can mediate oxidation of lysine residues that are acetylated (By similarity). Also able to catalyze deacetylation of lysine residues (By similarity). Required for maturation of neural crest derived cartilage elements. |
B8AL97 | CUCIN_ORYSI | Cupincin (EC 3.4.-.-) (52 kDa globulin-like protein) (allergen Ory s NRA) | MAKKKTSSSMARSQLAALLISLCFLSLASNAVGWSRRGEREEEDERRRHGGEGGRPYHFGEESFRHWTRTRHGRFSVLERFPDEQVVGAAVGGYRVAVLEAAPRAFLQPSHYDADEVFYVKEGEGVIVLLREGRKESFCVREGDAMVIPAGAIVYSANTHSSKWFRVVMLLNPVSTPGHFEEYFPVGGDRPESFFSAFSDDVLQAAFNTRREELEKVFERQREGGEITTAPEEQIRELSKSCSRGGGGGSGSEWEIKPSSLTGKSPYFSNNHGKLFELTGDECRHLKKLDLQIGLANITRGSMIAPNYNTRATKLAVVLQGSGYFEMACPHVSGGGSSERREREREHGRRREEEQGEEEHGERGEKARRYHKVRAQVREGSVIVIPASHPATIVASEGESLAVVCFFVGANHDEKVFLAGRNSPLRQLDDPAKKLVFGGSAAREADRVLAAQPEQILLRGPHGRGSVSDM | Seed storage protein (Probable). Globulin-like protein that acts as zinc metalloprotease. Cleaves specifically between Leu-15 and Tyr-16 of insulin B chain, and Gln-1 and Leu-2 of neurotensin (NT) peptide in vitro. May play a role as an initiating endopeptidase in germinating seeds. |
B8ANW0 | YUC8_ORYSI | Indole-3-pyruvate monooxygenase YUCCA8 (OsYUCCA8) (EC 1.14.13.168) (Flavin-containing monooxygenase YUCCA8) (OsFMOt) (Protein CONSTITUTIVELY WILTED 1) (OsCOW1) (Protein NARROW LEAF 7) (Protein RICE ETHYLENE-INSENSITIVE 7) | MQGQQKQNAGGGGGDNASPCIVLDGPIIVGAGPSGLAVAATLRQHGAPFTVVERSGGVADLWTNRTYDRLRLHLPKVFCELPHVAFPPDFPTYPTKHDFLRYLHSYAARFAIAPLLRRTVTRAWYDHPASLWRVTTTTTSSSATSVITEYASPWLVVASGENAEVVVPKVKGRERFAGEALHSSEYRSGERFRGMRVLVVGCGNSGMEMCLDLCEHGAMPFMSVRSGVHVLPREMFGASTFGIAMKLLRWLPIKMVDRFLLLVARMVLGDTEKYGLKRPKLGPLEIKNITGKSPVLDVGAWSLIKSGNIKIVPEVESFSGNGARFVDGNEMAFDAVIFATGYRSNVPSWLQEDGELFTEEGKLRSSGSSSEWRWRGPNGLYCVGFSGRGLLGAGADALRAAADIAGRWQETQQAAANISSV | Involved in auxin biosynthesis. Converts the indole-3-pyruvic acid (IPA) produced by the TAA family to indole-3-acetic acid (IAA) (By similarity). Seems not able to use tryptamine (TAM) as substrate (By similarity). Probably responsible for auxin biosynthesis in leaves and involved in the regulation of lateral leaf growth (Ref.3). Required for maintaining water homeostasis and an appropriate root to shoot ratio (By similarity). Required for the inhibition of root growth by ethylene in etiolated seedlings (By similarity). Functions downstream of the ethylene-response transcription factor EIL1 (By similarity). |
B8AVJ9 | APL25_ORYSI | APETALA2-like protein 5 | MWDLNDSPAAEAAPPPLSPSADDSGASSSSAAAVVEIPDDADDDSAAVVVVTRQFFPPAVPGGGGDPAPGNARAGWLRLAGAAPPVAATGPAASAAVSKKSRRGPRSRSSQYRGVTFYRRTGRWESHIWDCGKQVYLGGFDTAHAAARAYDRAAIKFRGVEADINFSLEDYEDDLKQMSNLTKEEFVHVLRRQSTGFPRGSSKYRGVTLHKCGRWEARMGQFLGKKYVYLGLFDTEEEAARAYDRAAIKCNGKDAVTNFDPSIYAGEFEPPAAATGDAAEHNLDLSLGSSAGSKRGNVDGGGDDEITGGGGGGTGSDQRVPMAFDLDWQTAAARSTKAKFDQNSNHPQMPPVLQVTHLPFSPRHHHQFLSNGDPGTAGGLSLTIGAGMAGHWPPQQQQGWGNAGGMSWPLPPHPPPPPTNAAAAATATAAAASSRFPPYIATQASTWLQKNGFHSLTRPT | Transcription factor. Involved in spikelet transition and development. Prevents lemma and palea elongation as well as grain growth. Required for seed shattering through specifying abscission zone (AZ) development. |
B8B183 | APO1_ORYSI | Protein ABERRANT PANICLE ORGANIZATION 1 (F-box protein 321) (OsFbox321) (Protein STRONG CULM 2) | MMNPRRLPPLPSSTSSASAADDMDPRVWRRLPQPLVDRVLACLPTPSFLRLRAACRRFYHLLFSSPFLHSHLLLSPHLPFFAFVVPAAGHLLLLDPTATASWSRLPLPLPPVAGGPAAFSPAAASAGLLAFLSDASGHKTLLLANPITRLLAALPISPTPRLSPTVGLAAGPTSIIAVVAGDDLVSPFAVKNISADTFVADAASVPPSGFWAPSSLLPRLSSLDPGAGMAFASGRFYCMSSSPFAVLVFDVAENVWSKVQPPMRRFLRSPALVELGGGREGAARVALVSAVEKSRLSVPRSVRLWTLRGGGGGGGGGAWTEVARMPPEVHAQFAAAEGGRGFECAAHGDYVVLAPRGPVAQAPTSALVFDSRRDEWRWAPPCPYVVVAHHGGAGAAGFRVFAYEPRLATPAIGLLDATAPVALHGMHDG | Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Together with FL/APO2, involved in the temporal regulation of meristem identity during both vegetative and reproductive developments in an APO2-dependent manner (By similarity). Promotes spikelet formation by suppressing the precocious conversion of inflorescence meristems to spikelet meristems, probably via a positive regulation of class-C floral homeotic genes, but not of class-B genes, and through the control of cell proliferation in meristems. Mediates culm development and strength/diameter enhancement at internodes. Required for the regulation of the plastochron, floral organ identity, and floral determinacy (By similarity). Controls the number of primary rachis branches (PRBs). May trigger the formation of vascular bundle systems which, consequently, promote carbohydrate translocation to panicles. Involved in ozone-induced grain yield regulation. |
B8BB68 | BAK1_ORYSI | LRR receptor kinase BAK1 (EC 2.7.11.1) (BRI1-associated receptor kinase 1 homolog) (Benzothiadiazole-induced SERK1) (Somatic embryogenesis receptor kinase 1) | MAAPRWAVWAVLLLRLLVPAARVLANMEGDALHSLRTNLVDPNNVLQSWDPTLVNPCTWFHVTCNNDNSVIRVDLGNAALSGTLVPQLGQLKNLQYLELYSNNISGTIPSELGNLTNLVSLDLYLNNFTGPIPDSLGNLLKLRFLRLNNNSLSGSIPKSLTAITALQVLDLSNNNLSGEVPSTGSFSLFTPISFANNPSLCGPGTTKPCPGAPPFSPPPPYNPPTPVQSPGSSSSTGAIAGGVAAGAALLFAIPAIGFAWYRRRKPQEHFFDVPAEEDPEVHLGQLKRFSLRELQVATDTFSNKNILGRGGFGKVYKGRLADGSLVAVKRLKEERTPGGELQFQTEVEMISMAVHRNLLRLRGFCMTPTERLLVYPYMANGSVASRLRERPPSEPPLDWRTRRRIALGSARGLSYLHDHCDPKIIHRDVKAANILLDEDFEAVVGDFGLAKLMDYKDTHVTTAVRGTIGHIAPEYLSTGKSSEKTDVFGYGIMLLELITGQRAFDLARLANDDDVMLLDWVKGLLKEKRLEMLVDPDLQSNYIDVEVESLIQVALLCTQGSPTERPKMAEVVRMLEGDGLAERWEEWQKIEVVRQEVELGPHRNSEWIVDSTDNLHAVELSGPR | LRR receptor kinase involved in defense response. Does not seem to be required specifically for XA21-mediated immunity or basal resistance to Xanthomonas oryzae pv. oryzae (Xoo), or immunity to Magnaporthe oryzae. Involved in brassinosteroid (BR) signaling pathway. Acts as coreceptor of BRI1. Forms at the plasma membrane a receptor complex with BRI1 which is activated in response to brassinolide. Phosphorylates BRI1. Required for normal plant growth and leaf development. Possesses kinase activity in vitro. |
B8CH91 | FADB_SHEPW | Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)] | MIYQSPTIEVELLEDNIAHLCFNAQGSVNKFDRETIDSLNAALDSIKQNNSIKGLMLTSAKPAFIVGADITEFLGLFAEEDAVLLSWLEEANVVFNKLEDLPFPTISAINGFALGAGCETILATDFRVADTTARIGLPETKLGIIPGFGGTVRLPRVVGTDNALEWITSGKDQRPEAALNVGAIDALVAPEQLQSAALKMLKDAIAEKLDWQTRRAKKLAPLTLPKLEAMMSFATAKGMVFKVAGKHYPAPMAVVSVIEKAAQLDRAGALKVEHQAFLKLAKTEVAQSLIGIFLNDQLVKGKAKKAGKLAKKVNSAAVLGAGIMGGGIAYQSASKGTPIVMKDIAQPALDLGLGEASKLLAAQVKRGRSNPAKMAAVLNNITPALDYAPVKAADVVVEAVVEHPKVKSMVLAEVEEHVSEDAIITSNTSTISINLLAKSLKKPERFCGMHFFNPVHKMPLVEVIRGEHSSDETVASVVAYASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSGLLADGADFAAIDKVMEKQFGWPMGPAYLLDVVGLDTGHHAQAVMAEGFPERMGKTGKDAIDVMFEAERFGQKNNKGFYQYSVDRRGKPKKDLDPTSYELLQGEFGERKAFESDEIIARTMIPMIIETVRCLEEGIIASPAEADMGLVYGLGFPPFRGGVFRYLDTMGVANFVALADKYAHLGGLYQVTDAMRELAANNGSYYQQA | Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}. |
B8EIZ7 | TMM_METSB | Trimethylamine monooxygenase (TMA monooxygenase) (Tmm) (EC 1.14.13.148) | MTRVAIIGAGPSGLAQLRAFQSAGKKGAAIPELVCFEKQSDWGGLWNYTWRTGVDEYGEPVHGSMYRYLWSNGPKECLEFADYSFEEHFGRPIPSYPPRAVLHDYIMGRVEKSDVRKFVRFSTVVRWIDFDETTQLFTVTVKDLKKDELYSETFDYVVVASGHFSTPNVPHFPGIEVFPGRVLHAHDFRDANEFVGKNLLVVGSSYSAEDIASQCYKYGAKSITFSYRSKPLNFDWPECFTVKPLLTKLTGKTAHFKDGSEAVVDAVLLCTGYLHHFPFLADNLRLKTNNRLYPAGLYKGIFWQDNPKLIYLGMQDQYFTFNMFDAQAWYARDVILGRIKLPAAEERQADIDHWRGLEEKLETAFDGIDFQTEYMRDLIPATDYPMFDLDKVAALFKEWEEDKVKSIMGYRDNSYVSIMTGNKAPPHHTKWMEALDDSFDAFQNRPEAAAE | Catalyzes the oxidation of trimethylamine (TMA) to produce trimethylamine N-oxide (TMAO). In vitro, has a broad substrate specificity, oxidizing many nitrogen- and sulfur-containing compounds, including dimethylamine (DMA), dimethylsulfide (DMS), dimethylsulfoxide (DMSO), cysteamine, methimazole and dimethylaniline. |
B8GYI7 | OBG_CAUVN | GTPase Obg/CgtA (EC 3.6.5.-) (CgtAC) (GTP-binding protein Obg) | MKFLDQCKIYIRSGNGGGGSVSFRREKYIEYGGPDGGDGGRGGDVWIEAVEGLNTLIDYRYQQHFKAGTGVHGMGRARHGAAGEDVVLKVPVGTEVLEEDKETLIADLDHAGMRLLLAKGGNGGWGNLHFKGPVNQAPKYANPGQEGEERWIWLRLKLIADVGLVGLPNAGKSTFLAAASAAKPKIADYPFTTLTPNLGVVDLSSSERFVLADIPGLIEGASEGAGLGTRFLGHVERSATLIHLIDATQDDVAGAYETIRGELEAYGDELADKAEILALNKIDALDEETLAEKVAELEAVSGIKPRLVSGVSGQGVTELLRAAYKQVRIRRGDLEEEIDDDEDHVDETPGGWTP | An essential GTPase which binds GTP, GDP and ppGpp with moderate affinity (with a twofold preference for GDP over GTP), shows high guanine nucleotide exchange rate constants for both nucleotides, and has a relatively low GTP hydrolysis rate. Deletion of the 159 N-terminal residues makes a protein that is non-functional in vivo but which retains nucleotide binding and GTPase activity. Required for cell cycle progression from G1 to S phase and for DNA replication. |
B8GZM2 | PLED_CAUVN | Response regulator PleD (Stalked cell differentiation-controlling protein) [Includes: Diguanylate cyclase (DGC) (EC 2.7.7.65) (Diguanylate kinase)] | MSARILVVDDIEANVRLLEAKLTAEYYEVSTAMDGPTALAMAARDLPDIILLDVMMPGMDGFTVCRKLKDDPTTRHIPVVLITALDGRGDRIQGLESGASDFLTKPIDDVMLFARVRSLTRFKLVIDELRQREASGRRMGVIAGAAARLDGLGGRVLIVDDNERQAQRVAAELGVEHRPVIESDPEKAKISAGGPVDLVIVNAAAKNFDGLRFTAALRSEERTRQLPVLAMVDPDDRGRMVKALEIGVNDILSRPIDPQELSARVKTQIQRKRYTDYLRNNLDHSLELAVTDQLTGLHNRRYMTGQLDSLVKRATLGGDPVSALLIDIDFFKKINDTFGHDIGDEVLREFALRLASNVRAIDLPCRYGGEEFVVIMPDTALADALRIAERIRMHVSGSPFTVAHGREMLNVTISIGVSATAGEGDTPEALLKRADEGVYQAKASGRNAVVGKAA | Response regulator that is part of a signal transduction pathway controlling cell differentiation in the swarmer-to-stalked cell transition. Catalyzes the condensation of two GTP molecules to the cyclic dinucleotide di-GMP (c-di-GMP), which acts as a secondary messenger. |
B8H444 | FTSH_CAUVN | ATP-dependent zinc metalloprotease FtsH (EC 3.4.24.-) | MNFRNLAIWLVIVAVLGGVFVVSQNSRTKSSSEISYSQLLKDVDAGKIKSAEIAGQTVLAKTADNKTLTVNAPMNSEELVNRMVAKNADVKFKSGSISFLAILVQLLPILLVVGVWLFLMRQMQGGAKGAMGFGKSKARLLTENKNRITFEDVAGVDEAKEELQEVVDFLKDPAKFQRLGGKIPKGALLVGPPGTGKTLIARAVAGEAGVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAGLGGGNDEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALLRPGRFDRQVVVPNPDVAGREKIIRVHMKNVPLAADVDVKTLARGTPGFSGADLANLVNEAALMAARKNRRMVTMQDFEQAKDKVMMGAERRSMAMNEEEKKLTAYHEGGHAIVALNVPLADPVHKATIVPRGRALGMVMQLPEGDRYSMKYQQMTSRLAIMMGGRVAEEIIFGKENITSGASSDIKAATDLARNMVTRWGYSDILGTVAYGDNQDEVFLGHSVARTQNVSEETARLIDSEVKRLVQYGLDEARRILTDKIDDLHTLGKALLEYETLSGEEIADILKGIPPKREEEEAATAVIAPSLVPLSPGAGASVTA | Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins. {ECO:0000255|HAMAP-Rule:MF_01458}. Absence of FtsH leads to increased sigma-32 levels, which suggests, in analogy to E.coli, that sigma-32 is a substrate for FtsH. May play a role in the general stress response, as overexpression leads to improved resistance to salt stress. |
B8JI71 | EYS_DANRE | Protein eyes shut homolog | MRNPKLAIIVFLLSCVIYGPVYSQVTCRRATSREWHTQPKNISVRWTLMENTCSSLTQCWSSFAETNGHFWTTGPYHFPQLCPLELQLGDLLFVSADGTLEQHGVQLIKVSKEEFDKCAILEPRKEQLVFASSINGTLQVESKWLMSGLNYFTIINRGSSHLCRFGLRIAVLVKPQLCQSSPLLRLCSGKGECRTTLKDDSFTCRCHKHFSGRYCENVDGCYEQPCLNGGTCLSEGSAYTDLPPYTCLCPAPFTGVNCSEIIGNQNCSKWCKEGACLKVSSTSYRCECFTGYTGTYCERKRLFCDSNPCRNDGRCEETANGYVCTCPGGFTGLNCETTAEADSYCKSSGCQLDEACATDKLNATCICVDPECLEQAEVCGTLPCLNGGICVVPNGQYHCRCRQGFSGKNCEEIIDFCKLLNINCLNEGLCLNRVGGYNCLCAPGWTGEFCQYLENACLAYPNRCLNGATCISMSQTTAPPHYMCTCLPGYTGPYCEAEVNECDSSPCQHQGTCTDFVGYYKCTCPSGYTGIDCEIDINSCWLPNATCPPETLCVDLPGDQLFKCHTPCPHYLQPCANGGHCVLHNITSYSCVCAPGWTGATCLVNINECVQHRCQNRATCVDEVGGYSCLCGHGYTGVHCELDFCSGHQCSEHAVCVDQQHNYTCRCMLGYEGTLCELETDECKSAPCTNNATCIDLVAGYQCLCAPGFKGRTCSESMNECWSRPCNNGGSCIDLVNDYICNCPLGFTGHDCSMPATGCTSNPCNTKGTSMCEEQQDGFKCVCHHGYTGLFCETSINHCVEGLCHHGSECVDLTKGFMCECLPGLRGRLCEVNIDDCLDKPCGALSICKDGINAYDCFCAPGFVGNNCEIEVNECLSQPCQNGASCSDELNSFSCLCLAGTTGSLCEINIDECQSSPCMNNGTCLDLSDGFKCICPSGFSGPECSMDINECVSYPCKNGGSCIDQPGNYYCRCLAPFKGLNCELLPCEAVNPCDNGAECVEEADLVLFPLGFQCRCRKGFTGPRCEVNIDECSSNPCLNGFCYDAVDGFYCLCNPGYAGVRCEQHINDCASNMCENNSTCVDLHLSYNCLCLPGWEGEYCQRETNECLSNPCKNNATCTDLLNAYRCVCPQGWTGLDCDEDVKECSSSPCLNGAHCVESDTPGEFSCTCPPFFTGPLCEQPYDPCELQRNPCLHNSTCRAQSDGTALCVCPVGFEGTRCEIDSDDCVSRPCQNRGICVDGVNSYSCFCEPGFSGLHCEEDINECASNPCQNQAVCQDLVNGFQCSCVPGYFGPHCNLDVNECDSSPCLHESVCINKPGGFACVCSAGFSGKWCELNVDECKSNPCRNNGSCIDGLNGYQCVCSRGFMGDHCERNTDECSSGPCVHGSCLDEIDAFSCQCEVGWTGHRCQININECEAHPCLNGGSCVDLLDKYACICADGFTGKNCDIDQNVCLQTSLNFSLCFNGGTCVDGPGVNFTCSCRPGFMGDFCEVEMNECCSEPCFNGAICQDLINGYQCHCRPGWTGLHCEDDINECLLQPCNQGMCIQNEPGHGYTCFCRPGFVGENCEYNYDDCLIQSCPETFSCKDGINNVSCVPVKTDTSSLPPISVVSWRSTDISTELQPTFAPVENLQHTEQPADASFGGYSGNSFLEFGGFEVAVPISVTVRFQTESMYGTLLYSASAKRSVFFIKLYISNGILQYDFLCNQKQGVQRINTAQWVADGNEHVVIFRQCLFPCVAEVTVSGVRTVRSAPGNYTSALRLQRTDHVFIGGLPRHRSPYKEAEPFHNYTGCIEIIEINKLRRFHMDHAIARNNVDNCRSQWHHEPPTSSTHSPTLLITVETPPGEWVRVLSPTQPAPVCPQGICLNGGTCRPVSLPSGASSFFCDCPLHFTGRLCEQDITVFSPRFDGNSFLELPSLTSLFQSDTYFPSRSSEDKRILYLTMKSRTPHGSLLYCREQDLGERFLHVFLQNARAVARLGCGAAHILTAVAAQNIRIDSLVAITVRYALPSQNNGQLCFIEIAADNGTANQQQKYMDEPVSEVVFGPTFLGGFPSVLELHHNSGNVSGFIGCIRELQMGSKELYVVGEAIRGQNIQNCDAAVCQHQPCRNGGTCISDAESWFCACPSLYSGKLCQFTACERNPCARGATCVPQTQLEAACLCPYGRQGLLCDEAINITRPKFSGLDEFGYSSYVAYPSIPSTGHFYEFHLKLTFANNASALRNNLILFSGQKGQGLSGDDFFALGVRNGRIVHKYNLGSGLATIISDRLNPRINIHTVHFGRYLKTGWLKVNGQKRRTGTSPGPLMGLNTFSQLYIGGYEEYTPELLPPGSRFQNSFQGCIFDMLFRTRQDGKFHALGGPDIRPLSGRNVGQCGVNPCSLVFCHNGGTCVDSGSSVYCQCVFGWKGALCSEKVSFCDAEHIPPPFCARGSTCVPLSDGYTCQCPLGSAGLHCQQAITISDPFFSGNQSSWMSFPPINIRHRTHVQLQFQTLSPEGILFYTAQHLSTHSGDFLSISLSAGFLQLRYNLGNQTIVLQSPKELDVTGVRWHTVKAGREGNSGFLIVDGESVTRNSSEGSTTLDVGANIFIGGISSLNTVSIDAVEKELVGFTGGIREVVVNGQELELTETGALDGANVGDWDGTACGYKVCKNGGHCHPSGDFSFTCICPSLWTGSRCQQSIQCLNNLCQHNSVCIHNSTSASYSCMCSLGWTGTHCDREVTLKTIRFIGNSYLKYKDPKYNSRNLMHTEVSLNFSTSAGDGLIFWMGKAESEDDDHLAVGLQDGYLKISVNLGERTALPLVYQNSFCCNYWNYLSITHNRTLIQVYVNEERVIFEDIDPFEQYVAVNYGGVIYLGGFELNRDVASVTSGVFTKGFEGSIKDVFLYQDTKQLQFLQTCEGFNVYQGEE | Required to maintain the integrity of photoreceptor cells. Specifically required for normal morphology of the photoreceptor ciliary pocket, and might thus facilitate protein trafficking between the photoreceptor inner and outer segments via the transition zone. |
B8JK39 | ITA9_MOUSE | Integrin alpha-9 | MGGPAAARTGAGGLRALLLALVAAGVPAGAYNLDAQRPVRFQGPSGSFFGYAVLEHFHDNTRWVLVGAPKADSKYSTSVKSPGAVFKCRVHTNPDRRCTELDMARGRTRGAPCGKTCRGDRDDEWMGVSLARQPRADGRVLACAHRWKNIYYEADHILPHGFCYLIPSNLQAKGKVLIPCYEEYKKKYGEEHGSCQAGIAGFFTEELVVMGAPGSFYWAGTLKVLNLTDNTYFKLNDEAIMNRRYTYLGYAVTAGHFSHPSITDVVGGAPQDEGIGKVYIFRADRRSGTLIKIFQASGKKMGSYFGSSLCAVDLNMDGLSDLLVGAPMFSEIRDEGQVTVYLNQGHGALEEQLTLTGDAAYNAHFGESIANLGDIDDDGFPDVAVGAPKEEDFAGAVYIYHGDANGIVPKYSMKLSGRRLNPTLRMFGQSISGGIDMDGNGYPDVTIGAFLSDSVVLLRARPVITVDVSIFLPGSINITAPQCHDGQQPVNCLNVTVCFRFHGKNVPGEIGLNYNLTADVAQKEKGQLPRVYFVLFGETAGQVSERLQLSHMDEVCHHYVAHVKRRVQDVISPIVFEAAYSLDEHVMGEEDRELPDLTPVLRWKKGQRISQKNQTVFERNCQSEDCAADLQLRGKLLLSSVDEKTPHLALGAVKNISLNISISNLGDDAYDANVSFNVSRELFFINMWQKEEMGISCELLESDFLKCSVGFPFMRSKSKYEFSVIFDTSHLSGEEEILSFIVTAQSGNLERSEALHDNTLTLTVPLVHEVDTSITGIVSPTSFVYGESVDASNFIQLDDQECHFQPVNITLQVYNMGPSTLPGSSVSISFPSRLSPGGAEMFQVQDMVVSQEKGNCSLQRNPTPCIIPQEQENIFHTIFAFFSKSGRKVLDCEKPGSFCLTLHCNLSALPKEESRTINLYMLLNTEILKKDSSSVIQFMARAKVKVEPALRVVEIANGNPEETLVVFEALHNLEPRGYVVGWIIAISLLVGILIFLLLAVLLWKMGFFRRRYKEIIEAEKNRKENEDGWDWVQKNQ | Integrin alpha-9/beta-1 (ITGA9:ITGB1) is a receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin. |
B8JLQ9 | CBPO_DANRE | Carboxypeptidase O (EC 3.4.17.-) | MMQASITSILVVLTLVAQDRLAGGLEHKSYDYTKYHTMDEISAWMNQMQRENPDVVSTMTYGQTYEKRNITLLKIGFSSTTPKKAIWMDCGIHAREWIAPAFCQHFVKEVLGSYKTDSRVNMLFKNLDFYITPVLNMDGYIYSWLNNSTRLWRKSRSPCHENSTCSGTDLNRNFYANWGMVGISRNCCSEVYNGATALSEPEAEAVTDFLGAHQNHLLCYLTIHSYGQLILVPYGHPNISAPNYDELMEVGLAAAKAIKAVHGKSYKVGSSPDVLYPNSGSSRDFARLIGIPYSFTFELRDEGQHGFILPEDQIQPTCQEAYEGAMSIINYVHDKNFKNTAITVTATLWTTLMALWISTSHVF | Carboxypeptidase which preferentially cleaves C-terminal acidic residues from peptides and proteins. Can also cleave C-terminal hydrophobic amino acids, with a preference for small residues over large residues. |
B8K1W0 | VM3DK_DABRR | Zinc metalloproteinase-disintegrin-like daborhagin-K (EC 3.4.24.-) (Haemorrhagic metalloproteinase russelysin) (Snake venom metalloproteinase) (SVMP) | MMQVLLVTICLAVFPYHGSSIILESGNVNDYEVVYPQKVTAMPKEAVKQPEQKYEDAMQYKFEVNGEPVLLHLEKNKDLFSEDYSETHYSPDGREITTKPLVQDHCYYHGHIQNDAHSSASISACNGLKGHFKLRGEMYLIEPLKLSDSEAHAVYKYENVEKEDEALKMCGVTQTNWESDEPIKKASLLVATSERNRYFNPYSYVELIITVDHSMVTKYKNDLTAIRTWVFELVNTINEIFKYLYIRVPLVGLEIWKNRDLINVTSAANVTLDLFGEWRKSYLLPRKIHDNSQLLTAIDLNGLTIGMAYVSTMCQSKYSVGVVQDHSKINLRVAVTMAHEIGHNLGLTHDGVYCTCGGYSCIMSAVLGDQPSKYFSNCSYNQYRRFLTEHNPECIINPPLRTDIVSPPACGNELLERGEECDCGSPENCRDPCCDAASCKLHSWVECESGKCCNQCRFKRAGTECRPARDECDKAEQCTGRSANCPVDEFHENGRPCLHNFGYCYNGKCPIMYHQCHALFGQNVTGVQDSCFQYNRLGVYYAYCRKENGRKIPCAPKDEKCGRLYCSYKSPGNQIPCLPYYIPSDENKGMVDHGTKCGDGKVCSNGQCVDLNIAY | Snake venom zinc metalloprotease that possesses high hemorrhagic activity (minimum hemorrhagic dose (MHD)=0.82 ug) when subcutaneously injected into mice. May also potently degrade alpha chain of fibrinogen (FGA). |
B8K1W2 | ABCBB_CANLF | Bile salt export pump (EC 7.6.2.-) | MSDAVILRSVKKFGEDNYGFESSTFYNNDKNSGLQDERKGDSSQVGFFQLFRFSSTTDIWLMFVGSLCAFLHGLSHPGVLLIFGTMTDVFIAYDTELQELKIPGKACVNNTIVWINSSLNQNVTNGTQCGLLDIESEMIKFASYYAGIALLVLITGYIQICFWVIAAARQIQKMRKISFRKVMRMEIGWFDCNSVGELNTRFSDDINRVNDAIADQMPIFIQRMTTSICGFLLGFYQGWKLTLVIISVSPLIGIGAAIIGLSVSKFTDYELKAYAKAGSVADEVISSMRTVAAFGGEKKEVERYEKNLVFAQRWGIRKGIVMGFFTGFMWCLIFLCYALAFWYGSKLVLEDGEYTAGTLVQIFLSILLGALNLGNASSCLEAFATGRAAATSIFHTIDRKPIIDCMSEDGYKLDRIKGEIEFHNVTFHYPSRPEVKILNNLSMVIKSGEMTAVVGSSGSGKSTALQLIQRFYDPSEGMVTLDGHDIRSLNIQWLRTQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVRAAKAANAYNFIMDLPEQFDTLVGEGGGQMSGGQKQRVAIARALVRNPKILLLDMATSALDNESEAMVQEALSKIQQGHTIISVAHRLSTVRAADVIIGFEHGTAVERGSHEELLERKGVYFTLVTLQSQGEPTANAEGIRGEEETDGVSLDNEQTFCRGSYQSSLRASLRQRSKSQLSYLAHEPPLAVVDHKSTYEEDRKDKDIPVEEEIEPAPVRRILKFNAPEWPYMLFGAVGAAVNGSVTPLYAFLFSQILGTFSLPDKEEQRSQINGVCLLFVAVGCVSLCTQFLQGYAFAKSGELLTKRLRKYGFRAMLGQDIGWFDDLRNSPGALTTRLATDASQVQGAAGSQIGMMVNSFTNVTVAMIIAFFFSWKLSLVIMCFFPFLALSGALQTRMLTGFATQDKEALEIAGQITNEALSNIRTVAGIGKERQFIEAFEAELEKPFKTAFRKANVYGFCFGFSQCIVFVANSASYRYGGYLIPNEGLHFSYVFRVISSVVLSATALGRASSYTPSYAKAKISAARFFQLLDRQPPIKVYSSAGEKWDNFQGQVDFVDCKFTYPSRPDTQVLNGLSVSVRPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSRKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDNTREIPMEKVIEAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRNPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNSDIIAVMSQGIVIEKGTHEELMAQKGAYYKLVTTGAPIS | Catalyzes the transport of the major hydrophobic bile salts, such as taurine and glycine-conjugated cholic acid across the canalicular membrane of hepatocytes in an ATP-dependent manner, therefore participates in hepatic bile acid homeostasis and consequently to lipid homeostasis through regulation of biliary lipid secretion in a bile salts dependent manner. Transports taurine-conjugated bile salts more rapidly than glycine-conjugated bile salts. Also transports non-bile acid compounds, such as pravastatin and fexofenadine in an ATP-dependent manner and may be involved in their biliary excretion (By similarity). |
B8LIX8 | IFT25_CHLRE | Intraflagellar transport protein 25 (Flagellar-associated protein 232) | MKDYAREENGGLVVMASCSDERFPPENMLDGKDNTFWVTTGMFPQEFVLRLESCIRVSKITTLSLNVRKLAVEKCDQDKPDQFEKVFEVELANRGDRLQTEVHQVNIRAKYLKFILLQGHGEFATVNRVSVVGGDDDGGGYDEPGGGYGSMQRQPSMGYGGGGGSAATGFAADPGNAAAGGGGGFEDEF | Component of the intraflagellar transport (IFT) complex B. Forms a subcomplex within the IFT complex B with IFT27. |
B8M0U4 | ARO1_TALSN | Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)] | MSMKMADPTKISILGRESIVADYSIWGTYIVQDLLTNLSSTTYVLVTDTNLGSIYLEKFSKIFNEAAAALSPPPRLLTKEIPPGENSKSRQGKADIEDWMLQQTCGRDTVIIALGGGVIGDLLGFVASTYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPQRIYIDIDFIDTLPEREFINGMAEVIKTAAISDEKEFAALERHADAILNAARSKARKGRFDAVRQELKDHIVASARHKAYVVTADEREGGLRNLLNLGHSIGHAIEAILSPQVLHGECVAIGMVKELELARYLGILKPVAVSRMIKCLSKYGLPTSLKDQRVRKHTAGKHCPLDQLMANMALDKKNDGPKKKVVLLSAIGQTYEPKASVVSNEDIRAVLAPSIEVIPGVPKSLNVVCAPPGSKSISNRALVLAALGSGTVRIKNLLHSDDTEVMLNALEHLGAATFAWEEEGEVLVVNGNGGKMQASPTELYLGNAGTASRFLTSVATLSGKGSVDFNILTGNNRMKQRPIGDLVDALTVNGAEIEYLEKAGSLPLKIAASGGFKGGRINLAAKVSSQYVSSLLMCAPYAKEPVVLKLVGGRPISLSYIEMTTAMMRSFGIDVQQSTTEEWTYHIPQGSYTNPAEYVIESDASSATYPLAIAAVTGTTCTVPNIGSASLQGDARFAVDVLRPMGCKVEQTATSTTVTGPADGVLRPLPNVDMEPMTDAFLGASVLAAIAQGEGSNHTTRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGIDRSTLRHPAGGVFCYDDHRVAFSFSILALVAPMPTLILEKECVGKTWPTYWDALKQKFGVRLEGKELDESVTTHHAPADRSNASVIIIGMRGAGKTTTGRWAAKVLNRKFIDLDVELEQTEGKSIPEIIKERGWQGFRDAELALFKRVLAERPTGHVLACGGGIVEIGEARKILTDYHKNKGNVLLVMRDIKRVMEFLNVDKTRPAYIEDMMSVWLRRKPWYHECSNVQYYSRHSSAPELALAVEDFGRFIQVVSGKIDYLAAIRKKRLSFFVSLTLPDLRDTGDLLRTVASGSDAVELRVDLLKDPSSDSAIPSAEYVAEQISFYRSKVALPIVFTVRTVSQGGKFPDDAHDAALELITLAIRSGCEFIDLEITFPEELLRKVTESKAHAKIIASHHDPQGKLNWANGSWIQYYNKALQYGDIIKLVGVAESLKDNTALKEFKDWAEQAHDVPVIAINMGDKGQLSRMLNGFLTPVSHPALPFKAAPGQLSAAEIRKGLSIMGEIPAKKFAIFGKPILASRSPAMHNTLFEQNGLPHVYTRLETDQTQDVKEFIRSPDFGGASVTIPLKLDIIPLIDEVLNEAEIIGAVNTIIPVEGKDGTTRLIGRNTDWSGIVRCLREAGAHSNEGKSSALVIGGGGTARAAIYALHHMGFSTVYVLGRSPEKIQNMASTFPTGFDIRVLENADDIETIPRVAVGTVPGDQPIEPNMREILCTIFKRSGQDPSADGASSVLLEMAYKPSVTPLMRLASDAGWKTIPGLEALVGQGVYQFEYWTGITPVYEVARNAVLGTNEK | The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. |
B8M9J8 | TROPB_TALSN | FAD-dependent monooxygenase tropB (EC 1.-.-.-) (Tropolone synthesis protein B) | MPGSLIDTRQQPLSVGIVGGGIIGVILAAGLVRRGIDVKVFEQARGFREIGAGMAFTANAVRCMEMLDPAIVWALRSSGAVPISIGDHQAEARDYLRWVDGYHESSKRLYQLDAGIRGFEACRRDQFLEALVKVLPEGIVECQKRLQKIHEKNETEKVTLEFADGTFAHVDCVIGADGIRSRVRQHLFGEDSPYSHPHYSHKFAFRGLITMENAISALGEDKARTLNMHVGPNAHLIHYPVANETMVNIAAFVSDPEEWPDKLSLVGPATREEAMGYFANWNPGLRAVLGFMPENIDRWAMFDTYDYPAPFFSRGKICLVGDAAHAAVPHHGAGACIGIEDALCATVLLAEVFVSTRGKSSIVRNRAIAAAFGSFNAVRRVRAQWFVDSSRRVCDLYQQPEWADPQKRIKAENCFEEIKDRSHKIWHFDYNSMLQEAIEKYRHNMGS | FAD-dependent monooxygenase part of the gene cluster that mediates the biosynthesis of the tropolone class of fungal maleic anhydrides. Within the pathway, tropB catalyzes a synthetically challenging asymmetric oxidative dearomatization reaction to convert 3-methylorcinaldehyde into a hydroxycyclohexadione. The pathway begins with the synthesis of 3-methylorcinaldehyde by the non-reducing polyketide synthase (PKS) tropA. 3-methylorcinaldehyde is the substrate for the FAD-dependent monooxygenase tropB to yield a dearomatized hydroxycyclohexadione. The 2-oxoglutarate-dependent dioxygenase tropC then performs the oxidative ring expansion to provide the first tropolone metabolite stipitaldehyde. Trop D converts stipitaldehyde into stipitacetal which is in turn converted to stipitalide by the short-chain dehydrogenase/reductase tropE. The next steps involve tropF, tropG, tropH, tropI and tropJ to form successive tropolone maleic anhydrides including stipitaldehydic, stipitatonic and stipitatic acids (Probable). |
B8N2C8 | CP51A_ASPFN | Sterol 14-alpha demethylase (EC 1.14.14.154) (Cytochrome P450 monooxygenase 51A) (Ergosterol biosynthesis protein cyp51A) | MIFSRSMASFTLVSAYAAAGLLAIIVLNLLRQLLFRNKTDPPLVFHWIPFLGSTVTYGMDPYAFFFSCRQKYGDIFTFILLGRKITVYLGIQGNEFILNGKLKDVNAEEIYSPLTTPVFGSDIVYDCPNSKLMEQKKFIKFGLTQAALESHVPLIEKEVLDYLKTSPNFKGTSGRVEITDAMAEITIFTAGRALQGEEVRKKLTAEFADLYHDLDRGFTPINFMLPWAPLPRNRKRDAAHARMREIYMDIINERRKNPDRETSDMIWNLMHCTYKNGQPLPDKEIAHMMITLLMAGQHSSSSISSWIMLRLASEPAVMEELYQEQITKLSPDGRTLPPLQYRDLDLLPLHQNLIKETLRLHLSIHSLMRKVKNPMPVPGTPYVVPADHVLLASPGVTALSDEYFPNASRWDPHRWENRVEKEDEEDIVDYGYGTVSKGTSSPYLPFGAGRHRCIGEKFAYVNLGVIVATMARHMKLFNVDGKKGVPATDYSSMFSGPSKPAIIGWERRFPEKS | Sterol 14alpha-demethylase, encoded by cyp51A, cyp51B and cyp51C, that plays a critical role in the third module of ergosterol biosynthesis pathway, being ergosterol the major sterol component in fungal membranes that participates in a variety of functions (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane (By similarity). In filamentous fungi, during the initial step of this module, lanosterol (lanosta-8,24-dien-3beta-ol) can be metabolized to eburicol (By similarity). Sterol 14alpha-demethylase catalyzes the three-step oxidative removal of the 14alpha-methyl group (C-32) of both these sterols in the form of formate, and converts eburicol and lanosterol to 14-demethyleburicol (4,4,24-trimethylergosta-8,14,24(28)-trienol) and 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol, respectively, which are further metabolized by other enzymes in the pathway to ergosterol (By similarity). Can also use susbtrates not intrinsic to fungi, such as 24,25-dihydrolanosterol (DHL), producing 4,4'-dimethyl-8,14-cholestadien-3-beta-ol, but at lower rates than the endogenous substrates (By similarity). As a target of azole drugs, plays a crucial role in azole susceptibility. |
B8N4Q9 | ARO1_ASPFN | Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)] | MAEPTKIKILGQESIIADFGLWRNYVAKDLISGCPSTTYVLITDTNIGSIYTPGFQKTFEDAATAVSPAPRLLVYHCPPGEVSKSRQTKADIEDWMLSQSPPCGRDTVVIALGGGVIGDLTGFVASTYMRGVRYVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPTRIYIDLEFLETLPVREFVNGMAEVIKTAAISSEEEFTALEDNAEAILTAVRSERKPGQRWFEGIEDILKARILASARHKAYVVSADEREGGLRNLLNWGHSIGHAIEAILTPQVLHGECVAIGMVKEAELARHLGILKGVAVARIVKCIAAYGLPTSLKDSRIRKLTAGKHCSVDQLLFNMALDKKNDGPKKKIVLLSAIGRTYEPKASVVPNEDIGVVLAPSIEVHPGVEPASNIICIPPGSKSISNRALVLAALGSGTCRVKNLLHSDDTEVMLNALERLGAATFSWEEEGEVLVVNGKGGNLQASPSELYLGNAGTASRFLTTVATLANASSVDSSILTGNNRMKQRPIGDLVDALTANGASVEYVERKGSLPLKVAASGGFAGGRINLAAKVSSQYVSSLLMCAPYAKEPVTLKLVGGKPISQPYIDMTTAMMRSFGIDVQKSTTEEHTYHIPQGRYVNPAEYVIESDASSATYPLAIAAITGTTCTVPNIGSKSLQGDARFAVEVLGPMGCTVKQTDTSTTVVGPSDGILRPLPNVDMEPMTDAFLTASVLAAVARGDGASHTTRIYGIANQRVKECNRIKAMKDELAKFGVVCREHDDGLEIDGIDRSTLRQPAGGVYCYDDHRVAFSFSVLSLVAPQPTLILEKECVGKTWPGWWDTLRQKFSAKLEGKELKEEESSPLAGAGRATASVFIIGMRGAGKTTTGRWVAKTLNRPFVDLDTELENVEGQTIPDIVKQRGWQGFRDAELSLLQRTLKERSSGYVLACGGGIVEIPEARKLLIDYHKNKGNVMLIMRDIKQVMDFLNIDKTRPAYVEDMMGVWLRRKPWFQECSNIQYYSQHATGKLAKASEDFTRFFNVVTGEADSLSIIKRKKHSFFVSLTLPDLRTAGDILEKVCVGSDAVELRVDLLKDPASDSDIPSVDYVAEQMAFLRSYVSLPLIFTIRTKSQGGRFPDDAHDAAMELYRLAFRSGSEFVDLEIAFPDEMLRAVTEMKGYSKIIASHHDPKGELSWANMSWMKYYNRALEYGDIIKLVGVAKNLDDNTALRKFKSWAEEAHETPLIAINMGDNGQLSRILNGFMTPVSHPSLPFKAAPGQLSATEIRKGLSLMGEIKQKKFAVFGTPVSGSRSPVLHNTLFSQAGLPHEYGRLETANVEDVKDFIRSPDFGGASVTIPLKLDIMPLLDHITPEAEIIGAVNTIIPVADGDKPARLVGSNTDWQGMTLSLHNAGVETANKDASALVIGGGGTARAAIYALHSMGFSPIYVIGRSAPKLQSMVSTFPSSYNIQVIDSPETLKTIPTVAIGTIPADKPIDPVMRETLCHMFERAQEADADVVKTGEKAHRVLLEMAYKPSVTALMQLASDSNWHTIPGLEVLVGQGWYQFKHWTGISPLYEDARAAVLSS | The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. |
B8N7E5 | RSP5_ASPFN | Probable E3 ubiquitin-protein ligase hulA (EC 2.3.2.26) (HECT ubiquitin ligase A) (HECT-type E3 ubiquitin transferase hulA) | MTCSQPNLRVTIIAADGLYKRDVFRFPDPFAVATVGGEQTHTTSVIKKTLNPYWNEMFDLRVNEDSILAIQIFDQKKFKKKDQGFLGVINVRIGDVIDLQMGGDEMLTRDLKKSNDNLVVHGKLIINLSTNLSTPNTNQANGLHRSHMQPSTSSGLVPQVSASTPQPSPGPSQADPTASNPSLHPQRVPSTTRPSSTIVPANGPPAPPNGQQGSRTNLSSFEDSQGRLPAGWERREDNLGRTYYVDHNTRTTTWTRPSNNYNEQTSRTQREASMQLERRAHQSRMLPEDRTGASSPNLQENQQQAQTPPAGGSASAVSMMATGATTAGTGELPPGWEQRTTPEGRPYFVDHNTRTTTWVDPRRQQYIRMYGQNANGTNTTIQQQPVSQLGPLPSGWEMRLTNTARVYFVDHNTKTTTWDDPRLPSSLDQGVPQYKRDFRRKLIYFRSQPALRIMSGQCHVKVRRNNIFEDSYAEIMRQSASDLKKRLMIKFDGEDGLDYGGLSREFFFLLSHEMFNPFYCLFEYSAHDNYTLQINPHSGVNPEHLNYFKFIGRVVGLAIFHRRFLDSFFIGAFYKMMLRKKVSLQDMEGVDEDLHRNLTWTLDNDIEGIIELTFAVDDEKFGERRTIDLKPGGRDIPVTNENKGEYVELVTEWKIVKRVEEQFNAFMSGFNELIPADLVNVFDERELELLIGGIADIDVDDWKKHTDYRGYQESDEVIQNFWKIVRTWDAEQKSRLLQFTTGTSRIPVNGFKDLQGSDGPRRFTIEKSGDPGALPKSHTCFNRLDLPPYKTNDVLEHKLSIAVEETLGFGQE | E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Probably involved in the regulatory network controlling carbon source utilization. |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.